data_4XX6 # _entry.id 4XX6 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4XX6 WWPDB D_1000206449 # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 4XX6 _pdbx_database_status.recvd_initial_deposition_date 2015-01-29 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _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 'Stogios, P.J.' 1 'Nocek, B.' 2 'Xu, X.' 3 'Cui, H.' 4 'Lowden, M.' 5 'Savchenko, A.' 6 # _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 'Crystal structure of a glycosylated endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Gloeophyllum trabeum.' _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 primary 'Stogios, P.J.' 1 primary 'Xu, X.' 2 primary 'Cui, H.' 3 primary 'Lowden, M.' 4 primary 'Savchenko, A.' 5 # _cell.entry_id 4XX6 _cell.length_a 52.414 _cell.length_b 99.345 _cell.length_c 147.267 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4XX6 _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man Beta-xylanase 35700.574 2 3.2.1.8 ? 'UNP residues 27-347' ? 2 non-polymer syn 'UNKNOWN ATOM OR ION' ? 2 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 15 ? ? ? ? 4 non-polymer man BETA-D-MANNOSE 180.156 5 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 20 ? ? ? ? 6 non-polymer syn 'MAGNESIUM ION' 24.305 2 ? ? ? ? 7 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120 3 ? ? ? ? 8 non-polymer syn 'HEXAETHYLENE GLYCOL' 282.331 2 ? ? ? ? 9 non-polymer nat GLYCEROL 92.094 7 ? ? ? ? 10 non-polymer syn 'CHLORIDE ION' 35.453 1 ? ? ? ? 11 water nat water 18.015 581 ? ? ? ? # _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 ;PTSPFETLRAAAAPRYFGAALGVPHLLNFTHDPLFDVTAVLQFNGATPENEMKWAYIEPERNQFNFTGGDIVAAFSAAND YVLRGHNLVWYQELAPWVETLTGEDLWNATVNHITTVMTHYKESFNIYAWDVVNEAFNDNGTYRENVWYTQLGPDYIPNA YAVARSVNTPSKLYINDYNTEGINNKSDALLAVVQSMKAHNLVDGVGFQCHFFVGELPPDLEQNFARFVAAGVEIAVTEL DIRMNLPPSQADIEQQARDYATVVNACKAQGAACVGITTWGITDLYSWIPSTYPGEGYALLFDDNYVPHPAFNATIQALL A ; _entity_poly.pdbx_seq_one_letter_code_can ;PTSPFETLRAAAAPRYFGAALGVPHLLNFTHDPLFDVTAVLQFNGATPENEMKWAYIEPERNQFNFTGGDIVAAFSAAND YVLRGHNLVWYQELAPWVETLTGEDLWNATVNHITTVMTHYKESFNIYAWDVVNEAFNDNGTYRENVWYTQLGPDYIPNA YAVARSVNTPSKLYINDYNTEGINNKSDALLAVVQSMKAHNLVDGVGFQCHFFVGELPPDLEQNFARFVAAGVEIAVTEL DIRMNLPPSQADIEQQARDYATVVNACKAQGAACVGITTWGITDLYSWIPSTYPGEGYALLFDDNYVPHPAFNATIQALL A ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 PRO n 1 2 THR n 1 3 SER n 1 4 PRO n 1 5 PHE n 1 6 GLU n 1 7 THR n 1 8 LEU n 1 9 ARG n 1 10 ALA n 1 11 ALA n 1 12 ALA n 1 13 ALA n 1 14 PRO n 1 15 ARG n 1 16 TYR n 1 17 PHE n 1 18 GLY n 1 19 ALA n 1 20 ALA n 1 21 LEU n 1 22 GLY n 1 23 VAL n 1 24 PRO n 1 25 HIS n 1 26 LEU n 1 27 LEU n 1 28 ASN n 1 29 PHE n 1 30 THR n 1 31 HIS n 1 32 ASP n 1 33 PRO n 1 34 LEU n 1 35 PHE n 1 36 ASP n 1 37 VAL n 1 38 THR n 1 39 ALA n 1 40 VAL n 1 41 LEU n 1 42 GLN n 1 43 PHE n 1 44 ASN n 1 45 GLY n 1 46 ALA n 1 47 THR n 1 48 PRO n 1 49 GLU n 1 50 ASN n 1 51 GLU n 1 52 MET n 1 53 LYS n 1 54 TRP n 1 55 ALA n 1 56 TYR n 1 57 ILE n 1 58 GLU n 1 59 PRO n 1 60 GLU n 1 61 ARG n 1 62 ASN n 1 63 GLN n 1 64 PHE n 1 65 ASN n 1 66 PHE n 1 67 THR n 1 68 GLY n 1 69 GLY n 1 70 ASP n 1 71 ILE n 1 72 VAL n 1 73 ALA n 1 74 ALA n 1 75 PHE n 1 76 SER n 1 77 ALA n 1 78 ALA n 1 79 ASN n 1 80 ASP n 1 81 TYR n 1 82 VAL n 1 83 LEU n 1 84 ARG n 1 85 GLY n 1 86 HIS n 1 87 ASN n 1 88 LEU n 1 89 VAL n 1 90 TRP n 1 91 TYR n 1 92 GLN n 1 93 GLU n 1 94 LEU n 1 95 ALA n 1 96 PRO n 1 97 TRP n 1 98 VAL n 1 99 GLU n 1 100 THR n 1 101 LEU n 1 102 THR n 1 103 GLY n 1 104 GLU n 1 105 ASP n 1 106 LEU n 1 107 TRP n 1 108 ASN n 1 109 ALA n 1 110 THR n 1 111 VAL n 1 112 ASN n 1 113 HIS n 1 114 ILE n 1 115 THR n 1 116 THR n 1 117 VAL n 1 118 MET n 1 119 THR n 1 120 HIS n 1 121 TYR n 1 122 LYS n 1 123 GLU n 1 124 SER n 1 125 PHE n 1 126 ASN n 1 127 ILE n 1 128 TYR n 1 129 ALA n 1 130 TRP n 1 131 ASP n 1 132 VAL n 1 133 VAL n 1 134 ASN n 1 135 GLU n 1 136 ALA n 1 137 PHE n 1 138 ASN n 1 139 ASP n 1 140 ASN n 1 141 GLY n 1 142 THR n 1 143 TYR n 1 144 ARG n 1 145 GLU n 1 146 ASN n 1 147 VAL n 1 148 TRP n 1 149 TYR n 1 150 THR n 1 151 GLN n 1 152 LEU n 1 153 GLY n 1 154 PRO n 1 155 ASP n 1 156 TYR n 1 157 ILE n 1 158 PRO n 1 159 ASN n 1 160 ALA n 1 161 TYR n 1 162 ALA n 1 163 VAL n 1 164 ALA n 1 165 ARG n 1 166 SER n 1 167 VAL n 1 168 ASN n 1 169 THR n 1 170 PRO n 1 171 SER n 1 172 LYS n 1 173 LEU n 1 174 TYR n 1 175 ILE n 1 176 ASN n 1 177 ASP n 1 178 TYR n 1 179 ASN n 1 180 THR n 1 181 GLU n 1 182 GLY n 1 183 ILE n 1 184 ASN n 1 185 ASN n 1 186 LYS n 1 187 SER n 1 188 ASP n 1 189 ALA n 1 190 LEU n 1 191 LEU n 1 192 ALA n 1 193 VAL n 1 194 VAL n 1 195 GLN n 1 196 SER n 1 197 MET n 1 198 LYS n 1 199 ALA n 1 200 HIS n 1 201 ASN n 1 202 LEU n 1 203 VAL n 1 204 ASP n 1 205 GLY n 1 206 VAL n 1 207 GLY n 1 208 PHE n 1 209 GLN n 1 210 CYS n 1 211 HIS n 1 212 PHE n 1 213 PHE n 1 214 VAL n 1 215 GLY n 1 216 GLU n 1 217 LEU n 1 218 PRO n 1 219 PRO n 1 220 ASP n 1 221 LEU n 1 222 GLU n 1 223 GLN n 1 224 ASN n 1 225 PHE n 1 226 ALA n 1 227 ARG n 1 228 PHE n 1 229 VAL n 1 230 ALA n 1 231 ALA n 1 232 GLY n 1 233 VAL n 1 234 GLU n 1 235 ILE n 1 236 ALA n 1 237 VAL n 1 238 THR n 1 239 GLU n 1 240 LEU n 1 241 ASP n 1 242 ILE n 1 243 ARG n 1 244 MET n 1 245 ASN n 1 246 LEU n 1 247 PRO n 1 248 PRO n 1 249 SER n 1 250 GLN n 1 251 ALA n 1 252 ASP n 1 253 ILE n 1 254 GLU n 1 255 GLN n 1 256 GLN n 1 257 ALA n 1 258 ARG n 1 259 ASP n 1 260 TYR n 1 261 ALA n 1 262 THR n 1 263 VAL n 1 264 VAL n 1 265 ASN n 1 266 ALA n 1 267 CYS n 1 268 LYS n 1 269 ALA n 1 270 GLN n 1 271 GLY n 1 272 ALA n 1 273 ALA n 1 274 CYS n 1 275 VAL n 1 276 GLY n 1 277 ILE n 1 278 THR n 1 279 THR n 1 280 TRP n 1 281 GLY n 1 282 ILE n 1 283 THR n 1 284 ASP n 1 285 LEU n 1 286 TYR n 1 287 SER n 1 288 TRP n 1 289 ILE n 1 290 PRO n 1 291 SER n 1 292 THR n 1 293 TYR n 1 294 PRO n 1 295 GLY n 1 296 GLU n 1 297 GLY n 1 298 TYR n 1 299 ALA n 1 300 LEU n 1 301 LEU n 1 302 PHE n 1 303 ASP n 1 304 ASP n 1 305 ASN n 1 306 TYR n 1 307 VAL n 1 308 PRO n 1 309 HIS n 1 310 PRO n 1 311 ALA n 1 312 PHE n 1 313 ASN n 1 314 ALA n 1 315 THR n 1 316 ILE n 1 317 GLN n 1 318 ALA n 1 319 LEU n 1 320 LEU n 1 321 ALA 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 321 _entity_src_gen.gene_src_common_name 'Brown rot fungus' _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene GLOTRDRAFT_138785 _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain 'ATCC 11539 / FP-39264 / Madison 617' _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 'Gloeophyllum trabeum' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 670483 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'Aspergillus niger' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5061 _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 plasmid _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ANIp7G _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code S7Q6I2_GLOTA _struct_ref.pdbx_db_accession S7Q6I2 _struct_ref.pdbx_db_isoform ? _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;PTSPFETLRAAAAPRYFGAALGVPHLLNFTHDPLFDVTAVLQFNGATPENEMKWAYIEPERNQFNFTGGDIVAAFSAAND YVLRGHNLVWYQELAPWVETLTGEDLWNATVNHITTVMTHYKESFNIYAWDVVNEAFNDNGTYRENVWYTQLGPDYIPNA YAVARSVNTPSKLYINDYNTEGINNKSDALLAVVQSMKAHNLVDGVGFQCHFFVGELPPDLEQNFARFVAAGVEIAVTEL DIRMNLPPSQADIEQQARDYATVVNACKAQGAACVGITTWGITDLYSWIPSTYPGEGYALLFDDNYVPHPAFNATIQALL A ; _struct_ref.pdbx_align_begin 27 # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4XX6 A 1 ? 321 ? S7Q6I2 27 ? 347 ? 27 347 2 1 4XX6 B 1 ? 321 ? S7Q6I2 27 ? 347 ? 27 347 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BMA D-saccharide . BETA-D-MANNOSE ? 'C6 H12 O6' 180.156 CL non-polymer . 'CHLORIDE ION' ? 'Cl -1' 35.453 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MG non-polymer . 'MAGNESIUM ION' ? 'Mg 2' 24.305 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 P6G non-polymer . 'HEXAETHYLENE GLYCOL' 'POLYETHYLENE GLYCOL PEG400' 'C12 H26 O7' 282.331 PEG non-polymer . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3' 106.120 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 UNX non-polymer . 'UNKNOWN ATOM OR ION' ? ? ? 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 4XX6 _exptl.crystals_number ? _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.69 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 54.2 _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 8.5 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '0.2 M Tris, pH 8.5, 0.2 M magnesium chloride, 30% (w/v) PEG 4K, subtlisin protease' _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_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'ADSC QUANTUM 315r' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2012-12-05 # _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 0.97918 _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 'APS BEAMLINE 19-ID' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.97918 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline 19-ID _diffrn_source.pdbx_synchrotron_site APS # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4XX6 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.000 _reflns.d_resolution_high 1.950 _reflns.number_obs 53797 _reflns.number_all ? _reflns.percent_possible_obs 94.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.03600 _reflns.pdbx_netI_over_sigmaI 20.9800 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 2.700 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.95 _reflns_shell.d_res_low 1.98 _reflns_shell.percent_possible_all 89.5 _reflns_shell.Rmerge_I_obs 0.48500 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.840 _reflns_shell.pdbx_redundancy 2.40 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4XX6 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 49319 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.340 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30.20 _refine.ls_d_res_high 1.95 _refine.ls_percent_reflns_obs 91.7 _refine.ls_R_factor_obs 0.156 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.154 _refine.ls_R_factor_R_free 0.204 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 3.920 _refine.ls_number_reflns_R_free 2011 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.details ? _refine.pdbx_starting_model 'PDB ENTRY 3CUI' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details 'Random selection' _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.200 _refine.pdbx_overall_phase_error 19.610 _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 5034 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 584 _refine_hist.number_atoms_solvent 581 _refine_hist.number_atoms_total 6199 _refine_hist.d_res_high 1.95 _refine_hist.d_res_low 30.20 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function f_bond_d 0.008 ? ? 5824 'X-RAY DIFFRACTION' ? f_angle_d 1.251 ? ? 8034 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 13.136 ? ? 2149 'X-RAY DIFFRACTION' ? f_chiral_restr 0.056 ? ? 981 'X-RAY DIFFRACTION' ? f_plane_restr 0.005 ? ? 966 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all 'X-RAY DIFFRACTION' . 1.9500 1.9993 2622 0.1833 35.00 0.2863 . . 107 . . 'X-RAY DIFFRACTION' . 1.9993 2.0534 2862 0.1594 39.00 0.2192 . . 117 . . 'X-RAY DIFFRACTION' . 2.0534 2.1138 3059 0.1591 41.00 0.2182 . . 125 . . 'X-RAY DIFFRACTION' . 2.1138 2.1820 3191 0.1583 43.00 0.2069 . . 130 . . 'X-RAY DIFFRACTION' . 2.1820 2.2599 3359 0.1601 45.00 0.2138 . . 136 . . 'X-RAY DIFFRACTION' . 2.2599 2.3504 3589 0.1604 49.00 0.2198 . . 147 . . 'X-RAY DIFFRACTION' . 2.3504 2.4573 3762 0.1566 51.00 0.2323 . . 154 . . 'X-RAY DIFFRACTION' . 2.4573 2.5868 3831 0.1603 52.00 0.2461 . . 156 . . 'X-RAY DIFFRACTION' . 2.5868 2.7488 3837 0.1577 52.00 0.2125 . . 156 . . 'X-RAY DIFFRACTION' . 2.7488 2.9608 3819 0.1551 52.00 0.2134 . . 156 . . 'X-RAY DIFFRACTION' . 2.9608 3.2585 3818 0.1541 51.00 0.2286 . . 155 . . 'X-RAY DIFFRACTION' . 3.2585 3.7292 3797 0.1354 51.00 0.1671 . . 155 . . 'X-RAY DIFFRACTION' . 3.7292 4.6956 3793 0.1232 51.00 0.1499 . . 155 . . 'X-RAY DIFFRACTION' . 4.6956 30.2050 3980 0.1853 54.00 0.2221 . . 162 . . # _struct.entry_id 4XX6 _struct.title 'Crystal structure of a glycosylated endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from Gloeophyllum trabeum' _struct.pdbx_descriptor GH10 _struct.pdbx_model_details ? _struct.pdbx_formula_weight ? _struct.pdbx_formula_weight_method ? _struct.pdbx_model_type_details ? _struct.pdbx_CASP_flag ? # _struct_keywords.entry_id 4XX6 _struct_keywords.text 'XYLANASE, FUNGUS, TIM BARREL, ALPHA8/BETA8 FOLD, GLYCOSIDE HYDROLASE FAMILY 10, GH10, HYDROLASE' _struct_keywords.pdbx_keywords HYDROLASE # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 3 ? E N N 3 ? F N N 4 ? G N N 5 ? H N N 5 ? I N N 5 ? J N N 5 ? K N N 5 ? L N N 3 ? M N N 3 ? N N N 4 ? O N N 5 ? P N N 5 ? Q N N 5 ? R N N 5 ? S N N 5 ? T N N 5 ? U N N 3 ? V N N 3 ? W N N 4 ? X N N 5 ? Y N N 3 ? Z N N 6 ? AA N N 7 ? BA N N 8 ? CA N N 8 ? DA N N 9 ? EA N N 9 ? FA N N 9 ? GA N N 9 ? HA N N 2 ? IA N N 3 ? JA N N 3 ? KA N N 4 ? LA N N 5 ? MA N N 5 ? NA N N 5 ? OA N N 3 ? PA N N 3 ? QA N N 4 ? RA N N 5 ? SA N N 5 ? TA N N 5 ? UA N N 5 ? VA N N 5 ? WA N N 3 ? XA N N 3 ? YA N N 3 ? ZA N N 3 ? AB N N 6 ? BB N N 10 ? CB N N 7 ? DB N N 7 ? EB N N 9 ? FB N N 9 ? GB N N 9 ? HB N N 11 ? IB N N 11 ? # 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 THR A 7 ? ALA A 13 ? THR A 33 ALA A 39 1 ? 7 HELX_P HELX_P2 AA2 GLY A 22 ? LEU A 27 ? GLY A 48 LEU A 53 1 ? 6 HELX_P HELX_P3 AA3 ASP A 32 ? PHE A 43 ? ASP A 58 PHE A 69 1 ? 12 HELX_P HELX_P4 AA4 LYS A 53 ? GLU A 58 ? LYS A 79 GLU A 84 1 ? 6 HELX_P HELX_P5 AA5 PHE A 66 ? ASN A 79 ? PHE A 92 ASN A 105 1 ? 14 HELX_P HELX_P6 AA6 ALA A 95 ? LEU A 101 ? ALA A 121 LEU A 127 5 ? 7 HELX_P HELX_P7 AA7 THR A 102 ? PHE A 125 ? THR A 128 PHE A 151 1 ? 24 HELX_P HELX_P8 AA8 ASN A 146 ? GLY A 153 ? ASN A 172 GLY A 179 1 ? 8 HELX_P HELX_P9 AA9 ASP A 155 ? VAL A 167 ? ASP A 181 VAL A 193 1 ? 13 HELX_P HELX_P10 AB1 ASN A 184 ? HIS A 200 ? ASN A 210 HIS A 226 1 ? 17 HELX_P HELX_P11 AB2 ASP A 220 ? ALA A 231 ? ASP A 246 ALA A 257 1 ? 12 HELX_P HELX_P12 AB3 SER A 249 ? ALA A 269 ? SER A 275 ALA A 295 1 ? 21 HELX_P HELX_P13 AB4 GLN A 270 ? ALA A 272 ? GLN A 296 ALA A 298 5 ? 3 HELX_P HELX_P14 AB5 THR A 283 ? SER A 287 ? THR A 309 SER A 313 5 ? 5 HELX_P HELX_P15 AB6 TRP A 288 ? TYR A 293 ? TRP A 314 TYR A 319 1 ? 6 HELX_P HELX_P16 AB7 HIS A 309 ? ALA A 321 ? HIS A 335 ALA A 347 1 ? 13 HELX_P HELX_P17 AB8 THR B 7 ? ALA B 13 ? THR B 33 ALA B 39 1 ? 7 HELX_P HELX_P18 AB9 GLY B 22 ? LEU B 27 ? GLY B 48 LEU B 53 1 ? 6 HELX_P HELX_P19 AC1 ASP B 32 ? PHE B 43 ? ASP B 58 PHE B 69 1 ? 12 HELX_P HELX_P20 AC2 LYS B 53 ? GLU B 58 ? LYS B 79 GLU B 84 1 ? 6 HELX_P HELX_P21 AC3 PHE B 66 ? ASN B 79 ? PHE B 92 ASN B 105 1 ? 14 HELX_P HELX_P22 AC4 TRP B 97 ? LEU B 101 ? TRP B 123 LEU B 127 5 ? 5 HELX_P HELX_P23 AC5 THR B 102 ? PHE B 125 ? THR B 128 PHE B 151 1 ? 24 HELX_P HELX_P24 AC6 ASN B 146 ? GLY B 153 ? ASN B 172 GLY B 179 1 ? 8 HELX_P HELX_P25 AC7 ASP B 155 ? VAL B 167 ? ASP B 181 VAL B 193 1 ? 13 HELX_P HELX_P26 AC8 ASN B 184 ? HIS B 200 ? ASN B 210 HIS B 226 1 ? 17 HELX_P HELX_P27 AC9 ASP B 220 ? ALA B 231 ? ASP B 246 ALA B 257 1 ? 12 HELX_P HELX_P28 AD1 SER B 249 ? ALA B 269 ? SER B 275 ALA B 295 1 ? 21 HELX_P HELX_P29 AD2 GLN B 270 ? ALA B 272 ? GLN B 296 ALA B 298 5 ? 3 HELX_P HELX_P30 AD3 THR B 283 ? SER B 287 ? THR B 309 SER B 313 5 ? 5 HELX_P HELX_P31 AD4 TRP B 288 ? TYR B 293 ? TRP B 314 TYR B 319 1 ? 6 HELX_P HELX_P32 AD5 HIS B 309 ? ALA B 321 ? HIS B 335 ALA B 347 1 ? 13 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 267 SG A ? ? 1_555 A CYS 274 SG ? ? A CYS 293 A CYS 300 1_555 ? ? ? ? ? ? ? 2.031 ? disulf2 disulf ? ? B CYS 267 SG A ? ? 1_555 B CYS 274 SG ? ? B CYS 293 B CYS 300 1_555 ? ? ? ? ? ? ? 2.041 ? covale1 covale one ? A ASN 28 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 54 A NAG 402 1_555 ? ? ? ? ? ? ? 1.422 ? covale2 covale one ? A ASN 65 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 91 A NAG 410 1_555 ? ? ? ? ? ? ? 1.426 ? metalc1 metalc ? ? A ASP 80 OD1 ? ? ? 1_555 Z MG . MG ? ? A ASP 106 A MG 424 1_555 ? ? ? ? ? ? ? 2.207 ? covale3 covale one ? A ASN 140 ND2 ? ? ? 1_555 U NAG . C1 ? ? A ASN 166 A NAG 419 1_555 ? ? ? ? ? ? ? 1.441 ? covale4 covale one ? A ASN 185 ND2 ? ? ? 1_555 Y NAG . C1 ? ? A ASN 211 A NAG 423 1_555 ? ? ? ? ? ? ? 1.446 ? covale5 covale one ? B ASN 28 ND2 ? ? ? 1_555 IA NAG . C1 ? ? B ASN 54 B NAG 402 1_555 ? ? ? ? ? ? ? 1.430 ? covale6 covale one ? B ASN 65 ND2 ? ? ? 1_555 OA NAG . C1 ? ? B ASN 91 B NAG 408 1_555 ? ? ? ? ? ? ? 1.429 ? covale7 covale one ? B ASN 140 ND2 ? ? ? 1_555 WA NAG . C1 ? ? B ASN 166 B NAG 416 1_555 ? ? ? ? ? ? ? 1.440 ? covale8 covale one ? B ASN 185 ND2 ? ? ? 1_555 XA NAG . C1 ? ? B ASN 211 B NAG 417 1_555 ? ? ? ? ? ? ? 1.437 ? covale9 covale one ? B ASN 313 ND2 ? ? ? 1_555 ZA NAG . C1 ? ? B ASN 339 B NAG 419 1_555 ? ? ? ? ? ? ? 1.439 ? covale10 covale both ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 402 A NAG 403 1_555 ? ? ? ? ? ? ? 1.424 ? covale11 covale both ? E NAG . O4 ? ? ? 1_555 F BMA . C1 ? ? A NAG 403 A BMA 404 1_555 ? ? ? ? ? ? ? 1.430 ? covale12 covale one ? F BMA . O3 ? ? ? 1_555 G MAN . C1 ? ? A BMA 404 A MAN 405 1_555 ? ? ? ? ? ? ? 1.439 ? covale13 covale one ? F BMA . O6 ? ? ? 1_555 I MAN . C1 ? ? A BMA 404 A MAN 407 1_555 ? ? ? ? ? ? ? 1.438 ? covale14 covale one ? G MAN . O2 ? ? ? 1_555 H MAN . C1 ? ? A MAN 405 A MAN 406 1_555 ? ? ? ? ? ? ? 1.443 ? covale15 covale one ? I MAN . O3 ? ? ? 1_555 J MAN . C1 ? ? A MAN 407 A MAN 408 1_555 ? ? ? ? ? ? ? 1.431 ? covale16 covale one ? I MAN . O6 ? ? ? 1_555 K MAN . C1 ? ? A MAN 407 A MAN 409 1_555 ? ? ? ? ? ? ? 1.435 ? covale17 covale both ? L NAG . O4 ? ? ? 1_555 M NAG . C1 ? ? A NAG 410 A NAG 411 1_555 ? ? ? ? ? ? ? 1.431 ? covale18 covale both ? M NAG . O4 ? ? ? 1_555 N BMA . C1 ? ? A NAG 411 A BMA 412 1_555 ? ? ? ? ? ? ? 1.445 ? covale19 covale one ? N BMA . O3 ? ? ? 1_555 T MAN . C1 ? ? A BMA 412 A MAN 418 1_555 ? ? ? ? ? ? ? 1.444 ? covale20 covale one ? N BMA . O6 ? ? ? 1_555 O MAN . C1 ? ? A BMA 412 A MAN 413 1_555 ? ? ? ? ? ? ? 1.431 ? covale21 covale one ? O MAN . O3 ? ? ? 1_555 P MAN . C1 ? ? A MAN 413 A MAN 414 1_555 ? ? ? ? ? ? ? 1.430 ? covale22 covale one ? O MAN . O6 ? ? ? 1_555 R MAN . C1 ? ? A MAN 413 A MAN 416 1_555 ? ? ? ? ? ? ? 1.437 ? covale23 covale one ? P MAN . O2 ? ? ? 1_555 Q MAN . C1 ? ? A MAN 414 A MAN 415 1_555 ? ? ? ? ? ? ? 1.445 ? covale24 covale one ? R MAN . O2 ? ? ? 1_555 S MAN . C1 ? ? A MAN 416 A MAN 417 1_555 ? ? ? ? ? ? ? 1.438 ? covale25 covale both ? U NAG . O4 ? ? ? 1_555 V NAG . C1 ? ? A NAG 419 A NAG 420 1_555 ? ? ? ? ? ? ? 1.439 ? covale26 covale both ? V NAG . O4 ? ? ? 1_555 W BMA . C1 ? ? A NAG 420 A BMA 421 1_555 ? ? ? ? ? ? ? 1.462 ? covale27 covale one ? W BMA . O3 ? ? ? 1_555 X MAN . C1 ? ? A BMA 421 A MAN 422 1_555 ? ? ? ? ? ? ? 1.458 ? metalc2 metalc ? ? Z MG . MG ? ? ? 1_555 IB HOH . O ? ? A MG 424 B HOH 551 1_555 ? ? ? ? ? ? ? 2.081 ? metalc3 metalc ? ? Z MG . MG ? ? ? 1_555 IB HOH . O ? ? A MG 424 B HOH 555 1_555 ? ? ? ? ? ? ? 2.100 ? metalc4 metalc ? ? Z MG . MG ? ? ? 1_555 IB HOH . O ? ? A MG 424 B HOH 597 1_555 ? ? ? ? ? ? ? 2.110 ? metalc5 metalc ? ? Z MG . MG ? ? ? 1_555 HB HOH . O ? ? A MG 424 A HOH 554 1_555 ? ? ? ? ? ? ? 2.094 ? metalc6 metalc ? ? Z MG . MG ? ? ? 1_555 HB HOH . O ? ? A MG 424 A HOH 677 1_555 ? ? ? ? ? ? ? 2.059 ? covale28 covale both ? IA NAG . O4 ? ? ? 1_555 JA NAG . C1 ? ? B NAG 402 B NAG 403 1_555 ? ? ? ? ? ? ? 1.439 ? covale29 covale both ? JA NAG . O4 ? ? ? 1_555 KA BMA . C1 ? ? B NAG 403 B BMA 404 1_555 ? ? ? ? ? ? ? 1.443 ? covale30 covale one ? KA BMA . O6 ? ? ? 1_555 LA MAN . C1 ? ? B BMA 404 B MAN 405 1_555 ? ? ? ? ? ? ? 1.419 ? covale31 covale one ? LA MAN . O2 ? ? ? 1_555 MA MAN . C1 ? ? B MAN 405 B MAN 406 1_555 ? ? ? ? ? ? ? 1.435 ? covale32 covale one ? MA MAN . O4 ? ? ? 1_555 NA MAN . C1 ? ? B MAN 406 B MAN 407 1_555 ? ? ? ? ? ? ? 1.467 ? covale33 covale both ? OA NAG . O4 ? ? ? 1_555 PA NAG . C1 ? ? B NAG 408 B NAG 409 1_555 ? ? ? ? ? ? ? 1.427 ? covale34 covale both ? PA NAG . O4 ? ? ? 1_555 QA BMA . C1 ? ? B NAG 409 B BMA 410 1_555 ? ? ? ? ? ? ? 1.430 ? covale35 covale one ? QA BMA . O6 ? ? ? 1_555 RA MAN . C1 ? ? B BMA 410 B MAN 411 1_555 ? ? ? ? ? ? ? 1.441 ? covale36 covale one ? RA MAN . O3 ? ? ? 1_555 SA MAN . C1 ? ? B MAN 411 B MAN 412 1_555 ? ? ? ? ? ? ? 1.432 ? covale37 covale one ? RA MAN . O6 ? ? ? 1_555 UA MAN . C1 ? ? B MAN 411 B MAN 414 1_555 ? ? ? ? ? ? ? 1.434 ? covale38 covale one ? SA MAN . O2 ? ? ? 1_555 TA MAN . C1 ? ? B MAN 412 B MAN 413 1_555 ? ? ? ? ? ? ? 1.437 ? covale39 covale one ? UA MAN . O2 ? ? ? 1_555 VA MAN . C1 ? ? B MAN 414 B MAN 415 1_555 ? ? ? ? ? ? ? 1.438 ? covale40 covale both ? XA NAG . O4 ? ? ? 1_555 YA NAG . C1 ? ? B NAG 417 B NAG 418 1_555 ? ? ? ? ? ? ? 1.448 ? metalc7 metalc ? ? AB MG . MG ? ? ? 1_555 HB HOH . O ? ? B MG 420 A HOH 536 1_555 ? ? ? ? ? ? ? 2.076 ? metalc8 metalc ? ? AB MG . MG ? ? ? 1_555 IB HOH . O ? ? B MG 420 B HOH 502 1_555 ? ? ? ? ? ? ? 2.044 ? metalc9 metalc ? ? AB MG . MG ? ? ? 1_555 IB HOH . O ? ? B MG 420 B HOH 572 1_555 ? ? ? ? ? ? ? 2.113 ? metalc10 metalc ? ? AB MG . MG ? ? ? 1_555 IB HOH . O ? ? B MG 420 B HOH 686 1_555 ? ? ? ? ? ? ? 2.092 ? metalc11 metalc ? ? AB MG . MG ? ? ? 1_555 HB HOH . O ? ? B MG 420 A HOH 587 1_555 ? ? ? ? ? ? ? 2.088 ? metalc12 metalc ? ? AB MG . MG ? ? ? 1_555 HB HOH . O ? ? B MG 420 A HOH 524 1_555 ? ? ? ? ? ? ? 2.077 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 PRO 4 A . ? PRO 30 A PHE 5 A ? PHE 31 A 1 -6.16 2 ALA 13 A . ? ALA 39 A PRO 14 A ? PRO 40 A 1 4.40 3 HIS 86 A . ? HIS 112 A ASN 87 A ? ASN 113 A 1 -6.66 4 LEU 246 A . ? LEU 272 A PRO 247 A ? PRO 273 A 1 -3.56 5 ALA 13 B . ? ALA 39 B PRO 14 B ? PRO 40 B 1 9.78 6 HIS 86 B . ? HIS 112 B ASN 87 B ? ASN 113 B 1 -7.93 7 LEU 246 B . ? LEU 272 B PRO 247 B ? PRO 273 B 1 -8.38 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 11 ? AA2 ? 11 ? # 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 3 4 ? parallel AA1 4 5 ? parallel AA1 5 6 ? parallel AA1 6 7 ? parallel AA1 7 8 ? parallel AA1 8 9 ? parallel AA1 9 10 ? parallel AA1 10 11 ? anti-parallel AA2 3 4 ? parallel AA2 4 5 ? parallel AA2 5 6 ? parallel AA2 6 7 ? parallel AA2 7 8 ? parallel AA2 8 9 ? parallel AA2 9 10 ? parallel AA2 10 11 ? 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 HIS A 211 ? PHE A 213 ? HIS A 237 PHE A 239 AA1 2 GLU A 296 ? GLY A 297 ? GLU A 322 GLY A 323 AA1 3 GLY A 205 ? PHE A 208 ? GLY A 231 PHE A 234 AA1 4 LYS A 172 ? ASP A 177 ? LYS A 198 ASP A 203 AA1 5 ALA A 129 ? ASN A 134 ? ALA A 155 ASN A 160 AA1 6 VAL A 82 ? VAL A 89 ? VAL A 108 VAL A 115 AA1 7 GLY A 45 ? PRO A 48 ? GLY A 71 PRO A 74 AA1 8 TYR A 16 ? LEU A 21 ? TYR A 42 LEU A 47 AA1 9 CYS A 274 ? THR A 279 ? CYS A 300 THR A 305 AA1 10 GLU A 234 ? ASN A 245 ? GLU A 260 ASN A 271 AA1 11 GLU A 296 ? GLY A 297 ? GLU A 322 GLY A 323 AA2 1 HIS B 211 ? PHE B 213 ? HIS B 237 PHE B 239 AA2 2 GLU B 296 ? GLY B 297 ? GLU B 322 GLY B 323 AA2 3 GLY B 205 ? PHE B 208 ? GLY B 231 PHE B 234 AA2 4 LYS B 172 ? ASP B 177 ? LYS B 198 ASP B 203 AA2 5 ILE B 127 ? ASN B 134 ? ILE B 153 ASN B 160 AA2 6 VAL B 82 ? VAL B 89 ? VAL B 108 VAL B 115 AA2 7 GLY B 45 ? PRO B 48 ? GLY B 71 PRO B 74 AA2 8 TYR B 16 ? LEU B 21 ? TYR B 42 LEU B 47 AA2 9 CYS B 274 ? THR B 279 ? CYS B 300 THR B 305 AA2 10 GLU B 234 ? ASN B 245 ? GLU B 260 ASN B 271 AA2 11 GLU B 296 ? GLY B 297 ? GLU B 322 GLY B 323 # 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 3 4 O GLY A 207 ? O GLY A 233 N ILE A 175 ? N ILE A 201 AA1 4 5 O TYR A 174 ? O TYR A 200 N TRP A 130 ? N TRP A 156 AA1 5 6 O ALA A 129 ? O ALA A 155 N GLY A 85 ? N GLY A 111 AA1 6 7 O VAL A 82 ? O VAL A 108 N ALA A 46 ? N ALA A 72 AA1 7 8 O THR A 47 ? O THR A 73 N LEU A 21 ? N LEU A 47 AA1 8 9 N GLY A 18 ? N GLY A 44 O ILE A 277 ? O ILE A 303 AA1 9 10 O THR A 278 ? O THR A 304 N LEU A 240 ? N LEU A 266 AA1 10 11 N MET A 244 ? N MET A 270 O GLY A 297 ? O GLY A 323 AA2 3 4 O GLY B 207 ? O GLY B 233 N ILE B 175 ? N ILE B 201 AA2 4 5 O TYR B 174 ? O TYR B 200 N TRP B 130 ? N TRP B 156 AA2 5 6 O ALA B 129 ? O ALA B 155 N GLY B 85 ? N GLY B 111 AA2 6 7 O ARG B 84 ? O ARG B 110 N ALA B 46 ? N ALA B 72 AA2 7 8 O THR B 47 ? O THR B 73 N LEU B 21 ? N LEU B 47 AA2 8 9 N GLY B 18 ? N GLY B 44 O ILE B 277 ? O ILE B 303 AA2 9 10 O THR B 278 ? O THR B 304 N LEU B 240 ? N LEU B 266 AA2 10 11 N MET B 244 ? N MET B 270 O GLY B 297 ? O GLY B 323 # 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 MG 424 ? 6 'binding site for residue MG A 424' AC2 Software A PEG 425 ? 4 'binding site for residue PEG A 425' AC3 Software A P6G 426 ? 6 'binding site for residue P6G A 426' AC4 Software A P6G 427 ? 6 'binding site for residue P6G A 427' AC5 Software A GOL 428 ? 4 'binding site for residue GOL A 428' AC6 Software A GOL 429 ? 2 'binding site for residue GOL A 429' AC7 Software A GOL 430 ? 6 'binding site for residue GOL A 430' AC8 Software B MG 420 ? 7 'binding site for residue MG B 420' AC9 Software B CL 421 ? 2 'binding site for residue CL B 421' AD1 Software B PEG 422 ? 4 'binding site for residue PEG B 422' AD2 Software B PEG 423 ? 2 'binding site for residue PEG B 423' AD3 Software B GOL 424 ? 2 'binding site for residue GOL B 424' AD4 Software B GOL 425 ? 1 'binding site for residue GOL B 425' AD5 Software A ASN 54 ? 30 'binding site for Poly-Saccharide residues NAG A 402 through MAN A 409 bound to ASN A 54' AD6 Software A ASN 91 ? 29 'binding site for Poly-Saccharide residues NAG A 410 through MAN A 418 bound to ASN A 91' AD7 Software A ASN 166 ? 8 'binding site for Poly-Saccharide residues NAG A 419 through MAN A 422 bound to ASN A 166' AD8 Software A NAG 423 ? 5 'binding site for Mono-Saccharide NAG A 423 bound to ASN A 211' AD9 Software B ASN 54 ? 21 'binding site for Poly-Saccharide residues NAG B 402 through MAN B 407 bound to ASN B 54' AE1 Software B ASN 91 ? 31 'binding site for Poly-Saccharide residues NAG B 408 through MAN B 415 bound to ASN B 91' AE2 Software B NAG 416 ? 1 'binding site for Mono-Saccharide NAG B 416 bound to ASN B 166' AE3 Software B ASN 211 ? 3 'binding site for Poly-Saccharide residues NAG B 417 through NAG B 418 bound to ASN B 211' AE4 Software B NAG 419 ? 3 'binding site for Mono-Saccharide NAG B 419 bound to ASN B 339' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 ASP A 80 ? ASP A 106 . ? 1_555 ? 2 AC1 6 HOH HB . ? HOH A 554 . ? 1_555 ? 3 AC1 6 HOH HB . ? HOH A 677 . ? 1_555 ? 4 AC1 6 HOH IB . ? HOH B 551 . ? 1_555 ? 5 AC1 6 HOH IB . ? HOH B 555 . ? 1_555 ? 6 AC1 6 HOH IB . ? HOH B 597 . ? 1_555 ? 7 AC2 4 TYR A 91 ? TYR A 117 . ? 1_555 ? 8 AC2 4 ARG A 144 ? ARG A 170 . ? 1_555 ? 9 AC2 4 ASN A 146 ? ASN A 172 . ? 1_555 ? 10 AC2 4 VAL A 147 ? VAL A 173 . ? 1_555 ? 11 AC3 6 ARG A 9 ? ARG A 35 . ? 1_555 ? 12 AC3 6 PRO A 14 ? PRO A 40 . ? 1_555 ? 13 AC3 6 ASN A 44 ? ASN A 70 . ? 1_555 ? 14 AC3 6 ASP A 80 ? ASP A 106 . ? 1_555 ? 15 AC3 6 VAL A 82 ? VAL A 108 . ? 1_555 ? 16 AC3 6 TYR A 128 ? TYR A 154 . ? 1_555 ? 17 AC4 6 LEU A 26 ? LEU A 52 . ? 1_555 ? 18 AC4 6 ASP A 36 ? ASP A 62 . ? 1_555 ? 19 AC4 6 ALA A 74 ? ALA A 100 . ? 1_555 ? 20 AC4 6 ASP B 36 ? ASP B 62 . ? 1_555 ? 21 AC4 6 PHE B 75 ? PHE B 101 . ? 1_555 ? 22 AC4 6 ALA B 78 ? ALA B 104 . ? 1_555 ? 23 AC5 4 GLU A 254 ? GLU A 280 . ? 1_555 ? 24 AC5 4 ALA A 257 ? ALA A 283 . ? 1_555 ? 25 AC5 4 HOH HB . ? HOH A 595 . ? 1_555 ? 26 AC5 4 GLU B 216 ? GLU B 242 . ? 2_355 ? 27 AC6 2 PRO A 154 ? PRO A 180 . ? 1_555 ? 28 AC6 2 THR B 2 ? THR B 28 . ? 3_454 ? 29 AC7 6 GLU A 135 ? GLU A 161 . ? 1_555 ? 30 AC7 6 TYR A 178 ? TYR A 204 . ? 1_555 ? 31 AC7 6 GLN A 209 ? GLN A 235 . ? 1_555 ? 32 AC7 6 TRP A 288 ? TRP A 314 . ? 1_555 ? 33 AC7 6 HOH HB . ? HOH A 538 . ? 1_555 ? 34 AC7 6 HOH HB . ? HOH A 560 . ? 1_555 ? 35 AC8 7 HOH HB . ? HOH A 524 . ? 1_555 ? 36 AC8 7 HOH HB . ? HOH A 536 . ? 1_555 ? 37 AC8 7 HOH HB . ? HOH A 587 . ? 1_555 ? 38 AC8 7 ASP B 80 ? ASP B 106 . ? 1_555 ? 39 AC8 7 HOH IB . ? HOH B 502 . ? 1_555 ? 40 AC8 7 HOH IB . ? HOH B 572 . ? 1_555 ? 41 AC8 7 HOH IB . ? HOH B 686 . ? 1_555 ? 42 AC9 2 TYR B 298 ? TYR B 324 . ? 1_555 ? 43 AC9 2 MAN LA . ? MAN B 405 . ? 1_555 ? 44 AD1 4 PRO B 14 ? PRO B 40 . ? 1_555 ? 45 AD1 4 ARG B 15 ? ARG B 41 . ? 1_555 ? 46 AD1 4 ALA B 272 ? ALA B 298 . ? 1_555 ? 47 AD1 4 HOH IB . ? HOH B 601 . ? 1_555 ? 48 AD2 2 TYR B 149 ? TYR B 175 . ? 1_555 ? 49 AD2 2 THR B 150 ? THR B 176 . ? 1_555 ? 50 AD3 2 HIS B 211 ? HIS B 237 . ? 1_555 ? 51 AD3 2 ARG B 243 ? ARG B 269 . ? 1_555 ? 52 AD4 1 TYR B 293 ? TYR B 319 . ? 1_555 ? 53 AD5 30 PRO A 24 ? PRO A 50 . ? 1_555 ? 54 AD5 30 HIS A 25 ? HIS A 51 . ? 1_555 ? 55 AD5 30 ASN A 28 ? ASN A 54 . ? 1_555 ? 56 AD5 30 HIS A 31 ? HIS A 57 . ? 1_555 ? 57 AD5 30 ASP A 32 ? ASP A 58 . ? 1_555 ? 58 AD5 30 THR A 169 ? THR A 195 . ? 3_444 ? 59 AD5 30 PRO A 170 ? PRO A 196 . ? 3_444 ? 60 AD5 30 SER A 171 ? SER A 197 . ? 3_444 ? 61 AD5 30 LYS A 172 ? LYS A 198 . ? 3_444 ? 62 AD5 30 ASN A 201 ? ASN A 227 . ? 3_444 ? 63 AD5 30 LEU A 285 ? LEU A 311 . ? 1_555 ? 64 AD5 30 TYR A 286 ? TYR A 312 . ? 1_555 ? 65 AD5 30 PRO A 290 ? PRO A 316 . ? 1_555 ? 66 AD5 30 PRO A 294 ? PRO A 320 . ? 1_555 ? 67 AD5 30 GLY A 295 ? GLY A 321 . ? 1_555 ? 68 AD5 30 ASP A 304 ? ASP A 330 . ? 1_555 ? 69 AD5 30 MAN Q . ? MAN A 415 . ? 1_555 ? 70 AD5 30 HOH HB . ? HOH A 507 . ? 1_555 ? 71 AD5 30 HOH HB . ? HOH A 508 . ? 1_555 ? 72 AD5 30 HOH HB . ? HOH A 535 . ? 1_555 ? 73 AD5 30 HOH HB . ? HOH A 562 . ? 1_555 ? 74 AD5 30 HOH HB . ? HOH A 575 . ? 1_555 ? 75 AD5 30 HOH HB . ? HOH A 583 . ? 1_555 ? 76 AD5 30 HOH HB . ? HOH A 601 . ? 3_444 ? 77 AD5 30 HOH HB . ? HOH A 619 . ? 1_555 ? 78 AD5 30 HOH HB . ? HOH A 637 . ? 1_555 ? 79 AD5 30 HOH HB . ? HOH A 643 . ? 1_555 ? 80 AD5 30 HOH HB . ? HOH A 654 . ? 1_555 ? 81 AD5 30 MAN VA . ? MAN B 415 . ? 3_444 ? 82 AD5 30 HOH IB . ? HOH B 514 . ? 3_444 ? 83 AD6 29 LEU A 27 ? LEU A 53 . ? 1_555 ? 84 AD6 29 HIS A 31 ? HIS A 57 . ? 1_555 ? 85 AD6 29 GLU A 51 ? GLU A 77 . ? 1_555 ? 86 AD6 29 ASN A 65 ? ASN A 91 . ? 1_555 ? 87 AD6 29 NAG D . ? NAG A 402 . ? 1_555 ? 88 AD6 29 HOH HB . ? HOH A 505 . ? 1_555 ? 89 AD6 29 HOH HB . ? HOH A 506 . ? 1_555 ? 90 AD6 29 HOH HB . ? HOH A 516 . ? 1_555 ? 91 AD6 29 HOH HB . ? HOH A 524 . ? 1_555 ? 92 AD6 29 HOH HB . ? HOH A 536 . ? 1_555 ? 93 AD6 29 HOH HB . ? HOH A 587 . ? 1_555 ? 94 AD6 29 HOH HB . ? HOH A 591 . ? 1_555 ? 95 AD6 29 HOH HB . ? HOH A 594 . ? 1_555 ? 96 AD6 29 HOH HB . ? HOH A 609 . ? 1_555 ? 97 AD6 29 HOH HB . ? HOH A 633 . ? 1_555 ? 98 AD6 29 HOH HB . ? HOH A 640 . ? 1_555 ? 99 AD6 29 HOH HB . ? HOH A 660 . ? 1_555 ? 100 AD6 29 HOH HB . ? HOH A 664 . ? 1_555 ? 101 AD6 29 HOH HB . ? HOH A 666 . ? 1_555 ? 102 AD6 29 HOH HB . ? HOH A 679 . ? 1_555 ? 103 AD6 29 HOH HB . ? HOH A 752 . ? 1_555 ? 104 AD6 29 HOH HB . ? HOH A 753 . ? 1_555 ? 105 AD6 29 ASP B 80 ? ASP B 106 . ? 1_555 ? 106 AD6 29 GLU B 123 ? GLU B 149 . ? 1_555 ? 107 AD6 29 SER B 124 ? SER B 150 . ? 1_555 ? 108 AD6 29 ASN B 126 ? ASN B 152 . ? 1_555 ? 109 AD6 29 PRO B 170 ? PRO B 196 . ? 1_555 ? 110 AD6 29 HOH IB . ? HOH B 540 . ? 1_555 ? 111 AD6 29 HOH IB . ? HOH B 605 . ? 1_555 ? 112 AD7 8 ASN A 138 ? ASN A 164 . ? 1_555 ? 113 AD7 8 ASN A 140 ? ASN A 166 . ? 1_555 ? 114 AD7 8 THR A 142 ? THR A 168 . ? 1_555 ? 115 AD7 8 GLU A 145 ? GLU A 171 . ? 1_555 ? 116 AD7 8 HOH HB . ? HOH A 589 . ? 1_555 ? 117 AD7 8 HOH HB . ? HOH A 674 . ? 1_555 ? 118 AD7 8 PRO B 1 ? PRO B 27 . ? 3_454 ? 119 AD7 8 HOH IB . ? HOH B 526 . ? 2_455 ? 120 AD8 5 ASN A 140 ? ASN A 166 . ? 1_555 ? 121 AD8 5 ASN A 185 ? ASN A 211 . ? 1_555 ? 122 AD8 5 HOH HB . ? HOH A 504 . ? 1_555 ? 123 AD8 5 HOH HB . ? HOH A 657 . ? 1_555 ? 124 AD8 5 PHE B 5 ? PHE B 31 . ? 3_454 ? 125 AD9 21 PRO B 24 ? PRO B 50 . ? 1_555 ? 126 AD9 21 HIS B 25 ? HIS B 51 . ? 1_555 ? 127 AD9 21 ASN B 28 ? ASN B 54 . ? 1_555 ? 128 AD9 21 HIS B 31 ? HIS B 57 . ? 1_555 ? 129 AD9 21 ASP B 32 ? ASP B 58 . ? 1_555 ? 130 AD9 21 LEU B 246 ? LEU B 272 . ? 1_555 ? 131 AD9 21 LEU B 285 ? LEU B 311 . ? 1_555 ? 132 AD9 21 TYR B 286 ? TYR B 312 . ? 1_555 ? 133 AD9 21 PRO B 290 ? PRO B 316 . ? 1_555 ? 134 AD9 21 SER B 291 ? SER B 317 . ? 1_555 ? 135 AD9 21 PRO B 294 ? PRO B 320 . ? 1_555 ? 136 AD9 21 GLY B 295 ? GLY B 321 . ? 1_555 ? 137 AD9 21 ASP B 304 ? ASP B 330 . ? 1_555 ? 138 AD9 21 MAN TA . ? MAN B 413 . ? 1_555 ? 139 AD9 21 CL BB . ? CL B 421 . ? 1_555 ? 140 AD9 21 HOH IB . ? HOH B 523 . ? 1_555 ? 141 AD9 21 HOH IB . ? HOH B 529 . ? 1_555 ? 142 AD9 21 HOH IB . ? HOH B 613 . ? 1_555 ? 143 AD9 21 HOH IB . ? HOH B 624 . ? 1_555 ? 144 AD9 21 HOH IB . ? HOH B 642 . ? 1_555 ? 145 AD9 21 HOH IB . ? HOH B 667 . ? 1_555 ? 146 AE1 31 ALA A 77 ? ALA A 103 . ? 1_555 ? 147 AE1 31 ASP A 80 ? ASP A 106 . ? 1_555 ? 148 AE1 31 GLU A 123 ? GLU A 149 . ? 1_555 ? 149 AE1 31 SER A 124 ? SER A 150 . ? 1_555 ? 150 AE1 31 PHE A 125 ? PHE A 151 . ? 1_555 ? 151 AE1 31 ASN A 126 ? ASN A 152 . ? 1_555 ? 152 AE1 31 PRO A 170 ? PRO A 196 . ? 1_555 ? 153 AE1 31 MAN K . ? MAN A 409 . ? 3_454 ? 154 AE1 31 HOH HB . ? HOH A 586 . ? 1_555 ? 155 AE1 31 LEU B 27 ? LEU B 53 . ? 1_555 ? 156 AE1 31 ASN B 28 ? ASN B 54 . ? 1_555 ? 157 AE1 31 HIS B 31 ? HIS B 57 . ? 1_555 ? 158 AE1 31 GLU B 51 ? GLU B 77 . ? 1_555 ? 159 AE1 31 ASN B 65 ? ASN B 91 . ? 1_555 ? 160 AE1 31 NAG IA . ? NAG B 402 . ? 1_555 ? 161 AE1 31 HOH IB . ? HOH B 514 . ? 1_555 ? 162 AE1 31 HOH IB . ? HOH B 517 . ? 1_555 ? 163 AE1 31 HOH IB . ? HOH B 527 . ? 1_555 ? 164 AE1 31 HOH IB . ? HOH B 530 . ? 1_555 ? 165 AE1 31 HOH IB . ? HOH B 548 . ? 1_555 ? 166 AE1 31 HOH IB . ? HOH B 551 . ? 1_555 ? 167 AE1 31 HOH IB . ? HOH B 555 . ? 1_555 ? 168 AE1 31 HOH IB . ? HOH B 574 . ? 1_555 ? 169 AE1 31 HOH IB . ? HOH B 575 . ? 1_555 ? 170 AE1 31 HOH IB . ? HOH B 586 . ? 1_555 ? 171 AE1 31 HOH IB . ? HOH B 597 . ? 1_555 ? 172 AE1 31 HOH IB . ? HOH B 607 . ? 1_555 ? 173 AE1 31 HOH IB . ? HOH B 617 . ? 1_555 ? 174 AE1 31 HOH IB . ? HOH B 626 . ? 1_555 ? 175 AE1 31 HOH IB . ? HOH B 653 . ? 1_555 ? 176 AE1 31 HOH IB . ? HOH B 772 . ? 1_555 ? 177 AE2 1 ASN B 140 ? ASN B 166 . ? 1_555 ? 178 AE3 3 SER A 291 ? SER A 317 . ? 2_454 ? 179 AE3 3 THR A 292 ? THR A 318 . ? 2_454 ? 180 AE3 3 ASN B 185 ? ASN B 211 . ? 1_555 ? 181 AE4 3 PRO B 310 ? PRO B 336 . ? 1_555 ? 182 AE4 3 ASN B 313 ? ASN B 339 . ? 1_555 ? 183 AE4 3 HOH IB . ? HOH B 501 . ? 1_555 ? # _atom_sites.entry_id 4XX6 _atom_sites.fract_transf_matrix[1][1] 0.019079 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.010066 _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] 0.006790 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CL MG N O S X # 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 . PRO A 1 4 ? -47.544 2.676 -35.612 1.00 97.82 ? 30 PRO A N 1 ATOM 2 C CA . PRO A 1 4 ? -48.384 2.804 -34.419 1.00 99.87 ? 30 PRO A CA 1 ATOM 3 C C . PRO A 1 4 ? -48.886 1.482 -33.847 1.00 99.49 ? 30 PRO A C 1 ATOM 4 O O . PRO A 1 4 ? -49.672 0.814 -34.524 1.00 94.79 ? 30 PRO A O 1 ATOM 5 C CB . PRO A 1 4 ? -49.545 3.640 -34.942 1.00 99.25 ? 30 PRO A CB 1 ATOM 6 C CG . PRO A 1 4 ? -48.881 4.588 -35.857 1.00 96.85 ? 30 PRO A CG 1 ATOM 7 C CD . PRO A 1 4 ? -47.806 3.772 -36.566 1.00 94.61 ? 30 PRO A CD 1 ATOM 8 N N . PHE A 1 5 ? -48.464 1.090 -32.640 1.00 100.77 ? 31 PHE A N 1 ATOM 9 C CA . PHE A 1 5 ? -47.437 1.754 -31.820 1.00 95.34 ? 31 PHE A CA 1 ATOM 10 C C . PHE A 1 5 ? -46.245 0.811 -31.599 1.00 82.79 ? 31 PHE A C 1 ATOM 11 O O . PHE A 1 5 ? -45.480 0.971 -30.648 1.00 76.87 ? 31 PHE A O 1 ATOM 12 C CB . PHE A 1 5 ? -48.000 2.155 -30.448 1.00 100.88 ? 31 PHE A CB 1 ATOM 13 C CG . PHE A 1 5 ? -49.067 3.225 -30.487 1.00 104.89 ? 31 PHE A CG 1 ATOM 14 C CD1 . PHE A 1 5 ? -49.144 4.138 -31.528 1.00 104.51 ? 31 PHE A CD1 1 ATOM 15 C CD2 . PHE A 1 5 ? -49.997 3.312 -29.460 1.00 104.46 ? 31 PHE A CD2 1 ATOM 16 C CE1 . PHE A 1 5 ? -50.127 5.115 -31.542 1.00 105.83 ? 31 PHE A CE1 1 ATOM 17 C CE2 . PHE A 1 5 ? -50.978 4.283 -29.466 1.00 104.66 ? 31 PHE A CE2 1 ATOM 18 C CZ . PHE A 1 5 ? -51.045 5.186 -30.508 1.00 106.48 ? 31 PHE A CZ 1 ATOM 19 N N . GLU A 1 6 ? -46.108 -0.176 -32.481 1.00 71.95 ? 32 GLU A N 1 ATOM 20 C CA . GLU A 1 6 ? -45.249 -1.344 -32.259 1.00 49.46 ? 32 GLU A CA 1 ATOM 21 C C . GLU A 1 6 ? -43.735 -1.083 -32.381 1.00 37.06 ? 32 GLU A C 1 ATOM 22 O O . GLU A 1 6 ? -42.925 -1.873 -31.902 1.00 37.34 ? 32 GLU A O 1 ATOM 23 C CB . GLU A 1 6 ? -45.662 -2.450 -33.239 1.00 47.64 ? 32 GLU A CB 1 ATOM 24 C CG . GLU A 1 6 ? -45.004 -3.796 -33.008 1.00 55.45 ? 32 GLU A CG 1 ATOM 25 C CD . GLU A 1 6 ? -45.312 -4.788 -34.112 1.00 65.75 ? 32 GLU A CD 1 ATOM 26 O OE1 . GLU A 1 6 ? -46.506 -4.966 -34.435 1.00 64.45 ? 32 GLU A OE1 1 ATOM 27 O OE2 . GLU A 1 6 ? -44.361 -5.386 -34.662 1.00 71.00 ? 32 GLU A OE2 1 ATOM 28 N N . THR A 1 7 ? -43.352 0.019 -33.016 1.00 28.46 ? 33 THR A N 1 ATOM 29 C CA . THR A 1 7 ? -41.939 0.329 -33.205 1.00 22.06 ? 33 THR A CA 1 ATOM 30 C C . THR A 1 7 ? -41.507 1.520 -32.349 1.00 23.78 ? 33 THR A C 1 ATOM 31 O O . THR A 1 7 ? -42.339 2.313 -31.881 1.00 18.27 ? 33 THR A O 1 ATOM 32 C CB . THR A 1 7 ? -41.635 0.645 -34.672 1.00 22.04 ? 33 THR A CB 1 ATOM 33 O OG1 . THR A 1 7 ? -42.384 1.803 -35.053 1.00 19.42 ? 33 THR A OG1 1 ATOM 34 C CG2 . THR A 1 7 ? -42.023 -0.533 -35.583 1.00 21.99 ? 33 THR A CG2 1 ATOM 35 N N . LEU A 1 8 ? -40.201 1.652 -32.155 1.00 19.37 ? 34 LEU A N 1 ATOM 36 C CA . LEU A 1 8 ? -39.656 2.782 -31.415 1.00 15.99 ? 34 LEU A CA 1 ATOM 37 C C . LEU A 1 8 ? -39.997 4.081 -32.123 1.00 19.38 ? 34 LEU A C 1 ATOM 38 O O . LEU A 1 8 ? -40.426 5.041 -31.493 1.00 18.47 ? 34 LEU A O 1 ATOM 39 C CB . LEU A 1 8 ? -38.137 2.652 -31.265 1.00 14.90 ? 34 LEU A CB 1 ATOM 40 C CG . LEU A 1 8 ? -37.616 1.482 -30.424 1.00 17.19 ? 34 LEU A CG 1 ATOM 41 C CD1 . LEU A 1 8 ? -36.119 1.287 -30.710 1.00 17.62 ? 34 LEU A CD1 1 ATOM 42 C CD2 . LEU A 1 8 ? -37.850 1.735 -28.934 1.00 17.45 ? 34 LEU A CD2 1 ATOM 43 N N . ARG A 1 9 ? -39.807 4.107 -33.441 1.00 15.65 ? 35 ARG A N 1 ATOM 44 C CA . ARG A 1 9 ? -40.064 5.328 -34.182 1.00 19.06 ? 35 ARG A CA 1 ATOM 45 C C . ARG A 1 9 ? -41.546 5.718 -34.084 1.00 20.67 ? 35 ARG A C 1 ATOM 46 O O . ARG A 1 9 ? -41.862 6.895 -33.946 1.00 17.26 ? 35 ARG A O 1 ATOM 47 C CB . ARG A 1 9 ? -39.630 5.178 -35.641 1.00 20.00 ? 35 ARG A CB 1 ATOM 48 C CG . ARG A 1 9 ? -40.309 4.040 -36.392 1.00 22.81 ? 35 ARG A CG 1 ATOM 49 C CD . ARG A 1 9 ? -39.741 3.928 -37.797 1.00 23.51 ? 35 ARG A CD 1 ATOM 50 N NE . ARG A 1 9 ? -40.152 5.047 -38.637 1.00 24.52 ? 35 ARG A NE 1 ATOM 51 C CZ . ARG A 1 9 ? -39.618 5.333 -39.822 1.00 27.74 ? 35 ARG A CZ 1 ATOM 52 N NH1 . ARG A 1 9 ? -38.622 4.601 -40.301 1.00 19.51 ? 35 ARG A NH1 1 ATOM 53 N NH2 . ARG A 1 9 ? -40.066 6.367 -40.524 1.00 28.97 ? 35 ARG A NH2 1 ATOM 54 N N . ALA A 1 10 ? -42.453 4.743 -34.113 1.00 19.77 ? 36 ALA A N 1 ATOM 55 C CA . ALA A 1 10 ? -43.880 5.073 -34.036 1.00 23.41 ? 36 ALA A CA 1 ATOM 56 C C . ALA A 1 10 ? -44.237 5.576 -32.641 1.00 26.73 ? 36 ALA A C 1 ATOM 57 O O . ALA A 1 10 ? -44.949 6.573 -32.485 1.00 22.01 ? 36 ALA A O 1 ATOM 58 C CB . ALA A 1 10 ? -44.748 3.862 -34.406 1.00 19.87 ? 36 ALA A CB 1 ATOM 59 N N . ALA A 1 11 ? -43.730 4.884 -31.628 1.00 22.01 ? 37 ALA A N 1 ATOM 60 C CA . ALA A 1 11 ? -44.030 5.220 -30.242 1.00 24.80 ? 37 ALA A CA 1 ATOM 61 C C . ALA A 1 11 ? -43.480 6.590 -29.850 1.00 24.43 ? 37 ALA A C 1 ATOM 62 O O . ALA A 1 11 ? -44.069 7.284 -29.019 1.00 23.13 ? 37 ALA A O 1 ATOM 63 C CB . ALA A 1 11 ? -43.486 4.154 -29.317 1.00 20.08 ? 37 ALA A CB 1 ATOM 64 N N . ALA A 1 12 ? -42.355 6.978 -30.449 1.00 18.94 ? 38 ALA A N 1 ATOM 65 C CA . ALA A 1 12 ? -41.687 8.223 -30.083 1.00 18.00 ? 38 ALA A CA 1 ATOM 66 C C . ALA A 1 12 ? -42.377 9.484 -30.623 1.00 24.49 ? 38 ALA A C 1 ATOM 67 O O . ALA A 1 12 ? -42.217 10.562 -30.048 1.00 19.41 ? 38 ALA A O 1 ATOM 68 C CB . ALA A 1 12 ? -40.226 8.192 -30.556 1.00 16.50 ? 38 ALA A CB 1 ATOM 69 N N . ALA A 1 13 ? -43.125 9.354 -31.720 1.00 22.87 ? 39 ALA A N 1 ATOM 70 C CA . ALA A 1 13 ? -43.711 10.520 -32.402 1.00 32.39 ? 39 ALA A CA 1 ATOM 71 C C . ALA A 1 13 ? -44.408 11.463 -31.415 1.00 29.03 ? 39 ALA A C 1 ATOM 72 O O . ALA A 1 13 ? -45.083 11.012 -30.487 1.00 27.38 ? 39 ALA A O 1 ATOM 73 C CB . ALA A 1 13 ? -44.686 10.069 -33.493 1.00 34.31 ? 39 ALA A CB 1 ATOM 74 N N . PRO A 1 14 ? -44.216 12.781 -31.589 1.00 22.33 ? 40 PRO A N 1 ATOM 75 C CA . PRO A 1 14 ? -43.486 13.456 -32.667 1.00 21.05 ? 40 PRO A CA 1 ATOM 76 C C . PRO A 1 14 ? -41.964 13.583 -32.458 1.00 22.69 ? 40 PRO A C 1 ATOM 77 O O . PRO A 1 14 ? -41.309 14.174 -33.308 1.00 23.27 ? 40 PRO A O 1 ATOM 78 C CB . PRO A 1 14 ? -44.118 14.841 -32.674 1.00 26.62 ? 40 PRO A CB 1 ATOM 79 C CG . PRO A 1 14 ? -44.391 15.090 -31.230 1.00 28.47 ? 40 PRO A CG 1 ATOM 80 C CD . PRO A 1 14 ? -44.816 13.752 -30.657 1.00 27.12 ? 40 PRO A CD 1 ATOM 81 N N . ARG A 1 15 ? -41.419 13.076 -31.357 1.00 21.67 ? 41 ARG A N 1 ATOM 82 C CA . ARG A 1 15 ? -39.964 13.030 -31.195 1.00 18.77 ? 41 ARG A CA 1 ATOM 83 C C . ARG A 1 15 ? -39.384 11.987 -32.132 1.00 19.85 ? 41 ARG A C 1 ATOM 84 O O . ARG A 1 15 ? -40.091 11.075 -32.541 1.00 16.31 ? 41 ARG A O 1 ATOM 85 C CB . ARG A 1 15 ? -39.574 12.692 -29.751 1.00 19.55 ? 41 ARG A CB 1 ATOM 86 C CG . ARG A 1 15 ? -40.096 13.678 -28.719 1.00 20.29 ? 41 ARG A CG 1 ATOM 87 C CD . ARG A 1 15 ? -39.604 13.316 -27.313 1.00 18.03 ? 41 ARG A CD 1 ATOM 88 N NE . ARG A 1 15 ? -40.067 14.310 -26.351 1.00 21.78 ? 41 ARG A NE 1 ATOM 89 C CZ . ARG A 1 15 ? -41.264 14.283 -25.785 1.00 27.13 ? 41 ARG A CZ 1 ATOM 90 N NH1 . ARG A 1 15 ? -42.109 13.309 -26.077 1.00 27.97 ? 41 ARG A NH1 1 ATOM 91 N NH2 . ARG A 1 15 ? -41.616 15.228 -24.934 1.00 32.45 ? 41 ARG A NH2 1 ATOM 92 N N . TYR A 1 16 ? -38.099 12.093 -32.456 1.00 14.90 ? 42 TYR A N 1 ATOM 93 C CA . TYR A 1 16 ? -37.475 11.044 -33.254 1.00 14.03 ? 42 TYR A CA 1 ATOM 94 C C . TYR A 1 16 ? -36.837 10.019 -32.316 1.00 15.35 ? 42 TYR A C 1 ATOM 95 O O . TYR A 1 16 ? -36.573 10.298 -31.147 1.00 13.68 ? 42 TYR A O 1 ATOM 96 C CB . TYR A 1 16 ? -36.419 11.601 -34.220 1.00 13.25 ? 42 TYR A CB 1 ATOM 97 C CG . TYR A 1 16 ? -35.245 12.253 -33.523 1.00 12.72 ? 42 TYR A CG 1 ATOM 98 C CD1 . TYR A 1 16 ? -34.191 11.486 -33.005 1.00 11.98 ? 42 TYR A CD1 1 ATOM 99 C CD2 . TYR A 1 16 ? -35.177 13.640 -33.390 1.00 14.17 ? 42 TYR A CD2 1 ATOM 100 C CE1 . TYR A 1 16 ? -33.125 12.071 -32.358 1.00 11.62 ? 42 TYR A CE1 1 ATOM 101 C CE2 . TYR A 1 16 ? -34.102 14.244 -32.739 1.00 13.98 ? 42 TYR A CE2 1 ATOM 102 C CZ . TYR A 1 16 ? -33.082 13.450 -32.229 1.00 23.17 ? 42 TYR A CZ 1 ATOM 103 O OH . TYR A 1 16 ? -32.016 14.037 -31.588 1.00 11.82 ? 42 TYR A OH 1 ATOM 104 N N . PHE A 1 17 ? -36.607 8.823 -32.833 1.00 14.80 ? 43 PHE A N 1 ATOM 105 C CA . PHE A 1 17 ? -35.824 7.842 -32.106 1.00 13.08 ? 43 PHE A CA 1 ATOM 106 C C . PHE A 1 17 ? -34.756 7.335 -33.056 1.00 12.07 ? 43 PHE A C 1 ATOM 107 O O . PHE A 1 17 ? -35.064 6.688 -34.053 1.00 13.30 ? 43 PHE A O 1 ATOM 108 C CB . PHE A 1 17 ? -36.681 6.698 -31.576 1.00 13.39 ? 43 PHE A CB 1 ATOM 109 C CG . PHE A 1 17 ? -36.051 5.996 -30.412 1.00 15.85 ? 43 PHE A CG 1 ATOM 110 C CD1 . PHE A 1 17 ? -35.017 5.085 -30.611 1.00 14.50 ? 43 PHE A CD1 1 ATOM 111 C CD2 . PHE A 1 17 ? -36.451 6.278 -29.122 1.00 14.66 ? 43 PHE A CD2 1 ATOM 112 C CE1 . PHE A 1 17 ? -34.418 4.449 -29.530 1.00 16.45 ? 43 PHE A CE1 1 ATOM 113 C CE2 . PHE A 1 17 ? -35.857 5.650 -28.047 1.00 17.84 ? 43 PHE A CE2 1 ATOM 114 C CZ . PHE A 1 17 ? -34.833 4.737 -28.258 1.00 13.47 ? 43 PHE A CZ 1 ATOM 115 N N . GLY A 1 18 ? -33.500 7.663 -32.761 1.00 11.92 ? 44 GLY A N 1 ATOM 116 C CA . GLY A 1 18 ? -32.437 7.462 -33.728 1.00 10.55 ? 44 GLY A CA 1 ATOM 117 C C . GLY A 1 18 ? -31.376 6.463 -33.306 1.00 11.29 ? 44 GLY A C 1 ATOM 118 O O . GLY A 1 18 ? -31.412 5.924 -32.192 1.00 10.47 ? 44 GLY A O 1 ATOM 119 N N . ALA A 1 19 ? -30.421 6.230 -34.205 1.00 9.74 ? 45 ALA A N 1 ATOM 120 C CA . ALA A 1 19 ? -29.308 5.329 -33.929 1.00 10.89 ? 45 ALA A CA 1 ATOM 121 C C . ALA A 1 19 ? -28.027 5.822 -34.570 1.00 9.10 ? 45 ALA A C 1 ATOM 122 O O . ALA A 1 19 ? -28.052 6.380 -35.659 1.00 9.22 ? 45 ALA A O 1 ATOM 123 C CB . ALA A 1 19 ? -29.623 3.910 -34.451 1.00 9.80 ? 45 ALA A CB 1 ATOM 124 N N . ALA A 1 20 ? -26.905 5.570 -33.914 1.00 9.03 ? 46 ALA A N 1 ATOM 125 C CA . ALA A 1 20 ? -25.612 5.738 -34.558 1.00 10.32 ? 46 ALA A CA 1 ATOM 126 C C . ALA A 1 20 ? -25.491 4.681 -35.642 1.00 11.44 ? 46 ALA A C 1 ATOM 127 O O . ALA A 1 20 ? -25.635 3.495 -35.361 1.00 12.47 ? 46 ALA A O 1 ATOM 128 C CB . ALA A 1 20 ? -24.482 5.587 -33.551 1.00 8.90 ? 46 ALA A CB 1 ATOM 129 N N . LEU A 1 21 ? -25.215 5.104 -36.865 1.00 9.73 ? 47 LEU A N 1 ATOM 130 C CA . LEU A 1 21 ? -25.074 4.174 -37.982 1.00 8.88 ? 47 LEU A CA 1 ATOM 131 C C . LEU A 1 21 ? -23.663 4.262 -38.526 1.00 12.17 ? 47 LEU A C 1 ATOM 132 O O . LEU A 1 21 ? -23.177 5.347 -38.872 1.00 15.22 ? 47 LEU A O 1 ATOM 133 C CB . LEU A 1 21 ? -26.076 4.489 -39.091 1.00 10.16 ? 47 LEU A CB 1 ATOM 134 C CG . LEU A 1 21 ? -27.553 4.476 -38.704 1.00 12.35 ? 47 LEU A CG 1 ATOM 135 C CD1 . LEU A 1 21 ? -28.398 4.898 -39.916 1.00 11.23 ? 47 LEU A CD1 1 ATOM 136 C CD2 . LEU A 1 21 ? -27.972 3.104 -38.147 1.00 9.32 ? 47 LEU A CD2 1 ATOM 137 N N . GLY A 1 22 ? -22.993 3.122 -38.577 1.00 9.95 ? 48 GLY A N 1 ATOM 138 C CA . GLY A 1 22 ? -21.651 3.071 -39.130 1.00 11.97 ? 48 GLY A CA 1 ATOM 139 C C . GLY A 1 22 ? -21.682 2.606 -40.565 1.00 11.70 ? 48 GLY A C 1 ATOM 140 O O . GLY A 1 22 ? -22.406 1.651 -40.914 1.00 11.50 ? 48 GLY A O 1 ATOM 141 N N . VAL A 1 23 ? -20.888 3.269 -41.403 1.00 9.87 ? 49 VAL A N 1 ATOM 142 C CA . VAL A 1 23 ? -20.768 2.872 -42.809 1.00 13.28 ? 49 VAL A CA 1 ATOM 143 C C . VAL A 1 23 ? -20.465 1.381 -43.019 1.00 10.80 ? 49 VAL A C 1 ATOM 144 O O . VAL A 1 23 ? -21.119 0.742 -43.849 1.00 11.02 ? 49 VAL A O 1 ATOM 145 C CB . VAL A 1 23 ? -19.700 3.731 -43.545 1.00 12.71 ? 49 VAL A CB 1 ATOM 146 C CG1 . VAL A 1 23 ? -19.336 3.103 -44.891 1.00 16.34 ? 49 VAL A CG1 1 ATOM 147 C CG2 . VAL A 1 23 ? -20.247 5.132 -43.764 1.00 17.17 ? 49 VAL A CG2 1 ATOM 148 N N . PRO A 1 24 ? -19.510 0.803 -42.261 1.00 12.85 ? 50 PRO A N 1 ATOM 149 C CA . PRO A 1 24 ? -19.248 -0.616 -42.526 1.00 11.82 ? 50 PRO A CA 1 ATOM 150 C C . PRO A 1 24 ? -20.466 -1.520 -42.263 1.00 11.75 ? 50 PRO A C 1 ATOM 151 O O . PRO A 1 24 ? -20.590 -2.524 -42.947 1.00 12.91 ? 50 PRO A O 1 ATOM 152 C CB . PRO A 1 24 ? -18.094 -0.953 -41.556 1.00 12.25 ? 50 PRO A CB 1 ATOM 153 C CG . PRO A 1 24 ? -17.442 0.380 -41.281 1.00 21.74 ? 50 PRO A CG 1 ATOM 154 C CD . PRO A 1 24 ? -18.589 1.343 -41.239 1.00 14.38 ? 50 PRO A CD 1 ATOM 155 N N . HIS A 1 25 ? -21.338 -1.177 -41.314 1.00 13.02 ? 51 HIS A N 1 ATOM 156 C CA . HIS A 1 25 ? -22.531 -1.999 -41.046 1.00 11.57 ? 51 HIS A CA 1 ATOM 157 C C . HIS A 1 25 ? -23.614 -1.788 -42.102 1.00 11.15 ? 51 HIS A C 1 ATOM 158 O O . HIS A 1 25 ? -24.260 -2.742 -42.526 1.00 12.87 ? 51 HIS A O 1 ATOM 159 C CB . HIS A 1 25 ? -23.101 -1.704 -39.645 1.00 10.94 ? 51 HIS A CB 1 ATOM 160 C CG . HIS A 1 25 ? -22.068 -1.733 -38.565 1.00 11.10 ? 51 HIS A CG 1 ATOM 161 N ND1 . HIS A 1 25 ? -21.210 -2.800 -38.384 1.00 17.91 ? 51 HIS A ND1 1 ATOM 162 C CD2 . HIS A 1 25 ? -21.735 -0.816 -37.623 1.00 16.45 ? 51 HIS A CD2 1 ATOM 163 C CE1 . HIS A 1 25 ? -20.394 -2.538 -37.375 1.00 15.45 ? 51 HIS A CE1 1 ATOM 164 N NE2 . HIS A 1 25 ? -20.690 -1.341 -36.898 1.00 15.03 ? 51 HIS A NE2 1 ATOM 165 N N . LEU A 1 26 ? -23.818 -0.539 -42.509 1.00 10.68 ? 52 LEU A N 1 ATOM 166 C CA . LEU A 1 26 ? -24.764 -0.219 -43.570 1.00 10.67 ? 52 LEU A CA 1 ATOM 167 C C . LEU A 1 26 ? -24.423 -0.964 -44.856 1.00 11.27 ? 52 LEU A C 1 ATOM 168 O O . LEU A 1 26 ? -25.308 -1.485 -45.538 1.00 11.57 ? 52 LEU A O 1 ATOM 169 C CB . LEU A 1 26 ? -24.784 1.290 -43.844 1.00 10.27 ? 52 LEU A CB 1 ATOM 170 C CG . LEU A 1 26 ? -25.357 2.176 -42.750 1.00 15.63 ? 52 LEU A CG 1 ATOM 171 C CD1 . LEU A 1 26 ? -25.225 3.637 -43.140 1.00 14.98 ? 52 LEU A CD1 1 ATOM 172 C CD2 . LEU A 1 26 ? -26.823 1.817 -42.500 1.00 15.67 ? 52 LEU A CD2 1 ATOM 173 N N . LEU A 1 27 ? -23.137 -1.023 -45.182 1.00 11.55 ? 53 LEU A N 1 ATOM 174 C CA . LEU A 1 27 ? -22.707 -1.695 -46.405 1.00 12.26 ? 53 LEU A CA 1 ATOM 175 C C . LEU A 1 27 ? -22.583 -3.204 -46.259 1.00 12.94 ? 53 LEU A C 1 ATOM 176 O O . LEU A 1 27 ? -22.173 -3.891 -47.203 1.00 13.65 ? 53 LEU A O 1 ATOM 177 C CB . LEU A 1 27 ? -21.373 -1.135 -46.873 1.00 20.13 ? 53 LEU A CB 1 ATOM 178 C CG . LEU A 1 27 ? -21.348 0.361 -47.177 1.00 29.60 ? 53 LEU A CG 1 ATOM 179 C CD1 . LEU A 1 27 ? -20.081 0.706 -47.945 1.00 22.42 ? 53 LEU A CD1 1 ATOM 180 C CD2 . LEU A 1 27 ? -22.607 0.810 -47.921 1.00 25.48 ? 53 LEU A CD2 1 ATOM 181 N N . ASN A 1 28 ? -22.938 -3.720 -45.087 1.00 12.77 ? 54 ASN A N 1 ATOM 182 C CA . ASN A 1 28 ? -22.880 -5.158 -44.815 1.00 13.80 ? 54 ASN A CA 1 ATOM 183 C C . ASN A 1 28 ? -24.244 -5.806 -45.014 1.00 19.79 ? 54 ASN A C 1 ATOM 184 O O . ASN A 1 28 ? -24.514 -6.864 -44.441 1.00 14.54 ? 54 ASN A O 1 ATOM 185 C CB . ASN A 1 28 ? -22.423 -5.394 -43.378 1.00 13.45 ? 54 ASN A CB 1 ATOM 186 C CG . ASN A 1 28 ? -21.724 -6.726 -43.165 1.00 16.82 ? 54 ASN A CG 1 ATOM 187 O OD1 . ASN A 1 28 ? -21.152 -7.336 -44.072 1.00 15.21 ? 54 ASN A OD1 1 ATOM 188 N ND2 . ASN A 1 28 ? -21.766 -7.176 -41.930 1.00 14.58 ? 54 ASN A ND2 1 ATOM 189 N N . PHE A 1 29 ? -25.106 -5.150 -45.793 1.00 13.37 ? 55 PHE A N 1 ATOM 190 C CA . PHE A 1 29 ? -26.496 -5.585 -45.973 1.00 13.57 ? 55 PHE A CA 1 ATOM 191 C C . PHE A 1 29 ? -26.605 -7.022 -46.487 1.00 25.97 ? 55 PHE A C 1 ATOM 192 O O . PHE A 1 29 ? -27.538 -7.743 -46.151 1.00 16.20 ? 55 PHE A O 1 ATOM 193 C CB . PHE A 1 29 ? -27.222 -4.637 -46.935 1.00 14.56 ? 55 PHE A CB 1 ATOM 194 C CG . PHE A 1 29 ? -28.656 -5.021 -47.216 1.00 16.96 ? 55 PHE A CG 1 ATOM 195 C CD1 . PHE A 1 29 ? -29.602 -5.029 -46.207 1.00 13.48 ? 55 PHE A CD1 1 ATOM 196 C CD2 . PHE A 1 29 ? -29.062 -5.334 -48.504 1.00 20.48 ? 55 PHE A CD2 1 ATOM 197 C CE1 . PHE A 1 29 ? -30.926 -5.363 -46.472 1.00 19.62 ? 55 PHE A CE1 1 ATOM 198 C CE2 . PHE A 1 29 ? -30.383 -5.670 -48.775 1.00 23.67 ? 55 PHE A CE2 1 ATOM 199 C CZ . PHE A 1 29 ? -31.316 -5.688 -47.755 1.00 20.08 ? 55 PHE A CZ 1 ATOM 200 N N . THR A 1 30 ? -25.648 -7.441 -47.301 1.00 15.11 ? 56 THR A N 1 ATOM 201 C CA . THR A 1 30 ? -25.656 -8.799 -47.815 1.00 16.18 ? 56 THR A CA 1 ATOM 202 C C . THR A 1 30 ? -25.467 -9.818 -46.692 1.00 18.41 ? 56 THR A C 1 ATOM 203 O O . THR A 1 30 ? -26.227 -10.787 -46.585 1.00 21.19 ? 56 THR A O 1 ATOM 204 C CB . THR A 1 30 ? -24.560 -8.991 -48.894 1.00 24.02 ? 56 THR A CB 1 ATOM 205 O OG1 . THR A 1 30 ? -24.892 -8.201 -50.045 1.00 27.61 ? 56 THR A OG1 1 ATOM 206 C CG2 . THR A 1 30 ? -24.462 -10.444 -49.304 1.00 25.76 ? 56 THR A CG2 1 ATOM 207 N N . HIS A 1 31 ? -24.465 -9.605 -45.850 1.00 16.42 ? 57 HIS A N 1 ATOM 208 C CA . HIS A 1 31 ? -24.119 -10.608 -44.841 1.00 21.84 ? 57 HIS A CA 1 ATOM 209 C C . HIS A 1 31 ? -24.876 -10.447 -43.532 1.00 19.20 ? 57 HIS A C 1 ATOM 210 O O . HIS A 1 31 ? -24.969 -11.383 -42.740 1.00 19.64 ? 57 HIS A O 1 ATOM 211 C CB . HIS A 1 31 ? -22.616 -10.583 -44.596 1.00 17.36 ? 57 HIS A CB 1 ATOM 212 C CG . HIS A 1 31 ? -21.833 -10.738 -45.857 1.00 24.35 ? 57 HIS A CG 1 ATOM 213 N ND1 . HIS A 1 31 ? -21.862 -11.896 -46.605 1.00 32.51 ? 57 HIS A ND1 1 ATOM 214 C CD2 . HIS A 1 31 ? -21.056 -9.865 -46.541 1.00 33.52 ? 57 HIS A CD2 1 ATOM 215 C CE1 . HIS A 1 31 ? -21.107 -11.743 -47.678 1.00 37.01 ? 57 HIS A CE1 1 ATOM 216 N NE2 . HIS A 1 31 ? -20.606 -10.519 -47.663 1.00 35.87 ? 57 HIS A NE2 1 ATOM 217 N N . ASP A 1 32 ? -25.442 -9.270 -43.330 1.00 15.57 ? 58 ASP A N 1 ATOM 218 C CA . ASP A 1 32 ? -26.165 -8.971 -42.101 1.00 15.15 ? 58 ASP A CA 1 ATOM 219 C C . ASP A 1 32 ? -27.302 -8.025 -42.418 1.00 17.44 ? 58 ASP A C 1 ATOM 220 O O . ASP A 1 32 ? -27.263 -6.861 -42.033 1.00 16.25 ? 58 ASP A O 1 ATOM 221 C CB . ASP A 1 32 ? -25.237 -8.344 -41.058 1.00 14.69 ? 58 ASP A CB 1 ATOM 222 C CG . ASP A 1 32 ? -25.923 -8.170 -39.706 1.00 31.05 ? 58 ASP A CG 1 ATOM 223 O OD1 . ASP A 1 32 ? -27.020 -8.742 -39.528 1.00 28.13 ? 58 ASP A OD1 1 ATOM 224 O OD2 . ASP A 1 32 ? -25.377 -7.463 -38.831 1.00 27.55 ? 58 ASP A OD2 1 ATOM 225 N N . PRO A 1 33 ? -28.316 -8.521 -43.133 1.00 15.60 ? 59 PRO A N 1 ATOM 226 C CA . PRO A 1 33 ? -29.404 -7.648 -43.567 1.00 17.14 ? 59 PRO A CA 1 ATOM 227 C C . PRO A 1 33 ? -30.203 -7.071 -42.404 1.00 16.75 ? 59 PRO A C 1 ATOM 228 O O . PRO A 1 33 ? -30.788 -6.008 -42.567 1.00 13.98 ? 59 PRO A O 1 ATOM 229 C CB . PRO A 1 33 ? -30.278 -8.571 -44.417 1.00 15.32 ? 59 PRO A CB 1 ATOM 230 C CG . PRO A 1 33 ? -29.909 -9.972 -43.983 1.00 17.53 ? 59 PRO A CG 1 ATOM 231 C CD . PRO A 1 33 ? -28.471 -9.905 -43.631 1.00 15.99 ? 59 PRO A CD 1 ATOM 232 N N . LEU A 1 34 ? -30.225 -7.751 -41.260 1.00 18.44 ? 60 LEU A N 1 ATOM 233 C CA . LEU A 1 34 ? -31.042 -7.296 -40.139 1.00 19.47 ? 60 LEU A CA 1 ATOM 234 C C . LEU A 1 34 ? -30.560 -5.950 -39.590 1.00 17.56 ? 60 LEU A C 1 ATOM 235 O O . LEU A 1 34 ? -31.320 -5.262 -38.927 1.00 14.20 ? 60 LEU A O 1 ATOM 236 C CB . LEU A 1 34 ? -31.072 -8.334 -39.014 1.00 15.04 ? 60 LEU A CB 1 ATOM 237 C CG . LEU A 1 34 ? -31.913 -9.583 -39.291 1.00 30.69 ? 60 LEU A CG 1 ATOM 238 C CD1 . LEU A 1 34 ? -32.029 -10.458 -38.063 1.00 23.59 ? 60 LEU A CD1 1 ATOM 239 C CD2 . LEU A 1 34 ? -33.288 -9.184 -39.779 1.00 32.24 ? 60 LEU A CD2 1 ATOM 240 N N . PHE A 1 35 ? -29.315 -5.564 -39.859 1.00 14.83 ? 61 PHE A N 1 ATOM 241 C CA . PHE A 1 35 ? -28.866 -4.260 -39.381 1.00 18.52 ? 61 PHE A CA 1 ATOM 242 C C . PHE A 1 35 ? -29.634 -3.152 -40.112 1.00 18.89 ? 61 PHE A C 1 ATOM 243 O O . PHE A 1 35 ? -30.272 -2.312 -39.475 1.00 17.15 ? 61 PHE A O 1 ATOM 244 C CB . PHE A 1 35 ? -27.358 -4.059 -39.558 1.00 13.04 ? 61 PHE A CB 1 ATOM 245 C CG . PHE A 1 35 ? -26.852 -2.785 -38.919 1.00 15.96 ? 61 PHE A CG 1 ATOM 246 C CD1 . PHE A 1 35 ? -26.838 -1.596 -39.628 1.00 10.69 ? 61 PHE A CD1 1 ATOM 247 C CD2 . PHE A 1 35 ? -26.432 -2.778 -37.594 1.00 11.23 ? 61 PHE A CD2 1 ATOM 248 C CE1 . PHE A 1 35 ? -26.390 -0.418 -39.043 1.00 18.87 ? 61 PHE A CE1 1 ATOM 249 C CE2 . PHE A 1 35 ? -25.984 -1.598 -36.989 1.00 15.19 ? 61 PHE A CE2 1 ATOM 250 C CZ . PHE A 1 35 ? -25.960 -0.415 -37.713 1.00 13.55 ? 61 PHE A CZ 1 ATOM 251 N N . ASP A 1 36 ? -29.594 -3.163 -41.443 1.00 12.92 ? 62 ASP A N 1 ATOM 252 C CA . ASP A 1 36 ? -30.294 -2.142 -42.208 1.00 11.56 ? 62 ASP A CA 1 ATOM 253 C C . ASP A 1 36 ? -31.810 -2.286 -42.072 1.00 21.14 ? 62 ASP A C 1 ATOM 254 O O . ASP A 1 36 ? -32.542 -1.295 -42.064 1.00 11.86 ? 62 ASP A O 1 ATOM 255 C CB . ASP A 1 36 ? -29.904 -2.198 -43.682 1.00 11.72 ? 62 ASP A CB 1 ATOM 256 C CG . ASP A 1 36 ? -28.487 -1.720 -43.930 1.00 22.26 ? 62 ASP A CG 1 ATOM 257 O OD1 . ASP A 1 36 ? -27.864 -1.162 -42.997 1.00 16.98 ? 62 ASP A OD1 1 ATOM 258 O OD2 . ASP A 1 36 ? -28.001 -1.892 -45.067 1.00 17.74 ? 62 ASP A OD2 1 ATOM 259 N N . VAL A 1 37 ? -32.282 -3.522 -41.984 1.00 14.00 ? 63 VAL A N 1 ATOM 260 C CA . VAL A 1 37 ? -33.722 -3.745 -41.856 1.00 16.51 ? 63 VAL A CA 1 ATOM 261 C C . VAL A 1 37 ? -34.235 -3.188 -40.525 1.00 21.65 ? 63 VAL A C 1 ATOM 262 O O . VAL A 1 37 ? -35.273 -2.510 -40.473 1.00 16.16 ? 63 VAL A O 1 ATOM 263 C CB . VAL A 1 37 ? -34.076 -5.233 -41.962 1.00 16.34 ? 63 VAL A CB 1 ATOM 264 C CG1 . VAL A 1 37 ? -35.518 -5.469 -41.524 1.00 23.93 ? 63 VAL A CG1 1 ATOM 265 C CG2 . VAL A 1 37 ? -33.846 -5.738 -43.401 1.00 18.64 ? 63 VAL A CG2 1 ATOM 266 N N . THR A 1 38 ? -33.501 -3.464 -39.450 1.00 14.05 ? 64 THR A N 1 ATOM 267 C CA . THR A 1 38 ? -33.917 -2.995 -38.138 1.00 12.96 ? 64 THR A CA 1 ATOM 268 C C . THR A 1 38 ? -33.859 -1.465 -38.125 1.00 20.61 ? 64 THR A C 1 ATOM 269 O O . THR A 1 38 ? -34.728 -0.818 -37.560 1.00 14.20 ? 64 THR A O 1 ATOM 270 C CB . THR A 1 38 ? -33.050 -3.600 -37.022 1.00 12.99 ? 64 THR A CB 1 ATOM 271 O OG1 . THR A 1 38 ? -33.189 -5.029 -37.048 1.00 17.94 ? 64 THR A OG1 1 ATOM 272 C CG2 . THR A 1 38 ? -33.487 -3.083 -35.635 1.00 16.23 ? 64 THR A CG2 1 ATOM 273 N N . ALA A 1 39 ? -32.856 -0.895 -38.786 1.00 14.25 ? 65 ALA A N 1 ATOM 274 C CA . ALA A 1 39 ? -32.743 0.556 -38.872 1.00 15.37 ? 65 ALA A CA 1 ATOM 275 C C . ALA A 1 39 ? -33.996 1.170 -39.508 1.00 22.81 ? 65 ALA A C 1 ATOM 276 O O . ALA A 1 39 ? -34.553 2.125 -38.982 1.00 21.59 ? 65 ALA A O 1 ATOM 277 C CB . ALA A 1 39 ? -31.505 0.946 -39.659 1.00 10.67 ? 65 ALA A CB 1 ATOM 278 N N . VAL A 1 40 ? -34.446 0.613 -40.631 1.00 13.29 ? 66 VAL A N 1 ATOM 279 C CA . VAL A 1 40 ? -35.599 1.167 -41.335 1.00 17.69 ? 66 VAL A CA 1 ATOM 280 C C . VAL A 1 40 ? -36.909 0.967 -40.557 1.00 19.84 ? 66 VAL A C 1 ATOM 281 O O . VAL A 1 40 ? -37.712 1.894 -40.408 1.00 20.31 ? 66 VAL A O 1 ATOM 282 C CB . VAL A 1 40 ? -35.720 0.550 -42.737 1.00 19.56 ? 66 VAL A CB 1 ATOM 283 C CG1 . VAL A 1 40 ? -37.054 0.913 -43.387 1.00 24.16 ? 66 VAL A CG1 1 ATOM 284 C CG2 . VAL A 1 40 ? -34.540 1.000 -43.601 1.00 22.86 ? 66 VAL A CG2 1 ATOM 285 N N . LEU A 1 41 ? -37.108 -0.225 -40.021 1.00 18.78 ? 67 LEU A N 1 ATOM 286 C CA . LEU A 1 41 ? -38.361 -0.529 -39.345 1.00 18.10 ? 67 LEU A CA 1 ATOM 287 C C . LEU A 1 41 ? -38.513 0.194 -37.996 1.00 23.22 ? 67 LEU A C 1 ATOM 288 O O . LEU A 1 41 ? -39.611 0.629 -37.646 1.00 15.73 ? 67 LEU A O 1 ATOM 289 C CB . LEU A 1 41 ? -38.488 -2.041 -39.151 1.00 18.19 ? 67 LEU A CB 1 ATOM 290 C CG . LEU A 1 41 ? -38.633 -2.860 -40.435 1.00 26.73 ? 67 LEU A CG 1 ATOM 291 C CD1 . LEU A 1 41 ? -38.801 -4.346 -40.126 1.00 28.89 ? 67 LEU A CD1 1 ATOM 292 C CD2 . LEU A 1 41 ? -39.793 -2.363 -41.289 1.00 29.77 ? 67 LEU A CD2 1 ATOM 293 N N . GLN A 1 42 ? -37.420 0.333 -37.246 1.00 13.73 ? 68 GLN A N 1 ATOM 294 C CA . GLN A 1 42 ? -37.517 0.758 -35.848 1.00 19.26 ? 68 GLN A CA 1 ATOM 295 C C . GLN A 1 42 ? -37.114 2.214 -35.573 1.00 20.85 ? 68 GLN A C 1 ATOM 296 O O . GLN A 1 42 ? -37.574 2.803 -34.602 1.00 17.66 ? 68 GLN A O 1 ATOM 297 C CB . GLN A 1 42 ? -36.652 -0.156 -34.954 1.00 13.70 ? 68 GLN A CB 1 ATOM 298 C CG . GLN A 1 42 ? -37.179 -1.579 -34.822 1.00 19.25 ? 68 GLN A CG 1 ATOM 299 C CD . GLN A 1 42 ? -38.505 -1.641 -34.088 1.00 24.72 ? 68 GLN A CD 1 ATOM 300 O OE1 . GLN A 1 42 ? -38.832 -0.759 -33.290 1.00 17.68 ? 68 GLN A OE1 1 ATOM 301 N NE2 . GLN A 1 42 ? -39.271 -2.694 -34.345 1.00 21.99 ? 68 GLN A NE2 1 ATOM 302 N N . PHE A 1 43 ? -36.234 2.773 -36.397 1.00 13.22 ? 69 PHE A N 1 ATOM 303 C CA . PHE A 1 43 ? -35.631 4.082 -36.114 1.00 12.06 ? 69 PHE A CA 1 ATOM 304 C C . PHE A 1 43 ? -36.005 5.136 -37.172 1.00 12.12 ? 69 PHE A C 1 ATOM 305 O O . PHE A 1 43 ? -36.278 4.784 -38.325 1.00 14.00 ? 69 PHE A O 1 ATOM 306 C CB . PHE A 1 43 ? -34.103 3.939 -36.025 1.00 11.26 ? 69 PHE A CB 1 ATOM 307 C CG . PHE A 1 43 ? -33.631 3.052 -34.897 1.00 11.31 ? 69 PHE A CG 1 ATOM 308 C CD1 . PHE A 1 43 ? -33.457 1.682 -35.094 1.00 16.49 ? 69 PHE A CD1 1 ATOM 309 C CD2 . PHE A 1 43 ? -33.344 3.590 -33.646 1.00 11.29 ? 69 PHE A CD2 1 ATOM 310 C CE1 . PHE A 1 43 ? -33.011 0.862 -34.058 1.00 11.70 ? 69 PHE A CE1 1 ATOM 311 C CE2 . PHE A 1 43 ? -32.891 2.782 -32.593 1.00 11.47 ? 69 PHE A CE2 1 ATOM 312 C CZ . PHE A 1 43 ? -32.719 1.423 -32.792 1.00 11.68 ? 69 PHE A CZ 1 ATOM 313 N N . ASN A 1 44 ? -36.054 6.416 -36.798 1.00 15.96 ? 70 ASN A N 1 ATOM 314 C CA . ASN A 1 44 ? -36.230 7.472 -37.808 1.00 12.26 ? 70 ASN A CA 1 ATOM 315 C C . ASN A 1 44 ? -35.312 8.660 -37.593 1.00 15.07 ? 70 ASN A C 1 ATOM 316 O O . ASN A 1 44 ? -35.598 9.781 -38.022 1.00 15.34 ? 70 ASN A O 1 ATOM 317 C CB . ASN A 1 44 ? -37.692 7.948 -37.897 1.00 15.41 ? 70 ASN A CB 1 ATOM 318 C CG . ASN A 1 44 ? -38.231 8.506 -36.586 1.00 20.07 ? 70 ASN A CG 1 ATOM 319 O OD1 . ASN A 1 44 ? -37.550 8.511 -35.562 1.00 14.96 ? 70 ASN A OD1 1 ATOM 320 N ND2 . ASN A 1 44 ? -39.479 8.978 -36.622 1.00 16.67 ? 70 ASN A ND2 1 ATOM 321 N N . GLY A 1 45 ? -34.192 8.393 -36.933 1.00 11.83 ? 71 GLY A N 1 ATOM 322 C CA . GLY A 1 45 ? -33.101 9.335 -36.818 1.00 10.70 ? 71 GLY A CA 1 ATOM 323 C C . GLY A 1 45 ? -31.778 8.602 -36.968 1.00 10.04 ? 71 GLY A C 1 ATOM 324 O O . GLY A 1 45 ? -31.670 7.392 -36.736 1.00 11.36 ? 71 GLY A O 1 ATOM 325 N N . ALA A 1 46 ? -30.754 9.329 -37.371 1.00 9.71 ? 72 ALA A N 1 ATOM 326 C CA . ALA A 1 46 ? -29.452 8.712 -37.534 1.00 12.10 ? 72 ALA A CA 1 ATOM 327 C C . ALA A 1 46 ? -28.362 9.708 -37.211 1.00 10.02 ? 72 ALA A C 1 ATOM 328 O O . ALA A 1 46 ? -28.529 10.926 -37.400 1.00 10.11 ? 72 ALA A O 1 ATOM 329 C CB . ALA A 1 46 ? -29.284 8.175 -38.947 1.00 11.09 ? 72 ALA A CB 1 ATOM 330 N N . THR A 1 47 ? -27.262 9.170 -36.692 1.00 8.92 ? 73 THR A N 1 ATOM 331 C CA . THR A 1 47 ? -26.024 9.901 -36.478 1.00 8.66 ? 73 THR A CA 1 ATOM 332 C C . THR A 1 47 ? -24.904 9.058 -37.089 1.00 8.53 ? 73 THR A C 1 ATOM 333 O O . THR A 1 47 ? -24.869 7.857 -36.852 1.00 9.10 ? 73 THR A O 1 ATOM 334 C CB . THR A 1 47 ? -25.748 10.123 -34.986 1.00 9.87 ? 73 THR A CB 1 ATOM 335 O OG1 . THR A 1 47 ? -26.892 10.716 -34.363 1.00 12.25 ? 73 THR A OG1 1 ATOM 336 C CG2 . THR A 1 47 ? -24.527 11.023 -34.814 1.00 9.97 ? 73 THR A CG2 1 ATOM 337 N N . PRO A 1 48 ? -24.011 9.662 -37.895 1.00 12.49 ? 74 PRO A N 1 ATOM 338 C CA . PRO A 1 48 ? -22.891 8.848 -38.389 1.00 10.79 ? 74 PRO A CA 1 ATOM 339 C C . PRO A 1 48 ? -21.988 8.482 -37.237 1.00 12.57 ? 74 PRO A C 1 ATOM 340 O O . PRO A 1 48 ? -21.616 9.355 -36.459 1.00 12.74 ? 74 PRO A O 1 ATOM 341 C CB . PRO A 1 48 ? -22.174 9.771 -39.387 1.00 13.80 ? 74 PRO A CB 1 ATOM 342 C CG . PRO A 1 48 ? -22.571 11.160 -38.964 1.00 17.70 ? 74 PRO A CG 1 ATOM 343 C CD . PRO A 1 48 ? -23.978 11.033 -38.429 1.00 16.01 ? 74 PRO A CD 1 ATOM 344 N N . GLU A 1 49 ? -21.666 7.204 -37.105 1.00 11.93 ? 75 GLU A N 1 ATOM 345 C CA . GLU A 1 49 ? -20.899 6.748 -35.954 1.00 15.26 ? 75 GLU A CA 1 ATOM 346 C C . GLU A 1 49 ? -19.493 7.366 -35.925 1.00 13.51 ? 75 GLU A C 1 ATOM 347 O O . GLU A 1 49 ? -19.008 7.794 -34.869 1.00 11.77 ? 75 GLU A O 1 ATOM 348 C CB . GLU A 1 49 ? -20.818 5.217 -35.974 1.00 15.11 ? 75 GLU A CB 1 ATOM 349 C CG . GLU A 1 49 ? -20.464 4.590 -34.637 1.00 23.56 ? 75 GLU A CG 1 ATOM 350 C CD . GLU A 1 49 ? -20.394 3.065 -34.706 1.00 39.92 ? 75 GLU A CD 1 ATOM 351 O OE1 . GLU A 1 49 ? -20.932 2.475 -35.674 1.00 37.54 ? 75 GLU A OE1 1 ATOM 352 O OE2 . GLU A 1 49 ? -19.793 2.454 -33.795 1.00 44.68 ? 75 GLU A OE2 1 ATOM 353 N N . ASN A 1 50 ? -18.847 7.430 -37.087 1.00 9.32 ? 76 ASN A N 1 ATOM 354 C CA . ASN A 1 50 ? -17.449 7.867 -37.161 1.00 14.13 ? 76 ASN A CA 1 ATOM 355 C C . ASN A 1 50 ? -17.116 8.780 -38.317 1.00 20.72 ? 76 ASN A C 1 ATOM 356 O O . ASN A 1 50 ? -16.234 9.622 -38.206 1.00 14.13 ? 76 ASN A O 1 ATOM 357 C CB . ASN A 1 50 ? -16.511 6.663 -37.276 1.00 15.38 ? 76 ASN A CB 1 ATOM 358 C CG . ASN A 1 50 ? -16.474 5.832 -36.025 1.00 20.30 ? 76 ASN A CG 1 ATOM 359 O OD1 . ASN A 1 50 ? -16.901 4.676 -36.021 1.00 24.89 ? 76 ASN A OD1 1 ATOM 360 N ND2 . ASN A 1 50 ? -15.961 6.411 -34.949 1.00 18.83 ? 76 ASN A ND2 1 ATOM 361 N N . GLU A 1 51 ? -17.780 8.604 -39.450 1.00 11.71 ? 77 GLU A N 1 ATOM 362 C CA . GLU A 1 51 ? -17.124 9.065 -40.672 1.00 15.77 ? 77 GLU A CA 1 ATOM 363 C C . GLU A 1 51 ? -17.279 10.545 -40.996 1.00 11.81 ? 77 GLU A C 1 ATOM 364 O O . GLU A 1 51 ? -16.693 11.017 -41.970 1.00 12.42 ? 77 GLU A O 1 ATOM 365 C CB . GLU A 1 51 ? -17.571 8.205 -41.857 1.00 29.77 ? 77 GLU A CB 1 ATOM 366 C CG . GLU A 1 51 ? -17.230 6.727 -41.616 1.00 38.70 ? 77 GLU A CG 1 ATOM 367 C CD . GLU A 1 51 ? -16.408 6.064 -42.714 1.00 46.11 ? 77 GLU A CD 1 ATOM 368 O OE1 . GLU A 1 51 ? -16.059 6.737 -43.712 1.00 47.56 ? 77 GLU A OE1 1 ATOM 369 O OE2 . GLU A 1 51 ? -16.111 4.853 -42.557 1.00 38.97 ? 77 GLU A OE2 1 ATOM 370 N N . MET A 1 52 ? -17.989 11.305 -40.169 1.00 12.48 ? 78 MET A N 1 ATOM 371 C CA . MET A 1 52 ? -17.910 12.762 -40.302 1.00 11.58 ? 78 MET A CA 1 ATOM 372 C C . MET A 1 52 ? -16.871 13.373 -39.364 1.00 15.03 ? 78 MET A C 1 ATOM 373 O O . MET A 1 52 ? -16.669 14.581 -39.376 1.00 17.56 ? 78 MET A O 1 ATOM 374 C CB . MET A 1 52 ? -19.270 13.425 -40.032 1.00 14.06 ? 78 MET A CB 1 ATOM 375 C CG . MET A 1 52 ? -20.281 13.231 -41.143 1.00 16.55 ? 78 MET A CG 1 ATOM 376 S SD . MET A 1 52 ? -21.783 14.224 -40.924 1.00 23.56 ? 78 MET A SD 1 ATOM 377 C CE . MET A 1 52 ? -22.847 13.442 -42.160 1.00 18.43 ? 78 MET A CE 1 ATOM 378 N N . LYS A 1 53 ? -16.235 12.557 -38.528 1.00 10.52 ? 79 LYS A N 1 ATOM 379 C CA . LYS A 1 53 ? -15.221 13.088 -37.613 1.00 11.40 ? 79 LYS A CA 1 ATOM 380 C C . LYS A 1 53 ? -13.973 13.504 -38.382 1.00 14.84 ? 79 LYS A C 1 ATOM 381 O O . LYS A 1 53 ? -13.702 13.008 -39.488 1.00 13.00 ? 79 LYS A O 1 ATOM 382 C CB . LYS A 1 53 ? -14.876 12.069 -36.526 1.00 15.49 ? 79 LYS A CB 1 ATOM 383 C CG . LYS A 1 53 ? -16.009 11.851 -35.529 1.00 16.90 ? 79 LYS A CG 1 ATOM 384 C CD . LYS A 1 53 ? -15.874 10.506 -34.854 1.00 25.61 ? 79 LYS A CD 1 ATOM 385 C CE . LYS A 1 53 ? -16.993 10.275 -33.848 1.00 23.25 ? 79 LYS A CE 1 ATOM 386 N NZ . LYS A 1 53 ? -16.854 8.912 -33.235 1.00 19.57 ? 79 LYS A NZ 1 ATOM 387 N N . TRP A 1 54 ? -13.213 14.415 -37.784 1.00 12.15 ? 80 TRP A N 1 ATOM 388 C CA . TRP A 1 54 ? -12.153 15.134 -38.486 1.00 13.02 ? 80 TRP A CA 1 ATOM 389 C C . TRP A 1 54 ? -11.115 14.222 -39.122 1.00 13.60 ? 80 TRP A C 1 ATOM 390 O O . TRP A 1 54 ? -10.685 14.459 -40.246 1.00 14.19 ? 80 TRP A O 1 ATOM 391 C CB . TRP A 1 54 ? -11.479 16.097 -37.510 1.00 13.50 ? 80 TRP A CB 1 ATOM 392 C CG . TRP A 1 54 ? -10.658 17.185 -38.118 1.00 14.44 ? 80 TRP A CG 1 ATOM 393 C CD1 . TRP A 1 54 ? -9.787 17.095 -39.173 1.00 18.02 ? 80 TRP A CD1 1 ATOM 394 C CD2 . TRP A 1 54 ? -10.621 18.540 -37.679 1.00 14.84 ? 80 TRP A CD2 1 ATOM 395 N NE1 . TRP A 1 54 ? -9.209 18.326 -39.408 1.00 18.63 ? 80 TRP A NE1 1 ATOM 396 C CE2 . TRP A 1 54 ? -9.713 19.227 -38.505 1.00 17.41 ? 80 TRP A CE2 1 ATOM 397 C CE3 . TRP A 1 54 ? -11.281 19.242 -36.668 1.00 19.34 ? 80 TRP A CE3 1 ATOM 398 C CZ2 . TRP A 1 54 ? -9.439 20.583 -38.342 1.00 18.65 ? 80 TRP A CZ2 1 ATOM 399 C CZ3 . TRP A 1 54 ? -11.008 20.584 -36.507 1.00 19.36 ? 80 TRP A CZ3 1 ATOM 400 C CH2 . TRP A 1 54 ? -10.095 21.238 -37.334 1.00 18.14 ? 80 TRP A CH2 1 ATOM 401 N N . ALA A 1 55 ? -10.700 13.183 -38.410 1.00 15.33 ? 81 ALA A N 1 ATOM 402 C CA . ALA A 1 55 ? -9.688 12.262 -38.941 1.00 14.32 ? 81 ALA A CA 1 ATOM 403 C C . ALA A 1 55 ? -10.130 11.595 -40.256 1.00 20.35 ? 81 ALA A C 1 ATOM 404 O O . ALA A 1 55 ? -9.299 11.220 -41.080 1.00 19.59 ? 81 ALA A O 1 ATOM 405 C CB . ALA A 1 55 ? -9.346 11.191 -37.898 1.00 18.74 ? 81 ALA A CB 1 ATOM 406 N N . TYR A 1 56 ? -11.437 11.444 -40.446 1.00 14.30 ? 82 TYR A N 1 ATOM 407 C CA . TYR A 1 56 ? -11.960 10.775 -41.640 1.00 15.24 ? 82 TYR A CA 1 ATOM 408 C C . TYR A 1 56 ? -12.285 11.770 -42.738 1.00 17.34 ? 82 TYR A C 1 ATOM 409 O O . TYR A 1 56 ? -12.044 11.510 -43.919 1.00 19.89 ? 82 TYR A O 1 ATOM 410 C CB . TYR A 1 56 ? -13.226 9.978 -41.306 1.00 16.55 ? 82 TYR A CB 1 ATOM 411 C CG . TYR A 1 56 ? -12.985 8.780 -40.432 1.00 23.23 ? 82 TYR A CG 1 ATOM 412 C CD1 . TYR A 1 56 ? -12.941 8.903 -39.045 1.00 22.44 ? 82 TYR A CD1 1 ATOM 413 C CD2 . TYR A 1 56 ? -12.803 7.520 -40.993 1.00 24.59 ? 82 TYR A CD2 1 ATOM 414 C CE1 . TYR A 1 56 ? -12.715 7.800 -38.237 1.00 26.67 ? 82 TYR A CE1 1 ATOM 415 C CE2 . TYR A 1 56 ? -12.578 6.417 -40.198 1.00 29.31 ? 82 TYR A CE2 1 ATOM 416 C CZ . TYR A 1 56 ? -12.536 6.562 -38.822 1.00 35.69 ? 82 TYR A CZ 1 ATOM 417 O OH . TYR A 1 56 ? -12.313 5.457 -38.036 1.00 48.58 ? 82 TYR A OH 1 ATOM 418 N N . ILE A 1 57 ? -12.835 12.910 -42.341 1.00 13.13 ? 83 ILE A N 1 ATOM 419 C CA . ILE A 1 57 ? -13.421 13.821 -43.308 1.00 13.28 ? 83 ILE A CA 1 ATOM 420 C C . ILE A 1 57 ? -12.404 14.850 -43.822 1.00 14.30 ? 83 ILE A C 1 ATOM 421 O O . ILE A 1 57 ? -12.552 15.347 -44.936 1.00 16.75 ? 83 ILE A O 1 ATOM 422 C CB . ILE A 1 57 ? -14.674 14.515 -42.708 1.00 14.76 ? 83 ILE A CB 1 ATOM 423 C CG1 . ILE A 1 57 ? -15.603 15.026 -43.821 1.00 19.67 ? 83 ILE A CG1 1 ATOM 424 C CG2 . ILE A 1 57 ? -14.283 15.608 -41.720 1.00 13.20 ? 83 ILE A CG2 1 ATOM 425 C CD1 . ILE A 1 57 ? -17.050 15.264 -43.360 1.00 16.06 ? 83 ILE A CD1 1 ATOM 426 N N . GLU A 1 58 ? -11.355 15.146 -43.053 1.00 14.76 ? 84 GLU A N 1 ATOM 427 C CA . GLU A 1 58 ? -10.269 15.980 -43.591 1.00 16.22 ? 84 GLU A CA 1 ATOM 428 C C . GLU A 1 58 ? -8.901 15.377 -43.245 1.00 18.39 ? 84 GLU A C 1 ATOM 429 O O . GLU A 1 58 ? -8.181 15.920 -42.404 1.00 17.07 ? 84 GLU A O 1 ATOM 430 C CB . GLU A 1 58 ? -10.366 17.425 -43.064 1.00 16.13 ? 84 GLU A CB 1 ATOM 431 C CG . GLU A 1 58 ? -9.581 18.438 -43.921 1.00 17.42 ? 84 GLU A CG 1 ATOM 432 C CD . GLU A 1 58 ? -9.466 19.834 -43.307 1.00 17.84 ? 84 GLU A CD 1 ATOM 433 O OE1 . GLU A 1 58 ? -10.094 20.108 -42.263 1.00 22.25 ? 84 GLU A OE1 1 ATOM 434 O OE2 . GLU A 1 58 ? -8.732 20.663 -43.886 1.00 19.03 ? 84 GLU A OE2 1 ATOM 435 N N . PRO A 1 59 ? -8.548 14.245 -43.887 1.00 20.50 ? 85 PRO A N 1 ATOM 436 C CA . PRO A 1 59 ? -7.377 13.439 -43.486 1.00 22.19 ? 85 PRO A CA 1 ATOM 437 C C . PRO A 1 59 ? -6.036 14.122 -43.766 1.00 24.30 ? 85 PRO A C 1 ATOM 438 O O . PRO A 1 59 ? -5.052 13.862 -43.066 1.00 24.52 ? 85 PRO A O 1 ATOM 439 C CB . PRO A 1 59 ? -7.527 12.157 -44.310 1.00 22.89 ? 85 PRO A CB 1 ATOM 440 C CG . PRO A 1 59 ? -8.378 12.552 -45.487 1.00 29.92 ? 85 PRO A CG 1 ATOM 441 C CD . PRO A 1 59 ? -9.295 13.637 -45.005 1.00 16.70 ? 85 PRO A CD 1 ATOM 442 N N . GLU A 1 60 ? -5.993 14.986 -44.771 1.00 19.75 ? 86 GLU A N 1 ATOM 443 C CA . GLU A 1 60 ? -4.873 15.918 -44.896 1.00 21.88 ? 86 GLU A CA 1 ATOM 444 C C . GLU A 1 60 ? -5.417 17.329 -45.047 1.00 26.81 ? 86 GLU A C 1 ATOM 445 O O . GLU A 1 60 ? -6.580 17.508 -45.419 1.00 20.43 ? 86 GLU A O 1 ATOM 446 C CB . GLU A 1 60 ? -3.967 15.568 -46.071 1.00 31.63 ? 86 GLU A CB 1 ATOM 447 C CG . GLU A 1 60 ? -3.914 14.100 -46.423 1.00 47.43 ? 86 GLU A CG 1 ATOM 448 C CD . GLU A 1 60 ? -3.311 13.862 -47.802 1.00 72.36 ? 86 GLU A CD 1 ATOM 449 O OE1 . GLU A 1 60 ? -2.785 14.828 -48.402 1.00 74.96 ? 86 GLU A OE1 1 ATOM 450 O OE2 . GLU A 1 60 ? -3.340 12.705 -48.279 1.00 83.81 ? 86 GLU A OE2 1 ATOM 451 N N . ARG A 1 61 ? -4.584 18.333 -44.778 1.00 23.81 ? 87 ARG A N 1 ATOM 452 C CA . ARG A 1 61 ? -5.079 19.708 -44.722 1.00 30.96 ? 87 ARG A CA 1 ATOM 453 C C . ARG A 1 61 ? -5.707 20.168 -46.048 1.00 28.00 ? 87 ARG A C 1 ATOM 454 O O . ARG A 1 61 ? -5.108 20.024 -47.108 1.00 23.51 ? 87 ARG A O 1 ATOM 455 C CB . ARG A 1 61 ? -3.963 20.666 -44.310 1.00 28.65 ? 87 ARG A CB 1 ATOM 456 C CG . ARG A 1 61 ? -4.479 22.046 -43.956 1.00 31.66 ? 87 ARG A CG 1 ATOM 457 C CD . ARG A 1 61 ? -3.414 22.912 -43.288 1.00 29.09 ? 87 ARG A CD 1 ATOM 458 N NE . ARG A 1 61 ? -3.975 24.209 -42.914 1.00 31.32 ? 87 ARG A NE 1 ATOM 459 C CZ . ARG A 1 61 ? -3.341 25.123 -42.186 1.00 33.45 ? 87 ARG A CZ 1 ATOM 460 N NH1 . ARG A 1 61 ? -2.115 24.888 -41.738 1.00 29.95 ? 87 ARG A NH1 1 ATOM 461 N NH2 . ARG A 1 61 ? -3.942 26.270 -41.901 1.00 30.94 ? 87 ARG A NH2 1 ATOM 462 N N . ASN A 1 62 ? -6.935 20.683 -45.950 1.00 29.97 ? 88 ASN A N 1 ATOM 463 C CA . ASN A 1 62 ? -7.745 21.158 -47.080 1.00 21.70 ? 88 ASN A CA 1 ATOM 464 C C . ASN A 1 62 ? -8.071 20.071 -48.123 1.00 30.23 ? 88 ASN A C 1 ATOM 465 O O . ASN A 1 62 ? -8.498 20.368 -49.244 1.00 24.93 ? 88 ASN A O 1 ATOM 466 C CB . ASN A 1 62 ? -7.062 22.352 -47.760 1.00 32.39 ? 88 ASN A CB 1 ATOM 467 C CG . ASN A 1 62 ? -8.053 23.270 -48.451 1.00 35.36 ? 88 ASN A CG 1 ATOM 468 O OD1 . ASN A 1 62 ? -9.199 23.414 -48.016 1.00 32.42 ? 88 ASN A OD1 1 ATOM 469 N ND2 . ASN A 1 62 ? -7.623 23.885 -49.543 1.00 35.05 ? 88 ASN A ND2 1 ATOM 470 N N . GLN A 1 63 ? -7.885 18.814 -47.739 1.00 20.83 ? 89 GLN A N 1 ATOM 471 C CA . GLN A 1 63 ? -8.257 17.686 -48.580 1.00 20.56 ? 89 GLN A CA 1 ATOM 472 C C . GLN A 1 63 ? -9.418 16.978 -47.900 1.00 22.27 ? 89 GLN A C 1 ATOM 473 O O . GLN A 1 63 ? -9.229 16.306 -46.894 1.00 27.64 ? 89 GLN A O 1 ATOM 474 C CB . GLN A 1 63 ? -7.080 16.725 -48.780 1.00 25.20 ? 89 GLN A CB 1 ATOM 475 C CG . GLN A 1 63 ? -5.807 17.368 -49.326 1.00 43.38 ? 89 GLN A CG 1 ATOM 476 C CD . GLN A 1 63 ? -5.791 17.439 -50.839 1.00 60.06 ? 89 GLN A CD 1 ATOM 477 O OE1 . GLN A 1 63 ? -5.952 18.512 -51.425 1.00 68.60 ? 89 GLN A OE1 1 ATOM 478 N NE2 . GLN A 1 63 ? -5.592 16.291 -51.482 1.00 62.12 ? 89 GLN A NE2 1 ATOM 479 N N . PHE A 1 64 ? -10.623 17.148 -48.426 1.00 18.44 ? 90 PHE A N 1 ATOM 480 C CA . PHE A 1 64 ? -11.786 16.616 -47.737 1.00 17.07 ? 90 PHE A CA 1 ATOM 481 C C . PHE A 1 64 ? -12.227 15.306 -48.379 1.00 20.86 ? 90 PHE A C 1 ATOM 482 O O . PHE A 1 64 ? -12.092 15.125 -49.578 1.00 24.05 ? 90 PHE A O 1 ATOM 483 C CB . PHE A 1 64 ? -12.916 17.653 -47.717 1.00 21.19 ? 90 PHE A CB 1 ATOM 484 C CG . PHE A 1 64 ? -12.608 18.857 -46.850 1.00 17.01 ? 90 PHE A CG 1 ATOM 485 C CD1 . PHE A 1 64 ? -11.861 19.914 -47.347 1.00 18.25 ? 90 PHE A CD1 1 ATOM 486 C CD2 . PHE A 1 64 ? -13.042 18.910 -45.535 1.00 20.93 ? 90 PHE A CD2 1 ATOM 487 C CE1 . PHE A 1 64 ? -11.561 21.016 -46.550 1.00 18.58 ? 90 PHE A CE1 1 ATOM 488 C CE2 . PHE A 1 64 ? -12.741 20.008 -44.727 1.00 16.45 ? 90 PHE A CE2 1 ATOM 489 C CZ . PHE A 1 64 ? -12.002 21.059 -45.236 1.00 21.15 ? 90 PHE A CZ 1 ATOM 490 N N . ASN A 1 65 ? -12.713 14.386 -47.552 1.00 15.69 ? 91 ASN A N 1 ATOM 491 C CA . ASN A 1 65 ? -13.224 13.117 -48.015 1.00 16.86 ? 91 ASN A CA 1 ATOM 492 C C . ASN A 1 65 ? -14.644 12.914 -47.468 1.00 14.20 ? 91 ASN A C 1 ATOM 493 O O . ASN A 1 65 ? -14.834 12.490 -46.327 1.00 13.47 ? 91 ASN A O 1 ATOM 494 C CB . ASN A 1 65 ? -12.289 11.985 -47.587 1.00 18.19 ? 91 ASN A CB 1 ATOM 495 C CG . ASN A 1 65 ? -12.700 10.652 -48.149 1.00 22.71 ? 91 ASN A CG 1 ATOM 496 O OD1 . ASN A 1 65 ? -13.678 10.544 -48.889 1.00 18.05 ? 91 ASN A OD1 1 ATOM 497 N ND2 . ASN A 1 65 ? -11.952 9.627 -47.810 1.00 15.59 ? 91 ASN A ND2 1 ATOM 498 N N . PHE A 1 66 ? -15.639 13.228 -48.286 1.00 14.19 ? 92 PHE A N 1 ATOM 499 C CA . PHE A 1 66 ? -17.033 13.193 -47.834 1.00 13.35 ? 92 PHE A CA 1 ATOM 500 C C . PHE A 1 66 ? -17.711 11.842 -48.043 1.00 13.62 ? 92 PHE A C 1 ATOM 501 O O . PHE A 1 66 ? -18.882 11.672 -47.700 1.00 13.19 ? 92 PHE A O 1 ATOM 502 C CB . PHE A 1 66 ? -17.836 14.286 -48.543 1.00 18.04 ? 92 PHE A CB 1 ATOM 503 C CG . PHE A 1 66 ? -17.391 15.676 -48.189 1.00 18.02 ? 92 PHE A CG 1 ATOM 504 C CD1 . PHE A 1 66 ? -17.592 16.170 -46.908 1.00 21.83 ? 92 PHE A CD1 1 ATOM 505 C CD2 . PHE A 1 66 ? -16.764 16.478 -49.120 1.00 18.70 ? 92 PHE A CD2 1 ATOM 506 C CE1 . PHE A 1 66 ? -17.167 17.443 -46.560 1.00 22.34 ? 92 PHE A CE1 1 ATOM 507 C CE2 . PHE A 1 66 ? -16.342 17.765 -48.783 1.00 21.03 ? 92 PHE A CE2 1 ATOM 508 C CZ . PHE A 1 66 ? -16.537 18.244 -47.499 1.00 18.32 ? 92 PHE A CZ 1 ATOM 509 N N . THR A 1 67 ? -16.974 10.876 -48.583 1.00 13.30 ? 93 THR A N 1 ATOM 510 C CA . THR A 1 67 ? -17.581 9.610 -48.998 1.00 13.12 ? 93 THR A CA 1 ATOM 511 C C . THR A 1 67 ? -18.354 8.930 -47.877 1.00 12.91 ? 93 THR A C 1 ATOM 512 O O . THR A 1 67 ? -19.526 8.542 -48.051 1.00 13.18 ? 93 THR A O 1 ATOM 513 C CB . THR A 1 67 ? -16.521 8.659 -49.523 1.00 13.79 ? 93 THR A CB 1 ATOM 514 O OG1 . THR A 1 67 ? -15.896 9.273 -50.644 1.00 16.67 ? 93 THR A OG1 1 ATOM 515 C CG2 . THR A 1 67 ? -17.145 7.333 -49.960 1.00 14.77 ? 93 THR A CG2 1 ATOM 516 N N . GLY A 1 68 ? -17.707 8.809 -46.720 1.00 13.34 ? 94 GLY A N 1 ATOM 517 C CA . GLY A 1 68 ? -18.297 8.125 -45.592 1.00 12.19 ? 94 GLY A CA 1 ATOM 518 C C . GLY A 1 68 ? -19.501 8.885 -45.074 1.00 14.12 ? 94 GLY A C 1 ATOM 519 O O . GLY A 1 68 ? -20.560 8.296 -44.849 1.00 11.26 ? 94 GLY A O 1 ATOM 520 N N . GLY A 1 69 ? -19.358 10.199 -44.888 1.00 10.76 ? 95 GLY A N 1 ATOM 521 C CA . GLY A 1 69 ? -20.481 10.979 -44.390 1.00 10.54 ? 95 GLY A CA 1 ATOM 522 C C . GLY A 1 69 ? -21.655 10.974 -45.361 1.00 11.62 ? 95 GLY A C 1 ATOM 523 O O . GLY A 1 69 ? -22.831 10.923 -44.953 1.00 13.25 ? 95 GLY A O 1 ATOM 524 N N . ASP A 1 70 ? -21.338 11.017 -46.651 1.00 15.13 ? 96 ASP A N 1 ATOM 525 C CA . ASP A 1 70 ? -22.368 11.006 -47.685 1.00 13.56 ? 96 ASP A CA 1 ATOM 526 C C . ASP A 1 70 ? -23.175 9.705 -47.686 1.00 15.61 ? 96 ASP A C 1 ATOM 527 O O . ASP A 1 70 ? -24.374 9.723 -47.951 1.00 13.91 ? 96 ASP A O 1 ATOM 528 C CB . ASP A 1 70 ? -21.752 11.218 -49.063 1.00 12.22 ? 96 ASP A CB 1 ATOM 529 C CG . ASP A 1 70 ? -21.310 12.661 -49.295 1.00 20.51 ? 96 ASP A CG 1 ATOM 530 O OD1 . ASP A 1 70 ? -21.562 13.530 -48.427 1.00 20.82 ? 96 ASP A OD1 1 ATOM 531 O OD2 . ASP A 1 70 ? -20.724 12.926 -50.362 1.00 21.40 ? 96 ASP A OD2 1 ATOM 532 N N . ILE A 1 71 ? -22.519 8.582 -47.401 1.00 10.95 ? 97 ILE A N 1 ATOM 533 C CA . ILE A 1 71 ? -23.229 7.317 -47.321 1.00 12.88 ? 97 ILE A CA 1 ATOM 534 C C . ILE A 1 71 ? -24.271 7.318 -46.194 1.00 21.49 ? 97 ILE A C 1 ATOM 535 O O . ILE A 1 71 ? -25.422 6.926 -46.406 1.00 10.29 ? 97 ILE A O 1 ATOM 536 C CB . ILE A 1 71 ? -22.255 6.146 -47.150 1.00 14.48 ? 97 ILE A CB 1 ATOM 537 C CG1 . ILE A 1 71 ? -21.477 5.956 -48.457 1.00 14.47 ? 97 ILE A CG1 1 ATOM 538 C CG2 . ILE A 1 71 ? -23.012 4.871 -46.815 1.00 10.69 ? 97 ILE A CG2 1 ATOM 539 C CD1 . ILE A 1 71 ? -20.257 5.103 -48.347 1.00 11.89 ? 97 ILE A CD1 1 ATOM 540 N N . VAL A 1 72 ? -23.894 7.780 -45.007 1.00 9.87 ? 98 VAL A N 1 ATOM 541 C CA . VAL A 1 72 ? -24.851 7.792 -43.899 1.00 9.50 ? 98 VAL A CA 1 ATOM 542 C C . VAL A 1 72 ? -25.971 8.793 -44.177 1.00 9.68 ? 98 VAL A C 1 ATOM 543 O O . VAL A 1 72 ? -27.164 8.521 -43.909 1.00 9.92 ? 98 VAL A O 1 ATOM 544 C CB . VAL A 1 72 ? -24.159 8.130 -42.551 1.00 14.71 ? 98 VAL A CB 1 ATOM 545 C CG1 . VAL A 1 72 ? -25.177 8.211 -41.432 1.00 15.85 ? 98 VAL A CG1 1 ATOM 546 C CG2 . VAL A 1 72 ? -23.131 7.061 -42.221 1.00 11.28 ? 98 VAL A CG2 1 ATOM 547 N N . ALA A 1 73 ? -25.592 9.948 -44.718 1.00 9.96 ? 99 ALA A N 1 ATOM 548 C CA . ALA A 1 73 ? -26.565 10.988 -45.019 1.00 12.88 ? 99 ALA A CA 1 ATOM 549 C C . ALA A 1 73 ? -27.563 10.519 -46.086 1.00 13.08 ? 99 ALA A C 1 ATOM 550 O O . ALA A 1 73 ? -28.733 10.880 -46.046 1.00 12.32 ? 99 ALA A O 1 ATOM 551 C CB . ALA A 1 73 ? -25.856 12.282 -45.481 1.00 10.71 ? 99 ALA A CB 1 ATOM 552 N N . ALA A 1 74 ? -27.096 9.734 -47.052 1.00 10.90 ? 100 ALA A N 1 ATOM 553 C CA . ALA A 1 74 ? -27.975 9.271 -48.124 1.00 16.44 ? 100 ALA A CA 1 ATOM 554 C C . ALA A 1 74 ? -28.959 8.228 -47.621 1.00 16.29 ? 100 ALA A C 1 ATOM 555 O O . ALA A 1 74 ? -30.125 8.224 -48.019 1.00 13.78 ? 100 ALA A O 1 ATOM 556 C CB . ALA A 1 74 ? -27.165 8.705 -49.302 1.00 15.64 ? 100 ALA A CB 1 ATOM 557 N N . PHE A 1 75 ? -28.482 7.328 -46.770 1.00 10.72 ? 101 PHE A N 1 ATOM 558 C CA . PHE A 1 75 ? -29.361 6.348 -46.137 1.00 11.07 ? 101 PHE A CA 1 ATOM 559 C C . PHE A 1 75 ? -30.452 7.072 -45.354 1.00 11.40 ? 101 PHE A C 1 ATOM 560 O O . PHE A 1 75 ? -31.641 6.754 -45.439 1.00 11.06 ? 101 PHE A O 1 ATOM 561 C CB . PHE A 1 75 ? -28.572 5.438 -45.212 1.00 10.20 ? 101 PHE A CB 1 ATOM 562 C CG . PHE A 1 75 ? -29.385 4.312 -44.617 1.00 14.51 ? 101 PHE A CG 1 ATOM 563 C CD1 . PHE A 1 75 ? -29.595 3.131 -45.331 1.00 16.92 ? 101 PHE A CD1 1 ATOM 564 C CD2 . PHE A 1 75 ? -29.942 4.437 -43.353 1.00 11.93 ? 101 PHE A CD2 1 ATOM 565 C CE1 . PHE A 1 75 ? -30.346 2.096 -44.785 1.00 15.10 ? 101 PHE A CE1 1 ATOM 566 C CE2 . PHE A 1 75 ? -30.684 3.406 -42.797 1.00 18.55 ? 101 PHE A CE2 1 ATOM 567 C CZ . PHE A 1 75 ? -30.876 2.230 -43.507 1.00 13.00 ? 101 PHE A CZ 1 ATOM 568 N N . SER A 1 76 ? -30.026 8.070 -44.601 1.00 10.42 ? 102 SER A N 1 ATOM 569 C CA . SER A 1 76 ? -30.942 8.892 -43.833 1.00 11.25 ? 102 SER A CA 1 ATOM 570 C C . SER A 1 76 ? -31.937 9.603 -44.759 1.00 11.79 ? 102 SER A C 1 ATOM 571 O O . SER A 1 76 ? -33.153 9.596 -44.509 1.00 14.45 ? 102 SER A O 1 ATOM 572 C CB . SER A 1 76 ? -30.141 9.895 -42.985 1.00 10.86 ? 102 SER A CB 1 ATOM 573 O OG . SER A 1 76 ? -30.996 10.896 -42.455 1.00 17.66 ? 102 SER A OG 1 ATOM 574 N N . ALA A 1 77 ? -31.435 10.184 -45.848 1.00 13.15 ? 103 ALA A N 1 ATOM 575 C CA . ALA A 1 77 ? -32.306 10.899 -46.790 1.00 13.99 ? 103 ALA A CA 1 ATOM 576 C C . ALA A 1 77 ? -33.334 9.979 -47.441 1.00 14.51 ? 103 ALA A C 1 ATOM 577 O O . ALA A 1 77 ? -34.517 10.345 -47.581 1.00 13.60 ? 103 ALA A O 1 ATOM 578 C CB . ALA A 1 77 ? -31.483 11.591 -47.852 1.00 13.57 ? 103 ALA A CB 1 ATOM 579 N N . ALA A 1 78 ? -32.898 8.785 -47.832 1.00 12.61 ? 104 ALA A N 1 ATOM 580 C CA . ALA A 1 78 ? -33.799 7.826 -48.460 1.00 13.63 ? 104 ALA A CA 1 ATOM 581 C C . ALA A 1 78 ? -34.972 7.491 -47.537 1.00 15.37 ? 104 ALA A C 1 ATOM 582 O O . ALA A 1 78 ? -36.095 7.323 -47.992 1.00 14.03 ? 104 ALA A O 1 ATOM 583 C CB . ALA A 1 78 ? -33.059 6.556 -48.834 1.00 12.81 ? 104 ALA A CB 1 ATOM 584 N N . ASN A 1 79 ? -34.696 7.380 -46.242 1.00 16.68 ? 105 ASN A N 1 ATOM 585 C CA . ASN A 1 79 ? -35.727 6.993 -45.284 1.00 19.55 ? 105 ASN A CA 1 ATOM 586 C C . ASN A 1 79 ? -36.393 8.181 -44.580 1.00 14.46 ? 105 ASN A C 1 ATOM 587 O O . ASN A 1 79 ? -37.131 7.988 -43.621 1.00 17.11 ? 105 ASN A O 1 ATOM 588 C CB . ASN A 1 79 ? -35.128 6.046 -44.244 1.00 17.70 ? 105 ASN A CB 1 ATOM 589 C CG . ASN A 1 79 ? -34.743 4.715 -44.834 1.00 21.37 ? 105 ASN A CG 1 ATOM 590 O OD1 . ASN A 1 79 ? -35.597 3.852 -45.031 1.00 20.15 ? 105 ASN A OD1 1 ATOM 591 N ND2 . ASN A 1 79 ? -33.448 4.532 -45.126 1.00 12.25 ? 105 ASN A ND2 1 ATOM 592 N N . ASP A 1 80 ? -36.143 9.390 -45.086 1.00 13.45 ? 106 ASP A N 1 ATOM 593 C CA . ASP A 1 80 ? -36.499 10.668 -44.438 1.00 24.78 ? 106 ASP A CA 1 ATOM 594 C C . ASP A 1 80 ? -36.334 10.634 -42.918 1.00 23.12 ? 106 ASP A C 1 ATOM 595 O O . ASP A 1 80 ? -37.259 10.933 -42.153 1.00 18.74 ? 106 ASP A O 1 ATOM 596 C CB . ASP A 1 80 ? -37.924 11.107 -44.788 1.00 30.22 ? 106 ASP A CB 1 ATOM 597 C CG . ASP A 1 80 ? -38.032 12.633 -45.009 1.00 41.33 ? 106 ASP A CG 1 ATOM 598 O OD1 . ASP A 1 80 ? -37.098 13.398 -44.622 1.00 20.46 ? 106 ASP A OD1 1 ATOM 599 O OD2 . ASP A 1 80 ? -39.061 13.067 -45.579 1.00 43.06 ? 106 ASP A OD2 1 ATOM 600 N N . TYR A 1 81 ? -35.135 10.262 -42.504 1.00 12.42 ? 107 TYR A N 1 ATOM 601 C CA . TYR A 1 81 ? -34.704 10.369 -41.118 1.00 12.94 ? 107 TYR A CA 1 ATOM 602 C C . TYR A 1 81 ? -34.428 11.800 -40.691 1.00 17.76 ? 107 TYR A C 1 ATOM 603 O O . TYR A 1 81 ? -34.169 12.671 -41.526 1.00 18.55 ? 107 TYR A O 1 ATOM 604 C CB . TYR A 1 81 ? -33.418 9.592 -40.899 1.00 11.12 ? 107 TYR A CB 1 ATOM 605 C CG . TYR A 1 81 ? -33.537 8.115 -40.752 1.00 14.90 ? 107 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 81 ? -34.741 7.451 -40.939 1.00 13.60 ? 107 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 81 ? -32.424 7.374 -40.386 1.00 21.81 ? 107 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 81 ? -34.809 6.071 -40.775 1.00 16.04 ? 107 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 81 ? -32.486 6.021 -40.224 1.00 33.08 ? 107 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 81 ? -33.673 5.367 -40.422 1.00 22.01 ? 107 TYR A CZ 1 ATOM 611 O OH . TYR A 1 81 ? -33.685 3.995 -40.241 1.00 30.35 ? 107 TYR A OH 1 ATOM 612 N N . VAL A 1 82 ? -34.430 12.018 -39.381 1.00 13.42 ? 108 VAL A N 1 ATOM 613 C CA . VAL A 1 82 ? -33.797 13.190 -38.804 1.00 11.96 ? 108 VAL A CA 1 ATOM 614 C C . VAL A 1 82 ? -32.293 12.928 -38.701 1.00 11.12 ? 108 VAL A C 1 ATOM 615 O O . VAL A 1 82 ? -31.863 12.008 -38.007 1.00 14.51 ? 108 VAL A O 1 ATOM 616 C CB . VAL A 1 82 ? -34.371 13.515 -37.419 1.00 14.94 ? 108 VAL A CB 1 ATOM 617 C CG1 . VAL A 1 82 ? -33.644 14.697 -36.808 1.00 15.97 ? 108 VAL A CG1 1 ATOM 618 C CG2 . VAL A 1 82 ? -35.883 13.789 -37.519 1.00 14.42 ? 108 VAL A CG2 1 ATOM 619 N N . LEU A 1 83 ? -31.497 13.727 -39.398 1.00 11.08 ? 109 LEU A N 1 ATOM 620 C CA . LEU A 1 83 ? -30.052 13.511 -39.442 1.00 20.33 ? 109 LEU A CA 1 ATOM 621 C C . LEU A 1 83 ? -29.282 14.484 -38.545 1.00 12.41 ? 109 LEU A C 1 ATOM 622 O O . LEU A 1 83 ? -29.480 15.697 -38.611 1.00 11.11 ? 109 LEU A O 1 ATOM 623 C CB . LEU A 1 83 ? -29.552 13.627 -40.885 1.00 14.89 ? 109 LEU A CB 1 ATOM 624 C CG . LEU A 1 83 ? -28.055 13.422 -41.098 1.00 16.99 ? 109 LEU A CG 1 ATOM 625 C CD1 . LEU A 1 83 ? -27.631 12.006 -40.655 1.00 16.31 ? 109 LEU A CD1 1 ATOM 626 C CD2 . LEU A 1 83 ? -27.710 13.692 -42.576 1.00 13.21 ? 109 LEU A CD2 1 ATOM 627 N N . ARG A 1 84 ? -28.414 13.948 -37.695 1.00 10.19 ? 110 ARG A N 1 ATOM 628 C CA . ARG A 1 84 ? -27.559 14.792 -36.861 1.00 9.95 ? 110 ARG A CA 1 ATOM 629 C C . ARG A 1 84 ? -26.127 14.697 -37.362 1.00 15.19 ? 110 ARG A C 1 ATOM 630 O O . ARG A 1 84 ? -25.585 13.606 -37.486 1.00 13.87 ? 110 ARG A O 1 ATOM 631 C CB . ARG A 1 84 ? -27.622 14.378 -35.383 1.00 9.81 ? 110 ARG A CB 1 ATOM 632 C CG . ARG A 1 84 ? -29.036 14.102 -34.827 1.00 24.46 ? 110 ARG A CG 1 ATOM 633 C CD . ARG A 1 84 ? -29.018 13.902 -33.282 1.00 14.21 ? 110 ARG A CD 1 ATOM 634 N NE . ARG A 1 84 ? -28.684 15.159 -32.612 1.00 19.74 ? 110 ARG A NE 1 ATOM 635 C CZ . ARG A 1 84 ? -27.494 15.443 -32.104 1.00 18.39 ? 110 ARG A CZ 1 ATOM 636 N NH1 . ARG A 1 84 ? -26.519 14.540 -32.142 1.00 19.96 ? 110 ARG A NH1 1 ATOM 637 N NH2 . ARG A 1 84 ? -27.283 16.630 -31.538 1.00 20.12 ? 110 ARG A NH2 1 ATOM 638 N N . GLY A 1 85 ? -25.519 15.837 -37.653 1.00 11.66 ? 111 GLY A N 1 ATOM 639 C CA . GLY A 1 85 ? -24.118 15.862 -38.026 1.00 14.63 ? 111 GLY A CA 1 ATOM 640 C C . GLY A 1 85 ? -23.245 15.763 -36.794 1.00 20.28 ? 111 GLY A C 1 ATOM 641 O O . GLY A 1 85 ? -23.484 16.445 -35.794 1.00 19.25 ? 111 GLY A O 1 ATOM 642 N N . HIS A 1 86 ? -22.207 14.939 -36.864 1.00 14.61 ? 112 HIS A N 1 ATOM 643 C CA . HIS A 1 86 ? -21.416 14.635 -35.671 1.00 16.95 ? 112 HIS A CA 1 ATOM 644 C C . HIS A 1 86 ? -19.994 14.184 -36.045 1.00 14.99 ? 112 HIS A C 1 ATOM 645 O O . HIS A 1 86 ? -19.841 13.184 -36.747 1.00 18.81 ? 112 HIS A O 1 ATOM 646 C CB . HIS A 1 86 ? -22.165 13.560 -34.875 1.00 25.70 ? 112 HIS A CB 1 ATOM 647 C CG . HIS A 1 86 ? -21.358 12.876 -33.815 1.00 29.55 ? 112 HIS A CG 1 ATOM 648 N ND1 . HIS A 1 86 ? -21.325 13.312 -32.508 1.00 31.63 ? 112 HIS A ND1 1 ATOM 649 C CD2 . HIS A 1 86 ? -20.603 11.751 -33.855 1.00 27.39 ? 112 HIS A CD2 1 ATOM 650 C CE1 . HIS A 1 86 ? -20.558 12.504 -31.796 1.00 34.84 ? 112 HIS A CE1 1 ATOM 651 N NE2 . HIS A 1 86 ? -20.106 11.551 -32.590 1.00 35.40 ? 112 HIS A NE2 1 ATOM 652 N N . ASN A 1 87 ? -18.949 14.907 -35.626 1.00 14.24 ? 113 ASN A N 1 ATOM 653 C CA . ASN A 1 87 ? -18.995 16.194 -34.939 1.00 14.31 ? 113 ASN A CA 1 ATOM 654 C C . ASN A 1 87 ? -17.866 17.048 -35.522 1.00 22.03 ? 113 ASN A C 1 ATOM 655 O O . ASN A 1 87 ? -17.050 16.533 -36.276 1.00 18.87 ? 113 ASN A O 1 ATOM 656 C CB . ASN A 1 87 ? -18.848 16.041 -33.422 1.00 17.57 ? 113 ASN A CB 1 ATOM 657 C CG . ASN A 1 87 ? -17.613 15.232 -33.015 1.00 23.10 ? 113 ASN A CG 1 ATOM 658 O OD1 . ASN A 1 87 ? -16.543 15.379 -33.590 1.00 24.16 ? 113 ASN A OD1 1 ATOM 659 N ND2 . ASN A 1 87 ? -17.767 14.381 -32.007 1.00 22.08 ? 113 ASN A ND2 1 ATOM 660 N N . LEU A 1 88 ? -17.792 18.332 -35.193 1.00 11.26 ? 114 LEU A N 1 ATOM 661 C CA . LEU A 1 88 ? -16.833 19.182 -35.918 1.00 17.88 ? 114 LEU A CA 1 ATOM 662 C C . LEU A 1 88 ? -15.550 19.513 -35.160 1.00 21.67 ? 114 LEU A C 1 ATOM 663 O O . LEU A 1 88 ? -14.475 19.583 -35.758 1.00 27.70 ? 114 LEU A O 1 ATOM 664 C CB . LEU A 1 88 ? -17.511 20.487 -36.344 1.00 14.53 ? 114 LEU A CB 1 ATOM 665 C CG . LEU A 1 88 ? -18.605 20.360 -37.416 1.00 13.59 ? 114 LEU A CG 1 ATOM 666 C CD1 . LEU A 1 88 ? -19.268 21.702 -37.647 1.00 15.12 ? 114 LEU A CD1 1 ATOM 667 C CD2 . LEU A 1 88 ? -18.056 19.805 -38.729 1.00 12.98 ? 114 LEU A CD2 1 ATOM 668 N N . VAL A 1 89 ? -15.659 19.759 -33.859 1.00 12.46 ? 115 VAL A N 1 ATOM 669 C CA . VAL A 1 89 ? -14.488 20.093 -33.049 1.00 13.04 ? 115 VAL A CA 1 ATOM 670 C C . VAL A 1 89 ? -14.437 19.187 -31.820 1.00 20.70 ? 115 VAL A C 1 ATOM 671 O O . VAL A 1 89 ? -15.309 19.254 -30.955 1.00 14.58 ? 115 VAL A O 1 ATOM 672 C CB . VAL A 1 89 ? -14.505 21.574 -32.604 1.00 17.73 ? 115 VAL A CB 1 ATOM 673 C CG1 . VAL A 1 89 ? -13.279 21.903 -31.747 1.00 17.61 ? 115 VAL A CG1 1 ATOM 674 C CG2 . VAL A 1 89 ? -14.592 22.516 -33.823 1.00 17.56 ? 115 VAL A CG2 1 ATOM 675 N N . TRP A 1 90 ? -13.412 18.345 -31.747 1.00 14.97 ? 116 TRP A N 1 ATOM 676 C CA . TRP A 1 90 ? -13.329 17.317 -30.713 1.00 12.68 ? 116 TRP A CA 1 ATOM 677 C C . TRP A 1 90 ? -11.873 16.917 -30.569 1.00 16.30 ? 116 TRP A C 1 ATOM 678 O O . TRP A 1 90 ? -11.176 16.796 -31.572 1.00 14.49 ? 116 TRP A O 1 ATOM 679 C CB . TRP A 1 90 ? -14.174 16.112 -31.093 1.00 11.93 ? 116 TRP A CB 1 ATOM 680 C CG . TRP A 1 90 ? -14.275 15.035 -30.054 1.00 15.06 ? 116 TRP A CG 1 ATOM 681 C CD1 . TRP A 1 90 ? -14.264 15.189 -28.693 1.00 17.78 ? 116 TRP A CD1 1 ATOM 682 C CD2 . TRP A 1 90 ? -14.415 13.631 -30.299 1.00 19.80 ? 116 TRP A CD2 1 ATOM 683 N NE1 . TRP A 1 90 ? -14.389 13.959 -28.077 1.00 11.99 ? 116 TRP A NE1 1 ATOM 684 C CE2 . TRP A 1 90 ? -14.488 12.990 -29.042 1.00 18.51 ? 116 TRP A CE2 1 ATOM 685 C CE3 . TRP A 1 90 ? -14.489 12.852 -31.462 1.00 20.15 ? 116 TRP A CE3 1 ATOM 686 C CZ2 . TRP A 1 90 ? -14.628 11.606 -28.915 1.00 17.75 ? 116 TRP A CZ2 1 ATOM 687 C CZ3 . TRP A 1 90 ? -14.626 11.477 -31.334 1.00 15.60 ? 116 TRP A CZ3 1 ATOM 688 C CH2 . TRP A 1 90 ? -14.697 10.869 -30.069 1.00 22.88 ? 116 TRP A CH2 1 ATOM 689 N N . TYR A 1 91 ? -11.401 16.719 -29.343 1.00 13.73 ? 117 TYR A N 1 ATOM 690 C CA . TYR A 1 91 ? -9.981 16.402 -29.159 1.00 16.67 ? 117 TYR A CA 1 ATOM 691 C C . TYR A 1 91 ? -9.614 14.992 -29.633 1.00 20.04 ? 117 TYR A C 1 ATOM 692 O O . TYR A 1 91 ? -8.444 14.708 -29.844 1.00 19.44 ? 117 TYR A O 1 ATOM 693 C CB . TYR A 1 91 ? -9.573 16.582 -27.696 1.00 18.66 ? 117 TYR A CB 1 ATOM 694 C CG . TYR A 1 91 ? -9.935 15.437 -26.774 1.00 20.58 ? 117 TYR A CG 1 ATOM 695 C CD1 . TYR A 1 91 ? -11.242 15.249 -26.347 1.00 18.95 ? 117 TYR A CD1 1 ATOM 696 C CD2 . TYR A 1 91 ? -8.957 14.562 -26.304 1.00 22.45 ? 117 TYR A CD2 1 ATOM 697 C CE1 . TYR A 1 91 ? -11.574 14.209 -25.481 1.00 20.26 ? 117 TYR A CE1 1 ATOM 698 C CE2 . TYR A 1 91 ? -9.273 13.520 -25.433 1.00 26.77 ? 117 TYR A CE2 1 ATOM 699 C CZ . TYR A 1 91 ? -10.581 13.349 -25.025 1.00 25.46 ? 117 TYR A CZ 1 ATOM 700 O OH . TYR A 1 91 ? -10.912 12.312 -24.171 1.00 22.24 ? 117 TYR A OH 1 ATOM 701 N N . GLN A 1 92 ? -10.602 14.116 -29.820 1.00 13.71 ? 118 GLN A N 1 ATOM 702 C CA . GLN A 1 92 ? -10.333 12.745 -30.282 1.00 20.55 ? 118 GLN A CA 1 ATOM 703 C C . GLN A 1 92 ? -10.675 12.535 -31.759 1.00 21.72 ? 118 GLN A C 1 ATOM 704 O O . GLN A 1 92 ? -11.415 13.326 -32.339 1.00 21.90 ? 118 GLN A O 1 ATOM 705 C CB . GLN A 1 92 ? -11.120 11.738 -29.447 1.00 25.42 ? 118 GLN A CB 1 ATOM 706 C CG . GLN A 1 92 ? -10.844 11.847 -27.974 1.00 37.11 ? 118 GLN A CG 1 ATOM 707 C CD . GLN A 1 92 ? -10.974 10.523 -27.268 1.00 52.69 ? 118 GLN A CD 1 ATOM 708 O OE1 . GLN A 1 92 ? -12.054 9.929 -27.232 1.00 56.47 ? 118 GLN A OE1 1 ATOM 709 N NE2 . GLN A 1 92 ? -9.868 10.041 -26.713 1.00 53.45 ? 118 GLN A NE2 1 ATOM 710 N N . GLU A 1 93 ? -10.170 11.441 -32.338 1.00 22.91 ? 119 GLU A N 1 ATOM 711 C CA . GLU A 1 93 ? -10.359 11.137 -33.765 1.00 22.11 ? 119 GLU A CA 1 ATOM 712 C C . GLU A 1 93 ? -10.122 12.400 -34.589 1.00 19.72 ? 119 GLU A C 1 ATOM 713 O O . GLU A 1 93 ? -10.914 12.785 -35.452 1.00 19.92 ? 119 GLU A O 1 ATOM 714 C CB . GLU A 1 93 ? -11.746 10.547 -34.032 1.00 23.37 ? 119 GLU A CB 1 ATOM 715 C CG . GLU A 1 93 ? -11.938 9.134 -33.429 1.00 31.87 ? 119 GLU A CG 1 ATOM 716 C CD . GLU A 1 93 ? -13.295 8.510 -33.756 1.00 45.48 ? 119 GLU A CD 1 ATOM 717 O OE1 . GLU A 1 93 ? -14.203 8.516 -32.883 1.00 34.11 ? 119 GLU A OE1 1 ATOM 718 O OE2 . GLU A 1 93 ? -13.452 8.003 -34.890 1.00 53.69 ? 119 GLU A OE2 1 ATOM 719 N N . LEU A 1 94 ? -9.018 13.048 -34.269 1.00 22.28 ? 120 LEU A N 1 ATOM 720 C CA . LEU A 1 94 ? -8.585 14.263 -34.922 1.00 23.53 ? 120 LEU A CA 1 ATOM 721 C C . LEU A 1 94 ? -7.430 13.907 -35.854 1.00 24.25 ? 120 LEU A C 1 ATOM 722 O O . LEU A 1 94 ? -6.557 13.130 -35.476 1.00 31.73 ? 120 LEU A O 1 ATOM 723 C CB . LEU A 1 94 ? -8.162 15.278 -33.862 1.00 25.55 ? 120 LEU A CB 1 ATOM 724 C CG . LEU A 1 94 ? -7.773 16.711 -34.193 1.00 21.80 ? 120 LEU A CG 1 ATOM 725 C CD1 . LEU A 1 94 ? -8.937 17.446 -34.848 1.00 17.07 ? 120 LEU A CD1 1 ATOM 726 C CD2 . LEU A 1 94 ? -7.353 17.389 -32.885 1.00 19.57 ? 120 LEU A CD2 1 ATOM 727 N N . ALA A 1 95 ? -7.424 14.440 -37.073 1.00 22.51 ? 121 ALA A N 1 ATOM 728 C CA . ALA A 1 95 ? -6.327 14.148 -37.994 1.00 20.71 ? 121 ALA A CA 1 ATOM 729 C C . ALA A 1 95 ? -5.008 14.660 -37.412 1.00 23.29 ? 121 ALA A C 1 ATOM 730 O O . ALA A 1 95 ? -4.925 15.812 -36.985 1.00 20.87 ? 121 ALA A O 1 ATOM 731 C CB . ALA A 1 95 ? -6.586 14.770 -39.364 1.00 22.16 ? 121 ALA A CB 1 ATOM 732 N N . PRO A 1 96 ? -3.969 13.804 -37.403 1.00 22.99 ? 122 PRO A N 1 ATOM 733 C CA . PRO A 1 96 ? -2.644 14.119 -36.845 1.00 26.02 ? 122 PRO A CA 1 ATOM 734 C C . PRO A 1 96 ? -2.091 15.502 -37.218 1.00 31.64 ? 122 PRO A C 1 ATOM 735 O O . PRO A 1 96 ? -1.477 16.143 -36.362 1.00 28.44 ? 122 PRO A O 1 ATOM 736 C CB . PRO A 1 96 ? -1.754 13.019 -37.430 1.00 31.64 ? 122 PRO A CB 1 ATOM 737 C CG . PRO A 1 96 ? -2.689 11.854 -37.596 1.00 35.94 ? 122 PRO A CG 1 ATOM 738 C CD . PRO A 1 96 ? -4.006 12.464 -38.012 1.00 27.69 ? 122 PRO A CD 1 ATOM 739 N N . TRP A 1 97 ? -2.308 15.960 -38.452 1.00 29.55 ? 123 TRP A N 1 ATOM 740 C CA . TRP A 1 97 ? -1.747 17.242 -38.889 1.00 24.70 ? 123 TRP A CA 1 ATOM 741 C C . TRP A 1 97 ? -2.297 18.452 -38.123 1.00 25.62 ? 123 TRP A C 1 ATOM 742 O O . TRP A 1 97 ? -1.643 19.491 -38.063 1.00 28.20 ? 123 TRP A O 1 ATOM 743 C CB . TRP A 1 97 ? -1.967 17.451 -40.399 1.00 25.62 ? 123 TRP A CB 1 ATOM 744 C CG . TRP A 1 97 ? -3.420 17.494 -40.851 1.00 21.43 ? 123 TRP A CG 1 ATOM 745 C CD1 . TRP A 1 97 ? -4.162 16.446 -41.326 1.00 20.54 ? 123 TRP A CD1 1 ATOM 746 C CD2 . TRP A 1 97 ? -4.282 18.644 -40.895 1.00 21.03 ? 123 TRP A CD2 1 ATOM 747 N NE1 . TRP A 1 97 ? -5.432 16.868 -41.645 1.00 22.17 ? 123 TRP A NE1 1 ATOM 748 C CE2 . TRP A 1 97 ? -5.531 18.212 -41.392 1.00 20.69 ? 123 TRP A CE2 1 ATOM 749 C CE3 . TRP A 1 97 ? -4.122 19.991 -40.557 1.00 23.38 ? 123 TRP A CE3 1 ATOM 750 C CZ2 . TRP A 1 97 ? -6.612 19.082 -41.559 1.00 24.71 ? 123 TRP A CZ2 1 ATOM 751 C CZ3 . TRP A 1 97 ? -5.199 20.852 -40.718 1.00 24.00 ? 123 TRP A CZ3 1 ATOM 752 C CH2 . TRP A 1 97 ? -6.428 20.394 -41.214 1.00 20.86 ? 123 TRP A CH2 1 ATOM 753 N N . VAL A 1 98 ? -3.487 18.331 -37.541 1.00 20.72 ? 124 VAL A N 1 ATOM 754 C CA . VAL A 1 98 ? -4.062 19.438 -36.784 1.00 24.19 ? 124 VAL A CA 1 ATOM 755 C C . VAL A 1 98 ? -3.292 19.718 -35.490 1.00 27.94 ? 124 VAL A C 1 ATOM 756 O O . VAL A 1 98 ? -3.096 20.872 -35.105 1.00 25.74 ? 124 VAL A O 1 ATOM 757 C CB . VAL A 1 98 ? -5.533 19.169 -36.419 1.00 24.39 ? 124 VAL A CB 1 ATOM 758 C CG1 . VAL A 1 98 ? -6.136 20.373 -35.702 1.00 18.97 ? 124 VAL A CG1 1 ATOM 759 C CG2 . VAL A 1 98 ? -6.330 18.833 -37.668 1.00 28.39 ? 124 VAL A CG2 1 ATOM 760 N N . GLU A 1 99 ? -2.839 18.653 -34.839 1.00 25.31 ? 125 GLU A N 1 ATOM 761 C CA . GLU A 1 99 ? -2.382 18.734 -33.454 1.00 32.92 ? 125 GLU A CA 1 ATOM 762 C C . GLU A 1 99 ? -1.093 19.515 -33.261 1.00 40.92 ? 125 GLU A C 1 ATOM 763 O O . GLU A 1 99 ? -0.758 19.897 -32.138 1.00 42.80 ? 125 GLU A O 1 ATOM 764 C CB . GLU A 1 99 ? -2.235 17.325 -32.882 1.00 34.35 ? 125 GLU A CB 1 ATOM 765 C CG . GLU A 1 99 ? -3.584 16.755 -32.457 1.00 31.91 ? 125 GLU A CG 1 ATOM 766 C CD . GLU A 1 99 ? -3.530 15.293 -32.096 1.00 51.61 ? 125 GLU A CD 1 ATOM 767 O OE1 . GLU A 1 99 ? -2.453 14.679 -32.260 1.00 61.84 ? 125 GLU A OE1 1 ATOM 768 O OE2 . GLU A 1 99 ? -4.569 14.759 -31.648 1.00 53.28 ? 125 GLU A OE2 1 ATOM 769 N N . THR A 1 100 ? -0.383 19.776 -34.352 1.00 40.65 ? 126 THR A N 1 ATOM 770 C CA . THR A 1 100 ? 0.863 20.522 -34.261 1.00 40.38 ? 126 THR A CA 1 ATOM 771 C C . THR A 1 100 ? 0.711 21.972 -34.719 1.00 37.73 ? 126 THR A C 1 ATOM 772 O O . THR A 1 100 ? 1.671 22.730 -34.688 1.00 35.75 ? 126 THR A O 1 ATOM 773 C CB . THR A 1 100 ? 1.979 19.838 -35.076 1.00 41.11 ? 126 THR A CB 1 ATOM 774 O OG1 . THR A 1 100 ? 1.503 19.545 -36.398 1.00 35.49 ? 126 THR A OG1 1 ATOM 775 C CG2 . THR A 1 100 ? 2.412 18.538 -34.388 1.00 38.59 ? 126 THR A CG2 1 ATOM 776 N N . LEU A 1 101 ? -0.493 22.362 -35.133 1.00 33.64 ? 127 LEU A N 1 ATOM 777 C CA . LEU A 1 101 ? -0.725 23.739 -35.568 1.00 31.90 ? 127 LEU A CA 1 ATOM 778 C C . LEU A 1 101 ? -0.825 24.657 -34.356 1.00 28.53 ? 127 LEU A C 1 ATOM 779 O O . LEU A 1 101 ? -1.346 24.266 -33.317 1.00 27.37 ? 127 LEU A O 1 ATOM 780 C CB . LEU A 1 101 ? -1.992 23.839 -36.428 1.00 32.84 ? 127 LEU A CB 1 ATOM 781 C CG . LEU A 1 101 ? -2.058 22.937 -37.671 1.00 28.72 ? 127 LEU A CG 1 ATOM 782 C CD1 . LEU A 1 101 ? -3.327 23.191 -38.455 1.00 27.54 ? 127 LEU A CD1 1 ATOM 783 C CD2 . LEU A 1 101 ? -0.833 23.133 -38.562 1.00 30.44 ? 127 LEU A CD2 1 ATOM 784 N N . THR A 1 102 ? -0.320 25.877 -34.487 1.00 26.97 ? 128 THR A N 1 ATOM 785 C CA . THR A 1 102 ? -0.330 26.821 -33.375 1.00 27.39 ? 128 THR A CA 1 ATOM 786 C C . THR A 1 102 ? -1.019 28.131 -33.752 1.00 35.82 ? 128 THR A C 1 ATOM 787 O O . THR A 1 102 ? -1.044 28.509 -34.927 1.00 35.74 ? 128 THR A O 1 ATOM 788 C CB . THR A 1 102 ? 1.107 27.137 -32.895 1.00 36.38 ? 128 THR A CB 1 ATOM 789 O OG1 . THR A 1 102 ? 1.866 27.688 -33.979 1.00 37.65 ? 128 THR A OG1 1 ATOM 790 C CG2 . THR A 1 102 ? 1.799 25.875 -32.393 1.00 42.64 ? 128 THR A CG2 1 ATOM 791 N N . GLY A 1 103 ? -1.571 28.818 -32.753 1.00 31.14 ? 129 GLY A N 1 ATOM 792 C CA . GLY A 1 103 ? -2.111 30.158 -32.935 1.00 35.02 ? 129 GLY A CA 1 ATOM 793 C C . GLY A 1 103 ? -3.108 30.345 -34.070 1.00 36.23 ? 129 GLY A C 1 ATOM 794 O O . GLY A 1 103 ? -4.002 29.518 -34.271 1.00 28.08 ? 129 GLY A O 1 ATOM 795 N N . GLU A 1 104 ? -2.948 31.437 -34.816 1.00 32.12 ? 130 GLU A N 1 ATOM 796 C CA . GLU A 1 104 ? -3.878 31.800 -35.889 1.00 30.22 ? 130 GLU A CA 1 ATOM 797 C C . GLU A 1 104 ? -3.956 30.737 -36.976 1.00 30.14 ? 130 GLU A C 1 ATOM 798 O O . GLU A 1 104 ? -4.983 30.601 -37.644 1.00 32.67 ? 130 GLU A O 1 ATOM 799 C CB . GLU A 1 104 ? -3.477 33.136 -36.523 1.00 38.36 ? 130 GLU A CB 1 ATOM 800 C CG . GLU A 1 104 ? -3.441 34.314 -35.549 1.00 54.86 ? 130 GLU A CG 1 ATOM 801 C CD . GLU A 1 104 ? -2.476 35.417 -35.981 1.00 67.19 ? 130 GLU A CD 1 ATOM 802 O OE1 . GLU A 1 104 ? -2.116 35.465 -37.178 1.00 69.54 ? 130 GLU A OE1 1 ATOM 803 O OE2 . GLU A 1 104 ? -2.073 36.233 -35.119 1.00 71.16 ? 130 GLU A OE2 1 ATOM 804 N N . ASP A 1 105 ? -2.863 30.002 -37.156 1.00 28.56 ? 131 ASP A N 1 ATOM 805 C CA . ASP A 1 105 ? -2.787 28.960 -38.172 1.00 30.42 ? 131 ASP A CA 1 ATOM 806 C C . ASP A 1 105 ? -3.770 27.829 -37.824 1.00 29.89 ? 131 ASP A C 1 ATOM 807 O O . ASP A 1 105 ? -4.509 27.341 -38.685 1.00 24.69 ? 131 ASP A O 1 ATOM 808 C CB . ASP A 1 105 ? -1.356 28.432 -38.286 1.00 36.82 ? 131 ASP A CB 1 ATOM 809 C CG . ASP A 1 105 ? -1.162 27.505 -39.479 1.00 41.60 ? 131 ASP A CG 1 ATOM 810 O OD1 . ASP A 1 105 ? -1.902 27.641 -40.476 1.00 37.89 ? 131 ASP A OD1 1 ATOM 811 O OD2 . ASP A 1 105 ? -0.264 26.640 -39.422 1.00 50.39 ? 131 ASP A OD2 1 ATOM 812 N N . LEU A 1 106 ? -3.770 27.438 -36.553 1.00 24.86 ? 132 LEU A N 1 ATOM 813 C CA . LEU A 1 106 ? -4.713 26.459 -36.039 1.00 23.21 ? 132 LEU A CA 1 ATOM 814 C C . LEU A 1 106 ? -6.146 26.950 -36.200 1.00 27.12 ? 132 LEU A C 1 ATOM 815 O O . LEU A 1 106 ? -7.028 26.200 -36.619 1.00 22.78 ? 132 LEU A O 1 ATOM 816 C CB . LEU A 1 106 ? -4.434 26.159 -34.565 1.00 23.00 ? 132 LEU A CB 1 ATOM 817 C CG . LEU A 1 106 ? -5.547 25.368 -33.863 1.00 23.39 ? 132 LEU A CG 1 ATOM 818 C CD1 . LEU A 1 106 ? -5.652 23.974 -34.437 1.00 20.60 ? 132 LEU A CD1 1 ATOM 819 C CD2 . LEU A 1 106 ? -5.304 25.319 -32.360 1.00 25.35 ? 132 LEU A CD2 1 ATOM 820 N N . TRP A 1 107 ? -6.381 28.210 -35.856 1.00 24.31 ? 133 TRP A N 1 ATOM 821 C CA . TRP A 1 107 ? -7.723 28.756 -35.970 1.00 22.57 ? 133 TRP A CA 1 ATOM 822 C C . TRP A 1 107 ? -8.171 28.794 -37.435 1.00 26.08 ? 133 TRP A C 1 ATOM 823 O O . TRP A 1 107 ? -9.313 28.446 -37.737 1.00 23.41 ? 133 TRP A O 1 ATOM 824 C CB . TRP A 1 107 ? -7.814 30.150 -35.338 1.00 23.48 ? 133 TRP A CB 1 ATOM 825 C CG . TRP A 1 107 ? -9.211 30.686 -35.385 1.00 28.23 ? 133 TRP A CG 1 ATOM 826 C CD1 . TRP A 1 107 ? -9.624 31.831 -35.990 1.00 29.92 ? 133 TRP A CD1 1 ATOM 827 C CD2 . TRP A 1 107 ? -10.393 30.067 -34.845 1.00 26.88 ? 133 TRP A CD2 1 ATOM 828 N NE1 . TRP A 1 107 ? -10.982 31.980 -35.845 1.00 33.97 ? 133 TRP A NE1 1 ATOM 829 C CE2 . TRP A 1 107 ? -11.479 30.911 -35.147 1.00 32.36 ? 133 TRP A CE2 1 ATOM 830 C CE3 . TRP A 1 107 ? -10.633 28.887 -34.127 1.00 28.27 ? 133 TRP A CE3 1 ATOM 831 C CZ2 . TRP A 1 107 ? -12.794 30.613 -34.762 1.00 35.02 ? 133 TRP A CZ2 1 ATOM 832 C CZ3 . TRP A 1 107 ? -11.941 28.589 -33.742 1.00 35.32 ? 133 TRP A CZ3 1 ATOM 833 C CH2 . TRP A 1 107 ? -13.003 29.450 -34.063 1.00 32.88 ? 133 TRP A CH2 1 ATOM 834 N N . ASN A 1 108 ? -7.278 29.193 -38.339 1.00 23.77 ? 134 ASN A N 1 ATOM 835 C CA . ASN A 1 108 ? -7.613 29.200 -39.767 1.00 23.99 ? 134 ASN A CA 1 ATOM 836 C C . ASN A 1 108 ? -8.004 27.815 -40.280 1.00 29.89 ? 134 ASN A C 1 ATOM 837 O O . ASN A 1 108 ? -8.963 27.674 -41.038 1.00 22.89 ? 134 ASN A O 1 ATOM 838 C CB . ASN A 1 108 ? -6.450 29.728 -40.609 1.00 32.71 ? 134 ASN A CB 1 ATOM 839 C CG . ASN A 1 108 ? -6.725 29.627 -42.109 1.00 50.41 ? 134 ASN A CG 1 ATOM 840 O OD1 . ASN A 1 108 ? -6.516 28.575 -42.729 1.00 53.57 ? 134 ASN A OD1 1 ATOM 841 N ND2 . ASN A 1 108 ? -7.198 30.721 -42.697 1.00 56.08 ? 134 ASN A ND2 1 ATOM 842 N N . ALA A 1 109 ? -7.254 26.795 -39.880 1.00 22.38 ? 135 ALA A N 1 ATOM 843 C CA . ALA A 1 109 ? -7.573 25.430 -40.286 1.00 21.30 ? 135 ALA A CA 1 ATOM 844 C C . ALA A 1 109 ? -8.939 25.021 -39.756 1.00 19.86 ? 135 ALA A C 1 ATOM 845 O O . ALA A 1 109 ? -9.676 24.286 -40.417 1.00 20.52 ? 135 ALA A O 1 ATOM 846 C CB . ALA A 1 109 ? -6.505 24.458 -39.800 1.00 25.10 ? 135 ALA A CB 1 ATOM 847 N N . THR A 1 110 ? -9.269 25.505 -38.559 1.00 19.61 ? 136 THR A N 1 ATOM 848 C CA . THR A 1 110 ? -10.503 25.125 -37.882 1.00 18.40 ? 136 THR A CA 1 ATOM 849 C C . THR A 1 110 ? -11.697 25.810 -38.541 1.00 18.37 ? 136 THR A C 1 ATOM 850 O O . THR A 1 110 ? -12.730 25.182 -38.770 1.00 17.46 ? 136 THR A O 1 ATOM 851 C CB . THR A 1 110 ? -10.443 25.473 -36.378 1.00 19.83 ? 136 THR A CB 1 ATOM 852 O OG1 . THR A 1 110 ? -9.345 24.773 -35.770 1.00 18.48 ? 136 THR A OG1 1 ATOM 853 C CG2 . THR A 1 110 ? -11.728 25.075 -35.681 1.00 18.39 ? 136 THR A CG2 1 ATOM 854 N N . VAL A 1 111 ? -11.548 27.094 -38.854 1.00 19.50 ? 137 VAL A N 1 ATOM 855 C CA . VAL A 1 111 ? -12.571 27.820 -39.592 1.00 19.79 ? 137 VAL A CA 1 ATOM 856 C C . VAL A 1 111 ? -12.853 27.132 -40.932 1.00 25.37 ? 137 VAL A C 1 ATOM 857 O O . VAL A 1 111 ? -14.010 26.929 -41.309 1.00 19.53 ? 137 VAL A O 1 ATOM 858 C CB . VAL A 1 111 ? -12.159 29.286 -39.847 1.00 21.64 ? 137 VAL A CB 1 ATOM 859 C CG1 . VAL A 1 111 ? -13.147 29.952 -40.788 1.00 25.10 ? 137 VAL A CG1 1 ATOM 860 C CG2 . VAL A 1 111 ? -12.057 30.055 -38.518 1.00 21.67 ? 137 VAL A CG2 1 ATOM 861 N N . ASN A 1 112 ? -11.789 26.755 -41.632 1.00 20.04 ? 138 ASN A N 1 ATOM 862 C CA . ASN A 1 112 ? -11.922 26.110 -42.927 1.00 19.99 ? 138 ASN A CA 1 ATOM 863 C C . ASN A 1 112 ? -12.597 24.732 -42.809 1.00 21.58 ? 138 ASN A C 1 ATOM 864 O O . ASN A 1 112 ? -13.390 24.349 -43.665 1.00 20.25 ? 138 ASN A O 1 ATOM 865 C CB . ASN A 1 112 ? -10.552 25.984 -43.594 1.00 20.99 ? 138 ASN A CB 1 ATOM 866 C CG . ASN A 1 112 ? -10.631 25.379 -44.983 1.00 26.24 ? 138 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 112 ? -11.229 25.961 -45.884 1.00 27.02 ? 138 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 112 ? -10.022 24.211 -45.164 1.00 26.02 ? 138 ASN A ND2 1 ATOM 869 N N . HIS A 1 113 ? -12.289 24.006 -41.739 1.00 17.81 ? 139 HIS A N 1 ATOM 870 C CA . HIS A 1 113 ? -12.909 22.706 -41.486 1.00 16.57 ? 139 HIS A CA 1 ATOM 871 C C . HIS A 1 113 ? -14.415 22.847 -41.288 1.00 22.10 ? 139 HIS A C 1 ATOM 872 O O . HIS A 1 113 ? -15.202 22.179 -41.956 1.00 16.85 ? 139 HIS A O 1 ATOM 873 C CB . HIS A 1 113 ? -12.295 22.029 -40.258 1.00 16.10 ? 139 HIS A CB 1 ATOM 874 C CG . HIS A 1 113 ? -12.791 20.634 -40.043 1.00 15.03 ? 139 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 113 ? -12.322 19.558 -40.765 1.00 14.98 ? 139 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 113 ? -13.730 20.141 -39.202 1.00 15.72 ? 139 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 113 ? -12.947 18.461 -40.376 1.00 14.05 ? 139 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 113 ? -13.816 18.788 -39.436 1.00 14.45 ? 139 HIS A NE2 1 ATOM 879 N N . ILE A 1 114 ? -14.798 23.718 -40.361 1.00 16.00 ? 140 ILE A N 1 ATOM 880 C CA . ILE A 1 114 ? -16.190 23.939 -40.024 1.00 15.56 ? 140 ILE A CA 1 ATOM 881 C C . ILE A 1 114 ? -16.968 24.418 -41.245 1.00 16.04 ? 140 ILE A C 1 ATOM 882 O O . ILE A 1 114 ? -18.025 23.879 -41.574 1.00 15.63 ? 140 ILE A O 1 ATOM 883 C CB . ILE A 1 114 ? -16.319 24.963 -38.876 1.00 18.92 ? 140 ILE A CB 1 ATOM 884 C CG1 . ILE A 1 114 ? -15.743 24.382 -37.584 1.00 21.23 ? 140 ILE A CG1 1 ATOM 885 C CG2 . ILE A 1 114 ? -17.767 25.373 -38.670 1.00 15.82 ? 140 ILE A CG2 1 ATOM 886 C CD1 . ILE A 1 114 ? -15.500 25.434 -36.501 1.00 16.61 ? 140 ILE A CD1 1 ATOM 887 N N . THR A 1 115 ? -16.417 25.406 -41.942 1.00 17.18 ? 141 THR A N 1 ATOM 888 C CA . THR A 1 115 ? -17.099 26.021 -43.065 1.00 17.91 ? 141 THR A CA 1 ATOM 889 C C . THR A 1 115 ? -17.260 25.058 -44.236 1.00 17.79 ? 141 THR A C 1 ATOM 890 O O . THR A 1 115 ? -18.338 24.964 -44.808 1.00 17.54 ? 141 THR A O 1 ATOM 891 C CB . THR A 1 115 ? -16.347 27.293 -43.556 1.00 19.39 ? 141 THR A CB 1 ATOM 892 O OG1 . THR A 1 115 ? -16.351 28.264 -42.506 1.00 27.82 ? 141 THR A OG1 1 ATOM 893 C CG2 . THR A 1 115 ? -17.028 27.889 -44.771 1.00 36.32 ? 141 THR A CG2 1 ATOM 894 N N . THR A 1 116 ? -16.193 24.359 -44.596 1.00 17.57 ? 142 THR A N 1 ATOM 895 C CA . THR A 1 116 ? -16.244 23.474 -45.757 1.00 17.93 ? 142 THR A CA 1 ATOM 896 C C . THR A 1 116 ? -17.192 22.301 -45.521 1.00 16.26 ? 142 THR A C 1 ATOM 897 O O . THR A 1 116 ? -18.000 21.967 -46.382 1.00 16.24 ? 142 THR A O 1 ATOM 898 C CB . THR A 1 116 ? -14.851 22.939 -46.113 1.00 25.45 ? 142 THR A CB 1 ATOM 899 O OG1 . THR A 1 116 ? -13.958 24.043 -46.292 1.00 19.08 ? 142 THR A OG1 1 ATOM 900 C CG2 . THR A 1 116 ? -14.895 22.096 -47.390 1.00 22.99 ? 142 THR A CG2 1 ATOM 901 N N . VAL A 1 117 ? -17.099 21.689 -44.348 1.00 15.36 ? 143 VAL A N 1 ATOM 902 C CA . VAL A 1 117 ? -17.947 20.548 -44.027 1.00 14.31 ? 143 VAL A CA 1 ATOM 903 C C . VAL A 1 117 ? -19.425 20.948 -43.982 1.00 22.68 ? 143 VAL A C 1 ATOM 904 O O . VAL A 1 117 ? -20.271 20.306 -44.607 1.00 13.93 ? 143 VAL A O 1 ATOM 905 C CB . VAL A 1 117 ? -17.538 19.899 -42.691 1.00 15.16 ? 143 VAL A CB 1 ATOM 906 C CG1 . VAL A 1 117 ? -18.563 18.820 -42.278 1.00 12.61 ? 143 VAL A CG1 1 ATOM 907 C CG2 . VAL A 1 117 ? -16.144 19.284 -42.815 1.00 13.75 ? 143 VAL A CG2 1 ATOM 908 N N . MET A 1 118 ? -19.738 22.024 -43.270 1.00 15.41 ? 144 MET A N 1 ATOM 909 C CA . MET A 1 118 ? -21.124 22.454 -43.163 1.00 18.42 ? 144 MET A CA 1 ATOM 910 C C . MET A 1 118 ? -21.689 22.912 -44.513 1.00 15.43 ? 144 MET A C 1 ATOM 911 O O . MET A 1 118 ? -22.834 22.589 -44.834 1.00 16.88 ? 144 MET A O 1 ATOM 912 C CB . MET A 1 118 ? -21.271 23.554 -42.112 1.00 15.34 ? 144 MET A CB 1 ATOM 913 C CG . MET A 1 118 ? -21.002 23.065 -40.688 1.00 14.23 ? 144 MET A CG 1 ATOM 914 S SD . MET A 1 118 ? -21.314 24.323 -39.410 1.00 15.45 ? 144 MET A SD 1 ATOM 915 C CE . MET A 1 118 ? -23.085 24.569 -39.573 1.00 15.02 ? 144 MET A CE 1 ATOM 916 N N . THR A 1 119 ? -20.895 23.627 -45.306 1.00 16.36 ? 145 THR A N 1 ATOM 917 C CA . THR A 1 119 ? -21.359 24.057 -46.617 1.00 17.30 ? 145 THR A CA 1 ATOM 918 C C . THR A 1 119 ? -21.683 22.842 -47.489 1.00 20.80 ? 145 THR A C 1 ATOM 919 O O . THR A 1 119 ? -22.712 22.815 -48.169 1.00 19.66 ? 145 THR A O 1 ATOM 920 C CB . THR A 1 119 ? -20.323 24.956 -47.332 1.00 18.49 ? 145 THR A CB 1 ATOM 921 O OG1 . THR A 1 119 ? -20.087 26.131 -46.541 1.00 22.73 ? 145 THR A OG1 1 ATOM 922 C CG2 . THR A 1 119 ? -20.834 25.382 -48.701 1.00 19.59 ? 145 THR A CG2 1 ATOM 923 N N . HIS A 1 120 ? -20.818 21.833 -47.454 1.00 19.21 ? 146 HIS A N 1 ATOM 924 C CA . HIS A 1 120 ? -21.044 20.614 -48.241 1.00 17.67 ? 146 HIS A CA 1 ATOM 925 C C . HIS A 1 120 ? -22.420 20.017 -47.942 1.00 15.13 ? 146 HIS A C 1 ATOM 926 O O . HIS A 1 120 ? -23.191 19.734 -48.858 1.00 15.43 ? 146 HIS A O 1 ATOM 927 C CB . HIS A 1 120 ? -19.966 19.564 -47.952 1.00 21.92 ? 146 HIS A CB 1 ATOM 928 C CG . HIS A 1 120 ? -20.237 18.239 -48.589 1.00 19.66 ? 146 HIS A CG 1 ATOM 929 N ND1 . HIS A 1 120 ? -19.821 17.931 -49.867 1.00 19.23 ? 146 HIS A ND1 1 ATOM 930 C CD2 . HIS A 1 120 ? -20.903 17.150 -48.137 1.00 21.32 ? 146 HIS A CD2 1 ATOM 931 C CE1 . HIS A 1 120 ? -20.207 16.704 -50.167 1.00 24.99 ? 146 HIS A CE1 1 ATOM 932 N NE2 . HIS A 1 120 ? -20.869 16.209 -49.139 1.00 21.37 ? 146 HIS A NE2 1 ATOM 933 N N . TYR A 1 121 ? -22.726 19.853 -46.654 1.00 14.36 ? 147 TYR A N 1 ATOM 934 C CA . TYR A 1 121 ? -23.968 19.175 -46.254 1.00 18.60 ? 147 TYR A CA 1 ATOM 935 C C . TYR A 1 121 ? -25.177 20.097 -46.361 1.00 17.99 ? 147 TYR A C 1 ATOM 936 O O . TYR A 1 121 ? -26.307 19.633 -46.515 1.00 25.78 ? 147 TYR A O 1 ATOM 937 C CB . TYR A 1 121 ? -23.828 18.577 -44.844 1.00 17.18 ? 147 TYR A CB 1 ATOM 938 C CG . TYR A 1 121 ? -22.986 17.337 -44.947 1.00 12.27 ? 147 TYR A CG 1 ATOM 939 C CD1 . TYR A 1 121 ? -23.492 16.197 -45.557 1.00 14.96 ? 147 TYR A CD1 1 ATOM 940 C CD2 . TYR A 1 121 ? -21.663 17.328 -44.525 1.00 12.26 ? 147 TYR A CD2 1 ATOM 941 C CE1 . TYR A 1 121 ? -22.717 15.070 -45.723 1.00 13.93 ? 147 TYR A CE1 1 ATOM 942 C CE2 . TYR A 1 121 ? -20.870 16.195 -44.674 1.00 13.78 ? 147 TYR A CE2 1 ATOM 943 C CZ . TYR A 1 121 ? -21.402 15.070 -45.285 1.00 16.76 ? 147 TYR A CZ 1 ATOM 944 O OH . TYR A 1 121 ? -20.625 13.938 -45.452 1.00 20.53 ? 147 TYR A OH 1 ATOM 945 N N . LYS A 1 122 ? -24.934 21.399 -46.337 1.00 17.34 ? 148 LYS A N 1 ATOM 946 C CA . LYS A 1 122 ? -26.005 22.363 -46.580 1.00 21.54 ? 148 LYS A CA 1 ATOM 947 C C . LYS A 1 122 ? -26.504 22.231 -48.017 1.00 26.05 ? 148 LYS A C 1 ATOM 948 O O . LYS A 1 122 ? -27.695 22.334 -48.273 1.00 23.51 ? 148 LYS A O 1 ATOM 949 C CB . LYS A 1 122 ? -25.518 23.790 -46.305 1.00 21.35 ? 148 LYS A CB 1 ATOM 950 C CG . LYS A 1 122 ? -26.517 24.900 -46.643 1.00 25.54 ? 148 LYS A CG 1 ATOM 951 C CD . LYS A 1 122 ? -25.854 26.278 -46.525 1.00 26.69 ? 148 LYS A CD 1 ATOM 952 C CE . LYS A 1 122 ? -26.802 27.405 -46.920 1.00 33.60 ? 148 LYS A CE 1 ATOM 953 N NZ . LYS A 1 122 ? -26.097 28.708 -47.013 1.00 38.56 ? 148 LYS A NZ 1 ATOM 954 N N . GLU A 1 123 ? -25.584 21.980 -48.943 1.00 17.12 ? 149 GLU A N 1 ATOM 955 C CA . GLU A 1 123 ? -25.916 21.911 -50.358 1.00 17.97 ? 149 GLU A CA 1 ATOM 956 C C . GLU A 1 123 ? -26.417 20.542 -50.795 1.00 26.31 ? 149 GLU A C 1 ATOM 957 O O . GLU A 1 123 ? -26.996 20.409 -51.861 1.00 30.18 ? 149 GLU A O 1 ATOM 958 C CB . GLU A 1 123 ? -24.694 22.278 -51.203 1.00 23.22 ? 149 GLU A CB 1 ATOM 959 C CG . GLU A 1 123 ? -24.131 23.677 -50.949 1.00 31.89 ? 149 GLU A CG 1 ATOM 960 C CD . GLU A 1 123 ? -22.720 23.841 -51.508 1.00 51.20 ? 149 GLU A CD 1 ATOM 961 O OE1 . GLU A 1 123 ? -22.009 22.816 -51.652 1.00 52.50 ? 149 GLU A OE1 1 ATOM 962 O OE2 . GLU A 1 123 ? -22.320 24.990 -51.804 1.00 58.61 ? 149 GLU A OE2 1 ATOM 963 N N . SER A 1 124 ? -26.182 19.520 -49.983 1.00 18.29 ? 150 SER A N 1 ATOM 964 C CA . SER A 1 124 ? -26.399 18.147 -50.437 1.00 19.82 ? 150 SER A CA 1 ATOM 965 C C . SER A 1 124 ? -27.503 17.414 -49.696 1.00 14.95 ? 150 SER A C 1 ATOM 966 O O . SER A 1 124 ? -28.175 16.550 -50.266 1.00 15.56 ? 150 SER A O 1 ATOM 967 C CB . SER A 1 124 ? -25.096 17.343 -50.307 1.00 25.46 ? 150 SER A CB 1 ATOM 968 O OG . SER A 1 124 ? -24.142 17.780 -51.261 1.00 43.07 ? 150 SER A OG 1 ATOM 969 N N . PHE A 1 125 ? -27.682 17.743 -48.425 1.00 16.53 ? 151 PHE A N 1 ATOM 970 C CA . PHE A 1 125 ? -28.573 16.962 -47.571 1.00 17.26 ? 151 PHE A CA 1 ATOM 971 C C . PHE A 1 125 ? -29.309 17.859 -46.596 1.00 18.65 ? 151 PHE A C 1 ATOM 972 O O . PHE A 1 125 ? -29.117 19.070 -46.603 1.00 17.59 ? 151 PHE A O 1 ATOM 973 C CB . PHE A 1 125 ? -27.785 15.888 -46.813 1.00 12.81 ? 151 PHE A CB 1 ATOM 974 C CG . PHE A 1 125 ? -27.193 14.825 -47.702 1.00 14.17 ? 151 PHE A CG 1 ATOM 975 C CD1 . PHE A 1 125 ? -27.986 13.793 -48.197 1.00 12.62 ? 151 PHE A CD1 1 ATOM 976 C CD2 . PHE A 1 125 ? -25.843 14.852 -48.042 1.00 15.42 ? 151 PHE A CD2 1 ATOM 977 C CE1 . PHE A 1 125 ? -27.447 12.819 -49.020 1.00 12.59 ? 151 PHE A CE1 1 ATOM 978 C CE2 . PHE A 1 125 ? -25.293 13.870 -48.862 1.00 15.42 ? 151 PHE A CE2 1 ATOM 979 C CZ . PHE A 1 125 ? -26.098 12.852 -49.355 1.00 13.89 ? 151 PHE A CZ 1 ATOM 980 N N . ASN A 1 126 ? -30.164 17.264 -45.766 1.00 17.41 ? 152 ASN A N 1 ATOM 981 C CA . ASN A 1 126 ? -30.836 18.013 -44.709 1.00 17.26 ? 152 ASN A CA 1 ATOM 982 C C . ASN A 1 126 ? -30.265 17.594 -43.368 1.00 14.26 ? 152 ASN A C 1 ATOM 983 O O . ASN A 1 126 ? -30.584 16.518 -42.865 1.00 19.65 ? 152 ASN A O 1 ATOM 984 C CB . ASN A 1 126 ? -32.352 17.782 -44.728 1.00 14.51 ? 152 ASN A CB 1 ATOM 985 C CG . ASN A 1 126 ? -33.058 18.576 -45.815 1.00 25.43 ? 152 ASN A CG 1 ATOM 986 O OD1 . ASN A 1 126 ? -32.914 19.793 -45.896 1.00 25.09 ? 152 ASN A OD1 1 ATOM 987 N ND2 . ASN A 1 126 ? -33.856 17.890 -46.637 1.00 21.48 ? 152 ASN A ND2 1 ATOM 988 N N . ILE A 1 127 ? -29.406 18.431 -42.797 1.00 13.07 ? 153 ILE A N 1 ATOM 989 C CA . ILE A 1 127 ? -28.856 18.130 -41.489 1.00 12.38 ? 153 ILE A CA 1 ATOM 990 C C . ILE A 1 127 ? -29.716 18.875 -40.467 1.00 12.85 ? 153 ILE A C 1 ATOM 991 O O . ILE A 1 127 ? -29.751 20.103 -40.458 1.00 13.59 ? 153 ILE A O 1 ATOM 992 C CB . ILE A 1 127 ? -27.364 18.532 -41.355 1.00 13.09 ? 153 ILE A CB 1 ATOM 993 C CG1 . ILE A 1 127 ? -26.430 17.487 -41.984 1.00 19.62 ? 153 ILE A CG1 1 ATOM 994 C CG2 . ILE A 1 127 ? -26.966 18.593 -39.886 1.00 11.78 ? 153 ILE A CG2 1 ATOM 995 C CD1 . ILE A 1 127 ? -26.762 17.082 -43.400 1.00 35.39 ? 153 ILE A CD1 1 ATOM 996 N N . TYR A 1 128 ? -30.427 18.130 -39.623 1.00 12.56 ? 154 TYR A N 1 ATOM 997 C CA . TYR A 1 128 ? -31.287 18.758 -38.626 1.00 13.13 ? 154 TYR A CA 1 ATOM 998 C C . TYR A 1 128 ? -30.481 19.513 -37.580 1.00 16.61 ? 154 TYR A C 1 ATOM 999 O O . TYR A 1 128 ? -30.827 20.639 -37.197 1.00 14.18 ? 154 TYR A O 1 ATOM 1000 C CB . TYR A 1 128 ? -32.164 17.729 -37.918 1.00 12.93 ? 154 TYR A CB 1 ATOM 1001 C CG . TYR A 1 128 ? -32.872 18.340 -36.731 1.00 13.54 ? 154 TYR A CG 1 ATOM 1002 C CD1 . TYR A 1 128 ? -33.946 19.201 -36.915 1.00 16.46 ? 154 TYR A CD1 1 ATOM 1003 C CD2 . TYR A 1 128 ? -32.460 18.074 -35.434 1.00 14.07 ? 154 TYR A CD2 1 ATOM 1004 C CE1 . TYR A 1 128 ? -34.598 19.779 -35.835 1.00 26.71 ? 154 TYR A CE1 1 ATOM 1005 C CE2 . TYR A 1 128 ? -33.106 18.656 -34.338 1.00 13.86 ? 154 TYR A CE2 1 ATOM 1006 C CZ . TYR A 1 128 ? -34.170 19.499 -34.553 1.00 23.98 ? 154 TYR A CZ 1 ATOM 1007 O OH . TYR A 1 128 ? -34.801 20.071 -33.479 1.00 18.73 ? 154 TYR A OH 1 ATOM 1008 N N . ALA A 1 129 ? -29.410 18.886 -37.109 1.00 12.28 ? 155 ALA A N 1 ATOM 1009 C CA . ALA A 1 129 ? -28.575 19.477 -36.064 1.00 12.72 ? 155 ALA A CA 1 ATOM 1010 C C . ALA A 1 129 ? -27.112 19.077 -36.230 1.00 17.02 ? 155 ALA A C 1 ATOM 1011 O O . ALA A 1 129 ? -26.815 17.950 -36.637 1.00 17.67 ? 155 ALA A O 1 ATOM 1012 C CB . ALA A 1 129 ? -29.074 19.050 -34.669 1.00 15.00 ? 155 ALA A CB 1 ATOM 1013 N N . TRP A 1 130 ? -26.217 20.005 -35.900 1.00 11.90 ? 156 TRP A N 1 ATOM 1014 C CA . TRP A 1 130 ? -24.773 19.763 -35.854 1.00 18.22 ? 156 TRP A CA 1 ATOM 1015 C C . TRP A 1 130 ? -24.256 19.762 -34.415 1.00 16.89 ? 156 TRP A C 1 ATOM 1016 O O . TRP A 1 130 ? -24.489 20.713 -33.677 1.00 13.01 ? 156 TRP A O 1 ATOM 1017 C CB . TRP A 1 130 ? -24.003 20.837 -36.638 1.00 14.69 ? 156 TRP A CB 1 ATOM 1018 C CG . TRP A 1 130 ? -23.819 20.548 -38.102 1.00 14.66 ? 156 TRP A CG 1 ATOM 1019 C CD1 . TRP A 1 130 ? -24.448 21.156 -39.157 1.00 17.00 ? 156 TRP A CD1 1 ATOM 1020 C CD2 . TRP A 1 130 ? -22.942 19.571 -38.664 1.00 14.20 ? 156 TRP A CD2 1 ATOM 1021 N NE1 . TRP A 1 130 ? -24.004 20.612 -40.347 1.00 17.34 ? 156 TRP A NE1 1 ATOM 1022 C CE2 . TRP A 1 130 ? -23.084 19.634 -40.065 1.00 12.61 ? 156 TRP A CE2 1 ATOM 1023 C CE3 . TRP A 1 130 ? -22.047 18.646 -38.114 1.00 13.82 ? 156 TRP A CE3 1 ATOM 1024 C CZ2 . TRP A 1 130 ? -22.373 18.802 -40.922 1.00 16.04 ? 156 TRP A CZ2 1 ATOM 1025 C CZ3 . TRP A 1 130 ? -21.345 17.820 -38.967 1.00 24.61 ? 156 TRP A CZ3 1 ATOM 1026 C CH2 . TRP A 1 130 ? -21.514 17.901 -40.353 1.00 18.93 ? 156 TRP A CH2 1 ATOM 1027 N N . ASP A 1 131 ? -23.556 18.704 -34.018 1.00 16.87 ? 157 ASP A N 1 ATOM 1028 C CA . ASP A 1 131 ? -22.714 18.778 -32.823 1.00 17.63 ? 157 ASP A CA 1 ATOM 1029 C C . ASP A 1 131 ? -21.450 19.515 -33.225 1.00 16.12 ? 157 ASP A C 1 ATOM 1030 O O . ASP A 1 131 ? -20.551 18.913 -33.817 1.00 17.81 ? 157 ASP A O 1 ATOM 1031 C CB . ASP A 1 131 ? -22.367 17.380 -32.275 1.00 16.81 ? 157 ASP A CB 1 ATOM 1032 C CG . ASP A 1 131 ? -23.589 16.627 -31.705 1.00 29.17 ? 157 ASP A CG 1 ATOM 1033 O OD1 . ASP A 1 131 ? -24.558 17.274 -31.235 1.00 28.50 ? 157 ASP A OD1 1 ATOM 1034 O OD2 . ASP A 1 131 ? -23.564 15.368 -31.716 1.00 26.45 ? 157 ASP A OD2 1 ATOM 1035 N N . VAL A 1 132 ? -21.375 20.813 -32.952 1.00 11.89 ? 158 VAL A N 1 ATOM 1036 C CA . VAL A 1 132 ? -20.215 21.579 -33.396 1.00 12.37 ? 158 VAL A CA 1 ATOM 1037 C C . VAL A 1 132 ? -19.008 21.287 -32.513 1.00 19.65 ? 158 VAL A C 1 ATOM 1038 O O . VAL A 1 132 ? -17.974 20.820 -32.996 1.00 26.73 ? 158 VAL A O 1 ATOM 1039 C CB . VAL A 1 132 ? -20.481 23.095 -33.399 1.00 14.85 ? 158 VAL A CB 1 ATOM 1040 C CG1 . VAL A 1 132 ? -19.213 23.845 -33.801 1.00 16.06 ? 158 VAL A CG1 1 ATOM 1041 C CG2 . VAL A 1 132 ? -21.622 23.424 -34.356 1.00 17.86 ? 158 VAL A CG2 1 ATOM 1042 N N . VAL A 1 133 ? -19.157 21.563 -31.218 1.00 13.44 ? 159 VAL A N 1 ATOM 1043 C CA . VAL A 1 133 ? -18.128 21.263 -30.228 1.00 12.70 ? 159 VAL A CA 1 ATOM 1044 C C . VAL A 1 133 ? -18.564 20.072 -29.387 1.00 18.06 ? 159 VAL A C 1 ATOM 1045 O O . VAL A 1 133 ? -19.695 20.029 -28.910 1.00 16.06 ? 159 VAL A O 1 ATOM 1046 C CB . VAL A 1 133 ? -17.865 22.477 -29.319 1.00 13.58 ? 159 VAL A CB 1 ATOM 1047 C CG1 . VAL A 1 133 ? -16.986 22.100 -28.133 1.00 14.22 ? 159 VAL A CG1 1 ATOM 1048 C CG2 . VAL A 1 133 ? -17.232 23.613 -30.130 1.00 16.51 ? 159 VAL A CG2 1 ATOM 1049 N N . ASN A 1 134 ? -17.666 19.107 -29.217 1.00 13.60 ? 160 ASN A N 1 ATOM 1050 C CA . ASN A 1 134 ? -17.932 17.910 -28.418 1.00 11.64 ? 160 ASN A CA 1 ATOM 1051 C C . ASN A 1 134 ? -16.911 17.801 -27.281 1.00 14.76 ? 160 ASN A C 1 ATOM 1052 O O . ASN A 1 134 ? -15.712 18.021 -27.498 1.00 14.69 ? 160 ASN A O 1 ATOM 1053 C CB . ASN A 1 134 ? -17.881 16.657 -29.318 1.00 13.23 ? 160 ASN A CB 1 ATOM 1054 C CG . ASN A 1 134 ? -18.391 15.408 -28.624 1.00 22.72 ? 160 ASN A CG 1 ATOM 1055 O OD1 . ASN A 1 134 ? -19.281 15.476 -27.773 1.00 26.61 ? 160 ASN A OD1 1 ATOM 1056 N ND2 . ASN A 1 134 ? -17.828 14.253 -28.987 1.00 16.48 ? 160 ASN A ND2 1 ATOM 1057 N N . GLU A 1 135 ? -17.392 17.509 -26.071 1.00 14.04 ? 161 GLU A N 1 ATOM 1058 C CA . GLU A 1 135 ? -16.542 17.215 -24.908 1.00 13.13 ? 161 GLU A CA 1 ATOM 1059 C C . GLU A 1 135 ? -15.497 18.299 -24.607 1.00 17.63 ? 161 GLU A C 1 ATOM 1060 O O . GLU A 1 135 ? -14.295 18.030 -24.536 1.00 17.76 ? 161 GLU A O 1 ATOM 1061 C CB . GLU A 1 135 ? -15.867 15.838 -25.102 1.00 16.84 ? 161 GLU A CB 1 ATOM 1062 C CG . GLU A 1 135 ? -16.915 14.683 -25.202 1.00 13.77 ? 161 GLU A CG 1 ATOM 1063 C CD . GLU A 1 135 ? -16.315 13.295 -25.494 1.00 20.42 ? 161 GLU A CD 1 ATOM 1064 O OE1 . GLU A 1 135 ? -15.069 13.144 -25.500 1.00 20.32 ? 161 GLU A OE1 1 ATOM 1065 O OE2 . GLU A 1 135 ? -17.105 12.345 -25.727 1.00 23.13 ? 161 GLU A OE2 1 ATOM 1066 N N . ALA A 1 136 ? -15.967 19.521 -24.388 1.00 14.61 ? 162 ALA A N 1 ATOM 1067 C CA . ALA A 1 136 ? -15.071 20.652 -24.161 1.00 20.61 ? 162 ALA A CA 1 ATOM 1068 C C . ALA A 1 136 ? -14.724 20.872 -22.684 1.00 17.97 ? 162 ALA A C 1 ATOM 1069 O O . ALA A 1 136 ? -13.940 21.755 -22.362 1.00 20.80 ? 162 ALA A O 1 ATOM 1070 C CB . ALA A 1 136 ? -15.679 21.918 -24.737 1.00 14.82 ? 162 ALA A CB 1 ATOM 1071 N N . PHE A 1 137 ? -15.301 20.079 -21.787 1.00 15.29 ? 163 PHE A N 1 ATOM 1072 C CA . PHE A 1 137 ? -15.075 20.273 -20.358 1.00 16.11 ? 163 PHE A CA 1 ATOM 1073 C C . PHE A 1 137 ? -14.464 19.051 -19.679 1.00 18.80 ? 163 PHE A C 1 ATOM 1074 O O . PHE A 1 137 ? -14.576 17.930 -20.183 1.00 15.65 ? 163 PHE A O 1 ATOM 1075 C CB . PHE A 1 137 ? -16.385 20.630 -19.657 1.00 17.99 ? 163 PHE A CB 1 ATOM 1076 C CG . PHE A 1 137 ? -17.017 21.863 -20.186 1.00 22.97 ? 163 PHE A CG 1 ATOM 1077 C CD1 . PHE A 1 137 ? -16.705 23.098 -19.641 1.00 21.41 ? 163 PHE A CD1 1 ATOM 1078 C CD2 . PHE A 1 137 ? -17.890 21.799 -21.258 1.00 21.51 ? 163 PHE A CD2 1 ATOM 1079 C CE1 . PHE A 1 137 ? -17.266 24.245 -20.140 1.00 21.05 ? 163 PHE A CE1 1 ATOM 1080 C CE2 . PHE A 1 137 ? -18.452 22.946 -21.771 1.00 23.36 ? 163 PHE A CE2 1 ATOM 1081 C CZ . PHE A 1 137 ? -18.138 24.173 -21.204 1.00 19.33 ? 163 PHE A CZ 1 ATOM 1082 N N . ASN A 1 138 ? -13.805 19.296 -18.547 1.00 22.90 ? 164 ASN A N 1 ATOM 1083 C CA . ASN A 1 138 ? -13.331 18.253 -17.644 1.00 18.72 ? 164 ASN A CA 1 ATOM 1084 C C . ASN A 1 138 ? -14.394 17.969 -16.595 1.00 23.55 ? 164 ASN A C 1 ATOM 1085 O O . ASN A 1 138 ? -15.259 18.808 -16.345 1.00 18.02 ? 164 ASN A O 1 ATOM 1086 C CB . ASN A 1 138 ? -12.030 18.672 -16.955 1.00 18.75 ? 164 ASN A CB 1 ATOM 1087 C CG . ASN A 1 138 ? -10.871 18.820 -17.926 1.00 18.78 ? 164 ASN A CG 1 ATOM 1088 O OD1 . ASN A 1 138 ? -10.691 17.992 -18.806 1.00 20.79 ? 164 ASN A OD1 1 ATOM 1089 N ND2 . ASN A 1 138 ? -10.072 19.884 -17.762 1.00 20.72 ? 164 ASN A ND2 1 ATOM 1090 N N . ASP A 1 139 ? -14.315 16.800 -15.967 1.00 23.64 ? 165 ASP A N 1 ATOM 1091 C CA . ASP A 1 139 ? -15.260 16.421 -14.916 1.00 30.07 ? 165 ASP A CA 1 ATOM 1092 C C . ASP A 1 139 ? -15.351 17.422 -13.735 1.00 27.02 ? 165 ASP A C 1 ATOM 1093 O O . ASP A 1 139 ? -16.423 17.571 -13.137 1.00 28.15 ? 165 ASP A O 1 ATOM 1094 C CB . ASP A 1 139 ? -14.914 15.014 -14.390 1.00 34.61 ? 165 ASP A CB 1 ATOM 1095 C CG . ASP A 1 139 ? -15.171 13.903 -15.431 1.00 47.58 ? 165 ASP A CG 1 ATOM 1096 O OD1 . ASP A 1 139 ? -16.024 14.068 -16.336 1.00 48.13 ? 165 ASP A OD1 1 ATOM 1097 O OD2 . ASP A 1 139 ? -14.512 12.846 -15.345 1.00 55.51 ? 165 ASP A OD2 1 ATOM 1098 N N . ASN A 1 140 ? -14.262 18.112 -13.385 1.00 20.23 ? 166 ASN A N 1 ATOM 1099 C CA . ASN A 1 140 ? -14.327 19.070 -12.279 1.00 21.31 ? 166 ASN A CA 1 ATOM 1100 C C . ASN A 1 140 ? -14.847 20.443 -12.687 1.00 24.89 ? 166 ASN A C 1 ATOM 1101 O O . ASN A 1 140 ? -14.830 21.378 -11.876 1.00 25.51 ? 166 ASN A O 1 ATOM 1102 C CB . ASN A 1 140 ? -12.959 19.259 -11.600 1.00 25.13 ? 166 ASN A CB 1 ATOM 1103 C CG . ASN A 1 140 ? -11.863 19.591 -12.584 1.00 30.05 ? 166 ASN A CG 1 ATOM 1104 O OD1 . ASN A 1 140 ? -12.139 20.020 -13.711 1.00 22.16 ? 166 ASN A OD1 1 ATOM 1105 N ND2 . ASN A 1 140 ? -10.605 19.389 -12.170 1.00 32.64 ? 166 ASN A ND2 1 ATOM 1106 N N . GLY A 1 141 ? -15.284 20.575 -13.935 1.00 26.80 ? 167 GLY A N 1 ATOM 1107 C CA . GLY A 1 141 ? -15.894 21.812 -14.386 1.00 33.55 ? 167 GLY A CA 1 ATOM 1108 C C . GLY A 1 141 ? -14.952 22.834 -15.005 1.00 32.49 ? 167 GLY A C 1 ATOM 1109 O O . GLY A 1 141 ? -15.361 23.959 -15.288 1.00 32.19 ? 167 GLY A O 1 ATOM 1110 N N . THR A 1 142 ? -13.694 22.459 -15.211 1.00 25.98 ? 168 THR A N 1 ATOM 1111 C CA . THR A 1 142 ? -12.759 23.321 -15.929 1.00 20.69 ? 168 THR A CA 1 ATOM 1112 C C . THR A 1 142 ? -12.825 23.028 -17.426 1.00 19.61 ? 168 THR A C 1 ATOM 1113 O O . THR A 1 142 ? -13.363 21.997 -17.836 1.00 19.69 ? 168 THR A O 1 ATOM 1114 C CB . THR A 1 142 ? -11.315 23.131 -15.436 1.00 22.92 ? 168 THR A CB 1 ATOM 1115 O OG1 . THR A 1 142 ? -10.940 21.753 -15.551 1.00 21.10 ? 168 THR A OG1 1 ATOM 1116 C CG2 . THR A 1 142 ? -11.190 23.563 -13.982 1.00 22.77 ? 168 THR A CG2 1 ATOM 1117 N N . TYR A 1 143 ? -12.277 23.921 -18.244 1.00 19.80 ? 169 TYR A N 1 ATOM 1118 C CA . TYR A 1 143 ? -12.190 23.665 -19.677 1.00 20.08 ? 169 TYR A CA 1 ATOM 1119 C C . TYR A 1 143 ? -11.166 22.573 -19.967 1.00 19.46 ? 169 TYR A C 1 ATOM 1120 O O . TYR A 1 143 ? -10.066 22.596 -19.418 1.00 19.67 ? 169 TYR A O 1 ATOM 1121 C CB . TYR A 1 143 ? -11.803 24.938 -20.429 1.00 20.12 ? 169 TYR A CB 1 ATOM 1122 C CG . TYR A 1 143 ? -12.845 26.032 -20.398 1.00 21.34 ? 169 TYR A CG 1 ATOM 1123 C CD1 . TYR A 1 143 ? -14.032 25.910 -21.120 1.00 23.25 ? 169 TYR A CD1 1 ATOM 1124 C CD2 . TYR A 1 143 ? -12.642 27.186 -19.655 1.00 20.82 ? 169 TYR A CD2 1 ATOM 1125 C CE1 . TYR A 1 143 ? -14.992 26.916 -21.094 1.00 24.65 ? 169 TYR A CE1 1 ATOM 1126 C CE2 . TYR A 1 143 ? -13.590 28.196 -19.625 1.00 25.72 ? 169 TYR A CE2 1 ATOM 1127 C CZ . TYR A 1 143 ? -14.761 28.059 -20.349 1.00 22.54 ? 169 TYR A CZ 1 ATOM 1128 O OH . TYR A 1 143 ? -15.700 29.061 -20.319 1.00 33.29 ? 169 TYR A OH 1 ATOM 1129 N N . ARG A 1 144 ? -11.524 21.617 -20.822 1.00 17.87 ? 170 ARG A N 1 ATOM 1130 C CA . ARG A 1 144 ? -10.564 20.610 -21.268 1.00 17.76 ? 170 ARG A CA 1 ATOM 1131 C C . ARG A 1 144 ? -9.425 21.289 -22.048 1.00 19.93 ? 170 ARG A C 1 ATOM 1132 O O . ARG A 1 144 ? -9.671 22.045 -22.991 1.00 18.13 ? 170 ARG A O 1 ATOM 1133 C CB . ARG A 1 144 ? -11.251 19.548 -22.141 1.00 25.39 ? 170 ARG A CB 1 ATOM 1134 C CG . ARG A 1 144 ? -10.326 18.422 -22.607 1.00 16.67 ? 170 ARG A CG 1 ATOM 1135 C CD . ARG A 1 144 ? -10.999 17.510 -23.643 1.00 15.66 ? 170 ARG A CD 1 ATOM 1136 N NE . ARG A 1 144 ? -12.167 16.786 -23.126 1.00 16.65 ? 170 ARG A NE 1 ATOM 1137 C CZ . ARG A 1 144 ? -12.088 15.705 -22.356 1.00 24.02 ? 170 ARG A CZ 1 ATOM 1138 N NH1 . ARG A 1 144 ? -10.896 15.233 -21.991 1.00 19.18 ? 170 ARG A NH1 1 ATOM 1139 N NH2 . ARG A 1 144 ? -13.192 15.096 -21.942 1.00 22.73 ? 170 ARG A NH2 1 ATOM 1140 N N . GLU A 1 145 ? -8.182 21.014 -21.661 1.00 20.94 ? 171 GLU A N 1 ATOM 1141 C CA . GLU A 1 145 ? -7.033 21.611 -22.340 1.00 22.32 ? 171 GLU A CA 1 ATOM 1142 C C . GLU A 1 145 ? -6.620 20.862 -23.614 1.00 28.06 ? 171 GLU A C 1 ATOM 1143 O O . GLU A 1 145 ? -5.512 20.333 -23.710 1.00 28.72 ? 171 GLU A O 1 ATOM 1144 C CB . GLU A 1 145 ? -5.839 21.710 -21.378 1.00 27.45 ? 171 GLU A CB 1 ATOM 1145 C CG . GLU A 1 145 ? -6.147 22.518 -20.135 1.00 31.54 ? 171 GLU A CG 1 ATOM 1146 C CD . GLU A 1 145 ? -4.931 23.232 -19.569 1.00 44.57 ? 171 GLU A CD 1 ATOM 1147 O OE1 . GLU A 1 145 ? -3.844 23.146 -20.182 1.00 51.81 ? 171 GLU A OE1 1 ATOM 1148 O OE2 . GLU A 1 145 ? -5.067 23.884 -18.514 1.00 48.77 ? 171 GLU A OE2 1 ATOM 1149 N N . ASN A 1 146 ? -7.514 20.845 -24.597 1.00 18.58 ? 172 ASN A N 1 ATOM 1150 C CA . ASN A 1 146 ? -7.200 20.326 -25.922 1.00 21.49 ? 172 ASN A CA 1 ATOM 1151 C C . ASN A 1 146 ? -6.399 21.357 -26.706 1.00 19.09 ? 172 ASN A C 1 ATOM 1152 O O . ASN A 1 146 ? -6.039 22.395 -26.162 1.00 21.80 ? 172 ASN A O 1 ATOM 1153 C CB . ASN A 1 146 ? -8.480 19.945 -26.669 1.00 17.03 ? 172 ASN A CB 1 ATOM 1154 C CG . ASN A 1 146 ? -9.491 21.092 -26.742 1.00 23.63 ? 172 ASN A CG 1 ATOM 1155 O OD1 . ASN A 1 146 ? -9.128 22.270 -26.796 1.00 17.49 ? 172 ASN A OD1 1 ATOM 1156 N ND2 . ASN A 1 146 ? -10.777 20.738 -26.754 1.00 17.10 ? 172 ASN A ND2 1 ATOM 1157 N N . VAL A 1 147 ? -6.134 21.095 -27.983 1.00 18.97 ? 173 VAL A N 1 ATOM 1158 C CA . VAL A 1 147 ? -5.245 21.980 -28.742 1.00 22.37 ? 173 VAL A CA 1 ATOM 1159 C C . VAL A 1 147 ? -5.823 23.399 -28.900 1.00 21.84 ? 173 VAL A C 1 ATOM 1160 O O . VAL A 1 147 ? -5.086 24.387 -28.795 1.00 21.25 ? 173 VAL A O 1 ATOM 1161 C CB . VAL A 1 147 ? -4.898 21.388 -30.138 1.00 29.45 ? 173 VAL A CB 1 ATOM 1162 C CG1 . VAL A 1 147 ? -6.152 21.070 -30.957 1.00 18.66 ? 173 VAL A CG1 1 ATOM 1163 C CG2 . VAL A 1 147 ? -3.964 22.323 -30.897 1.00 33.57 ? 173 VAL A CG2 1 ATOM 1164 N N . TRP A 1 148 ? -7.135 23.509 -29.102 1.00 19.12 ? 174 TRP A N 1 ATOM 1165 C CA . TRP A 1 148 ? -7.746 24.823 -29.290 1.00 22.10 ? 174 TRP A CA 1 ATOM 1166 C C . TRP A 1 148 ? -7.697 25.656 -28.008 1.00 20.04 ? 174 TRP A C 1 ATOM 1167 O O . TRP A 1 148 ? -7.376 26.845 -28.050 1.00 21.01 ? 174 TRP A O 1 ATOM 1168 C CB . TRP A 1 148 ? -9.187 24.682 -29.786 1.00 25.12 ? 174 TRP A CB 1 ATOM 1169 C CG . TRP A 1 148 ? -9.272 23.904 -31.057 1.00 18.89 ? 174 TRP A CG 1 ATOM 1170 C CD1 . TRP A 1 148 ? -9.080 24.372 -32.323 1.00 18.10 ? 174 TRP A CD1 1 ATOM 1171 C CD2 . TRP A 1 148 ? -9.558 22.505 -31.183 1.00 17.82 ? 174 TRP A CD2 1 ATOM 1172 N NE1 . TRP A 1 148 ? -9.237 23.354 -33.231 1.00 17.45 ? 174 TRP A NE1 1 ATOM 1173 C CE2 . TRP A 1 148 ? -9.528 22.197 -32.558 1.00 19.16 ? 174 TRP A CE2 1 ATOM 1174 C CE3 . TRP A 1 148 ? -9.841 21.485 -30.265 1.00 16.18 ? 174 TRP A CE3 1 ATOM 1175 C CZ2 . TRP A 1 148 ? -9.763 20.911 -33.040 1.00 15.89 ? 174 TRP A CZ2 1 ATOM 1176 C CZ3 . TRP A 1 148 ? -10.086 20.208 -30.744 1.00 18.95 ? 174 TRP A CZ3 1 ATOM 1177 C CH2 . TRP A 1 148 ? -10.037 19.930 -32.121 1.00 15.31 ? 174 TRP A CH2 1 ATOM 1178 N N . TYR A 1 149 ? -7.989 25.036 -26.870 1.00 19.65 ? 175 TYR A N 1 ATOM 1179 C CA . TYR A 1 149 ? -7.864 25.737 -25.595 1.00 20.40 ? 175 TYR A CA 1 ATOM 1180 C C . TYR A 1 149 ? -6.430 26.205 -25.368 1.00 25.11 ? 175 TYR A C 1 ATOM 1181 O O . TYR A 1 149 ? -6.185 27.357 -24.996 1.00 23.88 ? 175 TYR A O 1 ATOM 1182 C CB . TYR A 1 149 ? -8.297 24.856 -24.421 1.00 19.90 ? 175 TYR A CB 1 ATOM 1183 C CG . TYR A 1 149 ? -8.147 25.572 -23.088 1.00 20.80 ? 175 TYR A CG 1 ATOM 1184 C CD1 . TYR A 1 149 ? -9.164 26.387 -22.603 1.00 24.34 ? 175 TYR A CD1 1 ATOM 1185 C CD2 . TYR A 1 149 ? -6.981 25.466 -22.340 1.00 23.32 ? 175 TYR A CD2 1 ATOM 1186 C CE1 . TYR A 1 149 ? -9.035 27.063 -21.401 1.00 21.74 ? 175 TYR A CE1 1 ATOM 1187 C CE2 . TYR A 1 149 ? -6.839 26.145 -21.127 1.00 28.76 ? 175 TYR A CE2 1 ATOM 1188 C CZ . TYR A 1 149 ? -7.873 26.939 -20.666 1.00 29.44 ? 175 TYR A CZ 1 ATOM 1189 O OH . TYR A 1 149 ? -7.752 27.617 -19.472 1.00 31.58 ? 175 TYR A OH 1 ATOM 1190 N N . THR A 1 150 ? -5.485 25.299 -25.576 1.00 20.81 ? 176 THR A N 1 ATOM 1191 C CA . THR A 1 150 ? -4.072 25.605 -25.375 1.00 20.10 ? 176 THR A CA 1 ATOM 1192 C C . THR A 1 150 ? -3.592 26.751 -26.265 1.00 26.95 ? 176 THR A C 1 ATOM 1193 O O . THR A 1 150 ? -2.817 27.600 -25.839 1.00 25.95 ? 176 THR A O 1 ATOM 1194 C CB . THR A 1 150 ? -3.213 24.360 -25.642 1.00 35.61 ? 176 THR A CB 1 ATOM 1195 O OG1 . THR A 1 150 ? -3.543 23.349 -24.681 1.00 33.95 ? 176 THR A OG1 1 ATOM 1196 C CG2 . THR A 1 150 ? -1.735 24.690 -25.549 1.00 37.58 ? 176 THR A CG2 1 ATOM 1197 N N . GLN A 1 151 ? -4.069 26.791 -27.502 1.00 24.45 ? 177 GLN A N 1 ATOM 1198 C CA . GLN A 1 151 ? -3.578 27.781 -28.454 1.00 21.12 ? 177 GLN A CA 1 ATOM 1199 C C . GLN A 1 151 ? -4.425 29.050 -28.513 1.00 26.69 ? 177 GLN A C 1 ATOM 1200 O O . GLN A 1 151 ? -3.932 30.108 -28.878 1.00 26.10 ? 177 GLN A O 1 ATOM 1201 C CB . GLN A 1 151 ? -3.494 27.155 -29.843 1.00 22.26 ? 177 GLN A CB 1 ATOM 1202 C CG . GLN A 1 151 ? -2.453 26.059 -29.951 1.00 20.86 ? 177 GLN A CG 1 ATOM 1203 C CD . GLN A 1 151 ? -1.053 26.607 -29.793 1.00 21.96 ? 177 GLN A CD 1 ATOM 1204 O OE1 . GLN A 1 151 ? -0.763 27.726 -30.223 1.00 26.42 ? 177 GLN A OE1 1 ATOM 1205 N NE2 . GLN A 1 151 ? -0.179 25.836 -29.161 1.00 28.41 ? 177 GLN A NE2 1 ATOM 1206 N N . LEU A 1 152 ? -5.702 28.955 -28.156 1.00 20.63 ? 178 LEU A N 1 ATOM 1207 C CA . LEU A 1 152 ? -6.607 30.074 -28.375 1.00 24.96 ? 178 LEU A CA 1 ATOM 1208 C C . LEU A 1 152 ? -7.371 30.491 -27.120 1.00 23.83 ? 178 LEU A C 1 ATOM 1209 O O . LEU A 1 152 ? -8.081 31.487 -27.135 1.00 27.77 ? 178 LEU A O 1 ATOM 1210 C CB . LEU A 1 152 ? -7.606 29.728 -29.489 1.00 20.63 ? 178 LEU A CB 1 ATOM 1211 C CG . LEU A 1 152 ? -7.038 29.085 -30.764 1.00 24.82 ? 178 LEU A CG 1 ATOM 1212 C CD1 . LEU A 1 152 ? -8.158 28.432 -31.578 1.00 19.21 ? 178 LEU A CD1 1 ATOM 1213 C CD2 . LEU A 1 152 ? -6.279 30.105 -31.611 1.00 23.92 ? 178 LEU A CD2 1 ATOM 1214 N N . GLY A 1 153 ? -7.250 29.719 -26.044 1.00 24.55 ? 179 GLY A N 1 ATOM 1215 C CA . GLY A 1 153 ? -8.015 29.996 -24.838 1.00 20.39 ? 179 GLY A CA 1 ATOM 1216 C C . GLY A 1 153 ? -9.483 29.612 -25.002 1.00 30.45 ? 179 GLY A C 1 ATOM 1217 O O . GLY A 1 153 ? -9.905 29.171 -26.078 1.00 27.65 ? 179 GLY A O 1 ATOM 1218 N N . PRO A 1 154 ? -10.275 29.789 -23.933 1.00 30.47 ? 180 PRO A N 1 ATOM 1219 C CA . PRO A 1 154 ? -11.669 29.328 -23.845 1.00 28.81 ? 180 PRO A CA 1 ATOM 1220 C C . PRO A 1 154 ? -12.586 29.946 -24.906 1.00 25.21 ? 180 PRO A C 1 ATOM 1221 O O . PRO A 1 154 ? -13.661 29.410 -25.179 1.00 23.44 ? 180 PRO A O 1 ATOM 1222 C CB . PRO A 1 154 ? -12.110 29.781 -22.443 1.00 34.55 ? 180 PRO A CB 1 ATOM 1223 C CG . PRO A 1 154 ? -10.855 30.082 -21.707 1.00 35.43 ? 180 PRO A CG 1 ATOM 1224 C CD . PRO A 1 154 ? -9.848 30.509 -22.721 1.00 26.10 ? 180 PRO A CD 1 ATOM 1225 N N . ASP A 1 155 ? -12.173 31.063 -25.493 1.00 20.44 ? 181 ASP A N 1 ATOM 1226 C CA . ASP A 1 155 ? -13.008 31.730 -26.488 1.00 23.62 ? 181 ASP A CA 1 ATOM 1227 C C . ASP A 1 155 ? -13.250 30.893 -27.743 1.00 18.68 ? 181 ASP A C 1 ATOM 1228 O O . ASP A 1 155 ? -14.127 31.231 -28.543 1.00 19.99 ? 181 ASP A O 1 ATOM 1229 C CB . ASP A 1 155 ? -12.394 33.074 -26.893 1.00 37.18 ? 181 ASP A CB 1 ATOM 1230 C CG . ASP A 1 155 ? -12.589 34.150 -25.838 1.00 49.22 ? 181 ASP A CG 1 ATOM 1231 O OD1 . ASP A 1 155 ? -13.478 33.987 -24.975 1.00 59.45 ? 181 ASP A OD1 1 ATOM 1232 O OD2 . ASP A 1 155 ? -11.855 35.159 -25.868 1.00 56.52 ? 181 ASP A OD2 1 ATOM 1233 N N . TYR A 1 156 ? -12.480 29.820 -27.928 1.00 18.32 ? 182 TYR A N 1 ATOM 1234 C CA . TYR A 1 156 ? -12.621 29.019 -29.136 1.00 20.83 ? 182 TYR A CA 1 ATOM 1235 C C . TYR A 1 156 ? -14.017 28.431 -29.225 1.00 17.08 ? 182 TYR A C 1 ATOM 1236 O O . TYR A 1 156 ? -14.529 28.219 -30.317 1.00 20.86 ? 182 TYR A O 1 ATOM 1237 C CB . TYR A 1 156 ? -11.562 27.903 -29.208 1.00 19.11 ? 182 TYR A CB 1 ATOM 1238 C CG . TYR A 1 156 ? -11.884 26.602 -28.477 1.00 17.11 ? 182 TYR A CG 1 ATOM 1239 C CD1 . TYR A 1 156 ? -12.535 25.549 -29.133 1.00 16.14 ? 182 TYR A CD1 1 ATOM 1240 C CD2 . TYR A 1 156 ? -11.492 26.406 -27.153 1.00 17.00 ? 182 TYR A CD2 1 ATOM 1241 C CE1 . TYR A 1 156 ? -12.804 24.350 -28.483 1.00 15.55 ? 182 TYR A CE1 1 ATOM 1242 C CE2 . TYR A 1 156 ? -11.769 25.209 -26.488 1.00 16.43 ? 182 TYR A CE2 1 ATOM 1243 C CZ . TYR A 1 156 ? -12.423 24.189 -27.160 1.00 18.09 ? 182 TYR A CZ 1 ATOM 1244 O OH . TYR A 1 156 ? -12.701 23.003 -26.524 1.00 19.89 ? 182 TYR A OH 1 ATOM 1245 N N . ILE A 1 157 ? -14.643 28.199 -28.082 1.00 16.84 ? 183 ILE A N 1 ATOM 1246 C CA . ILE A 1 157 ? -15.943 27.532 -28.078 1.00 16.18 ? 183 ILE A CA 1 ATOM 1247 C C . ILE A 1 157 ? -17.021 28.450 -28.681 1.00 18.98 ? 183 ILE A C 1 ATOM 1248 O O . ILE A 1 157 ? -17.618 28.096 -29.701 1.00 16.06 ? 183 ILE A O 1 ATOM 1249 C CB . ILE A 1 157 ? -16.332 27.059 -26.650 1.00 15.97 ? 183 ILE A CB 1 ATOM 1250 C CG1 . ILE A 1 157 ? -15.334 26.005 -26.154 1.00 25.90 ? 183 ILE A CG1 1 ATOM 1251 C CG2 . ILE A 1 157 ? -17.778 26.572 -26.616 1.00 19.91 ? 183 ILE A CG2 1 ATOM 1252 C CD1 . ILE A 1 157 ? -15.460 25.665 -24.672 1.00 22.40 ? 183 ILE A CD1 1 ATOM 1253 N N . PRO A 1 158 ? -17.245 29.649 -28.100 1.00 20.15 ? 184 PRO A N 1 ATOM 1254 C CA . PRO A 1 158 ? -18.236 30.496 -28.779 1.00 24.37 ? 184 PRO A CA 1 ATOM 1255 C C . PRO A 1 158 ? -17.811 30.919 -30.200 1.00 26.30 ? 184 PRO A C 1 ATOM 1256 O O . PRO A 1 158 ? -18.678 31.082 -31.062 1.00 21.28 ? 184 PRO A O 1 ATOM 1257 C CB . PRO A 1 158 ? -18.352 31.727 -27.854 1.00 19.93 ? 184 PRO A CB 1 ATOM 1258 C CG . PRO A 1 158 ? -17.069 31.764 -27.095 1.00 19.30 ? 184 PRO A CG 1 ATOM 1259 C CD . PRO A 1 158 ? -16.701 30.305 -26.895 1.00 22.96 ? 184 PRO A CD 1 ATOM 1260 N N . ASN A 1 159 ? -16.512 31.080 -30.448 1.00 17.90 ? 185 ASN A N 1 ATOM 1261 C CA . ASN A 1 159 ? -16.058 31.460 -31.777 1.00 18.28 ? 185 ASN A CA 1 ATOM 1262 C C . ASN A 1 159 ? -16.393 30.377 -32.800 1.00 22.24 ? 185 ASN A C 1 ATOM 1263 O O . ASN A 1 159 ? -16.765 30.688 -33.935 1.00 18.81 ? 185 ASN A O 1 ATOM 1264 C CB . ASN A 1 159 ? -14.561 31.749 -31.781 1.00 18.83 ? 185 ASN A CB 1 ATOM 1265 C CG . ASN A 1 159 ? -14.208 33.019 -31.003 1.00 35.48 ? 185 ASN A CG 1 ATOM 1266 O OD1 . ASN A 1 159 ? -15.067 33.863 -30.757 1.00 27.21 ? 185 ASN A OD1 1 ATOM 1267 N ND2 . ASN A 1 159 ? -12.943 33.153 -30.618 1.00 33.64 ? 185 ASN A ND2 1 ATOM 1268 N N . ALA A 1 160 ? -16.272 29.115 -32.395 1.00 16.95 ? 186 ALA A N 1 ATOM 1269 C CA . ALA A 1 160 ? -16.628 28.000 -33.281 1.00 20.05 ? 186 ALA A CA 1 ATOM 1270 C C . ALA A 1 160 ? -18.107 28.046 -33.656 1.00 16.12 ? 186 ALA A C 1 ATOM 1271 O O . ALA A 1 160 ? -18.471 27.807 -34.816 1.00 16.06 ? 186 ALA A O 1 ATOM 1272 C CB . ALA A 1 160 ? -16.290 26.669 -32.637 1.00 15.70 ? 186 ALA A CB 1 ATOM 1273 N N . TYR A 1 161 ? -18.961 28.353 -32.683 1.00 16.06 ? 187 TYR A N 1 ATOM 1274 C CA . TYR A 1 161 ? -20.388 28.508 -32.967 1.00 15.96 ? 187 TYR A CA 1 ATOM 1275 C C . TYR A 1 161 ? -20.637 29.742 -33.829 1.00 18.38 ? 187 TYR A C 1 ATOM 1276 O O . TYR A 1 161 ? -21.487 29.702 -34.719 1.00 17.59 ? 187 TYR A O 1 ATOM 1277 C CB . TYR A 1 161 ? -21.201 28.531 -31.659 1.00 15.80 ? 187 TYR A CB 1 ATOM 1278 C CG . TYR A 1 161 ? -21.271 27.121 -31.102 1.00 17.42 ? 187 TYR A CG 1 ATOM 1279 C CD1 . TYR A 1 161 ? -22.249 26.232 -31.542 1.00 16.91 ? 187 TYR A CD1 1 ATOM 1280 C CD2 . TYR A 1 161 ? -20.314 26.656 -30.212 1.00 16.91 ? 187 TYR A CD2 1 ATOM 1281 C CE1 . TYR A 1 161 ? -22.279 24.924 -31.082 1.00 13.96 ? 187 TYR A CE1 1 ATOM 1282 C CE2 . TYR A 1 161 ? -20.336 25.358 -29.743 1.00 14.33 ? 187 TYR A CE2 1 ATOM 1283 C CZ . TYR A 1 161 ? -21.319 24.500 -30.186 1.00 18.73 ? 187 TYR A CZ 1 ATOM 1284 O OH . TYR A 1 161 ? -21.331 23.211 -29.733 1.00 14.81 ? 187 TYR A OH 1 ATOM 1285 N N . ALA A 1 162 ? -19.878 30.818 -33.607 1.00 17.36 ? 188 ALA A N 1 ATOM 1286 C CA . ALA A 1 162 ? -19.969 31.992 -34.488 1.00 21.30 ? 188 ALA A CA 1 ATOM 1287 C C . ALA A 1 162 ? -19.661 31.600 -35.945 1.00 21.23 ? 188 ALA A C 1 ATOM 1288 O O . ALA A 1 162 ? -20.385 31.966 -36.860 1.00 18.50 ? 188 ALA A O 1 ATOM 1289 C CB . ALA A 1 162 ? -19.024 33.097 -34.020 1.00 21.46 ? 188 ALA A CB 1 ATOM 1290 N N . VAL A 1 163 ? -18.602 30.825 -36.153 1.00 19.12 ? 189 VAL A N 1 ATOM 1291 C CA . VAL A 1 163 ? -18.261 30.384 -37.503 1.00 17.99 ? 189 VAL A CA 1 ATOM 1292 C C . VAL A 1 163 ? -19.382 29.532 -38.083 1.00 22.59 ? 189 VAL A C 1 ATOM 1293 O O . VAL A 1 163 ? -19.792 29.720 -39.227 1.00 18.23 ? 189 VAL A O 1 ATOM 1294 C CB . VAL A 1 163 ? -16.953 29.587 -37.523 1.00 20.08 ? 189 VAL A CB 1 ATOM 1295 C CG1 . VAL A 1 163 ? -16.711 29.002 -38.912 1.00 22.38 ? 189 VAL A CG1 1 ATOM 1296 C CG2 . VAL A 1 163 ? -15.781 30.485 -37.113 1.00 21.49 ? 189 VAL A CG2 1 ATOM 1297 N N . ALA A 1 164 ? -19.880 28.596 -37.283 1.00 16.68 ? 190 ALA A N 1 ATOM 1298 C CA . ALA A 1 164 ? -20.963 27.728 -37.729 1.00 16.17 ? 190 ALA A CA 1 ATOM 1299 C C . ALA A 1 164 ? -22.198 28.544 -38.130 1.00 16.59 ? 190 ALA A C 1 ATOM 1300 O O . ALA A 1 164 ? -22.803 28.289 -39.176 1.00 19.13 ? 190 ALA A O 1 ATOM 1301 C CB . ALA A 1 164 ? -21.309 26.710 -36.642 1.00 15.40 ? 190 ALA A CB 1 ATOM 1302 N N . ARG A 1 165 ? -22.559 29.533 -37.316 1.00 16.95 ? 191 ARG A N 1 ATOM 1303 C CA . ARG A 1 165 ? -23.682 30.411 -37.649 1.00 17.47 ? 191 ARG A CA 1 ATOM 1304 C C . ARG A 1 165 ? -23.479 31.111 -38.996 1.00 18.21 ? 191 ARG A C 1 ATOM 1305 O O . ARG A 1 165 ? -24.430 31.279 -39.759 1.00 18.49 ? 191 ARG A O 1 ATOM 1306 C CB . ARG A 1 165 ? -23.891 31.464 -36.559 1.00 17.86 ? 191 ARG A CB 1 ATOM 1307 C CG . ARG A 1 165 ? -24.612 30.963 -35.326 1.00 18.36 ? 191 ARG A CG 1 ATOM 1308 C CD . ARG A 1 165 ? -26.116 30.830 -35.564 1.00 21.71 ? 191 ARG A CD 1 ATOM 1309 N NE . ARG A 1 165 ? -26.805 30.614 -34.294 1.00 23.74 ? 191 ARG A NE 1 ATOM 1310 C CZ . ARG A 1 165 ? -27.578 29.569 -34.010 1.00 28.22 ? 191 ARG A CZ 1 ATOM 1311 N NH1 . ARG A 1 165 ? -27.795 28.620 -34.918 1.00 25.04 ? 191 ARG A NH1 1 ATOM 1312 N NH2 . ARG A 1 165 ? -28.145 29.481 -32.812 1.00 31.09 ? 191 ARG A NH2 1 ATOM 1313 N N . SER A 1 166 ? -22.241 31.507 -39.293 1.00 22.92 ? 192 SER A N 1 ATOM 1314 C CA . SER A 1 166 ? -21.985 32.305 -40.500 1.00 23.41 ? 192 SER A CA 1 ATOM 1315 C C . SER A 1 166 ? -22.137 31.495 -41.801 1.00 29.66 ? 192 SER A C 1 ATOM 1316 O O . SER A 1 166 ? -22.238 32.070 -42.888 1.00 24.31 ? 192 SER A O 1 ATOM 1317 C CB . SER A 1 166 ? -20.591 32.938 -40.435 1.00 24.49 ? 192 SER A CB 1 ATOM 1318 O OG . SER A 1 166 ? -19.570 31.985 -40.665 1.00 25.64 ? 192 SER A OG 1 ATOM 1319 N N . VAL A 1 167 ? -22.171 30.167 -41.696 1.00 19.93 ? 193 VAL A N 1 ATOM 1320 C CA . VAL A 1 167 ? -22.430 29.333 -42.871 1.00 18.39 ? 193 VAL A CA 1 ATOM 1321 C C . VAL A 1 167 ? -23.893 29.506 -43.316 1.00 27.35 ? 193 VAL A C 1 ATOM 1322 O O . VAL A 1 167 ? -24.233 29.250 -44.467 1.00 26.28 ? 193 VAL A O 1 ATOM 1323 C CB . VAL A 1 167 ? -22.123 27.830 -42.584 1.00 21.56 ? 193 VAL A CB 1 ATOM 1324 C CG1 . VAL A 1 167 ? -22.319 26.974 -43.822 1.00 22.29 ? 193 VAL A CG1 1 ATOM 1325 C CG2 . VAL A 1 167 ? -20.707 27.660 -42.086 1.00 22.02 ? 193 VAL A CG2 1 ATOM 1326 N N . ASN A 1 168 ? -24.751 29.969 -42.406 1.00 21.47 ? 194 ASN A N 1 ATOM 1327 C CA . ASN A 1 168 ? -26.178 30.163 -42.697 1.00 18.76 ? 194 ASN A CA 1 ATOM 1328 C C . ASN A 1 168 ? -26.884 28.899 -43.162 1.00 23.25 ? 194 ASN A C 1 ATOM 1329 O O . ASN A 1 168 ? -27.525 28.891 -44.205 1.00 26.79 ? 194 ASN A O 1 ATOM 1330 C CB . ASN A 1 168 ? -26.381 31.250 -43.755 1.00 22.93 ? 194 ASN A CB 1 ATOM 1331 C CG . ASN A 1 168 ? -25.873 32.591 -43.308 1.00 35.57 ? 194 ASN A CG 1 ATOM 1332 O OD1 . ASN A 1 168 ? -26.180 33.050 -42.208 1.00 42.62 ? 194 ASN A OD1 1 ATOM 1333 N ND2 . ASN A 1 168 ? -25.077 33.230 -44.155 1.00 37.35 ? 194 ASN A ND2 1 ATOM 1334 N N . THR A 1 169 ? -26.756 27.828 -42.395 1.00 17.33 ? 195 THR A N 1 ATOM 1335 C CA . THR A 1 169 ? -27.513 26.614 -42.655 1.00 22.53 ? 195 THR A CA 1 ATOM 1336 C C . THR A 1 169 ? -28.802 26.677 -41.848 1.00 21.33 ? 195 THR A C 1 ATOM 1337 O O . THR A 1 169 ? -28.939 27.527 -40.988 1.00 21.30 ? 195 THR A O 1 ATOM 1338 C CB . THR A 1 169 ? -26.725 25.348 -42.266 1.00 20.15 ? 195 THR A CB 1 ATOM 1339 O OG1 . THR A 1 169 ? -26.710 25.231 -40.841 1.00 21.44 ? 195 THR A OG1 1 ATOM 1340 C CG2 . THR A 1 169 ? -25.300 25.409 -42.792 1.00 22.42 ? 195 THR A CG2 1 ATOM 1341 N N . PRO A 1 170 ? -29.757 25.779 -42.117 1.00 20.51 ? 196 PRO A N 1 ATOM 1342 C CA . PRO A 1 170 ? -30.933 25.817 -41.247 1.00 19.24 ? 196 PRO A CA 1 ATOM 1343 C C . PRO A 1 170 ? -30.796 24.820 -40.099 1.00 22.09 ? 196 PRO A C 1 ATOM 1344 O O . PRO A 1 170 ? -31.769 24.523 -39.398 1.00 17.45 ? 196 PRO A O 1 ATOM 1345 C CB . PRO A 1 170 ? -32.069 25.432 -42.192 1.00 25.90 ? 196 PRO A CB 1 ATOM 1346 C CG . PRO A 1 170 ? -31.418 24.481 -43.158 1.00 27.62 ? 196 PRO A CG 1 ATOM 1347 C CD . PRO A 1 170 ? -29.963 24.905 -43.287 1.00 22.80 ? 196 PRO A CD 1 ATOM 1348 N N . SER A 1 171 ? -29.577 24.326 -39.906 1.00 15.05 ? 197 SER A N 1 ATOM 1349 C CA . SER A 1 171 ? -29.273 23.373 -38.844 1.00 14.33 ? 197 SER A CA 1 ATOM 1350 C C . SER A 1 171 ? -29.254 23.997 -37.443 1.00 19.23 ? 197 SER A C 1 ATOM 1351 O O . SER A 1 171 ? -28.710 25.090 -37.236 1.00 14.74 ? 197 SER A O 1 ATOM 1352 C CB . SER A 1 171 ? -27.921 22.711 -39.120 1.00 13.97 ? 197 SER A CB 1 ATOM 1353 O OG . SER A 1 171 ? -27.979 21.954 -40.312 1.00 15.38 ? 197 SER A OG 1 ATOM 1354 N N . LYS A 1 172 ? -29.849 23.296 -36.484 1.00 13.93 ? 198 LYS A N 1 ATOM 1355 C CA . LYS A 1 172 ? -29.659 23.621 -35.070 1.00 13.86 ? 198 LYS A CA 1 ATOM 1356 C C . LYS A 1 172 ? -28.199 23.373 -34.694 1.00 16.88 ? 198 LYS A C 1 ATOM 1357 O O . LYS A 1 172 ? -27.606 22.383 -35.134 1.00 17.35 ? 198 LYS A O 1 ATOM 1358 C CB . LYS A 1 172 ? -30.558 22.765 -34.174 1.00 13.53 ? 198 LYS A CB 1 ATOM 1359 C CG . LYS A 1 172 ? -32.050 22.803 -34.495 1.00 23.70 ? 198 LYS A CG 1 ATOM 1360 C CD . LYS A 1 172 ? -32.714 24.041 -33.944 1.00 25.91 ? 198 LYS A CD 1 ATOM 1361 C CE . LYS A 1 172 ? -34.215 24.035 -34.216 1.00 26.09 ? 198 LYS A CE 1 ATOM 1362 N NZ . LYS A 1 172 ? -34.782 25.371 -33.932 1.00 37.63 ? 198 LYS A NZ 1 ATOM 1363 N N . LEU A 1 173 ? -27.625 24.244 -33.867 1.00 13.81 ? 199 LEU A N 1 ATOM 1364 C CA . LEU A 1 173 ? -26.250 24.050 -33.419 1.00 17.97 ? 199 LEU A CA 1 ATOM 1365 C C . LEU A 1 173 ? -26.266 23.532 -31.993 1.00 13.57 ? 199 LEU A C 1 ATOM 1366 O O . LEU A 1 173 ? -26.866 24.140 -31.100 1.00 13.58 ? 199 LEU A O 1 ATOM 1367 C CB . LEU A 1 173 ? -25.439 25.346 -33.520 1.00 14.18 ? 199 LEU A CB 1 ATOM 1368 C CG . LEU A 1 173 ? -25.419 25.990 -34.915 1.00 20.57 ? 199 LEU A CG 1 ATOM 1369 C CD1 . LEU A 1 173 ? -24.533 27.229 -34.943 1.00 18.73 ? 199 LEU A CD1 1 ATOM 1370 C CD2 . LEU A 1 173 ? -24.992 24.991 -35.985 1.00 14.30 ? 199 LEU A CD2 1 ATOM 1371 N N . TYR A 1 174 ? -25.622 22.388 -31.795 1.00 12.83 ? 200 TYR A N 1 ATOM 1372 C CA . TYR A 1 174 ? -25.610 21.732 -30.501 1.00 12.58 ? 200 TYR A CA 1 ATOM 1373 C C . TYR A 1 174 ? -24.205 21.733 -29.926 1.00 12.59 ? 200 TYR A C 1 ATOM 1374 O O . TYR A 1 174 ? -23.215 21.769 -30.663 1.00 12.61 ? 200 TYR A O 1 ATOM 1375 C CB . TYR A 1 174 ? -26.090 20.285 -30.611 1.00 12.07 ? 200 TYR A CB 1 ATOM 1376 C CG . TYR A 1 174 ? -27.573 20.025 -30.491 1.00 17.38 ? 200 TYR A CG 1 ATOM 1377 C CD1 . TYR A 1 174 ? -28.467 20.461 -31.464 1.00 12.28 ? 200 TYR A CD1 1 ATOM 1378 C CD2 . TYR A 1 174 ? -28.075 19.268 -29.431 1.00 19.71 ? 200 TYR A CD2 1 ATOM 1379 C CE1 . TYR A 1 174 ? -29.823 20.182 -31.368 1.00 12.34 ? 200 TYR A CE1 1 ATOM 1380 C CE2 . TYR A 1 174 ? -29.429 18.989 -29.324 1.00 12.82 ? 200 TYR A CE2 1 ATOM 1381 C CZ . TYR A 1 174 ? -30.291 19.437 -30.303 1.00 16.45 ? 200 TYR A CZ 1 ATOM 1382 O OH . TYR A 1 174 ? -31.620 19.149 -30.198 1.00 14.56 ? 200 TYR A OH 1 ATOM 1383 N N . ILE A 1 175 ? -24.137 21.687 -28.607 1.00 12.64 ? 201 ILE A N 1 ATOM 1384 C CA . ILE A 1 175 ? -22.912 21.318 -27.918 1.00 12.60 ? 201 ILE A CA 1 ATOM 1385 C C . ILE A 1 175 ? -23.197 19.991 -27.207 1.00 12.21 ? 201 ILE A C 1 ATOM 1386 O O . ILE A 1 175 ? -24.313 19.784 -26.698 1.00 15.60 ? 201 ILE A O 1 ATOM 1387 C CB . ILE A 1 175 ? -22.454 22.420 -26.939 1.00 13.38 ? 201 ILE A CB 1 ATOM 1388 C CG1 . ILE A 1 175 ? -21.106 22.068 -26.304 1.00 13.17 ? 201 ILE A CG1 1 ATOM 1389 C CG2 . ILE A 1 175 ? -23.537 22.713 -25.877 1.00 16.39 ? 201 ILE A CG2 1 ATOM 1390 C CD1 . ILE A 1 175 ? -20.441 23.256 -25.569 1.00 13.79 ? 201 ILE A CD1 1 ATOM 1391 N N . ASN A 1 176 ? -22.222 19.082 -27.209 1.00 11.97 ? 202 ASN A N 1 ATOM 1392 C CA . ASN A 1 176 ? -22.435 17.690 -26.770 1.00 11.61 ? 202 ASN A CA 1 ATOM 1393 C C . ASN A 1 176 ? -21.406 17.330 -25.697 1.00 19.18 ? 202 ASN A C 1 ATOM 1394 O O . ASN A 1 176 ? -20.256 17.793 -25.749 1.00 11.98 ? 202 ASN A O 1 ATOM 1395 C CB . ASN A 1 176 ? -22.338 16.732 -27.984 1.00 11.21 ? 202 ASN A CB 1 ATOM 1396 C CG . ASN A 1 176 ? -22.908 15.326 -27.713 1.00 24.17 ? 202 ASN A CG 1 ATOM 1397 O OD1 . ASN A 1 176 ? -24.002 15.176 -27.167 1.00 21.47 ? 202 ASN A OD1 1 ATOM 1398 N ND2 . ASN A 1 176 ? -22.164 14.288 -28.129 1.00 21.74 ? 202 ASN A ND2 1 ATOM 1399 N N . ASP A 1 177 ? -21.806 16.534 -24.707 1.00 11.70 ? 203 ASP A N 1 ATOM 1400 C CA . ASP A 1 177 ? -20.843 16.072 -23.707 1.00 12.32 ? 203 ASP A CA 1 ATOM 1401 C C . ASP A 1 177 ? -21.377 14.867 -22.949 1.00 11.76 ? 203 ASP A C 1 ATOM 1402 O O . ASP A 1 177 ? -22.553 14.536 -23.070 1.00 11.58 ? 203 ASP A O 1 ATOM 1403 C CB . ASP A 1 177 ? -20.486 17.200 -22.726 1.00 12.42 ? 203 ASP A CB 1 ATOM 1404 C CG . ASP A 1 177 ? -18.996 17.190 -22.337 1.00 19.74 ? 203 ASP A CG 1 ATOM 1405 O OD1 . ASP A 1 177 ? -18.405 16.094 -22.248 1.00 14.57 ? 203 ASP A OD1 1 ATOM 1406 O OD2 . ASP A 1 177 ? -18.405 18.276 -22.134 1.00 17.39 ? 203 ASP A OD2 1 ATOM 1407 N N . TYR A 1 178 ? -20.500 14.214 -22.185 1.00 12.80 ? 204 TYR A N 1 ATOM 1408 C CA . TYR A 1 178 ? -20.882 13.099 -21.297 1.00 14.94 ? 204 TYR A CA 1 ATOM 1409 C C . TYR A 1 178 ? -20.560 13.489 -19.853 1.00 12.95 ? 204 TYR A C 1 ATOM 1410 O O . TYR A 1 178 ? -19.786 14.414 -19.634 1.00 12.83 ? 204 TYR A O 1 ATOM 1411 C CB . TYR A 1 178 ? -20.128 11.820 -21.664 1.00 11.73 ? 204 TYR A CB 1 ATOM 1412 C CG . TYR A 1 178 ? -18.648 11.956 -21.409 1.00 12.02 ? 204 TYR A CG 1 ATOM 1413 C CD1 . TYR A 1 178 ? -17.811 12.540 -22.361 1.00 15.16 ? 204 TYR A CD1 1 ATOM 1414 C CD2 . TYR A 1 178 ? -18.087 11.556 -20.199 1.00 16.89 ? 204 TYR A CD2 1 ATOM 1415 C CE1 . TYR A 1 178 ? -16.455 12.697 -22.119 1.00 20.35 ? 204 TYR A CE1 1 ATOM 1416 C CE2 . TYR A 1 178 ? -16.724 11.707 -19.948 1.00 21.13 ? 204 TYR A CE2 1 ATOM 1417 C CZ . TYR A 1 178 ? -15.915 12.271 -20.913 1.00 22.71 ? 204 TYR A CZ 1 ATOM 1418 O OH . TYR A 1 178 ? -14.559 12.421 -20.675 1.00 18.14 ? 204 TYR A OH 1 ATOM 1419 N N . ASN A 1 179 ? -21.113 12.752 -18.884 1.00 13.55 ? 205 ASN A N 1 ATOM 1420 C CA . ASN A 1 179 ? -20.966 13.048 -17.448 1.00 15.63 ? 205 ASN A CA 1 ATOM 1421 C C . ASN A 1 179 ? -21.533 14.422 -17.082 1.00 13.62 ? 205 ASN A C 1 ATOM 1422 O O . ASN A 1 179 ? -21.205 14.996 -16.046 1.00 14.18 ? 205 ASN A O 1 ATOM 1423 C CB . ASN A 1 179 ? -19.500 12.957 -17.000 1.00 18.35 ? 205 ASN A CB 1 ATOM 1424 C CG . ASN A 1 179 ? -19.058 11.530 -16.729 1.00 21.55 ? 205 ASN A CG 1 ATOM 1425 O OD1 . ASN A 1 179 ? -19.874 10.612 -16.677 1.00 25.89 ? 205 ASN A OD1 1 ATOM 1426 N ND2 . ASN A 1 179 ? -17.756 11.340 -16.550 1.00 17.79 ? 205 ASN A ND2 1 ATOM 1427 N N . THR A 1 180 ? -22.393 14.930 -17.952 1.00 13.48 ? 206 THR A N 1 ATOM 1428 C CA . THR A 1 180 ? -23.108 16.177 -17.733 1.00 13.58 ? 206 THR A CA 1 ATOM 1429 C C . THR A 1 180 ? -24.605 15.924 -17.589 1.00 19.33 ? 206 THR A C 1 ATOM 1430 O O . THR A 1 180 ? -25.402 16.860 -17.615 1.00 13.74 ? 206 THR A O 1 ATOM 1431 C CB . THR A 1 180 ? -22.902 17.139 -18.903 1.00 14.28 ? 206 THR A CB 1 ATOM 1432 O OG1 . THR A 1 180 ? -23.166 16.430 -20.118 1.00 13.44 ? 206 THR A OG1 1 ATOM 1433 C CG2 . THR A 1 180 ? -21.469 17.654 -18.923 1.00 13.57 ? 206 THR A CG2 1 ATOM 1434 N N . GLU A 1 181 ? -24.992 14.663 -17.450 1.00 13.38 ? 207 GLU A N 1 ATOM 1435 C CA . GLU A 1 181 ? -26.413 14.335 -17.443 1.00 15.26 ? 207 GLU A CA 1 ATOM 1436 C C . GLU A 1 181 ? -27.060 14.618 -16.084 1.00 16.68 ? 207 GLU A C 1 ATOM 1437 O O . GLU A 1 181 ? -28.221 14.987 -16.023 1.00 19.91 ? 207 GLU A O 1 ATOM 1438 C CB . GLU A 1 181 ? -26.636 12.869 -17.854 1.00 13.01 ? 207 GLU A CB 1 ATOM 1439 C CG . GLU A 1 181 ? -26.089 12.510 -19.247 1.00 12.41 ? 207 GLU A CG 1 ATOM 1440 C CD . GLU A 1 181 ? -24.638 12.032 -19.204 1.00 24.19 ? 207 GLU A CD 1 ATOM 1441 O OE1 . GLU A 1 181 ? -24.046 11.978 -18.103 1.00 19.15 ? 207 GLU A OE1 1 ATOM 1442 O OE2 . GLU A 1 181 ? -24.082 11.712 -20.268 1.00 19.43 ? 207 GLU A OE2 1 ATOM 1443 N N . GLY A 1 182 ? -26.308 14.452 -15.000 1.00 15.50 ? 208 GLY A N 1 ATOM 1444 C CA . GLY A 1 182 ? -26.793 14.819 -13.688 1.00 15.16 ? 208 GLY A CA 1 ATOM 1445 C C . GLY A 1 182 ? -26.427 16.247 -13.322 1.00 21.35 ? 208 GLY A C 1 ATOM 1446 O O . GLY A 1 182 ? -25.939 17.022 -14.145 1.00 19.65 ? 208 GLY A O 1 ATOM 1447 N N . ILE A 1 183 ? -26.686 16.606 -12.076 1.00 19.28 ? 209 ILE A N 1 ATOM 1448 C CA . ILE A 1 183 ? -26.287 17.910 -11.565 1.00 16.79 ? 209 ILE A CA 1 ATOM 1449 C C . ILE A 1 183 ? -24.953 17.732 -10.868 1.00 26.48 ? 209 ILE A C 1 ATOM 1450 O O . ILE A 1 183 ? -24.868 17.090 -9.825 1.00 18.40 ? 209 ILE A O 1 ATOM 1451 C CB . ILE A 1 183 ? -27.341 18.492 -10.593 1.00 17.50 ? 209 ILE A CB 1 ATOM 1452 C CG1 . ILE A 1 183 ? -28.650 18.759 -11.350 1.00 20.56 ? 209 ILE A CG1 1 ATOM 1453 C CG2 . ILE A 1 183 ? -26.820 19.759 -9.913 1.00 24.02 ? 209 ILE A CG2 1 ATOM 1454 C CD1 . ILE A 1 183 ? -29.822 19.096 -10.452 1.00 27.60 ? 209 ILE A CD1 1 ATOM 1455 N N . ASN A 1 184 ? -23.909 18.286 -11.462 1.00 16.91 ? 210 ASN A N 1 ATOM 1456 C CA . ASN A 1 184 ? -22.567 18.182 -10.909 1.00 23.60 ? 210 ASN A CA 1 ATOM 1457 C C . ASN A 1 184 ? -21.712 19.339 -11.421 1.00 20.13 ? 210 ASN A C 1 ATOM 1458 O O . ASN A 1 184 ? -22.203 20.200 -12.146 1.00 17.07 ? 210 ASN A O 1 ATOM 1459 C CB . ASN A 1 184 ? -21.951 16.835 -11.285 1.00 16.81 ? 210 ASN A CB 1 ATOM 1460 C CG . ASN A 1 184 ? -21.970 16.589 -12.791 1.00 20.96 ? 210 ASN A CG 1 ATOM 1461 O OD1 . ASN A 1 184 ? -21.566 17.445 -13.571 1.00 15.76 ? 210 ASN A OD1 1 ATOM 1462 N ND2 . ASN A 1 184 ? -22.462 15.420 -13.200 1.00 15.51 ? 210 ASN A ND2 1 ATOM 1463 N N . ASN A 1 185 ? -20.434 19.353 -11.059 1.00 18.32 ? 211 ASN A N 1 ATOM 1464 C CA . ASN A 1 185 ? -19.524 20.396 -11.529 1.00 17.72 ? 211 ASN A CA 1 ATOM 1465 C C . ASN A 1 185 ? -19.475 20.538 -13.053 1.00 16.98 ? 211 ASN A C 1 ATOM 1466 O O . ASN A 1 185 ? -19.412 21.649 -13.589 1.00 17.05 ? 211 ASN A O 1 ATOM 1467 C CB . ASN A 1 185 ? -18.117 20.121 -11.020 1.00 18.14 ? 211 ASN A CB 1 ATOM 1468 C CG . ASN A 1 185 ? -17.840 20.759 -9.676 1.00 28.36 ? 211 ASN A CG 1 ATOM 1469 O OD1 . ASN A 1 185 ? -18.753 21.046 -8.898 1.00 26.34 ? 211 ASN A OD1 1 ATOM 1470 N ND2 . ASN A 1 185 ? -16.553 20.979 -9.408 1.00 43.46 ? 211 ASN A ND2 1 ATOM 1471 N N . LYS A 1 186 ? -19.500 19.407 -13.747 1.00 16.35 ? 212 LYS A N 1 ATOM 1472 C CA . LYS A 1 186 ? -19.385 19.430 -15.193 1.00 15.71 ? 212 LYS A CA 1 ATOM 1473 C C . LYS A 1 186 ? -20.639 20.031 -15.837 1.00 21.42 ? 212 LYS A C 1 ATOM 1474 O O . LYS A 1 186 ? -20.523 20.914 -16.681 1.00 15.36 ? 212 LYS A O 1 ATOM 1475 C CB . LYS A 1 186 ? -19.113 18.023 -15.736 1.00 15.17 ? 212 LYS A CB 1 ATOM 1476 C CG . LYS A 1 186 ? -18.406 18.022 -17.102 1.00 14.71 ? 212 LYS A CG 1 ATOM 1477 C CD . LYS A 1 186 ? -18.077 16.601 -17.544 1.00 14.27 ? 212 LYS A CD 1 ATOM 1478 C CE . LYS A 1 186 ? -17.475 16.574 -18.951 1.00 13.85 ? 212 LYS A CE 1 ATOM 1479 N NZ . LYS A 1 186 ? -17.213 15.162 -19.395 1.00 13.45 ? 212 LYS A NZ 1 ATOM 1480 N N . SER A 1 187 ? -21.829 19.581 -15.427 1.00 15.38 ? 213 SER A N 1 ATOM 1481 C CA . SER A 1 187 ? -23.060 20.153 -15.971 1.00 15.23 ? 213 SER A CA 1 ATOM 1482 C C . SER A 1 187 ? -23.251 21.617 -15.550 1.00 15.81 ? 213 SER A C 1 ATOM 1483 O O . SER A 1 187 ? -23.797 22.402 -16.312 1.00 15.84 ? 213 SER A O 1 ATOM 1484 C CB . SER A 1 187 ? -24.282 19.329 -15.559 1.00 15.15 ? 213 SER A CB 1 ATOM 1485 O OG . SER A 1 187 ? -24.466 19.346 -14.158 1.00 18.19 ? 213 SER A OG 1 ATOM 1486 N N . ASP A 1 188 ? -22.796 21.990 -14.352 1.00 16.47 ? 214 ASP A N 1 ATOM 1487 C CA . ASP A 1 188 ? -22.824 23.394 -13.947 1.00 17.09 ? 214 ASP A CA 1 ATOM 1488 C C . ASP A 1 188 ? -22.011 24.250 -14.924 1.00 21.10 ? 214 ASP A C 1 ATOM 1489 O O . ASP A 1 188 ? -22.474 25.292 -15.385 1.00 17.16 ? 214 ASP A O 1 ATOM 1490 C CB . ASP A 1 188 ? -22.261 23.595 -12.537 1.00 17.86 ? 214 ASP A CB 1 ATOM 1491 C CG . ASP A 1 188 ? -23.156 23.034 -11.443 1.00 27.75 ? 214 ASP A CG 1 ATOM 1492 O OD1 . ASP A 1 188 ? -24.321 22.645 -11.709 1.00 21.00 ? 214 ASP A OD1 1 ATOM 1493 O OD2 . ASP A 1 188 ? -22.673 22.991 -10.293 1.00 33.57 ? 214 ASP A OD2 1 ATOM 1494 N N . ALA A 1 189 ? -20.791 23.807 -15.222 1.00 20.78 ? 215 ALA A N 1 ATOM 1495 C CA . ALA A 1 189 ? -19.907 24.539 -16.128 1.00 18.68 ? 215 ALA A CA 1 ATOM 1496 C C . ALA A 1 189 ? -20.516 24.633 -17.528 1.00 21.84 ? 215 ALA A C 1 ATOM 1497 O O . ALA A 1 189 ? -20.532 25.707 -18.139 1.00 16.48 ? 215 ALA A O 1 ATOM 1498 C CB . ALA A 1 189 ? -18.537 23.879 -16.191 1.00 16.78 ? 215 ALA A CB 1 ATOM 1499 N N . LEU A 1 190 ? -21.017 23.505 -18.027 1.00 15.64 ? 216 LEU A N 1 ATOM 1500 C CA . LEU A 1 190 ? -21.686 23.480 -19.321 1.00 15.15 ? 216 LEU A CA 1 ATOM 1501 C C . LEU A 1 190 ? -22.872 24.431 -19.349 1.00 15.41 ? 216 LEU A C 1 ATOM 1502 O O . LEU A 1 190 ? -23.050 25.174 -20.314 1.00 15.41 ? 216 LEU A O 1 ATOM 1503 C CB . LEU A 1 190 ? -22.158 22.064 -19.672 1.00 14.52 ? 216 LEU A CB 1 ATOM 1504 C CG . LEU A 1 190 ? -22.896 21.942 -21.017 1.00 15.14 ? 216 LEU A CG 1 ATOM 1505 C CD1 . LEU A 1 190 ? -22.000 22.365 -22.189 1.00 13.95 ? 216 LEU A CD1 1 ATOM 1506 C CD2 . LEU A 1 190 ? -23.444 20.527 -21.238 1.00 13.51 ? 216 LEU A CD2 1 ATOM 1507 N N . LEU A 1 191 ? -23.680 24.412 -18.290 1.00 15.70 ? 217 LEU A N 1 ATOM 1508 C CA . LEU A 1 191 ? -24.866 25.272 -18.226 1.00 16.03 ? 217 LEU A CA 1 ATOM 1509 C C . LEU A 1 191 ? -24.494 26.758 -18.291 1.00 16.87 ? 217 LEU A C 1 ATOM 1510 O O . LEU A 1 191 ? -25.147 27.546 -18.988 1.00 16.72 ? 217 LEU A O 1 ATOM 1511 C CB . LEU A 1 191 ? -25.662 24.991 -16.955 1.00 17.34 ? 217 LEU A CB 1 ATOM 1512 C CG . LEU A 1 191 ? -26.881 25.876 -16.695 1.00 21.05 ? 217 LEU A CG 1 ATOM 1513 C CD1 . LEU A 1 191 ? -27.840 25.790 -17.860 1.00 19.58 ? 217 LEU A CD1 1 ATOM 1514 C CD2 . LEU A 1 191 ? -27.575 25.476 -15.395 1.00 19.65 ? 217 LEU A CD2 1 ATOM 1515 N N . ALA A 1 192 ? -23.443 27.143 -17.580 1.00 18.82 ? 218 ALA A N 1 ATOM 1516 C CA . ALA A 1 192 ? -23.055 28.548 -17.574 1.00 24.41 ? 218 ALA A CA 1 ATOM 1517 C C . ALA A 1 192 ? -22.640 28.971 -18.977 1.00 17.44 ? 218 ALA A C 1 ATOM 1518 O O . ALA A 1 192 ? -23.036 30.036 -19.446 1.00 20.35 ? 218 ALA A O 1 ATOM 1519 C CB . ALA A 1 192 ? -21.949 28.807 -16.595 1.00 18.19 ? 218 ALA A CB 1 ATOM 1520 N N . VAL A 1 193 ? -21.887 28.120 -19.667 1.00 16.91 ? 219 VAL A N 1 ATOM 1521 C CA . VAL A 1 193 ? -21.448 28.459 -21.015 1.00 23.90 ? 219 VAL A CA 1 ATOM 1522 C C . VAL A 1 193 ? -22.633 28.463 -21.990 1.00 23.15 ? 219 VAL A C 1 ATOM 1523 O O . VAL A 1 193 ? -22.784 29.373 -22.799 1.00 17.11 ? 219 VAL A O 1 ATOM 1524 C CB . VAL A 1 193 ? -20.345 27.497 -21.498 1.00 17.91 ? 219 VAL A CB 1 ATOM 1525 C CG1 . VAL A 1 193 ? -20.055 27.707 -22.976 1.00 22.37 ? 219 VAL A CG1 1 ATOM 1526 C CG2 . VAL A 1 193 ? -19.074 27.724 -20.677 1.00 18.47 ? 219 VAL A CG2 1 ATOM 1527 N N . VAL A 1 194 ? -23.488 27.456 -21.896 1.00 17.05 ? 220 VAL A N 1 ATOM 1528 C CA . VAL A 1 194 ? -24.694 27.416 -22.720 1.00 16.02 ? 220 VAL A CA 1 ATOM 1529 C C . VAL A 1 194 ? -25.613 28.646 -22.487 1.00 18.06 ? 220 VAL A C 1 ATOM 1530 O O . VAL A 1 194 ? -26.176 29.199 -23.433 1.00 17.69 ? 220 VAL A O 1 ATOM 1531 C CB . VAL A 1 194 ? -25.464 26.108 -22.462 1.00 15.27 ? 220 VAL A CB 1 ATOM 1532 C CG1 . VAL A 1 194 ? -26.886 26.174 -23.031 1.00 15.18 ? 220 VAL A CG1 1 ATOM 1533 C CG2 . VAL A 1 194 ? -24.686 24.918 -23.055 1.00 14.61 ? 220 VAL A CG2 1 ATOM 1534 N N . GLN A 1 195 ? -25.754 29.090 -21.244 1.00 16.84 ? 221 GLN A N 1 ATOM 1535 C CA . GLN A 1 195 ? -26.616 30.242 -20.968 1.00 17.48 ? 221 GLN A CA 1 ATOM 1536 C C . GLN A 1 195 ? -26.080 31.472 -21.689 1.00 20.13 ? 221 GLN A C 1 ATOM 1537 O O . GLN A 1 195 ? -26.830 32.254 -22.287 1.00 19.29 ? 221 GLN A O 1 ATOM 1538 C CB . GLN A 1 195 ? -26.720 30.499 -19.461 1.00 22.24 ? 221 GLN A CB 1 ATOM 1539 C CG . GLN A 1 195 ? -27.811 29.669 -18.767 1.00 27.80 ? 221 GLN A CG 1 ATOM 1540 C CD . GLN A 1 195 ? -27.748 29.750 -17.245 1.00 37.42 ? 221 GLN A CD 1 ATOM 1541 O OE1 . GLN A 1 195 ? -26.716 30.099 -16.672 1.00 36.35 ? 221 GLN A OE1 1 ATOM 1542 N NE2 . GLN A 1 195 ? -28.856 29.420 -16.586 1.00 36.22 ? 221 GLN A NE2 1 ATOM 1543 N N . SER A 1 196 ? -24.768 31.624 -21.641 1.00 18.02 ? 222 SER A N 1 ATOM 1544 C CA . SER A 1 196 ? -24.110 32.719 -22.326 1.00 21.21 ? 222 SER A CA 1 ATOM 1545 C C . SER A 1 196 ? -24.260 32.605 -23.847 1.00 18.19 ? 222 SER A C 1 ATOM 1546 O O . SER A 1 196 ? -24.653 33.567 -24.514 1.00 18.64 ? 222 SER A O 1 ATOM 1547 C CB . SER A 1 196 ? -22.636 32.767 -21.935 1.00 21.45 ? 222 SER A CB 1 ATOM 1548 O OG . SER A 1 196 ? -21.949 33.698 -22.741 1.00 34.11 ? 222 SER A OG 1 ATOM 1549 N N . MET A 1 197 ? -23.956 31.433 -24.395 1.00 18.25 ? 223 MET A N 1 ATOM 1550 C CA . MET A 1 197 ? -23.997 31.267 -25.840 1.00 19.79 ? 223 MET A CA 1 ATOM 1551 C C . MET A 1 197 ? -25.425 31.422 -26.350 1.00 20.93 ? 223 MET A C 1 ATOM 1552 O O . MET A 1 197 ? -25.642 31.978 -27.431 1.00 18.42 ? 223 MET A O 1 ATOM 1553 C CB . MET A 1 197 ? -23.401 29.911 -26.264 1.00 16.48 ? 223 MET A CB 1 ATOM 1554 C CG . MET A 1 197 ? -21.865 29.922 -26.248 1.00 18.66 ? 223 MET A CG 1 ATOM 1555 S SD . MET A 1 197 ? -21.126 28.588 -27.210 1.00 27.09 ? 223 MET A SD 1 ATOM 1556 C CE . MET A 1 197 ? -21.976 27.166 -26.543 1.00 19.34 ? 223 MET A CE 1 ATOM 1557 N N . LYS A 1 198 ? -26.397 30.969 -25.562 1.00 18.96 ? 224 LYS A N 1 ATOM 1558 C CA . LYS A 1 198 ? -27.787 31.074 -25.972 1.00 19.09 ? 224 LYS A CA 1 ATOM 1559 C C . LYS A 1 198 ? -28.204 32.544 -25.995 1.00 20.57 ? 224 LYS A C 1 ATOM 1560 O O . LYS A 1 198 ? -28.891 33.001 -26.911 1.00 21.24 ? 224 LYS A O 1 ATOM 1561 C CB . LYS A 1 198 ? -28.689 30.256 -25.049 1.00 18.35 ? 224 LYS A CB 1 ATOM 1562 C CG . LYS A 1 198 ? -30.172 30.485 -25.287 1.00 20.71 ? 224 LYS A CG 1 ATOM 1563 C CD . LYS A 1 198 ? -30.600 30.026 -26.655 1.00 24.04 ? 224 LYS A CD 1 ATOM 1564 C CE . LYS A 1 198 ? -31.995 30.558 -26.980 1.00 30.49 ? 224 LYS A CE 1 ATOM 1565 N NZ . LYS A 1 198 ? -32.576 29.943 -28.208 1.00 37.88 ? 224 LYS A NZ 1 ATOM 1566 N N . ALA A 1 199 ? -27.761 33.286 -24.993 1.00 21.26 ? 225 ALA A N 1 ATOM 1567 C CA . ALA A 1 199 ? -28.035 34.716 -24.944 1.00 22.82 ? 225 ALA A CA 1 ATOM 1568 C C . ALA A 1 199 ? -27.488 35.374 -26.214 1.00 27.01 ? 225 ALA A C 1 ATOM 1569 O O . ALA A 1 199 ? -28.138 36.225 -26.823 1.00 26.82 ? 225 ALA A O 1 ATOM 1570 C CB . ALA A 1 199 ? -27.420 35.336 -23.703 1.00 23.56 ? 225 ALA A CB 1 ATOM 1571 N N . HIS A 1 200 ? -26.304 34.942 -26.627 1.00 23.26 ? 226 HIS A N 1 ATOM 1572 C CA . HIS A 1 200 ? -25.632 35.551 -27.769 1.00 24.29 ? 226 HIS A CA 1 ATOM 1573 C C . HIS A 1 200 ? -26.037 34.916 -29.104 1.00 23.92 ? 226 HIS A C 1 ATOM 1574 O O . HIS A 1 200 ? -25.372 35.141 -30.118 1.00 24.69 ? 226 HIS A O 1 ATOM 1575 C CB . HIS A 1 200 ? -24.111 35.464 -27.594 1.00 24.46 ? 226 HIS A CB 1 ATOM 1576 C CG . HIS A 1 200 ? -23.590 36.235 -26.417 1.00 35.21 ? 226 HIS A CG 1 ATOM 1577 N ND1 . HIS A 1 200 ? -22.410 35.915 -25.779 1.00 36.08 ? 226 HIS A ND1 1 ATOM 1578 C CD2 . HIS A 1 200 ? -24.084 37.316 -25.769 1.00 36.37 ? 226 HIS A CD2 1 ATOM 1579 C CE1 . HIS A 1 200 ? -22.203 36.761 -24.786 1.00 38.95 ? 226 HIS A CE1 1 ATOM 1580 N NE2 . HIS A 1 200 ? -23.203 37.624 -24.760 1.00 41.48 ? 226 HIS A NE2 1 ATOM 1581 N N . ASN A 1 201 ? -27.107 34.116 -29.102 1.00 22.94 ? 227 ASN A N 1 ATOM 1582 C CA . ASN A 1 201 ? -27.636 33.539 -30.344 1.00 22.83 ? 227 ASN A CA 1 ATOM 1583 C C . ASN A 1 201 ? -26.666 32.550 -31.022 1.00 30.72 ? 227 ASN A C 1 ATOM 1584 O O . ASN A 1 201 ? -26.702 32.357 -32.244 1.00 26.13 ? 227 ASN A O 1 ATOM 1585 C CB . ASN A 1 201 ? -28.001 34.679 -31.321 1.00 42.22 ? 227 ASN A CB 1 ATOM 1586 C CG . ASN A 1 201 ? -28.739 34.198 -32.559 1.00 38.97 ? 227 ASN A CG 1 ATOM 1587 O OD1 . ASN A 1 201 ? -29.487 33.222 -32.511 1.00 48.19 ? 227 ASN A OD1 1 ATOM 1588 N ND2 . ASN A 1 201 ? -28.511 34.874 -33.684 1.00 27.13 ? 227 ASN A ND2 1 ATOM 1589 N N . LEU A 1 202 ? -25.805 31.915 -30.231 1.00 21.18 ? 228 LEU A N 1 ATOM 1590 C CA . LEU A 1 202 ? -24.768 31.050 -30.794 1.00 25.29 ? 228 LEU A CA 1 ATOM 1591 C C . LEU A 1 202 ? -25.106 29.543 -30.742 1.00 23.85 ? 228 LEU A C 1 ATOM 1592 O O . LEU A 1 202 ? -24.644 28.767 -31.583 1.00 21.52 ? 228 LEU A O 1 ATOM 1593 C CB . LEU A 1 202 ? -23.434 31.317 -30.081 1.00 21.02 ? 228 LEU A CB 1 ATOM 1594 C CG . LEU A 1 202 ? -22.839 32.724 -30.260 1.00 26.02 ? 228 LEU A CG 1 ATOM 1595 C CD1 . LEU A 1 202 ? -21.507 32.871 -29.517 1.00 24.24 ? 228 LEU A CD1 1 ATOM 1596 C CD2 . LEU A 1 202 ? -22.680 33.091 -31.734 1.00 23.99 ? 228 LEU A CD2 1 ATOM 1597 N N . VAL A 1 203 ? -25.913 29.121 -29.776 1.00 19.37 ? 229 VAL A N 1 ATOM 1598 C CA . VAL A 1 203 ? -26.230 27.702 -29.657 1.00 17.05 ? 229 VAL A CA 1 ATOM 1599 C C . VAL A 1 203 ? -27.739 27.481 -29.538 1.00 20.73 ? 229 VAL A C 1 ATOM 1600 O O . VAL A 1 203 ? -28.458 28.318 -28.996 1.00 20.58 ? 229 VAL A O 1 ATOM 1601 C CB . VAL A 1 203 ? -25.473 27.072 -28.454 1.00 16.17 ? 229 VAL A CB 1 ATOM 1602 C CG1 . VAL A 1 203 ? -26.063 27.538 -27.131 1.00 23.51 ? 229 VAL A CG1 1 ATOM 1603 C CG2 . VAL A 1 203 ? -25.432 25.539 -28.541 1.00 16.91 ? 229 VAL A CG2 1 ATOM 1604 N N . ASP A 1 204 ? -28.217 26.356 -30.063 1.00 16.22 ? 230 ASP A N 1 ATOM 1605 C CA . ASP A 1 204 ? -29.652 26.043 -30.054 1.00 16.22 ? 230 ASP A CA 1 ATOM 1606 C C . ASP A 1 204 ? -29.997 24.878 -29.132 1.00 25.15 ? 230 ASP A C 1 ATOM 1607 O O . ASP A 1 204 ? -31.098 24.804 -28.577 1.00 15.23 ? 230 ASP A O 1 ATOM 1608 C CB . ASP A 1 204 ? -30.125 25.693 -31.462 1.00 16.79 ? 230 ASP A CB 1 ATOM 1609 C CG . ASP A 1 204 ? -29.888 26.809 -32.447 1.00 26.14 ? 230 ASP A CG 1 ATOM 1610 O OD1 . ASP A 1 204 ? -30.326 27.949 -32.172 1.00 21.13 ? 230 ASP A OD1 1 ATOM 1611 O OD2 . ASP A 1 204 ? -29.256 26.545 -33.486 1.00 18.51 ? 230 ASP A OD2 1 ATOM 1612 N N . GLY A 1 205 ? -29.063 23.943 -29.009 1.00 15.38 ? 231 GLY A N 1 ATOM 1613 C CA . GLY A 1 205 ? -29.350 22.675 -28.356 1.00 13.35 ? 231 GLY A CA 1 ATOM 1614 C C . GLY A 1 205 ? -28.199 22.178 -27.507 1.00 13.00 ? 231 GLY A C 1 ATOM 1615 O O . GLY A 1 205 ? -27.040 22.561 -27.713 1.00 12.81 ? 231 GLY A O 1 ATOM 1616 N N . VAL A 1 206 ? -28.528 21.352 -26.527 1.00 12.07 ? 232 VAL A N 1 ATOM 1617 C CA . VAL A 1 206 ? -27.520 20.645 -25.749 1.00 11.49 ? 232 VAL A CA 1 ATOM 1618 C C . VAL A 1 206 ? -27.737 19.152 -25.900 1.00 10.84 ? 232 VAL A C 1 ATOM 1619 O O . VAL A 1 206 ? -28.857 18.653 -25.697 1.00 10.87 ? 232 VAL A O 1 ATOM 1620 C CB . VAL A 1 206 ? -27.571 21.034 -24.250 1.00 11.67 ? 232 VAL A CB 1 ATOM 1621 C CG1 . VAL A 1 206 ? -26.605 20.164 -23.439 1.00 13.43 ? 232 VAL A CG1 1 ATOM 1622 C CG2 . VAL A 1 206 ? -27.229 22.505 -24.079 1.00 12.44 ? 232 VAL A CG2 1 ATOM 1623 N N . GLY A 1 207 ? -26.671 18.437 -26.256 1.00 10.50 ? 233 GLY A N 1 ATOM 1624 C CA . GLY A 1 207 ? -26.706 16.989 -26.344 1.00 9.99 ? 233 GLY A CA 1 ATOM 1625 C C . GLY A 1 207 ? -26.157 16.319 -25.087 1.00 19.85 ? 233 GLY A C 1 ATOM 1626 O O . GLY A 1 207 ? -25.067 16.653 -24.618 1.00 13.12 ? 233 GLY A O 1 ATOM 1627 N N . PHE A 1 208 ? -26.911 15.369 -24.538 1.00 9.42 ? 234 PHE A N 1 ATOM 1628 C CA . PHE A 1 208 ? -26.449 14.573 -23.401 1.00 9.28 ? 234 PHE A CA 1 ATOM 1629 C C . PHE A 1 208 ? -26.149 13.163 -23.873 1.00 8.94 ? 234 PHE A C 1 ATOM 1630 O O . PHE A 1 208 ? -27.058 12.478 -24.309 1.00 12.41 ? 234 PHE A O 1 ATOM 1631 C CB . PHE A 1 208 ? -27.508 14.550 -22.288 1.00 12.16 ? 234 PHE A CB 1 ATOM 1632 C CG . PHE A 1 208 ? -27.847 15.923 -21.749 1.00 11.84 ? 234 PHE A CG 1 ATOM 1633 C CD1 . PHE A 1 208 ? -27.064 16.506 -20.772 1.00 11.23 ? 234 PHE A CD1 1 ATOM 1634 C CD2 . PHE A 1 208 ? -28.946 16.616 -22.225 1.00 15.86 ? 234 PHE A CD2 1 ATOM 1635 C CE1 . PHE A 1 208 ? -27.360 17.766 -20.267 1.00 17.31 ? 234 PHE A CE1 1 ATOM 1636 C CE2 . PHE A 1 208 ? -29.264 17.879 -21.718 1.00 21.44 ? 234 PHE A CE2 1 ATOM 1637 C CZ . PHE A 1 208 ? -28.461 18.453 -20.738 1.00 11.33 ? 234 PHE A CZ 1 ATOM 1638 N N . GLN A 1 209 ? -24.890 12.728 -23.811 1.00 8.89 ? 235 GLN A N 1 ATOM 1639 C CA . GLN A 1 209 ? -24.532 11.444 -24.407 1.00 10.90 ? 235 GLN A CA 1 ATOM 1640 C C . GLN A 1 209 ? -25.250 10.264 -23.735 1.00 8.65 ? 235 GLN A C 1 ATOM 1641 O O . GLN A 1 209 ? -25.797 9.427 -24.425 1.00 11.61 ? 235 GLN A O 1 ATOM 1642 C CB . GLN A 1 209 ? -23.018 11.222 -24.364 1.00 8.92 ? 235 GLN A CB 1 ATOM 1643 C CG . GLN A 1 209 ? -22.266 12.121 -25.359 1.00 9.21 ? 235 GLN A CG 1 ATOM 1644 C CD . GLN A 1 209 ? -20.775 11.853 -25.338 1.00 10.43 ? 235 GLN A CD 1 ATOM 1645 O OE1 . GLN A 1 209 ? -20.333 10.768 -24.952 1.00 13.70 ? 235 GLN A OE1 1 ATOM 1646 N NE2 . GLN A 1 209 ? -19.994 12.831 -25.761 1.00 10.18 ? 235 GLN A NE2 1 ATOM 1647 N N . CYS A 1 210 ? -25.246 10.220 -22.402 1.00 9.26 ? 236 CYS A N 1 ATOM 1648 C CA . CYS A 1 210 ? -25.926 9.160 -21.647 1.00 10.29 ? 236 CYS A CA 1 ATOM 1649 C C . CYS A 1 210 ? -25.342 7.770 -21.891 1.00 13.00 ? 236 CYS A C 1 ATOM 1650 O O . CYS A 1 210 ? -26.082 6.822 -22.143 1.00 10.21 ? 236 CYS A O 1 ATOM 1651 C CB . CYS A 1 210 ? -27.433 9.131 -21.960 1.00 9.10 ? 236 CYS A CB 1 ATOM 1652 S SG . CYS A 1 210 ? -28.357 10.646 -21.482 1.00 13.04 ? 236 CYS A SG 1 ATOM 1653 N N . HIS A 1 211 ? -24.015 7.655 -21.806 1.00 9.44 ? 237 HIS A N 1 ATOM 1654 C CA . HIS A 1 211 ? -23.344 6.361 -21.681 1.00 12.50 ? 237 HIS A CA 1 ATOM 1655 C C . HIS A 1 211 ? -23.405 5.896 -20.216 1.00 16.78 ? 237 HIS A C 1 ATOM 1656 O O . HIS A 1 211 ? -22.528 6.227 -19.412 1.00 15.46 ? 237 HIS A O 1 ATOM 1657 C CB . HIS A 1 211 ? -21.890 6.487 -22.162 1.00 9.47 ? 237 HIS A CB 1 ATOM 1658 C CG . HIS A 1 211 ? -21.778 6.755 -23.628 1.00 9.25 ? 237 HIS A CG 1 ATOM 1659 N ND1 . HIS A 1 211 ? -22.124 5.819 -24.582 1.00 9.38 ? 237 HIS A ND1 1 ATOM 1660 C CD2 . HIS A 1 211 ? -21.372 7.855 -24.306 1.00 9.25 ? 237 HIS A CD2 1 ATOM 1661 C CE1 . HIS A 1 211 ? -21.924 6.327 -25.785 1.00 10.80 ? 237 HIS A CE1 1 ATOM 1662 N NE2 . HIS A 1 211 ? -21.481 7.566 -25.645 1.00 11.63 ? 237 HIS A NE2 1 ATOM 1663 N N . PHE A 1 212 ? -24.451 5.154 -19.861 1.00 11.53 ? 238 PHE A N 1 ATOM 1664 C CA . PHE A 1 212 ? -24.724 4.829 -18.463 1.00 10.74 ? 238 PHE A CA 1 ATOM 1665 C C . PHE A 1 212 ? -24.340 3.388 -18.105 1.00 11.96 ? 238 PHE A C 1 ATOM 1666 O O . PHE A 1 212 ? -24.237 2.523 -18.979 1.00 11.15 ? 238 PHE A O 1 ATOM 1667 C CB . PHE A 1 212 ? -26.227 5.056 -18.153 1.00 10.93 ? 238 PHE A CB 1 ATOM 1668 C CG . PHE A 1 212 ? -26.651 6.495 -18.199 1.00 11.53 ? 238 PHE A CG 1 ATOM 1669 C CD1 . PHE A 1 212 ? -25.843 7.483 -17.659 1.00 13.53 ? 238 PHE A CD1 1 ATOM 1670 C CD2 . PHE A 1 212 ? -27.869 6.862 -18.767 1.00 11.04 ? 238 PHE A CD2 1 ATOM 1671 C CE1 . PHE A 1 212 ? -26.232 8.815 -17.692 1.00 17.59 ? 238 PHE A CE1 1 ATOM 1672 C CE2 . PHE A 1 212 ? -28.261 8.189 -18.801 1.00 16.17 ? 238 PHE A CE2 1 ATOM 1673 C CZ . PHE A 1 212 ? -27.437 9.169 -18.268 1.00 12.78 ? 238 PHE A CZ 1 ATOM 1674 N N . PHE A 1 213 ? -24.144 3.133 -16.817 1.00 12.59 ? 239 PHE A N 1 ATOM 1675 C CA . PHE A 1 213 ? -23.986 1.770 -16.310 1.00 12.92 ? 239 PHE A CA 1 ATOM 1676 C C . PHE A 1 213 ? -25.277 1.406 -15.580 1.00 15.44 ? 239 PHE A C 1 ATOM 1677 O O . PHE A 1 213 ? -25.813 2.215 -14.809 1.00 16.30 ? 239 PHE A O 1 ATOM 1678 C CB . PHE A 1 213 ? -22.774 1.652 -15.375 1.00 13.78 ? 239 PHE A CB 1 ATOM 1679 C CG . PHE A 1 213 ? -22.372 0.224 -15.070 1.00 14.60 ? 239 PHE A CG 1 ATOM 1680 C CD1 . PHE A 1 213 ? -22.993 -0.484 -14.051 1.00 20.95 ? 239 PHE A CD1 1 ATOM 1681 C CD2 . PHE A 1 213 ? -21.390 -0.406 -15.815 1.00 20.40 ? 239 PHE A CD2 1 ATOM 1682 C CE1 . PHE A 1 213 ? -22.634 -1.808 -13.771 1.00 28.28 ? 239 PHE A CE1 1 ATOM 1683 C CE2 . PHE A 1 213 ? -21.018 -1.726 -15.546 1.00 20.28 ? 239 PHE A CE2 1 ATOM 1684 C CZ . PHE A 1 213 ? -21.644 -2.429 -14.516 1.00 22.55 ? 239 PHE A CZ 1 ATOM 1685 N N . VAL A 1 214 ? -25.778 0.200 -15.819 1.00 17.23 ? 240 VAL A N 1 ATOM 1686 C CA . VAL A 1 214 ? -27.081 -0.214 -15.276 1.00 16.79 ? 240 VAL A CA 1 ATOM 1687 C C . VAL A 1 214 ? -27.200 -0.019 -13.757 1.00 20.98 ? 240 VAL A C 1 ATOM 1688 O O . VAL A 1 214 ? -26.277 -0.316 -12.996 1.00 16.69 ? 240 VAL A O 1 ATOM 1689 C CB . VAL A 1 214 ? -27.374 -1.690 -15.608 1.00 21.34 ? 240 VAL A CB 1 ATOM 1690 C CG1 . VAL A 1 214 ? -26.306 -2.583 -15.010 1.00 22.26 ? 240 VAL A CG1 1 ATOM 1691 C CG2 . VAL A 1 214 ? -28.750 -2.088 -15.102 1.00 18.20 ? 240 VAL A CG2 1 ATOM 1692 N N . GLY A 1 215 ? -28.340 0.518 -13.333 1.00 18.45 ? 241 GLY A N 1 ATOM 1693 C CA . GLY A 1 215 ? -28.604 0.756 -11.928 1.00 24.00 ? 241 GLY A CA 1 ATOM 1694 C C . GLY A 1 215 ? -27.761 1.855 -11.306 1.00 28.94 ? 241 GLY A C 1 ATOM 1695 O O . GLY A 1 215 ? -27.735 1.990 -10.080 1.00 33.51 ? 241 GLY A O 1 ATOM 1696 N N . GLU A 1 216 ? -27.074 2.641 -12.136 1.00 23.96 ? 242 GLU A N 1 ATOM 1697 C CA . GLU A 1 216 ? -26.194 3.695 -11.626 1.00 22.53 ? 242 GLU A CA 1 ATOM 1698 C C . GLU A 1 216 ? -26.347 5.005 -12.371 1.00 18.46 ? 242 GLU A C 1 ATOM 1699 O O . GLU A 1 216 ? -25.375 5.701 -12.655 1.00 15.94 ? 242 GLU A O 1 ATOM 1700 C CB . GLU A 1 216 ? -24.750 3.227 -11.690 1.00 26.70 ? 242 GLU A CB 1 ATOM 1701 C CG . GLU A 1 216 ? -24.529 2.140 -10.673 1.00 32.93 ? 242 GLU A CG 1 ATOM 1702 C CD . GLU A 1 216 ? -23.328 1.304 -10.958 1.00 28.29 ? 242 GLU A CD 1 ATOM 1703 O OE1 . GLU A 1 216 ? -22.424 1.801 -11.668 1.00 31.04 ? 242 GLU A OE1 1 ATOM 1704 O OE2 . GLU A 1 216 ? -23.309 0.149 -10.469 1.00 27.89 ? 242 GLU A OE2 1 ATOM 1705 N N . LEU A 1 217 ? -27.582 5.347 -12.692 1.00 15.42 ? 243 LEU A N 1 ATOM 1706 C CA . LEU A 1 217 ? -27.827 6.582 -13.418 1.00 14.95 ? 243 LEU A CA 1 ATOM 1707 C C . LEU A 1 217 ? -27.633 7.772 -12.464 1.00 15.31 ? 243 LEU A C 1 ATOM 1708 O O . LEU A 1 217 ? -27.615 7.587 -11.262 1.00 18.13 ? 243 LEU A O 1 ATOM 1709 C CB . LEU A 1 217 ? -29.226 6.545 -14.037 1.00 16.63 ? 243 LEU A CB 1 ATOM 1710 C CG . LEU A 1 217 ? -29.279 5.957 -15.455 1.00 13.57 ? 243 LEU A CG 1 ATOM 1711 C CD1 . LEU A 1 217 ? -28.809 4.492 -15.521 1.00 15.97 ? 243 LEU A CD1 1 ATOM 1712 C CD2 . LEU A 1 217 ? -30.680 6.103 -16.016 1.00 22.94 ? 243 LEU A CD2 1 ATOM 1713 N N . PRO A 1 218 ? -27.438 8.983 -13.007 1.00 19.14 ? 244 PRO A N 1 ATOM 1714 C CA . PRO A 1 218 ? -27.324 10.184 -12.178 1.00 18.58 ? 244 PRO A CA 1 ATOM 1715 C C . PRO A 1 218 ? -28.604 10.386 -11.384 1.00 16.63 ? 244 PRO A C 1 ATOM 1716 O O . PRO A 1 218 ? -29.683 10.196 -11.954 1.00 22.70 ? 244 PRO A O 1 ATOM 1717 C CB . PRO A 1 218 ? -27.130 11.319 -13.201 1.00 18.62 ? 244 PRO A CB 1 ATOM 1718 C CG . PRO A 1 218 ? -26.667 10.667 -14.421 1.00 23.85 ? 244 PRO A CG 1 ATOM 1719 C CD . PRO A 1 218 ? -27.251 9.281 -14.438 1.00 21.45 ? 244 PRO A CD 1 ATOM 1720 N N . PRO A 1 219 ? -28.491 10.745 -10.100 1.00 18.13 ? 245 PRO A N 1 ATOM 1721 C CA . PRO A 1 219 ? -29.649 10.908 -9.214 1.00 19.63 ? 245 PRO A CA 1 ATOM 1722 C C . PRO A 1 219 ? -30.628 12.005 -9.628 1.00 32.68 ? 245 PRO A C 1 ATOM 1723 O O . PRO A 1 219 ? -31.824 11.877 -9.363 1.00 34.32 ? 245 PRO A O 1 ATOM 1724 C CB . PRO A 1 219 ? -29.006 11.267 -7.874 1.00 21.28 ? 245 PRO A CB 1 ATOM 1725 C CG . PRO A 1 219 ? -27.652 10.631 -7.948 1.00 23.04 ? 245 PRO A CG 1 ATOM 1726 C CD . PRO A 1 219 ? -27.223 10.843 -9.356 1.00 18.81 ? 245 PRO A CD 1 ATOM 1727 N N . ASP A 1 220 ? -30.144 13.076 -10.241 1.00 23.56 ? 246 ASP A N 1 ATOM 1728 C CA . ASP A 1 220 ? -31.044 14.188 -10.572 1.00 26.64 ? 246 ASP A CA 1 ATOM 1729 C C . ASP A 1 220 ? -31.100 14.419 -12.079 1.00 18.37 ? 246 ASP A C 1 ATOM 1730 O O . ASP A 1 220 ? -31.047 15.562 -12.536 1.00 19.88 ? 246 ASP A O 1 ATOM 1731 C CB . ASP A 1 220 ? -30.611 15.482 -9.868 1.00 22.68 ? 246 ASP A CB 1 ATOM 1732 C CG . ASP A 1 220 ? -30.684 15.382 -8.347 1.00 41.69 ? 246 ASP A CG 1 ATOM 1733 O OD1 . ASP A 1 220 ? -31.617 14.734 -7.813 1.00 39.22 ? 246 ASP A OD1 1 ATOM 1734 O OD2 . ASP A 1 220 ? -29.795 15.958 -7.683 1.00 47.69 ? 246 ASP A OD2 1 ATOM 1735 N N . LEU A 1 221 ? -31.216 13.330 -12.838 1.00 16.26 ? 247 LEU A N 1 ATOM 1736 C CA . LEU A 1 221 ? -31.261 13.392 -14.298 1.00 14.89 ? 247 LEU A CA 1 ATOM 1737 C C . LEU A 1 221 ? -32.329 14.370 -14.829 1.00 32.24 ? 247 LEU A C 1 ATOM 1738 O O . LEU A 1 221 ? -31.998 15.312 -15.547 1.00 14.54 ? 247 LEU A O 1 ATOM 1739 C CB . LEU A 1 221 ? -31.501 11.999 -14.871 1.00 23.28 ? 247 LEU A CB 1 ATOM 1740 C CG . LEU A 1 221 ? -31.479 11.888 -16.394 1.00 20.92 ? 247 LEU A CG 1 ATOM 1741 C CD1 . LEU A 1 221 ? -30.094 12.150 -16.941 1.00 20.29 ? 247 LEU A CD1 1 ATOM 1742 C CD2 . LEU A 1 221 ? -31.950 10.516 -16.829 1.00 21.61 ? 247 LEU A CD2 1 ATOM 1743 N N . GLU A 1 222 ? -33.598 14.149 -14.477 1.00 16.13 ? 248 GLU A N 1 ATOM 1744 C CA . GLU A 1 222 ? -34.686 15.003 -14.975 1.00 18.34 ? 248 GLU A CA 1 ATOM 1745 C C . GLU A 1 222 ? -34.535 16.469 -14.558 1.00 18.86 ? 248 GLU A C 1 ATOM 1746 O O . GLU A 1 222 ? -34.795 17.388 -15.346 1.00 17.27 ? 248 GLU A O 1 ATOM 1747 C CB . GLU A 1 222 ? -36.047 14.488 -14.498 1.00 22.95 ? 248 GLU A CB 1 ATOM 1748 C CG . GLU A 1 222 ? -37.236 15.158 -15.189 1.00 30.55 ? 248 GLU A CG 1 ATOM 1749 C CD . GLU A 1 222 ? -37.645 16.474 -14.546 1.00 42.21 ? 248 GLU A CD 1 ATOM 1750 O OE1 . GLU A 1 222 ? -37.631 16.553 -13.299 1.00 50.93 ? 248 GLU A OE1 1 ATOM 1751 O OE2 . GLU A 1 222 ? -37.970 17.434 -15.284 1.00 36.06 ? 248 GLU A OE2 1 ATOM 1752 N N . GLN A 1 223 ? -34.139 16.683 -13.313 1.00 18.11 ? 249 GLN A N 1 ATOM 1753 C CA . GLN A 1 223 ? -33.973 18.031 -12.788 1.00 18.93 ? 249 GLN A CA 1 ATOM 1754 C C . GLN A 1 223 ? -32.863 18.776 -13.543 1.00 17.78 ? 249 GLN A C 1 ATOM 1755 O O . GLN A 1 223 ? -32.965 19.972 -13.795 1.00 18.07 ? 249 GLN A O 1 ATOM 1756 C CB . GLN A 1 223 ? -33.678 17.981 -11.289 1.00 20.35 ? 249 GLN A CB 1 ATOM 1757 C CG . GLN A 1 223 ? -34.870 17.500 -10.444 1.00 37.18 ? 249 GLN A CG 1 ATOM 1758 C CD . GLN A 1 223 ? -35.242 16.021 -10.673 1.00 40.26 ? 249 GLN A CD 1 ATOM 1759 O OE1 . GLN A 1 223 ? -34.375 15.187 -10.955 1.00 28.67 ? 249 GLN A OE1 1 ATOM 1760 N NE2 . GLN A 1 223 ? -36.543 15.701 -10.557 1.00 30.25 ? 249 GLN A NE2 1 ATOM 1761 N N . ASN A 1 224 ? -31.808 18.066 -13.910 1.00 16.63 ? 250 ASN A N 1 ATOM 1762 C CA . ASN A 1 224 ? -30.760 18.682 -14.716 1.00 15.69 ? 250 ASN A CA 1 ATOM 1763 C C . ASN A 1 224 ? -31.219 19.023 -16.149 1.00 17.28 ? 250 ASN A C 1 ATOM 1764 O O . ASN A 1 224 ? -30.964 20.128 -16.628 1.00 14.89 ? 250 ASN A O 1 ATOM 1765 C CB . ASN A 1 224 ? -29.525 17.791 -14.776 1.00 15.48 ? 250 ASN A CB 1 ATOM 1766 C CG . ASN A 1 224 ? -28.394 18.443 -15.532 1.00 16.33 ? 250 ASN A CG 1 ATOM 1767 O OD1 . ASN A 1 224 ? -27.953 19.532 -15.170 1.00 16.59 ? 250 ASN A OD1 1 ATOM 1768 N ND2 . ASN A 1 224 ? -27.923 17.788 -16.598 1.00 16.62 ? 250 ASN A ND2 1 ATOM 1769 N N . PHE A 1 225 ? -31.887 18.087 -16.825 1.00 14.34 ? 251 PHE A N 1 ATOM 1770 C CA . PHE A 1 225 ? -32.496 18.390 -18.124 1.00 17.90 ? 251 PHE A CA 1 ATOM 1771 C C . PHE A 1 225 ? -33.352 19.665 -18.009 1.00 17.79 ? 251 PHE A C 1 ATOM 1772 O O . PHE A 1 225 ? -33.296 20.545 -18.861 1.00 16.03 ? 251 PHE A O 1 ATOM 1773 C CB . PHE A 1 225 ? -33.377 17.238 -18.633 1.00 13.77 ? 251 PHE A CB 1 ATOM 1774 C CG . PHE A 1 225 ? -32.611 16.027 -19.110 1.00 12.76 ? 251 PHE A CG 1 ATOM 1775 C CD1 . PHE A 1 225 ? -31.233 15.970 -19.015 1.00 19.90 ? 251 PHE A CD1 1 ATOM 1776 C CD2 . PHE A 1 225 ? -33.286 14.939 -19.649 1.00 16.82 ? 251 PHE A CD2 1 ATOM 1777 C CE1 . PHE A 1 225 ? -30.534 14.849 -19.446 1.00 19.38 ? 251 PHE A CE1 1 ATOM 1778 C CE2 . PHE A 1 225 ? -32.590 13.818 -20.103 1.00 17.11 ? 251 PHE A CE2 1 ATOM 1779 C CZ . PHE A 1 225 ? -31.217 13.772 -19.991 1.00 18.85 ? 251 PHE A CZ 1 ATOM 1780 N N . ALA A 1 226 ? -34.126 19.759 -16.935 1.00 17.48 ? 252 ALA A N 1 ATOM 1781 C CA . ALA A 1 226 ? -35.087 20.854 -16.784 1.00 23.70 ? 252 ALA A CA 1 ATOM 1782 C C . ALA A 1 226 ? -34.416 22.222 -16.716 1.00 24.85 ? 252 ALA A C 1 ATOM 1783 O O . ALA A 1 226 ? -34.959 23.202 -17.221 1.00 19.67 ? 252 ALA A O 1 ATOM 1784 C CB . ALA A 1 226 ? -35.959 20.631 -15.556 1.00 18.83 ? 252 ALA A CB 1 ATOM 1785 N N . ARG A 1 227 ? -33.237 22.309 -16.110 1.00 17.39 ? 253 ARG A N 1 ATOM 1786 C CA . ARG A 1 227 ? -32.616 23.622 -15.991 1.00 25.19 ? 253 ARG A CA 1 ATOM 1787 C C . ARG A 1 227 ? -31.921 24.063 -17.294 1.00 22.86 ? 253 ARG A C 1 ATOM 1788 O O . ARG A 1 227 ? -31.767 25.258 -17.541 1.00 17.47 ? 253 ARG A O 1 ATOM 1789 C CB . ARG A 1 227 ? -31.650 23.655 -14.808 1.00 25.64 ? 253 ARG A CB 1 ATOM 1790 C CG . ARG A 1 227 ? -30.407 22.853 -14.963 1.00 20.63 ? 253 ARG A CG 1 ATOM 1791 C CD . ARG A 1 227 ? -29.566 22.927 -13.692 1.00 23.56 ? 253 ARG A CD 1 ATOM 1792 N NE . ARG A 1 227 ? -28.355 22.129 -13.857 1.00 23.38 ? 253 ARG A NE 1 ATOM 1793 C CZ . ARG A 1 227 ? -27.218 22.342 -13.205 1.00 21.87 ? 253 ARG A CZ 1 ATOM 1794 N NH1 . ARG A 1 227 ? -27.131 23.335 -12.332 1.00 19.43 ? 253 ARG A NH1 1 ATOM 1795 N NH2 . ARG A 1 227 ? -26.169 21.560 -13.441 1.00 17.27 ? 253 ARG A NH2 1 ATOM 1796 N N . PHE A 1 228 ? -31.535 23.118 -18.147 1.00 15.68 ? 254 PHE A N 1 ATOM 1797 C CA . PHE A 1 228 ? -31.074 23.483 -19.484 1.00 15.03 ? 254 PHE A CA 1 ATOM 1798 C C . PHE A 1 228 ? -32.243 23.980 -20.337 1.00 15.46 ? 254 PHE A C 1 ATOM 1799 O O . PHE A 1 228 ? -32.122 24.947 -21.077 1.00 16.37 ? 254 PHE A O 1 ATOM 1800 C CB . PHE A 1 228 ? -30.377 22.299 -20.146 1.00 13.83 ? 254 PHE A CB 1 ATOM 1801 C CG . PHE A 1 228 ? -28.958 22.143 -19.709 1.00 13.84 ? 254 PHE A CG 1 ATOM 1802 C CD1 . PHE A 1 228 ? -28.651 21.448 -18.543 1.00 13.75 ? 254 PHE A CD1 1 ATOM 1803 C CD2 . PHE A 1 228 ? -27.934 22.737 -20.428 1.00 14.35 ? 254 PHE A CD2 1 ATOM 1804 C CE1 . PHE A 1 228 ? -27.346 21.326 -18.114 1.00 20.31 ? 254 PHE A CE1 1 ATOM 1805 C CE2 . PHE A 1 228 ? -26.614 22.618 -20.005 1.00 13.42 ? 254 PHE A CE2 1 ATOM 1806 C CZ . PHE A 1 228 ? -26.328 21.915 -18.841 1.00 15.28 ? 254 PHE A CZ 1 ATOM 1807 N N . VAL A 1 229 ? -33.385 23.320 -20.214 1.00 16.49 ? 255 VAL A N 1 ATOM 1808 C CA . VAL A 1 229 ? -34.582 23.734 -20.927 1.00 16.39 ? 255 VAL A CA 1 ATOM 1809 C C . VAL A 1 229 ? -35.029 25.119 -20.425 1.00 20.64 ? 255 VAL A C 1 ATOM 1810 O O . VAL A 1 229 ? -35.462 25.964 -21.210 1.00 22.38 ? 255 VAL A O 1 ATOM 1811 C CB . VAL A 1 229 ? -35.704 22.676 -20.767 1.00 16.64 ? 255 VAL A CB 1 ATOM 1812 C CG1 . VAL A 1 229 ? -37.045 23.219 -21.215 1.00 24.25 ? 255 VAL A CG1 1 ATOM 1813 C CG2 . VAL A 1 229 ? -35.347 21.392 -21.538 1.00 17.96 ? 255 VAL A CG2 1 ATOM 1814 N N . ALA A 1 230 ? -34.898 25.364 -19.124 1.00 21.50 ? 256 ALA A N 1 ATOM 1815 C CA . ALA A 1 230 ? -35.215 26.679 -18.563 1.00 19.76 ? 256 ALA A CA 1 ATOM 1816 C C . ALA A 1 230 ? -34.262 27.764 -19.096 1.00 19.67 ? 256 ALA A C 1 ATOM 1817 O O . ALA A 1 230 ? -34.604 28.942 -19.118 1.00 26.65 ? 256 ALA A O 1 ATOM 1818 C CB . ALA A 1 230 ? -35.173 26.636 -17.033 1.00 21.03 ? 256 ALA A CB 1 ATOM 1819 N N . ALA A 1 231 ? -33.074 27.360 -19.526 1.00 24.46 ? 257 ALA A N 1 ATOM 1820 C CA . ALA A 1 231 ? -32.124 28.285 -20.145 1.00 28.91 ? 257 ALA A CA 1 ATOM 1821 C C . ALA A 1 231 ? -32.497 28.592 -21.596 1.00 26.54 ? 257 ALA A C 1 ATOM 1822 O O . ALA A 1 231 ? -31.901 29.465 -22.225 1.00 24.09 ? 257 ALA A O 1 ATOM 1823 C CB . ALA A 1 231 ? -30.708 27.725 -20.080 1.00 17.58 ? 257 ALA A CB 1 ATOM 1824 N N . GLY A 1 232 ? -33.461 27.860 -22.139 1.00 23.98 ? 258 GLY A N 1 ATOM 1825 C CA . GLY A 1 232 ? -34.005 28.205 -23.441 1.00 26.08 ? 258 GLY A CA 1 ATOM 1826 C C . GLY A 1 232 ? -33.422 27.429 -24.605 1.00 25.14 ? 258 GLY A C 1 ATOM 1827 O O . GLY A 1 232 ? -33.595 27.816 -25.755 1.00 25.80 ? 258 GLY A O 1 ATOM 1828 N N . VAL A 1 233 ? -32.716 26.340 -24.322 1.00 17.18 ? 259 VAL A N 1 ATOM 1829 C CA . VAL A 1 233 ? -32.248 25.481 -25.408 1.00 16.33 ? 259 VAL A CA 1 ATOM 1830 C C . VAL A 1 233 ? -33.139 24.249 -25.508 1.00 18.99 ? 259 VAL A C 1 ATOM 1831 O O . VAL A 1 233 ? -33.836 23.908 -24.555 1.00 15.64 ? 259 VAL A O 1 ATOM 1832 C CB . VAL A 1 233 ? -30.772 25.043 -25.226 1.00 16.81 ? 259 VAL A CB 1 ATOM 1833 C CG1 . VAL A 1 233 ? -29.834 26.250 -25.324 1.00 15.28 ? 259 VAL A CG1 1 ATOM 1834 C CG2 . VAL A 1 233 ? -30.593 24.280 -23.910 1.00 14.18 ? 259 VAL A CG2 1 ATOM 1835 N N . GLU A 1 234 ? -33.149 23.611 -26.679 1.00 15.51 ? 260 GLU A N 1 ATOM 1836 C CA . GLU A 1 234 ? -33.716 22.286 -26.797 1.00 16.03 ? 260 GLU A CA 1 ATOM 1837 C C . GLU A 1 234 ? -32.641 21.301 -26.368 1.00 17.70 ? 260 GLU A C 1 ATOM 1838 O O . GLU A 1 234 ? -31.455 21.634 -26.308 1.00 13.02 ? 260 GLU A O 1 ATOM 1839 C CB . GLU A 1 234 ? -34.193 21.983 -28.225 1.00 16.26 ? 260 GLU A CB 1 ATOM 1840 C CG . GLU A 1 234 ? -33.075 21.867 -29.260 1.00 21.06 ? 260 GLU A CG 1 ATOM 1841 C CD . GLU A 1 234 ? -33.608 21.617 -30.672 1.00 27.36 ? 260 GLU A CD 1 ATOM 1842 O OE1 . GLU A 1 234 ? -33.147 20.655 -31.322 1.00 16.91 ? 260 GLU A OE1 1 ATOM 1843 O OE2 . GLU A 1 234 ? -34.486 22.383 -31.132 1.00 25.75 ? 260 GLU A OE2 1 ATOM 1844 N N . ILE A 1 235 ? -33.059 20.091 -26.044 1.00 13.14 ? 261 ILE A N 1 ATOM 1845 C CA . ILE A 1 235 ? -32.098 19.068 -25.671 1.00 12.08 ? 261 ILE A CA 1 ATOM 1846 C C . ILE A 1 235 ? -32.400 17.780 -26.417 1.00 12.13 ? 261 ILE A C 1 ATOM 1847 O O . ILE A 1 235 ? -33.507 17.578 -26.939 1.00 12.44 ? 261 ILE A O 1 ATOM 1848 C CB . ILE A 1 235 ? -32.096 18.783 -24.133 1.00 11.97 ? 261 ILE A CB 1 ATOM 1849 C CG1 . ILE A 1 235 ? -33.431 18.200 -23.679 1.00 13.33 ? 261 ILE A CG1 1 ATOM 1850 C CG2 . ILE A 1 235 ? -31.835 20.049 -23.338 1.00 12.45 ? 261 ILE A CG2 1 ATOM 1851 C CD1 . ILE A 1 235 ? -33.415 17.701 -22.228 1.00 14.74 ? 261 ILE A CD1 1 ATOM 1852 N N . ALA A 1 236 ? -31.402 16.905 -26.445 1.00 11.10 ? 262 ALA A N 1 ATOM 1853 C CA . ALA A 1 236 ? -31.547 15.586 -27.008 1.00 10.89 ? 262 ALA A CA 1 ATOM 1854 C C . ALA A 1 236 ? -30.629 14.619 -26.269 1.00 10.19 ? 262 ALA A C 1 ATOM 1855 O O . ALA A 1 236 ? -29.574 15.004 -25.785 1.00 11.37 ? 262 ALA A O 1 ATOM 1856 C CB . ALA A 1 236 ? -31.226 15.603 -28.487 1.00 11.36 ? 262 ALA A CB 1 ATOM 1857 N N . VAL A 1 237 ? -31.064 13.370 -26.160 1.00 11.63 ? 263 VAL A N 1 ATOM 1858 C CA . VAL A 1 237 ? -30.207 12.303 -25.677 1.00 11.59 ? 263 VAL A CA 1 ATOM 1859 C C . VAL A 1 237 ? -29.497 11.774 -26.907 1.00 11.72 ? 263 VAL A C 1 ATOM 1860 O O . VAL A 1 237 ? -30.150 11.353 -27.864 1.00 10.28 ? 263 VAL A O 1 ATOM 1861 C CB . VAL A 1 237 ? -31.015 11.211 -24.960 1.00 14.63 ? 263 VAL A CB 1 ATOM 1862 C CG1 . VAL A 1 237 ? -30.168 9.986 -24.705 1.00 13.37 ? 263 VAL A CG1 1 ATOM 1863 C CG2 . VAL A 1 237 ? -31.578 11.772 -23.651 1.00 17.62 ? 263 VAL A CG2 1 ATOM 1864 N N . THR A 1 238 ? -28.168 11.839 -26.920 1.00 9.16 ? 264 THR A N 1 ATOM 1865 C CA . THR A 1 238 ? -27.462 11.644 -28.183 1.00 11.28 ? 264 THR A CA 1 ATOM 1866 C C . THR A 1 238 ? -26.717 10.315 -28.386 1.00 11.44 ? 264 THR A C 1 ATOM 1867 O O . THR A 1 238 ? -26.467 9.925 -29.528 1.00 9.57 ? 264 THR A O 1 ATOM 1868 C CB . THR A 1 238 ? -26.443 12.779 -28.392 1.00 13.84 ? 264 THR A CB 1 ATOM 1869 O OG1 . THR A 1 238 ? -25.602 12.879 -27.225 1.00 10.31 ? 264 THR A OG1 1 ATOM 1870 C CG2 . THR A 1 238 ? -27.187 14.088 -28.606 1.00 12.81 ? 264 THR A CG2 1 ATOM 1871 N N . GLU A 1 239 ? -26.321 9.634 -27.320 1.00 10.63 ? 265 GLU A N 1 ATOM 1872 C CA . GLU A 1 239 ? -25.494 8.419 -27.499 1.00 8.91 ? 265 GLU A CA 1 ATOM 1873 C C . GLU A 1 239 ? -25.850 7.354 -26.468 1.00 8.81 ? 265 GLU A C 1 ATOM 1874 O O . GLU A 1 239 ? -24.975 6.727 -25.854 1.00 8.79 ? 265 GLU A O 1 ATOM 1875 C CB . GLU A 1 239 ? -24.001 8.768 -27.412 1.00 10.33 ? 265 GLU A CB 1 ATOM 1876 C CG . GLU A 1 239 ? -23.574 9.903 -28.361 1.00 9.28 ? 265 GLU A CG 1 ATOM 1877 C CD . GLU A 1 239 ? -22.072 10.224 -28.319 1.00 18.56 ? 265 GLU A CD 1 ATOM 1878 O OE1 . GLU A 1 239 ? -21.285 9.401 -27.807 1.00 12.17 ? 265 GLU A OE1 1 ATOM 1879 O OE2 . GLU A 1 239 ? -21.683 11.306 -28.815 1.00 16.95 ? 265 GLU A OE2 1 ATOM 1880 N N . LEU A 1 240 ? -27.146 7.161 -26.276 1.00 8.93 ? 266 LEU A N 1 ATOM 1881 C CA . LEU A 1 240 ? -27.619 6.326 -25.181 1.00 11.89 ? 266 LEU A CA 1 ATOM 1882 C C . LEU A 1 240 ? -27.149 4.884 -25.303 1.00 9.22 ? 266 LEU A C 1 ATOM 1883 O O . LEU A 1 240 ? -27.317 4.257 -26.343 1.00 10.21 ? 266 LEU A O 1 ATOM 1884 C CB . LEU A 1 240 ? -29.147 6.371 -25.112 1.00 11.28 ? 266 LEU A CB 1 ATOM 1885 C CG . LEU A 1 240 ? -29.882 5.606 -24.007 1.00 13.58 ? 266 LEU A CG 1 ATOM 1886 C CD1 . LEU A 1 240 ? -29.391 6.002 -22.609 1.00 9.78 ? 266 LEU A CD1 1 ATOM 1887 C CD2 . LEU A 1 240 ? -31.390 5.851 -24.130 1.00 10.45 ? 266 LEU A CD2 1 ATOM 1888 N N . ASP A 1 241 ? -26.535 4.373 -24.242 1.00 9.25 ? 267 ASP A N 1 ATOM 1889 C CA . ASP A 1 241 ? -26.454 2.923 -24.010 1.00 9.64 ? 267 ASP A CA 1 ATOM 1890 C C . ASP A 1 241 ? -26.311 2.697 -22.513 1.00 9.89 ? 267 ASP A C 1 ATOM 1891 O O . ASP A 1 241 ? -25.863 3.578 -21.761 1.00 9.76 ? 267 ASP A O 1 ATOM 1892 C CB . ASP A 1 241 ? -25.321 2.211 -24.821 1.00 9.74 ? 267 ASP A CB 1 ATOM 1893 C CG . ASP A 1 241 ? -23.969 2.954 -24.807 1.00 12.82 ? 267 ASP A CG 1 ATOM 1894 O OD1 . ASP A 1 241 ? -23.596 3.546 -23.778 1.00 13.44 ? 267 ASP A OD1 1 ATOM 1895 O OD2 . ASP A 1 241 ? -23.254 2.905 -25.842 1.00 12.87 ? 267 ASP A OD2 1 ATOM 1896 N N . ILE A 1 242 ? -26.763 1.534 -22.060 1.00 10.44 ? 268 ILE A N 1 ATOM 1897 C CA . ILE A 1 242 ? -26.803 1.267 -20.636 1.00 12.29 ? 268 ILE A CA 1 ATOM 1898 C C . ILE A 1 242 ? -26.218 -0.109 -20.381 1.00 13.07 ? 268 ILE A C 1 ATOM 1899 O O . ILE A 1 242 ? -26.893 -1.140 -20.524 1.00 12.05 ? 268 ILE A O 1 ATOM 1900 C CB . ILE A 1 242 ? -28.233 1.379 -20.074 1.00 11.90 ? 268 ILE A CB 1 ATOM 1901 C CG1 . ILE A 1 242 ? -28.812 2.772 -20.368 1.00 13.27 ? 268 ILE A CG1 1 ATOM 1902 C CG2 . ILE A 1 242 ? -28.222 1.126 -18.560 1.00 12.63 ? 268 ILE A CG2 1 ATOM 1903 C CD1 . ILE A 1 242 ? -30.245 2.962 -19.863 1.00 11.72 ? 268 ILE A CD1 1 ATOM 1904 N N . ARG A 1 243 ? -24.941 -0.110 -20.016 1.00 11.56 ? 269 ARG A N 1 ATOM 1905 C CA . ARG A 1 243 ? -24.163 -1.327 -20.048 1.00 12.09 ? 269 ARG A CA 1 ATOM 1906 C C . ARG A 1 243 ? -24.167 -2.060 -18.713 1.00 17.15 ? 269 ARG A C 1 ATOM 1907 O O . ARG A 1 243 ? -24.503 -1.488 -17.671 1.00 13.44 ? 269 ARG A O 1 ATOM 1908 C CB . ARG A 1 243 ? -22.730 -1.007 -20.479 1.00 12.40 ? 269 ARG A CB 1 ATOM 1909 C CG . ARG A 1 243 ? -21.947 -0.135 -19.495 1.00 14.26 ? 269 ARG A CG 1 ATOM 1910 C CD . ARG A 1 243 ? -20.582 0.285 -20.064 1.00 14.56 ? 269 ARG A CD 1 ATOM 1911 N NE . ARG A 1 243 ? -19.763 0.930 -19.037 1.00 12.50 ? 269 ARG A NE 1 ATOM 1912 C CZ . ARG A 1 243 ? -19.830 2.225 -18.739 1.00 22.42 ? 269 ARG A CZ 1 ATOM 1913 N NH1 . ARG A 1 243 ? -20.660 3.026 -19.399 1.00 15.89 ? 269 ARG A NH1 1 ATOM 1914 N NH2 . ARG A 1 243 ? -19.065 2.724 -17.784 1.00 24.10 ? 269 ARG A NH2 1 ATOM 1915 N N . MET A 1 244 ? -23.788 -3.333 -18.758 1.00 14.49 ? 270 MET A N 1 ATOM 1916 C CA . MET A 1 244 ? -23.753 -4.184 -17.562 1.00 15.60 ? 270 MET A CA 1 ATOM 1917 C C . MET A 1 244 ? -22.632 -5.192 -17.708 1.00 15.51 ? 270 MET A C 1 ATOM 1918 O O . MET A 1 244 ? -22.084 -5.344 -18.800 1.00 15.56 ? 270 MET A O 1 ATOM 1919 C CB . MET A 1 244 ? -25.093 -4.905 -17.363 1.00 15.49 ? 270 MET A CB 1 ATOM 1920 C CG . MET A 1 244 ? -25.411 -5.907 -18.471 1.00 15.54 ? 270 MET A CG 1 ATOM 1921 S SD . MET A 1 244 ? -27.116 -6.513 -18.437 1.00 21.62 ? 270 MET A SD 1 ATOM 1922 C CE . MET A 1 244 ? -28.030 -5.041 -18.923 1.00 18.11 ? 270 MET A CE 1 ATOM 1923 N N . ASN A 1 245 ? -22.281 -5.876 -16.619 1.00 16.70 ? 271 ASN A N 1 ATOM 1924 C CA . ASN A 1 245 ? -21.277 -6.934 -16.680 1.00 17.56 ? 271 ASN A CA 1 ATOM 1925 C C . ASN A 1 245 ? -21.826 -8.172 -17.373 1.00 20.31 ? 271 ASN A C 1 ATOM 1926 O O . ASN A 1 245 ? -23.005 -8.505 -17.209 1.00 18.79 ? 271 ASN A O 1 ATOM 1927 C CB . ASN A 1 245 ? -20.782 -7.311 -15.278 1.00 20.72 ? 271 ASN A CB 1 ATOM 1928 C CG . ASN A 1 245 ? -19.987 -6.197 -14.614 1.00 22.42 ? 271 ASN A CG 1 ATOM 1929 O OD1 . ASN A 1 245 ? -19.321 -5.403 -15.283 1.00 34.32 ? 271 ASN A OD1 1 ATOM 1930 N ND2 . ASN A 1 245 ? -20.055 -6.137 -13.292 1.00 27.36 ? 271 ASN A ND2 1 ATOM 1931 N N . LEU A 1 246 ? -20.971 -8.846 -18.143 1.00 19.34 ? 272 LEU A N 1 ATOM 1932 C CA . LEU A 1 246 ? -21.355 -10.069 -18.861 1.00 25.02 ? 272 LEU A CA 1 ATOM 1933 C C . LEU A 1 246 ? -20.846 -11.302 -18.125 1.00 28.88 ? 272 LEU A C 1 ATOM 1934 O O . LEU A 1 246 ? -19.780 -11.254 -17.516 1.00 23.89 ? 272 LEU A O 1 ATOM 1935 C CB . LEU A 1 246 ? -20.795 -10.065 -20.294 1.00 26.56 ? 272 LEU A CB 1 ATOM 1936 C CG . LEU A 1 246 ? -21.130 -8.873 -21.188 1.00 25.41 ? 272 LEU A CG 1 ATOM 1937 C CD1 . LEU A 1 246 ? -20.438 -9.013 -22.538 1.00 21.57 ? 272 LEU A CD1 1 ATOM 1938 C CD2 . LEU A 1 246 ? -22.629 -8.791 -21.357 1.00 21.49 ? 272 LEU A CD2 1 ATOM 1939 N N . PRO A 1 247 ? -21.592 -12.418 -18.190 1.00 35.59 ? 273 PRO A N 1 ATOM 1940 C CA . PRO A 1 247 ? -22.900 -12.573 -18.840 1.00 37.83 ? 273 PRO A CA 1 ATOM 1941 C C . PRO A 1 247 ? -24.012 -11.883 -18.056 1.00 35.61 ? 273 PRO A C 1 ATOM 1942 O O . PRO A 1 247 ? -23.904 -11.751 -16.839 1.00 36.49 ? 273 PRO A O 1 ATOM 1943 C CB . PRO A 1 247 ? -23.102 -14.092 -18.871 1.00 40.72 ? 273 PRO A CB 1 ATOM 1944 C CG . PRO A 1 247 ? -22.253 -14.608 -17.773 1.00 45.09 ? 273 PRO A CG 1 ATOM 1945 C CD . PRO A 1 247 ? -21.057 -13.705 -17.717 1.00 39.95 ? 273 PRO A CD 1 ATOM 1946 N N . PRO A 1 248 ? -25.060 -11.421 -18.751 1.00 36.14 ? 274 PRO A N 1 ATOM 1947 C CA . PRO A 1 248 ? -26.074 -10.603 -18.080 1.00 32.57 ? 274 PRO A CA 1 ATOM 1948 C C . PRO A 1 248 ? -26.912 -11.385 -17.074 1.00 34.32 ? 274 PRO A C 1 ATOM 1949 O O . PRO A 1 248 ? -27.455 -12.439 -17.402 1.00 34.99 ? 274 PRO A O 1 ATOM 1950 C CB . PRO A 1 248 ? -26.950 -10.099 -19.243 1.00 32.37 ? 274 PRO A CB 1 ATOM 1951 C CG . PRO A 1 248 ? -26.116 -10.283 -20.469 1.00 32.48 ? 274 PRO A CG 1 ATOM 1952 C CD . PRO A 1 248 ? -25.284 -11.498 -20.207 1.00 23.74 ? 274 PRO A CD 1 ATOM 1953 N N . SER A 1 249 ? -27.010 -10.866 -15.854 1.00 32.39 ? 275 SER A N 1 ATOM 1954 C CA . SER A 1 249 ? -27.912 -11.435 -14.860 1.00 31.50 ? 275 SER A CA 1 ATOM 1955 C C . SER A 1 249 ? -29.347 -11.020 -15.147 1.00 36.57 ? 275 SER A C 1 ATOM 1956 O O . SER A 1 249 ? -29.595 -10.017 -15.826 1.00 36.41 ? 275 SER A O 1 ATOM 1957 C CB . SER A 1 249 ? -27.526 -10.991 -13.456 1.00 34.16 ? 275 SER A CB 1 ATOM 1958 O OG . SER A 1 249 ? -27.789 -9.611 -13.292 1.00 39.34 ? 275 SER A OG 1 ATOM 1959 N N . GLN A 1 250 ? -30.291 -11.789 -14.621 1.00 33.62 ? 276 GLN A N 1 ATOM 1960 C CA . GLN A 1 250 ? -31.700 -11.470 -14.775 1.00 34.34 ? 276 GLN A CA 1 ATOM 1961 C C . GLN A 1 250 ? -32.010 -10.125 -14.121 1.00 29.87 ? 276 GLN A C 1 ATOM 1962 O O . GLN A 1 250 ? -32.746 -9.306 -14.677 1.00 35.14 ? 276 GLN A O 1 ATOM 1963 C CB . GLN A 1 250 ? -32.571 -12.578 -14.173 1.00 36.86 ? 276 GLN A CB 1 ATOM 1964 C CG . GLN A 1 250 ? -34.070 -12.338 -14.313 1.00 50.26 ? 276 GLN A CG 1 ATOM 1965 C CD . GLN A 1 250 ? -34.500 -12.134 -15.761 1.00 62.66 ? 276 GLN A CD 1 ATOM 1966 O OE1 . GLN A 1 250 ? -33.960 -12.758 -16.678 1.00 70.88 ? 276 GLN A OE1 1 ATOM 1967 N NE2 . GLN A 1 250 ? -35.470 -11.247 -15.971 1.00 61.61 ? 276 GLN A NE2 1 ATOM 1968 N N . ALA A 1 251 ? -31.424 -9.897 -12.950 1.00 28.14 ? 277 ALA A N 1 ATOM 1969 C CA . ALA A 1 251 ? -31.630 -8.656 -12.218 1.00 27.72 ? 277 ALA A CA 1 ATOM 1970 C C . ALA A 1 251 ? -31.143 -7.445 -13.016 1.00 26.52 ? 277 ALA A C 1 ATOM 1971 O O . ALA A 1 251 ? -31.802 -6.412 -13.038 1.00 27.24 ? 277 ALA A O 1 ATOM 1972 C CB . ALA A 1 251 ? -30.935 -8.719 -10.858 1.00 31.87 ? 277 ALA A CB 1 ATOM 1973 N N . ASP A 1 252 ? -30.003 -7.570 -13.686 1.00 23.83 ? 278 ASP A N 1 ATOM 1974 C CA . ASP A 1 252 ? -29.488 -6.444 -14.467 1.00 21.52 ? 278 ASP A CA 1 ATOM 1975 C C . ASP A 1 252 ? -30.296 -6.210 -15.737 1.00 23.84 ? 278 ASP A C 1 ATOM 1976 O O . ASP A 1 252 ? -30.491 -5.069 -16.149 1.00 19.05 ? 278 ASP A O 1 ATOM 1977 C CB . ASP A 1 252 ? -28.017 -6.653 -14.815 1.00 26.41 ? 278 ASP A CB 1 ATOM 1978 C CG . ASP A 1 252 ? -27.090 -6.249 -13.679 1.00 31.42 ? 278 ASP A CG 1 ATOM 1979 O OD1 . ASP A 1 252 ? -27.552 -5.532 -12.762 1.00 31.73 ? 278 ASP A OD1 1 ATOM 1980 O OD2 . ASP A 1 252 ? -25.900 -6.628 -13.715 1.00 33.78 ? 278 ASP A OD2 1 ATOM 1981 N N . ILE A 1 253 ? -30.774 -7.281 -16.357 1.00 20.55 ? 279 ILE A N 1 ATOM 1982 C CA . ILE A 1 253 ? -31.607 -7.128 -17.538 1.00 24.34 ? 279 ILE A CA 1 ATOM 1983 C C . ILE A 1 253 ? -32.892 -6.379 -17.179 1.00 19.73 ? 279 ILE A C 1 ATOM 1984 O O . ILE A 1 253 ? -33.313 -5.471 -17.905 1.00 20.16 ? 279 ILE A O 1 ATOM 1985 C CB . ILE A 1 253 ? -31.947 -8.494 -18.168 1.00 25.75 ? 279 ILE A CB 1 ATOM 1986 C CG1 . ILE A 1 253 ? -30.685 -9.160 -18.705 1.00 28.90 ? 279 ILE A CG1 1 ATOM 1987 C CG2 . ILE A 1 253 ? -32.914 -8.323 -19.303 1.00 28.35 ? 279 ILE A CG2 1 ATOM 1988 C CD1 . ILE A 1 253 ? -30.868 -10.642 -18.969 1.00 35.85 ? 279 ILE A CD1 1 ATOM 1989 N N . GLU A 1 254 ? -33.503 -6.757 -16.057 1.00 21.64 ? 280 GLU A N 1 ATOM 1990 C CA . GLU A 1 254 ? -34.711 -6.092 -15.584 1.00 24.44 ? 280 GLU A CA 1 ATOM 1991 C C . GLU A 1 254 ? -34.454 -4.624 -15.208 1.00 24.79 ? 280 GLU A C 1 ATOM 1992 O O . GLU A 1 254 ? -35.221 -3.740 -15.586 1.00 20.45 ? 280 GLU A O 1 ATOM 1993 C CB . GLU A 1 254 ? -35.308 -6.844 -14.392 1.00 28.75 ? 280 GLU A CB 1 ATOM 1994 C CG . GLU A 1 254 ? -36.003 -8.154 -14.759 1.00 42.94 ? 280 GLU A CG 1 ATOM 1995 C CD . GLU A 1 254 ? -36.599 -8.871 -13.539 1.00 61.70 ? 280 GLU A CD 1 ATOM 1996 O OE1 . GLU A 1 254 ? -35.886 -9.019 -12.520 1.00 65.86 ? 280 GLU A OE1 1 ATOM 1997 O OE2 . GLU A 1 254 ? -37.782 -9.282 -13.599 1.00 65.65 ? 280 GLU A OE2 1 ATOM 1998 N N . GLN A 1 255 ? -33.377 -4.364 -14.479 1.00 22.37 ? 281 GLN A N 1 ATOM 1999 C CA . GLN A 1 255 ? -33.027 -2.993 -14.110 1.00 20.19 ? 281 GLN A CA 1 ATOM 2000 C C . GLN A 1 255 ? -32.711 -2.141 -15.345 1.00 29.22 ? 281 GLN A C 1 ATOM 2001 O O . GLN A 1 255 ? -33.038 -0.958 -15.384 1.00 17.28 ? 281 GLN A O 1 ATOM 2002 C CB . GLN A 1 255 ? -31.841 -2.975 -13.136 1.00 20.89 ? 281 GLN A CB 1 ATOM 2003 C CG . GLN A 1 255 ? -31.494 -1.583 -12.589 1.00 23.55 ? 281 GLN A CG 1 ATOM 2004 C CD . GLN A 1 255 ? -32.685 -0.885 -11.944 1.00 24.45 ? 281 GLN A CD 1 ATOM 2005 O OE1 . GLN A 1 255 ? -33.455 -1.501 -11.198 1.00 23.35 ? 281 GLN A OE1 1 ATOM 2006 N NE2 . GLN A 1 255 ? -32.841 0.407 -12.230 1.00 20.40 ? 281 GLN A NE2 1 ATOM 2007 N N . GLN A 1 256 ? -32.091 -2.741 -16.358 1.00 16.98 ? 282 GLN A N 1 ATOM 2008 C CA . GLN A 1 256 ? -31.797 -2.013 -17.589 1.00 20.37 ? 282 GLN A CA 1 ATOM 2009 C C . GLN A 1 256 ? -33.085 -1.484 -18.219 1.00 19.29 ? 282 GLN A C 1 ATOM 2010 O O . GLN A 1 256 ? -33.124 -0.360 -18.731 1.00 13.79 ? 282 GLN A O 1 ATOM 2011 C CB . GLN A 1 256 ? -31.059 -2.892 -18.602 1.00 21.79 ? 282 GLN A CB 1 ATOM 2012 C CG . GLN A 1 256 ? -30.763 -2.152 -19.917 1.00 14.53 ? 282 GLN A CG 1 ATOM 2013 C CD . GLN A 1 256 ? -30.230 -3.057 -21.013 1.00 18.29 ? 282 GLN A CD 1 ATOM 2014 O OE1 . GLN A 1 256 ? -30.896 -4.002 -21.434 1.00 19.84 ? 282 GLN A OE1 1 ATOM 2015 N NE2 . GLN A 1 256 ? -29.020 -2.773 -21.474 1.00 13.19 ? 282 GLN A NE2 1 ATOM 2016 N N . ALA A 1 257 ? -34.120 -2.317 -18.197 1.00 16.02 ? 283 ALA A N 1 ATOM 2017 C CA . ALA A 1 257 ? -35.433 -1.911 -18.666 1.00 18.50 ? 283 ALA A CA 1 ATOM 2018 C C . ALA A 1 257 ? -35.887 -0.665 -17.905 1.00 16.45 ? 283 ALA A C 1 ATOM 2019 O O . ALA A 1 257 ? -36.325 0.306 -18.504 1.00 18.29 ? 283 ALA A O 1 ATOM 2020 C CB . ALA A 1 257 ? -36.447 -3.060 -18.501 1.00 18.08 ? 283 ALA A CB 1 ATOM 2021 N N . ARG A 1 258 ? -35.752 -0.686 -16.582 1.00 17.58 ? 284 ARG A N 1 ATOM 2022 C CA . ARG A 1 258 ? -36.183 0.450 -15.777 1.00 18.10 ? 284 ARG A CA 1 ATOM 2023 C C . ARG A 1 258 ? -35.350 1.691 -16.104 1.00 21.23 ? 284 ARG A C 1 ATOM 2024 O O . ARG A 1 258 ? -35.879 2.803 -16.162 1.00 16.45 ? 284 ARG A O 1 ATOM 2025 C CB . ARG A 1 258 ? -36.098 0.123 -14.287 1.00 19.90 ? 284 ARG A CB 1 ATOM 2026 C CG . ARG A 1 258 ? -36.954 -1.053 -13.888 1.00 21.83 ? 284 ARG A CG 1 ATOM 2027 C CD . ARG A 1 258 ? -36.894 -1.298 -12.387 1.00 23.92 ? 284 ARG A CD 1 ATOM 2028 N NE . ARG A 1 258 ? -37.445 -2.608 -12.048 1.00 28.34 ? 284 ARG A NE 1 ATOM 2029 C CZ . ARG A 1 258 ? -36.708 -3.658 -11.707 1.00 36.22 ? 284 ARG A CZ 1 ATOM 2030 N NH1 . ARG A 1 258 ? -35.390 -3.543 -11.628 1.00 25.53 ? 284 ARG A NH1 1 ATOM 2031 N NH2 . ARG A 1 258 ? -37.291 -4.815 -11.418 1.00 43.49 ? 284 ARG A NH2 1 ATOM 2032 N N . ASP A 1 259 ? -34.054 1.496 -16.338 1.00 15.56 ? 285 ASP A N 1 ATOM 2033 C CA . ASP A 1 259 ? -33.157 2.608 -16.660 1.00 15.05 ? 285 ASP A CA 1 ATOM 2034 C C . ASP A 1 259 ? -33.462 3.276 -18.003 1.00 14.37 ? 285 ASP A C 1 ATOM 2035 O O . ASP A 1 259 ? -33.448 4.505 -18.101 1.00 13.83 ? 285 ASP A O 1 ATOM 2036 C CB . ASP A 1 259 ? -31.702 2.140 -16.639 1.00 17.35 ? 285 ASP A CB 1 ATOM 2037 C CG . ASP A 1 259 ? -31.222 1.750 -15.226 1.00 25.82 ? 285 ASP A CG 1 ATOM 2038 O OD1 . ASP A 1 259 ? -31.712 2.319 -14.218 1.00 22.18 ? 285 ASP A OD1 1 ATOM 2039 O OD2 . ASP A 1 259 ? -30.345 0.869 -15.130 1.00 23.05 ? 285 ASP A OD2 1 ATOM 2040 N N . TYR A 1 260 ? -33.708 2.490 -19.047 1.00 12.62 ? 286 TYR A N 1 ATOM 2041 C CA . TYR A 1 260 ? -34.185 3.081 -20.299 1.00 13.61 ? 286 TYR A CA 1 ATOM 2042 C C . TYR A 1 260 ? -35.469 3.890 -20.086 1.00 12.62 ? 286 TYR A C 1 ATOM 2043 O O . TYR A 1 260 ? -35.594 5.004 -20.591 1.00 14.09 ? 286 TYR A O 1 ATOM 2044 C CB . TYR A 1 260 ? -34.416 2.013 -21.368 1.00 12.96 ? 286 TYR A CB 1 ATOM 2045 C CG . TYR A 1 260 ? -33.185 1.745 -22.196 1.00 11.83 ? 286 TYR A CG 1 ATOM 2046 C CD1 . TYR A 1 260 ? -32.911 2.514 -23.313 1.00 10.97 ? 286 TYR A CD1 1 ATOM 2047 C CD2 . TYR A 1 260 ? -32.284 0.745 -21.844 1.00 10.84 ? 286 TYR A CD2 1 ATOM 2048 C CE1 . TYR A 1 260 ? -31.772 2.289 -24.089 1.00 13.26 ? 286 TYR A CE1 1 ATOM 2049 C CE2 . TYR A 1 260 ? -31.126 0.520 -22.611 1.00 10.15 ? 286 TYR A CE2 1 ATOM 2050 C CZ . TYR A 1 260 ? -30.892 1.296 -23.739 1.00 9.35 ? 286 TYR A CZ 1 ATOM 2051 O OH . TYR A 1 260 ? -29.766 1.100 -24.531 1.00 11.22 ? 286 TYR A OH 1 ATOM 2052 N N . ALA A 1 261 ? -36.409 3.351 -19.327 1.00 13.97 ? 287 ALA A N 1 ATOM 2053 C CA . ALA A 1 261 ? -37.651 4.083 -19.065 1.00 15.04 ? 287 ALA A CA 1 ATOM 2054 C C . ALA A 1 261 ? -37.376 5.390 -18.308 1.00 17.02 ? 287 ALA A C 1 ATOM 2055 O O . ALA A 1 261 ? -38.046 6.404 -18.527 1.00 19.93 ? 287 ALA A O 1 ATOM 2056 C CB . ALA A 1 261 ? -38.632 3.215 -18.286 1.00 16.81 ? 287 ALA A CB 1 ATOM 2057 N N . THR A 1 262 ? -36.387 5.362 -17.425 1.00 17.68 ? 288 THR A N 1 ATOM 2058 C CA . THR A 1 262 ? -36.042 6.537 -16.637 1.00 22.44 ? 288 THR A CA 1 ATOM 2059 C C . THR A 1 262 ? -35.537 7.670 -17.541 1.00 18.36 ? 288 THR A C 1 ATOM 2060 O O . THR A 1 262 ? -35.904 8.839 -17.375 1.00 14.74 ? 288 THR A O 1 ATOM 2061 C CB . THR A 1 262 ? -34.983 6.194 -15.575 1.00 22.34 ? 288 THR A CB 1 ATOM 2062 O OG1 . THR A 1 262 ? -35.578 5.356 -14.575 1.00 20.42 ? 288 THR A OG1 1 ATOM 2063 C CG2 . THR A 1 262 ? -34.450 7.463 -14.915 1.00 19.81 ? 288 THR A CG2 1 ATOM 2064 N N . VAL A 1 263 ? -34.699 7.307 -18.501 1.00 12.92 ? 289 VAL A N 1 ATOM 2065 C CA . VAL A 1 263 ? -34.181 8.265 -19.465 1.00 12.03 ? 289 VAL A CA 1 ATOM 2066 C C . VAL A 1 263 ? -35.291 8.809 -20.359 1.00 15.36 ? 289 VAL A C 1 ATOM 2067 O O . VAL A 1 263 ? -35.374 10.017 -20.580 1.00 15.34 ? 289 VAL A O 1 ATOM 2068 C CB . VAL A 1 263 ? -33.081 7.624 -20.353 1.00 14.61 ? 289 VAL A CB 1 ATOM 2069 C CG1 . VAL A 1 263 ? -32.643 8.598 -21.431 1.00 13.47 ? 289 VAL A CG1 1 ATOM 2070 C CG2 . VAL A 1 263 ? -31.906 7.199 -19.485 1.00 11.32 ? 289 VAL A CG2 1 ATOM 2071 N N . VAL A 1 264 ? -36.154 7.925 -20.859 1.00 15.65 ? 290 VAL A N 1 ATOM 2072 C CA . VAL A 1 264 ? -37.299 8.357 -21.672 1.00 15.02 ? 290 VAL A CA 1 ATOM 2073 C C . VAL A 1 264 ? -38.190 9.335 -20.900 1.00 14.21 ? 290 VAL A C 1 ATOM 2074 O O . VAL A 1 264 ? -38.616 10.364 -21.441 1.00 19.13 ? 290 VAL A O 1 ATOM 2075 C CB . VAL A 1 264 ? -38.159 7.164 -22.136 1.00 20.91 ? 290 VAL A CB 1 ATOM 2076 C CG1 . VAL A 1 264 ? -39.493 7.652 -22.721 1.00 14.53 ? 290 VAL A CG1 1 ATOM 2077 C CG2 . VAL A 1 264 ? -37.393 6.302 -23.143 1.00 24.75 ? 290 VAL A CG2 1 ATOM 2078 N N . ASN A 1 265 ? -38.470 9.015 -19.639 1.00 15.15 ? 291 ASN A N 1 ATOM 2079 C CA . ASN A 1 265 ? -39.350 9.851 -18.822 1.00 22.60 ? 291 ASN A CA 1 ATOM 2080 C C . ASN A 1 265 ? -38.736 11.232 -18.534 1.00 18.53 ? 291 ASN A C 1 ATOM 2081 O O . ASN A 1 265 ? -39.442 12.232 -18.519 1.00 17.96 ? 291 ASN A O 1 ATOM 2082 C CB . ASN A 1 265 ? -39.714 9.129 -17.517 1.00 27.10 ? 291 ASN A CB 1 ATOM 2083 C CG . ASN A 1 265 ? -40.647 7.921 -17.751 1.00 35.24 ? 291 ASN A CG 1 ATOM 2084 O OD1 . ASN A 1 265 ? -41.405 7.885 -18.724 1.00 36.24 ? 291 ASN A OD1 1 ATOM 2085 N ND2 . ASN A 1 265 ? -40.577 6.933 -16.864 1.00 31.94 ? 291 ASN A ND2 1 ATOM 2086 N N . ALA A 1 266 ? -37.422 11.280 -18.327 1.00 15.66 ? 292 ALA A N 1 ATOM 2087 C CA . ALA A 1 266 ? -36.705 12.537 -18.126 1.00 22.08 ? 292 ALA A CA 1 ATOM 2088 C C . ALA A 1 266 ? -36.787 13.427 -19.376 1.00 15.34 ? 292 ALA A C 1 ATOM 2089 O O . ALA A 1 266 ? -36.885 14.653 -19.269 1.00 26.28 ? 292 ALA A O 1 ATOM 2090 C CB . ALA A 1 266 ? -35.242 12.260 -17.748 1.00 14.97 ? 292 ALA A CB 1 ATOM 2091 N N . CYS A 1 267 ? -36.745 12.799 -20.549 1.00 14.32 ? 293 CYS A N 1 ATOM 2092 C CA A CYS A 1 267 ? -36.926 13.517 -21.817 0.62 18.69 ? 293 CYS A CA 1 ATOM 2093 C CA B CYS A 1 267 ? -36.957 13.471 -21.829 0.38 20.21 ? 293 CYS A CA 1 ATOM 2094 C C . CYS A 1 267 ? -38.377 13.987 -21.996 1.00 17.68 ? 293 CYS A C 1 ATOM 2095 O O . CYS A 1 267 ? -38.624 15.174 -22.260 1.00 19.71 ? 293 CYS A O 1 ATOM 2096 C CB A CYS A 1 267 ? -36.496 12.633 -23.002 0.62 21.78 ? 293 CYS A CB 1 ATOM 2097 C CB B CYS A 1 267 ? -36.643 12.507 -22.965 0.38 22.97 ? 293 CYS A CB 1 ATOM 2098 S SG A CYS A 1 267 ? -36.819 13.316 -24.666 0.62 24.46 ? 293 CYS A SG 1 ATOM 2099 S SG B CYS A 1 267 ? -34.909 12.196 -23.148 0.38 23.38 ? 293 CYS A SG 1 ATOM 2100 N N . LYS A 1 268 ? -39.329 13.075 -21.852 1.00 16.05 ? 294 LYS A N 1 ATOM 2101 C CA . LYS A 1 268 ? -40.738 13.436 -21.999 1.00 17.65 ? 294 LYS A CA 1 ATOM 2102 C C . LYS A 1 268 ? -41.164 14.532 -21.044 1.00 24.71 ? 294 LYS A C 1 ATOM 2103 O O . LYS A 1 268 ? -42.031 15.338 -21.386 1.00 26.81 ? 294 LYS A O 1 ATOM 2104 C CB . LYS A 1 268 ? -41.630 12.214 -21.807 1.00 28.36 ? 294 LYS A CB 1 ATOM 2105 C CG . LYS A 1 268 ? -41.414 11.166 -22.873 1.00 33.59 ? 294 LYS A CG 1 ATOM 2106 C CD . LYS A 1 268 ? -42.486 10.108 -22.820 1.00 36.06 ? 294 LYS A CD 1 ATOM 2107 C CE . LYS A 1 268 ? -43.843 10.707 -23.131 1.00 37.92 ? 294 LYS A CE 1 ATOM 2108 N NZ . LYS A 1 268 ? -44.884 9.651 -23.126 1.00 45.57 ? 294 LYS A NZ 1 ATOM 2109 N N . ALA A 1 269 ? -40.565 14.571 -19.854 1.00 19.06 ? 295 ALA A N 1 ATOM 2110 C CA . ALA A 1 269 ? -40.904 15.592 -18.863 1.00 26.58 ? 295 ALA A CA 1 ATOM 2111 C C . ALA A 1 269 ? -40.639 17.005 -19.390 1.00 23.49 ? 295 ALA A C 1 ATOM 2112 O O . ALA A 1 269 ? -41.242 17.945 -18.917 1.00 25.65 ? 295 ALA A O 1 ATOM 2113 C CB . ALA A 1 269 ? -40.137 15.361 -17.550 1.00 22.34 ? 295 ALA A CB 1 ATOM 2114 N N . GLN A 1 270 ? -39.758 17.144 -20.377 1.00 19.65 ? 296 GLN A N 1 ATOM 2115 C CA . GLN A 1 270 ? -39.421 18.465 -20.932 1.00 21.59 ? 296 GLN A CA 1 ATOM 2116 C C . GLN A 1 270 ? -40.341 18.904 -22.076 1.00 25.06 ? 296 GLN A C 1 ATOM 2117 O O . GLN A 1 270 ? -40.171 19.997 -22.630 1.00 28.98 ? 296 GLN A O 1 ATOM 2118 C CB . GLN A 1 270 ? -37.971 18.490 -21.433 1.00 18.71 ? 296 GLN A CB 1 ATOM 2119 C CG . GLN A 1 270 ? -36.977 17.834 -20.482 1.00 17.84 ? 296 GLN A CG 1 ATOM 2120 C CD . GLN A 1 270 ? -37.137 18.318 -19.058 1.00 19.18 ? 296 GLN A CD 1 ATOM 2121 O OE1 . GLN A 1 270 ? -37.347 19.511 -18.809 1.00 26.85 ? 296 GLN A OE1 1 ATOM 2122 N NE2 . GLN A 1 270 ? -37.054 17.386 -18.103 1.00 19.73 ? 296 GLN A NE2 1 ATOM 2123 N N . GLY A 1 271 ? -41.308 18.063 -22.431 1.00 22.57 ? 297 GLY A N 1 ATOM 2124 C CA . GLY A 1 271 ? -42.252 18.405 -23.485 1.00 22.30 ? 297 GLY A CA 1 ATOM 2125 C C . GLY A 1 271 ? -41.570 18.676 -24.819 1.00 23.76 ? 297 GLY A C 1 ATOM 2126 O O . GLY A 1 271 ? -40.649 17.952 -25.221 1.00 20.79 ? 297 GLY A O 1 ATOM 2127 N N . ALA A 1 272 ? -41.993 19.735 -25.502 1.00 23.00 ? 298 ALA A N 1 ATOM 2128 C CA . ALA A 1 272 ? -41.496 19.998 -26.855 1.00 28.98 ? 298 ALA A CA 1 ATOM 2129 C C . ALA A 1 272 ? -40.004 20.328 -26.887 1.00 31.53 ? 298 ALA A C 1 ATOM 2130 O O . ALA A 1 272 ? -39.372 20.261 -27.945 1.00 26.24 ? 298 ALA A O 1 ATOM 2131 C CB . ALA A 1 272 ? -42.287 21.121 -27.499 1.00 26.14 ? 298 ALA A CB 1 ATOM 2132 N N . ALA A 1 273 ? -39.436 20.669 -25.737 1.00 21.28 ? 299 ALA A N 1 ATOM 2133 C CA . ALA A 1 273 ? -38.028 21.060 -25.694 1.00 20.52 ? 299 ALA A CA 1 ATOM 2134 C C . ALA A 1 273 ? -37.072 19.868 -25.824 1.00 18.52 ? 299 ALA A C 1 ATOM 2135 O O . ALA A 1 273 ? -35.905 20.045 -26.171 1.00 21.07 ? 299 ALA A O 1 ATOM 2136 C CB . ALA A 1 273 ? -37.736 21.827 -24.421 1.00 21.25 ? 299 ALA A CB 1 ATOM 2137 N N . CYS A 1 274 ? -37.544 18.658 -25.550 1.00 17.66 ? 300 CYS A N 1 ATOM 2138 C CA . CYS A 1 274 ? -36.703 17.477 -25.787 1.00 15.98 ? 300 CYS A CA 1 ATOM 2139 C C . CYS A 1 274 ? -37.120 16.830 -27.097 1.00 16.22 ? 300 CYS A C 1 ATOM 2140 O O . CYS A 1 274 ? -38.236 16.317 -27.208 1.00 19.69 ? 300 CYS A O 1 ATOM 2141 C CB . CYS A 1 274 ? -36.802 16.466 -24.647 1.00 15.30 ? 300 CYS A CB 1 ATOM 2142 S SG . CYS A 1 274 ? -35.739 15.015 -24.932 1.00 25.57 ? 300 CYS A SG 1 ATOM 2143 N N . VAL A 1 275 ? -36.240 16.854 -28.094 1.00 15.37 ? 301 VAL A N 1 ATOM 2144 C CA . VAL A 1 275 ? -36.673 16.546 -29.455 1.00 15.78 ? 301 VAL A CA 1 ATOM 2145 C C . VAL A 1 275 ? -36.493 15.106 -29.880 1.00 14.70 ? 301 VAL A C 1 ATOM 2146 O O . VAL A 1 275 ? -37.060 14.685 -30.894 1.00 15.24 ? 301 VAL A O 1 ATOM 2147 C CB . VAL A 1 275 ? -35.948 17.423 -30.471 1.00 16.91 ? 301 VAL A CB 1 ATOM 2148 C CG1 . VAL A 1 275 ? -36.239 18.899 -30.171 1.00 17.89 ? 301 VAL A CG1 1 ATOM 2149 C CG2 . VAL A 1 275 ? -34.457 17.147 -30.433 1.00 15.34 ? 301 VAL A CG2 1 ATOM 2150 N N . GLY A 1 276 ? -35.702 14.343 -29.132 1.00 13.41 ? 302 GLY A N 1 ATOM 2151 C CA . GLY A 1 276 ? -35.437 12.978 -29.543 1.00 14.76 ? 302 GLY A CA 1 ATOM 2152 C C . GLY A 1 276 ? -34.389 12.240 -28.727 1.00 13.85 ? 302 GLY A C 1 ATOM 2153 O O . GLY A 1 276 ? -33.683 12.822 -27.910 1.00 12.38 ? 302 GLY A O 1 ATOM 2154 N N . ILE A 1 277 ? -34.308 10.938 -28.971 1.00 10.77 ? 303 ILE A N 1 ATOM 2155 C CA . ILE A 1 277 ? -33.383 10.056 -28.292 1.00 9.86 ? 303 ILE A CA 1 ATOM 2156 C C . ILE A 1 277 ? -32.670 9.220 -29.340 1.00 13.31 ? 303 ILE A C 1 ATOM 2157 O O . ILE A 1 277 ? -33.307 8.691 -30.248 1.00 14.24 ? 303 ILE A O 1 ATOM 2158 C CB . ILE A 1 277 ? -34.111 9.132 -27.298 1.00 13.57 ? 303 ILE A CB 1 ATOM 2159 C CG1 . ILE A 1 277 ? -34.804 9.954 -26.204 1.00 18.49 ? 303 ILE A CG1 1 ATOM 2160 C CG2 . ILE A 1 277 ? -33.133 8.121 -26.697 1.00 10.62 ? 303 ILE A CG2 1 ATOM 2161 C CD1 . ILE A 1 277 ? -35.847 9.144 -25.391 1.00 18.71 ? 303 ILE A CD1 1 ATOM 2162 N N . THR A 1 278 ? -31.346 9.128 -29.222 1.00 10.59 ? 304 THR A N 1 ATOM 2163 C CA . THR A 1 278 ? -30.518 8.321 -30.113 1.00 11.89 ? 304 THR A CA 1 ATOM 2164 C C . THR A 1 278 ? -29.752 7.312 -29.281 1.00 13.18 ? 304 THR A C 1 ATOM 2165 O O . THR A 1 278 ? -29.127 7.706 -28.293 1.00 10.91 ? 304 THR A O 1 ATOM 2166 C CB . THR A 1 278 ? -29.510 9.180 -30.903 1.00 9.28 ? 304 THR A CB 1 ATOM 2167 O OG1 . THR A 1 278 ? -30.221 9.993 -31.818 1.00 12.27 ? 304 THR A OG1 1 ATOM 2168 C CG2 . THR A 1 278 ? -28.493 8.301 -31.703 1.00 9.32 ? 304 THR A CG2 1 ATOM 2169 N N . THR A 1 279 ? -29.803 6.031 -29.658 1.00 8.66 ? 305 THR A N 1 ATOM 2170 C CA . THR A 1 279 ? -28.966 5.026 -28.989 1.00 10.18 ? 305 THR A CA 1 ATOM 2171 C C . THR A 1 279 ? -27.668 4.859 -29.779 1.00 9.37 ? 305 THR A C 1 ATOM 2172 O O . THR A 1 279 ? -27.661 4.978 -30.998 1.00 10.08 ? 305 THR A O 1 ATOM 2173 C CB . THR A 1 279 ? -29.687 3.643 -28.835 1.00 8.14 ? 305 THR A CB 1 ATOM 2174 O OG1 . THR A 1 279 ? -30.152 3.178 -30.103 1.00 13.17 ? 305 THR A OG1 1 ATOM 2175 C CG2 . THR A 1 279 ? -30.883 3.770 -27.913 1.00 11.73 ? 305 THR A CG2 1 ATOM 2176 N N . TRP A 1 280 ? -26.564 4.604 -29.084 1.00 8.63 ? 306 TRP A N 1 ATOM 2177 C CA . TRP A 1 280 ? -25.279 4.541 -29.776 1.00 10.34 ? 306 TRP A CA 1 ATOM 2178 C C . TRP A 1 280 ? -25.062 3.169 -30.411 1.00 17.30 ? 306 TRP A C 1 ATOM 2179 O O . TRP A 1 280 ? -24.201 2.380 -29.988 1.00 9.13 ? 306 TRP A O 1 ATOM 2180 C CB . TRP A 1 280 ? -24.133 4.906 -28.830 1.00 8.78 ? 306 TRP A CB 1 ATOM 2181 C CG . TRP A 1 280 ? -22.970 5.416 -29.624 1.00 9.52 ? 306 TRP A CG 1 ATOM 2182 C CD1 . TRP A 1 280 ? -21.745 4.843 -29.732 1.00 17.48 ? 306 TRP A CD1 1 ATOM 2183 C CD2 . TRP A 1 280 ? -22.955 6.568 -30.486 1.00 11.85 ? 306 TRP A CD2 1 ATOM 2184 N NE1 . TRP A 1 280 ? -20.952 5.575 -30.590 1.00 18.02 ? 306 TRP A NE1 1 ATOM 2185 C CE2 . TRP A 1 280 ? -21.674 6.639 -31.065 1.00 12.44 ? 306 TRP A CE2 1 ATOM 2186 C CE3 . TRP A 1 280 ? -23.898 7.543 -30.819 1.00 12.92 ? 306 TRP A CE3 1 ATOM 2187 C CZ2 . TRP A 1 280 ? -21.308 7.656 -31.956 1.00 17.22 ? 306 TRP A CZ2 1 ATOM 2188 C CZ3 . TRP A 1 280 ? -23.536 8.548 -31.702 1.00 15.88 ? 306 TRP A CZ3 1 ATOM 2189 C CH2 . TRP A 1 280 ? -22.252 8.595 -32.258 1.00 16.27 ? 306 TRP A CH2 1 ATOM 2190 N N . GLY A 1 281 ? -25.861 2.905 -31.442 1.00 11.43 ? 307 GLY A N 1 ATOM 2191 C CA . GLY A 1 281 ? -25.833 1.644 -32.160 1.00 14.24 ? 307 GLY A CA 1 ATOM 2192 C C . GLY A 1 281 ? -27.226 1.054 -32.229 1.00 18.31 ? 307 GLY A C 1 ATOM 2193 O O . GLY A 1 281 ? -28.185 1.610 -31.677 1.00 14.77 ? 307 GLY A O 1 ATOM 2194 N N . ILE A 1 282 ? -27.353 -0.066 -32.926 1.00 12.59 ? 308 ILE A N 1 ATOM 2195 C CA . ILE A 1 282 ? -28.632 -0.745 -33.004 1.00 10.66 ? 308 ILE A CA 1 ATOM 2196 C C . ILE A 1 282 ? -28.554 -2.024 -32.183 1.00 11.19 ? 308 ILE A C 1 ATOM 2197 O O . ILE A 1 282 ? -29.280 -2.168 -31.197 1.00 13.13 ? 308 ILE A O 1 ATOM 2198 C CB . ILE A 1 282 ? -29.026 -1.036 -34.467 1.00 11.72 ? 308 ILE A CB 1 ATOM 2199 C CG1 . ILE A 1 282 ? -29.349 0.300 -35.186 1.00 11.75 ? 308 ILE A CG1 1 ATOM 2200 C CG2 . ILE A 1 282 ? -30.213 -2.009 -34.523 1.00 16.05 ? 308 ILE A CG2 1 ATOM 2201 C CD1 . ILE A 1 282 ? -29.651 0.170 -36.661 1.00 13.06 ? 308 ILE A CD1 1 ATOM 2202 N N . THR A 1 283 ? -27.634 -2.920 -32.555 1.00 12.46 ? 309 THR A N 1 ATOM 2203 C CA . THR A 1 283 ? -27.462 -4.206 -31.868 1.00 11.97 ? 309 THR A CA 1 ATOM 2204 C C . THR A 1 283 ? -26.196 -4.267 -31.014 1.00 11.74 ? 309 THR A C 1 ATOM 2205 O O . THR A 1 283 ? -25.166 -3.687 -31.386 1.00 14.92 ? 309 THR A O 1 ATOM 2206 C CB . THR A 1 283 ? -27.401 -5.378 -32.883 1.00 13.28 ? 309 THR A CB 1 ATOM 2207 O OG1 . THR A 1 283 ? -26.914 -6.556 -32.225 1.00 18.46 ? 309 THR A OG1 1 ATOM 2208 C CG2 . THR A 1 283 ? -26.436 -5.037 -34.022 1.00 13.69 ? 309 THR A CG2 1 ATOM 2209 N N . ASP A 1 284 ? -26.269 -5.003 -29.896 1.00 11.98 ? 310 ASP A N 1 ATOM 2210 C CA . ASP A 1 284 ? -25.105 -5.310 -29.053 1.00 12.24 ? 310 ASP A CA 1 ATOM 2211 C C . ASP A 1 284 ? -23.911 -5.865 -29.845 1.00 13.10 ? 310 ASP A C 1 ATOM 2212 O O . ASP A 1 284 ? -22.752 -5.698 -29.452 1.00 13.48 ? 310 ASP A O 1 ATOM 2213 C CB . ASP A 1 284 ? -25.463 -6.336 -27.960 1.00 12.94 ? 310 ASP A CB 1 ATOM 2214 C CG . ASP A 1 284 ? -26.581 -5.870 -27.020 1.00 23.15 ? 310 ASP A CG 1 ATOM 2215 O OD1 . ASP A 1 284 ? -26.735 -4.649 -26.766 1.00 13.59 ? 310 ASP A OD1 1 ATOM 2216 O OD2 . ASP A 1 284 ? -27.311 -6.760 -26.513 1.00 20.15 ? 310 ASP A OD2 1 ATOM 2217 N N . LEU A 1 285 ? -24.196 -6.541 -30.943 1.00 13.82 ? 311 LEU A N 1 ATOM 2218 C CA . LEU A 1 285 ? -23.158 -7.236 -31.700 1.00 15.63 ? 311 LEU A CA 1 ATOM 2219 C C . LEU A 1 285 ? -22.026 -6.312 -32.177 1.00 19.17 ? 311 LEU A C 1 ATOM 2220 O O . LEU A 1 285 ? -20.885 -6.753 -32.320 1.00 16.84 ? 311 LEU A O 1 ATOM 2221 C CB . LEU A 1 285 ? -23.783 -7.943 -32.899 1.00 15.91 ? 311 LEU A CB 1 ATOM 2222 C CG . LEU A 1 285 ? -22.917 -8.953 -33.657 1.00 20.77 ? 311 LEU A CG 1 ATOM 2223 C CD1 . LEU A 1 285 ? -22.589 -10.155 -32.770 1.00 18.49 ? 311 LEU A CD1 1 ATOM 2224 C CD2 . LEU A 1 285 ? -23.602 -9.396 -34.956 1.00 19.58 ? 311 LEU A CD2 1 ATOM 2225 N N . TYR A 1 286 ? -22.347 -5.046 -32.430 1.00 13.86 ? 312 TYR A N 1 ATOM 2226 C CA . TYR A 1 286 ? -21.353 -4.089 -32.918 1.00 13.97 ? 312 TYR A CA 1 ATOM 2227 C C . TYR A 1 286 ? -21.101 -2.942 -31.947 1.00 19.12 ? 312 TYR A C 1 ATOM 2228 O O . TYR A 1 286 ? -20.431 -1.986 -32.295 1.00 19.78 ? 312 TYR A O 1 ATOM 2229 C CB . TYR A 1 286 ? -21.785 -3.498 -34.272 1.00 14.13 ? 312 TYR A CB 1 ATOM 2230 C CG . TYR A 1 286 ? -22.126 -4.562 -35.277 1.00 17.98 ? 312 TYR A CG 1 ATOM 2231 C CD1 . TYR A 1 286 ? -21.194 -5.529 -35.626 1.00 16.63 ? 312 TYR A CD1 1 ATOM 2232 C CD2 . TYR A 1 286 ? -23.381 -4.609 -35.868 1.00 15.19 ? 312 TYR A CD2 1 ATOM 2233 C CE1 . TYR A 1 286 ? -21.502 -6.516 -36.536 1.00 18.20 ? 312 TYR A CE1 1 ATOM 2234 C CE2 . TYR A 1 286 ? -23.698 -5.590 -36.778 1.00 20.13 ? 312 TYR A CE2 1 ATOM 2235 C CZ . TYR A 1 286 ? -22.758 -6.544 -37.109 1.00 25.94 ? 312 TYR A CZ 1 ATOM 2236 O OH . TYR A 1 286 ? -23.070 -7.531 -38.025 1.00 28.15 ? 312 TYR A OH 1 ATOM 2237 N N . SER A 1 287 ? -21.646 -3.030 -30.740 1.00 16.24 ? 313 SER A N 1 ATOM 2238 C CA . SER A 1 287 ? -21.456 -1.972 -29.754 1.00 11.72 ? 313 SER A CA 1 ATOM 2239 C C . SER A 1 287 ? -19.977 -1.702 -29.479 1.00 20.39 ? 313 SER A C 1 ATOM 2240 O O . SER A 1 287 ? -19.182 -2.615 -29.440 1.00 13.56 ? 313 SER A O 1 ATOM 2241 C CB . SER A 1 287 ? -22.148 -2.343 -28.444 1.00 11.34 ? 313 SER A CB 1 ATOM 2242 O OG . SER A 1 287 ? -21.988 -1.320 -27.480 1.00 14.02 ? 313 SER A OG 1 ATOM 2243 N N . TRP A 1 288 ? -19.616 -0.446 -29.261 1.00 15.35 ? 314 TRP A N 1 ATOM 2244 C CA . TRP A 1 288 ? -18.252 -0.115 -28.875 1.00 15.86 ? 314 TRP A CA 1 ATOM 2245 C C . TRP A 1 288 ? -17.886 -0.630 -27.467 1.00 17.93 ? 314 TRP A C 1 ATOM 2246 O O . TRP A 1 288 ? -16.709 -0.748 -27.135 1.00 19.30 ? 314 TRP A O 1 ATOM 2247 C CB . TRP A 1 288 ? -18.058 1.411 -28.934 1.00 20.60 ? 314 TRP A CB 1 ATOM 2248 C CG . TRP A 1 288 ? -18.859 2.164 -27.887 1.00 18.58 ? 314 TRP A CG 1 ATOM 2249 C CD1 . TRP A 1 288 ? -20.231 2.234 -27.771 1.00 13.27 ? 314 TRP A CD1 1 ATOM 2250 C CD2 . TRP A 1 288 ? -18.330 2.948 -26.814 1.00 24.67 ? 314 TRP A CD2 1 ATOM 2251 N NE1 . TRP A 1 288 ? -20.576 3.009 -26.674 1.00 11.27 ? 314 TRP A NE1 1 ATOM 2252 C CE2 . TRP A 1 288 ? -19.425 3.468 -26.085 1.00 22.36 ? 314 TRP A CE2 1 ATOM 2253 C CE3 . TRP A 1 288 ? -17.030 3.271 -26.401 1.00 41.04 ? 314 TRP A CE3 1 ATOM 2254 C CZ2 . TRP A 1 288 ? -19.257 4.282 -24.962 1.00 34.41 ? 314 TRP A CZ2 1 ATOM 2255 C CZ3 . TRP A 1 288 ? -16.866 4.081 -25.286 1.00 49.14 ? 314 TRP A CZ3 1 ATOM 2256 C CH2 . TRP A 1 288 ? -17.975 4.576 -24.580 1.00 47.10 ? 314 TRP A CH2 1 ATOM 2257 N N . ILE A 1 289 ? -18.878 -0.965 -26.643 1.00 13.27 ? 315 ILE A N 1 ATOM 2258 C CA A ILE A 1 289 ? -18.602 -1.226 -25.227 0.47 14.42 ? 315 ILE A CA 1 ATOM 2259 C CA B ILE A 1 289 ? -18.621 -1.232 -25.221 0.53 14.49 ? 315 ILE A CA 1 ATOM 2260 C C . ILE A 1 289 ? -17.724 -2.453 -24.940 1.00 19.26 ? 315 ILE A C 1 ATOM 2261 O O . ILE A 1 289 ? -16.753 -2.350 -24.175 1.00 24.66 ? 315 ILE A O 1 ATOM 2262 C CB A ILE A 1 289 ? -19.912 -1.350 -24.435 0.47 14.83 ? 315 ILE A CB 1 ATOM 2263 C CB B ILE A 1 289 ? -19.943 -1.409 -24.436 0.53 14.54 ? 315 ILE A CB 1 ATOM 2264 C CG1 A ILE A 1 289 ? -20.439 0.046 -24.106 0.47 16.50 ? 315 ILE A CG1 1 ATOM 2265 C CG1 B ILE A 1 289 ? -20.801 -0.135 -24.498 0.53 12.91 ? 315 ILE A CG1 1 ATOM 2266 C CG2 A ILE A 1 289 ? -19.701 -2.140 -23.154 0.47 13.80 ? 315 ILE A CG2 1 ATOM 2267 C CG2 B ILE A 1 289 ? -19.653 -1.791 -22.995 0.53 14.46 ? 315 ILE A CG2 1 ATOM 2268 C CD1 A ILE A 1 289 ? -21.884 0.212 -24.393 0.47 10.88 ? 315 ILE A CD1 1 ATOM 2269 C CD1 B ILE A 1 289 ? -20.161 1.078 -23.844 0.53 11.99 ? 315 ILE A CD1 1 ATOM 2270 N N . PRO A 1 290 ? -18.032 -3.621 -25.547 1.00 15.24 ? 316 PRO A N 1 ATOM 2271 C CA . PRO A 1 290 ? -17.193 -4.747 -25.108 1.00 26.69 ? 316 PRO A CA 1 ATOM 2272 C C . PRO A 1 290 ? -15.739 -4.672 -25.550 1.00 32.71 ? 316 PRO A C 1 ATOM 2273 O O . PRO A 1 290 ? -14.920 -5.432 -25.035 1.00 34.61 ? 316 PRO A O 1 ATOM 2274 C CB . PRO A 1 290 ? -17.878 -5.973 -25.732 1.00 25.34 ? 316 PRO A CB 1 ATOM 2275 C CG . PRO A 1 290 ? -18.703 -5.444 -26.835 1.00 17.76 ? 316 PRO A CG 1 ATOM 2276 C CD . PRO A 1 290 ? -19.145 -4.074 -26.402 1.00 14.96 ? 316 PRO A CD 1 ATOM 2277 N N . SER A 1 291 ? -15.415 -3.769 -26.464 1.00 25.27 ? 317 SER A N 1 ATOM 2278 C CA . SER A 1 291 ? -14.032 -3.633 -26.894 1.00 33.84 ? 317 SER A CA 1 ATOM 2279 C C . SER A 1 291 ? -13.338 -2.539 -26.087 1.00 38.14 ? 317 SER A C 1 ATOM 2280 O O . SER A 1 291 ? -12.113 -2.476 -26.031 1.00 42.00 ? 317 SER A O 1 ATOM 2281 C CB . SER A 1 291 ? -13.959 -3.320 -28.382 1.00 32.60 ? 317 SER A CB 1 ATOM 2282 O OG . SER A 1 291 ? -14.179 -1.940 -28.597 1.00 44.37 ? 317 SER A OG 1 ATOM 2283 N N . THR A 1 292 ? -14.133 -1.680 -25.457 1.00 32.68 ? 318 THR A N 1 ATOM 2284 C CA . THR A 1 292 ? -13.598 -0.600 -24.643 1.00 37.80 ? 318 THR A CA 1 ATOM 2285 C C . THR A 1 292 ? -13.582 -0.997 -23.157 1.00 38.20 ? 318 THR A C 1 ATOM 2286 O O . THR A 1 292 ? -12.613 -0.726 -22.445 1.00 42.52 ? 318 THR A O 1 ATOM 2287 C CB . THR A 1 292 ? -14.408 0.695 -24.859 1.00 37.86 ? 318 THR A CB 1 ATOM 2288 O OG1 . THR A 1 292 ? -14.368 1.047 -26.249 1.00 45.20 ? 318 THR A OG1 1 ATOM 2289 C CG2 . THR A 1 292 ? -13.841 1.838 -24.044 1.00 27.51 ? 318 THR A CG2 1 ATOM 2290 N N . TYR A 1 293 ? -14.642 -1.664 -22.708 1.00 23.87 ? 319 TYR A N 1 ATOM 2291 C CA . TYR A 1 293 ? -14.718 -2.190 -21.342 1.00 24.29 ? 319 TYR A CA 1 ATOM 2292 C C . TYR A 1 293 ? -14.871 -3.695 -21.372 1.00 26.01 ? 319 TYR A C 1 ATOM 2293 O O . TYR A 1 293 ? -15.992 -4.197 -21.438 1.00 32.03 ? 319 TYR A O 1 ATOM 2294 C CB . TYR A 1 293 ? -15.895 -1.590 -20.573 1.00 27.37 ? 319 TYR A CB 1 ATOM 2295 C CG . TYR A 1 293 ? -15.962 -0.082 -20.585 1.00 34.68 ? 319 TYR A CG 1 ATOM 2296 C CD1 . TYR A 1 293 ? -15.138 0.675 -19.763 1.00 40.69 ? 319 TYR A CD1 1 ATOM 2297 C CD2 . TYR A 1 293 ? -16.861 0.582 -21.402 1.00 32.22 ? 319 TYR A CD2 1 ATOM 2298 C CE1 . TYR A 1 293 ? -15.202 2.055 -19.765 1.00 43.75 ? 319 TYR A CE1 1 ATOM 2299 C CE2 . TYR A 1 293 ? -16.933 1.962 -21.412 1.00 35.07 ? 319 TYR A CE2 1 ATOM 2300 C CZ . TYR A 1 293 ? -16.100 2.693 -20.592 1.00 38.95 ? 319 TYR A CZ 1 ATOM 2301 O OH . TYR A 1 293 ? -16.164 4.067 -20.597 1.00 48.36 ? 319 TYR A OH 1 ATOM 2302 N N . PRO A 1 294 ? -13.752 -4.422 -21.321 1.00 34.23 ? 320 PRO A N 1 ATOM 2303 C CA . PRO A 1 294 ? -13.801 -5.886 -21.397 1.00 34.66 ? 320 PRO A CA 1 ATOM 2304 C C . PRO A 1 294 ? -14.708 -6.483 -20.314 1.00 31.20 ? 320 PRO A C 1 ATOM 2305 O O . PRO A 1 294 ? -14.665 -6.054 -19.163 1.00 32.02 ? 320 PRO A O 1 ATOM 2306 C CB . PRO A 1 294 ? -12.332 -6.300 -21.193 1.00 38.45 ? 320 PRO A CB 1 ATOM 2307 C CG . PRO A 1 294 ? -11.689 -5.128 -20.519 1.00 41.45 ? 320 PRO A CG 1 ATOM 2308 C CD . PRO A 1 294 ? -12.391 -3.920 -21.072 1.00 42.42 ? 320 PRO A CD 1 ATOM 2309 N N . GLY A 1 295 ? -15.539 -7.448 -20.692 1.00 26.54 ? 321 GLY A N 1 ATOM 2310 C CA . GLY A 1 295 ? -16.439 -8.078 -19.745 1.00 26.29 ? 321 GLY A CA 1 ATOM 2311 C C . GLY A 1 295 ? -17.739 -7.317 -19.520 1.00 25.96 ? 321 GLY A C 1 ATOM 2312 O O . GLY A 1 295 ? -18.543 -7.710 -18.674 1.00 27.80 ? 321 GLY A O 1 ATOM 2313 N N . GLU A 1 296 ? -17.943 -6.233 -20.270 1.00 19.67 ? 322 GLU A N 1 ATOM 2314 C CA . GLU A 1 296 ? -19.190 -5.466 -20.213 1.00 22.94 ? 322 GLU A CA 1 ATOM 2315 C C . GLU A 1 296 ? -19.866 -5.415 -21.583 1.00 25.19 ? 322 GLU A C 1 ATOM 2316 O O . GLU A 1 296 ? -19.208 -5.533 -22.603 1.00 17.20 ? 322 GLU A O 1 ATOM 2317 C CB . GLU A 1 296 ? -18.929 -4.047 -19.717 1.00 17.61 ? 322 GLU A CB 1 ATOM 2318 C CG . GLU A 1 296 ? -18.378 -3.967 -18.299 1.00 24.20 ? 322 GLU A CG 1 ATOM 2319 C CD . GLU A 1 296 ? -18.149 -2.537 -17.841 1.00 29.33 ? 322 GLU A CD 1 ATOM 2320 O OE1 . GLU A 1 296 ? -18.749 -1.625 -18.443 1.00 31.69 ? 322 GLU A OE1 1 ATOM 2321 O OE2 . GLU A 1 296 ? -17.368 -2.318 -16.884 1.00 34.08 ? 322 GLU A OE2 1 ATOM 2322 N N . GLY A 1 297 ? -21.182 -5.260 -21.605 1.00 15.54 ? 323 GLY A N 1 ATOM 2323 C CA . GLY A 1 297 ? -21.913 -5.225 -22.860 1.00 14.43 ? 323 GLY A CA 1 ATOM 2324 C C . GLY A 1 297 ? -23.410 -5.239 -22.608 1.00 16.71 ? 323 GLY A C 1 ATOM 2325 O O . GLY A 1 297 ? -23.888 -4.702 -21.592 1.00 15.38 ? 323 GLY A O 1 ATOM 2326 N N . TYR A 1 298 ? -24.134 -5.864 -23.531 1.00 13.72 ? 324 TYR A N 1 ATOM 2327 C CA . TYR A 1 298 ? -25.581 -6.001 -23.470 1.00 19.66 ? 324 TYR A CA 1 ATOM 2328 C C . TYR A 1 298 ? -26.232 -4.638 -23.239 1.00 13.69 ? 324 TYR A C 1 ATOM 2329 O O . TYR A 1 298 ? -27.177 -4.518 -22.472 1.00 13.80 ? 324 TYR A O 1 ATOM 2330 C CB . TYR A 1 298 ? -25.979 -6.998 -22.372 1.00 16.54 ? 324 TYR A CB 1 ATOM 2331 C CG . TYR A 1 298 ? -27.322 -7.663 -22.627 1.00 17.20 ? 324 TYR A CG 1 ATOM 2332 C CD1 . TYR A 1 298 ? -27.469 -8.628 -23.629 1.00 21.45 ? 324 TYR A CD1 1 ATOM 2333 C CD2 . TYR A 1 298 ? -28.434 -7.325 -21.876 1.00 18.24 ? 324 TYR A CD2 1 ATOM 2334 C CE1 . TYR A 1 298 ? -28.691 -9.229 -23.867 1.00 27.24 ? 324 TYR A CE1 1 ATOM 2335 C CE2 . TYR A 1 298 ? -29.667 -7.921 -22.107 1.00 31.45 ? 324 TYR A CE2 1 ATOM 2336 C CZ . TYR A 1 298 ? -29.788 -8.868 -23.105 1.00 38.95 ? 324 TYR A CZ 1 ATOM 2337 O OH . TYR A 1 298 ? -31.013 -9.455 -23.332 1.00 52.71 ? 324 TYR A OH 1 ATOM 2338 N N . ALA A 1 299 ? -25.715 -3.603 -23.901 1.00 11.50 ? 325 ALA A N 1 ATOM 2339 C CA . ALA A 1 299 ? -26.067 -2.231 -23.507 1.00 10.73 ? 325 ALA A CA 1 ATOM 2340 C C . ALA A 1 299 ? -27.151 -1.572 -24.378 1.00 10.97 ? 325 ALA A C 1 ATOM 2341 O O . ALA A 1 299 ? -27.695 -0.533 -24.000 1.00 11.94 ? 325 ALA A O 1 ATOM 2342 C CB . ALA A 1 299 ? -24.814 -1.362 -23.504 1.00 10.54 ? 325 ALA A CB 1 ATOM 2343 N N . LEU A 1 300 ? -27.457 -2.169 -25.531 1.00 13.18 ? 326 LEU A N 1 ATOM 2344 C CA . LEU A 1 300 ? -28.367 -1.553 -26.502 1.00 9.58 ? 326 LEU A CA 1 ATOM 2345 C C . LEU A 1 300 ? -29.773 -2.167 -26.412 1.00 12.66 ? 326 LEU A C 1 ATOM 2346 O O . LEU A 1 300 ? -30.076 -2.885 -25.469 1.00 18.26 ? 326 LEU A O 1 ATOM 2347 C CB . LEU A 1 300 ? -27.789 -1.684 -27.906 1.00 9.58 ? 326 LEU A CB 1 ATOM 2348 C CG . LEU A 1 300 ? -26.562 -0.780 -28.135 1.00 11.04 ? 326 LEU A CG 1 ATOM 2349 C CD1 . LEU A 1 300 ? -25.839 -1.093 -29.462 1.00 9.61 ? 326 LEU A CD1 1 ATOM 2350 C CD2 . LEU A 1 300 ? -26.978 0.693 -28.097 1.00 12.83 ? 326 LEU A CD2 1 ATOM 2351 N N . LEU A 1 301 ? -30.636 -1.894 -27.380 1.00 12.38 ? 327 LEU A N 1 ATOM 2352 C CA . LEU A 1 301 ? -32.012 -2.368 -27.252 1.00 11.93 ? 327 LEU A CA 1 ATOM 2353 C C . LEU A 1 301 ? -32.271 -3.689 -27.971 1.00 15.64 ? 327 LEU A C 1 ATOM 2354 O O . LEU A 1 301 ? -33.326 -4.302 -27.781 1.00 13.93 ? 327 LEU A O 1 ATOM 2355 C CB . LEU A 1 301 ? -32.978 -1.300 -27.763 1.00 10.84 ? 327 LEU A CB 1 ATOM 2356 C CG . LEU A 1 301 ? -33.080 -0.090 -26.832 1.00 10.27 ? 327 LEU A CG 1 ATOM 2357 C CD1 . LEU A 1 301 ? -34.034 0.922 -27.438 1.00 21.60 ? 327 LEU A CD1 1 ATOM 2358 C CD2 . LEU A 1 301 ? -33.585 -0.543 -25.435 1.00 10.91 ? 327 LEU A CD2 1 ATOM 2359 N N . PHE A 1 302 ? -31.314 -4.119 -28.789 1.00 13.52 ? 328 PHE A N 1 ATOM 2360 C CA . PHE A 1 302 ? -31.423 -5.375 -29.542 1.00 13.87 ? 328 PHE A CA 1 ATOM 2361 C C . PHE A 1 302 ? -30.186 -6.209 -29.309 1.00 18.48 ? 328 PHE A C 1 ATOM 2362 O O . PHE A 1 302 ? -29.081 -5.671 -29.316 1.00 13.12 ? 328 PHE A O 1 ATOM 2363 C CB . PHE A 1 302 ? -31.596 -5.105 -31.045 1.00 13.38 ? 328 PHE A CB 1 ATOM 2364 C CG . PHE A 1 302 ? -32.826 -4.297 -31.376 1.00 20.39 ? 328 PHE A CG 1 ATOM 2365 C CD1 . PHE A 1 302 ? -32.782 -2.907 -31.383 1.00 12.48 ? 328 PHE A CD1 1 ATOM 2366 C CD2 . PHE A 1 302 ? -34.033 -4.928 -31.646 1.00 20.19 ? 328 PHE A CD2 1 ATOM 2367 C CE1 . PHE A 1 302 ? -33.918 -2.162 -31.672 1.00 19.72 ? 328 PHE A CE1 1 ATOM 2368 C CE2 . PHE A 1 302 ? -35.172 -4.191 -31.942 1.00 19.22 ? 328 PHE A CE2 1 ATOM 2369 C CZ . PHE A 1 302 ? -35.118 -2.809 -31.950 1.00 17.53 ? 328 PHE A CZ 1 ATOM 2370 N N . ASP A 1 303 ? -30.336 -7.519 -29.120 1.00 15.85 ? 329 ASP A N 1 ATOM 2371 C CA . ASP A 1 303 ? -29.148 -8.304 -28.796 1.00 15.04 ? 329 ASP A CA 1 ATOM 2372 C C . ASP A 1 303 ? -28.387 -8.755 -30.035 1.00 15.54 ? 329 ASP A C 1 ATOM 2373 O O . ASP A 1 303 ? -28.657 -8.298 -31.145 1.00 21.64 ? 329 ASP A O 1 ATOM 2374 C CB . ASP A 1 303 ? -29.500 -9.515 -27.914 1.00 20.25 ? 329 ASP A CB 1 ATOM 2375 C CG . ASP A 1 303 ? -30.433 -10.505 -28.590 1.00 31.33 ? 329 ASP A CG 1 ATOM 2376 O OD1 . ASP A 1 303 ? -30.489 -10.565 -29.842 1.00 30.57 ? 329 ASP A OD1 1 ATOM 2377 O OD2 . ASP A 1 303 ? -31.115 -11.250 -27.847 1.00 26.34 ? 329 ASP A OD2 1 ATOM 2378 N N . ASP A 1 304 ? -27.430 -9.654 -29.825 1.00 17.49 ? 330 ASP A N 1 ATOM 2379 C CA . ASP A 1 304 ? -26.587 -10.170 -30.898 1.00 21.94 ? 330 ASP A CA 1 ATOM 2380 C C . ASP A 1 304 ? -27.376 -10.847 -32.022 1.00 23.24 ? 330 ASP A C 1 ATOM 2381 O O . ASP A 1 304 ? -26.869 -10.999 -33.131 1.00 21.20 ? 330 ASP A O 1 ATOM 2382 C CB . ASP A 1 304 ? -25.562 -11.169 -30.351 1.00 22.90 ? 330 ASP A CB 1 ATOM 2383 C CG . ASP A 1 304 ? -24.458 -10.510 -29.536 1.00 28.76 ? 330 ASP A CG 1 ATOM 2384 O OD1 . ASP A 1 304 ? -24.375 -9.261 -29.505 1.00 26.65 ? 330 ASP A OD1 1 ATOM 2385 O OD2 . ASP A 1 304 ? -23.660 -11.262 -28.923 1.00 29.66 ? 330 ASP A OD2 1 ATOM 2386 N N . ASN A 1 305 ? -28.605 -11.264 -31.741 1.00 19.49 ? 331 ASN A N 1 ATOM 2387 C CA . ASN A 1 305 ? -29.449 -11.876 -32.772 1.00 20.41 ? 331 ASN A CA 1 ATOM 2388 C C . ASN A 1 305 ? -30.572 -10.955 -33.232 1.00 21.00 ? 331 ASN A C 1 ATOM 2389 O O . ASN A 1 305 ? -31.512 -11.402 -33.889 1.00 21.24 ? 331 ASN A O 1 ATOM 2390 C CB . ASN A 1 305 ? -30.054 -13.188 -32.263 1.00 30.55 ? 331 ASN A CB 1 ATOM 2391 C CG . ASN A 1 305 ? -29.011 -14.128 -31.683 1.00 32.02 ? 331 ASN A CG 1 ATOM 2392 O OD1 . ASN A 1 305 ? -29.058 -14.477 -30.497 1.00 37.25 ? 331 ASN A OD1 1 ATOM 2393 N ND2 . ASN A 1 305 ? -28.058 -14.533 -32.509 1.00 26.81 ? 331 ASN A ND2 1 ATOM 2394 N N . TYR A 1 306 ? -30.474 -9.678 -32.863 1.00 18.12 ? 332 TYR A N 1 ATOM 2395 C CA . TYR A 1 306 ? -31.497 -8.673 -33.173 1.00 19.62 ? 332 TYR A CA 1 ATOM 2396 C C . TYR A 1 306 ? -32.840 -8.973 -32.488 1.00 22.31 ? 332 TYR A C 1 ATOM 2397 O O . TYR A 1 306 ? -33.883 -8.459 -32.880 1.00 18.81 ? 332 TYR A O 1 ATOM 2398 C CB . TYR A 1 306 ? -31.670 -8.541 -34.693 1.00 18.44 ? 332 TYR A CB 1 ATOM 2399 C CG . TYR A 1 306 ? -30.450 -7.937 -35.361 1.00 18.72 ? 332 TYR A CG 1 ATOM 2400 C CD1 . TYR A 1 306 ? -30.312 -6.557 -35.455 1.00 18.36 ? 332 TYR A CD1 1 ATOM 2401 C CD2 . TYR A 1 306 ? -29.426 -8.741 -35.868 1.00 19.66 ? 332 TYR A CD2 1 ATOM 2402 C CE1 . TYR A 1 306 ? -29.203 -5.979 -36.056 1.00 18.12 ? 332 TYR A CE1 1 ATOM 2403 C CE2 . TYR A 1 306 ? -28.297 -8.169 -36.478 1.00 18.65 ? 332 TYR A CE2 1 ATOM 2404 C CZ . TYR A 1 306 ? -28.206 -6.786 -36.563 1.00 16.94 ? 332 TYR A CZ 1 ATOM 2405 O OH . TYR A 1 306 ? -27.124 -6.188 -37.142 1.00 16.99 ? 332 TYR A OH 1 ATOM 2406 N N . VAL A 1 307 ? -32.802 -9.787 -31.441 1.00 23.86 ? 333 VAL A N 1 ATOM 2407 C CA . VAL A 1 307 ? -33.973 -9.979 -30.592 1.00 19.67 ? 333 VAL A CA 1 ATOM 2408 C C . VAL A 1 307 ? -34.008 -8.863 -29.549 1.00 18.14 ? 333 VAL A C 1 ATOM 2409 O O . VAL A 1 307 ? -33.013 -8.619 -28.869 1.00 17.09 ? 333 VAL A O 1 ATOM 2410 C CB . VAL A 1 307 ? -33.950 -11.354 -29.902 1.00 23.76 ? 333 VAL A CB 1 ATOM 2411 C CG1 . VAL A 1 307 ? -35.089 -11.471 -28.882 1.00 22.21 ? 333 VAL A CG1 1 ATOM 2412 C CG2 . VAL A 1 307 ? -34.040 -12.460 -30.944 1.00 23.11 ? 333 VAL A CG2 1 ATOM 2413 N N . PRO A 1 308 ? -35.143 -8.162 -29.432 1.00 18.23 ? 334 PRO A N 1 ATOM 2414 C CA . PRO A 1 308 ? -35.186 -7.019 -28.512 1.00 16.92 ? 334 PRO A CA 1 ATOM 2415 C C . PRO A 1 308 ? -34.934 -7.416 -27.052 1.00 21.49 ? 334 PRO A C 1 ATOM 2416 O O . PRO A 1 308 ? -35.393 -8.475 -26.629 1.00 23.98 ? 334 PRO A O 1 ATOM 2417 C CB . PRO A 1 308 ? -36.611 -6.469 -28.692 1.00 20.12 ? 334 PRO A CB 1 ATOM 2418 C CG . PRO A 1 308 ? -37.099 -7.026 -29.994 1.00 27.65 ? 334 PRO A CG 1 ATOM 2419 C CD . PRO A 1 308 ? -36.411 -8.350 -30.161 1.00 19.74 ? 334 PRO A CD 1 ATOM 2420 N N . HIS A 1 309 ? -34.175 -6.597 -26.320 1.00 15.95 ? 335 HIS A N 1 ATOM 2421 C CA . HIS A 1 309 ? -34.070 -6.698 -24.857 1.00 16.05 ? 335 HIS A CA 1 ATOM 2422 C C . HIS A 1 309 ? -35.433 -6.441 -24.234 1.00 17.01 ? 335 HIS A C 1 ATOM 2423 O O . HIS A 1 309 ? -36.264 -5.789 -24.851 1.00 20.06 ? 335 HIS A O 1 ATOM 2424 C CB . HIS A 1 309 ? -33.080 -5.657 -24.282 1.00 14.57 ? 335 HIS A CB 1 ATOM 2425 C CG . HIS A 1 309 ? -31.651 -5.862 -24.672 1.00 21.06 ? 335 HIS A CG 1 ATOM 2426 N ND1 . HIS A 1 309 ? -30.604 -5.337 -23.939 1.00 20.67 ? 335 HIS A ND1 1 ATOM 2427 C CD2 . HIS A 1 309 ? -31.088 -6.496 -25.731 1.00 24.34 ? 335 HIS A CD2 1 ATOM 2428 C CE1 . HIS A 1 309 ? -29.459 -5.652 -24.523 1.00 20.56 ? 335 HIS A CE1 1 ATOM 2429 N NE2 . HIS A 1 309 ? -29.724 -6.355 -25.611 1.00 18.75 ? 335 HIS A NE2 1 ATOM 2430 N N . PRO A 1 310 ? -35.656 -6.907 -22.993 1.00 26.11 ? 336 PRO A N 1 ATOM 2431 C CA . PRO A 1 310 ? -36.823 -6.437 -22.231 1.00 24.21 ? 336 PRO A CA 1 ATOM 2432 C C . PRO A 1 310 ? -36.888 -4.906 -22.147 1.00 20.27 ? 336 PRO A C 1 ATOM 2433 O O . PRO A 1 310 ? -37.982 -4.349 -22.034 1.00 19.96 ? 336 PRO A O 1 ATOM 2434 C CB . PRO A 1 310 ? -36.603 -7.054 -20.849 1.00 24.67 ? 336 PRO A CB 1 ATOM 2435 C CG . PRO A 1 310 ? -35.890 -8.329 -21.149 1.00 30.28 ? 336 PRO A CG 1 ATOM 2436 C CD . PRO A 1 310 ? -34.950 -7.997 -22.293 1.00 21.80 ? 336 PRO A CD 1 ATOM 2437 N N . ALA A 1 311 ? -35.732 -4.246 -22.237 1.00 16.86 ? 337 ALA A N 1 ATOM 2438 C CA . ALA A 1 311 ? -35.671 -2.789 -22.257 1.00 14.97 ? 337 ALA A CA 1 ATOM 2439 C C . ALA A 1 311 ? -36.399 -2.216 -23.461 1.00 16.57 ? 337 ALA A C 1 ATOM 2440 O O . ALA A 1 311 ? -36.825 -1.065 -23.428 1.00 17.29 ? 337 ALA A O 1 ATOM 2441 C CB . ALA A 1 311 ? -34.223 -2.305 -22.247 1.00 13.43 ? 337 ALA A CB 1 ATOM 2442 N N . PHE A 1 312 ? -36.544 -3.011 -24.522 1.00 14.87 ? 338 PHE A N 1 ATOM 2443 C CA . PHE A 1 312 ? -37.237 -2.529 -25.714 1.00 14.93 ? 338 PHE A CA 1 ATOM 2444 C C . PHE A 1 312 ? -38.694 -2.227 -25.370 1.00 17.26 ? 338 PHE A C 1 ATOM 2445 O O . PHE A 1 312 ? -39.186 -1.122 -25.615 1.00 17.69 ? 338 PHE A O 1 ATOM 2446 C CB . PHE A 1 312 ? -37.157 -3.546 -26.843 1.00 23.06 ? 338 PHE A CB 1 ATOM 2447 C CG . PHE A 1 312 ? -37.926 -3.151 -28.066 1.00 24.24 ? 338 PHE A CG 1 ATOM 2448 C CD1 . PHE A 1 312 ? -37.334 -2.370 -29.049 1.00 24.27 ? 338 PHE A CD1 1 ATOM 2449 C CD2 . PHE A 1 312 ? -39.239 -3.562 -28.238 1.00 24.45 ? 338 PHE A CD2 1 ATOM 2450 C CE1 . PHE A 1 312 ? -38.044 -2.007 -30.181 1.00 26.47 ? 338 PHE A CE1 1 ATOM 2451 C CE2 . PHE A 1 312 ? -39.955 -3.204 -29.370 1.00 29.96 ? 338 PHE A CE2 1 ATOM 2452 C CZ . PHE A 1 312 ? -39.353 -2.421 -30.343 1.00 21.24 ? 338 PHE A CZ 1 ATOM 2453 N N . ASN A 1 313 ? -39.367 -3.221 -24.800 1.00 17.92 ? 339 ASN A N 1 ATOM 2454 C CA . ASN A 1 313 ? -40.745 -3.075 -24.338 1.00 34.40 ? 339 ASN A CA 1 ATOM 2455 C C . ASN A 1 313 ? -40.911 -1.940 -23.340 1.00 27.85 ? 339 ASN A C 1 ATOM 2456 O O . ASN A 1 313 ? -41.889 -1.194 -23.407 1.00 23.80 ? 339 ASN A O 1 ATOM 2457 C CB . ASN A 1 313 ? -41.246 -4.380 -23.706 1.00 42.79 ? 339 ASN A CB 1 ATOM 2458 C CG . ASN A 1 313 ? -41.266 -5.537 -24.691 1.00 61.71 ? 339 ASN A CG 1 ATOM 2459 O OD1 . ASN A 1 313 ? -40.216 -6.013 -25.131 1.00 74.95 ? 339 ASN A OD1 1 ATOM 2460 N ND2 . ASN A 1 313 ? -42.470 -6.004 -25.036 1.00 50.90 ? 339 ASN A ND2 1 ATOM 2461 N N . ALA A 1 314 ? -39.968 -1.815 -22.410 1.00 18.37 ? 340 ALA A N 1 ATOM 2462 C CA . ALA A 1 314 ? -40.055 -0.761 -21.400 1.00 27.73 ? 340 ALA A CA 1 ATOM 2463 C C . ALA A 1 314 ? -39.936 0.627 -22.033 1.00 24.53 ? 340 ALA A C 1 ATOM 2464 O O . ALA A 1 314 ? -40.578 1.579 -21.583 1.00 23.10 ? 340 ALA A O 1 ATOM 2465 C CB . ALA A 1 314 ? -38.988 -0.950 -20.343 1.00 25.36 ? 340 ALA A CB 1 ATOM 2466 N N . THR A 1 315 ? -39.114 0.727 -23.077 1.00 15.58 ? 341 THR A N 1 ATOM 2467 C CA . THR A 1 315 ? -38.912 1.984 -23.805 1.00 16.10 ? 341 THR A CA 1 ATOM 2468 C C . THR A 1 315 ? -40.176 2.355 -24.582 1.00 20.47 ? 341 THR A C 1 ATOM 2469 O O . THR A 1 315 ? -40.639 3.496 -24.501 1.00 18.05 ? 341 THR A O 1 ATOM 2470 C CB . THR A 1 315 ? -37.701 1.887 -24.759 1.00 16.84 ? 341 THR A CB 1 ATOM 2471 O OG1 . THR A 1 315 ? -36.520 1.630 -23.989 1.00 17.59 ? 341 THR A OG1 1 ATOM 2472 C CG2 . THR A 1 315 ? -37.499 3.187 -25.547 1.00 16.14 ? 341 THR A CG2 1 ATOM 2473 N N . ILE A 1 316 ? -40.742 1.389 -25.312 1.00 16.64 ? 342 ILE A N 1 ATOM 2474 C CA . ILE A 1 316 ? -42.016 1.591 -26.006 1.00 20.40 ? 342 ILE A CA 1 ATOM 2475 C C . ILE A 1 316 ? -43.086 2.094 -25.039 1.00 22.80 ? 342 ILE A C 1 ATOM 2476 O O . ILE A 1 316 ? -43.767 3.080 -25.309 1.00 27.91 ? 342 ILE A O 1 ATOM 2477 C CB . ILE A 1 316 ? -42.533 0.297 -26.670 1.00 19.54 ? 342 ILE A CB 1 ATOM 2478 C CG1 . ILE A 1 316 ? -41.618 -0.124 -27.816 1.00 30.68 ? 342 ILE A CG1 1 ATOM 2479 C CG2 . ILE A 1 316 ? -43.963 0.490 -27.184 1.00 21.64 ? 342 ILE A CG2 1 ATOM 2480 C CD1 . ILE A 1 316 ? -41.590 0.861 -28.939 1.00 28.91 ? 342 ILE A CD1 1 ATOM 2481 N N . GLN A 1 317 ? -43.221 1.412 -23.906 1.00 20.37 ? 343 GLN A N 1 ATOM 2482 C CA . GLN A 1 317 ? -44.254 1.751 -22.939 1.00 23.38 ? 343 GLN A CA 1 ATOM 2483 C C . GLN A 1 317 ? -44.047 3.147 -22.342 1.00 24.78 ? 343 GLN A C 1 ATOM 2484 O O . GLN A 1 317 ? -45.002 3.882 -22.125 1.00 28.55 ? 343 GLN A O 1 ATOM 2485 C CB . GLN A 1 317 ? -44.297 0.689 -21.846 1.00 27.18 ? 343 GLN A CB 1 ATOM 2486 C CG . GLN A 1 317 ? -44.863 -0.637 -22.348 1.00 43.85 ? 343 GLN A CG 1 ATOM 2487 C CD . GLN A 1 317 ? -44.612 -1.784 -21.397 1.00 62.23 ? 343 GLN A CD 1 ATOM 2488 O OE1 . GLN A 1 317 ? -44.178 -1.579 -20.262 1.00 75.00 ? 343 GLN A OE1 1 ATOM 2489 N NE2 . GLN A 1 317 ? -44.875 -3.005 -21.856 1.00 62.62 ? 343 GLN A NE2 1 ATOM 2490 N N . ALA A 1 318 ? -42.798 3.522 -22.105 1.00 23.14 ? 344 ALA A N 1 ATOM 2491 C CA . ALA A 1 318 ? -42.505 4.824 -21.521 1.00 22.45 ? 344 ALA A CA 1 ATOM 2492 C C . ALA A 1 318 ? -42.757 5.938 -22.533 1.00 26.44 ? 344 ALA A C 1 ATOM 2493 O O . ALA A 1 318 ? -43.235 7.011 -22.174 1.00 28.98 ? 344 ALA A O 1 ATOM 2494 C CB . ALA A 1 318 ? -41.073 4.868 -21.021 1.00 19.13 ? 344 ALA A CB 1 ATOM 2495 N N . LEU A 1 319 ? -42.434 5.675 -23.797 1.00 21.63 ? 345 LEU A N 1 ATOM 2496 C CA . LEU A 1 319 ? -42.669 6.636 -24.865 1.00 22.70 ? 345 LEU A CA 1 ATOM 2497 C C . LEU A 1 319 ? -44.162 6.899 -25.062 1.00 27.98 ? 345 LEU A C 1 ATOM 2498 O O . LEU A 1 319 ? -44.565 8.031 -25.300 1.00 33.19 ? 345 LEU A O 1 ATOM 2499 C CB . LEU A 1 319 ? -42.042 6.150 -26.179 1.00 20.71 ? 345 LEU A CB 1 ATOM 2500 C CG . LEU A 1 319 ? -40.512 6.224 -26.301 1.00 17.06 ? 345 LEU A CG 1 ATOM 2501 C CD1 . LEU A 1 319 ? -40.012 5.369 -27.483 1.00 14.57 ? 345 LEU A CD1 1 ATOM 2502 C CD2 . LEU A 1 319 ? -40.002 7.667 -26.415 1.00 15.87 ? 345 LEU A CD2 1 ATOM 2503 N N . LEU A 1 320 ? -44.978 5.855 -24.951 1.00 24.61 ? 346 LEU A N 1 ATOM 2504 C CA . LEU A 1 320 ? -46.416 5.981 -25.174 1.00 31.45 ? 346 LEU A CA 1 ATOM 2505 C C . LEU A 1 320 ? -47.137 6.587 -23.977 1.00 38.12 ? 346 LEU A C 1 ATOM 2506 O O . LEU A 1 320 ? -48.203 7.174 -24.126 1.00 43.92 ? 346 LEU A O 1 ATOM 2507 C CB . LEU A 1 320 ? -47.027 4.617 -25.500 1.00 25.31 ? 346 LEU A CB 1 ATOM 2508 C CG . LEU A 1 320 ? -46.604 3.997 -26.830 1.00 30.38 ? 346 LEU A CG 1 ATOM 2509 C CD1 . LEU A 1 320 ? -47.034 2.538 -26.921 1.00 31.09 ? 346 LEU A CD1 1 ATOM 2510 C CD2 . LEU A 1 320 ? -47.184 4.796 -27.974 1.00 27.85 ? 346 LEU A CD2 1 ATOM 2511 N N . ALA A 1 321 ? -46.557 6.449 -22.790 1.00 43.59 ? 347 ALA A N 1 ATOM 2512 C CA . ALA A 1 321 ? -47.228 6.890 -21.570 1.00 53.24 ? 347 ALA A CA 1 ATOM 2513 C C . ALA A 1 321 ? -46.741 8.261 -21.123 1.00 62.66 ? 347 ALA A C 1 ATOM 2514 O O . ALA A 1 321 ? -47.104 9.280 -21.710 1.00 68.70 ? 347 ALA A O 1 ATOM 2515 C CB . ALA A 1 321 ? -47.024 5.874 -20.463 1.00 57.84 ? 347 ALA A CB 1 ATOM 2516 N N . PRO B 1 1 ? -46.038 -24.937 -57.601 1.00 52.78 ? 27 PRO B N 1 ATOM 2517 C CA . PRO B 1 1 ? -44.997 -24.344 -56.755 1.00 47.09 ? 27 PRO B CA 1 ATOM 2518 C C . PRO B 1 1 ? -44.106 -23.376 -57.513 1.00 39.10 ? 27 PRO B C 1 ATOM 2519 O O . PRO B 1 1 ? -43.849 -23.535 -58.705 1.00 43.17 ? 27 PRO B O 1 ATOM 2520 C CB . PRO B 1 1 ? -44.172 -25.554 -56.280 1.00 41.48 ? 27 PRO B CB 1 ATOM 2521 C CG . PRO B 1 1 ? -44.873 -26.774 -56.804 1.00 47.62 ? 27 PRO B CG 1 ATOM 2522 C CD . PRO B 1 1 ? -45.738 -26.335 -57.944 1.00 55.21 ? 27 PRO B CD 1 ATOM 2523 N N . THR B 1 2 ? -43.631 -22.365 -56.809 1.00 38.43 ? 28 THR B N 1 ATOM 2524 C CA . THR B 1 2 ? -42.652 -21.481 -57.381 1.00 34.47 ? 28 THR B CA 1 ATOM 2525 C C . THR B 1 2 ? -41.291 -22.173 -57.418 1.00 30.68 ? 28 THR B C 1 ATOM 2526 O O . THR B 1 2 ? -41.141 -23.354 -57.089 1.00 26.61 ? 28 THR B O 1 ATOM 2527 C CB . THR B 1 2 ? -42.553 -20.152 -56.596 1.00 34.44 ? 28 THR B CB 1 ATOM 2528 O OG1 . THR B 1 2 ? -42.544 -20.419 -55.191 1.00 42.26 ? 28 THR B OG1 1 ATOM 2529 C CG2 . THR B 1 2 ? -43.741 -19.271 -56.904 1.00 41.69 ? 28 THR B CG2 1 ATOM 2530 N N . SER B 1 3 ? -40.306 -21.394 -57.817 1.00 26.51 ? 29 SER B N 1 ATOM 2531 C CA . SER B 1 3 ? -38.942 -21.832 -58.026 1.00 27.33 ? 29 SER B CA 1 ATOM 2532 C C . SER B 1 3 ? -38.047 -20.734 -57.544 1.00 25.94 ? 29 SER B C 1 ATOM 2533 O O . SER B 1 3 ? -38.466 -19.590 -57.517 1.00 26.38 ? 29 SER B O 1 ATOM 2534 C CB . SER B 1 3 ? -38.699 -22.108 -59.506 1.00 29.54 ? 29 SER B CB 1 ATOM 2535 O OG . SER B 1 3 ? -37.326 -21.997 -59.818 1.00 40.93 ? 29 SER B OG 1 ATOM 2536 N N . PRO B 1 4 ? -36.807 -21.065 -57.160 1.00 25.76 ? 30 PRO B N 1 ATOM 2537 C CA . PRO B 1 4 ? -35.855 -19.987 -56.880 1.00 21.52 ? 30 PRO B CA 1 ATOM 2538 C C . PRO B 1 4 ? -35.373 -19.243 -58.136 1.00 28.93 ? 30 PRO B C 1 ATOM 2539 O O . PRO B 1 4 ? -34.501 -18.385 -58.014 1.00 25.76 ? 30 PRO B O 1 ATOM 2540 C CB . PRO B 1 4 ? -34.681 -20.710 -56.202 1.00 26.21 ? 30 PRO B CB 1 ATOM 2541 C CG . PRO B 1 4 ? -34.829 -22.147 -56.557 1.00 31.26 ? 30 PRO B CG 1 ATOM 2542 C CD . PRO B 1 4 ? -36.294 -22.396 -56.788 1.00 33.12 ? 30 PRO B CD 1 ATOM 2543 N N . PHE B 1 5 ? -35.914 -19.549 -59.313 1.00 23.16 ? 31 PHE B N 1 ATOM 2544 C CA . PHE B 1 5 ? -35.441 -18.874 -60.531 1.00 21.77 ? 31 PHE B CA 1 ATOM 2545 C C . PHE B 1 5 ? -36.478 -17.931 -61.125 1.00 26.48 ? 31 PHE B C 1 ATOM 2546 O O . PHE B 1 5 ? -36.650 -17.880 -62.338 1.00 31.47 ? 31 PHE B O 1 ATOM 2547 C CB . PHE B 1 5 ? -35.017 -19.898 -61.589 1.00 21.32 ? 31 PHE B CB 1 ATOM 2548 C CG . PHE B 1 5 ? -33.837 -20.741 -61.181 1.00 24.20 ? 31 PHE B CG 1 ATOM 2549 C CD1 . PHE B 1 5 ? -32.577 -20.188 -61.073 1.00 23.38 ? 31 PHE B CD1 1 ATOM 2550 C CD2 . PHE B 1 5 ? -33.995 -22.097 -60.931 1.00 22.91 ? 31 PHE B CD2 1 ATOM 2551 C CE1 . PHE B 1 5 ? -31.489 -20.966 -60.705 1.00 22.96 ? 31 PHE B CE1 1 ATOM 2552 C CE2 . PHE B 1 5 ? -32.919 -22.885 -60.566 1.00 23.49 ? 31 PHE B CE2 1 ATOM 2553 C CZ . PHE B 1 5 ? -31.662 -22.317 -60.449 1.00 22.39 ? 31 PHE B CZ 1 ATOM 2554 N N . GLU B 1 6 ? -37.167 -17.181 -60.275 1.00 27.98 ? 32 GLU B N 1 ATOM 2555 C CA . GLU B 1 6 ? -38.166 -16.253 -60.771 1.00 33.12 ? 32 GLU B CA 1 ATOM 2556 C C . GLU B 1 6 ? -37.680 -14.816 -60.638 1.00 23.63 ? 32 GLU B C 1 ATOM 2557 O O . GLU B 1 6 ? -38.470 -13.872 -60.664 1.00 27.00 ? 32 GLU B O 1 ATOM 2558 C CB . GLU B 1 6 ? -39.491 -16.466 -60.041 1.00 36.77 ? 32 GLU B CB 1 ATOM 2559 C CG . GLU B 1 6 ? -40.260 -17.661 -60.585 1.00 46.80 ? 32 GLU B CG 1 ATOM 2560 C CD . GLU B 1 6 ? -41.299 -18.192 -59.623 1.00 58.56 ? 32 GLU B CD 1 ATOM 2561 O OE1 . GLU B 1 6 ? -41.848 -17.392 -58.835 1.00 65.70 ? 32 GLU B OE1 1 ATOM 2562 O OE2 . GLU B 1 6 ? -41.561 -19.416 -59.654 1.00 58.60 ? 32 GLU B OE2 1 ATOM 2563 N N . THR B 1 7 ? -36.370 -14.654 -60.497 1.00 16.46 ? 33 THR B N 1 ATOM 2564 C CA . THR B 1 7 ? -35.767 -13.327 -60.523 1.00 15.74 ? 33 THR B CA 1 ATOM 2565 C C . THR B 1 7 ? -34.733 -13.296 -61.623 1.00 22.80 ? 33 THR B C 1 ATOM 2566 O O . THR B 1 7 ? -34.166 -14.332 -61.973 1.00 15.24 ? 33 THR B O 1 ATOM 2567 C CB . THR B 1 7 ? -35.095 -12.938 -59.194 1.00 18.48 ? 33 THR B CB 1 ATOM 2568 O OG1 . THR B 1 7 ? -33.951 -13.774 -58.954 1.00 17.94 ? 33 THR B OG1 1 ATOM 2569 C CG2 . THR B 1 7 ? -36.070 -13.060 -58.040 1.00 19.39 ? 33 THR B CG2 1 ATOM 2570 N N . LEU B 1 8 ? -34.489 -12.113 -62.174 1.00 11.99 ? 34 LEU B N 1 ATOM 2571 C CA . LEU B 1 8 ? -33.543 -12.003 -63.268 1.00 15.29 ? 34 LEU B CA 1 ATOM 2572 C C . LEU B 1 8 ? -32.130 -12.356 -62.788 1.00 14.54 ? 34 LEU B C 1 ATOM 2573 O O . LEU B 1 8 ? -31.376 -13.028 -63.500 1.00 16.67 ? 34 LEU B O 1 ATOM 2574 C CB . LEU B 1 8 ? -33.587 -10.596 -63.873 1.00 15.29 ? 34 LEU B CB 1 ATOM 2575 C CG . LEU B 1 8 ? -34.887 -10.211 -64.587 1.00 13.94 ? 34 LEU B CG 1 ATOM 2576 C CD1 . LEU B 1 8 ? -35.064 -8.680 -64.591 1.00 14.61 ? 34 LEU B CD1 1 ATOM 2577 C CD2 . LEU B 1 8 ? -34.932 -10.787 -66.017 1.00 14.45 ? 34 LEU B CD2 1 ATOM 2578 N N . ARG B 1 9 ? -31.779 -11.919 -61.582 1.00 12.87 ? 35 ARG B N 1 ATOM 2579 C CA . ARG B 1 9 ? -30.431 -12.155 -61.064 1.00 15.69 ? 35 ARG B CA 1 ATOM 2580 C C . ARG B 1 9 ? -30.193 -13.645 -60.822 1.00 18.57 ? 35 ARG B C 1 ATOM 2581 O O . ARG B 1 9 ? -29.105 -14.143 -61.097 1.00 17.66 ? 35 ARG B O 1 ATOM 2582 C CB . ARG B 1 9 ? -30.173 -11.353 -59.777 1.00 12.48 ? 35 ARG B CB 1 ATOM 2583 C CG . ARG B 1 9 ? -31.166 -11.574 -58.642 1.00 20.84 ? 35 ARG B CG 1 ATOM 2584 C CD . ARG B 1 9 ? -30.878 -10.639 -57.472 1.00 18.85 ? 35 ARG B CD 1 ATOM 2585 N NE . ARG B 1 9 ? -29.637 -11.008 -56.800 1.00 21.97 ? 35 ARG B NE 1 ATOM 2586 C CZ . ARG B 1 9 ? -29.044 -10.289 -55.855 1.00 25.98 ? 35 ARG B CZ 1 ATOM 2587 N NH1 . ARG B 1 9 ? -29.553 -9.119 -55.464 1.00 20.83 ? 35 ARG B NH1 1 ATOM 2588 N NH2 . ARG B 1 9 ? -27.922 -10.734 -55.312 1.00 27.03 ? 35 ARG B NH2 1 ATOM 2589 N N . ALA B 1 10 ? -31.196 -14.367 -60.326 1.00 14.93 ? 36 ALA B N 1 ATOM 2590 C CA . ALA B 1 10 ? -31.005 -15.806 -60.093 1.00 20.34 ? 36 ALA B CA 1 ATOM 2591 C C . ALA B 1 10 ? -30.911 -16.578 -61.414 1.00 22.85 ? 36 ALA B C 1 ATOM 2592 O O . ALA B 1 10 ? -30.088 -17.484 -61.554 1.00 17.28 ? 36 ALA B O 1 ATOM 2593 C CB . ALA B 1 10 ? -32.125 -16.370 -59.223 1.00 20.05 ? 36 ALA B CB 1 ATOM 2594 N N . ALA B 1 11 ? -31.743 -16.226 -62.391 1.00 20.64 ? 37 ALA B N 1 ATOM 2595 C CA . ALA B 1 11 ? -31.707 -16.925 -63.671 1.00 19.77 ? 37 ALA B CA 1 ATOM 2596 C C . ALA B 1 11 ? -30.463 -16.588 -64.491 1.00 17.88 ? 37 ALA B C 1 ATOM 2597 O O . ALA B 1 11 ? -30.024 -17.397 -65.288 1.00 15.22 ? 37 ALA B O 1 ATOM 2598 C CB . ALA B 1 11 ? -32.975 -16.623 -64.490 1.00 14.81 ? 37 ALA B CB 1 ATOM 2599 N N . ALA B 1 12 ? -29.903 -15.398 -64.305 1.00 13.47 ? 38 ALA B N 1 ATOM 2600 C CA . ALA B 1 12 ? -28.745 -14.967 -65.096 1.00 15.63 ? 38 ALA B CA 1 ATOM 2601 C C . ALA B 1 12 ? -27.420 -15.618 -64.677 1.00 17.69 ? 38 ALA B C 1 ATOM 2602 O O . ALA B 1 12 ? -26.508 -15.723 -65.492 1.00 15.32 ? 38 ALA B O 1 ATOM 2603 C CB . ALA B 1 12 ? -28.597 -13.463 -65.026 1.00 13.38 ? 38 ALA B CB 1 ATOM 2604 N N . ALA B 1 13 ? -27.313 -16.022 -63.411 1.00 20.85 ? 39 ALA B N 1 ATOM 2605 C CA . ALA B 1 13 ? -26.070 -16.568 -62.855 1.00 21.60 ? 39 ALA B CA 1 ATOM 2606 C C . ALA B 1 13 ? -25.441 -17.605 -63.782 1.00 24.31 ? 39 ALA B C 1 ATOM 2607 O O . ALA B 1 13 ? -26.133 -18.494 -64.260 1.00 20.61 ? 39 ALA B O 1 ATOM 2608 C CB . ALA B 1 13 ? -26.331 -17.180 -61.475 1.00 22.73 ? 39 ALA B CB 1 ATOM 2609 N N . PRO B 1 14 ? -24.120 -17.511 -64.019 1.00 27.44 ? 40 PRO B N 1 ATOM 2610 C CA . PRO B 1 14 ? -23.146 -16.645 -63.343 1.00 26.66 ? 40 PRO B CA 1 ATOM 2611 C C . PRO B 1 14 ? -22.946 -15.261 -63.963 1.00 23.19 ? 40 PRO B C 1 ATOM 2612 O O . PRO B 1 14 ? -22.052 -14.535 -63.529 1.00 22.23 ? 40 PRO B O 1 ATOM 2613 C CB . PRO B 1 14 ? -21.854 -17.448 -63.468 1.00 25.92 ? 40 PRO B CB 1 ATOM 2614 C CG . PRO B 1 14 ? -21.985 -18.075 -64.819 1.00 21.91 ? 40 PRO B CG 1 ATOM 2615 C CD . PRO B 1 14 ? -23.464 -18.367 -65.026 1.00 25.67 ? 40 PRO B CD 1 ATOM 2616 N N . ARG B 1 15 ? -23.740 -14.896 -64.961 1.00 19.78 ? 41 ARG B N 1 ATOM 2617 C CA . ARG B 1 15 ? -23.666 -13.533 -65.488 1.00 16.24 ? 41 ARG B CA 1 ATOM 2618 C C . ARG B 1 15 ? -24.440 -12.629 -64.552 1.00 17.80 ? 41 ARG B C 1 ATOM 2619 O O . ARG B 1 15 ? -25.236 -13.107 -63.747 1.00 25.40 ? 41 ARG B O 1 ATOM 2620 C CB . ARG B 1 15 ? -24.223 -13.439 -66.905 1.00 21.07 ? 41 ARG B CB 1 ATOM 2621 C CG . ARG B 1 15 ? -23.480 -14.277 -67.932 1.00 17.03 ? 41 ARG B CG 1 ATOM 2622 C CD . ARG B 1 15 ? -24.075 -14.090 -69.327 1.00 16.91 ? 41 ARG B CD 1 ATOM 2623 N NE . ARG B 1 15 ? -23.327 -14.884 -70.299 1.00 27.33 ? 41 ARG B NE 1 ATOM 2624 C CZ . ARG B 1 15 ? -23.499 -16.185 -70.486 1.00 23.66 ? 41 ARG B CZ 1 ATOM 2625 N NH1 . ARG B 1 15 ? -24.427 -16.845 -69.797 1.00 28.04 ? 41 ARG B NH1 1 ATOM 2626 N NH2 . ARG B 1 15 ? -22.755 -16.824 -71.378 1.00 26.20 ? 41 ARG B NH2 1 ATOM 2627 N N . TYR B 1 16 ? -24.198 -11.327 -64.631 1.00 17.93 ? 42 TYR B N 1 ATOM 2628 C CA . TYR B 1 16 ? -25.002 -10.408 -63.850 1.00 12.33 ? 42 TYR B CA 1 ATOM 2629 C C . TYR B 1 16 ? -26.186 -9.928 -64.681 1.00 10.51 ? 42 TYR B C 1 ATOM 2630 O O . TYR B 1 16 ? -26.154 -9.941 -65.918 1.00 11.44 ? 42 TYR B O 1 ATOM 2631 C CB . TYR B 1 16 ? -24.175 -9.206 -63.348 1.00 13.00 ? 42 TYR B CB 1 ATOM 2632 C CG . TYR B 1 16 ? -23.622 -8.302 -64.436 1.00 16.24 ? 42 TYR B CG 1 ATOM 2633 C CD1 . TYR B 1 16 ? -24.419 -7.327 -65.048 1.00 12.36 ? 42 TYR B CD1 1 ATOM 2634 C CD2 . TYR B 1 16 ? -22.295 -8.420 -64.845 1.00 10.23 ? 42 TYR B CD2 1 ATOM 2635 C CE1 . TYR B 1 16 ? -23.907 -6.503 -66.054 1.00 12.68 ? 42 TYR B CE1 1 ATOM 2636 C CE2 . TYR B 1 16 ? -21.769 -7.596 -65.839 1.00 16.24 ? 42 TYR B CE2 1 ATOM 2637 C CZ . TYR B 1 16 ? -22.574 -6.645 -66.439 1.00 15.59 ? 42 TYR B CZ 1 ATOM 2638 O OH . TYR B 1 16 ? -22.042 -5.839 -67.429 1.00 11.53 ? 42 TYR B OH 1 ATOM 2639 N N . PHE B 1 17 ? -27.235 -9.497 -64.003 1.00 14.05 ? 43 PHE B N 1 ATOM 2640 C CA . PHE B 1 17 ? -28.291 -8.766 -64.699 1.00 12.35 ? 43 PHE B CA 1 ATOM 2641 C C . PHE B 1 17 ? -28.459 -7.446 -63.972 1.00 10.45 ? 43 PHE B C 1 ATOM 2642 O O . PHE B 1 17 ? -28.861 -7.434 -62.817 1.00 10.94 ? 43 PHE B O 1 ATOM 2643 C CB . PHE B 1 17 ? -29.597 -9.553 -64.734 1.00 13.47 ? 43 PHE B CB 1 ATOM 2644 C CG . PHE B 1 17 ? -30.490 -9.164 -65.880 1.00 13.41 ? 43 PHE B CG 1 ATOM 2645 C CD1 . PHE B 1 17 ? -31.250 -8.012 -65.809 1.00 13.24 ? 43 PHE B CD1 1 ATOM 2646 C CD2 . PHE B 1 17 ? -30.529 -9.924 -67.042 1.00 16.58 ? 43 PHE B CD2 1 ATOM 2647 C CE1 . PHE B 1 17 ? -32.061 -7.628 -66.879 1.00 18.44 ? 43 PHE B CE1 1 ATOM 2648 C CE2 . PHE B 1 17 ? -31.335 -9.547 -68.111 1.00 10.82 ? 43 PHE B CE2 1 ATOM 2649 C CZ . PHE B 1 17 ? -32.097 -8.400 -68.023 1.00 15.79 ? 43 PHE B CZ 1 ATOM 2650 N N . GLY B 1 18 ? -28.113 -6.336 -64.622 1.00 11.76 ? 44 GLY B N 1 ATOM 2651 C CA . GLY B 1 18 ? -28.039 -5.073 -63.904 1.00 9.88 ? 44 GLY B CA 1 ATOM 2652 C C . GLY B 1 18 ? -29.028 -4.013 -64.361 1.00 9.65 ? 44 GLY B C 1 ATOM 2653 O O . GLY B 1 18 ? -29.737 -4.203 -65.343 1.00 11.34 ? 44 GLY B O 1 ATOM 2654 N N . ALA B 1 19 ? -29.053 -2.881 -63.654 1.00 9.10 ? 45 ALA B N 1 ATOM 2655 C CA . ALA B 1 19 ? -29.946 -1.792 -64.025 1.00 12.48 ? 45 ALA B CA 1 ATOM 2656 C C . ALA B 1 19 ? -29.251 -0.447 -63.852 1.00 9.75 ? 45 ALA B C 1 ATOM 2657 O O . ALA B 1 19 ? -28.389 -0.294 -62.992 1.00 10.32 ? 45 ALA B O 1 ATOM 2658 C CB . ALA B 1 19 ? -31.221 -1.845 -63.179 1.00 13.18 ? 45 ALA B CB 1 ATOM 2659 N N . ALA B 1 20 ? -29.609 0.526 -64.674 1.00 8.75 ? 46 ALA B N 1 ATOM 2660 C CA . ALA B 1 20 ? -29.196 1.898 -64.414 1.00 11.94 ? 46 ALA B CA 1 ATOM 2661 C C . ALA B 1 20 ? -29.956 2.397 -63.193 1.00 15.49 ? 46 ALA B C 1 ATOM 2662 O O . ALA B 1 20 ? -31.199 2.330 -63.148 1.00 11.85 ? 46 ALA B O 1 ATOM 2663 C CB . ALA B 1 20 ? -29.476 2.794 -65.609 1.00 15.34 ? 46 ALA B CB 1 ATOM 2664 N N . LEU B 1 21 ? -29.221 2.892 -62.203 1.00 10.18 ? 47 LEU B N 1 ATOM 2665 C CA . LEU B 1 21 ? -29.851 3.428 -60.993 1.00 13.32 ? 47 LEU B CA 1 ATOM 2666 C C . LEU B 1 21 ? -29.546 4.916 -60.864 1.00 14.22 ? 47 LEU B C 1 ATOM 2667 O O . LEU B 1 21 ? -28.382 5.318 -60.928 1.00 17.89 ? 47 LEU B O 1 ATOM 2668 C CB . LEU B 1 21 ? -29.363 2.677 -59.750 1.00 8.40 ? 47 LEU B CB 1 ATOM 2669 C CG . LEU B 1 21 ? -29.506 1.154 -59.752 1.00 12.44 ? 47 LEU B CG 1 ATOM 2670 C CD1 . LEU B 1 21 ? -28.920 0.564 -58.468 1.00 12.79 ? 47 LEU B CD1 1 ATOM 2671 C CD2 . LEU B 1 21 ? -30.967 0.755 -59.923 1.00 13.53 ? 47 LEU B CD2 1 ATOM 2672 N N . GLY B 1 22 ? -30.586 5.733 -60.720 1.00 12.47 ? 48 GLY B N 1 ATOM 2673 C CA . GLY B 1 22 ? -30.400 7.155 -60.516 1.00 14.41 ? 48 GLY B CA 1 ATOM 2674 C C . GLY B 1 22 ? -30.584 7.508 -59.051 1.00 12.13 ? 48 GLY B C 1 ATOM 2675 O O . GLY B 1 22 ? -31.475 6.985 -58.381 1.00 12.74 ? 48 GLY B O 1 ATOM 2676 N N . VAL B 1 23 ? -29.738 8.394 -58.548 1.00 13.50 ? 49 VAL B N 1 ATOM 2677 C CA . VAL B 1 23 ? -29.846 8.823 -57.157 1.00 15.49 ? 49 VAL B CA 1 ATOM 2678 C C . VAL B 1 23 ? -31.259 9.301 -56.769 1.00 13.93 ? 49 VAL B C 1 ATOM 2679 O O . VAL B 1 23 ? -31.766 8.899 -55.722 1.00 13.96 ? 49 VAL B O 1 ATOM 2680 C CB . VAL B 1 23 ? -28.814 9.920 -56.837 1.00 19.72 ? 49 VAL B CB 1 ATOM 2681 C CG1 . VAL B 1 23 ? -29.087 10.535 -55.475 1.00 25.66 ? 49 VAL B CG1 1 ATOM 2682 C CG2 . VAL B 1 23 ? -27.416 9.329 -56.855 1.00 22.13 ? 49 VAL B CG2 1 ATOM 2683 N N . PRO B 1 24 ? -31.915 10.132 -57.608 1.00 16.27 ? 50 PRO B N 1 ATOM 2684 C CA . PRO B 1 24 ? -33.220 10.604 -57.130 1.00 13.42 ? 50 PRO B CA 1 ATOM 2685 C C . PRO B 1 24 ? -34.212 9.475 -56.857 1.00 14.72 ? 50 PRO B C 1 ATOM 2686 O O . PRO B 1 24 ? -35.055 9.608 -55.966 1.00 16.77 ? 50 PRO B O 1 ATOM 2687 C CB . PRO B 1 24 ? -33.715 11.496 -58.280 1.00 20.42 ? 50 PRO B CB 1 ATOM 2688 C CG . PRO B 1 24 ? -32.448 12.002 -58.921 1.00 18.30 ? 50 PRO B CG 1 ATOM 2689 C CD . PRO B 1 24 ? -31.511 10.810 -58.858 1.00 12.89 ? 50 PRO B CD 1 ATOM 2690 N N . HIS B 1 25 ? -34.097 8.377 -57.594 1.00 12.32 ? 51 HIS B N 1 ATOM 2691 C CA . HIS B 1 25 ? -35.009 7.248 -57.423 1.00 12.12 ? 51 HIS B CA 1 ATOM 2692 C C . HIS B 1 25 ? -34.634 6.412 -56.190 1.00 11.66 ? 51 HIS B C 1 ATOM 2693 O O . HIS B 1 25 ? -35.494 5.949 -55.449 1.00 15.17 ? 51 HIS B O 1 ATOM 2694 C CB . HIS B 1 25 ? -35.009 6.378 -58.691 1.00 16.27 ? 51 HIS B CB 1 ATOM 2695 C CG . HIS B 1 25 ? -35.257 7.151 -59.953 1.00 19.22 ? 51 HIS B CG 1 ATOM 2696 N ND1 . HIS B 1 25 ? -36.290 8.057 -60.076 1.00 17.13 ? 51 HIS B ND1 1 ATOM 2697 C CD2 . HIS B 1 25 ? -34.610 7.153 -61.147 1.00 17.11 ? 51 HIS B CD2 1 ATOM 2698 C CE1 . HIS B 1 25 ? -36.271 8.584 -61.291 1.00 15.12 ? 51 HIS B CE1 1 ATOM 2699 N NE2 . HIS B 1 25 ? -35.256 8.061 -61.957 1.00 16.25 ? 51 HIS B NE2 1 ATOM 2700 N N . LEU B 1 26 ? -33.339 6.218 -55.979 1.00 11.46 ? 52 LEU B N 1 ATOM 2701 C CA . LEU B 1 26 ? -32.859 5.481 -54.812 1.00 11.25 ? 52 LEU B CA 1 ATOM 2702 C C . LEU B 1 26 ? -33.283 6.171 -53.527 1.00 14.92 ? 52 LEU B C 1 ATOM 2703 O O . LEU B 1 26 ? -33.701 5.522 -52.562 1.00 12.22 ? 52 LEU B O 1 ATOM 2704 C CB . LEU B 1 26 ? -31.334 5.353 -54.846 1.00 10.13 ? 52 LEU B CB 1 ATOM 2705 C CG . LEU B 1 26 ? -30.699 4.514 -55.951 1.00 15.39 ? 52 LEU B CG 1 ATOM 2706 C CD1 . LEU B 1 26 ? -29.175 4.587 -55.813 1.00 13.89 ? 52 LEU B CD1 1 ATOM 2707 C CD2 . LEU B 1 26 ? -31.183 3.073 -55.867 1.00 14.26 ? 52 LEU B CD2 1 ATOM 2708 N N . LEU B 1 27 ? -33.181 7.499 -53.521 1.00 12.04 ? 53 LEU B N 1 ATOM 2709 C CA . LEU B 1 27 ? -33.494 8.289 -52.318 1.00 12.91 ? 53 LEU B CA 1 ATOM 2710 C C . LEU B 1 27 ? -34.995 8.531 -52.142 1.00 17.08 ? 53 LEU B C 1 ATOM 2711 O O . LEU B 1 27 ? -35.427 9.165 -51.178 1.00 14.75 ? 53 LEU B O 1 ATOM 2712 C CB . LEU B 1 27 ? -32.744 9.625 -52.364 1.00 20.02 ? 53 LEU B CB 1 ATOM 2713 C CG . LEU B 1 27 ? -31.415 9.666 -51.592 1.00 26.54 ? 53 LEU B CG 1 ATOM 2714 C CD1 . LEU B 1 27 ? -30.614 8.395 -51.781 1.00 23.49 ? 53 LEU B CD1 1 ATOM 2715 C CD2 . LEU B 1 27 ? -30.583 10.892 -51.974 1.00 27.84 ? 53 LEU B CD2 1 ATOM 2716 N N . ASN B 1 28 ? -35.787 8.000 -53.066 1.00 13.70 ? 54 ASN B N 1 ATOM 2717 C CA . ASN B 1 28 ? -37.248 8.183 -53.048 1.00 15.13 ? 54 ASN B CA 1 ATOM 2718 C C . ASN B 1 28 ? -37.982 7.072 -52.306 1.00 18.03 ? 54 ASN B C 1 ATOM 2719 O O . ASN B 1 28 ? -39.160 6.831 -52.534 1.00 17.18 ? 54 ASN B O 1 ATOM 2720 C CB . ASN B 1 28 ? -37.757 8.226 -54.476 1.00 14.67 ? 54 ASN B CB 1 ATOM 2721 C CG . ASN B 1 28 ? -39.068 8.963 -54.618 1.00 18.66 ? 54 ASN B CG 1 ATOM 2722 O OD1 . ASN B 1 28 ? -39.456 9.779 -53.783 1.00 16.99 ? 54 ASN B OD1 1 ATOM 2723 N ND2 . ASN B 1 28 ? -39.761 8.661 -55.691 1.00 22.45 ? 54 ASN B ND2 1 ATOM 2724 N N . PHE B 1 29 ? -37.276 6.380 -51.433 1.00 16.34 ? 55 PHE B N 1 ATOM 2725 C CA . PHE B 1 29 ? -37.786 5.128 -50.871 1.00 16.10 ? 55 PHE B CA 1 ATOM 2726 C C . PHE B 1 29 ? -39.086 5.275 -50.047 1.00 20.54 ? 55 PHE B C 1 ATOM 2727 O O . PHE B 1 29 ? -39.893 4.346 -49.996 1.00 19.15 ? 55 PHE B O 1 ATOM 2728 C CB . PHE B 1 29 ? -36.684 4.480 -50.022 1.00 16.99 ? 55 PHE B CB 1 ATOM 2729 C CG . PHE B 1 29 ? -37.101 3.211 -49.351 1.00 19.36 ? 55 PHE B CG 1 ATOM 2730 C CD1 . PHE B 1 29 ? -37.277 2.046 -50.089 1.00 13.41 ? 55 PHE B CD1 1 ATOM 2731 C CD2 . PHE B 1 29 ? -37.307 3.175 -47.984 1.00 24.74 ? 55 PHE B CD2 1 ATOM 2732 C CE1 . PHE B 1 29 ? -37.658 0.867 -49.466 1.00 22.34 ? 55 PHE B CE1 1 ATOM 2733 C CE2 . PHE B 1 29 ? -37.702 2.002 -47.353 1.00 30.10 ? 55 PHE B CE2 1 ATOM 2734 C CZ . PHE B 1 29 ? -37.874 0.847 -48.092 1.00 25.63 ? 55 PHE B CZ 1 ATOM 2735 N N . THR B 1 30 ? -39.310 6.423 -49.415 1.00 19.46 ? 56 THR B N 1 ATOM 2736 C CA . THR B 1 30 ? -40.537 6.574 -48.625 1.00 22.41 ? 56 THR B CA 1 ATOM 2737 C C . THR B 1 30 ? -41.764 6.840 -49.505 1.00 28.80 ? 56 THR B C 1 ATOM 2738 O O . THR B 1 30 ? -42.896 6.604 -49.084 1.00 28.88 ? 56 THR B O 1 ATOM 2739 C CB . THR B 1 30 ? -40.416 7.697 -47.571 1.00 28.06 ? 56 THR B CB 1 ATOM 2740 O OG1 . THR B 1 30 ? -40.155 8.953 -48.211 1.00 30.63 ? 56 THR B OG1 1 ATOM 2741 C CG2 . THR B 1 30 ? -39.278 7.380 -46.587 1.00 26.46 ? 56 THR B CG2 1 ATOM 2742 N N . HIS B 1 31 ? -41.539 7.311 -50.729 1.00 18.82 ? 57 HIS B N 1 ATOM 2743 C CA . HIS B 1 31 ? -42.643 7.578 -51.660 1.00 22.18 ? 57 HIS B CA 1 ATOM 2744 C C . HIS B 1 31 ? -42.802 6.491 -52.720 1.00 21.98 ? 57 HIS B C 1 ATOM 2745 O O . HIS B 1 31 ? -43.912 6.210 -53.165 1.00 20.77 ? 57 HIS B O 1 ATOM 2746 C CB . HIS B 1 31 ? -42.439 8.936 -52.331 1.00 19.34 ? 57 HIS B CB 1 ATOM 2747 C CG . HIS B 1 31 ? -42.459 10.076 -51.364 1.00 36.92 ? 57 HIS B CG 1 ATOM 2748 N ND1 . HIS B 1 31 ? -43.628 10.584 -50.840 1.00 47.96 ? 57 HIS B ND1 1 ATOM 2749 C CD2 . HIS B 1 31 ? -41.454 10.784 -50.796 1.00 43.72 ? 57 HIS B CD2 1 ATOM 2750 C CE1 . HIS B 1 31 ? -43.344 11.566 -50.003 1.00 45.14 ? 57 HIS B CE1 1 ATOM 2751 N NE2 . HIS B 1 31 ? -42.031 11.707 -49.957 1.00 42.81 ? 57 HIS B NE2 1 ATOM 2752 N N . ASP B 1 32 ? -41.688 5.893 -53.126 1.00 17.45 ? 58 ASP B N 1 ATOM 2753 C CA . ASP B 1 32 ? -41.695 4.820 -54.119 1.00 20.15 ? 58 ASP B CA 1 ATOM 2754 C C . ASP B 1 32 ? -40.778 3.676 -53.690 1.00 14.87 ? 58 ASP B C 1 ATOM 2755 O O . ASP B 1 32 ? -39.719 3.480 -54.287 1.00 18.33 ? 58 ASP B O 1 ATOM 2756 C CB . ASP B 1 32 ? -41.257 5.353 -55.486 1.00 15.44 ? 58 ASP B CB 1 ATOM 2757 C CG . ASP B 1 32 ? -41.307 4.287 -56.579 1.00 31.57 ? 58 ASP B CG 1 ATOM 2758 O OD1 . ASP B 1 32 ? -41.896 3.212 -56.339 1.00 28.53 ? 58 ASP B OD1 1 ATOM 2759 O OD2 . ASP B 1 32 ? -40.755 4.525 -57.678 1.00 24.16 ? 58 ASP B OD2 1 ATOM 2760 N N . PRO B 1 33 ? -41.177 2.910 -52.661 1.00 18.17 ? 59 PRO B N 1 ATOM 2761 C CA . PRO B 1 33 ? -40.268 1.863 -52.181 1.00 17.44 ? 59 PRO B CA 1 ATOM 2762 C C . PRO B 1 33 ? -40.050 0.753 -53.196 1.00 19.52 ? 59 PRO B C 1 ATOM 2763 O O . PRO B 1 33 ? -39.016 0.086 -53.129 1.00 19.30 ? 59 PRO B O 1 ATOM 2764 C CB . PRO B 1 33 ? -40.973 1.321 -50.938 1.00 20.42 ? 59 PRO B CB 1 ATOM 2765 C CG . PRO B 1 33 ? -42.411 1.628 -51.162 1.00 23.01 ? 59 PRO B CG 1 ATOM 2766 C CD . PRO B 1 33 ? -42.444 2.929 -51.907 1.00 21.15 ? 59 PRO B CD 1 ATOM 2767 N N . LEU B 1 34 ? -40.985 0.555 -54.124 1.00 17.03 ? 60 LEU B N 1 ATOM 2768 C CA . LEU B 1 34 ? -40.823 -0.520 -55.108 1.00 16.93 ? 60 LEU B CA 1 ATOM 2769 C C . LEU B 1 34 ? -39.572 -0.391 -55.986 1.00 16.12 ? 60 LEU B C 1 ATOM 2770 O O . LEU B 1 34 ? -39.056 -1.401 -56.492 1.00 13.56 ? 60 LEU B O 1 ATOM 2771 C CB . LEU B 1 34 ? -42.065 -0.617 -55.994 1.00 18.78 ? 60 LEU B CB 1 ATOM 2772 C CG . LEU B 1 34 ? -43.204 -1.298 -55.247 1.00 27.67 ? 60 LEU B CG 1 ATOM 2773 C CD1 . LEU B 1 34 ? -44.451 -1.389 -56.114 1.00 27.66 ? 60 LEU B CD1 1 ATOM 2774 C CD2 . LEU B 1 34 ? -42.750 -2.673 -54.791 1.00 32.65 ? 60 LEU B CD2 1 ATOM 2775 N N . PHE B 1 35 ? -39.081 0.829 -56.183 1.00 14.76 ? 61 PHE B N 1 ATOM 2776 C CA . PHE B 1 35 ? -37.871 1.009 -56.981 1.00 13.29 ? 61 PHE B CA 1 ATOM 2777 C C . PHE B 1 35 ? -36.697 0.300 -56.289 1.00 21.63 ? 61 PHE B C 1 ATOM 2778 O O . PHE B 1 35 ? -36.062 -0.580 -56.876 1.00 13.25 ? 61 PHE B O 1 ATOM 2779 C CB . PHE B 1 35 ? -37.557 2.490 -57.192 1.00 13.97 ? 61 PHE B CB 1 ATOM 2780 C CG . PHE B 1 35 ? -36.426 2.731 -58.147 1.00 10.91 ? 61 PHE B CG 1 ATOM 2781 C CD1 . PHE B 1 35 ? -35.117 2.765 -57.697 1.00 10.33 ? 61 PHE B CD1 1 ATOM 2782 C CD2 . PHE B 1 35 ? -36.678 2.902 -59.509 1.00 13.25 ? 61 PHE B CD2 1 ATOM 2783 C CE1 . PHE B 1 35 ? -34.060 2.973 -58.589 1.00 18.77 ? 61 PHE B CE1 1 ATOM 2784 C CE2 . PHE B 1 35 ? -35.641 3.120 -60.411 1.00 10.55 ? 61 PHE B CE2 1 ATOM 2785 C CZ . PHE B 1 35 ? -34.320 3.143 -59.949 1.00 16.87 ? 61 PHE B CZ 1 ATOM 2786 N N . ASP B 1 36 ? -36.416 0.666 -55.039 1.00 13.82 ? 62 ASP B N 1 ATOM 2787 C CA . ASP B 1 36 ? -35.304 0.037 -54.334 1.00 12.17 ? 62 ASP B CA 1 ATOM 2788 C C . ASP B 1 36 ? -35.574 -1.445 -54.068 1.00 13.40 ? 62 ASP B C 1 ATOM 2789 O O . ASP B 1 36 ? -34.660 -2.261 -54.167 1.00 12.51 ? 62 ASP B O 1 ATOM 2790 C CB . ASP B 1 36 ? -35.004 0.767 -53.012 1.00 16.38 ? 62 ASP B CB 1 ATOM 2791 C CG . ASP B 1 36 ? -34.389 2.143 -53.230 1.00 24.26 ? 62 ASP B CG 1 ATOM 2792 O OD1 . ASP B 1 36 ? -34.091 2.474 -54.398 1.00 19.60 ? 62 ASP B OD1 1 ATOM 2793 O OD2 . ASP B 1 36 ? -34.193 2.888 -52.240 1.00 17.73 ? 62 ASP B OD2 1 ATOM 2794 N N . VAL B 1 37 ? -36.822 -1.794 -53.742 1.00 15.34 ? 63 VAL B N 1 ATOM 2795 C CA . VAL B 1 37 ? -37.170 -3.191 -53.482 1.00 16.90 ? 63 VAL B CA 1 ATOM 2796 C C . VAL B 1 37 ? -36.928 -4.068 -54.721 1.00 17.70 ? 63 VAL B C 1 ATOM 2797 O O . VAL B 1 37 ? -36.314 -5.132 -54.637 1.00 17.00 ? 63 VAL B O 1 ATOM 2798 C CB . VAL B 1 37 ? -38.647 -3.342 -53.044 1.00 20.38 ? 63 VAL B CB 1 ATOM 2799 C CG1 . VAL B 1 37 ? -39.050 -4.809 -53.013 1.00 20.76 ? 63 VAL B CG1 1 ATOM 2800 C CG2 . VAL B 1 37 ? -38.874 -2.687 -51.687 1.00 22.49 ? 63 VAL B CG2 1 ATOM 2801 N N . THR B 1 38 ? -37.416 -3.611 -55.869 1.00 11.22 ? 64 THR B N 1 ATOM 2802 C CA . THR B 1 38 ? -37.235 -4.342 -57.117 1.00 12.73 ? 64 THR B CA 1 ATOM 2803 C C . THR B 1 38 ? -35.755 -4.409 -57.506 1.00 14.90 ? 64 THR B C 1 ATOM 2804 O O . THR B 1 38 ? -35.295 -5.416 -58.045 1.00 13.26 ? 64 THR B O 1 ATOM 2805 C CB . THR B 1 38 ? -38.044 -3.705 -58.252 1.00 16.70 ? 64 THR B CB 1 ATOM 2806 O OG1 . THR B 1 38 ? -39.425 -3.637 -57.863 1.00 17.26 ? 64 THR B OG1 1 ATOM 2807 C CG2 . THR B 1 38 ? -37.906 -4.514 -59.535 1.00 19.81 ? 64 THR B CG2 1 ATOM 2808 N N . ALA B 1 39 ? -35.004 -3.352 -57.211 1.00 14.84 ? 65 ALA B N 1 ATOM 2809 C CA . ALA B 1 39 ? -33.565 -3.370 -57.476 1.00 13.78 ? 65 ALA B CA 1 ATOM 2810 C C . ALA B 1 39 ? -32.907 -4.516 -56.714 1.00 16.40 ? 65 ALA B C 1 ATOM 2811 O O . ALA B 1 39 ? -32.152 -5.300 -57.288 1.00 17.12 ? 65 ALA B O 1 ATOM 2812 C CB . ALA B 1 39 ? -32.926 -2.042 -57.089 1.00 14.51 ? 65 ALA B CB 1 ATOM 2813 N N . VAL B 1 40 ? -33.229 -4.634 -55.425 1.00 12.32 ? 66 VAL B N 1 ATOM 2814 C CA . VAL B 1 40 ? -32.611 -5.649 -54.580 1.00 15.61 ? 66 VAL B CA 1 ATOM 2815 C C . VAL B 1 40 ? -33.056 -7.059 -54.949 1.00 12.23 ? 66 VAL B C 1 ATOM 2816 O O . VAL B 1 40 ? -32.234 -7.976 -55.005 1.00 18.63 ? 66 VAL B O 1 ATOM 2817 C CB . VAL B 1 40 ? -32.913 -5.404 -53.085 1.00 22.78 ? 66 VAL B CB 1 ATOM 2818 C CG1 . VAL B 1 40 ? -32.468 -6.598 -52.244 1.00 25.16 ? 66 VAL B CG1 1 ATOM 2819 C CG2 . VAL B 1 40 ? -32.218 -4.141 -52.618 1.00 23.01 ? 66 VAL B CG2 1 ATOM 2820 N N . LEU B 1 41 ? -34.353 -7.243 -55.192 1.00 11.41 ? 67 LEU B N 1 ATOM 2821 C CA . LEU B 1 41 ? -34.867 -8.574 -55.530 1.00 13.41 ? 67 LEU B CA 1 ATOM 2822 C C . LEU B 1 41 ? -34.477 -9.077 -56.917 1.00 16.35 ? 67 LEU B C 1 ATOM 2823 O O . LEU B 1 41 ? -34.215 -10.269 -57.103 1.00 19.52 ? 67 LEU B O 1 ATOM 2824 C CB . LEU B 1 41 ? -36.395 -8.591 -55.411 1.00 17.44 ? 67 LEU B CB 1 ATOM 2825 C CG . LEU B 1 41 ? -36.863 -8.320 -53.975 1.00 24.44 ? 67 LEU B CG 1 ATOM 2826 C CD1 . LEU B 1 41 ? -38.375 -8.431 -53.860 1.00 23.52 ? 67 LEU B CD1 1 ATOM 2827 C CD2 . LEU B 1 41 ? -36.166 -9.252 -52.990 1.00 29.50 ? 67 LEU B CD2 1 ATOM 2828 N N . GLN B 1 42 ? -34.452 -8.184 -57.901 1.00 13.64 ? 68 GLN B N 1 ATOM 2829 C CA . GLN B 1 42 ? -34.355 -8.637 -59.275 1.00 13.04 ? 68 GLN B CA 1 ATOM 2830 C C . GLN B 1 42 ? -32.965 -8.516 -59.894 1.00 19.39 ? 68 GLN B C 1 ATOM 2831 O O . GLN B 1 42 ? -32.622 -9.286 -60.785 1.00 13.31 ? 68 GLN B O 1 ATOM 2832 C CB . GLN B 1 42 ? -35.363 -7.880 -60.155 1.00 10.83 ? 68 GLN B CB 1 ATOM 2833 C CG . GLN B 1 42 ? -36.838 -8.274 -59.892 1.00 13.42 ? 68 GLN B CG 1 ATOM 2834 C CD . GLN B 1 42 ? -37.156 -9.700 -60.304 1.00 16.80 ? 68 GLN B CD 1 ATOM 2835 O OE1 . GLN B 1 42 ? -36.459 -10.288 -61.123 1.00 16.65 ? 68 GLN B OE1 1 ATOM 2836 N NE2 . GLN B 1 42 ? -38.227 -10.255 -59.748 1.00 18.21 ? 68 GLN B NE2 1 ATOM 2837 N N . PHE B 1 43 ? -32.169 -7.560 -59.428 1.00 11.26 ? 69 PHE B N 1 ATOM 2838 C CA . PHE B 1 43 ? -30.943 -7.205 -60.133 1.00 9.61 ? 69 PHE B CA 1 ATOM 2839 C C . PHE B 1 43 ? -29.713 -7.444 -59.277 1.00 10.49 ? 69 PHE B C 1 ATOM 2840 O O . PHE B 1 43 ? -29.795 -7.403 -58.052 1.00 11.58 ? 69 PHE B O 1 ATOM 2841 C CB . PHE B 1 43 ? -30.990 -5.736 -60.566 1.00 11.14 ? 69 PHE B CB 1 ATOM 2842 C CG . PHE B 1 43 ? -32.056 -5.439 -61.572 1.00 16.20 ? 69 PHE B CG 1 ATOM 2843 C CD1 . PHE B 1 43 ? -33.356 -5.144 -61.160 1.00 17.00 ? 69 PHE B CD1 1 ATOM 2844 C CD2 . PHE B 1 43 ? -31.776 -5.478 -62.932 1.00 13.39 ? 69 PHE B CD2 1 ATOM 2845 C CE1 . PHE B 1 43 ? -34.354 -4.887 -62.088 1.00 10.41 ? 69 PHE B CE1 1 ATOM 2846 C CE2 . PHE B 1 43 ? -32.772 -5.211 -63.882 1.00 12.49 ? 69 PHE B CE2 1 ATOM 2847 C CZ . PHE B 1 43 ? -34.069 -4.912 -63.454 1.00 9.36 ? 69 PHE B CZ 1 ATOM 2848 N N . ASN B 1 44 ? -28.566 -7.682 -59.912 1.00 11.44 ? 70 ASN B N 1 ATOM 2849 C CA . ASN B 1 44 ? -27.333 -7.777 -59.141 1.00 9.28 ? 70 ASN B CA 1 ATOM 2850 C C . ASN B 1 44 ? -26.159 -7.085 -59.814 1.00 12.12 ? 70 ASN B C 1 ATOM 2851 O O . ASN B 1 44 ? -24.999 -7.462 -59.616 1.00 11.86 ? 70 ASN B O 1 ATOM 2852 C CB . ASN B 1 44 ? -26.983 -9.242 -58.827 1.00 12.12 ? 70 ASN B CB 1 ATOM 2853 C CG . ASN B 1 44 ? -26.723 -10.081 -60.071 1.00 15.56 ? 70 ASN B CG 1 ATOM 2854 O OD1 . ASN B 1 44 ? -26.955 -9.650 -61.193 1.00 16.69 ? 70 ASN B OD1 1 ATOM 2855 N ND2 . ASN B 1 44 ? -26.259 -11.313 -59.858 1.00 21.52 ? 70 ASN B ND2 1 ATOM 2856 N N . GLY B 1 45 ? -26.475 -6.068 -60.604 1.00 10.85 ? 71 GLY B N 1 ATOM 2857 C CA . GLY B 1 45 ? -25.483 -5.179 -61.181 1.00 14.84 ? 71 GLY B CA 1 ATOM 2858 C C . GLY B 1 45 ? -26.077 -3.782 -61.243 1.00 10.37 ? 71 GLY B C 1 ATOM 2859 O O . GLY B 1 45 ? -27.297 -3.630 -61.247 1.00 9.45 ? 71 GLY B O 1 ATOM 2860 N N . ALA B 1 46 ? -25.231 -2.757 -61.266 1.00 8.83 ? 72 ALA B N 1 ATOM 2861 C CA . ALA B 1 46 ? -25.729 -1.397 -61.389 1.00 7.89 ? 72 ALA B CA 1 ATOM 2862 C C . ALA B 1 46 ? -24.756 -0.503 -62.145 1.00 11.66 ? 72 ALA B C 1 ATOM 2863 O O . ALA B 1 46 ? -23.545 -0.723 -62.139 1.00 10.86 ? 72 ALA B O 1 ATOM 2864 C CB . ALA B 1 46 ? -25.997 -0.804 -60.024 1.00 11.17 ? 72 ALA B CB 1 ATOM 2865 N N . THR B 1 47 ? -25.329 0.512 -62.766 1.00 8.02 ? 73 THR B N 1 ATOM 2866 C CA . THR B 1 47 ? -24.624 1.555 -63.477 1.00 8.34 ? 73 THR B CA 1 ATOM 2867 C C . THR B 1 47 ? -25.264 2.858 -63.020 1.00 10.67 ? 73 THR B C 1 ATOM 2868 O O . THR B 1 47 ? -26.487 2.974 -63.063 1.00 12.41 ? 73 THR B O 1 ATOM 2869 C CB . THR B 1 47 ? -24.775 1.392 -65.014 1.00 13.92 ? 73 THR B CB 1 ATOM 2870 O OG1 . THR B 1 47 ? -24.289 0.096 -65.412 1.00 15.24 ? 73 THR B OG1 1 ATOM 2871 C CG2 . THR B 1 47 ? -24.022 2.483 -65.757 1.00 10.90 ? 73 THR B CG2 1 ATOM 2872 N N . PRO B 1 48 ? -24.469 3.830 -62.559 1.00 14.20 ? 74 PRO B N 1 ATOM 2873 C CA . PRO B 1 48 ? -25.111 5.112 -62.213 1.00 12.78 ? 74 PRO B CA 1 ATOM 2874 C C . PRO B 1 48 ? -25.667 5.786 -63.451 1.00 9.56 ? 74 PRO B C 1 ATOM 2875 O O . PRO B 1 48 ? -24.966 5.960 -64.438 1.00 11.68 ? 74 PRO B O 1 ATOM 2876 C CB . PRO B 1 48 ? -23.971 5.934 -61.595 1.00 12.13 ? 74 PRO B CB 1 ATOM 2877 C CG . PRO B 1 48 ? -22.728 5.331 -62.188 1.00 22.31 ? 74 PRO B CG 1 ATOM 2878 C CD . PRO B 1 48 ? -23.020 3.856 -62.318 1.00 19.15 ? 74 PRO B CD 1 ATOM 2879 N N . GLU B 1 49 ? -26.931 6.180 -63.388 1.00 9.76 ? 75 GLU B N 1 ATOM 2880 C CA . GLU B 1 49 ? -27.608 6.691 -64.558 1.00 12.24 ? 75 GLU B CA 1 ATOM 2881 C C . GLU B 1 49 ? -27.017 8.026 -65.046 1.00 21.88 ? 75 GLU B C 1 ATOM 2882 O O . GLU B 1 49 ? -26.909 8.254 -66.245 1.00 17.54 ? 75 GLU B O 1 ATOM 2883 C CB . GLU B 1 49 ? -29.107 6.831 -64.248 1.00 12.82 ? 75 GLU B CB 1 ATOM 2884 C CG . GLU B 1 49 ? -29.959 7.225 -65.434 1.00 20.44 ? 75 GLU B CG 1 ATOM 2885 C CD . GLU B 1 49 ? -31.401 7.461 -65.017 1.00 34.88 ? 75 GLU B CD 1 ATOM 2886 O OE1 . GLU B 1 49 ? -31.807 6.928 -63.957 1.00 29.63 ? 75 GLU B OE1 1 ATOM 2887 O OE2 . GLU B 1 49 ? -32.112 8.193 -65.728 1.00 35.90 ? 75 GLU B OE2 1 ATOM 2888 N N . ASN B 1 50 ? -26.604 8.895 -64.127 1.00 11.38 ? 76 ASN B N 1 ATOM 2889 C CA . ASN B 1 50 ? -26.092 10.208 -64.526 1.00 19.57 ? 76 ASN B CA 1 ATOM 2890 C C . ASN B 1 50 ? -24.941 10.731 -63.695 1.00 15.82 ? 76 ASN B C 1 ATOM 2891 O O . ASN B 1 50 ? -24.143 11.517 -64.184 1.00 16.72 ? 76 ASN B O 1 ATOM 2892 C CB . ASN B 1 50 ? -27.195 11.268 -64.462 1.00 13.17 ? 76 ASN B CB 1 ATOM 2893 C CG . ASN B 1 50 ? -28.268 11.050 -65.493 1.00 22.03 ? 76 ASN B CG 1 ATOM 2894 O OD1 . ASN B 1 50 ? -28.012 11.158 -66.686 1.00 23.68 ? 76 ASN B OD1 1 ATOM 2895 N ND2 . ASN B 1 50 ? -29.482 10.762 -65.042 1.00 21.06 ? 76 ASN B ND2 1 ATOM 2896 N N . GLU B 1 51 ? -24.885 10.328 -62.425 1.00 12.19 ? 77 GLU B N 1 ATOM 2897 C CA . GLU B 1 51 ? -24.123 11.096 -61.434 1.00 19.39 ? 77 GLU B CA 1 ATOM 2898 C C . GLU B 1 51 ? -22.603 10.950 -61.518 1.00 15.49 ? 77 GLU B C 1 ATOM 2899 O O . GLU B 1 51 ? -21.879 11.669 -60.829 1.00 14.59 ? 77 GLU B O 1 ATOM 2900 C CB . GLU B 1 51 ? -24.595 10.732 -60.020 1.00 31.02 ? 77 GLU B CB 1 ATOM 2901 C CG . GLU B 1 51 ? -26.063 11.092 -59.750 1.00 46.21 ? 77 GLU B CG 1 ATOM 2902 C CD . GLU B 1 51 ? -26.298 12.574 -59.459 1.00 57.01 ? 77 GLU B CD 1 ATOM 2903 O OE1 . GLU B 1 51 ? -25.310 13.341 -59.391 1.00 59.58 ? 77 GLU B OE1 1 ATOM 2904 O OE2 . GLU B 1 51 ? -27.480 12.965 -59.283 1.00 51.57 ? 77 GLU B OE2 1 ATOM 2905 N N . MET B 1 52 ? -22.110 10.042 -62.355 1.00 18.05 ? 78 MET B N 1 ATOM 2906 C CA . MET B 1 52 ? -20.671 9.967 -62.575 1.00 16.74 ? 78 MET B CA 1 ATOM 2907 C C . MET B 1 52 ? -20.267 10.658 -63.880 1.00 19.55 ? 78 MET B C 1 ATOM 2908 O O . MET B 1 52 ? -19.088 10.718 -64.211 1.00 21.94 ? 78 MET B O 1 ATOM 2909 C CB . MET B 1 52 ? -20.182 8.517 -62.582 1.00 21.86 ? 78 MET B CB 1 ATOM 2910 C CG . MET B 1 52 ? -20.034 7.899 -61.194 1.00 23.27 ? 78 MET B CG 1 ATOM 2911 S SD . MET B 1 52 ? -19.231 6.284 -61.284 1.00 27.17 ? 78 MET B SD 1 ATOM 2912 C CE . MET B 1 52 ? -19.702 5.568 -59.693 1.00 16.97 ? 78 MET B CE 1 ATOM 2913 N N . LYS B 1 53 ? -21.238 11.193 -64.612 1.00 13.40 ? 79 LYS B N 1 ATOM 2914 C CA . LYS B 1 53 ? -20.927 11.959 -65.832 1.00 20.13 ? 79 LYS B CA 1 ATOM 2915 C C . LYS B 1 53 ? -20.272 13.316 -65.509 1.00 20.75 ? 79 LYS B C 1 ATOM 2916 O O . LYS B 1 53 ? -20.438 13.851 -64.413 1.00 16.68 ? 79 LYS B O 1 ATOM 2917 C CB . LYS B 1 53 ? -22.186 12.156 -66.672 1.00 17.05 ? 79 LYS B CB 1 ATOM 2918 C CG . LYS B 1 53 ? -22.745 10.840 -67.203 1.00 20.66 ? 79 LYS B CG 1 ATOM 2919 C CD . LYS B 1 53 ? -24.127 10.988 -67.791 1.00 30.78 ? 79 LYS B CD 1 ATOM 2920 C CE . LYS B 1 53 ? -24.672 9.631 -68.250 1.00 23.55 ? 79 LYS B CE 1 ATOM 2921 N NZ . LYS B 1 53 ? -26.118 9.733 -68.644 1.00 22.46 ? 79 LYS B NZ 1 ATOM 2922 N N . TRP B 1 54 ? -19.528 13.854 -66.478 1.00 18.45 ? 80 TRP B N 1 ATOM 2923 C CA . TRP B 1 54 ? -18.604 14.972 -66.255 1.00 25.16 ? 80 TRP B CA 1 ATOM 2924 C C . TRP B 1 54 ? -19.269 16.210 -65.627 1.00 20.08 ? 80 TRP B C 1 ATOM 2925 O O . TRP B 1 54 ? -18.750 16.788 -64.671 1.00 19.25 ? 80 TRP B O 1 ATOM 2926 C CB . TRP B 1 54 ? -17.931 15.343 -67.587 1.00 21.29 ? 80 TRP B CB 1 ATOM 2927 C CG . TRP B 1 54 ? -16.649 16.130 -67.445 1.00 20.15 ? 80 TRP B CG 1 ATOM 2928 C CD1 . TRP B 1 54 ? -16.438 17.208 -66.638 1.00 20.93 ? 80 TRP B CD1 1 ATOM 2929 C CD2 . TRP B 1 54 ? -15.416 15.912 -68.153 1.00 23.81 ? 80 TRP B CD2 1 ATOM 2930 N NE1 . TRP B 1 54 ? -15.155 17.668 -66.788 1.00 26.37 ? 80 TRP B NE1 1 ATOM 2931 C CE2 . TRP B 1 54 ? -14.505 16.892 -67.712 1.00 26.07 ? 80 TRP B CE2 1 ATOM 2932 C CE3 . TRP B 1 54 ? -14.995 14.981 -69.113 1.00 23.69 ? 80 TRP B CE3 1 ATOM 2933 C CZ2 . TRP B 1 54 ? -13.192 16.977 -68.200 1.00 24.56 ? 80 TRP B CZ2 1 ATOM 2934 C CZ3 . TRP B 1 54 ? -13.683 15.063 -69.598 1.00 23.42 ? 80 TRP B CZ3 1 ATOM 2935 C CH2 . TRP B 1 54 ? -12.804 16.057 -69.140 1.00 26.06 ? 80 TRP B CH2 1 ATOM 2936 N N . ALA B 1 55 ? -20.419 16.598 -66.167 1.00 21.15 ? 81 ALA B N 1 ATOM 2937 C CA . ALA B 1 55 ? -21.163 17.771 -65.707 1.00 23.11 ? 81 ALA B CA 1 ATOM 2938 C C . ALA B 1 55 ? -21.489 17.728 -64.209 1.00 25.59 ? 81 ALA B C 1 ATOM 2939 O O . ALA B 1 55 ? -21.568 18.773 -63.560 1.00 21.27 ? 81 ALA B O 1 ATOM 2940 C CB . ALA B 1 55 ? -22.452 17.915 -66.511 1.00 20.23 ? 81 ALA B CB 1 ATOM 2941 N N . TYR B 1 56 ? -21.691 16.526 -63.666 1.00 17.69 ? 82 TYR B N 1 ATOM 2942 C CA . TYR B 1 56 ? -22.025 16.379 -62.246 1.00 17.08 ? 82 TYR B CA 1 ATOM 2943 C C . TYR B 1 56 ? -20.787 16.198 -61.376 1.00 18.45 ? 82 TYR B C 1 ATOM 2944 O O . TYR B 1 56 ? -20.676 16.756 -60.283 1.00 18.77 ? 82 TYR B O 1 ATOM 2945 C CB . TYR B 1 56 ? -22.930 15.175 -62.017 1.00 20.31 ? 82 TYR B CB 1 ATOM 2946 C CG . TYR B 1 56 ? -24.292 15.242 -62.641 1.00 23.93 ? 82 TYR B CG 1 ATOM 2947 C CD1 . TYR B 1 56 ? -24.474 14.984 -63.998 1.00 23.18 ? 82 TYR B CD1 1 ATOM 2948 C CD2 . TYR B 1 56 ? -25.412 15.500 -61.864 1.00 29.77 ? 82 TYR B CD2 1 ATOM 2949 C CE1 . TYR B 1 56 ? -25.735 15.015 -64.569 1.00 27.27 ? 82 TYR B CE1 1 ATOM 2950 C CE2 . TYR B 1 56 ? -26.676 15.532 -62.421 1.00 41.30 ? 82 TYR B CE2 1 ATOM 2951 C CZ . TYR B 1 56 ? -26.833 15.289 -63.774 1.00 42.44 ? 82 TYR B CZ 1 ATOM 2952 O OH . TYR B 1 56 ? -28.094 15.330 -64.328 1.00 47.95 ? 82 TYR B OH 1 ATOM 2953 N N . ILE B 1 57 ? -19.856 15.388 -61.856 1.00 17.09 ? 83 ILE B N 1 ATOM 2954 C CA . ILE B 1 57 ? -18.767 14.953 -60.993 1.00 19.20 ? 83 ILE B CA 1 ATOM 2955 C C . ILE B 1 57 ? -17.592 15.940 -60.996 1.00 18.43 ? 83 ILE B C 1 ATOM 2956 O O . ILE B 1 57 ? -16.849 16.003 -60.024 1.00 18.80 ? 83 ILE B O 1 ATOM 2957 C CB . ILE B 1 57 ? -18.304 13.533 -61.391 1.00 16.82 ? 83 ILE B CB 1 ATOM 2958 C CG1 . ILE B 1 57 ? -17.551 12.862 -60.235 1.00 21.56 ? 83 ILE B CG1 1 ATOM 2959 C CG2 . ILE B 1 57 ? -17.513 13.560 -62.698 1.00 15.58 ? 83 ILE B CG2 1 ATOM 2960 C CD1 . ILE B 1 57 ? -17.564 11.337 -60.322 1.00 15.33 ? 83 ILE B CD1 1 ATOM 2961 N N . GLU B 1 58 ? -17.432 16.720 -62.067 1.00 19.13 ? 84 GLU B N 1 ATOM 2962 C CA . GLU B 1 58 ? -16.466 17.833 -62.065 1.00 20.92 ? 84 GLU B CA 1 ATOM 2963 C C . GLU B 1 58 ? -17.105 19.109 -62.619 1.00 24.94 ? 84 GLU B C 1 ATOM 2964 O O . GLU B 1 58 ? -16.798 19.534 -63.743 1.00 25.34 ? 84 GLU B O 1 ATOM 2965 C CB . GLU B 1 58 ? -15.202 17.493 -62.869 1.00 20.14 ? 84 GLU B CB 1 ATOM 2966 C CG . GLU B 1 58 ? -14.041 18.471 -62.588 1.00 21.59 ? 84 GLU B CG 1 ATOM 2967 C CD . GLU B 1 58 ? -12.828 18.272 -63.488 1.00 22.96 ? 84 GLU B CD 1 ATOM 2968 O OE1 . GLU B 1 58 ? -12.820 17.326 -64.306 1.00 27.88 ? 84 GLU B OE1 1 ATOM 2969 O OE2 . GLU B 1 58 ? -11.876 19.071 -63.385 1.00 26.90 ? 84 GLU B OE2 1 ATOM 2970 N N . PRO B 1 59 ? -18.000 19.731 -61.828 1.00 27.82 ? 85 PRO B N 1 ATOM 2971 C CA . PRO B 1 59 ? -18.806 20.861 -62.320 1.00 25.84 ? 85 PRO B CA 1 ATOM 2972 C C . PRO B 1 59 ? -18.003 22.136 -62.551 1.00 27.15 ? 85 PRO B C 1 ATOM 2973 O O . PRO B 1 59 ? -18.429 22.989 -63.325 1.00 33.10 ? 85 PRO B O 1 ATOM 2974 C CB . PRO B 1 59 ? -19.845 21.065 -61.208 1.00 25.35 ? 85 PRO B CB 1 ATOM 2975 C CG . PRO B 1 59 ? -19.226 20.486 -59.980 1.00 24.63 ? 85 PRO B CG 1 ATOM 2976 C CD . PRO B 1 59 ? -18.372 19.332 -60.455 1.00 24.15 ? 85 PRO B CD 1 ATOM 2977 N N . GLU B 1 60 ? -16.873 22.270 -61.868 1.00 29.05 ? 86 GLU B N 1 ATOM 2978 C CA . GLU B 1 60 ? -15.929 23.353 -62.140 1.00 36.68 ? 86 GLU B CA 1 ATOM 2979 C C . GLU B 1 60 ? -14.542 22.746 -62.215 1.00 31.77 ? 86 GLU B C 1 ATOM 2980 O O . GLU B 1 60 ? -14.312 21.680 -61.662 1.00 24.93 ? 86 GLU B O 1 ATOM 2981 C CB . GLU B 1 60 ? -16.003 24.440 -61.072 1.00 39.41 ? 86 GLU B CB 1 ATOM 2982 C CG . GLU B 1 60 ? -17.326 25.190 -61.077 1.00 57.16 ? 86 GLU B CG 1 ATOM 2983 C CD . GLU B 1 60 ? -17.421 26.228 -59.973 1.00 75.47 ? 86 GLU B CD 1 ATOM 2984 O OE1 . GLU B 1 60 ? -16.545 26.234 -59.078 1.00 78.63 ? 86 GLU B OE1 1 ATOM 2985 O OE2 . GLU B 1 60 ? -18.370 27.043 -60.004 1.00 83.19 ? 86 GLU B OE2 1 ATOM 2986 N N . ARG B 1 61 ? -13.620 23.400 -62.911 1.00 29.50 ? 87 ARG B N 1 ATOM 2987 C CA . ARG B 1 61 ? -12.331 22.777 -63.186 1.00 27.84 ? 87 ARG B CA 1 ATOM 2988 C C . ARG B 1 61 ? -11.583 22.398 -61.907 1.00 38.11 ? 87 ARG B C 1 ATOM 2989 O O . ARG B 1 61 ? -11.412 23.216 -61.008 1.00 28.10 ? 87 ARG B O 1 ATOM 2990 C CB . ARG B 1 61 ? -11.465 23.687 -64.049 1.00 32.90 ? 87 ARG B CB 1 ATOM 2991 C CG . ARG B 1 61 ? -10.213 23.005 -64.528 1.00 29.94 ? 87 ARG B CG 1 ATOM 2992 C CD . ARG B 1 61 ? -9.501 23.823 -65.583 1.00 32.05 ? 87 ARG B CD 1 ATOM 2993 N NE . ARG B 1 61 ? -8.358 23.087 -66.098 1.00 35.09 ? 87 ARG B NE 1 ATOM 2994 C CZ . ARG B 1 61 ? -7.595 23.489 -67.104 1.00 39.68 ? 87 ARG B CZ 1 ATOM 2995 N NH1 . ARG B 1 61 ? -7.845 24.642 -67.715 1.00 39.24 ? 87 ARG B NH1 1 ATOM 2996 N NH2 . ARG B 1 61 ? -6.581 22.731 -67.495 1.00 39.34 ? 87 ARG B NH2 1 ATOM 2997 N N . ASN B 1 62 ? -11.175 21.133 -61.842 1.00 27.36 ? 88 ASN B N 1 ATOM 2998 C CA . ASN B 1 62 ? -10.460 20.567 -60.698 1.00 31.48 ? 88 ASN B CA 1 ATOM 2999 C C . ASN B 1 62 ? -11.241 20.654 -59.384 1.00 26.19 ? 88 ASN B C 1 ATOM 3000 O O . ASN B 1 62 ? -10.668 20.538 -58.302 1.00 28.24 ? 88 ASN B O 1 ATOM 3001 C CB . ASN B 1 62 ? -9.094 21.236 -60.531 1.00 31.43 ? 88 ASN B CB 1 ATOM 3002 C CG . ASN B 1 62 ? -8.101 20.357 -59.780 1.00 37.40 ? 88 ASN B CG 1 ATOM 3003 O OD1 . ASN B 1 62 ? -8.114 19.130 -59.907 1.00 37.06 ? 88 ASN B OD1 1 ATOM 3004 N ND2 . ASN B 1 62 ? -7.240 20.983 -58.990 1.00 40.37 ? 88 ASN B ND2 1 ATOM 3005 N N . GLN B 1 63 ? -12.550 20.842 -59.478 1.00 25.01 ? 89 GLN B N 1 ATOM 3006 C CA . GLN B 1 63 ? -13.396 20.801 -58.292 1.00 25.67 ? 89 GLN B CA 1 ATOM 3007 C C . GLN B 1 63 ? -14.371 19.651 -58.452 1.00 32.50 ? 89 GLN B C 1 ATOM 3008 O O . GLN B 1 63 ? -15.311 19.721 -59.240 1.00 34.68 ? 89 GLN B O 1 ATOM 3009 C CB . GLN B 1 63 ? -14.121 22.126 -58.086 1.00 30.45 ? 89 GLN B CB 1 ATOM 3010 C CG . GLN B 1 63 ? -13.153 23.308 -57.941 1.00 39.46 ? 89 GLN B CG 1 ATOM 3011 C CD . GLN B 1 63 ? -13.855 24.607 -57.615 1.00 49.22 ? 89 GLN B CD 1 ATOM 3012 O OE1 . GLN B 1 63 ? -14.972 24.609 -57.091 1.00 50.18 ? 89 GLN B OE1 1 ATOM 3013 N NE2 . GLN B 1 63 ? -13.203 25.725 -57.923 1.00 55.92 ? 89 GLN B NE2 1 ATOM 3014 N N . PHE B 1 64 ? -14.132 18.582 -57.711 1.00 20.49 ? 90 PHE B N 1 ATOM 3015 C CA . PHE B 1 64 ? -14.869 17.347 -57.935 1.00 27.50 ? 90 PHE B CA 1 ATOM 3016 C C . PHE B 1 64 ? -16.003 17.167 -56.943 1.00 20.93 ? 90 PHE B C 1 ATOM 3017 O O . PHE B 1 64 ? -15.893 17.560 -55.784 1.00 23.21 ? 90 PHE B O 1 ATOM 3018 C CB . PHE B 1 64 ? -13.912 16.162 -57.881 1.00 18.23 ? 90 PHE B CB 1 ATOM 3019 C CG . PHE B 1 64 ? -12.963 16.132 -59.032 1.00 21.10 ? 90 PHE B CG 1 ATOM 3020 C CD1 . PHE B 1 64 ? -11.793 16.873 -58.999 1.00 20.14 ? 90 PHE B CD1 1 ATOM 3021 C CD2 . PHE B 1 64 ? -13.263 15.396 -60.171 1.00 22.58 ? 90 PHE B CD2 1 ATOM 3022 C CE1 . PHE B 1 64 ? -10.928 16.860 -60.068 1.00 20.86 ? 90 PHE B CE1 1 ATOM 3023 C CE2 . PHE B 1 64 ? -12.398 15.383 -61.247 1.00 22.23 ? 90 PHE B CE2 1 ATOM 3024 C CZ . PHE B 1 64 ? -11.232 16.112 -61.198 1.00 20.28 ? 90 PHE B CZ 1 ATOM 3025 N N . ASN B 1 65 ? -17.095 16.576 -57.410 1.00 17.47 ? 91 ASN B N 1 ATOM 3026 C CA . ASN B 1 65 ? -18.234 16.308 -56.544 1.00 16.75 ? 91 ASN B CA 1 ATOM 3027 C C . ASN B 1 65 ? -18.644 14.840 -56.632 1.00 15.34 ? 91 ASN B C 1 ATOM 3028 O O . ASN B 1 65 ? -19.386 14.440 -57.529 1.00 14.88 ? 91 ASN B O 1 ATOM 3029 C CB . ASN B 1 65 ? -19.398 17.221 -56.912 1.00 19.82 ? 91 ASN B CB 1 ATOM 3030 C CG . ASN B 1 65 ? -20.573 17.071 -55.972 1.00 21.98 ? 91 ASN B CG 1 ATOM 3031 O OD1 . ASN B 1 65 ? -20.533 16.297 -55.014 1.00 17.59 ? 91 ASN B OD1 1 ATOM 3032 N ND2 . ASN B 1 65 ? -21.626 17.822 -56.238 1.00 20.08 ? 91 ASN B ND2 1 ATOM 3033 N N . PHE B 1 66 ? -18.163 14.045 -55.681 1.00 14.78 ? 92 PHE B N 1 ATOM 3034 C CA . PHE B 1 66 ? -18.340 12.598 -55.745 1.00 13.63 ? 92 PHE B CA 1 ATOM 3035 C C . PHE B 1 66 ? -19.613 12.124 -55.060 1.00 14.53 ? 92 PHE B C 1 ATOM 3036 O O . PHE B 1 66 ? -19.908 10.931 -55.056 1.00 16.31 ? 92 PHE B O 1 ATOM 3037 C CB . PHE B 1 66 ? -17.129 11.896 -55.130 1.00 13.86 ? 92 PHE B CB 1 ATOM 3038 C CG . PHE B 1 66 ? -15.878 12.050 -55.945 1.00 16.16 ? 92 PHE B CG 1 ATOM 3039 C CD1 . PHE B 1 66 ? -15.764 11.421 -57.169 1.00 15.55 ? 92 PHE B CD1 1 ATOM 3040 C CD2 . PHE B 1 66 ? -14.834 12.845 -55.502 1.00 20.63 ? 92 PHE B CD2 1 ATOM 3041 C CE1 . PHE B 1 66 ? -14.622 11.577 -57.951 1.00 21.16 ? 92 PHE B CE1 1 ATOM 3042 C CE2 . PHE B 1 66 ? -13.685 12.989 -56.268 1.00 22.86 ? 92 PHE B CE2 1 ATOM 3043 C CZ . PHE B 1 66 ? -13.585 12.357 -57.491 1.00 20.59 ? 92 PHE B CZ 1 ATOM 3044 N N . THR B 1 67 ? -20.369 13.053 -54.494 1.00 13.61 ? 93 THR B N 1 ATOM 3045 C CA . THR B 1 67 ? -21.541 12.686 -53.688 1.00 13.28 ? 93 THR B CA 1 ATOM 3046 C C . THR B 1 67 ? -22.506 11.746 -54.428 1.00 12.46 ? 93 THR B C 1 ATOM 3047 O O . THR B 1 67 ? -22.862 10.692 -53.910 1.00 12.68 ? 93 THR B O 1 ATOM 3048 C CB . THR B 1 67 ? -22.297 13.946 -53.227 1.00 14.26 ? 93 THR B CB 1 ATOM 3049 O OG1 . THR B 1 67 ? -21.438 14.705 -52.370 1.00 19.63 ? 93 THR B OG1 1 ATOM 3050 C CG2 . THR B 1 67 ? -23.558 13.580 -52.462 1.00 14.08 ? 93 THR B CG2 1 ATOM 3051 N N . GLY B 1 68 ? -22.901 12.106 -55.646 1.00 12.60 ? 94 GLY B N 1 ATOM 3052 C CA . GLY B 1 68 ? -23.870 11.314 -56.385 1.00 12.45 ? 94 GLY B CA 1 ATOM 3053 C C . GLY B 1 68 ? -23.361 9.937 -56.771 1.00 15.94 ? 94 GLY B C 1 ATOM 3054 O O . GLY B 1 68 ? -24.068 8.939 -56.637 1.00 10.51 ? 94 GLY B O 1 ATOM 3055 N N . GLY B 1 69 ? -22.127 9.881 -57.256 1.00 11.15 ? 95 GLY B N 1 ATOM 3056 C CA . GLY B 1 69 ? -21.543 8.623 -57.669 1.00 10.53 ? 95 GLY B CA 1 ATOM 3057 C C . GLY B 1 69 ? -21.319 7.710 -56.476 1.00 13.98 ? 95 GLY B C 1 ATOM 3058 O O . GLY B 1 69 ? -21.500 6.497 -56.569 1.00 15.44 ? 95 GLY B O 1 ATOM 3059 N N . ASP B 1 70 ? -20.932 8.303 -55.353 1.00 10.53 ? 96 ASP B N 1 ATOM 3060 C CA . ASP B 1 70 ? -20.739 7.570 -54.105 1.00 11.66 ? 96 ASP B CA 1 ATOM 3061 C C . ASP B 1 70 ? -22.033 6.918 -53.594 1.00 15.62 ? 96 ASP B C 1 ATOM 3062 O O . ASP B 1 70 ? -21.991 5.821 -53.033 1.00 12.26 ? 96 ASP B O 1 ATOM 3063 C CB . ASP B 1 70 ? -20.162 8.488 -53.030 1.00 12.60 ? 96 ASP B CB 1 ATOM 3064 C CG . ASP B 1 70 ? -18.680 8.789 -53.253 1.00 21.46 ? 96 ASP B CG 1 ATOM 3065 O OD1 . ASP B 1 70 ? -18.099 8.253 -54.230 1.00 20.44 ? 96 ASP B OD1 1 ATOM 3066 O OD2 . ASP B 1 70 ? -18.101 9.558 -52.456 1.00 17.20 ? 96 ASP B OD2 1 ATOM 3067 N N . ILE B 1 71 ? -23.169 7.586 -53.779 1.00 11.24 ? 97 ILE B N 1 ATOM 3068 C CA . ILE B 1 71 ? -24.447 7.022 -53.338 1.00 9.96 ? 97 ILE B CA 1 ATOM 3069 C C . ILE B 1 71 ? -24.794 5.758 -54.142 1.00 12.66 ? 97 ILE B C 1 ATOM 3070 O O . ILE B 1 71 ? -25.197 4.731 -53.573 1.00 9.11 ? 97 ILE B O 1 ATOM 3071 C CB . ILE B 1 71 ? -25.592 8.058 -53.459 1.00 12.62 ? 97 ILE B CB 1 ATOM 3072 C CG1 . ILE B 1 71 ? -25.345 9.244 -52.511 1.00 14.29 ? 97 ILE B CG1 1 ATOM 3073 C CG2 . ILE B 1 71 ? -26.931 7.419 -53.165 1.00 11.59 ? 97 ILE B CG2 1 ATOM 3074 C CD1 . ILE B 1 71 ? -26.342 10.394 -52.665 1.00 11.99 ? 97 ILE B CD1 1 ATOM 3075 N N . VAL B 1 72 ? -24.640 5.824 -55.463 1.00 9.16 ? 98 VAL B N 1 ATOM 3076 C CA . VAL B 1 72 ? -24.915 4.652 -56.303 1.00 14.39 ? 98 VAL B CA 1 ATOM 3077 C C . VAL B 1 72 ? -23.931 3.532 -55.974 1.00 13.56 ? 98 VAL B C 1 ATOM 3078 O O . VAL B 1 72 ? -24.327 2.376 -55.825 1.00 9.04 ? 98 VAL B O 1 ATOM 3079 C CB . VAL B 1 72 ? -24.840 4.977 -57.817 1.00 15.09 ? 98 VAL B CB 1 ATOM 3080 C CG1 . VAL B 1 72 ? -24.980 3.700 -58.653 1.00 11.56 ? 98 VAL B CG1 1 ATOM 3081 C CG2 . VAL B 1 72 ? -25.928 5.952 -58.198 1.00 12.43 ? 98 VAL B CG2 1 ATOM 3082 N N . ALA B 1 73 ? -22.654 3.887 -55.844 1.00 8.65 ? 99 ALA B N 1 ATOM 3083 C CA . ALA B 1 73 ? -21.605 2.909 -55.544 1.00 18.54 ? 99 ALA B CA 1 ATOM 3084 C C . ALA B 1 73 ? -21.827 2.246 -54.181 1.00 14.13 ? 99 ALA B C 1 ATOM 3085 O O . ALA B 1 73 ? -21.618 1.040 -54.017 1.00 11.23 ? 99 ALA B O 1 ATOM 3086 C CB . ALA B 1 73 ? -20.225 3.570 -55.592 1.00 9.02 ? 99 ALA B CB 1 ATOM 3087 N N . ALA B 1 74 ? -22.268 3.023 -53.199 1.00 8.94 ? 100 ALA B N 1 ATOM 3088 C CA . ALA B 1 74 ? -22.551 2.458 -51.874 1.00 13.59 ? 100 ALA B CA 1 ATOM 3089 C C . ALA B 1 74 ? -23.753 1.493 -51.893 1.00 14.83 ? 100 ALA B C 1 ATOM 3090 O O . ALA B 1 74 ? -23.736 0.455 -51.226 1.00 11.26 ? 100 ALA B O 1 ATOM 3091 C CB . ALA B 1 74 ? -22.786 3.574 -50.859 1.00 12.70 ? 100 ALA B CB 1 ATOM 3092 N N . PHE B 1 75 ? -24.800 1.845 -52.630 1.00 8.90 ? 101 PHE B N 1 ATOM 3093 C CA . PHE B 1 75 ? -25.950 0.950 -52.786 1.00 12.25 ? 101 PHE B CA 1 ATOM 3094 C C . PHE B 1 75 ? -25.498 -0.366 -53.415 1.00 8.63 ? 101 PHE B C 1 ATOM 3095 O O . PHE B 1 75 ? -25.878 -1.459 -52.988 1.00 12.36 ? 101 PHE B O 1 ATOM 3096 C CB . PHE B 1 75 ? -27.022 1.602 -53.646 1.00 8.56 ? 101 PHE B CB 1 ATOM 3097 C CG . PHE B 1 75 ? -28.304 0.820 -53.709 1.00 12.05 ? 101 PHE B CG 1 ATOM 3098 C CD1 . PHE B 1 75 ? -29.246 0.939 -52.692 1.00 14.46 ? 101 PHE B CD1 1 ATOM 3099 C CD2 . PHE B 1 75 ? -28.558 -0.040 -54.765 1.00 15.09 ? 101 PHE B CD2 1 ATOM 3100 C CE1 . PHE B 1 75 ? -30.435 0.225 -52.737 1.00 18.30 ? 101 PHE B CE1 1 ATOM 3101 C CE2 . PHE B 1 75 ? -29.758 -0.771 -54.816 1.00 9.22 ? 101 PHE B CE2 1 ATOM 3102 C CZ . PHE B 1 75 ? -30.691 -0.622 -53.799 1.00 13.51 ? 101 PHE B CZ 1 ATOM 3103 N N . SER B 1 76 ? -24.665 -0.241 -54.433 1.00 8.84 ? 102 SER B N 1 ATOM 3104 C CA A SER B 1 76 ? -24.127 -1.401 -55.115 0.48 12.01 ? 102 SER B CA 1 ATOM 3105 C CA B SER B 1 76 ? -24.098 -1.382 -55.126 0.52 12.56 ? 102 SER B CA 1 ATOM 3106 C C . SER B 1 76 ? -23.262 -2.244 -54.172 1.00 12.48 ? 102 SER B C 1 ATOM 3107 O O . SER B 1 76 ? -23.402 -3.474 -54.127 1.00 13.53 ? 102 SER B O 1 ATOM 3108 C CB A SER B 1 76 ? -23.331 -0.956 -56.334 0.48 13.98 ? 102 SER B CB 1 ATOM 3109 C CB B SER B 1 76 ? -23.245 -0.899 -56.300 0.52 14.36 ? 102 SER B CB 1 ATOM 3110 O OG A SER B 1 76 ? -24.124 -0.087 -57.119 0.48 14.58 ? 102 SER B OG 1 ATOM 3111 O OG B SER B 1 76 ? -22.549 -1.970 -56.903 0.52 8.13 ? 102 SER B OG 1 ATOM 3112 N N . ALA B 1 77 ? -22.394 -1.595 -53.406 1.00 11.59 ? 103 ALA B N 1 ATOM 3113 C CA . ALA B 1 77 ? -21.518 -2.312 -52.464 1.00 13.45 ? 103 ALA B CA 1 ATOM 3114 C C . ALA B 1 77 ? -22.321 -3.062 -51.407 1.00 16.36 ? 103 ALA B C 1 ATOM 3115 O O . ALA B 1 77 ? -22.003 -4.209 -51.061 1.00 12.78 ? 103 ALA B O 1 ATOM 3116 C CB . ALA B 1 77 ? -20.543 -1.348 -51.769 1.00 11.00 ? 103 ALA B CB 1 ATOM 3117 N N . ALA B 1 78 ? -23.335 -2.393 -50.868 1.00 9.47 ? 104 ALA B N 1 ATOM 3118 C CA . ALA B 1 78 ? -24.153 -2.977 -49.808 1.00 11.02 ? 104 ALA B CA 1 ATOM 3119 C C . ALA B 1 78 ? -24.832 -4.255 -50.297 1.00 15.02 ? 104 ALA B C 1 ATOM 3120 O O . ALA B 1 78 ? -25.041 -5.182 -49.528 1.00 13.00 ? 104 ALA B O 1 ATOM 3121 C CB . ALA B 1 78 ? -25.210 -1.967 -49.307 1.00 14.49 ? 104 ALA B CB 1 ATOM 3122 N N . ASN B 1 79 ? -25.177 -4.280 -51.579 1.00 10.86 ? 105 ASN B N 1 ATOM 3123 C CA . ASN B 1 79 ? -25.884 -5.402 -52.173 1.00 12.82 ? 105 ASN B CA 1 ATOM 3124 C C . ASN B 1 79 ? -24.975 -6.404 -52.897 1.00 12.00 ? 105 ASN B C 1 ATOM 3125 O O . ASN B 1 79 ? -25.470 -7.346 -53.532 1.00 17.01 ? 105 ASN B O 1 ATOM 3126 C CB . ASN B 1 79 ? -26.940 -4.874 -53.146 1.00 14.34 ? 105 ASN B CB 1 ATOM 3127 C CG . ASN B 1 79 ? -28.151 -4.339 -52.431 1.00 21.07 ? 105 ASN B CG 1 ATOM 3128 O OD1 . ASN B 1 79 ? -28.974 -5.109 -51.945 1.00 19.25 ? 105 ASN B OD1 1 ATOM 3129 N ND2 . ASN B 1 79 ? -28.265 -3.016 -52.347 1.00 15.96 ? 105 ASN B ND2 1 ATOM 3130 N N . ASP B 1 80 ? -23.661 -6.196 -52.795 1.00 13.23 ? 106 ASP B N 1 ATOM 3131 C CA . ASP B 1 80 ? -22.660 -7.037 -53.469 1.00 14.89 ? 106 ASP B CA 1 ATOM 3132 C C . ASP B 1 80 ? -22.866 -7.075 -54.991 1.00 16.26 ? 106 ASP B C 1 ATOM 3133 O O . ASP B 1 80 ? -22.651 -8.107 -55.639 1.00 14.09 ? 106 ASP B O 1 ATOM 3134 C CB . ASP B 1 80 ? -22.694 -8.461 -52.891 1.00 29.62 ? 106 ASP B CB 1 ATOM 3135 C CG . ASP B 1 80 ? -21.318 -9.073 -52.778 1.00 57.07 ? 106 ASP B CG 1 ATOM 3136 O OD1 . ASP B 1 80 ? -20.411 -8.375 -52.280 1.00 72.52 ? 106 ASP B OD1 1 ATOM 3137 O OD2 . ASP B 1 80 ? -21.123 -10.230 -53.197 1.00 69.45 ? 106 ASP B OD2 1 ATOM 3138 N N . TYR B 1 81 ? -23.253 -5.935 -55.562 1.00 10.41 ? 107 TYR B N 1 ATOM 3139 C CA . TYR B 1 81 ? -23.483 -5.818 -57.009 1.00 11.27 ? 107 TYR B CA 1 ATOM 3140 C C . TYR B 1 81 ? -22.216 -5.811 -57.834 1.00 19.31 ? 107 TYR B C 1 ATOM 3141 O O . TYR B 1 81 ? -21.167 -5.400 -57.348 1.00 10.99 ? 107 TYR B O 1 ATOM 3142 C CB . TYR B 1 81 ? -24.203 -4.519 -57.338 1.00 9.58 ? 107 TYR B CB 1 ATOM 3143 C CG . TYR B 1 81 ? -25.705 -4.507 -57.156 1.00 12.34 ? 107 TYR B CG 1 ATOM 3144 C CD1 . TYR B 1 81 ? -26.399 -5.609 -56.667 1.00 10.86 ? 107 TYR B CD1 1 ATOM 3145 C CD2 . TYR B 1 81 ? -26.423 -3.380 -57.497 1.00 16.39 ? 107 TYR B CD2 1 ATOM 3146 C CE1 . TYR B 1 81 ? -27.794 -5.561 -56.527 1.00 13.39 ? 107 TYR B CE1 1 ATOM 3147 C CE2 . TYR B 1 81 ? -27.785 -3.325 -57.364 1.00 21.47 ? 107 TYR B CE2 1 ATOM 3148 C CZ . TYR B 1 81 ? -28.470 -4.407 -56.892 1.00 20.27 ? 107 TYR B CZ 1 ATOM 3149 O OH . TYR B 1 81 ? -29.841 -4.296 -56.789 1.00 22.92 ? 107 TYR B OH 1 ATOM 3150 N N . VAL B 1 82 ? -22.339 -6.184 -59.107 1.00 8.92 ? 108 VAL B N 1 ATOM 3151 C CA . VAL B 1 82 ? -21.328 -5.806 -60.103 1.00 15.69 ? 108 VAL B CA 1 ATOM 3152 C C . VAL B 1 82 ? -21.545 -4.349 -60.520 1.00 16.71 ? 108 VAL B C 1 ATOM 3153 O O . VAL B 1 82 ? -22.565 -4.013 -61.121 1.00 12.66 ? 108 VAL B O 1 ATOM 3154 C CB . VAL B 1 82 ? -21.379 -6.715 -61.351 1.00 13.83 ? 108 VAL B CB 1 ATOM 3155 C CG1 . VAL B 1 82 ? -20.301 -6.294 -62.363 1.00 13.00 ? 108 VAL B CG1 1 ATOM 3156 C CG2 . VAL B 1 82 ? -21.194 -8.164 -60.934 1.00 13.25 ? 108 VAL B CG2 1 ATOM 3157 N N . LEU B 1 83 ? -20.602 -3.477 -60.177 1.00 11.99 ? 109 LEU B N 1 ATOM 3158 C CA . LEU B 1 83 ? -20.752 -2.049 -60.444 1.00 8.47 ? 109 LEU B CA 1 ATOM 3159 C C . LEU B 1 83 ? -19.974 -1.594 -61.676 1.00 10.77 ? 109 LEU B C 1 ATOM 3160 O O . LEU B 1 83 ? -18.766 -1.833 -61.785 1.00 12.79 ? 109 LEU B O 1 ATOM 3161 C CB . LEU B 1 83 ? -20.293 -1.234 -59.227 1.00 13.05 ? 109 LEU B CB 1 ATOM 3162 C CG . LEU B 1 83 ? -20.315 0.294 -59.362 1.00 12.40 ? 109 LEU B CG 1 ATOM 3163 C CD1 . LEU B 1 83 ? -21.743 0.807 -59.580 1.00 11.68 ? 109 LEU B CD1 1 ATOM 3164 C CD2 . LEU B 1 83 ? -19.705 0.930 -58.090 1.00 13.78 ? 109 LEU B CD2 1 ATOM 3165 N N . ARG B 1 84 ? -20.666 -0.932 -62.590 1.00 9.26 ? 110 ARG B N 1 ATOM 3166 C CA . ARG B 1 84 ? -20.033 -0.366 -63.781 1.00 12.13 ? 110 ARG B CA 1 ATOM 3167 C C . ARG B 1 84 ? -19.932 1.165 -63.661 1.00 14.87 ? 110 ARG B C 1 ATOM 3168 O O . ARG B 1 84 ? -20.922 1.839 -63.414 1.00 14.92 ? 110 ARG B O 1 ATOM 3169 C CB . ARG B 1 84 ? -20.808 -0.738 -65.055 1.00 13.31 ? 110 ARG B CB 1 ATOM 3170 C CG . ARG B 1 84 ? -20.971 -2.248 -65.334 1.00 22.87 ? 110 ARG B CG 1 ATOM 3171 C CD . ARG B 1 84 ? -21.621 -2.530 -66.736 1.00 19.11 ? 110 ARG B CD 1 ATOM 3172 N NE . ARG B 1 84 ? -20.610 -2.506 -67.795 1.00 15.48 ? 110 ARG B NE 1 ATOM 3173 C CZ . ARG B 1 84 ? -20.343 -1.461 -68.573 1.00 22.83 ? 110 ARG B CZ 1 ATOM 3174 N NH1 . ARG B 1 84 ? -21.051 -0.336 -68.466 1.00 19.13 ? 110 ARG B NH1 1 ATOM 3175 N NH2 . ARG B 1 84 ? -19.365 -1.548 -69.475 1.00 19.14 ? 110 ARG B NH2 1 ATOM 3176 N N . GLY B 1 85 ? -18.728 1.703 -63.821 1.00 11.27 ? 111 GLY B N 1 ATOM 3177 C CA . GLY B 1 85 ? -18.537 3.139 -63.822 1.00 10.98 ? 111 GLY B CA 1 ATOM 3178 C C . GLY B 1 85 ? -18.839 3.681 -65.202 1.00 20.02 ? 111 GLY B C 1 ATOM 3179 O O . GLY B 1 85 ? -18.474 3.077 -66.201 1.00 19.60 ? 111 GLY B O 1 ATOM 3180 N N . HIS B 1 86 ? -19.490 4.836 -65.254 1.00 19.19 ? 112 HIS B N 1 ATOM 3181 C CA . HIS B 1 86 ? -20.053 5.328 -66.493 1.00 22.53 ? 112 HIS B CA 1 ATOM 3182 C C . HIS B 1 86 ? -20.374 6.819 -66.343 1.00 19.25 ? 112 HIS B C 1 ATOM 3183 O O . HIS B 1 86 ? -21.141 7.192 -65.461 1.00 20.43 ? 112 HIS B O 1 ATOM 3184 C CB . HIS B 1 86 ? -21.297 4.488 -66.823 1.00 24.17 ? 112 HIS B CB 1 ATOM 3185 C CG . HIS B 1 86 ? -22.199 5.076 -67.861 1.00 25.62 ? 112 HIS B CG 1 ATOM 3186 N ND1 . HIS B 1 86 ? -22.129 4.727 -69.193 1.00 33.91 ? 112 HIS B ND1 1 ATOM 3187 C CD2 . HIS B 1 86 ? -23.232 5.944 -67.754 1.00 31.31 ? 112 HIS B CD2 1 ATOM 3188 C CE1 . HIS B 1 86 ? -23.061 5.381 -69.867 1.00 32.28 ? 112 HIS B CE1 1 ATOM 3189 N NE2 . HIS B 1 86 ? -23.743 6.126 -69.017 1.00 33.03 ? 112 HIS B NE2 1 ATOM 3190 N N . ASN B 1 87 ? -19.743 7.686 -67.131 1.00 17.74 ? 113 ASN B N 1 ATOM 3191 C CA . ASN B 1 87 ? -18.639 7.362 -68.029 1.00 23.71 ? 113 ASN B CA 1 ATOM 3192 C C . ASN B 1 87 ? -17.640 8.515 -67.968 1.00 21.78 ? 113 ASN B C 1 ATOM 3193 O O . ASN B 1 87 ? -17.934 9.544 -67.369 1.00 19.46 ? 113 ASN B O 1 ATOM 3194 C CB . ASN B 1 87 ? -19.144 7.137 -69.457 1.00 24.32 ? 113 ASN B CB 1 ATOM 3195 C CG . ASN B 1 87 ? -19.995 8.293 -69.968 1.00 28.06 ? 113 ASN B CG 1 ATOM 3196 O OD1 . ASN B 1 87 ? -19.616 9.458 -69.855 1.00 28.05 ? 113 ASN B OD1 1 ATOM 3197 N ND2 . ASN B 1 87 ? -21.153 7.970 -70.529 1.00 32.73 ? 113 ASN B ND2 1 ATOM 3198 N N . LEU B 1 88 ? -16.477 8.377 -68.593 1.00 14.79 ? 114 LEU B N 1 ATOM 3199 C CA . LEU B 1 88 ? -15.427 9.366 -68.360 1.00 18.65 ? 114 LEU B CA 1 ATOM 3200 C C . LEU B 1 88 ? -15.296 10.421 -69.459 1.00 27.19 ? 114 LEU B C 1 ATOM 3201 O O . LEU B 1 88 ? -15.061 11.594 -69.178 1.00 30.61 ? 114 LEU B O 1 ATOM 3202 C CB . LEU B 1 88 ? -14.091 8.651 -68.166 1.00 16.88 ? 114 LEU B CB 1 ATOM 3203 C CG . LEU B 1 88 ? -14.081 7.741 -66.924 1.00 16.58 ? 114 LEU B CG 1 ATOM 3204 C CD1 . LEU B 1 88 ? -12.815 6.893 -66.862 1.00 17.75 ? 114 LEU B CD1 1 ATOM 3205 C CD2 . LEU B 1 88 ? -14.235 8.555 -65.657 1.00 17.35 ? 114 LEU B CD2 1 ATOM 3206 N N . VAL B 1 89 ? -15.429 9.994 -70.706 1.00 17.46 ? 115 VAL B N 1 ATOM 3207 C CA . VAL B 1 89 ? -15.213 10.870 -71.854 1.00 24.09 ? 115 VAL B CA 1 ATOM 3208 C C . VAL B 1 89 ? -16.393 10.737 -72.821 1.00 25.29 ? 115 VAL B C 1 ATOM 3209 O O . VAL B 1 89 ? -16.546 9.709 -73.479 1.00 28.36 ? 115 VAL B O 1 ATOM 3210 C CB . VAL B 1 89 ? -13.893 10.538 -72.586 1.00 24.18 ? 115 VAL B CB 1 ATOM 3211 C CG1 . VAL B 1 89 ? -13.728 11.405 -73.856 1.00 26.99 ? 115 VAL B CG1 1 ATOM 3212 C CG2 . VAL B 1 89 ? -12.686 10.689 -71.648 1.00 22.79 ? 115 VAL B CG2 1 ATOM 3213 N N . TRP B 1 90 ? -17.212 11.784 -72.899 1.00 19.39 ? 116 TRP B N 1 ATOM 3214 C CA . TRP B 1 90 ? -18.463 11.764 -73.656 1.00 19.44 ? 116 TRP B CA 1 ATOM 3215 C C . TRP B 1 90 ? -18.831 13.185 -74.072 1.00 22.25 ? 116 TRP B C 1 ATOM 3216 O O . TRP B 1 90 ? -18.634 14.118 -73.308 1.00 22.27 ? 116 TRP B O 1 ATOM 3217 C CB . TRP B 1 90 ? -19.587 11.149 -72.808 1.00 17.97 ? 116 TRP B CB 1 ATOM 3218 C CG . TRP B 1 90 ? -20.863 10.884 -73.550 1.00 25.11 ? 116 TRP B CG 1 ATOM 3219 C CD1 . TRP B 1 90 ? -21.002 10.560 -74.869 1.00 28.06 ? 116 TRP B CD1 1 ATOM 3220 C CD2 . TRP B 1 90 ? -22.185 10.917 -73.004 1.00 18.42 ? 116 TRP B CD2 1 ATOM 3221 N NE1 . TRP B 1 90 ? -22.334 10.384 -75.178 1.00 22.63 ? 116 TRP B NE1 1 ATOM 3222 C CE2 . TRP B 1 90 ? -23.079 10.602 -74.050 1.00 22.22 ? 116 TRP B CE2 1 ATOM 3223 C CE3 . TRP B 1 90 ? -22.700 11.189 -71.730 1.00 20.94 ? 116 TRP B CE3 1 ATOM 3224 C CZ2 . TRP B 1 90 ? -24.460 10.552 -73.862 1.00 25.91 ? 116 TRP B CZ2 1 ATOM 3225 C CZ3 . TRP B 1 90 ? -24.069 11.134 -71.541 1.00 25.02 ? 116 TRP B CZ3 1 ATOM 3226 C CH2 . TRP B 1 90 ? -24.935 10.819 -72.604 1.00 29.07 ? 116 TRP B CH2 1 ATOM 3227 N N . TYR B 1 91 ? -19.382 13.356 -75.267 1.00 25.55 ? 117 TYR B N 1 ATOM 3228 C CA . TYR B 1 91 ? -19.699 14.704 -75.740 1.00 25.17 ? 117 TYR B CA 1 ATOM 3229 C C . TYR B 1 91 ? -20.946 15.299 -75.072 1.00 25.10 ? 117 TYR B C 1 ATOM 3230 O O . TYR B 1 91 ? -21.149 16.505 -75.100 1.00 30.89 ? 117 TYR B O 1 ATOM 3231 C CB . TYR B 1 91 ? -19.868 14.703 -77.262 1.00 25.15 ? 117 TYR B CB 1 ATOM 3232 C CG . TYR B 1 91 ? -21.233 14.274 -77.766 1.00 24.25 ? 117 TYR B CG 1 ATOM 3233 C CD1 . TYR B 1 91 ? -21.609 12.940 -77.760 1.00 22.88 ? 117 TYR B CD1 1 ATOM 3234 C CD2 . TYR B 1 91 ? -22.125 15.206 -78.286 1.00 34.25 ? 117 TYR B CD2 1 ATOM 3235 C CE1 . TYR B 1 91 ? -22.843 12.543 -78.236 1.00 35.13 ? 117 TYR B CE1 1 ATOM 3236 C CE2 . TYR B 1 91 ? -23.362 14.824 -78.770 1.00 38.87 ? 117 TYR B CE2 1 ATOM 3237 C CZ . TYR B 1 91 ? -23.717 13.489 -78.743 1.00 36.08 ? 117 TYR B CZ 1 ATOM 3238 O OH . TYR B 1 91 ? -24.946 13.098 -79.213 1.00 34.44 ? 117 TYR B OH 1 ATOM 3239 N N . GLN B 1 92 ? -21.782 14.459 -74.475 1.00 25.33 ? 118 GLN B N 1 ATOM 3240 C CA . GLN B 1 92 ? -22.951 14.958 -73.759 1.00 28.26 ? 118 GLN B CA 1 ATOM 3241 C C . GLN B 1 92 ? -22.754 14.989 -72.245 1.00 25.81 ? 118 GLN B C 1 ATOM 3242 O O . GLN B 1 92 ? -21.908 14.267 -71.696 1.00 22.16 ? 118 GLN B O 1 ATOM 3243 C CB . GLN B 1 92 ? -24.175 14.115 -74.100 1.00 28.70 ? 118 GLN B CB 1 ATOM 3244 C CG . GLN B 1 92 ? -24.455 14.112 -75.584 1.00 40.95 ? 118 GLN B CG 1 ATOM 3245 C CD . GLN B 1 92 ? -25.919 13.986 -75.913 1.00 51.88 ? 118 GLN B CD 1 ATOM 3246 O OE1 . GLN B 1 92 ? -26.440 14.732 -76.741 1.00 65.06 ? 118 GLN B OE1 1 ATOM 3247 N NE2 . GLN B 1 92 ? -26.595 13.033 -75.278 1.00 55.95 ? 118 GLN B NE2 1 ATOM 3248 N N . GLU B 1 93 ? -23.560 15.824 -71.589 1.00 27.62 ? 119 GLU B N 1 ATOM 3249 C CA . GLU B 1 93 ? -23.542 15.990 -70.132 1.00 31.67 ? 119 GLU B CA 1 ATOM 3250 C C . GLU B 1 93 ? -22.124 16.314 -69.696 1.00 28.83 ? 119 GLU B C 1 ATOM 3251 O O . GLU B 1 93 ? -21.601 15.789 -68.717 1.00 28.25 ? 119 GLU B O 1 ATOM 3252 C CB . GLU B 1 93 ? -24.108 14.746 -69.424 1.00 30.67 ? 119 GLU B CB 1 ATOM 3253 C CG . GLU B 1 93 ? -25.603 14.549 -69.722 1.00 43.15 ? 119 GLU B CG 1 ATOM 3254 C CD . GLU B 1 93 ? -26.257 13.443 -68.909 1.00 47.70 ? 119 GLU B CD 1 ATOM 3255 O OE1 . GLU B 1 93 ? -26.604 12.389 -69.495 1.00 40.86 ? 119 GLU B OE1 1 ATOM 3256 O OE2 . GLU B 1 93 ? -26.441 13.630 -67.687 1.00 47.97 ? 119 GLU B OE2 1 ATOM 3257 N N . LEU B 1 94 ? -21.521 17.201 -70.470 1.00 26.69 ? 120 LEU B N 1 ATOM 3258 C CA . LEU B 1 94 ? -20.173 17.681 -70.236 1.00 34.59 ? 120 LEU B CA 1 ATOM 3259 C C . LEU B 1 94 ? -20.234 19.026 -69.517 1.00 29.83 ? 120 LEU B C 1 ATOM 3260 O O . LEU B 1 94 ? -21.055 19.871 -69.859 1.00 31.07 ? 120 LEU B O 1 ATOM 3261 C CB . LEU B 1 94 ? -19.438 17.806 -71.572 1.00 29.35 ? 120 LEU B CB 1 ATOM 3262 C CG . LEU B 1 94 ? -17.954 18.148 -71.609 1.00 33.89 ? 120 LEU B CG 1 ATOM 3263 C CD1 . LEU B 1 94 ? -17.159 17.066 -70.913 1.00 34.09 ? 120 LEU B CD1 1 ATOM 3264 C CD2 . LEU B 1 94 ? -17.506 18.292 -73.054 1.00 28.30 ? 120 LEU B CD2 1 ATOM 3265 N N . ALA B 1 95 ? -19.391 19.216 -68.507 1.00 26.50 ? 121 ALA B N 1 ATOM 3266 C CA . ALA B 1 95 ? -19.321 20.504 -67.838 1.00 24.52 ? 121 ALA B CA 1 ATOM 3267 C C . ALA B 1 95 ? -18.981 21.567 -68.873 1.00 35.31 ? 121 ALA B C 1 ATOM 3268 O O . ALA B 1 95 ? -18.058 21.385 -69.665 1.00 28.79 ? 121 ALA B O 1 ATOM 3269 C CB . ALA B 1 95 ? -18.295 20.492 -66.735 1.00 25.16 ? 121 ALA B CB 1 ATOM 3270 N N . PRO B 1 96 ? -19.739 22.672 -68.874 1.00 38.05 ? 122 PRO B N 1 ATOM 3271 C CA . PRO B 1 96 ? -19.599 23.762 -69.849 1.00 40.89 ? 122 PRO B CA 1 ATOM 3272 C C . PRO B 1 96 ? -18.192 24.357 -69.934 1.00 41.23 ? 122 PRO B C 1 ATOM 3273 O O . PRO B 1 96 ? -17.835 24.889 -70.984 1.00 51.08 ? 122 PRO B O 1 ATOM 3274 C CB . PRO B 1 96 ? -20.593 24.810 -69.340 1.00 45.38 ? 122 PRO B CB 1 ATOM 3275 C CG . PRO B 1 96 ? -21.617 24.026 -68.604 1.00 41.82 ? 122 PRO B CG 1 ATOM 3276 C CD . PRO B 1 96 ? -20.869 22.897 -67.955 1.00 35.79 ? 122 PRO B CD 1 ATOM 3277 N N . TRP B 1 97 ? -17.407 24.273 -68.865 1.00 39.00 ? 123 TRP B N 1 ATOM 3278 C CA . TRP B 1 97 ? -16.066 24.860 -68.881 1.00 32.18 ? 123 TRP B CA 1 ATOM 3279 C C . TRP B 1 97 ? -15.114 24.086 -69.782 1.00 33.14 ? 123 TRP B C 1 ATOM 3280 O O . TRP B 1 97 ? -14.141 24.639 -70.287 1.00 35.98 ? 123 TRP B O 1 ATOM 3281 C CB . TRP B 1 97 ? -15.481 24.941 -67.467 1.00 32.47 ? 123 TRP B CB 1 ATOM 3282 C CG . TRP B 1 97 ? -15.346 23.629 -66.736 1.00 32.21 ? 123 TRP B CG 1 ATOM 3283 C CD1 . TRP B 1 97 ? -16.249 23.083 -65.870 1.00 28.70 ? 123 TRP B CD1 1 ATOM 3284 C CD2 . TRP B 1 97 ? -14.234 22.722 -66.777 1.00 28.58 ? 123 TRP B CD2 1 ATOM 3285 N NE1 . TRP B 1 97 ? -15.773 21.888 -65.379 1.00 33.06 ? 123 TRP B NE1 1 ATOM 3286 C CE2 . TRP B 1 97 ? -14.539 21.645 -65.918 1.00 32.46 ? 123 TRP B CE2 1 ATOM 3287 C CE3 . TRP B 1 97 ? -13.014 22.716 -67.454 1.00 31.63 ? 123 TRP B CE3 1 ATOM 3288 C CZ2 . TRP B 1 97 ? -13.670 20.574 -65.722 1.00 28.84 ? 123 TRP B CZ2 1 ATOM 3289 C CZ3 . TRP B 1 97 ? -12.152 21.651 -67.257 1.00 32.96 ? 123 TRP B CZ3 1 ATOM 3290 C CH2 . TRP B 1 97 ? -12.486 20.594 -66.400 1.00 32.46 ? 123 TRP B CH2 1 ATOM 3291 N N . VAL B 1 98 ? -15.405 22.808 -69.991 1.00 30.18 ? 124 VAL B N 1 ATOM 3292 C CA . VAL B 1 98 ? -14.539 21.953 -70.789 1.00 34.18 ? 124 VAL B CA 1 ATOM 3293 C C . VAL B 1 98 ? -14.515 22.358 -72.262 1.00 37.41 ? 124 VAL B C 1 ATOM 3294 O O . VAL B 1 98 ? -13.461 22.343 -72.900 1.00 38.75 ? 124 VAL B O 1 ATOM 3295 C CB . VAL B 1 98 ? -14.973 20.476 -70.681 1.00 31.01 ? 124 VAL B CB 1 ATOM 3296 C CG1 . VAL B 1 98 ? -13.985 19.573 -71.414 1.00 27.61 ? 124 VAL B CG1 1 ATOM 3297 C CG2 . VAL B 1 98 ? -15.074 20.078 -69.227 1.00 26.22 ? 124 VAL B CG2 1 ATOM 3298 N N . GLU B 1 99 ? -15.673 22.735 -72.796 1.00 40.39 ? 125 GLU B N 1 ATOM 3299 C CA . GLU B 1 99 ? -15.805 22.954 -74.232 1.00 44.81 ? 125 GLU B CA 1 ATOM 3300 C C . GLU B 1 99 ? -15.226 24.287 -74.687 1.00 44.78 ? 125 GLU B C 1 ATOM 3301 O O . GLU B 1 99 ? -15.339 24.646 -75.851 1.00 54.83 ? 125 GLU B O 1 ATOM 3302 C CB . GLU B 1 99 ? -17.272 22.855 -74.648 1.00 50.42 ? 125 GLU B CB 1 ATOM 3303 C CG . GLU B 1 99 ? -17.747 21.424 -74.839 1.00 56.96 ? 125 GLU B CG 1 ATOM 3304 C CD . GLU B 1 99 ? -19.259 21.300 -74.807 1.00 67.06 ? 125 GLU B CD 1 ATOM 3305 O OE1 . GLU B 1 99 ? -19.930 22.314 -74.522 1.00 71.86 ? 125 GLU B OE1 1 ATOM 3306 O OE2 . GLU B 1 99 ? -19.776 20.190 -75.061 1.00 70.68 ? 125 GLU B OE2 1 ATOM 3307 N N . THR B 1 100 ? -14.602 25.013 -73.768 1.00 48.84 ? 126 THR B N 1 ATOM 3308 C CA . THR B 1 100 ? -13.924 26.260 -74.110 1.00 57.44 ? 126 THR B CA 1 ATOM 3309 C C . THR B 1 100 ? -12.410 26.061 -74.085 1.00 54.71 ? 126 THR B C 1 ATOM 3310 O O . THR B 1 100 ? -11.644 27.012 -74.229 1.00 54.73 ? 126 THR B O 1 ATOM 3311 C CB . THR B 1 100 ? -14.301 27.392 -73.142 1.00 61.85 ? 126 THR B CB 1 ATOM 3312 O OG1 . THR B 1 100 ? -13.547 27.256 -71.932 1.00 67.79 ? 126 THR B OG1 1 ATOM 3313 C CG2 . THR B 1 100 ? -15.786 27.342 -72.818 1.00 63.82 ? 126 THR B CG2 1 ATOM 3314 N N . LEU B 1 101 ? -11.990 24.814 -73.895 1.00 48.56 ? 127 LEU B N 1 ATOM 3315 C CA . LEU B 1 101 ? -10.576 24.483 -73.755 1.00 44.71 ? 127 LEU B CA 1 ATOM 3316 C C . LEU B 1 101 ? -9.990 23.957 -75.060 1.00 45.82 ? 127 LEU B C 1 ATOM 3317 O O . LEU B 1 101 ? -10.659 23.244 -75.815 1.00 45.17 ? 127 LEU B O 1 ATOM 3318 C CB . LEU B 1 101 ? -10.379 23.453 -72.638 1.00 38.42 ? 127 LEU B CB 1 ATOM 3319 C CG . LEU B 1 101 ? -10.740 23.905 -71.220 1.00 39.98 ? 127 LEU B CG 1 ATOM 3320 C CD1 . LEU B 1 101 ? -10.382 22.819 -70.221 1.00 38.42 ? 127 LEU B CD1 1 ATOM 3321 C CD2 . LEU B 1 101 ? -10.042 25.212 -70.860 1.00 43.64 ? 127 LEU B CD2 1 ATOM 3322 N N . THR B 1 102 ? -8.735 24.301 -75.325 1.00 41.99 ? 128 THR B N 1 ATOM 3323 C CA . THR B 1 102 ? -8.106 23.916 -76.581 1.00 45.43 ? 128 THR B CA 1 ATOM 3324 C C . THR B 1 102 ? -6.770 23.220 -76.373 1.00 48.58 ? 128 THR B C 1 ATOM 3325 O O . THR B 1 102 ? -6.125 23.392 -75.340 1.00 41.39 ? 128 THR B O 1 ATOM 3326 C CB . THR B 1 102 ? -7.878 25.136 -77.486 1.00 53.14 ? 128 THR B CB 1 ATOM 3327 O OG1 . THR B 1 102 ? -7.100 26.113 -76.779 1.00 53.82 ? 128 THR B OG1 1 ATOM 3328 C CG2 . THR B 1 102 ? -9.208 25.745 -77.899 1.00 50.72 ? 128 THR B CG2 1 ATOM 3329 N N . GLY B 1 103 ? -6.372 22.431 -77.368 1.00 49.02 ? 129 GLY B N 1 ATOM 3330 C CA . GLY B 1 103 ? -5.050 21.831 -77.414 1.00 47.45 ? 129 GLY B CA 1 ATOM 3331 C C . GLY B 1 103 ? -4.612 21.134 -76.143 1.00 48.12 ? 129 GLY B C 1 ATOM 3332 O O . GLY B 1 103 ? -5.389 20.409 -75.512 1.00 48.86 ? 129 GLY B O 1 ATOM 3333 N N . GLU B 1 104 ? -3.364 21.374 -75.760 1.00 52.10 ? 130 GLU B N 1 ATOM 3334 C CA . GLU B 1 104 ? -2.747 20.671 -74.644 1.00 49.63 ? 130 GLU B CA 1 ATOM 3335 C C . GLU B 1 104 ? -3.461 20.935 -73.323 1.00 47.15 ? 130 GLU B C 1 ATOM 3336 O O . GLU B 1 104 ? -3.419 20.112 -72.410 1.00 41.13 ? 130 GLU B O 1 ATOM 3337 C CB . GLU B 1 104 ? -1.269 21.058 -74.526 1.00 53.43 ? 130 GLU B CB 1 ATOM 3338 C CG . GLU B 1 104 ? -0.460 20.089 -73.681 1.00 63.93 ? 130 GLU B CG 1 ATOM 3339 C CD . GLU B 1 104 ? -0.755 18.636 -74.034 1.00 77.80 ? 130 GLU B CD 1 ATOM 3340 O OE1 . GLU B 1 104 ? -0.665 18.279 -75.232 1.00 85.20 ? 130 GLU B OE1 1 ATOM 3341 O OE2 . GLU B 1 104 ? -1.093 17.853 -73.117 1.00 77.11 ? 130 GLU B OE2 1 ATOM 3342 N N . ASP B 1 105 ? -4.119 22.084 -73.228 1.00 39.52 ? 131 ASP B N 1 ATOM 3343 C CA . ASP B 1 105 ? -4.867 22.435 -72.028 1.00 40.98 ? 131 ASP B CA 1 ATOM 3344 C C . ASP B 1 105 ? -6.116 21.555 -71.863 1.00 47.06 ? 131 ASP B C 1 ATOM 3345 O O . ASP B 1 105 ? -6.434 21.092 -70.758 1.00 38.37 ? 131 ASP B O 1 ATOM 3346 C CB . ASP B 1 105 ? -5.258 23.908 -72.072 1.00 47.36 ? 131 ASP B CB 1 ATOM 3347 C CG . ASP B 1 105 ? -5.863 24.380 -70.779 1.00 56.48 ? 131 ASP B CG 1 ATOM 3348 O OD1 . ASP B 1 105 ? -5.457 23.869 -69.716 1.00 62.98 ? 131 ASP B OD1 1 ATOM 3349 O OD2 . ASP B 1 105 ? -6.745 25.260 -70.823 1.00 66.41 ? 131 ASP B OD2 1 ATOM 3350 N N . LEU B 1 106 ? -6.824 21.329 -72.965 1.00 43.71 ? 132 LEU B N 1 ATOM 3351 C CA . LEU B 1 106 ? -7.958 20.416 -72.958 1.00 39.31 ? 132 LEU B CA 1 ATOM 3352 C C . LEU B 1 106 ? -7.502 19.028 -72.536 1.00 36.69 ? 132 LEU B C 1 ATOM 3353 O O . LEU B 1 106 ? -8.121 18.388 -71.685 1.00 33.33 ? 132 LEU B O 1 ATOM 3354 C CB . LEU B 1 106 ? -8.617 20.357 -74.335 1.00 38.64 ? 132 LEU B CB 1 ATOM 3355 C CG . LEU B 1 106 ? -9.656 19.248 -74.521 1.00 33.83 ? 132 LEU B CG 1 ATOM 3356 C CD1 . LEU B 1 106 ? -10.903 19.514 -73.688 1.00 34.51 ? 132 LEU B CD1 1 ATOM 3357 C CD2 . LEU B 1 106 ? -10.003 19.088 -75.993 1.00 36.31 ? 132 LEU B CD2 1 ATOM 3358 N N . TRP B 1 107 ? -6.401 18.575 -73.124 1.00 40.02 ? 133 TRP B N 1 ATOM 3359 C CA . TRP B 1 107 ? -5.893 17.250 -72.823 1.00 41.09 ? 133 TRP B CA 1 ATOM 3360 C C . TRP B 1 107 ? -5.508 17.110 -71.351 1.00 36.38 ? 133 TRP B C 1 ATOM 3361 O O . TRP B 1 107 ? -5.838 16.106 -70.719 1.00 29.16 ? 133 TRP B O 1 ATOM 3362 C CB . TRP B 1 107 ? -4.695 16.898 -73.707 1.00 40.45 ? 133 TRP B CB 1 ATOM 3363 C CG . TRP B 1 107 ? -4.207 15.527 -73.399 1.00 36.55 ? 133 TRP B CG 1 ATOM 3364 C CD1 . TRP B 1 107 ? -2.975 15.177 -72.936 1.00 41.36 ? 133 TRP B CD1 1 ATOM 3365 C CD2 . TRP B 1 107 ? -4.969 14.316 -73.474 1.00 37.18 ? 133 TRP B CD2 1 ATOM 3366 N NE1 . TRP B 1 107 ? -2.913 13.816 -72.738 1.00 35.42 ? 133 TRP B NE1 1 ATOM 3367 C CE2 . TRP B 1 107 ? -4.125 13.265 -73.060 1.00 36.16 ? 133 TRP B CE2 1 ATOM 3368 C CE3 . TRP B 1 107 ? -6.282 14.019 -73.854 1.00 35.89 ? 133 TRP B CE3 1 ATOM 3369 C CZ2 . TRP B 1 107 ? -4.550 11.938 -73.014 1.00 31.48 ? 133 TRP B CZ2 1 ATOM 3370 C CZ3 . TRP B 1 107 ? -6.706 12.695 -73.810 1.00 42.39 ? 133 TRP B CZ3 1 ATOM 3371 C CH2 . TRP B 1 107 ? -5.840 11.673 -73.393 1.00 38.29 ? 133 TRP B CH2 1 ATOM 3372 N N . ASN B 1 108 ? -4.825 18.114 -70.804 1.00 35.29 ? 134 ASN B N 1 ATOM 3373 C CA . ASN B 1 108 ? -4.471 18.095 -69.381 1.00 37.61 ? 134 ASN B CA 1 ATOM 3374 C C . ASN B 1 108 ? -5.705 18.070 -68.463 1.00 29.70 ? 134 ASN B C 1 ATOM 3375 O O . ASN B 1 108 ? -5.692 17.426 -67.412 1.00 28.40 ? 134 ASN B O 1 ATOM 3376 C CB . ASN B 1 108 ? -3.583 19.296 -69.032 1.00 43.26 ? 134 ASN B CB 1 ATOM 3377 C CG . ASN B 1 108 ? -2.154 19.136 -69.542 1.00 58.30 ? 134 ASN B CG 1 ATOM 3378 O OD1 . ASN B 1 108 ? -1.824 18.139 -70.190 1.00 58.45 ? 134 ASN B OD1 1 ATOM 3379 N ND2 . ASN B 1 108 ? -1.302 20.124 -69.257 1.00 61.89 ? 134 ASN B ND2 1 ATOM 3380 N N . ALA B 1 109 ? -6.768 18.767 -68.862 1.00 30.92 ? 135 ALA B N 1 ATOM 3381 C CA . ALA B 1 109 ? -8.002 18.760 -68.083 1.00 29.20 ? 135 ALA B CA 1 ATOM 3382 C C . ALA B 1 109 ? -8.663 17.385 -68.152 1.00 29.35 ? 135 ALA B C 1 ATOM 3383 O O . ALA B 1 109 ? -9.291 16.931 -67.189 1.00 28.25 ? 135 ALA B O 1 ATOM 3384 C CB . ALA B 1 109 ? -8.952 19.838 -68.571 1.00 29.09 ? 135 ALA B CB 1 ATOM 3385 N N . THR B 1 110 ? -8.513 16.726 -69.298 1.00 28.52 ? 136 THR B N 1 ATOM 3386 C CA . THR B 1 110 ? -9.096 15.408 -69.510 1.00 24.96 ? 136 THR B CA 1 ATOM 3387 C C . THR B 1 110 ? -8.318 14.370 -68.721 1.00 27.83 ? 136 THR B C 1 ATOM 3388 O O . THR B 1 110 ? -8.907 13.535 -68.038 1.00 22.60 ? 136 THR B O 1 ATOM 3389 C CB . THR B 1 110 ? -9.112 15.044 -71.004 1.00 25.62 ? 136 THR B CB 1 ATOM 3390 O OG1 . THR B 1 110 ? -9.856 16.039 -71.702 1.00 27.75 ? 136 THR B OG1 1 ATOM 3391 C CG2 . THR B 1 110 ? -9.768 13.691 -71.235 1.00 24.11 ? 136 THR B CG2 1 ATOM 3392 N N . VAL B 1 111 ? -6.990 14.447 -68.789 1.00 26.79 ? 137 VAL B N 1 ATOM 3393 C CA . VAL B 1 111 ? -6.145 13.543 -68.017 1.00 28.28 ? 137 VAL B CA 1 ATOM 3394 C C . VAL B 1 111 ? -6.449 13.655 -66.524 1.00 23.89 ? 137 VAL B C 1 ATOM 3395 O O . VAL B 1 111 ? -6.624 12.644 -65.846 1.00 24.10 ? 137 VAL B O 1 ATOM 3396 C CB . VAL B 1 111 ? -4.644 13.812 -68.264 1.00 26.66 ? 137 VAL B CB 1 ATOM 3397 C CG1 . VAL B 1 111 ? -3.788 12.991 -67.307 1.00 26.33 ? 137 VAL B CG1 1 ATOM 3398 C CG2 . VAL B 1 111 ? -4.291 13.479 -69.702 1.00 27.67 ? 137 VAL B CG2 1 ATOM 3399 N N . ASN B 1 112 ? -6.549 14.884 -66.026 1.00 24.54 ? 138 ASN B N 1 ATOM 3400 C CA . ASN B 1 112 ? -6.883 15.117 -64.629 1.00 29.76 ? 138 ASN B CA 1 ATOM 3401 C C . ASN B 1 112 ? -8.260 14.548 -64.286 1.00 24.98 ? 138 ASN B C 1 ATOM 3402 O O . ASN B 1 112 ? -8.462 13.989 -63.209 1.00 21.02 ? 138 ASN B O 1 ATOM 3403 C CB . ASN B 1 112 ? -6.834 16.614 -64.310 1.00 25.02 ? 138 ASN B CB 1 ATOM 3404 C CG . ASN B 1 112 ? -7.072 16.909 -62.836 1.00 32.94 ? 138 ASN B CG 1 ATOM 3405 O OD1 . ASN B 1 112 ? -6.314 16.468 -61.976 1.00 30.71 ? 138 ASN B OD1 1 ATOM 3406 N ND2 . ASN B 1 112 ? -8.115 17.675 -62.543 1.00 37.51 ? 138 ASN B ND2 1 ATOM 3407 N N . HIS B 1 113 ? -9.203 14.684 -65.209 1.00 27.98 ? 139 HIS B N 1 ATOM 3408 C CA . HIS B 1 113 ? -10.542 14.151 -64.978 1.00 23.28 ? 139 HIS B CA 1 ATOM 3409 C C . HIS B 1 113 ? -10.492 12.627 -64.846 1.00 23.13 ? 139 HIS B C 1 ATOM 3410 O O . HIS B 1 113 ? -11.017 12.056 -63.884 1.00 18.82 ? 139 HIS B O 1 ATOM 3411 C CB . HIS B 1 113 ? -11.497 14.570 -66.105 1.00 20.63 ? 139 HIS B CB 1 ATOM 3412 C CG . HIS B 1 113 ? -12.916 14.141 -65.883 1.00 22.37 ? 139 HIS B CG 1 ATOM 3413 N ND1 . HIS B 1 113 ? -13.768 14.806 -65.028 1.00 19.05 ? 139 HIS B ND1 1 ATOM 3414 C CD2 . HIS B 1 113 ? -13.630 13.111 -66.400 1.00 21.20 ? 139 HIS B CD2 1 ATOM 3415 C CE1 . HIS B 1 113 ? -14.945 14.204 -65.022 1.00 17.95 ? 139 HIS B CE1 1 ATOM 3416 N NE2 . HIS B 1 113 ? -14.888 13.169 -65.841 1.00 18.10 ? 139 HIS B NE2 1 ATOM 3417 N N . ILE B 1 114 ? -9.842 11.966 -65.797 1.00 22.38 ? 140 ILE B N 1 ATOM 3418 C CA . ILE B 1 114 ? -9.826 10.510 -65.801 1.00 18.63 ? 140 ILE B CA 1 ATOM 3419 C C . ILE B 1 114 ? -9.093 9.968 -64.573 1.00 20.23 ? 140 ILE B C 1 ATOM 3420 O O . ILE B 1 114 ? -9.602 9.082 -63.881 1.00 17.22 ? 140 ILE B O 1 ATOM 3421 C CB . ILE B 1 114 ? -9.178 9.958 -67.081 1.00 19.40 ? 140 ILE B CB 1 ATOM 3422 C CG1 . ILE B 1 114 ? -10.068 10.249 -68.295 1.00 19.54 ? 140 ILE B CG1 1 ATOM 3423 C CG2 . ILE B 1 114 ? -8.956 8.459 -66.965 1.00 24.88 ? 140 ILE B CG2 1 ATOM 3424 C CD1 . ILE B 1 114 ? -9.321 10.188 -69.626 1.00 20.85 ? 140 ILE B CD1 1 ATOM 3425 N N . THR B 1 115 ? -7.904 10.498 -64.291 1.00 19.78 ? 141 THR B N 1 ATOM 3426 C CA . THR B 1 115 ? -7.116 9.966 -63.178 1.00 19.42 ? 141 THR B CA 1 ATOM 3427 C C . THR B 1 115 ? -7.760 10.255 -61.822 1.00 25.36 ? 141 THR B C 1 ATOM 3428 O O . THR B 1 115 ? -7.793 9.371 -60.971 1.00 17.89 ? 141 THR B O 1 ATOM 3429 C CB . THR B 1 115 ? -5.658 10.511 -63.161 1.00 24.82 ? 141 THR B CB 1 ATOM 3430 O OG1 . THR B 1 115 ? -5.660 11.930 -62.962 1.00 25.99 ? 141 THR B OG1 1 ATOM 3431 C CG2 . THR B 1 115 ? -4.954 10.188 -64.458 1.00 21.99 ? 141 THR B CG2 1 ATOM 3432 N N . THR B 1 116 ? -8.273 11.469 -61.618 1.00 18.86 ? 142 THR B N 1 ATOM 3433 C CA . THR B 1 116 ? -8.876 11.821 -60.328 1.00 18.29 ? 142 THR B CA 1 ATOM 3434 C C . THR B 1 116 ? -10.123 10.979 -60.045 1.00 18.10 ? 142 THR B C 1 ATOM 3435 O O . THR B 1 116 ? -10.324 10.515 -58.917 1.00 17.77 ? 142 THR B O 1 ATOM 3436 C CB . THR B 1 116 ? -9.267 13.320 -60.243 1.00 19.02 ? 142 THR B CB 1 ATOM 3437 O OG1 . THR B 1 116 ? -8.100 14.131 -60.402 1.00 23.51 ? 142 THR B OG1 1 ATOM 3438 C CG2 . THR B 1 116 ? -9.910 13.643 -58.886 1.00 22.23 ? 142 THR B CG2 1 ATOM 3439 N N . VAL B 1 117 ? -10.962 10.776 -61.058 1.00 17.35 ? 143 VAL B N 1 ATOM 3440 C CA . VAL B 1 117 ? -12.196 10.023 -60.842 1.00 15.11 ? 143 VAL B CA 1 ATOM 3441 C C . VAL B 1 117 ? -11.879 8.546 -60.613 1.00 22.06 ? 143 VAL B C 1 ATOM 3442 O O . VAL B 1 117 ? -12.368 7.941 -59.664 1.00 15.45 ? 143 VAL B O 1 ATOM 3443 C CB . VAL B 1 117 ? -13.182 10.185 -62.022 1.00 14.93 ? 143 VAL B CB 1 ATOM 3444 C CG1 . VAL B 1 117 ? -14.339 9.187 -61.899 1.00 14.10 ? 143 VAL B CG1 1 ATOM 3445 C CG2 . VAL B 1 117 ? -13.722 11.621 -62.057 1.00 16.55 ? 143 VAL B CG2 1 ATOM 3446 N N . MET B 1 118 ? -11.025 7.967 -61.449 1.00 14.96 ? 144 MET B N 1 ATOM 3447 C CA . MET B 1 118 ? -10.708 6.555 -61.285 1.00 18.13 ? 144 MET B CA 1 ATOM 3448 C C . MET B 1 118 ? -9.968 6.274 -59.971 1.00 18.27 ? 144 MET B C 1 ATOM 3449 O O . MET B 1 118 ? -10.178 5.231 -59.358 1.00 15.77 ? 144 MET B O 1 ATOM 3450 C CB . MET B 1 118 ? -9.898 6.050 -62.478 1.00 15.28 ? 144 MET B CB 1 ATOM 3451 C CG . MET B 1 118 ? -10.719 5.970 -63.759 1.00 20.09 ? 144 MET B CG 1 ATOM 3452 S SD . MET B 1 118 ? -9.743 5.325 -65.135 1.00 20.81 ? 144 MET B SD 1 ATOM 3453 C CE . MET B 1 118 ? -9.652 3.597 -64.677 1.00 18.58 ? 144 MET B CE 1 ATOM 3454 N N . THR B 1 119 ? -9.120 7.204 -59.541 1.00 15.62 ? 145 THR B N 1 ATOM 3455 C CA . THR B 1 119 ? -8.346 7.036 -58.313 1.00 15.98 ? 145 THR B CA 1 ATOM 3456 C C . THR B 1 119 ? -9.283 7.036 -57.117 1.00 20.06 ? 145 THR B C 1 ATOM 3457 O O . THR B 1 119 ? -9.167 6.200 -56.219 1.00 15.30 ? 145 THR B O 1 ATOM 3458 C CB . THR B 1 119 ? -7.281 8.154 -58.156 1.00 20.05 ? 145 THR B CB 1 ATOM 3459 O OG1 . THR B 1 119 ? -6.301 8.027 -59.200 1.00 20.34 ? 145 THR B OG1 1 ATOM 3460 C CG2 . THR B 1 119 ? -6.583 8.075 -56.803 1.00 25.14 ? 145 THR B CG2 1 ATOM 3461 N N . HIS B 1 120 ? -10.231 7.963 -57.129 1.00 14.85 ? 146 HIS B N 1 ATOM 3462 C CA . HIS B 1 120 ? -11.227 8.036 -56.072 1.00 16.38 ? 146 HIS B CA 1 ATOM 3463 C C . HIS B 1 120 ? -11.944 6.701 -55.892 1.00 13.26 ? 146 HIS B C 1 ATOM 3464 O O . HIS B 1 120 ? -12.081 6.216 -54.760 1.00 13.07 ? 146 HIS B O 1 ATOM 3465 C CB . HIS B 1 120 ? -12.247 9.140 -56.366 1.00 20.17 ? 146 HIS B CB 1 ATOM 3466 C CG . HIS B 1 120 ? -13.424 9.136 -55.443 1.00 20.69 ? 146 HIS B CG 1 ATOM 3467 N ND1 . HIS B 1 120 ? -13.416 9.785 -54.227 1.00 18.25 ? 146 HIS B ND1 1 ATOM 3468 C CD2 . HIS B 1 120 ? -14.644 8.555 -55.553 1.00 24.44 ? 146 HIS B CD2 1 ATOM 3469 C CE1 . HIS B 1 120 ? -14.587 9.619 -53.636 1.00 20.25 ? 146 HIS B CE1 1 ATOM 3470 N NE2 . HIS B 1 120 ? -15.350 8.875 -54.417 1.00 21.43 ? 146 HIS B NE2 1 ATOM 3471 N N . TYR B 1 121 ? -12.391 6.103 -56.991 1.00 15.04 ? 147 TYR B N 1 ATOM 3472 C CA . TYR B 1 121 ? -13.202 4.895 -56.878 1.00 13.47 ? 147 TYR B CA 1 ATOM 3473 C C . TYR B 1 121 ? -12.340 3.669 -56.678 1.00 15.24 ? 147 TYR B C 1 ATOM 3474 O O . TYR B 1 121 ? -12.802 2.681 -56.110 1.00 22.18 ? 147 TYR B O 1 ATOM 3475 C CB . TYR B 1 121 ? -14.135 4.745 -58.090 1.00 12.29 ? 147 TYR B CB 1 ATOM 3476 C CG . TYR B 1 121 ? -15.268 5.718 -57.942 1.00 20.27 ? 147 TYR B CG 1 ATOM 3477 C CD1 . TYR B 1 121 ? -16.275 5.490 -57.002 1.00 18.66 ? 147 TYR B CD1 1 ATOM 3478 C CD2 . TYR B 1 121 ? -15.302 6.901 -58.672 1.00 18.77 ? 147 TYR B CD2 1 ATOM 3479 C CE1 . TYR B 1 121 ? -17.298 6.399 -56.816 1.00 15.24 ? 147 TYR B CE1 1 ATOM 3480 C CE2 . TYR B 1 121 ? -16.323 7.818 -58.490 1.00 19.32 ? 147 TYR B CE2 1 ATOM 3481 C CZ . TYR B 1 121 ? -17.320 7.558 -57.560 1.00 16.40 ? 147 TYR B CZ 1 ATOM 3482 O OH . TYR B 1 121 ? -18.332 8.465 -57.364 1.00 18.33 ? 147 TYR B OH 1 ATOM 3483 N N . LYS B 1 122 ? -11.086 3.739 -57.115 1.00 13.08 ? 148 LYS B N 1 ATOM 3484 C CA . LYS B 1 122 ? -10.114 2.700 -56.806 1.00 15.52 ? 148 LYS B CA 1 ATOM 3485 C C . LYS B 1 122 ? -9.950 2.572 -55.289 1.00 13.76 ? 148 LYS B C 1 ATOM 3486 O O . LYS B 1 122 ? -9.858 1.471 -54.761 1.00 21.96 ? 148 LYS B O 1 ATOM 3487 C CB . LYS B 1 122 ? -8.764 3.015 -57.450 1.00 16.63 ? 148 LYS B CB 1 ATOM 3488 C CG . LYS B 1 122 ? -7.670 1.987 -57.205 1.00 24.38 ? 148 LYS B CG 1 ATOM 3489 C CD . LYS B 1 122 ? -6.327 2.534 -57.732 1.00 25.21 ? 148 LYS B CD 1 ATOM 3490 C CE . LYS B 1 122 ? -5.174 1.577 -57.497 1.00 34.37 ? 148 LYS B CE 1 ATOM 3491 N NZ . LYS B 1 122 ? -3.889 2.148 -58.009 1.00 33.61 ? 148 LYS B NZ 1 ATOM 3492 N N . GLU B 1 123 ? -9.923 3.708 -54.595 1.00 17.40 ? 149 GLU B N 1 ATOM 3493 C CA . GLU B 1 123 ? -9.660 3.704 -53.158 1.00 18.13 ? 149 GLU B CA 1 ATOM 3494 C C . GLU B 1 123 ? -10.890 3.418 -52.308 1.00 20.31 ? 149 GLU B C 1 ATOM 3495 O O . GLU B 1 123 ? -10.766 3.094 -51.130 1.00 21.82 ? 149 GLU B O 1 ATOM 3496 C CB . GLU B 1 123 ? -9.059 5.044 -52.729 1.00 22.09 ? 149 GLU B CB 1 ATOM 3497 C CG . GLU B 1 123 ? -7.709 5.343 -53.345 1.00 36.27 ? 149 GLU B CG 1 ATOM 3498 C CD . GLU B 1 123 ? -7.304 6.798 -53.177 1.00 48.49 ? 149 GLU B CD 1 ATOM 3499 O OE1 . GLU B 1 123 ? -8.207 7.666 -53.123 1.00 45.08 ? 149 GLU B OE1 1 ATOM 3500 O OE2 . GLU B 1 123 ? -6.086 7.072 -53.105 1.00 54.44 ? 149 GLU B OE2 1 ATOM 3501 N N . SER B 1 124 ? -12.084 3.553 -52.868 1.00 13.50 ? 150 SER B N 1 ATOM 3502 C CA . SER B 1 124 ? -13.251 3.489 -51.993 1.00 17.58 ? 150 SER B CA 1 ATOM 3503 C C . SER B 1 124 ? -14.283 2.416 -52.319 1.00 16.20 ? 150 SER B C 1 ATOM 3504 O O . SER B 1 124 ? -15.029 2.011 -51.426 1.00 14.57 ? 150 SER B O 1 ATOM 3505 C CB . SER B 1 124 ? -13.940 4.847 -51.963 1.00 21.08 ? 150 SER B CB 1 ATOM 3506 O OG . SER B 1 124 ? -14.275 5.264 -53.266 1.00 34.38 ? 150 SER B OG 1 ATOM 3507 N N . PHE B 1 125 ? -14.331 1.959 -53.571 1.00 13.66 ? 151 PHE B N 1 ATOM 3508 C CA . PHE B 1 125 ? -15.317 0.954 -53.980 1.00 17.31 ? 151 PHE B CA 1 ATOM 3509 C C . PHE B 1 125 ? -14.711 -0.068 -54.934 1.00 19.10 ? 151 PHE B C 1 ATOM 3510 O O . PHE B 1 125 ? -13.547 0.025 -55.288 1.00 17.94 ? 151 PHE B O 1 ATOM 3511 C CB . PHE B 1 125 ? -16.530 1.618 -54.639 1.00 18.26 ? 151 PHE B CB 1 ATOM 3512 C CG . PHE B 1 125 ? -17.258 2.592 -53.748 1.00 17.90 ? 151 PHE B CG 1 ATOM 3513 C CD1 . PHE B 1 125 ? -18.202 2.144 -52.835 1.00 12.42 ? 151 PHE B CD1 1 ATOM 3514 C CD2 . PHE B 1 125 ? -17.009 3.955 -53.836 1.00 10.26 ? 151 PHE B CD2 1 ATOM 3515 C CE1 . PHE B 1 125 ? -18.894 3.045 -52.020 1.00 14.65 ? 151 PHE B CE1 1 ATOM 3516 C CE2 . PHE B 1 125 ? -17.692 4.860 -53.026 1.00 18.23 ? 151 PHE B CE2 1 ATOM 3517 C CZ . PHE B 1 125 ? -18.644 4.401 -52.116 1.00 12.14 ? 151 PHE B CZ 1 ATOM 3518 N N . ASN B 1 126 ? -15.501 -1.055 -55.339 1.00 17.94 ? 152 ASN B N 1 ATOM 3519 C CA . ASN B 1 126 ? -15.053 -1.997 -56.362 1.00 21.02 ? 152 ASN B CA 1 ATOM 3520 C C . ASN B 1 126 ? -15.771 -1.763 -57.684 1.00 17.60 ? 152 ASN B C 1 ATOM 3521 O O . ASN B 1 126 ? -16.932 -2.132 -57.854 1.00 16.21 ? 152 ASN B O 1 ATOM 3522 C CB . ASN B 1 126 ? -15.258 -3.439 -55.902 1.00 21.21 ? 152 ASN B CB 1 ATOM 3523 C CG . ASN B 1 126 ? -14.271 -3.850 -54.826 1.00 24.49 ? 152 ASN B CG 1 ATOM 3524 O OD1 . ASN B 1 126 ? -14.663 -4.304 -53.748 1.00 29.65 ? 152 ASN B OD1 1 ATOM 3525 N ND2 . ASN B 1 126 ? -12.979 -3.691 -55.110 1.00 28.43 ? 152 ASN B ND2 1 ATOM 3526 N N . ILE B 1 127 ? -15.072 -1.136 -58.621 1.00 12.83 ? 153 ILE B N 1 ATOM 3527 C CA . ILE B 1 127 ? -15.626 -0.911 -59.952 1.00 13.62 ? 153 ILE B CA 1 ATOM 3528 C C . ILE B 1 127 ? -15.229 -2.071 -60.840 1.00 12.83 ? 153 ILE B C 1 ATOM 3529 O O . ILE B 1 127 ? -14.039 -2.273 -61.073 1.00 13.56 ? 153 ILE B O 1 ATOM 3530 C CB . ILE B 1 127 ? -15.107 0.382 -60.562 1.00 16.17 ? 153 ILE B CB 1 ATOM 3531 C CG1 . ILE B 1 127 ? -15.319 1.549 -59.591 1.00 22.98 ? 153 ILE B CG1 1 ATOM 3532 C CG2 . ILE B 1 127 ? -15.718 0.609 -61.937 1.00 21.52 ? 153 ILE B CG2 1 ATOM 3533 C CD1 . ILE B 1 127 ? -16.623 2.244 -59.742 1.00 20.49 ? 153 ILE B CD1 1 ATOM 3534 N N . TYR B 1 128 ? -16.199 -2.843 -61.323 1.00 12.53 ? 154 TYR B N 1 ATOM 3535 C CA . TYR B 1 128 ? -15.862 -3.980 -62.180 1.00 13.00 ? 154 TYR B CA 1 ATOM 3536 C C . TYR B 1 128 ? -15.307 -3.500 -63.509 1.00 16.62 ? 154 TYR B C 1 ATOM 3537 O O . TYR B 1 128 ? -14.346 -4.066 -64.039 1.00 13.24 ? 154 TYR B O 1 ATOM 3538 C CB . TYR B 1 128 ? -17.070 -4.880 -62.451 1.00 12.92 ? 154 TYR B CB 1 ATOM 3539 C CG . TYR B 1 128 ? -16.746 -5.914 -63.513 1.00 11.20 ? 154 TYR B CG 1 ATOM 3540 C CD1 . TYR B 1 128 ? -15.895 -6.970 -63.223 1.00 21.36 ? 154 TYR B CD1 1 ATOM 3541 C CD2 . TYR B 1 128 ? -17.248 -5.806 -64.816 1.00 16.32 ? 154 TYR B CD2 1 ATOM 3542 C CE1 . TYR B 1 128 ? -15.558 -7.901 -64.173 1.00 20.68 ? 154 TYR B CE1 1 ATOM 3543 C CE2 . TYR B 1 128 ? -16.907 -6.738 -65.792 1.00 16.18 ? 154 TYR B CE2 1 ATOM 3544 C CZ . TYR B 1 128 ? -16.070 -7.785 -65.457 1.00 20.72 ? 154 TYR B CZ 1 ATOM 3545 O OH . TYR B 1 128 ? -15.714 -8.733 -66.387 1.00 23.35 ? 154 TYR B OH 1 ATOM 3546 N N . ALA B 1 129 ? -15.935 -2.460 -64.048 1.00 10.98 ? 155 ALA B N 1 ATOM 3547 C CA . ALA B 1 129 ? -15.596 -1.950 -65.364 1.00 11.47 ? 155 ALA B CA 1 ATOM 3548 C C . ALA B 1 129 ? -15.846 -0.454 -65.483 1.00 19.07 ? 155 ALA B C 1 ATOM 3549 O O . ALA B 1 129 ? -16.769 0.085 -64.879 1.00 19.16 ? 155 ALA B O 1 ATOM 3550 C CB . ALA B 1 129 ? -16.373 -2.680 -66.418 1.00 12.41 ? 155 ALA B CB 1 ATOM 3551 N N . TRP B 1 130 ? -15.013 0.203 -66.279 1.00 15.30 ? 156 TRP B N 1 ATOM 3552 C CA . TRP B 1 130 ? -15.179 1.613 -66.595 1.00 19.71 ? 156 TRP B CA 1 ATOM 3553 C C . TRP B 1 130 ? -15.539 1.803 -68.063 1.00 20.70 ? 156 TRP B C 1 ATOM 3554 O O . TRP B 1 130 ? -14.799 1.349 -68.924 1.00 16.92 ? 156 TRP B O 1 ATOM 3555 C CB . TRP B 1 130 ? -13.890 2.385 -66.292 1.00 14.83 ? 156 TRP B CB 1 ATOM 3556 C CG . TRP B 1 130 ? -13.825 2.930 -64.903 1.00 16.10 ? 156 TRP B CG 1 ATOM 3557 C CD1 . TRP B 1 130 ? -13.041 2.497 -63.874 1.00 18.16 ? 156 TRP B CD1 1 ATOM 3558 C CD2 . TRP B 1 130 ? -14.595 4.018 -64.395 1.00 14.73 ? 156 TRP B CD2 1 ATOM 3559 N NE1 . TRP B 1 130 ? -13.276 3.260 -62.749 1.00 19.12 ? 156 TRP B NE1 1 ATOM 3560 C CE2 . TRP B 1 130 ? -14.228 4.199 -63.047 1.00 17.96 ? 156 TRP B CE2 1 ATOM 3561 C CE3 . TRP B 1 130 ? -15.559 4.864 -64.957 1.00 15.94 ? 156 TRP B CE3 1 ATOM 3562 C CZ2 . TRP B 1 130 ? -14.791 5.187 -62.250 1.00 18.81 ? 156 TRP B CZ2 1 ATOM 3563 C CZ3 . TRP B 1 130 ? -16.114 5.842 -64.168 1.00 18.06 ? 156 TRP B CZ3 1 ATOM 3564 C CH2 . TRP B 1 130 ? -15.730 5.997 -62.827 1.00 14.35 ? 156 TRP B CH2 1 ATOM 3565 N N . ASP B 1 131 ? -16.659 2.465 -68.352 1.00 19.34 ? 157 ASP B N 1 ATOM 3566 C CA . ASP B 1 131 ? -16.877 3.004 -69.700 1.00 17.00 ? 157 ASP B CA 1 ATOM 3567 C C . ASP B 1 131 ? -16.005 4.258 -69.793 1.00 20.68 ? 157 ASP B C 1 ATOM 3568 O O . ASP B 1 131 ? -16.379 5.305 -69.278 1.00 20.92 ? 157 ASP B O 1 ATOM 3569 C CB . ASP B 1 131 ? -18.355 3.362 -69.968 1.00 18.13 ? 157 ASP B CB 1 ATOM 3570 C CG . ASP B 1 131 ? -19.283 2.136 -70.020 1.00 29.86 ? 157 ASP B CG 1 ATOM 3571 O OD1 . ASP B 1 131 ? -18.825 1.032 -70.382 1.00 27.15 ? 157 ASP B OD1 1 ATOM 3572 O OD2 . ASP B 1 131 ? -20.491 2.284 -69.713 1.00 26.23 ? 157 ASP B OD2 1 ATOM 3573 N N . VAL B 1 132 ? -14.832 4.152 -70.413 1.00 17.36 ? 158 VAL B N 1 ATOM 3574 C CA . VAL B 1 132 ? -13.894 5.278 -70.452 1.00 17.55 ? 158 VAL B CA 1 ATOM 3575 C C . VAL B 1 132 ? -14.323 6.259 -71.547 1.00 26.03 ? 158 VAL B C 1 ATOM 3576 O O . VAL B 1 132 ? -14.619 7.419 -71.272 1.00 27.25 ? 158 VAL B O 1 ATOM 3577 C CB . VAL B 1 132 ? -12.446 4.790 -70.687 1.00 18.16 ? 158 VAL B CB 1 ATOM 3578 C CG1 . VAL B 1 132 ? -11.462 5.966 -70.792 1.00 17.83 ? 158 VAL B CG1 1 ATOM 3579 C CG2 . VAL B 1 132 ? -12.033 3.829 -69.576 1.00 19.81 ? 158 VAL B CG2 1 ATOM 3580 N N . VAL B 1 133 ? -14.382 5.781 -72.786 1.00 17.13 ? 159 VAL B N 1 ATOM 3581 C CA . VAL B 1 133 ? -14.874 6.592 -73.895 1.00 17.99 ? 159 VAL B CA 1 ATOM 3582 C C . VAL B 1 133 ? -16.272 6.119 -74.282 1.00 23.29 ? 159 VAL B C 1 ATOM 3583 O O . VAL B 1 133 ? -16.513 4.911 -74.410 1.00 16.97 ? 159 VAL B O 1 ATOM 3584 C CB . VAL B 1 133 ? -13.910 6.523 -75.097 1.00 19.45 ? 159 VAL B CB 1 ATOM 3585 C CG1 . VAL B 1 133 ? -14.492 7.198 -76.337 1.00 20.45 ? 159 VAL B CG1 1 ATOM 3586 C CG2 . VAL B 1 133 ? -12.578 7.162 -74.721 1.00 20.34 ? 159 VAL B CG2 1 ATOM 3587 N N . ASN B 1 134 ? -17.195 7.065 -74.446 1.00 20.94 ? 160 ASN B N 1 ATOM 3588 C CA . ASN B 1 134 ? -18.581 6.739 -74.822 1.00 18.70 ? 160 ASN B CA 1 ATOM 3589 C C . ASN B 1 134 ? -18.999 7.466 -76.104 1.00 22.28 ? 160 ASN B C 1 ATOM 3590 O O . ASN B 1 134 ? -18.781 8.675 -76.232 1.00 22.23 ? 160 ASN B O 1 ATOM 3591 C CB . ASN B 1 134 ? -19.533 7.092 -73.666 1.00 23.94 ? 160 ASN B CB 1 ATOM 3592 C CG . ASN B 1 134 ? -20.966 6.635 -73.911 1.00 27.48 ? 160 ASN B CG 1 ATOM 3593 O OD1 . ASN B 1 134 ? -21.209 5.526 -74.392 1.00 28.32 ? 160 ASN B OD1 1 ATOM 3594 N ND2 . ASN B 1 134 ? -21.925 7.495 -73.578 1.00 28.64 ? 160 ASN B ND2 1 ATOM 3595 N N . GLU B 1 135 ? -19.574 6.726 -77.055 1.00 18.34 ? 161 GLU B N 1 ATOM 3596 C CA . GLU B 1 135 ? -20.200 7.308 -78.249 1.00 22.09 ? 161 GLU B CA 1 ATOM 3597 C C . GLU B 1 135 ? -19.231 8.161 -79.053 1.00 28.27 ? 161 GLU B C 1 ATOM 3598 O O . GLU B 1 135 ? -19.482 9.343 -79.305 1.00 27.79 ? 161 GLU B O 1 ATOM 3599 C CB . GLU B 1 135 ? -21.447 8.127 -77.852 1.00 19.55 ? 161 GLU B CB 1 ATOM 3600 C CG . GLU B 1 135 ? -22.607 7.242 -77.351 1.00 19.68 ? 161 GLU B CG 1 ATOM 3601 C CD . GLU B 1 135 ? -23.853 8.014 -76.881 1.00 28.61 ? 161 GLU B CD 1 ATOM 3602 O OE1 . GLU B 1 135 ? -23.980 9.230 -77.154 1.00 24.44 ? 161 GLU B OE1 1 ATOM 3603 O OE2 . GLU B 1 135 ? -24.714 7.390 -76.221 1.00 27.85 ? 161 GLU B OE2 1 ATOM 3604 N N . ALA B 1 136 ? -18.129 7.543 -79.472 1.00 21.56 ? 162 ALA B N 1 ATOM 3605 C CA . ALA B 1 136 ? -17.060 8.260 -80.163 1.00 28.43 ? 162 ALA B CA 1 ATOM 3606 C C . ALA B 1 136 ? -17.259 8.305 -81.678 1.00 29.51 ? 162 ALA B C 1 ATOM 3607 O O . ALA B 1 136 ? -16.488 8.950 -82.401 1.00 34.15 ? 162 ALA B O 1 ATOM 3608 C CB . ALA B 1 136 ? -15.707 7.623 -79.827 1.00 23.17 ? 162 ALA B CB 1 ATOM 3609 N N . PHE B 1 137 ? -18.291 7.631 -82.170 1.00 25.56 ? 163 PHE B N 1 ATOM 3610 C CA . PHE B 1 137 ? -18.440 7.493 -83.615 1.00 25.71 ? 163 PHE B CA 1 ATOM 3611 C C . PHE B 1 137 ? -19.750 8.049 -84.150 1.00 26.13 ? 163 PHE B C 1 ATOM 3612 O O . PHE B 1 137 ? -20.760 8.025 -83.472 1.00 24.97 ? 163 PHE B O 1 ATOM 3613 C CB . PHE B 1 137 ? -18.298 6.021 -84.002 1.00 28.62 ? 163 PHE B CB 1 ATOM 3614 C CG . PHE B 1 137 ? -16.942 5.461 -83.700 1.00 32.74 ? 163 PHE B CG 1 ATOM 3615 C CD1 . PHE B 1 137 ? -15.912 5.571 -84.623 1.00 35.01 ? 163 PHE B CD1 1 ATOM 3616 C CD2 . PHE B 1 137 ? -16.681 4.863 -82.477 1.00 28.72 ? 163 PHE B CD2 1 ATOM 3617 C CE1 . PHE B 1 137 ? -14.648 5.079 -84.338 1.00 34.69 ? 163 PHE B CE1 1 ATOM 3618 C CE2 . PHE B 1 137 ? -15.419 4.365 -82.186 1.00 33.93 ? 163 PHE B CE2 1 ATOM 3619 C CZ . PHE B 1 137 ? -14.404 4.477 -83.114 1.00 32.97 ? 163 PHE B CZ 1 ATOM 3620 N N . ASN B 1 138 ? -19.713 8.563 -85.374 1.00 34.94 ? 164 ASN B N 1 ATOM 3621 C CA . ASN B 1 138 ? -20.930 8.934 -86.087 1.00 38.81 ? 164 ASN B CA 1 ATOM 3622 C C . ASN B 1 138 ? -21.634 7.694 -86.603 1.00 38.49 ? 164 ASN B C 1 ATOM 3623 O O . ASN B 1 138 ? -21.009 6.646 -86.762 1.00 33.09 ? 164 ASN B O 1 ATOM 3624 C CB . ASN B 1 138 ? -20.618 9.875 -87.251 1.00 36.57 ? 164 ASN B CB 1 ATOM 3625 C CG . ASN B 1 138 ? -20.295 11.282 -86.790 1.00 38.08 ? 164 ASN B CG 1 ATOM 3626 O OD1 . ASN B 1 138 ? -20.907 11.802 -85.851 1.00 36.10 ? 164 ASN B OD1 1 ATOM 3627 N ND2 . ASN B 1 138 ? -19.326 11.906 -87.445 1.00 35.18 ? 164 ASN B ND2 1 ATOM 3628 N N . ASP B 1 139 ? -22.927 7.814 -86.891 1.00 35.25 ? 165 ASP B N 1 ATOM 3629 C CA . ASP B 1 139 ? -23.689 6.664 -87.349 1.00 33.43 ? 165 ASP B CA 1 ATOM 3630 C C . ASP B 1 139 ? -23.197 6.113 -88.688 1.00 29.31 ? 165 ASP B C 1 ATOM 3631 O O . ASP B 1 139 ? -23.546 4.989 -89.048 1.00 46.08 ? 165 ASP B O 1 ATOM 3632 C CB . ASP B 1 139 ? -25.177 7.010 -87.439 1.00 43.78 ? 165 ASP B CB 1 ATOM 3633 C CG . ASP B 1 139 ? -25.869 6.998 -86.075 1.00 45.28 ? 165 ASP B CG 1 ATOM 3634 O OD1 . ASP B 1 139 ? -25.344 6.367 -85.128 1.00 34.44 ? 165 ASP B OD1 1 ATOM 3635 O OD2 . ASP B 1 139 ? -26.948 7.615 -85.948 1.00 49.31 ? 165 ASP B OD2 1 ATOM 3636 N N . ASN B 1 140 ? -22.382 6.878 -89.418 1.00 38.96 ? 166 ASN B N 1 ATOM 3637 C CA . ASN B 1 140 ? -21.791 6.375 -90.663 1.00 32.58 ? 166 ASN B CA 1 ATOM 3638 C C . ASN B 1 140 ? -20.375 5.825 -90.495 1.00 48.74 ? 166 ASN B C 1 ATOM 3639 O O . ASN B 1 140 ? -19.737 5.430 -91.473 1.00 44.49 ? 166 ASN B O 1 ATOM 3640 C CB . ASN B 1 140 ? -21.782 7.457 -91.758 1.00 38.02 ? 166 ASN B CB 1 ATOM 3641 C CG . ASN B 1 140 ? -21.133 8.761 -91.314 1.00 46.68 ? 166 ASN B CG 1 ATOM 3642 O OD1 . ASN B 1 140 ? -20.278 8.784 -90.427 1.00 44.62 ? 166 ASN B OD1 1 ATOM 3643 N ND2 . ASN B 1 140 ? -21.543 9.861 -91.944 1.00 55.37 ? 166 ASN B ND2 1 ATOM 3644 N N . GLY B 1 141 ? -19.878 5.806 -89.263 1.00 49.77 ? 167 GLY B N 1 ATOM 3645 C CA . GLY B 1 141 ? -18.578 5.215 -88.999 1.00 50.13 ? 167 GLY B CA 1 ATOM 3646 C C . GLY B 1 141 ? -17.443 6.198 -88.771 1.00 47.28 ? 167 GLY B C 1 ATOM 3647 O O . GLY B 1 141 ? -16.436 5.850 -88.159 1.00 47.81 ? 167 GLY B O 1 ATOM 3648 N N . THR B 1 142 ? -17.590 7.424 -89.259 1.00 35.89 ? 168 THR B N 1 ATOM 3649 C CA . THR B 1 142 ? -16.566 8.439 -89.037 1.00 35.37 ? 168 THR B CA 1 ATOM 3650 C C . THR B 1 142 ? -16.520 8.841 -87.562 1.00 35.46 ? 168 THR B C 1 ATOM 3651 O O . THR B 1 142 ? -17.484 8.633 -86.823 1.00 31.03 ? 168 THR B O 1 ATOM 3652 C CB . THR B 1 142 ? -16.807 9.692 -89.892 1.00 36.10 ? 168 THR B CB 1 ATOM 3653 O OG1 . THR B 1 142 ? -18.072 10.271 -89.547 1.00 38.88 ? 168 THR B OG1 1 ATOM 3654 C CG2 . THR B 1 142 ? -16.791 9.344 -91.378 1.00 42.09 ? 168 THR B CG2 1 ATOM 3655 N N . TYR B 1 143 ? -15.392 9.402 -87.135 1.00 40.13 ? 169 TYR B N 1 ATOM 3656 C CA . TYR B 1 143 ? -15.249 9.903 -85.770 1.00 38.17 ? 169 TYR B CA 1 ATOM 3657 C C . TYR B 1 143 ? -16.215 11.053 -85.509 1.00 34.34 ? 169 TYR B C 1 ATOM 3658 O O . TYR B 1 143 ? -16.350 11.952 -86.338 1.00 34.28 ? 169 TYR B O 1 ATOM 3659 C CB . TYR B 1 143 ? -13.816 10.379 -85.517 1.00 39.84 ? 169 TYR B CB 1 ATOM 3660 C CG . TYR B 1 143 ? -12.783 9.286 -85.404 1.00 32.37 ? 169 TYR B CG 1 ATOM 3661 C CD1 . TYR B 1 143 ? -12.573 8.630 -84.203 1.00 34.63 ? 169 TYR B CD1 1 ATOM 3662 C CD2 . TYR B 1 143 ? -11.988 8.936 -86.491 1.00 38.67 ? 169 TYR B CD2 1 ATOM 3663 C CE1 . TYR B 1 143 ? -11.623 7.640 -84.084 1.00 38.17 ? 169 TYR B CE1 1 ATOM 3664 C CE2 . TYR B 1 143 ? -11.030 7.944 -86.381 1.00 39.22 ? 169 TYR B CE2 1 ATOM 3665 C CZ . TYR B 1 143 ? -10.853 7.301 -85.170 1.00 39.32 ? 169 TYR B CZ 1 ATOM 3666 O OH . TYR B 1 143 ? -9.902 6.313 -85.043 1.00 42.65 ? 169 TYR B OH 1 ATOM 3667 N N . ARG B 1 144 ? -16.880 11.024 -84.360 1.00 29.89 ? 170 ARG B N 1 ATOM 3668 C CA . ARG B 1 144 ? -17.733 12.128 -83.929 1.00 32.18 ? 170 ARG B CA 1 ATOM 3669 C C . ARG B 1 144 ? -16.902 13.393 -83.664 1.00 39.80 ? 170 ARG B C 1 ATOM 3670 O O . ARG B 1 144 ? -15.837 13.316 -83.044 1.00 37.29 ? 170 ARG B O 1 ATOM 3671 C CB . ARG B 1 144 ? -18.515 11.735 -82.671 1.00 34.49 ? 170 ARG B CB 1 ATOM 3672 C CG . ARG B 1 144 ? -19.561 12.750 -82.242 1.00 31.38 ? 170 ARG B CG 1 ATOM 3673 C CD . ARG B 1 144 ? -20.158 12.417 -80.881 1.00 32.67 ? 170 ARG B CD 1 ATOM 3674 N NE . ARG B 1 144 ? -20.948 11.192 -80.884 1.00 34.79 ? 170 ARG B NE 1 ATOM 3675 C CZ . ARG B 1 144 ? -22.182 11.098 -81.373 1.00 36.05 ? 170 ARG B CZ 1 ATOM 3676 N NH1 . ARG B 1 144 ? -22.761 12.160 -81.922 1.00 28.32 ? 170 ARG B NH1 1 ATOM 3677 N NH2 . ARG B 1 144 ? -22.833 9.938 -81.319 1.00 29.30 ? 170 ARG B NH2 1 ATOM 3678 N N . GLU B 1 145 ? -17.409 14.546 -84.116 1.00 36.11 ? 171 GLU B N 1 ATOM 3679 C CA . GLU B 1 145 ? -16.680 15.826 -84.063 1.00 38.85 ? 171 GLU B CA 1 ATOM 3680 C C . GLU B 1 145 ? -16.660 16.519 -82.677 1.00 38.19 ? 171 GLU B C 1 ATOM 3681 O O . GLU B 1 145 ? -16.695 17.747 -82.569 1.00 46.96 ? 171 GLU B O 1 ATOM 3682 C CB . GLU B 1 145 ? -17.233 16.781 -85.167 1.00 67.50 ? 171 GLU B CB 1 ATOM 3683 C CG . GLU B 1 145 ? -18.327 17.797 -84.758 1.00 76.40 ? 171 GLU B CG 1 ATOM 3684 C CD . GLU B 1 145 ? -18.575 18.894 -85.794 1.00 88.62 ? 171 GLU B CD 1 ATOM 3685 O OE1 . GLU B 1 145 ? -18.183 18.723 -86.974 1.00 91.32 ? 171 GLU B OE1 1 ATOM 3686 O OE2 . GLU B 1 145 ? -19.155 19.938 -85.412 1.00 91.41 ? 171 GLU B OE2 1 ATOM 3687 N N . ASN B 1 146 ? -16.525 15.745 -81.602 1.00 34.35 ? 172 ASN B N 1 ATOM 3688 C CA . ASN B 1 146 ? -16.554 16.354 -80.269 1.00 34.80 ? 172 ASN B CA 1 ATOM 3689 C C . ASN B 1 146 ? -15.297 17.162 -80.022 1.00 37.00 ? 172 ASN B C 1 ATOM 3690 O O . ASN B 1 146 ? -14.425 17.244 -80.886 1.00 41.10 ? 172 ASN B O 1 ATOM 3691 C CB . ASN B 1 146 ? -16.747 15.305 -79.163 1.00 30.78 ? 172 ASN B CB 1 ATOM 3692 C CG . ASN B 1 146 ? -15.747 14.171 -79.234 1.00 31.90 ? 172 ASN B CG 1 ATOM 3693 O OD1 . ASN B 1 146 ? -14.607 14.349 -79.657 1.00 34.76 ? 172 ASN B OD1 1 ATOM 3694 N ND2 . ASN B 1 146 ? -16.176 12.988 -78.807 1.00 29.79 ? 172 ASN B ND2 1 ATOM 3695 N N . VAL B 1 147 ? -15.206 17.763 -78.845 1.00 32.30 ? 173 VAL B N 1 ATOM 3696 C CA . VAL B 1 147 ? -14.132 18.706 -78.586 1.00 36.11 ? 173 VAL B CA 1 ATOM 3697 C C . VAL B 1 147 ? -12.754 18.033 -78.620 1.00 35.81 ? 173 VAL B C 1 ATOM 3698 O O . VAL B 1 147 ? -11.792 18.623 -79.106 1.00 37.75 ? 173 VAL B O 1 ATOM 3699 C CB . VAL B 1 147 ? -14.351 19.445 -77.248 1.00 35.11 ? 173 VAL B CB 1 ATOM 3700 C CG1 . VAL B 1 147 ? -14.229 18.500 -76.048 1.00 32.79 ? 173 VAL B CG1 1 ATOM 3701 C CG2 . VAL B 1 147 ? -13.381 20.607 -77.138 1.00 37.33 ? 173 VAL B CG2 1 ATOM 3702 N N . TRP B 1 148 ? -12.666 16.784 -78.173 1.00 36.10 ? 174 TRP B N 1 ATOM 3703 C CA . TRP B 1 148 ? -11.386 16.082 -78.169 1.00 34.14 ? 174 TRP B CA 1 ATOM 3704 C C . TRP B 1 148 ? -10.915 15.726 -79.576 1.00 38.21 ? 174 TRP B C 1 ATOM 3705 O O . TRP B 1 148 ? -9.742 15.898 -79.892 1.00 35.18 ? 174 TRP B O 1 ATOM 3706 C CB . TRP B 1 148 ? -11.459 14.815 -77.321 1.00 28.95 ? 174 TRP B CB 1 ATOM 3707 C CG . TRP B 1 148 ? -11.850 15.092 -75.916 1.00 29.02 ? 174 TRP B CG 1 ATOM 3708 C CD1 . TRP B 1 148 ? -11.039 15.509 -74.903 1.00 27.71 ? 174 TRP B CD1 1 ATOM 3709 C CD2 . TRP B 1 148 ? -13.161 14.987 -75.368 1.00 26.23 ? 174 TRP B CD2 1 ATOM 3710 N NE1 . TRP B 1 148 ? -11.768 15.673 -73.753 1.00 30.66 ? 174 TRP B NE1 1 ATOM 3711 C CE2 . TRP B 1 148 ? -13.076 15.354 -74.012 1.00 28.63 ? 174 TRP B CE2 1 ATOM 3712 C CE3 . TRP B 1 148 ? -14.402 14.610 -75.891 1.00 28.70 ? 174 TRP B CE3 1 ATOM 3713 C CZ2 . TRP B 1 148 ? -14.185 15.359 -73.171 1.00 27.23 ? 174 TRP B CZ2 1 ATOM 3714 C CZ3 . TRP B 1 148 ? -15.501 14.620 -75.055 1.00 25.16 ? 174 TRP B CZ3 1 ATOM 3715 C CH2 . TRP B 1 148 ? -15.386 14.988 -73.711 1.00 25.54 ? 174 TRP B CH2 1 ATOM 3716 N N . TYR B 1 149 ? -11.811 15.228 -80.421 1.00 32.29 ? 175 TYR B N 1 ATOM 3717 C CA . TYR B 1 149 ? -11.390 14.837 -81.761 1.00 33.70 ? 175 TYR B CA 1 ATOM 3718 C C . TYR B 1 149 ? -10.934 16.052 -82.553 1.00 44.05 ? 175 TYR B C 1 ATOM 3719 O O . TYR B 1 149 ? -9.947 15.993 -83.277 1.00 41.39 ? 175 TYR B O 1 ATOM 3720 C CB . TYR B 1 149 ? -12.500 14.121 -82.526 1.00 35.56 ? 175 TYR B CB 1 ATOM 3721 C CG . TYR B 1 149 ? -12.100 13.812 -83.964 1.00 41.98 ? 175 TYR B CG 1 ATOM 3722 C CD1 . TYR B 1 149 ? -11.316 12.698 -84.267 1.00 37.36 ? 175 TYR B CD1 1 ATOM 3723 C CD2 . TYR B 1 149 ? -12.489 14.645 -85.013 1.00 40.05 ? 175 TYR B CD2 1 ATOM 3724 C CE1 . TYR B 1 149 ? -10.944 12.417 -85.572 1.00 39.28 ? 175 TYR B CE1 1 ATOM 3725 C CE2 . TYR B 1 149 ? -12.118 14.374 -86.318 1.00 42.55 ? 175 TYR B CE2 1 ATOM 3726 C CZ . TYR B 1 149 ? -11.347 13.259 -86.593 1.00 45.72 ? 175 TYR B CZ 1 ATOM 3727 O OH . TYR B 1 149 ? -10.981 12.984 -87.893 1.00 52.99 ? 175 TYR B OH 1 ATOM 3728 N N . THR B 1 150 ? -11.668 17.148 -82.407 1.00 42.52 ? 176 THR B N 1 ATOM 3729 C CA . THR B 1 150 ? -11.358 18.389 -83.102 1.00 44.03 ? 176 THR B CA 1 ATOM 3730 C C . THR B 1 150 ? -10.001 18.937 -82.682 1.00 49.99 ? 176 THR B C 1 ATOM 3731 O O . THR B 1 150 ? -9.216 19.407 -83.511 1.00 53.53 ? 176 THR B O 1 ATOM 3732 C CB . THR B 1 150 ? -12.434 19.457 -82.842 1.00 39.90 ? 176 THR B CB 1 ATOM 3733 O OG1 . THR B 1 150 ? -13.702 18.975 -83.299 1.00 54.14 ? 176 THR B OG1 1 ATOM 3734 C CG2 . THR B 1 150 ? -12.097 20.743 -83.574 1.00 50.80 ? 176 THR B CG2 1 ATOM 3735 N N . GLN B 1 151 ? -9.719 18.866 -81.389 1.00 39.13 ? 177 GLN B N 1 ATOM 3736 C CA . GLN B 1 151 ? -8.485 19.427 -80.863 1.00 39.08 ? 177 GLN B CA 1 ATOM 3737 C C . GLN B 1 151 ? -7.310 18.469 -80.950 1.00 40.00 ? 177 GLN B C 1 ATOM 3738 O O . GLN B 1 151 ? -6.167 18.900 -80.986 1.00 43.42 ? 177 GLN B O 1 ATOM 3739 C CB . GLN B 1 151 ? -8.682 19.855 -79.412 1.00 36.78 ? 177 GLN B CB 1 ATOM 3740 C CG . GLN B 1 151 ? -9.611 21.032 -79.255 1.00 35.51 ? 177 GLN B CG 1 ATOM 3741 C CD . GLN B 1 151 ? -9.095 22.262 -79.960 1.00 40.10 ? 177 GLN B CD 1 ATOM 3742 O OE1 . GLN B 1 151 ? -7.889 22.448 -80.099 1.00 45.60 ? 177 GLN B OE1 1 ATOM 3743 N NE2 . GLN B 1 151 ? -10.006 23.109 -80.414 1.00 46.05 ? 177 GLN B NE2 1 ATOM 3744 N N . LEU B 1 152 ? -7.582 17.168 -80.982 1.00 37.02 ? 178 LEU B N 1 ATOM 3745 C CA . LEU B 1 152 ? -6.511 16.195 -80.777 1.00 31.24 ? 178 LEU B CA 1 ATOM 3746 C C . LEU B 1 152 ? -6.422 15.097 -81.842 1.00 36.91 ? 178 LEU B C 1 ATOM 3747 O O . LEU B 1 152 ? -5.431 14.373 -81.901 1.00 35.44 ? 178 LEU B O 1 ATOM 3748 C CB . LEU B 1 152 ? -6.675 15.553 -79.395 1.00 33.40 ? 178 LEU B CB 1 ATOM 3749 C CG . LEU B 1 152 ? -6.971 16.512 -78.237 1.00 33.94 ? 178 LEU B CG 1 ATOM 3750 C CD1 . LEU B 1 152 ? -7.503 15.763 -77.022 1.00 33.33 ? 178 LEU B CD1 1 ATOM 3751 C CD2 . LEU B 1 152 ? -5.720 17.295 -77.880 1.00 39.92 ? 178 LEU B CD2 1 ATOM 3752 N N . GLY B 1 153 ? -7.452 14.965 -82.672 1.00 31.01 ? 179 GLY B N 1 ATOM 3753 C CA . GLY B 1 153 ? -7.477 13.908 -83.667 1.00 43.06 ? 179 GLY B CA 1 ATOM 3754 C C . GLY B 1 153 ? -7.818 12.564 -83.050 1.00 43.31 ? 179 GLY B C 1 ATOM 3755 O O . GLY B 1 153 ? -8.031 12.474 -81.849 1.00 38.79 ? 179 GLY B O 1 ATOM 3756 N N . PRO B 1 154 ? -7.839 11.502 -83.869 1.00 45.79 ? 180 PRO B N 1 ATOM 3757 C CA . PRO B 1 154 ? -8.308 10.174 -83.440 1.00 42.21 ? 180 PRO B CA 1 ATOM 3758 C C . PRO B 1 154 ? -7.541 9.559 -82.260 1.00 40.33 ? 180 PRO B C 1 ATOM 3759 O O . PRO B 1 154 ? -8.097 8.707 -81.567 1.00 31.16 ? 180 PRO B O 1 ATOM 3760 C CB . PRO B 1 154 ? -8.119 9.315 -84.694 1.00 36.95 ? 180 PRO B CB 1 ATOM 3761 C CG . PRO B 1 154 ? -7.055 10.029 -85.491 1.00 46.91 ? 180 PRO B CG 1 ATOM 3762 C CD . PRO B 1 154 ? -7.310 11.487 -85.244 1.00 44.20 ? 180 PRO B CD 1 ATOM 3763 N N . ASP B 1 155 ? -6.304 9.980 -82.022 1.00 33.77 ? 181 ASP B N 1 ATOM 3764 C CA . ASP B 1 155 ? -5.505 9.356 -80.974 1.00 31.08 ? 181 ASP B CA 1 ATOM 3765 C C . ASP B 1 155 ? -6.001 9.655 -79.556 1.00 30.25 ? 181 ASP B C 1 ATOM 3766 O O . ASP B 1 155 ? -5.511 9.042 -78.608 1.00 27.46 ? 181 ASP B O 1 ATOM 3767 C CB . ASP B 1 155 ? -4.038 9.772 -81.098 1.00 40.30 ? 181 ASP B CB 1 ATOM 3768 C CG . ASP B 1 155 ? -3.237 8.825 -81.982 1.00 48.48 ? 181 ASP B CG 1 ATOM 3769 O OD1 . ASP B 1 155 ? -3.854 8.115 -82.803 1.00 50.07 ? 181 ASP B OD1 1 ATOM 3770 O OD2 . ASP B 1 155 ? -1.993 8.783 -81.853 1.00 59.76 ? 181 ASP B OD2 1 ATOM 3771 N N . TYR B 1 156 ? -6.961 10.571 -79.405 1.00 27.95 ? 182 TYR B N 1 ATOM 3772 C CA . TYR B 1 156 ? -7.501 10.887 -78.075 1.00 32.45 ? 182 TYR B CA 1 ATOM 3773 C C . TYR B 1 156 ? -8.149 9.655 -77.458 1.00 30.16 ? 182 TYR B C 1 ATOM 3774 O O . TYR B 1 156 ? -8.149 9.490 -76.233 1.00 25.15 ? 182 TYR B O 1 ATOM 3775 C CB . TYR B 1 156 ? -8.507 12.053 -78.120 1.00 25.03 ? 182 TYR B CB 1 ATOM 3776 C CG . TYR B 1 156 ? -9.975 11.695 -78.370 1.00 25.45 ? 182 TYR B CG 1 ATOM 3777 C CD1 . TYR B 1 156 ? -10.835 11.364 -77.313 1.00 22.85 ? 182 TYR B CD1 1 ATOM 3778 C CD2 . TYR B 1 156 ? -10.510 11.727 -79.656 1.00 24.55 ? 182 TYR B CD2 1 ATOM 3779 C CE1 . TYR B 1 156 ? -12.180 11.052 -77.548 1.00 28.71 ? 182 TYR B CE1 1 ATOM 3780 C CE2 . TYR B 1 156 ? -11.851 11.416 -79.895 1.00 27.01 ? 182 TYR B CE2 1 ATOM 3781 C CZ . TYR B 1 156 ? -12.677 11.080 -78.843 1.00 28.06 ? 182 TYR B CZ 1 ATOM 3782 O OH . TYR B 1 156 ? -14.003 10.776 -79.091 1.00 27.41 ? 182 TYR B OH 1 ATOM 3783 N N . ILE B 1 157 ? -8.687 8.786 -78.307 1.00 28.84 ? 183 ILE B N 1 ATOM 3784 C CA . ILE B 1 157 ? -9.339 7.585 -77.815 1.00 24.69 ? 183 ILE B CA 1 ATOM 3785 C C . ILE B 1 157 ? -8.290 6.656 -77.193 1.00 22.00 ? 183 ILE B C 1 ATOM 3786 O O . ILE B 1 157 ? -8.358 6.404 -75.995 1.00 21.19 ? 183 ILE B O 1 ATOM 3787 C CB . ILE B 1 157 ? -10.156 6.874 -78.920 1.00 27.93 ? 183 ILE B CB 1 ATOM 3788 C CG1 . ILE B 1 157 ? -11.337 7.756 -79.343 1.00 25.74 ? 183 ILE B CG1 1 ATOM 3789 C CG2 . ILE B 1 157 ? -10.631 5.507 -78.437 1.00 24.66 ? 183 ILE B CG2 1 ATOM 3790 C CD1 . ILE B 1 157 ? -12.110 7.234 -80.547 1.00 25.36 ? 183 ILE B CD1 1 ATOM 3791 N N . PRO B 1 158 ? -7.295 6.177 -77.970 1.00 26.86 ? 184 PRO B N 1 ATOM 3792 C CA . PRO B 1 158 ? -6.352 5.300 -77.261 1.00 22.94 ? 184 PRO B CA 1 ATOM 3793 C C . PRO B 1 158 ? -5.553 6.019 -76.186 1.00 23.24 ? 184 PRO B C 1 ATOM 3794 O O . PRO B 1 158 ? -5.158 5.386 -75.210 1.00 22.70 ? 184 PRO B O 1 ATOM 3795 C CB . PRO B 1 158 ? -5.422 4.801 -78.376 1.00 27.06 ? 184 PRO B CB 1 ATOM 3796 C CG . PRO B 1 158 ? -5.503 5.858 -79.439 1.00 32.18 ? 184 PRO B CG 1 ATOM 3797 C CD . PRO B 1 158 ? -6.947 6.293 -79.402 1.00 24.17 ? 184 PRO B CD 1 ATOM 3798 N N . ASN B 1 159 ? -5.312 7.314 -76.358 1.00 23.84 ? 185 ASN B N 1 ATOM 3799 C CA . ASN B 1 159 ? -4.628 8.070 -75.321 1.00 24.10 ? 185 ASN B CA 1 ATOM 3800 C C . ASN B 1 159 ? -5.412 8.069 -74.002 1.00 23.07 ? 185 ASN B C 1 ATOM 3801 O O . ASN B 1 159 ? -4.825 7.970 -72.923 1.00 22.76 ? 185 ASN B O 1 ATOM 3802 C CB . ASN B 1 159 ? -4.371 9.499 -75.788 1.00 26.51 ? 185 ASN B CB 1 ATOM 3803 C CG . ASN B 1 159 ? -3.249 9.577 -76.811 1.00 37.96 ? 185 ASN B CG 1 ATOM 3804 O OD1 . ASN B 1 159 ? -2.494 8.616 -76.994 1.00 32.60 ? 185 ASN B OD1 1 ATOM 3805 N ND2 . ASN B 1 159 ? -3.133 10.722 -77.483 1.00 37.12 ? 185 ASN B ND2 1 ATOM 3806 N N . ALA B 1 160 ? -6.738 8.152 -74.095 1.00 24.34 ? 186 ALA B N 1 ATOM 3807 C CA . ALA B 1 160 ? -7.580 8.117 -72.898 1.00 23.86 ? 186 ALA B CA 1 ATOM 3808 C C . ALA B 1 160 ? -7.446 6.775 -72.185 1.00 21.70 ? 186 ALA B C 1 ATOM 3809 O O . ALA B 1 160 ? -7.361 6.717 -70.952 1.00 19.70 ? 186 ALA B O 1 ATOM 3810 C CB . ALA B 1 160 ? -9.044 8.390 -73.254 1.00 22.54 ? 186 ALA B CB 1 ATOM 3811 N N . TYR B 1 161 ? -7.414 5.697 -72.958 1.00 20.13 ? 187 TYR B N 1 ATOM 3812 C CA . TYR B 1 161 ? -7.261 4.377 -72.365 1.00 23.88 ? 187 TYR B CA 1 ATOM 3813 C C . TYR B 1 161 ? -5.871 4.184 -71.748 1.00 21.13 ? 187 TYR B C 1 ATOM 3814 O O . TYR B 1 161 ? -5.748 3.550 -70.696 1.00 19.90 ? 187 TYR B O 1 ATOM 3815 C CB . TYR B 1 161 ? -7.589 3.297 -73.398 1.00 23.86 ? 187 TYR B CB 1 ATOM 3816 C CG . TYR B 1 161 ? -9.095 3.207 -73.570 1.00 21.52 ? 187 TYR B CG 1 ATOM 3817 C CD1 . TYR B 1 161 ? -9.866 2.385 -72.749 1.00 22.38 ? 187 TYR B CD1 1 ATOM 3818 C CD2 . TYR B 1 161 ? -9.755 4.023 -74.482 1.00 25.44 ? 187 TYR B CD2 1 ATOM 3819 C CE1 . TYR B 1 161 ? -11.276 2.344 -72.880 1.00 18.75 ? 187 TYR B CE1 1 ATOM 3820 C CE2 . TYR B 1 161 ? -11.131 3.989 -74.618 1.00 21.80 ? 187 TYR B CE2 1 ATOM 3821 C CZ . TYR B 1 161 ? -11.888 3.156 -73.816 1.00 23.58 ? 187 TYR B CZ 1 ATOM 3822 O OH . TYR B 1 161 ? -13.261 3.154 -73.967 1.00 18.18 ? 187 TYR B OH 1 ATOM 3823 N N . ALA B 1 162 ? -4.830 4.745 -72.361 1.00 21.46 ? 188 ALA B N 1 ATOM 3824 C CA . ALA B 1 162 ? -3.509 4.654 -71.749 1.00 22.19 ? 188 ALA B CA 1 ATOM 3825 C C . ALA B 1 162 ? -3.472 5.415 -70.412 1.00 24.81 ? 188 ALA B C 1 ATOM 3826 O O . ALA B 1 162 ? -2.812 4.990 -69.462 1.00 24.74 ? 188 ALA B O 1 ATOM 3827 C CB . ALA B 1 162 ? -2.441 5.180 -72.697 1.00 23.56 ? 188 ALA B CB 1 ATOM 3828 N N . VAL B 1 163 ? -4.176 6.539 -70.338 1.00 24.96 ? 189 VAL B N 1 ATOM 3829 C CA . VAL B 1 163 ? -4.271 7.275 -69.086 1.00 23.59 ? 189 VAL B CA 1 ATOM 3830 C C . VAL B 1 163 ? -5.023 6.420 -68.058 1.00 23.44 ? 189 VAL B C 1 ATOM 3831 O O . VAL B 1 163 ? -4.610 6.317 -66.903 1.00 20.36 ? 189 VAL B O 1 ATOM 3832 C CB . VAL B 1 163 ? -4.973 8.638 -69.280 1.00 28.92 ? 189 VAL B CB 1 ATOM 3833 C CG1 . VAL B 1 163 ? -5.290 9.281 -67.936 1.00 25.72 ? 189 VAL B CG1 1 ATOM 3834 C CG2 . VAL B 1 163 ? -4.104 9.568 -70.131 1.00 22.96 ? 189 VAL B CG2 1 ATOM 3835 N N . ALA B 1 164 ? -6.110 5.784 -68.490 1.00 19.74 ? 190 ALA B N 1 ATOM 3836 C CA . ALA B 1 164 ? -6.891 4.918 -67.596 1.00 23.73 ? 190 ALA B CA 1 ATOM 3837 C C . ALA B 1 164 ? -6.067 3.712 -67.121 1.00 18.69 ? 190 ALA B C 1 ATOM 3838 O O . ALA B 1 164 ? -6.118 3.331 -65.944 1.00 22.47 ? 190 ALA B O 1 ATOM 3839 C CB . ALA B 1 164 ? -8.167 4.452 -68.285 1.00 17.69 ? 190 ALA B CB 1 ATOM 3840 N N . ARG B 1 165 ? -5.303 3.121 -68.038 1.00 19.35 ? 191 ARG B N 1 ATOM 3841 C CA . ARG B 1 165 ? -4.384 2.034 -67.695 1.00 19.80 ? 191 ARG B CA 1 ATOM 3842 C C . ARG B 1 165 ? -3.363 2.458 -66.639 1.00 27.30 ? 191 ARG B C 1 ATOM 3843 O O . ARG B 1 165 ? -2.995 1.665 -65.768 1.00 25.83 ? 191 ARG B O 1 ATOM 3844 C CB . ARG B 1 165 ? -3.644 1.535 -68.939 1.00 20.64 ? 191 ARG B CB 1 ATOM 3845 C CG . ARG B 1 165 ? -4.446 0.591 -69.827 1.00 20.24 ? 191 ARG B CG 1 ATOM 3846 C CD . ARG B 1 165 ? -4.661 -0.762 -69.158 1.00 29.09 ? 191 ARG B CD 1 ATOM 3847 N NE . ARG B 1 165 ? -5.114 -1.741 -70.134 1.00 19.92 ? 191 ARG B NE 1 ATOM 3848 C CZ . ARG B 1 165 ? -6.153 -2.549 -69.973 1.00 26.51 ? 191 ARG B CZ 1 ATOM 3849 N NH1 . ARG B 1 165 ? -6.854 -2.525 -68.843 1.00 20.24 ? 191 ARG B NH1 1 ATOM 3850 N NH2 . ARG B 1 165 ? -6.483 -3.394 -70.950 1.00 21.66 ? 191 ARG B NH2 1 ATOM 3851 N N . SER B 1 166 ? -2.908 3.706 -66.713 1.00 24.54 ? 192 SER B N 1 ATOM 3852 C CA . SER B 1 166 ? -1.849 4.172 -65.814 1.00 23.89 ? 192 SER B CA 1 ATOM 3853 C C . SER B 1 166 ? -2.327 4.337 -64.380 1.00 27.26 ? 192 SER B C 1 ATOM 3854 O O . SER B 1 166 ? -1.508 4.452 -63.462 1.00 24.41 ? 192 SER B O 1 ATOM 3855 C CB . SER B 1 166 ? -1.255 5.495 -66.307 1.00 26.39 ? 192 SER B CB 1 ATOM 3856 O OG . SER B 1 166 ? -2.156 6.564 -66.098 1.00 29.80 ? 192 SER B OG 1 ATOM 3857 N N . VAL B 1 167 ? -3.644 4.352 -64.181 1.00 20.11 ? 193 VAL B N 1 ATOM 3858 C CA . VAL B 1 167 ? -4.186 4.491 -62.844 1.00 19.61 ? 193 VAL B CA 1 ATOM 3859 C C . VAL B 1 167 ? -3.983 3.176 -62.092 1.00 25.96 ? 193 VAL B C 1 ATOM 3860 O O . VAL B 1 167 ? -4.012 3.142 -60.861 1.00 26.30 ? 193 VAL B O 1 ATOM 3861 C CB . VAL B 1 167 ? -5.692 4.896 -62.859 1.00 21.16 ? 193 VAL B CB 1 ATOM 3862 C CG1 . VAL B 1 167 ? -6.195 5.143 -61.435 1.00 24.31 ? 193 VAL B CG1 1 ATOM 3863 C CG2 . VAL B 1 167 ? -5.888 6.159 -63.675 1.00 26.71 ? 193 VAL B CG2 1 ATOM 3864 N N . ASN B 1 168 ? -3.762 2.098 -62.838 1.00 21.53 ? 194 ASN B N 1 ATOM 3865 C CA . ASN B 1 168 ? -3.474 0.796 -62.241 1.00 20.14 ? 194 ASN B CA 1 ATOM 3866 C C . ASN B 1 168 ? -4.607 0.294 -61.365 1.00 21.67 ? 194 ASN B C 1 ATOM 3867 O O . ASN B 1 168 ? -4.375 -0.130 -60.231 1.00 23.27 ? 194 ASN B O 1 ATOM 3868 C CB . ASN B 1 168 ? -2.186 0.854 -61.409 1.00 28.76 ? 194 ASN B CB 1 ATOM 3869 C CG . ASN B 1 168 ? -1.194 -0.212 -61.799 1.00 45.68 ? 194 ASN B CG 1 ATOM 3870 O OD1 . ASN B 1 168 ? -1.090 -0.572 -62.968 1.00 47.63 ? 194 ASN B OD1 1 ATOM 3871 N ND2 . ASN B 1 168 ? -0.456 -0.728 -60.819 1.00 56.78 ? 194 ASN B ND2 1 ATOM 3872 N N . THR B 1 169 ? -5.829 0.352 -61.890 1.00 18.43 ? 195 THR B N 1 ATOM 3873 C CA . THR B 1 169 ? -6.995 -0.168 -61.186 1.00 18.75 ? 195 THR B CA 1 ATOM 3874 C C . THR B 1 169 ? -7.236 -1.616 -61.589 1.00 22.31 ? 195 THR B C 1 ATOM 3875 O O . THR B 1 169 ? -6.708 -2.080 -62.594 1.00 21.42 ? 195 THR B O 1 ATOM 3876 C CB . THR B 1 169 ? -8.265 0.636 -61.495 1.00 20.44 ? 195 THR B CB 1 ATOM 3877 O OG1 . THR B 1 169 ? -8.775 0.248 -62.777 1.00 19.69 ? 195 THR B OG1 1 ATOM 3878 C CG2 . THR B 1 169 ? -7.983 2.113 -61.489 1.00 22.91 ? 195 THR B CG2 1 ATOM 3879 N N . PRO B 1 170 ? -8.040 -2.339 -60.810 1.00 23.88 ? 196 PRO B N 1 ATOM 3880 C CA . PRO B 1 170 ? -8.422 -3.685 -61.238 1.00 24.30 ? 196 PRO B CA 1 ATOM 3881 C C . PRO B 1 170 ? -9.596 -3.699 -62.226 1.00 23.01 ? 196 PRO B C 1 ATOM 3882 O O . PRO B 1 170 ? -10.056 -4.777 -62.590 1.00 26.00 ? 196 PRO B O 1 ATOM 3883 C CB . PRO B 1 170 ? -8.824 -4.358 -59.925 1.00 25.41 ? 196 PRO B CB 1 ATOM 3884 C CG . PRO B 1 170 ? -9.292 -3.225 -59.066 1.00 30.90 ? 196 PRO B CG 1 ATOM 3885 C CD . PRO B 1 170 ? -8.396 -2.080 -59.402 1.00 28.69 ? 196 PRO B CD 1 ATOM 3886 N N . SER B 1 171 ? -10.062 -2.529 -62.652 1.00 18.81 ? 197 SER B N 1 ATOM 3887 C CA . SER B 1 171 ? -11.263 -2.434 -63.486 1.00 14.71 ? 197 SER B CA 1 ATOM 3888 C C . SER B 1 171 ? -11.007 -2.798 -64.952 1.00 15.05 ? 197 SER B C 1 ATOM 3889 O O . SER B 1 171 ? -9.974 -2.437 -65.514 1.00 17.83 ? 197 SER B O 1 ATOM 3890 C CB . SER B 1 171 ? -11.830 -1.020 -63.408 1.00 16.47 ? 197 SER B CB 1 ATOM 3891 O OG . SER B 1 171 ? -12.143 -0.666 -62.067 1.00 18.60 ? 197 SER B OG 1 ATOM 3892 N N . LYS B 1 172 ? -11.949 -3.504 -65.570 1.00 14.74 ? 198 LYS B N 1 ATOM 3893 C CA . LYS B 1 172 ? -11.937 -3.666 -67.025 1.00 16.00 ? 198 LYS B CA 1 ATOM 3894 C C . LYS B 1 172 ? -12.204 -2.321 -67.700 1.00 14.81 ? 198 LYS B C 1 ATOM 3895 O O . LYS B 1 172 ? -13.117 -1.586 -67.314 1.00 19.25 ? 198 LYS B O 1 ATOM 3896 C CB . LYS B 1 172 ? -12.991 -4.686 -67.475 1.00 18.83 ? 198 LYS B CB 1 ATOM 3897 C CG . LYS B 1 172 ? -12.961 -6.006 -66.723 1.00 22.21 ? 198 LYS B CG 1 ATOM 3898 C CD . LYS B 1 172 ? -11.694 -6.775 -67.042 1.00 26.15 ? 198 LYS B CD 1 ATOM 3899 C CE . LYS B 1 172 ? -11.656 -8.111 -66.326 1.00 37.79 ? 198 LYS B CE 1 ATOM 3900 N NZ . LYS B 1 172 ? -12.817 -8.969 -66.667 1.00 40.80 ? 198 LYS B NZ 1 ATOM 3901 N N . LEU B 1 173 ? -11.445 -2.011 -68.734 1.00 15.45 ? 199 LEU B N 1 ATOM 3902 C CA . LEU B 1 173 ? -11.697 -0.790 -69.477 1.00 18.20 ? 199 LEU B CA 1 ATOM 3903 C C . LEU B 1 173 ? -12.550 -1.108 -70.694 1.00 15.35 ? 199 LEU B C 1 ATOM 3904 O O . LEU B 1 173 ? -12.170 -1.903 -71.554 1.00 17.15 ? 199 LEU B O 1 ATOM 3905 C CB . LEU B 1 173 ? -10.390 -0.116 -69.893 1.00 16.28 ? 199 LEU B CB 1 ATOM 3906 C CG . LEU B 1 173 ? -9.439 0.146 -68.712 1.00 17.57 ? 199 LEU B CG 1 ATOM 3907 C CD1 . LEU B 1 173 ? -8.146 0.831 -69.198 1.00 18.17 ? 199 LEU B CD1 1 ATOM 3908 C CD2 . LEU B 1 173 ? -10.093 0.930 -67.546 1.00 15.84 ? 199 LEU B CD2 1 ATOM 3909 N N . TYR B 1 174 ? -13.717 -0.482 -70.749 1.00 14.73 ? 200 TYR B N 1 ATOM 3910 C CA . TYR B 1 174 ? -14.642 -0.674 -71.856 1.00 14.67 ? 200 TYR B CA 1 ATOM 3911 C C . TYR B 1 174 ? -14.730 0.560 -72.741 1.00 16.29 ? 200 TYR B C 1 ATOM 3912 O O . TYR B 1 174 ? -14.504 1.691 -72.286 1.00 16.00 ? 200 TYR B O 1 ATOM 3913 C CB . TYR B 1 174 ? -16.049 -0.969 -71.342 1.00 13.84 ? 200 TYR B CB 1 ATOM 3914 C CG . TYR B 1 174 ? -16.385 -2.395 -70.985 1.00 19.29 ? 200 TYR B CG 1 ATOM 3915 C CD1 . TYR B 1 174 ? -15.710 -3.076 -69.977 1.00 13.78 ? 200 TYR B CD1 1 ATOM 3916 C CD2 . TYR B 1 174 ? -17.427 -3.038 -71.626 1.00 13.59 ? 200 TYR B CD2 1 ATOM 3917 C CE1 . TYR B 1 174 ? -16.060 -4.374 -69.637 1.00 15.17 ? 200 TYR B CE1 1 ATOM 3918 C CE2 . TYR B 1 174 ? -17.775 -4.316 -71.310 1.00 13.59 ? 200 TYR B CE2 1 ATOM 3919 C CZ . TYR B 1 174 ? -17.101 -4.983 -70.314 1.00 19.37 ? 200 TYR B CZ 1 ATOM 3920 O OH . TYR B 1 174 ? -17.498 -6.260 -70.021 1.00 15.64 ? 200 TYR B OH 1 ATOM 3921 N N . ILE B 1 175 ? -15.115 0.332 -73.991 1.00 15.32 ? 201 ILE B N 1 ATOM 3922 C CA . ILE B 1 175 ? -15.596 1.381 -74.872 1.00 15.55 ? 201 ILE B CA 1 ATOM 3923 C C . ILE B 1 175 ? -17.066 1.061 -75.138 1.00 15.65 ? 201 ILE B C 1 ATOM 3924 O O . ILE B 1 175 ? -17.446 -0.110 -75.246 1.00 15.14 ? 201 ILE B O 1 ATOM 3925 C CB . ILE B 1 175 ? -14.740 1.485 -76.188 1.00 20.54 ? 201 ILE B CB 1 ATOM 3926 C CG1 . ILE B 1 175 ? -15.201 2.656 -77.070 1.00 17.02 ? 201 ILE B CG1 1 ATOM 3927 C CG2 . ILE B 1 175 ? -14.665 0.146 -76.943 1.00 17.04 ? 201 ILE B CG2 1 ATOM 3928 C CD1 . ILE B 1 175 ? -14.174 3.081 -78.123 1.00 18.21 ? 201 ILE B CD1 1 ATOM 3929 N N . ASN B 1 176 ? -17.896 2.095 -75.185 1.00 14.75 ? 202 ASN B N 1 ATOM 3930 C CA . ASN B 1 176 ? -19.353 1.921 -75.219 1.00 14.19 ? 202 ASN B CA 1 ATOM 3931 C C . ASN B 1 176 ? -19.948 2.704 -76.380 1.00 19.92 ? 202 ASN B C 1 ATOM 3932 O O . ASN B 1 176 ? -19.460 3.794 -76.697 1.00 17.62 ? 202 ASN B O 1 ATOM 3933 C CB . ASN B 1 176 ? -19.952 2.382 -73.874 1.00 13.38 ? 202 ASN B CB 1 ATOM 3934 C CG . ASN B 1 176 ? -21.396 1.922 -73.661 1.00 18.95 ? 202 ASN B CG 1 ATOM 3935 O OD1 . ASN B 1 176 ? -21.738 0.752 -73.853 1.00 23.03 ? 202 ASN B OD1 1 ATOM 3936 N ND2 . ASN B 1 176 ? -22.243 2.850 -73.229 1.00 14.85 ? 202 ASN B ND2 1 ATOM 3937 N N . ASP B 1 177 ? -20.979 2.161 -77.032 1.00 14.60 ? 203 ASP B N 1 ATOM 3938 C CA . ASP B 1 177 ? -21.655 2.908 -78.101 1.00 15.09 ? 203 ASP B CA 1 ATOM 3939 C C . ASP B 1 177 ? -23.013 2.300 -78.442 1.00 16.79 ? 203 ASP B C 1 ATOM 3940 O O . ASP B 1 177 ? -23.347 1.201 -77.986 1.00 16.96 ? 203 ASP B O 1 ATOM 3941 C CB . ASP B 1 177 ? -20.778 2.971 -79.366 1.00 16.17 ? 203 ASP B CB 1 ATOM 3942 C CG . ASP B 1 177 ? -20.848 4.330 -80.053 1.00 25.00 ? 203 ASP B CG 1 ATOM 3943 O OD1 . ASP B 1 177 ? -21.945 4.928 -80.064 1.00 19.81 ? 203 ASP B OD1 1 ATOM 3944 O OD2 . ASP B 1 177 ? -19.803 4.829 -80.543 1.00 21.75 ? 203 ASP B OD2 1 ATOM 3945 N N . TYR B 1 178 ? -23.792 3.025 -79.244 1.00 19.35 ? 204 TYR B N 1 ATOM 3946 C CA . TYR B 1 178 ? -25.091 2.545 -79.721 1.00 15.12 ? 204 TYR B CA 1 ATOM 3947 C C . TYR B 1 178 ? -25.074 2.430 -81.248 1.00 16.15 ? 204 TYR B C 1 ATOM 3948 O O . TYR B 1 178 ? -24.172 2.967 -81.905 1.00 17.74 ? 204 TYR B O 1 ATOM 3949 C CB . TYR B 1 178 ? -26.220 3.490 -79.264 1.00 14.72 ? 204 TYR B CB 1 ATOM 3950 C CG . TYR B 1 178 ? -26.124 4.855 -79.903 1.00 17.61 ? 204 TYR B CG 1 ATOM 3951 C CD1 . TYR B 1 178 ? -25.308 5.835 -79.354 1.00 22.43 ? 204 TYR B CD1 1 ATOM 3952 C CD2 . TYR B 1 178 ? -26.829 5.163 -81.070 1.00 23.08 ? 204 TYR B CD2 1 ATOM 3953 C CE1 . TYR B 1 178 ? -25.188 7.081 -79.941 1.00 22.91 ? 204 TYR B CE1 1 ATOM 3954 C CE2 . TYR B 1 178 ? -26.716 6.424 -81.666 1.00 21.50 ? 204 TYR B CE2 1 ATOM 3955 C CZ . TYR B 1 178 ? -25.893 7.374 -81.086 1.00 28.49 ? 204 TYR B CZ 1 ATOM 3956 O OH . TYR B 1 178 ? -25.749 8.624 -81.633 1.00 29.55 ? 204 TYR B OH 1 ATOM 3957 N N . ASN B 1 179 ? -26.081 1.749 -81.808 1.00 16.27 ? 205 ASN B N 1 ATOM 3958 C CA . ASN B 1 179 ? -26.170 1.471 -83.250 1.00 20.38 ? 205 ASN B CA 1 ATOM 3959 C C . ASN B 1 179 ? -24.938 0.743 -83.804 1.00 23.04 ? 205 ASN B C 1 ATOM 3960 O O . ASN B 1 179 ? -24.619 0.828 -84.997 1.00 19.06 ? 205 ASN B O 1 ATOM 3961 C CB . ASN B 1 179 ? -26.410 2.764 -84.041 1.00 26.99 ? 205 ASN B CB 1 ATOM 3962 C CG . ASN B 1 179 ? -27.856 3.224 -83.976 1.00 25.39 ? 205 ASN B CG 1 ATOM 3963 O OD1 . ASN B 1 179 ? -28.733 2.486 -83.528 1.00 33.73 ? 205 ASN B OD1 1 ATOM 3964 N ND2 . ASN B 1 179 ? -28.112 4.440 -84.430 1.00 25.82 ? 205 ASN B ND2 1 ATOM 3965 N N . THR B 1 180 ? -24.270 0.015 -82.919 1.00 17.45 ? 206 THR B N 1 ATOM 3966 C CA . THR B 1 180 ? -23.096 -0.771 -83.241 1.00 18.04 ? 206 THR B CA 1 ATOM 3967 C C . THR B 1 180 ? -23.412 -2.242 -82.995 1.00 22.29 ? 206 THR B C 1 ATOM 3968 O O . THR B 1 180 ? -22.534 -3.088 -83.043 1.00 22.09 ? 206 THR B O 1 ATOM 3969 C CB . THR B 1 180 ? -21.900 -0.354 -82.377 1.00 20.14 ? 206 THR B CB 1 ATOM 3970 O OG1 . THR B 1 180 ? -22.330 -0.286 -81.011 1.00 21.63 ? 206 THR B OG1 1 ATOM 3971 C CG2 . THR B 1 180 ? -21.399 1.015 -82.798 1.00 18.67 ? 206 THR B CG2 1 ATOM 3972 N N . GLU B 1 181 ? -24.681 -2.535 -82.737 1.00 17.40 ? 207 GLU B N 1 ATOM 3973 C CA . GLU B 1 181 ? -25.092 -3.882 -82.357 1.00 23.19 ? 207 GLU B CA 1 ATOM 3974 C C . GLU B 1 181 ? -25.095 -4.866 -83.529 1.00 23.48 ? 207 GLU B C 1 ATOM 3975 O O . GLU B 1 181 ? -24.725 -6.028 -83.357 1.00 24.22 ? 207 GLU B O 1 ATOM 3976 C CB . GLU B 1 181 ? -26.477 -3.843 -81.702 1.00 18.57 ? 207 GLU B CB 1 ATOM 3977 C CG . GLU B 1 181 ? -26.531 -2.986 -80.404 1.00 19.74 ? 207 GLU B CG 1 ATOM 3978 C CD . GLU B 1 181 ? -26.729 -1.507 -80.678 1.00 26.31 ? 207 GLU B CD 1 ATOM 3979 O OE1 . GLU B 1 181 ? -27.058 -1.166 -81.835 1.00 22.86 ? 207 GLU B OE1 1 ATOM 3980 O OE2 . GLU B 1 181 ? -26.571 -0.687 -79.743 1.00 24.47 ? 207 GLU B OE2 1 ATOM 3981 N N . GLY B 1 182 ? -25.517 -4.409 -84.708 1.00 19.13 ? 208 GLY B N 1 ATOM 3982 C CA . GLY B 1 182 ? -25.454 -5.231 -85.902 1.00 20.37 ? 208 GLY B CA 1 ATOM 3983 C C . GLY B 1 182 ? -24.164 -5.001 -86.665 1.00 26.07 ? 208 GLY B C 1 ATOM 3984 O O . GLY B 1 182 ? -23.348 -4.156 -86.278 1.00 22.45 ? 208 GLY B O 1 ATOM 3985 N N . ILE B 1 183 ? -23.967 -5.758 -87.741 1.00 25.26 ? 209 ILE B N 1 ATOM 3986 C CA . ILE B 1 183 ? -22.820 -5.541 -88.618 1.00 24.74 ? 209 ILE B CA 1 ATOM 3987 C C . ILE B 1 183 ? -23.134 -4.407 -89.588 1.00 34.58 ? 209 ILE B C 1 ATOM 3988 O O . ILE B 1 183 ? -23.990 -4.540 -90.457 1.00 31.63 ? 209 ILE B O 1 ATOM 3989 C CB . ILE B 1 183 ? -22.449 -6.807 -89.402 1.00 32.02 ? 209 ILE B CB 1 ATOM 3990 C CG1 . ILE B 1 183 ? -22.104 -7.945 -88.435 1.00 32.63 ? 209 ILE B CG1 1 ATOM 3991 C CG2 . ILE B 1 183 ? -21.288 -6.516 -90.356 1.00 29.46 ? 209 ILE B CG2 1 ATOM 3992 C CD1 . ILE B 1 183 ? -21.664 -9.229 -89.116 1.00 35.62 ? 209 ILE B CD1 1 ATOM 3993 N N . ASN B 1 184 ? -22.447 -3.284 -89.429 1.00 24.03 ? 210 ASN B N 1 ATOM 3994 C CA . ASN B 1 184 ? -22.723 -2.108 -90.251 1.00 24.86 ? 210 ASN B CA 1 ATOM 3995 C C . ASN B 1 184 ? -21.498 -1.198 -90.243 1.00 29.89 ? 210 ASN B C 1 ATOM 3996 O O . ASN B 1 184 ? -20.477 -1.560 -89.666 1.00 24.70 ? 210 ASN B O 1 ATOM 3997 C CB . ASN B 1 184 ? -23.975 -1.374 -89.737 1.00 23.67 ? 210 ASN B CB 1 ATOM 3998 C CG . ASN B 1 184 ? -23.864 -0.980 -88.275 1.00 22.23 ? 210 ASN B CG 1 ATOM 3999 O OD1 . ASN B 1 184 ? -22.822 -0.493 -87.831 1.00 23.77 ? 210 ASN B OD1 1 ATOM 4000 N ND2 . ASN B 1 184 ? -24.940 -1.189 -87.512 1.00 24.83 ? 210 ASN B ND2 1 ATOM 4001 N N . ASN B 1 185 ? -21.590 -0.028 -90.865 1.00 26.16 ? 211 ASN B N 1 ATOM 4002 C CA . ASN B 1 185 ? -20.432 0.864 -90.942 1.00 30.92 ? 211 ASN B CA 1 ATOM 4003 C C . ASN B 1 185 ? -19.972 1.363 -89.577 1.00 29.19 ? 211 ASN B C 1 ATOM 4004 O O . ASN B 1 185 ? -18.782 1.584 -89.359 1.00 26.75 ? 211 ASN B O 1 ATOM 4005 C CB . ASN B 1 185 ? -20.737 2.055 -91.847 1.00 35.58 ? 211 ASN B CB 1 ATOM 4006 C CG . ASN B 1 185 ? -20.473 1.751 -93.313 1.00 44.10 ? 211 ASN B CG 1 ATOM 4007 O OD1 . ASN B 1 185 ? -20.315 0.593 -93.695 1.00 33.45 ? 211 ASN B OD1 1 ATOM 4008 N ND2 . ASN B 1 185 ? -20.418 2.784 -94.138 1.00 55.40 ? 211 ASN B ND2 1 ATOM 4009 N N . LYS B 1 186 ? -20.907 1.536 -88.655 1.00 23.54 ? 212 LYS B N 1 ATOM 4010 C CA . LYS B 1 186 ? -20.548 2.032 -87.335 1.00 22.70 ? 212 LYS B CA 1 ATOM 4011 C C . LYS B 1 186 ? -19.804 0.959 -86.540 1.00 24.55 ? 212 LYS B C 1 ATOM 4012 O O . LYS B 1 186 ? -18.765 1.236 -85.940 1.00 25.99 ? 212 LYS B O 1 ATOM 4013 C CB . LYS B 1 186 ? -21.790 2.514 -86.566 1.00 21.37 ? 212 LYS B CB 1 ATOM 4014 C CG . LYS B 1 186 ? -21.442 3.522 -85.469 1.00 20.66 ? 212 LYS B CG 1 ATOM 4015 C CD . LYS B 1 186 ? -22.669 4.021 -84.713 1.00 22.35 ? 212 LYS B CD 1 ATOM 4016 C CE . LYS B 1 186 ? -22.273 5.098 -83.706 1.00 22.04 ? 212 LYS B CE 1 ATOM 4017 N NZ . LYS B 1 186 ? -23.434 5.521 -82.885 1.00 18.39 ? 212 LYS B NZ 1 ATOM 4018 N N . SER B 1 187 ? -20.314 -0.269 -86.535 1.00 25.34 ? 213 SER B N 1 ATOM 4019 C CA . SER B 1 187 ? -19.632 -1.334 -85.799 1.00 21.32 ? 213 SER B CA 1 ATOM 4020 C C . SER B 1 187 ? -18.302 -1.735 -86.465 1.00 24.52 ? 213 SER B C 1 ATOM 4021 O O . SER B 1 187 ? -17.354 -2.109 -85.767 1.00 22.28 ? 213 SER B O 1 ATOM 4022 C CB . SER B 1 187 ? -20.529 -2.559 -85.641 1.00 20.99 ? 213 SER B CB 1 ATOM 4023 O OG . SER B 1 187 ? -20.988 -3.022 -86.891 1.00 23.58 ? 213 SER B OG 1 ATOM 4024 N N . ASP B 1 188 ? -18.229 -1.656 -87.795 1.00 23.72 ? 214 ASP B N 1 ATOM 4025 C CA . ASP B 1 188 ? -16.965 -1.905 -88.497 1.00 25.02 ? 214 ASP B CA 1 ATOM 4026 C C . ASP B 1 188 ? -15.879 -0.954 -87.995 1.00 29.54 ? 214 ASP B C 1 ATOM 4027 O O . ASP B 1 188 ? -14.755 -1.372 -87.704 1.00 29.68 ? 214 ASP B O 1 ATOM 4028 C CB . ASP B 1 188 ? -17.119 -1.744 -90.020 1.00 26.41 ? 214 ASP B CB 1 ATOM 4029 C CG . ASP B 1 188 ? -17.931 -2.863 -90.666 1.00 41.33 ? 214 ASP B CG 1 ATOM 4030 O OD1 . ASP B 1 188 ? -18.134 -3.928 -90.040 1.00 36.15 ? 214 ASP B OD1 1 ATOM 4031 O OD2 . ASP B 1 188 ? -18.356 -2.676 -91.826 1.00 44.81 ? 214 ASP B OD2 1 ATOM 4032 N N . ALA B 1 189 ? -16.222 0.327 -87.893 1.00 27.56 ? 215 ALA B N 1 ATOM 4033 C CA . ALA B 1 189 ? -15.289 1.343 -87.413 1.00 29.64 ? 215 ALA B CA 1 ATOM 4034 C C . ALA B 1 189 ? -14.880 1.099 -85.963 1.00 34.38 ? 215 ALA B C 1 ATOM 4035 O O . ALA B 1 189 ? -13.694 1.182 -85.618 1.00 25.81 ? 215 ALA B O 1 ATOM 4036 C CB . ALA B 1 189 ? -15.894 2.721 -87.557 1.00 24.66 ? 215 ALA B CB 1 ATOM 4037 N N . LEU B 1 190 ? -15.863 0.808 -85.115 1.00 22.29 ? 216 LEU B N 1 ATOM 4038 C CA . LEU B 1 190 ? -15.597 0.499 -83.713 1.00 21.23 ? 216 LEU B CA 1 ATOM 4039 C C . LEU B 1 190 ? -14.679 -0.712 -83.597 1.00 27.77 ? 216 LEU B C 1 ATOM 4040 O O . LEU B 1 190 ? -13.730 -0.703 -82.812 1.00 21.45 ? 216 LEU B O 1 ATOM 4041 C CB . LEU B 1 190 ? -16.908 0.244 -82.942 1.00 20.02 ? 216 LEU B CB 1 ATOM 4042 C CG . LEU B 1 190 ? -16.797 -0.075 -81.444 1.00 18.94 ? 216 LEU B CG 1 ATOM 4043 C CD1 . LEU B 1 190 ? -16.217 1.103 -80.705 1.00 18.70 ? 216 LEU B CD1 1 ATOM 4044 C CD2 . LEU B 1 190 ? -18.169 -0.434 -80.862 1.00 22.53 ? 216 LEU B CD2 1 ATOM 4045 N N . LEU B 1 191 ? -14.973 -1.740 -84.393 1.00 22.16 ? 217 LEU B N 1 ATOM 4046 C CA . LEU B 1 191 ? -14.213 -2.984 -84.386 1.00 31.08 ? 217 LEU B CA 1 ATOM 4047 C C . LEU B 1 191 ? -12.746 -2.740 -84.742 1.00 33.98 ? 217 LEU B C 1 ATOM 4048 O O . LEU B 1 191 ? -11.853 -3.275 -84.090 1.00 24.72 ? 217 LEU B O 1 ATOM 4049 C CB . LEU B 1 191 ? -14.828 -3.994 -85.358 1.00 27.96 ? 217 LEU B CB 1 ATOM 4050 C CG . LEU B 1 191 ? -14.144 -5.361 -85.464 1.00 32.02 ? 217 LEU B CG 1 ATOM 4051 C CD1 . LEU B 1 191 ? -14.030 -6.033 -84.109 1.00 27.42 ? 217 LEU B CD1 1 ATOM 4052 C CD2 . LEU B 1 191 ? -14.879 -6.258 -86.448 1.00 30.46 ? 217 LEU B CD2 1 ATOM 4053 N N . ALA B 1 192 ? -12.508 -1.929 -85.770 1.00 32.45 ? 218 ALA B N 1 ATOM 4054 C CA . ALA B 1 192 ? -11.147 -1.566 -86.170 1.00 31.42 ? 218 ALA B CA 1 ATOM 4055 C C . ALA B 1 192 ? -10.392 -0.864 -85.045 1.00 36.25 ? 218 ALA B C 1 ATOM 4056 O O . ALA B 1 192 ? -9.200 -1.126 -84.824 1.00 28.78 ? 218 ALA B O 1 ATOM 4057 C CB . ALA B 1 192 ? -11.183 -0.682 -87.417 1.00 28.64 ? 218 ALA B CB 1 ATOM 4058 N N . VAL B 1 193 ? -11.077 0.023 -84.324 1.00 29.51 ? 219 VAL B N 1 ATOM 4059 C CA . VAL B 1 193 ? -10.424 0.754 -83.235 1.00 29.92 ? 219 VAL B CA 1 ATOM 4060 C C . VAL B 1 193 ? -10.170 -0.157 -82.038 1.00 27.33 ? 219 VAL B C 1 ATOM 4061 O O . VAL B 1 193 ? -9.110 -0.093 -81.405 1.00 26.56 ? 219 VAL B O 1 ATOM 4062 C CB . VAL B 1 193 ? -11.247 1.975 -82.787 1.00 28.84 ? 219 VAL B CB 1 ATOM 4063 C CG1 . VAL B 1 193 ? -10.664 2.581 -81.512 1.00 28.90 ? 219 VAL B CG1 1 ATOM 4064 C CG2 . VAL B 1 193 ? -11.283 3.012 -83.904 1.00 30.65 ? 219 VAL B CG2 1 ATOM 4065 N N . VAL B 1 194 ? -11.128 -1.022 -81.742 1.00 22.09 ? 220 VAL B N 1 ATOM 4066 C CA . VAL B 1 194 ? -10.957 -1.987 -80.664 1.00 21.49 ? 220 VAL B CA 1 ATOM 4067 C C . VAL B 1 194 ? -9.802 -2.945 -80.979 1.00 24.96 ? 220 VAL B C 1 ATOM 4068 O O . VAL B 1 194 ? -8.997 -3.269 -80.102 1.00 22.47 ? 220 VAL B O 1 ATOM 4069 C CB . VAL B 1 194 ? -12.241 -2.788 -80.421 1.00 20.68 ? 220 VAL B CB 1 ATOM 4070 C CG1 . VAL B 1 194 ? -11.961 -3.964 -79.491 1.00 22.88 ? 220 VAL B CG1 1 ATOM 4071 C CG2 . VAL B 1 194 ? -13.318 -1.870 -79.834 1.00 20.52 ? 220 VAL B CG2 1 ATOM 4072 N N . GLN B 1 195 ? -9.722 -3.379 -82.234 1.00 23.57 ? 221 GLN B N 1 ATOM 4073 C CA . GLN B 1 195 ? -8.627 -4.247 -82.673 1.00 24.76 ? 221 GLN B CA 1 ATOM 4074 C C . GLN B 1 195 ? -7.292 -3.546 -82.507 1.00 25.38 ? 221 GLN B C 1 ATOM 4075 O O . GLN B 1 195 ? -6.325 -4.142 -82.031 1.00 25.81 ? 221 GLN B O 1 ATOM 4076 C CB . GLN B 1 195 ? -8.819 -4.672 -84.126 1.00 25.89 ? 221 GLN B CB 1 ATOM 4077 C CG . GLN B 1 195 ? -9.832 -5.791 -84.307 1.00 40.07 ? 221 GLN B CG 1 ATOM 4078 C CD . GLN B 1 195 ? -10.103 -6.099 -85.772 1.00 45.84 ? 221 GLN B CD 1 ATOM 4079 O OE1 . GLN B 1 195 ? -9.848 -5.268 -86.648 1.00 48.03 ? 221 GLN B OE1 1 ATOM 4080 N NE2 . GLN B 1 195 ? -10.628 -7.295 -86.044 1.00 40.86 ? 221 GLN B NE2 1 ATOM 4081 N N . SER B 1 196 ? -7.254 -2.278 -82.901 1.00 25.54 ? 222 SER B N 1 ATOM 4082 C CA . SER B 1 196 ? -6.065 -1.457 -82.746 1.00 26.18 ? 222 SER B CA 1 ATOM 4083 C C . SER B 1 196 ? -5.704 -1.288 -81.266 1.00 29.43 ? 222 SER B C 1 ATOM 4084 O O . SER B 1 196 ? -4.553 -1.465 -80.867 1.00 25.88 ? 222 SER B O 1 ATOM 4085 C CB . SER B 1 196 ? -6.278 -0.097 -83.403 1.00 26.51 ? 222 SER B CB 1 ATOM 4086 O OG . SER B 1 196 ? -5.083 0.661 -83.388 1.00 27.39 ? 222 SER B OG 1 ATOM 4087 N N . MET B 1 197 ? -6.696 -0.969 -80.445 1.00 24.00 ? 223 MET B N 1 ATOM 4088 C CA . MET B 1 197 ? -6.435 -0.782 -79.028 1.00 25.29 ? 223 MET B CA 1 ATOM 4089 C C . MET B 1 197 ? -6.060 -2.091 -78.360 1.00 23.16 ? 223 MET B C 1 ATOM 4090 O O . MET B 1 197 ? -5.193 -2.114 -77.492 1.00 23.26 ? 223 MET B O 1 ATOM 4091 C CB . MET B 1 197 ? -7.636 -0.143 -78.336 1.00 21.95 ? 223 MET B CB 1 ATOM 4092 C CG . MET B 1 197 ? -7.693 1.349 -78.565 1.00 31.52 ? 223 MET B CG 1 ATOM 4093 S SD . MET B 1 197 ? -8.645 2.139 -77.276 1.00 27.46 ? 223 MET B SD 1 ATOM 4094 C CE . MET B 1 197 ? -10.192 1.247 -77.450 1.00 25.85 ? 223 MET B CE 1 ATOM 4095 N N . LYS B 1 198 ? -6.688 -3.183 -78.782 1.00 21.92 ? 224 LYS B N 1 ATOM 4096 C CA . LYS B 1 198 ? -6.349 -4.495 -78.240 1.00 22.95 ? 224 LYS B CA 1 ATOM 4097 C C . LYS B 1 198 ? -4.888 -4.849 -78.560 1.00 25.95 ? 224 LYS B C 1 ATOM 4098 O O . LYS B 1 198 ? -4.179 -5.416 -77.726 1.00 21.60 ? 224 LYS B O 1 ATOM 4099 C CB . LYS B 1 198 ? -7.287 -5.572 -78.782 1.00 26.03 ? 224 LYS B CB 1 ATOM 4100 C CG . LYS B 1 198 ? -7.249 -6.874 -77.995 1.00 35.58 ? 224 LYS B CG 1 ATOM 4101 C CD . LYS B 1 198 ? -7.485 -6.624 -76.510 1.00 37.95 ? 224 LYS B CD 1 ATOM 4102 C CE . LYS B 1 198 ? -7.454 -7.918 -75.706 1.00 40.34 ? 224 LYS B CE 1 ATOM 4103 N NZ . LYS B 1 198 ? -6.210 -8.701 -75.929 1.00 48.16 ? 224 LYS B NZ 1 ATOM 4104 N N . ALA B 1 199 ? -4.443 -4.490 -79.761 1.00 22.16 ? 225 ALA B N 1 ATOM 4105 C CA . ALA B 1 199 ? -3.055 -4.709 -80.178 1.00 23.00 ? 225 ALA B CA 1 ATOM 4106 C C . ALA B 1 199 ? -2.053 -3.987 -79.268 1.00 23.05 ? 225 ALA B C 1 ATOM 4107 O O . ALA B 1 199 ? -0.871 -4.356 -79.202 1.00 23.60 ? 225 ALA B O 1 ATOM 4108 C CB . ALA B 1 199 ? -2.872 -4.262 -81.638 1.00 23.86 ? 225 ALA B CB 1 ATOM 4109 N N . HIS B 1 200 ? -2.530 -2.952 -78.580 1.00 22.58 ? 226 HIS B N 1 ATOM 4110 C CA . HIS B 1 200 ? -1.703 -2.183 -77.650 1.00 22.73 ? 226 HIS B CA 1 ATOM 4111 C C . HIS B 1 200 ? -2.130 -2.385 -76.196 1.00 22.06 ? 226 HIS B C 1 ATOM 4112 O O . HIS B 1 200 ? -1.776 -1.591 -75.322 1.00 22.14 ? 226 HIS B O 1 ATOM 4113 C CB . HIS B 1 200 ? -1.733 -0.702 -78.023 1.00 23.07 ? 226 HIS B CB 1 ATOM 4114 C CG . HIS B 1 200 ? -1.100 -0.417 -79.351 1.00 25.16 ? 226 HIS B CG 1 ATOM 4115 N ND1 . HIS B 1 200 ? -1.813 -0.408 -80.531 1.00 31.31 ? 226 HIS B ND1 1 ATOM 4116 C CD2 . HIS B 1 200 ? 0.188 -0.177 -79.691 1.00 24.87 ? 226 HIS B CD2 1 ATOM 4117 C CE1 . HIS B 1 200 ? -0.995 -0.152 -81.537 1.00 28.64 ? 226 HIS B CE1 1 ATOM 4118 N NE2 . HIS B 1 200 ? 0.225 -0.007 -81.053 1.00 28.01 ? 226 HIS B NE2 1 ATOM 4119 N N . ASN B 1 201 ? -2.876 -3.463 -75.957 1.00 21.55 ? 227 ASN B N 1 ATOM 4120 C CA . ASN B 1 201 ? -3.295 -3.867 -74.617 1.00 21.07 ? 227 ASN B CA 1 ATOM 4121 C C . ASN B 1 201 ? -4.070 -2.775 -73.871 1.00 20.61 ? 227 ASN B C 1 ATOM 4122 O O . ASN B 1 201 ? -4.027 -2.704 -72.638 1.00 22.70 ? 227 ASN B O 1 ATOM 4123 C CB . ASN B 1 201 ? -2.066 -4.294 -73.789 1.00 21.57 ? 227 ASN B CB 1 ATOM 4124 C CG . ASN B 1 201 ? -1.412 -5.564 -74.326 1.00 27.20 ? 227 ASN B CG 1 ATOM 4125 O OD1 . ASN B 1 201 ? -2.091 -6.559 -74.564 1.00 32.55 ? 227 ASN B OD1 1 ATOM 4126 N ND2 . ASN B 1 201 ? -0.093 -5.525 -74.538 1.00 25.94 ? 227 ASN B ND2 1 ATOM 4127 N N . LEU B 1 202 ? -4.782 -1.930 -74.608 1.00 20.43 ? 228 LEU B N 1 ATOM 4128 C CA . LEU B 1 202 ? -5.418 -0.749 -74.006 1.00 20.17 ? 228 LEU B CA 1 ATOM 4129 C C . LEU B 1 202 ? -6.907 -0.900 -73.646 1.00 20.27 ? 228 LEU B C 1 ATOM 4130 O O . LEU B 1 202 ? -7.449 -0.059 -72.920 1.00 21.11 ? 228 LEU B O 1 ATOM 4131 C CB . LEU B 1 202 ? -5.278 0.451 -74.943 1.00 20.63 ? 228 LEU B CB 1 ATOM 4132 C CG . LEU B 1 202 ? -3.859 0.958 -75.221 1.00 21.55 ? 228 LEU B CG 1 ATOM 4133 C CD1 . LEU B 1 202 ? -3.903 2.023 -76.309 1.00 22.10 ? 228 LEU B CD1 1 ATOM 4134 C CD2 . LEU B 1 202 ? -3.251 1.519 -73.943 1.00 21.83 ? 228 LEU B CD2 1 ATOM 4135 N N . VAL B 1 203 ? -7.569 -1.933 -74.165 1.00 19.01 ? 229 VAL B N 1 ATOM 4136 C CA . VAL B 1 203 ? -9.013 -2.070 -73.952 1.00 18.29 ? 229 VAL B CA 1 ATOM 4137 C C . VAL B 1 203 ? -9.338 -3.515 -73.586 1.00 18.82 ? 229 VAL B C 1 ATOM 4138 O O . VAL B 1 203 ? -8.697 -4.450 -74.076 1.00 19.15 ? 229 VAL B O 1 ATOM 4139 C CB . VAL B 1 203 ? -9.819 -1.619 -75.208 1.00 18.20 ? 229 VAL B CB 1 ATOM 4140 C CG1 . VAL B 1 203 ? -9.667 -2.617 -76.339 1.00 18.51 ? 229 VAL B CG1 1 ATOM 4141 C CG2 . VAL B 1 203 ? -11.307 -1.388 -74.876 1.00 17.48 ? 229 VAL B CG2 1 ATOM 4142 N N . ASP B 1 204 ? -10.308 -3.696 -72.694 1.00 17.55 ? 230 ASP B N 1 ATOM 4143 C CA . ASP B 1 204 ? -10.681 -5.025 -72.230 1.00 17.46 ? 230 ASP B CA 1 ATOM 4144 C C . ASP B 1 204 ? -12.049 -5.456 -72.726 1.00 20.70 ? 230 ASP B C 1 ATOM 4145 O O . ASP B 1 204 ? -12.323 -6.651 -72.884 1.00 17.12 ? 230 ASP B O 1 ATOM 4146 C CB . ASP B 1 204 ? -10.686 -5.065 -70.702 1.00 18.27 ? 230 ASP B CB 1 ATOM 4147 C CG . ASP B 1 204 ? -9.343 -4.717 -70.125 1.00 22.69 ? 230 ASP B CG 1 ATOM 4148 O OD1 . ASP B 1 204 ? -8.355 -5.349 -70.551 1.00 25.53 ? 230 ASP B OD1 1 ATOM 4149 O OD2 . ASP B 1 204 ? -9.271 -3.793 -69.293 1.00 22.25 ? 230 ASP B OD2 1 ATOM 4150 N N . GLY B 1 205 ? -12.913 -4.479 -72.940 1.00 16.53 ? 231 GLY B N 1 ATOM 4151 C CA . GLY B 1 205 ? -14.317 -4.783 -73.153 1.00 16.03 ? 231 GLY B CA 1 ATOM 4152 C C . GLY B 1 205 ? -14.995 -3.832 -74.110 1.00 15.82 ? 231 GLY B C 1 ATOM 4153 O O . GLY B 1 205 ? -14.553 -2.692 -74.274 1.00 16.47 ? 231 GLY B O 1 ATOM 4154 N N . VAL B 1 206 ? -16.053 -4.316 -74.758 1.00 15.61 ? 232 VAL B N 1 ATOM 4155 C CA . VAL B 1 206 ? -16.919 -3.462 -75.567 1.00 15.41 ? 232 VAL B CA 1 ATOM 4156 C C . VAL B 1 206 ? -18.354 -3.533 -75.042 1.00 14.76 ? 232 VAL B C 1 ATOM 4157 O O . VAL B 1 206 ? -18.891 -4.624 -74.823 1.00 14.66 ? 232 VAL B O 1 ATOM 4158 C CB . VAL B 1 206 ? -16.904 -3.860 -77.065 1.00 15.95 ? 232 VAL B CB 1 ATOM 4159 C CG1 . VAL B 1 206 ? -17.936 -3.055 -77.845 1.00 15.83 ? 232 VAL B CG1 1 ATOM 4160 C CG2 . VAL B 1 206 ? -15.531 -3.650 -77.648 1.00 16.92 ? 232 VAL B CG2 1 ATOM 4161 N N . GLY B 1 207 ? -18.952 -2.364 -74.826 1.00 14.40 ? 233 GLY B N 1 ATOM 4162 C CA . GLY B 1 207 ? -20.330 -2.265 -74.382 1.00 13.81 ? 233 GLY B CA 1 ATOM 4163 C C . GLY B 1 207 ? -21.243 -1.925 -75.542 1.00 14.73 ? 233 GLY B C 1 ATOM 4164 O O . GLY B 1 207 ? -20.985 -0.987 -76.293 1.00 17.02 ? 233 GLY B O 1 ATOM 4165 N N . PHE B 1 208 ? -22.294 -2.719 -75.705 1.00 13.55 ? 234 PHE B N 1 ATOM 4166 C CA . PHE B 1 208 ? -23.322 -2.457 -76.707 1.00 13.57 ? 234 PHE B CA 1 ATOM 4167 C C . PHE B 1 208 ? -24.545 -1.903 -75.999 1.00 13.44 ? 234 PHE B C 1 ATOM 4168 O O . PHE B 1 208 ? -25.151 -2.603 -75.184 1.00 12.50 ? 234 PHE B O 1 ATOM 4169 C CB . PHE B 1 208 ? -23.667 -3.733 -77.467 1.00 13.93 ? 234 PHE B CB 1 ATOM 4170 C CG . PHE B 1 208 ? -22.503 -4.309 -78.220 1.00 14.70 ? 234 PHE B CG 1 ATOM 4171 C CD1 . PHE B 1 208 ? -21.634 -5.186 -77.597 1.00 18.29 ? 234 PHE B CD1 1 ATOM 4172 C CD2 . PHE B 1 208 ? -22.273 -3.962 -79.541 1.00 15.39 ? 234 PHE B CD2 1 ATOM 4173 C CE1 . PHE B 1 208 ? -20.539 -5.717 -78.279 1.00 17.43 ? 234 PHE B CE1 1 ATOM 4174 C CE2 . PHE B 1 208 ? -21.169 -4.497 -80.240 1.00 17.97 ? 234 PHE B CE2 1 ATOM 4175 C CZ . PHE B 1 208 ? -20.315 -5.371 -79.602 1.00 18.41 ? 234 PHE B CZ 1 ATOM 4176 N N . GLN B 1 209 ? -24.901 -0.655 -76.280 1.00 12.84 ? 235 GLN B N 1 ATOM 4177 C CA . GLN B 1 209 ? -25.986 -0.030 -75.520 1.00 12.25 ? 235 GLN B CA 1 ATOM 4178 C C . GLN B 1 209 ? -27.319 -0.761 -75.738 1.00 12.52 ? 235 GLN B C 1 ATOM 4179 O O . GLN B 1 209 ? -28.067 -0.982 -74.792 1.00 13.35 ? 235 GLN B O 1 ATOM 4180 C CB . GLN B 1 209 ? -26.110 1.457 -75.870 1.00 12.43 ? 235 GLN B CB 1 ATOM 4181 C CG . GLN B 1 209 ? -24.940 2.302 -75.327 1.00 13.12 ? 235 GLN B CG 1 ATOM 4182 C CD . GLN B 1 209 ? -25.091 3.771 -75.642 1.00 17.44 ? 235 GLN B CD 1 ATOM 4183 O OE1 . GLN B 1 209 ? -26.192 4.247 -75.912 1.00 17.43 ? 235 GLN B OE1 1 ATOM 4184 N NE2 . GLN B 1 209 ? -23.977 4.497 -75.632 1.00 17.05 ? 235 GLN B NE2 1 ATOM 4185 N N . CYS B 1 210 ? -27.596 -1.174 -76.969 1.00 12.35 ? 236 CYS B N 1 ATOM 4186 C CA . CYS B 1 210 ? -28.851 -1.892 -77.266 1.00 12.20 ? 236 CYS B CA 1 ATOM 4187 C C . CYS B 1 210 ? -30.121 -1.093 -76.934 1.00 17.80 ? 236 CYS B C 1 ATOM 4188 O O . CYS B 1 210 ? -31.071 -1.622 -76.329 1.00 11.75 ? 236 CYS B O 1 ATOM 4189 C CB . CYS B 1 210 ? -28.886 -3.242 -76.538 1.00 12.06 ? 236 CYS B CB 1 ATOM 4190 S SG . CYS B 1 210 ? -27.647 -4.437 -77.124 1.00 16.60 ? 236 CYS B SG 1 ATOM 4191 N N . HIS B 1 211 ? -30.155 0.173 -77.340 1.00 11.80 ? 237 HIS B N 1 ATOM 4192 C CA . HIS B 1 211 ? -31.416 0.910 -77.328 1.00 12.61 ? 237 HIS B CA 1 ATOM 4193 C C . HIS B 1 211 ? -32.161 0.589 -78.607 1.00 19.27 ? 237 HIS B C 1 ATOM 4194 O O . HIS B 1 211 ? -31.981 1.269 -79.608 1.00 20.92 ? 237 HIS B O 1 ATOM 4195 C CB . HIS B 1 211 ? -31.217 2.426 -77.225 1.00 11.60 ? 237 HIS B CB 1 ATOM 4196 C CG . HIS B 1 211 ? -30.560 2.862 -75.956 1.00 11.30 ? 237 HIS B CG 1 ATOM 4197 N ND1 . HIS B 1 211 ? -31.216 2.867 -74.743 1.00 11.87 ? 237 HIS B ND1 1 ATOM 4198 C CD2 . HIS B 1 211 ? -29.304 3.306 -75.712 1.00 12.02 ? 237 HIS B CD2 1 ATOM 4199 C CE1 . HIS B 1 211 ? -30.388 3.291 -73.802 1.00 13.20 ? 237 HIS B CE1 1 ATOM 4200 N NE2 . HIS B 1 211 ? -29.218 3.550 -74.361 1.00 11.33 ? 237 HIS B NE2 1 ATOM 4201 N N . PHE B 1 212 ? -32.991 -0.447 -78.576 1.00 11.76 ? 238 PHE B N 1 ATOM 4202 C CA . PHE B 1 212 ? -33.659 -0.929 -79.778 1.00 12.35 ? 238 PHE B CA 1 ATOM 4203 C C . PHE B 1 212 ? -35.100 -0.441 -79.873 1.00 12.09 ? 238 PHE B C 1 ATOM 4204 O O . PHE B 1 212 ? -35.706 -0.099 -78.859 1.00 11.33 ? 238 PHE B O 1 ATOM 4205 C CB . PHE B 1 212 ? -33.682 -2.458 -79.815 1.00 18.92 ? 238 PHE B CB 1 ATOM 4206 C CG . PHE B 1 212 ? -32.331 -3.098 -79.940 1.00 13.02 ? 238 PHE B CG 1 ATOM 4207 C CD1 . PHE B 1 212 ? -31.492 -2.793 -81.006 1.00 19.00 ? 238 PHE B CD1 1 ATOM 4208 C CD2 . PHE B 1 212 ? -31.917 -4.047 -79.005 1.00 12.75 ? 238 PHE B CD2 1 ATOM 4209 C CE1 . PHE B 1 212 ? -30.250 -3.398 -81.126 1.00 18.64 ? 238 PHE B CE1 1 ATOM 4210 C CE2 . PHE B 1 212 ? -30.677 -4.670 -79.124 1.00 13.23 ? 238 PHE B CE2 1 ATOM 4211 C CZ . PHE B 1 212 ? -29.838 -4.341 -80.183 1.00 13.95 ? 238 PHE B CZ 1 ATOM 4212 N N . PHE B 1 213 ? -35.634 -0.431 -81.098 1.00 12.81 ? 239 PHE B N 1 ATOM 4213 C CA . PHE B 1 213 ? -37.072 -0.316 -81.318 1.00 12.71 ? 239 PHE B CA 1 ATOM 4214 C C . PHE B 1 213 ? -37.607 -1.724 -81.538 1.00 13.30 ? 239 PHE B C 1 ATOM 4215 O O . PHE B 1 213 ? -36.977 -2.537 -82.237 1.00 13.73 ? 239 PHE B O 1 ATOM 4216 C CB . PHE B 1 213 ? -37.404 0.583 -82.525 1.00 13.76 ? 239 PHE B CB 1 ATOM 4217 C CG . PHE B 1 213 ? -38.818 1.099 -82.510 1.00 16.14 ? 239 PHE B CG 1 ATOM 4218 C CD1 . PHE B 1 213 ? -39.871 0.284 -82.894 1.00 15.72 ? 239 PHE B CD1 1 ATOM 4219 C CD2 . PHE B 1 213 ? -39.095 2.384 -82.071 1.00 16.70 ? 239 PHE B CD2 1 ATOM 4220 C CE1 . PHE B 1 213 ? -41.172 0.742 -82.830 1.00 16.27 ? 239 PHE B CE1 1 ATOM 4221 C CE2 . PHE B 1 213 ? -40.394 2.851 -82.019 1.00 16.20 ? 239 PHE B CE2 1 ATOM 4222 C CZ . PHE B 1 213 ? -41.435 2.039 -82.407 1.00 14.49 ? 239 PHE B CZ 1 ATOM 4223 N N . VAL B 1 214 ? -38.753 -2.028 -80.938 1.00 13.42 ? 240 VAL B N 1 ATOM 4224 C CA . VAL B 1 214 ? -39.308 -3.370 -81.054 1.00 12.71 ? 240 VAL B CA 1 ATOM 4225 C C . VAL B 1 214 ? -39.404 -3.824 -82.525 1.00 13.96 ? 240 VAL B C 1 ATOM 4226 O O . VAL B 1 214 ? -39.775 -3.047 -83.410 1.00 14.45 ? 240 VAL B O 1 ATOM 4227 C CB . VAL B 1 214 ? -40.702 -3.452 -80.373 1.00 15.83 ? 240 VAL B CB 1 ATOM 4228 C CG1 . VAL B 1 214 ? -41.693 -2.513 -81.048 1.00 14.17 ? 240 VAL B CG1 1 ATOM 4229 C CG2 . VAL B 1 214 ? -41.218 -4.879 -80.385 1.00 17.48 ? 240 VAL B CG2 1 ATOM 4230 N N . GLY B 1 215 ? -39.026 -5.075 -82.777 1.00 14.61 ? 241 GLY B N 1 ATOM 4231 C CA . GLY B 1 215 ? -39.104 -5.664 -84.104 1.00 15.97 ? 241 GLY B CA 1 ATOM 4232 C C . GLY B 1 215 ? -38.020 -5.176 -85.051 1.00 17.80 ? 241 GLY B C 1 ATOM 4233 O O . GLY B 1 215 ? -38.017 -5.511 -86.243 1.00 22.26 ? 241 GLY B O 1 ATOM 4234 N N . GLU B 1 216 ? -37.089 -4.383 -84.532 1.00 16.99 ? 242 GLU B N 1 ATOM 4235 C CA . GLU B 1 216 ? -36.067 -3.803 -85.393 1.00 16.90 ? 242 GLU B CA 1 ATOM 4236 C C . GLU B 1 216 ? -34.663 -4.109 -84.909 1.00 18.36 ? 242 GLU B C 1 ATOM 4237 O O . GLU B 1 216 ? -33.743 -3.319 -85.110 1.00 21.33 ? 242 GLU B O 1 ATOM 4238 C CB . GLU B 1 216 ? -36.286 -2.297 -85.514 1.00 23.44 ? 242 GLU B CB 1 ATOM 4239 C CG . GLU B 1 216 ? -37.603 -1.974 -86.216 1.00 24.59 ? 242 GLU B CG 1 ATOM 4240 C CD . GLU B 1 216 ? -37.856 -0.490 -86.378 1.00 37.19 ? 242 GLU B CD 1 ATOM 4241 O OE1 . GLU B 1 216 ? -36.977 0.322 -86.025 1.00 47.09 ? 242 GLU B OE1 1 ATOM 4242 O OE2 . GLU B 1 216 ? -38.951 -0.138 -86.855 1.00 48.73 ? 242 GLU B OE2 1 ATOM 4243 N N . LEU B 1 217 ? -34.488 -5.275 -84.298 1.00 17.70 ? 243 LEU B N 1 ATOM 4244 C CA . LEU B 1 217 ? -33.151 -5.723 -83.925 1.00 16.54 ? 243 LEU B CA 1 ATOM 4245 C C . LEU B 1 217 ? -32.374 -6.089 -85.186 1.00 18.80 ? 243 LEU B C 1 ATOM 4246 O O . LEU B 1 217 ? -32.954 -6.542 -86.166 1.00 22.80 ? 243 LEU B O 1 ATOM 4247 C CB . LEU B 1 217 ? -33.214 -6.915 -82.972 1.00 18.84 ? 243 LEU B CB 1 ATOM 4248 C CG . LEU B 1 217 ? -33.329 -6.542 -81.490 1.00 18.40 ? 243 LEU B CG 1 ATOM 4249 C CD1 . LEU B 1 217 ? -34.600 -5.728 -81.214 1.00 14.62 ? 243 LEU B CD1 1 ATOM 4250 C CD2 . LEU B 1 217 ? -33.275 -7.806 -80.620 1.00 17.18 ? 243 LEU B CD2 1 ATOM 4251 N N . PRO B 1 218 ? -31.058 -5.873 -85.177 1.00 20.65 ? 244 PRO B N 1 ATOM 4252 C CA . PRO B 1 218 ? -30.326 -6.278 -86.379 1.00 19.44 ? 244 PRO B CA 1 ATOM 4253 C C . PRO B 1 218 ? -30.365 -7.794 -86.532 1.00 21.60 ? 244 PRO B C 1 ATOM 4254 O O . PRO B 1 218 ? -30.281 -8.514 -85.535 1.00 27.60 ? 244 PRO B O 1 ATOM 4255 C CB . PRO B 1 218 ? -28.903 -5.774 -86.120 1.00 25.93 ? 244 PRO B CB 1 ATOM 4256 C CG . PRO B 1 218 ? -28.813 -5.565 -84.640 1.00 26.50 ? 244 PRO B CG 1 ATOM 4257 C CD . PRO B 1 218 ? -30.199 -5.248 -84.158 1.00 23.61 ? 244 PRO B CD 1 ATOM 4258 N N . PRO B 1 219 ? -30.497 -8.280 -87.763 1.00 21.64 ? 245 PRO B N 1 ATOM 4259 C CA . PRO B 1 219 ? -30.583 -9.729 -87.977 1.00 32.64 ? 245 PRO B CA 1 ATOM 4260 C C . PRO B 1 219 ? -29.254 -10.440 -87.729 1.00 30.26 ? 245 PRO B C 1 ATOM 4261 O O . PRO B 1 219 ? -29.252 -11.661 -87.571 1.00 36.03 ? 245 PRO B O 1 ATOM 4262 C CB . PRO B 1 219 ? -30.997 -9.840 -89.450 1.00 33.48 ? 245 PRO B CB 1 ATOM 4263 C CG . PRO B 1 219 ? -30.424 -8.610 -90.077 1.00 40.94 ? 245 PRO B CG 1 ATOM 4264 C CD . PRO B 1 219 ? -30.536 -7.525 -89.029 1.00 36.24 ? 245 PRO B CD 1 ATOM 4265 N N . ASP B 1 220 ? -28.150 -9.694 -87.696 1.00 23.62 ? 246 ASP B N 1 ATOM 4266 C CA . ASP B 1 220 ? -26.825 -10.292 -87.466 1.00 22.84 ? 246 ASP B CA 1 ATOM 4267 C C . ASP B 1 220 ? -26.215 -9.908 -86.111 1.00 22.44 ? 246 ASP B C 1 ATOM 4268 O O . ASP B 1 220 ? -24.991 -9.805 -85.972 1.00 24.90 ? 246 ASP B O 1 ATOM 4269 C CB . ASP B 1 220 ? -25.859 -9.915 -88.596 1.00 28.93 ? 246 ASP B CB 1 ATOM 4270 C CG . ASP B 1 220 ? -26.027 -8.474 -89.075 1.00 43.67 ? 246 ASP B CG 1 ATOM 4271 O OD1 . ASP B 1 220 ? -26.570 -7.632 -88.328 1.00 34.07 ? 246 ASP B OD1 1 ATOM 4272 O OD2 . ASP B 1 220 ? -25.605 -8.182 -90.217 1.00 54.81 ? 246 ASP B OD2 1 ATOM 4273 N N . LEU B 1 221 ? -27.077 -9.716 -85.116 1.00 20.23 ? 247 LEU B N 1 ATOM 4274 C CA . LEU B 1 221 ? -26.665 -9.413 -83.744 1.00 18.98 ? 247 LEU B CA 1 ATOM 4275 C C . LEU B 1 221 ? -25.633 -10.397 -83.186 1.00 23.37 ? 247 LEU B C 1 ATOM 4276 O O . LEU B 1 221 ? -24.556 -9.989 -82.730 1.00 19.41 ? 247 LEU B O 1 ATOM 4277 C CB . LEU B 1 221 ? -27.900 -9.386 -82.828 1.00 20.57 ? 247 LEU B CB 1 ATOM 4278 C CG . LEU B 1 221 ? -27.690 -9.002 -81.363 1.00 20.12 ? 247 LEU B CG 1 ATOM 4279 C CD1 . LEU B 1 221 ? -27.160 -7.591 -81.279 1.00 19.86 ? 247 LEU B CD1 1 ATOM 4280 C CD2 . LEU B 1 221 ? -28.987 -9.119 -80.563 1.00 19.79 ? 247 LEU B CD2 1 ATOM 4281 N N . GLU B 1 222 ? -25.949 -11.690 -83.211 1.00 20.86 ? 248 GLU B N 1 ATOM 4282 C CA . GLU B 1 222 ? -25.050 -12.686 -82.620 1.00 21.93 ? 248 GLU B CA 1 ATOM 4283 C C . GLU B 1 222 ? -23.731 -12.765 -83.378 1.00 21.11 ? 248 GLU B C 1 ATOM 4284 O O . GLU B 1 222 ? -22.654 -12.872 -82.768 1.00 23.93 ? 248 GLU B O 1 ATOM 4285 C CB . GLU B 1 222 ? -25.715 -14.065 -82.571 1.00 32.13 ? 248 GLU B CB 1 ATOM 4286 C CG . GLU B 1 222 ? -24.943 -15.093 -81.731 1.00 27.91 ? 248 GLU B CG 1 ATOM 4287 C CD . GLU B 1 222 ? -23.811 -15.762 -82.492 1.00 50.18 ? 248 GLU B CD 1 ATOM 4288 O OE1 . GLU B 1 222 ? -24.016 -16.092 -83.682 1.00 63.73 ? 248 GLU B OE1 1 ATOM 4289 O OE2 . GLU B 1 222 ? -22.715 -15.956 -81.904 1.00 48.65 ? 248 GLU B OE2 1 ATOM 4290 N N . GLN B 1 223 ? -23.808 -12.705 -84.703 1.00 22.14 ? 249 GLN B N 1 ATOM 4291 C CA . GLN B 1 223 ? -22.609 -12.711 -85.537 1.00 28.66 ? 249 GLN B CA 1 ATOM 4292 C C . GLN B 1 223 ? -21.722 -11.502 -85.215 1.00 22.25 ? 249 GLN B C 1 ATOM 4293 O O . GLN B 1 223 ? -20.505 -11.618 -85.120 1.00 22.49 ? 249 GLN B O 1 ATOM 4294 C CB . GLN B 1 223 ? -22.991 -12.725 -87.022 1.00 31.56 ? 249 GLN B CB 1 ATOM 4295 C CG . GLN B 1 223 ? -21.811 -12.820 -87.986 1.00 45.82 ? 249 GLN B CG 1 ATOM 4296 C CD . GLN B 1 223 ? -22.257 -12.992 -89.438 1.00 57.20 ? 249 GLN B CD 1 ATOM 4297 O OE1 . GLN B 1 223 ? -23.401 -12.694 -89.791 1.00 57.27 ? 249 GLN B OE1 1 ATOM 4298 N NE2 . GLN B 1 223 ? -21.351 -13.469 -90.284 1.00 64.10 ? 249 GLN B NE2 1 ATOM 4299 N N . ASN B 1 224 ? -22.329 -10.338 -85.029 1.00 22.34 ? 250 ASN B N 1 ATOM 4300 C CA . ASN B 1 224 ? -21.537 -9.164 -84.680 1.00 20.68 ? 250 ASN B CA 1 ATOM 4301 C C . ASN B 1 224 ? -20.901 -9.297 -83.283 1.00 24.17 ? 250 ASN B C 1 ATOM 4302 O O . ASN B 1 224 ? -19.725 -8.972 -83.107 1.00 25.49 ? 250 ASN B O 1 ATOM 4303 C CB . ASN B 1 224 ? -22.390 -7.895 -84.767 1.00 20.05 ? 250 ASN B CB 1 ATOM 4304 C CG . ASN B 1 224 ? -21.583 -6.634 -84.526 1.00 19.63 ? 250 ASN B CG 1 ATOM 4305 O OD1 . ASN B 1 224 ? -20.552 -6.413 -85.165 1.00 21.27 ? 250 ASN B OD1 1 ATOM 4306 N ND2 . ASN B 1 224 ? -22.035 -5.811 -83.586 1.00 18.53 ? 250 ASN B ND2 1 ATOM 4307 N N . PHE B 1 225 ? -21.661 -9.781 -82.299 1.00 26.26 ? 251 PHE B N 1 ATOM 4308 C CA . PHE B 1 225 ? -21.108 -10.016 -80.960 1.00 26.06 ? 251 PHE B CA 1 ATOM 4309 C C . PHE B 1 225 ? -19.895 -10.949 -81.047 1.00 19.24 ? 251 PHE B C 1 ATOM 4310 O O . PHE B 1 225 ? -18.865 -10.716 -80.408 1.00 19.00 ? 251 PHE B O 1 ATOM 4311 C CB . PHE B 1 225 ? -22.156 -10.625 -80.015 1.00 24.20 ? 251 PHE B CB 1 ATOM 4312 C CG . PHE B 1 225 ? -23.154 -9.624 -79.450 1.00 18.72 ? 251 PHE B CG 1 ATOM 4313 C CD1 . PHE B 1 225 ? -23.174 -8.306 -79.881 1.00 16.54 ? 251 PHE B CD1 1 ATOM 4314 C CD2 . PHE B 1 225 ? -24.063 -10.020 -78.474 1.00 19.80 ? 251 PHE B CD2 1 ATOM 4315 C CE1 . PHE B 1 225 ? -24.100 -7.390 -79.348 1.00 23.77 ? 251 PHE B CE1 1 ATOM 4316 C CE2 . PHE B 1 225 ? -24.994 -9.112 -77.935 1.00 21.75 ? 251 PHE B CE2 1 ATOM 4317 C CZ . PHE B 1 225 ? -25.014 -7.799 -78.388 1.00 17.91 ? 251 PHE B CZ 1 ATOM 4318 N N . ALA B 1 226 ? -20.021 -11.994 -81.859 1.00 20.50 ? 252 ALA B N 1 ATOM 4319 C CA . ALA B 1 226 ? -18.969 -13.010 -81.989 1.00 25.67 ? 252 ALA B CA 1 ATOM 4320 C C . ALA B 1 226 ? -17.662 -12.472 -82.559 1.00 27.47 ? 252 ALA B C 1 ATOM 4321 O O . ALA B 1 226 ? -16.579 -12.901 -82.142 1.00 28.94 ? 252 ALA B O 1 ATOM 4322 C CB . ALA B 1 226 ? -19.459 -14.176 -82.847 1.00 23.14 ? 252 ALA B CB 1 ATOM 4323 N N . ARG B 1 227 ? -17.732 -11.562 -83.527 1.00 25.13 ? 253 ARG B N 1 ATOM 4324 C CA . ARG B 1 227 ? -16.488 -11.064 -84.103 1.00 25.65 ? 253 ARG B CA 1 ATOM 4325 C C . ARG B 1 227 ? -15.776 -10.104 -83.148 1.00 29.76 ? 253 ARG B C 1 ATOM 4326 O O . ARG B 1 227 ? -14.565 -9.935 -83.231 1.00 21.67 ? 253 ARG B O 1 ATOM 4327 C CB . ARG B 1 227 ? -16.731 -10.400 -85.457 1.00 29.47 ? 253 ARG B CB 1 ATOM 4328 C CG . ARG B 1 227 ? -17.363 -9.047 -85.416 1.00 25.88 ? 253 ARG B CG 1 ATOM 4329 C CD . ARG B 1 227 ? -17.658 -8.572 -86.843 1.00 29.10 ? 253 ARG B CD 1 ATOM 4330 N NE . ARG B 1 227 ? -18.348 -7.289 -86.807 1.00 30.80 ? 253 ARG B NE 1 ATOM 4331 C CZ . ARG B 1 227 ? -18.244 -6.346 -87.733 1.00 23.37 ? 253 ARG B CZ 1 ATOM 4332 N NH1 . ARG B 1 227 ? -17.462 -6.534 -88.791 1.00 27.41 ? 253 ARG B NH1 1 ATOM 4333 N NH2 . ARG B 1 227 ? -18.930 -5.211 -87.600 1.00 22.81 ? 253 ARG B NH2 1 ATOM 4334 N N . PHE B 1 228 ? -16.511 -9.491 -82.223 1.00 25.09 ? 254 PHE B N 1 ATOM 4335 C CA . PHE B 1 228 ? -15.857 -8.670 -81.199 1.00 19.45 ? 254 PHE B CA 1 ATOM 4336 C C . PHE B 1 228 ? -15.169 -9.558 -80.177 1.00 19.40 ? 254 PHE B C 1 ATOM 4337 O O . PHE B 1 228 ? -14.037 -9.299 -79.767 1.00 19.44 ? 254 PHE B O 1 ATOM 4338 C CB . PHE B 1 228 ? -16.867 -7.736 -80.518 1.00 18.42 ? 254 PHE B CB 1 ATOM 4339 C CG . PHE B 1 228 ? -17.044 -6.441 -81.240 1.00 22.43 ? 254 PHE B CG 1 ATOM 4340 C CD1 . PHE B 1 228 ? -17.924 -6.344 -82.312 1.00 24.28 ? 254 PHE B CD1 1 ATOM 4341 C CD2 . PHE B 1 228 ? -16.313 -5.325 -80.876 1.00 20.46 ? 254 PHE B CD2 1 ATOM 4342 C CE1 . PHE B 1 228 ? -18.083 -5.148 -82.988 1.00 19.03 ? 254 PHE B CE1 1 ATOM 4343 C CE2 . PHE B 1 228 ? -16.457 -4.125 -81.562 1.00 18.41 ? 254 PHE B CE2 1 ATOM 4344 C CZ . PHE B 1 228 ? -17.345 -4.037 -82.614 1.00 25.37 ? 254 PHE B CZ 1 ATOM 4345 N N . VAL B 1 229 ? -15.865 -10.609 -79.767 1.00 21.35 ? 255 VAL B N 1 ATOM 4346 C CA . VAL B 1 229 ? -15.284 -11.601 -78.882 1.00 22.29 ? 255 VAL B CA 1 ATOM 4347 C C . VAL B 1 229 ? -14.052 -12.209 -79.559 1.00 28.63 ? 255 VAL B C 1 ATOM 4348 O O . VAL B 1 229 ? -13.030 -12.436 -78.911 1.00 23.65 ? 255 VAL B O 1 ATOM 4349 C CB . VAL B 1 229 ? -16.307 -12.702 -78.528 1.00 24.07 ? 255 VAL B CB 1 ATOM 4350 C CG1 . VAL B 1 229 ? -15.621 -13.858 -77.818 1.00 24.67 ? 255 VAL B CG1 1 ATOM 4351 C CG2 . VAL B 1 229 ? -17.462 -12.115 -77.684 1.00 18.77 ? 255 VAL B CG2 1 ATOM 4352 N N . ALA B 1 230 ? -14.147 -12.428 -80.873 1.00 23.35 ? 256 ALA B N 1 ATOM 4353 C CA . ALA B 1 230 ? -13.049 -13.003 -81.654 1.00 23.65 ? 256 ALA B CA 1 ATOM 4354 C C . ALA B 1 230 ? -11.823 -12.100 -81.635 1.00 29.25 ? 256 ALA B C 1 ATOM 4355 O O . ALA B 1 230 ? -10.703 -12.567 -81.821 1.00 28.23 ? 256 ALA B O 1 ATOM 4356 C CB . ALA B 1 230 ? -13.491 -13.264 -83.098 1.00 23.55 ? 256 ALA B CB 1 ATOM 4357 N N . ALA B 1 231 ? -12.032 -10.805 -81.415 1.00 26.46 ? 257 ALA B N 1 ATOM 4358 C CA . ALA B 1 231 ? -10.916 -9.867 -81.368 1.00 25.81 ? 257 ALA B CA 1 ATOM 4359 C C . ALA B 1 231 ? -10.290 -9.821 -79.978 1.00 27.83 ? 257 ALA B C 1 ATOM 4360 O O . ALA B 1 231 ? -9.395 -9.019 -79.722 1.00 30.85 ? 257 ALA B O 1 ATOM 4361 C CB . ALA B 1 231 ? -11.357 -8.479 -81.787 1.00 21.20 ? 257 ALA B CB 1 ATOM 4362 N N . GLY B 1 232 ? -10.759 -10.680 -79.081 1.00 22.90 ? 258 GLY B N 1 ATOM 4363 C CA . GLY B 1 232 ? -10.145 -10.799 -77.773 1.00 20.46 ? 258 GLY B CA 1 ATOM 4364 C C . GLY B 1 232 ? -10.681 -9.893 -76.678 1.00 24.86 ? 258 GLY B C 1 ATOM 4365 O O . GLY B 1 232 ? -10.029 -9.703 -75.655 1.00 23.49 ? 258 GLY B O 1 ATOM 4366 N N . VAL B 1 233 ? -11.867 -9.331 -76.862 1.00 26.92 ? 259 VAL B N 1 ATOM 4367 C CA . VAL B 1 233 ? -12.452 -8.558 -75.776 1.00 23.95 ? 259 VAL B CA 1 ATOM 4368 C C . VAL B 1 233 ? -13.637 -9.285 -75.177 1.00 22.12 ? 259 VAL B C 1 ATOM 4369 O O . VAL B 1 233 ? -14.231 -10.156 -75.805 1.00 20.66 ? 259 VAL B O 1 ATOM 4370 C CB . VAL B 1 233 ? -12.916 -7.162 -76.222 1.00 21.06 ? 259 VAL B CB 1 ATOM 4371 C CG1 . VAL B 1 233 ? -11.723 -6.308 -76.628 1.00 29.35 ? 259 VAL B CG1 1 ATOM 4372 C CG2 . VAL B 1 233 ? -13.969 -7.271 -77.336 1.00 20.99 ? 259 VAL B CG2 1 ATOM 4373 N N . GLU B 1 234 ? -13.978 -8.921 -73.953 1.00 19.28 ? 260 GLU B N 1 ATOM 4374 C CA . GLU B 1 234 ? -15.233 -9.358 -73.377 1.00 18.39 ? 260 GLU B CA 1 ATOM 4375 C C . GLU B 1 234 ? -16.289 -8.359 -73.830 1.00 16.29 ? 260 GLU B C 1 ATOM 4376 O O . GLU B 1 234 ? -15.963 -7.260 -74.279 1.00 16.14 ? 260 GLU B O 1 ATOM 4377 C CB . GLU B 1 234 ? -15.151 -9.449 -71.848 1.00 19.12 ? 260 GLU B CB 1 ATOM 4378 C CG . GLU B 1 234 ? -15.020 -8.115 -71.111 1.00 18.64 ? 260 GLU B CG 1 ATOM 4379 C CD . GLU B 1 234 ? -15.001 -8.291 -69.587 1.00 25.28 ? 260 GLU B CD 1 ATOM 4380 O OE1 . GLU B 1 234 ? -14.113 -9.016 -69.088 1.00 20.59 ? 260 GLU B OE1 1 ATOM 4381 O OE2 . GLU B 1 234 ? -15.872 -7.718 -68.885 1.00 17.22 ? 260 GLU B OE2 1 ATOM 4382 N N . ILE B 1 235 ? -17.549 -8.756 -73.767 1.00 16.01 ? 261 ILE B N 1 ATOM 4383 C CA . ILE B 1 235 ? -18.609 -7.839 -74.136 1.00 15.41 ? 261 ILE B CA 1 ATOM 4384 C C . ILE B 1 235 ? -19.700 -7.836 -73.079 1.00 14.87 ? 261 ILE B C 1 ATOM 4385 O O . ILE B 1 235 ? -19.791 -8.743 -72.243 1.00 16.46 ? 261 ILE B O 1 ATOM 4386 C CB . ILE B 1 235 ? -19.235 -8.185 -75.512 1.00 17.05 ? 261 ILE B CB 1 ATOM 4387 C CG1 . ILE B 1 235 ? -20.079 -9.457 -75.424 1.00 20.12 ? 261 ILE B CG1 1 ATOM 4388 C CG2 . ILE B 1 235 ? -18.179 -8.330 -76.578 1.00 18.86 ? 261 ILE B CG2 1 ATOM 4389 C CD1 . ILE B 1 235 ? -20.900 -9.702 -76.663 1.00 22.54 ? 261 ILE B CD1 1 ATOM 4390 N N . ALA B 1 236 ? -20.519 -6.792 -73.125 1.00 14.29 ? 262 ALA B N 1 ATOM 4391 C CA . ALA B 1 236 ? -21.663 -6.649 -72.250 1.00 13.77 ? 262 ALA B CA 1 ATOM 4392 C C . ALA B 1 236 ? -22.726 -5.842 -72.967 1.00 13.31 ? 262 ALA B C 1 ATOM 4393 O O . ALA B 1 236 ? -22.425 -4.954 -73.773 1.00 13.34 ? 262 ALA B O 1 ATOM 4394 C CB . ALA B 1 236 ? -21.282 -5.960 -70.929 1.00 13.60 ? 262 ALA B CB 1 ATOM 4395 N N . VAL B 1 237 ? -23.972 -6.167 -72.664 1.00 12.99 ? 263 VAL B N 1 ATOM 4396 C CA . VAL B 1 237 ? -25.084 -5.342 -73.078 1.00 16.00 ? 263 VAL B CA 1 ATOM 4397 C C . VAL B 1 237 ? -25.287 -4.306 -71.972 1.00 12.64 ? 263 VAL B C 1 ATOM 4398 O O . VAL B 1 237 ? -25.562 -4.663 -70.827 1.00 14.33 ? 263 VAL B O 1 ATOM 4399 C CB . VAL B 1 237 ? -26.337 -6.189 -73.298 1.00 15.18 ? 263 VAL B CB 1 ATOM 4400 C CG1 . VAL B 1 237 ? -27.573 -5.294 -73.481 1.00 15.23 ? 263 VAL B CG1 1 ATOM 4401 C CG2 . VAL B 1 237 ? -26.119 -7.124 -74.493 1.00 15.64 ? 263 VAL B CG2 1 ATOM 4402 N N . THR B 1 238 ? -25.137 -3.029 -72.299 1.00 11.92 ? 264 THR B N 1 ATOM 4403 C CA . THR B 1 238 ? -24.967 -2.033 -71.253 1.00 11.75 ? 264 THR B CA 1 ATOM 4404 C C . THR B 1 238 ? -26.170 -1.135 -70.962 1.00 12.21 ? 264 THR B C 1 ATOM 4405 O O . THR B 1 238 ? -26.268 -0.613 -69.858 1.00 11.37 ? 264 THR B O 1 ATOM 4406 C CB . THR B 1 238 ? -23.777 -1.116 -71.574 1.00 12.63 ? 264 THR B CB 1 ATOM 4407 O OG1 . THR B 1 238 ? -23.936 -0.575 -72.891 1.00 12.24 ? 264 THR B OG1 1 ATOM 4408 C CG2 . THR B 1 238 ? -22.457 -1.912 -71.509 1.00 12.60 ? 264 THR B CG2 1 ATOM 4409 N N . GLU B 1 239 ? -27.066 -0.924 -71.926 1.00 11.10 ? 265 GLU B N 1 ATOM 4410 C CA . GLU B 1 239 ? -28.186 0.017 -71.699 1.00 10.71 ? 265 GLU B CA 1 ATOM 4411 C C . GLU B 1 239 ? -29.495 -0.468 -72.345 1.00 11.48 ? 265 GLU B C 1 ATOM 4412 O O . GLU B 1 239 ? -30.210 0.311 -72.984 1.00 12.59 ? 265 GLU B O 1 ATOM 4413 C CB . GLU B 1 239 ? -27.834 1.421 -72.232 1.00 10.96 ? 265 GLU B CB 1 ATOM 4414 C CG . GLU B 1 239 ? -26.469 1.971 -71.729 1.00 11.40 ? 265 GLU B CG 1 ATOM 4415 C CD . GLU B 1 239 ? -26.126 3.381 -72.227 1.00 20.89 ? 265 GLU B CD 1 ATOM 4416 O OE1 . GLU B 1 239 ? -27.018 4.067 -72.757 1.00 18.02 ? 265 GLU B OE1 1 ATOM 4417 O OE2 . GLU B 1 239 ? -24.953 3.803 -72.071 1.00 22.63 ? 265 GLU B OE2 1 ATOM 4418 N N . LEU B 1 240 ? -29.795 -1.749 -72.193 1.00 10.40 ? 266 LEU B N 1 ATOM 4419 C CA . LEU B 1 240 ? -30.888 -2.363 -72.938 1.00 10.32 ? 266 LEU B CA 1 ATOM 4420 C C . LEU B 1 240 ? -32.263 -1.741 -72.640 1.00 9.84 ? 266 LEU B C 1 ATOM 4421 O O . LEU B 1 240 ? -32.671 -1.620 -71.483 1.00 9.73 ? 266 LEU B O 1 ATOM 4422 C CB . LEU B 1 240 ? -30.932 -3.862 -72.650 1.00 10.54 ? 266 LEU B CB 1 ATOM 4423 C CG . LEU B 1 240 ? -31.998 -4.703 -73.348 1.00 11.59 ? 266 LEU B CG 1 ATOM 4424 C CD1 . LEU B 1 240 ? -31.872 -4.645 -74.880 1.00 11.09 ? 266 LEU B CD1 1 ATOM 4425 C CD2 . LEU B 1 240 ? -31.849 -6.127 -72.853 1.00 11.03 ? 266 LEU B CD2 1 ATOM 4426 N N . ASP B 1 241 ? -32.944 -1.320 -73.696 1.00 9.86 ? 267 ASP B N 1 ATOM 4427 C CA . ASP B 1 241 ? -34.390 -1.116 -73.639 1.00 9.49 ? 267 ASP B CA 1 ATOM 4428 C C . ASP B 1 241 ? -34.945 -1.261 -75.049 1.00 9.82 ? 267 ASP B C 1 ATOM 4429 O O . ASP B 1 241 ? -34.244 -1.055 -76.040 1.00 11.44 ? 267 ASP B O 1 ATOM 4430 C CB . ASP B 1 241 ? -34.784 0.231 -72.994 1.00 9.14 ? 267 ASP B CB 1 ATOM 4431 C CG . ASP B 1 241 ? -33.987 1.421 -73.503 1.00 10.94 ? 267 ASP B CG 1 ATOM 4432 O OD1 . ASP B 1 241 ? -33.563 1.447 -74.684 1.00 13.55 ? 267 ASP B OD1 1 ATOM 4433 O OD2 . ASP B 1 241 ? -33.823 2.382 -72.703 1.00 18.12 ? 267 ASP B OD2 1 ATOM 4434 N N . ILE B 1 242 ? -36.191 -1.695 -75.137 1.00 9.65 ? 268 ILE B N 1 ATOM 4435 C CA . ILE B 1 242 ? -36.769 -2.036 -76.420 1.00 10.11 ? 268 ILE B CA 1 ATOM 4436 C C . ILE B 1 242 ? -38.128 -1.369 -76.517 1.00 9.80 ? 268 ILE B C 1 ATOM 4437 O O . ILE B 1 242 ? -39.121 -1.873 -75.999 1.00 9.49 ? 268 ILE B O 1 ATOM 4438 C CB . ILE B 1 242 ? -36.867 -3.569 -76.605 1.00 10.51 ? 268 ILE B CB 1 ATOM 4439 C CG1 . ILE B 1 242 ? -35.472 -4.194 -76.387 1.00 10.82 ? 268 ILE B CG1 1 ATOM 4440 C CG2 . ILE B 1 242 ? -37.400 -3.905 -78.017 1.00 11.21 ? 268 ILE B CG2 1 ATOM 4441 C CD1 . ILE B 1 242 ? -35.403 -5.691 -76.538 1.00 13.94 ? 268 ILE B CD1 1 ATOM 4442 N N . ARG B 1 243 ? -38.147 -0.219 -77.184 1.00 10.32 ? 269 ARG B N 1 ATOM 4443 C CA . ARG B 1 243 ? -39.282 0.686 -77.097 1.00 9.67 ? 269 ARG B CA 1 ATOM 4444 C C . ARG B 1 243 ? -40.303 0.469 -78.213 1.00 13.93 ? 269 ARG B C 1 ATOM 4445 O O . ARG B 1 243 ? -40.049 -0.238 -79.189 1.00 10.78 ? 269 ARG B O 1 ATOM 4446 C CB . ARG B 1 243 ? -38.784 2.131 -77.093 1.00 9.76 ? 269 ARG B CB 1 ATOM 4447 C CG . ARG B 1 243 ? -38.068 2.560 -78.363 1.00 10.59 ? 269 ARG B CG 1 ATOM 4448 C CD . ARG B 1 243 ? -37.413 3.925 -78.187 1.00 13.16 ? 269 ARG B CD 1 ATOM 4449 N NE . ARG B 1 243 ? -36.968 4.504 -79.458 1.00 12.87 ? 269 ARG B NE 1 ATOM 4450 C CZ . ARG B 1 243 ? -35.798 4.251 -80.029 1.00 19.68 ? 269 ARG B CZ 1 ATOM 4451 N NH1 . ARG B 1 243 ? -34.936 3.430 -79.443 1.00 17.77 ? 269 ARG B NH1 1 ATOM 4452 N NH2 . ARG B 1 243 ? -35.485 4.823 -81.185 1.00 23.89 ? 269 ARG B NH2 1 ATOM 4453 N N . MET B 1 244 ? -41.470 1.083 -78.051 1.00 10.62 ? 270 MET B N 1 ATOM 4454 C CA . MET B 1 244 ? -42.581 0.901 -78.985 1.00 10.89 ? 270 MET B CA 1 ATOM 4455 C C . MET B 1 244 ? -43.519 2.088 -78.872 1.00 13.89 ? 270 MET B C 1 ATOM 4456 O O . MET B 1 244 ? -43.470 2.805 -77.878 1.00 11.81 ? 270 MET B O 1 ATOM 4457 C CB . MET B 1 244 ? -43.324 -0.401 -78.683 1.00 10.04 ? 270 MET B CB 1 ATOM 4458 C CG . MET B 1 244 ? -44.075 -0.440 -77.317 1.00 11.32 ? 270 MET B CG 1 ATOM 4459 S SD . MET B 1 244 ? -44.708 -2.098 -76.866 1.00 14.41 ? 270 MET B SD 1 ATOM 4460 C CE . MET B 1 244 ? -43.170 -2.979 -76.581 1.00 10.92 ? 270 MET B CE 1 ATOM 4461 N N . ASN B 1 245 ? -44.364 2.300 -79.880 1.00 10.89 ? 271 ASN B N 1 ATOM 4462 C CA . ASN B 1 245 ? -45.415 3.314 -79.783 1.00 13.98 ? 271 ASN B CA 1 ATOM 4463 C C . ASN B 1 245 ? -46.416 2.996 -78.685 1.00 16.35 ? 271 ASN B C 1 ATOM 4464 O O . ASN B 1 245 ? -46.716 1.829 -78.429 1.00 13.33 ? 271 ASN B O 1 ATOM 4465 C CB . ASN B 1 245 ? -46.173 3.460 -81.110 1.00 15.02 ? 271 ASN B CB 1 ATOM 4466 C CG . ASN B 1 245 ? -45.397 4.233 -82.132 1.00 26.34 ? 271 ASN B CG 1 ATOM 4467 O OD1 . ASN B 1 245 ? -44.427 4.905 -81.804 1.00 24.12 ? 271 ASN B OD1 1 ATOM 4468 N ND2 . ASN B 1 245 ? -45.823 4.154 -83.386 1.00 28.15 ? 271 ASN B ND2 1 ATOM 4469 N N . LEU B 1 246 ? -46.935 4.044 -78.050 1.00 11.45 ? 272 LEU B N 1 ATOM 4470 C CA . LEU B 1 246 ? -47.948 3.908 -77.003 1.00 16.26 ? 272 LEU B CA 1 ATOM 4471 C C . LEU B 1 246 ? -49.335 4.305 -77.539 1.00 12.88 ? 272 LEU B C 1 ATOM 4472 O O . LEU B 1 246 ? -49.434 5.141 -78.430 1.00 17.69 ? 272 LEU B O 1 ATOM 4473 C CB . LEU B 1 246 ? -47.584 4.767 -75.784 1.00 18.18 ? 272 LEU B CB 1 ATOM 4474 C CG . LEU B 1 246 ? -46.205 4.558 -75.132 1.00 13.95 ? 272 LEU B CG 1 ATOM 4475 C CD1 . LEU B 1 246 ? -46.017 5.574 -74.019 1.00 18.59 ? 272 LEU B CD1 1 ATOM 4476 C CD2 . LEU B 1 246 ? -46.045 3.128 -74.586 1.00 7.80 ? 272 LEU B CD2 1 ATOM 4477 N N . PRO B 1 247 ? -50.403 3.686 -77.023 1.00 12.27 ? 273 PRO B N 1 ATOM 4478 C CA . PRO B 1 247 ? -50.400 2.535 -76.110 1.00 17.36 ? 273 PRO B CA 1 ATOM 4479 C C . PRO B 1 247 ? -49.905 1.274 -76.824 1.00 16.36 ? 273 PRO B C 1 ATOM 4480 O O . PRO B 1 247 ? -50.021 1.180 -78.051 1.00 13.78 ? 273 PRO B O 1 ATOM 4481 C CB . PRO B 1 247 ? -51.870 2.405 -75.699 1.00 19.26 ? 273 PRO B CB 1 ATOM 4482 C CG . PRO B 1 247 ? -52.627 3.028 -76.808 1.00 18.18 ? 273 PRO B CG 1 ATOM 4483 C CD . PRO B 1 247 ? -51.773 4.126 -77.361 1.00 16.74 ? 273 PRO B CD 1 ATOM 4484 N N . PRO B 1 248 ? -49.327 0.332 -76.075 1.00 15.87 ? 274 PRO B N 1 ATOM 4485 C CA . PRO B 1 248 ? -48.681 -0.815 -76.724 1.00 12.24 ? 274 PRO B CA 1 ATOM 4486 C C . PRO B 1 248 ? -49.674 -1.758 -77.396 1.00 15.58 ? 274 PRO B C 1 ATOM 4487 O O . PRO B 1 248 ? -50.692 -2.103 -76.798 1.00 15.30 ? 274 PRO B O 1 ATOM 4488 C CB . PRO B 1 248 ? -47.973 -1.523 -75.567 1.00 14.44 ? 274 PRO B CB 1 ATOM 4489 C CG . PRO B 1 248 ? -47.936 -0.532 -74.457 1.00 17.20 ? 274 PRO B CG 1 ATOM 4490 C CD . PRO B 1 248 ? -49.136 0.324 -74.614 1.00 15.71 ? 274 PRO B CD 1 ATOM 4491 N N . SER B 1 249 ? -49.387 -2.162 -78.625 1.00 13.21 ? 275 SER B N 1 ATOM 4492 C CA . SER B 1 249 ? -50.208 -3.167 -79.295 1.00 14.30 ? 275 SER B CA 1 ATOM 4493 C C . SER B 1 249 ? -49.854 -4.559 -78.788 1.00 14.76 ? 275 SER B C 1 ATOM 4494 O O . SER B 1 249 ? -48.731 -4.793 -78.326 1.00 12.87 ? 275 SER B O 1 ATOM 4495 C CB . SER B 1 249 ? -50.003 -3.110 -80.807 1.00 17.78 ? 275 SER B CB 1 ATOM 4496 O OG . SER B 1 249 ? -48.661 -3.468 -81.122 1.00 15.67 ? 275 SER B OG 1 ATOM 4497 N N . GLN B 1 250 ? -50.801 -5.486 -78.897 1.00 15.19 ? 276 GLN B N 1 ATOM 4498 C CA . GLN B 1 250 ? -50.537 -6.878 -78.570 1.00 24.62 ? 276 GLN B CA 1 ATOM 4499 C C . GLN B 1 250 ? -49.378 -7.418 -79.394 1.00 16.89 ? 276 GLN B C 1 ATOM 4500 O O . GLN B 1 250 ? -48.559 -8.187 -78.886 1.00 14.47 ? 276 GLN B O 1 ATOM 4501 C CB . GLN B 1 250 ? -51.783 -7.737 -78.793 1.00 27.09 ? 276 GLN B CB 1 ATOM 4502 C CG . GLN B 1 250 ? -52.926 -7.400 -77.847 1.00 39.33 ? 276 GLN B CG 1 ATOM 4503 C CD . GLN B 1 250 ? -54.144 -8.292 -78.046 1.00 47.71 ? 276 GLN B CD 1 ATOM 4504 O OE1 . GLN B 1 250 ? -54.214 -9.071 -79.002 1.00 51.70 ? 276 GLN B OE1 1 ATOM 4505 N NE2 . GLN B 1 250 ? -55.113 -8.178 -77.143 1.00 44.62 ? 276 GLN B NE2 1 ATOM 4506 N N . ALA B 1 251 ? -49.274 -6.987 -80.647 1.00 15.41 ? 277 ALA B N 1 ATOM 4507 C CA . ALA B 1 251 ? -48.209 -7.499 -81.495 1.00 15.37 ? 277 ALA B CA 1 ATOM 4508 C C . ALA B 1 251 ? -46.850 -7.001 -80.998 1.00 16.41 ? 277 ALA B C 1 ATOM 4509 O O . ALA B 1 251 ? -45.891 -7.775 -80.932 1.00 13.47 ? 277 ALA B O 1 ATOM 4510 C CB . ALA B 1 251 ? -48.436 -7.107 -82.955 1.00 16.53 ? 277 ALA B CB 1 ATOM 4511 N N . ASP B 1 252 ? -46.765 -5.726 -80.625 1.00 12.98 ? 278 ASP B N 1 ATOM 4512 C CA . ASP B 1 252 ? -45.487 -5.174 -80.155 1.00 11.74 ? 278 ASP B CA 1 ATOM 4513 C C . ASP B 1 252 ? -45.101 -5.752 -78.795 1.00 18.14 ? 278 ASP B C 1 ATOM 4514 O O . ASP B 1 252 ? -43.931 -6.000 -78.532 1.00 10.20 ? 278 ASP B O 1 ATOM 4515 C CB . ASP B 1 252 ? -45.537 -3.645 -80.085 1.00 15.69 ? 278 ASP B CB 1 ATOM 4516 C CG . ASP B 1 252 ? -45.346 -2.990 -81.461 1.00 21.91 ? 278 ASP B CG 1 ATOM 4517 O OD1 . ASP B 1 252 ? -45.025 -3.726 -82.417 1.00 19.25 ? 278 ASP B OD1 1 ATOM 4518 O OD2 . ASP B 1 252 ? -45.502 -1.751 -81.591 1.00 22.45 ? 278 ASP B OD2 1 ATOM 4519 N N . ILE B 1 253 ? -46.084 -5.973 -77.933 1.00 11.13 ? 279 ILE B N 1 ATOM 4520 C CA . ILE B 1 253 ? -45.825 -6.607 -76.646 1.00 10.74 ? 279 ILE B CA 1 ATOM 4521 C C . ILE B 1 253 ? -45.196 -8.000 -76.819 1.00 12.63 ? 279 ILE B C 1 ATOM 4522 O O . ILE B 1 253 ? -44.234 -8.345 -76.131 1.00 10.49 ? 279 ILE B O 1 ATOM 4523 C CB . ILE B 1 253 ? -47.131 -6.709 -75.817 1.00 13.43 ? 279 ILE B CB 1 ATOM 4524 C CG1 . ILE B 1 253 ? -47.550 -5.325 -75.326 1.00 15.20 ? 279 ILE B CG1 1 ATOM 4525 C CG2 . ILE B 1 253 ? -46.958 -7.619 -74.615 1.00 13.45 ? 279 ILE B CG2 1 ATOM 4526 C CD1 . ILE B 1 253 ? -48.986 -5.323 -74.770 1.00 21.32 ? 279 ILE B CD1 1 ATOM 4527 N N . GLU B 1 254 ? -45.747 -8.793 -77.728 1.00 12.70 ? 280 GLU B N 1 ATOM 4528 C CA . GLU B 1 254 ? -45.234 -10.146 -77.982 1.00 16.15 ? 280 GLU B CA 1 ATOM 4529 C C . GLU B 1 254 ? -43.875 -10.113 -78.661 1.00 12.39 ? 280 GLU B C 1 ATOM 4530 O O . GLU B 1 254 ? -43.004 -10.885 -78.315 1.00 12.37 ? 280 GLU B O 1 ATOM 4531 C CB . GLU B 1 254 ? -46.220 -10.959 -78.836 1.00 14.66 ? 280 GLU B CB 1 ATOM 4532 C CG . GLU B 1 254 ? -47.527 -11.258 -78.125 1.00 60.67 ? 280 GLU B CG 1 ATOM 4533 C CD . GLU B 1 254 ? -47.309 -11.984 -76.808 1.00 69.53 ? 280 GLU B CD 1 ATOM 4534 O OE1 . GLU B 1 254 ? -46.839 -13.144 -76.844 1.00 74.08 ? 280 GLU B OE1 1 ATOM 4535 O OE2 . GLU B 1 254 ? -47.595 -11.393 -75.739 1.00 66.39 ? 280 GLU B OE2 1 ATOM 4536 N N . GLN B 1 255 ? -43.703 -9.220 -79.632 1.00 12.21 ? 281 GLN B N 1 ATOM 4537 C CA . GLN B 1 255 ? -42.425 -9.089 -80.307 1.00 11.97 ? 281 GLN B CA 1 ATOM 4538 C C . GLN B 1 255 ? -41.341 -8.628 -79.329 1.00 11.69 ? 281 GLN B C 1 ATOM 4539 O O . GLN B 1 255 ? -40.193 -9.076 -79.402 1.00 13.64 ? 281 GLN B O 1 ATOM 4540 C CB . GLN B 1 255 ? -42.546 -8.121 -81.485 1.00 12.37 ? 281 GLN B CB 1 ATOM 4541 C CG . GLN B 1 255 ? -41.249 -8.021 -82.329 1.00 12.64 ? 281 GLN B CG 1 ATOM 4542 C CD . GLN B 1 255 ? -40.752 -9.369 -82.818 1.00 20.88 ? 281 GLN B CD 1 ATOM 4543 O OE1 . GLN B 1 255 ? -41.532 -10.212 -83.258 1.00 17.97 ? 281 GLN B OE1 1 ATOM 4544 N NE2 . GLN B 1 255 ? -39.445 -9.583 -82.726 1.00 14.51 ? 281 GLN B NE2 1 ATOM 4545 N N . GLN B 1 256 ? -41.704 -7.755 -78.392 1.00 9.86 ? 282 GLN B N 1 ATOM 4546 C CA . GLN B 1 256 ? -40.737 -7.298 -77.383 1.00 8.88 ? 282 GLN B CA 1 ATOM 4547 C C . GLN B 1 256 ? -40.216 -8.477 -76.563 1.00 11.46 ? 282 GLN B C 1 ATOM 4548 O O . GLN B 1 256 ? -39.030 -8.549 -76.254 1.00 10.48 ? 282 GLN B O 1 ATOM 4549 C CB . GLN B 1 256 ? -41.348 -6.257 -76.446 1.00 8.35 ? 282 GLN B CB 1 ATOM 4550 C CG . GLN B 1 256 ? -40.372 -5.787 -75.339 1.00 11.03 ? 282 GLN B CG 1 ATOM 4551 C CD . GLN B 1 256 ? -41.026 -4.904 -74.296 1.00 11.59 ? 282 GLN B CD 1 ATOM 4552 O OE1 . GLN B 1 256 ? -41.928 -5.337 -73.571 1.00 11.38 ? 282 GLN B OE1 1 ATOM 4553 N NE2 . GLN B 1 256 ? -40.558 -3.659 -74.196 1.00 11.55 ? 282 GLN B NE2 1 ATOM 4554 N N . ALA B 1 257 ? -41.110 -9.392 -76.203 1.00 11.77 ? 283 ALA B N 1 ATOM 4555 C CA . ALA B 1 257 ? -40.712 -10.597 -75.485 1.00 10.19 ? 283 ALA B CA 1 ATOM 4556 C C . ALA B 1 257 ? -39.706 -11.391 -76.319 1.00 16.32 ? 283 ALA B C 1 ATOM 4557 O O . ALA B 1 257 ? -38.687 -11.838 -75.803 1.00 16.80 ? 283 ALA B O 1 ATOM 4558 C CB . ALA B 1 257 ? -41.950 -11.459 -75.144 1.00 13.18 ? 283 ALA B CB 1 ATOM 4559 N N . ARG B 1 258 ? -39.985 -11.560 -77.610 1.00 11.58 ? 284 ARG B N 1 ATOM 4560 C CA . ARG B 1 258 ? -39.049 -12.278 -78.483 1.00 12.16 ? 284 ARG B CA 1 ATOM 4561 C C . ARG B 1 258 ? -37.709 -11.554 -78.620 1.00 12.35 ? 284 ARG B C 1 ATOM 4562 O O . ARG B 1 258 ? -36.660 -12.203 -78.668 1.00 14.68 ? 284 ARG B O 1 ATOM 4563 C CB . ARG B 1 258 ? -39.669 -12.512 -79.867 1.00 13.95 ? 284 ARG B CB 1 ATOM 4564 C CG . ARG B 1 258 ? -40.761 -13.577 -79.856 1.00 19.65 ? 284 ARG B CG 1 ATOM 4565 C CD . ARG B 1 258 ? -41.261 -13.926 -81.268 1.00 24.20 ? 284 ARG B CD 1 ATOM 4566 N NE . ARG B 1 258 ? -41.950 -12.799 -81.869 1.00 31.12 ? 284 ARG B NE 1 ATOM 4567 C CZ . ARG B 1 258 ? -43.271 -12.689 -81.972 1.00 28.75 ? 284 ARG B CZ 1 ATOM 4568 N NH1 . ARG B 1 258 ? -44.062 -13.658 -81.529 1.00 28.28 ? 284 ARG B NH1 1 ATOM 4569 N NH2 . ARG B 1 258 ? -43.794 -11.604 -82.530 1.00 16.44 ? 284 ARG B NH2 1 ATOM 4570 N N . ASP B 1 259 ? -37.745 -10.223 -78.670 1.00 11.24 ? 285 ASP B N 1 ATOM 4571 C CA . ASP B 1 259 ? -36.537 -9.404 -78.797 1.00 15.47 ? 285 ASP B CA 1 ATOM 4572 C C . ASP B 1 259 ? -35.643 -9.486 -77.561 1.00 12.51 ? 285 ASP B C 1 ATOM 4573 O O . ASP B 1 259 ? -34.430 -9.636 -77.681 1.00 11.49 ? 285 ASP B O 1 ATOM 4574 C CB . ASP B 1 259 ? -36.897 -7.941 -79.066 1.00 13.70 ? 285 ASP B CB 1 ATOM 4575 C CG . ASP B 1 259 ? -37.520 -7.732 -80.439 1.00 22.75 ? 285 ASP B CG 1 ATOM 4576 O OD1 . ASP B 1 259 ? -37.287 -8.557 -81.361 1.00 21.23 ? 285 ASP B OD1 1 ATOM 4577 O OD2 . ASP B 1 259 ? -38.233 -6.721 -80.597 1.00 16.13 ? 285 ASP B OD2 1 ATOM 4578 N N . TYR B 1 260 ? -36.228 -9.390 -76.370 1.00 11.10 ? 286 TYR B N 1 ATOM 4579 C CA . TYR B 1 260 ? -35.424 -9.589 -75.164 1.00 8.89 ? 286 TYR B CA 1 ATOM 4580 C C . TYR B 1 260 ? -34.762 -10.970 -75.176 1.00 10.94 ? 286 TYR B C 1 ATOM 4581 O O . TYR B 1 260 ? -33.583 -11.092 -74.857 1.00 13.38 ? 286 TYR B O 1 ATOM 4582 C CB . TYR B 1 260 ? -36.269 -9.402 -73.904 1.00 8.21 ? 286 TYR B CB 1 ATOM 4583 C CG . TYR B 1 260 ? -36.252 -7.985 -73.357 1.00 10.10 ? 286 TYR B CG 1 ATOM 4584 C CD1 . TYR B 1 260 ? -35.266 -7.577 -72.458 1.00 9.22 ? 286 TYR B CD1 1 ATOM 4585 C CD2 . TYR B 1 260 ? -37.230 -7.055 -73.727 1.00 11.84 ? 286 TYR B CD2 1 ATOM 4586 C CE1 . TYR B 1 260 ? -35.246 -6.275 -71.945 1.00 9.37 ? 286 TYR B CE1 1 ATOM 4587 C CE2 . TYR B 1 260 ? -37.218 -5.753 -73.231 1.00 10.75 ? 286 TYR B CE2 1 ATOM 4588 C CZ . TYR B 1 260 ? -36.222 -5.369 -72.337 1.00 17.96 ? 286 TYR B CZ 1 ATOM 4589 O OH . TYR B 1 260 ? -36.204 -4.077 -71.836 1.00 11.24 ? 286 TYR B OH 1 ATOM 4590 N N . ALA B 1 261 ? -35.506 -12.008 -75.561 1.00 10.74 ? 287 ALA B N 1 ATOM 4591 C CA . ALA B 1 261 ? -34.923 -13.352 -75.612 1.00 11.54 ? 287 ALA B CA 1 ATOM 4592 C C . ALA B 1 261 ? -33.820 -13.432 -76.669 1.00 16.66 ? 287 ALA B C 1 ATOM 4593 O O . ALA B 1 261 ? -32.821 -14.129 -76.477 1.00 17.23 ? 287 ALA B O 1 ATOM 4594 C CB . ALA B 1 261 ? -36.001 -14.411 -75.890 1.00 12.75 ? 287 ALA B CB 1 ATOM 4595 N N . THR B 1 262 ? -33.985 -12.710 -77.775 1.00 15.16 ? 288 THR B N 1 ATOM 4596 C CA . THR B 1 262 ? -32.954 -12.701 -78.819 1.00 17.96 ? 288 THR B CA 1 ATOM 4597 C C . THR B 1 262 ? -31.635 -12.116 -78.305 1.00 15.47 ? 288 THR B C 1 ATOM 4598 O O . THR B 1 262 ? -30.550 -12.644 -78.579 1.00 13.02 ? 288 THR B O 1 ATOM 4599 C CB . THR B 1 262 ? -33.409 -11.901 -80.041 1.00 21.94 ? 288 THR B CB 1 ATOM 4600 O OG1 . THR B 1 262 ? -34.505 -12.579 -80.656 1.00 16.77 ? 288 THR B OG1 1 ATOM 4601 C CG2 . THR B 1 262 ? -32.278 -11.777 -81.051 1.00 21.08 ? 288 THR B CG2 1 ATOM 4602 N N . VAL B 1 263 ? -31.742 -11.018 -77.569 1.00 10.91 ? 289 VAL B N 1 ATOM 4603 C CA . VAL B 1 263 ? -30.572 -10.377 -76.994 1.00 10.63 ? 289 VAL B CA 1 ATOM 4604 C C . VAL B 1 263 ? -29.911 -11.307 -75.981 1.00 14.36 ? 289 VAL B C 1 ATOM 4605 O O . VAL B 1 263 ? -28.692 -11.433 -75.967 1.00 14.62 ? 289 VAL B O 1 ATOM 4606 C CB . VAL B 1 263 ? -30.929 -9.036 -76.306 1.00 11.38 ? 289 VAL B CB 1 ATOM 4607 C CG1 . VAL B 1 263 ? -29.715 -8.474 -75.584 1.00 11.25 ? 289 VAL B CG1 1 ATOM 4608 C CG2 . VAL B 1 263 ? -31.464 -8.025 -77.324 1.00 9.43 ? 289 VAL B CG2 1 ATOM 4609 N N . VAL B 1 264 ? -30.709 -11.957 -75.132 1.00 10.91 ? 290 VAL B N 1 ATOM 4610 C CA . VAL B 1 264 ? -30.146 -12.906 -74.162 1.00 11.63 ? 290 VAL B CA 1 ATOM 4611 C C . VAL B 1 264 ? -29.410 -14.039 -74.880 1.00 13.92 ? 290 VAL B C 1 ATOM 4612 O O . VAL B 1 264 ? -28.284 -14.413 -74.507 1.00 13.79 ? 290 VAL B O 1 ATOM 4613 C CB . VAL B 1 264 ? -31.221 -13.507 -73.237 1.00 18.23 ? 290 VAL B CB 1 ATOM 4614 C CG1 . VAL B 1 264 ? -30.659 -14.719 -72.455 1.00 14.93 ? 290 VAL B CG1 1 ATOM 4615 C CG2 . VAL B 1 264 ? -31.751 -12.442 -72.284 1.00 12.23 ? 290 VAL B CG2 1 ATOM 4616 N N . ASN B 1 265 ? -30.031 -14.558 -75.934 1.00 20.20 ? 291 ASN B N 1 ATOM 4617 C CA . ASN B 1 265 ? -29.445 -15.648 -76.697 1.00 15.94 ? 291 ASN B CA 1 ATOM 4618 C C . ASN B 1 265 ? -28.132 -15.243 -77.363 1.00 19.83 ? 291 ASN B C 1 ATOM 4619 O O . ASN B 1 265 ? -27.178 -16.016 -77.376 1.00 22.31 ? 291 ASN B O 1 ATOM 4620 C CB . ASN B 1 265 ? -30.440 -16.158 -77.744 1.00 22.17 ? 291 ASN B CB 1 ATOM 4621 C CG . ASN B 1 265 ? -31.626 -16.872 -77.111 1.00 33.29 ? 291 ASN B CG 1 ATOM 4622 O OD1 . ASN B 1 265 ? -31.543 -17.350 -75.978 1.00 35.99 ? 291 ASN B OD1 1 ATOM 4623 N ND2 . ASN B 1 265 ? -32.729 -16.951 -77.841 1.00 31.85 ? 291 ASN B ND2 1 ATOM 4624 N N . ALA B 1 266 ? -28.076 -14.028 -77.901 1.00 16.13 ? 292 ALA B N 1 ATOM 4625 C CA . ALA B 1 266 ? -26.860 -13.571 -78.567 1.00 19.41 ? 292 ALA B CA 1 ATOM 4626 C C . ALA B 1 266 ? -25.731 -13.442 -77.547 1.00 19.16 ? 292 ALA B C 1 ATOM 4627 O O . ALA B 1 266 ? -24.564 -13.728 -77.850 1.00 18.67 ? 292 ALA B O 1 ATOM 4628 C CB . ALA B 1 266 ? -27.101 -12.261 -79.291 1.00 17.92 ? 292 ALA B CB 1 ATOM 4629 N N . CYS B 1 267 ? -26.090 -13.026 -76.333 1.00 21.17 ? 293 CYS B N 1 ATOM 4630 C CA A CYS B 1 267 ? -25.121 -12.965 -75.234 0.56 22.09 ? 293 CYS B CA 1 ATOM 4631 C CA B CYS B 1 267 ? -25.162 -12.978 -75.211 0.44 23.66 ? 293 CYS B CA 1 ATOM 4632 C C . CYS B 1 267 ? -24.624 -14.359 -74.861 1.00 21.96 ? 293 CYS B C 1 ATOM 4633 O O . CYS B 1 267 ? -23.412 -14.610 -74.884 1.00 22.55 ? 293 CYS B O 1 ATOM 4634 C CB A CYS B 1 267 ? -25.719 -12.279 -73.997 0.56 26.54 ? 293 CYS B CB 1 ATOM 4635 C CB B CYS B 1 267 ? -25.860 -12.369 -73.994 0.44 27.97 ? 293 CYS B CB 1 ATOM 4636 S SG A CYS B 1 267 ? -24.612 -12.254 -72.541 0.56 18.71 ? 293 CYS B SG 1 ATOM 4637 S SG B CYS B 1 267 ? -26.173 -10.609 -74.153 0.44 37.77 ? 293 CYS B SG 1 ATOM 4638 N N . LYS B 1 268 ? -25.543 -15.266 -74.544 1.00 16.12 ? 294 LYS B N 1 ATOM 4639 C CA . LYS B 1 268 ? -25.159 -16.602 -74.090 1.00 24.23 ? 294 LYS B CA 1 ATOM 4640 C C . LYS B 1 268 ? -24.375 -17.371 -75.141 1.00 28.15 ? 294 LYS B C 1 ATOM 4641 O O . LYS B 1 268 ? -23.577 -18.241 -74.799 1.00 28.40 ? 294 LYS B O 1 ATOM 4642 C CB . LYS B 1 268 ? -26.386 -17.412 -73.676 1.00 29.74 ? 294 LYS B CB 1 ATOM 4643 C CG . LYS B 1 268 ? -27.207 -16.774 -72.559 1.00 30.02 ? 294 LYS B CG 1 ATOM 4644 C CD . LYS B 1 268 ? -28.382 -17.654 -72.199 1.00 34.23 ? 294 LYS B CD 1 ATOM 4645 C CE . LYS B 1 268 ? -27.905 -19.007 -71.721 1.00 38.79 ? 294 LYS B CE 1 ATOM 4646 N NZ . LYS B 1 268 ? -29.043 -19.925 -71.476 1.00 36.05 ? 294 LYS B NZ 1 ATOM 4647 N N . ALA B 1 269 ? -24.581 -17.048 -76.417 1.00 19.34 ? 295 ALA B N 1 ATOM 4648 C CA . ALA B 1 269 ? -23.850 -17.738 -77.473 1.00 23.89 ? 295 ALA B CA 1 ATOM 4649 C C . ALA B 1 269 ? -22.350 -17.431 -77.393 1.00 27.21 ? 295 ALA B C 1 ATOM 4650 O O . ALA B 1 269 ? -21.540 -18.105 -78.017 1.00 23.85 ? 295 ALA B O 1 ATOM 4651 C CB . ALA B 1 269 ? -24.404 -17.361 -78.840 1.00 21.77 ? 295 ALA B CB 1 ATOM 4652 N N . GLN B 1 270 ? -21.987 -16.419 -76.613 1.00 21.99 ? 296 GLN B N 1 ATOM 4653 C CA . GLN B 1 270 ? -20.588 -15.994 -76.502 1.00 23.91 ? 296 GLN B CA 1 ATOM 4654 C C . GLN B 1 270 ? -19.877 -16.630 -75.314 1.00 25.08 ? 296 GLN B C 1 ATOM 4655 O O . GLN B 1 270 ? -18.717 -16.322 -75.038 1.00 27.23 ? 296 GLN B O 1 ATOM 4656 C CB . GLN B 1 270 ? -20.502 -14.469 -76.375 1.00 20.23 ? 296 GLN B CB 1 ATOM 4657 C CG . GLN B 1 270 ? -21.340 -13.703 -77.378 1.00 20.84 ? 296 GLN B CG 1 ATOM 4658 C CD . GLN B 1 270 ? -21.176 -14.212 -78.801 1.00 28.35 ? 296 GLN B CD 1 ATOM 4659 O OE1 . GLN B 1 270 ? -20.069 -14.526 -79.233 1.00 28.21 ? 296 GLN B OE1 1 ATOM 4660 N NE2 . GLN B 1 270 ? -22.286 -14.299 -79.535 1.00 24.06 ? 296 GLN B NE2 1 ATOM 4661 N N . GLY B 1 271 ? -20.586 -17.486 -74.589 1.00 28.36 ? 297 GLY B N 1 ATOM 4662 C CA . GLY B 1 271 ? -20.037 -18.106 -73.400 1.00 28.54 ? 297 GLY B CA 1 ATOM 4663 C C . GLY B 1 271 ? -19.568 -17.109 -72.355 1.00 25.22 ? 297 GLY B C 1 ATOM 4664 O O . GLY B 1 271 ? -20.219 -16.098 -72.087 1.00 25.11 ? 297 GLY B O 1 ATOM 4665 N N . ALA B 1 272 ? -18.409 -17.394 -71.777 1.00 26.05 ? 298 ALA B N 1 ATOM 4666 C CA . ALA B 1 272 ? -17.876 -16.608 -70.674 1.00 25.45 ? 298 ALA B CA 1 ATOM 4667 C C . ALA B 1 272 ? -17.487 -15.186 -71.092 1.00 22.83 ? 298 ALA B C 1 ATOM 4668 O O . ALA B 1 272 ? -17.300 -14.318 -70.243 1.00 25.55 ? 298 ALA B O 1 ATOM 4669 C CB . ALA B 1 272 ? -16.677 -17.327 -70.064 1.00 31.10 ? 298 ALA B CB 1 ATOM 4670 N N . ALA B 1 273 ? -17.376 -14.962 -72.398 1.00 22.87 ? 299 ALA B N 1 ATOM 4671 C CA . ALA B 1 273 ? -16.970 -13.675 -72.956 1.00 22.45 ? 299 ALA B CA 1 ATOM 4672 C C . ALA B 1 273 ? -18.065 -12.610 -72.862 1.00 22.80 ? 299 ALA B C 1 ATOM 4673 O O . ALA B 1 273 ? -17.774 -11.421 -72.898 1.00 21.45 ? 299 ALA B O 1 ATOM 4674 C CB . ALA B 1 273 ? -16.539 -13.848 -74.409 1.00 23.52 ? 299 ALA B CB 1 ATOM 4675 N N . CYS B 1 274 ? -19.322 -13.027 -72.760 1.00 20.89 ? 300 CYS B N 1 ATOM 4676 C CA . CYS B 1 274 ? -20.391 -12.069 -72.486 1.00 17.41 ? 300 CYS B CA 1 ATOM 4677 C C . CYS B 1 274 ? -20.702 -12.121 -70.997 1.00 18.47 ? 300 CYS B C 1 ATOM 4678 O O . CYS B 1 274 ? -21.204 -13.131 -70.500 1.00 21.94 ? 300 CYS B O 1 ATOM 4679 C CB . CYS B 1 274 ? -21.648 -12.364 -73.311 1.00 16.49 ? 300 CYS B CB 1 ATOM 4680 S SG . CYS B 1 274 ? -22.967 -11.131 -72.987 1.00 26.54 ? 300 CYS B SG 1 ATOM 4681 N N . VAL B 1 275 ? -20.401 -11.044 -70.277 1.00 16.75 ? 301 VAL B N 1 ATOM 4682 C CA . VAL B 1 275 ? -20.388 -11.115 -68.825 1.00 17.00 ? 301 VAL B CA 1 ATOM 4683 C C . VAL B 1 275 ? -21.688 -10.664 -68.159 1.00 18.50 ? 301 VAL B C 1 ATOM 4684 O O . VAL B 1 275 ? -21.915 -10.951 -66.986 1.00 16.03 ? 301 VAL B O 1 ATOM 4685 C CB . VAL B 1 275 ? -19.229 -10.277 -68.246 1.00 29.05 ? 301 VAL B CB 1 ATOM 4686 C CG1 . VAL B 1 275 ? -17.874 -10.824 -68.725 1.00 19.63 ? 301 VAL B CG1 1 ATOM 4687 C CG2 . VAL B 1 275 ? -19.386 -8.826 -68.639 1.00 17.18 ? 301 VAL B CG2 1 ATOM 4688 N N . GLY B 1 276 ? -22.538 -9.958 -68.896 1.00 14.40 ? 302 GLY B N 1 ATOM 4689 C CA . GLY B 1 276 ? -23.787 -9.524 -68.317 1.00 13.33 ? 302 GLY B CA 1 ATOM 4690 C C . GLY B 1 276 ? -24.638 -8.613 -69.182 1.00 13.22 ? 302 GLY B C 1 ATOM 4691 O O . GLY B 1 276 ? -24.224 -8.122 -70.234 1.00 13.08 ? 302 GLY B O 1 ATOM 4692 N N . ILE B 1 277 ? -25.850 -8.398 -68.705 1.00 11.31 ? 303 ILE B N 1 ATOM 4693 C CA . ILE B 1 277 ? -26.826 -7.571 -69.371 1.00 10.29 ? 303 ILE B CA 1 ATOM 4694 C C . ILE B 1 277 ? -27.340 -6.547 -68.371 1.00 17.47 ? 303 ILE B C 1 ATOM 4695 O O . ILE B 1 277 ? -27.662 -6.901 -67.229 1.00 14.74 ? 303 ILE B O 1 ATOM 4696 C CB . ILE B 1 277 ? -28.012 -8.405 -69.898 1.00 9.79 ? 303 ILE B CB 1 ATOM 4697 C CG1 . ILE B 1 277 ? -27.519 -9.380 -70.973 1.00 19.61 ? 303 ILE B CG1 1 ATOM 4698 C CG2 . ILE B 1 277 ? -29.114 -7.495 -70.434 1.00 8.88 ? 303 ILE B CG2 1 ATOM 4699 C CD1 . ILE B 1 277 ? -28.444 -10.527 -71.234 1.00 17.90 ? 303 ILE B CD1 1 ATOM 4700 N N . THR B 1 278 ? -27.411 -5.295 -68.807 1.00 9.73 ? 304 THR B N 1 ATOM 4701 C CA . THR B 1 278 ? -27.966 -4.200 -68.002 1.00 9.64 ? 304 THR B CA 1 ATOM 4702 C C . THR B 1 278 ? -29.122 -3.527 -68.749 1.00 13.23 ? 304 THR B C 1 ATOM 4703 O O . THR B 1 278 ? -28.984 -3.182 -69.922 1.00 12.05 ? 304 THR B O 1 ATOM 4704 C CB . THR B 1 278 ? -26.882 -3.141 -67.674 1.00 10.56 ? 304 THR B CB 1 ATOM 4705 O OG1 . THR B 1 278 ? -25.859 -3.732 -66.857 1.00 11.52 ? 304 THR B OG1 1 ATOM 4706 C CG2 . THR B 1 278 ? -27.490 -1.899 -66.947 1.00 10.74 ? 304 THR B CG2 1 ATOM 4707 N N . THR B 1 279 ? -30.264 -3.339 -68.086 1.00 9.97 ? 305 THR B N 1 ATOM 4708 C CA . THR B 1 279 ? -31.359 -2.585 -68.713 1.00 9.69 ? 305 THR B CA 1 ATOM 4709 C C . THR B 1 279 ? -31.233 -1.141 -68.256 1.00 12.67 ? 305 THR B C 1 ATOM 4710 O O . THR B 1 279 ? -30.778 -0.880 -67.139 1.00 9.58 ? 305 THR B O 1 ATOM 4711 C CB . THR B 1 279 ? -32.773 -3.122 -68.348 1.00 8.81 ? 305 THR B CB 1 ATOM 4712 O OG1 . THR B 1 279 ? -32.902 -3.240 -66.920 1.00 9.81 ? 305 THR B OG1 1 ATOM 4713 C CG2 . THR B 1 279 ? -33.024 -4.483 -69.017 1.00 12.29 ? 305 THR B CG2 1 ATOM 4714 N N . TRP B 1 280 ? -31.619 -0.206 -69.119 1.00 11.78 ? 306 TRP B N 1 ATOM 4715 C CA . TRP B 1 280 ? -31.425 1.195 -68.809 1.00 9.47 ? 306 TRP B CA 1 ATOM 4716 C C . TRP B 1 280 ? -32.596 1.712 -67.976 1.00 11.20 ? 306 TRP B C 1 ATOM 4717 O O . TRP B 1 280 ? -33.390 2.535 -68.423 1.00 10.43 ? 306 TRP B O 1 ATOM 4718 C CB . TRP B 1 280 ? -31.243 2.038 -70.077 1.00 9.88 ? 306 TRP B CB 1 ATOM 4719 C CG . TRP B 1 280 ? -30.538 3.316 -69.721 1.00 11.24 ? 306 TRP B CG 1 ATOM 4720 C CD1 . TRP B 1 280 ? -31.041 4.589 -69.789 1.00 19.58 ? 306 TRP B CD1 1 ATOM 4721 C CD2 . TRP B 1 280 ? -29.227 3.430 -69.165 1.00 17.98 ? 306 TRP B CD2 1 ATOM 4722 N NE1 . TRP B 1 280 ? -30.106 5.488 -69.323 1.00 20.77 ? 306 TRP B NE1 1 ATOM 4723 C CE2 . TRP B 1 280 ? -28.986 4.801 -68.935 1.00 14.91 ? 306 TRP B CE2 1 ATOM 4724 C CE3 . TRP B 1 280 ? -28.228 2.504 -68.844 1.00 13.70 ? 306 TRP B CE3 1 ATOM 4725 C CZ2 . TRP B 1 280 ? -27.791 5.267 -68.405 1.00 15.08 ? 306 TRP B CZ2 1 ATOM 4726 C CZ3 . TRP B 1 280 ? -27.045 2.971 -68.311 1.00 17.00 ? 306 TRP B CZ3 1 ATOM 4727 C CH2 . TRP B 1 280 ? -26.831 4.341 -68.111 1.00 20.11 ? 306 TRP B CH2 1 ATOM 4728 N N . GLY B 1 281 ? -32.671 1.211 -66.751 1.00 9.72 ? 307 GLY B N 1 ATOM 4729 C CA . GLY B 1 281 ? -33.755 1.515 -65.838 1.00 10.05 ? 307 GLY B CA 1 ATOM 4730 C C . GLY B 1 281 ? -34.319 0.237 -65.255 1.00 15.66 ? 307 GLY B C 1 ATOM 4731 O O . GLY B 1 281 ? -33.929 -0.880 -65.638 1.00 12.11 ? 307 GLY B O 1 ATOM 4732 N N . ILE B 1 282 ? -35.232 0.413 -64.311 1.00 11.56 ? 308 ILE B N 1 ATOM 4733 C CA . ILE B 1 282 ? -36.005 -0.681 -63.759 1.00 15.01 ? 308 ILE B CA 1 ATOM 4734 C C . ILE B 1 282 ? -37.428 -0.631 -64.314 1.00 16.32 ? 308 ILE B C 1 ATOM 4735 O O . ILE B 1 282 ? -37.859 -1.549 -65.014 1.00 12.90 ? 308 ILE B O 1 ATOM 4736 C CB . ILE B 1 282 ? -36.002 -0.617 -62.219 1.00 14.27 ? 308 ILE B CB 1 ATOM 4737 C CG1 . ILE B 1 282 ? -34.575 -0.873 -61.716 1.00 12.06 ? 308 ILE B CG1 1 ATOM 4738 C CG2 . ILE B 1 282 ? -37.002 -1.617 -61.613 1.00 16.65 ? 308 ILE B CG2 1 ATOM 4739 C CD1 . ILE B 1 282 ? -34.426 -0.827 -60.196 1.00 13.67 ? 308 ILE B CD1 1 ATOM 4740 N N . THR B 1 283 ? -38.134 0.460 -64.031 1.00 14.73 ? 309 THR B N 1 ATOM 4741 C CA . THR B 1 283 ? -39.526 0.608 -64.443 1.00 13.58 ? 309 THR B CA 1 ATOM 4742 C C . THR B 1 283 ? -39.697 1.652 -65.556 1.00 10.20 ? 309 THR B C 1 ATOM 4743 O O . THR B 1 283 ? -38.979 2.660 -65.597 1.00 10.70 ? 309 THR B O 1 ATOM 4744 C CB . THR B 1 283 ? -40.423 1.001 -63.248 1.00 11.84 ? 309 THR B CB 1 ATOM 4745 O OG1 . THR B 1 283 ? -41.691 1.467 -63.725 1.00 18.64 ? 309 THR B OG1 1 ATOM 4746 C CG2 . THR B 1 283 ? -39.787 2.129 -62.438 1.00 12.89 ? 309 THR B CG2 1 ATOM 4747 N N . ASP B 1 284 ? -40.660 1.398 -66.437 1.00 10.04 ? 310 ASP B N 1 ATOM 4748 C CA . ASP B 1 284 ? -41.071 2.314 -67.499 1.00 14.63 ? 310 ASP B CA 1 ATOM 4749 C C . ASP B 1 284 ? -41.345 3.716 -66.950 1.00 10.97 ? 310 ASP B C 1 ATOM 4750 O O . ASP B 1 284 ? -41.221 4.714 -67.663 1.00 14.90 ? 310 ASP B O 1 ATOM 4751 C CB . ASP B 1 284 ? -42.358 1.819 -68.189 1.00 13.70 ? 310 ASP B CB 1 ATOM 4752 C CG . ASP B 1 284 ? -42.179 0.512 -68.945 1.00 15.37 ? 310 ASP B CG 1 ATOM 4753 O OD1 . ASP B 1 284 ? -41.051 0.196 -69.363 1.00 13.78 ? 310 ASP B OD1 1 ATOM 4754 O OD2 . ASP B 1 284 ? -43.189 -0.211 -69.128 1.00 15.30 ? 310 ASP B OD2 1 ATOM 4755 N N . LEU B 1 285 ? -41.739 3.768 -65.684 1.00 11.90 ? 311 LEU B N 1 ATOM 4756 C CA . LEU B 1 285 ? -42.237 4.999 -65.078 1.00 14.21 ? 311 LEU B CA 1 ATOM 4757 C C . LEU B 1 285 ? -41.224 6.122 -65.173 1.00 13.88 ? 311 LEU B C 1 ATOM 4758 O O . LEU B 1 285 ? -41.594 7.289 -65.309 1.00 17.45 ? 311 LEU B O 1 ATOM 4759 C CB . LEU B 1 285 ? -42.600 4.748 -63.612 1.00 19.28 ? 311 LEU B CB 1 ATOM 4760 C CG . LEU B 1 285 ? -43.360 5.855 -62.879 1.00 23.06 ? 311 LEU B CG 1 ATOM 4761 C CD1 . LEU B 1 285 ? -44.706 6.099 -63.532 1.00 22.66 ? 311 LEU B CD1 1 ATOM 4762 C CD2 . LEU B 1 285 ? -43.537 5.494 -61.412 1.00 22.06 ? 311 LEU B CD2 1 ATOM 4763 N N . TYR B 1 286 ? -39.938 5.761 -65.093 1.00 16.95 ? 312 TYR B N 1 ATOM 4764 C CA . TYR B 1 286 ? -38.847 6.739 -65.059 1.00 14.20 ? 312 TYR B CA 1 ATOM 4765 C C . TYR B 1 286 ? -37.929 6.624 -66.285 1.00 22.02 ? 312 TYR B C 1 ATOM 4766 O O . TYR B 1 286 ? -36.880 7.267 -66.349 1.00 19.85 ? 312 TYR B O 1 ATOM 4767 C CB . TYR B 1 286 ? -38.001 6.573 -63.776 1.00 14.89 ? 312 TYR B CB 1 ATOM 4768 C CG . TYR B 1 286 ? -38.818 6.613 -62.505 1.00 20.93 ? 312 TYR B CG 1 ATOM 4769 C CD1 . TYR B 1 286 ? -39.603 7.723 -62.195 1.00 18.89 ? 312 TYR B CD1 1 ATOM 4770 C CD2 . TYR B 1 286 ? -38.810 5.545 -61.616 1.00 19.50 ? 312 TYR B CD2 1 ATOM 4771 C CE1 . TYR B 1 286 ? -40.363 7.768 -61.028 1.00 18.81 ? 312 TYR B CE1 1 ATOM 4772 C CE2 . TYR B 1 286 ? -39.569 5.576 -60.450 1.00 18.49 ? 312 TYR B CE2 1 ATOM 4773 C CZ . TYR B 1 286 ? -40.348 6.691 -60.169 1.00 22.25 ? 312 TYR B CZ 1 ATOM 4774 O OH . TYR B 1 286 ? -41.104 6.738 -59.016 1.00 22.17 ? 312 TYR B OH 1 ATOM 4775 N N . SER B 1 287 ? -38.314 5.797 -67.246 1.00 18.39 ? 313 SER B N 1 ATOM 4776 C CA . SER B 1 287 ? -37.518 5.620 -68.453 1.00 14.67 ? 313 SER B CA 1 ATOM 4777 C C . SER B 1 287 ? -37.292 6.953 -69.158 1.00 14.17 ? 313 SER B C 1 ATOM 4778 O O . SER B 1 287 ? -38.181 7.783 -69.196 1.00 13.58 ? 313 SER B O 1 ATOM 4779 C CB . SER B 1 287 ? -38.214 4.632 -69.397 1.00 15.67 ? 313 SER B CB 1 ATOM 4780 O OG . SER B 1 287 ? -37.546 4.557 -70.647 1.00 15.34 ? 313 SER B OG 1 ATOM 4781 N N . TRP B 1 288 ? -36.108 7.148 -69.734 1.00 14.46 ? 314 TRP B N 1 ATOM 4782 C CA . TRP B 1 288 ? -35.811 8.352 -70.516 1.00 14.46 ? 314 TRP B CA 1 ATOM 4783 C C . TRP B 1 288 ? -36.638 8.410 -71.814 1.00 18.87 ? 314 TRP B C 1 ATOM 4784 O O . TRP B 1 288 ? -36.763 9.462 -72.438 1.00 15.79 ? 314 TRP B O 1 ATOM 4785 C CB . TRP B 1 288 ? -34.321 8.408 -70.877 1.00 20.56 ? 314 TRP B CB 1 ATOM 4786 C CG . TRP B 1 288 ? -33.936 7.273 -71.799 1.00 20.16 ? 314 TRP B CG 1 ATOM 4787 C CD1 . TRP B 1 288 ? -33.779 5.961 -71.462 1.00 16.14 ? 314 TRP B CD1 1 ATOM 4788 C CD2 . TRP B 1 288 ? -33.716 7.351 -73.214 1.00 29.01 ? 314 TRP B CD2 1 ATOM 4789 N NE1 . TRP B 1 288 ? -33.448 5.214 -72.581 1.00 15.48 ? 314 TRP B NE1 1 ATOM 4790 C CE2 . TRP B 1 288 ? -33.404 6.050 -73.665 1.00 23.59 ? 314 TRP B CE2 1 ATOM 4791 C CE3 . TRP B 1 288 ? -33.750 8.396 -74.143 1.00 41.47 ? 314 TRP B CE3 1 ATOM 4792 C CZ2 . TRP B 1 288 ? -33.129 5.768 -75.003 1.00 39.43 ? 314 TRP B CZ2 1 ATOM 4793 C CZ3 . TRP B 1 288 ? -33.475 8.115 -75.471 1.00 50.56 ? 314 TRP B CZ3 1 ATOM 4794 C CH2 . TRP B 1 288 ? -33.169 6.813 -75.889 1.00 49.03 ? 314 TRP B CH2 1 ATOM 4795 N N . ILE B 1 289 ? -37.200 7.281 -72.232 1.00 15.98 ? 315 ILE B N 1 ATOM 4796 C CA . ILE B 1 289 ? -37.789 7.244 -73.576 1.00 21.05 ? 315 ILE B CA 1 ATOM 4797 C C . ILE B 1 289 ? -39.007 8.174 -73.806 1.00 14.02 ? 315 ILE B C 1 ATOM 4798 O O . ILE B 1 289 ? -38.976 8.975 -74.743 1.00 22.00 ? 315 ILE B O 1 ATOM 4799 C CB . ILE B 1 289 ? -38.129 5.789 -73.960 1.00 20.73 ? 315 ILE B CB 1 ATOM 4800 C CG1 . ILE B 1 289 ? -36.823 5.087 -74.325 1.00 17.05 ? 315 ILE B CG1 1 ATOM 4801 C CG2 . ILE B 1 289 ? -39.084 5.742 -75.145 1.00 13.16 ? 315 ILE B CG2 1 ATOM 4802 C CD1 . ILE B 1 289 ? -36.697 3.744 -73.773 1.00 21.17 ? 315 ILE B CD1 1 ATOM 4803 N N . PRO B 1 290 ? -40.051 8.115 -72.953 1.00 17.62 ? 316 PRO B N 1 ATOM 4804 C CA . PRO B 1 290 ? -41.214 8.978 -73.234 1.00 24.32 ? 316 PRO B CA 1 ATOM 4805 C C . PRO B 1 290 ? -40.896 10.466 -73.332 1.00 28.00 ? 316 PRO B C 1 ATOM 4806 O O . PRO B 1 290 ? -41.623 11.196 -74.003 1.00 27.37 ? 316 PRO B O 1 ATOM 4807 C CB . PRO B 1 290 ? -42.146 8.749 -72.036 1.00 20.89 ? 316 PRO B CB 1 ATOM 4808 C CG . PRO B 1 290 ? -41.660 7.555 -71.349 1.00 22.42 ? 316 PRO B CG 1 ATOM 4809 C CD . PRO B 1 290 ? -40.223 7.337 -71.712 1.00 16.78 ? 316 PRO B CD 1 ATOM 4810 N N . SER B 1 291 ? -39.844 10.922 -72.662 1.00 32.18 ? 317 SER B N 1 ATOM 4811 C CA . SER B 1 291 ? -39.542 12.349 -72.682 1.00 34.88 ? 317 SER B CA 1 ATOM 4812 C C . SER B 1 291 ? -38.627 12.714 -73.853 1.00 28.74 ? 317 SER B C 1 ATOM 4813 O O . SER B 1 291 ? -38.505 13.874 -74.214 1.00 38.67 ? 317 SER B O 1 ATOM 4814 C CB . SER B 1 291 ? -38.916 12.784 -71.353 1.00 36.37 ? 317 SER B CB 1 ATOM 4815 O OG . SER B 1 291 ? -37.705 12.094 -71.110 1.00 35.94 ? 317 SER B OG 1 ATOM 4816 N N . THR B 1 292 ? -37.985 11.714 -74.438 1.00 26.53 ? 318 THR B N 1 ATOM 4817 C CA . THR B 1 292 ? -37.158 11.927 -75.617 1.00 28.68 ? 318 THR B CA 1 ATOM 4818 C C . THR B 1 292 ? -37.958 11.686 -76.897 1.00 35.46 ? 318 THR B C 1 ATOM 4819 O O . THR B 1 292 ? -37.987 12.535 -77.781 1.00 40.52 ? 318 THR B O 1 ATOM 4820 C CB . THR B 1 292 ? -35.929 11.012 -75.596 1.00 30.86 ? 318 THR B CB 1 ATOM 4821 O OG1 . THR B 1 292 ? -35.278 11.128 -74.326 1.00 39.38 ? 318 THR B OG1 1 ATOM 4822 C CG2 . THR B 1 292 ? -34.953 11.390 -76.703 1.00 22.72 ? 318 THR B CG2 1 ATOM 4823 N N . TYR B 1 293 ? -38.606 10.526 -76.988 1.00 25.68 ? 319 TYR B N 1 ATOM 4824 C CA . TYR B 1 293 ? -39.471 10.208 -78.121 1.00 26.14 ? 319 TYR B CA 1 ATOM 4825 C C . TYR B 1 293 ? -40.939 10.233 -77.705 1.00 26.03 ? 319 TYR B C 1 ATOM 4826 O O . TYR B 1 293 ? -41.472 9.220 -77.257 1.00 26.52 ? 319 TYR B O 1 ATOM 4827 C CB . TYR B 1 293 ? -39.138 8.832 -78.688 1.00 28.82 ? 319 TYR B CB 1 ATOM 4828 C CG . TYR B 1 293 ? -37.674 8.575 -78.939 1.00 32.69 ? 319 TYR B CG 1 ATOM 4829 C CD1 . TYR B 1 293 ? -37.027 9.141 -80.028 1.00 43.18 ? 319 TYR B CD1 1 ATOM 4830 C CD2 . TYR B 1 293 ? -36.948 7.733 -78.111 1.00 39.76 ? 319 TYR B CD2 1 ATOM 4831 C CE1 . TYR B 1 293 ? -35.689 8.894 -80.273 1.00 42.69 ? 319 TYR B CE1 1 ATOM 4832 C CE2 . TYR B 1 293 ? -35.610 7.478 -78.348 1.00 47.65 ? 319 TYR B CE2 1 ATOM 4833 C CZ . TYR B 1 293 ? -34.987 8.062 -79.434 1.00 50.22 ? 319 TYR B CZ 1 ATOM 4834 O OH . TYR B 1 293 ? -33.655 7.814 -79.676 1.00 54.00 ? 319 TYR B OH 1 ATOM 4835 N N . PRO B 1 294 ? -41.595 11.390 -77.831 1.00 31.72 ? 320 PRO B N 1 ATOM 4836 C CA . PRO B 1 294 ? -42.984 11.487 -77.376 1.00 31.41 ? 320 PRO B CA 1 ATOM 4837 C C . PRO B 1 294 ? -43.888 10.459 -78.055 1.00 28.46 ? 320 PRO B C 1 ATOM 4838 O O . PRO B 1 294 ? -43.795 10.236 -79.264 1.00 30.04 ? 320 PRO B O 1 ATOM 4839 C CB . PRO B 1 294 ? -43.387 12.919 -77.757 1.00 36.19 ? 320 PRO B CB 1 ATOM 4840 C CG . PRO B 1 294 ? -42.330 13.403 -78.684 1.00 36.38 ? 320 PRO B CG 1 ATOM 4841 C CD . PRO B 1 294 ? -41.087 12.670 -78.344 1.00 37.44 ? 320 PRO B CD 1 ATOM 4842 N N . GLY B 1 295 ? -44.742 9.821 -77.266 1.00 22.92 ? 321 GLY B N 1 ATOM 4843 C CA . GLY B 1 295 ? -45.608 8.785 -77.790 1.00 22.07 ? 321 GLY B CA 1 ATOM 4844 C C . GLY B 1 295 ? -44.965 7.408 -77.835 1.00 21.40 ? 321 GLY B C 1 ATOM 4845 O O . GLY B 1 295 ? -45.572 6.456 -78.338 1.00 15.03 ? 321 GLY B O 1 ATOM 4846 N N . GLU B 1 296 ? -43.738 7.294 -77.327 1.00 14.76 ? 322 GLU B N 1 ATOM 4847 C CA . GLU B 1 296 ? -43.081 5.982 -77.243 1.00 13.20 ? 322 GLU B CA 1 ATOM 4848 C C . GLU B 1 296 ? -42.775 5.624 -75.798 1.00 12.84 ? 322 GLU B C 1 ATOM 4849 O O . GLU B 1 296 ? -42.667 6.507 -74.946 1.00 14.97 ? 322 GLU B O 1 ATOM 4850 C CB . GLU B 1 296 ? -41.790 5.951 -78.073 1.00 13.37 ? 322 GLU B CB 1 ATOM 4851 C CG . GLU B 1 296 ? -41.991 6.279 -79.540 1.00 16.46 ? 322 GLU B CG 1 ATOM 4852 C CD . GLU B 1 296 ? -40.696 6.237 -80.336 1.00 29.09 ? 322 GLU B CD 1 ATOM 4853 O OE1 . GLU B 1 296 ? -39.681 5.733 -79.810 1.00 23.11 ? 322 GLU B OE1 1 ATOM 4854 O OE2 . GLU B 1 296 ? -40.695 6.714 -81.489 1.00 33.64 ? 322 GLU B OE2 1 ATOM 4855 N N . GLY B 1 297 ? -42.626 4.333 -75.516 1.00 11.99 ? 323 GLY B N 1 ATOM 4856 C CA . GLY B 1 297 ? -42.339 3.907 -74.160 1.00 11.87 ? 323 GLY B CA 1 ATOM 4857 C C . GLY B 1 297 ? -42.441 2.409 -74.008 1.00 12.03 ? 323 GLY B C 1 ATOM 4858 O O . GLY B 1 297 ? -42.095 1.671 -74.933 1.00 9.54 ? 323 GLY B O 1 ATOM 4859 N N . TYR B 1 298 ? -42.907 1.973 -72.837 1.00 9.71 ? 324 TYR B N 1 ATOM 4860 C CA . TYR B 1 298 ? -43.079 0.557 -72.524 1.00 13.21 ? 324 TYR B CA 1 ATOM 4861 C C . TYR B 1 298 ? -41.828 -0.259 -72.865 1.00 9.11 ? 324 TYR B C 1 ATOM 4862 O O . TYR B 1 298 ? -41.924 -1.365 -73.387 1.00 12.63 ? 324 TYR B O 1 ATOM 4863 C CB . TYR B 1 298 ? -44.291 -0.020 -73.274 1.00 11.54 ? 324 TYR B CB 1 ATOM 4864 C CG . TYR B 1 298 ? -44.885 -1.226 -72.581 1.00 8.88 ? 324 TYR B CG 1 ATOM 4865 C CD1 . TYR B 1 298 ? -45.500 -1.101 -71.341 1.00 13.62 ? 324 TYR B CD1 1 ATOM 4866 C CD2 . TYR B 1 298 ? -44.819 -2.487 -73.160 1.00 15.96 ? 324 TYR B CD2 1 ATOM 4867 C CE1 . TYR B 1 298 ? -46.049 -2.217 -70.694 1.00 24.75 ? 324 TYR B CE1 1 ATOM 4868 C CE2 . TYR B 1 298 ? -45.368 -3.601 -72.531 1.00 15.72 ? 324 TYR B CE2 1 ATOM 4869 C CZ . TYR B 1 298 ? -45.972 -3.465 -71.301 1.00 25.46 ? 324 TYR B CZ 1 ATOM 4870 O OH . TYR B 1 298 ? -46.496 -4.582 -70.682 1.00 25.77 ? 324 TYR B OH 1 ATOM 4871 N N . ALA B 1 299 ? -40.655 0.281 -72.569 1.00 10.69 ? 325 ALA B N 1 ATOM 4872 C CA . ALA B 1 299 ? -39.418 -0.301 -73.104 1.00 9.66 ? 325 ALA B CA 1 ATOM 4873 C C . ALA B 1 299 ? -38.666 -1.241 -72.161 1.00 11.14 ? 325 ALA B C 1 ATOM 4874 O O . ALA B 1 299 ? -37.748 -1.968 -72.606 1.00 9.47 ? 325 ALA B O 1 ATOM 4875 C CB . ALA B 1 299 ? -38.477 0.828 -73.543 1.00 9.05 ? 325 ALA B CB 1 ATOM 4876 N N . LEU B 1 300 ? -38.987 -1.190 -70.867 1.00 7.04 ? 326 LEU B N 1 ATOM 4877 C CA . LEU B 1 300 ? -38.189 -1.911 -69.872 1.00 9.95 ? 326 LEU B CA 1 ATOM 4878 C C . LEU B 1 300 ? -38.896 -3.206 -69.510 1.00 15.11 ? 326 LEU B C 1 ATOM 4879 O O . LEU B 1 300 ? -39.805 -3.605 -70.209 1.00 12.49 ? 326 LEU B O 1 ATOM 4880 C CB . LEU B 1 300 ? -37.935 -1.031 -68.638 1.00 7.91 ? 326 LEU B CB 1 ATOM 4881 C CG . LEU B 1 300 ? -36.942 0.115 -68.944 1.00 13.55 ? 326 LEU B CG 1 ATOM 4882 C CD1 . LEU B 1 300 ? -36.967 1.180 -67.851 1.00 12.67 ? 326 LEU B CD1 1 ATOM 4883 C CD2 . LEU B 1 300 ? -35.501 -0.400 -69.163 1.00 8.58 ? 326 LEU B CD2 1 ATOM 4884 N N . LEU B 1 301 ? -38.477 -3.883 -68.442 1.00 11.73 ? 327 LEU B N 1 ATOM 4885 C CA . LEU B 1 301 ? -39.111 -5.159 -68.100 1.00 9.47 ? 327 LEU B CA 1 ATOM 4886 C C . LEU B 1 301 ? -40.226 -5.033 -67.062 1.00 9.58 ? 327 LEU B C 1 ATOM 4887 O O . LEU B 1 301 ? -40.954 -5.992 -66.819 1.00 12.15 ? 327 LEU B O 1 ATOM 4888 C CB . LEU B 1 301 ? -38.056 -6.154 -67.600 1.00 9.82 ? 327 LEU B CB 1 ATOM 4889 C CG . LEU B 1 301 ? -37.097 -6.614 -68.700 1.00 8.56 ? 327 LEU B CG 1 ATOM 4890 C CD1 . LEU B 1 301 ? -36.085 -7.605 -68.143 1.00 13.00 ? 327 LEU B CD1 1 ATOM 4891 C CD2 . LEU B 1 301 ? -37.890 -7.239 -69.841 1.00 10.87 ? 327 LEU B CD2 1 ATOM 4892 N N . PHE B 1 302 ? -40.355 -3.864 -66.445 1.00 9.11 ? 328 PHE B N 1 ATOM 4893 C CA . PHE B 1 302 ? -41.376 -3.639 -65.421 1.00 9.87 ? 328 PHE B CA 1 ATOM 4894 C C . PHE B 1 302 ? -42.180 -2.406 -65.801 1.00 11.95 ? 328 PHE B C 1 ATOM 4895 O O . PHE B 1 302 ? -41.605 -1.382 -66.187 1.00 11.55 ? 328 PHE B O 1 ATOM 4896 C CB . PHE B 1 302 ? -40.747 -3.475 -64.027 1.00 13.49 ? 328 PHE B CB 1 ATOM 4897 C CG . PHE B 1 302 ? -39.974 -4.685 -63.576 1.00 14.07 ? 328 PHE B CG 1 ATOM 4898 C CD1 . PHE B 1 302 ? -40.606 -5.702 -62.886 1.00 16.93 ? 328 PHE B CD1 1 ATOM 4899 C CD2 . PHE B 1 302 ? -38.626 -4.819 -63.879 1.00 12.75 ? 328 PHE B CD2 1 ATOM 4900 C CE1 . PHE B 1 302 ? -39.895 -6.837 -62.484 1.00 23.18 ? 328 PHE B CE1 1 ATOM 4901 C CE2 . PHE B 1 302 ? -37.917 -5.947 -63.492 1.00 14.08 ? 328 PHE B CE2 1 ATOM 4902 C CZ . PHE B 1 302 ? -38.557 -6.955 -62.791 1.00 18.61 ? 328 PHE B CZ 1 ATOM 4903 N N . ASP B 1 303 ? -43.505 -2.489 -65.696 1.00 15.13 ? 329 ASP B N 1 ATOM 4904 C CA . ASP B 1 303 ? -44.323 -1.379 -66.165 1.00 12.09 ? 329 ASP B CA 1 ATOM 4905 C C . ASP B 1 303 ? -44.475 -0.306 -65.093 1.00 16.88 ? 329 ASP B C 1 ATOM 4906 O O . ASP B 1 303 ? -43.832 -0.367 -64.028 1.00 14.28 ? 329 ASP B O 1 ATOM 4907 C CB . ASP B 1 303 ? -45.701 -1.866 -66.663 1.00 18.56 ? 329 ASP B CB 1 ATOM 4908 C CG . ASP B 1 303 ? -46.629 -2.380 -65.550 1.00 33.07 ? 329 ASP B CG 1 ATOM 4909 O OD1 . ASP B 1 303 ? -46.405 -2.123 -64.344 1.00 25.55 ? 329 ASP B OD1 1 ATOM 4910 O OD2 . ASP B 1 303 ? -47.640 -3.033 -65.910 1.00 31.99 ? 329 ASP B OD2 1 ATOM 4911 N N . ASP B 1 304 ? -45.358 0.654 -65.363 1.00 14.32 ? 330 ASP B N 1 ATOM 4912 C CA . ASP B 1 304 ? -45.578 1.789 -64.459 1.00 19.09 ? 330 ASP B CA 1 ATOM 4913 C C . ASP B 1 304 ? -45.988 1.392 -63.036 1.00 26.80 ? 330 ASP B C 1 ATOM 4914 O O . ASP B 1 304 ? -45.782 2.156 -62.090 1.00 26.45 ? 330 ASP B O 1 ATOM 4915 C CB . ASP B 1 304 ? -46.651 2.731 -65.037 1.00 20.03 ? 330 ASP B CB 1 ATOM 4916 C CG . ASP B 1 304 ? -46.132 3.585 -66.188 1.00 28.19 ? 330 ASP B CG 1 ATOM 4917 O OD1 . ASP B 1 304 ? -44.906 3.565 -66.455 1.00 23.69 ? 330 ASP B OD1 1 ATOM 4918 O OD2 . ASP B 1 304 ? -46.955 4.289 -66.825 1.00 28.04 ? 330 ASP B OD2 1 ATOM 4919 N N . ASN B 1 305 ? -46.573 0.210 -62.879 1.00 19.25 ? 331 ASN B N 1 ATOM 4920 C CA . ASN B 1 305 ? -46.967 -0.281 -61.557 1.00 20.63 ? 331 ASN B CA 1 ATOM 4921 C C . ASN B 1 305 ? -46.053 -1.402 -61.039 1.00 22.71 ? 331 ASN B C 1 ATOM 4922 O O . ASN B 1 305 ? -46.396 -2.093 -60.080 1.00 23.83 ? 331 ASN B O 1 ATOM 4923 C CB . ASN B 1 305 ? -48.420 -0.770 -61.595 1.00 28.16 ? 331 ASN B CB 1 ATOM 4924 C CG . ASN B 1 305 ? -49.385 0.310 -62.053 1.00 35.01 ? 331 ASN B CG 1 ATOM 4925 O OD1 . ASN B 1 305 ? -50.157 0.116 -62.990 1.00 40.77 ? 331 ASN B OD1 1 ATOM 4926 N ND2 . ASN B 1 305 ? -49.331 1.464 -61.397 1.00 33.51 ? 331 ASN B ND2 1 ATOM 4927 N N . TYR B 1 306 ? -44.896 -1.554 -61.680 1.00 18.38 ? 332 TYR B N 1 ATOM 4928 C CA . TYR B 1 306 ? -43.884 -2.579 -61.369 1.00 23.51 ? 332 TYR B CA 1 ATOM 4929 C C . TYR B 1 306 ? -44.368 -4.002 -61.650 1.00 24.67 ? 332 TYR B C 1 ATOM 4930 O O . TYR B 1 306 ? -43.802 -4.972 -61.156 1.00 23.80 ? 332 TYR B O 1 ATOM 4931 C CB . TYR B 1 306 ? -43.407 -2.464 -59.915 1.00 20.81 ? 332 TYR B CB 1 ATOM 4932 C CG . TYR B 1 306 ? -42.571 -1.223 -59.676 1.00 24.78 ? 332 TYR B CG 1 ATOM 4933 C CD1 . TYR B 1 306 ? -41.184 -1.255 -59.805 1.00 25.61 ? 332 TYR B CD1 1 ATOM 4934 C CD2 . TYR B 1 306 ? -43.171 -0.016 -59.336 1.00 25.34 ? 332 TYR B CD2 1 ATOM 4935 C CE1 . TYR B 1 306 ? -40.419 -0.112 -59.590 1.00 15.35 ? 332 TYR B CE1 1 ATOM 4936 C CE2 . TYR B 1 306 ? -42.419 1.120 -59.116 1.00 25.03 ? 332 TYR B CE2 1 ATOM 4937 C CZ . TYR B 1 306 ? -41.050 1.071 -59.251 1.00 23.01 ? 332 TYR B CZ 1 ATOM 4938 O OH . TYR B 1 306 ? -40.318 2.218 -59.034 1.00 19.57 ? 332 TYR B OH 1 ATOM 4939 N N . VAL B 1 307 ? -45.413 -4.114 -62.454 1.00 22.46 ? 333 VAL B N 1 ATOM 4940 C CA . VAL B 1 307 ? -45.855 -5.403 -62.960 1.00 20.92 ? 333 VAL B CA 1 ATOM 4941 C C . VAL B 1 307 ? -44.970 -5.764 -64.143 1.00 18.10 ? 333 VAL B C 1 ATOM 4942 O O . VAL B 1 307 ? -44.780 -4.955 -65.046 1.00 15.99 ? 333 VAL B O 1 ATOM 4943 C CB . VAL B 1 307 ? -47.329 -5.368 -63.393 1.00 25.10 ? 333 VAL B CB 1 ATOM 4944 C CG1 . VAL B 1 307 ? -47.781 -6.740 -63.899 1.00 27.35 ? 333 VAL B CG1 1 ATOM 4945 C CG2 . VAL B 1 307 ? -48.206 -4.879 -62.238 1.00 20.98 ? 333 VAL B CG2 1 ATOM 4946 N N . PRO B 1 308 ? -44.403 -6.973 -64.134 1.00 16.89 ? 334 PRO B N 1 ATOM 4947 C CA . PRO B 1 308 ? -43.495 -7.367 -65.220 1.00 14.72 ? 334 PRO B CA 1 ATOM 4948 C C . PRO B 1 308 ? -44.199 -7.411 -66.570 1.00 13.11 ? 334 PRO B C 1 ATOM 4949 O O . PRO B 1 308 ? -45.362 -7.827 -66.614 1.00 14.58 ? 334 PRO B O 1 ATOM 4950 C CB . PRO B 1 308 ? -43.035 -8.771 -64.804 1.00 22.74 ? 334 PRO B CB 1 ATOM 4951 C CG . PRO B 1 308 ? -43.311 -8.861 -63.326 1.00 26.13 ? 334 PRO B CG 1 ATOM 4952 C CD . PRO B 1 308 ? -44.501 -7.992 -63.073 1.00 18.28 ? 334 PRO B CD 1 ATOM 4953 N N . HIS B 1 309 ? -43.532 -6.946 -67.626 1.00 13.79 ? 335 HIS B N 1 ATOM 4954 C CA . HIS B 1 309 ? -43.955 -7.189 -69.012 1.00 11.42 ? 335 HIS B CA 1 ATOM 4955 C C . HIS B 1 309 ? -43.933 -8.685 -69.286 1.00 15.94 ? 335 HIS B C 1 ATOM 4956 O O . HIS B 1 309 ? -43.249 -9.418 -68.585 1.00 16.24 ? 335 HIS B O 1 ATOM 4957 C CB . HIS B 1 309 ? -43.018 -6.512 -70.030 1.00 10.27 ? 335 HIS B CB 1 ATOM 4958 C CG . HIS B 1 309 ? -42.968 -5.018 -69.939 1.00 18.45 ? 335 HIS B CG 1 ATOM 4959 N ND1 . HIS B 1 309 ? -42.525 -4.232 -70.981 1.00 18.09 ? 335 HIS B ND1 1 ATOM 4960 C CD2 . HIS B 1 309 ? -43.296 -4.166 -68.937 1.00 20.76 ? 335 HIS B CD2 1 ATOM 4961 C CE1 . HIS B 1 309 ? -42.594 -2.959 -70.630 1.00 20.09 ? 335 HIS B CE1 1 ATOM 4962 N NE2 . HIS B 1 309 ? -43.049 -2.892 -69.390 1.00 18.58 ? 335 HIS B NE2 1 ATOM 4963 N N . PRO B 1 310 ? -44.646 -9.140 -70.335 1.00 17.05 ? 336 PRO B N 1 ATOM 4964 C CA . PRO B 1 310 ? -44.457 -10.521 -70.805 1.00 14.45 ? 336 PRO B CA 1 ATOM 4965 C C . PRO B 1 310 ? -43.002 -10.807 -71.177 1.00 15.15 ? 336 PRO B C 1 ATOM 4966 O O . PRO B 1 310 ? -42.543 -11.946 -71.031 1.00 18.05 ? 336 PRO B O 1 ATOM 4967 C CB . PRO B 1 310 ? -45.373 -10.605 -72.038 1.00 16.47 ? 336 PRO B CB 1 ATOM 4968 C CG . PRO B 1 310 ? -46.489 -9.601 -71.736 1.00 16.68 ? 336 PRO B CG 1 ATOM 4969 C CD . PRO B 1 310 ? -45.723 -8.444 -71.073 1.00 12.72 ? 336 PRO B CD 1 ATOM 4970 N N . ALA B 1 311 ? -42.284 -9.787 -71.639 1.00 10.19 ? 337 ALA B N 1 ATOM 4971 C CA . ALA B 1 311 ? -40.845 -9.911 -71.903 1.00 14.12 ? 337 ALA B CA 1 ATOM 4972 C C . ALA B 1 311 ? -40.026 -10.375 -70.691 1.00 15.53 ? 337 ALA B C 1 ATOM 4973 O O . ALA B 1 311 ? -38.923 -10.898 -70.852 1.00 13.51 ? 337 ALA B O 1 ATOM 4974 C CB . ALA B 1 311 ? -40.288 -8.594 -72.407 1.00 8.48 ? 337 ALA B CB 1 ATOM 4975 N N . PHE B 1 312 ? -40.548 -10.160 -69.487 1.00 13.97 ? 338 PHE B N 1 ATOM 4976 C CA . PHE B 1 312 ? -39.875 -10.629 -68.271 1.00 13.68 ? 338 PHE B CA 1 ATOM 4977 C C . PHE B 1 312 ? -39.861 -12.154 -68.251 1.00 12.21 ? 338 PHE B C 1 ATOM 4978 O O . PHE B 1 312 ? -38.814 -12.756 -68.055 1.00 12.51 ? 338 PHE B O 1 ATOM 4979 C CB . PHE B 1 312 ? -40.564 -10.083 -67.004 1.00 11.37 ? 338 PHE B CB 1 ATOM 4980 C CG . PHE B 1 312 ? -40.023 -10.650 -65.716 1.00 14.37 ? 338 PHE B CG 1 ATOM 4981 C CD1 . PHE B 1 312 ? -38.964 -10.031 -65.055 1.00 15.60 ? 338 PHE B CD1 1 ATOM 4982 C CD2 . PHE B 1 312 ? -40.585 -11.792 -65.150 1.00 18.97 ? 338 PHE B CD2 1 ATOM 4983 C CE1 . PHE B 1 312 ? -38.468 -10.551 -63.863 1.00 16.19 ? 338 PHE B CE1 1 ATOM 4984 C CE2 . PHE B 1 312 ? -40.089 -12.322 -63.954 1.00 16.37 ? 338 PHE B CE2 1 ATOM 4985 C CZ . PHE B 1 312 ? -39.028 -11.698 -63.314 1.00 20.80 ? 338 PHE B CZ 1 ATOM 4986 N N . ASN B 1 313 ? -41.022 -12.778 -68.439 1.00 13.28 ? 339 ASN B N 1 ATOM 4987 C CA . ASN B 1 313 ? -41.073 -14.242 -68.538 1.00 22.02 ? 339 ASN B CA 1 ATOM 4988 C C . ASN B 1 313 ? -40.146 -14.794 -69.633 1.00 19.36 ? 339 ASN B C 1 ATOM 4989 O O . ASN B 1 313 ? -39.450 -15.787 -69.428 1.00 15.72 ? 339 ASN B O 1 ATOM 4990 C CB . ASN B 1 313 ? -42.502 -14.714 -68.801 1.00 19.26 ? 339 ASN B CB 1 ATOM 4991 C CG . ASN B 1 313 ? -43.332 -14.817 -67.532 1.00 32.89 ? 339 ASN B CG 1 ATOM 4992 O OD1 . ASN B 1 313 ? -42.807 -14.722 -66.423 1.00 34.21 ? 339 ASN B OD1 1 ATOM 4993 N ND2 . ASN B 1 313 ? -44.639 -15.014 -67.693 1.00 44.15 ? 339 ASN B ND2 1 ATOM 4994 N N . ALA B 1 314 ? -40.143 -14.141 -70.793 1.00 16.61 ? 340 ALA B N 1 ATOM 4995 C CA . ALA B 1 314 ? -39.324 -14.580 -71.919 1.00 21.93 ? 340 ALA B CA 1 ATOM 4996 C C . ALA B 1 314 ? -37.835 -14.432 -71.623 1.00 16.06 ? 340 ALA B C 1 ATOM 4997 O O . ALA B 1 314 ? -37.027 -15.247 -72.057 1.00 14.86 ? 340 ALA B O 1 ATOM 4998 C CB . ALA B 1 314 ? -39.679 -13.802 -73.171 1.00 17.39 ? 340 ALA B CB 1 ATOM 4999 N N . THR B 1 315 ? -37.476 -13.389 -70.883 1.00 11.76 ? 341 THR B N 1 ATOM 5000 C CA . THR B 1 315 ? -36.076 -13.175 -70.531 1.00 17.04 ? 341 THR B CA 1 ATOM 5001 C C . THR B 1 315 ? -35.588 -14.246 -69.569 1.00 12.70 ? 341 THR B C 1 ATOM 5002 O O . THR B 1 315 ? -34.502 -14.796 -69.754 1.00 13.17 ? 341 THR B O 1 ATOM 5003 C CB . THR B 1 315 ? -35.860 -11.786 -69.916 1.00 15.07 ? 341 THR B CB 1 ATOM 5004 O OG1 . THR B 1 315 ? -36.296 -10.803 -70.859 1.00 13.61 ? 341 THR B OG1 1 ATOM 5005 C CG2 . THR B 1 315 ? -34.362 -11.564 -69.576 1.00 14.55 ? 341 THR B CG2 1 ATOM 5006 N N . ILE B 1 316 ? -36.386 -14.533 -68.542 1.00 13.55 ? 342 ILE B N 1 ATOM 5007 C CA . ILE B 1 316 ? -36.072 -15.604 -67.598 1.00 19.74 ? 342 ILE B CA 1 ATOM 5008 C C . ILE B 1 316 ? -35.901 -16.955 -68.311 1.00 21.26 ? 342 ILE B C 1 ATOM 5009 O O . ILE B 1 316 ? -34.961 -17.706 -68.036 1.00 20.10 ? 342 ILE B O 1 ATOM 5010 C CB . ILE B 1 316 ? -37.185 -15.751 -66.525 1.00 25.29 ? 342 ILE B CB 1 ATOM 5011 C CG1 . ILE B 1 316 ? -37.266 -14.496 -65.652 1.00 21.60 ? 342 ILE B CG1 1 ATOM 5012 C CG2 . ILE B 1 316 ? -36.960 -17.001 -65.656 1.00 24.00 ? 342 ILE B CG2 1 ATOM 5013 C CD1 . ILE B 1 316 ? -36.151 -14.384 -64.670 1.00 24.05 ? 342 ILE B CD1 1 ATOM 5014 N N . GLN B 1 317 ? -36.828 -17.276 -69.208 1.00 16.97 ? 343 GLN B N 1 ATOM 5015 C CA . GLN B 1 317 ? -36.769 -18.566 -69.899 1.00 20.39 ? 343 GLN B CA 1 ATOM 5016 C C . GLN B 1 317 ? -35.519 -18.651 -70.761 1.00 19.72 ? 343 GLN B C 1 ATOM 5017 O O . GLN B 1 317 ? -34.887 -19.702 -70.838 1.00 21.06 ? 343 GLN B O 1 ATOM 5018 C CB . GLN B 1 317 ? -38.023 -18.798 -70.759 1.00 22.82 ? 343 GLN B CB 1 ATOM 5019 C CG . GLN B 1 317 ? -39.295 -19.002 -69.944 1.00 42.51 ? 343 GLN B CG 1 ATOM 5020 C CD . GLN B 1 317 ? -39.219 -20.224 -69.033 1.00 60.17 ? 343 GLN B CD 1 ATOM 5021 O OE1 . GLN B 1 317 ? -39.373 -20.116 -67.812 1.00 59.78 ? 343 GLN B OE1 1 ATOM 5022 N NE2 . GLN B 1 317 ? -38.984 -21.393 -69.626 1.00 64.23 ? 343 GLN B NE2 1 ATOM 5023 N N . ALA B 1 318 ? -35.148 -17.537 -71.393 1.00 18.10 ? 344 ALA B N 1 ATOM 5024 C CA . ALA B 1 318 ? -33.960 -17.520 -72.238 1.00 18.39 ? 344 ALA B CA 1 ATOM 5025 C C . ALA B 1 318 ? -32.685 -17.617 -71.398 1.00 24.56 ? 344 ALA B C 1 ATOM 5026 O O . ALA B 1 318 ? -31.744 -18.304 -71.776 1.00 18.72 ? 344 ALA B O 1 ATOM 5027 C CB . ALA B 1 318 ? -33.933 -16.263 -73.103 1.00 22.04 ? 344 ALA B CB 1 ATOM 5028 N N . LEU B 1 319 ? -32.644 -16.922 -70.267 1.00 18.16 ? 345 LEU B N 1 ATOM 5029 C CA . LEU B 1 319 ? -31.505 -17.067 -69.358 1.00 18.14 ? 345 LEU B CA 1 ATOM 5030 C C . LEU B 1 319 ? -31.353 -18.510 -68.872 1.00 20.12 ? 345 LEU B C 1 ATOM 5031 O O . LEU B 1 319 ? -30.238 -18.999 -68.719 1.00 19.71 ? 345 LEU B O 1 ATOM 5032 C CB . LEU B 1 319 ? -31.642 -16.112 -68.161 1.00 15.41 ? 345 LEU B CB 1 ATOM 5033 C CG . LEU B 1 319 ? -31.462 -14.625 -68.509 1.00 14.28 ? 345 LEU B CG 1 ATOM 5034 C CD1 . LEU B 1 319 ? -31.918 -13.727 -67.360 1.00 14.94 ? 345 LEU B CD1 1 ATOM 5035 C CD2 . LEU B 1 319 ? -29.985 -14.345 -68.846 1.00 17.81 ? 345 LEU B CD2 1 ATOM 5036 N N . LEU B 1 320 ? -32.466 -19.202 -68.648 1.00 19.56 ? 346 LEU B N 1 ATOM 5037 C CA . LEU B 1 320 ? -32.411 -20.568 -68.119 1.00 26.90 ? 346 LEU B CA 1 ATOM 5038 C C . LEU B 1 320 ? -32.073 -21.628 -69.163 1.00 39.14 ? 346 LEU B C 1 ATOM 5039 O O . LEU B 1 320 ? -31.565 -22.691 -68.827 1.00 43.57 ? 346 LEU B O 1 ATOM 5040 C CB . LEU B 1 320 ? -33.739 -20.938 -67.458 1.00 25.97 ? 346 LEU B CB 1 ATOM 5041 C CG . LEU B 1 320 ? -34.082 -20.178 -66.174 1.00 26.51 ? 346 LEU B CG 1 ATOM 5042 C CD1 . LEU B 1 320 ? -35.427 -20.658 -65.650 1.00 30.30 ? 346 LEU B CD1 1 ATOM 5043 C CD2 . LEU B 1 320 ? -32.996 -20.377 -65.135 1.00 26.22 ? 346 LEU B CD2 1 ATOM 5044 N N . ALA B 1 321 ? -32.361 -21.349 -70.428 1.00 29.67 ? 347 ALA B N 1 ATOM 5045 C CA . ALA B 1 321 ? -32.205 -22.362 -71.465 1.00 36.77 ? 347 ALA B CA 1 ATOM 5046 C C . ALA B 1 321 ? -30.784 -22.379 -72.010 1.00 47.22 ? 347 ALA B C 1 ATOM 5047 O O . ALA B 1 321 ? -29.820 -22.188 -71.266 1.00 56.78 ? 347 ALA B O 1 ATOM 5048 C CB . ALA B 1 321 ? -33.207 -22.127 -72.586 1.00 32.92 ? 347 ALA B CB 1 HETATM 5049 X UNK . UNX C 2 . ? -19.456 5.930 -39.909 1.00 30.00 ? 401 UNX A UNK 1 HETATM 5050 C C1 . NAG D 3 . ? -21.089 -8.349 -41.496 1.00 14.79 ? 402 NAG A C1 1 HETATM 5051 C C2 . NAG D 3 . ? -20.291 -7.859 -40.289 1.00 14.27 ? 402 NAG A C2 1 HETATM 5052 C C3 . NAG D 3 . ? -19.560 -9.010 -39.627 1.00 12.63 ? 402 NAG A C3 1 HETATM 5053 C C4 . NAG D 3 . ? -20.521 -10.141 -39.297 1.00 17.94 ? 402 NAG A C4 1 HETATM 5054 C C5 . NAG D 3 . ? -21.317 -10.533 -40.540 1.00 22.10 ? 402 NAG A C5 1 HETATM 5055 C C6 . NAG D 3 . ? -22.400 -11.546 -40.254 1.00 29.40 ? 402 NAG A C6 1 HETATM 5056 C C7 . NAG D 3 . ? -19.606 -5.516 -40.423 1.00 24.57 ? 402 NAG A C7 1 HETATM 5057 C C8 . NAG D 3 . ? -18.525 -4.555 -40.816 1.00 19.20 ? 402 NAG A C8 1 HETATM 5058 N N2 . NAG D 3 . ? -19.349 -6.809 -40.644 1.00 15.15 ? 402 NAG A N2 1 HETATM 5059 O O3 . NAG D 3 . ? -18.952 -8.528 -38.437 1.00 14.45 ? 402 NAG A O3 1 HETATM 5060 O O4 . NAG D 3 . ? -19.745 -11.259 -38.885 1.00 17.08 ? 402 NAG A O4 1 HETATM 5061 O O5 . NAG D 3 . ? -21.974 -9.385 -41.097 1.00 16.40 ? 402 NAG A O5 1 HETATM 5062 O O6 . NAG D 3 . ? -22.640 -12.353 -41.400 1.00 33.35 ? 402 NAG A O6 1 HETATM 5063 O O7 . NAG D 3 . ? -20.680 -5.139 -39.954 1.00 20.61 ? 402 NAG A O7 1 HETATM 5064 C C1 . NAG E 3 . ? -20.013 -11.578 -37.523 1.00 20.47 ? 403 NAG A C1 1 HETATM 5065 C C2 . NAG E 3 . ? -19.302 -12.901 -37.223 1.00 23.67 ? 403 NAG A C2 1 HETATM 5066 C C3 . NAG E 3 . ? -19.431 -13.258 -35.746 1.00 27.89 ? 403 NAG A C3 1 HETATM 5067 C C4 . NAG E 3 . ? -19.055 -12.077 -34.856 1.00 19.87 ? 403 NAG A C4 1 HETATM 5068 C C5 . NAG E 3 . ? -19.778 -10.811 -35.310 1.00 14.06 ? 403 NAG A C5 1 HETATM 5069 C C6 . NAG E 3 . ? -19.339 -9.581 -34.547 1.00 12.80 ? 403 NAG A C6 1 HETATM 5070 C C7 . NAG E 3 . ? -19.219 -14.409 -39.159 1.00 24.97 ? 403 NAG A C7 1 HETATM 5071 C C8 . NAG E 3 . ? -19.899 -15.530 -39.890 1.00 28.37 ? 403 NAG A C8 1 HETATM 5072 N N2 . NAG E 3 . ? -19.830 -13.975 -38.051 1.00 25.11 ? 403 NAG A N2 1 HETATM 5073 O O3 . NAG E 3 . ? -18.579 -14.367 -35.476 1.00 24.12 ? 403 NAG A O3 1 HETATM 5074 O O4 . NAG E 3 . ? -19.524 -12.349 -33.543 1.00 25.74 ? 403 NAG A O4 1 HETATM 5075 O O5 . NAG E 3 . ? -19.502 -10.567 -36.692 1.00 16.75 ? 403 NAG A O5 1 HETATM 5076 O O6 . NAG E 3 . ? -17.932 -9.416 -34.636 1.00 17.84 ? 403 NAG A O6 1 HETATM 5077 O O7 . NAG E 3 . ? -18.169 -13.917 -39.555 1.00 21.04 ? 403 NAG A O7 1 HETATM 5078 C C1 . BMA F 4 . ? -18.457 -12.653 -32.640 1.00 30.84 ? 404 BMA A C1 1 HETATM 5079 C C2 . BMA F 4 . ? -18.992 -12.296 -31.265 1.00 23.73 ? 404 BMA A C2 1 HETATM 5080 C C3 . BMA F 4 . ? -18.022 -12.714 -30.176 1.00 28.32 ? 404 BMA A C3 1 HETATM 5081 C C4 . BMA F 4 . ? -17.511 -14.149 -30.379 1.00 31.74 ? 404 BMA A C4 1 HETATM 5082 C C5 . BMA F 4 . ? -17.021 -14.356 -31.806 1.00 27.48 ? 404 BMA A C5 1 HETATM 5083 C C6 . BMA F 4 . ? -16.614 -15.791 -32.057 1.00 20.40 ? 404 BMA A C6 1 HETATM 5084 O O2 . BMA F 4 . ? -20.186 -13.022 -31.036 1.00 18.82 ? 404 BMA A O2 1 HETATM 5085 O O3 . BMA F 4 . ? -18.633 -12.621 -28.883 1.00 27.87 ? 404 BMA A O3 1 HETATM 5086 O O4 . BMA F 4 . ? -16.417 -14.362 -29.534 1.00 28.79 ? 404 BMA A O4 1 HETATM 5087 O O5 . BMA F 4 . ? -18.088 -14.016 -32.704 1.00 30.76 ? 404 BMA A O5 1 HETATM 5088 O O6 . BMA F 4 . ? -16.368 -15.914 -33.463 1.00 24.76 ? 404 BMA A O6 1 HETATM 5089 C C1 . MAN G 5 . ? -18.059 -11.535 -28.133 1.00 31.16 ? 405 MAN A C1 1 HETATM 5090 C C2 . MAN G 5 . ? -18.513 -11.663 -26.673 1.00 28.52 ? 405 MAN A C2 1 HETATM 5091 C C3 . MAN G 5 . ? -20.026 -11.450 -26.634 1.00 35.70 ? 405 MAN A C3 1 HETATM 5092 C C4 . MAN G 5 . ? -20.397 -10.080 -27.224 1.00 29.39 ? 405 MAN A C4 1 HETATM 5093 C C5 . MAN G 5 . ? -19.833 -9.956 -28.658 1.00 26.80 ? 405 MAN A C5 1 HETATM 5094 C C6 . MAN G 5 . ? -20.035 -8.583 -29.274 1.00 35.34 ? 405 MAN A C6 1 HETATM 5095 O O2 . MAN G 5 . ? -17.937 -10.617 -25.911 1.00 38.36 ? 405 MAN A O2 1 HETATM 5096 O O3 . MAN G 5 . ? -20.567 -11.579 -25.322 1.00 33.37 ? 405 MAN A O3 1 HETATM 5097 O O4 . MAN G 5 . ? -21.817 -9.956 -27.253 1.00 38.23 ? 405 MAN A O4 1 HETATM 5098 O O5 . MAN G 5 . ? -18.393 -10.246 -28.665 1.00 25.54 ? 405 MAN A O5 1 HETATM 5099 O O6 . MAN G 5 . ? -19.369 -8.578 -30.536 1.00 34.04 ? 405 MAN A O6 1 HETATM 5100 C C1 . MAN H 5 . ? -17.188 -11.109 -24.780 1.00 44.26 ? 406 MAN A C1 1 HETATM 5101 C C2 . MAN H 5 . ? -16.913 -9.922 -23.821 1.00 52.89 ? 406 MAN A C2 1 HETATM 5102 C C3 . MAN H 5 . ? -15.840 -8.992 -24.444 1.00 46.91 ? 406 MAN A C3 1 HETATM 5103 C C4 . MAN H 5 . ? -14.616 -9.794 -24.856 1.00 46.58 ? 406 MAN A C4 1 HETATM 5104 C C5 . MAN H 5 . ? -15.073 -10.873 -25.846 1.00 49.19 ? 406 MAN A C5 1 HETATM 5105 C C6 . MAN H 5 . ? -13.940 -11.686 -26.421 1.00 58.46 ? 406 MAN A C6 1 HETATM 5106 O O2 . MAN H 5 . ? -16.395 -10.390 -22.585 1.00 54.10 ? 406 MAN A O2 1 HETATM 5107 O O3 . MAN H 5 . ? -15.455 -7.898 -23.601 1.00 41.58 ? 406 MAN A O3 1 HETATM 5108 O O4 . MAN H 5 . ? -13.675 -8.934 -25.476 1.00 49.60 ? 406 MAN A O4 1 HETATM 5109 O O5 . MAN H 5 . ? -15.986 -11.751 -25.162 1.00 41.36 ? 406 MAN A O5 1 HETATM 5110 O O6 . MAN H 5 . ? -13.512 -11.026 -27.610 1.00 64.50 ? 406 MAN A O6 1 HETATM 5111 C C1 . MAN I 5 . ? -15.707 -17.164 -33.723 1.00 26.17 ? 407 MAN A C1 1 HETATM 5112 C C2 . MAN I 5 . ? -15.207 -17.142 -35.173 1.00 33.20 ? 407 MAN A C2 1 HETATM 5113 C C3 . MAN I 5 . ? -16.478 -17.091 -36.054 1.00 37.59 ? 407 MAN A C3 1 HETATM 5114 C C4 . MAN I 5 . ? -17.350 -18.315 -35.787 1.00 28.71 ? 407 MAN A C4 1 HETATM 5115 C C5 . MAN I 5 . ? -17.788 -18.276 -34.301 1.00 29.73 ? 407 MAN A C5 1 HETATM 5116 C C6 . MAN I 5 . ? -18.623 -19.483 -33.887 1.00 33.85 ? 407 MAN A C6 1 HETATM 5117 O O2 . MAN I 5 . ? -14.506 -18.337 -35.443 1.00 34.89 ? 407 MAN A O2 1 HETATM 5118 O O3 . MAN I 5 . ? -16.369 -16.845 -37.488 1.00 45.06 ? 407 MAN A O3 1 HETATM 5119 O O4 . MAN I 5 . ? -18.478 -18.289 -36.655 1.00 30.30 ? 407 MAN A O4 1 HETATM 5120 O O5 . MAN I 5 . ? -16.582 -18.249 -33.468 1.00 24.63 ? 407 MAN A O5 1 HETATM 5121 O O6 . MAN I 5 . ? -17.927 -20.647 -34.348 1.00 30.78 ? 407 MAN A O6 1 HETATM 5122 C C1 . MAN J 5 . ? -15.070 -16.780 -38.085 1.00 62.35 ? 408 MAN A C1 1 HETATM 5123 C C2 . MAN J 5 . ? -14.600 -15.309 -38.250 1.00 77.47 ? 408 MAN A C2 1 HETATM 5124 C C3 . MAN J 5 . ? -13.201 -15.283 -38.885 1.00 76.88 ? 408 MAN A C3 1 HETATM 5125 C C4 . MAN J 5 . ? -12.908 -16.593 -39.634 1.00 76.10 ? 408 MAN A C4 1 HETATM 5126 C C5 . MAN J 5 . ? -14.194 -17.020 -40.344 1.00 70.04 ? 408 MAN A C5 1 HETATM 5127 C C6 . MAN J 5 . ? -13.996 -18.136 -41.349 1.00 67.01 ? 408 MAN A C6 1 HETATM 5128 O O2 . MAN J 5 . ? -14.496 -14.645 -37.004 1.00 79.32 ? 408 MAN A O2 1 HETATM 5129 O O3 . MAN J 5 . ? -12.198 -15.026 -37.920 1.00 75.63 ? 408 MAN A O3 1 HETATM 5130 O O4 . MAN J 5 . ? -11.869 -16.415 -40.578 1.00 86.16 ? 408 MAN A O4 1 HETATM 5131 O O5 . MAN J 5 . ? -15.112 -17.480 -39.336 1.00 70.63 ? 408 MAN A O5 1 HETATM 5132 O O6 . MAN J 5 . ? -15.277 -18.627 -41.718 1.00 66.68 ? 408 MAN A O6 1 HETATM 5133 C C1 . MAN K 5 . ? -18.637 -21.860 -34.058 1.00 27.68 ? 409 MAN A C1 1 HETATM 5134 C C2 . MAN K 5 . ? -17.743 -22.998 -34.549 1.00 34.06 ? 409 MAN A C2 1 HETATM 5135 C C3 . MAN K 5 . ? -17.731 -22.987 -36.084 1.00 35.38 ? 409 MAN A C3 1 HETATM 5136 C C4 . MAN K 5 . ? -19.151 -22.976 -36.679 1.00 31.46 ? 409 MAN A C4 1 HETATM 5137 C C5 . MAN K 5 . ? -19.961 -21.832 -36.080 1.00 31.38 ? 409 MAN A C5 1 HETATM 5138 C C6 . MAN K 5 . ? -21.416 -21.833 -36.542 1.00 33.98 ? 409 MAN A C6 1 HETATM 5139 O O2 . MAN K 5 . ? -18.236 -24.256 -34.115 1.00 30.80 ? 409 MAN A O2 1 HETATM 5140 O O3 . MAN K 5 . ? -16.974 -24.062 -36.622 1.00 32.85 ? 409 MAN A O3 1 HETATM 5141 O O4 . MAN K 5 . ? -19.080 -22.769 -38.082 1.00 32.79 ? 409 MAN A O4 1 HETATM 5142 O O5 . MAN K 5 . ? -19.933 -21.923 -34.633 1.00 23.55 ? 409 MAN A O5 1 HETATM 5143 O O6 . MAN K 5 . ? -22.201 -21.126 -35.584 1.00 39.00 ? 409 MAN A O6 1 HETATM 5144 C C1 . NAG L 3 . ? -12.244 8.315 -48.286 1.00 14.31 ? 410 NAG A C1 1 HETATM 5145 C C2 . NAG L 3 . ? -10.971 7.460 -48.367 1.00 17.68 ? 410 NAG A C2 1 HETATM 5146 C C3 . NAG L 3 . ? -11.314 6.026 -48.755 1.00 15.77 ? 410 NAG A C3 1 HETATM 5147 C C4 . NAG L 3 . ? -12.419 5.459 -47.874 1.00 10.45 ? 410 NAG A C4 1 HETATM 5148 C C5 . NAG L 3 . ? -13.611 6.410 -47.889 1.00 17.02 ? 410 NAG A C5 1 HETATM 5149 C C6 . NAG L 3 . ? -14.763 5.984 -47.006 1.00 12.25 ? 410 NAG A C6 1 HETATM 5150 C C7 . NAG L 3 . ? -8.946 8.714 -49.012 1.00 30.17 ? 410 NAG A C7 1 HETATM 5151 C C8 . NAG L 3 . ? -8.708 8.921 -47.555 1.00 21.26 ? 410 NAG A C8 1 HETATM 5152 N N2 . NAG L 3 . ? -10.040 8.020 -49.336 1.00 17.57 ? 410 NAG A N2 1 HETATM 5153 O O3 . NAG L 3 . ? -10.144 5.229 -48.632 1.00 23.54 ? 410 NAG A O3 1 HETATM 5154 O O4 . NAG L 3 . ? -12.798 4.218 -48.460 1.00 11.85 ? 410 NAG A O4 1 HETATM 5155 O O5 . NAG L 3 . ? -13.184 7.696 -47.425 1.00 17.74 ? 410 NAG A O5 1 HETATM 5156 O O6 . NAG L 3 . ? -14.343 5.776 -45.667 1.00 13.54 ? 410 NAG A O6 1 HETATM 5157 O O7 . NAG L 3 . ? -8.185 9.161 -49.868 1.00 40.79 ? 410 NAG A O7 1 HETATM 5158 C C1 . NAG M 3 . ? -12.849 3.162 -47.495 1.00 15.26 ? 411 NAG A C1 1 HETATM 5159 C C2 . NAG M 3 . ? -13.466 1.977 -48.227 1.00 14.18 ? 411 NAG A C2 1 HETATM 5160 C C3 . NAG M 3 . ? -13.474 0.741 -47.330 1.00 17.27 ? 411 NAG A C3 1 HETATM 5161 C C4 . NAG M 3 . ? -12.075 0.484 -46.781 1.00 17.49 ? 411 NAG A C4 1 HETATM 5162 C C5 . NAG M 3 . ? -11.521 1.750 -46.123 1.00 18.38 ? 411 NAG A C5 1 HETATM 5163 C C6 . NAG M 3 . ? -10.085 1.611 -45.672 1.00 19.80 ? 411 NAG A C6 1 HETATM 5164 C C7 . NAG M 3 . ? -15.879 2.506 -47.983 1.00 13.70 ? 411 NAG A C7 1 HETATM 5165 C C8 . NAG M 3 . ? -17.153 2.798 -48.730 1.00 11.59 ? 411 NAG A C8 1 HETATM 5166 N N2 . NAG M 3 . ? -14.797 2.278 -48.738 1.00 11.26 ? 411 NAG A N2 1 HETATM 5167 O O3 . NAG M 3 . ? -13.900 -0.367 -48.115 1.00 15.61 ? 411 NAG A O3 1 HETATM 5168 O O4 . NAG M 3 . ? -12.109 -0.560 -45.816 1.00 25.36 ? 411 NAG A O4 1 HETATM 5169 O O5 . NAG M 3 . ? -11.544 2.829 -47.068 1.00 16.43 ? 411 NAG A O5 1 HETATM 5170 O O6 . NAG M 3 . ? -9.224 1.368 -46.779 1.00 26.36 ? 411 NAG A O6 1 HETATM 5171 O O7 . NAG M 3 . ? -15.837 2.496 -46.759 1.00 14.95 ? 411 NAG A O7 1 HETATM 5172 C C1 . BMA N 4 . ? -11.208 -1.624 -46.196 1.00 23.03 ? 412 BMA A C1 1 HETATM 5173 C C2 . BMA N 4 . ? -11.223 -2.627 -45.071 1.00 29.10 ? 412 BMA A C2 1 HETATM 5174 C C3 . BMA N 4 . ? -10.417 -3.890 -45.487 1.00 41.49 ? 412 BMA A C3 1 HETATM 5175 C C4 . BMA N 4 . ? -10.812 -4.394 -46.891 1.00 28.93 ? 412 BMA A C4 1 HETATM 5176 C C5 . BMA N 4 . ? -10.754 -3.259 -47.885 1.00 26.64 ? 412 BMA A C5 1 HETATM 5177 C C6 . BMA N 4 . ? -11.279 -3.693 -49.233 1.00 29.34 ? 412 BMA A C6 1 HETATM 5178 O O2 . BMA N 4 . ? -12.561 -3.030 -44.832 1.00 36.93 ? 412 BMA A O2 1 HETATM 5179 O O3 . BMA N 4 . ? -10.550 -4.966 -44.563 1.00 52.10 ? 412 BMA A O3 1 HETATM 5180 O O4 . BMA N 4 . ? -9.926 -5.408 -47.324 1.00 36.38 ? 412 BMA A O4 1 HETATM 5181 O O5 . BMA N 4 . ? -11.605 -2.221 -47.408 1.00 23.70 ? 412 BMA A O5 1 HETATM 5182 O O6 . BMA N 4 . ? -12.437 -4.520 -48.993 1.00 24.73 ? 412 BMA A O6 1 HETATM 5183 C C1 . MAN O 5 . ? -13.311 -4.443 -50.123 1.00 25.43 ? 413 MAN A C1 1 HETATM 5184 C C2 . MAN O 5 . ? -14.654 -5.050 -49.766 1.00 21.20 ? 413 MAN A C2 1 HETATM 5185 C C3 . MAN O 5 . ? -14.475 -6.558 -49.521 1.00 20.33 ? 413 MAN A C3 1 HETATM 5186 C C4 . MAN O 5 . ? -13.638 -7.239 -50.647 1.00 26.80 ? 413 MAN A C4 1 HETATM 5187 C C5 . MAN O 5 . ? -12.360 -6.457 -50.959 1.00 27.80 ? 413 MAN A C5 1 HETATM 5188 C C6 . MAN O 5 . ? -11.662 -6.981 -52.197 1.00 31.36 ? 413 MAN A C6 1 HETATM 5189 O O2 . MAN O 5 . ? -15.519 -4.924 -50.894 1.00 20.86 ? 413 MAN A O2 1 HETATM 5190 O O3 . MAN O 5 . ? -15.711 -7.191 -49.489 1.00 24.05 ? 413 MAN A O3 1 HETATM 5191 O O4 . MAN O 5 . ? -13.297 -8.562 -50.285 1.00 34.82 ? 413 MAN A O4 1 HETATM 5192 O O5 . MAN O 5 . ? -12.748 -5.104 -51.234 1.00 24.13 ? 413 MAN A O5 1 HETATM 5193 O O6 . MAN O 5 . ? -12.670 -7.059 -53.197 1.00 31.88 ? 413 MAN A O6 1 HETATM 5194 C C1 . MAN P 5 . ? -16.176 -7.312 -48.142 1.00 27.67 ? 414 MAN A C1 1 HETATM 5195 C C2 . MAN P 5 . ? -16.982 -8.593 -48.101 1.00 29.57 ? 414 MAN A C2 1 HETATM 5196 C C3 . MAN P 5 . ? -18.159 -8.418 -49.054 1.00 35.07 ? 414 MAN A C3 1 HETATM 5197 C C4 . MAN P 5 . ? -19.002 -7.182 -48.675 1.00 31.26 ? 414 MAN A C4 1 HETATM 5198 C C5 . MAN P 5 . ? -18.099 -5.918 -48.604 1.00 29.07 ? 414 MAN A C5 1 HETATM 5199 C C6 . MAN P 5 . ? -18.847 -4.688 -48.067 1.00 34.48 ? 414 MAN A C6 1 HETATM 5200 O O2 . MAN P 5 . ? -17.524 -8.785 -46.805 1.00 38.17 ? 414 MAN A O2 1 HETATM 5201 O O3 . MAN P 5 . ? -18.982 -9.563 -49.108 1.00 36.41 ? 414 MAN A O3 1 HETATM 5202 O O4 . MAN P 5 . ? -20.017 -6.994 -49.648 1.00 34.50 ? 414 MAN A O4 1 HETATM 5203 O O5 . MAN P 5 . ? -16.951 -6.194 -47.742 1.00 27.48 ? 414 MAN A O5 1 HETATM 5204 O O6 . MAN P 5 . ? -18.360 -3.510 -48.720 1.00 30.40 ? 414 MAN A O6 1 HETATM 5205 C C1 . MAN Q 5 . ? -16.611 -9.605 -46.042 1.00 48.82 ? 415 MAN A C1 1 HETATM 5206 C C2 . MAN Q 5 . ? -17.388 -10.428 -44.979 1.00 73.50 ? 415 MAN A C2 1 HETATM 5207 C C3 . MAN Q 5 . ? -17.776 -9.552 -43.776 1.00 67.44 ? 415 MAN A C3 1 HETATM 5208 C C4 . MAN Q 5 . ? -16.597 -8.681 -43.280 1.00 64.46 ? 415 MAN A C4 1 HETATM 5209 C C5 . MAN Q 5 . ? -15.950 -7.911 -44.464 1.00 74.21 ? 415 MAN A C5 1 HETATM 5210 C C6 . MAN Q 5 . ? -14.736 -7.082 -44.056 1.00 72.64 ? 415 MAN A C6 1 HETATM 5211 O O2 . MAN Q 5 . ? -16.588 -11.483 -44.464 1.00 77.03 ? 415 MAN A O2 1 HETATM 5212 O O3 . MAN Q 5 . ? -18.278 -10.347 -42.706 1.00 65.11 ? 415 MAN A O3 1 HETATM 5213 O O4 . MAN Q 5 . ? -17.045 -7.757 -42.285 1.00 55.78 ? 415 MAN A O4 1 HETATM 5214 O O5 . MAN Q 5 . ? -15.537 -8.865 -45.469 1.00 63.97 ? 415 MAN A O5 1 HETATM 5215 O O6 . MAN Q 5 . ? -14.146 -6.533 -45.229 1.00 71.51 ? 415 MAN A O6 1 HETATM 5216 C C1 . MAN R 5 . ? -12.177 -7.627 -54.422 1.00 37.94 ? 416 MAN A C1 1 HETATM 5217 C C2 . MAN R 5 . ? -13.095 -7.145 -55.530 1.00 44.75 ? 416 MAN A C2 1 HETATM 5218 C C3 . MAN R 5 . ? -14.492 -7.661 -55.235 1.00 41.67 ? 416 MAN A C3 1 HETATM 5219 C C4 . MAN R 5 . ? -14.478 -9.188 -55.172 1.00 43.80 ? 416 MAN A C4 1 HETATM 5220 C C5 . MAN R 5 . ? -13.447 -9.664 -54.129 1.00 44.79 ? 416 MAN A C5 1 HETATM 5221 C C6 . MAN R 5 . ? -13.280 -11.173 -54.137 1.00 55.39 ? 416 MAN A C6 1 HETATM 5222 O O2 . MAN R 5 . ? -12.729 -7.759 -56.741 1.00 51.05 ? 416 MAN A O2 1 HETATM 5223 O O3 . MAN R 5 . ? -15.438 -7.226 -56.204 1.00 41.88 ? 416 MAN A O3 1 HETATM 5224 O O4 . MAN R 5 . ? -15.757 -9.663 -54.815 1.00 42.15 ? 416 MAN A O4 1 HETATM 5225 O O5 . MAN R 5 . ? -12.149 -9.039 -54.393 1.00 36.65 ? 416 MAN A O5 1 HETATM 5226 O O6 . MAN R 5 . ? -11.944 -11.481 -53.758 1.00 64.55 ? 416 MAN A O6 1 HETATM 5227 C C1 . MAN S 5 . ? -12.089 -6.806 -57.607 1.00 55.17 ? 417 MAN A C1 1 HETATM 5228 C C2 . MAN S 5 . ? -12.151 -7.378 -59.027 1.00 59.62 ? 417 MAN A C2 1 HETATM 5229 C C3 . MAN S 5 . ? -11.221 -8.588 -59.126 1.00 61.21 ? 417 MAN A C3 1 HETATM 5230 C C4 . MAN S 5 . ? -9.808 -8.256 -58.623 1.00 60.41 ? 417 MAN A C4 1 HETATM 5231 C C5 . MAN S 5 . ? -9.863 -7.649 -57.199 1.00 59.69 ? 417 MAN A C5 1 HETATM 5232 C C6 . MAN S 5 . ? -8.501 -7.191 -56.691 1.00 57.88 ? 417 MAN A C6 1 HETATM 5233 O O2 . MAN S 5 . ? -11.697 -6.435 -59.976 1.00 58.95 ? 417 MAN A O2 1 HETATM 5234 O O3 . MAN S 5 . ? -11.157 -9.083 -60.454 1.00 67.10 ? 417 MAN A O3 1 HETATM 5235 O O4 . MAN S 5 . ? -9.022 -9.437 -58.609 1.00 62.00 ? 417 MAN A O4 1 HETATM 5236 O O5 . MAN S 5 . ? -10.758 -6.508 -57.202 1.00 56.76 ? 417 MAN A O5 1 HETATM 5237 O O6 . MAN S 5 . ? -8.673 -6.605 -55.407 1.00 58.48 ? 417 MAN A O6 1 HETATM 5238 C C1 . MAN T 5 . ? -10.181 -4.575 -43.223 1.00 68.00 ? 418 MAN A C1 1 HETATM 5239 C C2 . MAN T 5 . ? -8.688 -4.131 -43.142 1.00 90.55 ? 418 MAN A C2 1 HETATM 5240 C C3 . MAN T 5 . ? -7.730 -5.348 -43.086 1.00 87.78 ? 418 MAN A C3 1 HETATM 5241 C C4 . MAN T 5 . ? -8.259 -6.473 -42.166 1.00 85.79 ? 418 MAN A C4 1 HETATM 5242 C C5 . MAN T 5 . ? -9.716 -6.793 -42.542 1.00 83.25 ? 418 MAN A C5 1 HETATM 5243 C C6 . MAN T 5 . ? -10.321 -7.931 -41.746 1.00 83.43 ? 418 MAN A C6 1 HETATM 5244 O O2 . MAN T 5 . ? -8.462 -3.358 -41.972 1.00 92.36 ? 418 MAN A O2 1 HETATM 5245 O O3 . MAN T 5 . ? -6.408 -4.969 -42.690 1.00 81.79 ? 418 MAN A O3 1 HETATM 5246 O O4 . MAN T 5 . ? -7.453 -7.636 -42.302 1.00 83.39 ? 418 MAN A O4 1 HETATM 5247 O O5 . MAN T 5 . ? -10.486 -5.603 -42.304 1.00 79.17 ? 418 MAN A O5 1 HETATM 5248 O O6 . MAN T 5 . ? -10.948 -8.821 -42.663 1.00 83.87 ? 418 MAN A O6 1 HETATM 5249 C C1 . NAG U 3 . ? -9.496 19.612 -13.062 1.00 24.18 ? 419 NAG A C1 1 HETATM 5250 C C2 . NAG U 3 . ? -8.182 20.073 -12.453 1.00 36.47 ? 419 NAG A C2 1 HETATM 5251 C C3 . NAG U 3 . ? -7.145 20.327 -13.560 1.00 40.29 ? 419 NAG A C3 1 HETATM 5252 C C4 . NAG U 3 . ? -7.102 19.204 -14.599 1.00 42.86 ? 419 NAG A C4 1 HETATM 5253 C C5 . NAG U 3 . ? -8.495 18.700 -14.978 1.00 33.43 ? 419 NAG A C5 1 HETATM 5254 C C6 . NAG U 3 . ? -8.452 17.408 -15.752 1.00 33.04 ? 419 NAG A C6 1 HETATM 5255 C C7 . NAG U 3 . ? -8.569 21.273 -10.334 1.00 45.47 ? 419 NAG A C7 1 HETATM 5256 C C8 . NAG U 3 . ? -8.520 19.932 -9.660 1.00 48.56 ? 419 NAG A C8 1 HETATM 5257 N N2 . NAG U 3 . ? -8.389 21.276 -11.661 1.00 36.00 ? 419 NAG A N2 1 HETATM 5258 O O3 . NAG U 3 . ? -5.858 20.477 -12.969 1.00 44.82 ? 419 NAG A O3 1 HETATM 5259 O O4 . NAG U 3 . ? -6.562 19.709 -15.817 1.00 52.57 ? 419 NAG A O4 1 HETATM 5260 O O5 . NAG U 3 . ? -9.278 18.444 -13.808 1.00 28.03 ? 419 NAG A O5 1 HETATM 5261 O O6 . NAG U 3 . ? -7.936 16.364 -14.939 1.00 31.42 ? 419 NAG A O6 1 HETATM 5262 O O7 . NAG U 3 . ? -8.756 22.310 -9.705 1.00 52.18 ? 419 NAG A O7 1 HETATM 5263 C C1 . NAG V 3 . ? -5.220 19.291 -16.124 1.00 58.70 ? 420 NAG A C1 1 HETATM 5264 C C2 . NAG V 3 . ? -5.048 19.204 -17.648 1.00 58.84 ? 420 NAG A C2 1 HETATM 5265 C C3 . NAG V 3 . ? -3.589 18.904 -18.000 1.00 65.53 ? 420 NAG A C3 1 HETATM 5266 C C4 . NAG V 3 . ? -2.650 19.908 -17.337 1.00 68.41 ? 420 NAG A C4 1 HETATM 5267 C C5 . NAG V 3 . ? -2.928 19.942 -15.836 1.00 63.43 ? 420 NAG A C5 1 HETATM 5268 C C6 . NAG V 3 . ? -2.120 20.985 -15.102 1.00 61.03 ? 420 NAG A C6 1 HETATM 5269 C C7 . NAG V 3 . ? -6.995 18.482 -18.987 1.00 44.53 ? 420 NAG A C7 1 HETATM 5270 C C8 . NAG V 3 . ? -7.758 17.301 -19.512 1.00 41.83 ? 420 NAG A C8 1 HETATM 5271 N N2 . NAG V 3 . ? -5.925 18.198 -18.230 1.00 54.57 ? 420 NAG A N2 1 HETATM 5272 O O3 . NAG V 3 . ? -3.439 18.915 -19.416 1.00 65.48 ? 420 NAG A O3 1 HETATM 5273 O O4 . NAG V 3 . ? -1.291 19.509 -17.501 1.00 71.27 ? 420 NAG A O4 1 HETATM 5274 O O5 . NAG V 3 . ? -4.309 20.248 -15.595 1.00 60.58 ? 420 NAG A O5 1 HETATM 5275 O O6 . NAG V 3 . ? -2.640 21.201 -13.797 1.00 54.30 ? 420 NAG A O6 1 HETATM 5276 O O7 . NAG V 3 . ? -7.340 19.636 -19.226 1.00 27.92 ? 420 NAG A O7 1 HETATM 5277 C C1 . BMA W 4 . ? -0.451 20.216 -18.466 1.00 78.68 ? 421 BMA A C1 1 HETATM 5278 C C2 . BMA W 4 . ? -1.152 20.884 -19.651 1.00 80.91 ? 421 BMA A C2 1 HETATM 5279 C C3 . BMA W 4 . ? -0.084 20.949 -20.738 1.00 83.84 ? 421 BMA A C3 1 HETATM 5280 C C4 . BMA W 4 . ? 1.062 21.874 -20.264 1.00 84.99 ? 421 BMA A C4 1 HETATM 5281 C C5 . BMA W 4 . ? 1.662 21.348 -18.920 1.00 72.59 ? 421 BMA A C5 1 HETATM 5282 C C6 . BMA W 4 . ? 2.688 22.304 -18.305 1.00 67.37 ? 421 BMA A C6 1 HETATM 5283 O O2 . BMA W 4 . ? -1.509 22.217 -19.347 1.00 81.78 ? 421 BMA A O2 1 HETATM 5284 O O3 . BMA W 4 . ? -0.582 21.334 -22.037 1.00 83.34 ? 421 BMA A O3 1 HETATM 5285 O O4 . BMA W 4 . ? 2.076 21.940 -21.247 1.00 88.50 ? 421 BMA A O4 1 HETATM 5286 O O5 . BMA W 4 . ? 0.577 21.090 -17.948 1.00 78.06 ? 421 BMA A O5 1 HETATM 5287 O O6 . BMA W 4 . ? 3.595 21.553 -17.491 1.00 62.35 ? 421 BMA A O6 1 HETATM 5288 C C1 . MAN X 5 . ? -1.077 20.228 -22.847 1.00 86.26 ? 422 MAN A C1 1 HETATM 5289 C C2 . MAN X 5 . ? -0.716 18.794 -22.333 1.00 100.79 ? 422 MAN A C2 1 HETATM 5290 C C3 . MAN X 5 . ? -0.622 17.826 -23.513 1.00 97.42 ? 422 MAN A C3 1 HETATM 5291 C C4 . MAN X 5 . ? 0.425 18.279 -24.551 1.00 88.20 ? 422 MAN A C4 1 HETATM 5292 C C5 . MAN X 5 . ? 0.517 19.820 -24.623 1.00 88.34 ? 422 MAN A C5 1 HETATM 5293 C C6 . MAN X 5 . ? 0.856 20.321 -26.018 1.00 85.05 ? 422 MAN A C6 1 HETATM 5294 O O2 . MAN X 5 . ? -1.722 18.277 -21.458 1.00 101.21 ? 422 MAN A O2 1 HETATM 5295 O O3 . MAN X 5 . ? -1.896 17.622 -24.135 1.00 99.28 ? 422 MAN A O3 1 HETATM 5296 O O4 . MAN X 5 . ? 1.691 17.734 -24.213 1.00 80.44 ? 422 MAN A O4 1 HETATM 5297 O O5 . MAN X 5 . ? -0.756 20.384 -24.233 1.00 89.29 ? 422 MAN A O5 1 HETATM 5298 O O6 . MAN X 5 . ? 1.233 21.690 -25.929 1.00 79.62 ? 422 MAN A O6 1 HETATM 5299 C C1 . NAG Y 3 . ? -15.889 21.578 -8.272 1.00 47.77 ? 423 NAG A C1 1 HETATM 5300 C C2 . NAG Y 3 . ? -16.190 23.069 -8.079 1.00 54.22 ? 423 NAG A C2 1 HETATM 5301 C C3 . NAG Y 3 . ? -15.256 23.673 -7.026 1.00 56.31 ? 423 NAG A C3 1 HETATM 5302 C C4 . NAG Y 3 . ? -15.240 22.830 -5.756 1.00 57.06 ? 423 NAG A C4 1 HETATM 5303 C C5 . NAG Y 3 . ? -14.951 21.376 -6.111 1.00 58.89 ? 423 NAG A C5 1 HETATM 5304 C C6 . NAG Y 3 . ? -14.956 20.454 -4.919 1.00 59.53 ? 423 NAG A C6 1 HETATM 5305 C C7 . NAG Y 3 . ? -17.006 24.506 -9.910 1.00 73.83 ? 423 NAG A C7 1 HETATM 5306 C C8 . NAG Y 3 . ? -16.655 25.141 -11.221 1.00 73.60 ? 423 NAG A C8 1 HETATM 5307 N N2 . NAG Y 3 . ? -16.042 23.772 -9.344 1.00 69.43 ? 423 NAG A N2 1 HETATM 5308 O O3 . NAG Y 3 . ? -15.680 24.999 -6.733 1.00 57.30 ? 423 NAG A O3 1 HETATM 5309 O O4 . NAG Y 3 . ? -14.245 23.309 -4.857 1.00 55.07 ? 423 NAG A O4 1 HETATM 5310 O O5 . NAG Y 3 . ? -15.959 20.901 -7.015 1.00 60.81 ? 423 NAG A O5 1 HETATM 5311 O O6 . NAG Y 3 . ? -13.826 19.595 -4.955 1.00 57.53 ? 423 NAG A O6 1 HETATM 5312 O O7 . NAG Y 3 . ? -18.109 24.654 -9.388 1.00 72.90 ? 423 NAG A O7 1 HETATM 5313 MG MG . MG Z 6 . ? -35.278 14.234 -45.549 1.00 21.02 ? 424 MG A MG 1 HETATM 5314 C C1 . PEG AA 7 . ? -7.376 16.743 -23.905 1.00 47.51 ? 425 PEG A C1 1 HETATM 5315 O O1 . PEG AA 7 . ? -7.792 15.707 -23.012 1.00 40.77 ? 425 PEG A O1 1 HETATM 5316 C C2 . PEG AA 7 . ? -6.235 16.250 -24.834 1.00 53.90 ? 425 PEG A C2 1 HETATM 5317 O O2 . PEG AA 7 . ? -6.025 17.218 -25.875 1.00 50.34 ? 425 PEG A O2 1 HETATM 5318 C C3 . PEG AA 7 . ? -5.457 16.682 -27.090 1.00 50.53 ? 425 PEG A C3 1 HETATM 5319 C C4 . PEG AA 7 . ? -5.279 17.802 -28.111 1.00 49.40 ? 425 PEG A C4 1 HETATM 5320 O O4 . PEG AA 7 . ? -6.498 18.078 -28.781 1.00 42.24 ? 425 PEG A O4 1 HETATM 5321 C C2 . P6G BA 8 . ? -37.709 20.167 -38.644 1.00 81.79 ? 426 P6G A C2 1 HETATM 5322 C C3 . P6G BA 8 . ? -38.511 19.067 -37.943 1.00 80.36 ? 426 P6G A C3 1 HETATM 5323 O O4 . P6G BA 8 . ? -37.806 18.633 -36.766 1.00 79.17 ? 426 P6G A O4 1 HETATM 5324 C C5 . P6G BA 8 . ? -38.543 17.577 -36.146 1.00 71.93 ? 426 P6G A C5 1 HETATM 5325 C C6 . P6G BA 8 . ? -37.818 17.008 -34.924 1.00 66.80 ? 426 P6G A C6 1 HETATM 5326 O O7 . P6G BA 8 . ? -38.555 15.897 -34.342 1.00 63.59 ? 426 P6G A O7 1 HETATM 5327 C C8 . P6G BA 8 . ? -38.712 15.065 -35.507 1.00 58.38 ? 426 P6G A C8 1 HETATM 5328 C C9 . P6G BA 8 . ? -39.248 13.656 -35.624 1.00 59.91 ? 426 P6G A C9 1 HETATM 5329 O O10 . P6G BA 8 . ? -39.133 13.615 -37.067 1.00 70.01 ? 426 P6G A O10 1 HETATM 5330 C C11 . P6G BA 8 . ? -39.363 12.360 -37.682 1.00 68.48 ? 426 P6G A C11 1 HETATM 5331 C C12 . P6G BA 8 . ? -39.379 12.528 -39.218 1.00 67.94 ? 426 P6G A C12 1 HETATM 5332 O O13 . P6G BA 8 . ? -39.560 11.212 -39.777 1.00 70.79 ? 426 P6G A O13 1 HETATM 5333 C C14 . P6G BA 8 . ? -40.698 10.650 -39.118 1.00 68.82 ? 426 P6G A C14 1 HETATM 5334 C C15 . P6G BA 8 . ? -40.948 9.212 -39.457 1.00 59.36 ? 426 P6G A C15 1 HETATM 5335 O O16 . P6G BA 8 . ? -42.032 8.909 -38.579 1.00 58.77 ? 426 P6G A O16 1 HETATM 5336 C C17 . P6G BA 8 . ? -42.294 7.520 -38.630 1.00 55.51 ? 426 P6G A C17 1 HETATM 5337 C C18 . P6G BA 8 . ? -43.352 7.122 -37.640 1.00 50.21 ? 426 P6G A C18 1 HETATM 5338 O O19 . P6G BA 8 . ? -43.469 5.706 -37.830 1.00 54.97 ? 426 P6G A O19 1 HETATM 5339 O O4 . P6G CA 8 . ? -30.660 -1.951 -48.952 1.00 47.30 ? 427 P6G A O4 1 HETATM 5340 C C5 . P6G CA 8 . ? -29.750 -0.902 -49.306 1.00 44.84 ? 427 P6G A C5 1 HETATM 5341 C C6 . P6G CA 8 . ? -28.779 -0.595 -48.158 1.00 37.41 ? 427 P6G A C6 1 HETATM 5342 O O7 . P6G CA 8 . ? -27.940 0.468 -48.646 1.00 38.52 ? 427 P6G A O7 1 HETATM 5343 C C8 . P6G CA 8 . ? -26.910 0.927 -47.752 1.00 36.83 ? 427 P6G A C8 1 HETATM 5344 C C9 . P6G CA 8 . ? -26.166 1.997 -48.548 1.00 44.71 ? 427 P6G A C9 1 HETATM 5345 O O10 . P6G CA 8 . ? -27.114 3.023 -48.855 1.00 56.29 ? 427 P6G A O10 1 HETATM 5346 C C11 . P6G CA 8 . ? -26.578 4.022 -49.736 1.00 53.19 ? 427 P6G A C11 1 HETATM 5347 C C12 . P6G CA 8 . ? -27.563 5.154 -50.068 1.00 54.45 ? 427 P6G A C12 1 HETATM 5348 O O13 . P6G CA 8 . ? -28.847 4.853 -50.702 1.00 54.36 ? 427 P6G A O13 1 HETATM 5349 C C14 . P6G CA 8 . ? -29.709 4.066 -49.851 1.00 46.80 ? 427 P6G A C14 1 HETATM 5350 C C15 . P6G CA 8 . ? -31.056 3.774 -50.469 1.00 36.59 ? 427 P6G A C15 1 HETATM 5351 O O16 . P6G CA 8 . ? -31.814 2.994 -49.531 1.00 38.16 ? 427 P6G A O16 1 HETATM 5352 C C1 . GOL DA 9 . ? -40.165 -1.647 -16.265 1.00 63.84 ? 428 GOL A C1 1 HETATM 5353 O O1 . GOL DA 9 . ? -41.291 -1.096 -16.913 1.00 68.50 ? 428 GOL A O1 1 HETATM 5354 C C2 . GOL DA 9 . ? -40.237 -3.171 -16.295 1.00 64.19 ? 428 GOL A C2 1 HETATM 5355 O O2 . GOL DA 9 . ? -40.624 -3.606 -17.583 1.00 65.64 ? 428 GOL A O2 1 HETATM 5356 C C3 . GOL DA 9 . ? -38.867 -3.744 -15.939 1.00 62.01 ? 428 GOL A C3 1 HETATM 5357 O O3 . GOL DA 9 . ? -38.872 -5.149 -16.061 1.00 63.16 ? 428 GOL A O3 1 HETATM 5358 C C1 . GOL EA 9 . ? -5.284 31.125 -21.411 1.00 62.32 ? 429 GOL A C1 1 HETATM 5359 O O1 . GOL EA 9 . ? -5.349 29.837 -21.986 1.00 58.90 ? 429 GOL A O1 1 HETATM 5360 C C2 . GOL EA 9 . ? -6.175 31.208 -20.172 1.00 62.25 ? 429 GOL A C2 1 HETATM 5361 O O2 . GOL EA 9 . ? -5.464 31.794 -19.099 1.00 58.94 ? 429 GOL A O2 1 HETATM 5362 C C3 . GOL EA 9 . ? -7.399 32.057 -20.494 1.00 62.63 ? 429 GOL A C3 1 HETATM 5363 O O3 . GOL EA 9 . ? -8.234 32.142 -19.361 1.00 62.03 ? 429 GOL A O3 1 HETATM 5364 C C1 . GOL FA 9 . ? -16.346 9.492 -23.783 1.00 85.77 ? 430 GOL A C1 1 HETATM 5365 O O1 . GOL FA 9 . ? -17.573 9.605 -24.472 1.00 83.67 ? 430 GOL A O1 1 HETATM 5366 C C2 . GOL FA 9 . ? -16.440 8.351 -22.778 1.00 86.96 ? 430 GOL A C2 1 HETATM 5367 O O2 . GOL FA 9 . ? -17.681 7.697 -22.925 1.00 85.49 ? 430 GOL A O2 1 HETATM 5368 C C3 . GOL FA 9 . ? -15.292 7.371 -23.000 1.00 89.25 ? 430 GOL A C3 1 HETATM 5369 O O3 . GOL FA 9 . ? -14.094 7.922 -22.497 1.00 90.00 ? 430 GOL A O3 1 HETATM 5370 C C1 . GOL GA 9 . ? -18.466 38.872 -30.303 1.00 71.98 ? 431 GOL A C1 1 HETATM 5371 O O1 . GOL GA 9 . ? -17.108 39.106 -30.612 1.00 74.45 ? 431 GOL A O1 1 HETATM 5372 C C2 . GOL GA 9 . ? -18.728 37.377 -30.108 1.00 69.91 ? 431 GOL A C2 1 HETATM 5373 O O2 . GOL GA 9 . ? -19.502 37.158 -28.945 1.00 71.16 ? 431 GOL A O2 1 HETATM 5374 C C3 . GOL GA 9 . ? -19.465 36.804 -31.315 1.00 61.94 ? 431 GOL A C3 1 HETATM 5375 O O3 . GOL GA 9 . ? -18.567 36.620 -32.388 1.00 57.00 ? 431 GOL A O3 1 HETATM 5376 X UNK . UNX HA 2 . ? -27.395 9.043 -60.876 1.00 30.00 ? 401 UNX B UNK 1 HETATM 5377 C C1 . NAG IA 3 . ? -40.989 9.300 -56.049 1.00 13.55 ? 402 NAG B C1 1 HETATM 5378 C C2 . NAG IA 3 . ? -40.777 9.700 -57.512 1.00 15.55 ? 402 NAG B C2 1 HETATM 5379 C C3 . NAG IA 3 . ? -42.033 10.348 -58.083 1.00 21.36 ? 402 NAG B C3 1 HETATM 5380 C C4 . NAG IA 3 . ? -43.255 9.479 -57.831 1.00 22.69 ? 402 NAG B C4 1 HETATM 5381 C C5 . NAG IA 3 . ? -43.338 9.150 -56.345 1.00 23.99 ? 402 NAG B C5 1 HETATM 5382 C C6 . NAG IA 3 . ? -44.503 8.257 -55.984 1.00 27.50 ? 402 NAG B C6 1 HETATM 5383 C C7 . NAG IA 3 . ? -38.442 10.222 -58.094 1.00 22.75 ? 402 NAG B C7 1 HETATM 5384 C C8 . NAG IA 3 . ? -37.410 11.304 -58.195 1.00 21.20 ? 402 NAG B C8 1 HETATM 5385 N N2 . NAG IA 3 . ? -39.646 10.605 -57.656 1.00 16.58 ? 402 NAG B N2 1 HETATM 5386 O O3 . NAG IA 3 . ? -41.827 10.539 -59.479 1.00 22.58 ? 402 NAG B O3 1 HETATM 5387 O O4 . NAG IA 3 . ? -44.415 10.212 -58.210 1.00 26.43 ? 402 NAG B O4 1 HETATM 5388 O O5 . NAG IA 3 . ? -42.141 8.470 -55.939 1.00 20.48 ? 402 NAG B O5 1 HETATM 5389 O O6 . NAG IA 3 . ? -44.427 7.008 -56.656 1.00 42.73 ? 402 NAG B O6 1 HETATM 5390 O O7 . NAG IA 3 . ? -38.188 9.050 -58.368 1.00 19.09 ? 402 NAG B O7 1 HETATM 5391 C C1 . NAG JA 3 . ? -44.974 9.765 -59.458 1.00 20.47 ? 403 NAG B C1 1 HETATM 5392 C C2 . NAG JA 3 . ? -46.346 10.427 -59.555 1.00 22.16 ? 403 NAG B C2 1 HETATM 5393 C C3 . NAG JA 3 . ? -47.036 10.047 -60.868 1.00 24.72 ? 403 NAG B C3 1 HETATM 5394 C C4 . NAG JA 3 . ? -46.110 10.305 -62.055 1.00 25.84 ? 403 NAG B C4 1 HETATM 5395 C C5 . NAG JA 3 . ? -44.758 9.637 -61.797 1.00 26.50 ? 403 NAG B C5 1 HETATM 5396 C C6 . NAG JA 3 . ? -43.738 9.904 -62.877 1.00 21.30 ? 403 NAG B C6 1 HETATM 5397 C C7 . NAG JA 3 . ? -47.426 10.896 -57.396 1.00 35.29 ? 403 NAG B C7 1 HETATM 5398 C C8 . NAG JA 3 . ? -48.281 10.347 -56.295 1.00 38.06 ? 403 NAG B C8 1 HETATM 5399 N N2 . NAG JA 3 . ? -47.172 10.064 -58.414 1.00 25.64 ? 403 NAG B N2 1 HETATM 5400 O O3 . NAG JA 3 . ? -48.217 10.839 -60.938 1.00 36.65 ? 403 NAG B O3 1 HETATM 5401 O O4 . NAG JA 3 . ? -46.592 9.760 -63.283 1.00 34.67 ? 403 NAG B O4 1 HETATM 5402 O O5 . NAG JA 3 . ? -44.203 10.120 -60.569 1.00 23.39 ? 403 NAG B O5 1 HETATM 5403 O O6 . NAG JA 3 . ? -43.564 11.296 -63.100 1.00 31.15 ? 403 NAG B O6 1 HETATM 5404 O O7 . NAG JA 3 . ? -46.993 12.045 -57.372 1.00 39.83 ? 403 NAG B O7 1 HETATM 5405 C C1 . BMA KA 4 . ? -47.952 10.053 -63.665 1.00 55.14 ? 404 BMA B C1 1 HETATM 5406 C C2 . BMA KA 4 . ? -48.203 11.562 -63.817 1.00 70.20 ? 404 BMA B C2 1 HETATM 5407 C C3 . BMA KA 4 . ? -49.532 11.736 -64.494 1.00 83.45 ? 404 BMA B C3 1 HETATM 5408 C C4 . BMA KA 4 . ? -49.412 11.279 -65.945 1.00 96.00 ? 404 BMA B C4 1 HETATM 5409 C C5 . BMA KA 4 . ? -48.695 9.891 -66.050 1.00 55.53 ? 404 BMA B C5 1 HETATM 5410 C C6 . BMA KA 4 . ? -47.444 9.950 -66.841 1.00 39.78 ? 404 BMA B C6 1 HETATM 5411 O O2 . BMA KA 4 . ? -47.200 12.174 -64.620 1.00 75.73 ? 404 BMA B O2 1 HETATM 5412 O O3 . BMA KA 4 . ? -49.990 13.084 -64.409 1.00 80.66 ? 404 BMA B O3 1 HETATM 5413 O O4 . BMA KA 4 . ? -50.699 11.191 -66.563 1.00 103.43 ? 404 BMA B O4 1 HETATM 5414 O O5 . BMA KA 4 . ? -48.410 9.248 -64.758 1.00 61.43 ? 404 BMA B O5 1 HETATM 5415 O O6 . BMA KA 4 . ? -47.717 9.169 -67.977 1.00 27.47 ? 404 BMA B O6 1 HETATM 5416 C C1 . MAN LA 5 . ? -46.734 9.436 -68.965 1.00 33.34 ? 405 MAN B C1 1 HETATM 5417 C C2 . MAN LA 5 . ? -47.231 8.706 -70.186 1.00 35.62 ? 405 MAN B C2 1 HETATM 5418 C C3 . MAN LA 5 . ? -47.152 7.197 -69.923 1.00 38.73 ? 405 MAN B C3 1 HETATM 5419 C C4 . MAN LA 5 . ? -45.744 6.774 -69.447 1.00 32.88 ? 405 MAN B C4 1 HETATM 5420 C C5 . MAN LA 5 . ? -45.331 7.610 -68.220 1.00 32.68 ? 405 MAN B C5 1 HETATM 5421 C C6 . MAN LA 5 . ? -43.906 7.319 -67.745 1.00 32.90 ? 405 MAN B C6 1 HETATM 5422 O O2 . MAN LA 5 . ? -46.386 9.002 -71.266 1.00 41.19 ? 405 MAN B O2 1 HETATM 5423 O O3 . MAN LA 5 . ? -47.515 6.448 -71.063 1.00 38.75 ? 405 MAN B O3 1 HETATM 5424 O O4 . MAN LA 5 . ? -45.759 5.410 -69.076 1.00 36.85 ? 405 MAN B O4 1 HETATM 5425 O O5 . MAN LA 5 . ? -45.430 9.012 -68.553 1.00 26.63 ? 405 MAN B O5 1 HETATM 5426 O O6 . MAN LA 5 . ? -43.562 8.261 -66.712 1.00 32.18 ? 405 MAN B O6 1 HETATM 5427 C C1 . MAN MA 5 . ? -47.173 9.367 -72.409 1.00 47.59 ? 406 MAN B C1 1 HETATM 5428 C C2 . MAN MA 5 . ? -46.224 9.513 -73.568 1.00 47.52 ? 406 MAN B C2 1 HETATM 5429 C C3 . MAN MA 5 . ? -45.253 10.630 -73.238 1.00 42.44 ? 406 MAN B C3 1 HETATM 5430 C C4 . MAN MA 5 . ? -46.010 11.957 -72.925 1.00 83.61 ? 406 MAN B C4 1 HETATM 5431 C C5 . MAN MA 5 . ? -47.203 11.745 -71.924 1.00 54.11 ? 406 MAN B C5 1 HETATM 5432 C C6 . MAN MA 5 . ? -48.195 12.898 -71.915 1.00 61.43 ? 406 MAN B C6 1 HETATM 5433 O O2 . MAN MA 5 . ? -46.928 9.919 -74.734 1.00 51.49 ? 406 MAN B O2 1 HETATM 5434 O O3 . MAN MA 5 . ? -44.340 10.807 -74.309 1.00 41.83 ? 406 MAN B O3 1 HETATM 5435 O O4 . MAN MA 5 . ? -45.097 13.061 -72.530 1.00 88.54 ? 406 MAN B O4 1 HETATM 5436 O O5 . MAN MA 5 . ? -47.942 10.536 -72.221 1.00 50.74 ? 406 MAN B O5 1 HETATM 5437 O O6 . MAN MA 5 . ? -47.609 13.988 -71.216 1.00 66.58 ? 406 MAN B O6 1 HETATM 5438 C C1 . MAN NA 5 . ? -44.485 13.126 -71.198 1.00 98.47 ? 407 MAN B C1 1 HETATM 5439 C C2 . MAN NA 5 . ? -43.053 12.540 -71.181 1.00 100.05 ? 407 MAN B C2 1 HETATM 5440 C C3 . MAN NA 5 . ? -42.809 11.796 -69.853 1.00 99.11 ? 407 MAN B C3 1 HETATM 5441 C C4 . MAN NA 5 . ? -43.224 12.651 -68.639 1.00 101.24 ? 407 MAN B C4 1 HETATM 5442 C C5 . MAN NA 5 . ? -44.697 13.123 -68.773 1.00 106.16 ? 407 MAN B C5 1 HETATM 5443 C C6 . MAN NA 5 . ? -44.866 14.632 -68.633 1.00 105.09 ? 407 MAN B C6 1 HETATM 5444 O O2 . MAN NA 5 . ? -42.102 13.590 -71.240 1.00 101.33 ? 407 MAN B O2 1 HETATM 5445 O O3 . MAN NA 5 . ? -41.449 11.377 -69.712 1.00 96.29 ? 407 MAN B O3 1 HETATM 5446 O O4 . MAN NA 5 . ? -43.068 11.902 -67.435 1.00 99.40 ? 407 MAN B O4 1 HETATM 5447 O O5 . MAN NA 5 . ? -45.242 12.704 -70.054 1.00 104.48 ? 407 MAN B O5 1 HETATM 5448 O O6 . MAN NA 5 . ? -44.230 15.046 -67.428 1.00 105.05 ? 407 MAN B O6 1 HETATM 5449 C C1 . NAG OA 3 . ? -22.799 17.768 -55.423 1.00 22.17 ? 408 NAG B C1 1 HETATM 5450 C C2 . NAG OA 3 . ? -23.541 19.116 -55.435 1.00 16.58 ? 408 NAG B C2 1 HETATM 5451 C C3 . NAG OA 3 . ? -24.843 19.029 -54.639 1.00 19.78 ? 408 NAG B C3 1 HETATM 5452 C C4 . NAG OA 3 . ? -25.661 17.810 -55.047 1.00 18.38 ? 408 NAG B C4 1 HETATM 5453 C C5 . NAG OA 3 . ? -24.783 16.567 -54.976 1.00 17.73 ? 408 NAG B C5 1 HETATM 5454 C C6 . NAG OA 3 . ? -25.481 15.296 -55.397 1.00 17.69 ? 408 NAG B C6 1 HETATM 5455 C C7 . NAG OA 3 . ? -22.277 21.221 -55.590 1.00 38.68 ? 408 NAG B C7 1 HETATM 5456 C C8 . NAG OA 3 . ? -22.740 21.294 -57.010 1.00 29.75 ? 408 NAG B C8 1 HETATM 5457 N N2 . NAG OA 3 . ? -22.689 20.160 -54.889 1.00 21.63 ? 408 NAG B N2 1 HETATM 5458 O O3 . NAG OA 3 . ? -25.601 20.216 -54.858 1.00 23.28 ? 408 NAG B O3 1 HETATM 5459 O O4 . NAG OA 3 . ? -26.735 17.665 -54.126 1.00 18.60 ? 408 NAG B O4 1 HETATM 5460 O O5 . NAG OA 3 . ? -23.665 16.740 -55.855 1.00 16.93 ? 408 NAG B O5 1 HETATM 5461 O O6 . NAG OA 3 . ? -25.876 15.354 -56.759 1.00 17.23 ? 408 NAG B O6 1 HETATM 5462 O O7 . NAG OA 3 . ? -21.559 22.085 -55.094 1.00 53.12 ? 408 NAG B O7 1 HETATM 5463 C C1 . NAG PA 3 . ? -27.995 17.524 -54.781 1.00 17.37 ? 409 NAG B C1 1 HETATM 5464 C C2 . NAG PA 3 . ? -28.981 17.254 -53.655 1.00 15.82 ? 409 NAG B C2 1 HETATM 5465 C C3 . NAG PA 3 . ? -30.409 17.213 -54.185 1.00 17.00 ? 409 NAG B C3 1 HETATM 5466 C C4 . NAG PA 3 . ? -30.708 18.453 -55.019 1.00 22.67 ? 409 NAG B C4 1 HETATM 5467 C C5 . NAG PA 3 . ? -29.639 18.641 -56.088 1.00 18.95 ? 409 NAG B C5 1 HETATM 5468 C C6 . NAG PA 3 . ? -29.808 19.904 -56.902 1.00 30.71 ? 409 NAG B C6 1 HETATM 5469 C C7 . NAG PA 3 . ? -28.663 14.801 -53.440 1.00 18.08 ? 409 NAG B C7 1 HETATM 5470 C C8 . NAG PA 3 . ? -28.317 13.692 -52.488 1.00 17.80 ? 409 NAG B C8 1 HETATM 5471 N N2 . NAG PA 3 . ? -28.661 16.038 -52.922 1.00 15.76 ? 409 NAG B N2 1 HETATM 5472 O O3 . NAG PA 3 . ? -31.296 17.152 -53.072 1.00 14.98 ? 409 NAG B O3 1 HETATM 5473 O O4 . NAG PA 3 . ? -31.968 18.284 -55.651 1.00 27.50 ? 409 NAG B O4 1 HETATM 5474 O O5 . NAG PA 3 . ? -28.355 18.726 -55.457 1.00 20.64 ? 409 NAG B O5 1 HETATM 5475 O O6 . NAG PA 3 . ? -29.550 21.064 -56.122 1.00 32.85 ? 409 NAG B O6 1 HETATM 5476 O O7 . NAG PA 3 . ? -28.926 14.584 -54.620 1.00 17.44 ? 409 NAG B O7 1 HETATM 5477 C C1 . BMA QA 4 . ? -32.859 19.323 -55.236 1.00 28.99 ? 410 BMA B C1 1 HETATM 5478 C C2 . BMA QA 4 . ? -34.102 19.211 -56.106 1.00 28.94 ? 410 BMA B C2 1 HETATM 5479 C C3 . BMA QA 4 . ? -35.161 20.214 -55.643 1.00 34.73 ? 410 BMA B C3 1 HETATM 5480 C C4 . BMA QA 4 . ? -35.372 20.140 -54.116 1.00 34.66 ? 410 BMA B C4 1 HETATM 5481 C C5 . BMA QA 4 . ? -34.025 20.272 -53.383 1.00 33.12 ? 410 BMA B C5 1 HETATM 5482 C C6 . BMA QA 4 . ? -34.152 20.095 -51.895 1.00 24.91 ? 410 BMA B C6 1 HETATM 5483 O O2 . BMA QA 4 . ? -34.671 17.895 -55.976 1.00 28.70 ? 410 BMA B O2 1 HETATM 5484 O O3 . BMA QA 4 . ? -36.398 20.012 -56.332 1.00 43.38 ? 410 BMA B O3 1 HETATM 5485 O O4 . BMA QA 4 . ? -36.223 21.186 -53.698 1.00 40.85 ? 410 BMA B O4 1 HETATM 5486 O O5 . BMA QA 4 . ? -33.153 19.235 -53.858 1.00 33.17 ? 410 BMA B O5 1 HETATM 5487 O O6 . BMA QA 4 . ? -34.856 18.868 -51.686 1.00 23.37 ? 410 BMA B O6 1 HETATM 5488 C C1 . MAN RA 5 . ? -34.621 18.357 -50.359 1.00 28.42 ? 411 MAN B C1 1 HETATM 5489 C C2 . MAN RA 5 . ? -35.361 17.037 -50.216 1.00 23.23 ? 411 MAN B C2 1 HETATM 5490 C C3 . MAN RA 5 . ? -36.881 17.301 -50.209 1.00 21.39 ? 411 MAN B C3 1 HETATM 5491 C C4 . MAN RA 5 . ? -37.284 18.408 -49.224 1.00 26.53 ? 411 MAN B C4 1 HETATM 5492 C C5 . MAN RA 5 . ? -36.417 19.656 -49.381 1.00 34.66 ? 411 MAN B C5 1 HETATM 5493 C C6 . MAN RA 5 . ? -36.657 20.668 -48.264 1.00 32.48 ? 411 MAN B C6 1 HETATM 5494 O O2 . MAN RA 5 . ? -35.022 16.455 -48.957 1.00 20.61 ? 411 MAN B O2 1 HETATM 5495 O O3 . MAN RA 5 . ? -37.595 16.169 -49.819 1.00 22.85 ? 411 MAN B O3 1 HETATM 5496 O O4 . MAN RA 5 . ? -38.658 18.741 -49.406 1.00 26.95 ? 411 MAN B O4 1 HETATM 5497 O O5 . MAN RA 5 . ? -35.008 19.252 -49.326 1.00 27.60 ? 411 MAN B O5 1 HETATM 5498 O O6 . MAN RA 5 . ? -36.357 19.972 -47.062 1.00 34.30 ? 411 MAN B O6 1 HETATM 5499 C C1 . MAN SA 5 . ? -37.960 15.368 -50.949 1.00 24.73 ? 412 MAN B C1 1 HETATM 5500 C C2 . MAN SA 5 . ? -39.269 14.726 -50.545 1.00 27.52 ? 412 MAN B C2 1 HETATM 5501 C C3 . MAN SA 5 . ? -39.004 13.783 -49.369 1.00 23.84 ? 412 MAN B C3 1 HETATM 5502 C C4 . MAN SA 5 . ? -37.917 12.755 -49.715 1.00 23.75 ? 412 MAN B C4 1 HETATM 5503 C C5 . MAN SA 5 . ? -36.640 13.448 -50.209 1.00 22.93 ? 412 MAN B C5 1 HETATM 5504 C C6 . MAN SA 5 . ? -35.622 12.435 -50.715 1.00 26.09 ? 412 MAN B C6 1 HETATM 5505 O O2 . MAN SA 5 . ? -39.779 13.926 -51.614 1.00 35.59 ? 412 MAN B O2 1 HETATM 5506 O O3 . MAN SA 5 . ? -40.177 13.102 -48.994 1.00 23.30 ? 412 MAN B O3 1 HETATM 5507 O O4 . MAN SA 5 . ? -37.614 11.962 -48.558 1.00 25.87 ? 412 MAN B O4 1 HETATM 5508 O O5 . MAN SA 5 . ? -36.967 14.390 -51.294 1.00 28.78 ? 412 MAN B O5 1 HETATM 5509 O O6 . MAN SA 5 . ? -34.362 13.095 -50.867 1.00 30.28 ? 412 MAN B O6 1 HETATM 5510 C C1 . MAN TA 5 . ? -40.799 14.660 -52.312 1.00 50.44 ? 413 MAN B C1 1 HETATM 5511 C C2 . MAN TA 5 . ? -41.729 13.645 -52.993 1.00 62.70 ? 413 MAN B C2 1 HETATM 5512 C C3 . MAN TA 5 . ? -41.054 13.050 -54.243 1.00 63.60 ? 413 MAN B C3 1 HETATM 5513 C C4 . MAN TA 5 . ? -40.356 14.121 -55.113 1.00 58.64 ? 413 MAN B C4 1 HETATM 5514 C C5 . MAN TA 5 . ? -39.434 14.984 -54.237 1.00 58.72 ? 413 MAN B C5 1 HETATM 5515 C C6 . MAN TA 5 . ? -38.720 16.082 -55.008 1.00 59.86 ? 413 MAN B C6 1 HETATM 5516 O O2 . MAN TA 5 . ? -42.942 14.256 -53.415 1.00 70.02 ? 413 MAN B O2 1 HETATM 5517 O O3 . MAN TA 5 . ? -41.990 12.327 -55.023 1.00 71.79 ? 413 MAN B O3 1 HETATM 5518 O O4 . MAN TA 5 . ? -39.595 13.503 -56.143 1.00 52.54 ? 413 MAN B O4 1 HETATM 5519 O O5 . MAN TA 5 . ? -40.250 15.592 -53.220 1.00 54.44 ? 413 MAN B O5 1 HETATM 5520 O O6 . MAN TA 5 . ? -37.774 16.704 -54.143 1.00 62.10 ? 413 MAN B O6 1 HETATM 5521 C C1 . MAN UA 5 . ? -36.614 20.752 -45.886 1.00 35.92 ? 414 MAN B C1 1 HETATM 5522 C C2 . MAN UA 5 . ? -36.044 20.002 -44.673 1.00 38.18 ? 414 MAN B C2 1 HETATM 5523 C C3 . MAN UA 5 . ? -36.818 18.726 -44.489 1.00 33.65 ? 414 MAN B C3 1 HETATM 5524 C C4 . MAN UA 5 . ? -38.301 19.061 -44.290 1.00 31.92 ? 414 MAN B C4 1 HETATM 5525 C C5 . MAN UA 5 . ? -38.814 19.851 -45.501 1.00 30.57 ? 414 MAN B C5 1 HETATM 5526 C C6 . MAN UA 5 . ? -40.244 20.334 -45.335 1.00 46.87 ? 414 MAN B C6 1 HETATM 5527 O O2 . MAN UA 5 . ? -36.292 20.739 -43.478 1.00 45.31 ? 414 MAN B O2 1 HETATM 5528 O O3 . MAN UA 5 . ? -36.322 17.974 -43.382 1.00 34.50 ? 414 MAN B O3 1 HETATM 5529 O O4 . MAN UA 5 . ? -39.055 17.874 -44.157 1.00 38.83 ? 414 MAN B O4 1 HETATM 5530 O O5 . MAN UA 5 . ? -37.981 21.022 -45.714 1.00 28.62 ? 414 MAN B O5 1 HETATM 5531 O O6 . MAN UA 5 . ? -40.453 21.389 -46.277 1.00 50.34 ? 414 MAN B O6 1 HETATM 5532 C C1 . MAN VA 5 . ? -35.095 21.425 -43.072 1.00 47.00 ? 415 MAN B C1 1 HETATM 5533 C C2 . MAN VA 5 . ? -35.242 21.856 -41.599 1.00 47.86 ? 415 MAN B C2 1 HETATM 5534 C C3 . MAN VA 5 . ? -36.183 23.061 -41.501 1.00 47.32 ? 415 MAN B C3 1 HETATM 5535 C C4 . MAN VA 5 . ? -35.770 24.167 -42.475 1.00 44.34 ? 415 MAN B C4 1 HETATM 5536 C C5 . MAN VA 5 . ? -35.722 23.600 -43.913 1.00 44.95 ? 415 MAN B C5 1 HETATM 5537 C C6 . MAN VA 5 . ? -35.297 24.612 -44.964 1.00 48.39 ? 415 MAN B C6 1 HETATM 5538 O O2 . MAN VA 5 . ? -33.994 22.273 -41.084 1.00 45.53 ? 415 MAN B O2 1 HETATM 5539 O O3 . MAN VA 5 . ? -36.237 23.577 -40.180 1.00 55.25 ? 415 MAN B O3 1 HETATM 5540 O O4 . MAN VA 5 . ? -36.694 25.235 -42.402 1.00 45.13 ? 415 MAN B O4 1 HETATM 5541 O O5 . MAN VA 5 . ? -34.770 22.510 -43.938 1.00 43.36 ? 415 MAN B O5 1 HETATM 5542 O O6 . MAN VA 5 . ? -34.679 23.901 -46.042 1.00 56.24 ? 415 MAN B O6 1 HETATM 5543 C C1 . NAG WA 3 . ? -21.043 11.175 -91.633 1.00 40.33 ? 416 NAG B C1 1 HETATM 5544 C C2 . NAG WA 3 . ? -20.543 11.922 -92.863 1.00 61.32 ? 416 NAG B C2 1 HETATM 5545 C C3 . NAG WA 3 . ? -20.014 13.293 -92.458 1.00 65.99 ? 416 NAG B C3 1 HETATM 5546 C C4 . NAG WA 3 . ? -21.094 14.071 -91.718 1.00 62.95 ? 416 NAG B C4 1 HETATM 5547 C C5 . NAG WA 3 . ? -21.631 13.262 -90.538 1.00 56.89 ? 416 NAG B C5 1 HETATM 5548 C C6 . NAG WA 3 . ? -22.838 13.908 -89.900 1.00 58.32 ? 416 NAG B C6 1 HETATM 5549 C C7 . NAG WA 3 . ? -19.744 10.509 -94.706 1.00 65.44 ? 416 NAG B C7 1 HETATM 5550 C C8 . NAG WA 3 . ? -21.137 10.601 -95.255 1.00 65.26 ? 416 NAG B C8 1 HETATM 5551 N N2 . NAG WA 3 . ? -19.519 11.161 -93.561 1.00 65.51 ? 416 NAG B N2 1 HETATM 5552 O O3 . NAG WA 3 . ? -19.607 14.004 -93.621 1.00 72.07 ? 416 NAG B O3 1 HETATM 5553 O O4 . NAG WA 3 . ? -20.571 15.305 -91.237 1.00 66.38 ? 416 NAG B O4 1 HETATM 5554 O O5 . NAG WA 3 . ? -22.052 11.957 -90.971 1.00 54.07 ? 416 NAG B O5 1 HETATM 5555 O O6 . NAG WA 3 . ? -22.728 13.955 -88.484 1.00 62.09 ? 416 NAG B O6 1 HETATM 5556 O O7 . NAG WA 3 . ? -18.863 9.870 -95.273 1.00 68.65 ? 416 NAG B O7 1 HETATM 5557 C C1 . NAG XA 3 . ? -20.156 2.500 -95.522 1.00 41.36 ? 417 NAG B C1 1 HETATM 5558 C C2 . NAG XA 3 . ? -20.887 3.428 -96.483 1.00 51.15 ? 417 NAG B C2 1 HETATM 5559 C C3 . NAG XA 3 . ? -20.575 3.045 -97.931 1.00 58.26 ? 417 NAG B C3 1 HETATM 5560 C C4 . NAG XA 3 . ? -19.070 2.953 -98.158 1.00 59.21 ? 417 NAG B C4 1 HETATM 5561 C C5 . NAG XA 3 . ? -18.448 2.035 -97.107 1.00 59.21 ? 417 NAG B C5 1 HETATM 5562 C C6 . NAG XA 3 . ? -16.941 1.951 -97.180 1.00 62.34 ? 417 NAG B C6 1 HETATM 5563 C C7 . NAG XA 3 . ? -22.984 4.340 -95.586 1.00 60.71 ? 417 NAG B C7 1 HETATM 5564 C C8 . NAG XA 3 . ? -22.166 5.505 -95.110 1.00 65.47 ? 417 NAG B C8 1 HETATM 5565 N N2 . NAG XA 3 . ? -22.319 3.382 -96.240 1.00 51.23 ? 417 NAG B N2 1 HETATM 5566 O O3 . NAG XA 3 . ? -21.143 4.008 -98.811 1.00 62.06 ? 417 NAG B O3 1 HETATM 5567 O O4 . NAG XA 3 . ? -18.825 2.429 -99.460 1.00 68.77 ? 417 NAG B O4 1 HETATM 5568 O O5 . NAG XA 3 . ? -18.767 2.524 -95.798 1.00 51.74 ? 417 NAG B O5 1 HETATM 5569 O O6 . NAG XA 3 . ? -16.473 0.705 -96.679 1.00 64.08 ? 417 NAG B O6 1 HETATM 5570 O O7 . NAG XA 3 . ? -24.192 4.272 -95.390 1.00 63.03 ? 417 NAG B O7 1 HETATM 5571 C C1 . NAG YA 3 . ? -17.928 3.271 -100.224 1.00 76.83 ? 418 NAG B C1 1 HETATM 5572 C C2 . NAG YA 3 . ? -17.365 2.473 -101.399 1.00 77.63 ? 418 NAG B C2 1 HETATM 5573 C C3 . NAG YA 3 . ? -16.353 3.316 -102.169 1.00 86.16 ? 418 NAG B C3 1 HETATM 5574 C C4 . NAG YA 3 . ? -16.969 4.648 -102.575 1.00 86.99 ? 418 NAG B C4 1 HETATM 5575 C C5 . NAG YA 3 . ? -17.566 5.352 -101.357 1.00 86.53 ? 418 NAG B C5 1 HETATM 5576 C C6 . NAG YA 3 . ? -18.307 6.622 -101.710 1.00 86.43 ? 418 NAG B C6 1 HETATM 5577 C C7 . NAG YA 3 . ? -17.318 0.036 -101.105 1.00 79.41 ? 418 NAG B C7 1 HETATM 5578 C C8 . NAG YA 3 . ? -16.549 -1.132 -100.562 1.00 78.73 ? 418 NAG B C8 1 HETATM 5579 N N2 . NAG YA 3 . ? -16.753 1.236 -100.940 1.00 77.29 ? 418 NAG B N2 1 HETATM 5580 O O3 . NAG YA 3 . ? -15.922 2.608 -103.327 1.00 92.34 ? 418 NAG B O3 1 HETATM 5581 O O4 . NAG YA 3 . ? -15.971 5.474 -103.167 1.00 85.01 ? 418 NAG B O4 1 HETATM 5582 O O5 . NAG YA 3 . ? -18.511 4.488 -100.705 1.00 82.36 ? 418 NAG B O5 1 HETATM 5583 O O6 . NAG YA 3 . ? -17.636 7.774 -101.217 1.00 86.23 ? 418 NAG B O6 1 HETATM 5584 O O7 . NAG YA 3 . ? -18.400 -0.101 -101.666 1.00 82.53 ? 418 NAG B O7 1 HETATM 5585 C C1 . NAG ZA 3 . ? -45.541 -15.148 -66.580 1.00 39.74 ? 419 NAG B C1 1 HETATM 5586 C C2 . NAG ZA 3 . ? -46.902 -14.492 -66.838 1.00 50.35 ? 419 NAG B C2 1 HETATM 5587 C C3 . NAG ZA 3 . ? -47.856 -14.763 -65.673 1.00 59.01 ? 419 NAG B C3 1 HETATM 5588 C C4 . NAG ZA 3 . ? -47.941 -16.257 -65.393 1.00 62.94 ? 419 NAG B C4 1 HETATM 5589 C C5 . NAG ZA 3 . ? -46.540 -16.799 -65.142 1.00 62.76 ? 419 NAG B C5 1 HETATM 5590 C C6 . NAG ZA 3 . ? -46.513 -18.293 -64.922 1.00 71.53 ? 419 NAG B C6 1 HETATM 5591 C C7 . NAG ZA 3 . ? -47.015 -12.468 -68.230 1.00 50.78 ? 419 NAG B C7 1 HETATM 5592 C C8 . NAG ZA 3 . ? -47.435 -13.371 -69.350 1.00 48.79 ? 419 NAG B C8 1 HETATM 5593 N N2 . NAG ZA 3 . ? -46.764 -13.061 -67.056 1.00 49.86 ? 419 NAG B N2 1 HETATM 5594 O O3 . NAG ZA 3 . ? -49.149 -14.251 -65.979 1.00 56.12 ? 419 NAG B O3 1 HETATM 5595 O O4 . NAG ZA 3 . ? -48.767 -16.502 -64.259 1.00 63.64 ? 419 NAG B O4 1 HETATM 5596 O O5 . NAG ZA 3 . ? -45.722 -16.536 -66.291 1.00 54.31 ? 419 NAG B O5 1 HETATM 5597 O O6 . NAG ZA 3 . ? -45.243 -18.726 -64.452 1.00 77.06 ? 419 NAG B O6 1 HETATM 5598 O O7 . NAG ZA 3 . ? -46.903 -11.255 -68.381 1.00 54.18 ? 419 NAG B O7 1 HETATM 5599 MG MG . MG AB 6 . ? -18.743 -5.710 -53.626 1.00 23.62 ? 420 MG B MG 1 HETATM 5600 CL CL . CL BB 10 . ? -44.618 3.479 -70.771 0.91 21.54 ? 421 CL B CL 1 HETATM 5601 C C1 . PEG CB 7 . ? -20.223 -17.768 -67.913 1.00 44.68 ? 422 PEG B C1 1 HETATM 5602 O O1 . PEG CB 7 . ? -20.640 -18.499 -69.063 1.00 42.48 ? 422 PEG B O1 1 HETATM 5603 C C2 . PEG CB 7 . ? -20.308 -16.240 -68.161 1.00 50.12 ? 422 PEG B C2 1 HETATM 5604 O O2 . PEG CB 7 . ? -19.992 -15.538 -66.944 1.00 53.71 ? 422 PEG B O2 1 HETATM 5605 C C3 . PEG CB 7 . ? -18.614 -15.125 -66.815 1.00 55.62 ? 422 PEG B C3 1 HETATM 5606 C C4 . PEG CB 7 . ? -18.384 -14.538 -65.425 1.00 63.52 ? 422 PEG B C4 1 HETATM 5607 O O4 . PEG CB 7 . ? -19.213 -13.407 -65.227 1.00 67.83 ? 422 PEG B O4 1 HETATM 5608 C C1 . PEG DB 7 . ? -8.428 15.402 -87.306 1.00 44.06 ? 423 PEG B C1 1 HETATM 5609 O O1 . PEG DB 7 . ? -8.616 15.562 -88.711 1.00 47.58 ? 423 PEG B O1 1 HETATM 5610 C C2 . PEG DB 7 . ? -9.261 16.466 -86.542 1.00 58.89 ? 423 PEG B C2 1 HETATM 5611 O O2 . PEG DB 7 . ? -8.423 17.539 -86.074 1.00 59.49 ? 423 PEG B O2 1 HETATM 5612 C C3 . PEG DB 7 . ? -7.102 17.127 -85.656 1.00 60.90 ? 423 PEG B C3 1 HETATM 5613 C C4 . PEG DB 7 . ? -6.427 18.255 -84.887 1.00 62.48 ? 423 PEG B C4 1 HETATM 5614 O O4 . PEG DB 7 . ? -5.184 17.793 -84.402 1.00 66.87 ? 423 PEG B O4 1 HETATM 5615 C C1 . GOL EB 9 . ? -32.203 4.041 -81.243 1.00 58.11 ? 424 GOL B C1 1 HETATM 5616 O O1 . GOL EB 9 . ? -30.925 4.590 -81.003 1.00 60.60 ? 424 GOL B O1 1 HETATM 5617 C C2 . GOL EB 9 . ? -32.249 3.385 -82.619 1.00 58.32 ? 424 GOL B C2 1 HETATM 5618 O O2 . GOL EB 9 . ? -32.339 1.984 -82.488 1.00 59.08 ? 424 GOL B O2 1 HETATM 5619 C C3 . GOL EB 9 . ? -33.441 3.903 -83.418 1.00 59.95 ? 424 GOL B C3 1 HETATM 5620 O O3 . GOL EB 9 . ? -33.990 2.864 -84.201 1.00 59.49 ? 424 GOL B O3 1 HETATM 5621 C C1 . GOL FB 9 . ? -31.294 9.990 -78.504 1.00 78.76 ? 425 GOL B C1 1 HETATM 5622 O O1 . GOL FB 9 . ? -31.762 10.253 -79.809 1.00 79.25 ? 425 GOL B O1 1 HETATM 5623 C C2 . GOL FB 9 . ? -29.983 9.210 -78.558 1.00 79.32 ? 425 GOL B C2 1 HETATM 5624 O O2 . GOL FB 9 . ? -29.113 9.704 -77.563 1.00 85.70 ? 425 GOL B O2 1 HETATM 5625 C C3 . GOL FB 9 . ? -30.254 7.727 -78.315 1.00 71.89 ? 425 GOL B C3 1 HETATM 5626 O O3 . GOL FB 9 . ? -29.044 7.025 -78.134 1.00 61.93 ? 425 GOL B O3 1 HETATM 5627 C C1 . GOL GB 9 . ? -42.155 -0.337 -47.014 1.00 81.85 ? 426 GOL B C1 1 HETATM 5628 O O1 . GOL GB 9 . ? -41.111 -0.211 -46.073 1.00 84.93 ? 426 GOL B O1 1 HETATM 5629 C C2 . GOL GB 9 . ? -41.743 -1.285 -48.138 1.00 78.21 ? 426 GOL B C2 1 HETATM 5630 O O2 . GOL GB 9 . ? -40.751 -2.183 -47.684 1.00 75.62 ? 426 GOL B O2 1 HETATM 5631 C C3 . GOL GB 9 . ? -42.966 -2.062 -48.614 1.00 76.26 ? 426 GOL B C3 1 HETATM 5632 O O3 . GOL GB 9 . ? -42.583 -3.004 -49.591 1.00 75.32 ? 426 GOL B O3 1 HETATM 5633 O O . HOH HB 11 . ? -32.865 9.921 -9.109 1.00 22.52 ? 501 HOH A O 1 HETATM 5634 O O . HOH HB 11 . ? -39.839 18.837 -15.351 1.00 60.72 ? 502 HOH A O 1 HETATM 5635 O O . HOH HB 11 . ? -3.104 24.625 -21.847 1.00 43.26 ? 503 HOH A O 1 HETATM 5636 O O . HOH HB 11 . ? -20.413 25.162 -9.738 1.00 44.43 ? 504 HOH A O 1 HETATM 5637 O O . HOH HB 11 . ? -17.287 -2.771 -50.769 1.00 28.40 ? 505 HOH A O 1 HETATM 5638 O O . HOH HB 11 . ? -12.834 -4.302 -59.667 1.00 35.31 ? 506 HOH A O 1 HETATM 5639 O O . HOH HB 11 . ? -17.152 -8.871 -31.599 1.00 41.02 ? 507 HOH A O 1 HETATM 5640 O O . HOH HB 11 . ? -21.658 -13.867 -43.133 1.00 42.02 ? 508 HOH A O 1 HETATM 5641 O O . HOH HB 11 . ? -41.635 0.670 -39.134 1.00 30.90 ? 509 HOH A O 1 HETATM 5642 O O . HOH HB 11 . ? -24.246 17.524 -22.125 1.00 18.71 ? 510 HOH A O 1 HETATM 5643 O O . HOH HB 11 . ? -32.563 -10.336 -25.977 1.00 46.18 ? 511 HOH A O 1 HETATM 5644 O O . HOH HB 11 . ? -28.820 -10.243 -40.496 1.00 27.55 ? 512 HOH A O 1 HETATM 5645 O O . HOH HB 11 . ? -30.352 12.508 -30.434 1.00 11.98 ? 513 HOH A O 1 HETATM 5646 O O . HOH HB 11 . ? -19.584 22.548 -50.941 1.00 50.96 ? 514 HOH A O 1 HETATM 5647 O O . HOH HB 11 . ? -4.659 11.832 -41.584 1.00 38.18 ? 515 HOH A O 1 HETATM 5648 O O . HOH HB 11 . ? -16.922 -9.164 -52.599 1.00 40.36 ? 516 HOH A O 1 HETATM 5649 O O . HOH HB 11 . ? -44.129 9.744 -27.154 1.00 43.58 ? 517 HOH A O 1 HETATM 5650 O O . HOH HB 11 . ? -23.236 0.922 -27.585 1.00 12.54 ? 518 HOH A O 1 HETATM 5651 O O . HOH HB 11 . ? -19.831 -0.339 -34.680 1.00 30.92 ? 519 HOH A O 1 HETATM 5652 O O . HOH HB 11 . ? -29.566 10.191 -34.309 1.00 16.37 ? 520 HOH A O 1 HETATM 5653 O O . HOH HB 11 . ? 0.579 20.136 -39.226 1.00 32.73 ? 521 HOH A O 1 HETATM 5654 O O . HOH HB 11 . ? -18.596 16.458 -12.250 1.00 25.00 ? 522 HOH A O 1 HETATM 5655 O O . HOH HB 11 . ? -12.314 15.293 -16.657 1.00 31.67 ? 523 HOH A O 1 HETATM 5656 O O . HOH HB 11 . ? -19.821 -5.626 -51.853 1.00 16.43 ? 524 HOH A O 1 HETATM 5657 O O . HOH HB 11 . ? -18.624 12.006 -51.618 1.00 23.30 ? 525 HOH A O 1 HETATM 5658 O O . HOH HB 11 . ? -41.182 9.369 -34.457 1.00 24.41 ? 526 HOH A O 1 HETATM 5659 O O . HOH HB 11 . ? -38.964 21.276 -17.748 1.00 32.99 ? 527 HOH A O 1 HETATM 5660 O O . HOH HB 11 . ? -19.108 10.743 -37.352 1.00 11.18 ? 528 HOH A O 1 HETATM 5661 O O . HOH HB 11 . ? -37.546 23.599 -17.365 1.00 29.34 ? 529 HOH A O 1 HETATM 5662 O O . HOH HB 11 . ? -12.646 4.728 -35.537 1.00 53.70 ? 530 HOH A O 1 HETATM 5663 O O . HOH HB 11 . ? -21.203 4.031 -12.329 1.00 41.00 ? 531 HOH A O 1 HETATM 5664 O O . HOH HB 11 . ? -8.702 23.119 -42.947 1.00 21.72 ? 532 HOH A O 1 HETATM 5665 O O . HOH HB 11 . ? -31.019 16.444 -32.000 1.00 14.19 ? 533 HOH A O 1 HETATM 5666 O O . HOH HB 11 . ? -10.956 9.403 -45.078 1.00 19.70 ? 534 HOH A O 1 HETATM 5667 O O . HOH HB 11 . ? -18.496 -19.796 -38.822 1.00 44.13 ? 535 HOH A O 1 HETATM 5668 O O . HOH HB 11 . ? -17.631 -6.015 -55.352 1.00 24.01 ? 536 HOH A O 1 HETATM 5669 O O . HOH HB 11 . ? -22.781 2.600 -21.444 1.00 12.47 ? 537 HOH A O 1 HETATM 5670 O O A HOH HB 11 . ? -16.614 8.976 -26.861 0.36 15.55 ? 538 HOH A O 1 HETATM 5671 O O B HOH HB 11 . ? -18.294 9.822 -27.378 0.64 32.70 ? 538 HOH A O 1 HETATM 5672 O O . HOH HB 11 . ? -11.005 31.488 -31.324 1.00 36.76 ? 539 HOH A O 1 HETATM 5673 O O . HOH HB 11 . ? -24.371 5.287 -15.076 1.00 18.64 ? 540 HOH A O 1 HETATM 5674 O O . HOH HB 11 . ? -22.344 9.709 -20.414 1.00 18.59 ? 541 HOH A O 1 HETATM 5675 O O . HOH HB 11 . ? -19.040 11.570 -28.810 1.00 23.17 ? 542 HOH A O 1 HETATM 5676 O O . HOH HB 11 . ? -15.784 16.078 -21.811 1.00 17.54 ? 543 HOH A O 1 HETATM 5677 O O . HOH HB 11 . ? 2.348 21.378 -38.129 1.00 55.27 ? 544 HOH A O 1 HETATM 5678 O O . HOH HB 11 . ? -33.697 3.885 -13.394 1.00 17.89 ? 545 HOH A O 1 HETATM 5679 O O . HOH HB 11 . ? -31.305 -13.796 -28.599 1.00 33.93 ? 546 HOH A O 1 HETATM 5680 O O . HOH HB 11 . ? -14.796 31.485 -19.679 1.00 41.57 ? 547 HOH A O 1 HETATM 5681 O O . HOH HB 11 . ? -32.624 15.462 -41.509 1.00 21.07 ? 548 HOH A O 1 HETATM 5682 O O . HOH HB 11 . ? -31.234 27.528 -16.244 1.00 25.83 ? 549 HOH A O 1 HETATM 5683 O O . HOH HB 11 . ? -25.557 -12.196 -40.262 1.00 33.61 ? 550 HOH A O 1 HETATM 5684 O O . HOH HB 11 . ? -12.021 23.005 -23.837 1.00 16.75 ? 551 HOH A O 1 HETATM 5685 O O . HOH HB 11 . ? -25.051 -8.560 -15.369 1.00 22.69 ? 552 HOH A O 1 HETATM 5686 O O . HOH HB 11 . ? 1.135 26.508 -37.136 1.00 36.47 ? 553 HOH A O 1 HETATM 5687 O O . HOH HB 11 . ? -34.187 13.088 -44.177 1.00 16.77 ? 554 HOH A O 1 HETATM 5688 O O . HOH HB 11 . ? -11.736 15.384 -34.036 1.00 23.75 ? 555 HOH A O 1 HETATM 5689 O O . HOH HB 11 . ? -23.450 1.540 -35.881 1.00 18.41 ? 556 HOH A O 1 HETATM 5690 O O . HOH HB 11 . ? -41.977 11.976 -17.641 1.00 38.33 ? 557 HOH A O 1 HETATM 5691 O O . HOH HB 11 . ? -13.298 11.634 -23.116 1.00 42.49 ? 558 HOH A O 1 HETATM 5692 O O . HOH HB 11 . ? -41.801 10.870 -27.400 1.00 29.26 ? 559 HOH A O 1 HETATM 5693 O O . HOH HB 11 . ? -18.531 7.088 -20.437 1.00 58.92 ? 560 HOH A O 1 HETATM 5694 O O . HOH HB 11 . ? -23.529 -5.363 -14.012 1.00 20.41 ? 561 HOH A O 1 HETATM 5695 O O . HOH HB 11 . ? -22.339 -14.764 -37.423 1.00 30.30 ? 562 HOH A O 1 HETATM 5696 O O . HOH HB 11 . ? -37.935 3.383 -14.490 1.00 19.64 ? 563 HOH A O 1 HETATM 5697 O O A HOH HB 11 . ? -31.727 8.636 -12.819 0.54 13.91 ? 564 HOH A O 1 HETATM 5698 O O B HOH HB 11 . ? -32.448 10.186 -12.036 0.46 21.53 ? 564 HOH A O 1 HETATM 5699 O O . HOH HB 11 . ? -0.381 22.614 -31.392 1.00 37.24 ? 565 HOH A O 1 HETATM 5700 O O A HOH HB 11 . ? -6.703 11.135 -40.291 0.60 14.75 ? 566 HOH A O 1 HETATM 5701 O O B HOH HB 11 . ? -5.907 9.535 -38.364 0.40 16.75 ? 566 HOH A O 1 HETATM 5702 O O . HOH HB 11 . ? -39.046 5.948 -43.012 1.00 40.00 ? 567 HOH A O 1 HETATM 5703 O O . HOH HB 11 . ? -31.405 29.677 -33.979 1.00 37.83 ? 568 HOH A O 1 HETATM 5704 O O . HOH HB 11 . ? -15.209 16.751 -38.284 1.00 22.16 ? 569 HOH A O 1 HETATM 5705 O O . HOH HB 11 . ? -18.707 -3.487 -44.665 1.00 21.63 ? 570 HOH A O 1 HETATM 5706 O O . HOH HB 11 . ? -33.358 -5.038 -20.868 1.00 15.22 ? 571 HOH A O 1 HETATM 5707 O O . HOH HB 11 . ? -20.585 15.231 -30.704 1.00 41.59 ? 572 HOH A O 1 HETATM 5708 O O . HOH HB 11 . ? -13.369 11.886 -18.269 1.00 30.15 ? 573 HOH A O 1 HETATM 5709 O O . HOH HB 11 . ? -34.250 21.958 -12.416 1.00 29.21 ? 574 HOH A O 1 HETATM 5710 O O . HOH HB 11 . ? -17.254 -6.382 -38.283 1.00 44.69 ? 575 HOH A O 1 HETATM 5711 O O . HOH HB 11 . ? -31.018 14.656 -45.723 1.00 18.23 ? 576 HOH A O 1 HETATM 5712 O O . HOH HB 11 . ? -29.342 30.706 -30.033 1.00 39.78 ? 577 HOH A O 1 HETATM 5713 O O . HOH HB 11 . ? -38.260 4.139 -44.401 1.00 33.35 ? 578 HOH A O 1 HETATM 5714 O O . HOH HB 11 . ? -17.020 11.632 -44.651 1.00 16.41 ? 579 HOH A O 1 HETATM 5715 O O . HOH HB 11 . ? -26.377 11.551 -31.748 1.00 12.85 ? 580 HOH A O 1 HETATM 5716 O O . HOH HB 11 . ? -36.069 25.520 -23.860 1.00 31.73 ? 581 HOH A O 1 HETATM 5717 O O . HOH HB 11 . ? -22.205 -5.525 -26.756 1.00 18.59 ? 582 HOH A O 1 HETATM 5718 O O . HOH HB 11 . ? -23.120 -11.232 -24.341 1.00 33.82 ? 583 HOH A O 1 HETATM 5719 O O . HOH HB 11 . ? -24.661 21.584 -43.021 1.00 16.35 ? 584 HOH A O 1 HETATM 5720 O O . HOH HB 11 . ? -18.780 19.929 -24.318 1.00 17.11 ? 585 HOH A O 1 HETATM 5721 O O . HOH HB 11 . ? -32.857 22.275 -38.207 1.00 16.98 ? 586 HOH A O 1 HETATM 5722 O O . HOH HB 11 . ? -17.102 -6.458 -52.574 1.00 23.24 ? 587 HOH A O 1 HETATM 5723 O O . HOH HB 11 . ? -23.948 7.485 -11.077 1.00 37.04 ? 588 HOH A O 1 HETATM 5724 O O . HOH HB 11 . ? -11.589 16.909 -13.959 1.00 25.91 ? 589 HOH A O 1 HETATM 5725 O O . HOH HB 11 . ? -19.241 14.752 -14.093 1.00 30.80 ? 590 HOH A O 1 HETATM 5726 O O . HOH HB 11 . ? -22.490 -6.330 -48.503 1.00 22.39 ? 591 HOH A O 1 HETATM 5727 O O . HOH HB 11 . ? -36.974 10.169 -15.176 1.00 29.47 ? 592 HOH A O 1 HETATM 5728 O O . HOH HB 11 . ? -25.051 -1.691 -33.336 1.00 13.06 ? 593 HOH A O 1 HETATM 5729 O O . HOH HB 11 . ? -15.298 -10.493 -50.591 1.00 37.64 ? 594 HOH A O 1 HETATM 5730 O O . HOH HB 11 . ? -39.959 -5.058 -19.880 1.00 39.94 ? 595 HOH A O 1 HETATM 5731 O O . HOH HB 11 . ? -25.715 -1.532 -10.539 1.00 48.20 ? 596 HOH A O 1 HETATM 5732 O O . HOH HB 11 . ? -46.407 8.774 -29.412 1.00 53.39 ? 597 HOH A O 1 HETATM 5733 O O . HOH HB 11 . ? -22.314 9.498 -17.495 1.00 31.99 ? 598 HOH A O 1 HETATM 5734 O O . HOH HB 11 . ? -33.998 -6.187 -11.297 1.00 37.09 ? 599 HOH A O 1 HETATM 5735 O O . HOH HB 11 . ? -31.561 12.080 -35.209 1.00 20.69 ? 600 HOH A O 1 HETATM 5736 O O . HOH HB 11 . ? -27.451 27.574 -37.657 1.00 18.49 ? 601 HOH A O 1 HETATM 5737 O O . HOH HB 11 . ? -13.002 33.764 -36.685 1.00 61.39 ? 602 HOH A O 1 HETATM 5738 O O . HOH HB 11 . ? -6.605 24.854 -43.714 1.00 25.74 ? 603 HOH A O 1 HETATM 5739 O O . HOH HB 11 . ? -22.295 -7.425 -12.151 1.00 32.60 ? 604 HOH A O 1 HETATM 5740 O O . HOH HB 11 . ? -20.654 33.290 -25.223 1.00 29.58 ? 605 HOH A O 1 HETATM 5741 O O . HOH HB 11 . ? -1.630 27.805 -23.272 1.00 42.14 ? 606 HOH A O 1 HETATM 5742 O O . HOH HB 11 . ? -23.463 10.243 -15.932 1.00 41.49 ? 607 HOH A O 1 HETATM 5743 O O . HOH HB 11 . ? -19.377 17.682 -9.009 1.00 24.22 ? 608 HOH A O 1 HETATM 5744 O O . HOH HB 11 . ? -12.352 7.299 -44.314 1.00 41.94 ? 609 HOH A O 1 HETATM 5745 O O . HOH HB 11 . ? -21.862 32.108 -45.714 1.00 49.99 ? 610 HOH A O 1 HETATM 5746 O O . HOH HB 11 . ? 2.317 26.892 -28.273 1.00 48.53 ? 611 HOH A O 1 HETATM 5747 O O . HOH HB 11 . ? -14.276 15.561 -35.314 1.00 23.16 ? 612 HOH A O 1 HETATM 5748 O O . HOH HB 11 . ? -9.715 32.655 -25.106 1.00 36.18 ? 613 HOH A O 1 HETATM 5749 O O . HOH HB 11 . ? 4.365 27.101 -35.231 1.00 66.06 ? 614 HOH A O 1 HETATM 5750 O O . HOH HB 11 . ? -25.531 27.613 -39.686 1.00 25.20 ? 615 HOH A O 1 HETATM 5751 O O . HOH HB 11 . ? -19.002 1.407 -37.490 1.00 30.79 ? 616 HOH A O 1 HETATM 5752 O O . HOH HB 11 . ? -27.129 6.042 -8.903 1.00 18.89 ? 617 HOH A O 1 HETATM 5753 O O . HOH HB 11 . ? -28.058 30.685 -47.673 1.00 50.35 ? 618 HOH A O 1 HETATM 5754 O O . HOH HB 11 . ? -15.588 -19.717 -44.349 1.00 59.03 ? 619 HOH A O 1 HETATM 5755 O O . HOH HB 11 . ? -21.597 21.010 -8.525 1.00 49.90 ? 620 HOH A O 1 HETATM 5756 O O . HOH HB 11 . ? -28.553 20.845 -44.423 1.00 30.02 ? 621 HOH A O 1 HETATM 5757 O O . HOH HB 11 . ? -33.074 26.853 -29.012 1.00 39.18 ? 622 HOH A O 1 HETATM 5758 O O . HOH HB 11 . ? -24.188 26.944 -13.763 1.00 35.40 ? 623 HOH A O 1 HETATM 5759 O O . HOH HB 11 . ? -21.682 1.443 -31.048 1.00 32.54 ? 624 HOH A O 1 HETATM 5760 O O . HOH HB 11 . ? -26.396 -9.464 -26.962 1.00 19.93 ? 625 HOH A O 1 HETATM 5761 O O . HOH HB 11 . ? -34.254 25.251 -30.836 1.00 34.77 ? 626 HOH A O 1 HETATM 5762 O O . HOH HB 11 . ? -27.155 -4.144 -43.021 1.00 18.01 ? 627 HOH A O 1 HETATM 5763 O O . HOH HB 11 . ? -27.430 -3.229 -11.008 1.00 53.12 ? 628 HOH A O 1 HETATM 5764 O O . HOH HB 11 . ? -30.214 3.747 -12.185 1.00 19.15 ? 629 HOH A O 1 HETATM 5765 O O . HOH HB 11 . ? -44.298 14.690 -23.966 1.00 34.13 ? 630 HOH A O 1 HETATM 5766 O O . HOH HB 11 . ? -35.995 29.309 -26.423 1.00 44.09 ? 631 HOH A O 1 HETATM 5767 O O A HOH HB 11 . ? -34.432 12.539 -12.208 0.45 11.11 ? 632 HOH A O 1 HETATM 5768 O O B HOH HB 11 . ? -34.478 11.397 -13.499 0.55 28.98 ? 632 HOH A O 1 HETATM 5769 O O . HOH HB 11 . ? -7.398 5.612 -49.498 1.00 51.66 ? 633 HOH A O 1 HETATM 5770 O O . HOH HB 11 . ? -23.714 12.623 -30.778 1.00 20.11 ? 634 HOH A O 1 HETATM 5771 O O . HOH HB 11 . ? -18.585 9.689 -30.959 1.00 24.52 ? 635 HOH A O 1 HETATM 5772 O O . HOH HB 11 . ? -41.872 1.616 -18.980 1.00 23.61 ? 636 HOH A O 1 HETATM 5773 O O . HOH HB 11 . ? -23.164 -8.213 -25.350 1.00 9.90 ? 637 HOH A O 1 HETATM 5774 O O . HOH HB 11 . ? -27.008 22.177 -43.053 1.00 18.00 ? 638 HOH A O 1 HETATM 5775 O O . HOH HB 11 . ? -17.915 3.586 -38.533 1.00 18.71 ? 639 HOH A O 1 HETATM 5776 O O . HOH HB 11 . ? -14.903 9.598 -45.864 1.00 18.04 ? 640 HOH A O 1 HETATM 5777 O O . HOH HB 11 . ? -15.460 13.678 -51.182 1.00 24.61 ? 641 HOH A O 1 HETATM 5778 O O . HOH HB 11 . ? -38.868 17.315 -9.752 1.00 48.69 ? 642 HOH A O 1 HETATM 5779 O O . HOH HB 11 . ? -23.598 -5.464 -40.176 1.00 21.74 ? 643 HOH A O 1 HETATM 5780 O O . HOH HB 11 . ? -25.160 29.285 -14.308 1.00 38.23 ? 644 HOH A O 1 HETATM 5781 O O . HOH HB 11 . ? -27.342 31.119 -39.340 1.00 35.25 ? 645 HOH A O 1 HETATM 5782 O O . HOH HB 11 . ? -17.927 22.508 -49.285 1.00 36.76 ? 646 HOH A O 1 HETATM 5783 O O . HOH HB 11 . ? -17.653 0.586 -16.314 1.00 32.62 ? 647 HOH A O 1 HETATM 5784 O O . HOH HB 11 . ? -13.901 11.722 -51.589 1.00 34.01 ? 648 HOH A O 1 HETATM 5785 O O . HOH HB 11 . ? -30.903 15.417 -50.346 1.00 28.36 ? 649 HOH A O 1 HETATM 5786 O O . HOH HB 11 . ? -1.705 17.811 -44.310 1.00 27.55 ? 650 HOH A O 1 HETATM 5787 O O . HOH HB 11 . ? -18.666 -6.019 -45.012 1.00 37.00 ? 651 HOH A O 1 HETATM 5788 O O . HOH HB 11 . ? -30.390 28.640 -44.970 1.00 42.07 ? 652 HOH A O 1 HETATM 5789 O O . HOH HB 11 . ? -7.236 12.697 -31.900 1.00 36.98 ? 653 HOH A O 1 HETATM 5790 O O . HOH HB 11 . ? -22.514 -13.458 -32.854 1.00 44.73 ? 654 HOH A O 1 HETATM 5791 O O . HOH HB 11 . ? -11.181 18.674 -50.932 1.00 35.42 ? 655 HOH A O 1 HETATM 5792 O O . HOH HB 11 . ? -13.432 7.729 -51.342 1.00 42.04 ? 656 HOH A O 1 HETATM 5793 O O . HOH HB 11 . ? -15.381 25.416 -3.060 1.00 36.55 ? 657 HOH A O 1 HETATM 5794 O O . HOH HB 11 . ? -12.673 18.300 -27.038 1.00 18.10 ? 658 HOH A O 1 HETATM 5795 O O . HOH HB 11 . ? -23.728 12.932 -14.997 1.00 19.38 ? 659 HOH A O 1 HETATM 5796 O O . HOH HB 11 . ? -14.928 -2.875 -46.832 1.00 33.45 ? 660 HOH A O 1 HETATM 5797 O O . HOH HB 11 . ? -24.223 -14.216 -28.974 1.00 61.02 ? 661 HOH A O 1 HETATM 5798 O O . HOH HB 11 . ? -37.382 22.191 -31.945 1.00 46.58 ? 662 HOH A O 1 HETATM 5799 O O . HOH HB 11 . ? -5.225 23.330 -51.284 1.00 48.97 ? 663 HOH A O 1 HETATM 5800 O O . HOH HB 11 . ? -10.024 -13.781 -53.412 1.00 62.04 ? 664 HOH A O 1 HETATM 5801 O O . HOH HB 11 . ? -36.027 -6.053 -37.103 1.00 42.34 ? 665 HOH A O 1 HETATM 5802 O O . HOH HB 11 . ? -11.062 8.403 -52.150 1.00 26.54 ? 666 HOH A O 1 HETATM 5803 O O . HOH HB 11 . ? -30.596 0.110 -29.699 1.00 9.19 ? 667 HOH A O 1 HETATM 5804 O O . HOH HB 11 . ? -31.304 13.189 -44.413 1.00 16.13 ? 668 HOH A O 1 HETATM 5805 O O . HOH HB 11 . ? -26.837 -11.792 -36.062 1.00 40.48 ? 669 HOH A O 1 HETATM 5806 O O . HOH HB 11 . ? -7.295 27.431 -45.441 1.00 53.95 ? 670 HOH A O 1 HETATM 5807 O O . HOH HB 11 . ? -0.100 22.660 -42.256 1.00 37.54 ? 671 HOH A O 1 HETATM 5808 O O . HOH HB 11 . ? -9.662 17.074 -10.411 1.00 48.44 ? 672 HOH A O 1 HETATM 5809 O O . HOH HB 11 . ? -26.513 -9.181 -10.545 1.00 49.41 ? 673 HOH A O 1 HETATM 5810 O O . HOH HB 11 . ? -7.122 14.006 -13.161 1.00 40.05 ? 674 HOH A O 1 HETATM 5811 O O . HOH HB 11 . ? -28.858 25.752 -11.574 1.00 34.28 ? 675 HOH A O 1 HETATM 5812 O O . HOH HB 11 . ? -8.548 9.146 -31.112 1.00 32.26 ? 676 HOH A O 1 HETATM 5813 O O . HOH HB 11 . ? -33.579 14.835 -46.545 1.00 15.99 ? 677 HOH A O 1 HETATM 5814 O O . HOH HB 11 . ? -23.117 -3.471 -25.546 1.00 19.60 ? 678 HOH A O 1 HETATM 5815 O O . HOH HB 11 . ? -17.788 -12.227 -50.089 1.00 61.38 ? 679 HOH A O 1 HETATM 5816 O O A HOH HB 11 . ? -16.274 29.529 -23.324 0.53 20.19 ? 680 HOH A O 1 HETATM 5817 O O B HOH HB 11 . ? -15.706 31.408 -23.159 0.47 22.62 ? 680 HOH A O 1 HETATM 5818 O O . HOH HB 11 . ? -15.029 18.395 -8.635 1.00 35.18 ? 681 HOH A O 1 HETATM 5819 O O . HOH HB 11 . ? -24.979 -6.716 -10.746 1.00 47.06 ? 682 HOH A O 1 HETATM 5820 O O . HOH HB 11 . ? -14.483 6.276 -19.190 1.00 52.74 ? 683 HOH A O 1 HETATM 5821 O O A HOH HB 11 . ? 1.511 24.643 -41.030 0.53 19.18 ? 684 HOH A O 1 HETATM 5822 O O B HOH HB 11 . ? 2.605 22.584 -41.135 0.47 31.75 ? 684 HOH A O 1 HETATM 5823 O O . HOH HB 11 . ? -38.228 22.685 -29.539 1.00 56.68 ? 685 HOH A O 1 HETATM 5824 O O . HOH HB 11 . ? -44.469 21.459 -24.694 1.00 34.85 ? 686 HOH A O 1 HETATM 5825 O O . HOH HB 11 . ? -30.447 20.671 -48.933 1.00 46.87 ? 687 HOH A O 1 HETATM 5826 O O . HOH HB 11 . ? -2.063 13.765 -40.665 1.00 38.92 ? 688 HOH A O 1 HETATM 5827 O O . HOH HB 11 . ? -29.844 32.100 -21.445 1.00 52.84 ? 689 HOH A O 1 HETATM 5828 O O . HOH HB 11 . ? -9.117 -9.427 -53.698 1.00 49.60 ? 690 HOH A O 1 HETATM 5829 O O A HOH HB 11 . ? -22.895 40.712 -25.212 0.34 13.32 ? 691 HOH A O 1 HETATM 5830 O O B HOH HB 11 . ? -28.730 -8.738 -50.326 0.66 33.75 ? 691 HOH A O 1 HETATM 5831 O O . HOH HB 11 . ? -36.108 6.208 -11.598 1.00 35.99 ? 692 HOH A O 1 HETATM 5832 O O . HOH HB 11 . ? -20.202 5.976 -17.314 1.00 53.22 ? 693 HOH A O 1 HETATM 5833 O O . HOH HB 11 . ? -19.081 -3.389 -12.119 1.00 56.12 ? 694 HOH A O 1 HETATM 5834 O O . HOH HB 11 . ? -27.150 14.038 -10.285 1.00 12.71 ? 695 HOH A O 1 HETATM 5835 O O . HOH HB 11 . ? -13.676 20.421 -28.073 1.00 28.74 ? 696 HOH A O 1 HETATM 5836 O O . HOH HB 11 . ? -40.723 15.945 -13.614 1.00 56.47 ? 697 HOH A O 1 HETATM 5837 O O . HOH HB 11 . ? -15.476 -5.972 -59.114 1.00 29.69 ? 698 HOH A O 1 HETATM 5838 O O . HOH HB 11 . ? -29.448 -12.310 -25.357 1.00 40.29 ? 699 HOH A O 1 HETATM 5839 O O . HOH HB 11 . ? -31.856 30.446 -16.851 1.00 42.74 ? 700 HOH A O 1 HETATM 5840 O O . HOH HB 11 . ? -25.414 -10.928 -37.858 1.00 56.62 ? 701 HOH A O 1 HETATM 5841 O O . HOH HB 11 . ? -24.750 25.783 -11.307 1.00 44.14 ? 702 HOH A O 1 HETATM 5842 O O . HOH HB 11 . ? -41.740 -5.461 -36.501 1.00 55.88 ? 703 HOH A O 1 HETATM 5843 O O . HOH HB 11 . ? -17.486 -1.783 -46.167 1.00 34.32 ? 704 HOH A O 1 HETATM 5844 O O . HOH HB 11 . ? -2.318 18.606 -47.868 1.00 39.08 ? 705 HOH A O 1 HETATM 5845 O O . HOH HB 11 . ? -24.163 13.377 -11.374 1.00 22.44 ? 706 HOH A O 1 HETATM 5846 O O . HOH HB 11 . ? 2.626 24.421 -37.277 1.00 46.68 ? 707 HOH A O 1 HETATM 5847 O O . HOH HB 11 . ? -19.202 7.981 -14.909 1.00 43.44 ? 708 HOH A O 1 HETATM 5848 O O . HOH HB 11 . ? -0.450 33.375 -34.029 1.00 41.37 ? 709 HOH A O 1 HETATM 5849 O O . HOH HB 11 . ? -21.734 -11.204 -14.465 1.00 41.34 ? 710 HOH A O 1 HETATM 5850 O O . HOH HB 11 . ? -6.148 9.968 -36.179 1.00 60.35 ? 711 HOH A O 1 HETATM 5851 O O . HOH HB 11 . ? -10.772 21.569 -51.265 1.00 45.76 ? 712 HOH A O 1 HETATM 5852 O O . HOH HB 11 . ? -8.987 -0.138 -49.679 1.00 69.60 ? 713 HOH A O 1 HETATM 5853 O O . HOH HB 11 . ? -24.890 -13.469 -33.999 1.00 59.52 ? 714 HOH A O 1 HETATM 5854 O O . HOH HB 11 . ? -26.232 23.285 -9.118 1.00 42.25 ? 715 HOH A O 1 HETATM 5855 O O . HOH HB 11 . ? -4.275 20.614 -10.058 1.00 50.80 ? 716 HOH A O 1 HETATM 5856 O O . HOH HB 11 . ? -16.360 -11.156 -40.115 1.00 50.03 ? 717 HOH A O 1 HETATM 5857 O O . HOH HB 11 . ? -22.257 -4.561 -11.343 1.00 40.92 ? 718 HOH A O 1 HETATM 5858 O O . HOH HB 11 . ? -35.193 30.780 -16.387 1.00 69.60 ? 719 HOH A O 1 HETATM 5859 O O . HOH HB 11 . ? -45.168 16.326 -20.770 1.00 56.19 ? 720 HOH A O 1 HETATM 5860 O O . HOH HB 11 . ? -28.642 29.545 -13.244 1.00 45.79 ? 721 HOH A O 1 HETATM 5861 O O . HOH HB 11 . ? -40.627 -5.052 -11.159 1.00 39.75 ? 722 HOH A O 1 HETATM 5862 O O . HOH HB 11 . ? -37.466 -5.538 -34.563 1.00 45.91 ? 723 HOH A O 1 HETATM 5863 O O . HOH HB 11 . ? -22.874 -0.088 -33.670 1.00 26.44 ? 724 HOH A O 1 HETATM 5864 O O . HOH HB 11 . ? -29.635 -0.403 -8.616 1.00 37.58 ? 725 HOH A O 1 HETATM 5865 O O . HOH HB 11 . ? -15.313 3.357 -39.565 1.00 35.86 ? 726 HOH A O 1 HETATM 5866 O O . HOH HB 11 . ? -16.527 33.602 -41.011 1.00 55.65 ? 727 HOH A O 1 HETATM 5867 O O . HOH HB 11 . ? -17.909 -5.197 -33.199 1.00 48.17 ? 728 HOH A O 1 HETATM 5868 O O . HOH HB 11 . ? 1.668 18.152 -30.303 1.00 51.98 ? 729 HOH A O 1 HETATM 5869 O O . HOH HB 11 . ? -38.597 12.260 -15.083 1.00 30.96 ? 730 HOH A O 1 HETATM 5870 O O . HOH HB 11 . ? -34.835 -12.268 -34.961 1.00 50.20 ? 731 HOH A O 1 HETATM 5871 O O . HOH HB 11 . ? -30.836 31.784 -18.461 1.00 44.67 ? 732 HOH A O 1 HETATM 5872 O O . HOH HB 11 . ? -28.241 24.373 -9.057 1.00 57.19 ? 733 HOH A O 1 HETATM 5873 O O . HOH HB 11 . ? -13.636 -12.152 -42.484 1.00 61.90 ? 734 HOH A O 1 HETATM 5874 O O . HOH HB 11 . ? -11.900 14.270 -18.650 1.00 49.90 ? 735 HOH A O 1 HETATM 5875 O O . HOH HB 11 . ? -33.837 27.891 -31.260 1.00 50.16 ? 736 HOH A O 1 HETATM 5876 O O A HOH HB 11 . ? -37.297 24.424 -14.726 0.50 22.69 ? 737 HOH A O 1 HETATM 5877 O O B HOH HB 11 . ? -35.417 24.377 -13.713 0.50 18.30 ? 737 HOH A O 1 HETATM 5878 O O A HOH HB 11 . ? -10.393 34.323 -33.125 0.60 36.20 ? 738 HOH A O 1 HETATM 5879 O O B HOH HB 11 . ? -8.816 33.139 -31.935 0.40 26.18 ? 738 HOH A O 1 HETATM 5880 O O . HOH HB 11 . ? -38.518 25.742 -18.827 1.00 43.57 ? 739 HOH A O 1 HETATM 5881 O O . HOH HB 11 . ? -16.494 35.600 -27.506 1.00 59.01 ? 740 HOH A O 1 HETATM 5882 O O . HOH HB 11 . ? -1.053 15.875 -18.128 1.00 44.05 ? 741 HOH A O 1 HETATM 5883 O O . HOH HB 11 . ? 1.912 22.889 -30.114 1.00 42.63 ? 742 HOH A O 1 HETATM 5884 O O . HOH HB 11 . ? -11.693 -0.533 -51.128 1.00 54.28 ? 743 HOH A O 1 HETATM 5885 O O . HOH HB 11 . ? -19.911 30.989 -45.647 1.00 44.10 ? 744 HOH A O 1 HETATM 5886 O O . HOH HB 11 . ? -22.352 8.040 -15.459 1.00 55.36 ? 745 HOH A O 1 HETATM 5887 O O . HOH HB 11 . ? -8.346 -12.346 -54.636 1.00 50.50 ? 746 HOH A O 1 HETATM 5888 O O . HOH HB 11 . ? -29.274 -15.622 -16.356 1.00 57.87 ? 747 HOH A O 1 HETATM 5889 O O . HOH HB 11 . ? -20.988 -13.468 -21.806 1.00 48.07 ? 748 HOH A O 1 HETATM 5890 O O . HOH HB 11 . ? -12.042 15.427 -11.826 1.00 44.87 ? 749 HOH A O 1 HETATM 5891 O O . HOH HB 11 . ? -31.790 29.185 -42.961 1.00 33.47 ? 750 HOH A O 1 HETATM 5892 O O . HOH HB 11 . ? -33.483 -2.028 -46.315 1.00 48.48 ? 751 HOH A O 1 HETATM 5893 O O A HOH HB 11 . ? -13.856 0.300 -42.475 0.50 23.21 ? 752 HOH A O 1 HETATM 5894 O O B HOH HB 11 . ? -14.476 -0.925 -43.811 0.50 21.11 ? 752 HOH A O 1 HETATM 5895 O O A HOH HB 11 . ? -6.741 4.339 -46.902 0.52 35.89 ? 753 HOH A O 1 HETATM 5896 O O B HOH HB 11 . ? -8.798 4.819 -46.402 0.48 27.97 ? 753 HOH A O 1 HETATM 5897 O O . HOH HB 11 . ? -40.534 17.675 -31.489 1.00 41.07 ? 754 HOH A O 1 HETATM 5898 O O . HOH HB 11 . ? -0.018 24.338 -15.865 1.00 52.28 ? 755 HOH A O 1 HETATM 5899 O O . HOH HB 11 . ? -23.553 9.538 -12.953 1.00 50.46 ? 756 HOH A O 1 HETATM 5900 O O . HOH HB 11 . ? -42.478 17.341 -28.664 1.00 34.42 ? 757 HOH A O 1 HETATM 5901 O O A HOH HB 11 . ? -42.845 3.970 -18.183 0.44 22.05 ? 758 HOH A O 1 HETATM 5902 O O B HOH HB 11 . ? -42.214 4.377 -16.283 0.56 45.23 ? 758 HOH A O 1 HETATM 5903 O O . HOH HB 11 . ? -44.829 19.159 -20.988 1.00 42.89 ? 759 HOH A O 1 HETATM 5904 O O A HOH HB 11 . ? -26.945 -12.684 -27.208 0.50 63.71 ? 760 HOH A O 1 HETATM 5905 O O B HOH HB 11 . ? -26.944 -12.673 -27.191 0.50 63.73 ? 760 HOH A O 1 HETATM 5906 O O . HOH HB 11 . ? -1.406 15.413 -43.308 1.00 43.57 ? 761 HOH A O 1 HETATM 5907 O O . HOH HB 11 . ? -29.389 32.226 -13.819 1.00 42.47 ? 762 HOH A O 1 HETATM 5908 O O . HOH HB 11 . ? -8.461 7.418 -41.903 1.00 54.68 ? 763 HOH A O 1 HETATM 5909 O O . HOH HB 11 . ? -11.044 4.993 -43.556 1.00 43.47 ? 764 HOH A O 1 HETATM 5910 O O . HOH HB 11 . ? -24.658 -4.146 -10.349 1.00 73.13 ? 765 HOH A O 1 HETATM 5911 O O . HOH HB 11 . ? -23.186 -12.967 -36.068 1.00 37.04 ? 766 HOH A O 1 HETATM 5912 O O . HOH HB 11 . ? -10.496 10.527 -20.565 1.00 71.64 ? 767 HOH A O 1 HETATM 5913 O O . HOH HB 11 . ? -23.096 -12.957 -22.450 1.00 37.50 ? 768 HOH A O 1 HETATM 5914 O O . HOH HB 11 . ? -18.423 15.957 -9.842 1.00 47.23 ? 769 HOH A O 1 HETATM 5915 O O . HOH HB 11 . ? -36.968 25.087 -27.306 1.00 53.82 ? 770 HOH A O 1 HETATM 5916 O O . HOH HB 11 . ? -47.555 -0.457 -23.812 1.00 59.84 ? 771 HOH A O 1 HETATM 5917 O O . HOH HB 11 . ? -23.090 -10.057 -13.098 1.00 43.22 ? 772 HOH A O 1 HETATM 5918 O O . HOH HB 11 . ? -17.555 -4.140 -36.833 1.00 41.11 ? 773 HOH A O 1 HETATM 5919 O O . HOH HB 11 . ? -5.863 9.516 -46.383 1.00 69.59 ? 774 HOH A O 1 HETATM 5920 O O . HOH HB 11 . ? -26.593 34.897 -18.918 1.00 46.18 ? 775 HOH A O 1 HETATM 5921 O O . HOH HB 11 . ? -17.879 31.629 -23.002 1.00 46.75 ? 776 HOH A O 1 HETATM 5922 O O . HOH HB 11 . ? -30.312 27.085 -13.266 1.00 43.39 ? 777 HOH A O 1 HETATM 5923 O O . HOH HB 11 . ? -34.911 -2.171 -49.726 1.00 42.38 ? 778 HOH A O 1 HETATM 5924 O O . HOH HB 11 . ? -2.581 33.043 -40.738 1.00 47.32 ? 779 HOH A O 1 HETATM 5925 O O . HOH HB 11 . ? -36.951 -14.198 -12.979 1.00 60.81 ? 780 HOH A O 1 HETATM 5926 O O . HOH HB 11 . ? -32.320 19.804 -8.250 1.00 54.20 ? 781 HOH A O 1 HETATM 5927 O O . HOH HB 11 . ? -11.850 3.200 -33.990 1.00 62.43 ? 782 HOH A O 1 HETATM 5928 O O . HOH HB 11 . ? 2.581 13.831 -36.174 1.00 53.53 ? 783 HOH A O 1 HETATM 5929 O O . HOH HB 11 . ? -28.780 -10.516 -8.793 1.00 52.10 ? 784 HOH A O 1 HETATM 5930 O O . HOH HB 11 . ? -32.293 23.025 -10.249 1.00 44.48 ? 785 HOH A O 1 HETATM 5931 O O . HOH HB 11 . ? -30.374 26.135 -46.795 1.00 47.03 ? 786 HOH A O 1 HETATM 5932 O O . HOH HB 11 . ? -8.180 8.125 -44.540 1.00 61.82 ? 787 HOH A O 1 HETATM 5933 O O . HOH HB 11 . ? -31.421 25.039 -11.086 1.00 55.83 ? 788 HOH A O 1 HETATM 5934 O O . HOH HB 11 . ? -1.141 11.276 -44.064 1.00 62.19 ? 789 HOH A O 1 HETATM 5935 O O . HOH HB 11 . ? -6.139 8.579 -43.570 1.00 42.43 ? 790 HOH A O 1 HETATM 5936 O O . HOH HB 11 . ? 1.847 12.811 -38.044 1.00 54.16 ? 791 HOH A O 1 HETATM 5937 O O . HOH HB 11 . ? -14.381 3.569 -30.833 1.00 50.19 ? 792 HOH A O 1 HETATM 5938 O O . HOH HB 11 . ? -24.587 -15.682 -21.917 1.00 52.70 ? 793 HOH A O 1 HETATM 5939 O O . HOH IB 11 . ? -50.698 -17.243 -63.449 1.00 55.39 ? 501 HOH B O 1 HETATM 5940 O O . HOH IB 11 . ? -19.458 -7.550 -54.158 1.00 23.63 ? 502 HOH B O 1 HETATM 5941 O O . HOH IB 11 . ? -27.110 -5.503 -89.243 1.00 27.82 ? 503 HOH B O 1 HETATM 5942 O O . HOH IB 11 . ? -42.046 10.017 -80.876 1.00 47.81 ? 504 HOH B O 1 HETATM 5943 O O . HOH IB 11 . ? -20.492 23.296 -64.569 1.00 45.08 ? 505 HOH B O 1 HETATM 5944 O O . HOH IB 11 . ? -18.169 -4.131 -58.567 1.00 19.36 ? 506 HOH B O 1 HETATM 5945 O O . HOH IB 11 . ? -42.991 6.664 -82.743 1.00 35.86 ? 507 HOH B O 1 HETATM 5946 O O . HOH IB 11 . ? -49.825 -2.785 -64.805 1.00 28.21 ? 508 HOH B O 1 HETATM 5947 O O . HOH IB 11 . ? -26.491 -13.321 -61.324 1.00 27.41 ? 509 HOH B O 1 HETATM 5948 O O . HOH IB 11 . ? -24.245 -9.355 -91.965 1.00 55.79 ? 510 HOH B O 1 HETATM 5949 O O . HOH IB 11 . ? -11.799 -9.083 -70.070 1.00 44.63 ? 511 HOH B O 1 HETATM 5950 O O . HOH IB 11 . ? -51.373 -2.476 -74.400 1.00 25.89 ? 512 HOH B O 1 HETATM 5951 O O . HOH IB 11 . ? -48.611 -2.374 -68.142 1.00 59.43 ? 513 HOH B O 1 HETATM 5952 O O . HOH IB 11 . ? -35.439 22.738 -37.933 1.00 44.40 ? 514 HOH B O 1 HETATM 5953 O O . HOH IB 11 . ? -21.770 20.953 -64.857 1.00 32.82 ? 515 HOH B O 1 HETATM 5954 O O . HOH IB 11 . ? -29.305 0.294 -82.353 1.00 38.47 ? 516 HOH B O 1 HETATM 5955 O O . HOH IB 11 . ? -31.938 21.143 -42.095 1.00 37.55 ? 517 HOH B O 1 HETATM 5956 O O . HOH IB 11 . ? -20.781 -1.126 -79.161 1.00 19.59 ? 518 HOH B O 1 HETATM 5957 O O . HOH IB 11 . ? -38.145 2.600 -86.024 1.00 39.59 ? 519 HOH B O 1 HETATM 5958 O O . HOH IB 11 . ? -9.800 18.620 -64.818 1.00 20.74 ? 520 HOH B O 1 HETATM 5959 O O . HOH IB 11 . ? -34.294 -14.609 -82.210 1.00 41.67 ? 521 HOH B O 1 HETATM 5960 O O . HOH IB 11 . ? -14.719 10.982 -81.558 1.00 20.97 ? 522 HOH B O 1 HETATM 5961 O O . HOH IB 11 . ? -47.994 3.909 -70.864 1.00 37.24 ? 523 HOH B O 1 HETATM 5962 O O . HOH IB 11 . ? -44.590 0.586 -82.267 1.00 14.33 ? 524 HOH B O 1 HETATM 5963 O O . HOH IB 11 . ? -27.144 7.401 -75.300 1.00 50.94 ? 525 HOH B O 1 HETATM 5964 O O . HOH IB 11 . ? -21.507 -15.821 -91.388 1.00 50.11 ? 526 HOH B O 1 HETATM 5965 O O . HOH IB 11 . ? -33.013 14.686 -49.305 1.00 15.92 ? 527 HOH B O 1 HETATM 5966 O O . HOH IB 11 . ? -22.418 18.241 -59.027 1.00 26.40 ? 528 HOH B O 1 HETATM 5967 O O . HOH IB 11 . ? -49.182 8.702 -75.300 1.00 47.36 ? 529 HOH B O 1 HETATM 5968 O O . HOH IB 11 . ? -37.491 9.293 -49.563 1.00 19.37 ? 530 HOH B O 1 HETATM 5969 O O . HOH IB 11 . ? -25.214 -2.415 -64.681 1.00 13.65 ? 531 HOH B O 1 HETATM 5970 O O . HOH IB 11 . ? -6.690 1.075 -64.725 1.00 19.16 ? 532 HOH B O 1 HETATM 5971 O O . HOH IB 11 . ? -5.822 9.673 -53.391 1.00 39.92 ? 533 HOH B O 1 HETATM 5972 O O . HOH IB 11 . ? -29.243 14.123 -57.706 1.00 54.77 ? 534 HOH B O 1 HETATM 5973 O O . HOH IB 11 . ? -4.505 12.908 -76.942 1.00 48.62 ? 535 HOH B O 1 HETATM 5974 O O . HOH IB 11 . ? -8.756 9.998 -54.225 1.00 46.49 ? 536 HOH B O 1 HETATM 5975 O O . HOH IB 11 . ? -23.355 8.360 -64.618 1.00 13.02 ? 537 HOH B O 1 HETATM 5976 O O . HOH IB 11 . ? -19.548 -5.078 -67.857 1.00 17.94 ? 538 HOH B O 1 HETATM 5977 O O . HOH IB 11 . ? -33.054 -14.060 -56.483 1.00 33.01 ? 539 HOH B O 1 HETATM 5978 O O . HOH IB 11 . ? -8.935 2.592 -49.288 1.00 30.20 ? 540 HOH B O 1 HETATM 5979 O O . HOH IB 11 . ? -22.033 7.340 -81.151 1.00 20.61 ? 541 HOH B O 1 HETATM 5980 O O . HOH IB 11 . ? -23.828 -4.285 -68.620 1.00 10.36 ? 542 HOH B O 1 HETATM 5981 O O . HOH IB 11 . ? -17.680 4.741 -78.957 1.00 22.08 ? 543 HOH B O 1 HETATM 5982 O O . HOH IB 11 . ? -12.574 -9.914 -84.982 1.00 37.07 ? 544 HOH B O 1 HETATM 5983 O O . HOH IB 11 . ? -34.127 -15.829 -79.798 1.00 43.20 ? 545 HOH B O 1 HETATM 5984 O O . HOH IB 11 . ? -16.249 -15.393 -81.289 1.00 28.27 ? 546 HOH B O 1 HETATM 5985 O O . HOH IB 11 . ? -50.293 2.442 -80.371 1.00 34.73 ? 547 HOH B O 1 HETATM 5986 O O . HOH IB 11 . ? -24.827 16.660 -58.820 1.00 34.80 ? 548 HOH B O 1 HETATM 5987 O O . HOH IB 11 . ? -36.026 -10.755 -82.160 1.00 19.08 ? 549 HOH B O 1 HETATM 5988 O O . HOH IB 11 . ? -34.509 7.895 -64.606 1.00 28.78 ? 550 HOH B O 1 HETATM 5989 O O . HOH IB 11 . ? -35.626 12.746 -46.961 1.00 15.72 ? 551 HOH B O 1 HETATM 5990 O O . HOH IB 11 . ? -34.029 5.069 -67.881 1.00 24.17 ? 552 HOH B O 1 HETATM 5991 O O . HOH IB 11 . ? -33.761 -16.768 -55.998 1.00 33.93 ? 553 HOH B O 1 HETATM 5992 O O . HOH IB 11 . ? -35.317 3.055 -70.528 1.00 17.15 ? 554 HOH B O 1 HETATM 5993 O O . HOH IB 11 . ? -35.017 15.722 -44.090 1.00 20.11 ? 555 HOH B O 1 HETATM 5994 O O . HOH IB 11 . ? -20.927 4.631 -71.687 1.00 58.41 ? 556 HOH B O 1 HETATM 5995 O O . HOH IB 11 . ? -47.181 -0.399 -79.963 1.00 13.28 ? 557 HOH B O 1 HETATM 5996 O O . HOH IB 11 . ? -6.135 -5.139 -73.564 1.00 22.04 ? 558 HOH B O 1 HETATM 5997 O O . HOH IB 11 . ? -23.302 -4.307 -63.707 1.00 17.91 ? 559 HOH B O 1 HETATM 5998 O O . HOH IB 11 . ? -17.207 11.773 -65.922 1.00 24.36 ? 560 HOH B O 1 HETATM 5999 O O . HOH IB 11 . ? -9.752 -0.958 -55.955 1.00 42.89 ? 561 HOH B O 1 HETATM 6000 O O . HOH IB 11 . ? -29.781 -14.081 -80.748 1.00 25.07 ? 562 HOH B O 1 HETATM 6001 O O . HOH IB 11 . ? -47.706 -2.331 -83.399 1.00 19.25 ? 563 HOH B O 1 HETATM 6002 O O . HOH IB 11 . ? -0.598 3.412 -69.413 1.00 37.40 ? 564 HOH B O 1 HETATM 6003 O O . HOH IB 11 . ? -33.881 -12.055 -55.076 1.00 26.24 ? 565 HOH B O 1 HETATM 6004 O O . HOH IB 11 . ? -24.186 -0.079 -68.180 1.00 14.90 ? 566 HOH B O 1 HETATM 6005 O O . HOH IB 11 . ? -24.773 6.421 -72.814 1.00 21.67 ? 567 HOH B O 1 HETATM 6006 O O . HOH IB 11 . ? -35.574 11.948 -54.658 1.00 22.83 ? 568 HOH B O 1 HETATM 6007 O O . HOH IB 11 . ? -37.007 3.533 -53.924 1.00 21.70 ? 569 HOH B O 1 HETATM 6008 O O . HOH IB 11 . ? -28.598 1.146 -79.550 1.00 19.89 ? 570 HOH B O 1 HETATM 6009 O O . HOH IB 11 . ? -20.666 12.090 -58.408 1.00 21.46 ? 571 HOH B O 1 HETATM 6010 O O . HOH IB 11 . ? -20.074 -4.714 -54.930 1.00 13.61 ? 572 HOH B O 1 HETATM 6011 O O . HOH IB 11 . ? -32.693 4.618 -62.767 1.00 16.63 ? 573 HOH B O 1 HETATM 6012 O O . HOH IB 11 . ? -40.619 17.351 -48.076 1.00 40.17 ? 574 HOH B O 1 HETATM 6013 O O . HOH IB 11 . ? -33.790 13.021 -53.554 1.00 41.20 ? 575 HOH B O 1 HETATM 6014 O O . HOH IB 11 . ? -19.389 13.953 -70.627 1.00 28.61 ? 576 HOH B O 1 HETATM 6015 O O . HOH IB 11 . ? -26.601 -15.831 -68.246 1.00 26.86 ? 577 HOH B O 1 HETATM 6016 O O . HOH IB 11 . ? -12.673 -5.942 -62.897 1.00 21.84 ? 578 HOH B O 1 HETATM 6017 O O . HOH IB 11 . ? -34.674 -5.562 -88.091 1.00 48.53 ? 579 HOH B O 1 HETATM 6018 O O . HOH IB 11 . ? -28.962 -18.638 -59.312 1.00 28.00 ? 580 HOH B O 1 HETATM 6019 O O . HOH IB 11 . ? -35.108 1.843 -76.988 1.00 10.71 ? 581 HOH B O 1 HETATM 6020 O O . HOH IB 11 . ? -11.736 3.175 -60.352 1.00 18.66 ? 582 HOH B O 1 HETATM 6021 O O . HOH IB 11 . ? -36.523 -14.792 -79.642 1.00 26.28 ? 583 HOH B O 1 HETATM 6022 O O . HOH IB 11 . ? -13.451 -3.088 -89.445 1.00 37.07 ? 584 HOH B O 1 HETATM 6023 O O . HOH IB 11 . ? -11.052 0.699 -59.916 1.00 18.35 ? 585 HOH B O 1 HETATM 6024 O O . HOH IB 11 . ? -36.541 19.512 -59.058 1.00 50.19 ? 586 HOH B O 1 HETATM 6025 O O . HOH IB 11 . ? -31.313 -10.484 -83.866 1.00 31.35 ? 587 HOH B O 1 HETATM 6026 O O . HOH IB 11 . ? -45.599 1.000 -68.452 1.00 20.37 ? 588 HOH B O 1 HETATM 6027 O O . HOH IB 11 . ? -41.739 4.621 -70.395 1.00 15.83 ? 589 HOH B O 1 HETATM 6028 O O . HOH IB 11 . ? -47.097 -4.945 -67.870 1.00 39.69 ? 590 HOH B O 1 HETATM 6029 O O . HOH IB 11 . ? -43.356 -7.738 -73.442 1.00 9.78 ? 591 HOH B O 1 HETATM 6030 O O . HOH IB 11 . ? -32.428 -10.386 -53.582 1.00 39.30 ? 592 HOH B O 1 HETATM 6031 O O . HOH IB 11 . ? -12.248 -0.363 -57.750 1.00 23.30 ? 593 HOH B O 1 HETATM 6032 O O . HOH IB 11 . ? -25.950 -13.493 -86.352 1.00 24.34 ? 594 HOH B O 1 HETATM 6033 O O . HOH IB 11 . ? -41.638 -3.076 -85.522 1.00 24.32 ? 595 HOH B O 1 HETATM 6034 O O . HOH IB 11 . ? -37.639 -16.990 -74.185 1.00 20.63 ? 596 HOH B O 1 HETATM 6035 O O . HOH IB 11 . ? -36.460 15.540 -46.710 1.00 22.46 ? 597 HOH B O 1 HETATM 6036 O O . HOH IB 11 . ? -44.750 -6.220 -83.705 1.00 21.27 ? 598 HOH B O 1 HETATM 6037 O O . HOH IB 11 . ? -18.246 -1.372 -54.764 1.00 19.43 ? 599 HOH B O 1 HETATM 6038 O O . HOH IB 11 . ? -18.714 -16.907 -79.940 1.00 52.13 ? 600 HOH B O 1 HETATM 6039 O O . HOH IB 11 . ? -18.860 -10.940 -63.878 1.00 55.25 ? 601 HOH B O 1 HETATM 6040 O O . HOH IB 11 . ? -24.574 -13.118 -92.337 1.00 61.01 ? 602 HOH B O 1 HETATM 6041 O O . HOH IB 11 . ? -12.275 18.725 -55.573 1.00 29.95 ? 603 HOH B O 1 HETATM 6042 O O . HOH IB 11 . ? -43.761 1.923 -54.635 1.00 31.85 ? 604 HOH B O 1 HETATM 6043 O O . HOH IB 11 . ? -9.332 -7.491 -62.196 1.00 41.50 ? 605 HOH B O 1 HETATM 6044 O O . HOH IB 11 . ? -7.512 -1.078 -87.115 1.00 32.18 ? 606 HOH B O 1 HETATM 6045 O O . HOH IB 11 . ? -21.877 19.925 -52.163 1.00 27.71 ? 607 HOH B O 1 HETATM 6046 O O . HOH IB 11 . ? -43.959 -2.295 -84.652 1.00 22.16 ? 608 HOH B O 1 HETATM 6047 O O . HOH IB 11 . ? -18.530 11.432 -77.597 1.00 21.00 ? 609 HOH B O 1 HETATM 6048 O O . HOH IB 11 . ? -44.477 -25.389 -60.793 1.00 47.85 ? 610 HOH B O 1 HETATM 6049 O O . HOH IB 11 . ? 1.248 -7.982 -75.153 1.00 34.80 ? 611 HOH B O 1 HETATM 6050 O O . HOH IB 11 . ? -46.244 2.877 -59.353 1.00 45.22 ? 612 HOH B O 1 HETATM 6051 O O . HOH IB 11 . ? -48.031 7.349 -58.043 1.00 45.97 ? 613 HOH B O 1 HETATM 6052 O O . HOH IB 11 . ? -8.864 11.096 -56.512 1.00 26.40 ? 614 HOH B O 1 HETATM 6053 O O . HOH IB 11 . ? -36.569 2.942 -63.998 1.00 15.51 ? 615 HOH B O 1 HETATM 6054 O O . HOH IB 11 . ? -47.834 -7.359 -68.016 1.00 42.70 ? 616 HOH B O 1 HETATM 6055 O O . HOH IB 11 . ? -22.326 14.584 -57.237 1.00 20.33 ? 617 HOH B O 1 HETATM 6056 O O . HOH IB 11 . ? -8.732 6.016 -82.410 1.00 29.48 ? 618 HOH B O 1 HETATM 6057 O O . HOH IB 11 . ? -18.801 16.772 -52.749 1.00 29.22 ? 619 HOH B O 1 HETATM 6058 O O . HOH IB 11 . ? -23.433 2.280 -70.014 1.00 22.45 ? 620 HOH B O 1 HETATM 6059 O O . HOH IB 11 . ? -33.738 -0.856 -83.243 1.00 16.35 ? 621 HOH B O 1 HETATM 6060 O O . HOH IB 11 . ? -19.051 12.103 -68.823 1.00 22.41 ? 622 HOH B O 1 HETATM 6061 O O . HOH IB 11 . ? -13.895 -11.106 -65.018 1.00 60.39 ? 623 HOH B O 1 HETATM 6062 O O . HOH IB 11 . ? -38.585 6.396 -57.170 1.00 24.35 ? 624 HOH B O 1 HETATM 6063 O O . HOH IB 11 . ? -36.449 -7.591 -83.975 1.00 14.37 ? 625 HOH B O 1 HETATM 6064 O O . HOH IB 11 . ? -39.027 15.909 -46.331 1.00 23.90 ? 626 HOH B O 1 HETATM 6065 O O . HOH IB 11 . ? -25.831 7.301 -70.720 1.00 33.06 ? 627 HOH B O 1 HETATM 6066 O O . HOH IB 11 . ? -27.689 -18.907 -77.187 1.00 41.29 ? 628 HOH B O 1 HETATM 6067 O O . HOH IB 11 . ? -18.733 -5.649 -92.351 1.00 44.89 ? 629 HOH B O 1 HETATM 6068 O O . HOH IB 11 . ? -0.480 22.708 -70.407 1.00 39.75 ? 630 HOH B O 1 HETATM 6069 O O . HOH IB 11 . ? -37.958 6.240 -82.494 1.00 24.98 ? 631 HOH B O 1 HETATM 6070 O O . HOH IB 11 . ? -52.028 0.720 -65.205 1.00 73.82 ? 632 HOH B O 1 HETATM 6071 O O . HOH IB 11 . ? -9.208 18.736 -56.458 1.00 45.58 ? 633 HOH B O 1 HETATM 6072 O O . HOH IB 11 . ? -3.612 -1.231 -65.553 1.00 41.39 ? 634 HOH B O 1 HETATM 6073 O O . HOH IB 11 . ? -27.051 -1.893 -85.088 1.00 20.97 ? 635 HOH B O 1 HETATM 6074 O O . HOH IB 11 . ? -4.731 2.109 -80.817 1.00 24.84 ? 636 HOH B O 1 HETATM 6075 O O . HOH IB 11 . ? -5.710 -7.050 -82.019 1.00 34.49 ? 637 HOH B O 1 HETATM 6076 O O . HOH IB 11 . ? -17.288 14.990 -53.002 1.00 34.54 ? 638 HOH B O 1 HETATM 6077 O O . HOH IB 11 . ? -39.528 -8.949 -57.409 1.00 35.92 ? 639 HOH B O 1 HETATM 6078 O O . HOH IB 11 . ? -29.901 10.537 -62.097 1.00 25.70 ? 640 HOH B O 1 HETATM 6079 O O . HOH IB 11 . ? -40.813 -6.206 -57.245 1.00 37.00 ? 641 HOH B O 1 HETATM 6080 O O . HOH IB 11 . ? -40.720 12.127 -63.462 1.00 63.68 ? 642 HOH B O 1 HETATM 6081 O O . HOH IB 11 . ? -6.872 -1.183 -66.174 1.00 35.94 ? 643 HOH B O 1 HETATM 6082 O O . HOH IB 11 . ? -25.547 17.573 -72.979 1.00 40.62 ? 644 HOH B O 1 HETATM 6083 O O . HOH IB 11 . ? -19.867 -2.184 -55.588 1.00 16.08 ? 645 HOH B O 1 HETATM 6084 O O . HOH IB 11 . ? -0.323 -0.659 -72.872 1.00 39.59 ? 646 HOH B O 1 HETATM 6085 O O . HOH IB 11 . ? -26.242 -12.629 -56.918 1.00 34.86 ? 647 HOH B O 1 HETATM 6086 O O . HOH IB 11 . ? -36.087 -3.421 -66.568 1.00 11.62 ? 648 HOH B O 1 HETATM 6087 O O . HOH IB 11 . ? -23.774 1.153 -92.581 1.00 25.44 ? 649 HOH B O 1 HETATM 6088 O O . HOH IB 11 . ? -45.059 9.059 -81.741 1.00 56.62 ? 650 HOH B O 1 HETATM 6089 O O . HOH IB 11 . ? -41.158 -12.457 -85.252 1.00 41.62 ? 651 HOH B O 1 HETATM 6090 O O . HOH IB 11 . ? -40.038 3.069 -71.557 1.00 18.13 ? 652 HOH B O 1 HETATM 6091 O O . HOH IB 11 . ? -33.960 15.796 -53.568 1.00 39.80 ? 653 HOH B O 1 HETATM 6092 O O . HOH IB 11 . ? -28.391 -13.696 -57.440 1.00 32.28 ? 654 HOH B O 1 HETATM 6093 O O . HOH IB 11 . ? -15.863 -0.783 -50.583 1.00 42.09 ? 655 HOH B O 1 HETATM 6094 O O . HOH IB 11 . ? -16.996 -19.985 -72.492 1.00 30.63 ? 656 HOH B O 1 HETATM 6095 O O . HOH IB 11 . ? -48.593 2.894 -83.343 1.00 32.28 ? 657 HOH B O 1 HETATM 6096 O O . HOH IB 11 . ? -40.498 -6.980 -87.224 1.00 29.18 ? 658 HOH B O 1 HETATM 6097 O O . HOH IB 11 . ? -13.683 16.287 -54.114 1.00 45.10 ? 659 HOH B O 1 HETATM 6098 O O . HOH IB 11 . ? -4.872 20.439 -66.372 1.00 52.67 ? 660 HOH B O 1 HETATM 6099 O O . HOH IB 11 . ? -9.243 -13.671 -84.294 1.00 49.00 ? 661 HOH B O 1 HETATM 6100 O O . HOH IB 11 . ? -0.150 7.971 -79.524 1.00 52.11 ? 662 HOH B O 1 HETATM 6101 O O . HOH IB 11 . ? -16.297 10.409 -76.811 1.00 32.25 ? 663 HOH B O 1 HETATM 6102 O O . HOH IB 11 . ? -3.574 6.682 -58.682 1.00 51.95 ? 664 HOH B O 1 HETATM 6103 O O . HOH IB 11 . ? -28.908 -12.527 -83.464 1.00 36.41 ? 665 HOH B O 1 HETATM 6104 O O . HOH IB 11 . ? -0.843 10.500 -79.539 1.00 45.56 ? 666 HOH B O 1 HETATM 6105 O O . HOH IB 11 . ? -43.533 16.301 -71.641 1.00 55.97 ? 667 HOH B O 1 HETATM 6106 O O . HOH IB 11 . ? -18.901 24.993 -66.243 1.00 43.14 ? 668 HOH B O 1 HETATM 6107 O O . HOH IB 11 . ? -33.003 15.418 -56.823 1.00 44.91 ? 669 HOH B O 1 HETATM 6108 O O . HOH IB 11 . ? -8.237 -8.024 -72.123 1.00 39.37 ? 670 HOH B O 1 HETATM 6109 O O . HOH IB 11 . ? -3.001 14.957 -80.045 1.00 56.54 ? 671 HOH B O 1 HETATM 6110 O O . HOH IB 11 . ? -21.932 15.105 -82.541 1.00 40.99 ? 672 HOH B O 1 HETATM 6111 O O . HOH IB 11 . ? -1.796 15.537 -76.239 1.00 62.20 ? 673 HOH B O 1 HETATM 6112 O O . HOH IB 11 . ? -14.680 26.058 -64.190 1.00 44.49 ? 674 HOH B O 1 HETATM 6113 O O . HOH IB 11 . ? -13.893 11.480 -88.941 1.00 39.59 ? 675 HOH B O 1 HETATM 6114 O O . HOH IB 11 . ? -3.690 25.229 -74.604 1.00 48.91 ? 676 HOH B O 1 HETATM 6115 O O . HOH IB 11 . ? -25.783 -10.974 -91.639 1.00 58.88 ? 677 HOH B O 1 HETATM 6116 O O . HOH IB 11 . ? -1.686 -1.455 -70.955 1.00 31.94 ? 678 HOH B O 1 HETATM 6117 O O A HOH IB 11 . ? -24.255 -19.700 -71.116 0.51 29.10 ? 679 HOH B O 1 HETATM 6118 O O B HOH IB 11 . ? -22.779 -19.252 -72.433 0.49 28.67 ? 679 HOH B O 1 HETATM 6119 O O . HOH IB 11 . ? -50.192 -9.662 -76.168 1.00 42.90 ? 680 HOH B O 1 HETATM 6120 O O . HOH IB 11 . ? -53.936 -7.915 -81.923 1.00 24.82 ? 681 HOH B O 1 HETATM 6121 O O . HOH IB 11 . ? -11.475 -1.921 -52.970 1.00 48.80 ? 682 HOH B O 1 HETATM 6122 O O . HOH IB 11 . ? -32.278 22.657 -56.177 1.00 52.22 ? 683 HOH B O 1 HETATM 6123 O O . HOH IB 11 . ? -27.396 -2.987 -88.372 1.00 24.29 ? 684 HOH B O 1 HETATM 6124 O O . HOH IB 11 . ? -38.647 -19.792 -63.900 1.00 51.83 ? 685 HOH B O 1 HETATM 6125 O O . HOH IB 11 . ? -17.778 -3.895 -53.239 1.00 17.93 ? 686 HOH B O 1 HETATM 6126 O O . HOH IB 11 . ? -24.374 10.336 -85.591 1.00 50.25 ? 687 HOH B O 1 HETATM 6127 O O . HOH IB 11 . ? -32.383 9.537 -62.216 1.00 30.92 ? 688 HOH B O 1 HETATM 6128 O O . HOH IB 11 . ? -35.372 15.676 -41.368 1.00 40.36 ? 689 HOH B O 1 HETATM 6129 O O . HOH IB 11 . ? -45.072 -12.973 -64.335 1.00 51.33 ? 690 HOH B O 1 HETATM 6130 O O . HOH IB 11 . ? -7.594 -6.891 -67.812 1.00 41.56 ? 691 HOH B O 1 HETATM 6131 O O . HOH IB 11 . ? -20.491 -18.260 -81.429 1.00 58.42 ? 692 HOH B O 1 HETATM 6132 O O . HOH IB 11 . ? -43.089 14.163 -74.848 1.00 50.64 ? 693 HOH B O 1 HETATM 6133 O O . HOH IB 11 . ? -15.905 -9.220 -89.792 1.00 43.22 ? 694 HOH B O 1 HETATM 6134 O O . HOH IB 11 . ? -43.440 -14.517 -72.866 1.00 41.64 ? 695 HOH B O 1 HETATM 6135 O O . HOH IB 11 . ? -21.169 -16.503 -85.275 1.00 54.01 ? 696 HOH B O 1 HETATM 6136 O O . HOH IB 11 . ? -21.503 -11.660 -62.013 1.00 39.48 ? 697 HOH B O 1 HETATM 6137 O O A HOH IB 11 . ? -25.592 11.086 -83.835 0.49 23.95 ? 698 HOH B O 1 HETATM 6138 O O B HOH IB 11 . ? -25.572 12.215 -82.683 0.51 20.00 ? 698 HOH B O 1 HETATM 6139 O O . HOH IB 11 . ? -14.578 -7.351 -90.212 1.00 53.78 ? 699 HOH B O 1 HETATM 6140 O O . HOH IB 11 . ? -38.177 -12.537 -83.548 1.00 25.11 ? 700 HOH B O 1 HETATM 6141 O O . HOH IB 11 . ? -5.413 12.378 -59.381 1.00 54.91 ? 701 HOH B O 1 HETATM 6142 O O . HOH IB 11 . ? -30.000 13.376 -61.481 1.00 41.14 ? 702 HOH B O 1 HETATM 6143 O O . HOH IB 11 . ? -33.963 18.780 -41.113 1.00 36.60 ? 703 HOH B O 1 HETATM 6144 O O . HOH IB 11 . ? -25.705 2.802 -87.505 1.00 39.32 ? 704 HOH B O 1 HETATM 6145 O O . HOH IB 11 . ? -39.188 11.751 -61.192 1.00 43.59 ? 705 HOH B O 1 HETATM 6146 O O . HOH IB 11 . ? -45.409 11.253 -53.641 1.00 45.95 ? 706 HOH B O 1 HETATM 6147 O O . HOH IB 11 . ? -13.236 9.240 -89.793 1.00 48.94 ? 707 HOH B O 1 HETATM 6148 O O . HOH IB 11 . ? -2.835 18.099 -80.934 1.00 62.78 ? 708 HOH B O 1 HETATM 6149 O O . HOH IB 11 . ? -42.897 -16.614 -80.183 1.00 49.20 ? 709 HOH B O 1 HETATM 6150 O O . HOH IB 11 . ? -18.687 -7.755 -57.834 1.00 45.03 ? 710 HOH B O 1 HETATM 6151 O O . HOH IB 11 . ? -45.619 4.697 -50.117 1.00 44.49 ? 711 HOH B O 1 HETATM 6152 O O . HOH IB 11 . ? -4.157 16.595 -59.241 1.00 61.75 ? 712 HOH B O 1 HETATM 6153 O O . HOH IB 11 . ? -34.909 10.101 -66.941 1.00 49.89 ? 713 HOH B O 1 HETATM 6154 O O . HOH IB 11 . ? -30.773 -14.225 -55.954 1.00 51.74 ? 714 HOH B O 1 HETATM 6155 O O . HOH IB 11 . ? -26.354 -18.184 -82.079 1.00 52.49 ? 715 HOH B O 1 HETATM 6156 O O . HOH IB 11 . ? -28.514 -12.876 -52.574 1.00 45.49 ? 716 HOH B O 1 HETATM 6157 O O . HOH IB 11 . ? -16.616 0.224 -93.174 1.00 41.84 ? 717 HOH B O 1 HETATM 6158 O O . HOH IB 11 . ? -38.242 22.346 -58.266 1.00 50.54 ? 718 HOH B O 1 HETATM 6159 O O A HOH IB 11 . ? -22.819 -12.171 -60.208 0.56 28.54 ? 719 HOH B O 1 HETATM 6160 O O B HOH IB 11 . ? -22.560 -11.662 -58.773 0.44 23.23 ? 719 HOH B O 1 HETATM 6161 O O . HOH IB 11 . ? -27.938 8.001 -71.172 1.00 61.18 ? 720 HOH B O 1 HETATM 6162 O O . HOH IB 11 . ? -2.786 23.245 -67.436 1.00 74.14 ? 721 HOH B O 1 HETATM 6163 O O . HOH IB 11 . ? -2.127 3.058 -79.707 1.00 33.50 ? 722 HOH B O 1 HETATM 6164 O O . HOH IB 11 . ? -28.335 -16.561 -80.719 1.00 40.33 ? 723 HOH B O 1 HETATM 6165 O O . HOH IB 11 . ? -29.549 7.024 -73.512 1.00 51.88 ? 724 HOH B O 1 HETATM 6166 O O . HOH IB 11 . ? -10.994 -11.787 -65.386 1.00 54.33 ? 725 HOH B O 1 HETATM 6167 O O . HOH IB 11 . ? -7.817 -12.865 -79.695 1.00 47.33 ? 726 HOH B O 1 HETATM 6168 O O . HOH IB 11 . ? -34.772 4.934 -64.426 1.00 35.02 ? 727 HOH B O 1 HETATM 6169 O O . HOH IB 11 . ? -1.809 5.793 -79.167 1.00 24.67 ? 728 HOH B O 1 HETATM 6170 O O . HOH IB 11 . ? -28.847 9.137 -73.975 1.00 66.32 ? 729 HOH B O 1 HETATM 6171 O O . HOH IB 11 . ? -30.960 15.833 -58.170 1.00 56.59 ? 730 HOH B O 1 HETATM 6172 O O A HOH IB 11 . ? -14.026 1.436 -90.607 0.45 17.58 ? 731 HOH B O 1 HETATM 6173 O O B HOH IB 11 . ? -13.499 -0.431 -90.871 0.55 30.43 ? 731 HOH B O 1 HETATM 6174 O O . HOH IB 11 . ? -39.931 -11.326 -56.683 1.00 51.66 ? 732 HOH B O 1 HETATM 6175 O O . HOH IB 11 . ? -42.395 2.940 -47.450 1.00 48.68 ? 733 HOH B O 1 HETATM 6176 O O . HOH IB 11 . ? -0.022 14.940 -70.212 1.00 55.91 ? 734 HOH B O 1 HETATM 6177 O O . HOH IB 11 . ? -48.155 15.028 -59.243 1.00 51.96 ? 735 HOH B O 1 HETATM 6178 O O . HOH IB 11 . ? 0.310 12.705 -71.269 1.00 49.72 ? 736 HOH B O 1 HETATM 6179 O O A HOH IB 11 . ? -41.755 -23.257 -61.774 0.32 12.41 ? 737 HOH B O 1 HETATM 6180 O O B HOH IB 11 . ? -41.066 -21.048 -61.709 0.68 40.73 ? 737 HOH B O 1 HETATM 6181 O O . HOH IB 11 . ? -51.903 6.578 -75.185 1.00 62.04 ? 738 HOH B O 1 HETATM 6182 O O A HOH IB 11 . ? -3.331 10.179 -58.441 0.62 41.05 ? 739 HOH B O 1 HETATM 6183 O O B HOH IB 11 . ? -2.409 11.545 -58.948 0.38 24.33 ? 739 HOH B O 1 HETATM 6184 O O . HOH IB 11 . ? -50.400 2.662 -65.727 1.00 60.87 ? 740 HOH B O 1 HETATM 6185 O O . HOH IB 11 . ? 1.380 -3.816 -59.673 1.00 51.83 ? 741 HOH B O 1 HETATM 6186 O O . HOH IB 11 . ? -1.644 21.399 -65.723 1.00 53.84 ? 742 HOH B O 1 HETATM 6187 O O . HOH IB 11 . ? -32.519 12.311 -63.387 1.00 77.04 ? 743 HOH B O 1 HETATM 6188 O O . HOH IB 11 . ? -41.849 -15.061 -61.987 1.00 67.06 ? 744 HOH B O 1 HETATM 6189 O O . HOH IB 11 . ? -47.489 0.855 -57.910 1.00 54.44 ? 745 HOH B O 1 HETATM 6190 O O . HOH IB 11 . ? -0.188 3.805 -81.584 1.00 42.05 ? 746 HOH B O 1 HETATM 6191 O O . HOH IB 11 . ? -5.928 -9.474 -72.131 1.00 43.40 ? 747 HOH B O 1 HETATM 6192 O O . HOH IB 11 . ? -41.960 -11.247 -60.307 1.00 46.44 ? 748 HOH B O 1 HETATM 6193 O O . HOH IB 11 . ? -18.063 -11.438 -89.511 1.00 47.76 ? 749 HOH B O 1 HETATM 6194 O O . HOH IB 11 . ? -37.974 -3.138 -45.045 1.00 46.15 ? 750 HOH B O 1 HETATM 6195 O O . HOH IB 11 . ? -11.303 26.519 -67.152 1.00 53.60 ? 751 HOH B O 1 HETATM 6196 O O . HOH IB 11 . ? -23.989 -14.635 -60.056 1.00 49.79 ? 752 HOH B O 1 HETATM 6197 O O . HOH IB 11 . ? -50.400 -9.400 -68.796 1.00 60.14 ? 753 HOH B O 1 HETATM 6198 O O . HOH IB 11 . ? -50.707 5.784 -73.398 1.00 44.85 ? 754 HOH B O 1 HETATM 6199 O O . HOH IB 11 . ? -17.375 26.794 -64.061 1.00 50.00 ? 755 HOH B O 1 HETATM 6200 O O . HOH IB 11 . ? -21.195 -21.522 -74.252 1.00 53.38 ? 756 HOH B O 1 HETATM 6201 O O . HOH IB 11 . ? -49.930 3.670 -72.856 1.00 21.98 ? 757 HOH B O 1 HETATM 6202 O O . HOH IB 11 . ? -5.296 2.979 -54.244 1.00 53.06 ? 758 HOH B O 1 HETATM 6203 O O . HOH IB 11 . ? -33.745 12.849 -70.267 1.00 59.24 ? 759 HOH B O 1 HETATM 6204 O O . HOH IB 11 . ? -46.473 -5.884 -85.639 1.00 23.19 ? 760 HOH B O 1 HETATM 6205 O O . HOH IB 11 . ? -12.244 -12.525 -72.738 1.00 50.21 ? 761 HOH B O 1 HETATM 6206 O O . HOH IB 11 . ? -27.945 -12.844 -91.385 1.00 43.62 ? 762 HOH B O 1 HETATM 6207 O O . HOH IB 11 . ? -34.090 -10.278 -84.433 1.00 30.49 ? 763 HOH B O 1 HETATM 6208 O O . HOH IB 11 . ? -6.562 3.059 -50.297 1.00 59.56 ? 764 HOH B O 1 HETATM 6209 O O . HOH IB 11 . ? -43.418 -13.417 -62.382 1.00 61.04 ? 765 HOH B O 1 HETATM 6210 O O . HOH IB 11 . ? -48.506 -5.134 -57.876 1.00 59.26 ? 766 HOH B O 1 HETATM 6211 O O . HOH IB 11 . ? -36.083 -15.679 -54.994 1.00 42.18 ? 767 HOH B O 1 HETATM 6212 O O A HOH IB 11 . ? -49.129 -0.258 -68.985 0.61 40.85 ? 768 HOH B O 1 HETATM 6213 O O B HOH IB 11 . ? -48.566 1.961 -69.097 0.39 28.64 ? 768 HOH B O 1 HETATM 6214 O O . HOH IB 11 . ? -47.057 -7.363 -59.310 1.00 57.78 ? 769 HOH B O 1 HETATM 6215 O O . HOH IB 11 . ? -39.996 -18.308 -73.499 1.00 55.82 ? 770 HOH B O 1 HETATM 6216 O O . HOH IB 11 . ? -0.110 7.978 -71.842 1.00 45.54 ? 771 HOH B O 1 HETATM 6217 O O . HOH IB 11 . ? -23.415 20.976 -60.002 1.00 51.91 ? 772 HOH B O 1 HETATM 6218 O O . HOH IB 11 . ? -2.734 7.607 -56.344 1.00 44.00 ? 773 HOH B O 1 HETATM 6219 O O . HOH IB 11 . ? -28.520 -19.623 -79.887 1.00 60.30 ? 774 HOH B O 1 HETATM 6220 O O . HOH IB 11 . ? -6.948 -1.999 -56.118 1.00 43.68 ? 775 HOH B O 1 HETATM 6221 O O . HOH IB 11 . ? -51.475 -5.649 -64.988 1.00 43.18 ? 776 HOH B O 1 HETATM 6222 O O . HOH IB 11 . ? -17.765 -10.232 -61.810 1.00 43.95 ? 777 HOH B O 1 HETATM 6223 O O . HOH IB 11 . ? -24.458 21.559 -66.400 1.00 53.34 ? 778 HOH B O 1 HETATM 6224 O O . HOH IB 11 . ? -50.503 -8.303 -66.741 1.00 59.18 ? 779 HOH B O 1 HETATM 6225 O O . HOH IB 11 . ? 0.212 1.956 -72.082 1.00 35.61 ? 780 HOH B O 1 HETATM 6226 O O . HOH IB 11 . ? -2.668 11.041 -53.250 1.00 47.20 ? 781 HOH B O 1 HETATM 6227 O O . HOH IB 11 . ? -22.748 -22.834 -72.193 1.00 50.59 ? 782 HOH B O 1 HETATM 6228 O O . HOH IB 11 . ? -33.419 15.786 -64.734 1.00 49.15 ? 783 HOH B O 1 HETATM 6229 O O . HOH IB 11 . ? -42.091 -7.327 -54.836 1.00 47.54 ? 784 HOH B O 1 HETATM 6230 O O . HOH IB 11 . ? -33.105 17.542 -63.214 1.00 55.95 ? 785 HOH B O 1 HETATM 6231 O O . HOH IB 11 . ? -32.968 14.840 -61.597 1.00 51.93 ? 786 HOH B O 1 HETATM 6232 O O . HOH IB 11 . ? -35.433 13.885 -60.398 1.00 47.78 ? 787 HOH B O 1 HETATM 6233 O O . HOH IB 11 . ? -48.906 -7.557 -56.412 1.00 51.99 ? 788 HOH B 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 . PRO A 4 ? 1.0876 1.3753 1.2538 -0.0785 0.0152 -0.0673 30 PRO A N 2 C CA . PRO A 4 ? 1.1062 1.4115 1.2771 -0.0825 0.0252 -0.0726 30 PRO A CA 3 C C . PRO A 4 ? 1.1068 1.4093 1.2641 -0.1037 0.0308 -0.0711 30 PRO A C 4 O O . PRO A 4 ? 1.0427 1.3550 1.2038 -0.1105 0.0268 -0.0717 30 PRO A O 5 C CB . PRO A 4 ? 1.0803 1.4155 1.2752 -0.0689 0.0209 -0.0795 30 PRO A CB 6 C CG . PRO A 4 ? 1.0506 1.3778 1.2514 -0.0506 0.0116 -0.0776 30 PRO A CG 7 C CD . PRO A 4 ? 1.0366 1.3378 1.2205 -0.0591 0.0063 -0.0701 30 PRO A CD 8 N N . PHE A 5 ? 1.1334 1.4217 1.2737 -0.1141 0.0394 -0.0690 31 PHE A N 9 C CA . PHE A 5 ? 1.0722 1.3456 1.2047 -0.1083 0.0438 -0.0674 31 PHE A CA 10 C C . PHE A 5 ? 0.9340 1.1709 1.0405 -0.1198 0.0429 -0.0581 31 PHE A C 11 O O . PHE A 5 ? 0.8687 1.0899 0.9622 -0.1216 0.0477 -0.0555 31 PHE A O 12 C CB . PHE A 5 ? 1.1376 1.4251 1.2704 -0.1106 0.0545 -0.0733 31 PHE A CB 13 C CG . PHE A 5 ? 1.1691 1.4894 1.3268 -0.0969 0.0559 -0.0832 31 PHE A CG 14 C CD1 . PHE A 5 ? 1.1547 1.4847 1.3315 -0.0784 0.0478 -0.0854 31 PHE A CD1 15 C CD2 . PHE A 5 ? 1.1563 1.4958 1.3170 -0.1023 0.0650 -0.0902 31 PHE A CD2 16 C CE1 . PHE A 5 ? 1.1556 1.5117 1.3537 -0.0646 0.0479 -0.0939 31 PHE A CE1 17 C CE2 . PHE A 5 ? 1.1416 1.5097 1.3252 -0.0892 0.0661 -0.0997 31 PHE A CE2 18 C CZ . PHE A 5 ? 1.1560 1.5315 1.3584 -0.0698 0.0572 -0.1013 31 PHE A CZ 19 N N . GLU A 6 ? 0.8045 1.0265 0.9028 -0.1271 0.0362 -0.0532 32 GLU A N 20 C CA . GLU A 6 ? 0.5404 0.7264 0.6124 -0.1391 0.0347 -0.0447 32 GLU A CA 21 C C . GLU A 6 ? 0.3967 0.5533 0.4583 -0.1317 0.0308 -0.0388 32 GLU A C 22 O O . GLU A 6 ? 0.4174 0.5439 0.4576 -0.1396 0.0303 -0.0321 32 GLU A O 23 C CB . GLU A 6 ? 0.5212 0.7005 0.5884 -0.1472 0.0287 -0.0428 32 GLU A CB 24 C CG . GLU A 6 ? 0.6414 0.7839 0.6816 -0.1588 0.0269 -0.0351 32 GLU A CG 25 C CD . GLU A 6 ? 0.7759 0.9103 0.8120 -0.1644 0.0206 -0.0341 32 GLU A CD 26 O OE1 . GLU A 6 ? 0.7478 0.9064 0.7946 -0.1695 0.0213 -0.0388 32 GLU A OE1 27 O OE2 . GLU A 6 ? 0.8572 0.9610 0.8796 -0.1632 0.0150 -0.0291 32 GLU A OE2 28 N N . THR A 7 ? 0.2833 0.4419 0.3561 -0.1121 0.0267 -0.0401 33 THR A N 29 C CA . THR A 7 ? 0.2167 0.3440 0.2777 -0.1003 0.0222 -0.0340 33 THR A CA 30 C C . THR A 7 ? 0.2373 0.3658 0.3007 -0.0889 0.0263 -0.0355 33 THR A C 31 O O . THR A 7 ? 0.1539 0.3088 0.2315 -0.0855 0.0315 -0.0423 33 THR A O 32 C CB . THR A 7 ? 0.2161 0.3383 0.2831 -0.0879 0.0139 -0.0332 33 THR A CB 33 O OG1 . THR A 7 ? 0.1674 0.3161 0.2543 -0.0758 0.0132 -0.0390 33 THR A OG1 34 C CG2 . THR A 7 ? 0.2178 0.3369 0.2807 -0.0991 0.0094 -0.0325 33 THR A CG2 35 N N . LEU A 8 ? 0.1950 0.2955 0.2454 -0.0829 0.0239 -0.0299 34 LEU A N 36 C CA . LEU A 8 ? 0.1530 0.2510 0.2037 -0.0725 0.0267 -0.0310 34 LEU A CA 37 C C . LEU A 8 ? 0.1849 0.2983 0.2531 -0.0562 0.0248 -0.0359 34 LEU A C 38 O O . LEU A 8 ? 0.1657 0.2939 0.2423 -0.0501 0.0294 -0.0414 34 LEU A O 39 C CB . LEU A 8 ? 0.1548 0.2211 0.1903 -0.0690 0.0228 -0.0241 34 LEU A CB 40 C CG . LEU A 8 ? 0.1969 0.2431 0.2132 -0.0824 0.0230 -0.0184 34 LEU A CG 41 C CD1 . LEU A 8 ? 0.2150 0.2326 0.2217 -0.0757 0.0165 -0.0122 34 LEU A CD1 42 C CD2 . LEU A 8 ? 0.2009 0.2525 0.2097 -0.0895 0.0298 -0.0199 34 LEU A CD2 43 N N . ARG A 9 ? 0.1382 0.2463 0.2102 -0.0492 0.0177 -0.0339 35 ARG A N 44 C CA . ARG A 9 ? 0.1737 0.2916 0.2589 -0.0337 0.0143 -0.0370 35 ARG A CA 45 C C . ARG A 9 ? 0.1764 0.3284 0.2806 -0.0324 0.0167 -0.0450 35 ARG A C 46 O O . ARG A 9 ? 0.1260 0.2886 0.2411 -0.0198 0.0172 -0.0497 35 ARG A O 47 C CB . ARG A 9 ? 0.1905 0.2961 0.2732 -0.0287 0.0063 -0.0330 35 ARG A CB 48 C CG . ARG A 9 ? 0.2231 0.3367 0.3069 -0.0390 0.0033 -0.0331 35 ARG A CG 49 C CD . ARG A 9 ? 0.2389 0.3373 0.3169 -0.0341 -0.0040 -0.0295 35 ARG A CD 50 N NE . ARG A 9 ? 0.2450 0.3536 0.3330 -0.0209 -0.0092 -0.0313 35 ARG A NE 51 C CZ . ARG A 9 ? 0.2924 0.3874 0.3743 -0.0143 -0.0152 -0.0281 35 ARG A CZ 52 N NH1 . ARG A 9 ? 0.2002 0.2730 0.2679 -0.0189 -0.0157 -0.0241 35 ARG A NH1 53 N NH2 . ARG A 9 ? 0.3029 0.4058 0.3920 -0.0028 -0.0208 -0.0290 35 ARG A NH2 54 N N . ALA A 10 ? 0.1577 0.3271 0.2663 -0.0454 0.0182 -0.0471 36 ALA A N 55 C CA . ALA A 10 ? 0.1845 0.3907 0.3142 -0.0446 0.0206 -0.0556 36 ALA A CA 56 C C . ALA A 10 ? 0.2203 0.4409 0.3542 -0.0458 0.0307 -0.0617 36 ALA A C 57 O O . ALA A 10 ? 0.1472 0.3903 0.2987 -0.0345 0.0325 -0.0694 36 ALA A O 58 C CB . ALA A 10 ? 0.1331 0.3555 0.2663 -0.0606 0.0200 -0.0566 36 ALA A CB 59 N N . ALA A 11 ? 0.1711 0.3774 0.2877 -0.0592 0.0370 -0.0585 37 ALA A N 60 C CA . ALA A 11 ? 0.2029 0.4207 0.3188 -0.0636 0.0473 -0.0640 37 ALA A CA 61 C C . ALA A 11 ? 0.2005 0.4101 0.3175 -0.0469 0.0481 -0.0666 37 ALA A C 62 O O . ALA A 11 ? 0.1749 0.4034 0.3005 -0.0438 0.0558 -0.0751 37 ALA A O 63 C CB . ALA A 11 ? 0.1572 0.3557 0.2499 -0.0817 0.0517 -0.0581 37 ALA A CB 64 N N . ALA A 12 ? 0.1433 0.3249 0.2515 -0.0369 0.0407 -0.0600 38 ALA A N 65 C CA . ALA A 12 ? 0.1365 0.3053 0.2423 -0.0232 0.0409 -0.0614 38 ALA A CA 66 C C . ALA A 12 ? 0.2066 0.3917 0.3320 -0.0053 0.0384 -0.0685 38 ALA A C 67 O O . ALA A 12 ? 0.1432 0.3250 0.2694 0.0047 0.0412 -0.0731 38 ALA A O 68 C CB . ALA A 12 ? 0.1341 0.2687 0.2242 -0.0200 0.0342 -0.0521 38 ALA A CB 69 N N . ALA A 13 ? 0.1761 0.3769 0.3160 -0.0012 0.0323 -0.0693 39 ALA A N 70 C CA . ALA A 13 ? 0.2871 0.4995 0.4442 0.0173 0.0268 -0.0744 39 ALA A CA 71 C C . ALA A 13 ? 0.2339 0.4656 0.4037 0.0255 0.0343 -0.0855 39 ALA A C 72 O O . ALA A 13 ? 0.2037 0.4579 0.3787 0.0152 0.0440 -0.0920 39 ALA A O 73 C CB . ALA A 13 ? 0.2987 0.5335 0.4715 0.0174 0.0200 -0.0753 39 ALA A CB 74 N N . PRO A 14 ? 0.1512 0.3727 0.3244 0.0435 0.0305 -0.0880 40 PRO A N 75 C CA . PRO A 14 ? 0.1461 0.3411 0.3124 0.0556 0.0196 -0.0808 40 PRO A CA 76 C C . PRO A 14 ? 0.1872 0.3451 0.3299 0.0521 0.0196 -0.0727 40 PRO A C 77 O O . PRO A 14 ? 0.2041 0.3400 0.3399 0.0605 0.0119 -0.0670 40 PRO A O 78 C CB . PRO A 14 ? 0.2093 0.4119 0.3902 0.0753 0.0172 -0.0890 40 PRO A CB 79 C CG . PRO A 14 ? 0.2292 0.4418 0.4109 0.0721 0.0292 -0.0978 40 PRO A CG 80 C CD . PRO A 14 ? 0.2032 0.4398 0.3876 0.0532 0.0377 -0.0996 40 PRO A CD 81 N N . ARG A 15 ? 0.1804 0.3320 0.3109 0.0399 0.0277 -0.0723 41 ARG A N 82 C CA . ARG A 15 ? 0.1611 0.2809 0.2712 0.0354 0.0266 -0.0644 41 ARG A CA 83 C C . ARG A 15 ? 0.1808 0.2899 0.2835 0.0273 0.0210 -0.0550 41 ARG A C 84 O O . ARG A 15 ? 0.1283 0.2538 0.2377 0.0205 0.0203 -0.0549 41 ARG A O 85 C CB . ARG A 15 ? 0.1758 0.2927 0.2744 0.0242 0.0354 -0.0662 41 ARG A CB 86 C CG . ARG A 15 ? 0.1802 0.3071 0.2838 0.0308 0.0425 -0.0766 41 ARG A CG 87 C CD . ARG A 15 ? 0.1588 0.2797 0.2466 0.0182 0.0504 -0.0775 41 ARG A CD 88 N NE . ARG A 15 ? 0.2026 0.3315 0.2934 0.0246 0.0578 -0.0884 41 ARG A NE 89 C CZ . ARG A 15 ? 0.2565 0.4146 0.3598 0.0236 0.0661 -0.0986 41 ARG A CZ 90 N NH1 . ARG A 15 ? 0.2557 0.4376 0.3694 0.0152 0.0677 -0.0985 41 ARG A NH1 91 N NH2 . ARG A 15 ? 0.3212 0.4851 0.4267 0.0305 0.0731 -0.1096 41 ARG A NH2 92 N N . TYR A 16 ? 0.1317 0.2138 0.2205 0.0273 0.0174 -0.0479 42 TYR A N 93 C CA . TYR A 16 ? 0.1266 0.1983 0.2080 0.0195 0.0134 -0.0402 42 TYR A CA 94 C C . TYR A 16 ? 0.1496 0.2140 0.2195 0.0061 0.0177 -0.0373 42 TYR A C 95 O O . TYR A 16 ? 0.1313 0.1929 0.1956 0.0036 0.0226 -0.0395 42 TYR A O 96 C CB . TYR A 16 ? 0.1270 0.1758 0.2006 0.0260 0.0075 -0.0344 42 TYR A CB 97 C CG . TYR A 16 ? 0.1303 0.1594 0.1934 0.0268 0.0094 -0.0329 42 TYR A CG 98 C CD1 . TYR A 16 ? 0.1284 0.1456 0.1812 0.0175 0.0110 -0.0287 42 TYR A CD1 99 C CD2 . TYR A 16 ? 0.1512 0.1726 0.2145 0.0371 0.0089 -0.0358 42 TYR A CD2 100 C CE1 . TYR A 16 ? 0.1318 0.1335 0.1763 0.0176 0.0120 -0.0277 42 TYR A CE1 101 C CE2 . TYR A 16 ? 0.1581 0.1617 0.2115 0.0364 0.0105 -0.0349 42 TYR A CE2 102 C CZ . TYR A 16 ? 0.2802 0.2754 0.3248 0.0263 0.0120 -0.0309 42 TYR A CZ 103 O OH . TYR A 16 ? 0.1445 0.1242 0.1803 0.0251 0.0127 -0.0302 42 TYR A OH 104 N N . PHE A 17 ? 0.1456 0.2058 0.2109 -0.0024 0.0153 -0.0324 43 PHE A N 105 C CA . PHE A 17 ? 0.1324 0.1797 0.1850 -0.0134 0.0169 -0.0282 43 PHE A CA 106 C C . PHE A 17 ? 0.1279 0.1565 0.1741 -0.0129 0.0115 -0.0220 43 PHE A C 107 O O . PHE A 17 ? 0.1420 0.1729 0.1905 -0.0146 0.0085 -0.0207 43 PHE A O 108 C CB . PHE A 17 ? 0.1322 0.1924 0.1841 -0.0263 0.0205 -0.0293 43 PHE A CB 109 C CG . PHE A 17 ? 0.1725 0.2200 0.2097 -0.0367 0.0229 -0.0260 43 PHE A CG 110 C CD1 . PHE A 17 ? 0.1662 0.1926 0.1923 -0.0410 0.0184 -0.0192 43 PHE A CD1 111 C CD2 . PHE A 17 ? 0.1558 0.2116 0.1895 -0.0415 0.0293 -0.0298 43 PHE A CD2 112 C CE1 . PHE A 17 ? 0.2001 0.2132 0.2119 -0.0495 0.0188 -0.0155 43 PHE A CE1 113 C CE2 . PHE A 17 ? 0.2061 0.2483 0.2235 -0.0514 0.0304 -0.0259 43 PHE A CE2 114 C CZ . PHE A 17 ? 0.1617 0.1820 0.1682 -0.0551 0.0244 -0.0183 43 PHE A CZ 115 N N . GLY A 18 ? 0.1343 0.1456 0.1731 -0.0107 0.0106 -0.0190 44 GLY A N 116 C CA . GLY A 18 ? 0.1231 0.1194 0.1585 -0.0080 0.0064 -0.0147 44 GLY A CA 117 C C . GLY A 18 ? 0.1399 0.1221 0.1668 -0.0142 0.0051 -0.0106 44 GLY A C 118 O O . GLY A 18 ? 0.1320 0.1130 0.1530 -0.0211 0.0065 -0.0099 44 GLY A O 119 N N . ALA A 19 ? 0.1243 0.0955 0.1502 -0.0115 0.0022 -0.0081 45 ALA A N 120 C CA . ALA A 19 ? 0.1450 0.1031 0.1655 -0.0147 0.0000 -0.0049 45 ALA A CA 121 C C . ALA A 19 ? 0.1246 0.0743 0.1469 -0.0089 -0.0013 -0.0041 45 ALA A C 122 O O . ALA A 19 ? 0.1246 0.0758 0.1498 -0.0046 -0.0008 -0.0050 45 ALA A O 123 C CB . ALA A 19 ? 0.1334 0.0880 0.1510 -0.0201 -0.0018 -0.0039 45 ALA A CB 124 N N . ALA A 20 ? 0.1271 0.0685 0.1475 -0.0095 -0.0031 -0.0023 46 ALA A N 125 C CA . ALA A 20 ? 0.1441 0.0799 0.1681 -0.0055 -0.0041 -0.0021 46 ALA A CA 126 C C . ALA A 20 ? 0.1592 0.0914 0.1839 -0.0053 -0.0048 -0.0024 46 ALA A C 127 O O . ALA A 20 ? 0.1752 0.1021 0.1965 -0.0086 -0.0071 -0.0014 46 ALA A O 128 C CB . ALA A 20 ? 0.1281 0.0584 0.1518 -0.0061 -0.0070 -0.0005 46 ALA A CB 129 N N . LEU A 21 ? 0.1365 0.0697 0.1635 -0.0021 -0.0029 -0.0039 47 LEU A N 130 C CA . LEU A 21 ? 0.1271 0.0568 0.1535 -0.0020 -0.0028 -0.0054 47 LEU A CA 131 C C . LEU A 21 ? 0.1680 0.0952 0.1990 0.0013 -0.0014 -0.0070 47 LEU A C 132 O O . LEU A 21 ? 0.2051 0.1351 0.2378 0.0028 0.0011 -0.0072 47 LEU A O 133 C CB . LEU A 21 ? 0.1427 0.0770 0.1663 -0.0022 -0.0016 -0.0063 47 LEU A CB 134 C CG . LEU A 21 ? 0.1685 0.1101 0.1908 -0.0051 -0.0027 -0.0060 47 LEU A CG 135 C CD1 . LEU A 21 ? 0.1529 0.1001 0.1738 -0.0038 -0.0030 -0.0070 47 LEU A CD1 136 C CD2 . LEU A 21 ? 0.1320 0.0705 0.1515 -0.0109 -0.0044 -0.0057 47 LEU A CD2 137 N N . GLY A 22 ? 0.1411 0.0627 0.1741 0.0023 -0.0030 -0.0084 48 GLY A N 138 C CA . GLY A 22 ? 0.1642 0.0864 0.2042 0.0060 -0.0010 -0.0114 48 GLY A CA 139 C C . GLY A 22 ? 0.1621 0.0829 0.1995 0.0064 0.0025 -0.0152 48 GLY A C 140 O O . GLY A 22 ? 0.1635 0.0784 0.1951 0.0048 0.0011 -0.0160 48 GLY A O 141 N N . VAL A 23 ? 0.1364 0.0621 0.1766 0.0074 0.0074 -0.0177 49 VAL A N 142 C CA . VAL A 23 ? 0.1812 0.1058 0.2175 0.0072 0.0117 -0.0221 49 VAL A CA 143 C C . VAL A 23 ? 0.1514 0.0695 0.1896 0.0100 0.0106 -0.0266 49 VAL A C 144 O O . VAL A 23 ? 0.1587 0.0714 0.1885 0.0082 0.0113 -0.0288 49 VAL A O 145 C CB . VAL A 23 ? 0.1706 0.1020 0.2102 0.0067 0.0181 -0.0246 49 VAL A CB 146 C CG1 . VAL A 23 ? 0.2180 0.1486 0.2541 0.0066 0.0235 -0.0307 49 VAL A CG1 147 C CG2 . VAL A 23 ? 0.2295 0.1616 0.2611 0.0031 0.0191 -0.0203 49 VAL A CG2 148 N N . PRO A 24 ? 0.1740 0.0915 0.2226 0.0146 0.0081 -0.0281 50 PRO A N 149 C CA . PRO A 24 ? 0.1638 0.0721 0.2133 0.0185 0.0065 -0.0327 50 PRO A CA 150 C C . PRO A 24 ? 0.1710 0.0663 0.2092 0.0150 0.0015 -0.0300 50 PRO A C 151 O O . PRO A 24 ? 0.1904 0.0764 0.2237 0.0156 0.0019 -0.0345 50 PRO A O 152 C CB . PRO A 24 ? 0.1643 0.0740 0.2273 0.0250 0.0023 -0.0333 50 PRO A CB 153 C CG . PRO A 24 ? 0.2770 0.2011 0.3480 0.0238 0.0051 -0.0318 50 PRO A CG 154 C CD . PRO A 24 ? 0.1875 0.1116 0.2472 0.0171 0.0060 -0.0263 50 PRO A CD 155 N N . HIS A 25 ? 0.1886 0.0836 0.2224 0.0107 -0.0024 -0.0237 51 HIS A N 156 C CA . HIS A 25 ? 0.1771 0.0622 0.2004 0.0053 -0.0063 -0.0213 51 HIS A CA 157 C C . HIS A 25 ? 0.1732 0.0619 0.1884 0.0001 -0.0034 -0.0225 51 HIS A C 158 O O . HIS A 25 ? 0.2006 0.0805 0.2080 -0.0036 -0.0049 -0.0244 51 HIS A O 159 C CB . HIS A 25 ? 0.1695 0.0553 0.1910 0.0016 -0.0104 -0.0149 51 HIS A CB 160 C CG . HIS A 25 ? 0.1701 0.0536 0.1982 0.0060 -0.0143 -0.0129 51 HIS A CG 161 N ND1 . HIS A 25 ? 0.2587 0.1340 0.2876 0.0109 -0.0175 -0.0141 51 HIS A ND1 162 C CD2 . HIS A 25 ? 0.2339 0.1249 0.2663 0.0064 -0.0153 -0.0096 51 HIS A CD2 163 C CE1 . HIS A 25 ? 0.2246 0.1032 0.2591 0.0141 -0.0211 -0.0114 51 HIS A CE1 164 N NE2 . HIS A 25 ? 0.2158 0.1027 0.2524 0.0110 -0.0201 -0.0089 51 HIS A NE2 165 N N . LEU A 26 ? 0.1631 0.0634 0.1793 -0.0004 -0.0001 -0.0213 52 LEU A N 166 C CA . LEU A 26 ? 0.1642 0.0685 0.1728 -0.0041 0.0013 -0.0221 52 LEU A CA 167 C C . LEU A 26 ? 0.1757 0.0737 0.1787 -0.0039 0.0040 -0.0281 52 LEU A C 168 O O . LEU A 26 ? 0.1835 0.0784 0.1778 -0.0085 0.0027 -0.0297 52 LEU A O 169 C CB . LEU A 26 ? 0.1554 0.0696 0.1651 -0.0030 0.0037 -0.0198 52 LEU A CB 170 C CG . LEU A 26 ? 0.2199 0.1406 0.2332 -0.0032 0.0015 -0.0150 52 LEU A CG 171 C CD1 . LEU A 26 ? 0.2101 0.1362 0.2230 -0.0013 0.0036 -0.0133 52 LEU A CD1 172 C CD2 . LEU A 26 ? 0.2204 0.1444 0.2304 -0.0077 -0.0019 -0.0136 52 LEU A CD2 173 N N . LEU A 27 ? 0.1778 0.0749 0.1862 0.0010 0.0081 -0.0322 53 LEU A N 174 C CA . LEU A 27 ? 0.1902 0.0821 0.1935 0.0016 0.0122 -0.0394 53 LEU A CA 175 C C . LEU A 27 ? 0.2039 0.0818 0.2061 0.0033 0.0095 -0.0437 53 LEU A C 176 O O . LEU A 27 ? 0.2162 0.0880 0.2145 0.0048 0.0130 -0.0511 53 LEU A O 177 C CB . LEU A 27 ? 0.2850 0.1842 0.2955 0.0057 0.0189 -0.0433 53 LEU A CB 178 C CG . LEU A 27 ? 0.4022 0.3116 0.4109 0.0031 0.0221 -0.0395 53 LEU A CG 179 C CD1 . LEU A 27 ? 0.3080 0.2235 0.3203 0.0043 0.0303 -0.0449 53 LEU A CD1 180 C CD2 . LEU A 27 ? 0.3550 0.2634 0.3496 -0.0024 0.0202 -0.0363 53 LEU A CD2 181 N N . ASN A 28 ? 0.2033 0.0745 0.2073 0.0028 0.0035 -0.0394 54 ASN A N 182 C CA . ASN A 28 ? 0.2234 0.0770 0.2240 0.0038 -0.0005 -0.0421 54 ASN A CA 183 C C . ASN A 28 ? 0.3063 0.1518 0.2939 -0.0053 -0.0038 -0.0409 54 ASN A C 184 O O . ASN A 28 ? 0.2467 0.0765 0.2291 -0.0077 -0.0086 -0.0400 54 ASN A O 185 C CB . ASN A 28 ? 0.2182 0.0676 0.2254 0.0073 -0.0058 -0.0370 54 ASN A CB 186 C CG . ASN A 28 ? 0.2656 0.1027 0.2708 0.0124 -0.0075 -0.0386 54 ASN A CG 187 O OD1 . ASN A 28 ? 0.2471 0.0792 0.2514 0.0168 -0.0043 -0.0456 54 ASN A OD1 188 N ND2 . ASN A 28 ? 0.2392 0.0713 0.2436 0.0117 -0.0126 -0.0323 54 ASN A ND2 189 N N . PHE A 29 ? 0.2234 0.0793 0.2054 -0.0109 -0.0018 -0.0405 55 PHE A N 190 C CA . PHE A 29 ? 0.2298 0.0837 0.2019 -0.0205 -0.0053 -0.0393 55 PHE A CA 191 C C . PHE A 29 ? 0.3968 0.2314 0.3585 -0.0238 -0.0069 -0.0450 55 PHE A C 192 O O . PHE A 29 ? 0.2781 0.1051 0.2326 -0.0322 -0.0111 -0.0434 55 PHE A O 193 C CB . PHE A 29 ? 0.2388 0.1072 0.2073 -0.0238 -0.0038 -0.0390 55 PHE A CB 194 C CG . PHE A 29 ? 0.2710 0.1416 0.2317 -0.0334 -0.0079 -0.0386 55 PHE A CG 195 C CD1 . PHE A 29 ? 0.2239 0.1005 0.1879 -0.0389 -0.0115 -0.0337 55 PHE A CD1 196 C CD2 . PHE A 29 ? 0.3199 0.1883 0.2699 -0.0376 -0.0080 -0.0434 55 PHE A CD2 197 C CE1 . PHE A 29 ? 0.3013 0.1837 0.2606 -0.0485 -0.0150 -0.0339 55 PHE A CE1 198 C CE2 . PHE A 29 ? 0.3608 0.2336 0.3050 -0.0470 -0.0126 -0.0433 55 PHE A CE2 199 C CZ . PHE A 29 ? 0.3107 0.1915 0.2607 -0.0524 -0.0161 -0.0387 55 PHE A CZ 200 N N . THR A 30 ? 0.2623 0.0888 0.2229 -0.0177 -0.0032 -0.0524 56 THR A N 201 C CA . THR A 30 ? 0.2839 0.0941 0.2367 -0.0191 -0.0044 -0.0584 56 THR A CA 202 C C . THR A 30 ? 0.3132 0.1144 0.2717 -0.0173 -0.0087 -0.0545 56 THR A C 203 O O . THR A 30 ? 0.3541 0.1462 0.3049 -0.0243 -0.0121 -0.0536 56 THR A O 204 C CB . THR A 30 ? 0.3836 0.1918 0.3373 -0.0113 0.0014 -0.0678 56 THR A CB 205 O OG1 . THR A 30 ? 0.4297 0.2455 0.3739 -0.0158 0.0065 -0.0709 56 THR A OG1 206 C CG2 . THR A 30 ? 0.4114 0.2058 0.3615 -0.0106 -0.0004 -0.0737 56 THR A CG2 207 N N . HIS A 31 ? 0.2835 0.0868 0.2534 -0.0088 -0.0080 -0.0519 57 HIS A N 208 C CA . HIS A 31 ? 0.3552 0.1477 0.3267 -0.0064 -0.0113 -0.0481 57 HIS A CA 209 C C . HIS A 31 ? 0.3220 0.1163 0.2911 -0.0130 -0.0163 -0.0385 57 HIS A C 210 O O . HIS A 31 ? 0.3329 0.1158 0.2975 -0.0147 -0.0202 -0.0347 57 HIS A O 211 C CB . HIS A 31 ? 0.2951 0.0880 0.2764 0.0059 -0.0087 -0.0498 57 HIS A CB 212 C CG . HIS A 31 ? 0.3839 0.1755 0.3659 0.0122 -0.0022 -0.0597 57 HIS A CG 213 N ND1 . HIS A 31 ? 0.4931 0.2718 0.4702 0.0119 -0.0009 -0.0667 57 HIS A ND1 214 C CD2 . HIS A 31 ? 0.4958 0.2975 0.4803 0.0182 0.0029 -0.0641 57 HIS A CD2 215 C CE1 . HIS A 31 ? 0.5500 0.3304 0.5258 0.0175 0.0063 -0.0752 57 HIS A CE1 216 N NE2 . HIS A 31 ? 0.5305 0.3242 0.5082 0.0220 0.0072 -0.0733 57 HIS A NE2 217 N N . ASP A 32 ? 0.2711 0.0787 0.2417 -0.0169 -0.0159 -0.0351 58 ASP A N 218 C CA . ASP A 32 ? 0.2650 0.0767 0.2339 -0.0234 -0.0192 -0.0271 58 ASP A CA 219 C C . ASP A 32 ? 0.2910 0.1146 0.2572 -0.0316 -0.0184 -0.0263 58 ASP A C 220 O O . ASP A 32 ? 0.2703 0.1049 0.2422 -0.0300 -0.0177 -0.0236 58 ASP A O 221 C CB . ASP A 32 ? 0.2545 0.0715 0.2321 -0.0160 -0.0198 -0.0227 58 ASP A CB 222 C CG . ASP A 32 ? 0.4623 0.2814 0.4360 -0.0229 -0.0231 -0.0151 58 ASP A CG 223 O OD1 . ASP A 32 ? 0.4297 0.2449 0.3942 -0.0331 -0.0245 -0.0133 58 ASP A OD1 224 O OD2 . ASP A 32 ? 0.4141 0.2394 0.3934 -0.0189 -0.0239 -0.0114 58 ASP A OD2 225 N N . PRO A 33 ? 0.2711 0.0929 0.2287 -0.0404 -0.0189 -0.0289 59 PRO A N 226 C CA . PRO A 33 ? 0.2861 0.1227 0.2425 -0.0478 -0.0183 -0.0288 59 PRO A CA 227 C C . PRO A 33 ? 0.2750 0.1255 0.2358 -0.0534 -0.0190 -0.0225 59 PRO A C 228 O O . PRO A 33 ? 0.2305 0.1023 0.1984 -0.0531 -0.0173 -0.0216 59 PRO A O 229 C CB . PRO A 33 ? 0.2684 0.0990 0.2146 -0.0572 -0.0198 -0.0329 59 PRO A CB 230 C CG . PRO A 33 ? 0.3032 0.1174 0.2455 -0.0563 -0.0214 -0.0324 59 PRO A CG 231 C CD . PRO A 33 ? 0.2833 0.0914 0.2330 -0.0434 -0.0202 -0.0323 59 PRO A CD 232 N N . LEU A 34 ? 0.3012 0.1413 0.2580 -0.0575 -0.0213 -0.0184 60 LEU A N 233 C CA . LEU A 34 ? 0.3104 0.1614 0.2682 -0.0653 -0.0212 -0.0135 60 LEU A CA 234 C C . LEU A 34 ? 0.2769 0.1440 0.2462 -0.0564 -0.0187 -0.0110 60 LEU A C 235 O O . LEU A 34 ? 0.2275 0.1112 0.2009 -0.0604 -0.0170 -0.0088 60 LEU A O 236 C CB . LEU A 34 ? 0.2601 0.1005 0.2108 -0.0694 -0.0229 -0.0089 60 LEU A CB 237 C CG . LEU A 34 ? 0.4640 0.2971 0.4050 -0.0792 -0.0241 -0.0099 60 LEU A CG 238 C CD1 . LEU A 34 ? 0.3808 0.2031 0.3123 -0.0846 -0.0258 -0.0044 60 LEU A CD1 239 C CD2 . LEU A 34 ? 0.4768 0.3285 0.4198 -0.0902 -0.0225 -0.0123 60 LEU A CD2 240 N N . PHE A 35 ? 0.2420 0.1049 0.2165 -0.0449 -0.0182 -0.0120 61 PHE A N 241 C CA . PHE A 35 ? 0.2807 0.1578 0.2650 -0.0378 -0.0160 -0.0100 61 PHE A CA 242 C C . PHE A 35 ? 0.2765 0.1743 0.2669 -0.0372 -0.0131 -0.0117 61 PHE A C 243 O O . PHE A 35 ? 0.2480 0.1604 0.2431 -0.0385 -0.0118 -0.0097 61 PHE A O 244 C CB . PHE A 35 ? 0.2117 0.0823 0.2015 -0.0269 -0.0158 -0.0113 61 PHE A CB 245 C CG . PHE A 35 ? 0.2417 0.1245 0.2401 -0.0215 -0.0141 -0.0089 61 PHE A CG 246 C CD1 . PHE A 35 ? 0.1683 0.0651 0.1728 -0.0175 -0.0105 -0.0104 61 PHE A CD1 247 C CD2 . PHE A 35 ? 0.1834 0.0619 0.1814 -0.0214 -0.0167 -0.0048 61 PHE A CD2 248 C CE1 . PHE A 35 ? 0.2669 0.1724 0.2778 -0.0134 -0.0090 -0.0085 61 PHE A CE1 249 C CE2 . PHE A 35 ? 0.2278 0.1167 0.2325 -0.0174 -0.0154 -0.0032 61 PHE A CE2 250 C CZ . PHE A 35 ? 0.2005 0.1026 0.2119 -0.0135 -0.0113 -0.0053 61 PHE A CZ 251 N N . ASP A 36 ? 0.2011 0.0994 0.1905 -0.0350 -0.0123 -0.0155 62 ASP A N 252 C CA . ASP A 36 ? 0.1770 0.0921 0.1702 -0.0338 -0.0113 -0.0164 62 ASP A CA 253 C C . ASP A 36 ? 0.2941 0.2217 0.2874 -0.0424 -0.0131 -0.0163 62 ASP A C 254 O O . ASP A 36 ? 0.1685 0.1135 0.1685 -0.0408 -0.0130 -0.0158 62 ASP A O 255 C CB . ASP A 36 ? 0.1818 0.0929 0.1706 -0.0310 -0.0105 -0.0203 62 ASP A CB 256 C CG . ASP A 36 ? 0.3162 0.2221 0.3077 -0.0225 -0.0073 -0.0211 62 ASP A CG 257 O OD1 . ASP A 36 ? 0.2465 0.1541 0.2446 -0.0184 -0.0064 -0.0183 62 ASP A OD1 258 O OD2 . ASP A 36 ? 0.2620 0.1631 0.2488 -0.0208 -0.0053 -0.0250 62 ASP A OD2 259 N N . VAL A 37 ? 0.2089 0.1278 0.1952 -0.0516 -0.0148 -0.0173 63 VAL A N 260 C CA . VAL A 37 ? 0.2357 0.1685 0.2231 -0.0617 -0.0161 -0.0179 63 VAL A CA 261 C C . VAL A 37 ? 0.2941 0.2403 0.2882 -0.0638 -0.0141 -0.0151 63 VAL A C 262 O O . VAL A 37 ? 0.2143 0.1827 0.2172 -0.0652 -0.0136 -0.0162 63 VAL A O 263 C CB . VAL A 37 ? 0.2420 0.1601 0.2186 -0.0731 -0.0182 -0.0194 63 VAL A CB 264 C CG1 . VAL A 37 ? 0.3319 0.2663 0.3108 -0.0858 -0.0186 -0.0196 63 VAL A CG1 265 C CG2 . VAL A 37 ? 0.2768 0.1850 0.2464 -0.0723 -0.0200 -0.0240 63 VAL A CG2 266 N N . THR A 38 ? 0.2035 0.1367 0.1937 -0.0637 -0.0130 -0.0119 64 THR A N 267 C CA . THR A 38 ? 0.1851 0.1288 0.1786 -0.0667 -0.0106 -0.0095 64 THR A CA 268 C C . THR A 38 ? 0.2726 0.2329 0.2774 -0.0563 -0.0085 -0.0101 64 THR A C 269 O O . THR A 38 ? 0.1830 0.1619 0.1948 -0.0579 -0.0062 -0.0111 64 THR A O 270 C CB . THR A 38 ? 0.1951 0.1190 0.1795 -0.0684 -0.0112 -0.0054 64 THR A CB 271 O OG1 . THR A 38 ? 0.2679 0.1735 0.2402 -0.0783 -0.0139 -0.0046 64 THR A OG1 272 C CG2 . THR A 38 ? 0.2323 0.1669 0.2175 -0.0727 -0.0082 -0.0032 64 THR A CG2 273 N N . ALA A 39 ? 0.1939 0.1474 0.2002 -0.0460 -0.0091 -0.0101 65 ALA A N 274 C CA . ALA A 39 ? 0.2015 0.1664 0.2159 -0.0367 -0.0078 -0.0103 65 ALA A CA 275 C C . ALA A 39 ? 0.2868 0.2715 0.3085 -0.0362 -0.0087 -0.0129 65 ALA A C 276 O O . ALA A 39 ? 0.2640 0.2630 0.2934 -0.0327 -0.0073 -0.0136 65 ALA A O 277 C CB . ALA A 39 ? 0.1462 0.1001 0.1593 -0.0283 -0.0080 -0.0100 65 ALA A CB 278 N N . VAL A 40 ? 0.1668 0.1522 0.1860 -0.0393 -0.0116 -0.0147 66 VAL A N 279 C CA . VAL A 40 ? 0.2137 0.2182 0.2401 -0.0381 -0.0143 -0.0169 66 VAL A CA 280 C C . VAL A 40 ? 0.2315 0.2562 0.2661 -0.0456 -0.0133 -0.0191 66 VAL A C 281 O O . VAL A 40 ? 0.2271 0.2716 0.2731 -0.0408 -0.0136 -0.0210 66 VAL A O 282 C CB . VAL A 40 ? 0.2414 0.2409 0.2611 -0.0409 -0.0183 -0.0185 66 VAL A CB 283 C CG1 . VAL A 40 ? 0.2900 0.3109 0.3171 -0.0416 -0.0228 -0.0208 66 VAL A CG1 284 C CG2 . VAL A 40 ? 0.2904 0.2749 0.3031 -0.0329 -0.0182 -0.0173 66 VAL A CG2 285 N N . LEU A 41 ? 0.2217 0.2413 0.2507 -0.0575 -0.0119 -0.0191 67 LEU A N 286 C CA . LEU A 41 ? 0.2042 0.2438 0.2399 -0.0675 -0.0100 -0.0215 67 LEU A CA 287 C C . LEU A 41 ? 0.2633 0.3136 0.3052 -0.0656 -0.0047 -0.0216 67 LEU A C 288 O O . LEU A 41 ? 0.1560 0.2316 0.2100 -0.0672 -0.0027 -0.0254 67 LEU A O 289 C CB . LEU A 41 ? 0.2132 0.2402 0.2376 -0.0825 -0.0099 -0.0208 67 LEU A CB 290 C CG . LEU A 41 ? 0.3260 0.3455 0.3442 -0.0870 -0.0147 -0.0225 67 LEU A CG 291 C CD1 . LEU A 41 ? 0.3625 0.3669 0.3683 -0.1027 -0.0145 -0.0220 67 LEU A CD1 292 C CD2 . LEU A 41 ? 0.3517 0.3976 0.3820 -0.0864 -0.0183 -0.0265 67 LEU A CD2 293 N N . GLN A 42 ? 0.1516 0.1841 0.1859 -0.0622 -0.0025 -0.0182 68 GLN A N 294 C CA . GLN A 42 ? 0.2192 0.2579 0.2546 -0.0638 0.0026 -0.0183 68 GLN A CA 295 C C . GLN A 42 ? 0.2357 0.2786 0.2780 -0.0504 0.0040 -0.0191 68 GLN A C 296 O O . GLN A 42 ? 0.1894 0.2451 0.2365 -0.0504 0.0085 -0.0217 68 GLN A O 297 C CB . GLN A 42 ? 0.1618 0.1771 0.1817 -0.0712 0.0034 -0.0136 68 GLN A CB 298 C CG . GLN A 42 ? 0.2373 0.2465 0.2477 -0.0869 0.0031 -0.0126 68 GLN A CG 299 C CD . GLN A 42 ? 0.2971 0.3297 0.3124 -0.0985 0.0083 -0.0158 68 GLN A CD 300 O OE1 . GLN A 42 ? 0.2002 0.2490 0.2225 -0.0955 0.0131 -0.0183 68 GLN A OE1 301 N NE2 . GLN A 42 ? 0.2631 0.2980 0.2746 -0.1124 0.0078 -0.0166 68 GLN A NE2 302 N N . PHE A 43 ? 0.1433 0.1742 0.1847 -0.0400 0.0006 -0.0173 69 PHE A N 303 C CA . PHE A 43 ? 0.1284 0.1570 0.1727 -0.0289 0.0015 -0.0173 69 PHE A CA 304 C C . PHE A 43 ? 0.1236 0.1606 0.1761 -0.0182 -0.0018 -0.0190 69 PHE A C 305 O O . PHE A 43 ? 0.1471 0.1852 0.1997 -0.0184 -0.0058 -0.0188 69 PHE A O 306 C CB . PHE A 43 ? 0.1292 0.1347 0.1640 -0.0266 0.0007 -0.0131 69 PHE A CB 307 C CG . PHE A 43 ? 0.1364 0.1312 0.1622 -0.0350 0.0021 -0.0106 69 PHE A CG 308 C CD1 . PHE A 43 ? 0.2086 0.1916 0.2265 -0.0429 0.0000 -0.0084 69 PHE A CD1 309 C CD2 . PHE A 43 ? 0.1371 0.1313 0.1606 -0.0348 0.0049 -0.0104 69 PHE A CD2 310 C CE1 . PHE A 43 ? 0.1556 0.1255 0.1632 -0.0500 -0.0001 -0.0052 69 PHE A CE1 311 C CE2 . PHE A 43 ? 0.1468 0.1294 0.1595 -0.0427 0.0050 -0.0072 69 PHE A CE2 312 C CZ . PHE A 43 ? 0.1564 0.1264 0.1611 -0.0500 0.0021 -0.0042 69 PHE A CZ 313 N N . ASN A 44 ? 0.1689 0.2104 0.2269 -0.0091 -0.0006 -0.0208 70 ASN A N 314 C CA . ASN A 44 ? 0.1201 0.1631 0.1824 0.0019 -0.0051 -0.0211 70 ASN A CA 315 C C . ASN A 44 ? 0.1618 0.1906 0.2202 0.0104 -0.0045 -0.0196 70 ASN A C 316 O O . ASN A 44 ? 0.1638 0.1935 0.2256 0.0200 -0.0074 -0.0205 70 ASN A O 317 C CB . ASN A 44 ? 0.1473 0.2146 0.2236 0.0062 -0.0067 -0.0261 70 ASN A CB 318 C CG . ASN A 44 ? 0.1992 0.2798 0.2835 0.0078 -0.0010 -0.0311 70 ASN A CG 319 O OD1 . ASN A 44 ? 0.1400 0.2110 0.2175 0.0045 0.0039 -0.0305 70 ASN A OD1 320 N ND2 . ASN A 44 ? 0.1434 0.2476 0.2426 0.0130 -0.0019 -0.0367 70 ASN A ND2 321 N N . GLY A 45 ? 0.1282 0.1427 0.1787 0.0065 -0.0016 -0.0172 71 GLY A N 322 C CA . GLY A 45 ? 0.1207 0.1200 0.1661 0.0118 -0.0012 -0.0153 71 GLY A CA 323 C C . GLY A 45 ? 0.1198 0.1042 0.1575 0.0069 -0.0010 -0.0116 71 GLY A C 324 O O . GLY A 45 ? 0.1375 0.1213 0.1730 -0.0002 -0.0005 -0.0108 71 GLY A O 325 N N . ALA A 46 ? 0.1212 0.0931 0.1548 0.0107 -0.0015 -0.0097 72 ALA A N 326 C CA . ALA A 46 ? 0.1565 0.1174 0.1857 0.0072 -0.0009 -0.0073 72 ALA A CA 327 C C . ALA A 46 ? 0.1340 0.0855 0.1610 0.0096 0.0002 -0.0065 72 ALA A C 328 O O . ALA A 46 ? 0.1365 0.0852 0.1624 0.0143 -0.0002 -0.0068 72 ALA A O 329 C CB . ALA A 46 ? 0.1458 0.1034 0.1721 0.0067 -0.0024 -0.0063 72 ALA A CB 330 N N . THR A 47 ? 0.1221 0.0683 0.1485 0.0061 0.0008 -0.0055 73 THR A N 331 C CA . THR A 47 ? 0.1216 0.0603 0.1471 0.0066 0.0015 -0.0049 73 THR A CA 332 C C . THR A 47 ? 0.1204 0.0560 0.1475 0.0046 0.0016 -0.0042 73 THR A C 333 O O . THR A 47 ? 0.1269 0.0634 0.1553 0.0026 0.0004 -0.0041 73 THR A O 334 C CB . THR A 47 ? 0.1371 0.0756 0.1624 0.0047 0.0015 -0.0056 73 THR A CB 335 O OG1 . THR A 47 ? 0.1658 0.1092 0.1903 0.0065 0.0025 -0.0077 73 THR A OG1 336 C CG2 . THR A 47 ? 0.1407 0.0725 0.1654 0.0045 0.0018 -0.0054 73 THR A CG2 337 N N . PRO A 48 ? 0.1723 0.1038 0.1987 0.0050 0.0033 -0.0040 74 PRO A N 338 C CA . PRO A 48 ? 0.1495 0.0809 0.1797 0.0037 0.0044 -0.0048 74 PRO A CA 339 C C . PRO A 48 ? 0.1697 0.1022 0.2056 0.0027 0.0025 -0.0051 74 PRO A C 340 O O . PRO A 48 ? 0.1721 0.1038 0.2081 0.0018 0.0021 -0.0048 74 PRO A O 341 C CB . PRO A 48 ? 0.1894 0.1178 0.2170 0.0028 0.0076 -0.0049 74 PRO A CB 342 C CG . PRO A 48 ? 0.2419 0.1657 0.2648 0.0034 0.0071 -0.0034 74 PRO A CG 343 C CD . PRO A 48 ? 0.2200 0.1463 0.2418 0.0064 0.0045 -0.0033 74 PRO A CD 344 N N . GLU A 49 ? 0.1603 0.0931 0.1998 0.0030 0.0006 -0.0056 75 GLU A N 345 C CA . GLU A 49 ? 0.2012 0.1337 0.2449 0.0028 -0.0033 -0.0051 75 GLU A CA 346 C C . GLU A 49 ? 0.1752 0.1116 0.2266 0.0029 -0.0026 -0.0066 75 GLU A C 347 O O . GLU A 49 ? 0.1523 0.0896 0.2052 0.0015 -0.0056 -0.0058 75 GLU A O 348 C CB . GLU A 49 ? 0.2000 0.1290 0.2451 0.0040 -0.0063 -0.0052 75 GLU A CB 349 C CG . GLU A 49 ? 0.3084 0.2335 0.3532 0.0035 -0.0124 -0.0030 75 GLU A CG 350 C CD . GLU A 49 ? 0.5184 0.4358 0.5626 0.0052 -0.0163 -0.0027 75 GLU A CD 351 O OE1 . GLU A 49 ? 0.4899 0.4046 0.5319 0.0054 -0.0138 -0.0044 75 GLU A OE1 352 O OE2 . GLU A 49 ? 0.5802 0.4925 0.6250 0.0063 -0.0225 -0.0009 75 GLU A OE2 353 N N . ASN A 50 ? 0.1196 0.0592 0.1755 0.0035 0.0014 -0.0090 76 ASN A N 354 C CA . ASN A 50 ? 0.1750 0.1215 0.2405 0.0025 0.0029 -0.0114 76 ASN A CA 355 C C . ASN A 50 ? 0.2584 0.2068 0.3220 -0.0006 0.0095 -0.0128 76 ASN A C 356 O O . ASN A 50 ? 0.1722 0.1248 0.2399 -0.0043 0.0113 -0.0138 76 ASN A O 357 C CB . ASN A 50 ? 0.1852 0.1369 0.2622 0.0066 0.0011 -0.0145 76 ASN A CB 358 C CG . ASN A 50 ? 0.2479 0.1964 0.3268 0.0092 -0.0069 -0.0125 76 ASN A CG 359 O OD1 . ASN A 50 ? 0.3090 0.2510 0.3855 0.0122 -0.0098 -0.0120 76 ASN A OD1 360 N ND2 . ASN A 50 ? 0.2276 0.1789 0.3090 0.0073 -0.0110 -0.0111 76 ASN A ND2 361 N N . GLU A 51 ? 0.1480 0.0927 0.2043 -0.0003 0.0130 -0.0130 77 GLU A N 362 C CA . GLU A 51 ? 0.1987 0.1462 0.2541 -0.0036 0.0196 -0.0152 77 GLU A CA 363 C C . GLU A 51 ? 0.1541 0.0954 0.1992 -0.0087 0.0221 -0.0124 77 GLU A C 364 O O . GLU A 51 ? 0.1626 0.1048 0.2045 -0.0134 0.0278 -0.0136 77 GLU A O 365 C CB . GLU A 51 ? 0.3782 0.3241 0.4288 -0.0020 0.0224 -0.0172 77 GLU A CB 366 C CG . GLU A 51 ? 0.4868 0.4363 0.5473 0.0030 0.0202 -0.0208 77 GLU A CG 367 C CD . GLU A 51 ? 0.5770 0.5323 0.6426 0.0038 0.0261 -0.0270 77 GLU A CD 368 O OE1 . GLU A 51 ? 0.5962 0.5540 0.6569 -0.0009 0.0329 -0.0285 77 GLU A OE1 369 O OE2 . GLU A 51 ? 0.4836 0.4398 0.5572 0.0091 0.0240 -0.0306 77 GLU A OE2 370 N N . MET A 52 ? 0.1667 0.1011 0.2062 -0.0083 0.0183 -0.0092 78 MET A N 371 C CA . MET A 52 ? 0.1610 0.0872 0.1916 -0.0128 0.0199 -0.0071 78 MET A CA 372 C C . MET A 52 ? 0.2012 0.1310 0.2389 -0.0170 0.0194 -0.0083 78 MET A C 373 O O . MET A 52 ? 0.2383 0.1601 0.2686 -0.0219 0.0206 -0.0070 78 MET A O 374 C CB . MET A 52 ? 0.1996 0.1150 0.2197 -0.0093 0.0162 -0.0039 78 MET A CB 375 C CG . MET A 52 ? 0.2356 0.1466 0.2467 -0.0066 0.0161 -0.0021 78 MET A CG 376 S SD . MET A 52 ? 0.3312 0.2315 0.3324 -0.0015 0.0114 0.0009 78 MET A SD 377 C CE . MET A 52 ? 0.2672 0.1696 0.2634 0.0017 0.0099 0.0019 78 MET A CE 378 N N . LYS A 53 ? 0.1362 0.0765 0.1869 -0.0152 0.0167 -0.0106 79 LYS A N 379 C CA . LYS A 53 ? 0.1432 0.0887 0.2012 -0.0195 0.0149 -0.0120 79 LYS A CA 380 C C . LYS A 53 ? 0.1820 0.1358 0.2461 -0.0264 0.0207 -0.0147 79 LYS A C 381 O O . LYS A 53 ? 0.1560 0.1154 0.2225 -0.0266 0.0259 -0.0167 79 LYS A O 382 C CB . LYS A 53 ? 0.1883 0.1425 0.2578 -0.0154 0.0089 -0.0132 79 LYS A CB 383 C CG . LYS A 53 ? 0.2114 0.1575 0.2731 -0.0116 0.0038 -0.0105 79 LYS A CG 384 C CD . LYS A 53 ? 0.3176 0.2688 0.3867 -0.0072 -0.0016 -0.0106 79 LYS A CD 385 C CE . LYS A 53 ? 0.2935 0.2371 0.3530 -0.0057 -0.0056 -0.0079 79 LYS A CE 386 N NZ . LYS A 53 ? 0.2449 0.1900 0.3086 -0.0024 -0.0114 -0.0070 79 LYS A NZ 387 N N . TRP A 54 ? 0.1467 0.1019 0.2129 -0.0331 0.0201 -0.0154 80 TRP A N 388 C CA . TRP A 54 ? 0.1551 0.1160 0.2236 -0.0428 0.0264 -0.0175 80 TRP A CA 389 C C . TRP A 54 ? 0.1499 0.1313 0.2358 -0.0426 0.0308 -0.0226 80 TRP A C 390 O O . TRP A 54 ? 0.1570 0.1417 0.2406 -0.0486 0.0387 -0.0243 80 TRP A O 391 C CB . TRP A 54 ? 0.1607 0.1215 0.2309 -0.0502 0.0235 -0.0182 80 TRP A CB 392 C CG . TRP A 54 ? 0.1743 0.1341 0.2404 -0.0628 0.0296 -0.0190 80 TRP A CG 393 C CD1 . TRP A 54 ? 0.2133 0.1857 0.2858 -0.0695 0.0376 -0.0218 80 TRP A CD1 394 C CD2 . TRP A 54 ? 0.1886 0.1333 0.2421 -0.0714 0.0286 -0.0173 80 TRP A CD2 395 N NE1 . TRP A 54 ? 0.2259 0.1919 0.2900 -0.0830 0.0417 -0.0214 80 TRP A NE1 396 C CE2 . TRP A 54 ? 0.2206 0.1682 0.2725 -0.0841 0.0358 -0.0184 80 TRP A CE2 397 C CE3 . TRP A 54 ? 0.2548 0.1828 0.2972 -0.0698 0.0228 -0.0154 80 TRP A CE3 398 C CZ2 . TRP A 54 ? 0.2458 0.1782 0.2847 -0.0959 0.0366 -0.0171 80 TRP A CZ2 399 C CZ3 . TRP A 54 ? 0.2641 0.1771 0.2943 -0.0801 0.0235 -0.0149 80 TRP A CZ3 400 C CH2 . TRP A 54 ? 0.2490 0.1633 0.2771 -0.0932 0.0299 -0.0154 80 TRP A CH2 401 N N . ALA A 55 ? 0.1617 0.1565 0.2643 -0.0357 0.0256 -0.0254 81 ALA A N 402 C CA . ALA A 55 ? 0.1358 0.1509 0.2575 -0.0332 0.0289 -0.0314 81 ALA A CA 403 C C . ALA A 55 ? 0.2148 0.2274 0.3311 -0.0299 0.0357 -0.0329 81 ALA A C 404 O O . ALA A 55 ? 0.1966 0.2240 0.3237 -0.0313 0.0427 -0.0387 81 ALA A O 405 C CB . ALA A 55 ? 0.1831 0.2078 0.3210 -0.0240 0.0198 -0.0331 81 ALA A CB 406 N N . TYR A 56 ? 0.1495 0.1447 0.2493 -0.0259 0.0338 -0.0283 82 TYR A N 407 C CA . TYR A 56 ? 0.1650 0.1565 0.2577 -0.0230 0.0388 -0.0295 82 TYR A CA 408 C C . TYR A 56 ? 0.2010 0.1823 0.2754 -0.0313 0.0456 -0.0269 82 TYR A C 409 O O . TYR A 56 ? 0.2332 0.2181 0.3044 -0.0340 0.0531 -0.0300 82 TYR A O 410 C CB . TYR A 56 ? 0.1879 0.1675 0.2732 -0.0148 0.0325 -0.0261 82 TYR A CB 411 C CG . TYR A 56 ? 0.2660 0.2516 0.3652 -0.0066 0.0259 -0.0281 82 TYR A CG 412 C CD1 . TYR A 56 ? 0.2547 0.2398 0.3581 -0.0053 0.0180 -0.0255 82 TYR A CD1 413 C CD2 . TYR A 56 ? 0.2794 0.2692 0.3857 -0.0005 0.0271 -0.0327 82 TYR A CD2 414 C CE1 . TYR A 56 ? 0.3040 0.2919 0.4173 0.0018 0.0108 -0.0263 82 TYR A CE1 415 C CE2 . TYR A 56 ? 0.3349 0.3267 0.4521 0.0074 0.0200 -0.0340 82 TYR A CE2 416 C CZ . TYR A 56 ? 0.4151 0.4056 0.5354 0.0083 0.0115 -0.0303 82 TYR A CZ 417 O OH . TYR A 56 ? 0.5759 0.5656 0.7043 0.0157 0.0034 -0.0306 82 TYR A OH 418 N N . ILE A 57 ? 0.1567 0.1240 0.2180 -0.0354 0.0428 -0.0214 83 ILE A N 419 C CA . ILE A 57 ? 0.1708 0.1225 0.2111 -0.0411 0.0463 -0.0172 83 ILE A CA 420 C C . ILE A 57 ? 0.1845 0.1379 0.2210 -0.0538 0.0534 -0.0179 83 ILE A C 421 O O . ILE A 57 ? 0.2243 0.1680 0.2441 -0.0602 0.0586 -0.0157 83 ILE A O 422 C CB . ILE A 57 ? 0.2002 0.1334 0.2270 -0.0375 0.0392 -0.0111 83 ILE A CB 423 C CG1 . ILE A 57 ? 0.2749 0.1917 0.2808 -0.0385 0.0401 -0.0067 83 ILE A CG1 424 C CG2 . ILE A 57 ? 0.1821 0.1105 0.2090 -0.0422 0.0367 -0.0098 83 ILE A CG2 425 C CD1 . ILE A 57 ? 0.2362 0.1401 0.2337 -0.0307 0.0326 -0.0024 83 ILE A CD1 426 N N . GLU A 58 ? 0.1814 0.1470 0.2323 -0.0584 0.0536 -0.0209 84 GLU A N 427 C CA . GLU A 58 ? 0.1983 0.1698 0.2483 -0.0722 0.0616 -0.0228 84 GLU A CA 428 C C . GLU A 58 ? 0.2072 0.2075 0.2842 -0.0735 0.0645 -0.0308 84 GLU A C 429 O O . GLU A 58 ? 0.1846 0.1925 0.2715 -0.0789 0.0621 -0.0319 84 GLU A O 430 C CB . GLU A 58 ? 0.2076 0.1613 0.2438 -0.0805 0.0587 -0.0179 84 GLU A CB 431 C CG . GLU A 58 ? 0.2289 0.1790 0.2538 -0.0970 0.0673 -0.0175 84 GLU A CG 432 C CD . GLU A 58 ? 0.2440 0.1768 0.2571 -0.1065 0.0644 -0.0138 84 GLU A CD 433 O OE1 . GLU A 58 ? 0.3041 0.2256 0.3156 -0.0996 0.0558 -0.0115 84 GLU A OE1 434 O OE2 . GLU A 58 ? 0.2627 0.1936 0.2668 -0.1199 0.0701 -0.0133 84 GLU A OE2 435 N N . PRO A 59 ? 0.2242 0.2409 0.3137 -0.0681 0.0693 -0.0367 85 PRO A N 436 C CA . PRO A 59 ? 0.2265 0.2716 0.3452 -0.0646 0.0700 -0.0450 85 PRO A CA 437 C C . PRO A 59 ? 0.2429 0.3076 0.3727 -0.0781 0.0784 -0.0502 85 PRO A C 438 O O . PRO A 59 ? 0.2297 0.3174 0.3845 -0.0769 0.0760 -0.0557 85 PRO A O 439 C CB . PRO A 59 ? 0.2315 0.2831 0.3552 -0.0554 0.0740 -0.0501 85 PRO A CB 440 C CG . PRO A 59 ? 0.3360 0.3683 0.4326 -0.0607 0.0797 -0.0459 85 PRO A CG 441 C CD . PRO A 59 ? 0.1833 0.1915 0.2596 -0.0641 0.0732 -0.0363 85 PRO A CD 442 N N . GLU A 60 ? 0.1942 0.2505 0.3055 -0.0915 0.0878 -0.0484 86 GLU A N 443 C CA . GLU A 60 ? 0.2153 0.2846 0.3315 -0.1080 0.0950 -0.0512 86 GLU A CA 444 C C . GLU A 60 ? 0.2975 0.3375 0.3839 -0.1204 0.0948 -0.0424 86 GLU A C 445 O O . GLU A 60 ? 0.2335 0.2467 0.2959 -0.1163 0.0918 -0.0353 86 GLU A O 446 C CB . GLU A 60 ? 0.3294 0.4201 0.4525 -0.1139 0.1079 -0.0591 86 GLU A CB 447 C CG . GLU A 60 ? 0.5172 0.6257 0.6592 -0.1006 0.1109 -0.0673 86 GLU A CG 448 C CD . GLU A 60 ? 0.8312 0.9504 0.9678 -0.1054 0.1229 -0.0735 86 GLU A CD 449 O OE1 . GLU A 60 ? 0.8700 0.9865 0.9915 -0.1193 0.1284 -0.0717 86 GLU A OE1 450 O OE2 . GLU A 60 ? 0.9696 1.0986 1.1161 -0.0949 0.1262 -0.0804 86 GLU A OE2 451 N N . ARG A 61 ? 0.2591 0.3020 0.3436 -0.1311 0.0945 -0.0418 87 ARG A N 452 C CA . ARG A 61 ? 0.3693 0.3816 0.4254 -0.1388 0.0905 -0.0330 87 ARG A CA 453 C C . ARG A 61 ? 0.3497 0.3389 0.3753 -0.1434 0.0956 -0.0275 87 ARG A C 454 O O . ARG A 61 ? 0.2901 0.2903 0.3131 -0.1499 0.1047 -0.0309 87 ARG A O 455 C CB . ARG A 61 ? 0.3360 0.3567 0.3958 -0.1500 0.0901 -0.0343 87 ARG A CB 456 C CG . ARG A 61 ? 0.3933 0.3822 0.4276 -0.1553 0.0839 -0.0262 87 ARG A CG 457 C CD . ARG A 61 ? 0.3556 0.3531 0.3966 -0.1655 0.0821 -0.0281 87 ARG A CD 458 N NE . ARG A 61 ? 0.4027 0.3680 0.4193 -0.1688 0.0759 -0.0212 87 ARG A NE 459 C CZ . ARG A 61 ? 0.4301 0.3938 0.4469 -0.1768 0.0724 -0.0215 87 ARG A CZ 460 N NH1 . ARG A 61 ? 0.3681 0.3614 0.4085 -0.1826 0.0739 -0.0278 87 ARG A NH1 461 N NH2 . ARG A 61 ? 0.4163 0.3490 0.4103 -0.1781 0.0671 -0.0159 87 ARG A NH2 462 N N . ASN A 62 ? 0.3925 0.3505 0.3956 -0.1390 0.0888 -0.0193 88 ASN A N 463 C CA . ASN A 62 ? 0.3065 0.2387 0.2793 -0.1408 0.0899 -0.0126 88 ASN A CA 464 C C . ASN A 62 ? 0.4124 0.3519 0.3843 -0.1373 0.0967 -0.0152 88 ASN A C 465 O O . ASN A 62 ? 0.3588 0.2822 0.3062 -0.1409 0.0990 -0.0110 88 ASN A O 466 C CB . ASN A 62 ? 0.4509 0.3746 0.4053 -0.1545 0.0934 -0.0102 88 ASN A CB 467 C CG . ASN A 62 ? 0.5112 0.4000 0.4322 -0.1546 0.0886 -0.0011 88 ASN A CG 468 O OD1 . ASN A 62 ? 0.4834 0.3523 0.3963 -0.1442 0.0798 0.0041 88 ASN A OD1 469 N ND2 . ASN A 62 ? 0.5161 0.3979 0.4178 -0.1659 0.0940 0.0005 88 ASN A ND2 470 N N . GLN A 63 ? 0.2768 0.2398 0.2749 -0.1299 0.0993 -0.0223 89 GLN A N 471 C CA . GLN A 63 ? 0.2707 0.2408 0.2698 -0.1230 0.1039 -0.0257 89 GLN A CA 472 C C . GLN A 63 ? 0.2938 0.2557 0.2968 -0.1049 0.0923 -0.0230 89 GLN A C 473 O O . GLN A 63 ? 0.3491 0.3258 0.3753 -0.0953 0.0872 -0.0269 89 GLN A O 474 C CB . GLN A 63 ? 0.3085 0.3140 0.3352 -0.1233 0.1132 -0.0372 89 GLN A CB 475 C CG . GLN A 63 ? 0.5341 0.5534 0.5607 -0.1366 0.1210 -0.0410 89 GLN A CG 476 C CD . GLN A 63 ? 0.7550 0.7680 0.7589 -0.1440 0.1296 -0.0412 89 GLN A CD 477 O OE1 . GLN A 63 ? 0.8795 0.8711 0.8558 -0.1539 0.1291 -0.0343 89 GLN A OE1 478 N NE2 . GLN A 63 ? 0.7717 0.8024 0.7864 -0.1387 0.1368 -0.0495 89 GLN A NE2 479 N N . PHE A 64 ? 0.2610 0.1991 0.2407 -0.1007 0.0877 -0.0162 90 PHE A N 480 C CA . PHE A 64 ? 0.2451 0.1756 0.2278 -0.0854 0.0769 -0.0135 90 PHE A CA 481 C C . PHE A 64 ? 0.2893 0.2279 0.2755 -0.0767 0.0781 -0.0172 90 PHE A C 482 O O . PHE A 64 ? 0.3337 0.2722 0.3080 -0.0823 0.0854 -0.0188 90 PHE A O 483 C CB . PHE A 64 ? 0.3151 0.2162 0.2739 -0.0845 0.0692 -0.0042 90 PHE A CB 484 C CG . PHE A 64 ? 0.2665 0.1570 0.2230 -0.0905 0.0662 -0.0013 90 PHE A CG 485 C CD1 . PHE A 64 ? 0.2897 0.1712 0.2324 -0.1060 0.0722 0.0008 90 PHE A CD1 486 C CD2 . PHE A 64 ? 0.3129 0.2022 0.2800 -0.0816 0.0579 -0.0010 90 PHE A CD2 487 C CE1 . PHE A 64 ? 0.2978 0.1701 0.2382 -0.1103 0.0680 0.0028 90 PHE A CE1 488 C CE2 . PHE A 64 ? 0.2608 0.1395 0.2248 -0.0874 0.0553 0.0007 90 PHE A CE2 489 C CZ . PHE A 64 ? 0.3278 0.1973 0.2786 -0.1018 0.0602 0.0026 90 PHE A CZ 490 N N . ASN A 65 ? 0.2165 0.1614 0.2180 -0.0639 0.0712 -0.0190 91 ASN A N 491 C CA . ASN A 65 ? 0.2289 0.1784 0.2332 -0.0554 0.0708 -0.0224 91 ASN A CA 492 C C . ASN A 65 ? 0.2014 0.1378 0.2001 -0.0455 0.0602 -0.0171 91 ASN A C 493 O O . ASN A 65 ? 0.1860 0.1270 0.1987 -0.0381 0.0541 -0.0176 91 ASN A O 494 C CB . ASN A 65 ? 0.2294 0.2017 0.2600 -0.0501 0.0736 -0.0312 91 ASN A CB 495 C CG . ASN A 65 ? 0.2851 0.2602 0.3174 -0.0422 0.0741 -0.0357 91 ASN A CG 496 O OD1 . ASN A 65 ? 0.2367 0.1984 0.2508 -0.0417 0.0727 -0.0326 91 ASN A OD1 497 N ND2 . ASN A 65 ? 0.1823 0.1739 0.2362 -0.0360 0.0754 -0.0434 91 ASN A ND2 498 N N . PHE A 66 ? 0.2135 0.1344 0.1914 -0.0460 0.0580 -0.0122 92 PHE A N 499 C CA . PHE A 66 ? 0.2080 0.1183 0.1809 -0.0376 0.0483 -0.0074 92 PHE A CA 500 C C . PHE A 66 ? 0.2081 0.1239 0.1856 -0.0303 0.0459 -0.0106 92 PHE A C 501 O O . PHE A 66 ? 0.2052 0.1157 0.1804 -0.0241 0.0385 -0.0076 92 PHE A O 502 C CB . PHE A 66 ? 0.2818 0.1725 0.2311 -0.0406 0.0450 -0.0003 92 PHE A CB 503 C CG . PHE A 66 ? 0.2876 0.1672 0.2299 -0.0468 0.0452 0.0038 92 PHE A CG 504 C CD1 . PHE A 66 ? 0.3336 0.2110 0.2848 -0.0424 0.0398 0.0050 92 PHE A CD1 505 C CD2 . PHE A 66 ? 0.3050 0.1752 0.2304 -0.0582 0.0510 0.0060 92 PHE A CD2 506 C CE1 . PHE A 66 ? 0.3465 0.2118 0.2905 -0.0485 0.0399 0.0079 92 PHE A CE1 507 C CE2 . PHE A 66 ? 0.3413 0.1988 0.2588 -0.0653 0.0510 0.0098 92 PHE A CE2 508 C CZ . PHE A 66 ? 0.3047 0.1594 0.2319 -0.0601 0.0453 0.0105 92 PHE A CZ 509 N N . THR A 67 ? 0.1981 0.1249 0.1825 -0.0313 0.0524 -0.0173 93 THR A N 510 C CA . THR A 67 ? 0.1951 0.1236 0.1798 -0.0261 0.0509 -0.0207 93 THR A CA 511 C C . THR A 67 ? 0.1886 0.1178 0.1843 -0.0178 0.0426 -0.0197 93 THR A C 512 O O . THR A 67 ? 0.1962 0.1198 0.1847 -0.0148 0.0373 -0.0176 93 THR A O 513 C CB . THR A 67 ? 0.1965 0.1369 0.1907 -0.0268 0.0592 -0.0296 93 THR A CB 514 O OG1 . THR A 67 ? 0.2373 0.1775 0.2188 -0.0361 0.0679 -0.0308 93 THR A OG1 515 C CG2 . THR A 67 ? 0.2100 0.1488 0.2025 -0.0217 0.0574 -0.0337 93 THR A CG2 516 N N . GLY A 68 ? 0.1858 0.1226 0.1983 -0.0150 0.0415 -0.0211 94 GLY A N 517 C CA . GLY A 68 ? 0.1681 0.1054 0.1896 -0.0086 0.0344 -0.0201 94 GLY A CA 518 C C . GLY A 68 ? 0.1979 0.1272 0.2114 -0.0075 0.0282 -0.0139 94 GLY A C 519 O O . GLY A 68 ? 0.1629 0.0902 0.1748 -0.0042 0.0234 -0.0128 94 GLY A O 520 N N . GLY A 69 ? 0.1585 0.0833 0.1671 -0.0105 0.0284 -0.0104 95 GLY A N 521 C CA . GLY A 69 ? 0.1604 0.0777 0.1625 -0.0080 0.0227 -0.0056 95 GLY A CA 522 C C . GLY A 69 ? 0.1802 0.0915 0.1696 -0.0067 0.0199 -0.0033 95 GLY A C 523 O O . GLY A 69 ? 0.2010 0.1121 0.1905 -0.0024 0.0144 -0.0016 95 GLY A O 524 N N . ASP A 70 ? 0.2294 0.1372 0.2080 -0.0110 0.0238 -0.0037 96 ASP A N 525 C CA . ASP A 70 ? 0.2163 0.1181 0.1809 -0.0106 0.0203 -0.0014 96 ASP A CA 526 C C . ASP A 70 ? 0.2384 0.1468 0.2080 -0.0073 0.0172 -0.0042 96 ASP A C 527 O O . ASP A 70 ? 0.2191 0.1262 0.1833 -0.0049 0.0113 -0.0020 96 ASP A O 528 C CB . ASP A 70 ? 0.2060 0.1024 0.1557 -0.0173 0.0258 -0.0016 96 ASP A CB 529 C CG . ASP A 70 ? 0.3187 0.2038 0.2567 -0.0222 0.0271 0.0031 96 ASP A CG 530 O OD1 . ASP A 70 ? 0.3234 0.2035 0.2643 -0.0192 0.0231 0.0064 96 ASP A OD1 531 O OD2 . ASP A 70 ? 0.3363 0.2163 0.2604 -0.0296 0.0325 0.0034 96 ASP A OD2 532 N N . ILE A 71 ? 0.1736 0.0887 0.1536 -0.0073 0.0207 -0.0092 97 ILE A N 533 C CA . ILE A 71 ? 0.1959 0.1142 0.1794 -0.0053 0.0177 -0.0119 97 ILE A CA 534 C C . ILE A 71 ? 0.3017 0.2230 0.2920 -0.0019 0.0115 -0.0093 97 ILE A C 535 O O . ILE A 71 ? 0.1603 0.0832 0.1476 -0.0015 0.0070 -0.0088 97 ILE A O 536 C CB . ILE A 71 ? 0.2118 0.1335 0.2048 -0.0049 0.0219 -0.0177 97 ILE A CB 537 C CG1 . ILE A 71 ? 0.2146 0.1354 0.1999 -0.0084 0.0288 -0.0221 97 ILE A CG1 538 C CG2 . ILE A 71 ? 0.1629 0.0843 0.1588 -0.0033 0.0178 -0.0195 97 ILE A CG2 539 C CD1 . ILE A 71 ? 0.1763 0.1023 0.1732 -0.0068 0.0343 -0.0288 97 ILE A CD1 540 N N . VAL A 72 ? 0.1508 0.0740 0.1500 -0.0001 0.0113 -0.0080 98 VAL A N 541 C CA . VAL A 72 ? 0.1432 0.0700 0.1479 0.0024 0.0068 -0.0063 98 VAL A CA 542 C C . VAL A 72 ? 0.1475 0.0738 0.1464 0.0046 0.0029 -0.0034 98 VAL A C 543 O O . VAL A 72 ? 0.1478 0.0801 0.1491 0.0061 -0.0010 -0.0034 98 VAL A O 544 C CB . VAL A 72 ? 0.2059 0.1339 0.2191 0.0033 0.0074 -0.0060 98 VAL A CB 545 C CG1 . VAL A 72 ? 0.2179 0.1498 0.2345 0.0049 0.0039 -0.0048 98 VAL A CG1 546 C CG2 . VAL A 72 ? 0.1596 0.0888 0.1800 0.0026 0.0092 -0.0088 98 VAL A CG2 547 N N . ALA A 73 ? 0.1559 0.0751 0.1473 0.0048 0.0038 -0.0010 99 ALA A N 548 C CA . ALA A 73 ? 0.1962 0.1118 0.1812 0.0084 -0.0010 0.0021 99 ALA A CA 549 C C . ALA A 73 ? 0.2002 0.1182 0.1788 0.0087 -0.0054 0.0024 99 ALA A C 550 O O . ALA A 73 ? 0.1887 0.1108 0.1685 0.0131 -0.0112 0.0035 99 ALA A O 551 C CB . ALA A 73 ? 0.1764 0.0793 0.1511 0.0073 0.0004 0.0053 99 ALA A CB 552 N N . ALA A 74 ? 0.1753 0.0916 0.1472 0.0041 -0.0027 0.0008 100 ALA A N 553 C CA . ALA A 74 ? 0.2478 0.1655 0.2115 0.0030 -0.0071 0.0007 100 ALA A CA 554 C C . ALA A 74 ? 0.2387 0.1679 0.2122 0.0033 -0.0102 -0.0020 100 ALA A C 555 O O . ALA A 74 ? 0.2054 0.1405 0.1778 0.0046 -0.0165 -0.0015 100 ALA A O 556 C CB . ALA A 74 ? 0.2434 0.1553 0.1955 -0.0027 -0.0024 -0.0013 100 ALA A CB 557 N N . PHE A 75 ? 0.1641 0.0964 0.1468 0.0014 -0.0063 -0.0050 101 PHE A N 558 C CA . PHE A 75 ? 0.1630 0.1041 0.1535 -0.0001 -0.0087 -0.0071 101 PHE A CA 559 C C . PHE A 75 ? 0.1612 0.1121 0.1597 0.0039 -0.0127 -0.0056 101 PHE A C 560 O O . PHE A 75 ? 0.1524 0.1137 0.1543 0.0032 -0.0170 -0.0066 101 PHE A O 561 C CB . PHE A 75 ? 0.1504 0.0895 0.1475 -0.0021 -0.0047 -0.0091 101 PHE A CB 562 C CG . PHE A 75 ? 0.2018 0.1461 0.2033 -0.0058 -0.0068 -0.0108 101 PHE A CG 563 C CD1 . PHE A 75 ? 0.2352 0.1763 0.2314 -0.0105 -0.0075 -0.0137 101 PHE A CD1 564 C CD2 . PHE A 75 ? 0.1641 0.1157 0.1736 -0.0057 -0.0075 -0.0098 101 PHE A CD2 565 C CE1 . PHE A 75 ? 0.2104 0.1544 0.2090 -0.0156 -0.0095 -0.0149 101 PHE A CE1 566 C CE2 . PHE A 75 ? 0.2458 0.2016 0.2574 -0.0111 -0.0087 -0.0110 101 PHE A CE2 567 C CZ . PHE A 75 ? 0.1788 0.1301 0.1849 -0.0164 -0.0099 -0.0133 101 PHE A CZ 568 N N . SER A 76 ? 0.1485 0.0969 0.1503 0.0079 -0.0111 -0.0039 102 SER A N 569 C CA . SER A 76 ? 0.1540 0.1104 0.1631 0.0129 -0.0138 -0.0036 102 SER A CA 570 C C . SER A 76 ? 0.1609 0.1203 0.1668 0.0176 -0.0203 -0.0022 102 SER A C 571 O O . SER A 76 ? 0.1872 0.1605 0.2015 0.0202 -0.0242 -0.0040 102 SER A O 572 C CB . SER A 76 ? 0.1511 0.1002 0.1613 0.0160 -0.0108 -0.0025 102 SER A CB 573 O OG . SER A 76 ? 0.2340 0.1879 0.2491 0.0223 -0.0135 -0.0028 102 SER A OG 574 N N . ALA A 77 ? 0.1865 0.1335 0.1798 0.0183 -0.0218 0.0008 103 ALA A N 575 C CA . ALA A 77 ? 0.1992 0.1457 0.1865 0.0231 -0.0296 0.0032 103 ALA A CA 576 C C . ALA A 77 ? 0.2010 0.1601 0.1901 0.0204 -0.0347 0.0012 103 ALA A C 577 O O . ALA A 77 ? 0.1839 0.1539 0.1788 0.0257 -0.0421 0.0010 103 ALA A O 578 C CB . ALA A 77 ? 0.2058 0.1343 0.1755 0.0219 -0.0297 0.0074 103 ALA A CB 579 N N . ALA A 78 ? 0.1787 0.1368 0.1635 0.0125 -0.0311 -0.0008 104 ALA A N 580 C CA . ALA A 78 ? 0.1884 0.1565 0.1731 0.0081 -0.0356 -0.0032 104 ALA A CA 581 C C . ALA A 78 ? 0.1982 0.1861 0.1998 0.0088 -0.0378 -0.0062 104 ALA A C 582 O O . ALA A 78 ? 0.1755 0.1766 0.1810 0.0087 -0.0446 -0.0074 104 ALA A O 583 C CB . ALA A 78 ? 0.1825 0.1439 0.1602 -0.0002 -0.0304 -0.0060 104 ALA A CB 584 N N . ASN A 79 ? 0.2106 0.2014 0.2219 0.0086 -0.0320 -0.0075 105 ASN A N 585 C CA . ASN A 79 ? 0.2357 0.2453 0.2616 0.0071 -0.0321 -0.0108 105 ASN A CA 586 C C . ASN A 79 ? 0.1640 0.1842 0.2012 0.0163 -0.0338 -0.0113 105 ASN A C 587 O O . ASN A 79 ? 0.1879 0.2243 0.2377 0.0152 -0.0318 -0.0147 105 ASN A O 588 C CB . ASN A 79 ? 0.2130 0.2190 0.2406 0.0001 -0.0251 -0.0121 105 ASN A CB 589 C CG . ASN A 79 ? 0.2650 0.2628 0.2840 -0.0084 -0.0241 -0.0131 105 ASN A CG 590 O OD1 . ASN A 79 ? 0.2459 0.2529 0.2668 -0.0150 -0.0266 -0.0154 105 ASN A OD1 591 N ND2 . ASN A 79 ? 0.1582 0.1389 0.1683 -0.0085 -0.0205 -0.0119 105 ASN A ND2 592 N N . ASP A 80 ? 0.1564 0.1665 0.1880 0.0248 -0.0374 -0.0083 106 ASP A N 593 C CA . ASP A 80 ? 0.2964 0.3092 0.3358 0.0352 -0.0387 -0.0088 106 ASP A CA 594 C C . ASP A 80 ? 0.2706 0.2887 0.3191 0.0341 -0.0312 -0.0120 106 ASP A C 595 O O . ASP A 80 ? 0.2051 0.2401 0.2670 0.0382 -0.0310 -0.0162 106 ASP A O 596 C CB . ASP A 80 ? 0.3556 0.3866 0.4060 0.0427 -0.0472 -0.0110 106 ASP A CB 597 C CG . ASP A 80 ? 0.5003 0.5214 0.5486 0.0559 -0.0531 -0.0088 106 ASP A CG 598 O OD1 . ASP A 80 ? 0.2451 0.2471 0.2853 0.0584 -0.0491 -0.0065 106 ASP A OD1 599 O OD2 . ASP A 80 ? 0.5167 0.5484 0.5711 0.0638 -0.0624 -0.0093 106 ASP A OD2 600 N N . TYR A 81 ? 0.1422 0.1465 0.1832 0.0284 -0.0250 -0.0103 107 TYR A N 601 C CA . TYR A 81 ? 0.1476 0.1513 0.1926 0.0272 -0.0187 -0.0121 107 TYR A CA 602 C C . TYR A 81 ? 0.2119 0.2067 0.2562 0.0359 -0.0186 -0.0119 107 TYR A C 603 O O . TYR A 81 ? 0.2286 0.2109 0.2654 0.0414 -0.0227 -0.0089 107 TYR A O 604 C CB . TYR A 81 ? 0.1315 0.1223 0.1687 0.0197 -0.0141 -0.0100 107 TYR A CB 605 C CG . TYR A 81 ? 0.1774 0.1734 0.2153 0.0106 -0.0124 -0.0110 107 TYR A CG 606 C CD1 . TYR A 81 ? 0.1536 0.1654 0.1975 0.0071 -0.0147 -0.0134 107 TYR A CD1 607 C CD2 . TYR A 81 ? 0.2705 0.2551 0.3031 0.0054 -0.0090 -0.0096 107 TYR A CD2 608 C CE1 . TYR A 81 ? 0.1848 0.1978 0.2269 -0.0026 -0.0132 -0.0140 107 TYR A CE1 609 C CE2 . TYR A 81 ? 0.4134 0.3986 0.4448 -0.0024 -0.0082 -0.0102 107 TYR A CE2 610 C CZ . TYR A 81 ? 0.2678 0.2656 0.3027 -0.0069 -0.0101 -0.0122 107 TYR A CZ 611 O OH . TYR A 81 ? 0.3757 0.3703 0.4071 -0.0158 -0.0094 -0.0126 107 TYR A OH 612 N N . VAL A 82 ? 0.1538 0.1527 0.2034 0.0360 -0.0139 -0.0151 108 VAL A N 613 C CA . VAL A 82 ? 0.1411 0.1267 0.1867 0.0412 -0.0122 -0.0151 108 VAL A CA 614 C C . VAL A 82 ? 0.1390 0.1085 0.1749 0.0345 -0.0090 -0.0115 108 VAL A C 615 O O . VAL A 82 ? 0.1808 0.1532 0.2174 0.0274 -0.0053 -0.0119 108 VAL A O 616 C CB . VAL A 82 ? 0.1724 0.1691 0.2263 0.0432 -0.0080 -0.0208 108 VAL A CB 617 C CG1 . VAL A 82 ? 0.1928 0.1733 0.2406 0.0476 -0.0064 -0.0213 108 VAL A CG1 618 C CG2 . VAL A 82 ? 0.1547 0.1715 0.2217 0.0507 -0.0108 -0.0257 108 VAL A CG2 619 N N . LEU A 83 ? 0.1472 0.0999 0.1741 0.0367 -0.0106 -0.0081 109 LEU A N 620 C CA . LEU A 83 ? 0.2706 0.2113 0.2905 0.0303 -0.0074 -0.0055 109 LEU A CA 621 C C . LEU A 83 ? 0.1748 0.1048 0.1918 0.0309 -0.0051 -0.0061 109 LEU A C 622 O O . LEU A 83 ? 0.1628 0.0834 0.1760 0.0366 -0.0070 -0.0062 109 LEU A O 623 C CB . LEU A 83 ? 0.2083 0.1386 0.2188 0.0293 -0.0095 -0.0015 109 LEU A CB 624 C CG . LEU A 83 ? 0.2399 0.1607 0.2449 0.0227 -0.0055 0.0003 109 LEU A CG 625 C CD1 . LEU A 83 ? 0.2264 0.1558 0.2376 0.0173 -0.0026 -0.0014 109 LEU A CD1 626 C CD2 . LEU A 83 ? 0.1990 0.1100 0.1928 0.0213 -0.0067 0.0036 109 LEU A CD2 627 N N . ARG A 84 ? 0.1461 0.0766 0.1644 0.0250 -0.0017 -0.0067 110 ARG A N 628 C CA . ARG A 84 ? 0.1473 0.0682 0.1623 0.0238 0.0001 -0.0074 110 ARG A CA 629 C C . ARG A 84 ? 0.2178 0.1305 0.2290 0.0181 0.0013 -0.0046 110 ARG A C 630 O O . ARG A 84 ? 0.1980 0.1164 0.2126 0.0139 0.0023 -0.0040 110 ARG A O 631 C CB . ARG A 84 ? 0.1419 0.0702 0.1607 0.0211 0.0022 -0.0105 110 ARG A CB 632 C CG . ARG A 84 ? 0.3210 0.2628 0.3454 0.0241 0.0028 -0.0141 110 ARG A CG 633 C CD . ARG A 84 ? 0.1899 0.1361 0.2139 0.0202 0.0057 -0.0172 110 ARG A CD 634 N NE . ARG A 84 ? 0.2648 0.2011 0.2842 0.0228 0.0066 -0.0200 110 ARG A NE 635 C CZ . ARG A 84 ? 0.2528 0.1791 0.2668 0.0183 0.0065 -0.0190 110 ARG A CZ 636 N NH1 . ARG A 84 ? 0.2726 0.1990 0.2868 0.0121 0.0054 -0.0154 110 ARG A NH1 637 N NH2 . ARG A 84 ? 0.2798 0.1961 0.2886 0.0202 0.0071 -0.0221 110 ARG A NH2 638 N N . GLY A 85 ? 0.1798 0.0792 0.1840 0.0178 0.0014 -0.0034 111 GLY A N 639 C CA . GLY A 85 ? 0.2199 0.1142 0.2219 0.0112 0.0036 -0.0017 111 GLY A CA 640 C C . GLY A 85 ? 0.2890 0.1860 0.2954 0.0069 0.0048 -0.0038 111 GLY A C 641 O O . GLY A 85 ? 0.2778 0.1711 0.2825 0.0082 0.0041 -0.0060 111 GLY A O 642 N N . HIS A 86 ? 0.2131 0.1166 0.2252 0.0022 0.0061 -0.0036 112 HIS A N 643 C CA . HIS A 86 ? 0.2394 0.1477 0.2570 -0.0011 0.0053 -0.0052 112 HIS A CA 644 C C . HIS A 86 ? 0.2106 0.1241 0.2349 -0.0059 0.0066 -0.0053 112 HIS A C 645 O O . HIS A 86 ? 0.2553 0.1751 0.2844 -0.0050 0.0075 -0.0051 112 HIS A O 646 C CB . HIS A 86 ? 0.3463 0.2627 0.3675 0.0011 0.0034 -0.0058 112 HIS A CB 647 C CG . HIS A 86 ? 0.3921 0.3131 0.4177 -0.0021 0.0012 -0.0063 112 HIS A CG 648 N ND1 . HIS A 86 ? 0.4201 0.3393 0.4424 -0.0040 -0.0004 -0.0076 112 HIS A ND1 649 C CD2 . HIS A 86 ? 0.3605 0.2872 0.3930 -0.0031 -0.0005 -0.0056 112 HIS A CD2 650 C CE1 . HIS A 86 ? 0.4581 0.3815 0.4842 -0.0065 -0.0038 -0.0070 112 HIS A CE1 651 N NE2 . HIS A 86 ? 0.4614 0.3892 0.4945 -0.0054 -0.0041 -0.0058 112 HIS A NE2 652 N N . ASN A 87 ? 0.2014 0.1132 0.2267 -0.0109 0.0068 -0.0062 113 ASN A N 653 C CA . ASN A 87 ? 0.2081 0.1096 0.2259 -0.0131 0.0061 -0.0070 113 ASN A CA 654 C C . ASN A 87 ? 0.3079 0.2050 0.3241 -0.0204 0.0087 -0.0069 113 ASN A C 655 O O . ASN A 87 ? 0.2627 0.1684 0.2858 -0.0234 0.0113 -0.0070 113 ASN A O 656 C CB . ASN A 87 ? 0.2477 0.1524 0.2674 -0.0140 0.0027 -0.0089 113 ASN A CB 657 C CG . ASN A 87 ? 0.3101 0.2266 0.3408 -0.0176 0.0004 -0.0095 113 ASN A CG 658 O OD1 . ASN A 87 ? 0.3201 0.2411 0.3569 -0.0218 0.0020 -0.0100 113 ASN A OD1 659 N ND2 . ASN A 87 ? 0.2948 0.2164 0.3277 -0.0160 -0.0037 -0.0094 113 ASN A ND2 660 N N . LEU A 88 ? 0.1790 0.0628 0.1860 -0.0239 0.0086 -0.0074 114 LEU A N 661 C CA . LEU A 88 ? 0.2664 0.1438 0.2692 -0.0325 0.0117 -0.0067 114 LEU A CA 662 C C . LEU A 88 ? 0.3104 0.1936 0.3192 -0.0414 0.0111 -0.0093 114 LEU A C 663 O O . LEU A 88 ? 0.3828 0.2730 0.3968 -0.0493 0.0144 -0.0097 114 LEU A O 664 C CB . LEU A 88 ? 0.2372 0.0918 0.2232 -0.0320 0.0118 -0.0047 114 LEU A CB 665 C CG . LEU A 88 ? 0.2297 0.0779 0.2087 -0.0247 0.0117 -0.0014 114 LEU A CG 666 C CD1 . LEU A 88 ? 0.2593 0.0901 0.2252 -0.0217 0.0090 0.0005 114 LEU A CD1 667 C CD2 . LEU A 88 ? 0.2193 0.0743 0.1995 -0.0290 0.0157 0.0008 114 LEU A CD2 668 N N . VAL A 89 ? 0.1948 0.0758 0.2027 -0.0410 0.0072 -0.0116 115 VAL A N 669 C CA . VAL A 89 ? 0.1986 0.0853 0.2115 -0.0497 0.0052 -0.0143 115 VAL A CA 670 C C . VAL A 89 ? 0.2887 0.1880 0.3100 -0.0463 -0.0002 -0.0159 115 VAL A C 671 O O . VAL A 89 ? 0.2161 0.1083 0.2296 -0.0418 -0.0025 -0.0166 115 VAL A O 672 C CB . VAL A 89 ? 0.2697 0.1361 0.2680 -0.0557 0.0048 -0.0157 115 VAL A CB 673 C CG1 . VAL A 89 ? 0.2641 0.1375 0.2676 -0.0661 0.0021 -0.0189 115 VAL A CG1 674 C CG2 . VAL A 89 ? 0.2762 0.1277 0.2634 -0.0585 0.0086 -0.0127 115 VAL A CG2 675 N N . TRP A 90 ? 0.2048 0.1226 0.2414 -0.0483 -0.0022 -0.0166 116 TRP A N 676 C CA . TRP A 90 ? 0.1698 0.0984 0.2137 -0.0444 -0.0084 -0.0169 116 TRP A CA 677 C C . TRP A 90 ? 0.2040 0.1508 0.2645 -0.0490 -0.0118 -0.0188 116 TRP A C 678 O O . TRP A 90 ? 0.1741 0.1310 0.2453 -0.0511 -0.0075 -0.0197 116 TRP A O 679 C CB . TRP A 90 ? 0.1585 0.0902 0.2048 -0.0351 -0.0080 -0.0146 116 TRP A CB 680 C CG . TRP A 90 ? 0.1951 0.1328 0.2444 -0.0313 -0.0146 -0.0137 116 TRP A CG 681 C CD1 . TRP A 90 ? 0.2326 0.1675 0.2754 -0.0337 -0.0202 -0.0143 116 TRP A CD1 682 C CD2 . TRP A 90 ? 0.2502 0.1951 0.3071 -0.0249 -0.0165 -0.0119 116 TRP A CD2 683 N NE1 . TRP A 90 ? 0.1569 0.0965 0.2019 -0.0297 -0.0258 -0.0121 116 TRP A NE1 684 C CE2 . TRP A 90 ? 0.2348 0.1797 0.2886 -0.0240 -0.0238 -0.0107 116 TRP A CE2 685 C CE3 . TRP A 90 ? 0.2506 0.2002 0.3148 -0.0204 -0.0130 -0.0114 116 TRP A CE3 686 C CZ2 . TRP A 90 ? 0.2230 0.1708 0.2806 -0.0188 -0.0279 -0.0083 116 TRP A CZ2 687 C CZ3 . TRP A 90 ? 0.1902 0.1433 0.2592 -0.0148 -0.0168 -0.0100 116 TRP A CZ3 688 C CH2 . TRP A 90 ? 0.2842 0.2355 0.3497 -0.0140 -0.0244 -0.0082 116 TRP A CH2 689 N N . TYR A 91 ? 0.1688 0.1211 0.2319 -0.0507 -0.0194 -0.0198 117 TYR A N 690 C CA . TYR A 91 ? 0.1936 0.1653 0.2746 -0.0546 -0.0241 -0.0221 117 TYR A CA 691 C C . TYR A 91 ? 0.2252 0.2126 0.3234 -0.0463 -0.0259 -0.0216 117 TYR A C 692 O O . TYR A 91 ? 0.2052 0.2114 0.3221 -0.0478 -0.0276 -0.0245 117 TYR A O 693 C CB . TYR A 91 ? 0.2194 0.1921 0.2973 -0.0586 -0.0334 -0.0231 117 TYR A CB 694 C CG . TYR A 91 ? 0.2440 0.2175 0.3203 -0.0512 -0.0417 -0.0204 117 TYR A CG 695 C CD1 . TYR A 91 ? 0.2343 0.1923 0.2935 -0.0470 -0.0405 -0.0179 117 TYR A CD1 696 C CD2 . TYR A 91 ? 0.2573 0.2470 0.3489 -0.0489 -0.0510 -0.0204 117 TYR A CD2 697 C CE1 . TYR A 91 ? 0.2525 0.2097 0.3075 -0.0424 -0.0477 -0.0149 117 TYR A CE1 698 C CE2 . TYR A 91 ? 0.3145 0.3012 0.4015 -0.0429 -0.0597 -0.0169 117 TYR A CE2 699 C CZ . TYR A 91 ? 0.3101 0.2798 0.3776 -0.0406 -0.0576 -0.0139 117 TYR A CZ 700 O OH . TYR A 91 ? 0.2732 0.2383 0.3334 -0.0365 -0.0656 -0.0099 117 TYR A OH 701 N N . GLN A 92 ? 0.1493 0.1295 0.2420 -0.0376 -0.0253 -0.0187 118 GLN A N 702 C CA . GLN A 92 ? 0.2277 0.2188 0.3344 -0.0293 -0.0271 -0.0186 118 GLN A CA 703 C C . GLN A 92 ? 0.2418 0.2328 0.3505 -0.0265 -0.0177 -0.0192 118 GLN A C 704 O O . GLN A 92 ? 0.2522 0.2316 0.3482 -0.0295 -0.0111 -0.0181 118 GLN A O 705 C CB . GLN A 92 ? 0.2949 0.2773 0.3934 -0.0227 -0.0339 -0.0148 118 GLN A CB 706 C CG . GLN A 92 ? 0.4454 0.4262 0.5385 -0.0257 -0.0436 -0.0137 118 GLN A CG 707 C CD . GLN A 92 ? 0.6437 0.6223 0.7360 -0.0192 -0.0527 -0.0102 118 GLN A CD 708 O OE1 . GLN A 92 ? 0.6995 0.6664 0.7799 -0.0160 -0.0512 -0.0071 118 GLN A OE1 709 N NE2 . GLN A 92 ? 0.6454 0.6352 0.7503 -0.0175 -0.0626 -0.0107 118 GLN A NE2 710 N N . GLU A 93 ? 0.2481 0.2507 0.3716 -0.0202 -0.0179 -0.0211 119 GLU A N 711 C CA . GLU A 93 ? 0.2367 0.2408 0.3624 -0.0180 -0.0090 -0.0227 119 GLU A CA 712 C C . GLU A 93 ? 0.2080 0.2119 0.3293 -0.0273 -0.0002 -0.0241 119 GLU A C 713 O O . GLU A 93 ? 0.2187 0.2112 0.3271 -0.0285 0.0062 -0.0223 119 GLU A O 714 C CB . GLU A 93 ? 0.2625 0.2513 0.3742 -0.0125 -0.0080 -0.0192 119 GLU A CB 715 C CG . GLU A 93 ? 0.3696 0.3569 0.4846 -0.0042 -0.0157 -0.0178 119 GLU A CG 716 C CD . GLU A 93 ? 0.5508 0.5246 0.6527 -0.0006 -0.0141 -0.0148 119 GLU A CD 717 O OE1 . GLU A 93 ? 0.4145 0.3778 0.5039 -0.0013 -0.0178 -0.0111 119 GLU A OE1 718 O OE2 . GLU A 93 ? 0.6538 0.6283 0.7577 0.0022 -0.0088 -0.0168 119 GLU A OE2 719 N N . LEU A 94 ? 0.2331 0.2491 0.3644 -0.0345 -0.0009 -0.0270 120 LEU A N 720 C CA . LEU A 94 ? 0.2502 0.2663 0.3776 -0.0457 0.0067 -0.0284 120 LEU A CA 721 C C . LEU A 94 ? 0.2455 0.2839 0.3921 -0.0479 0.0130 -0.0340 120 LEU A C 722 O O . LEU A 94 ? 0.3266 0.3847 0.4941 -0.0433 0.0084 -0.0380 120 LEU A O 723 C CB . LEU A 94 ? 0.2775 0.2915 0.4018 -0.0541 0.0017 -0.0283 120 LEU A CB 724 C CG . LEU A 94 ? 0.2347 0.2429 0.3506 -0.0677 0.0074 -0.0290 120 LEU A CG 725 C CD1 . LEU A 94 ? 0.1912 0.1740 0.2836 -0.0685 0.0127 -0.0248 120 LEU A CD1 726 C CD2 . LEU A 94 ? 0.2072 0.2144 0.3220 -0.0740 -0.0002 -0.0298 120 LEU A CD2 727 N N . ALA A 95 ? 0.2265 0.2625 0.3661 -0.0546 0.0234 -0.0347 121 ALA A N 728 C CA . ALA A 95 ? 0.1905 0.2491 0.3474 -0.0582 0.0313 -0.0411 121 ALA A CA 729 C C . ALA A 95 ? 0.2101 0.2898 0.3850 -0.0670 0.0296 -0.0456 121 ALA A C 730 O O . ALA A 95 ? 0.1858 0.2568 0.3505 -0.0779 0.0288 -0.0434 121 ALA A O 731 C CB . ALA A 95 ? 0.2171 0.2665 0.3583 -0.0665 0.0429 -0.0402 121 ALA A CB 732 N N . PRO A 96 ? 0.1879 0.2956 0.3901 -0.0620 0.0286 -0.0524 122 PRO A N 733 C CA . PRO A 96 ? 0.2101 0.3439 0.4348 -0.0688 0.0258 -0.0578 122 PRO A CA 734 C C . PRO A 96 ? 0.2826 0.4186 0.5011 -0.0881 0.0340 -0.0587 122 PRO A C 735 O O . PRO A 96 ? 0.2375 0.3809 0.4622 -0.0961 0.0282 -0.0596 122 PRO A O 736 C CB . PRO A 96 ? 0.2620 0.4251 0.5150 -0.0605 0.0292 -0.0663 122 PRO A CB 737 C CG . PRO A 96 ? 0.3238 0.4718 0.5699 -0.0447 0.0261 -0.0638 122 PRO A CG 738 C CD . PRO A 96 ? 0.2406 0.3570 0.4544 -0.0490 0.0304 -0.0561 122 PRO A CD 739 N N . TRP A 97 ? 0.2633 0.3913 0.4680 -0.0961 0.0465 -0.0583 123 TRP A N 740 C CA . TRP A 97 ? 0.2070 0.3323 0.3993 -0.1134 0.0535 -0.0574 123 TRP A CA 741 C C . TRP A 97 ? 0.2354 0.3332 0.4047 -0.1215 0.0477 -0.0507 123 TRP A C 742 O O . TRP A 97 ? 0.2710 0.3675 0.4330 -0.1333 0.0487 -0.0496 123 TRP A O 743 C CB . TRP A 97 ? 0.2271 0.3438 0.4027 -0.1188 0.0665 -0.0565 123 TRP A CB 744 C CG . TRP A 97 ? 0.1924 0.2781 0.3437 -0.1158 0.0682 -0.0503 123 TRP A CG 745 C CD1 . TRP A 97 ? 0.1829 0.2646 0.3329 -0.1021 0.0685 -0.0500 123 TRP A CD1 746 C CD2 . TRP A 97 ? 0.2092 0.2608 0.3291 -0.1225 0.0670 -0.0420 123 TRP A CD2 747 N NE1 . TRP A 97 ? 0.2238 0.2736 0.3451 -0.1005 0.0674 -0.0421 123 TRP A NE1 748 C CE2 . TRP A 97 ? 0.2171 0.2483 0.3208 -0.1126 0.0667 -0.0374 123 TRP A CE2 749 C CE3 . TRP A 97 ? 0.2502 0.2854 0.3527 -0.1327 0.0643 -0.0375 123 TRP A CE3 750 C CZ2 . TRP A 97 ? 0.2888 0.2866 0.3634 -0.1143 0.0648 -0.0296 123 TRP A CZ2 751 C CZ3 . TRP A 97 ? 0.2797 0.2798 0.3525 -0.1334 0.0624 -0.0298 123 TRP A CZ3 752 C CH2 . TRP A 97 ? 0.2500 0.2325 0.3102 -0.1248 0.0629 -0.0262 123 TRP A CH2 753 N N . VAL A 98 ? 0.1855 0.2599 0.3418 -0.1137 0.0412 -0.0460 124 VAL A N 754 C CA . VAL A 98 ? 0.2456 0.2932 0.3802 -0.1197 0.0360 -0.0410 124 VAL A CA 755 C C . VAL A 98 ? 0.2852 0.3448 0.4315 -0.1236 0.0266 -0.0434 124 VAL A C 756 O O . VAL A 98 ? 0.2667 0.3131 0.3983 -0.1330 0.0247 -0.0410 124 VAL A O 757 C CB . VAL A 98 ? 0.2630 0.2844 0.3793 -0.1063 0.0302 -0.0350 124 VAL A CB 758 C CG1 . VAL A 98 ? 0.2111 0.2048 0.3050 -0.1120 0.0261 -0.0312 124 VAL A CG1 759 C CG2 . VAL A 98 ? 0.3213 0.3316 0.4257 -0.1012 0.0375 -0.0321 124 VAL A CG2 760 N N . GLU A 99 ? 0.2360 0.3191 0.4065 -0.1141 0.0194 -0.0473 125 GLU A N 761 C CA . GLU A 99 ? 0.3270 0.4177 0.5059 -0.1149 0.0075 -0.0486 125 GLU A CA 762 C C . GLU A 99 ? 0.4203 0.5276 0.6069 -0.1275 0.0071 -0.0512 125 GLU A C 763 O O . GLU A 99 ? 0.4438 0.5518 0.6306 -0.1312 -0.0025 -0.0513 125 GLU A O 764 C CB . GLU A 99 ? 0.3326 0.4409 0.5315 -0.0988 -0.0018 -0.0500 125 GLU A CB 765 C CG . GLU A 99 ? 0.3161 0.3996 0.4968 -0.0856 -0.0068 -0.0439 125 GLU A CG 766 C CD . GLU A 99 ? 0.5562 0.6520 0.7528 -0.0701 -0.0147 -0.0444 125 GLU A CD 767 O OE1 . GLU A 99 ? 0.6676 0.7914 0.8907 -0.0674 -0.0162 -0.0498 125 GLU A OE1 768 O OE2 . GLU A 99 ? 0.5882 0.6655 0.7707 -0.0607 -0.0194 -0.0396 125 GLU A OE2 769 N N . THR A 100 ? 0.4114 0.5308 0.6023 -0.1340 0.0173 -0.0528 126 THR A N 770 C CA . THR A 100 ? 0.4003 0.5354 0.5986 -0.1458 0.0177 -0.0549 126 THR A CA 771 C C . THR A 100 ? 0.3841 0.4935 0.5559 -0.1593 0.0241 -0.0509 126 THR A C 772 O O . THR A 100 ? 0.3552 0.4734 0.5299 -0.1706 0.0253 -0.0524 126 THR A O 773 C CB . THR A 100 ? 0.3893 0.5592 0.6133 -0.1442 0.0243 -0.0609 126 THR A CB 774 O OG1 . THR A 100 ? 0.3228 0.4865 0.5390 -0.1419 0.0363 -0.0608 126 THR A OG1 775 C CG2 . THR A 100 ? 0.3390 0.5356 0.5916 -0.1301 0.0147 -0.0652 126 THR A CG2 776 N N . LEU A 101 ? 0.3516 0.4289 0.4975 -0.1575 0.0275 -0.0457 127 LEU A N 777 C CA . LEU A 101 ? 0.3478 0.3973 0.4667 -0.1678 0.0321 -0.0413 127 LEU A CA 778 C C . LEU A 101 ? 0.3147 0.3468 0.4224 -0.1717 0.0232 -0.0401 127 LEU A C 779 O O . LEU A 101 ? 0.3009 0.3288 0.4101 -0.1642 0.0146 -0.0403 127 LEU A O 780 C CB . LEU A 101 ? 0.3771 0.3982 0.4725 -0.1625 0.0372 -0.0360 127 LEU A CB 781 C CG . LEU A 101 ? 0.3184 0.3522 0.4207 -0.1583 0.0462 -0.0372 127 LEU A CG 782 C CD1 . LEU A 101 ? 0.3223 0.3253 0.3986 -0.1541 0.0496 -0.0311 127 LEU A CD1 783 C CD2 . LEU A 101 ? 0.3300 0.3854 0.4412 -0.1689 0.0551 -0.0408 127 LEU A CD2 784 N N . THR A 102 ? 0.3025 0.3242 0.3979 -0.1838 0.0257 -0.0394 128 THR A N 785 C CA . THR A 102 ? 0.3170 0.3223 0.4014 -0.1883 0.0183 -0.0394 128 THR A CA 786 C C . THR A 102 ? 0.4466 0.4147 0.4998 -0.1923 0.0215 -0.0350 128 THR A C 787 O O . THR A 102 ? 0.4520 0.4120 0.4940 -0.1969 0.0296 -0.0322 128 THR A O 788 C CB . THR A 102 ? 0.4170 0.4468 0.5186 -0.2000 0.0159 -0.0441 128 THR A CB 789 O OG1 . THR A 102 ? 0.4315 0.4675 0.5314 -0.2116 0.0256 -0.0443 128 THR A OG1 790 C CG2 . THR A 102 ? 0.4733 0.5401 0.6068 -0.1941 0.0102 -0.0485 128 THR A CG2 791 N N . GLY A 103 ? 0.3995 0.3453 0.4383 -0.1903 0.0149 -0.0346 129 GLY A N 792 C CA . GLY A 103 ? 0.4693 0.3808 0.4803 -0.1938 0.0165 -0.0315 129 GLY A CA 793 C C . GLY A 103 ? 0.4983 0.3874 0.4908 -0.1878 0.0219 -0.0259 129 GLY A C 794 O O . GLY A 103 ? 0.3949 0.2829 0.3891 -0.1756 0.0217 -0.0241 129 GLY A O 795 N N . GLU A 104 ? 0.4586 0.3293 0.4325 -0.1968 0.0263 -0.0231 130 GLU A N 796 C CA . GLU A 104 ? 0.4497 0.2957 0.4027 -0.1919 0.0299 -0.0174 130 GLU A CA 797 C C . GLU A 104 ? 0.4402 0.3027 0.4024 -0.1882 0.0358 -0.0157 130 GLU A C 798 O O . GLU A 104 ? 0.4817 0.3281 0.4316 -0.1791 0.0365 -0.0114 130 GLU A O 799 C CB . GLU A 104 ? 0.5666 0.3924 0.4986 -0.2047 0.0333 -0.0148 130 GLU A CB 800 C CG . GLU A 104 ? 0.7867 0.5919 0.7060 -0.2091 0.0281 -0.0164 130 GLU A CG 801 C CD . GLU A 104 ? 0.9494 0.7470 0.8565 -0.2271 0.0318 -0.0161 130 GLU A CD 802 O OE1 . GLU A 104 ? 0.9804 0.7801 0.8817 -0.2348 0.0384 -0.0132 130 GLU A OE1 803 O OE2 . GLU A 104 ? 1.0040 0.7933 0.9064 -0.2342 0.0281 -0.0189 130 GLU A OE2 804 N N . ASP A 105 ? 0.4020 0.2971 0.3862 -0.1951 0.0398 -0.0196 131 ASP A N 805 C CA . ASP A 105 ? 0.4157 0.3295 0.4105 -0.1924 0.0464 -0.0196 131 ASP A CA 806 C C . ASP A 105 ? 0.4052 0.3218 0.4086 -0.1765 0.0425 -0.0194 131 ASP A C 807 O O . ASP A 105 ? 0.3437 0.2540 0.3404 -0.1697 0.0458 -0.0164 131 ASP A O 808 C CB . ASP A 105 ? 0.4762 0.4271 0.4958 -0.2019 0.0510 -0.0254 131 ASP A CB 809 C CG . ASP A 105 ? 0.5274 0.4973 0.5560 -0.2008 0.0597 -0.0265 131 ASP A CG 810 O OD1 . ASP A 105 ? 0.4934 0.4440 0.5023 -0.1987 0.0638 -0.0220 131 ASP A OD1 811 O OD2 . ASP A 105 ? 0.6182 0.6227 0.6735 -0.2014 0.0622 -0.0324 131 ASP A OD2 812 N N . LEU A 106 ? 0.3341 0.2595 0.3510 -0.1714 0.0351 -0.0226 132 LEU A N 813 C CA . LEU A 106 ? 0.3111 0.2366 0.3340 -0.1575 0.0306 -0.0225 132 LEU A CA 814 C C . LEU A 106 ? 0.3793 0.2722 0.3787 -0.1480 0.0287 -0.0175 132 LEU A C 815 O O . LEU A 106 ? 0.3257 0.2158 0.3242 -0.1380 0.0294 -0.0155 132 LEU A O 816 C CB . LEU A 106 ? 0.3002 0.2370 0.3368 -0.1556 0.0222 -0.0266 132 LEU A CB 817 C CG . LEU A 106 ? 0.3073 0.2375 0.3439 -0.1420 0.0166 -0.0262 132 LEU A CG 818 C CD1 . LEU A 106 ? 0.2602 0.2096 0.3129 -0.1355 0.0196 -0.0271 132 LEU A CD1 819 C CD2 . LEU A 106 ? 0.3280 0.2637 0.3713 -0.1419 0.0078 -0.0298 132 LEU A CD2 820 N N . TRP A 107 ? 0.3577 0.2269 0.3391 -0.1507 0.0260 -0.0160 133 TRP A N 821 C CA . TRP A 107 ? 0.3519 0.1922 0.3133 -0.1405 0.0236 -0.0120 133 TRP A CA 822 C C . TRP A 107 ? 0.4037 0.2341 0.3529 -0.1393 0.0286 -0.0069 133 TRP A C 823 O O . TRP A 107 ? 0.3753 0.1956 0.3186 -0.1275 0.0271 -0.0042 133 TRP A O 824 C CB . TRP A 107 ? 0.3765 0.1938 0.3217 -0.1437 0.0200 -0.0123 133 TRP A CB 825 C CG . TRP A 107 ? 0.4512 0.2419 0.3793 -0.1315 0.0171 -0.0094 133 TRP A CG 826 C CD1 . TRP A 107 ? 0.4880 0.2530 0.3956 -0.1322 0.0171 -0.0058 133 TRP A CD1 827 C CD2 . TRP A 107 ? 0.4339 0.2227 0.3650 -0.1165 0.0135 -0.0101 133 TRP A CD2 828 N NE1 . TRP A 107 ? 0.5476 0.2961 0.4472 -0.1178 0.0134 -0.0045 133 TRP A NE1 829 C CE2 . TRP A 107 ? 0.5173 0.2810 0.4313 -0.1082 0.0116 -0.0073 133 TRP A CE2 830 C CE3 . TRP A 107 ? 0.4405 0.2466 0.3869 -0.1096 0.0115 -0.0129 133 TRP A CE3 831 C CZ2 . TRP A 107 ? 0.5529 0.3110 0.4667 -0.0932 0.0085 -0.0079 133 TRP A CZ2 832 C CZ3 . TRP A 107 ? 0.5333 0.3317 0.4769 -0.0955 0.0087 -0.0130 133 TRP A CZ3 833 C CH2 . TRP A 107 ? 0.5149 0.2910 0.4433 -0.0875 0.0075 -0.0108 133 TRP A CH2 834 N N . ASN A 108 ? 0.3745 0.2088 0.3197 -0.1518 0.0345 -0.0059 134 ASN A N 835 C CA . ASN A 108 ? 0.3848 0.2103 0.3166 -0.1524 0.0394 -0.0013 134 ASN A CA 836 C C . ASN A 108 ? 0.4500 0.2918 0.3938 -0.1445 0.0422 -0.0016 134 ASN A C 837 O O . ASN A 108 ? 0.3698 0.1982 0.3015 -0.1369 0.0420 0.0025 134 ASN A O 838 C CB . ASN A 108 ? 0.4948 0.3261 0.4218 -0.1688 0.0464 -0.0014 134 ASN A CB 839 C CG . ASN A 108 ? 0.7262 0.5504 0.6386 -0.1705 0.0520 0.0029 134 ASN A CG 840 O OD1 . ASN A 108 ? 0.7558 0.6001 0.6797 -0.1699 0.0575 0.0011 134 ASN A OD1 841 N ND2 . ASN A 108 ? 0.8165 0.6115 0.7029 -0.1727 0.0503 0.0082 134 ASN A ND2 842 N N . ALA A 109 ? 0.3373 0.2082 0.3050 -0.1461 0.0443 -0.0067 135 ALA A N 843 C CA . ALA A 109 ? 0.3141 0.2009 0.2945 -0.1387 0.0471 -0.0080 135 ALA A CA 844 C C . ALA A 109 ? 0.3015 0.1747 0.2783 -0.1238 0.0407 -0.0060 135 ALA A C 845 O O . ALA A 109 ? 0.3111 0.1829 0.2858 -0.1165 0.0423 -0.0042 135 ALA A O 846 C CB . ALA A 109 ? 0.3413 0.2622 0.3503 -0.1419 0.0491 -0.0147 135 ALA A CB 847 N N . THR A 110 ? 0.3019 0.1658 0.2775 -0.1197 0.0337 -0.0067 136 THR A N 848 C CA . THR A 110 ? 0.2903 0.1447 0.2643 -0.1059 0.0280 -0.0061 136 THR A CA 849 C C . THR A 110 ? 0.3050 0.1344 0.2586 -0.0983 0.0262 -0.0010 136 THR A C 850 O O . THR A 110 ? 0.2946 0.1213 0.2474 -0.0874 0.0247 0.0006 136 THR A O 851 C CB . THR A 110 ? 0.3074 0.1606 0.2854 -0.1047 0.0218 -0.0095 136 THR A CB 852 O OG1 . THR A 110 ? 0.2754 0.1534 0.2734 -0.1112 0.0218 -0.0141 136 THR A OG1 853 C CG2 . THR A 110 ? 0.2926 0.1376 0.2685 -0.0909 0.0170 -0.0095 136 THR A CG2 854 N N . VAL A 111 ? 0.3304 0.1423 0.2682 -0.1040 0.0261 0.0015 137 VAL A N 855 C CA . VAL A 111 ? 0.3483 0.1368 0.2669 -0.0976 0.0239 0.0064 137 VAL A CA 856 C C . VAL A 111 ? 0.4193 0.2107 0.3339 -0.0965 0.0276 0.0099 137 VAL A C 857 O O . VAL A 111 ? 0.3504 0.1329 0.2589 -0.0855 0.0243 0.0127 137 VAL A O 858 C CB . VAL A 111 ? 0.3840 0.1530 0.2853 -0.1064 0.0237 0.0085 137 VAL A CB 859 C CG1 . VAL A 111 ? 0.4423 0.1879 0.3237 -0.1003 0.0210 0.0141 137 VAL A CG1 860 C CG2 . VAL A 111 ? 0.3863 0.1485 0.2886 -0.1063 0.0195 0.0048 137 VAL A CG2 861 N N . ASN A 112 ? 0.3457 0.1512 0.2645 -0.1081 0.0346 0.0091 138 ASN A N 862 C CA . ASN A 112 ? 0.3457 0.1546 0.2594 -0.1091 0.0394 0.0115 138 ASN A CA 863 C C . ASN A 112 ? 0.3572 0.1786 0.2841 -0.0985 0.0390 0.0099 138 ASN A C 864 O O . ASN A 112 ? 0.3454 0.1603 0.2636 -0.0929 0.0388 0.0130 138 ASN A O 865 C CB . ASN A 112 ? 0.3514 0.1767 0.2694 -0.1241 0.0483 0.0092 138 ASN A CB 866 C CG . ASN A 112 ? 0.4194 0.2478 0.3298 -0.1265 0.0544 0.0108 138 ASN A CG 867 O OD1 . ASN A 112 ? 0.4434 0.2515 0.3318 -0.1262 0.0528 0.0163 138 ASN A OD1 868 N ND2 . ASN A 112 ? 0.4019 0.2561 0.3306 -0.1287 0.0613 0.0057 138 ASN A ND2 869 N N . HIS A 113 ? 0.2972 0.1355 0.2440 -0.0961 0.0382 0.0049 139 HIS A N 870 C CA . HIS A 113 ? 0.2738 0.1226 0.2331 -0.0863 0.0375 0.0030 139 HIS A CA 871 C C . HIS A 113 ? 0.3525 0.1850 0.3023 -0.0726 0.0305 0.0062 139 HIS A C 872 O O . HIS A 113 ? 0.2875 0.1185 0.2342 -0.0660 0.0306 0.0080 139 HIS A O 873 C CB . HIS A 113 ? 0.2544 0.1220 0.2353 -0.0864 0.0366 -0.0028 139 HIS A CB 874 C CG . HIS A 113 ? 0.2308 0.1139 0.2264 -0.0749 0.0351 -0.0048 139 HIS A CG 875 N ND1 . HIS A 113 ? 0.2193 0.1225 0.2272 -0.0740 0.0398 -0.0073 139 HIS A ND1 876 C CD2 . HIS A 113 ? 0.2386 0.1211 0.2378 -0.0629 0.0289 -0.0049 139 HIS A CD2 877 C CE1 . HIS A 113 ? 0.2014 0.1134 0.2191 -0.0621 0.0359 -0.0083 139 HIS A CE1 878 N NE2 . HIS A 113 ? 0.2122 0.1124 0.2245 -0.0558 0.0294 -0.0066 139 HIS A NE2 879 N N . ILE A 114 ? 0.2799 0.1019 0.2261 -0.0686 0.0248 0.0061 140 ILE A N 880 C CA . ILE A 114 ? 0.2798 0.0906 0.2207 -0.0554 0.0186 0.0075 140 ILE A CA 881 C C . ILE A 114 ? 0.2963 0.0920 0.2211 -0.0519 0.0172 0.0127 140 ILE A C 882 O O . ILE A 114 ? 0.2912 0.0868 0.2158 -0.0422 0.0145 0.0141 140 ILE A O 883 C CB . ILE A 114 ? 0.3260 0.1278 0.2649 -0.0536 0.0144 0.0053 140 ILE A CB 884 C CG1 . ILE A 114 ? 0.3457 0.1619 0.2991 -0.0556 0.0142 0.0003 140 ILE A CG1 885 C CG2 . ILE A 114 ? 0.2923 0.0831 0.2257 -0.0404 0.0093 0.0060 140 ILE A CG2 886 C CD1 . ILE A 114 ? 0.2912 0.0990 0.2410 -0.0581 0.0114 -0.0025 140 ILE A CD1 887 N N . THR A 115 ? 0.3195 0.1028 0.2303 -0.0606 0.0187 0.0158 141 THR A N 888 C CA . THR A 115 ? 0.3406 0.1066 0.2332 -0.0582 0.0161 0.0212 141 THR A CA 889 C C . THR A 115 ? 0.3382 0.1099 0.2276 -0.0589 0.0191 0.0235 141 THR A C 890 O O . THR A 115 ? 0.3401 0.1042 0.2221 -0.0502 0.0144 0.0266 141 THR A O 891 C CB . THR A 115 ? 0.3702 0.1204 0.2463 -0.0694 0.0174 0.0240 141 THR A CB 892 O OG1 . THR A 115 ? 0.4799 0.2210 0.3563 -0.0678 0.0139 0.0218 141 THR A OG1 893 C CG2 . THR A 115 ? 0.5980 0.3288 0.4533 -0.0674 0.0140 0.0300 141 THR A CG2 894 N N . THR A 116 ? 0.3288 0.1146 0.2241 -0.0694 0.0269 0.0215 142 THR A N 895 C CA . THR A 116 ? 0.3333 0.1240 0.2240 -0.0717 0.0313 0.0229 142 THR A CA 896 C C . THR A 116 ? 0.3059 0.1047 0.2071 -0.0601 0.0287 0.0214 142 THR A C 897 O O . THR A 116 ? 0.3111 0.1037 0.2022 -0.0555 0.0264 0.0245 142 THR A O 898 C CB . THR A 116 ? 0.4202 0.2282 0.3187 -0.0852 0.0417 0.0190 142 THR A CB 899 O OG1 . THR A 116 ? 0.3445 0.1465 0.2338 -0.0967 0.0441 0.0200 142 THR A OG1 900 C CG2 . THR A 116 ? 0.3899 0.2022 0.2814 -0.0884 0.0475 0.0196 142 THR A CG2 901 N N . VAL A 117 ? 0.2839 0.0959 0.2039 -0.0557 0.0285 0.0167 143 VAL A N 902 C CA . VAL A 117 ? 0.2625 0.0864 0.1947 -0.0445 0.0258 0.0145 143 VAL A CA 903 C C . VAL A 117 ? 0.3763 0.1857 0.2997 -0.0329 0.0176 0.0178 143 VAL A C 904 O O . VAL A 117 ? 0.2645 0.0779 0.1868 -0.0264 0.0151 0.0190 143 VAL A O 905 C CB . VAL A 117 ? 0.2598 0.1025 0.2136 -0.0417 0.0257 0.0090 143 VAL A CB 906 C CG1 . VAL A 117 ? 0.2200 0.0744 0.1846 -0.0298 0.0217 0.0074 143 VAL A CG1 907 C CG2 . VAL A 117 ? 0.2313 0.0931 0.1980 -0.0504 0.0327 0.0050 143 VAL A CG2 908 N N . MET A 118 ? 0.2875 0.0888 0.2092 -0.0291 0.0128 0.0180 144 MET A N 909 C CA . MET A 118 ? 0.3289 0.1232 0.2476 -0.0169 0.0054 0.0194 144 MET A CA 910 C C . MET A 118 ? 0.3017 0.0818 0.2028 -0.0158 0.0018 0.0251 144 MET A C 911 O O . MET A 118 ? 0.3200 0.1006 0.2209 -0.0062 -0.0035 0.0263 144 MET A O 912 C CB . MET A 118 ? 0.2914 0.0794 0.2118 -0.0137 0.0024 0.0174 144 MET A CB 913 C CG . MET A 118 ? 0.2677 0.0691 0.2038 -0.0129 0.0041 0.0118 144 MET A CG 914 S SD . MET A 118 ? 0.2861 0.0789 0.2222 -0.0087 0.0010 0.0083 144 MET A SD 915 C CE . MET A 118 ? 0.2819 0.0713 0.2175 0.0064 -0.0047 0.0084 144 MET A CE 916 N N . THR A 119 ? 0.3224 0.0907 0.2086 -0.0260 0.0043 0.0286 145 THR A N 917 C CA . THR A 119 ? 0.3456 0.0992 0.2123 -0.0262 0.0006 0.0344 145 THR A CA 918 C C . THR A 119 ? 0.3883 0.1491 0.2531 -0.0258 0.0018 0.0354 145 THR A C 919 O O . THR A 119 ? 0.3787 0.1332 0.2351 -0.0186 -0.0050 0.0388 145 THR A O 920 C CB . THR A 119 ? 0.3708 0.1114 0.2204 -0.0396 0.0045 0.0376 145 THR A CB 921 O OG1 . THR A 119 ? 0.4277 0.1589 0.2771 -0.0399 0.0026 0.0367 145 THR A OG1 922 C CG2 . THR A 119 ? 0.3977 0.1219 0.2248 -0.0402 -0.0001 0.0438 145 THR A CG2 923 N N . HIS A 120 ? 0.3609 0.1350 0.2340 -0.0334 0.0102 0.0321 146 HIS A N 924 C CA . HIS A 120 ? 0.3378 0.1224 0.2114 -0.0333 0.0125 0.0314 146 HIS A CA 925 C C . HIS A 120 ? 0.2992 0.0926 0.1829 -0.0193 0.0046 0.0303 146 HIS A C 926 O O . HIS A 120 ? 0.3069 0.0981 0.1814 -0.0160 0.0000 0.0330 146 HIS A O 927 C CB . HIS A 120 ? 0.3774 0.1863 0.2692 -0.0393 0.0219 0.0248 146 HIS A CB 928 C CG . HIS A 120 ? 0.3413 0.1665 0.2391 -0.0368 0.0237 0.0218 146 HIS A CG 929 N ND1 . HIS A 120 ? 0.3405 0.1651 0.2251 -0.0447 0.0290 0.0222 146 HIS A ND1 930 C CD2 . HIS A 120 ? 0.3519 0.1927 0.2654 -0.0279 0.0209 0.0181 146 HIS A CD2 931 C CE1 . HIS A 120 ? 0.4060 0.2449 0.2986 -0.0402 0.0292 0.0184 146 HIS A CE1 932 N NE2 . HIS A 120 ? 0.3513 0.1996 0.2612 -0.0303 0.0241 0.0162 146 HIS A NE2 933 N N . TYR A 121 ? 0.2801 0.0836 0.1819 -0.0120 0.0031 0.0263 147 TYR A N 934 C CA . TYR A 121 ? 0.3254 0.1417 0.2396 -0.0006 -0.0026 0.0241 147 TYR A CA 935 C C . TYR A 121 ? 0.3253 0.1272 0.2311 0.0094 -0.0121 0.0275 147 TYR A C 936 O O . TYR A 121 ? 0.4190 0.2301 0.3305 0.0178 -0.0178 0.0269 147 TYR A O 937 C CB . TYR A 121 ? 0.2949 0.1281 0.2299 0.0021 0.0000 0.0183 147 TYR A CB 938 C CG . TYR A 121 ? 0.2237 0.0738 0.1686 -0.0039 0.0066 0.0149 147 TYR A CG 939 C CD1 . TYR A 121 ? 0.2530 0.1143 0.2011 -0.0020 0.0060 0.0137 147 TYR A CD1 940 C CD2 . TYR A 121 ? 0.2204 0.0744 0.1710 -0.0115 0.0128 0.0127 147 TYR A CD2 941 C CE1 . TYR A 121 ? 0.2331 0.1071 0.1891 -0.0066 0.0117 0.0101 147 TYR A CE1 942 C CE2 . TYR A 121 ? 0.2312 0.1006 0.1919 -0.0154 0.0182 0.0090 147 TYR A CE2 943 C CZ . TYR A 121 ? 0.2653 0.1434 0.2282 -0.0125 0.0178 0.0076 147 TYR A CZ 944 O OH . TYR A 121 ? 0.3054 0.1966 0.2779 -0.0151 0.0228 0.0032 147 TYR A OH 945 N N . LYS A 122 ? 0.3270 0.1102 0.2215 0.0082 -0.0139 0.0305 148 LYS A N 946 C CA . LYS A 122 ? 0.3853 0.1592 0.2741 0.0177 -0.0229 0.0330 148 LYS A CA 947 C C . LYS A 122 ? 0.4507 0.2160 0.3230 0.0179 -0.0286 0.0386 148 LYS A C 948 O O . LYS A 122 ? 0.4177 0.1843 0.2913 0.0284 -0.0374 0.0396 148 LYS A O 949 C CB . LYS A 122 ? 0.3902 0.1495 0.2716 0.0147 -0.0227 0.0341 148 LYS A CB 950 C CG . LYS A 122 ? 0.4503 0.1963 0.3238 0.0241 -0.0318 0.0368 148 LYS A CG 951 C CD . LYS A 122 ? 0.4750 0.2023 0.3369 0.0187 -0.0311 0.0384 148 LYS A CD 952 C CE . LYS A 122 ? 0.5710 0.2822 0.4235 0.0280 -0.0404 0.0412 148 LYS A CE 953 N NZ . LYS A 122 ? 0.6465 0.3356 0.4833 0.0212 -0.0401 0.0438 148 LYS A NZ 954 N N . GLU A 123 ? 0.3451 0.1033 0.2022 0.0058 -0.0235 0.0419 149 GLU A N 955 C CA . GLU A 123 ? 0.3657 0.1140 0.2029 0.0034 -0.0281 0.0475 149 GLU A CA 956 C C . GLU A 123 ? 0.4640 0.2288 0.3070 0.0051 -0.0286 0.0455 149 GLU A C 957 O O . GLU A 123 ? 0.5191 0.2793 0.3483 0.0057 -0.0348 0.0494 149 GLU A O 958 C CB . GLU A 123 ? 0.4427 0.1792 0.2605 -0.0120 -0.0208 0.0506 149 GLU A CB 959 C CG . GLU A 123 ? 0.5591 0.2821 0.3705 -0.0160 -0.0202 0.0519 149 GLU A CG 960 C CD . GLU A 123 ? 0.8094 0.5278 0.6080 -0.0329 -0.0102 0.0528 149 GLU A CD 961 O OE1 . GLU A 123 ? 0.8201 0.5512 0.6234 -0.0408 -0.0011 0.0498 149 GLU A OE1 962 O OE2 . GLU A 123 ? 0.9132 0.6160 0.6978 -0.0385 -0.0111 0.0558 149 GLU A OE2 963 N N . SER A 124 ? 0.3469 0.1356 0.2125 0.0051 -0.0219 0.0385 150 SER A N 964 C CA . SER A 124 ? 0.3572 0.1656 0.2302 0.0036 -0.0198 0.0348 150 SER A CA 965 C C . SER A 124 ? 0.2819 0.1101 0.1759 0.0135 -0.0244 0.0304 150 SER A C 966 O O . SER A 124 ? 0.2855 0.1246 0.1809 0.0145 -0.0275 0.0292 150 SER A O 967 C CB . SER A 124 ? 0.4226 0.2420 0.3026 -0.0065 -0.0076 0.0301 150 SER A CB 968 O OG . SER A 124 ? 0.6567 0.4628 0.5170 -0.0176 -0.0022 0.0332 150 SER A OG 969 N N . PHE A 125 ? 0.2954 0.1282 0.2045 0.0195 -0.0243 0.0277 151 PHE A N 970 C CA . PHE A 125 ? 0.2908 0.1444 0.2204 0.0263 -0.0260 0.0226 151 PHE A CA 971 C C . PHE A 125 ? 0.3063 0.1582 0.2443 0.0364 -0.0306 0.0215 151 PHE A C 972 O O . PHE A 125 ? 0.3028 0.1352 0.2302 0.0388 -0.0331 0.0247 151 PHE A O 973 C CB . PHE A 125 ? 0.2251 0.0932 0.1683 0.0204 -0.0172 0.0176 151 PHE A CB 974 C CG . PHE A 125 ? 0.2424 0.1151 0.1809 0.0126 -0.0126 0.0166 151 PHE A CG 975 C CD1 . PHE A 125 ? 0.2180 0.1021 0.1593 0.0133 -0.0156 0.0148 151 PHE A CD1 976 C CD2 . PHE A 125 ? 0.2625 0.1291 0.1944 0.0042 -0.0050 0.0166 151 PHE A CD2 977 C CE1 . PHE A 125 ? 0.2186 0.1051 0.1545 0.0065 -0.0112 0.0128 151 PHE A CE1 978 C CE2 . PHE A 125 ? 0.2620 0.1336 0.1904 -0.0021 0.0001 0.0143 151 PHE A CE2 979 C CZ . PHE A 125 ? 0.2392 0.1196 0.1689 -0.0006 -0.0031 0.0123 151 PHE A CZ 980 N N . ASN A 126 ? 0.2780 0.1494 0.2340 0.0419 -0.0313 0.0166 152 ASN A N 981 C CA . ASN A 126 ? 0.2722 0.1455 0.2383 0.0512 -0.0337 0.0136 152 ASN A CA 982 C C . ASN A 126 ? 0.2272 0.1096 0.2049 0.0473 -0.0257 0.0089 152 ASN A C 983 O O . ASN A 126 ? 0.2852 0.1863 0.2750 0.0452 -0.0230 0.0053 152 ASN A O 984 C CB . ASN A 126 ? 0.2275 0.1181 0.2058 0.0606 -0.0406 0.0108 152 ASN A CB 985 C CG . ASN A 126 ? 0.3730 0.2523 0.3408 0.0683 -0.0513 0.0154 152 ASN A CG 986 O OD1 . ASN A 126 ? 0.3794 0.2375 0.3366 0.0736 -0.0551 0.0183 152 ASN A OD1 987 N ND2 . ASN A 126 ? 0.3180 0.2103 0.2879 0.0690 -0.0571 0.0159 152 ASN A ND2 988 N N . ILE A 127 ? 0.2188 0.0866 0.1911 0.0453 -0.0225 0.0092 153 ILE A N 989 C CA . ILE A 127 ? 0.2046 0.0797 0.1861 0.0417 -0.0163 0.0050 153 ILE A CA 990 C C . ILE A 127 ? 0.2076 0.0845 0.1961 0.0508 -0.0180 0.0005 153 ILE A C 991 O O . ILE A 127 ? 0.2254 0.0847 0.2061 0.0560 -0.0209 0.0011 153 ILE A O 992 C CB . ILE A 127 ? 0.2208 0.0824 0.1943 0.0330 -0.0114 0.0067 153 ILE A CB 993 C CG1 . ILE A 127 ? 0.3014 0.1694 0.2745 0.0239 -0.0071 0.0081 153 ILE A CG1 994 C CG2 . ILE A 127 ? 0.2002 0.0660 0.1814 0.0316 -0.0076 0.0023 153 ILE A CG2 995 C CD1 . ILE A 127 ? 0.5039 0.3714 0.4694 0.0233 -0.0096 0.0113 153 ILE A CD1 996 N N . TYR A 128 ? 0.1927 0.0897 0.1949 0.0525 -0.0161 -0.0044 154 TYR A N 997 C CA . TYR A 128 ? 0.1956 0.0978 0.2055 0.0608 -0.0162 -0.0101 154 TYR A CA 998 C C . TYR A 128 ? 0.2456 0.1349 0.2505 0.0585 -0.0123 -0.0125 154 TYR A C 999 O O . TYR A 128 ? 0.2193 0.0977 0.2218 0.0661 -0.0140 -0.0155 154 TYR A O 1000 C CB . TYR A 128 ? 0.1797 0.1075 0.2039 0.0602 -0.0135 -0.0150 154 TYR A CB 1001 C CG . TYR A 128 ? 0.1828 0.1173 0.2144 0.0668 -0.0111 -0.0222 154 TYR A CG 1002 C CD1 . TYR A 128 ? 0.2172 0.1537 0.2545 0.0794 -0.0155 -0.0258 154 TYR A CD1 1003 C CD2 . TYR A 128 ? 0.1879 0.1262 0.2203 0.0608 -0.0048 -0.0258 154 TYR A CD2 1004 C CE1 . TYR A 128 ? 0.3421 0.2856 0.3870 0.0862 -0.0125 -0.0339 154 TYR A CE1 1005 C CE2 . TYR A 128 ? 0.1816 0.1259 0.2191 0.0662 -0.0017 -0.0334 154 TYR A CE2 1006 C CZ . TYR A 128 ? 0.3065 0.2539 0.3508 0.0789 -0.0049 -0.0379 154 TYR A CZ 1007 O OH . TYR A 128 ? 0.2358 0.1899 0.2858 0.0848 -0.0009 -0.0467 154 TYR A OH 1008 N N . ALA A 129 ? 0.1909 0.0813 0.1944 0.0483 -0.0077 -0.0115 155 ALA A N 1009 C CA . ALA A 129 ? 0.2011 0.0817 0.2003 0.0444 -0.0045 -0.0139 155 ALA A CA 1010 C C . ALA A 129 ? 0.2589 0.1344 0.2535 0.0337 -0.0022 -0.0101 155 ALA A C 1011 O O . ALA A 129 ? 0.2620 0.1482 0.2610 0.0290 -0.0012 -0.0078 155 ALA A O 1012 C CB . ALA A 129 ? 0.2224 0.1178 0.2295 0.0444 -0.0008 -0.0200 155 ALA A CB 1013 N N . TRP A 130 ? 0.2020 0.0617 0.1886 0.0299 -0.0015 -0.0101 156 TRP A N 1014 C CA . TRP A 130 ? 0.2833 0.1408 0.2681 0.0195 0.0008 -0.0081 156 TRP A CA 1015 C C . TRP A 130 ? 0.2647 0.1254 0.2517 0.0153 0.0025 -0.0120 156 TRP A C 1016 O O . TRP A 130 ? 0.2206 0.0713 0.2024 0.0177 0.0024 -0.0157 156 TRP A O 1017 C CB . TRP A 130 ? 0.2475 0.0885 0.2222 0.0152 0.0003 -0.0047 156 TRP A CB 1018 C CG . TRP A 130 ? 0.2493 0.0880 0.2196 0.0131 0.0000 0.0004 156 TRP A CG 1019 C CD1 . TRP A 130 ? 0.2845 0.1144 0.2470 0.0173 -0.0032 0.0039 156 TRP A CD1 1020 C CD2 . TRP A 130 ? 0.2398 0.0866 0.2132 0.0061 0.0032 0.0021 156 TRP A CD2 1021 N NE1 . TRP A 130 ? 0.2910 0.1196 0.2481 0.0125 -0.0020 0.0079 156 TRP A NE1 1022 C CE2 . TRP A 130 ? 0.2247 0.0650 0.1896 0.0057 0.0025 0.0063 156 TRP A CE2 1023 C CE3 . TRP A 130 ? 0.2267 0.0880 0.2105 0.0005 0.0061 0.0002 156 TRP A CE3 1024 C CZ2 . TRP A 130 ? 0.2648 0.1135 0.2313 -0.0004 0.0060 0.0076 156 TRP A CZ2 1025 C CZ3 . TRP A 130 ? 0.3594 0.2290 0.3466 -0.0042 0.0088 0.0015 156 TRP A CZ3 1026 C CH2 . TRP A 130 ? 0.2924 0.1561 0.2710 -0.0048 0.0094 0.0047 156 TRP A CH2 1027 N N . ASP A 131 ? 0.2580 0.1313 0.2517 0.0094 0.0036 -0.0115 157 ASP A N 1028 C CA . ASP A 131 ? 0.2675 0.1413 0.2610 0.0034 0.0038 -0.0139 157 ASP A CA 1029 C C . ASP A 131 ? 0.2532 0.1167 0.2427 -0.0037 0.0040 -0.0124 157 ASP A C 1030 O O . ASP A 131 ? 0.2703 0.1409 0.2653 -0.0086 0.0047 -0.0100 157 ASP A O 1031 C CB . ASP A 131 ? 0.2493 0.1386 0.2509 0.0002 0.0033 -0.0133 157 ASP A CB 1032 C CG . ASP A 131 ? 0.4017 0.3009 0.4056 0.0043 0.0037 -0.0149 157 ASP A CG 1033 O OD1 . ASP A 131 ? 0.3952 0.2920 0.3956 0.0088 0.0049 -0.0185 157 ASP A OD1 1034 O OD2 . ASP A 131 ? 0.3623 0.2714 0.3713 0.0027 0.0030 -0.0129 157 ASP A OD2 1035 N N . VAL A 132 ? 0.2083 0.0553 0.1882 -0.0046 0.0037 -0.0143 158 VAL A N 1036 C CA . VAL A 132 ? 0.2184 0.0572 0.1943 -0.0129 0.0040 -0.0126 158 VAL A CA 1037 C C . VAL A 132 ? 0.3070 0.1522 0.2873 -0.0220 0.0038 -0.0146 158 VAL A C 1038 O O . VAL A 132 ? 0.3911 0.2458 0.3786 -0.0284 0.0046 -0.0128 158 VAL A O 1039 C CB . VAL A 132 ? 0.2579 0.0819 0.2245 -0.0115 0.0028 -0.0133 158 VAL A CB 1040 C CG1 . VAL A 132 ? 0.2767 0.0943 0.2392 -0.0220 0.0035 -0.0114 158 VAL A CG1 1041 C CG2 . VAL A 132 ? 0.2988 0.1176 0.2624 -0.0024 0.0018 -0.0109 158 VAL A CG2 1042 N N . VAL A 133 ? 0.2300 0.0733 0.2072 -0.0222 0.0022 -0.0187 159 VAL A N 1043 C CA . VAL A 133 ? 0.2163 0.0684 0.1977 -0.0299 -0.0001 -0.0205 159 VAL A CA 1044 C C . VAL A 133 ? 0.2773 0.1442 0.2646 -0.0262 -0.0019 -0.0210 159 VAL A C 1045 O O . VAL A 133 ? 0.2540 0.1192 0.2369 -0.0201 -0.0010 -0.0230 159 VAL A O 1046 C CB . VAL A 133 ? 0.2364 0.0732 0.2065 -0.0351 -0.0012 -0.0249 159 VAL A CB 1047 C CG1 . VAL A 133 ? 0.2400 0.0871 0.2134 -0.0422 -0.0049 -0.0271 159 VAL A CG1 1048 C CG2 . VAL A 133 ? 0.2773 0.1059 0.2444 -0.0397 -0.0003 -0.0230 159 VAL A CG2 1049 N N . ASN A 134 ? 0.2127 0.0939 0.2100 -0.0299 -0.0046 -0.0192 160 ASN A N 1050 C CA . ASN A 134 ? 0.1830 0.0754 0.1839 -0.0276 -0.0076 -0.0185 160 ASN A CA 1051 C C . ASN A 134 ? 0.2207 0.1178 0.2222 -0.0343 -0.0131 -0.0197 160 ASN A C 1052 O O . ASN A 134 ? 0.2160 0.1175 0.2245 -0.0399 -0.0151 -0.0198 160 ASN A O 1053 C CB . ASN A 134 ? 0.1956 0.0994 0.2077 -0.0239 -0.0074 -0.0149 160 ASN A CB 1054 C CG . ASN A 134 ? 0.3131 0.2240 0.3260 -0.0212 -0.0102 -0.0134 160 ASN A CG 1055 O OD1 . ASN A 134 ? 0.3665 0.2740 0.3706 -0.0204 -0.0098 -0.0149 160 ASN A OD1 1056 N ND2 . ASN A 134 ? 0.2278 0.1477 0.2505 -0.0202 -0.0128 -0.0109 160 ASN A ND2 1057 N N . GLU A 135 ? 0.2146 0.1110 0.2080 -0.0345 -0.0155 -0.0210 161 GLU A N 1058 C CA . GLU A 135 ? 0.2021 0.1028 0.1938 -0.0404 -0.0224 -0.0213 161 GLU A CA 1059 C C . GLU A 135 ? 0.2610 0.1578 0.2511 -0.0483 -0.0248 -0.0244 161 GLU A C 1060 O O . GLU A 135 ? 0.2560 0.1627 0.2560 -0.0528 -0.0302 -0.0235 161 GLU A O 1061 C CB . GLU A 135 ? 0.2405 0.1544 0.2449 -0.0387 -0.0278 -0.0169 161 GLU A CB 1062 C CG . GLU A 135 ? 0.2017 0.1170 0.2045 -0.0329 -0.0265 -0.0138 161 GLU A CG 1063 C CD . GLU A 135 ? 0.2791 0.2033 0.2932 -0.0300 -0.0318 -0.0097 161 GLU A CD 1064 O OE1 . GLU A 135 ? 0.2719 0.2036 0.2966 -0.0315 -0.0372 -0.0095 161 GLU A OE1 1065 O OE2 . GLU A 135 ? 0.3141 0.2379 0.3270 -0.0261 -0.0306 -0.0071 161 GLU A OE2 1066 N N . ALA A 136 ? 0.2316 0.1140 0.2095 -0.0500 -0.0210 -0.0287 162 ALA A N 1067 C CA . ALA A 136 ? 0.3114 0.1864 0.2854 -0.0586 -0.0226 -0.0320 162 ALA A CA 1068 C C . ALA A 136 ? 0.2823 0.1550 0.2454 -0.0654 -0.0282 -0.0356 162 ALA A C 1069 O O . ALA A 136 ? 0.3213 0.1885 0.2805 -0.0738 -0.0306 -0.0388 162 ALA A O 1070 C CB . ALA A 136 ? 0.2473 0.1038 0.2120 -0.0572 -0.0165 -0.0349 162 ALA A CB 1071 N N . PHE A 137 ? 0.2493 0.1256 0.2061 -0.0628 -0.0304 -0.0349 163 PHE A N 1072 C CA . PHE A 137 ? 0.2656 0.1383 0.2082 -0.0696 -0.0356 -0.0382 163 PHE A CA 1073 C C . PHE A 137 ? 0.2941 0.1797 0.2404 -0.0715 -0.0449 -0.0335 163 PHE A C 1074 O O . PHE A 137 ? 0.2476 0.1426 0.2046 -0.0657 -0.0459 -0.0282 163 PHE A O 1075 C CB . PHE A 137 ? 0.2989 0.1605 0.2243 -0.0667 -0.0296 -0.0430 163 PHE A CB 1076 C CG . PHE A 137 ? 0.3684 0.2153 0.2892 -0.0632 -0.0220 -0.0482 163 PHE A CG 1077 C CD1 . PHE A 137 ? 0.3578 0.1896 0.2660 -0.0694 -0.0221 -0.0547 163 PHE A CD1 1078 C CD2 . PHE A 137 ? 0.3475 0.1940 0.2758 -0.0539 -0.0157 -0.0466 163 PHE A CD2 1079 C CE1 . PHE A 137 ? 0.3596 0.1765 0.2638 -0.0647 -0.0160 -0.0589 163 PHE A CE1 1080 C CE2 . PHE A 137 ? 0.3775 0.2088 0.3012 -0.0496 -0.0104 -0.0508 163 PHE A CE2 1081 C CZ . PHE A 137 ? 0.3363 0.1511 0.2473 -0.0549 -0.0106 -0.0571 163 PHE A CZ 1082 N N . ASN A 138 ? 0.3497 0.2340 0.2862 -0.0798 -0.0523 -0.0357 164 ASN A N 1083 C CA . ASN A 138 ? 0.2951 0.1873 0.2290 -0.0820 -0.0628 -0.0314 164 ASN A CA 1084 C C . ASN A 138 ? 0.3666 0.2499 0.2783 -0.0827 -0.0607 -0.0322 164 ASN A C 1085 O O . ASN A 138 ? 0.3046 0.1770 0.2031 -0.0833 -0.0522 -0.0383 164 ASN A O 1086 C CB . ASN A 138 ? 0.2939 0.1905 0.2280 -0.0913 -0.0733 -0.0332 164 ASN A CB 1087 C CG . ASN A 138 ? 0.2818 0.1918 0.2399 -0.0920 -0.0757 -0.0325 164 ASN A CG 1088 O OD1 . ASN A 138 ? 0.2975 0.2188 0.2736 -0.0849 -0.0754 -0.0283 164 ASN A OD1 1089 N ND2 . ASN A 138 ? 0.3068 0.2158 0.2646 -0.1014 -0.0776 -0.0374 164 ASN A ND2 1090 N N . ASP A 139 ? 0.3678 0.2553 0.2749 -0.0830 -0.0684 -0.0265 165 ASP A N 1091 C CA . ASP A 139 ? 0.4597 0.3393 0.3437 -0.0859 -0.0666 -0.0265 165 ASP A CA 1092 C C . ASP A 139 ? 0.4320 0.3013 0.2932 -0.0949 -0.0659 -0.0338 165 ASP A C 1093 O O . ASP A 139 ? 0.4546 0.3169 0.2980 -0.0963 -0.0579 -0.0378 165 ASP A O 1094 C CB . ASP A 139 ? 0.5171 0.3999 0.3978 -0.0865 -0.0778 -0.0179 165 ASP A CB 1095 C CG . ASP A 139 ? 0.6737 0.5626 0.5713 -0.0775 -0.0764 -0.0116 165 ASP A CG 1096 O OD1 . ASP A 139 ? 0.6778 0.5676 0.5832 -0.0719 -0.0652 -0.0136 165 ASP A OD1 1097 O OD2 . ASP A 139 ? 0.7713 0.6636 0.6743 -0.0756 -0.0874 -0.0048 165 ASP A OD2 1098 N N . ASN A 140 ? 0.3461 0.2152 0.2074 -0.1014 -0.0736 -0.0365 166 ASN A N 1099 C CA . ASN A 140 ? 0.3712 0.2291 0.2094 -0.1104 -0.0732 -0.0442 166 ASN A CA 1100 C C . ASN A 140 ? 0.4197 0.2684 0.2575 -0.1083 -0.0610 -0.0531 166 ASN A C 1101 O O . ASN A 140 ? 0.4343 0.2761 0.2589 -0.1124 -0.0585 -0.0592 166 ASN A O 1102 C CB . ASN A 140 ? 0.4169 0.2811 0.2568 -0.1167 -0.0853 -0.0425 166 ASN A CB 1103 C CG . ASN A 140 ? 0.4672 0.3419 0.3328 -0.1155 -0.0892 -0.0418 166 ASN A CG 1104 O OD1 . ASN A 140 ? 0.3634 0.2368 0.2419 -0.1112 -0.0810 -0.0439 166 ASN A OD1 1105 N ND2 . ASN A 140 ? 0.4935 0.3796 0.3671 -0.1194 -0.1015 -0.0389 166 ASN A ND2 1106 N N . GLY A 141 ? 0.4383 0.2878 0.2923 -0.1002 -0.0534 -0.0529 167 GLY A N 1107 C CA . GLY A 141 ? 0.5284 0.3659 0.3803 -0.0971 -0.0430 -0.0607 167 GLY A CA 1108 C C . GLY A 141 ? 0.5114 0.3476 0.3755 -0.0985 -0.0441 -0.0618 167 GLY A C 1109 O O . GLY A 141 ? 0.5120 0.3372 0.3738 -0.0953 -0.0367 -0.0671 167 GLY A O 1110 N N . THR A 142 ? 0.4206 0.2685 0.2980 -0.1032 -0.0535 -0.0568 168 THR A N 1111 C CA . THR A 142 ? 0.3485 0.1981 0.2393 -0.1058 -0.0536 -0.0574 168 THR A CA 1112 C C . THR A 142 ? 0.3275 0.1812 0.2366 -0.1000 -0.0496 -0.0534 168 THR A C 1113 O O . THR A 142 ? 0.3249 0.1838 0.2393 -0.0941 -0.0491 -0.0492 168 THR A O 1114 C CB . THR A 142 ? 0.3697 0.2330 0.2680 -0.1142 -0.0649 -0.0553 168 THR A CB 1115 O OG1 . THR A 142 ? 0.3380 0.2162 0.2476 -0.1125 -0.0734 -0.0488 168 THR A OG1 1116 C CG2 . THR A 142 ? 0.3762 0.2340 0.2551 -0.1205 -0.0689 -0.0593 168 THR A CG2 1117 N N . TYR A 143 ? 0.3274 0.1793 0.2456 -0.1017 -0.0463 -0.0542 169 TYR A N 1118 C CA . TYR A 143 ? 0.3238 0.1806 0.2585 -0.0977 -0.0426 -0.0501 169 TYR A CA 1119 C C . TYR A 143 ? 0.3029 0.1803 0.2560 -0.1007 -0.0506 -0.0454 169 TYR A C 1120 O O . TYR A 143 ? 0.3000 0.1887 0.2586 -0.1080 -0.0581 -0.0461 169 TYR A O 1121 C CB . TYR A 143 ? 0.3261 0.1750 0.2633 -0.1002 -0.0374 -0.0517 169 TYR A CB 1122 C CG . TYR A 143 ? 0.3536 0.1816 0.2759 -0.0948 -0.0304 -0.0556 169 TYR A CG 1123 C CD1 . TYR A 143 ? 0.3805 0.2010 0.3019 -0.0842 -0.0240 -0.0544 169 TYR A CD1 1124 C CD2 . TYR A 143 ? 0.3549 0.1712 0.2650 -0.0997 -0.0306 -0.0606 169 TYR A CD2 1125 C CE1 . TYR A 143 ? 0.4077 0.2109 0.3180 -0.0778 -0.0187 -0.0583 169 TYR A CE1 1126 C CE2 . TYR A 143 ? 0.4274 0.2246 0.3252 -0.0937 -0.0249 -0.0647 169 TYR A CE2 1127 C CZ . TYR A 143 ? 0.3888 0.1801 0.2876 -0.0823 -0.0193 -0.0636 169 TYR A CZ 1128 O OH . TYR A 143 ? 0.5340 0.3080 0.4230 -0.0752 -0.0147 -0.0680 169 TYR A OH 1129 N N . ARG A 144 ? 0.2758 0.1619 0.2413 -0.0922 -0.0482 -0.0405 170 ARG A N 1130 C CA . ARG A 144 ? 0.2598 0.1681 0.2469 -0.0910 -0.0537 -0.0362 170 ARG A CA 1131 C C . ARG A 144 ? 0.2802 0.1962 0.2810 -0.0992 -0.0528 -0.0379 170 ARG A C 1132 O O . ARG A 144 ? 0.2613 0.1673 0.2605 -0.1002 -0.0445 -0.0387 170 ARG A O 1133 C CB . ARG A 144 ? 0.3513 0.2653 0.3479 -0.0795 -0.0494 -0.0313 170 ARG A CB 1134 C CG . ARG A 144 ? 0.2265 0.1619 0.2452 -0.0763 -0.0548 -0.0278 170 ARG A CG 1135 C CD . ARG A 144 ? 0.2100 0.1483 0.2368 -0.0659 -0.0491 -0.0240 170 ARG A CD 1136 N NE . ARG A 144 ? 0.2293 0.1594 0.2439 -0.0595 -0.0490 -0.0213 170 ARG A NE 1137 C CZ . ARG A 144 ? 0.3214 0.2562 0.3352 -0.0571 -0.0571 -0.0181 170 ARG A CZ 1138 N NH1 . ARG A 144 ? 0.2519 0.1994 0.2774 -0.0587 -0.0671 -0.0172 170 ARG A NH1 1139 N NH2 . ARG A 144 ? 0.3119 0.2386 0.3131 -0.0532 -0.0557 -0.0157 170 ARG A NH2 1140 N N . GLU A 145 ? 0.2824 0.2167 0.2966 -0.1053 -0.0615 -0.0385 171 GLU A N 1141 C CA . GLU A 145 ? 0.2911 0.2369 0.3202 -0.1148 -0.0604 -0.0409 171 GLU A CA 1142 C C . GLU A 145 ? 0.3498 0.3142 0.4020 -0.1092 -0.0560 -0.0383 171 GLU A C 1143 O O . GLU A 145 ? 0.3428 0.3317 0.4167 -0.1108 -0.0614 -0.0391 171 GLU A O 1144 C CB . GLU A 145 ? 0.3486 0.3101 0.3845 -0.1229 -0.0707 -0.0437 171 GLU A CB 1145 C CG . GLU A 145 ? 0.4134 0.3585 0.4264 -0.1266 -0.0727 -0.0468 171 GLU A CG 1146 C CD . GLU A 145 ? 0.5731 0.5289 0.5914 -0.1366 -0.0776 -0.0509 171 GLU A CD 1147 O OE1 . GLU A 145 ? 0.6503 0.6273 0.6910 -0.1409 -0.0787 -0.0518 171 GLU A OE1 1148 O OE2 . GLU A 145 ? 0.6364 0.5800 0.6367 -0.1404 -0.0801 -0.0537 171 GLU A OE2 1149 N N . ASN A 146 ? 0.2349 0.1883 0.2826 -0.1024 -0.0464 -0.0360 172 ASN A N 1150 C CA . ASN A 146 ? 0.2614 0.2285 0.3267 -0.0987 -0.0403 -0.0344 172 ASN A CA 1151 C C . ASN A 146 ? 0.2291 0.1980 0.2983 -0.1113 -0.0342 -0.0371 172 ASN A C 1152 O O . ASN A 146 ? 0.2695 0.2297 0.3292 -0.1227 -0.0360 -0.0401 172 ASN A O 1153 C CB . ASN A 146 ? 0.2122 0.1660 0.2690 -0.0878 -0.0331 -0.0308 172 ASN A CB 1154 C CG . ASN A 146 ? 0.3124 0.2388 0.3465 -0.0896 -0.0272 -0.0311 172 ASN A CG 1155 O OD1 . ASN A 146 ? 0.2409 0.1566 0.2670 -0.0998 -0.0251 -0.0336 172 ASN A OD1 1156 N ND2 . ASN A 146 ? 0.2369 0.1519 0.2610 -0.0794 -0.0248 -0.0289 172 ASN A ND2 1157 N N . VAL A 147 ? 0.2202 0.1992 0.3015 -0.1103 -0.0267 -0.0363 173 VAL A N 1158 C CA . VAL A 147 ? 0.2600 0.2438 0.3459 -0.1243 -0.0205 -0.0389 173 VAL A CA 1159 C C . VAL A 147 ? 0.2718 0.2255 0.3325 -0.1281 -0.0158 -0.0368 173 VAL A C 1160 O O . VAL A 147 ? 0.2656 0.2181 0.3237 -0.1371 -0.0155 -0.0380 173 VAL A O 1161 C CB . VAL A 147 ? 0.3390 0.3393 0.4406 -0.1219 -0.0121 -0.0384 173 VAL A CB 1162 C CG1 . VAL A 147 ? 0.2126 0.1950 0.3012 -0.1110 -0.0060 -0.0340 173 VAL A CG1 1163 C CG2 . VAL A 147 ? 0.3891 0.3944 0.4920 -0.1345 -0.0057 -0.0392 173 VAL A CG2 1164 N N . TRP A 148 ? 0.2510 0.1813 0.2942 -0.1196 -0.0127 -0.0339 174 TRP A N 1165 C CA . TRP A 148 ? 0.3047 0.2084 0.3265 -0.1195 -0.0091 -0.0322 174 TRP A CA 1166 C C . TRP A 148 ? 0.2857 0.1789 0.2967 -0.1226 -0.0144 -0.0354 174 TRP A C 1167 O O . TRP A 148 ? 0.3052 0.1867 0.3064 -0.1291 -0.0128 -0.0359 174 TRP A O 1168 C CB . TRP A 148 ? 0.3534 0.2386 0.3624 -0.1078 -0.0057 -0.0289 174 TRP A CB 1169 C CG . TRP A 148 ? 0.2689 0.1627 0.2862 -0.1050 -0.0003 -0.0260 174 TRP A CG 1170 C CD1 . TRP A 148 ? 0.2614 0.1514 0.2750 -0.1085 0.0060 -0.0231 174 TRP A CD1 1171 C CD2 . TRP A 148 ? 0.2463 0.1544 0.2762 -0.0976 -0.0006 -0.0258 174 TRP A CD2 1172 N NE1 . TRP A 148 ? 0.2466 0.1473 0.2692 -0.1046 0.0103 -0.0218 174 TRP A NE1 1173 C CE2 . TRP A 148 ? 0.2605 0.1731 0.2945 -0.0967 0.0063 -0.0235 174 TRP A CE2 1174 C CE3 . TRP A 148 ? 0.2193 0.1385 0.2569 -0.0883 -0.0068 -0.0262 174 TRP A CE3 1175 C CZ2 . TRP A 148 ? 0.2097 0.1379 0.2562 -0.0865 0.0072 -0.0223 174 TRP A CZ2 1176 C CZ3 . TRP A 148 ? 0.2457 0.1789 0.2952 -0.0783 -0.0063 -0.0243 174 TRP A CZ3 1177 C CH2 . TRP A 148 ? 0.1965 0.1342 0.2509 -0.0773 0.0007 -0.0228 174 TRP A CH2 1178 N N . TYR A 149 ? 0.2795 0.1763 0.2907 -0.1187 -0.0208 -0.0376 175 TYR A N 1179 C CA . TYR A 149 ? 0.2951 0.1842 0.2957 -0.1225 -0.0258 -0.0413 175 TYR A CA 1180 C C . TYR A 149 ? 0.3467 0.2502 0.3574 -0.1349 -0.0290 -0.0438 175 TYR A C 1181 O O . TYR A 149 ? 0.3390 0.2300 0.3384 -0.1411 -0.0288 -0.0459 175 TYR A O 1182 C CB . TYR A 149 ? 0.2879 0.1815 0.2867 -0.1175 -0.0326 -0.0427 175 TYR A CB 1183 C CG . TYR A 149 ? 0.3061 0.1920 0.2922 -0.1221 -0.0375 -0.0468 175 TYR A CG 1184 C CD1 . TYR A 149 ? 0.3654 0.2282 0.3311 -0.1177 -0.0344 -0.0489 175 TYR A CD1 1185 C CD2 . TYR A 149 ? 0.3295 0.2321 0.3245 -0.1307 -0.0452 -0.0492 175 TYR A CD2 1186 C CE1 . TYR A 149 ? 0.3394 0.1945 0.2924 -0.1223 -0.0381 -0.0533 175 TYR A CE1 1187 C CE2 . TYR A 149 ? 0.4054 0.3002 0.3871 -0.1354 -0.0496 -0.0531 175 TYR A CE2 1188 C CZ . TYR A 149 ? 0.4295 0.2998 0.3894 -0.1315 -0.0457 -0.0552 175 TYR A CZ 1189 O OH . TYR A 149 ? 0.4640 0.3260 0.4098 -0.1365 -0.0494 -0.0597 175 TYR A OH 1190 N N . THR A 150 ? 0.2921 0.1457 0.3529 -0.0794 -0.0215 -0.0315 176 THR A N 1191 C CA . THR A 150 ? 0.2752 0.1380 0.3506 -0.0861 -0.0243 -0.0354 176 THR A CA 1192 C C . THR A 150 ? 0.3619 0.2212 0.4408 -0.0926 -0.0180 -0.0329 176 THR A C 1193 O O . THR A 150 ? 0.3474 0.2068 0.4318 -0.0981 -0.0202 -0.0367 176 THR A O 1194 C CB . THR A 150 ? 0.4615 0.3407 0.5509 -0.0856 -0.0259 -0.0354 176 THR A CB 1195 O OG1 . THR A 150 ? 0.4415 0.3248 0.5237 -0.0787 -0.0323 -0.0371 176 THR A OG1 1196 C CG2 . THR A 150 ? 0.4769 0.3669 0.5842 -0.0926 -0.0282 -0.0395 176 THR A CG2 1197 N N . GLN A 151 ? 0.3329 0.1885 0.4077 -0.0917 -0.0106 -0.0263 177 GLN A N 1198 C CA . GLN A 151 ? 0.2909 0.1433 0.3683 -0.0977 -0.0051 -0.0228 177 GLN A CA 1199 C C . GLN A 151 ? 0.3720 0.2072 0.4351 -0.0974 -0.0042 -0.0205 177 GLN A C 1200 O O . GLN A 151 ? 0.3652 0.1956 0.4307 -0.1029 -0.0024 -0.0193 177 GLN A O 1201 C CB . GLN A 151 ? 0.3021 0.1605 0.3831 -0.0972 0.0020 -0.0168 177 GLN A CB 1202 C CG . GLN A 151 ? 0.2730 0.1490 0.3707 -0.0987 0.0021 -0.0190 177 GLN A CG 1203 C CD . GLN A 151 ? 0.2791 0.1635 0.3919 -0.1064 0.0014 -0.0227 177 GLN A CD 1204 O OE1 . GLN A 151 ? 0.3381 0.2160 0.4498 -0.1116 0.0047 -0.0208 177 GLN A OE1 1205 N NE2 . GLN A 151 ? 0.3512 0.2499 0.4784 -0.1068 -0.0036 -0.0279 177 GLN A NE2 1206 N N . LEU A 152 ? 0.3028 0.1289 0.3522 -0.0907 -0.0056 -0.0200 178 LEU A N 1207 C CA . LEU A 152 ? 0.3667 0.1776 0.4041 -0.0890 -0.0053 -0.0170 178 LEU A CA 1208 C C . LEU A 152 ? 0.3586 0.1613 0.3855 -0.0855 -0.0089 -0.0223 178 LEU A C 1209 O O . LEU A 152 ? 0.4140 0.2068 0.4341 -0.0830 -0.0102 -0.0207 178 LEU A O 1210 C CB . LEU A 152 ? 0.3142 0.1232 0.3465 -0.0829 -0.0021 -0.0099 178 LEU A CB 1211 C CG . LEU A 152 ? 0.3619 0.1800 0.4010 -0.0847 0.0041 -0.0051 178 LEU A CG 1212 C CD1 . LEU A 152 ? 0.2936 0.1110 0.3251 -0.0774 0.0068 -0.0002 178 LEU A CD1 1213 C CD2 . LEU A 152 ? 0.3499 0.1651 0.3937 -0.0912 0.0079 -0.0016 178 LEU A CD2 1214 N N . GLY A 153 ? 0.3649 0.1739 0.3939 -0.0843 -0.0110 -0.0287 179 GLY A N 1215 C CA . GLY A 153 ? 0.3159 0.1200 0.3391 -0.0801 -0.0123 -0.0346 179 GLY A CA 1216 C C . GLY A 153 ? 0.4454 0.2482 0.4635 -0.0708 -0.0091 -0.0321 179 GLY A C 1217 O O . GLY A 153 ? 0.4086 0.2143 0.4278 -0.0675 -0.0053 -0.0262 179 GLY A O 1218 N N . PRO A 154 ? 0.4484 0.2476 0.4616 -0.0663 -0.0120 -0.0365 180 PRO A N 1219 C CA . PRO A 154 ? 0.4299 0.2284 0.4366 -0.0580 -0.0114 -0.0348 180 PRO A CA 1220 C C . PRO A 154 ? 0.3848 0.1795 0.3937 -0.0540 -0.0074 -0.0296 180 PRO A C 1221 O O . PRO A 154 ? 0.3634 0.1595 0.3676 -0.0478 -0.0066 -0.0268 180 PRO A O 1222 C CB . PRO A 154 ? 0.5065 0.3002 0.5061 -0.0562 -0.0149 -0.0412 180 PRO A CB 1223 C CG . PRO A 154 ? 0.5164 0.3109 0.5189 -0.0629 -0.0193 -0.0463 180 PRO A CG 1224 C CD . PRO A 154 ? 0.3948 0.1904 0.4065 -0.0695 -0.0163 -0.0435 180 PRO A CD 1225 N N . ASP A 155 ? 0.3236 0.1145 0.3386 -0.0573 -0.0063 -0.0278 181 ASP A N 1226 C CA . ASP A 155 ? 0.3655 0.1515 0.3804 -0.0536 -0.0051 -0.0222 181 ASP A CA 1227 C C . ASP A 155 ? 0.3020 0.0921 0.3155 -0.0514 -0.0037 -0.0151 181 ASP A C 1228 O O . ASP A 155 ? 0.3211 0.1069 0.3314 -0.0475 -0.0024 -0.0109 181 ASP A O 1229 C CB . ASP A 155 ? 0.5376 0.3171 0.5581 -0.0583 -0.0056 -0.0208 181 ASP A CB 1230 C CG . ASP A 155 ? 0.6922 0.4650 0.7128 -0.0587 -0.0062 -0.0272 181 ASP A CG 1231 O OD1 . ASP A 155 ? 0.8245 0.5958 0.8387 -0.0542 -0.0063 -0.0315 181 ASP A OD1 1232 O OD2 . ASP A 155 ? 0.7841 0.5526 0.8107 -0.0636 -0.0071 -0.0279 181 ASP A OD2 1233 N N . TYR A 156 ? 0.2943 0.0921 0.3098 -0.0539 -0.0039 -0.0142 182 TYR A N 1234 C CA . TYR A 156 ? 0.3257 0.1269 0.3390 -0.0525 -0.0021 -0.0080 182 TYR A CA 1235 C C . TYR A 156 ? 0.2800 0.0823 0.2868 -0.0446 -0.0010 -0.0072 182 TYR A C 1236 O O . TYR A 156 ? 0.3289 0.1313 0.3324 -0.0419 0.0010 -0.0023 182 TYR A O 1237 C CB . TYR A 156 ? 0.3002 0.1095 0.3163 -0.0567 -0.0026 -0.0079 182 TYR A CB 1238 C CG . TYR A 156 ? 0.2731 0.0891 0.2877 -0.0528 -0.0033 -0.0111 182 TYR A CG 1239 C CD1 . TYR A 156 ? 0.2610 0.0807 0.2714 -0.0483 -0.0014 -0.0077 182 TYR A CD1 1240 C CD2 . TYR A 156 ? 0.2714 0.0885 0.2859 -0.0545 -0.0046 -0.0178 182 TYR A CD2 1241 C CE1 . TYR A 156 ? 0.2528 0.0774 0.2608 -0.0451 -0.0021 -0.0101 182 TYR A CE1 1242 C CE2 . TYR A 156 ? 0.2648 0.0856 0.2738 -0.0513 -0.0070 -0.0195 182 TYR A CE2 1243 C CZ . TYR A 156 ? 0.2853 0.1099 0.2921 -0.0466 -0.0052 -0.0156 182 TYR A CZ 1244 O OH . TYR A 156 ? 0.3084 0.1366 0.3108 -0.0432 -0.0078 -0.0169 182 TYR A OH 1245 N N . ILE A 157 ? 0.2776 0.0805 0.2816 -0.0412 -0.0022 -0.0122 183 ILE A N 1246 C CA . ILE A 157 ? 0.2704 0.0756 0.2688 -0.0342 -0.0015 -0.0118 183 ILE A CA 1247 C C . ILE A 157 ? 0.3083 0.1078 0.3050 -0.0302 -0.0007 -0.0096 183 ILE A C 1248 O O . ILE A 157 ? 0.2714 0.0725 0.2661 -0.0270 0.0005 -0.0054 183 ILE A O 1249 C CB . ILE A 157 ? 0.2686 0.0752 0.2630 -0.0321 -0.0030 -0.0175 183 ILE A CB 1250 C CG1 . ILE A 157 ? 0.3926 0.2044 0.3873 -0.0353 -0.0044 -0.0190 183 ILE A CG1 1251 C CG2 . ILE A 157 ? 0.3193 0.1278 0.3093 -0.0252 -0.0021 -0.0173 183 ILE A CG2 1252 C CD1 . ILE A 157 ? 0.3505 0.1615 0.3390 -0.0345 -0.0071 -0.0245 183 ILE A CD1 1253 N N . PRO A 158 ? 0.3252 0.1177 0.3226 -0.0305 -0.0014 -0.0125 184 PRO A N 1254 C CA . PRO A 158 ? 0.3809 0.1677 0.3773 -0.0266 -0.0007 -0.0101 184 PRO A CA 1255 C C . PRO A 158 ? 0.4064 0.1897 0.4032 -0.0288 0.0004 -0.0035 184 PRO A C 1256 O O . PRO A 158 ? 0.3445 0.1255 0.3386 -0.0246 0.0011 -0.0001 184 PRO A O 1257 C CB . PRO A 158 ? 0.3268 0.1060 0.3245 -0.0275 -0.0016 -0.0148 184 PRO A CB 1258 C CG . PRO A 158 ? 0.3176 0.0974 0.3182 -0.0337 -0.0027 -0.0181 184 PRO A CG 1259 C CD . PRO A 158 ? 0.3615 0.1504 0.3603 -0.0339 -0.0028 -0.0183 184 PRO A CD 1260 N N . ASN A 159 ? 0.2991 0.0818 0.2991 -0.0353 0.0007 -0.0019 185 ASN A N 1261 C CA . ASN A 159 ? 0.3054 0.0845 0.3045 -0.0380 0.0025 0.0045 185 ASN A CA 1262 C C . ASN A 159 ? 0.3552 0.1399 0.3498 -0.0351 0.0043 0.0087 185 ASN A C 1263 O O . ASN A 159 ? 0.3147 0.0951 0.3051 -0.0335 0.0059 0.0137 185 ASN A O 1264 C CB . ASN A 159 ? 0.3109 0.0896 0.3148 -0.0463 0.0027 0.0049 185 ASN A CB 1265 C CG . ASN A 159 ? 0.5227 0.2941 0.5314 -0.0497 0.0008 0.0014 185 ASN A CG 1266 O OD1 . ASN A 159 ? 0.4206 0.1852 0.4281 -0.0460 0.0003 0.0001 185 ASN A OD1 1267 N ND2 . ASN A 159 ? 0.4971 0.2699 0.5111 -0.0567 -0.0004 -0.0005 185 ASN A ND2 1268 N N . ALA A 160 ? 0.2852 0.0787 0.2802 -0.0343 0.0041 0.0065 186 ALA A N 1269 C CA . ALA A 160 ? 0.3239 0.1230 0.3151 -0.0313 0.0057 0.0096 186 ALA A CA 1270 C C . ALA A 160 ? 0.2760 0.0734 0.2631 -0.0240 0.0052 0.0103 186 ALA A C 1271 O O . ALA A 160 ? 0.2770 0.0737 0.2597 -0.0218 0.0066 0.0145 186 ALA A O 1272 C CB . ALA A 160 ? 0.2652 0.0732 0.2582 -0.0315 0.0053 0.0066 186 ALA A CB 1273 N N . TYR A 161 ? 0.2750 0.0716 0.2634 -0.0205 0.0033 0.0060 187 TYR A N 1274 C CA . TYR A 161 ? 0.2750 0.0702 0.2613 -0.0139 0.0027 0.0060 187 TYR A CA 1275 C C . TYR A 161 ? 0.3095 0.0951 0.2937 -0.0133 0.0029 0.0098 187 TYR A C 1276 O O . TYR A 161 ? 0.3011 0.0852 0.2820 -0.0089 0.0028 0.0125 187 TYR A O 1277 C CB . TYR A 161 ? 0.2716 0.0687 0.2601 -0.0108 0.0015 0.0000 187 TYR A CB 1278 C CG . TYR A 161 ? 0.2891 0.0954 0.2776 -0.0097 0.0016 -0.0024 187 TYR A CG 1279 C CD1 . TYR A 161 ? 0.2810 0.0927 0.2687 -0.0049 0.0019 -0.0020 187 TYR A CD1 1280 C CD2 . TYR A 161 ? 0.2813 0.0905 0.2707 -0.0137 0.0014 -0.0049 187 TYR A CD2 1281 C CE1 . TYR A 161 ? 0.2410 0.0606 0.2288 -0.0042 0.0022 -0.0039 187 TYR A CE1 1282 C CE2 . TYR A 161 ? 0.2465 0.0630 0.2352 -0.0127 0.0015 -0.0065 187 TYR A CE2 1283 C CZ . TYR A 161 ? 0.3007 0.1223 0.2887 -0.0080 0.0021 -0.0058 187 TYR A CZ 1284 O OH . TYR A 161 ? 0.2490 0.0773 0.2365 -0.0072 0.0025 -0.0072 187 TYR A OH 1285 N N . ALA A 162 ? 0.2983 0.0770 0.2845 -0.0179 0.0030 0.0101 188 ALA A N 1286 C CA . ALA A 162 ? 0.3523 0.1207 0.3361 -0.0181 0.0034 0.0146 188 ALA A CA 1287 C C . ALA A 162 ? 0.3537 0.1215 0.3315 -0.0188 0.0053 0.0211 188 ALA A C 1288 O O . ALA A 162 ? 0.3226 0.0849 0.2953 -0.0149 0.0052 0.0249 188 ALA A O 1289 C CB . ALA A 162 ? 0.3555 0.1171 0.3430 -0.0240 0.0035 0.0139 188 ALA A CB 1290 N N . VAL A 163 ? 0.3250 0.0984 0.3030 -0.0236 0.0072 0.0223 189 VAL A N 1291 C CA . VAL A 163 ? 0.3129 0.0860 0.2847 -0.0246 0.0100 0.0280 189 VAL A CA 1292 C C . VAL A 163 ? 0.3716 0.1483 0.3385 -0.0177 0.0091 0.0286 189 VAL A C 1293 O O . VAL A 163 ? 0.3205 0.0920 0.2801 -0.0152 0.0097 0.0332 189 VAL A O 1294 C CB . VAL A 163 ? 0.3361 0.1162 0.3105 -0.0309 0.0128 0.0282 189 VAL A CB 1295 C CG1 . VAL A 163 ? 0.3674 0.1480 0.3348 -0.0312 0.0165 0.0334 189 VAL A CG1 1296 C CG2 . VAL A 163 ? 0.3534 0.1298 0.3331 -0.0383 0.0136 0.0280 189 VAL A CG2 1297 N N . ALA A 164 ? 0.2927 0.0778 0.2633 -0.0147 0.0076 0.0238 190 ALA A N 1298 C CA . ALA A 164 ? 0.2858 0.0752 0.2535 -0.0084 0.0066 0.0234 190 ALA A CA 1299 C C . ALA A 164 ? 0.2943 0.0769 0.2593 -0.0026 0.0043 0.0244 190 ALA A C 1300 O O . ALA A 164 ? 0.3289 0.1098 0.2879 0.0014 0.0038 0.0273 190 ALA A O 1301 C CB . ALA A 164 ? 0.2711 0.0701 0.2442 -0.0066 0.0055 0.0178 190 ALA A CB 1302 N N . ARG A 165 ? 0.2987 0.0772 0.2680 -0.0020 0.0030 0.0217 191 ARG A N 1303 C CA . ARG A 165 ? 0.3081 0.0796 0.2760 0.0033 0.0011 0.0225 191 ARG A CA 1304 C C . ARG A 165 ? 0.3236 0.0852 0.2832 0.0031 0.0014 0.0294 191 ARG A C 1305 O O . ARG A 165 ? 0.3299 0.0878 0.2850 0.0087 -0.0006 0.0314 191 ARG A O 1306 C CB . ARG A 165 ? 0.3125 0.0799 0.2863 0.0030 0.0004 0.0186 191 ARG A CB 1307 C CG . ARG A 165 ? 0.3143 0.0892 0.2943 0.0057 -0.0002 0.0118 191 ARG A CG 1308 C CD . ARG A 165 ? 0.3558 0.1322 0.3368 0.0130 -0.0014 0.0103 191 ARG A CD 1309 N NE . ARG A 165 ? 0.3776 0.1596 0.3650 0.0149 -0.0011 0.0037 191 ARG A NE 1310 C CZ . ARG A 165 ? 0.4302 0.2214 0.4205 0.0180 -0.0008 0.0005 191 ARG A CZ 1311 N NH1 . ARG A 165 ? 0.3892 0.1851 0.3771 0.0200 -0.0013 0.0029 191 ARG A NH1 1312 N NH2 . ARG A 165 ? 0.4636 0.2586 0.4590 0.0191 0.0000 -0.0054 191 ARG A NH2 1313 N N . SER A 166 ? 0.3853 0.1427 0.3427 -0.0034 0.0038 0.0329 192 SER A N 1314 C CA . SER A 166 ? 0.3979 0.1447 0.3470 -0.0044 0.0048 0.0398 192 SER A CA 1315 C C . SER A 166 ? 0.4800 0.2277 0.4192 -0.0020 0.0055 0.0441 192 SER A C 1316 O O . SER A 166 ? 0.4184 0.1570 0.3484 -0.0008 0.0056 0.0499 192 SER A O 1317 C CB . SER A 166 ? 0.4124 0.1551 0.3630 -0.0127 0.0080 0.0421 192 SER A CB 1318 O OG . SER A 166 ? 0.4247 0.1746 0.3747 -0.0176 0.0112 0.0429 192 SER A OG 1319 N N . VAL A 167 ? 0.3530 0.1109 0.2933 -0.0010 0.0059 0.0414 193 VAL A N 1320 C CA . VAL A 167 ? 0.3363 0.0951 0.2674 0.0020 0.0061 0.0446 193 VAL A CA 1321 C C . VAL A 167 ? 0.4520 0.2076 0.3795 0.0105 0.0015 0.0444 193 VAL A C 1322 O O . VAL A 167 ? 0.4430 0.1951 0.3603 0.0139 0.0005 0.0481 193 VAL A O 1323 C CB . VAL A 167 ? 0.3714 0.1419 0.3058 0.0012 0.0077 0.0411 193 VAL A CB 1324 C CG1 . VAL A 167 ? 0.3840 0.1546 0.3084 0.0041 0.0083 0.0442 193 VAL A CG1 1325 C CG2 . VAL A 167 ? 0.3744 0.1487 0.3136 -0.0068 0.0117 0.0407 193 VAL A CG2 1326 N N . ASN A 168 ? 0.3745 0.1312 0.3102 0.0139 -0.0013 0.0400 194 ASN A N 1327 C CA . ASN A 168 ? 0.3410 0.0958 0.2759 0.0219 -0.0057 0.0390 194 ASN A CA 1328 C C . ASN A 168 ? 0.3958 0.1585 0.3290 0.0267 -0.0076 0.0370 194 ASN A C 1329 O O . ASN A 168 ? 0.4448 0.2033 0.3699 0.0318 -0.0107 0.0398 194 ASN A O 1330 C CB . ASN A 168 ? 0.4014 0.1433 0.3265 0.0241 -0.0074 0.0451 194 ASN A CB 1331 C CG . ASN A 168 ? 0.5635 0.2966 0.4912 0.0202 -0.0059 0.0468 194 ASN A CG 1332 O OD1 . ASN A 168 ? 0.6491 0.3838 0.5866 0.0204 -0.0063 0.0421 194 ASN A OD1 1333 N ND2 . ASN A 168 ? 0.5922 0.3158 0.5110 0.0164 -0.0039 0.0533 194 ASN A ND2 1334 N N . THR A 169 ? 0.3147 0.0883 0.2553 0.0253 -0.0061 0.0323 195 THR A N 1335 C CA . THR A 169 ? 0.3776 0.1593 0.3192 0.0299 -0.0080 0.0293 195 THR A CA 1336 C C . THR A 169 ? 0.3573 0.1442 0.3090 0.0349 -0.0103 0.0236 195 THR A C 1337 O O . THR A 169 ? 0.3556 0.1405 0.3131 0.0340 -0.0097 0.0217 195 THR A O 1338 C CB . THR A 169 ? 0.3434 0.1342 0.2880 0.0259 -0.0047 0.0272 195 THR A CB 1339 O OG1 . THR A 169 ? 0.3539 0.1515 0.3095 0.0236 -0.0034 0.0220 195 THR A OG1 1340 C CG2 . THR A 169 ? 0.3761 0.1624 0.3134 0.0196 -0.0009 0.0321 195 THR A CG2 1341 N N . PRO A 170 ? 0.3437 0.1376 0.2979 0.0400 -0.0127 0.0206 196 PRO A N 1342 C CA . PRO A 170 ? 0.3221 0.1219 0.2872 0.0438 -0.0135 0.0148 196 PRO A CA 1343 C C . PRO A 170 ? 0.3514 0.1622 0.3258 0.0408 -0.0100 0.0097 196 PRO A C 1344 O O . PRO A 170 ? 0.2876 0.1050 0.2706 0.0434 -0.0094 0.0046 196 PRO A O 1345 C CB . PRO A 170 ? 0.4063 0.2080 0.3698 0.0509 -0.0182 0.0141 196 PRO A CB 1346 C CG . PRO A 170 ? 0.4307 0.2330 0.3856 0.0500 -0.0186 0.0169 196 PRO A CG 1347 C CD . PRO A 170 ? 0.3748 0.1698 0.3216 0.0434 -0.0151 0.0221 196 PRO A CD 1348 N N . SER A 171 ? 0.2626 0.0747 0.2346 0.0351 -0.0073 0.0111 197 SER A N 1349 C CA . SER A 171 ? 0.2481 0.0694 0.2272 0.0319 -0.0044 0.0071 197 SER A CA 1350 C C . SER A 171 ? 0.3077 0.1296 0.2934 0.0295 -0.0027 0.0037 197 SER A C 1351 O O . SER A 171 ? 0.2540 0.0686 0.2374 0.0270 -0.0026 0.0056 197 SER A O 1352 C CB . SER A 171 ? 0.2450 0.0669 0.2191 0.0269 -0.0025 0.0099 197 SER A CB 1353 O OG . SER A 171 ? 0.2647 0.0868 0.2328 0.0294 -0.0035 0.0119 197 SER A OG 1354 N N . LYS A 172 ? 0.2353 0.0654 0.2287 0.0302 -0.0012 -0.0013 198 LYS A N 1355 C CA . LYS A 172 ? 0.2326 0.0637 0.2304 0.0273 0.0003 -0.0048 198 LYS A CA 1356 C C . LYS A 172 ? 0.2722 0.1030 0.2661 0.0215 0.0007 -0.0031 198 LYS A C 1357 O O . LYS A 172 ? 0.2776 0.1123 0.2692 0.0200 0.0011 -0.0015 198 LYS A O 1358 C CB . LYS A 172 ? 0.2230 0.0629 0.2282 0.0289 0.0018 -0.0102 198 LYS A CB 1359 C CG . LYS A 172 ? 0.3498 0.1919 0.3589 0.0343 0.0033 -0.0123 198 LYS A CG 1360 C CD . LYS A 172 ? 0.3792 0.2158 0.3895 0.0363 0.0044 -0.0141 198 LYS A CD 1361 C CE . LYS A 172 ? 0.3811 0.2182 0.3921 0.0423 0.0059 -0.0162 198 LYS A CE 1362 N NZ . LYS A 172 ? 0.5298 0.3592 0.5409 0.0450 0.0059 -0.0172 198 LYS A NZ 1363 N N . LEU A 173 ? 0.2350 0.0612 0.2285 0.0184 0.0009 -0.0038 199 LEU A N 1364 C CA . LEU A 173 ? 0.2887 0.1148 0.2793 0.0129 0.0015 -0.0027 199 LEU A CA 1365 C C . LEU A 173 ? 0.2306 0.0614 0.2234 0.0118 0.0019 -0.0073 199 LEU A C 1366 O O . LEU A 173 ? 0.2307 0.0597 0.2256 0.0130 0.0018 -0.0109 199 LEU A O 1367 C CB . LEU A 173 ? 0.2445 0.0618 0.2326 0.0095 0.0013 -0.0002 199 LEU A CB 1368 C CG . LEU A 173 ? 0.3291 0.1396 0.3129 0.0105 0.0009 0.0050 199 LEU A CG 1369 C CD1 . LEU A 173 ? 0.3094 0.1111 0.2912 0.0064 0.0010 0.0075 199 LEU A CD1 1370 C CD2 . LEU A 173 ? 0.2500 0.0636 0.2296 0.0101 0.0015 0.0085 199 LEU A CD2 1371 N N . TYR A 174 ? 0.2200 0.0562 0.2115 0.0097 0.0026 -0.0071 200 TYR A N 1372 C CA . TYR A 174 ? 0.2155 0.0554 0.2070 0.0089 0.0032 -0.0107 200 TYR A CA 1373 C C . TYR A 174 ? 0.2170 0.0553 0.2060 0.0039 0.0034 -0.0100 200 TYR A C 1374 O O . TYR A 174 ? 0.2180 0.0550 0.2063 0.0010 0.0035 -0.0066 200 TYR A O 1375 C CB . TYR A 174 ? 0.2062 0.0537 0.1987 0.0109 0.0040 -0.0113 200 TYR A CB 1376 C CG . TYR A 174 ? 0.2714 0.1221 0.2670 0.0154 0.0039 -0.0145 200 TYR A CG 1377 C CD1 . TYR A 174 ? 0.2058 0.0559 0.2050 0.0190 0.0026 -0.0141 200 TYR A CD1 1378 C CD2 . TYR A 174 ? 0.2999 0.1541 0.2949 0.0161 0.0054 -0.0177 200 TYR A CD2 1379 C CE1 . TYR A 174 ? 0.2041 0.0579 0.2068 0.0232 0.0021 -0.0175 200 TYR A CE1 1380 C CE2 . TYR A 174 ? 0.2110 0.0679 0.2082 0.0200 0.0056 -0.0208 200 TYR A CE2 1381 C CZ . TYR A 174 ? 0.2559 0.1124 0.2567 0.0237 0.0033 -0.0210 200 TYR A CZ 1382 O OH . TYR A 174 ? 0.2309 0.0900 0.2324 0.0277 0.0035 -0.0241 200 TYR A OH 1383 N N . ILE A 175 ? 0.2183 0.0561 0.2058 0.0029 0.0037 -0.0134 201 ILE A N 1384 C CA . ILE A 175 ? 0.2187 0.0561 0.2039 -0.0012 0.0036 -0.0136 201 ILE A CA 1385 C C . ILE A 175 ? 0.2126 0.0551 0.1961 0.0001 0.0048 -0.0151 201 ILE A C 1386 O O . ILE A 175 ? 0.2554 0.0992 0.2383 0.0032 0.0059 -0.0176 201 ILE A O 1387 C CB . ILE A 175 ? 0.2314 0.0623 0.2147 -0.0038 0.0027 -0.0164 201 ILE A CB 1388 C CG1 . ILE A 175 ? 0.2297 0.0599 0.2110 -0.0084 0.0018 -0.0169 201 ILE A CG1 1389 C CG2 . ILE A 175 ? 0.2709 0.1000 0.2520 -0.0009 0.0034 -0.0208 201 ILE A CG2 1390 C CD1 . ILE A 175 ? 0.2401 0.0634 0.2202 -0.0119 0.0003 -0.0196 201 ILE A CD1 1391 N N . ASN A 176 ? 0.2090 0.0540 0.1920 -0.0022 0.0048 -0.0136 202 ASN A N 1392 C CA . ASN A 176 ? 0.2033 0.0528 0.1851 -0.0008 0.0061 -0.0140 202 ASN A CA 1393 C C . ASN A 176 ? 0.3017 0.1482 0.2791 -0.0037 0.0051 -0.0151 202 ASN A C 1394 O O . ASN A 176 ? 0.2113 0.0550 0.1890 -0.0074 0.0031 -0.0146 202 ASN A O 1395 C CB . ASN A 176 ? 0.1950 0.0504 0.1806 0.0002 0.0067 -0.0109 202 ASN A CB 1396 C CG . ASN A 176 ? 0.3573 0.2178 0.3431 0.0025 0.0085 -0.0114 202 ASN A CG 1397 O OD1 . ASN A 176 ? 0.3232 0.1844 0.3082 0.0048 0.0098 -0.0135 202 ASN A OD1 1398 N ND2 . ASN A 176 ? 0.3249 0.1887 0.3125 0.0017 0.0087 -0.0095 202 ASN A ND2 1399 N N . ASP A 177 ? 0.2085 0.0547 0.1812 -0.0024 0.0063 -0.0167 203 ASP A N 1400 C CA . ASP A 177 ? 0.2200 0.0619 0.1863 -0.0047 0.0044 -0.0176 203 ASP A CA 1401 C C . ASP A 177 ? 0.2145 0.0566 0.1756 -0.0026 0.0064 -0.0178 203 ASP A C 1402 O O . ASP A 177 ? 0.2106 0.0560 0.1735 0.0002 0.0098 -0.0180 203 ASP A O 1403 C CB . ASP A 177 ? 0.2257 0.0602 0.1861 -0.0070 0.0021 -0.0209 203 ASP A CB 1404 C CG . ASP A 177 ? 0.3204 0.1513 0.2783 -0.0110 -0.0027 -0.0212 203 ASP A CG 1405 O OD1 . ASP A 177 ? 0.2532 0.0887 0.2116 -0.0109 -0.0043 -0.0195 203 ASP A OD1 1406 O OD2 . ASP A 177 ? 0.2918 0.1190 0.2499 -0.0141 -0.0053 -0.0232 203 ASP A OD2 1407 N N . TYR A 178 ? 0.2314 0.0690 0.1859 -0.0039 0.0039 -0.0176 204 TYR A N 1408 C CA . TYR A 178 ? 0.2609 0.0979 0.2088 -0.0021 0.0055 -0.0173 204 TYR A CA 1409 C C . TYR A 178 ? 0.2418 0.0722 0.1780 -0.0032 0.0029 -0.0198 204 TYR A C 1410 O O . TYR A 178 ? 0.2411 0.0695 0.1766 -0.0057 -0.0013 -0.0216 204 TYR A O 1411 C CB . TYR A 178 ? 0.2162 0.0604 0.1689 -0.0017 0.0037 -0.0138 204 TYR A CB 1412 C CG . TYR A 178 ? 0.2186 0.0655 0.1725 -0.0040 -0.0025 -0.0135 204 TYR A CG 1413 C CD1 . TYR A 178 ? 0.2537 0.1054 0.2169 -0.0063 -0.0046 -0.0130 204 TYR A CD1 1414 C CD2 . TYR A 178 ? 0.2839 0.1283 0.2294 -0.0040 -0.0064 -0.0138 204 TYR A CD2 1415 C CE1 . TYR A 178 ? 0.3174 0.1724 0.2836 -0.0088 -0.0101 -0.0133 204 TYR A CE1 1416 C CE2 . TYR A 178 ? 0.3358 0.1835 0.2837 -0.0060 -0.0129 -0.0141 204 TYR A CE2 1417 C CZ . TYR A 178 ? 0.3500 0.2036 0.3093 -0.0085 -0.0146 -0.0141 204 TYR A CZ 1418 O OH . TYR A 178 ? 0.2892 0.1471 0.2528 -0.0107 -0.0208 -0.0149 204 TYR A OH 1419 N N . ASN A 179 ? 0.2537 0.0807 0.1806 -0.0016 0.0053 -0.0199 205 ASN A N 1420 C CA . ASN A 179 ? 0.2869 0.1067 0.2000 -0.0022 0.0034 -0.0224 205 ASN A CA 1421 C C . ASN A 179 ? 0.2651 0.0782 0.1740 -0.0029 0.0050 -0.0271 205 ASN A C 1422 O O . ASN A 179 ? 0.2777 0.0848 0.1763 -0.0041 0.0022 -0.0302 205 ASN A O 1423 C CB . ASN A 179 ? 0.3215 0.1430 0.2325 -0.0039 -0.0045 -0.0217 205 ASN A CB 1424 C CG . ASN A 179 ? 0.3618 0.1863 0.2705 -0.0023 -0.0062 -0.0178 205 ASN A CG 1425 O OD1 . ASN A 179 ? 0.4180 0.2415 0.3242 -0.0004 -0.0011 -0.0157 205 ASN A OD1 1426 N ND2 . ASN A 179 ? 0.3126 0.1406 0.2229 -0.0032 -0.0135 -0.0170 205 ASN A ND2 1427 N N . THR A 180 ? 0.2604 0.0742 0.1774 -0.0020 0.0091 -0.0279 206 THR A N 1428 C CA . THR A 180 ? 0.2618 0.0746 0.1796 -0.0017 0.0109 -0.0316 206 THR A CA 1429 C C . THR A 180 ? 0.3333 0.1487 0.2524 0.0011 0.0176 -0.0326 206 THR A C 1430 O O . THR A 180 ? 0.2609 0.0774 0.1838 0.0022 0.0194 -0.0353 206 THR A O 1431 C CB . THR A 180 ? 0.2643 0.0830 0.1951 -0.0024 0.0088 -0.0308 206 THR A CB 1432 O OG1 . THR A 180 ? 0.2473 0.0746 0.1888 -0.0010 0.0103 -0.0270 206 THR A OG1 1433 C CG2 . THR A 180 ? 0.2565 0.0722 0.1868 -0.0059 0.0028 -0.0310 206 THR A CG2 1434 N N . GLU A 181 ? 0.2586 0.0748 0.1752 0.0022 0.0211 -0.0305 207 GLU A N 1435 C CA . GLU A 181 ? 0.2798 0.0999 0.2002 0.0043 0.0277 -0.0314 207 GLU A CA 1436 C C . GLU A 181 ? 0.3048 0.1167 0.2123 0.0045 0.0322 -0.0353 207 GLU A C 1437 O O . GLU A 181 ? 0.3431 0.1581 0.2553 0.0060 0.0368 -0.0379 207 GLU A O 1438 C CB . GLU A 181 ? 0.2487 0.0730 0.1726 0.0050 0.0305 -0.0277 207 GLU A CB 1439 C CG . GLU A 181 ? 0.2338 0.0670 0.1705 0.0051 0.0266 -0.0243 207 GLU A CG 1440 C CD . GLU A 181 ? 0.3858 0.2154 0.3179 0.0035 0.0217 -0.0216 207 GLU A CD 1441 O OE1 . GLU A 181 ? 0.3294 0.1499 0.2482 0.0025 0.0201 -0.0223 207 GLU A OE1 1442 O OE2 . GLU A 181 ? 0.3202 0.1564 0.2616 0.0034 0.0191 -0.0190 207 GLU A OE2 1443 N N . GLY A 182 ? 0.2988 0.1003 0.1900 0.0031 0.0306 -0.0361 208 GLY A N 1444 C CA . GLY A 182 ? 0.3021 0.0952 0.1788 0.0031 0.0344 -0.0402 208 GLY A CA 1445 C C . GLY A 182 ? 0.3822 0.1724 0.2565 0.0023 0.0302 -0.0445 208 GLY A C 1446 O O . GLY A 182 ? 0.3554 0.1503 0.2408 0.0017 0.0253 -0.0442 208 GLY A O 1447 N N . ILE A 183 ? 0.3636 0.1458 0.2232 0.0022 0.0327 -0.0486 209 ILE A N 1448 C CA . ILE A 183 ? 0.3346 0.1130 0.1903 0.0012 0.0285 -0.0532 209 ILE A CA 1449 C C . ILE A 183 ? 0.4651 0.2351 0.3057 -0.0009 0.0214 -0.0535 209 ILE A C 1450 O O . ILE A 183 ? 0.3710 0.1341 0.1941 -0.0009 0.0224 -0.0537 209 ILE A O 1451 C CB . ILE A 183 ? 0.3468 0.1224 0.1958 0.0024 0.0348 -0.0583 209 ILE A CB 1452 C CG1 . ILE A 183 ? 0.3767 0.1615 0.2429 0.0048 0.0403 -0.0587 209 ILE A CG1 1453 C CG2 . ILE A 183 ? 0.4332 0.2036 0.2760 0.0013 0.0301 -0.0635 209 ILE A CG2 1454 C CD1 . ILE A 183 ? 0.4679 0.2512 0.3295 0.0062 0.0476 -0.0634 209 ILE A CD1 1455 N N . ASN A 184 ? 0.3407 0.1128 0.1889 -0.0028 0.0138 -0.0530 210 ASN A N 1456 C CA . ASN A 184 ? 0.4296 0.1985 0.2687 -0.0049 0.0053 -0.0530 210 ASN A CA 1457 C C . ASN A 184 ? 0.3825 0.1516 0.2306 -0.0075 -0.0012 -0.0556 210 ASN A C 1458 O O . ASN A 184 ? 0.3373 0.1118 0.1994 -0.0072 0.0013 -0.0560 210 ASN A O 1459 C CB . ASN A 184 ? 0.3401 0.1161 0.1826 -0.0047 0.0027 -0.0463 210 ASN A CB 1460 C CG . ASN A 184 ? 0.3834 0.1680 0.2449 -0.0045 0.0036 -0.0423 210 ASN A CG 1461 O OD1 . ASN A 184 ? 0.3133 0.0999 0.1856 -0.0060 0.0007 -0.0433 210 ASN A OD1 1462 N ND2 . ASN A 184 ? 0.3117 0.1008 0.1768 -0.0028 0.0079 -0.0378 210 ASN A ND2 1463 N N . ASN A 185 ? 0.3602 0.1303 0.2055 -0.0099 -0.0097 -0.0557 211 ASN A N 1464 C CA . ASN A 185 ? 0.3492 0.1199 0.2041 -0.0131 -0.0158 -0.0580 211 ASN A CA 1465 C C . ASN A 185 ? 0.3313 0.1089 0.2051 -0.0138 -0.0143 -0.0540 211 ASN A C 1466 O O . ASN A 185 ? 0.3275 0.1078 0.2124 -0.0153 -0.0143 -0.0553 211 ASN A O 1467 C CB . ASN A 185 ? 0.3545 0.1282 0.2065 -0.0153 -0.0252 -0.0580 211 ASN A CB 1468 C CG . ASN A 185 ? 0.4919 0.2574 0.3283 -0.0163 -0.0297 -0.0645 211 ASN A CG 1469 O OD1 . ASN A 185 ? 0.4733 0.2308 0.2967 -0.0146 -0.0248 -0.0682 211 ASN A OD1 1470 N ND2 . ASN A 185 ? 0.6816 0.4497 0.5198 -0.0191 -0.0391 -0.0663 211 ASN A ND2 1471 N N . LYS A 186 ? 0.3188 0.1037 0.1987 -0.0124 -0.0126 -0.0483 212 LYS A N 1472 C CA . LYS A 186 ? 0.3032 0.0945 0.1991 -0.0129 -0.0115 -0.0444 212 LYS A CA 1473 C C . LYS A 186 ? 0.3718 0.1661 0.2759 -0.0106 -0.0047 -0.0442 212 LYS A C 1474 O O . LYS A 186 ? 0.2900 0.0878 0.2056 -0.0116 -0.0050 -0.0437 212 LYS A O 1475 C CB . LYS A 186 ? 0.2916 0.0920 0.1927 -0.0116 -0.0113 -0.0386 212 LYS A CB 1476 C CG . LYS A 186 ? 0.2780 0.0862 0.1947 -0.0133 -0.0129 -0.0351 212 LYS A CG 1477 C CD . LYS A 186 ? 0.2680 0.0849 0.1893 -0.0118 -0.0130 -0.0301 212 LYS A CD 1478 C CE . LYS A 186 ? 0.2552 0.0798 0.1912 -0.0133 -0.0134 -0.0269 212 LYS A CE 1479 N NZ . LYS A 186 ? 0.2459 0.0786 0.1865 -0.0114 -0.0131 -0.0227 212 LYS A NZ 1480 N N . SER A 187 ? 0.2972 0.0910 0.1962 -0.0073 0.0012 -0.0446 213 SER A N 1481 C CA . SER A 187 ? 0.2907 0.0889 0.1989 -0.0047 0.0064 -0.0450 213 SER A CA 1482 C C . SER A 187 ? 0.2993 0.0937 0.2078 -0.0052 0.0056 -0.0497 213 SER A C 1483 O O . SER A 187 ? 0.2950 0.0927 0.2143 -0.0039 0.0068 -0.0495 213 SER A O 1484 C CB . SER A 187 ? 0.2909 0.0899 0.1947 -0.0017 0.0128 -0.0450 213 SER A CB 1485 O OG . SER A 187 ? 0.3374 0.1282 0.2255 -0.0017 0.0143 -0.0490 213 SER A OG 1486 N N . ASP A 188 ? 0.3142 0.1011 0.2104 -0.0068 0.0032 -0.0542 214 ASP A N 1487 C CA . ASP A 188 ? 0.3231 0.1062 0.2201 -0.0077 0.0019 -0.0591 214 ASP A CA 1488 C C . ASP A 188 ? 0.3690 0.1543 0.2785 -0.0103 -0.0020 -0.0575 214 ASP A C 1489 O O . ASP A 188 ? 0.3161 0.1017 0.2342 -0.0095 -0.0009 -0.0586 214 ASP A O 1490 C CB . ASP A 188 ? 0.3406 0.1158 0.2220 -0.0095 -0.0013 -0.0642 214 ASP A CB 1491 C CG . ASP A 188 ? 0.4720 0.2432 0.3392 -0.0069 0.0036 -0.0666 214 ASP A CG 1492 O OD1 . ASP A 188 ? 0.3841 0.1588 0.2550 -0.0039 0.0102 -0.0651 214 ASP A OD1 1493 O OD2 . ASP A 188 ? 0.5530 0.3177 0.4049 -0.0081 0.0008 -0.0701 214 ASP A OD2 1494 N N . ALA A 189 ? 0.3643 0.1507 0.2746 -0.0136 -0.0067 -0.0551 215 ALA A N 1495 C CA . ALA A 189 ? 0.3331 0.1216 0.2549 -0.0169 -0.0098 -0.0535 215 ALA A CA 1496 C C . ALA A 189 ? 0.3671 0.1613 0.3014 -0.0149 -0.0061 -0.0487 215 ALA A C 1497 O O . ALA A 189 ? 0.2968 0.0903 0.2393 -0.0157 -0.0060 -0.0487 215 ALA A O 1498 C CB . ALA A 189 ? 0.3088 0.0987 0.2301 -0.0206 -0.0152 -0.0519 215 ALA A CB 1499 N N . LEU A 190 ? 0.2865 0.0861 0.2219 -0.0123 -0.0035 -0.0449 216 LEU A N 1500 C CA . LEU A 190 ? 0.2748 0.0803 0.2206 -0.0099 -0.0007 -0.0407 216 LEU A CA 1501 C C . LEU A 190 ? 0.2775 0.0815 0.2266 -0.0067 0.0017 -0.0430 216 LEU A C 1502 O O . LEU A 190 ? 0.2744 0.0792 0.2319 -0.0062 0.0016 -0.0411 216 LEU A O 1503 C CB . LEU A 190 ? 0.2649 0.0763 0.2106 -0.0073 0.0018 -0.0374 216 LEU A CB 1504 C CG . LEU A 190 ? 0.2671 0.0851 0.2229 -0.0046 0.0039 -0.0336 216 LEU A CG 1505 C CD1 . LEU A 190 ? 0.2491 0.0687 0.2123 -0.0072 0.0017 -0.0301 216 LEU A CD1 1506 C CD2 . LEU A 190 ? 0.2446 0.0685 0.2003 -0.0022 0.0064 -0.0313 216 LEU A CD2 1507 N N . LEU A 191 ? 0.2845 0.0857 0.2264 -0.0045 0.0039 -0.0472 217 LEU A N 1508 C CA . LEU A 191 ? 0.2879 0.0878 0.2333 -0.0011 0.0061 -0.0501 217 LEU A CA 1509 C C . LEU A 191 ? 0.2990 0.0935 0.2483 -0.0028 0.0037 -0.0524 217 LEU A C 1510 O O . LEU A 191 ? 0.2946 0.0890 0.2518 -0.0005 0.0040 -0.0520 217 LEU A O 1511 C CB . LEU A 191 ? 0.3085 0.1059 0.2445 0.0008 0.0094 -0.0547 217 LEU A CB 1512 C CG . LEU A 191 ? 0.3549 0.1508 0.2940 0.0044 0.0118 -0.0590 217 LEU A CG 1513 C CD1 . LEU A 191 ? 0.3305 0.1325 0.2808 0.0080 0.0127 -0.0560 217 LEU A CD1 1514 C CD2 . LEU A 191 ? 0.3414 0.1350 0.2700 0.0058 0.0160 -0.0634 217 LEU A CD2 1515 N N . ALA A 192 ? 0.3272 0.1166 0.2711 -0.0068 0.0010 -0.0550 218 ALA A N 1516 C CA . ALA A 192 ? 0.3986 0.1824 0.3464 -0.0088 -0.0010 -0.0576 218 ALA A CA 1517 C C . ALA A 192 ? 0.3063 0.0918 0.2647 -0.0101 -0.0019 -0.0525 218 ALA A C 1518 O O . ALA A 192 ? 0.3421 0.1243 0.3067 -0.0091 -0.0016 -0.0527 218 ALA A O 1519 C CB . ALA A 192 ? 0.3239 0.1028 0.2645 -0.0132 -0.0044 -0.0616 218 ALA A CB 1520 N N . VAL A 193 ? 0.2975 0.0877 0.2574 -0.0122 -0.0027 -0.0477 219 VAL A N 1521 C CA . VAL A 193 ? 0.3827 0.1743 0.3512 -0.0137 -0.0030 -0.0426 219 VAL A CA 1522 C C . VAL A 193 ? 0.3705 0.1650 0.3441 -0.0088 -0.0009 -0.0394 219 VAL A C 1523 O O . VAL A 193 ? 0.2932 0.0847 0.2723 -0.0085 -0.0010 -0.0374 219 VAL A O 1524 C CB . VAL A 193 ? 0.3050 0.1014 0.2740 -0.0170 -0.0041 -0.0388 219 VAL A CB 1525 C CG1 . VAL A 193 ? 0.3582 0.1566 0.3350 -0.0179 -0.0035 -0.0331 219 VAL A CG1 1526 C CG2 . VAL A 193 ? 0.3141 0.1073 0.2802 -0.0224 -0.0073 -0.0422 219 VAL A CG2 1527 N N . VAL A 194 ? 0.2921 0.0921 0.2637 -0.0052 0.0007 -0.0391 220 VAL A N 1528 C CA . VAL A 194 ? 0.2763 0.0795 0.2530 -0.0005 0.0020 -0.0373 220 VAL A CA 1529 C C . VAL A 194 ? 0.3029 0.1007 0.2824 0.0024 0.0021 -0.0409 220 VAL A C 1530 O O . VAL A 194 ? 0.2966 0.0936 0.2820 0.0048 0.0019 -0.0386 220 VAL A O 1531 C CB . VAL A 194 ? 0.2654 0.0751 0.2396 0.0025 0.0039 -0.0375 220 VAL A CB 1532 C CG1 . VAL A 194 ? 0.2616 0.0741 0.2411 0.0076 0.0048 -0.0377 220 VAL A CG1 1533 C CG2 . VAL A 194 ? 0.2553 0.0706 0.2292 0.0005 0.0037 -0.0330 220 VAL A CG2 1534 N N . GLN A 195 ? 0.2904 0.0839 0.2654 0.0022 0.0025 -0.0465 221 GLN A N 1535 C CA . GLN A 195 ? 0.2992 0.0877 0.2774 0.0051 0.0027 -0.0506 221 GLN A CA 1536 C C . GLN A 195 ? 0.3331 0.1152 0.3166 0.0031 0.0012 -0.0486 221 GLN A C 1537 O O . GLN A 195 ? 0.3214 0.1008 0.3108 0.0061 0.0014 -0.0481 221 GLN A O 1538 C CB . GLN A 195 ? 0.3631 0.1476 0.3343 0.0048 0.0034 -0.0574 221 GLN A CB 1539 C CG . GLN A 195 ? 0.4336 0.2222 0.4005 0.0086 0.0062 -0.0603 221 GLN A CG 1540 C CD . GLN A 195 ? 0.5601 0.3446 0.5172 0.0077 0.0076 -0.0665 221 GLN A CD 1541 O OE1 . GLN A 195 ? 0.5499 0.3297 0.5018 0.0037 0.0058 -0.0682 221 GLN A OE1 1542 N NE2 . GLN A 195 ? 0.5453 0.3314 0.4993 0.0114 0.0109 -0.0701 221 GLN A NE2 1543 N N . SER A 196 ? 0.3079 0.0875 0.2894 -0.0022 0.0000 -0.0473 222 SER A N 1544 C CA . SER A 196 ? 0.3488 0.1222 0.3348 -0.0050 -0.0009 -0.0450 222 SER A CA 1545 C C . SER A 196 ? 0.3084 0.0837 0.2989 -0.0037 -0.0006 -0.0381 222 SER A C 1546 O O . SER A 196 ? 0.3147 0.0845 0.3091 -0.0021 -0.0003 -0.0364 222 SER A O 1547 C CB . SER A 196 ? 0.3533 0.1248 0.3370 -0.0113 -0.0024 -0.0455 222 SER A CB 1548 O OG . SER A 196 ? 0.5138 0.2799 0.5024 -0.0145 -0.0028 -0.0424 222 SER A OG 1549 N N . MET A 197 ? 0.3073 0.0898 0.2965 -0.0042 -0.0005 -0.0341 223 MET A N 1550 C CA . MET A 197 ? 0.3252 0.1094 0.3171 -0.0033 -0.0003 -0.0277 223 MET A CA 1551 C C . MET A 197 ? 0.3386 0.1233 0.3335 0.0027 0.0004 -0.0275 223 MET A C 1552 O O . MET A 197 ? 0.3073 0.0883 0.3043 0.0041 0.0004 -0.0234 223 MET A O 1553 C CB . MET A 197 ? 0.2813 0.0734 0.2714 -0.0048 -0.0002 -0.0243 223 MET A CB 1554 C CG . MET A 197 ? 0.3095 0.1005 0.2991 -0.0111 -0.0009 -0.0229 223 MET A CG 1555 S SD . MET A 197 ? 0.4138 0.2125 0.4031 -0.0129 -0.0005 -0.0176 223 MET A SD 1556 C CE . MET A 197 ? 0.3139 0.1207 0.3003 -0.0088 0.0001 -0.0200 223 MET A CE 1557 N N . LYS A 198 ? 0.3204 0.0828 0.3172 0.0104 0.0010 -0.0225 224 LYS A N 1558 C CA . LYS A 198 ? 0.3232 0.0842 0.3178 0.0196 0.0008 -0.0182 224 LYS A CA 1559 C C . LYS A 198 ? 0.3455 0.0902 0.3460 0.0228 0.0015 -0.0180 224 LYS A C 1560 O O . LYS A 198 ? 0.3578 0.0933 0.3559 0.0272 -0.0002 -0.0095 224 LYS A O 1561 C CB . LYS A 198 ? 0.3089 0.0839 0.3043 0.0268 0.0020 -0.0247 224 LYS A CB 1562 C CG . LYS A 198 ? 0.3378 0.1116 0.3374 0.0370 0.0019 -0.0216 224 LYS A CG 1563 C CD . LYS A 198 ? 0.3820 0.1552 0.3762 0.0383 -0.0029 -0.0105 224 LYS A CD 1564 C CE . LYS A 198 ? 0.4632 0.2318 0.4634 0.0485 -0.0056 -0.0068 224 LYS A CE 1565 N NZ . LYS A 198 ? 0.5581 0.3283 0.5528 0.0510 -0.0139 0.0024 224 LYS A NZ 1566 N N . ALA A 199 ? 0.3543 0.0948 0.3585 0.0205 0.0037 -0.0272 225 ALA A N 1567 C CA . ALA A 199 ? 0.3793 0.1021 0.3858 0.0227 0.0057 -0.0279 225 ALA A CA 1568 C C . ALA A 199 ? 0.4357 0.1456 0.4451 0.0172 0.0038 -0.0166 225 ALA A C 1569 O O . ALA A 199 ? 0.4380 0.1337 0.4471 0.0221 0.0036 -0.0103 225 ALA A O 1570 C CB . ALA A 199 ? 0.3920 0.1078 0.3953 0.0190 0.0087 -0.0397 225 ALA A CB 1571 N N . HIS A 200 ? 0.3862 0.1003 0.3974 0.0076 0.0014 -0.0133 226 HIS A N 1572 C CA . HIS A 200 ? 0.4045 0.1037 0.4147 0.0011 -0.0008 -0.0020 226 HIS A CA 1573 C C . HIS A 200 ? 0.4061 0.1020 0.4007 0.0033 0.0003 0.0111 226 HIS A C 1574 O O . HIS A 200 ? 0.4226 0.1073 0.4081 -0.0029 0.0026 0.0216 226 HIS A O 1575 C CB . HIS A 200 ? 0.4070 0.1052 0.4173 -0.0110 -0.0046 -0.0033 226 HIS A CB 1576 C CG . HIS A 200 ? 0.5462 0.2367 0.5550 -0.0141 -0.0137 -0.0145 226 HIS A CG 1577 N ND1 . HIS A 200 ? 0.5680 0.2492 0.5535 -0.0244 -0.0097 -0.0198 226 HIS A ND1 1578 C CD2 . HIS A 200 ? 0.5723 0.2436 0.5662 -0.0120 0.0180 -0.0219 226 HIS A CD2 1579 C CE1 . HIS A 200 ? 0.6120 0.2784 0.5897 -0.0270 -0.0025 -0.0301 226 HIS A CE1 1580 N NE2 . HIS A 200 ? 0.6498 0.3042 0.6222 -0.0191 0.0047 -0.0309 226 HIS A NE2 1581 N N . ASN A 201 ? 0.3924 0.0991 0.3801 0.0120 -0.0007 0.0104 227 ASN A N 1582 C CA . ASN A 201 ? 0.3978 0.1022 0.3675 0.0154 -0.0024 0.0213 227 ASN A CA 1583 C C . ASN A 201 ? 0.5010 0.2097 0.4565 0.0077 0.0020 0.0261 227 ASN A C 1584 O O . ASN A 201 ? 0.4525 0.1518 0.3884 0.0078 0.0028 0.0363 227 ASN A O 1585 C CB . ASN A 201 ? 0.6528 0.3357 0.6158 0.0181 -0.0044 0.0318 227 ASN A CB 1586 C CG . ASN A 201 ? 0.6205 0.2983 0.5621 0.0237 -0.0094 0.0419 227 ASN A CG 1587 O OD1 . ASN A 201 ? 0.7339 0.4248 0.6724 0.0292 -0.0141 0.0393 227 ASN A OD1 1588 N ND2 . ASN A 201 ? 0.4824 0.1402 0.4082 0.0221 -0.0092 0.0534 227 ASN A ND2 1589 N N . LEU A 202 ? 0.3732 0.0949 0.3368 0.0017 0.0052 0.0186 228 LEU A N 1590 C CA . LEU A 202 ? 0.4270 0.1529 0.3810 -0.0058 0.0123 0.0224 228 LEU A CA 1591 C C . LEU A 202 ? 0.4061 0.1477 0.3522 -0.0025 0.0122 0.0197 228 LEU A C 1592 O O . LEU A 202 ? 0.3815 0.1229 0.3133 -0.0053 0.0181 0.0250 228 LEU A O 1593 C CB . LEU A 202 ? 0.3667 0.0957 0.3362 -0.0157 0.0160 0.0171 228 LEU A CB 1594 C CG . LEU A 202 ? 0.4334 0.1451 0.4102 -0.0219 0.0165 0.0208 228 LEU A CG 1595 C CD1 . LEU A 202 ? 0.4044 0.1202 0.3966 -0.0324 0.0180 0.0146 228 LEU A CD1 1596 C CD2 . LEU A 202 ? 0.4181 0.1143 0.3789 -0.0241 0.0241 0.0349 228 LEU A CD2 1597 N N . VAL A 203 ? 0.3423 0.0965 0.2972 0.0037 0.0067 0.0116 229 VAL A N 1598 C CA . VAL A 203 ? 0.3097 0.0783 0.2597 0.0063 0.0062 0.0092 229 VAL A CA 1599 C C . VAL A 203 ? 0.3543 0.1275 0.3058 0.0161 -0.0011 0.0083 229 VAL A C 1600 O O . VAL A 203 ? 0.3496 0.1206 0.3118 0.0212 -0.0038 0.0053 229 VAL A O 1601 C CB . VAL A 203 ? 0.2900 0.0730 0.2513 0.0024 0.0086 -0.0001 229 VAL A CB 1602 C CG1 . VAL A 203 ? 0.3774 0.1652 0.3505 0.0071 0.0045 -0.0094 229 VAL A CG1 1603 C CG2 . VAL A 203 ? 0.2973 0.0927 0.2525 0.0027 0.0104 -0.0005 229 VAL A CG2 1604 N N . ASP A 204 ? 0.2982 0.0773 0.2407 0.0187 -0.0039 0.0106 230 ASP A N 1605 C CA . ASP A 204 ? 0.2946 0.0792 0.2425 0.0273 -0.0118 0.0104 230 ASP A CA 1606 C C . ASP A 204 ? 0.3983 0.2008 0.3565 0.0292 -0.0111 0.0039 230 ASP A C 1607 O O . ASP A 204 ? 0.2653 0.0758 0.2374 0.0359 -0.0140 0.0011 230 ASP A O 1608 C CB . ASP A 204 ? 0.3108 0.0861 0.2409 0.0296 -0.0193 0.0183 230 ASP A CB 1609 C CG . ASP A 204 ? 0.4407 0.1960 0.3564 0.0288 -0.0200 0.0261 230 ASP A CG 1610 O OD1 . ASP A 204 ? 0.3756 0.1253 0.3019 0.0322 -0.0217 0.0265 230 ASP A OD1 1611 O OD2 . ASP A 204 ? 0.3557 0.0995 0.2482 0.0250 -0.0176 0.0318 230 ASP A OD2 1612 N N . GLY A 205 ? 0.2746 0.0830 0.2267 0.0235 -0.0064 0.0022 231 GLY A N 1613 C CA . GLY A 205 ? 0.2421 0.0651 0.2002 0.0250 -0.0061 -0.0021 231 GLY A CA 1614 C C . GLY A 205 ? 0.2350 0.0653 0.1936 0.0195 0.0009 -0.0071 231 GLY A C 1615 O O . GLY A 205 ? 0.2357 0.0607 0.1902 0.0133 0.0051 -0.0065 231 GLY A O 1616 N N . VAL A 206 ? 0.2170 0.0591 0.1824 0.0220 0.0021 -0.0118 232 VAL A N 1617 C CA . VAL A 206 ? 0.2068 0.0579 0.1719 0.0176 0.0065 -0.0159 232 VAL A CA 1618 C C . VAL A 206 ? 0.1940 0.0579 0.1602 0.0177 0.0062 -0.0142 232 VAL A C 1619 O O . VAL A 206 ? 0.1897 0.0605 0.1628 0.0222 0.0044 -0.0137 232 VAL A O 1620 C CB . VAL A 206 ? 0.2066 0.0609 0.1757 0.0200 0.0083 -0.0232 232 VAL A CB 1621 C CG1 . VAL A 206 ? 0.2260 0.0905 0.1937 0.0164 0.0096 -0.0265 232 VAL A CG1 1622 C CG2 . VAL A 206 ? 0.2198 0.0632 0.1899 0.0187 0.0073 -0.0260 232 VAL A CG2 1623 N N . GLY A 207 ? 0.1899 0.0569 0.1522 0.0128 0.0086 -0.0133 233 GLY A N 1624 C CA . GLY A 207 ? 0.1797 0.0568 0.1428 0.0127 0.0086 -0.0125 233 GLY A CA 1625 C C . GLY A 207 ? 0.2991 0.1875 0.2675 0.0121 0.0106 -0.0161 233 GLY A C 1626 O O . GLY A 207 ? 0.2133 0.1021 0.1830 0.0091 0.0117 -0.0189 233 GLY A O 1627 N N . PHE A 208 ? 0.1632 0.0597 0.1351 0.0149 0.0104 -0.0156 234 PHE A N 1628 C CA . PHE A 208 ? 0.1587 0.0629 0.1310 0.0151 0.0119 -0.0172 234 PHE A CA 1629 C C . PHE A 208 ? 0.1523 0.0613 0.1263 0.0138 0.0116 -0.0146 234 PHE A C 1630 O O . PHE A 208 ? 0.1946 0.1049 0.1719 0.0147 0.0109 -0.0121 234 PHE A O 1631 C CB . PHE A 208 ? 0.1940 0.1009 0.1669 0.0196 0.0148 -0.0177 234 PHE A CB 1632 C CG . PHE A 208 ? 0.1932 0.0934 0.1633 0.0224 0.0160 -0.0216 234 PHE A CG 1633 C CD1 . PHE A 208 ? 0.1902 0.0856 0.1510 0.0223 0.0152 -0.0268 234 PHE A CD1 1634 C CD2 . PHE A 208 ? 0.2425 0.1400 0.2199 0.0255 0.0166 -0.0207 234 PHE A CD2 1635 C CE1 . PHE A 208 ? 0.2716 0.1580 0.2282 0.0251 0.0161 -0.0317 234 PHE A CE1 1636 C CE2 . PHE A 208 ? 0.3164 0.2062 0.2921 0.0291 0.0183 -0.0248 234 PHE A CE2 1637 C CZ . PHE A 208 ? 0.1943 0.0777 0.1584 0.0287 0.0187 -0.0307 234 PHE A CZ 1638 N N . GLN A 209 ? 0.1507 0.0622 0.1252 0.0116 0.0116 -0.0157 235 GLN A N 1639 C CA . GLN A 209 ? 0.1745 0.0885 0.1510 0.0111 0.0121 -0.0139 235 GLN A CA 1640 C C . GLN A 209 ? 0.1442 0.0621 0.1224 0.0132 0.0116 -0.0116 235 GLN A C 1641 O O . GLN A 209 ? 0.1815 0.0980 0.1615 0.0130 0.0110 -0.0099 235 GLN A O 1642 C CB . GLN A 209 ? 0.1464 0.0639 0.1285 0.0094 0.0129 -0.0157 235 GLN A CB 1643 C CG . GLN A 209 ? 0.1511 0.0642 0.1347 0.0061 0.0169 -0.0165 235 GLN A CG 1644 C CD . GLN A 209 ? 0.1600 0.0795 0.1567 0.0043 0.0192 -0.0182 235 GLN A CD 1645 O OE1 . GLN A 209 ? 0.1972 0.1229 0.2003 0.0066 0.0176 -0.0183 235 GLN A OE1 1646 N NE2 . GLN A 209 ? 0.1551 0.0729 0.1587 0.0004 0.0233 -0.0189 235 GLN A NE2 1647 N N . CYS A 210 ? 0.1519 0.0723 0.1277 0.0152 0.0116 -0.0114 236 CYS A N 1648 C CA . CYS A 210 ? 0.1646 0.0864 0.1400 0.0170 0.0135 -0.0075 236 CYS A CA 1649 C C . CYS A 210 ? 0.1976 0.1200 0.1765 0.0167 0.0119 -0.0053 236 CYS A C 1650 O O . CYS A 210 ? 0.1610 0.0824 0.1447 0.0162 0.0131 -0.0022 236 CYS A O 1651 C CB . CYS A 210 ? 0.1470 0.0695 0.1294 0.0171 0.0165 -0.0052 236 CYS A CB 1652 S SG . CYS A 210 ? 0.1972 0.1191 0.1792 0.0196 0.0200 -0.0073 236 CYS A SG 1653 N N . HIS A 211 ? 0.1519 0.0756 0.1314 0.0171 0.0088 -0.0072 237 HIS A N 1654 C CA . HIS A 211 ? 0.1894 0.1131 0.1726 0.0187 0.0069 -0.0051 237 HIS A CA 1655 C C . HIS A 211 ? 0.2473 0.1687 0.2216 0.0218 0.0048 -0.0010 237 HIS A C 1656 O O . HIS A 211 ? 0.2320 0.1536 0.2017 0.0238 -0.0009 -0.0025 237 HIS A O 1657 C CB . HIS A 211 ? 0.1467 0.0744 0.1389 0.0187 0.0049 -0.0087 237 HIS A CB 1658 C CG . HIS A 211 ? 0.1431 0.0695 0.1389 0.0164 0.0097 -0.0114 237 HIS A CG 1659 N ND1 . HIS A 211 ? 0.1468 0.0679 0.1416 0.0166 0.0122 -0.0112 237 HIS A ND1 1660 C CD2 . HIS A 211 ? 0.1426 0.0692 0.1397 0.0138 0.0127 -0.0141 237 HIS A CD2 1661 C CE1 . HIS A 211 ? 0.1671 0.0844 0.1587 0.0150 0.0165 -0.0139 237 HIS A CE1 1662 N NE2 . HIS A 211 ? 0.1759 0.0966 0.1693 0.0131 0.0177 -0.0149 237 HIS A NE2 1663 N N . PHE A 212 ? 0.1831 0.1006 0.1543 0.0220 0.0090 0.0042 238 PHE A N 1664 C CA . PHE A 212 ? 0.1797 0.0915 0.1367 0.0249 0.0104 0.0095 238 PHE A CA 1665 C C . PHE A 212 ? 0.1973 0.1033 0.1537 0.0270 0.0081 0.0155 238 PHE A C 1666 O O . PHE A 212 ? 0.1826 0.0891 0.1521 0.0257 0.0076 0.0157 238 PHE A O 1667 C CB . PHE A 212 ? 0.1830 0.0938 0.1384 0.0238 0.0201 0.0127 238 PHE A CB 1668 C CG . PHE A 212 ? 0.1903 0.1041 0.1438 0.0237 0.0225 0.0075 238 PHE A CG 1669 C CD1 . PHE A 212 ? 0.2204 0.1321 0.1616 0.0257 0.0175 0.0024 238 PHE A CD1 1670 C CD2 . PHE A 212 ? 0.1785 0.0964 0.1445 0.0219 0.0282 0.0075 238 PHE A CD2 1671 C CE1 . PHE A 212 ? 0.2723 0.1843 0.2117 0.0258 0.0196 -0.0026 238 PHE A CE1 1672 C CE2 . PHE A 212 ? 0.2432 0.1626 0.2086 0.0229 0.0300 0.0030 238 PHE A CE2 1673 C CZ . PHE A 212 ? 0.2063 0.1218 0.1573 0.0248 0.0263 -0.0021 238 PHE A CZ 1674 N N . PHE A 213 ? 0.2139 0.1120 0.1524 0.0307 0.0064 0.0204 239 PHE A N 1675 C CA . PHE A 213 ? 0.2226 0.1115 0.1568 0.0332 0.0052 0.0284 239 PHE A CA 1676 C C . PHE A 213 ? 0.2610 0.1416 0.1842 0.0322 0.0172 0.0367 239 PHE A C 1677 O O . PHE A 213 ? 0.2781 0.1561 0.1850 0.0332 0.0233 0.0368 239 PHE A O 1678 C CB . PHE A 213 ? 0.2402 0.1231 0.1602 0.0390 -0.0067 0.0294 239 PHE A CB 1679 C CG . PHE A 213 ? 0.2541 0.1273 0.1735 0.0425 -0.0109 0.0373 239 PHE A CG 1680 C CD1 . PHE A 213 ? 0.3467 0.2044 0.2448 0.0445 -0.0058 0.0480 239 PHE A CD1 1681 C CD2 . PHE A 213 ? 0.3189 0.1971 0.2592 0.0443 -0.0184 0.0346 239 PHE A CD2 1682 C CE1 . PHE A 213 ? 0.4438 0.2898 0.3408 0.0479 -0.0099 0.0564 239 PHE A CE1 1683 C CE2 . PHE A 213 ? 0.3204 0.1883 0.2618 0.0485 -0.0226 0.0417 239 PHE A CE2 1684 C CZ . PHE A 213 ? 0.3622 0.2133 0.2815 0.0502 -0.0193 0.0529 239 PHE A CZ 1685 N N . VAL A 214 ? 0.2818 0.1576 0.2153 0.0300 0.0217 0.0434 240 VAL A N 1686 C CA . VAL A 214 ? 0.2789 0.1487 0.2105 0.0274 0.0354 0.0519 240 VAL A CA 1687 C C . VAL A 214 ? 0.3469 0.2039 0.2464 0.0319 0.0419 0.0590 240 VAL A C 1688 O O . VAL A 214 ? 0.3037 0.1495 0.1808 0.0372 0.0333 0.0621 240 VAL A O 1689 C CB . VAL A 214 ? 0.3339 0.1965 0.2803 0.0244 0.0372 0.0590 240 VAL A CB 1690 C CG1 . VAL A 214 ? 0.3549 0.2044 0.2865 0.0298 0.0288 0.0646 240 VAL A CG1 1691 C CG2 . VAL A 214 ? 0.2940 0.1522 0.2454 0.0201 0.0528 0.0681 240 VAL A CG2 1692 N N . GLY A 215 ? 0.3154 0.1734 0.2121 0.0303 0.0567 0.0611 241 GLY A N 1693 C CA . GLY A 215 ? 0.4019 0.2456 0.2645 0.0349 0.0667 0.0672 241 GLY A CA 1694 C C . GLY A 215 ? 0.4756 0.3149 0.3090 0.0408 0.0570 0.0594 241 GLY A C 1695 O O . GLY A 215 ? 0.5515 0.3739 0.3477 0.0460 0.0613 0.0636 241 GLY A O 1696 N N . GLU A 216 ? 0.4032 0.2556 0.2517 0.0399 0.0441 0.0482 242 GLU A N 1697 C CA . GLU A 216 ? 0.3934 0.2423 0.2203 0.0442 0.0326 0.0398 242 GLU A CA 1698 C C . GLU A 216 ? 0.3319 0.1943 0.1754 0.0416 0.0321 0.0287 242 GLU A C 1699 O O . GLU A 216 ? 0.2976 0.1643 0.1438 0.0418 0.0186 0.0205 242 GLU A O 1700 C CB . GLU A 216 ? 0.4466 0.2943 0.2734 0.0465 0.0130 0.0385 242 GLU A CB 1701 C CG . GLU A 216 ? 0.5405 0.3695 0.3411 0.0512 0.0111 0.0495 242 GLU A CG 1702 C CD . GLU A 216 ? 0.4775 0.3074 0.2900 0.0533 -0.0059 0.0508 242 GLU A CD 1703 O OE1 . GLU A 216 ? 0.5005 0.3442 0.3346 0.0524 -0.0179 0.0415 242 GLU A OE1 1704 O OE2 . GLU A 216 ? 0.4806 0.2969 0.2820 0.0561 -0.0057 0.0616 242 GLU A OE2 1705 N N . LEU A 217 ? 0.2867 0.1553 0.1437 0.0392 0.0468 0.0291 243 LEU A N 1706 C CA . LEU A 217 ? 0.2721 0.1514 0.1447 0.0375 0.0463 0.0199 243 LEU A CA 1707 C C . LEU A 217 ? 0.2894 0.1586 0.1338 0.0423 0.0458 0.0131 243 LEU A C 1708 O O . LEU A 217 ? 0.3410 0.1948 0.1533 0.0470 0.0494 0.0163 243 LEU A O 1709 C CB . LEU A 217 ? 0.2813 0.1704 0.1800 0.0344 0.0597 0.0225 243 LEU A CB 1710 C CG . LEU A 217 ? 0.2281 0.1290 0.1586 0.0289 0.0535 0.0226 243 LEU A CG 1711 C CD1 . LEU A 217 ? 0.2593 0.1561 0.1916 0.0272 0.0495 0.0294 243 LEU A CD1 1712 C CD2 . LEU A 217 ? 0.3350 0.2451 0.2917 0.0263 0.0630 0.0238 243 LEU A CD2 1713 N N . PRO A 218 ? 0.3328 0.2078 0.1866 0.0413 0.0405 0.0037 244 PRO A N 1714 C CA . PRO A 218 ? 0.3377 0.2014 0.1670 0.0455 0.0397 -0.0043 244 PRO A CA 1715 C C . PRO A 218 ? 0.3202 0.1763 0.1354 0.0500 0.0594 -0.0019 244 PRO A C 1716 O O . PRO A 218 ? 0.3848 0.2519 0.2258 0.0482 0.0719 0.0022 244 PRO A O 1717 C CB . PRO A 218 ? 0.3275 0.2006 0.1793 0.0422 0.0336 -0.0126 244 PRO A CB 1718 C CG . PRO A 218 ? 0.3803 0.2667 0.2594 0.0368 0.0269 -0.0097 244 PRO A CG 1719 C CD . PRO A 218 ? 0.3470 0.2361 0.2318 0.0363 0.0344 0.0001 244 PRO A CD 1720 N N . PRO A 219 ? 0.3588 0.1959 0.1343 0.0560 0.0620 -0.0046 245 PRO A N 1721 C CA . PRO A 219 ? 0.3875 0.2143 0.1442 0.0615 0.0841 -0.0022 245 PRO A CA 1722 C C . PRO A 219 ? 0.5430 0.3776 0.3209 0.0630 0.0959 -0.0085 245 PRO A C 1723 O O . PRO A 219 ? 0.5591 0.3973 0.3475 0.0647 0.1155 -0.0035 245 PRO A O 1724 C CB . PRO A 219 ? 0.4318 0.2356 0.1410 0.0670 0.0769 -0.0067 245 PRO A CB 1725 C CG . PRO A 219 ? 0.4589 0.2590 0.1574 0.0654 0.0550 -0.0057 245 PRO A CG 1726 C CD . PRO A 219 ? 0.3827 0.2053 0.1268 0.0584 0.0438 -0.0091 245 PRO A CD 1727 N N . ASP A 220 ? 0.4226 0.2609 0.2117 0.0616 0.0831 -0.0185 246 ASP A N 1728 C CA . ASP A 220 ? 0.4537 0.2968 0.2616 0.0639 0.0923 -0.0243 246 ASP A CA 1729 C C . ASP A 220 ? 0.3291 0.1903 0.1785 0.0584 0.0840 -0.0244 246 ASP A C 1730 O O . ASP A 220 ? 0.3457 0.2061 0.2037 0.0589 0.0787 -0.0320 246 ASP A O 1731 C CB . ASP A 220 ? 0.4146 0.2454 0.2018 0.0662 0.0837 -0.0347 246 ASP A CB 1732 C CG . ASP A 220 ? 0.6733 0.4877 0.4231 0.0707 0.0893 -0.0339 246 ASP A CG 1733 O OD1 . ASP A 220 ? 0.6428 0.4572 0.3903 0.0731 0.1073 -0.0258 246 ASP A OD1 1734 O OD2 . ASP A 220 ? 0.7625 0.5631 0.4863 0.0715 0.0753 -0.0413 246 ASP A OD2 1735 N N . LEU A 221 ? 0.2898 0.1650 0.1628 0.0531 0.0824 -0.0158 247 LEU A N 1736 C CA . LEU A 221 ? 0.2562 0.1462 0.1635 0.0478 0.0734 -0.0151 247 LEU A CA 1737 C C . LEU A 221 ? 0.4661 0.3618 0.3969 0.0506 0.0797 -0.0182 247 LEU A C 1738 O O . LEU A 221 ? 0.2401 0.1350 0.1776 0.0497 0.0700 -0.0234 247 LEU A O 1739 C CB . LEU A 221 ? 0.3524 0.2533 0.2787 0.0429 0.0737 -0.0059 247 LEU A CB 1740 C CG . LEU A 221 ? 0.3093 0.2218 0.2639 0.0377 0.0632 -0.0054 247 LEU A CG 1741 C CD1 . LEU A 221 ? 0.3052 0.2147 0.2511 0.0346 0.0484 -0.0096 247 LEU A CD1 1742 C CD2 . LEU A 221 ? 0.3092 0.2297 0.2820 0.0337 0.0650 0.0024 247 LEU A CD2 1743 N N . GLU A 222 ? 0.2556 0.1566 0.2007 0.0541 0.0960 -0.0142 248 GLU A N 1744 C CA . GLU A 222 ? 0.2717 0.1800 0.2452 0.0579 0.1013 -0.0166 248 GLU A CA 1745 C C . GLU A 222 ? 0.2876 0.1835 0.2454 0.0637 0.1013 -0.0262 248 GLU A C 1746 O O . GLU A 222 ? 0.2604 0.1593 0.2366 0.0644 0.0940 -0.0294 248 GLU A O 1747 C CB . GLU A 222 ? 0.3198 0.2371 0.3150 0.0610 0.1212 -0.0108 248 GLU A CB 1748 C CG . GLU A 222 ? 0.3982 0.3285 0.4339 0.0637 0.1226 -0.0116 248 GLU A CG 1749 C CD . GLU A 222 ? 0.5507 0.4752 0.5779 0.0694 0.1273 -0.0180 248 GLU A CD 1750 O OE1 . GLU A 222 ? 0.6735 0.5882 0.6735 0.0721 0.1391 -0.0193 248 GLU A OE1 1751 O OE2 . GLU A 222 ? 0.4654 0.3933 0.5113 0.0717 0.1185 -0.0219 248 GLU A OE2 1752 N N . GLN A 223 ? 0.2936 0.1768 0.2176 0.0660 0.1056 -0.0297 249 GLN A N 1753 C CA . GLN A 223 ? 0.3125 0.1852 0.2215 0.0692 0.1020 -0.0387 249 GLN A CA 1754 C C . GLN A 223 ? 0.3006 0.1677 0.2071 0.0654 0.0834 -0.0447 249 GLN A C 1755 O O . GLN A 223 ? 0.3030 0.1669 0.2167 0.0668 0.0788 -0.0504 249 GLN A O 1756 C CB . GLN A 223 ? 0.3483 0.2063 0.2187 0.0720 0.1079 -0.0411 249 GLN A CB 1757 C CG . GLN A 223 ? 0.5601 0.4207 0.4318 0.0761 0.1289 -0.0352 249 GLN A CG 1758 C CD . GLN A 223 ? 0.5911 0.4619 0.4767 0.0728 0.1376 -0.0237 249 GLN A CD 1759 O OE1 . GLN A 223 ? 0.4482 0.3172 0.3238 0.0690 0.1289 -0.0205 249 GLN A OE1 1760 N NE2 . GLN A 223 ? 0.4521 0.3337 0.3636 0.0742 0.1547 -0.0176 249 GLN A NE2 1761 N N . ASN A 224 ? 0.2896 0.1550 0.1874 0.0604 0.0734 -0.0429 250 ASN A N 1762 C CA . ASN A 224 ? 0.2778 0.1398 0.1786 0.0554 0.0574 -0.0470 250 ASN A CA 1763 C C . ASN A 224 ? 0.2852 0.1554 0.2161 0.0536 0.0541 -0.0438 250 ASN A C 1764 O O . ASN A 224 ? 0.2546 0.1201 0.1908 0.0523 0.0466 -0.0476 250 ASN A O 1765 C CB . ASN A 224 ? 0.2783 0.1411 0.1687 0.0496 0.0466 -0.0447 250 ASN A CB 1766 C CG . ASN A 224 ? 0.2876 0.1486 0.1845 0.0435 0.0321 -0.0484 250 ASN A CG 1767 O OD1 . ASN A 224 ? 0.2978 0.1470 0.1856 0.0438 0.0269 -0.0564 250 ASN A OD1 1768 N ND2 . ASN A 224 ? 0.2817 0.1542 0.1956 0.0374 0.0263 -0.0424 250 ASN A ND2 1769 N N . PHE A 225 ? 0.2360 0.1208 0.1880 0.0520 0.0568 -0.0357 251 PHE A N 1770 C CA . PHE A 225 ? 0.2699 0.1618 0.2483 0.0511 0.0518 -0.0323 251 PHE A CA 1771 C C . PHE A 225 ? 0.2673 0.1536 0.2549 0.0582 0.0563 -0.0368 251 PHE A C 1772 O O . PHE A 225 ? 0.2438 0.1259 0.2393 0.0577 0.0474 -0.0374 251 PHE A O 1773 C CB . PHE A 225 ? 0.2050 0.1121 0.2061 0.0498 0.0545 -0.0245 251 PHE A CB 1774 C CG . PHE A 225 ? 0.1918 0.1040 0.1889 0.0427 0.0475 -0.0199 251 PHE A CG 1775 C CD1 . PHE A 225 ? 0.2911 0.1968 0.2683 0.0387 0.0408 -0.0222 251 PHE A CD1 1776 C CD2 . PHE A 225 ? 0.2332 0.1564 0.2496 0.0403 0.0474 -0.0138 251 PHE A CD2 1777 C CE1 . PHE A 225 ? 0.2832 0.1937 0.2593 0.0335 0.0355 -0.0183 251 PHE A CE1 1778 C CE2 . PHE A 225 ? 0.2374 0.1630 0.2496 0.0346 0.0413 -0.0105 251 PHE A CE2 1779 C CZ . PHE A 225 ? 0.2683 0.1876 0.2602 0.0317 0.0362 -0.0127 251 PHE A CZ 1780 N N . ALA A 226 ? 0.2633 0.1517 0.2491 0.0636 0.0686 -0.0387 252 ALA A N 1781 C CA . ALA A 226 ? 0.3376 0.2263 0.3366 0.0698 0.0724 -0.0420 252 ALA A CA 1782 C C . ALA A 226 ? 0.3617 0.2360 0.3467 0.0701 0.0639 -0.0496 252 ALA A C 1783 O O . ALA A 226 ? 0.2918 0.1642 0.2915 0.0738 0.0601 -0.0509 252 ALA A O 1784 C CB . ALA A 226 ? 0.2754 0.1680 0.2721 0.0750 0.0895 -0.0426 252 ALA A CB 1785 N N . ARG A 227 ? 0.2794 0.1432 0.2381 0.0661 0.0595 -0.0545 253 ARG A N 1786 C CA . ARG A 227 ? 0.3854 0.2362 0.3357 0.0652 0.0516 -0.0621 253 ARG A CA 1787 C C . ARG A 227 ? 0.3532 0.2011 0.3142 0.0591 0.0390 -0.0593 253 ARG A C 1788 O O . ARG A 227 ? 0.2867 0.1254 0.2516 0.0590 0.0337 -0.0629 253 ARG A O 1789 C CB . ARG A 227 ? 0.4042 0.2447 0.3255 0.0630 0.0500 -0.0689 253 ARG A CB 1790 C CG . ARG A 227 ? 0.3444 0.1849 0.2547 0.0557 0.0412 -0.0668 253 ARG A CG 1791 C CD . ARG A 227 ? 0.3945 0.2241 0.2764 0.0550 0.0373 -0.0738 253 ARG A CD 1792 N NE . ARG A 227 ? 0.3942 0.2249 0.2693 0.0487 0.0270 -0.0718 253 ARG A NE 1793 C CZ . ARG A 227 ? 0.3832 0.2052 0.2426 0.0453 0.0157 -0.0778 253 ARG A CZ 1794 N NH1 . ARG A 227 ? 0.3608 0.1708 0.2068 0.0470 0.0133 -0.0863 253 ARG A NH1 1795 N NH2 . ARG A 227 ? 0.3239 0.1492 0.1829 0.0402 0.0059 -0.0756 253 ARG A NH2 1796 N N . PHE A 228 ? 0.2586 0.1131 0.2240 0.0541 0.0351 -0.0523 254 PHE A N 1797 C CA . PHE A 228 ? 0.2484 0.0998 0.2230 0.0491 0.0259 -0.0478 254 PHE A CA 1798 C C . PHE A 228 ? 0.2473 0.0997 0.2406 0.0546 0.0245 -0.0437 254 PHE A C 1799 O O . PHE A 228 ? 0.2601 0.1037 0.2581 0.0536 0.0180 -0.0425 254 PHE A O 1800 C CB . PHE A 228 ? 0.2322 0.0893 0.2042 0.0430 0.0229 -0.0421 254 PHE A CB 1801 C CG . PHE A 228 ? 0.2381 0.0916 0.1963 0.0365 0.0189 -0.0457 254 PHE A CG 1802 C CD1 . PHE A 228 ? 0.2411 0.0962 0.1850 0.0376 0.0216 -0.0494 254 PHE A CD1 1803 C CD2 . PHE A 228 ? 0.2456 0.0934 0.2061 0.0296 0.0125 -0.0451 254 PHE A CD2 1804 C CE1 . PHE A 228 ? 0.3290 0.1803 0.2623 0.0325 0.0148 -0.0532 254 PHE A CE1 1805 C CE2 . PHE A 228 ? 0.2367 0.0824 0.1909 0.0236 0.0081 -0.0489 254 PHE A CE2 1806 C CZ . PHE A 228 ? 0.2639 0.1116 0.2052 0.0254 0.0077 -0.0535 254 PHE A CZ 1807 N N . VAL A 229 ? 0.2524 0.1157 0.2583 0.0603 0.0307 -0.0409 255 VAL A N 1808 C CA . VAL A 229 ? 0.2435 0.1096 0.2697 0.0666 0.0280 -0.0370 255 VAL A CA 1809 C C . VAL A 229 ? 0.3002 0.1571 0.3268 0.0733 0.0292 -0.0427 255 VAL A C 1810 O O . VAL A 229 ? 0.3229 0.1719 0.3556 0.0769 0.0224 -0.0397 255 VAL A O 1811 C CB . VAL A 229 ? 0.2337 0.1176 0.2808 0.0698 0.0352 -0.0331 255 VAL A CB 1812 C CG1 . VAL A 229 ? 0.3197 0.2095 0.3923 0.0769 0.0331 -0.0306 255 VAL A CG1 1813 C CG2 . VAL A 229 ? 0.2472 0.1378 0.2974 0.0635 0.0304 -0.0271 255 VAL A CG2 1814 N N . ALA A 230 ? 0.3150 0.1704 0.3312 0.0751 0.0379 -0.0506 256 ALA A N 1815 C CA . ALA A 230 ? 0.2970 0.1419 0.3117 0.0813 0.0391 -0.0579 256 ALA A CA 1816 C C . ALA A 230 ? 0.3035 0.1323 0.3118 0.0764 0.0277 -0.0602 256 ALA A C 1817 O O . ALA A 230 ? 0.3942 0.2121 0.4063 0.0815 0.0246 -0.0636 256 ALA A O 1818 C CB . ALA A 230 ? 0.3183 0.1626 0.3180 0.0835 0.0508 -0.0662 256 ALA A CB 1819 N N . ALA A 231 ? 0.3669 0.1947 0.3679 0.0661 0.0228 -0.0577 257 ALA A N 1820 C CA . ALA A 231 ? 0.4271 0.2429 0.4285 0.0585 0.0164 -0.0570 257 ALA A CA 1821 C C . ALA A 231 ? 0.3933 0.2076 0.4073 0.0573 0.0123 -0.0463 257 ALA A C 1822 O O . ALA A 231 ? 0.3677 0.1688 0.3788 0.0523 0.0120 -0.0426 257 ALA A O 1823 C CB . ALA A 231 ? 0.2881 0.1041 0.2759 0.0483 0.0150 -0.0568 257 ALA A CB 1824 N N . GLY A 232 ? 0.3565 0.1794 0.3751 0.0634 0.0074 -0.0410 258 GLY A N 1825 C CA . GLY A 232 ? 0.3889 0.1991 0.4030 0.0658 0.0117 -0.0279 258 GLY A CA 1826 C C . GLY A 232 ? 0.3756 0.1895 0.3901 0.0583 0.0049 -0.0208 258 GLY A C 1827 O O . GLY A 232 ? 0.3864 0.1936 0.4004 0.0583 -0.0026 -0.0135 258 GLY A O 1828 N N . VAL A 233 ? 0.2725 0.0966 0.2837 0.0524 0.0059 -0.0230 259 VAL A N 1829 C CA . VAL A 233 ? 0.2634 0.0897 0.2672 0.0469 -0.0006 -0.0164 259 VAL A CA 1830 C C . VAL A 233 ? 0.2902 0.1293 0.3020 0.0510 -0.0026 -0.0145 259 VAL A C 1831 O O . VAL A 233 ? 0.2415 0.0897 0.2629 0.0565 0.0028 -0.0187 259 VAL A O 1832 C CB . VAL A 233 ? 0.2735 0.1004 0.2650 0.0377 0.0008 -0.0188 259 VAL A CB 1833 C CG1 . VAL A 233 ? 0.2596 0.0740 0.2468 0.0325 0.0010 -0.0196 259 VAL A CG1 1834 C CG2 . VAL A 233 ? 0.2367 0.0742 0.2278 0.0382 0.0058 -0.0262 259 VAL A CG2 1835 N N . GLU A 234 ? 0.2476 0.0868 0.2549 0.0484 -0.0110 -0.0082 260 GLU A N 1836 C CA . GLU A 234 ? 0.2471 0.0989 0.2631 0.0493 -0.0145 -0.0073 260 GLU A CA 1837 C C . GLU A 234 ? 0.2709 0.1260 0.2755 0.0431 -0.0092 -0.0100 260 GLU A C 1838 O O . GLU A 234 ? 0.2190 0.0670 0.2087 0.0375 -0.0055 -0.0111 260 GLU A O 1839 C CB . GLU A 234 ? 0.2522 0.1004 0.2651 0.0493 -0.0275 -0.0009 260 GLU A CB 1840 C CG . GLU A 234 ? 0.3267 0.1613 0.3124 0.0427 -0.0298 0.0030 260 GLU A CG 1841 C CD . GLU A 234 ? 0.4123 0.2390 0.3880 0.0439 -0.0433 0.0085 260 GLU A CD 1842 O OE1 . GLU A 234 ? 0.2865 0.1098 0.2463 0.0401 -0.0460 0.0095 260 GLU A OE1 1843 O OE2 . GLU A 234 ? 0.3913 0.2138 0.3733 0.0491 -0.0519 0.0114 260 GLU A OE2 1844 N N . ILE A 235 ? 0.2045 0.0755 0.2192 0.0425 -0.0075 -0.0103 261 ILE A N 1845 C CA . ILE A 235 ? 0.1923 0.0700 0.1968 0.0362 -0.0023 -0.0114 261 ILE A CA 1846 C C . ILE A 235 ? 0.1896 0.0741 0.1972 0.0338 -0.0080 -0.0082 261 ILE A C 1847 O O . ILE A 235 ? 0.1876 0.0754 0.2098 0.0370 -0.0156 -0.0060 261 ILE A O 1848 C CB . ILE A 235 ? 0.1862 0.0737 0.1949 0.0375 0.0081 -0.0160 261 ILE A CB 1849 C CG1 . ILE A 235 ? 0.1919 0.0923 0.2221 0.0421 0.0117 -0.0150 261 ILE A CG1 1850 C CG2 . ILE A 235 ? 0.1973 0.0753 0.2002 0.0404 0.0126 -0.0212 261 ILE A CG2 1851 C CD1 . ILE A 235 ? 0.2081 0.1156 0.2363 0.0431 0.0241 -0.0176 261 ILE A CD1 1852 N N . ALA A 236 ? 0.1797 0.0661 0.1757 0.0284 -0.0052 -0.0084 262 ALA A N 1853 C CA . ALA A 236 ? 0.1751 0.0663 0.1723 0.0260 -0.0093 -0.0068 262 ALA A CA 1854 C C . ALA A 236 ? 0.1653 0.0636 0.1583 0.0223 -0.0020 -0.0083 262 ALA A C 1855 O O . ALA A 236 ? 0.1839 0.0802 0.1679 0.0206 0.0030 -0.0102 262 ALA A O 1856 C CB . ALA A 236 ? 0.1914 0.0688 0.1715 0.0244 -0.0173 -0.0045 262 ALA A CB 1857 N N . VAL A 237 ? 0.1779 0.0841 0.1798 0.0213 -0.0027 -0.0073 263 VAL A N 1858 C CA . VAL A 237 ? 0.1777 0.0879 0.1747 0.0184 0.0019 -0.0077 263 VAL A CA 1859 C C . VAL A 237 ? 0.1862 0.0883 0.1708 0.0157 -0.0025 -0.0078 263 VAL A C 1860 O O . VAL A 237 ? 0.1695 0.0669 0.1543 0.0157 -0.0101 -0.0073 263 VAL A O 1861 C CB . VAL A 237 ? 0.2081 0.1277 0.2202 0.0184 0.0046 -0.0057 263 VAL A CB 1862 C CG1 . VAL A 237 ? 0.1938 0.1142 0.1999 0.0158 0.0068 -0.0051 263 VAL A CG1 1863 C CG2 . VAL A 237 ? 0.2416 0.1671 0.2608 0.0217 0.0132 -0.0055 263 VAL A CG2 1864 N N . THR A 238 ? 0.1583 0.0577 0.1322 0.0139 0.0020 -0.0091 264 THR A N 1865 C CA . THR A 238 ? 0.1932 0.0825 0.1531 0.0123 0.0014 -0.0093 264 THR A CA 1866 C C . THR A 238 ? 0.1955 0.0858 0.1533 0.0111 0.0038 -0.0107 264 THR A C 1867 O O . THR A 238 ? 0.1796 0.0595 0.1244 0.0109 0.0031 -0.0116 264 THR A O 1868 C CB . THR A 238 ? 0.2301 0.1136 0.1822 0.0107 0.0066 -0.0093 264 THR A CB 1869 O OG1 . THR A 238 ? 0.1791 0.0721 0.1404 0.0096 0.0112 -0.0112 264 THR A OG1 1870 C CG2 . THR A 238 ? 0.2202 0.0965 0.1700 0.0123 0.0031 -0.0077 264 THR A CG2 1871 N N . GLU A 239 ? 0.1787 0.0787 0.1464 0.0112 0.0068 -0.0109 265 GLU A N 1872 C CA . GLU A 239 ? 0.1571 0.0571 0.1245 0.0111 0.0091 -0.0121 265 GLU A CA 1873 C C . GLU A 239 ? 0.1500 0.0569 0.1277 0.0118 0.0080 -0.0104 265 GLU A C 1874 O O . GLU A 239 ? 0.1474 0.0580 0.1287 0.0127 0.0103 -0.0102 265 GLU A O 1875 C CB . GLU A 239 ? 0.1740 0.0765 0.1422 0.0105 0.0154 -0.0134 265 GLU A CB 1876 C CG . GLU A 239 ? 0.1663 0.0609 0.1253 0.0089 0.0195 -0.0136 265 GLU A CG 1877 C CD . GLU A 239 ? 0.2798 0.1786 0.2467 0.0072 0.0271 -0.0147 265 GLU A CD 1878 O OE1 . GLU A 239 ? 0.1922 0.0993 0.1711 0.0083 0.0283 -0.0160 265 GLU A OE1 1879 O OE2 . GLU A 239 ? 0.2623 0.1559 0.2259 0.0048 0.0318 -0.0138 265 GLU A OE2 1880 N N . LEU A 240 ? 0.1491 0.0571 0.1331 0.0115 0.0046 -0.0085 266 LEU A N 1881 C CA . LEU A 240 ? 0.1814 0.0949 0.1752 0.0117 0.0063 -0.0052 266 LEU A CA 1882 C C . LEU A 240 ? 0.1484 0.0583 0.1436 0.0115 0.0058 -0.0048 266 LEU A C 1883 O O . LEU A 240 ? 0.1638 0.0664 0.1577 0.0104 0.0018 -0.0074 266 LEU A O 1884 C CB . LEU A 240 ? 0.1686 0.0849 0.1749 0.0108 0.0045 -0.0030 266 LEU A CB 1885 C CG . LEU A 240 ? 0.1920 0.1134 0.2106 0.0103 0.0095 0.0019 266 LEU A CG 1886 C CD1 . LEU A 240 ? 0.1459 0.0700 0.1557 0.0129 0.0171 0.0042 266 LEU A CD1 1887 C CD2 . LEU A 240 ? 0.1443 0.0707 0.1820 0.0092 0.0085 0.0034 266 LEU A CD2 1888 N N . ASP A 241 ? 0.1477 0.0603 0.1435 0.0130 0.0087 -0.0021 267 ASP A N 1889 C CA . ASP A 241 ? 0.1525 0.0609 0.1529 0.0132 0.0084 0.0006 267 ASP A CA 1890 C C . ASP A 241 ? 0.1556 0.0663 0.1539 0.0152 0.0115 0.0063 267 ASP A C 1891 O O . ASP A 241 ? 0.1552 0.0697 0.1460 0.0171 0.0124 0.0061 267 ASP A O 1892 C CB . ASP A 241 ? 0.1563 0.0593 0.1544 0.0150 0.0071 -0.0034 267 ASP A CB 1893 C CG . ASP A 241 ? 0.1948 0.1026 0.1898 0.0174 0.0091 -0.0062 267 ASP A CG 1894 O OD1 . ASP A 241 ? 0.2006 0.1146 0.1954 0.0184 0.0089 -0.0042 267 ASP A OD1 1895 O OD2 . ASP A 241 ? 0.1972 0.1015 0.1903 0.0182 0.0111 -0.0107 267 ASP A OD2 1896 N N . ILE A 242 ? 0.1625 0.0685 0.1656 0.0145 0.0128 0.0116 268 ILE A N 1897 C CA . ILE A 242 ? 0.1889 0.0930 0.1850 0.0165 0.0169 0.0187 268 ILE A CA 1898 C C . ILE A 242 ? 0.2016 0.0971 0.1979 0.0183 0.0148 0.0230 268 ILE A C 1899 O O . ILE A 242 ? 0.1877 0.0769 0.1932 0.0156 0.0165 0.0269 268 ILE A O 1900 C CB . ILE A 242 ? 0.1816 0.0871 0.1833 0.0139 0.0248 0.0239 268 ILE A CB 1901 C CG1 . ILE A 242 ? 0.1956 0.1092 0.1996 0.0134 0.0261 0.0193 268 ILE A CG1 1902 C CG2 . ILE A 242 ? 0.1977 0.0974 0.1847 0.0167 0.0315 0.0319 268 ILE A CG2 1903 C CD1 . ILE A 242 ? 0.1708 0.0882 0.1862 0.0118 0.0352 0.0236 268 ILE A CD1 1904 N N . ARG A 243 ? 0.1850 0.0801 0.1741 0.0230 0.0100 0.0220 269 ARG A N 1905 C CA . ARG A 243 ? 0.1930 0.0806 0.1857 0.0261 0.0060 0.0241 269 ARG A CA 1906 C C . ARG A 243 ? 0.2639 0.1418 0.2457 0.0291 0.0061 0.0341 269 ARG A C 1907 O O . ARG A 243 ? 0.2224 0.0994 0.1889 0.0298 0.0089 0.0385 269 ARG A O 1908 C CB . ARG A 243 ? 0.1936 0.0871 0.1905 0.0302 0.0005 0.0176 269 ARG A CB 1909 C CG . ARG A 243 ? 0.2181 0.1170 0.2067 0.0334 -0.0044 0.0178 269 ARG A CG 1910 C CD . ARG A 243 ? 0.2147 0.1225 0.2162 0.0357 -0.0088 0.0108 269 ARG A CD 1911 N NE . ARG A 243 ? 0.1886 0.1003 0.1859 0.0387 -0.0173 0.0110 269 ARG A NE 1912 C CZ . ARG A 243 ? 0.3149 0.2316 0.3054 0.0363 -0.0181 0.0075 269 ARG A CZ 1913 N NH1 . ARG A 243 ? 0.2321 0.1512 0.2205 0.0314 -0.0104 0.0045 269 ARG A NH1 1914 N NH2 . ARG A 243 ? 0.3374 0.2551 0.3233 0.0390 -0.0283 0.0066 269 ARG A NH2 1915 N N . MET A 244 ? 0.2318 0.0999 0.2189 0.0314 0.0033 0.0378 270 MET A N 1916 C CA . MET A 244 ? 0.2544 0.1090 0.2292 0.0347 0.0028 0.0490 270 MET A CA 1917 C C . MET A 244 ? 0.2532 0.1009 0.2351 0.0408 -0.0056 0.0493 270 MET A C 1918 O O . MET A 244 ? 0.2469 0.0997 0.2448 0.0416 -0.0077 0.0408 270 MET A O 1919 C CB . MET A 244 ? 0.2553 0.1006 0.2327 0.0290 0.0125 0.0572 270 MET A CB 1920 C CG . MET A 244 ? 0.2506 0.0911 0.2489 0.0252 0.0119 0.0540 270 MET A CG 1921 S SD . MET A 244 ? 0.3245 0.1617 0.3354 0.0154 0.0212 0.0599 270 MET A SD 1922 C CE . MET A 244 ? 0.2721 0.1254 0.2904 0.0111 0.0263 0.0538 270 MET A CE 1923 N N . ASN A 245 ? 0.2770 0.1116 0.2458 0.0460 -0.0099 0.0593 271 ASN A N 1924 C CA . ASN A 245 ? 0.2877 0.1139 0.2654 0.0529 -0.0185 0.0609 271 ASN A CA 1925 C C . ASN A 245 ? 0.3209 0.1378 0.3130 0.0489 -0.0143 0.0616 271 ASN A C 1926 O O . ASN A 245 ? 0.3048 0.1162 0.2930 0.0414 -0.0069 0.0663 271 ASN A O 1927 C CB . ASN A 245 ? 0.3377 0.1533 0.2962 0.0591 -0.0263 0.0717 271 ASN A CB 1928 C CG . ASN A 245 ? 0.3619 0.1838 0.3063 0.0643 -0.0367 0.0687 271 ASN A CG 1929 O OD1 . ASN A 245 ? 0.5012 0.3406 0.4622 0.0642 -0.0404 0.0576 271 ASN A OD1 1930 N ND2 . ASN A 245 ? 0.4370 0.2491 0.3535 0.0666 -0.0402 0.0771 271 ASN A ND2 1931 N N . LEU A 246 ? 0.3043 0.1219 0.3087 0.0539 -0.0164 0.0544 272 LEU A N 1932 C CA . LEU A 246 ? 0.3776 0.1851 0.3880 0.0509 -0.0136 0.0512 272 LEU A CA 1933 C C . LEU A 246 ? 0.4329 0.2259 0.4386 0.0572 -0.0167 0.0594 272 LEU A C 1934 O O . LEU A 246 ? 0.3676 0.1650 0.3752 0.0657 -0.0225 0.0630 272 LEU A O 1935 C CB . LEU A 246 ? 0.3893 0.2054 0.4146 0.0519 -0.0125 0.0375 272 LEU A CB 1936 C CG . LEU A 246 ? 0.3693 0.1982 0.3978 0.0470 -0.0092 0.0287 272 LEU A CG 1937 C CD1 . LEU A 246 ? 0.3169 0.1492 0.3534 0.0496 -0.0072 0.0165 272 LEU A CD1 1938 C CD2 . LEU A 246 ? 0.3221 0.1476 0.3470 0.0373 -0.0054 0.0302 272 LEU A CD2 1939 N N . PRO A 247 ? 0.5239 0.3011 0.5273 0.0525 -0.0144 0.0624 273 PRO A N 1940 C CA . PRO A 247 ? 0.5507 0.3267 0.5600 0.0412 -0.0093 0.0593 273 PRO A CA 1941 C C . PRO A 247 ? 0.5235 0.3031 0.5265 0.0333 -0.0048 0.0677 273 PRO A C 1942 O O . PRO A 247 ? 0.5407 0.3155 0.5301 0.0354 -0.0060 0.0786 273 PRO A O 1943 C CB . PRO A 247 ? 0.5928 0.3505 0.6040 0.0404 -0.0093 0.0622 273 PRO A CB 1944 C CG . PRO A 247 ? 0.6563 0.4021 0.6550 0.0496 -0.0135 0.0720 273 PRO A CG 1945 C CD . PRO A 247 ? 0.5853 0.3466 0.5861 0.0590 -0.0168 0.0686 273 PRO A CD 1946 N N . PRO A 248 ? 0.6082 0.3213 0.4437 0.0279 0.0086 0.0780 274 PRO A N 1947 C CA . PRO A 248 ? 0.5622 0.2870 0.3881 0.0156 0.0164 0.0815 274 PRO A CA 1948 C C . PRO A 248 ? 0.5947 0.3048 0.4048 0.0089 0.0271 0.0943 274 PRO A C 1949 O O . PRO A 248 ? 0.6053 0.2995 0.4245 -0.0001 0.0344 0.0964 274 PRO A O 1950 C CB . PRO A 248 ? 0.5464 0.2861 0.3975 -0.0022 0.0233 0.0693 274 PRO A CB 1951 C CG . PRO A 248 ? 0.5404 0.2834 0.4105 0.0044 0.0159 0.0574 274 PRO A CG 1952 C CD . PRO A 248 ? 0.4419 0.1584 0.3018 0.0187 0.0118 0.0647 274 PRO A CD 1953 N N . SER A 249 ? 0.5765 0.2916 0.3626 0.0134 0.0279 0.1021 275 SER A N 1954 C CA . SER A 249 ? 0.5741 0.2781 0.3446 0.0061 0.0409 0.1140 275 SER A CA 1955 C C . SER A 249 ? 0.6267 0.3464 0.4162 -0.0145 0.0563 0.1099 275 SER A C 1956 O O . SER A 249 ? 0.6116 0.3535 0.4183 -0.0206 0.0556 0.0987 275 SER A O 1957 C CB . SER A 249 ? 0.6188 0.3241 0.3552 0.0191 0.0365 0.1218 275 SER A CB 1958 O OG . SER A 249 ? 0.6766 0.4068 0.4114 0.0169 0.0365 0.1139 275 SER A OG 1959 N N . GLN A 250 ? 0.5935 0.3026 0.3815 -0.0249 0.0699 0.1192 276 GLN A N 1960 C CA . GLN A 250 ? 0.5891 0.3167 0.3991 -0.0433 0.0841 0.1160 276 GLN A CA 1961 C C . GLN A 250 ? 0.5276 0.2795 0.3277 -0.0412 0.0884 0.1132 276 GLN A C 1962 O O . GLN A 250 ? 0.5778 0.3550 0.4022 -0.0510 0.0926 0.1034 276 GLN A O 1963 C CB . GLN A 250 ? 0.6272 0.3377 0.4354 -0.0536 0.0980 0.1283 276 GLN A CB 1964 C CG . GLN A 250 ? 0.7805 0.5128 0.6166 -0.0726 0.1124 0.1252 276 GLN A CG 1965 C CD . GLN A 250 ? 0.9181 0.6687 0.7940 -0.0841 0.1062 0.1099 276 GLN A CD 1966 O OE1 . GLN A 250 ? 1.0239 0.7607 0.9085 -0.0832 0.0958 0.1043 276 GLN A OE1 1967 N NE2 . GLN A 250 ? 0.8865 0.6687 0.7856 -0.0934 0.1120 0.1023 276 GLN A NE2 1968 N N . ALA A 251 ? 0.5201 0.2646 0.2844 -0.0271 0.0857 0.1207 277 ALA A N 1969 C CA . ALA A 251 ? 0.5131 0.2774 0.2626 -0.0228 0.0884 0.1169 277 ALA A CA 1970 C C . ALA A 251 ? 0.4869 0.2716 0.2491 -0.0198 0.0772 0.1026 277 ALA A C 1971 O O . ALA A 251 ? 0.4855 0.2926 0.2571 -0.0250 0.0838 0.0950 277 ALA A O 1972 C CB . ALA A 251 ? 0.5848 0.3351 0.2909 -0.0065 0.0829 0.1257 277 ALA A CB 1973 N N . ASP A 252 ? 0.4551 0.2318 0.2185 -0.0112 0.0610 0.0991 278 ASP A N 1974 C CA . ASP A 252 ? 0.4153 0.2107 0.1915 -0.0090 0.0501 0.0860 278 ASP A CA 1975 C C . ASP A 252 ? 0.4248 0.2388 0.2423 -0.0247 0.0558 0.0755 278 ASP A C 1976 O O . ASP A 252 ? 0.3485 0.1904 0.1848 -0.0267 0.0526 0.0631 278 ASP A O 1977 C CB . ASP A 252 ? 0.4777 0.2701 0.2557 0.0056 0.0296 0.0822 278 ASP A CB 1978 C CG . ASP A 252 ? 0.5516 0.3437 0.2986 0.0229 0.0157 0.0842 278 ASP A CG 1979 O OD1 . ASP A 252 ? 0.5608 0.3590 0.2858 0.0234 0.0205 0.0842 278 ASP A OD1 1980 O OD2 . ASP A 252 ? 0.5836 0.3708 0.3292 0.0368 -0.0008 0.0844 278 ASP A OD2 1981 N N . ILE A 253 ? 0.3839 0.1819 0.2151 -0.0351 0.0627 0.0795 279 ILE A N 1982 C CA . ILE A 253 ? 0.4145 0.2287 0.2816 -0.0499 0.0660 0.0692 279 ILE A CA 1983 C C . ILE A 253 ? 0.3433 0.1827 0.2237 -0.0594 0.0785 0.0669 279 ILE A C 1984 O O . ILE A 253 ? 0.3327 0.1968 0.2364 -0.0641 0.0763 0.0557 279 ILE A O 1985 C CB . ILE A 253 ? 0.4315 0.2312 0.3156 -0.0578 0.0669 0.0703 279 ILE A CB 1986 C CG1 . ILE A 253 ? 0.4814 0.2594 0.3575 -0.0469 0.0549 0.0694 279 ILE A CG1 1987 C CG2 . ILE A 253 ? 0.4460 0.2657 0.3653 -0.0718 0.0672 0.0586 279 ILE A CG2 1988 C CD1 . ILE A 253 ? 0.5746 0.3307 0.4570 -0.0511 0.0565 0.0730 279 ILE A CD1 1989 N N . GLU A 254 ? 0.3729 0.2087 0.2407 -0.0601 0.0903 0.0769 280 GLU A N 1990 C CA . GLU A 254 ? 0.3963 0.2560 0.2762 -0.0667 0.1038 0.0754 280 GLU A CA 1991 C C . GLU A 254 ? 0.3997 0.2757 0.2664 -0.0577 0.1026 0.0685 280 GLU A C 1992 O O . GLU A 254 ? 0.3284 0.2300 0.2187 -0.0625 0.1070 0.0596 280 GLU A O 1993 C CB . GLU A 254 ? 0.4595 0.3088 0.3240 -0.0683 0.1176 0.0885 280 GLU A CB 1994 C CG . GLU A 254 ? 0.6354 0.4748 0.5214 -0.0817 0.1230 0.0939 280 GLU A CG 1995 C CD . GLU A 254 ? 0.8826 0.7099 0.7517 -0.0845 0.1388 0.1082 280 GLU A CD 1996 O OE1 . GLU A 254 ? 0.9552 0.7628 0.7847 -0.0724 0.1389 0.1177 280 GLU A OE1 1997 O OE2 . GLU A 254 ? 0.9203 0.7584 0.8156 -0.0988 0.1506 0.1100 280 GLU A OE2 1998 N N . GLN A 255 ? 0.3861 0.2479 0.2161 -0.0437 0.0947 0.0715 281 GLN A N 1999 C CA . GLN A 255 ? 0.3567 0.2347 0.1757 -0.0338 0.0883 0.0615 281 GLN A CA 2000 C C . GLN A 255 ? 0.4525 0.3526 0.3051 -0.0343 0.0737 0.0462 281 GLN A C 2001 O O . GLN A 255 ? 0.2914 0.2115 0.1538 -0.0324 0.0735 0.0361 281 GLN A O 2002 C CB . GLN A 255 ? 0.3850 0.2462 0.1626 -0.0180 0.0761 0.0652 281 GLN A CB 2003 C CG . GLN A 255 ? 0.4174 0.2942 0.1831 -0.0081 0.0676 0.0527 281 GLN A CG 2004 C CD . GLN A 255 ? 0.4270 0.3147 0.1871 -0.0108 0.0868 0.0507 281 GLN A CD 2005 O OE1 . GLN A 255 ? 0.4168 0.3004 0.1699 -0.0137 0.1014 0.0604 281 GLN A OE1 2006 N NE2 . GLN A 255 ? 0.3629 0.2718 0.1402 -0.0091 0.0826 0.0356 281 GLN A NE2 2007 N N . GLN A 256 ? 0.2945 0.1884 0.1624 -0.0362 0.0629 0.0448 282 GLN A N 2008 C CA . GLN A 256 ? 0.3224 0.2339 0.2178 -0.0368 0.0516 0.0322 282 GLN A CA 2009 C C . GLN A 256 ? 0.2926 0.2246 0.2158 -0.0465 0.0595 0.0264 282 GLN A C 2010 O O . GLN A 256 ? 0.2125 0.1619 0.1494 -0.0437 0.0539 0.0166 282 GLN A O 2011 C CB . GLN A 256 ? 0.3411 0.2407 0.2460 -0.0374 0.0427 0.0321 282 GLN A CB 2012 C CG . GLN A 256 ? 0.2361 0.1516 0.1644 -0.0377 0.0335 0.0203 282 GLN A CG 2013 C CD . GLN A 256 ? 0.2849 0.1885 0.2214 -0.0389 0.0282 0.0190 282 GLN A CD 2014 O OE1 . GLN A 256 ? 0.3063 0.1988 0.2486 -0.0476 0.0330 0.0213 282 GLN A OE1 2015 N NE2 . GLN A 256 ? 0.2192 0.1247 0.1573 -0.0303 0.0189 0.0144 282 GLN A NE2 2016 N N . ALA A 257 ? 0.2488 0.1779 0.1819 -0.0577 0.0720 0.0325 283 ALA A N 2017 C CA . ALA A 257 ? 0.2624 0.2147 0.2259 -0.0666 0.0793 0.0273 283 ALA A CA 2018 C C . ALA A 257 ? 0.2315 0.2018 0.1916 -0.0596 0.0862 0.0234 283 ALA A C 2019 O O . ALA A 257 ? 0.2411 0.2319 0.2221 -0.0577 0.0820 0.0141 283 ALA A O 2020 C CB . ALA A 257 ? 0.2547 0.2014 0.2308 -0.0813 0.0939 0.0354 283 ALA A CB 2021 N N . ARG A 258 ? 0.2594 0.2192 0.1895 -0.0542 0.0962 0.0303 284 ARG A N 2022 C CA . ARG A 258 ? 0.2642 0.2375 0.1861 -0.0465 0.1042 0.0253 284 ARG A CA 2023 C C . ARG A 258 ? 0.3032 0.2813 0.2223 -0.0359 0.0876 0.0134 284 ARG A C 2024 O O . ARG A 258 ? 0.2332 0.2274 0.1643 -0.0317 0.0896 0.0047 284 ARG A O 2025 C CB . ARG A 258 ? 0.3060 0.2624 0.1876 -0.0415 0.1173 0.0348 284 ARG A CB 2026 C CG . ARG A 258 ? 0.3296 0.2820 0.2178 -0.0509 0.1318 0.0471 284 ARG A CG 2027 C CD . ARG A 258 ? 0.3734 0.3121 0.2232 -0.0430 0.1401 0.0559 284 ARG A CD 2028 N NE . ARG A 258 ? 0.4318 0.3603 0.2849 -0.0520 0.1503 0.0691 284 ARG A NE 2029 C CZ . ARG A 258 ? 0.5492 0.4497 0.3772 -0.0505 0.1455 0.0800 284 ARG A CZ 2030 N NH1 . ARG A 258 ? 0.4293 0.3123 0.2283 -0.0393 0.1298 0.0793 284 ARG A NH1 2031 N NH2 . ARG A 258 ? 0.6431 0.5335 0.4757 -0.0594 0.1560 0.0916 284 ARG A NH2 2032 N N . ASP A 259 ? 0.2403 0.2045 0.1464 -0.0318 0.0720 0.0131 285 ASP A N 2033 C CA . ASP A 259 ? 0.2326 0.2003 0.1392 -0.0243 0.0572 0.0025 285 ASP A CA 2034 C C . ASP A 259 ? 0.2086 0.1906 0.1469 -0.0273 0.0518 -0.0049 285 ASP A C 2035 O O . ASP A 259 ? 0.1980 0.1867 0.1409 -0.0222 0.0484 -0.0134 285 ASP A O 2036 C CB . ASP A 259 ? 0.2711 0.2247 0.1634 -0.0200 0.0429 0.0042 285 ASP A CB 2037 C CG . ASP A 259 ? 0.3959 0.3345 0.2507 -0.0126 0.0431 0.0099 285 ASP A CG 2038 O OD1 . ASP A 259 ? 0.3564 0.2954 0.1910 -0.0083 0.0509 0.0079 285 ASP A OD1 2039 O OD2 . ASP A 259 ? 0.3690 0.2944 0.2125 -0.0096 0.0350 0.0163 285 ASP A OD2 2040 N N . TYR A 260 ? 0.1798 0.1631 0.1367 -0.0348 0.0501 -0.0018 286 TYR A N 2041 C CA . TYR A 260 ? 0.1797 0.1759 0.1617 -0.0366 0.0452 -0.0079 286 TYR A CA 2042 C C . TYR A 260 ? 0.1559 0.1704 0.1532 -0.0351 0.0536 -0.0116 286 TYR A C 2043 O O . TYR A 260 ? 0.1690 0.1907 0.1755 -0.0294 0.0486 -0.0180 286 TYR A O 2044 C CB . TYR A 260 ? 0.1673 0.1616 0.1635 -0.0451 0.0420 -0.0055 286 TYR A CB 2045 C CG . TYR A 260 ? 0.1593 0.1410 0.1492 -0.0430 0.0313 -0.0066 286 TYR A CG 2046 C CD1 . TYR A 260 ? 0.1443 0.1302 0.1422 -0.0401 0.0236 -0.0121 286 TYR A CD1 2047 C CD2 . TYR A 260 ? 0.1571 0.1223 0.1326 -0.0427 0.0301 -0.0014 286 TYR A CD2 2048 C CE1 . TYR A 260 ? 0.1785 0.1542 0.1712 -0.0380 0.0172 -0.0129 286 TYR A CE1 2049 C CE2 . TYR A 260 ? 0.1518 0.1086 0.1252 -0.0392 0.0219 -0.0032 286 TYR A CE2 2050 C CZ . TYR A 260 ? 0.1365 0.0996 0.1193 -0.0376 0.0167 -0.0092 286 TYR A CZ 2051 O OH . TYR A 260 ? 0.1628 0.1190 0.1444 -0.0343 0.0122 -0.0109 286 TYR A OH 2052 N N . ALA A 261 ? 0.1697 0.1909 0.1701 -0.0395 0.0675 -0.0071 287 ALA A N 2053 C CA . ALA A 261 ? 0.1701 0.2123 0.1890 -0.0368 0.0777 -0.0110 287 ALA A CA 2054 C C . ALA A 261 ? 0.2017 0.2414 0.2035 -0.0245 0.0791 -0.0176 287 ALA A C 2055 O O . ALA A 261 ? 0.2287 0.2820 0.2467 -0.0177 0.0802 -0.0243 287 ALA A O 2056 C CB . ALA A 261 ? 0.1878 0.2377 0.2134 -0.0448 0.0961 -0.0040 287 ALA A CB 2057 N N . THR A 262 ? 0.2270 0.2485 0.1963 -0.0208 0.0777 -0.0166 288 THR A N 2058 C CA . THR A 262 ? 0.2958 0.3114 0.2455 -0.0102 0.0772 -0.0250 288 THR A CA 2059 C C . THR A 262 ? 0.2406 0.2547 0.2022 -0.0059 0.0634 -0.0334 288 THR A C 2060 O O . THR A 262 ? 0.1932 0.2094 0.1573 0.0021 0.0654 -0.0416 288 THR A O 2061 C CB . THR A 262 ? 0.3135 0.3100 0.2255 -0.0074 0.0737 -0.0231 288 THR A CB 2062 O OG1 . THR A 262 ? 0.2958 0.2900 0.1899 -0.0089 0.0899 -0.0145 288 THR A OG1 2063 C CG2 . THR A 262 ? 0.2904 0.2790 0.1834 0.0023 0.0678 -0.0351 288 THR A CG2 2064 N N . VAL A 263 ? 0.1717 0.1800 0.1393 -0.0108 0.0512 -0.0309 289 VAL A N 2065 C CA . VAL A 263 ? 0.1583 0.1628 0.1360 -0.0083 0.0406 -0.0360 289 VAL A CA 2066 C C . VAL A 263 ? 0.1883 0.2055 0.1897 -0.0056 0.0422 -0.0371 289 VAL A C 2067 O O . VAL A 263 ? 0.1882 0.2018 0.1930 0.0015 0.0398 -0.0427 289 VAL A O 2068 C CB . VAL A 263 ? 0.1930 0.1901 0.1721 -0.0141 0.0306 -0.0321 289 VAL A CB 2069 C CG1 . VAL A 263 ? 0.1767 0.1693 0.1657 -0.0124 0.0235 -0.0353 289 VAL A CG1 2070 C CG2 . VAL A 263 ? 0.1612 0.1480 0.1208 -0.0142 0.0262 -0.0319 289 VAL A CG2 2071 N N . VAL A 264 ? 0.1818 0.2130 0.2001 -0.0109 0.0451 -0.0321 290 VAL A N 2072 C CA . VAL A 264 ? 0.1597 0.2075 0.2033 -0.0074 0.0440 -0.0337 290 VAL A CA 2073 C C . VAL A 264 ? 0.1440 0.2019 0.1942 0.0026 0.0536 -0.0393 290 VAL A C 2074 O O . VAL A 264 ? 0.2016 0.2622 0.2630 0.0120 0.0493 -0.0431 290 VAL A O 2075 C CB . VAL A 264 ? 0.2221 0.2863 0.2862 -0.0166 0.0454 -0.0296 290 VAL A CB 2076 C CG1 . VAL A 264 ? 0.1232 0.2111 0.2179 -0.0115 0.0438 -0.0329 290 VAL A CG1 2077 C CG2 . VAL A 264 ? 0.2764 0.3291 0.3350 -0.0242 0.0347 -0.0264 290 VAL A CG2 2078 N N . ASN A 265 ? 0.1579 0.2191 0.1986 0.0020 0.0673 -0.0393 291 ASN A N 2079 C CA . ASN A 265 ? 0.2474 0.3187 0.2925 0.0125 0.0798 -0.0453 291 ASN A CA 2080 C C . ASN A 265 ? 0.2084 0.2604 0.2353 0.0236 0.0752 -0.0541 291 ASN A C 2081 O O . ASN A 265 ? 0.1957 0.2529 0.2339 0.0351 0.0788 -0.0603 291 ASN A O 2082 C CB . ASN A 265 ? 0.3072 0.3830 0.3395 0.0091 0.0980 -0.0423 291 ASN A CB 2083 C CG . ASN A 265 ? 0.3941 0.4915 0.4533 -0.0023 0.1068 -0.0344 291 ASN A CG 2084 O OD1 . ASN A 265 ? 0.3884 0.5058 0.4826 -0.0041 0.1012 -0.0350 291 ASN A OD1 2085 N ND2 . ASN A 265 ? 0.3599 0.4516 0.4019 -0.0101 0.1197 -0.0271 291 ASN A ND2 2086 N N . ALA A 266 ? 0.1880 0.2177 0.1895 0.0201 0.0667 -0.0551 292 ALA A N 2087 C CA . ALA A 266 ? 0.2809 0.2901 0.2680 0.0270 0.0604 -0.0643 292 ALA A CA 2088 C C . ALA A 266 ? 0.1910 0.1957 0.1962 0.0313 0.0516 -0.0645 292 ALA A C 2089 O O . ALA A 266 ? 0.3342 0.3265 0.3377 0.0409 0.0515 -0.0719 292 ALA A O 2090 C CB . ALA A 266 ? 0.2044 0.1961 0.1684 0.0201 0.0512 -0.0652 292 ALA A CB 2091 N N . CYS A 267 ? 0.1711 0.1827 0.1903 0.0250 0.0443 -0.0562 293 CYS A N 2092 C CA A CYS A 267 ? 0.2238 0.2309 0.2556 0.0302 0.0361 -0.0539 293 CYS A CA 2093 C CA B CYS A 267 ? 0.2425 0.2505 0.2749 0.0300 0.0362 -0.0537 293 CYS A CA 2094 C C . CYS A 267 ? 0.1979 0.2227 0.2513 0.0421 0.0397 -0.0554 293 CYS A C 2095 O O . CYS A 267 ? 0.2264 0.2403 0.2822 0.0539 0.0376 -0.0586 293 CYS A O 2096 C CB A CYS A 267 ? 0.2610 0.2700 0.2963 0.0212 0.0276 -0.0456 293 CYS A CB 2097 C CB B CYS A 267 ? 0.2744 0.2868 0.3117 0.0210 0.0282 -0.0454 293 CYS A CB 2098 S SG A CYS A 267 ? 0.2942 0.2975 0.3376 0.0285 0.0171 -0.0406 293 CYS A SG 2099 S SG B CYS A 267 ? 0.2924 0.2846 0.3114 0.0108 0.0229 -0.0432 293 CYS A SG 2100 N N . LYS A 268 ? 0.1622 0.2141 0.2337 0.0392 0.0452 -0.0532 294 LYS A N 2101 C CA . LYS A 268 ? 0.1649 0.2409 0.2648 0.0502 0.0485 -0.0553 294 LYS A CA 2102 C C . LYS A 268 ? 0.2564 0.3286 0.3540 0.0644 0.0594 -0.0638 294 LYS A C 2103 O O . LYS A 268 ? 0.2735 0.3545 0.3905 0.0789 0.0583 -0.0665 294 LYS A O 2104 C CB . LYS A 268 ? 0.2823 0.3896 0.4058 0.0414 0.0556 -0.0526 294 LYS A CB 2105 C CG . LYS A 268 ? 0.3452 0.4564 0.4746 0.0290 0.0434 -0.0464 294 LYS A CG 2106 C CD . LYS A 268 ? 0.3557 0.4984 0.5162 0.0204 0.0487 -0.0453 294 LYS A CD 2107 C CE . LYS A 268 ? 0.3567 0.5295 0.5547 0.0323 0.0472 -0.0495 294 LYS A CE 2108 N NZ . LYS A 268 ? 0.4296 0.6366 0.6651 0.0212 0.0519 -0.0493 294 LYS A NZ 2109 N N . ALA A 269 ? 0.1979 0.2560 0.2703 0.0618 0.0691 -0.0688 295 ALA A N 2110 C CA . ALA A 269 ? 0.2986 0.3489 0.3623 0.0755 0.0801 -0.0792 295 ALA A CA 2111 C C . ALA A 269 ? 0.2692 0.2941 0.3292 0.0875 0.0711 -0.0841 295 ALA A C 2112 O O . ALA A 269 ? 0.2968 0.3181 0.3596 0.1028 0.0784 -0.0925 295 ALA A O 2113 C CB . ALA A 269 ? 0.2616 0.2964 0.2908 0.0701 0.0881 -0.0843 295 ALA A CB 2114 N N . GLN A 270 ? 0.2290 0.2349 0.2826 0.0811 0.0568 -0.0783 296 GLN A N 2115 C CA . GLN A 270 ? 0.2653 0.2416 0.3133 0.0904 0.0496 -0.0805 296 GLN A CA 2116 C C . GLN A 270 ? 0.2991 0.2838 0.3693 0.1035 0.0426 -0.0742 296 GLN A C 2117 O O . GLN A 270 ? 0.3595 0.3172 0.4242 0.1131 0.0370 -0.0734 296 GLN A O 2118 C CB . GLN A 270 ? 0.2437 0.1936 0.2737 0.0769 0.0403 -0.0766 296 GLN A CB 2119 C CG . GLN A 270 ? 0.2397 0.1867 0.2514 0.0633 0.0423 -0.0810 296 GLN A CG 2120 C CD . GLN A 270 ? 0.2637 0.2044 0.2606 0.0699 0.0511 -0.0945 296 GLN A CD 2121 O OE1 . GLN A 270 ? 0.3685 0.2898 0.3619 0.0811 0.0531 -0.1035 296 GLN A OE1 2122 N NE2 . GLN A 270 ? 0.2702 0.2245 0.2551 0.0639 0.0570 -0.0959 296 GLN A NE2 2123 N N . GLY A 271 ? 0.2474 0.2679 0.3424 0.1040 0.0421 -0.0696 297 GLY A N 2124 C CA . GLY A 271 ? 0.2320 0.2655 0.3499 0.1176 0.0323 -0.0648 297 GLY A CA 2125 C C . GLY A 271 ? 0.2637 0.2723 0.3666 0.1160 0.0172 -0.0550 297 GLY A C 2126 O O . GLY A 271 ? 0.2337 0.2347 0.3217 0.0999 0.0133 -0.0497 297 GLY A O 2127 N N . ALA A 272 ? 0.2585 0.2522 0.3633 0.1339 0.0098 -0.0521 298 ALA A N 2128 C CA . ALA A 272 ? 0.3477 0.3176 0.4356 0.1347 -0.0034 -0.0407 298 ALA A CA 2129 C C . ALA A 272 ? 0.4034 0.3335 0.4612 0.1214 0.0005 -0.0379 298 ALA A C 2130 O O . ALA A 272 ? 0.3477 0.2603 0.3889 0.1164 -0.0062 -0.0277 298 ALA A O 2131 C CB . ALA A 272 ? 0.3139 0.2723 0.4070 0.1590 -0.0115 -0.0370 298 ALA A CB 2132 N N . ALA A 273 ? 0.2801 0.1972 0.3313 0.1156 0.0113 -0.0473 299 ALA A N 2133 C CA . ALA A 273 ? 0.2892 0.1717 0.3188 0.1025 0.0139 -0.0468 299 ALA A CA 2134 C C . ALA A 273 ? 0.2622 0.1558 0.2858 0.0821 0.0133 -0.0434 299 ALA A C 2135 O O . ALA A 273 ? 0.3064 0.1771 0.3171 0.0710 0.0137 -0.0397 299 ALA A O 2136 C CB . ALA A 273 ? 0.3059 0.1710 0.3304 0.1034 0.0224 -0.0603 299 ALA A CB 2137 N N . CYS A 274 ? 0.2362 0.1640 0.2709 0.0769 0.0132 -0.0446 300 CYS A N 2138 C CA . CYS A 274 ? 0.2141 0.1502 0.2430 0.0601 0.0118 -0.0406 300 CYS A CA 2139 C C . CYS A 274 ? 0.2123 0.1599 0.2439 0.0611 0.0029 -0.0313 300 CYS A C 2140 O O . CYS A 274 ? 0.2419 0.2162 0.2902 0.0666 -0.0010 -0.0319 300 CYS A O 2141 C CB . CYS A 274 ? 0.1958 0.1554 0.2301 0.0520 0.0177 -0.0469 300 CYS A CB 2142 S SG . CYS A 274 ? 0.3263 0.2919 0.3532 0.0339 0.0154 -0.0418 300 CYS A SG 2143 N N . VAL A 275 ? 0.2135 0.1414 0.2291 0.0558 0.0000 -0.0234 301 VAL A N 2144 C CA . VAL A 275 ? 0.2195 0.1502 0.2296 0.0611 -0.0097 -0.0149 301 VAL A CA 2145 C C . VAL A 275 ? 0.2002 0.1487 0.2097 0.0499 -0.0132 -0.0141 301 VAL A C 2146 O O . VAL A 275 ? 0.2055 0.1616 0.2121 0.0544 -0.0234 -0.0105 301 VAL A O 2147 C CB . VAL A 275 ? 0.2530 0.1488 0.2405 0.0643 -0.0095 -0.0051 301 VAL A CB 2148 C CG1 . VAL A 275 ? 0.2734 0.1459 0.2606 0.0769 -0.0070 -0.0052 301 VAL A CG1 2149 C CG2 . VAL A 275 ? 0.2413 0.1231 0.2186 0.0482 -0.0007 -0.0038 301 VAL A CG2 2150 N N . GLY A 276 ? 0.1818 0.1353 0.1926 0.0365 -0.0063 -0.0180 302 GLY A N 2151 C CA . GLY A 276 ? 0.1958 0.1607 0.2045 0.0266 -0.0089 -0.0172 302 GLY A CA 2152 C C . GLY A 276 ? 0.1845 0.1497 0.1921 0.0141 -0.0015 -0.0200 302 GLY A C 2153 O O . GLY A 276 ? 0.1694 0.1251 0.1759 0.0118 0.0044 -0.0227 302 GLY A O 2154 N N . ILE A 277 ? 0.1421 0.1173 0.1499 0.0067 -0.0035 -0.0200 303 ILE A N 2155 C CA . ILE A 277 ? 0.1308 0.1066 0.1371 -0.0030 0.0015 -0.0216 303 ILE A CA 2156 C C . ILE A 277 ? 0.1806 0.1492 0.1760 -0.0073 -0.0002 -0.0186 303 ILE A C 2157 O O . ILE A 277 ? 0.1923 0.1643 0.1845 -0.0059 -0.0066 -0.0181 303 ILE A O 2158 C CB . ILE A 277 ? 0.1679 0.1617 0.1858 -0.0072 0.0033 -0.0247 303 ILE A CB 2159 C CG1 . ILE A 277 ? 0.2251 0.2261 0.2513 -0.0017 0.0080 -0.0285 303 ILE A CG1 2160 C CG2 . ILE A 277 ? 0.1336 0.1241 0.1458 -0.0151 0.0068 -0.0245 303 ILE A CG2 2161 C CD1 . ILE A 277 ? 0.2167 0.2379 0.2563 -0.0047 0.0126 -0.0301 303 ILE A CD1 2162 N N . THR A 278 ? 0.1508 0.1102 0.1413 -0.0117 0.0051 -0.0177 304 THR A N 2163 C CA . THR A 278 ? 0.1727 0.1254 0.1537 -0.0146 0.0066 -0.0157 304 THR A CA 2164 C C . THR A 278 ? 0.1853 0.1431 0.1722 -0.0201 0.0090 -0.0181 304 THR A C 2165 O O . THR A 278 ? 0.1537 0.1135 0.1475 -0.0216 0.0112 -0.0197 304 THR A O 2166 C CB . THR A 278 ? 0.1474 0.0850 0.1200 -0.0134 0.0130 -0.0114 304 THR A CB 2167 O OG1 . THR A 278 ? 0.1925 0.1205 0.1532 -0.0066 0.0103 -0.0071 304 THR A OG1 2168 C CG2 . THR A 278 ? 0.1522 0.0850 0.1168 -0.0158 0.0184 -0.0102 304 THR A CG2 2169 N N . THR A 279 ? 0.1293 0.0876 0.1123 -0.0222 0.0074 -0.0187 305 THR A N 2170 C CA . THR A 279 ? 0.1473 0.1061 0.1335 -0.0251 0.0095 -0.0195 305 THR A CA 2171 C C . THR A 279 ? 0.1406 0.0922 0.1231 -0.0236 0.0146 -0.0188 305 THR A C 2172 O O . THR A 279 ? 0.1559 0.0999 0.1274 -0.0215 0.0167 -0.0180 305 THR A O 2173 C CB . THR A 279 ? 0.1215 0.0809 0.1068 -0.0285 0.0065 -0.0205 305 THR A CB 2174 O OG1 . THR A 279 ? 0.1899 0.1435 0.1670 -0.0285 0.0031 -0.0226 305 THR A OG1 2175 C CG2 . THR A 279 ? 0.1609 0.1305 0.1543 -0.0309 0.0053 -0.0205 305 THR A CG2 2176 N N . TRP A 280 ? 0.1271 0.0821 0.1186 -0.0237 0.0167 -0.0194 306 TRP A N 2177 C CA . TRP A 280 ? 0.1482 0.1014 0.1433 -0.0220 0.0235 -0.0192 306 TRP A CA 2178 C C . TRP A 280 ? 0.2412 0.1878 0.2284 -0.0190 0.0251 -0.0204 306 TRP A C 2179 O O . TRP A 280 ? 0.1342 0.0832 0.1295 -0.0162 0.0257 -0.0214 306 TRP A O 2180 C CB . TRP A 280 ? 0.1188 0.0823 0.1326 -0.0228 0.0234 -0.0206 306 TRP A CB 2181 C CG . TRP A 280 ? 0.1238 0.0893 0.1485 -0.0233 0.0329 -0.0201 306 TRP A CG 2182 C CD1 . TRP A 280 ? 0.2171 0.1906 0.2566 -0.0207 0.0374 -0.0215 306 TRP A CD1 2183 C CD2 . TRP A 280 ? 0.1567 0.1153 0.1785 -0.0261 0.0412 -0.0171 306 TRP A CD2 2184 N NE1 . TRP A 280 ? 0.2203 0.1952 0.2693 -0.0232 0.0497 -0.0199 306 TRP A NE1 2185 C CE2 . TRP A 280 ? 0.1578 0.1211 0.1937 -0.0269 0.0525 -0.0164 306 TRP A CE2 2186 C CE3 . TRP A 280 ? 0.1780 0.1261 0.1869 -0.0270 0.0406 -0.0141 306 TRP A CE3 2187 C CZ2 . TRP A 280 ? 0.2209 0.1767 0.2565 -0.0304 0.0652 -0.0118 306 TRP A CZ2 2188 C CZ3 . TRP A 280 ? 0.2197 0.1578 0.2258 -0.0288 0.0509 -0.0093 306 TRP A CZ3 2189 C CH2 . TRP A 280 ? 0.2197 0.1606 0.2379 -0.0313 0.0639 -0.0076 306 TRP A CH2 2190 N N . GLY A 281 ? 0.1756 0.1126 0.1460 -0.0186 0.0244 -0.0212 307 GLY A N 2191 C CA . GLY A 281 ? 0.2188 0.1450 0.1774 -0.0161 0.0248 -0.0247 307 GLY A CA 2192 C C . GLY A 281 ? 0.2746 0.1961 0.2251 -0.0200 0.0156 -0.0273 307 GLY A C 2193 O O . GLY A 281 ? 0.2248 0.1548 0.1817 -0.0237 0.0102 -0.0258 307 GLY A O 2194 N N . ILE A 282 ? 0.2104 0.1190 0.1490 -0.0193 0.0140 -0.0324 308 ILE A N 2195 C CA . ILE A 282 ? 0.1881 0.0928 0.1240 -0.0252 0.0046 -0.0366 308 ILE A CA 2196 C C . ILE A 282 ? 0.1950 0.0918 0.1383 -0.0286 0.0046 -0.0371 308 ILE A C 2197 O O . ILE A 282 ? 0.2135 0.1165 0.1686 -0.0350 0.0021 -0.0340 308 ILE A O 2198 C CB . ILE A 282 ? 0.2128 0.1053 0.1270 -0.0232 -0.0002 -0.0439 308 ILE A CB 2199 C CG1 . ILE A 282 ? 0.2147 0.1133 0.1186 -0.0193 -0.0021 -0.0409 308 ILE A CG1 2200 C CG2 . ILE A 282 ? 0.2684 0.1564 0.1850 -0.0313 -0.0113 -0.0510 308 ILE A CG2 2201 C CD1 . ILE A 282 ? 0.2454 0.1306 0.1203 -0.0146 -0.0075 -0.0468 308 ILE A CD1 2202 N N . THR A 283 ? 0.2187 0.1005 0.1541 -0.0232 0.0092 -0.0401 309 THR A N 2203 C CA . THR A 283 ? 0.2161 0.0839 0.1550 -0.0242 0.0094 -0.0397 309 THR A CA 2204 C C . THR A 283 ? 0.2090 0.0804 0.1568 -0.0159 0.0149 -0.0337 309 THR A C 2205 O O . THR A 283 ? 0.2455 0.1254 0.1961 -0.0084 0.0205 -0.0339 309 THR A O 2206 C CB . THR A 283 ? 0.2459 0.0895 0.1693 -0.0223 0.0088 -0.0491 309 THR A CB 2207 O OG1 . THR A 283 ? 0.3158 0.1432 0.2425 -0.0195 0.0111 -0.0470 309 THR A OG1 2208 C CG2 . THR A 283 ? 0.2564 0.0979 0.1660 -0.0118 0.0157 -0.0535 309 THR A CG2 2209 N N . ASP A 284 ? 0.2129 0.0773 0.1651 -0.0171 0.0133 -0.0284 310 ASP A N 2210 C CA . ASP A 284 ? 0.2140 0.0786 0.1722 -0.0073 0.0148 -0.0231 310 ASP A CA 2211 C C . ASP A 284 ? 0.2277 0.0845 0.1856 0.0046 0.0196 -0.0281 310 ASP A C 2212 O O . ASP A 284 ? 0.2248 0.0928 0.1947 0.0144 0.0210 -0.0259 310 ASP A O 2213 C CB . ASP A 284 ? 0.2300 0.0777 0.1840 -0.0089 0.0126 -0.0162 310 ASP A CB 2214 C CG . ASP A 284 ? 0.3563 0.2122 0.3110 -0.0195 0.0114 -0.0102 310 ASP A CG 2215 O OD1 . ASP A 284 ? 0.2260 0.1038 0.1867 -0.0213 0.0106 -0.0100 310 ASP A OD1 2216 O OD2 . ASP A 284 ? 0.3258 0.1645 0.2752 -0.0261 0.0127 -0.0057 310 ASP A OD2 2217 N N . LEU A 285 ? 0.2472 0.0856 0.1922 0.0041 0.0218 -0.0360 311 LEU A N 2218 C CA . LEU A 285 ? 0.2753 0.1020 0.2167 0.0166 0.0283 -0.0419 311 LEU A CA 2219 C C . LEU A 285 ? 0.3088 0.1582 0.2615 0.0247 0.0367 -0.0427 311 LEU A C 2220 O O . LEU A 285 ? 0.2760 0.1261 0.2376 0.0373 0.0431 -0.0445 311 LEU A O 2221 C CB . LEU A 285 ? 0.2923 0.0977 0.2144 0.0135 0.0281 -0.0521 311 LEU A CB 2222 C CG . LEU A 285 ? 0.3595 0.1525 0.2770 0.0257 0.0332 -0.0587 311 LEU A CG 2223 C CD1 . LEU A 285 ? 0.3336 0.1104 0.2585 0.0313 0.0304 -0.0544 311 LEU A CD1 2224 C CD2 . LEU A 285 ? 0.3538 0.1366 0.2536 0.0213 0.0303 -0.0689 311 LEU A CD2 2225 N N . TYR A 286 ? 0.2351 0.1023 0.1893 0.0176 0.0376 -0.0411 312 TYR A N 2226 C CA . TYR A 286 ? 0.2263 0.1126 0.1918 0.0221 0.0476 -0.0408 312 TYR A CA 2227 C C . TYR A 286 ? 0.2762 0.1870 0.2632 0.0175 0.0443 -0.0343 312 TYR A C 2228 O O . TYR A 286 ? 0.2754 0.2018 0.2743 0.0174 0.0521 -0.0335 312 TYR A O 2229 C CB . TYR A 286 ? 0.2373 0.1180 0.1815 0.0192 0.0541 -0.0445 312 TYR A CB 2230 C CG . TYR A 286 ? 0.3034 0.1583 0.2214 0.0232 0.0552 -0.0535 312 TYR A CG 2231 C CD1 . TYR A 286 ? 0.2899 0.1342 0.2076 0.0351 0.0637 -0.0590 312 TYR A CD1 2232 C CD2 . TYR A 286 ? 0.2803 0.1217 0.1752 0.0158 0.0465 -0.0578 312 TYR A CD2 2233 C CE1 . TYR A 286 ? 0.3229 0.1487 0.2197 0.0375 0.0611 -0.0666 312 TYR A CE1 2234 C CE2 . TYR A 286 ? 0.3552 0.1789 0.2307 0.0181 0.0432 -0.0663 312 TYR A CE2 2235 C CZ . TYR A 286 ? 0.4312 0.2471 0.3073 0.0283 0.0504 -0.0704 312 TYR A CZ 2236 O OH . TYR A 286 ? 0.4705 0.2701 0.3291 0.0301 0.0465 -0.0795 312 TYR A OH 2237 N N . SER A 287 ? 0.2381 0.1502 0.2287 0.0133 0.0335 -0.0299 313 SER A N 2238 C CA . SER A 287 ? 0.1689 0.1010 0.1754 0.0095 0.0288 -0.0259 313 SER A CA 2239 C C . SER A 287 ? 0.2635 0.2151 0.2961 0.0168 0.0314 -0.0266 313 SER A C 2240 O O . SER A 287 ? 0.1750 0.1250 0.2154 0.0270 0.0321 -0.0277 313 SER A O 2241 C CB . SER A 287 ? 0.1673 0.0948 0.1688 0.0068 0.0185 -0.0214 313 SER A CB 2242 O OG . SER A 287 ? 0.1920 0.1366 0.2042 0.0041 0.0133 -0.0194 313 SER A OG 2243 N N . TRP A 288 ? 0.1882 0.1581 0.2369 0.0114 0.0320 -0.0264 314 TRP A N 2244 C CA . TRP A 288 ? 0.1765 0.1692 0.2567 0.0157 0.0321 -0.0282 314 TRP A CA 2245 C C . TRP A 288 ? 0.1978 0.1972 0.2864 0.0223 0.0167 -0.0272 314 TRP A C 2246 O O . TRP A 288 ? 0.2000 0.2180 0.3154 0.0298 0.0133 -0.0296 314 TRP A O 2247 C CB . TRP A 288 ? 0.2268 0.2339 0.3222 0.0057 0.0356 -0.0289 314 TRP A CB 2248 C CG . TRP A 288 ? 0.2041 0.2103 0.2917 -0.0015 0.0237 -0.0281 314 TRP A CG 2249 C CD1 . TRP A 288 ? 0.1508 0.1412 0.2121 -0.0057 0.0206 -0.0256 314 TRP A CD1 2250 C CD2 . TRP A 288 ? 0.2694 0.2917 0.3762 -0.0045 0.0135 -0.0314 314 TRP A CD2 2251 N NE1 . TRP A 288 ? 0.1236 0.1189 0.1855 -0.0100 0.0113 -0.0266 314 TRP A NE1 2252 C CE2 . TRP A 288 ? 0.2499 0.2627 0.3369 -0.0095 0.0062 -0.0306 314 TRP A CE2 2253 C CE3 . TRP A 288 ? 0.4578 0.5030 0.5986 -0.0035 0.0093 -0.0361 314 TRP A CE3 2254 C CZ2 . TRP A 288 ? 0.3972 0.4187 0.4915 -0.0126 -0.0048 -0.0350 314 TRP A CZ2 2255 C CZ3 . TRP A 288 ? 0.5538 0.6090 0.7042 -0.0080 -0.0041 -0.0409 314 TRP A CZ3 2256 C CH2 . TRP A 288 ? 0.5414 0.5827 0.6657 -0.0121 -0.0108 -0.0406 314 TRP A CH2 2257 N N . ILE A 289 ? 0.1514 0.1360 0.2169 0.0204 0.0075 -0.0235 315 ILE A N 2258 C CA A ILE A 289 ? 0.1643 0.1533 0.2305 0.0262 -0.0071 -0.0212 315 ILE A CA 2259 C CA B ILE A 289 ? 0.1654 0.1541 0.2311 0.0262 -0.0071 -0.0212 315 ILE A CA 2260 C C . ILE A 289 ? 0.2242 0.2109 0.2968 0.0415 -0.0123 -0.0195 315 ILE A C 2261 O O . ILE A 289 ? 0.2802 0.2850 0.3718 0.0493 -0.0236 -0.0210 315 ILE A O 2262 C CB A ILE A 289 ? 0.1849 0.1567 0.2220 0.0210 -0.0116 -0.0162 315 ILE A CB 2263 C CB B ILE A 289 ? 0.1819 0.1526 0.2180 0.0211 -0.0116 -0.0159 315 ILE A CB 2264 C CG1 A ILE A 289 ? 0.2028 0.1843 0.2400 0.0107 -0.0128 -0.0190 315 ILE A CG1 2265 C CG1 B ILE A 289 ? 0.1611 0.1363 0.1931 0.0090 -0.0087 -0.0181 315 ILE A CG1 2266 C CG2 A ILE A 289 ? 0.1781 0.1429 0.2036 0.0305 -0.0234 -0.0109 315 ILE A CG2 2267 C CG2 B ILE A 289 ? 0.1838 0.1539 0.2118 0.0291 -0.0251 -0.0121 315 ILE A CG2 2268 C CD1 A ILE A 289 ? 0.1424 0.1107 0.1603 0.0022 -0.0067 -0.0167 315 ILE A CD1 2269 C CD1 B ILE A 289 ? 0.1376 0.1320 0.1859 0.0067 -0.0157 -0.0231 315 ILE A CD1 2270 N N . PRO A 290 ? 0.1856 0.1497 0.2436 0.0467 -0.0057 -0.0171 316 PRO A N 2271 C CA . PRO A 290 ? 0.3305 0.2897 0.3938 0.0633 -0.0123 -0.0147 316 PRO A CA 2272 C C . PRO A 290 ? 0.3860 0.3710 0.4859 0.0741 -0.0102 -0.0205 316 PRO A C 2273 O O . PRO A 290 ? 0.4055 0.3934 0.5161 0.0900 -0.0188 -0.0190 316 PRO A O 2274 C CB . PRO A 290 ? 0.3325 0.2579 0.3724 0.0651 -0.0046 -0.0124 316 PRO A CB 2275 C CG . PRO A 290 ? 0.2405 0.1620 0.2722 0.0515 0.0069 -0.0169 316 PRO A CG 2276 C CD . PRO A 290 ? 0.1978 0.1377 0.2328 0.0394 0.0037 -0.0167 316 PRO A CD 2277 N N . SER A 291 ? 0.2789 0.2827 0.3985 0.0662 0.0016 -0.0264 317 SER A N 2278 C CA . SER A 291 ? 0.3646 0.3968 0.5242 0.0746 0.0070 -0.0319 317 SER A CA 2279 C C . SER A 291 ? 0.3975 0.4629 0.5886 0.0695 -0.0044 -0.0351 317 SER A C 2280 O O . SER A 291 ? 0.4231 0.5179 0.6546 0.0773 -0.0065 -0.0396 317 SER A O 2281 C CB . SER A 291 ? 0.3476 0.3802 0.5108 0.0693 0.0292 -0.0359 317 SER A CB 2282 O OG . SER A 291 ? 0.4904 0.5356 0.6600 0.0533 0.0342 -0.0366 317 SER A OG 2283 N N . THR A 292 ? 0.3354 0.3965 0.5098 0.0566 -0.0121 -0.0338 318 THR A N 2284 C CA . THR A 292 ? 0.3834 0.4705 0.5823 0.0504 -0.0245 -0.0387 318 THR A CA 2285 C C . THR A 292 ? 0.3935 0.4788 0.5792 0.0596 -0.0482 -0.0368 318 THR A C 2286 O O . THR A 292 ? 0.4301 0.5414 0.6440 0.0649 -0.0638 -0.0422 318 THR A O 2287 C CB . THR A 292 ? 0.3894 0.4715 0.5776 0.0320 -0.0180 -0.0399 318 THR A CB 2288 O OG1 . THR A 292 ? 0.4800 0.5613 0.6761 0.0253 0.0035 -0.0400 318 THR A OG1 2289 C CG2 . THR A 292 ? 0.2421 0.3473 0.4557 0.0244 -0.0308 -0.0470 318 THR A CG2 2290 N N . TYR A 293 ? 0.2366 0.2912 0.3793 0.0618 -0.0506 -0.0290 319 TYR A N 2291 C CA . TYR A 293 ? 0.2525 0.2979 0.3726 0.0722 -0.0697 -0.0242 319 TYR A CA 2292 C C . TYR A 293 ? 0.2899 0.3091 0.3891 0.0863 -0.0681 -0.0151 319 TYR A C 2293 O O . TYR A 293 ? 0.3876 0.3765 0.4528 0.0813 -0.0601 -0.0081 319 TYR A O 2294 C CB . TYR A 293 ? 0.3085 0.3381 0.3933 0.0615 -0.0726 -0.0217 319 TYR A CB 2295 C CG . TYR A 293 ? 0.3906 0.4374 0.4898 0.0469 -0.0723 -0.0307 319 TYR A CG 2296 C CD1 . TYR A 293 ? 0.4528 0.5224 0.5710 0.0476 -0.0896 -0.0393 319 TYR A CD1 2297 C CD2 . TYR A 293 ? 0.3644 0.4026 0.4573 0.0329 -0.0562 -0.0310 319 TYR A CD2 2298 C CE1 . TYR A 293 ? 0.4835 0.5641 0.6146 0.0335 -0.0891 -0.0483 319 TYR A CE1 2299 C CE2 . TYR A 293 ? 0.3930 0.4420 0.4975 0.0207 -0.0555 -0.0383 319 TYR A CE2 2300 C CZ . TYR A 293 ? 0.4292 0.4979 0.5528 0.0204 -0.0712 -0.0471 319 TYR A CZ 2301 O OH . TYR A 293 ? 0.5424 0.6175 0.6776 0.0076 -0.0703 -0.0552 319 TYR A OH 2302 N N . PRO A 294 ? 0.3828 0.4133 0.5045 0.1038 -0.0758 -0.0156 320 PRO A N 2303 C CA . PRO A 294 ? 0.4039 0.4057 0.5072 0.1192 -0.0739 -0.0073 320 PRO A CA 2304 C C . PRO A 294 ? 0.3874 0.3551 0.4429 0.1214 -0.0820 0.0047 320 PRO A C 2305 O O . PRO A 294 ? 0.4000 0.3740 0.4427 0.1235 -0.0980 0.0065 320 PRO A O 2306 C CB . PRO A 294 ? 0.4314 0.4585 0.5710 0.1400 -0.0866 -0.0106 320 PRO A CB 2307 C CG . PRO A 294 ? 0.4478 0.5130 0.6143 0.1352 -0.1025 -0.0187 320 PRO A CG 2308 C CD . PRO A 294 ? 0.4582 0.5286 0.6250 0.1110 -0.0886 -0.0241 320 PRO A CD 2309 N N . GLY A 295 ? 0.3498 0.2805 0.3783 0.1201 -0.0700 0.0122 321 GLY A N 2310 C CA . GLY A 295 ? 0.3727 0.2688 0.3576 0.1202 -0.0729 0.0250 321 GLY A CA 2311 C C . GLY A 295 ? 0.3774 0.2683 0.3405 0.0997 -0.0651 0.0261 321 GLY A C 2312 O O . GLY A 295 ? 0.4209 0.2865 0.3491 0.0979 -0.0648 0.0368 321 GLY A O 2313 N N . GLU A 296 ? 0.2833 0.1973 0.2669 0.0853 -0.0575 0.0158 322 GLU A N 2314 C CA . GLU A 296 ? 0.3308 0.2419 0.2988 0.0673 -0.0493 0.0155 322 GLU A CA 2315 C C . GLU A 296 ? 0.3578 0.2648 0.3345 0.0547 -0.0334 0.0106 322 GLU A C 2316 O O . GLU A 296 ? 0.2469 0.1618 0.2449 0.0581 -0.0288 0.0045 322 GLU A O 2317 C CB . GLU A 296 ? 0.2501 0.1897 0.2293 0.0621 -0.0575 0.0077 322 GLU A CB 2318 C CG . GLU A 296 ? 0.3368 0.2807 0.3020 0.0735 -0.0758 0.0102 322 GLU A CG 2319 C CD . GLU A 296 ? 0.3897 0.3590 0.3657 0.0669 -0.0846 -0.0004 322 GLU A CD 2320 O OE1 . GLU A 296 ? 0.4144 0.3904 0.3992 0.0524 -0.0739 -0.0063 322 GLU A OE1 2321 O OE2 . GLU A 296 ? 0.4463 0.4273 0.4213 0.0767 -0.1034 -0.0034 322 GLU A OE2 2322 N N . GLY A 297 ? 0.2452 0.1403 0.2050 0.0411 -0.0252 0.0132 323 GLY A N 2323 C CA . GLY A 297 ? 0.2306 0.1216 0.1958 0.0299 -0.0137 0.0082 323 GLY A CA 2324 C C . GLY A 297 ? 0.2694 0.1481 0.2176 0.0167 -0.0074 0.0124 323 GLY A C 2325 O O . GLY A 297 ? 0.2546 0.1381 0.1919 0.0138 -0.0093 0.0163 323 GLY A O 2326 N N . TYR A 298 ? 0.2368 0.1006 0.1839 0.0092 -0.0001 0.0106 324 TYR A N 2327 C CA . TYR A 298 ? 0.3176 0.1726 0.2568 -0.0046 0.0060 0.0131 324 TYR A CA 2328 C C . TYR A 298 ? 0.2325 0.1109 0.1768 -0.0119 0.0067 0.0102 324 TYR A C 2329 O O . TYR A 298 ? 0.2366 0.1145 0.1734 -0.0185 0.0107 0.0151 324 TYR A O 2330 C CB . TYR A 298 ? 0.2923 0.1233 0.2131 -0.0045 0.0084 0.0250 324 TYR A CB 2331 C CG . TYR A 298 ? 0.3064 0.1214 0.2256 -0.0195 0.0170 0.0269 324 TYR A CG 2332 C CD1 . TYR A 298 ? 0.3656 0.1606 0.2888 -0.0235 0.0185 0.0220 324 TYR A CD1 2333 C CD2 . TYR A 298 ? 0.3188 0.1395 0.2346 -0.0299 0.0238 0.0322 324 TYR A CD2 2334 C CE1 . TYR A 298 ? 0.4417 0.2247 0.3685 -0.0391 0.0243 0.0218 324 TYR A CE1 2335 C CE2 . TYR A 298 ? 0.4873 0.2982 0.4093 -0.0452 0.0320 0.0332 324 TYR A CE2 2336 C CZ . TYR A 298 ? 0.5853 0.3798 0.5150 -0.0500 0.0308 0.0276 324 TYR A CZ 2337 O OH . TYR A 298 ? 0.7533 0.5512 0.6984 -0.0635 0.0345 0.0261 324 TYR A OH 2338 N N . ALA A 299 ? 0.1940 0.0917 0.1513 -0.0102 0.0045 0.0027 325 ALA A N 2339 C CA . ALA A 299 ? 0.1765 0.0934 0.1378 -0.0137 0.0037 0.0002 325 ALA A CA 2340 C C . ALA A 299 ? 0.1749 0.0991 0.1427 -0.0228 0.0077 -0.0043 325 ALA A C 2341 O O . ALA A 299 ? 0.1824 0.1189 0.1524 -0.0254 0.0083 -0.0057 325 ALA A O 2342 C CB . ALA A 299 ? 0.1652 0.0975 0.1378 -0.0070 -0.0017 -0.0044 325 ALA A CB 2343 N N . LEU A 300 ? 0.2050 0.1210 0.1746 -0.0261 0.0093 -0.0075 326 LEU A N 2344 C CA . LEU A 300 ? 0.1552 0.0788 0.1298 -0.0321 0.0097 -0.0124 326 LEU A CA 2345 C C . LEU A 300 ? 0.1949 0.1149 0.1713 -0.0417 0.0109 -0.0117 326 LEU A C 2346 O O . LEU A 300 ? 0.2694 0.1817 0.2428 -0.0448 0.0143 -0.0059 326 LEU A O 2347 C CB . LEU A 300 ? 0.1577 0.0758 0.1305 -0.0289 0.0095 -0.0179 326 LEU A CB 2348 C CG . LEU A 300 ? 0.1715 0.0988 0.1490 -0.0220 0.0112 -0.0188 326 LEU A CG 2349 C CD1 . LEU A 300 ? 0.1573 0.0772 0.1305 -0.0175 0.0152 -0.0230 326 LEU A CD1 2350 C CD2 . LEU A 300 ? 0.1883 0.1290 0.1703 -0.0244 0.0109 -0.0190 326 LEU A CD2 2351 N N . LEU A 301 ? 0.1874 0.1134 0.1695 -0.0465 0.0081 -0.0171 327 LEU A N 2352 C CA . LEU A 301 ? 0.1773 0.1066 0.1693 -0.0568 0.0084 -0.0177 327 LEU A CA 2353 C C . LEU A 301 ? 0.2306 0.1422 0.2215 -0.0635 0.0057 -0.0220 327 LEU A C 2354 O O . LEU A 301 ? 0.2049 0.1168 0.2077 -0.0746 0.0066 -0.0224 327 LEU A O 2355 C CB . LEU A 301 ? 0.1530 0.1026 0.1564 -0.0579 0.0043 -0.0219 327 LEU A CB 2356 C CG . LEU A 301 ? 0.1394 0.1042 0.1466 -0.0534 0.0085 -0.0183 327 LEU A CG 2357 C CD1 . LEU A 301 ? 0.2733 0.2553 0.2921 -0.0520 0.0038 -0.0224 327 LEU A CD1 2358 C CD2 . LEU A 301 ? 0.1459 0.1124 0.1564 -0.0583 0.0174 -0.0123 327 LEU A CD2 2359 N N . PHE A 302 ? 0.2130 0.1092 0.1914 -0.0572 0.0033 -0.0259 328 PHE A N 2360 C CA . PHE A 302 ? 0.2255 0.1019 0.1996 -0.0607 0.0002 -0.0319 328 PHE A CA 2361 C C . PHE A 302 ? 0.2950 0.1497 0.2573 -0.0525 0.0045 -0.0290 328 PHE A C 2362 O O . PHE A 302 ? 0.2281 0.0859 0.1846 -0.0421 0.0068 -0.0276 328 PHE A O 2363 C CB . PHE A 302 ? 0.2210 0.0992 0.1883 -0.0584 -0.0078 -0.0425 328 PHE A CB 2364 C CG . PHE A 302 ? 0.2993 0.1978 0.2778 -0.0646 -0.0150 -0.0461 328 PHE A CG 2365 C CD1 . PHE A 302 ? 0.1932 0.1092 0.1717 -0.0588 -0.0151 -0.0432 328 PHE A CD1 2366 C CD2 . PHE A 302 ? 0.2898 0.1935 0.2841 -0.0734 -0.0223 -0.0513 328 PHE A CD2 2367 C CE1 . PHE A 302 ? 0.2745 0.2101 0.2649 -0.0612 -0.0226 -0.0458 328 PHE A CE1 2368 C CE2 . PHE A 302 ? 0.2654 0.1908 0.2741 -0.0779 -0.0306 -0.0552 328 PHE A CE2 2369 C CZ . PHE A 302 ? 0.2398 0.1808 0.2454 -0.0717 -0.0309 -0.0526 328 PHE A CZ 2370 N N . ASP A 303 ? 0.2672 0.1045 0.2304 -0.0550 0.0051 -0.0277 329 ASP A N 2371 C CA . ASP A 303 ? 0.2675 0.0838 0.2203 -0.0449 0.0087 -0.0240 329 ASP A CA 2372 C C . ASP A 303 ? 0.2803 0.0856 0.2246 -0.0361 0.0070 -0.0337 329 ASP A C 2373 O O . ASP A 303 ? 0.3558 0.1693 0.2972 -0.0369 0.0035 -0.0427 329 ASP A O 2374 C CB . ASP A 303 ? 0.3390 0.1371 0.2934 -0.0493 0.0116 -0.0160 329 ASP A CB 2375 C CG . ASP A 303 ? 0.4792 0.2689 0.4424 -0.0589 0.0081 -0.0227 329 ASP A CG 2376 O OD1 . ASP A 303 ? 0.4697 0.2599 0.4320 -0.0580 0.0024 -0.0349 329 ASP A OD1 2377 O OD2 . ASP A 303 ? 0.4166 0.1975 0.3866 -0.0673 0.0112 -0.0157 329 ASP A OD2 2378 N N . ASP A 304 ? 0.3132 0.0994 0.2520 -0.0263 0.0099 -0.0316 330 ASP A N 2379 C CA . ASP A 304 ? 0.3756 0.1511 0.3069 -0.0157 0.0109 -0.0407 330 ASP A CA 2380 C C . ASP A 304 ? 0.3957 0.1632 0.3241 -0.0224 0.0062 -0.0520 330 ASP A C 2381 O O . ASP A 304 ? 0.3748 0.1375 0.2931 -0.0150 0.0071 -0.0615 330 ASP A O 2382 C CB . ASP A 304 ? 0.3947 0.1509 0.3245 -0.0035 0.0140 -0.0359 330 ASP A CB 2383 C CG . ASP A 304 ? 0.4652 0.2299 0.3978 0.0087 0.0168 -0.0283 330 ASP A CG 2384 O OD1 . ASP A 304 ? 0.4304 0.2157 0.3665 0.0074 0.0176 -0.0281 330 ASP A OD1 2385 O OD2 . ASP A 304 ? 0.4807 0.2324 0.4138 0.0205 0.0169 -0.0227 330 ASP A OD2 2386 N N . ASN A 305 ? 0.3455 0.1118 0.2833 -0.0360 0.0018 -0.0514 331 ASN A N 2387 C CA . ASN A 305 ? 0.3587 0.1190 0.2978 -0.0433 -0.0048 -0.0638 331 ASN A CA 2388 C C . ASN A 305 ? 0.3562 0.1393 0.3023 -0.0528 -0.0119 -0.0686 331 ASN A C 2389 O O . ASN A 305 ? 0.3573 0.1396 0.3101 -0.0611 -0.0193 -0.0787 331 ASN A O 2390 C CB . ASN A 305 ? 0.4900 0.2308 0.4400 -0.0520 -0.0056 -0.0621 331 ASN A CB 2391 C CG . ASN A 305 ? 0.5190 0.2355 0.4621 -0.0418 0.0005 -0.0555 331 ASN A CG 2392 O OD1 . ASN A 305 ? 0.5864 0.2952 0.5338 -0.0440 0.0043 -0.0425 331 ASN A OD1 2393 N ND2 . ASN A 305 ? 0.4611 0.1654 0.3923 -0.0293 0.0019 -0.0639 331 ASN A ND2 2394 N N . TYR A 306 ? 0.3132 0.1161 0.2592 -0.0511 -0.0101 -0.0621 332 TYR A N 2395 C CA . TYR A 306 ? 0.3222 0.1477 0.2755 -0.0580 -0.0168 -0.0649 332 TYR A CA 2396 C C . TYR A 306 ? 0.3452 0.1798 0.3228 -0.0719 -0.0202 -0.0624 332 TYR A C 2397 O O . TYR A 306 ? 0.2910 0.1434 0.2805 -0.0783 -0.0280 -0.0679 332 TYR A O 2398 C CB . TYR A 306 ? 0.3120 0.1374 0.2511 -0.0548 -0.0243 -0.0782 332 TYR A CB 2399 C CG . TYR A 306 ? 0.3249 0.1461 0.2404 -0.0413 -0.0187 -0.0783 332 TYR A CG 2400 C CD1 . TYR A 306 ? 0.3175 0.1535 0.2266 -0.0377 -0.0177 -0.0738 332 TYR A CD1 2401 C CD2 . TYR A 306 ? 0.3478 0.1500 0.2493 -0.0320 -0.0128 -0.0825 332 TYR A CD2 2402 C CE1 . TYR A 306 ? 0.3222 0.1542 0.2122 -0.0263 -0.0099 -0.0730 332 TYR A CE1 2403 C CE2 . TYR A 306 ? 0.3412 0.1424 0.2249 -0.0195 -0.0048 -0.0821 332 TYR A CE2 2404 C CZ . TYR A 306 ? 0.3163 0.1326 0.1949 -0.0175 -0.0028 -0.0770 332 TYR A CZ 2405 O OH . TYR A 306 ? 0.3219 0.1378 0.1859 -0.0067 0.0076 -0.0757 332 TYR A OH 2406 N N . VAL A 307 ? 0.3663 0.1889 0.3513 -0.0760 -0.0139 -0.0534 333 VAL A N 2407 C CA . VAL A 307 ? 0.3031 0.1346 0.3097 -0.0890 -0.0131 -0.0470 333 VAL A CA 2408 C C . VAL A 307 ? 0.2764 0.1275 0.2854 -0.0885 -0.0059 -0.0361 333 VAL A C 2409 O O . VAL A 307 ? 0.2697 0.1145 0.2651 -0.0803 0.0014 -0.0285 333 VAL A O 2410 C CB . VAL A 307 ? 0.3622 0.1692 0.3714 -0.0939 -0.0078 -0.0405 333 VAL A CB 2411 C CG1 . VAL A 307 ? 0.3330 0.1496 0.3613 -0.1076 -0.0031 -0.0305 333 VAL A CG1 2412 C CG2 . VAL A 307 ? 0.3603 0.1476 0.3703 -0.0957 -0.0155 -0.0533 333 VAL A CG2 2413 N N . PRO A 308 ? 0.2634 0.1387 0.2904 -0.0964 -0.0085 -0.0364 334 PRO A N 2414 C CA . PRO A 308 ? 0.2397 0.1344 0.2690 -0.0947 -0.0009 -0.0285 334 PRO A CA 2415 C C . PRO A 308 ? 0.3020 0.1876 0.3270 -0.0958 0.0123 -0.0153 334 PRO A C 2416 O O . PRO A 308 ? 0.3354 0.2090 0.3666 -0.1033 0.0162 -0.0106 334 PRO A O 2417 C CB . PRO A 308 ? 0.2630 0.1846 0.3166 -0.1035 -0.0059 -0.0320 334 PRO A CB 2418 C CG . PRO A 308 ? 0.3588 0.2757 0.4162 -0.1074 -0.0208 -0.0434 334 PRO A CG 2419 C CD . PRO A 308 ? 0.2725 0.1588 0.3185 -0.1065 -0.0198 -0.0446 334 PRO A CD 2420 N N . HIS A 309 ? 0.2353 0.1236 0.2471 -0.0881 0.0183 -0.0095 335 HIS A N 2421 C CA . HIS A 309 ? 0.2410 0.1239 0.2448 -0.0881 0.0300 0.0029 335 HIS A CA 2422 C C . HIS A 309 ? 0.2399 0.1434 0.2630 -0.0978 0.0375 0.0062 335 HIS A C 2423 O O . HIS A 309 ? 0.2642 0.1911 0.3070 -0.1016 0.0326 -0.0014 335 HIS A O 2424 C CB . HIS A 309 ? 0.2271 0.1124 0.2138 -0.0781 0.0318 0.0060 335 HIS A CB 2425 C CG . HIS A 309 ? 0.3194 0.1901 0.2909 -0.0657 0.0254 0.0047 335 HIS A CG 2426 N ND1 . HIS A 309 ? 0.3176 0.1910 0.2768 -0.0533 0.0244 0.0094 335 HIS A ND1 2427 C CD2 . HIS A 309 ? 0.3669 0.2224 0.3355 -0.0631 0.0199 -0.0020 335 HIS A CD2 2428 C CE1 . HIS A 309 ? 0.3212 0.1847 0.2753 -0.0440 0.0191 0.0063 335 HIS A CE1 2429 N NE2 . HIS A 309 ? 0.3010 0.1526 0.2590 -0.0491 0.0176 -0.0004 335 HIS A NE2 2430 N N . PRO A 310 ? 0.3599 0.2557 0.3764 -0.1002 0.0497 0.0179 336 PRO A N 2431 C CA . PRO A 310 ? 0.3231 0.2415 0.3551 -0.1065 0.0605 0.0217 336 PRO A CA 2432 C C . PRO A 310 ? 0.2640 0.2070 0.2991 -0.1008 0.0612 0.0167 336 PRO A C 2433 O O . PRO A 310 ? 0.2441 0.2128 0.3014 -0.1048 0.0658 0.0143 336 PRO A O 2434 C CB . PRO A 310 ? 0.3424 0.2420 0.3528 -0.1049 0.0736 0.0361 336 PRO A CB 2435 C CG . PRO A 310 ? 0.4277 0.2964 0.4264 -0.1042 0.0682 0.0391 336 PRO A CG 2436 C CD . PRO A 310 ? 0.3225 0.1880 0.3179 -0.0969 0.0543 0.0283 336 PRO A CD 2437 N N . ALA A 311 ? 0.2302 0.1652 0.2451 -0.0916 0.0564 0.0148 337 ALA A N 2438 C CA . ALA A 311 ? 0.1981 0.1557 0.2149 -0.0819 0.0523 0.0092 337 ALA A CA 2439 C C . ALA A 311 ? 0.2029 0.1816 0.2449 -0.0846 0.0432 -0.0013 337 ALA A C 2440 O O . ALA A 311 ? 0.2021 0.2016 0.2531 -0.0789 0.0426 -0.0050 337 ALA A O 2441 C CB . ALA A 311 ? 0.1893 0.1370 0.1838 -0.0685 0.0438 0.0086 337 ALA A CB 2442 N N . PHE A 312 ? 0.1810 0.1521 0.2320 -0.0919 0.0350 -0.0065 338 PHE A N 2443 C CA . PHE A 312 ? 0.1692 0.1586 0.2396 -0.0932 0.0233 -0.0168 338 PHE A CA 2444 C C . PHE A 312 ? 0.1791 0.1968 0.2798 -0.0990 0.0281 -0.0174 338 PHE A C 2445 O O . PHE A 312 ? 0.1723 0.2132 0.2867 -0.0933 0.0245 -0.0223 338 PHE A O 2446 C CB . PHE A 312 ? 0.2777 0.2520 0.3465 -0.0970 0.0118 -0.0223 338 PHE A CB 2447 C CG . PHE A 312 ? 0.2822 0.2731 0.3658 -0.0977 -0.0024 -0.0326 338 PHE A CG 2448 C CD1 . PHE A 312 ? 0.2876 0.2773 0.3572 -0.0891 -0.0123 -0.0393 338 PHE A CD1 2449 C CD2 . PHE A 312 ? 0.2707 0.2780 0.3802 -0.1067 -0.0065 -0.0351 338 PHE A CD2 2450 C CE1 . PHE A 312 ? 0.3082 0.3112 0.3864 -0.0880 -0.0271 -0.0484 338 PHE A CE1 2451 C CE2 . PHE A 312 ? 0.3315 0.3546 0.4522 -0.1063 -0.0222 -0.0446 338 PHE A CE2 2452 C CZ . PHE A 312 ? 0.2280 0.2481 0.3311 -0.0960 -0.0332 -0.0510 338 PHE A CZ 2453 N N . ASN A 313 ? 0.1850 0.2003 0.2956 -0.1079 0.0358 -0.0115 339 ASN A N 2454 C CA . ASN A 313 ? 0.3750 0.4171 0.5148 -0.1135 0.0431 -0.0103 339 ASN A CA 2455 C C . ASN A 313 ? 0.2861 0.3454 0.4265 -0.1058 0.0564 -0.0074 339 ASN A C 2456 O O . ASN A 313 ? 0.2164 0.3050 0.3828 -0.1035 0.0568 -0.0118 339 ASN A O 2457 C CB . ASN A 313 ? 0.4833 0.5146 0.6278 -0.1250 0.0527 -0.0021 339 ASN A CB 2458 C CG . ASN A 313 ? 0.7274 0.7424 0.8750 -0.1337 0.0396 -0.0065 339 ASN A CG 2459 O OD1 . ASN A 313 ? 0.9118 0.8999 1.0362 -0.1300 0.0330 -0.0075 339 ASN A OD1 2460 N ND2 . ASN A 313 ? 0.5753 0.6067 0.7518 -0.1453 0.0361 -0.0098 339 ASN A ND2 2461 N N . ALA A 314 ? 0.1821 0.2231 0.2929 -0.1005 0.0666 -0.0007 340 ALA A N 2462 C CA . ALA A 314 ? 0.2987 0.3517 0.4033 -0.0924 0.0795 0.0011 340 ALA A CA 2463 C C . ALA A 314 ? 0.2516 0.3197 0.3606 -0.0800 0.0681 -0.0079 340 ALA A C 2464 O O . ALA A 314 ? 0.2231 0.3112 0.3433 -0.0728 0.0748 -0.0104 340 ALA A O 2465 C CB . ALA A 314 ? 0.2905 0.3173 0.3556 -0.0873 0.0878 0.0097 340 ALA A CB 2466 N N . THR A 315 ? 0.1460 0.2018 0.2440 -0.0758 0.0513 -0.0120 341 THR A N 2467 C CA . THR A 315 ? 0.1504 0.2137 0.2477 -0.0637 0.0395 -0.0182 341 THR A CA 2468 C C . THR A 315 ? 0.1853 0.2760 0.3164 -0.0641 0.0327 -0.0247 341 THR A C 2469 O O . THR A 315 ? 0.1464 0.2526 0.2868 -0.0536 0.0326 -0.0275 341 THR A O 2470 C CB . THR A 315 ? 0.1739 0.2160 0.2499 -0.0603 0.0265 -0.0195 341 THR A CB 2471 O OG1 . THR A 315 ? 0.1988 0.2206 0.2489 -0.0580 0.0314 -0.0143 341 THR A OG1 2472 C CG2 . THR A 315 ? 0.1647 0.2107 0.2379 -0.0488 0.0167 -0.0239 341 THR A CG2 2473 N N . ILE A 316 ? 0.1287 0.2247 0.2789 -0.0757 0.0259 -0.0277 342 ILE A N 2474 C CA . ILE A 316 ? 0.1540 0.2800 0.3413 -0.0774 0.0169 -0.0349 342 ILE A CA 2475 C C . ILE A 316 ? 0.1653 0.3199 0.3810 -0.0757 0.0318 -0.0337 342 ILE A C 2476 O O . ILE A 316 ? 0.2154 0.3937 0.4514 -0.0650 0.0265 -0.0386 342 ILE A O 2477 C CB . ILE A 316 ? 0.1398 0.2633 0.3392 -0.0910 0.0084 -0.0371 342 ILE A CB 2478 C CG1 . ILE A 316 ? 0.2974 0.3963 0.4721 -0.0910 -0.0072 -0.0417 342 ILE A CG1 2479 C CG2 . ILE A 316 ? 0.1441 0.2992 0.3788 -0.0911 -0.0010 -0.0422 342 ILE A CG2 2480 C CD1 . ILE A 316 ? 0.2736 0.3802 0.4448 -0.0789 -0.0247 -0.0487 342 ILE A CD1 2481 N N . GLN A 317 ? 0.1385 0.2866 0.3490 -0.0831 0.0499 -0.0257 343 GLN A N 2482 C CA . GLN A 317 ? 0.1626 0.3332 0.3923 -0.0806 0.0658 -0.0227 343 GLN A CA 2483 C C . GLN A 317 ? 0.1806 0.3582 0.4025 -0.0647 0.0739 -0.0253 343 GLN A C 2484 O O . GLN A 317 ? 0.2124 0.4151 0.4573 -0.0562 0.0782 -0.0280 343 GLN A O 2485 C CB . GLN A 317 ? 0.2196 0.3761 0.4371 -0.0911 0.0834 -0.0123 343 GLN A CB 2486 C CG . GLN A 317 ? 0.4256 0.5806 0.6600 -0.1068 0.0776 -0.0106 343 GLN A CG 2487 C CD . GLN A 317 ? 0.6724 0.8041 0.8878 -0.1165 0.0924 0.0007 343 GLN A CD 2488 O OE1 . GLN A 317 ? 0.8463 0.9667 1.0367 -0.1111 0.1081 0.0079 343 GLN A OE1 2489 N NE2 . GLN A 317 ? 0.6774 0.7997 0.9021 -0.1302 0.0867 0.0020 343 GLN A NE2 2490 N N . ALA A 318 ? 0.1806 0.3326 0.3659 -0.0586 0.0735 -0.0241 344 ALA A N 2491 C CA . ALA A 318 ? 0.1790 0.3276 0.3465 -0.0422 0.0776 -0.0263 344 ALA A CA 2492 C C . ALA A 318 ? 0.2216 0.3805 0.4024 -0.0294 0.0613 -0.0331 344 ALA A C 2493 O O . ALA A 318 ? 0.2474 0.4177 0.4360 -0.0162 0.0662 -0.0370 344 ALA A O 2494 C CB . ALA A 318 ? 0.1631 0.2783 0.2853 -0.0392 0.0767 -0.0226 344 ALA A CB 2495 N N . LEU A 319 ? 0.1631 0.3153 0.3435 -0.0320 0.0424 -0.0343 345 LEU A N 2496 C CA . LEU A 319 ? 0.1723 0.3303 0.3600 -0.0195 0.0258 -0.0387 345 LEU A CA 2497 C C . LEU A 319 ? 0.2115 0.4074 0.4441 -0.0152 0.0240 -0.0436 345 LEU A C 2498 O O . LEU A 319 ? 0.2721 0.4763 0.5127 0.0009 0.0188 -0.0465 345 LEU A O 2499 C CB . LEU A 319 ? 0.1573 0.2992 0.3305 -0.0237 0.0075 -0.0386 345 LEU A CB 2500 C CG . LEU A 319 ? 0.1358 0.2434 0.2689 -0.0229 0.0062 -0.0348 345 LEU A CG 2501 C CD1 . LEU A 319 ? 0.1125 0.2070 0.2341 -0.0297 -0.0068 -0.0352 345 LEU A CD1 2502 C CD2 . LEU A 319 ? 0.1306 0.2252 0.2471 -0.0082 0.0038 -0.0346 345 LEU A CD2 2503 N N . LEU A 320 ? 0.1508 0.3694 0.4150 -0.0295 0.0286 -0.0446 346 LEU A N 2504 C CA . LEU A 320 ? 0.2127 0.4650 0.5171 -0.0267 0.0249 -0.0475 346 LEU A CA 2505 C C . LEU A 320 ? 0.2880 0.5561 0.6043 -0.0187 0.0457 -0.0456 346 LEU A C 2506 O O . LEU A 320 ? 0.3436 0.6373 0.6878 -0.0087 0.0426 -0.0479 346 LEU A O 2507 C CB . LEU A 320 ? 0.1274 0.3865 0.4477 -0.0451 0.0209 -0.0459 346 LEU A CB 2508 C CG . LEU A 320 ? 0.1996 0.4452 0.5096 -0.0515 -0.0020 -0.0498 346 LEU A CG 2509 C CD1 . LEU A 320 ? 0.2061 0.4499 0.5254 -0.0711 -0.0018 -0.0484 346 LEU A CD1 2510 C CD2 . LEU A 320 ? 0.1579 0.4196 0.4807 -0.0376 -0.0246 -0.0557 346 LEU A CD2 2511 N N . ALA A 321 ? 0.3707 0.6226 0.6630 -0.0219 0.0663 -0.0413 347 ALA A N 2512 C CA . ALA A 321 ? 0.4877 0.7511 0.7840 -0.0150 0.0874 -0.0393 347 ALA A CA 2513 C C . ALA A 321 ? 0.6179 0.8695 0.8934 0.0042 0.0920 -0.0440 347 ALA A C 2514 O O . ALA A 321 ? 0.6868 0.9475 0.9761 0.0198 0.0813 -0.0492 347 ALA A O 2515 C CB . ALA A 321 ? 0.5565 0.8074 0.8339 -0.0288 0.1069 -0.0312 347 ALA A CB 2516 N N . PRO B 1 ? 0.7363 0.6366 0.6323 -0.2396 -0.0331 0.0151 27 PRO B N 2517 C CA . PRO B 1 ? 0.6706 0.5591 0.5593 -0.2292 -0.0339 0.0215 27 PRO B CA 2518 C C . PRO B 1 ? 0.5626 0.4587 0.4641 -0.2113 -0.0359 0.0152 27 PRO B C 2519 O O . PRO B 1 ? 0.6125 0.5055 0.5222 -0.2046 -0.0402 0.0067 27 PRO B O 2520 C CB . PRO B 1 ? 0.6225 0.4624 0.4912 -0.2297 -0.0424 0.0283 27 PRO B CB 2521 C CG . PRO B 1 ? 0.7058 0.5325 0.5710 -0.2422 -0.0450 0.0257 27 PRO B CG 2522 C CD . PRO B 1 ? 0.7842 0.6452 0.6685 -0.2441 -0.0408 0.0150 27 PRO B CD 2523 N N . THR B 2 ? 0.5502 0.4570 0.4528 -0.2040 -0.0327 0.0191 28 THR B N 2524 C CA . THR B 2 ? 0.4961 0.4055 0.4080 -0.1877 -0.0353 0.0144 28 THR B CA 2525 C C . THR B 2 ? 0.4667 0.3329 0.3663 -0.1775 -0.0450 0.0160 28 THR B C 2526 O O . THR B 2 ? 0.4302 0.2651 0.3157 -0.1822 -0.0500 0.0203 28 THR B O 2527 C CB . THR B 2 ? 0.4855 0.4198 0.4031 -0.1830 -0.0288 0.0176 28 THR B CB 2528 O OG1 . THR B 2 ? 0.5939 0.5163 0.4953 -0.1902 -0.0266 0.0274 28 THR B OG1 2529 C CG2 . THR B 2 ? 0.5556 0.5367 0.4919 -0.1859 -0.0204 0.0123 28 THR B CG2 2530 N N . SER B 3 ? 0.4116 0.2782 0.3176 -0.1626 -0.0478 0.0121 29 SER B N 2531 C CA . SER B 3 ? 0.4352 0.2686 0.3346 -0.1479 -0.0567 0.0107 29 SER B CA 2532 C C . SER B 3 ? 0.4120 0.2574 0.3162 -0.1304 -0.0544 0.0129 29 SER B C 2533 O O . SER B 3 ? 0.4022 0.2819 0.3183 -0.1272 -0.0468 0.0118 29 SER B O 2534 C CB . SER B 3 ? 0.4602 0.2932 0.3690 -0.1399 -0.0608 -0.0016 29 SER B CB 2535 O OG . SER B 3 ? 0.6087 0.4278 0.5188 -0.1196 -0.0660 -0.0056 29 SER B OG 2536 N N . PRO B 4 ? 0.4221 0.2392 0.3175 -0.1185 -0.0616 0.0155 30 PRO B N 2537 C CA . PRO B 4 ? 0.3616 0.1923 0.2638 -0.1010 -0.0599 0.0155 30 PRO B CA 2538 C C . PRO B 4 ? 0.4428 0.2942 0.3621 -0.0854 -0.0585 0.0048 30 PRO B C 2539 O O . PRO B 4 ? 0.3976 0.2587 0.3227 -0.0713 -0.0576 0.0041 30 PRO B O 2540 C CB . PRO B 4 ? 0.4377 0.2321 0.3261 -0.0934 -0.0694 0.0207 30 PRO B CB 2541 C CG . PRO B 4 ? 0.5164 0.2767 0.3947 -0.1015 -0.0773 0.0199 30 PRO B CG 2542 C CD . PRO B 4 ? 0.5360 0.3082 0.4144 -0.1220 -0.0715 0.0200 30 PRO B CD 2543 N N . PHE B 5 ? 0.3649 0.2238 0.2913 -0.0889 -0.0585 -0.0032 31 PHE B N 2544 C CA . PHE B 5 ? 0.3362 0.2146 0.2764 -0.0753 -0.0575 -0.0126 31 PHE B CA 2545 C C . PHE B 5 ? 0.3793 0.2946 0.3323 -0.0793 -0.0503 -0.0147 31 PHE B C 2546 O O . PHE B 5 ? 0.4358 0.3637 0.3964 -0.0770 -0.0508 -0.0224 31 PHE B O 2547 C CB . PHE B 5 ? 0.3373 0.1967 0.2760 -0.0722 -0.0642 -0.0221 31 PHE B CB 2548 C CG . PHE B 5 ? 0.3884 0.2131 0.3179 -0.0633 -0.0724 -0.0221 31 PHE B CG 2549 C CD1 . PHE B 5 ? 0.3757 0.2029 0.3097 -0.0463 -0.0738 -0.0234 31 PHE B CD1 2550 C CD2 . PHE B 5 ? 0.3880 0.1775 0.3050 -0.0721 -0.0794 -0.0210 31 PHE B CD2 2551 C CE1 . PHE B 5 ? 0.3824 0.1801 0.3098 -0.0367 -0.0822 -0.0240 31 PHE B CE1 2552 C CE2 . PHE B 5 ? 0.4091 0.1651 0.3181 -0.0623 -0.0883 -0.0209 31 PHE B CE2 2553 C CZ . PHE B 5 ? 0.3914 0.1529 0.3064 -0.0438 -0.0898 -0.0226 31 PHE B CZ 2554 N N . GLU B 6 ? 0.3916 0.3248 0.3469 -0.0847 -0.0441 -0.0083 32 GLU B N 2555 C CA . GLU B 6 ? 0.4404 0.4087 0.4092 -0.0867 -0.0381 -0.0104 32 GLU B CA 2556 C C . GLU B 6 ? 0.3110 0.2981 0.2888 -0.0728 -0.0340 -0.0093 32 GLU B C 2557 O O . GLU B 6 ? 0.3411 0.3553 0.3295 -0.0729 -0.0288 -0.0089 32 GLU B O 2558 C CB . GLU B 6 ? 0.4835 0.4627 0.4508 -0.1037 -0.0335 -0.0062 32 GLU B CB 2559 C CG . GLU B 6 ? 0.6147 0.5854 0.5779 -0.1190 -0.0367 -0.0093 32 GLU B CG 2560 C CD . GLU B 6 ? 0.7658 0.7371 0.7222 -0.1387 -0.0332 -0.0037 32 GLU B CD 2561 O OE1 . GLU B 6 ? 0.8469 0.8410 0.8082 -0.1407 -0.0263 0.0000 32 GLU B OE1 2562 O OE2 . GLU B 6 ? 0.7774 0.7260 0.7232 -0.1526 -0.0373 -0.0033 32 GLU B OE2 2563 N N . THR B 7 ? 0.2262 0.1987 0.2006 -0.0608 -0.0368 -0.0092 33 THR B N 2564 C CA . THR B 7 ? 0.2092 0.1969 0.1918 -0.0482 -0.0337 -0.0090 33 THR B CA 2565 C C . THR B 7 ? 0.2985 0.2833 0.2843 -0.0371 -0.0374 -0.0147 33 THR B C 2566 O O . THR B 7 ? 0.2112 0.1768 0.1909 -0.0366 -0.0427 -0.0184 33 THR B O 2567 C CB . THR B 7 ? 0.2490 0.2276 0.2255 -0.0447 -0.0326 -0.0036 33 THR B CB 2568 O OG1 . THR B 7 ? 0.2541 0.2064 0.2211 -0.0403 -0.0390 -0.0034 33 THR B OG1 2569 C CG2 . THR B 7 ? 0.2614 0.2428 0.2323 -0.0568 -0.0285 0.0017 33 THR B CG2 2570 N N . LEU B 8 ? 0.1523 0.1559 0.1473 -0.0286 -0.0346 -0.0156 34 LEU B N 2571 C CA . LEU B 8 ? 0.1928 0.1979 0.1904 -0.0197 -0.0370 -0.0208 34 LEU B CA 2572 C C . LEU B 8 ? 0.1910 0.1777 0.1835 -0.0120 -0.0402 -0.0220 34 LEU B C 2573 O O . LEU B 8 ? 0.2212 0.1999 0.2124 -0.0075 -0.0440 -0.0283 34 LEU B O 2574 C CB . LEU B 8 ? 0.1822 0.2097 0.1891 -0.0137 -0.0334 -0.0196 34 LEU B CB 2575 C CG . LEU B 8 ? 0.1560 0.2040 0.1696 -0.0184 -0.0319 -0.0192 34 LEU B CG 2576 C CD1 . LEU B 8 ? 0.1561 0.2210 0.1780 -0.0123 -0.0286 -0.0149 34 LEU B CD1 2577 C CD2 . LEU B 8 ? 0.1609 0.2140 0.1740 -0.0197 -0.0352 -0.0252 34 LEU B CD2 2578 N N . ARG B 9 ? 0.1725 0.1540 0.1625 -0.0103 -0.0390 -0.0167 35 ARG B N 2579 C CA . ARG B 9 ? 0.2142 0.1815 0.2005 -0.0025 -0.0427 -0.0174 35 ARG B CA 2580 C C . ARG B 9 ? 0.2622 0.2041 0.2393 -0.0044 -0.0493 -0.0188 35 ARG B C 2581 O O . ARG B 9 ? 0.2540 0.1860 0.2311 0.0041 -0.0541 -0.0237 35 ARG B O 2582 C CB . ARG B 9 ? 0.1738 0.1419 0.1583 -0.0013 -0.0404 -0.0115 35 ARG B CB 2583 C CG . ARG B 9 ? 0.2840 0.2470 0.2611 -0.0113 -0.0385 -0.0053 35 ARG B CG 2584 C CD . ARG B 9 ? 0.2577 0.2252 0.2334 -0.0095 -0.0355 -0.0014 35 ARG B CD 2585 N NE . ARG B 9 ? 0.3045 0.2568 0.2736 -0.0037 -0.0410 -0.0004 35 ARG B NE 2586 C CZ . ARG B 9 ? 0.3552 0.3097 0.3224 -0.0007 -0.0403 0.0016 35 ARG B CZ 2587 N NH1 . ARG B 9 ? 0.2834 0.2532 0.2547 -0.0024 -0.0337 0.0023 35 ARG B NH1 2588 N NH2 . ARG B 9 ? 0.3745 0.3163 0.3362 0.0047 -0.0466 0.0024 35 ARG B NH2 2589 N N . ALA B 10 ? 0.2221 0.1532 0.1918 -0.0156 -0.0499 -0.0149 36 ALA B N 2590 C CA . ALA B 10 ? 0.3037 0.2061 0.2631 -0.0184 -0.0571 -0.0153 36 ALA B CA 2591 C C . ALA B 10 ? 0.3360 0.2341 0.2983 -0.0164 -0.0603 -0.0249 36 ALA B C 2592 O O . ALA B 10 ? 0.2734 0.1510 0.2323 -0.0099 -0.0670 -0.0296 36 ALA B O 2593 C CB . ALA B 10 ? 0.3069 0.1988 0.2562 -0.0334 -0.0564 -0.0079 36 ALA B CB 2594 N N . ALA B 11 ? 0.2992 0.2171 0.2680 -0.0212 -0.0562 -0.0286 37 ALA B N 2595 C CA . ALA B 11 ? 0.2881 0.2043 0.2586 -0.0204 -0.0589 -0.0387 37 ALA B CA 2596 C C . ALA B 11 ? 0.2592 0.1841 0.2362 -0.0065 -0.0595 -0.0467 37 ALA B C 2597 O O . ALA B 11 ? 0.2285 0.1448 0.2050 -0.0027 -0.0632 -0.0563 37 ALA B O 2598 C CB . ALA B 11 ? 0.2167 0.1542 0.1918 -0.0300 -0.0550 -0.0401 37 ALA B CB 2599 N N . ALA B 12 ? 0.1954 0.1378 0.1786 0.0003 -0.0555 -0.0434 38 ALA B N 2600 C CA . ALA B 12 ? 0.2165 0.1713 0.2061 0.0114 -0.0548 -0.0504 38 ALA B CA 2601 C C . ALA B 12 ? 0.2484 0.1867 0.2372 0.0220 -0.0602 -0.0549 38 ALA B C 2602 O O . ALA B 12 ? 0.2141 0.1600 0.2080 0.0304 -0.0608 -0.0643 38 ALA B O 2603 C CB . ALA B 12 ? 0.1784 0.1556 0.1743 0.0136 -0.0490 -0.0449 38 ALA B CB 2604 N N . ALA B 13 ? 0.2973 0.2152 0.2799 0.0216 -0.0643 -0.0481 39 ALA B N 2605 C CA . ALA B 13 ? 0.3119 0.2145 0.2941 0.0326 -0.0708 -0.0506 39 ALA B CA 2606 C C . ALA B 13 ? 0.3486 0.2420 0.3331 0.0406 -0.0757 -0.0635 39 ALA B C 2607 O O . ALA B 13 ? 0.3080 0.1875 0.2876 0.0348 -0.0779 -0.0674 39 ALA B O 2608 C CB . ALA B 13 ? 0.3387 0.2151 0.3098 0.0283 -0.0761 -0.0409 39 ALA B CB 2609 N N . PRO B 14 ? 0.3827 0.2846 0.3753 0.0538 -0.0774 -0.0711 40 PRO B N 2610 C CA . PRO B 14 ? 0.3666 0.2816 0.3649 0.0609 -0.0766 -0.0674 40 PRO B CA 2611 C C . PRO B 14 ? 0.3089 0.2568 0.3154 0.0596 -0.0678 -0.0679 40 PRO B C 2612 O O . PRO B 14 ? 0.2907 0.2510 0.3030 0.0650 -0.0669 -0.0666 40 PRO B O 2613 C CB . PRO B 14 ? 0.3574 0.2656 0.3616 0.0757 -0.0836 -0.0778 40 PRO B CB 2614 C CG . PRO B 14 ? 0.3039 0.2176 0.3109 0.0757 -0.0817 -0.0892 40 PRO B CG 2615 C CD . PRO B 14 ? 0.3596 0.2591 0.3568 0.0629 -0.0807 -0.0861 40 PRO B CD 2616 N N . ARG B 15 ? 0.2611 0.2227 0.2679 0.0524 -0.0620 -0.0695 41 ARG B N 2617 C CA . ARG B 15 ? 0.2052 0.1943 0.2175 0.0499 -0.0545 -0.0673 41 ARG B CA 2618 C C . ARG B 15 ? 0.2262 0.2148 0.2354 0.0426 -0.0516 -0.0546 41 ARG B C 2619 O O . ARG B 15 ? 0.3305 0.3017 0.3329 0.0374 -0.0540 -0.0487 41 ARG B O 2620 C CB . ARG B 15 ? 0.2613 0.2655 0.2740 0.0452 -0.0504 -0.0727 41 ARG B CB 2621 C CG . ARG B 15 ? 0.2078 0.2159 0.2233 0.0520 -0.0521 -0.0872 41 ARG B CG 2622 C CD . ARG B 15 ? 0.2010 0.2266 0.2149 0.0460 -0.0478 -0.0919 41 ARG B CD 2623 N NE . ARG B 15 ? 0.3303 0.3615 0.3466 0.0525 -0.0487 -0.1075 41 ARG B NE 2624 C CZ . ARG B 15 ? 0.2911 0.3034 0.3044 0.0549 -0.0539 -0.1170 41 ARG B CZ 2625 N NH1 . ARG B 15 ? 0.3573 0.3438 0.3642 0.0495 -0.0586 -0.1112 41 ARG B NH1 2626 N NH2 . ARG B 15 ? 0.3192 0.3397 0.3367 0.0607 -0.0532 -0.1289 41 ARG B NH2 2627 N N . TYR B 16 ? 0.2201 0.2273 0.2340 0.0418 -0.0463 -0.0509 42 TYR B N 2628 C CA . TYR B 16 ? 0.1496 0.1574 0.1614 0.0356 -0.0431 -0.0407 42 TYR B CA 2629 C C . TYR B 16 ? 0.1231 0.1415 0.1349 0.0287 -0.0391 -0.0381 42 TYR B C 2630 O O . TYR B 16 ? 0.1303 0.1605 0.1438 0.0286 -0.0378 -0.0431 42 TYR B O 2631 C CB . TYR B 16 ? 0.1530 0.1715 0.1694 0.0381 -0.0404 -0.0377 42 TYR B CB 2632 C CG . TYR B 16 ? 0.1853 0.2245 0.2075 0.0386 -0.0359 -0.0403 42 TYR B CG 2633 C CD1 . TYR B 16 ? 0.1327 0.1821 0.1550 0.0331 -0.0314 -0.0352 42 TYR B CD1 2634 C CD2 . TYR B 16 ? 0.1040 0.1531 0.1315 0.0444 -0.0365 -0.0477 42 TYR B CD2 2635 C CE1 . TYR B 16 ? 0.1301 0.1964 0.1553 0.0323 -0.0279 -0.0361 42 TYR B CE1 2636 C CE2 . TYR B 16 ? 0.1722 0.2413 0.2036 0.0428 -0.0318 -0.0497 42 TYR B CE2 2637 C CZ . TYR B 16 ? 0.1623 0.2386 0.1914 0.0362 -0.0276 -0.0431 42 TYR B CZ 2638 O OH . TYR B 16 ? 0.1043 0.1986 0.1351 0.0334 -0.0235 -0.0436 42 TYR B OH 2639 N N . PHE B 17 ? 0.1694 0.1854 0.1792 0.0230 -0.0373 -0.0307 43 PHE B N 2640 C CA . PHE B 17 ? 0.1425 0.1722 0.1548 0.0183 -0.0337 -0.0275 43 PHE B CA 2641 C C . PHE B 17 ? 0.1156 0.1506 0.1309 0.0183 -0.0302 -0.0207 43 PHE B C 2642 O O . PHE B 17 ? 0.1251 0.1523 0.1383 0.0163 -0.0298 -0.0171 43 PHE B O 2643 C CB . PHE B 17 ? 0.1592 0.1841 0.1684 0.0113 -0.0350 -0.0269 43 PHE B CB 2644 C CG . PHE B 17 ? 0.1520 0.1932 0.1642 0.0079 -0.0335 -0.0269 43 PHE B CG 2645 C CD1 . PHE B 17 ? 0.1443 0.1978 0.1611 0.0069 -0.0306 -0.0206 43 PHE B CD1 2646 C CD2 . PHE B 17 ? 0.1917 0.2362 0.2021 0.0065 -0.0357 -0.0336 43 PHE B CD2 2647 C CE1 . PHE B 17 ? 0.2040 0.2730 0.2236 0.0048 -0.0306 -0.0198 43 PHE B CE1 2648 C CE2 . PHE B 17 ? 0.1126 0.1738 0.1248 0.0032 -0.0352 -0.0331 43 PHE B CE2 2649 C CZ . PHE B 17 ? 0.1700 0.2433 0.1867 0.0026 -0.0331 -0.0256 43 PHE B CZ 2650 N N . GLY B 18 ? 0.1267 0.1741 0.1460 0.0202 -0.0276 -0.0191 44 GLY B N 2651 C CA . GLY B 18 ? 0.1015 0.1504 0.1235 0.0211 -0.0248 -0.0140 44 GLY B CA 2652 C C . GLY B 18 ? 0.0943 0.1524 0.1199 0.0198 -0.0226 -0.0089 44 GLY B C 2653 O O . GLY B 18 ? 0.1129 0.1790 0.1390 0.0180 -0.0235 -0.0086 44 GLY B O 2654 N N . ALA B 19 ? 0.0869 0.1436 0.1151 0.0211 -0.0203 -0.0051 45 ALA B N 2655 C CA . ALA B 19 ? 0.1262 0.1894 0.1587 0.0218 -0.0192 -0.0004 45 ALA B CA 2656 C C . ALA B 19 ? 0.0920 0.1523 0.1261 0.0239 -0.0176 0.0026 45 ALA B C 2657 O O . ALA B 19 ? 0.1019 0.1555 0.1348 0.0241 -0.0165 0.0006 45 ALA B O 2658 C CB . ALA B 19 ? 0.1339 0.1975 0.1694 0.0211 -0.0180 0.0002 45 ALA B CB 2659 N N . ALA B 20 ? 0.0772 0.1418 0.1135 0.0249 -0.0180 0.0075 46 ALA B N 2660 C CA . ALA B 20 ? 0.1193 0.1775 0.1569 0.0262 -0.0168 0.0110 46 ALA B CA 2661 C C . ALA B 20 ? 0.1646 0.2171 0.2067 0.0292 -0.0153 0.0099 46 ALA B C 2662 O O . ALA B 20 ? 0.1153 0.1731 0.1618 0.0315 -0.0156 0.0103 46 ALA B O 2663 C CB . ALA B 20 ? 0.1613 0.2226 0.1988 0.0265 -0.0188 0.0179 46 ALA B CB 2664 N N . LEU B 21 ? 0.1005 0.1445 0.1417 0.0290 -0.0134 0.0075 47 LEU B N 2665 C CA . LEU B 21 ? 0.1408 0.1801 0.1852 0.0316 -0.0112 0.0049 47 LEU B CA 2666 C C . LEU B 21 ? 0.1547 0.1843 0.2011 0.0336 -0.0108 0.0065 47 LEU B C 2667 O O . LEU B 21 ? 0.2043 0.2282 0.2474 0.0303 -0.0108 0.0069 47 LEU B O 2668 C CB . LEU B 21 ? 0.0808 0.1173 0.1208 0.0292 -0.0098 -0.0002 47 LEU B CB 2669 C CG . LEU B 21 ? 0.1320 0.1727 0.1681 0.0266 -0.0110 -0.0015 47 LEU B CG 2670 C CD1 . LEU B 21 ? 0.1403 0.1752 0.1704 0.0244 -0.0107 -0.0048 47 LEU B CD1 2671 C CD2 . LEU B 21 ? 0.1420 0.1904 0.1816 0.0267 -0.0104 -0.0008 47 LEU B CD2 2672 N N . GLY B 22 ? 0.1311 0.1592 0.1836 0.0388 -0.0107 0.0071 48 GLY B N 2673 C CA . GLY B 22 ? 0.1593 0.1745 0.2138 0.0415 -0.0108 0.0078 48 GLY B CA 2674 C C . GLY B 22 ? 0.1313 0.1420 0.1875 0.0434 -0.0074 0.0000 48 GLY B C 2675 O O . GLY B 22 ? 0.1351 0.1548 0.1942 0.0455 -0.0052 -0.0044 48 GLY B O 2676 N N . VAL B 23 ? 0.1537 0.1516 0.2075 0.0415 -0.0068 -0.0022 49 VAL B N 2677 C CA . VAL B 23 ? 0.1803 0.1737 0.2346 0.0428 -0.0036 -0.0108 49 VAL B CA 2678 C C . VAL B 23 ? 0.1568 0.1532 0.2194 0.0513 -0.0021 -0.0150 49 VAL B C 2679 O O . VAL B 23 ? 0.1542 0.1590 0.2171 0.0517 0.0017 -0.0220 49 VAL B O 2680 C CB . VAL B 23 ? 0.2402 0.2176 0.2916 0.0396 -0.0039 -0.0126 49 VAL B CB 2681 C CG1 . VAL B 23 ? 0.3169 0.2889 0.3691 0.0420 -0.0009 -0.0226 49 VAL B CG1 2682 C CG2 . VAL B 23 ? 0.2721 0.2521 0.3167 0.0312 -0.0045 -0.0117 49 VAL B CG2 2683 N N . PRO B 24 ? 0.1857 0.1771 0.2553 0.0581 -0.0052 -0.0106 50 PRO B N 2684 C CA . PRO B 24 ? 0.1446 0.1411 0.2243 0.0676 -0.0037 -0.0166 50 PRO B CA 2685 C C . PRO B 24 ? 0.1523 0.1714 0.2357 0.0677 -0.0009 -0.0194 50 PRO B C 2686 O O . PRO B 24 ? 0.1732 0.2013 0.2626 0.0720 0.0031 -0.0279 50 PRO B O 2687 C CB . PRO B 24 ? 0.2338 0.2221 0.3200 0.0752 -0.0095 -0.0091 50 PRO B CB 2688 C CG . PRO B 24 ? 0.2159 0.1861 0.2932 0.0685 -0.0125 -0.0017 50 PRO B CG 2689 C CD . PRO B 24 ? 0.1471 0.1270 0.2156 0.0580 -0.0100 -0.0011 50 PRO B CD 2690 N N . HIS B 25 ? 0.1200 0.1485 0.1995 0.0623 -0.0025 -0.0131 51 HIS B N 2691 C CA . HIS B 25 ? 0.1102 0.1582 0.1921 0.0604 -0.0003 -0.0150 51 HIS B CA 2692 C C . HIS B 25 ? 0.1061 0.1572 0.1796 0.0528 0.0044 -0.0204 51 HIS B C 2693 O O . HIS B 25 ? 0.1454 0.2099 0.2211 0.0518 0.0084 -0.0255 51 HIS B O 2694 C CB . HIS B 25 ? 0.1611 0.2159 0.2411 0.0569 -0.0043 -0.0070 51 HIS B CB 2695 C CG . HIS B 25 ? 0.1979 0.2495 0.2830 0.0629 -0.0098 -0.0001 51 HIS B CG 2696 N ND1 . HIS B 25 ? 0.1665 0.2213 0.2629 0.0729 -0.0117 -0.0010 51 HIS B ND1 2697 C CD2 . HIS B 25 ? 0.1748 0.2209 0.2544 0.0604 -0.0141 0.0080 51 HIS B CD2 2698 C CE1 . HIS B 25 ? 0.1428 0.1922 0.2396 0.0762 -0.0178 0.0076 51 HIS B CE1 2699 N NE2 . HIS B 25 ? 0.1622 0.2068 0.2483 0.0680 -0.0189 0.0133 51 HIS B NE2 2700 N N . LEU B 26 ? 0.1109 0.1504 0.1743 0.0472 0.0036 -0.0190 52 LEU B N 2701 C CA . LEU B 26 ? 0.1111 0.1513 0.1651 0.0407 0.0065 -0.0230 52 LEU B CA 2702 C C . LEU B 26 ? 0.1568 0.1985 0.2118 0.0427 0.0112 -0.0318 52 LEU B C 2703 O O . LEU B 26 ? 0.1211 0.1720 0.1713 0.0384 0.0150 -0.0357 52 LEU B O 2704 C CB . LEU B 26 ? 0.1036 0.1323 0.1490 0.0362 0.0037 -0.0206 52 LEU B CB 2705 C CG . LEU B 26 ? 0.1711 0.1999 0.2138 0.0334 -0.0002 -0.0140 52 LEU B CG 2706 C CD1 . LEU B 26 ? 0.1568 0.1773 0.1935 0.0300 -0.0022 -0.0140 52 LEU B CD1 2707 C CD2 . LEU B 26 ? 0.1553 0.1923 0.1942 0.0296 -0.0003 -0.0128 52 LEU B CD2 2708 N N . LEU B 27 ? 0.1218 0.1537 0.1822 0.0487 0.0111 -0.0353 53 LEU B N 2709 C CA . LEU B 27 ? 0.1325 0.1641 0.1941 0.0515 0.0156 -0.0458 53 LEU B CA 2710 C C . LEU B 27 ? 0.1763 0.2232 0.2495 0.0586 0.0193 -0.0516 53 LEU B C 2711 O O . LEU B 27 ? 0.1448 0.1950 0.2206 0.0620 0.0238 -0.0620 53 LEU B O 2712 C CB . LEU B 27 ? 0.2286 0.2409 0.2912 0.0548 0.0136 -0.0481 53 LEU B CB 2713 C CG . LEU B 27 ? 0.3183 0.3208 0.3694 0.0472 0.0135 -0.0508 53 LEU B CG 2714 C CD1 . LEU B 27 ? 0.2811 0.2883 0.3232 0.0393 0.0112 -0.0438 53 LEU B CD1 2715 C CD2 . LEU B 27 ? 0.3409 0.3236 0.3932 0.0481 0.0104 -0.0505 53 LEU B CD2 2716 N N . ASN B 28 ? 0.1273 0.1857 0.2077 0.0606 0.0174 -0.0459 54 ASN B N 2717 C CA . ASN B 28 ? 0.1346 0.2116 0.2286 0.0677 0.0201 -0.0510 54 ASN B CA 2718 C C . ASN B 28 ? 0.1651 0.2638 0.2564 0.0600 0.0257 -0.0543 54 ASN B C 2719 O O . ASN B 28 ? 0.1440 0.2627 0.2461 0.0625 0.0273 -0.0561 54 ASN B O 2720 C CB . ASN B 28 ? 0.1245 0.2045 0.2282 0.0734 0.0142 -0.0430 54 ASN B CB 2721 C CG . ASN B 28 ? 0.1663 0.2577 0.2851 0.0837 0.0144 -0.0471 54 ASN B CG 2722 O OD1 . ASN B 28 ? 0.1447 0.2345 0.2663 0.0880 0.0181 -0.0551 54 ASN B OD1 2723 N ND2 . ASN B 28 ? 0.2090 0.3099 0.3342 0.0854 0.0102 -0.0400 54 ASN B ND2 2724 N N . PHE B 29 ? 0.1498 0.2447 0.2262 0.0499 0.0282 -0.0545 55 PHE B N 2725 C CA . PHE B 29 ? 0.1439 0.2545 0.2135 0.0396 0.0320 -0.0538 55 PHE B CA 2726 C C . PHE B 29 ? 0.1895 0.3242 0.2669 0.0403 0.0397 -0.0637 55 PHE B C 2727 O O . PHE B 29 ? 0.1658 0.3182 0.2436 0.0330 0.0424 -0.0622 55 PHE B O 2728 C CB . PHE B 29 ? 0.1653 0.2641 0.2161 0.0299 0.0319 -0.0515 55 PHE B CB 2729 C CG . PHE B 29 ? 0.1951 0.3049 0.2354 0.0182 0.0350 -0.0494 55 PHE B CG 2730 C CD1 . PHE B 29 ? 0.1202 0.2310 0.1584 0.0123 0.0317 -0.0411 55 PHE B CD1 2731 C CD2 . PHE B 29 ? 0.2637 0.3817 0.2948 0.0123 0.0411 -0.0558 55 PHE B CD2 2732 C CE1 . PHE B 29 ? 0.2347 0.3522 0.2620 0.0003 0.0341 -0.0383 55 PHE B CE1 2733 C CE2 . PHE B 29 ? 0.3325 0.4593 0.3519 -0.0001 0.0439 -0.0524 55 PHE B CE2 2734 C CZ . PHE B 29 ? 0.2771 0.4023 0.2946 -0.0063 0.0402 -0.0432 55 PHE B CZ 2735 N N . THR B 30 ? 0.1729 0.3093 0.2570 0.0485 0.0434 -0.0744 56 THR B N 2736 C CA . THR B 30 ? 0.2009 0.3593 0.2912 0.0485 0.0502 -0.0833 56 THR B CA 2737 C C . THR B 30 ? 0.2724 0.4423 0.3795 0.0559 0.0475 -0.0814 56 THR B C 2738 O O . THR B 30 ? 0.2649 0.4555 0.3769 0.0530 0.0518 -0.0855 56 THR B O 2739 C CB . THR B 30 ? 0.2757 0.4269 0.3636 0.0530 0.0534 -0.0936 56 THR B CB 2740 O OG1 . THR B 30 ? 0.3115 0.4438 0.4084 0.0654 0.0482 -0.0940 56 THR B OG1 2741 C CG2 . THR B 30 ? 0.2645 0.4069 0.3339 0.0441 0.0559 -0.0959 56 THR B CG2 2742 N N . HIS B 31 ? 0.1476 0.3049 0.2626 0.0645 0.0403 -0.0749 57 HIS B N 2743 C CA . HIS B 31 ? 0.1820 0.3491 0.3116 0.0716 0.0366 -0.0720 57 HIS B CA 2744 C C . HIS B 31 ? 0.1764 0.3519 0.3070 0.0659 0.0326 -0.0628 57 HIS B C 2745 O O . HIS B 31 ? 0.1522 0.3450 0.2920 0.0659 0.0319 -0.0619 57 HIS B O 2746 C CB . HIS B 31 ? 0.1503 0.2978 0.2869 0.0847 0.0308 -0.0702 57 HIS B CB 2747 C CG . HIS B 31 ? 0.3753 0.5148 0.5126 0.0910 0.0342 -0.0800 57 HIS B CG 2748 N ND1 . HIS B 31 ? 0.5068 0.6615 0.6540 0.0964 0.0378 -0.0883 57 HIS B ND1 2749 C CD2 . HIS B 31 ? 0.4711 0.5899 0.6003 0.0921 0.0347 -0.0838 57 HIS B CD2 2750 C CE1 . HIS B 31 ? 0.4758 0.6187 0.6207 0.1011 0.0403 -0.0968 57 HIS B CE1 2751 N NE2 . HIS B 31 ? 0.4574 0.5781 0.5911 0.0981 0.0384 -0.0942 57 HIS B NE2 2752 N N . ASP B 32 ? 0.1260 0.2896 0.2474 0.0612 0.0297 -0.0566 58 ASP B N 2753 C CA . ASP B 32 ? 0.1583 0.3282 0.2790 0.0553 0.0257 -0.0484 58 ASP B CA 2754 C C . ASP B 32 ? 0.1014 0.2602 0.2035 0.0416 0.0267 -0.0437 58 ASP B C 2755 O O . ASP B 32 ? 0.1548 0.2938 0.2478 0.0403 0.0215 -0.0365 58 ASP B O 2756 C CB . ASP B 32 ? 0.1024 0.2575 0.2266 0.0632 0.0171 -0.0403 58 ASP B CB 2757 C CG . ASP B 32 ? 0.3055 0.4663 0.4275 0.0567 0.0124 -0.0323 58 ASP B CG 2758 O OD1 . ASP B 32 ? 0.2625 0.4388 0.3829 0.0469 0.0154 -0.0332 58 ASP B OD1 2759 O OD2 . ASP B 32 ? 0.2165 0.3647 0.3368 0.0602 0.0058 -0.0249 58 ASP B OD2 2760 N N . PRO B 33 ? 0.1414 0.3123 0.2367 0.0312 0.0330 -0.0472 59 PRO B N 2761 C CA . PRO B 33 ? 0.1436 0.2996 0.2193 0.0190 0.0326 -0.0417 59 PRO B CA 2762 C C . PRO B 33 ? 0.1737 0.3232 0.2448 0.0127 0.0268 -0.0328 59 PRO B C 2763 O O . PRO B 33 ? 0.1818 0.3127 0.2387 0.0073 0.0237 -0.0276 59 PRO B O 2764 C CB . PRO B 33 ? 0.1778 0.3504 0.2478 0.0087 0.0404 -0.0466 59 PRO B CB 2765 C CG . PRO B 33 ? 0.1948 0.3962 0.2833 0.0125 0.0443 -0.0529 59 PRO B CG 2766 C CD . PRO B 33 ? 0.1668 0.3656 0.2712 0.0294 0.0405 -0.0559 59 PRO B CD 2767 N N . LEU B 34 ? 0.1329 0.2980 0.2160 0.0139 0.0251 -0.0319 60 LEU B N 2768 C CA . LEU B 34 ? 0.1350 0.2947 0.2134 0.0074 0.0197 -0.0251 60 LEU B CA 2769 C C . LEU B 34 ? 0.1342 0.2717 0.2067 0.0124 0.0131 -0.0195 60 LEU B C 2770 O O . LEU B 34 ? 0.1081 0.2353 0.1718 0.0061 0.0094 -0.0150 60 LEU B O 2771 C CB . LEU B 34 ? 0.1459 0.3285 0.2392 0.0084 0.0184 -0.0260 60 LEU B CB 2772 C CG . LEU B 34 ? 0.2502 0.4553 0.3459 -0.0025 0.0246 -0.0301 60 LEU B CG 2773 C CD1 . LEU B 34 ? 0.2358 0.4671 0.3480 -0.0018 0.0230 -0.0318 60 LEU B CD1 2774 C CD2 . LEU B 34 ? 0.3241 0.5150 0.4014 -0.0179 0.0249 -0.0254 60 LEU B CD2 2775 N N . PHE B 35 ? 0.1177 0.2479 0.1952 0.0231 0.0118 -0.0203 61 PHE B N 2776 C CA . PHE B 35 ? 0.1072 0.2188 0.1790 0.0263 0.0065 -0.0152 61 PHE B CA 2777 C C . PHE B 35 ? 0.2233 0.3185 0.2800 0.0197 0.0065 -0.0139 61 PHE B C 2778 O O . PHE B 35 ? 0.1224 0.2091 0.1720 0.0158 0.0026 -0.0101 61 PHE B O 2779 C CB . PHE B 35 ? 0.1158 0.2208 0.1943 0.0371 0.0053 -0.0159 61 PHE B CB 2780 C CG . PHE B 35 ? 0.0837 0.1736 0.1574 0.0389 0.0003 -0.0102 61 PHE B CG 2781 C CD1 . PHE B 35 ? 0.0849 0.1589 0.1487 0.0365 0.0004 -0.0099 61 PHE B CD1 2782 C CD2 . PHE B 35 ? 0.1103 0.2040 0.1890 0.0424 -0.0045 -0.0052 61 PHE B CD2 2783 C CE1 . PHE B 35 ? 0.1965 0.2601 0.2566 0.0372 -0.0035 -0.0054 61 PHE B CE1 2784 C CE2 . PHE B 35 ? 0.0818 0.1639 0.1550 0.0427 -0.0083 0.0000 61 PHE B CE2 2785 C CZ . PHE B 35 ? 0.1697 0.2373 0.2340 0.0398 -0.0074 -0.0004 61 PHE B CZ 2786 N N . ASP B 36 ? 0.1274 0.2187 0.1791 0.0190 0.0103 -0.0177 62 ASP B N 2787 C CA . ASP B 36 ? 0.1160 0.1928 0.1534 0.0136 0.0092 -0.0161 62 ASP B CA 2788 C C . ASP B 36 ? 0.1348 0.2115 0.1628 0.0035 0.0087 -0.0132 62 ASP B C 2789 O O . ASP B 36 ? 0.1313 0.1942 0.1497 0.0006 0.0044 -0.0096 62 ASP B O 2790 C CB . ASP B 36 ? 0.1717 0.2461 0.2047 0.0143 0.0132 -0.0211 62 ASP B CB 2791 C CG . ASP B 36 ? 0.2719 0.3390 0.3109 0.0228 0.0124 -0.0236 62 ASP B CG 2792 O OD1 . ASP B 36 ? 0.2124 0.2752 0.2571 0.0274 0.0086 -0.0200 62 ASP B OD1 2793 O OD2 . ASP B 36 ? 0.1906 0.2556 0.2274 0.0241 0.0155 -0.0292 62 ASP B OD2 2794 N N . VAL B 37 ? 0.1533 0.2451 0.1844 -0.0020 0.0128 -0.0148 63 VAL B N 2795 C CA . VAL B 37 ? 0.1768 0.2671 0.1982 -0.0136 0.0123 -0.0115 63 VAL B CA 2796 C C . VAL B 37 ? 0.1895 0.2721 0.2109 -0.0148 0.0063 -0.0076 63 VAL B C 2797 O O . VAL B 37 ? 0.1897 0.2566 0.1995 -0.0201 0.0024 -0.0041 63 VAL B O 2798 C CB . VAL B 37 ? 0.2117 0.3240 0.2387 -0.0206 0.0185 -0.0145 63 VAL B CB 2799 C CG1 . VAL B 37 ? 0.2208 0.3299 0.2382 -0.0342 0.0173 -0.0101 63 VAL B CG1 2800 C CG2 . VAL B 37 ? 0.2366 0.3572 0.2608 -0.0214 0.0252 -0.0195 63 VAL B CG2 2801 N N . THR B 38 ? 0.0997 0.1930 0.1337 -0.0092 0.0051 -0.0086 64 THR B N 2802 C CA . THR B 38 ? 0.1203 0.2091 0.1544 -0.0101 -0.0003 -0.0063 64 THR B CA 2803 C C . THR B 38 ? 0.1561 0.2265 0.1836 -0.0052 -0.0049 -0.0046 64 THR B C 2804 O O . THR B 38 ? 0.1407 0.2010 0.1622 -0.0081 -0.0090 -0.0036 64 THR B O 2805 C CB . THR B 38 ? 0.1602 0.2660 0.2084 -0.0047 -0.0012 -0.0074 64 THR B CB 2806 O OG1 . THR B 38 ? 0.1576 0.2840 0.2142 -0.0085 0.0030 -0.0100 64 THR B OG1 2807 C CG2 . THR B 38 ? 0.2010 0.3040 0.2478 -0.0069 -0.0065 -0.0059 64 THR B CG2 2808 N N . ALA B 39 ? 0.1560 0.2227 0.1850 0.0021 -0.0040 -0.0052 65 ALA B N 2809 C CA . ALA B 39 ? 0.1490 0.2018 0.1727 0.0059 -0.0077 -0.0043 65 ALA B CA 2810 C C . ALA B 39 ? 0.1910 0.2297 0.2025 0.0009 -0.0102 -0.0033 65 ALA B C 2811 O O . ALA B 39 ? 0.2045 0.2338 0.2121 0.0015 -0.0148 -0.0029 65 ALA B O 2812 C CB . ALA B 39 ? 0.1578 0.2091 0.1845 0.0122 -0.0060 -0.0055 65 ALA B CB 2813 N N . VAL B 40 ? 0.1420 0.1794 0.1468 -0.0040 -0.0075 -0.0029 66 VAL B N 2814 C CA . VAL B 40 ? 0.1931 0.2155 0.1844 -0.0087 -0.0108 -0.0003 66 VAL B CA 2815 C C . VAL B 40 ? 0.1547 0.1695 0.1404 -0.0158 -0.0140 0.0021 66 VAL B C 2816 O O . VAL B 40 ? 0.2438 0.2422 0.2218 -0.0154 -0.0199 0.0036 66 VAL B O 2817 C CB . VAL B 40 ? 0.2860 0.3101 0.2693 -0.0137 -0.0069 0.0001 66 VAL B CB 2818 C CG1 . VAL B 40 ? 0.3270 0.3348 0.2941 -0.0202 -0.0113 0.0048 66 VAL B CG1 2819 C CG2 . VAL B 40 ? 0.2870 0.3138 0.2734 -0.0069 -0.0051 -0.0032 66 VAL B CG2 2820 N N . LEU B 41 ? 0.1391 0.1655 0.1290 -0.0223 -0.0106 0.0018 67 LEU B N 2821 C CA . LEU B 41 ? 0.1687 0.1876 0.1531 -0.0311 -0.0135 0.0036 67 LEU B CA 2822 C C . LEU B 41 ? 0.2064 0.2201 0.1949 -0.0271 -0.0185 0.0014 67 LEU B C 2823 O O . LEU B 41 ? 0.2546 0.2517 0.2352 -0.0310 -0.0234 0.0021 67 LEU B O 2824 C CB . LEU B 41 ? 0.2122 0.2491 0.2014 -0.0404 -0.0080 0.0030 67 LEU B CB 2825 C CG . LEU B 41 ? 0.3009 0.3439 0.2839 -0.0468 -0.0024 0.0044 67 LEU B CG 2826 C CD1 . LEU B 41 ? 0.2803 0.3443 0.2690 -0.0569 0.0034 0.0030 67 LEU B CD1 2827 C CD2 . LEU B 41 ? 0.3787 0.3991 0.3430 -0.0531 -0.0061 0.0099 67 LEU B CD2 2828 N N . GLN B 42 ? 0.1637 0.1908 0.1638 -0.0196 -0.0174 -0.0015 68 GLN B N 2829 C CA . GLN B 42 ? 0.1547 0.1822 0.1584 -0.0178 -0.0210 -0.0041 68 GLN B CA 2830 C C . GLN B 42 ? 0.2379 0.2576 0.2414 -0.0088 -0.0246 -0.0062 68 GLN B C 2831 O O . GLN B 42 ? 0.1632 0.1773 0.1653 -0.0082 -0.0283 -0.0093 68 GLN B O 2832 C CB . GLN B 42 ? 0.1156 0.1650 0.1311 -0.0169 -0.0185 -0.0054 68 GLN B CB 2833 C CG . GLN B 42 ? 0.1434 0.2050 0.1616 -0.0268 -0.0159 -0.0052 68 GLN B CG 2834 C CD . GLN B 42 ? 0.1915 0.2439 0.2032 -0.0365 -0.0194 -0.0064 68 GLN B CD 2835 O OE1 . GLN B 42 ? 0.1943 0.2355 0.2026 -0.0340 -0.0240 -0.0087 68 GLN B OE1 2836 N NE2 . GLN B 42 ? 0.2080 0.2657 0.2182 -0.0482 -0.0171 -0.0055 68 GLN B NE2 2837 N N . PHE B 43 ? 0.1340 0.1546 0.1392 -0.0023 -0.0231 -0.0054 69 PHE B N 2838 C CA . PHE B 43 ? 0.1125 0.1323 0.1202 0.0054 -0.0252 -0.0077 69 PHE B CA 2839 C C . PHE B 43 ? 0.1299 0.1370 0.1318 0.0088 -0.0279 -0.0078 69 PHE B C 2840 O O . PHE B 43 ? 0.1473 0.1488 0.1439 0.0064 -0.0272 -0.0051 69 PHE B O 2841 C CB . PHE B 43 ? 0.1247 0.1581 0.1406 0.0097 -0.0217 -0.0068 69 PHE B CB 2842 C CG . PHE B 43 ? 0.1821 0.2291 0.2043 0.0084 -0.0207 -0.0063 69 PHE B CG 2843 C CD1 . PHE B 43 ? 0.1878 0.2438 0.2142 0.0052 -0.0179 -0.0048 69 PHE B CD1 2844 C CD2 . PHE B 43 ? 0.1439 0.1968 0.1681 0.0103 -0.0227 -0.0078 69 PHE B CD2 2845 C CE1 . PHE B 43 ? 0.0973 0.1677 0.1306 0.0048 -0.0181 -0.0044 69 PHE B CE1 2846 C CE2 . PHE B 43 ? 0.1264 0.1927 0.1554 0.0091 -0.0228 -0.0067 69 PHE B CE2 2847 C CZ . PHE B 43 ? 0.0821 0.1571 0.1162 0.0068 -0.0210 -0.0049 69 PHE B CZ 2848 N N . ASN B 44 ? 0.1422 0.1471 0.1455 0.0146 -0.0311 -0.0114 70 ASN B N 2849 C CA . ASN B 44 ? 0.1185 0.1154 0.1188 0.0192 -0.0342 -0.0120 70 ASN B CA 2850 C C . ASN B 44 ? 0.1488 0.1556 0.1560 0.0253 -0.0338 -0.0157 70 ASN B C 2851 O O . ASN B 44 ? 0.1467 0.1500 0.1539 0.0304 -0.0377 -0.0187 70 ASN B O 2852 C CB . ASN B 44 ? 0.1628 0.1421 0.1557 0.0197 -0.0406 -0.0130 70 ASN B CB 2853 C CG . ASN B 44 ? 0.2058 0.1839 0.2015 0.0227 -0.0435 -0.0191 70 ASN B CG 2854 O OD1 . ASN B 44 ? 0.2136 0.2051 0.2153 0.0227 -0.0404 -0.0219 70 ASN B OD1 2855 N ND2 . ASN B 44 ? 0.2888 0.2496 0.2792 0.0254 -0.0500 -0.0212 70 ASN B ND2 2856 N N . GLY B 45 ? 0.1265 0.1462 0.1396 0.0246 -0.0296 -0.0151 71 GLY B N 2857 C CA . GLY B 45 ? 0.1718 0.2016 0.1903 0.0277 -0.0280 -0.0168 71 GLY B CA 2858 C C . GLY B 45 ? 0.1119 0.1484 0.1336 0.0255 -0.0236 -0.0126 71 GLY B C 2859 O O . GLY B 45 ? 0.1001 0.1372 0.1219 0.0231 -0.0219 -0.0097 71 GLY B O 2860 N N . ALA B 46 ? 0.0899 0.1310 0.1147 0.0263 -0.0219 -0.0124 72 ALA B N 2861 C CA . ALA B 46 ? 0.0761 0.1199 0.1037 0.0248 -0.0186 -0.0083 72 ALA B CA 2862 C C . ALA B 46 ? 0.1207 0.1712 0.1509 0.0239 -0.0173 -0.0079 72 ALA B C 2863 O O . ALA B 46 ? 0.1090 0.1634 0.1401 0.0242 -0.0182 -0.0116 72 ALA B O 2864 C CB . ALA B 46 ? 0.1203 0.1572 0.1468 0.0245 -0.0173 -0.0075 72 ALA B CB 2865 N N . THR B 47 ? 0.0737 0.1257 0.1052 0.0225 -0.0156 -0.0031 73 THR B N 2866 C CA . THR B 47 ? 0.0763 0.1320 0.1085 0.0197 -0.0142 -0.0003 73 THR B CA 2867 C C . THR B 47 ? 0.1084 0.1550 0.1420 0.0197 -0.0131 0.0043 73 THR B C 2868 O O . THR B 47 ? 0.1307 0.1753 0.1655 0.0224 -0.0135 0.0069 73 THR B O 2869 C CB . THR B 47 ? 0.1443 0.2098 0.1748 0.0179 -0.0144 0.0022 73 THR B CB 2870 O OG1 . THR B 47 ? 0.1587 0.2319 0.1884 0.0190 -0.0153 -0.0041 73 THR B OG1 2871 C CG2 . THR B 47 ? 0.1053 0.1743 0.1344 0.0131 -0.0127 0.0064 73 THR B CG2 2872 N N . PRO B 48 ? 0.1547 0.1961 0.1887 0.0171 -0.0119 0.0043 74 PRO B N 2873 C CA . PRO B 48 ? 0.1400 0.1702 0.1753 0.0179 -0.0114 0.0079 74 PRO B CA 2874 C C . PRO B 48 ? 0.0997 0.1293 0.1342 0.0175 -0.0125 0.0156 74 PRO B C 2875 O O . PRO B 48 ? 0.1260 0.1606 0.1573 0.0127 -0.0124 0.0191 74 PRO B O 2876 C CB . PRO B 48 ? 0.1338 0.1584 0.1688 0.0134 -0.0103 0.0057 74 PRO B CB 2877 C CG . PRO B 48 ? 0.2588 0.2958 0.2931 0.0091 -0.0101 0.0038 74 PRO B CG 2878 C CD . PRO B 48 ? 0.2159 0.2615 0.2501 0.0134 -0.0114 0.0005 74 PRO B CD 2879 N N . GLU B 49 ? 0.1029 0.1277 0.1402 0.0227 -0.0136 0.0183 75 GLU B N 2880 C CA . GLU B 49 ? 0.1343 0.1596 0.1710 0.0239 -0.0163 0.0262 75 GLU B CA 2881 C C . GLU B 49 ? 0.2615 0.2752 0.2947 0.0199 -0.0171 0.0330 75 GLU B C 2882 O O . GLU B 49 ? 0.2072 0.2239 0.2353 0.0165 -0.0190 0.0404 75 GLU B O 2883 C CB . GLU B 49 ? 0.1399 0.1645 0.1827 0.0316 -0.0178 0.0264 75 GLU B CB 2884 C CG . GLU B 49 ? 0.2353 0.2629 0.2783 0.0345 -0.0220 0.0345 75 GLU B CG 2885 C CD . GLU B 49 ? 0.4147 0.4439 0.4665 0.0432 -0.0237 0.0334 75 GLU B CD 2886 O OE1 . GLU B 49 ? 0.3454 0.3785 0.4019 0.0451 -0.0206 0.0258 75 GLU B OE1 2887 O OE2 . GLU B 49 ? 0.4276 0.4548 0.4816 0.0479 -0.0281 0.0401 75 GLU B OE2 2888 N N . ASN B 50 ? 0.1326 0.1327 0.1671 0.0191 -0.0159 0.0306 76 ASN B N 2889 C CA . ASN B 50 ? 0.2425 0.2278 0.2732 0.0142 -0.0171 0.0372 76 ASN B CA 2890 C C . ASN B 50 ? 0.1979 0.1753 0.2278 0.0076 -0.0145 0.0324 76 ASN B C 2891 O O . ASN B 50 ? 0.2134 0.1835 0.2385 -0.0008 -0.0146 0.0374 76 ASN B O 2892 C CB . ASN B 50 ? 0.1658 0.1347 0.1997 0.0218 -0.0206 0.0416 76 ASN B CB 2893 C CG . ASN B 50 ? 0.2755 0.2516 0.3099 0.0274 -0.0247 0.0487 76 ASN B CG 2894 O OD1 . ASN B 50 ? 0.2980 0.2767 0.3253 0.0224 -0.0270 0.0575 76 ASN B OD1 2895 N ND2 . ASN B 50 ? 0.2590 0.2399 0.3014 0.0371 -0.0256 0.0448 76 ASN B ND2 2896 N N . GLU B 51 ? 0.1502 0.1289 0.1840 0.0104 -0.0125 0.0229 77 GLU B N 2897 C CA . GLU B 51 ? 0.2451 0.2127 0.2789 0.0061 -0.0111 0.0177 77 GLU B CA 2898 C C . GLU B 51 ? 0.1938 0.1698 0.2250 -0.0043 -0.0095 0.0158 77 GLU B C 2899 O O . GLU B 51 ? 0.1852 0.1530 0.2162 -0.0099 -0.0088 0.0120 77 GLU B O 2900 C CB . GLU B 51 ? 0.3912 0.3590 0.4284 0.0121 -0.0097 0.0082 77 GLU B CB 2901 C CG . GLU B 51 ? 0.5845 0.5451 0.6261 0.0219 -0.0104 0.0078 77 GLU B CG 2902 C CD . GLU B 51 ? 0.7280 0.6671 0.7711 0.0238 -0.0115 0.0075 77 GLU B CD 2903 O OE1 . GLU B 51 ? 0.7655 0.6932 0.8051 0.0159 -0.0116 0.0077 77 GLU B OE1 2904 O OE2 . GLU B 51 ? 0.6591 0.5928 0.7075 0.0332 -0.0124 0.0064 77 GLU B OE2 2905 N N . MET B 52 ? 0.2207 0.2144 0.2507 -0.0070 -0.0089 0.0174 78 MET B N 2906 C CA . MET B 52 ? 0.2005 0.2057 0.2299 -0.0166 -0.0072 0.0154 78 MET B CA 2907 C C . MET B 52 ? 0.2379 0.2428 0.2621 -0.0256 -0.0067 0.0244 78 MET B C 2908 O O . MET B 52 ? 0.2646 0.2810 0.2881 -0.0353 -0.0045 0.0234 78 MET B O 2909 C CB . MET B 52 ? 0.2574 0.2838 0.2894 -0.0138 -0.0067 0.0093 78 MET B CB 2910 C CG . MET B 52 ? 0.2737 0.3015 0.3089 -0.0090 -0.0075 0.0006 78 MET B CG 2911 S SD . MET B 52 ? 0.3149 0.3645 0.3531 -0.0060 -0.0084 -0.0058 78 MET B SD 2912 C CE . MET B 52 ? 0.1879 0.2312 0.2259 0.0015 -0.0109 -0.0115 78 MET B CE 2913 N N . LYS B 53 ? 0.1653 0.1583 0.1855 -0.0230 -0.0089 0.0335 79 LYS B N 2914 C CA . LYS B 53 ? 0.2543 0.2437 0.2669 -0.0324 -0.0092 0.0441 79 LYS B CA 2915 C C . LYS B 53 ? 0.2694 0.2398 0.2791 -0.0425 -0.0091 0.0470 79 LYS B C 2916 O O . LYS B 53 ? 0.2220 0.1765 0.2354 -0.0393 -0.0099 0.0418 79 LYS B O 2917 C CB . LYS B 53 ? 0.2193 0.2005 0.2281 -0.0259 -0.0131 0.0538 79 LYS B CB 2918 C CG . LYS B 53 ? 0.2578 0.2592 0.2680 -0.0191 -0.0131 0.0514 79 LYS B CG 2919 C CD . LYS B 53 ? 0.3887 0.3835 0.3975 -0.0110 -0.0177 0.0589 79 LYS B CD 2920 C CE . LYS B 53 ? 0.2897 0.3048 0.3001 -0.0056 -0.0178 0.0552 79 LYS B CE 2921 N NZ . LYS B 53 ? 0.2768 0.2881 0.2884 0.0031 -0.0226 0.0608 79 LYS B NZ 2922 N N . TRP B 54 ? 0.2421 0.2144 0.2444 -0.0556 -0.0079 0.0549 80 TRP B N 2923 C CA . TRP B 54 ? 0.3326 0.2917 0.3317 -0.0693 -0.0069 0.0568 80 TRP B CA 2924 C C . TRP B 54 ? 0.2804 0.2043 0.2782 -0.0662 -0.0109 0.0599 80 TRP B C 2925 O O . TRP B 54 ? 0.2726 0.1855 0.2733 -0.0707 -0.0102 0.0532 80 TRP B O 2926 C CB . TRP B 54 ? 0.2845 0.2508 0.2735 -0.0844 -0.0051 0.0675 80 TRP B CB 2927 C CG . TRP B 54 ? 0.2711 0.2364 0.2580 -0.1023 -0.0021 0.0671 80 TRP B CG 2928 C CD1 . TRP B 54 ? 0.2894 0.2293 0.2763 -0.1079 -0.0036 0.0662 80 TRP B CD1 2929 C CD2 . TRP B 54 ? 0.3093 0.3012 0.2940 -0.1178 0.0032 0.0669 80 TRP B CD2 2930 N NE1 . TRP B 54 ? 0.3561 0.3047 0.3409 -0.1267 0.0001 0.0660 80 TRP B NE1 2931 C CE2 . TRP B 54 ? 0.3416 0.3234 0.3255 -0.1331 0.0046 0.0665 80 TRP B CE2 2932 C CE3 . TRP B 54 ? 0.2973 0.3217 0.2810 -0.1203 0.0072 0.0660 80 TRP B CE3 2933 C CZ2 . TRP B 54 ? 0.3150 0.3203 0.2979 -0.1516 0.0100 0.0657 80 TRP B CZ2 2934 C CZ3 . TRP B 54 ? 0.2862 0.3345 0.2691 -0.1374 0.0129 0.0644 80 TRP B CZ3 2935 C CH2 . TRP B 54 ? 0.3227 0.3621 0.3054 -0.1531 0.0143 0.0646 80 TRP B CH2 2936 N N . ALA B 55 ? 0.3008 0.2078 0.2949 -0.0579 -0.0155 0.0693 81 ALA B N 2937 C CA . ALA B 55 ? 0.3372 0.2101 0.3308 -0.0524 -0.0202 0.0724 81 ALA B CA 2938 C C . ALA B 55 ? 0.3673 0.2342 0.3707 -0.0426 -0.0194 0.0583 81 ALA B C 2939 O O . ALA B 55 ? 0.3214 0.1619 0.3250 -0.0428 -0.0214 0.0561 81 ALA B O 2940 C CB . ALA B 55 ? 0.3049 0.1680 0.2958 -0.0413 -0.0259 0.0830 81 ALA B CB 2941 N N . TYR B 56 ? 0.2570 0.1474 0.2676 -0.0344 -0.0168 0.0488 82 TYR B N 2942 C CA . TYR B 56 ? 0.2476 0.1356 0.2657 -0.0258 -0.0157 0.0359 82 TYR B CA 2943 C C . TYR B 56 ? 0.2613 0.1592 0.2807 -0.0352 -0.0122 0.0260 82 TYR B C 2944 O O . TYR B 56 ? 0.2688 0.1543 0.2902 -0.0352 -0.0121 0.0176 82 TYR B O 2945 C CB . TYR B 56 ? 0.2805 0.1870 0.3043 -0.0131 -0.0150 0.0314 82 TYR B CB 2946 C CG . TYR B 56 ? 0.3276 0.2287 0.3529 -0.0019 -0.0186 0.0382 82 TYR B CG 2947 C CD1 . TYR B 56 ? 0.3172 0.2258 0.3377 -0.0035 -0.0208 0.0492 82 TYR B CD1 2948 C CD2 . TYR B 56 ? 0.4023 0.2944 0.4343 0.0106 -0.0198 0.0326 82 TYR B CD2 2949 C CE1 . TYR B 56 ? 0.3692 0.2754 0.3916 0.0070 -0.0249 0.0553 82 TYR B CE1 2950 C CE2 . TYR B 56 ? 0.5476 0.4385 0.5830 0.0216 -0.0234 0.0379 82 TYR B CE2 2951 C CZ . TYR B 56 ? 0.5614 0.4592 0.5921 0.0198 -0.0265 0.0496 82 TYR B CZ 2952 O OH . TYR B 56 ? 0.6297 0.5280 0.6643 0.0308 -0.0310 0.0549 82 TYR B OH 2953 N N . ILE B 57 ? 0.2361 0.1582 0.2550 -0.0427 -0.0098 0.0262 83 ILE B N 2954 C CA . ILE B 57 ? 0.2564 0.1942 0.2789 -0.0484 -0.0074 0.0159 83 ILE B CA 2955 C C . ILE B 57 ? 0.2499 0.1808 0.2697 -0.0646 -0.0066 0.0161 83 ILE B C 2956 O O . ILE B 57 ? 0.2520 0.1876 0.2749 -0.0691 -0.0059 0.0067 83 ILE B O 2957 C CB . ILE B 57 ? 0.2150 0.1836 0.2405 -0.0467 -0.0057 0.0137 83 ILE B CB 2958 C CG1 . ILE B 57 ? 0.2684 0.2519 0.2990 -0.0460 -0.0052 0.0020 83 ILE B CG1 2959 C CG2 . ILE B 57 ? 0.1961 0.1776 0.2181 -0.0577 -0.0039 0.0209 83 ILE B CG2 2960 C CD1 . ILE B 57 ? 0.1807 0.1870 0.2147 -0.0380 -0.0052 -0.0013 83 ILE B CD1 2961 N N . GLU B 58 ? 0.2645 0.1845 0.2779 -0.0742 -0.0069 0.0272 84 GLU B N 2962 C CA . GLU B 58 ? 0.2926 0.2001 0.3021 -0.0913 -0.0064 0.0288 84 GLU B CA 2963 C C . GLU B 58 ? 0.3582 0.2301 0.3595 -0.0939 -0.0098 0.0402 84 GLU B C 2964 O O . GLU B 58 ? 0.3671 0.2355 0.3603 -0.1050 -0.0098 0.0523 84 GLU B O 2965 C CB . GLU B 58 ? 0.2740 0.2085 0.2827 -0.1062 -0.0026 0.0311 84 GLU B CB 2966 C CG . GLU B 58 ? 0.2948 0.2235 0.3020 -0.1254 -0.0013 0.0291 84 GLU B CG 2967 C CD . GLU B 58 ? 0.3030 0.2597 0.3096 -0.1420 0.0030 0.0321 84 GLU B CD 2968 O OE1 . GLU B 58 ? 0.3566 0.3385 0.3641 -0.1378 0.0052 0.0343 84 GLU B OE1 2969 O OE2 . GLU B 58 ? 0.3542 0.3085 0.3594 -0.1598 0.0044 0.0314 84 GLU B OE2 2970 N N . PRO B 59 ? 0.4031 0.2480 0.4058 -0.0834 -0.0130 0.0364 85 PRO B N 2971 C CA . PRO B 59 ? 0.3920 0.2012 0.3886 -0.0810 -0.0178 0.0468 85 PRO B CA 2972 C C . PRO B 59 ? 0.4198 0.2034 0.4082 -0.0992 -0.0190 0.0526 85 PRO B C 2973 O O . PRO B 59 ? 0.5070 0.2634 0.4873 -0.1011 -0.0233 0.0656 85 PRO B O 2974 C CB . PRO B 59 ? 0.3889 0.1820 0.3922 -0.0642 -0.0198 0.0366 85 PRO B CB 2975 C CG . PRO B 59 ? 0.3715 0.1837 0.3808 -0.0654 -0.0160 0.0210 85 PRO B CG 2976 C CD . PRO B 59 ? 0.3528 0.2013 0.3632 -0.0720 -0.0125 0.0220 85 PRO B CD 2977 N N . GLU B 60 ? 0.4405 0.2323 0.4309 -0.1126 -0.0158 0.0433 86 GLU B N 2978 C CA . GLU B 60 ? 0.5458 0.3193 0.5285 -0.1339 -0.0159 0.0485 86 GLU B CA 2979 C C . GLU B 60 ? 0.4704 0.2808 0.4560 -0.1498 -0.0104 0.0439 86 GLU B C 2980 O O . GLU B 60 ? 0.3702 0.2121 0.3649 -0.1424 -0.0078 0.0332 86 GLU B O 2981 C CB . GLU B 60 ? 0.5896 0.3334 0.5743 -0.1327 -0.0178 0.0387 86 GLU B CB 2982 C CG . GLU B 60 ? 0.8260 0.5362 0.8098 -0.1155 -0.0223 0.0422 86 GLU B CG 2983 C CD . GLU B 60 ? 1.0649 0.7501 1.0524 -0.1124 -0.0226 0.0299 86 GLU B CD 2984 O OE1 . GLU B 60 ? 1.1005 0.7953 1.0916 -0.1222 -0.0202 0.0176 86 GLU B OE1 2985 O OE2 . GLU B 60 ? 1.1719 0.8298 1.1590 -0.0999 -0.0253 0.0320 86 GLU B OE2 2986 N N . ARG B 61 ? 0.4426 0.2553 0.4230 -0.1667 -0.0081 0.0506 87 ARG B N 2987 C CA . ARG B 61 ? 0.4068 0.2598 0.3912 -0.1800 -0.0027 0.0469 87 ARG B CA 2988 C C . ARG B 61 ? 0.5270 0.3988 0.5222 -0.1820 -0.0014 0.0298 87 ARG B C 2989 O O . ARG B 61 ? 0.4061 0.2589 0.4028 -0.1842 -0.0032 0.0224 87 ARG B O 2990 C CB . ARG B 61 ? 0.4736 0.3255 0.4510 -0.1960 -0.0004 0.0553 87 ARG B CB 2991 C CG . ARG B 61 ? 0.4201 0.3162 0.4015 -0.2074 0.0053 0.0521 87 ARG B CG 2992 C CD . ARG B 61 ? 0.4502 0.3456 0.4220 -0.2229 0.0076 0.0623 87 ARG B CD 2993 N NE . ARG B 61 ? 0.4722 0.4127 0.4483 -0.2315 0.0134 0.0580 87 ARG B NE 2994 C CZ . ARG B 61 ? 0.5292 0.4809 0.4975 -0.2453 0.0167 0.0648 87 ARG B CZ 2995 N NH1 . ARG B 61 ? 0.5386 0.4587 0.4938 -0.2533 0.0145 0.0776 87 ARG B NH1 2996 N NH2 . ARG B 61 ? 0.5087 0.5035 0.4823 -0.2505 0.0219 0.0584 87 ARG B NH2 2997 N N . ASN B 62 ? 0.3755 0.2855 0.3784 -0.1799 0.0013 0.0233 88 ASN B N 2998 C CA . ASN B 62 ? 0.4159 0.3505 0.4298 -0.1783 0.0018 0.0073 88 ASN B CA 2999 C C . ASN B 62 ? 0.3549 0.2693 0.3708 -0.1635 -0.0019 -0.0024 88 ASN B C 3000 O O . ASN B 62 ? 0.3751 0.3008 0.3970 -0.1651 -0.0026 -0.0151 88 ASN B O 3001 C CB . ASN B 62 ? 0.4102 0.3572 0.4271 -0.1934 0.0036 0.0029 88 ASN B CB 3002 C CG . ASN B 62 ? 0.4685 0.4551 0.4975 -0.1922 0.0044 -0.0108 88 ASN B CG 3003 O OD1 . ASN B 62 ? 0.4524 0.4675 0.4880 -0.1836 0.0053 -0.0140 88 ASN B OD1 3004 N ND2 . ASN B 62 ? 0.5044 0.4927 0.5367 -0.1999 0.0033 -0.0188 88 ASN B ND2 3005 N N . GLN B 63 ? 0.3506 0.2378 0.3619 -0.1492 -0.0043 0.0031 89 GLN B N 3006 C CA . GLN B 63 ? 0.3629 0.2358 0.3766 -0.1337 -0.0068 -0.0067 89 GLN B CA 3007 C C . GLN B 63 ? 0.4439 0.3303 0.4606 -0.1141 -0.0068 -0.0050 89 GLN B C 3008 O O . GLN B 63 ? 0.4772 0.3501 0.4902 -0.1062 -0.0078 0.0050 89 GLN B O 3009 C CB . GLN B 63 ? 0.4405 0.2686 0.4479 -0.1336 -0.0098 -0.0046 89 GLN B CB 3010 C CG . GLN B 63 ? 0.5618 0.3724 0.5651 -0.1549 -0.0102 -0.0061 89 GLN B CG 3011 C CD . GLN B 63 ? 0.7003 0.4693 0.7006 -0.1497 -0.0133 -0.0063 89 GLN B CD 3012 O OE1 . GLN B 63 ? 0.7186 0.4690 0.7190 -0.1339 -0.0154 -0.0108 89 GLN B OE1 3013 N NE2 . GLN B 63 ? 0.7900 0.5459 0.7888 -0.1620 -0.0132 -0.0022 89 GLN B NE2 3014 N N . PHE B 64 ? 0.2809 0.1939 0.3038 -0.1067 -0.0062 -0.0145 90 PHE B N 3015 C CA . PHE B 64 ? 0.3633 0.2926 0.3889 -0.0910 -0.0059 -0.0127 90 PHE B CA 3016 C C . PHE B 64 ? 0.2840 0.2013 0.3100 -0.0757 -0.0073 -0.0189 90 PHE B C 3017 O O . PHE B 64 ? 0.3153 0.2252 0.3413 -0.0763 -0.0081 -0.0289 90 PHE B O 3018 C CB . PHE B 64 ? 0.2316 0.1976 0.2634 -0.0920 -0.0049 -0.0178 90 PHE B CB 3019 C CG . PHE B 64 ? 0.2617 0.2457 0.2944 -0.1045 -0.0024 -0.0118 90 PHE B CG 3020 C CD1 . PHE B 64 ? 0.2476 0.2364 0.2812 -0.1222 -0.0013 -0.0142 90 PHE B CD1 3021 C CD2 . PHE B 64 ? 0.2763 0.2732 0.3084 -0.0997 -0.0009 -0.0043 90 PHE B CD2 3022 C CE1 . PHE B 64 ? 0.2500 0.2582 0.2844 -0.1349 0.0019 -0.0090 90 PHE B CE1 3023 C CE2 . PHE B 64 ? 0.2656 0.2812 0.2977 -0.1118 0.0022 0.0004 90 PHE B CE2 3024 C CZ . PHE B 64 ? 0.2384 0.2605 0.2718 -0.1295 0.0039 -0.0018 90 PHE B CZ 3025 N N . ASN B 65 ? 0.2402 0.1573 0.2663 -0.0627 -0.0075 -0.0135 91 ASN B N 3026 C CA . ASN B 65 ? 0.2330 0.1433 0.2602 -0.0486 -0.0080 -0.0191 91 ASN B CA 3027 C C . ASN B 65 ? 0.2067 0.1398 0.2363 -0.0386 -0.0075 -0.0186 91 ASN B C 3028 O O . ASN B 65 ? 0.2003 0.1350 0.2301 -0.0323 -0.0075 -0.0108 91 ASN B O 3029 C CB . ASN B 65 ? 0.2816 0.1644 0.3072 -0.0418 -0.0092 -0.0138 91 ASN B CB 3030 C CG . ASN B 65 ? 0.3098 0.1875 0.3379 -0.0279 -0.0089 -0.0214 91 ASN B CG 3031 O OD1 . ASN B 65 ? 0.2487 0.1419 0.2776 -0.0246 -0.0076 -0.0298 91 ASN B OD1 3032 N ND2 . ASN B 65 ? 0.2924 0.1491 0.3215 -0.0199 -0.0104 -0.0183 91 ASN B ND2 3033 N N . PHE B 66 ? 0.1937 0.1433 0.2245 -0.0374 -0.0076 -0.0268 92 PHE B N 3034 C CA . PHE B 66 ? 0.1719 0.1418 0.2042 -0.0298 -0.0079 -0.0263 92 PHE B CA 3035 C C . PHE B 66 ? 0.1851 0.1508 0.2162 -0.0183 -0.0076 -0.0287 92 PHE B C 3036 O O . PHE B 66 ? 0.2032 0.1821 0.2346 -0.0123 -0.0081 -0.0279 92 PHE B O 3037 C CB . PHE B 66 ? 0.1675 0.1576 0.2015 -0.0339 -0.0095 -0.0326 92 PHE B CB 3038 C CG . PHE B 66 ? 0.1912 0.1943 0.2286 -0.0443 -0.0092 -0.0306 92 PHE B CG 3039 C CD1 . PHE B 66 ? 0.1785 0.1943 0.2181 -0.0436 -0.0082 -0.0243 92 PHE B CD1 3040 C CD2 . PHE B 66 ? 0.2471 0.2512 0.2856 -0.0558 -0.0096 -0.0356 92 PHE B CD2 3041 C CE1 . PHE B 66 ? 0.2433 0.2743 0.2862 -0.0539 -0.0069 -0.0231 92 PHE B CE1 3042 C CE2 . PHE B 66 ? 0.2689 0.2883 0.3114 -0.0667 -0.0087 -0.0341 92 PHE B CE2 3043 C CZ . PHE B 66 ? 0.2347 0.2681 0.2794 -0.0656 -0.0070 -0.0278 92 PHE B CZ 3044 N N . THR B 67 ? 0.1799 0.1275 0.2100 -0.0156 -0.0067 -0.0322 93 THR B N 3045 C CA . THR B 67 ? 0.1761 0.1229 0.2056 -0.0060 -0.0055 -0.0365 93 THR B CA 3046 C C . THR B 67 ? 0.1622 0.1174 0.1938 0.0020 -0.0052 -0.0298 93 THR B C 3047 O O . THR B 67 ? 0.1617 0.1285 0.1917 0.0059 -0.0048 -0.0317 93 THR B O 3048 C CB . THR B 67 ? 0.1952 0.1213 0.2254 -0.0028 -0.0043 -0.0414 93 THR B CB 3049 O OG1 . THR B 67 ? 0.2666 0.1853 0.2938 -0.0107 -0.0046 -0.0498 93 THR B OG1 3050 C CG2 . THR B 67 ? 0.1916 0.1209 0.2224 0.0070 -0.0020 -0.0467 93 THR B CG2 3051 N N . GLY B 68 ? 0.1652 0.1144 0.1993 0.0034 -0.0058 -0.0215 94 GLY B N 3052 C CA . GLY B 68 ? 0.1599 0.1171 0.1962 0.0104 -0.0059 -0.0157 94 GLY B CA 3053 C C . GLY B 68 ? 0.1984 0.1738 0.2334 0.0089 -0.0065 -0.0136 94 GLY B C 3054 O O . GLY B 68 ? 0.1266 0.1108 0.1618 0.0140 -0.0063 -0.0138 94 GLY B O 3055 N N . GLY B 69 ? 0.1360 0.1175 0.1703 0.0017 -0.0073 -0.0121 95 GLY B N 3056 C CA . GLY B 69 ? 0.1224 0.1209 0.1567 0.0013 -0.0082 -0.0115 95 GLY B CA 3057 C C . GLY B 69 ? 0.1643 0.1698 0.1969 0.0037 -0.0093 -0.0180 95 GLY B C 3058 O O . GLY B 69 ? 0.1802 0.1943 0.2120 0.0075 -0.0105 -0.0175 95 GLY B O 3059 N N . ASP B 70 ? 0.1230 0.1233 0.1537 0.0009 -0.0093 -0.0238 96 ASP B N 3060 C CA . ASP B 70 ? 0.1368 0.1425 0.1637 0.0024 -0.0110 -0.0293 96 ASP B CA 3061 C C . ASP B 70 ? 0.1887 0.1925 0.2123 0.0085 -0.0098 -0.0290 96 ASP B C 3062 O O . ASP B 70 ? 0.1456 0.1555 0.1649 0.0102 -0.0119 -0.0296 96 ASP B O 3063 C CB . ASP B 70 ? 0.1513 0.1517 0.1759 -0.0026 -0.0110 -0.0361 96 ASP B CB 3064 C CG . ASP B 70 ? 0.2599 0.2681 0.2874 -0.0101 -0.0130 -0.0378 96 ASP B CG 3065 O OD1 . ASP B 70 ? 0.2419 0.2610 0.2735 -0.0108 -0.0139 -0.0341 96 ASP B OD1 3066 O OD2 . ASP B 70 ? 0.2074 0.2125 0.2336 -0.0157 -0.0135 -0.0438 96 ASP B OD2 3067 N N . ILE B 71 ? 0.1354 0.1308 0.1609 0.0116 -0.0069 -0.0280 97 ILE B N 3068 C CA . ILE B 71 ? 0.1191 0.1163 0.1431 0.0164 -0.0050 -0.0284 97 ILE B CA 3069 C C . ILE B 71 ? 0.1505 0.1556 0.1750 0.0185 -0.0065 -0.0228 97 ILE B C 3070 O O . ILE B 71 ? 0.1056 0.1151 0.1256 0.0192 -0.0069 -0.0230 97 ILE B O 3071 C CB . ILE B 71 ? 0.1538 0.1431 0.1827 0.0207 -0.0020 -0.0294 97 ILE B CB 3072 C CG1 . ILE B 71 ? 0.1786 0.1580 0.2063 0.0191 -0.0005 -0.0371 97 ILE B CG1 3073 C CG2 . ILE B 71 ? 0.1383 0.1343 0.1677 0.0251 0.0003 -0.0299 97 ILE B CG2 3074 C CD1 . ILE B 71 ? 0.1510 0.1197 0.1847 0.0248 0.0015 -0.0392 97 ILE B CD1 3075 N N . VAL B 72 ? 0.1043 0.1108 0.1331 0.0188 -0.0074 -0.0177 98 VAL B N 3076 C CA . VAL B 72 ? 0.1679 0.1819 0.1970 0.0205 -0.0088 -0.0138 98 VAL B CA 3077 C C . VAL B 72 ? 0.1569 0.1761 0.1822 0.0192 -0.0119 -0.0155 98 VAL B C 3078 O O . VAL B 72 ? 0.1000 0.1211 0.1222 0.0207 -0.0134 -0.0148 98 VAL B O 3079 C CB . VAL B 72 ? 0.1747 0.1907 0.2078 0.0202 -0.0092 -0.0085 98 VAL B CB 3080 C CG1 . VAL B 72 ? 0.1274 0.1519 0.1599 0.0213 -0.0109 -0.0065 98 VAL B CG1 3081 C CG2 . VAL B 72 ? 0.1419 0.1518 0.1785 0.0231 -0.0079 -0.0055 98 VAL B CG2 3082 N N . ALA B 73 ? 0.0938 0.1151 0.1198 0.0164 -0.0134 -0.0179 99 ALA B N 3083 C CA . ALA B 73 ? 0.2174 0.2453 0.2418 0.0168 -0.0173 -0.0202 99 ALA B CA 3084 C C . ALA B 73 ? 0.1652 0.1895 0.1823 0.0178 -0.0195 -0.0219 99 ALA B C 3085 O O . ALA B 73 ? 0.1291 0.1546 0.1430 0.0202 -0.0235 -0.0213 99 ALA B O 3086 C CB . ALA B 73 ? 0.0935 0.1274 0.1216 0.0130 -0.0182 -0.0232 99 ALA B CB 3087 N N . ALA B 74 ? 0.1022 0.1215 0.1158 0.0158 -0.0172 -0.0242 100 ALA B N 3088 C CA . ALA B 74 ? 0.1649 0.1820 0.1694 0.0153 -0.0186 -0.0255 100 ALA B CA 3089 C C . ALA B 74 ? 0.1828 0.1977 0.1832 0.0166 -0.0176 -0.0217 100 ALA B C 3090 O O . ALA B 74 ? 0.1409 0.1539 0.1331 0.0160 -0.0209 -0.0200 100 ALA B O 3091 C CB . ALA B 74 ? 0.1557 0.1696 0.1573 0.0126 -0.0153 -0.0304 100 ALA B CB 3092 N N . PHE B 75 ? 0.1058 0.1208 0.1115 0.0177 -0.0134 -0.0202 101 PHE B N 3093 C CA . PHE B 75 ? 0.1488 0.1644 0.1524 0.0177 -0.0123 -0.0171 101 PHE B CA 3094 C C . PHE B 75 ? 0.1039 0.1184 0.1059 0.0186 -0.0172 -0.0139 101 PHE B C 3095 O O . PHE B 75 ? 0.1546 0.1654 0.1495 0.0169 -0.0192 -0.0117 101 PHE B O 3096 C CB . PHE B 75 ? 0.0983 0.1168 0.1102 0.0196 -0.0083 -0.0162 101 PHE B CB 3097 C CG . PHE B 75 ? 0.1415 0.1637 0.1526 0.0185 -0.0066 -0.0142 101 PHE B CG 3098 C CD1 . PHE B 75 ? 0.1719 0.1975 0.1799 0.0163 -0.0026 -0.0165 101 PHE B CD1 3099 C CD2 . PHE B 75 ? 0.1786 0.2027 0.1919 0.0187 -0.0088 -0.0108 101 PHE B CD2 3100 C CE1 . PHE B 75 ? 0.2186 0.2502 0.2265 0.0137 -0.0006 -0.0149 101 PHE B CE1 3101 C CE2 . PHE B 75 ? 0.1031 0.1313 0.1158 0.0161 -0.0073 -0.0093 101 PHE B CE2 3102 C CZ . PHE B 75 ? 0.1568 0.1893 0.1672 0.0133 -0.0032 -0.0111 101 PHE B CZ 3103 N N . SER B 76 ? 0.1034 0.1207 0.1117 0.0210 -0.0190 -0.0142 102 SER B N 3104 C CA A SER B 76 ? 0.1434 0.1609 0.1518 0.0232 -0.0234 -0.0135 102 SER B CA 3105 C CA B SER B 76 ? 0.1504 0.1680 0.1589 0.0232 -0.0234 -0.0135 102 SER B CA 3106 C C . SER B 76 ? 0.1531 0.1662 0.1548 0.0243 -0.0292 -0.0141 102 SER B C 3107 O O . SER B 76 ? 0.1703 0.1769 0.1670 0.0253 -0.0331 -0.0123 102 SER B O 3108 C CB A SER B 76 ? 0.1633 0.1882 0.1798 0.0248 -0.0231 -0.0148 102 SER B CB 3109 C CB B SER B 76 ? 0.1680 0.1931 0.1846 0.0248 -0.0232 -0.0150 102 SER B CB 3110 O OG A SER B 76 ? 0.1687 0.1959 0.1895 0.0237 -0.0188 -0.0128 102 SER B OG 3111 O OG B SER B 76 ? 0.0879 0.1154 0.1056 0.0279 -0.0272 -0.0167 102 SER B OG 3112 N N . ALA B 77 ? 0.1412 0.1568 0.1423 0.0239 -0.0303 -0.0166 103 ALA B N 3113 C CA . ALA B 77 ? 0.1677 0.1807 0.1625 0.0256 -0.0371 -0.0169 103 ALA B CA 3114 C C . ALA B 77 ? 0.2122 0.2153 0.1941 0.0228 -0.0386 -0.0128 103 ALA B C 3115 O O . ALA B 77 ? 0.1717 0.1672 0.1468 0.0248 -0.0453 -0.0101 103 ALA B O 3116 C CB . ALA B 77 ? 0.1341 0.1537 0.1303 0.0242 -0.0378 -0.0207 103 ALA B CB 3117 N N . ALA B 78 ? 0.1261 0.1293 0.1043 0.0180 -0.0326 -0.0125 104 ALA B N 3118 C CA . ALA B 78 ? 0.1522 0.1492 0.1174 0.0132 -0.0324 -0.0090 104 ALA B CA 3119 C C . ALA B 78 ? 0.2066 0.1956 0.1684 0.0123 -0.0343 -0.0042 104 ALA B C 3120 O O . ALA B 78 ? 0.1881 0.1682 0.1375 0.0088 -0.0380 0.0005 104 ALA B O 3121 C CB . ALA B 78 ? 0.1944 0.1969 0.1593 0.0089 -0.0242 -0.0116 104 ALA B CB 3122 N N . ASN B 79 ? 0.1496 0.1414 0.1215 0.0145 -0.0321 -0.0051 105 ASN B N 3123 C CA . ASN B 79 ? 0.1773 0.1624 0.1472 0.0129 -0.0334 -0.0020 105 ASN B CA 3124 C C . ASN B 79 ? 0.1687 0.1467 0.1406 0.0186 -0.0406 -0.0025 105 ASN B C 3125 O O . ASN B 79 ? 0.2347 0.2058 0.2057 0.0177 -0.0422 -0.0013 105 ASN B O 3126 C CB . ASN B 79 ? 0.1905 0.1844 0.1698 0.0117 -0.0270 -0.0033 105 ASN B CB 3127 C CG . ASN B 79 ? 0.2747 0.2744 0.2516 0.0061 -0.0206 -0.0028 105 ASN B CG 3128 O OD1 . ASN B 79 ? 0.2552 0.2516 0.2244 -0.0002 -0.0200 0.0003 105 ASN B OD1 3129 N ND2 . ASN B 79 ? 0.2048 0.2131 0.1885 0.0081 -0.0158 -0.0063 105 ASN B ND2 3130 N N . ASP B 80 ? 0.1822 0.1630 0.1574 0.0244 -0.0449 -0.0052 106 ASP B N 3131 C CA . ASP B 80 ? 0.2027 0.1806 0.1824 0.0318 -0.0516 -0.0078 106 ASP B CA 3132 C C . ASP B 80 ? 0.2146 0.1989 0.2043 0.0338 -0.0484 -0.0116 106 ASP B C 3133 O O . ASP B 80 ? 0.1889 0.1669 0.1796 0.0377 -0.0527 -0.0136 106 ASP B O 3134 C CB . ASP B 80 ? 0.3992 0.3585 0.3676 0.0324 -0.0595 -0.0035 106 ASP B CB 3135 C CG . ASP B 80 ? 0.7472 0.7035 0.7177 0.0417 -0.0688 -0.0060 106 ASP B CG 3136 O OD1 . ASP B 80 ? 0.9382 0.9052 0.9122 0.0445 -0.0702 -0.0081 106 ASP B OD1 3137 O OD2 . ASP B 80 ? 0.9083 0.8524 0.8781 0.0467 -0.0750 -0.0066 106 ASP B OD2 3138 N N . TYR B 81 ? 0.1342 0.1305 0.1308 0.0313 -0.0414 -0.0127 107 TYR B N 3139 C CA . TYR B 81 ? 0.1399 0.1441 0.1444 0.0321 -0.0382 -0.0153 107 TYR B CA 3140 C C . TYR B 81 ? 0.2357 0.2496 0.2483 0.0377 -0.0401 -0.0208 107 TYR B C 3141 O O . TYR B 81 ? 0.1277 0.1470 0.1429 0.0401 -0.0418 -0.0228 107 TYR B O 3142 C CB . TYR B 81 ? 0.1140 0.1271 0.1228 0.0284 -0.0314 -0.0137 107 TYR B CB 3143 C CG . TYR B 81 ? 0.1509 0.1614 0.1566 0.0237 -0.0280 -0.0102 107 TYR B CG 3144 C CD1 . TYR B 81 ? 0.1379 0.1388 0.1361 0.0205 -0.0301 -0.0081 107 TYR B CD1 3145 C CD2 . TYR B 81 ? 0.1979 0.2161 0.2089 0.0223 -0.0229 -0.0091 107 TYR B CD2 3146 C CE1 . TYR B 81 ? 0.1697 0.1725 0.1667 0.0151 -0.0263 -0.0056 107 TYR B CE1 3147 C CE2 . TYR B 81 ? 0.2618 0.2816 0.2725 0.0190 -0.0198 -0.0071 107 TYR B CE2 3148 C CZ . TYR B 81 ? 0.2506 0.2646 0.2549 0.0151 -0.0211 -0.0057 107 TYR B CZ 3149 O OH . TYR B 81 ? 0.2818 0.3015 0.2875 0.0110 -0.0174 -0.0045 107 TYR B OH 3150 N N . VAL B 82 ? 0.1011 0.1200 0.1178 0.0389 -0.0390 -0.0238 108 VAL B N 3151 C CA . VAL B 82 ? 0.1790 0.2132 0.2039 0.0417 -0.0376 -0.0291 108 VAL B CA 3152 C C . VAL B 82 ? 0.1874 0.2319 0.2155 0.0366 -0.0314 -0.0261 108 VAL B C 3153 O O . VAL B 82 ? 0.1365 0.1811 0.1634 0.0332 -0.0281 -0.0227 108 VAL B O 3154 C CB . VAL B 82 ? 0.1539 0.1910 0.1808 0.0444 -0.0384 -0.0343 108 VAL B CB 3155 C CG1 . VAL B 82 ? 0.1342 0.1906 0.1690 0.0463 -0.0359 -0.0403 108 VAL B CG1 3156 C CG2 . VAL B 82 ? 0.1524 0.1750 0.1759 0.0499 -0.0454 -0.0374 108 VAL B CG2 3157 N N . LEU B 83 ? 0.1239 0.1759 0.1558 0.0360 -0.0304 -0.0270 109 LEU B N 3158 C CA . LEU B 83 ? 0.0770 0.1342 0.1107 0.0306 -0.0253 -0.0236 109 LEU B CA 3159 C C . LEU B 83 ? 0.0993 0.1717 0.1381 0.0286 -0.0226 -0.0258 109 LEU B C 3160 O O . LEU B 83 ? 0.1194 0.2031 0.1633 0.0304 -0.0238 -0.0314 109 LEU B O 3161 C CB . LEU B 83 ? 0.1360 0.1903 0.1694 0.0287 -0.0256 -0.0230 109 LEU B CB 3162 C CG . LEU B 83 ? 0.1267 0.1825 0.1618 0.0231 -0.0212 -0.0203 109 LEU B CG 3163 C CD1 . LEU B 83 ? 0.1212 0.1687 0.1536 0.0218 -0.0183 -0.0150 109 LEU B CD1 3164 C CD2 . LEU B 83 ? 0.1453 0.1985 0.1797 0.0212 -0.0222 -0.0221 109 LEU B CD2 3165 N N . ARG B 84 ? 0.0800 0.1542 0.1176 0.0246 -0.0190 -0.0213 110 ARG B N 3166 C CA . ARG B 84 ? 0.1111 0.1991 0.1508 0.0205 -0.0159 -0.0215 110 ARG B CA 3167 C C . ARG B 84 ? 0.1467 0.2322 0.1860 0.0140 -0.0130 -0.0158 110 ARG B C 3168 O O . ARG B 84 ? 0.1522 0.2260 0.1888 0.0132 -0.0125 -0.0099 110 ARG B O 3169 C CB . ARG B 84 ? 0.1257 0.2178 0.1622 0.0200 -0.0149 -0.0199 110 ARG B CB 3170 C CG . ARG B 84 ? 0.2466 0.3395 0.2829 0.0254 -0.0177 -0.0263 110 ARG B CG 3171 C CD . ARG B 84 ? 0.1977 0.2979 0.2305 0.0234 -0.0165 -0.0260 110 ARG B CD 3172 N NE . ARG B 84 ? 0.1451 0.2638 0.1793 0.0214 -0.0138 -0.0310 110 ARG B NE 3173 C CZ . ARG B 84 ? 0.2356 0.3644 0.2675 0.0146 -0.0102 -0.0262 110 ARG B CZ 3174 N NH1 . ARG B 84 ? 0.1928 0.3126 0.2213 0.0104 -0.0096 -0.0159 110 ARG B NH1 3175 N NH2 . ARG B 84 ? 0.1820 0.3301 0.2149 0.0119 -0.0071 -0.0318 110 ARG B NH2 3176 N N . GLY B 85 ? 0.0964 0.1929 0.1391 0.0093 -0.0113 -0.0180 111 GLY B N 3177 C CA . GLY B 85 ? 0.0944 0.1869 0.1360 0.0015 -0.0087 -0.0127 111 GLY B CA 3178 C C . GLY B 85 ? 0.2089 0.3054 0.2461 -0.0040 -0.0061 -0.0063 111 GLY B C 3179 O O . GLY B 85 ? 0.1986 0.3104 0.2357 -0.0046 -0.0048 -0.0090 111 GLY B O 3180 N N . HIS B 86 ? 0.2044 0.2871 0.2377 -0.0077 -0.0057 0.0019 112 HIS B N 3181 C CA . HIS B 86 ? 0.2488 0.3312 0.2761 -0.0114 -0.0050 0.0101 112 HIS B CA 3182 C C . HIS B 86 ? 0.2142 0.2788 0.2382 -0.0162 -0.0053 0.0187 112 HIS B C 3183 O O . HIS B 86 ? 0.2339 0.2827 0.2597 -0.0111 -0.0070 0.0194 112 HIS B O 3184 C CB . HIS B 86 ? 0.2705 0.3514 0.2964 -0.0039 -0.0073 0.0108 112 HIS B CB 3185 C CG . HIS B 86 ? 0.2920 0.3694 0.3120 -0.0057 -0.0084 0.0203 112 HIS B CG 3186 N ND1 . HIS B 86 ? 0.3941 0.4854 0.4087 -0.0091 -0.0078 0.0221 112 HIS B ND1 3187 C CD2 . HIS B 86 ? 0.3696 0.4318 0.3882 -0.0035 -0.0107 0.0281 112 HIS B CD2 3188 C CE1 . HIS B 86 ? 0.3775 0.4621 0.3868 -0.0096 -0.0102 0.0318 112 HIS B CE1 3189 N NE2 . HIS B 86 ? 0.3919 0.4587 0.4044 -0.0055 -0.0123 0.0355 112 HIS B NE2 3190 N N . ASN B 87 ? 0.1960 0.2627 0.2154 -0.0263 -0.0034 0.0246 113 ASN B N 3191 C CA . ASN B 87 ? 0.2647 0.3533 0.2828 -0.0342 0.0000 0.0223 113 ASN B CA 3192 C C . ASN B 87 ? 0.2416 0.3279 0.2582 -0.0468 0.0024 0.0254 113 ASN B C 3193 O O . ASN B 87 ? 0.2198 0.2845 0.2350 -0.0486 0.0007 0.0302 113 ASN B O 3194 C CB . ASN B 87 ? 0.2723 0.3694 0.2825 -0.0359 0.0001 0.0284 113 ASN B CB 3195 C CG . ASN B 87 ? 0.3287 0.4070 0.3304 -0.0391 -0.0026 0.0421 113 ASN B CG 3196 O OD1 . ASN B 87 ? 0.3340 0.3994 0.3323 -0.0471 -0.0024 0.0485 113 ASN B OD1 3197 N ND2 . ASN B 87 ? 0.3898 0.4657 0.3881 -0.0326 -0.0059 0.0465 113 ASN B ND2 3198 N N . LEU B 88 ? 0.1456 0.2539 0.1625 -0.0559 0.0064 0.0222 114 LEU B N 3199 C CA . LEU B 88 ? 0.1942 0.3030 0.2115 -0.0690 0.0089 0.0233 114 LEU B CA 3200 C C . LEU B 88 ? 0.3076 0.4122 0.3135 -0.0835 0.0109 0.0356 114 LEU B C 3201 O O . LEU B 88 ? 0.3579 0.4451 0.3602 -0.0931 0.0106 0.0417 114 LEU B O 3202 C CB . LEU B 88 ? 0.1588 0.2968 0.1859 -0.0712 0.0122 0.0110 114 LEU B CB 3203 C CG . LEU B 88 ? 0.1513 0.2900 0.1886 -0.0581 0.0089 0.0002 114 LEU B CG 3204 C CD1 . LEU B 88 ? 0.1524 0.3218 0.2004 -0.0573 0.0108 -0.0120 114 LEU B CD1 3205 C CD2 . LEU B 88 ? 0.1680 0.2848 0.2066 -0.0585 0.0062 0.0011 114 LEU B CD2 3206 N N . VAL B 89 ? 0.1816 0.3013 0.1805 -0.0857 0.0127 0.0391 115 VAL B N 3207 C CA . VAL B 89 ? 0.2700 0.3897 0.2558 -0.1008 0.0148 0.0513 115 VAL B CA 3208 C C . VAL B 89 ? 0.2911 0.4036 0.2661 -0.0957 0.0114 0.0610 115 VAL B C 3209 O O . VAL B 89 ? 0.3233 0.4563 0.2980 -0.0906 0.0126 0.0556 115 VAL B O 3210 C CB . VAL B 89 ? 0.2591 0.4140 0.2456 -0.1132 0.0220 0.0451 115 VAL B CB 3211 C CG1 . VAL B 89 ? 0.2999 0.4559 0.2698 -0.1307 0.0245 0.0591 115 VAL B CG1 3212 C CG2 . VAL B 89 ? 0.2338 0.3995 0.2325 -0.1187 0.0248 0.0352 115 VAL B CG2 3213 N N . TRP B 90 ? 0.2291 0.3123 0.1955 -0.0967 0.0064 0.0747 116 TRP B N 3214 C CA . TRP B 90 ? 0.2358 0.3093 0.1935 -0.0899 0.0012 0.0845 116 TRP B CA 3215 C C . TRP B 90 ? 0.2850 0.3305 0.2300 -0.0979 -0.0033 0.1021 116 TRP B C 3216 O O . TRP B 90 ? 0.2922 0.3147 0.2393 -0.1010 -0.0045 0.1045 116 TRP B O 3217 C CB . TRP B 90 ? 0.2172 0.2805 0.1851 -0.0714 -0.0033 0.0784 116 TRP B CB 3218 C CG . TRP B 90 ? 0.3104 0.3711 0.2726 -0.0632 -0.0085 0.0853 116 TRP B CG 3219 C CD1 . TRP B 90 ? 0.3461 0.4227 0.2973 -0.0679 -0.0086 0.0907 116 TRP B CD1 3220 C CD2 . TRP B 90 ? 0.2294 0.2731 0.1971 -0.0493 -0.0144 0.0867 116 TRP B CD2 3221 N NE1 . TRP B 90 ? 0.2800 0.3501 0.2297 -0.0576 -0.0150 0.0957 116 TRP B NE1 3222 C CE2 . TRP B 90 ? 0.2776 0.3283 0.2382 -0.0460 -0.0184 0.0933 116 TRP B CE2 3223 C CE3 . TRP B 90 ? 0.2641 0.2894 0.2422 -0.0396 -0.0164 0.0824 116 TRP B CE3 3224 C CZ2 . TRP B 90 ? 0.3262 0.3672 0.2912 -0.0333 -0.0246 0.0957 116 TRP B CZ2 3225 C CZ3 . TRP B 90 ? 0.3175 0.3336 0.2996 -0.0270 -0.0217 0.0844 116 TRP B CZ3 3226 C CH2 . TRP B 90 ? 0.3678 0.3923 0.3442 -0.0239 -0.0259 0.0911 116 TRP B CH2 3227 N N . TYR B 91 ? 0.3312 0.3771 0.2624 -0.1009 -0.0064 0.1143 117 TYR B N 3228 C CA . TYR B 91 ? 0.3404 0.3581 0.2578 -0.1087 -0.0119 0.1327 117 TYR B CA 3229 C C . TYR B 91 ? 0.3487 0.3337 0.2711 -0.0936 -0.0205 0.1376 117 TYR B C 3230 O O . TYR B 91 ? 0.4346 0.3895 0.3495 -0.0974 -0.0256 0.1502 117 TYR B O 3231 C CB . TYR B 91 ? 0.3415 0.3709 0.2433 -0.1148 -0.0133 0.1419 117 TYR B CB 3232 C CG . TYR B 91 ? 0.3312 0.3596 0.2307 -0.1010 -0.0205 0.1464 117 TYR B CG 3233 C CD1 . TYR B 91 ? 0.3033 0.3566 0.2093 -0.0922 -0.0188 0.1364 117 TYR B CD1 3234 C CD2 . TYR B 91 ? 0.4685 0.4723 0.3605 -0.0963 -0.0290 0.1588 117 TYR B CD2 3235 C CE1 . TYR B 91 ? 0.4587 0.5132 0.3631 -0.0809 -0.0256 0.1398 117 TYR B CE1 3236 C CE2 . TYR B 91 ? 0.5264 0.5325 0.4180 -0.0837 -0.0356 0.1615 117 TYR B CE2 3237 C CZ . TYR B 91 ? 0.4803 0.5123 0.3784 -0.0766 -0.0339 0.1518 117 TYR B CZ 3238 O OH . TYR B 91 ? 0.4579 0.4938 0.3569 -0.0650 -0.0405 0.1531 117 TYR B OH 3239 N N . GLN B 92 ? 0.3455 0.3363 0.2806 -0.0766 -0.0221 0.1275 118 GLN B N 3240 C CA . GLN B 92 ? 0.3888 0.3538 0.3312 -0.0617 -0.0291 0.1294 118 GLN B CA 3241 C C . GLN B 92 ? 0.3561 0.3115 0.3130 -0.0555 -0.0264 0.1165 118 GLN B C 3242 O O . GLN B 92 ? 0.3015 0.2751 0.2653 -0.0587 -0.0199 0.1041 118 GLN B O 3243 C CB . GLN B 92 ? 0.3889 0.3662 0.3352 -0.0476 -0.0333 0.1279 118 GLN B CB 3244 C CG . GLN B 92 ? 0.5461 0.5329 0.4771 -0.0532 -0.0371 0.1407 118 GLN B CG 3245 C CD . GLN B 92 ? 0.6845 0.6690 0.6176 -0.0391 -0.0455 0.1456 118 GLN B CD 3246 O OE1 . GLN B 92 ? 0.8587 0.8314 0.7821 -0.0389 -0.0520 0.1575 118 GLN B OE1 3247 N NE2 . GLN B 92 ? 0.7272 0.7240 0.6744 -0.0267 -0.0447 0.1330 118 GLN B NE2 3248 N N . GLU B 93 ? 0.3868 0.3143 0.3482 -0.0460 -0.0319 0.1192 119 GLU B N 3249 C CA . GLU B 93 ? 0.4379 0.3538 0.4116 -0.0394 -0.0301 0.1073 119 GLU B CA 3250 C C . GLU B 93 ? 0.4024 0.3183 0.3747 -0.0542 -0.0244 0.1028 119 GLU B C 3251 O O . GLU B 93 ? 0.3885 0.3149 0.3699 -0.0532 -0.0199 0.0895 119 GLU B O 3252 C CB . GLU B 93 ? 0.4145 0.3503 0.4006 -0.0267 -0.0278 0.0938 119 GLU B CB 3253 C CG . GLU B 93 ? 0.5716 0.5067 0.5613 -0.0123 -0.0336 0.0975 119 GLU B CG 3254 C CD . GLU B 93 ? 0.6199 0.5709 0.6217 -0.0011 -0.0315 0.0847 119 GLU B CD 3255 O OE1 . GLU B 93 ? 0.5261 0.4985 0.5277 0.0010 -0.0312 0.0834 119 GLU B OE1 3256 O OE2 . GLU B 93 ? 0.6235 0.5652 0.6338 0.0050 -0.0301 0.0761 119 GLU B OE2 3257 N N . LEU B 94 ? 0.3833 0.2876 0.3431 -0.0687 -0.0252 0.1148 120 LEU B N 3258 C CA . LEU B 94 ? 0.4845 0.3883 0.4415 -0.0858 -0.0202 0.1128 120 LEU B CA 3259 C C . LEU B 94 ? 0.4370 0.3029 0.3933 -0.0877 -0.0240 0.1155 120 LEU B C 3260 O O . LEU B 94 ? 0.4642 0.3019 0.4145 -0.0827 -0.0310 0.1268 120 LEU B O 3261 C CB . LEU B 94 ? 0.4188 0.3352 0.3614 -0.1031 -0.0180 0.1243 120 LEU B CB 3262 C CG . LEU B 94 ? 0.4742 0.4001 0.4132 -0.1240 -0.0116 0.1227 120 LEU B CG 3263 C CD1 . LEU B 94 ? 0.4614 0.4198 0.4141 -0.1222 -0.0049 0.1049 120 LEU B CD1 3264 C CD2 . LEU B 94 ? 0.4042 0.3432 0.3279 -0.1381 -0.0097 0.1342 120 LEU B CD2 3265 N N . ALA B 95 ? 0.3931 0.2579 0.3558 -0.0940 -0.0200 0.1046 121 ALA B N 3266 C CA . ALA B 95 ? 0.3805 0.2093 0.3418 -0.0981 -0.0231 0.1056 121 ALA B CA 3267 C C . ALA B 95 ? 0.5291 0.3377 0.4749 -0.1132 -0.0256 0.1221 121 ALA B C 3268 O O . ALA B 95 ? 0.4415 0.2717 0.3804 -0.1281 -0.0208 0.1257 121 ALA B O 3269 C CB . ALA B 95 ? 0.3837 0.2197 0.3525 -0.1060 -0.0181 0.0915 121 ALA B CB 3270 N N . PRO B 96 ? 0.5758 0.3511 0.5186 -0.1044 -0.0313 0.1271 122 PRO B N 3271 C CA . PRO B 96 ? 0.6219 0.3799 0.5517 -0.1121 -0.0333 0.1395 122 PRO B CA 3272 C C . PRO B 96 ? 0.6274 0.3875 0.5517 -0.1338 -0.0280 0.1392 122 PRO B C 3273 O O . PRO B 96 ? 0.7566 0.5152 0.6687 -0.1444 -0.0280 0.1503 122 PRO B O 3274 C CB . PRO B 96 ? 0.6900 0.4111 0.6230 -0.0971 -0.0396 0.1394 122 PRO B CB 3275 C CG . PRO B 96 ? 0.6388 0.3659 0.5843 -0.0777 -0.0418 0.1307 122 PRO B CG 3276 C CD . PRO B 96 ? 0.5511 0.3052 0.5037 -0.0848 -0.0362 0.1205 122 PRO B CD 3277 N N . TRP B 97 ? 0.5946 0.3596 0.5276 -0.1404 -0.0237 0.1264 123 TRP B N 3278 C CA . TRP B 97 ? 0.5078 0.2772 0.4376 -0.1606 -0.0188 0.1247 123 TRP B CA 3279 C C . TRP B 97 ? 0.5083 0.3171 0.4339 -0.1744 -0.0127 0.1268 123 TRP B C 3280 O O . TRP B 97 ? 0.5446 0.3587 0.4637 -0.1909 -0.0095 0.1301 123 TRP B O 3281 C CB . TRP B 97 ? 0.5083 0.2760 0.4495 -0.1634 -0.0163 0.1090 123 TRP B CB 3282 C CG . TRP B 97 ? 0.4915 0.2886 0.4438 -0.1588 -0.0132 0.0968 123 TRP B CG 3283 C CD1 . TRP B 97 ? 0.4464 0.2373 0.4069 -0.1426 -0.0162 0.0894 123 TRP B CD1 3284 C CD2 . TRP B 97 ? 0.4304 0.2680 0.3875 -0.1700 -0.0068 0.0898 123 TRP B CD2 3285 N NE1 . TRP B 97 ? 0.4871 0.3123 0.4567 -0.1422 -0.0120 0.0783 123 TRP B NE1 3286 C CE2 . TRP B 97 ? 0.4710 0.3237 0.4387 -0.1602 -0.0066 0.0791 123 TRP B CE2 3287 C CE3 . TRP B 97 ? 0.4613 0.3251 0.4155 -0.1865 -0.0013 0.0908 123 TRP B CE3 3288 C CZ2 . TRP B 97 ? 0.4081 0.3029 0.3850 -0.1626 -0.0010 0.0682 123 TRP B CZ2 3289 C CZ3 . TRP B 97 ? 0.4612 0.3664 0.4248 -0.1905 0.0042 0.0802 123 TRP B CZ3 3290 C CH2 . TRP B 97 ? 0.4464 0.3658 0.4212 -0.1796 0.0040 0.0696 123 TRP B CH2 3291 N N . VAL B 98 ? 0.4599 0.2970 0.3896 -0.1672 -0.0111 0.1242 124 VAL B N 3292 C CA . VAL B 98 ? 0.4976 0.3757 0.4255 -0.1776 -0.0047 0.1230 124 VAL B CA 3293 C C . VAL B 98 ? 0.5432 0.4226 0.4556 -0.1850 -0.0053 0.1367 124 VAL B C 3294 O O . VAL B 98 ? 0.5539 0.4565 0.4620 -0.1998 0.0001 0.1363 124 VAL B O 3295 C CB . VAL B 98 ? 0.4452 0.3515 0.3814 -0.1666 -0.0031 0.1168 124 VAL B CB 3296 C CG1 . VAL B 98 ? 0.3871 0.3381 0.3239 -0.1758 0.0042 0.1119 124 VAL B CG1 3297 C CG2 . VAL B 98 ? 0.3809 0.2843 0.3311 -0.1593 -0.0034 0.1041 124 VAL B CG2 3298 N N . GLU B 99 ? 0.5915 0.4471 0.4960 -0.1744 -0.0121 0.1482 125 GLU B N 3299 C CA . GLU B 99 ? 0.6513 0.5107 0.5407 -0.1795 -0.0137 0.1612 125 GLU B CA 3300 C C . GLU B 99 ? 0.6620 0.4997 0.5399 -0.1942 -0.0145 0.1703 125 GLU B C 3301 O O . GLU B 99 ? 0.7946 0.6304 0.6584 -0.1996 -0.0166 0.1824 125 GLU B O 3302 C CB . GLU B 99 ? 0.7285 0.5728 0.6144 -0.1620 -0.0214 0.1698 125 GLU B CB 3303 C CG . GLU B 99 ? 0.7992 0.6743 0.6906 -0.1522 -0.0201 0.1647 125 GLU B CG 3304 C CD . GLU B 99 ? 0.9318 0.7909 0.8254 -0.1321 -0.0282 0.1693 125 GLU B CD 3305 O OE1 . GLU B 99 ? 1.0043 0.8289 0.8972 -0.1243 -0.0345 0.1746 125 GLU B OE1 3306 O OE2 . GLU B 99 ? 0.9688 0.8511 0.8658 -0.1236 -0.0281 0.1666 125 GLU B OE2 3307 N N . THR B 100 ? 0.7169 0.5384 0.6003 -0.2011 -0.0130 0.1645 126 THR B N 3308 C CA . THR B 100 ? 0.8356 0.6378 0.7090 -0.2170 -0.0131 0.1720 126 THR B CA 3309 C C . THR B 100 ? 0.7899 0.6230 0.6657 -0.2361 -0.0049 0.1639 126 THR B C 3310 O O . THR B 100 ? 0.7960 0.6181 0.6654 -0.2517 -0.0038 0.1677 126 THR B O 3311 C CB . THR B 100 ? 0.9047 0.6636 0.7818 -0.2120 -0.0179 0.1713 126 THR B CB 3312 O OG1 . THR B 100 ? 0.9729 0.7396 0.8633 -0.2163 -0.0135 0.1562 126 THR B OG1 3313 C CG2 . THR B 100 ? 0.9360 0.6717 0.8172 -0.1890 -0.0251 0.1731 126 THR B CG2 3314 N N . LEU B 101 ? 0.6956 0.5680 0.5815 -0.2340 0.0007 0.1522 127 LEU B N 3315 C CA . LEU B 101 ? 0.6334 0.5401 0.5254 -0.2484 0.0084 0.1415 127 LEU B CA 3316 C C . LEU B 101 ? 0.6387 0.5803 0.5219 -0.2580 0.0130 0.1444 127 LEU B C 3317 O O . LEU B 101 ? 0.6281 0.5813 0.5068 -0.2495 0.0119 0.1484 127 LEU B O 3318 C CB . LEU B 101 ? 0.5401 0.4694 0.4503 -0.2394 0.0115 0.1248 127 LEU B CB 3319 C CG . LEU B 101 ? 0.5660 0.4669 0.4862 -0.2320 0.0080 0.1183 127 LEU B CG 3320 C CD1 . LEU B 101 ? 0.5312 0.4603 0.4681 -0.2255 0.0114 0.1019 127 LEU B CD1 3321 C CD2 . LEU B 101 ? 0.6210 0.4991 0.5382 -0.2460 0.0077 0.1194 127 LEU B CD2 3322 N N . THR B 102 ? 0.5849 0.5445 0.4659 -0.2758 0.0182 0.1417 128 THR B N 3323 C CA . THR B 102 ? 0.6206 0.6130 0.4925 -0.2865 0.0227 0.1437 128 THR B CA 3324 C C . THR B 102 ? 0.6418 0.6787 0.5252 -0.2940 0.0306 0.1278 128 THR B C 3325 O O . THR B 102 ? 0.5464 0.5848 0.4415 -0.2966 0.0323 0.1181 128 THR B O 3326 C CB . THR B 102 ? 0.7314 0.7031 0.5846 -0.3034 0.0209 0.1590 128 THR B CB 3327 O OG1 . THR B 102 ? 0.7446 0.7004 0.6001 -0.3161 0.0217 0.1572 128 THR B OG1 3328 C CG2 . THR B 102 ? 0.7183 0.6496 0.5593 -0.2943 0.0124 0.1751 128 THR B CG2 3329 N N . GLY B 103 ? 0.6363 0.7100 0.5164 -0.2967 0.0349 0.1246 129 GLY B N 3330 C CA . GLY B 103 ? 0.5986 0.7165 0.4877 -0.3044 0.0422 0.1102 129 GLY B CA 3331 C C . GLY B 103 ? 0.5946 0.7290 0.5047 -0.2945 0.0442 0.0932 129 GLY B C 3332 O O . GLY B 103 ? 0.6023 0.7323 0.5220 -0.2772 0.0418 0.0886 129 GLY B O 3333 N N . GLU B 104 ? 0.6363 0.7899 0.5532 -0.3058 0.0483 0.0842 130 GLU B N 3334 C CA . GLU B 104 ? 0.5910 0.7668 0.5279 -0.2974 0.0502 0.0671 130 GLU B CA 3335 C C . GLU B 104 ? 0.5674 0.7112 0.5127 -0.2872 0.0452 0.0668 130 GLU B C 3336 O O . GLU B 104 ? 0.4815 0.6390 0.4424 -0.2743 0.0449 0.0544 130 GLU B O 3337 C CB . GLU B 104 ? 0.6296 0.8297 0.5706 -0.3132 0.0548 0.0592 130 GLU B CB 3338 C CG . GLU B 104 ? 0.7443 0.9794 0.7056 -0.3035 0.0572 0.0401 130 GLU B CG 3339 C CD . GLU B 104 ? 0.9084 1.1708 0.8770 -0.2859 0.0583 0.0312 130 GLU B CD 3340 O OE1 . GLU B 104 ? 0.9986 1.2799 0.9587 -0.2891 0.0613 0.0328 130 GLU B OE1 3341 O OE2 . GLU B 104 ? 0.8945 1.1585 0.8769 -0.2690 0.0559 0.0224 130 GLU B OE2 3342 N N . ASP B 105 ? 0.4888 0.5893 0.4233 -0.2927 0.0407 0.0801 131 ASP B N 3343 C CA . ASP B 105 ? 0.5164 0.5833 0.4573 -0.2833 0.0356 0.0798 131 ASP B CA 3344 C C . ASP B 105 ? 0.5944 0.6547 0.5389 -0.2636 0.0324 0.0801 131 ASP B C 3345 O O . ASP B 105 ? 0.4810 0.5386 0.4381 -0.2520 0.0305 0.0713 131 ASP B O 3346 C CB . ASP B 105 ? 0.6167 0.6379 0.5447 -0.2931 0.0313 0.0935 131 ASP B CB 3347 C CG . ASP B 105 ? 0.7411 0.7285 0.6764 -0.2849 0.0263 0.0906 131 ASP B CG 3348 O OD1 . ASP B 105 ? 0.8132 0.8164 0.7635 -0.2797 0.0273 0.0765 131 ASP B OD1 3349 O OD2 . ASP B 105 ? 0.8840 0.8292 0.8099 -0.2829 0.0211 0.1018 131 ASP B OD2 3350 N N . LEU B 106 ? 0.5565 0.6148 0.4894 -0.2605 0.0315 0.0904 132 LEU B N 3351 C CA . LEU B 106 ? 0.5004 0.5573 0.4360 -0.2429 0.0290 0.0907 132 LEU B CA 3352 C C . LEU B 106 ? 0.4486 0.5451 0.4003 -0.2332 0.0329 0.0744 132 LEU B C 3353 O O . LEU B 106 ? 0.4038 0.4968 0.3658 -0.2195 0.0307 0.0685 132 LEU B O 3354 C CB . LEU B 106 ? 0.4976 0.5526 0.4179 -0.2428 0.0277 0.1033 132 LEU B CB 3355 C CG . LEU B 106 ? 0.4332 0.4960 0.3562 -0.2258 0.0260 0.1024 132 LEU B CG 3356 C CD1 . LEU B 106 ? 0.4534 0.4794 0.3784 -0.2132 0.0195 0.1076 132 LEU B CD1 3357 C CD2 . LEU B 106 ? 0.4666 0.5381 0.3750 -0.2281 0.0258 0.1118 132 LEU B CD2 3358 N N . TRP B 107 ? 0.4777 0.6113 0.4316 -0.2400 0.0383 0.0666 133 TRP B N 3359 C CA . TRP B 107 ? 0.4736 0.6450 0.4427 -0.2292 0.0414 0.0504 133 TRP B CA 3360 C C . TRP B 107 ? 0.4082 0.5804 0.3936 -0.2236 0.0401 0.0389 133 TRP B C 3361 O O . TRP B 107 ? 0.3095 0.4918 0.3067 -0.2085 0.0389 0.0299 133 TRP B O 3362 C CB . TRP B 107 ? 0.4529 0.6627 0.4214 -0.2376 0.0470 0.0432 133 TRP B CB 3363 C CG . TRP B 107 ? 0.3864 0.6315 0.3707 -0.2239 0.0490 0.0261 133 TRP B CG 3364 C CD1 . TRP B 107 ? 0.4337 0.7073 0.4304 -0.2245 0.0517 0.0121 133 TRP B CD1 3365 C CD2 . TRP B 107 ? 0.3899 0.6430 0.3795 -0.2064 0.0478 0.0212 133 TRP B CD2 3366 N NE1 . TRP B 107 ? 0.3464 0.6438 0.3555 -0.2074 0.0517 -0.0011 133 TRP B NE1 3367 C CE2 . TRP B 107 ? 0.3613 0.6463 0.3663 -0.1964 0.0495 0.0040 133 TRP B CE2 3368 C CE3 . TRP B 107 ? 0.3817 0.6177 0.3643 -0.1979 0.0451 0.0297 133 TRP B CE3 3369 C CZ2 . TRP B 107 ? 0.2950 0.5927 0.3082 -0.1784 0.0483 -0.0050 133 TRP B CZ2 3370 C CZ3 . TRP B 107 ? 0.4560 0.7076 0.4471 -0.1812 0.0446 0.0205 133 TRP B CZ3 3371 C CH2 . TRP B 107 ? 0.3893 0.6702 0.3954 -0.1716 0.0462 0.0033 133 TRP B CH2 3372 N N . ASN B 108 ? 0.3981 0.5593 0.3836 -0.2359 0.0400 0.0390 134 ASN B N 3373 C CA . ASN B 108 ? 0.4231 0.5833 0.4227 -0.2317 0.0380 0.0284 134 ASN B CA 3374 C C . ASN B 108 ? 0.3322 0.4616 0.3345 -0.2199 0.0327 0.0307 134 ASN B C 3375 O O . ASN B 108 ? 0.3087 0.4464 0.3240 -0.2094 0.0308 0.0199 134 ASN B O 3376 C CB . ASN B 108 ? 0.4985 0.6494 0.4959 -0.2485 0.0385 0.0291 134 ASN B CB 3377 C CG . ASN B 108 ? 0.6752 0.8643 0.6755 -0.2587 0.0437 0.0216 134 ASN B CG 3378 O OD1 . ASN B 108 ? 0.6652 0.8868 0.6689 -0.2525 0.0469 0.0155 134 ASN B OD1 3379 N ND2 . ASN B 108 ? 0.7225 0.9076 0.7215 -0.2743 0.0446 0.0215 134 ASN B ND2 3380 N N . ALA B 109 ? 0.3638 0.4578 0.3532 -0.2212 0.0298 0.0447 135 ALA B N 3381 C CA . ALA B 109 ? 0.3515 0.4157 0.3423 -0.2097 0.0247 0.0471 135 ALA B CA 3382 C C . ALA B 109 ? 0.3449 0.4280 0.3424 -0.1942 0.0248 0.0428 135 ALA B C 3383 O O . ALA B 109 ? 0.3308 0.4064 0.3363 -0.1834 0.0217 0.0374 135 ALA B O 3384 C CB . ALA B 109 ? 0.3693 0.3912 0.3448 -0.2129 0.0209 0.0631 135 ALA B CB 3385 N N . THR B 110 ? 0.3274 0.4352 0.3211 -0.1934 0.0282 0.0446 136 THR B N 3386 C CA . THR B 110 ? 0.2741 0.4009 0.2733 -0.1791 0.0285 0.0402 136 THR B CA 3387 C C . THR B 110 ? 0.2943 0.4523 0.3108 -0.1703 0.0297 0.0230 136 THR B C 3388 O O . THR B 110 ? 0.2243 0.3844 0.2499 -0.1570 0.0272 0.0171 136 THR B O 3389 C CB . THR B 110 ? 0.2803 0.4240 0.2693 -0.1810 0.0315 0.0456 136 THR B CB 3390 O OG1 . THR B 110 ? 0.3230 0.4359 0.2953 -0.1878 0.0288 0.0624 136 THR B OG1 3391 C CG2 . THR B 110 ? 0.2535 0.4148 0.2478 -0.1657 0.0316 0.0405 136 THR B CG2 3392 N N . VAL B 111 ? 0.2720 0.4532 0.2928 -0.1774 0.0328 0.0151 137 VAL B N 3393 C CA . VAL B 111 ? 0.2763 0.4851 0.3130 -0.1681 0.0327 -0.0007 137 VAL B CA 3394 C C . VAL B 111 ? 0.2231 0.4159 0.2685 -0.1623 0.0278 -0.0054 137 VAL B C 3395 O O . VAL B 111 ? 0.2189 0.4222 0.2747 -0.1476 0.0250 -0.0142 137 VAL B O 3396 C CB . VAL B 111 ? 0.2468 0.4803 0.2859 -0.1783 0.0363 -0.0073 137 VAL B CB 3397 C CG1 . VAL B 111 ? 0.2294 0.4866 0.2844 -0.1677 0.0346 -0.0226 137 VAL B CG1 3398 C CG2 . VAL B 111 ? 0.2550 0.5098 0.2865 -0.1822 0.0410 -0.0059 137 VAL B CG2 3399 N N . ASN B 112 ? 0.2424 0.4078 0.2822 -0.1736 0.0262 0.0005 138 ASN B N 3400 C CA . ASN B 112 ? 0.3127 0.4599 0.3583 -0.1696 0.0214 -0.0043 138 ASN B CA 3401 C C . ASN B 112 ? 0.2576 0.3884 0.3032 -0.1566 0.0180 -0.0021 138 ASN B C 3402 O O . ASN B 112 ? 0.2056 0.3351 0.2579 -0.1430 0.0139 -0.0107 138 ASN B O 3403 C CB . ASN B 112 ? 0.2658 0.3817 0.3031 -0.1838 0.0204 0.0018 138 ASN B CB 3404 C CG . ASN B 112 ? 0.3705 0.4684 0.4127 -0.1804 0.0156 -0.0054 138 ASN B CG 3405 O OD1 . ASN B 112 ? 0.3321 0.4504 0.3846 -0.1765 0.0142 -0.0171 138 ASN B OD1 3406 N ND2 . ASN B 112 ? 0.4443 0.5029 0.4781 -0.1810 0.0127 0.0012 138 ASN B ND2 3407 N N . HIS B 113 ? 0.3051 0.4184 0.3394 -0.1540 0.0184 0.0096 139 HIS B N 3408 C CA . HIS B 113 ? 0.2532 0.3467 0.2847 -0.1345 0.0144 0.0118 139 HIS B CA 3409 C C . HIS B 113 ? 0.2391 0.3596 0.2802 -0.1188 0.0140 0.0020 139 HIS B C 3410 O O . HIS B 113 ? 0.1857 0.2985 0.2309 -0.1044 0.0100 -0.0037 139 HIS B O 3411 C CB . HIS B 113 ? 0.2305 0.3045 0.2488 -0.1354 0.0144 0.0263 139 HIS B CB 3412 C CG . HIS B 113 ? 0.2598 0.3142 0.2760 -0.1167 0.0101 0.0288 139 HIS B CG 3413 N ND1 . HIS B 113 ? 0.2291 0.2512 0.2435 -0.1101 0.0059 0.0303 139 HIS B ND1 3414 C CD2 . HIS B 113 ? 0.2417 0.3059 0.2580 -0.1038 0.0095 0.0290 139 HIS B CD2 3415 C CE1 . HIS B 113 ? 0.2176 0.2326 0.2318 -0.0942 0.0033 0.0316 139 HIS B CE1 3416 N NE2 . HIS B 113 ? 0.2111 0.2505 0.2261 -0.0905 0.0052 0.0311 139 HIS B NE2 3417 N N . ILE B 114 ? 0.2181 0.3700 0.2623 -0.1219 0.0180 -0.0003 140 ILE B N 3418 C CA . ILE B 114 ? 0.1603 0.3348 0.2129 -0.1065 0.0173 -0.0095 140 ILE B CA 3419 C C . ILE B 114 ? 0.1716 0.3598 0.2372 -0.0999 0.0141 -0.0221 140 ILE B C 3420 O O . ILE B 114 ? 0.1341 0.3173 0.2029 -0.0840 0.0097 -0.0268 140 ILE B O 3421 C CB . ILE B 114 ? 0.1586 0.3659 0.2126 -0.1117 0.0227 -0.0116 140 ILE B CB 3422 C CG1 . ILE B 114 ? 0.1695 0.3639 0.2091 -0.1150 0.0245 0.0010 140 ILE B CG1 3423 C CG2 . ILE B 114 ? 0.2164 0.4475 0.2815 -0.0956 0.0213 -0.0238 140 ILE B CG2 3424 C CD1 . ILE B 114 ? 0.1789 0.3995 0.2138 -0.1253 0.0305 0.0013 140 ILE B CD1 3425 N N . THR B 115 ? 0.1578 0.3634 0.2302 -0.1127 0.0158 -0.0273 141 THR B N 3426 C CA . THR B 115 ? 0.1456 0.3638 0.2283 -0.1043 0.0117 -0.0387 141 THR B CA 3427 C C . THR B 115 ? 0.2292 0.4232 0.3111 -0.0998 0.0061 -0.0394 141 THR B C 3428 O O . THR B 115 ? 0.1313 0.3297 0.2186 -0.0862 0.0011 -0.0462 141 THR B O 3429 C CB . THR B 115 ? 0.2078 0.4423 0.2931 -0.1145 0.0141 -0.0432 141 THR B CB 3430 O OG1 . THR B 115 ? 0.2313 0.4462 0.3101 -0.1313 0.0153 -0.0369 141 THR B OG1 3431 C CG2 . THR B 115 ? 0.1648 0.4220 0.2485 -0.1172 0.0196 -0.0440 141 THR B CG2 3432 N N . THR B 116 ? 0.1599 0.3243 0.2323 -0.1092 0.0065 -0.0321 142 THR B N 3433 C CA . THR B 116 ? 0.1624 0.3010 0.2315 -0.1035 0.0019 -0.0337 142 THR B CA 3434 C C . THR B 116 ? 0.1665 0.2897 0.2315 -0.0852 -0.0010 -0.0318 142 THR B C 3435 O O . THR B 116 ? 0.1630 0.2825 0.2295 -0.0758 -0.0053 -0.0375 142 THR B O 3436 C CB . THR B 116 ? 0.1854 0.2922 0.2450 -0.1159 0.0029 -0.0269 142 THR B CB 3437 O OG1 . THR B 116 ? 0.2372 0.3562 0.2998 -0.1351 0.0054 -0.0288 142 THR B OG1 3438 C CG2 . THR B 116 ? 0.2352 0.3175 0.2918 -0.1090 -0.0013 -0.0310 142 THR B CG2 3439 N N . VAL B 117 ? 0.1615 0.2769 0.2207 -0.0812 0.0011 -0.0238 143 VAL B N 3440 C CA . VAL B 117 ? 0.1390 0.2406 0.1946 -0.0656 -0.0013 -0.0219 143 VAL B CA 3441 C C . VAL B 117 ? 0.2175 0.3404 0.2802 -0.0538 -0.0038 -0.0293 143 VAL B C 3442 O O . VAL B 117 ? 0.1365 0.2517 0.1987 -0.0434 -0.0077 -0.0323 143 VAL B O 3443 C CB . VAL B 117 ? 0.1432 0.2326 0.1913 -0.0647 0.0009 -0.0116 143 VAL B CB 3444 C CG1 . VAL B 117 ? 0.1354 0.2183 0.1821 -0.0492 -0.0015 -0.0111 143 VAL B CG1 3445 C CG2 . VAL B 117 ? 0.1758 0.2368 0.2162 -0.0726 0.0012 -0.0035 143 VAL B CG2 3446 N N . MET B 118 ? 0.1165 0.2663 0.1856 -0.0556 -0.0018 -0.0327 144 MET B N 3447 C CA . MET B 118 ? 0.1483 0.3161 0.2246 -0.0431 -0.0049 -0.0403 144 MET B CA 3448 C C . MET B 118 ? 0.1452 0.3208 0.2283 -0.0393 -0.0103 -0.0484 144 MET B C 3449 O O . MET B 118 ? 0.1134 0.2881 0.1978 -0.0267 -0.0153 -0.0517 144 MET B O 3450 C CB . MET B 118 ? 0.1003 0.2972 0.1832 -0.0454 -0.0012 -0.0441 144 MET B CB 3451 C CG . MET B 118 ? 0.1658 0.3570 0.2407 -0.0458 0.0026 -0.0370 144 MET B CG 3452 S SD . MET B 118 ? 0.1601 0.3887 0.2418 -0.0486 0.0077 -0.0437 144 MET B SD 3453 C CE . MET B 118 ? 0.1282 0.3614 0.2163 -0.0281 0.0020 -0.0541 144 MET B CE 3454 N N . THR B 119 ? 0.1083 0.2906 0.1947 -0.0510 -0.0097 -0.0510 145 THR B N 3455 C CA . THR B 119 ? 0.1074 0.2998 0.2001 -0.0490 -0.0152 -0.0589 145 THR B CA 3456 C C . THR B 119 ? 0.1708 0.3368 0.2545 -0.0422 -0.0195 -0.0569 145 THR B C 3457 O O . THR B 119 ? 0.1090 0.2786 0.1939 -0.0323 -0.0256 -0.0610 145 THR B O 3458 C CB . THR B 119 ? 0.1535 0.3576 0.2506 -0.0653 -0.0132 -0.0620 145 THR B CB 3459 O OG1 . THR B 119 ? 0.1489 0.3739 0.2501 -0.0686 -0.0083 -0.0629 145 THR B OG1 3460 C CG2 . THR B 119 ? 0.2163 0.4235 0.3152 -0.0619 -0.0190 -0.0682 145 THR B CG2 3461 N N . HIS B 120 ? 0.1167 0.2566 0.1909 -0.0472 -0.0163 -0.0505 146 HIS B N 3462 C CA . HIS B 120 ? 0.1468 0.2631 0.2125 -0.0412 -0.0188 -0.0493 146 HIS B CA 3463 C C . HIS B 120 ? 0.1089 0.2228 0.1721 -0.0268 -0.0220 -0.0482 146 HIS B C 3464 O O . HIS B 120 ? 0.1088 0.2191 0.1687 -0.0208 -0.0267 -0.0509 146 HIS B O 3465 C CB . HIS B 120 ? 0.2063 0.2961 0.2641 -0.0463 -0.0147 -0.0427 146 HIS B CB 3466 C CG . HIS B 120 ? 0.2225 0.2910 0.2727 -0.0387 -0.0160 -0.0421 146 HIS B CG 3467 N ND1 . HIS B 120 ? 0.1961 0.2547 0.2427 -0.0417 -0.0176 -0.0473 146 HIS B ND1 3468 C CD2 . HIS B 120 ? 0.2752 0.3326 0.3210 -0.0290 -0.0156 -0.0379 146 HIS B CD2 3469 C CE1 . HIS B 120 ? 0.2287 0.2718 0.2689 -0.0339 -0.0175 -0.0463 146 HIS B CE1 3470 N NE2 . HIS B 120 ? 0.2439 0.2864 0.2840 -0.0264 -0.0164 -0.0404 146 HIS B NE2 3471 N N . TYR B 121 ? 0.1306 0.2465 0.1945 -0.0222 -0.0197 -0.0441 147 TYR B N 3472 C CA . TYR B 121 ? 0.1138 0.2236 0.1743 -0.0101 -0.0224 -0.0426 147 TYR B CA 3473 C C . TYR B 121 ? 0.1281 0.2558 0.1951 -0.0020 -0.0278 -0.0484 147 TYR B C 3474 O O . TYR B 121 ? 0.2198 0.3401 0.2828 0.0072 -0.0323 -0.0480 147 TYR B O 3475 C CB . TYR B 121 ? 0.1020 0.2050 0.1598 -0.0084 -0.0184 -0.0365 147 TYR B CB 3476 C CG . TYR B 121 ? 0.2128 0.2938 0.2635 -0.0114 -0.0156 -0.0307 147 TYR B CG 3477 C CD1 . TYR B 121 ? 0.1994 0.2652 0.2443 -0.0056 -0.0172 -0.0300 147 TYR B CD1 3478 C CD2 . TYR B 121 ? 0.1960 0.2713 0.2457 -0.0203 -0.0117 -0.0262 147 TYR B CD2 3479 C CE1 . TYR B 121 ? 0.1635 0.2116 0.2039 -0.0071 -0.0147 -0.0265 147 TYR B CE1 3480 C CE2 . TYR B 121 ? 0.2119 0.2657 0.2563 -0.0213 -0.0102 -0.0216 147 TYR B CE2 3481 C CZ . TYR B 121 ? 0.1803 0.2217 0.2210 -0.0139 -0.0116 -0.0226 147 TYR B CZ 3482 O OH . TYR B 121 ? 0.2121 0.2348 0.2495 -0.0134 -0.0100 -0.0197 147 TYR B OH 3483 N N . LYS B 122 ? 0.0896 0.2408 0.1666 -0.0057 -0.0276 -0.0538 148 LYS B N 3484 C CA . LYS B 122 ? 0.1112 0.2818 0.1968 0.0028 -0.0338 -0.0607 148 LYS B CA 3485 C C . LYS B 122 ? 0.0924 0.2565 0.1740 0.0060 -0.0408 -0.0622 148 LYS B C 3486 O O . LYS B 122 ? 0.1989 0.3579 0.2774 0.0165 -0.0461 -0.0619 148 LYS B O 3487 C CB . LYS B 122 ? 0.1150 0.3077 0.2090 -0.0030 -0.0300 -0.0652 148 LYS B CB 3488 C CG . LYS B 122 ? 0.2083 0.4117 0.3065 0.0067 -0.0337 -0.0704 148 LYS B CG 3489 C CD . LYS B 122 ? 0.2083 0.4351 0.3146 -0.0011 -0.0294 -0.0754 148 LYS B CD 3490 C CE . LYS B 122 ? 0.3178 0.5580 0.4300 0.0087 -0.0333 -0.0820 148 LYS B CE 3491 N NZ . LYS B 122 ? 0.2973 0.5623 0.4175 0.0006 -0.0289 -0.0876 148 LYS B NZ 3492 N N . GLU B 123 ? 0.1414 0.3001 0.2195 -0.0038 -0.0396 -0.0622 149 GLU B N 3493 C CA . GLU B 123 ? 0.1527 0.3094 0.2267 -0.0028 -0.0462 -0.0648 149 GLU B CA 3494 C C . GLU B 123 ? 0.1933 0.3252 0.2531 0.0018 -0.0476 -0.0598 149 GLU B C 3495 O O . GLU B 123 ? 0.2150 0.3452 0.2690 0.0047 -0.0539 -0.0610 149 GLU B O 3496 C CB . GLU B 123 ? 0.2008 0.3624 0.2763 -0.0161 -0.0441 -0.0686 149 GLU B CB 3497 C CG . GLU B 123 ? 0.3693 0.5531 0.4558 -0.0220 -0.0416 -0.0721 149 GLU B CG 3498 C CD . GLU B 123 ? 0.5235 0.7082 0.6107 -0.0381 -0.0382 -0.0746 149 GLU B CD 3499 O OE1 . GLU B 123 ? 0.4894 0.6539 0.5694 -0.0451 -0.0349 -0.0722 149 GLU B OE1 3500 O OE2 . GLU B 123 ? 0.5916 0.7923 0.6848 -0.0429 -0.0380 -0.0780 149 GLU B OE2 3501 N N . SER B 124 ? 0.1149 0.2293 0.1688 0.0019 -0.0419 -0.0541 150 SER B N 3502 C CA . SER B 124 ? 0.1775 0.2716 0.2190 0.0039 -0.0419 -0.0505 150 SER B CA 3503 C C . SER B 124 ? 0.1654 0.2484 0.2017 0.0120 -0.0420 -0.0451 150 SER B C 3504 O O . SER B 124 ? 0.1521 0.2232 0.1782 0.0144 -0.0439 -0.0427 150 SER B O 3505 C CB . SER B 124 ? 0.2276 0.3081 0.2652 -0.0043 -0.0353 -0.0498 150 SER B CB 3506 O OG . SER B 124 ? 0.3953 0.4735 0.4375 -0.0066 -0.0297 -0.0462 150 SER B OG 3507 N N . PHE B 125 ? 0.1297 0.2172 0.1721 0.0150 -0.0398 -0.0436 151 PHE B N 3508 C CA . PHE B 125 ? 0.1809 0.2580 0.2189 0.0214 -0.0399 -0.0393 151 PHE B CA 3509 C C . PHE B 125 ? 0.1973 0.2856 0.2430 0.0280 -0.0425 -0.0416 151 PHE B C 3510 O O . PHE B 125 ? 0.1734 0.2796 0.2286 0.0279 -0.0436 -0.0467 151 PHE B O 3511 C CB . PHE B 125 ? 0.1975 0.2634 0.2328 0.0177 -0.0328 -0.0348 151 PHE B CB 3512 C CG . PHE B 125 ? 0.1990 0.2532 0.2279 0.0131 -0.0300 -0.0339 151 PHE B CG 3513 C CD1 . PHE B 125 ? 0.1363 0.1797 0.1560 0.0153 -0.0308 -0.0320 151 PHE B CD1 3514 C CD2 . PHE B 125 ? 0.1016 0.1552 0.1331 0.0062 -0.0262 -0.0354 151 PHE B CD2 3515 C CE1 . PHE B 125 ? 0.1691 0.2041 0.1836 0.0117 -0.0274 -0.0329 151 PHE B CE1 3516 C CE2 . PHE B 125 ? 0.2083 0.2499 0.2344 0.0031 -0.0237 -0.0363 151 PHE B CE2 3517 C CZ . PHE B 125 ? 0.1365 0.1701 0.1547 0.0064 -0.0240 -0.0357 151 PHE B CZ 3518 N N . ASN B 126 ? 0.1869 0.2657 0.2289 0.0334 -0.0432 -0.0388 152 ASN B N 3519 C CA . ASN B 126 ? 0.2207 0.3084 0.2696 0.0397 -0.0449 -0.0423 152 ASN B CA 3520 C C . ASN B 126 ? 0.1771 0.2648 0.2269 0.0367 -0.0382 -0.0404 152 ASN B C 3521 O O . ASN B 126 ? 0.1661 0.2404 0.2095 0.0371 -0.0369 -0.0361 152 ASN B O 3522 C CB . ASN B 126 ? 0.2286 0.3048 0.2726 0.0485 -0.0522 -0.0416 152 ASN B CB 3523 C CG . ASN B 126 ? 0.2703 0.3471 0.3131 0.0521 -0.0587 -0.0431 152 ASN B CG 3524 O OD1 . ASN B 126 ? 0.3435 0.4067 0.3765 0.0537 -0.0641 -0.0389 152 ASN B OD1 3525 N ND2 . ASN B 126 ? 0.3117 0.4049 0.3636 0.0529 -0.0580 -0.0486 152 ASN B ND2 3526 N N . ILE B 127 ? 0.1086 0.2129 0.1660 0.0327 -0.0340 -0.0434 153 ILE B N 3527 C CA . ILE B 127 ? 0.1179 0.2247 0.1751 0.0293 -0.0283 -0.0412 153 ILE B CA 3528 C C . ILE B 127 ? 0.1028 0.2200 0.1648 0.0362 -0.0299 -0.0474 153 ILE B C 3529 O O . ILE B 127 ? 0.1043 0.2376 0.1735 0.0380 -0.0303 -0.0539 153 ILE B O 3530 C CB . ILE B 127 ? 0.1451 0.2635 0.2058 0.0198 -0.0227 -0.0403 153 ILE B CB 3531 C CG1 . ILE B 127 ? 0.2363 0.3435 0.2933 0.0136 -0.0219 -0.0364 153 ILE B CG1 3532 C CG2 . ILE B 127 ? 0.2131 0.3332 0.2712 0.0161 -0.0178 -0.0366 153 ILE B CG2 3533 C CD1 . ILE B 127 ? 0.2128 0.3029 0.2628 0.0105 -0.0187 -0.0291 153 ILE B CD1 3534 N N . TYR B 128 ? 0.1042 0.2106 0.1611 0.0394 -0.0303 -0.0457 154 TYR B N 3535 C CA . TYR B 128 ? 0.1067 0.2201 0.1670 0.0459 -0.0317 -0.0527 154 TYR B CA 3536 C C . TYR B 128 ? 0.1440 0.2785 0.2089 0.0412 -0.0257 -0.0564 154 TYR B C 3537 O O . TYR B 128 ? 0.0963 0.2420 0.1646 0.0441 -0.0251 -0.0641 154 TYR B O 3538 C CB . TYR B 128 ? 0.1132 0.2108 0.1669 0.0487 -0.0335 -0.0507 154 TYR B CB 3539 C CG . TYR B 128 ? 0.0883 0.1928 0.1446 0.0538 -0.0339 -0.0591 154 TYR B CG 3540 C CD1 . TYR B 128 ? 0.2178 0.3184 0.2755 0.0611 -0.0385 -0.0658 154 TYR B CD1 3541 C CD2 . TYR B 128 ? 0.1505 0.2640 0.2058 0.0503 -0.0293 -0.0602 154 TYR B CD2 3542 C CE1 . TYR B 128 ? 0.2067 0.3126 0.2665 0.0658 -0.0390 -0.0747 154 TYR B CE1 3543 C CE2 . TYR B 128 ? 0.1448 0.2671 0.2028 0.0551 -0.0296 -0.0699 154 TYR B CE2 3544 C CZ . TYR B 128 ? 0.2035 0.3204 0.2633 0.0627 -0.0343 -0.0774 154 TYR B CZ 3545 O OH . TYR B 128 ? 0.2343 0.3572 0.2958 0.0673 -0.0349 -0.0877 154 TYR B OH 3546 N N . ALA B 129 ? 0.0738 0.2087 0.1348 0.0325 -0.0205 -0.0496 155 ALA B N 3547 C CA . ALA B 129 ? 0.0737 0.2267 0.1356 0.0261 -0.0148 -0.0505 155 ALA B CA 3548 C C . ALA B 129 ? 0.1723 0.3226 0.2298 0.0152 -0.0105 -0.0412 155 ALA B C 3549 O O . ALA B 129 ? 0.1813 0.3129 0.2336 0.0138 -0.0114 -0.0336 155 ALA B O 3550 C CB . ALA B 129 ? 0.0875 0.2396 0.1446 0.0280 -0.0140 -0.0517 155 ALA B CB 3551 N N . TRP B 130 ? 0.1175 0.2866 0.1773 0.0073 -0.0058 -0.0422 156 TRP B N 3552 C CA . TRP B 130 ? 0.1763 0.3417 0.2307 -0.0041 -0.0020 -0.0328 156 TRP B CA 3553 C C . TRP B 130 ? 0.1885 0.3620 0.2359 -0.0100 0.0019 -0.0287 156 TRP B C 3554 O O . TRP B 130 ? 0.1323 0.3283 0.1823 -0.0115 0.0049 -0.0355 156 TRP B O 3555 C CB . TRP B 130 ? 0.1077 0.2873 0.1683 -0.0120 0.0003 -0.0354 156 TRP B CB 3556 C CG . TRP B 130 ? 0.1280 0.2933 0.1905 -0.0119 -0.0028 -0.0339 156 TRP B CG 3557 C CD1 . TRP B 130 ? 0.1494 0.3208 0.2197 -0.0069 -0.0064 -0.0413 156 TRP B CD1 3558 C CD2 . TRP B 130 ? 0.1204 0.2631 0.1763 -0.0167 -0.0028 -0.0250 156 TRP B CD2 3559 N NE1 . TRP B 130 ? 0.1680 0.3226 0.2358 -0.0094 -0.0084 -0.0376 156 TRP B NE1 3560 C CE2 . TRP B 130 ? 0.1621 0.2988 0.2216 -0.0152 -0.0059 -0.0283 156 TRP B CE2 3561 C CE3 . TRP B 130 ? 0.1437 0.2708 0.1911 -0.0215 -0.0011 -0.0150 156 TRP B CE3 3562 C CZ2 . TRP B 130 ? 0.1813 0.2973 0.2362 -0.0185 -0.0065 -0.0233 156 TRP B CZ2 3563 C CZ3 . TRP B 130 ? 0.1787 0.2845 0.2230 -0.0236 -0.0022 -0.0097 156 TRP B CZ3 3564 C CH2 . TRP B 130 ? 0.1322 0.2327 0.1802 -0.0223 -0.0044 -0.0145 156 TRP B CH2 3565 N N . ASP B 131 ? 0.1797 0.3367 0.2185 -0.0131 0.0016 -0.0180 157 ASP B N 3566 C CA . ASP B 131 ? 0.1505 0.3146 0.1807 -0.0214 0.0048 -0.0113 157 ASP B CA 3567 C C . ASP B 131 ? 0.1961 0.3646 0.2251 -0.0339 0.0083 -0.0062 157 ASP B C 3568 O O . ASP B 131 ? 0.2066 0.3558 0.2326 -0.0377 0.0070 0.0023 157 ASP B O 3569 C CB . ASP B 131 ? 0.1738 0.3191 0.1959 -0.0199 0.0020 -0.0009 157 ASP B CB 3570 C CG . ASP B 131 ? 0.3232 0.4659 0.3456 -0.0101 -0.0011 -0.0055 157 ASP B CG 3571 O OD1 . ASP B 131 ? 0.2831 0.4401 0.3085 -0.0064 -0.0005 -0.0155 157 ASP B OD1 3572 O OD2 . ASP B 131 ? 0.2832 0.4098 0.3034 -0.0064 -0.0043 0.0005 157 ASP B OD2 3573 N N . VAL B 132 ? 0.1446 0.3387 0.1764 -0.0406 0.0129 -0.0122 158 VAL B N 3574 C CA . VAL B 132 ? 0.1449 0.3456 0.1764 -0.0545 0.0166 -0.0084 158 VAL B CA 3575 C C . VAL B 132 ? 0.2590 0.4538 0.2764 -0.0665 0.0187 0.0051 158 VAL B C 3576 O O . VAL B 132 ? 0.2834 0.4569 0.2952 -0.0732 0.0173 0.0159 158 VAL B O 3577 C CB . VAL B 132 ? 0.1381 0.3725 0.1793 -0.0578 0.0211 -0.0207 158 VAL B CB 3578 C CG1 . VAL B 132 ? 0.1309 0.3748 0.1716 -0.0748 0.0256 -0.0167 158 VAL B CG1 3579 C CG2 . VAL B 132 ? 0.1533 0.3913 0.2080 -0.0445 0.0172 -0.0329 158 VAL B CG2 3580 N N . VAL B 133 ? 0.1425 0.3550 0.1534 -0.0688 0.0214 0.0045 159 VAL B N 3581 C CA . VAL B 133 ? 0.1603 0.3676 0.1557 -0.0794 0.0223 0.0183 159 VAL B CA 3582 C C . VAL B 133 ? 0.2339 0.4282 0.2228 -0.0697 0.0173 0.0228 159 VAL B C 3583 O O . VAL B 133 ? 0.1488 0.3539 0.1421 -0.0598 0.0167 0.0126 159 VAL B O 3584 C CB . VAL B 133 ? 0.1698 0.4093 0.1599 -0.0920 0.0293 0.0154 159 VAL B CB 3585 C CG1 . VAL B 133 ? 0.1901 0.4254 0.1613 -0.1026 0.0294 0.0302 159 VAL B CG1 3586 C CG2 . VAL B 133 ? 0.1754 0.4258 0.1715 -0.1031 0.0334 0.0122 159 VAL B CG2 3587 N N . ASN B 134 ? 0.2152 0.3861 0.1944 -0.0722 0.0133 0.0376 160 ASN B N 3588 C CA . ASN B 134 ? 0.1922 0.3522 0.1661 -0.0634 0.0079 0.0428 160 ASN B CA 3589 C C . ASN B 134 ? 0.2433 0.4026 0.2005 -0.0729 0.0066 0.0571 160 ASN B C 3590 O O . ASN B 134 ? 0.2497 0.3959 0.1992 -0.0830 0.0063 0.0693 160 ASN B O 3591 C CB . ASN B 134 ? 0.2658 0.3977 0.2460 -0.0534 0.0025 0.0462 160 ASN B CB 3592 C CG . ASN B 134 ? 0.3138 0.4384 0.2921 -0.0434 -0.0029 0.0491 160 ASN B CG 3593 O OD1 . ASN B 134 ? 0.3192 0.4590 0.2979 -0.0391 -0.0027 0.0417 160 ASN B OD1 3594 N ND2 . ASN B 134 ? 0.3364 0.4382 0.3134 -0.0398 -0.0079 0.0592 160 ASN B ND2 3595 N N . GLU B 135 ? 0.1911 0.3638 0.1418 -0.0702 0.0055 0.0558 161 GLU B N 3596 C CA . GLU B 135 ? 0.2447 0.4161 0.1787 -0.0770 0.0023 0.0700 161 GLU B CA 3597 C C . GLU B 135 ? 0.3242 0.5048 0.2452 -0.0947 0.0069 0.0786 161 GLU B C 3598 O O . GLU B 135 ? 0.3281 0.4891 0.2387 -0.1018 0.0032 0.0948 161 GLU B O 3599 C CB . GLU B 135 ? 0.2229 0.3642 0.1558 -0.0700 -0.0062 0.0832 161 GLU B CB 3600 C CG . GLU B 135 ? 0.2225 0.3600 0.1652 -0.0545 -0.0108 0.0762 161 GLU B CG 3601 C CD . GLU B 135 ? 0.3435 0.4553 0.2884 -0.0461 -0.0186 0.0869 161 GLU B CD 3602 O OE1 . GLU B 135 ? 0.2990 0.3942 0.2355 -0.0510 -0.0222 0.1013 161 GLU B OE1 3603 O OE2 . GLU B 135 ? 0.3315 0.4399 0.2869 -0.0345 -0.0213 0.0803 161 GLU B OE2 3604 N N . ALA B 136 ? 0.2290 0.4377 0.1525 -0.1007 0.0142 0.0662 162 ALA B N 3605 C CA . ALA B 136 ? 0.3152 0.5316 0.2333 -0.1151 0.0178 0.0684 162 ALA B CA 3606 C C . ALA B 136 ? 0.3301 0.5563 0.2348 -0.1214 0.0162 0.0729 162 ALA B C 3607 O O . ALA B 136 ? 0.3893 0.6217 0.2866 -0.1343 0.0186 0.0766 162 ALA B O 3608 C CB . ALA B 136 ? 0.2361 0.4773 0.1671 -0.1165 0.0250 0.0509 162 ALA B CB 3609 N N . PHE B 137 ? 0.2805 0.5089 0.1820 -0.1130 0.0121 0.0724 163 PHE B N 3610 C CA . PHE B 137 ? 0.2814 0.5236 0.1720 -0.1187 0.0112 0.0738 163 PHE B CA 3611 C C . PHE B 137 ? 0.2968 0.5198 0.1760 -0.1162 0.0028 0.0894 163 PHE B C 3612 O O . PHE B 137 ? 0.2867 0.4925 0.1696 -0.1055 -0.0028 0.0938 163 PHE B O 3613 C CB . PHE B 137 ? 0.3068 0.5758 0.2047 -0.1123 0.0146 0.0551 163 PHE B CB 3614 C CG . PHE B 137 ? 0.3481 0.6383 0.2575 -0.1140 0.0219 0.0387 163 PHE B CG 3615 C CD1 . PHE B 137 ? 0.3710 0.6824 0.2767 -0.1252 0.0264 0.0342 163 PHE B CD1 3616 C CD2 . PHE B 137 ? 0.2928 0.5818 0.2168 -0.1041 0.0237 0.0280 163 PHE B CD2 3617 C CE1 . PHE B 137 ? 0.3564 0.6880 0.2739 -0.1256 0.0320 0.0187 163 PHE B CE1 3618 C CE2 . PHE B 137 ? 0.3485 0.6564 0.2842 -0.1040 0.0291 0.0127 163 PHE B CE2 3619 C CZ . PHE B 137 ? 0.3302 0.6594 0.2630 -0.1144 0.0329 0.0079 163 PHE B CZ 3620 N N . ASN B 138 ? 0.4116 0.6386 0.2774 -0.1260 0.0014 0.0976 164 ASN B N 3621 C CA . ASN B 138 ? 0.4684 0.6826 0.3236 -0.1229 -0.0068 0.1103 164 ASN B CA 3622 C C . ASN B 138 ? 0.4573 0.6896 0.3154 -0.1150 -0.0079 0.0995 164 ASN B C 3623 O O . ASN B 138 ? 0.3787 0.6353 0.2433 -0.1152 -0.0017 0.0831 164 ASN B O 3624 C CB . ASN B 138 ? 0.4458 0.6590 0.2846 -0.1366 -0.0080 0.1226 164 ASN B CB 3625 C CG . ASN B 138 ? 0.4757 0.6616 0.3094 -0.1432 -0.0099 0.1371 164 ASN B CG 3626 O OD1 . ASN B 138 ? 0.4578 0.6173 0.2966 -0.1347 -0.0148 0.1440 164 ASN B OD1 3627 N ND2 . ASN B 138 ? 0.4401 0.6323 0.2642 -0.1585 -0.0061 0.1411 164 ASN B ND2 3628 N N . ASP B 139 ? 0.4218 0.6422 0.2755 -0.1079 -0.0161 0.1080 165 ASP B N 3629 C CA . ASP B 139 ? 0.3927 0.6284 0.2493 -0.1008 -0.0177 0.0978 165 ASP B CA 3630 C C . ASP B 139 ? 0.3343 0.5964 0.1829 -0.1099 -0.0135 0.0905 165 ASP B C 3631 O O . ASP B 139 ? 0.5400 0.8181 0.3926 -0.1054 -0.0127 0.0780 165 ASP B O 3632 C CB . ASP B 139 ? 0.5302 0.7491 0.3843 -0.0920 -0.0279 0.1088 165 ASP B CB 3633 C CG . ASP B 139 ? 0.5509 0.7516 0.4179 -0.0792 -0.0317 0.1088 165 ASP B CG 3634 O OD1 . ASP B 139 ? 0.4086 0.6135 0.2864 -0.0759 -0.0264 0.0976 165 ASP B OD1 3635 O OD2 . ASP B 139 ? 0.6079 0.7909 0.4748 -0.0718 -0.0401 0.1195 165 ASP B OD2 3636 N N . ASN B 140 ? 0.4586 0.7254 0.2962 -0.1231 -0.0108 0.0976 166 ASN B N 3637 C CA . ASN B 140 ? 0.3711 0.6654 0.2016 -0.1327 -0.0061 0.0898 166 ASN B CA 3638 C C . ASN B 140 ? 0.5655 0.8817 0.4047 -0.1380 0.0037 0.0740 166 ASN B C 3639 O O . ASN B 140 ? 0.5049 0.8458 0.3399 -0.1462 0.0084 0.0660 166 ASN B O 3640 C CB . ASN B 140 ? 0.4474 0.7379 0.2591 -0.1450 -0.0093 0.1064 166 ASN B CB 3641 C CG . ASN B 140 ? 0.5652 0.8363 0.3721 -0.1530 -0.0091 0.1197 166 ASN B CG 3642 O OD1 . ASN B 140 ? 0.5360 0.8065 0.3530 -0.1538 -0.0037 0.1134 166 ASN B OD1 3643 N ND2 . ASN B 140 ? 0.6861 0.9405 0.4773 -0.1590 -0.0154 0.1382 166 ASN B ND2 3644 N N . GLY B 141 ? 0.5771 0.8853 0.4287 -0.1330 0.0065 0.0690 167 GLY B N 3645 C CA . GLY B 141 ? 0.5711 0.9002 0.4335 -0.1354 0.0148 0.0526 167 GLY B CA 3646 C C . GLY B 141 ? 0.5362 0.8639 0.3966 -0.1469 0.0187 0.0582 167 GLY B C 3647 O O . GLY B 141 ? 0.5351 0.8742 0.4074 -0.1463 0.0242 0.0459 167 GLY B O 3648 N N . THR B 142 ? 0.4016 0.7148 0.2472 -0.1573 0.0154 0.0765 168 THR B N 3649 C CA . THR B 142 ? 0.3976 0.7063 0.2401 -0.1694 0.0186 0.0829 168 THR B CA 3650 C C . THR B 142 ? 0.4027 0.6889 0.2557 -0.1630 0.0180 0.0852 168 THR B C 3651 O O . THR B 142 ? 0.3507 0.6193 0.2091 -0.1504 0.0133 0.0875 168 THR B O 3652 C CB . THR B 142 ? 0.4183 0.7122 0.2413 -0.1818 0.0143 0.1030 168 THR B CB 3653 O OG1 . THR B 142 ? 0.4655 0.7277 0.2838 -0.1733 0.0055 0.1181 168 THR B OG1 3654 C CG2 . THR B 142 ? 0.4901 0.8078 0.3013 -0.1898 0.0153 0.1013 168 THR B CG2 3655 N N . TYR B 143 ? 0.4602 0.7483 0.3163 -0.1719 0.0226 0.0840 169 TYR B N 3656 C CA . TYR B 143 ? 0.4395 0.7064 0.3046 -0.1681 0.0223 0.0865 169 TYR B CA 3657 C C . TYR B 143 ? 0.4065 0.6361 0.2620 -0.1675 0.0147 0.1067 169 TYR B C 3658 O O . TYR B 143 ? 0.4143 0.6336 0.2547 -0.1772 0.0116 0.1207 169 TYR B O 3659 C CB . TYR B 143 ? 0.4559 0.7333 0.3246 -0.1801 0.0285 0.0818 169 TYR B CB 3660 C CG . TYR B 143 ? 0.3454 0.6562 0.2283 -0.1772 0.0351 0.0603 169 TYR B CG 3661 C CD1 . TYR B 143 ? 0.3680 0.6798 0.2679 -0.1655 0.0367 0.0482 169 TYR B CD1 3662 C CD2 . TYR B 143 ? 0.4163 0.7574 0.2955 -0.1860 0.0395 0.0519 169 TYR B CD2 3663 C CE1 . TYR B 143 ? 0.3989 0.7390 0.3122 -0.1610 0.0415 0.0284 169 TYR B CE1 3664 C CE2 . TYR B 143 ? 0.4088 0.7795 0.3020 -0.1819 0.0447 0.0314 169 TYR B CE2 3665 C CZ . TYR B 143 ? 0.4048 0.7738 0.3152 -0.1687 0.0453 0.0199 169 TYR B CZ 3666 O OH . TYR B 143 ? 0.4333 0.8294 0.3578 -0.1629 0.0492 -0.0004 169 TYR B OH 3667 N N . ARG B 144 ? 0.3540 0.5633 0.2184 -0.1557 0.0115 0.1080 170 ARG B N 3668 C CA . ARG B 144 ? 0.3973 0.5696 0.2559 -0.1531 0.0040 0.1251 170 ARG B CA 3669 C C . ARG B 144 ? 0.5009 0.6562 0.3550 -0.1661 0.0054 0.1336 170 ARG B C 3670 O O . ARG B 144 ? 0.4627 0.6286 0.3257 -0.1714 0.0117 0.1241 170 ARG B O 3671 C CB . ARG B 144 ? 0.4272 0.5850 0.2982 -0.1379 0.0011 0.1222 170 ARG B CB 3672 C CG . ARG B 144 ? 0.4015 0.5220 0.2687 -0.1317 -0.0077 0.1378 170 ARG B CG 3673 C CD . ARG B 144 ? 0.4176 0.5254 0.2983 -0.1182 -0.0098 0.1339 170 ARG B CD 3674 N NE . ARG B 144 ? 0.4372 0.5609 0.3238 -0.1059 -0.0111 0.1254 170 ARG B NE 3675 C CZ . ARG B 144 ? 0.4565 0.5740 0.3394 -0.0969 -0.0186 0.1312 170 ARG B CZ 3676 N NH1 . ARG B 144 ? 0.3688 0.4649 0.2422 -0.0979 -0.0256 0.1457 170 ARG B NH1 3677 N NH2 . ARG B 144 ? 0.3637 0.4965 0.2529 -0.0867 -0.0194 0.1218 170 ARG B NH2 3678 N N . GLU B 145 ? 0.4676 0.5960 0.3084 -0.1704 -0.0010 0.1508 171 GLU B N 3679 C CA . GLU B 145 ? 0.5110 0.6206 0.3444 -0.1841 -0.0005 0.1603 171 GLU B CA 3680 C C . GLU B 145 ? 0.5093 0.5898 0.3520 -0.1805 -0.0019 0.1620 171 GLU B C 3681 O O . GLU B 145 ? 0.6328 0.6831 0.4682 -0.1859 -0.0059 0.1740 171 GLU B O 3682 C CB . GLU B 145 ? 0.8864 0.9776 0.7008 -0.1899 -0.0073 0.1781 171 GLU B CB 3683 C CG . GLU B 145 ? 1.0146 1.0630 0.8254 -0.1806 -0.0172 0.1930 171 GLU B CG 3684 C CD . GLU B 145 ? 1.1821 1.2113 0.9738 -0.1888 -0.0232 0.2106 171 GLU B CD 3685 O OE1 . GLU B 145 ? 1.2132 1.2639 0.9927 -0.2000 -0.0208 0.2125 171 GLU B OE1 3686 O OE2 . GLU B 145 ? 1.2308 1.2229 1.0195 -0.1838 -0.0303 0.2221 171 GLU B OE2 3687 N N . ASN B 146 ? 0.4523 0.5419 0.3110 -0.1721 0.0016 0.1492 172 ASN B N 3688 C CA . ASN B 146 ? 0.4638 0.5266 0.3316 -0.1685 0.0001 0.1500 172 ASN B CA 3689 C C . ASN B 146 ? 0.4928 0.5533 0.3600 -0.1842 0.0048 0.1490 172 ASN B C 3690 O O . ASN B 146 ? 0.5405 0.6208 0.4003 -0.1975 0.0092 0.1482 172 ASN B O 3691 C CB . ASN B 146 ? 0.4037 0.4774 0.2883 -0.1562 0.0024 0.1370 172 ASN B CB 3692 C CG . ASN B 146 ? 0.4017 0.5155 0.2950 -0.1590 0.0110 0.1203 172 ASN B CG 3693 O OD1 . ASN B 146 ? 0.4328 0.5638 0.3242 -0.1716 0.0163 0.1160 172 ASN B OD1 3694 N ND2 . ASN B 146 ? 0.3665 0.4954 0.2699 -0.1465 0.0120 0.1101 172 ASN B ND2 3695 N N . VAL B 147 ? 0.4384 0.4754 0.3135 -0.1829 0.0039 0.1485 173 VAL B N 3696 C CA . VAL B 147 ? 0.4897 0.5189 0.3633 -0.1980 0.0070 0.1490 173 VAL B CA 3697 C C . VAL B 147 ? 0.4702 0.5390 0.3514 -0.2075 0.0160 0.1345 173 VAL B C 3698 O O . VAL B 147 ? 0.4946 0.5705 0.3693 -0.2230 0.0193 0.1360 173 VAL B O 3699 C CB . VAL B 147 ? 0.4855 0.4813 0.3673 -0.1937 0.0038 0.1493 173 VAL B CB 3700 C CG1 . VAL B 147 ? 0.4452 0.4556 0.3450 -0.1848 0.0072 0.1345 173 VAL B CG1 3701 C CG2 . VAL B 147 ? 0.5197 0.5020 0.3969 -0.2100 0.0056 0.1523 173 VAL B CG2 3702 N N . TRP B 148 ? 0.4605 0.5560 0.3553 -0.1978 0.0197 0.1203 174 TRP B N 3703 C CA . TRP B 148 ? 0.4198 0.5534 0.3240 -0.2034 0.0274 0.1048 174 TRP B CA 3704 C C . TRP B 148 ? 0.4651 0.6272 0.3596 -0.2112 0.0306 0.1037 174 TRP B C 3705 O O . TRP B 148 ? 0.4200 0.6024 0.3143 -0.2235 0.0356 0.0982 174 TRP B O 3706 C CB . TRP B 148 ? 0.3419 0.4947 0.2635 -0.1890 0.0296 0.0896 174 TRP B CB 3707 C CG . TRP B 148 ? 0.3474 0.4761 0.2790 -0.1824 0.0268 0.0891 174 TRP B CG 3708 C CD1 . TRP B 148 ? 0.3285 0.4545 0.2700 -0.1875 0.0287 0.0825 174 TRP B CD1 3709 C CD2 . TRP B 148 ? 0.3198 0.4242 0.2525 -0.1698 0.0213 0.0952 174 TRP B CD2 3710 N NE1 . TRP B 148 ? 0.3719 0.4727 0.3202 -0.1792 0.0247 0.0836 174 TRP B NE1 3711 C CE2 . TRP B 148 ? 0.3525 0.4397 0.2957 -0.1682 0.0203 0.0915 174 TRP B CE2 3712 C CE3 . TRP B 148 ? 0.3560 0.4526 0.2819 -0.1596 0.0168 0.1028 174 TRP B CE3 3713 C CZ2 . TRP B 148 ? 0.3418 0.4038 0.2888 -0.1570 0.0151 0.0953 174 TRP B CZ2 3714 C CZ3 . TRP B 148 ? 0.3179 0.3902 0.2478 -0.1478 0.0115 0.1070 174 TRP B CZ3 3715 C CH2 . TRP B 148 ? 0.3249 0.3794 0.2661 -0.1447 0.0104 0.1018 174 TRP B CH2 3716 N N . TYR B 149 ? 0.3918 0.5566 0.2786 -0.2044 0.0277 0.1083 175 TYR B N 3717 C CA . TYR B 149 ? 0.4032 0.5961 0.2812 -0.2118 0.0307 0.1060 175 TYR B CA 3718 C C . TYR B 149 ? 0.5431 0.7256 0.4048 -0.2299 0.0303 0.1190 175 TYR B C 3719 O O . TYR B 149 ? 0.5019 0.7108 0.3599 -0.2420 0.0353 0.1138 175 TYR B O 3720 C CB . TYR B 149 ? 0.4275 0.6239 0.2996 -0.2015 0.0270 0.1086 175 TYR B CB 3721 C CG . TYR B 149 ? 0.5032 0.7270 0.3650 -0.2105 0.0297 0.1069 175 TYR B CG 3722 C CD1 . TYR B 149 ? 0.4287 0.6910 0.2996 -0.2091 0.0358 0.0887 175 TYR B CD1 3723 C CD2 . TYR B 149 ? 0.4893 0.7000 0.3323 -0.2202 0.0258 0.1229 175 TYR B CD2 3724 C CE1 . TYR B 149 ? 0.4476 0.7355 0.3095 -0.2176 0.0383 0.0861 175 TYR B CE1 3725 C CE2 . TYR B 149 ? 0.5157 0.7522 0.3487 -0.2295 0.0284 0.1212 175 TYR B CE2 3726 C CZ . TYR B 149 ? 0.5396 0.8152 0.3823 -0.2285 0.0349 0.1025 175 TYR B CZ 3727 O OH . TYR B 149 ? 0.6260 0.9281 0.4592 -0.2378 0.0376 0.1000 175 TYR B OH 3728 N N . THR B 150 ? 0.4273 0.6893 0.4990 -0.1382 0.0635 0.1033 176 THR B N 3729 C CA . THR B 150 ? 0.4478 0.7054 0.5199 -0.1485 0.0663 0.1193 176 THR B CA 3730 C C . THR B 150 ? 0.5196 0.7795 0.6003 -0.1596 0.0686 0.1164 176 THR B C 3731 O O . THR B 150 ? 0.5595 0.8344 0.6398 -0.1672 0.0708 0.1238 176 THR B O 3732 C CB . THR B 150 ? 0.4062 0.6307 0.4791 -0.1501 0.0667 0.1330 176 THR B CB 3733 O OG1 . THR B 150 ? 0.5892 0.8138 0.6541 -0.1396 0.0643 0.1367 176 THR B OG1 3734 C CG2 . THR B 150 ? 0.5461 0.7643 0.6199 -0.1604 0.0695 0.1497 176 THR B CG2 3735 N N . GLN B 151 ? 0.3838 0.6305 0.4725 -0.1607 0.0678 0.1054 177 GLN B N 3736 C CA . GLN B 151 ? 0.3799 0.6274 0.4778 -0.1713 0.0695 0.1017 177 GLN B CA 3737 C C . GLN B 151 ? 0.3811 0.6597 0.4790 -0.1692 0.0686 0.0887 177 GLN B C 3738 O O . GLN B 151 ? 0.4193 0.7081 0.5225 -0.1782 0.0703 0.0885 177 GLN B O 3739 C CB . GLN B 151 ? 0.3567 0.5770 0.4637 -0.1738 0.0684 0.0953 177 GLN B CB 3740 C CG . GLN B 151 ? 0.3514 0.5377 0.4601 -0.1782 0.0695 0.1080 177 GLN B CG 3741 C CD . GLN B 151 ? 0.4105 0.5911 0.5220 -0.1901 0.0731 0.1220 177 GLN B CD 3742 O OE1 . GLN B 151 ? 0.4732 0.6696 0.5899 -0.1985 0.0749 0.1198 177 GLN B OE1 3743 N NE2 . GLN B 151 ? 0.4944 0.6526 0.6026 -0.1907 0.0741 0.1368 177 GLN B NE2 3744 N N . LEU B 152 ? 0.3405 0.6335 0.4327 -0.1570 0.0659 0.0777 178 LEU B N 3745 C CA . LEU B 152 ? 0.2590 0.5757 0.3522 -0.1531 0.0643 0.0629 178 LEU B CA 3746 C C . LEU B 152 ? 0.3247 0.6689 0.4088 -0.1443 0.0631 0.0583 178 LEU B C 3747 O O . LEU B 152 ? 0.2989 0.6646 0.3830 -0.1417 0.0621 0.0477 178 LEU B O 3748 C CB . LEU B 152 ? 0.2886 0.5939 0.3865 -0.1461 0.0614 0.0491 178 LEU B CB 3749 C CG . LEU B 152 ? 0.3021 0.5792 0.4085 -0.1530 0.0616 0.0512 178 LEU B CG 3750 C CD1 . LEU B 152 ? 0.2971 0.5636 0.4056 -0.1437 0.0581 0.0391 178 LEU B CD1 3751 C CD2 . LEU B 152 ? 0.3739 0.6544 0.4886 -0.1649 0.0630 0.0506 178 LEU B CD2 3752 N N . GLY B 153 ? 0.2526 0.5963 0.3292 -0.1395 0.0628 0.0655 179 GLY B N 3753 C CA . GLY B 153 ? 0.3996 0.7684 0.4680 -0.1310 0.0610 0.0597 179 GLY B CA 3754 C C . GLY B 153 ? 0.4032 0.7715 0.4709 -0.1181 0.0575 0.0436 179 GLY B C 3755 O O . GLY B 153 ? 0.3502 0.7000 0.4236 -0.1158 0.0565 0.0378 179 GLY B O 3756 N N . PRO B 154 ? 0.4299 0.8189 0.4911 -0.1098 0.0554 0.0358 180 PRO B N 3757 C CA . PRO B 154 ? 0.3856 0.7723 0.4458 -0.0971 0.0520 0.0212 180 PRO B CA 3758 C C . PRO B 154 ? 0.3611 0.7435 0.4278 -0.0931 0.0505 0.0079 180 PRO B C 3759 O O . PRO B 154 ? 0.2483 0.6194 0.3163 -0.0837 0.0479 -0.0011 180 PRO B O 3760 C CB . PRO B 154 ? 0.3125 0.7261 0.3654 -0.0918 0.0504 0.0154 180 PRO B CB 3761 C CG . PRO B 154 ? 0.4320 0.8666 0.4839 -0.1015 0.0528 0.0227 180 PRO B CG 3762 C CD . PRO B 154 ? 0.4024 0.8194 0.4576 -0.1125 0.0560 0.0394 180 PRO B CD 3763 N N . ASP B 155 ? 0.2736 0.6651 0.3444 -0.1000 0.0519 0.0072 181 ASP B N 3764 C CA . ASP B 155 ? 0.2379 0.6289 0.3141 -0.0957 0.0500 -0.0053 181 ASP B CA 3765 C C . ASP B 155 ? 0.2339 0.5990 0.3166 -0.0953 0.0492 -0.0059 181 ASP B C 3766 O O . ASP B 155 ? 0.1978 0.5612 0.2845 -0.0899 0.0470 -0.0162 181 ASP B O 3767 C CB . ASP B 155 ? 0.3476 0.7572 0.4265 -0.1036 0.0516 -0.0058 181 ASP B CB 3768 C CG . ASP B 155 ? 0.4433 0.8810 0.5176 -0.0982 0.0504 -0.0146 181 ASP B CG 3769 O OD1 . ASP B 155 ? 0.4633 0.9078 0.5315 -0.0912 0.0490 -0.0173 181 ASP B OD1 3770 O OD2 . ASP B 155 ? 0.5800 1.0336 0.6569 -0.1009 0.0507 -0.0195 181 ASP B OD2 3771 N N . TYR B 156 ? 0.2107 0.5567 0.2944 -0.1006 0.0508 0.0050 182 TYR B N 3772 C CA . TYR B 156 ? 0.2736 0.5959 0.3634 -0.1005 0.0499 0.0041 182 TYR B CA 3773 C C . TYR B 156 ? 0.2470 0.5627 0.3362 -0.0871 0.0463 -0.0065 182 TYR B C 3774 O O . TYR B 156 ? 0.1857 0.4898 0.2800 -0.0841 0.0444 -0.0125 182 TYR B O 3775 C CB . TYR B 156 ? 0.1861 0.4885 0.2765 -0.1079 0.0521 0.0178 182 TYR B CB 3776 C CG . TYR B 156 ? 0.1966 0.4882 0.2823 -0.1004 0.0512 0.0212 182 TYR B CG 3777 C CD1 . TYR B 156 ? 0.1685 0.4424 0.2573 -0.0941 0.0491 0.0166 182 TYR B CD1 3778 C CD2 . TYR B 156 ? 0.1848 0.4850 0.2629 -0.0999 0.0522 0.0294 182 TYR B CD2 3779 C CE1 . TYR B 156 ? 0.2470 0.5122 0.3318 -0.0877 0.0483 0.0199 182 TYR B CE1 3780 C CE2 . TYR B 156 ? 0.2203 0.5121 0.2940 -0.0932 0.0511 0.0325 182 TYR B CE2 3781 C CZ . TYR B 156 ? 0.2382 0.5124 0.3154 -0.0872 0.0493 0.0278 182 TYR B CZ 3782 O OH . TYR B 156 ? 0.2336 0.5010 0.3068 -0.0808 0.0483 0.0311 182 TYR B OH 3783 N N . ILE B 157 ? 0.2298 0.5532 0.3128 -0.0791 0.0452 -0.0090 183 ILE B N 3784 C CA . ILE B 157 ? 0.1798 0.4957 0.2626 -0.0667 0.0419 -0.0185 183 ILE B CA 3785 C C . ILE B 157 ? 0.1422 0.4657 0.2278 -0.0604 0.0394 -0.0310 183 ILE B C 3786 O O . ILE B 157 ? 0.1346 0.4456 0.2249 -0.0564 0.0373 -0.0354 183 ILE B O 3787 C CB . ILE B 157 ? 0.2210 0.5434 0.2969 -0.0604 0.0411 -0.0191 183 ILE B CB 3788 C CG1 . ILE B 157 ? 0.1974 0.5100 0.2706 -0.0651 0.0430 -0.0062 183 ILE B CG1 3789 C CG2 . ILE B 157 ? 0.1816 0.4970 0.2584 -0.0479 0.0374 -0.0305 183 ILE B CG2 3790 C CD1 . ILE B 157 ? 0.1919 0.5142 0.2576 -0.0605 0.0423 -0.0054 183 ILE B CD1 3791 N N . PRO B 158 ? 0.1976 0.5425 0.2806 -0.0597 0.0394 -0.0361 184 PRO B N 3792 C CA . PRO B 158 ? 0.1452 0.4951 0.2313 -0.0530 0.0369 -0.0473 184 PRO B CA 3793 C C . PRO B 158 ? 0.1480 0.4951 0.2400 -0.0592 0.0373 -0.0464 184 PRO B C 3794 O O . PRO B 158 ? 0.1412 0.4848 0.2365 -0.0528 0.0347 -0.0538 184 PRO B O 3795 C CB . PRO B 158 ? 0.1902 0.5654 0.2725 -0.0523 0.0372 -0.0523 184 PRO B CB 3796 C CG . PRO B 158 ? 0.2530 0.6381 0.3315 -0.0629 0.0406 -0.0414 184 PRO B CG 3797 C CD . PRO B 158 ? 0.1584 0.5241 0.2356 -0.0635 0.0412 -0.0332 184 PRO B CD 3798 N N . ASN B 159 ? 0.1547 0.5031 0.2481 -0.0716 0.0405 -0.0374 185 ASN B N 3799 C CA . ASN B 159 ? 0.1571 0.5017 0.2567 -0.0785 0.0407 -0.0371 185 ASN B CA 3800 C C . ASN B 159 ? 0.1500 0.4728 0.2535 -0.0747 0.0385 -0.0387 185 ASN B C 3801 O O . ASN B 159 ? 0.1451 0.4671 0.2527 -0.0734 0.0365 -0.0445 185 ASN B O 3802 C CB . ASN B 159 ? 0.1866 0.5328 0.2878 -0.0934 0.0445 -0.0263 185 ASN B CB 3803 C CG . ASN B 159 ? 0.3242 0.6952 0.4231 -0.0984 0.0464 -0.0256 185 ASN B CG 3804 O OD1 . ASN B 159 ? 0.2513 0.6392 0.3483 -0.0914 0.0448 -0.0347 185 ASN B OD1 3805 N ND2 . ASN B 159 ? 0.3127 0.6860 0.4119 -0.1107 0.0498 -0.0144 185 ASN B ND2 3806 N N . ALA B 160 ? 0.1720 0.4790 0.2739 -0.0725 0.0386 -0.0338 186 ALA B N 3807 C CA . ALA B 160 ? 0.1712 0.4589 0.2765 -0.0684 0.0365 -0.0353 186 ALA B CA 3808 C C . ALA B 160 ? 0.1437 0.4315 0.2491 -0.0554 0.0325 -0.0452 186 ALA B C 3809 O O . ALA B 160 ? 0.1197 0.4001 0.2287 -0.0529 0.0302 -0.0489 186 ALA B O 3810 C CB . ALA B 160 ? 0.1600 0.4332 0.2633 -0.0680 0.0375 -0.0279 186 ALA B CB 3811 N N . TYR B 161 ? 0.1225 0.4184 0.2239 -0.0473 0.0316 -0.0493 187 TYR B N 3812 C CA . TYR B 161 ? 0.1704 0.4646 0.2723 -0.0353 0.0279 -0.0578 187 TYR B CA 3813 C C . TYR B 161 ? 0.1306 0.4372 0.2352 -0.0349 0.0267 -0.0636 187 TYR B C 3814 O O . TYR B 161 ? 0.1161 0.4169 0.2230 -0.0278 0.0236 -0.0679 187 TYR B O 3815 C CB . TYR B 161 ? 0.1700 0.4688 0.2678 -0.0277 0.0271 -0.0615 187 TYR B CB 3816 C CG . TYR B 161 ? 0.1462 0.4293 0.2424 -0.0249 0.0268 -0.0574 187 TYR B CG 3817 C CD1 . TYR B 161 ? 0.1616 0.4288 0.2597 -0.0160 0.0237 -0.0600 187 TYR B CD1 3818 C CD2 . TYR B 161 ? 0.1964 0.4807 0.2894 -0.0317 0.0298 -0.0498 187 TYR B CD2 3819 C CE1 . TYR B 161 ? 0.1207 0.3743 0.2176 -0.0138 0.0235 -0.0561 187 TYR B CE1 3820 C CE2 . TYR B 161 ? 0.1551 0.4266 0.2467 -0.0293 0.0296 -0.0459 187 TYR B CE2 3821 C CZ . TYR B 161 ? 0.1819 0.4384 0.2756 -0.0204 0.0264 -0.0495 187 TYR B CZ 3822 O OH . TYR B 161 ? 0.1177 0.3628 0.2102 -0.0183 0.0263 -0.0454 187 TYR B OH 3823 N N . ALA B 162 ? 0.1290 0.4530 0.2332 -0.0428 0.0290 -0.0632 188 ALA B N 3824 C CA . ALA B 162 ? 0.1330 0.4702 0.2400 -0.0432 0.0280 -0.0685 188 ALA B CA 3825 C C . ALA B 162 ? 0.1677 0.4957 0.2791 -0.0478 0.0271 -0.0674 188 ALA B C 3826 O O . ALA B 162 ? 0.1648 0.4967 0.2784 -0.0432 0.0246 -0.0728 188 ALA B O 3827 C CB . ALA B 162 ? 0.1435 0.5021 0.2495 -0.0516 0.0308 -0.0676 188 ALA B CB 3828 N N . VAL B 163 ? 0.1730 0.4894 0.2858 -0.0568 0.0291 -0.0607 189 VAL B N 3829 C CA . VAL B 163 ? 0.1575 0.4641 0.2745 -0.0612 0.0280 -0.0609 189 VAL B CA 3830 C C . VAL B 163 ? 0.1600 0.4537 0.2769 -0.0496 0.0244 -0.0643 189 VAL B C 3831 O O . VAL B 163 ? 0.1201 0.4146 0.2391 -0.0472 0.0219 -0.0686 189 VAL B O 3832 C CB . VAL B 163 ? 0.2285 0.5230 0.3476 -0.0732 0.0308 -0.0531 189 VAL B CB 3833 C CG1 . VAL B 163 ? 0.1907 0.4725 0.3141 -0.0763 0.0291 -0.0550 189 VAL B CG1 3834 C CG2 . VAL B 163 ? 0.1485 0.4551 0.2688 -0.0859 0.0343 -0.0486 189 VAL B CG2 3835 N N . ALA B 164 ? 0.1176 0.4006 0.2318 -0.0425 0.0239 -0.0620 190 ALA B N 3836 C CA . ALA B 164 ? 0.1725 0.4425 0.2865 -0.0316 0.0205 -0.0640 190 ALA B CA 3837 C C . ALA B 164 ? 0.1061 0.3839 0.2200 -0.0218 0.0174 -0.0699 190 ALA B C 3838 O O . ALA B 164 ? 0.1553 0.4279 0.2705 -0.0161 0.0144 -0.0716 190 ALA B O 3839 C CB . ALA B 164 ? 0.1009 0.3591 0.2123 -0.0267 0.0208 -0.0604 190 ALA B CB 3840 N N . ARG B 165 ? 0.1105 0.4016 0.2230 -0.0197 0.0180 -0.0729 191 ARG B N 3841 C CA . ARG B 165 ? 0.1127 0.4132 0.2262 -0.0112 0.0154 -0.0786 191 ARG B CA 3842 C C . ARG B 165 ? 0.2036 0.5141 0.3197 -0.0140 0.0143 -0.0811 191 ARG B C 3843 O O . ARG B 165 ? 0.1842 0.4957 0.3015 -0.0059 0.0112 -0.0838 191 ARG B O 3844 C CB . ARG B 165 ? 0.1186 0.4349 0.2306 -0.0103 0.0167 -0.0822 191 ARG B CB 3845 C CG . ARG B 165 ? 0.1167 0.4258 0.2266 -0.0033 0.0162 -0.0831 191 ARG B CG 3846 C CD . ARG B 165 ? 0.2312 0.5305 0.3436 0.0089 0.0124 -0.0861 191 ARG B CD 3847 N NE . ARG B 165 ? 0.1161 0.4130 0.2277 0.0149 0.0120 -0.0893 191 ARG B NE 3848 C CZ . ARG B 165 ? 0.2049 0.4848 0.3175 0.0215 0.0100 -0.0884 191 ARG B CZ 3849 N NH1 . ARG B 165 ? 0.1305 0.3942 0.2444 0.0236 0.0084 -0.0836 191 ARG B NH1 3850 N NH2 . ARG B 165 ? 0.1437 0.4236 0.2559 0.0259 0.0097 -0.0927 191 ARG B NH2 3851 N N . SER B 166 ? 0.1658 0.4837 0.2828 -0.0259 0.0168 -0.0799 192 SER B N 3852 C CA . SER B 166 ? 0.1527 0.4827 0.2723 -0.0300 0.0160 -0.0833 192 SER B CA 3853 C C . SER B 166 ? 0.1985 0.5180 0.3193 -0.0278 0.0134 -0.0835 192 SER B C 3854 O O . SER B 166 ? 0.1585 0.4881 0.2808 -0.0283 0.0117 -0.0873 192 SER B O 3855 C CB . SER B 166 ? 0.1806 0.5202 0.3019 -0.0446 0.0195 -0.0817 192 SER B CB 3856 O OG . SER B 166 ? 0.2284 0.5530 0.3510 -0.0529 0.0209 -0.0773 192 SER B OG 3857 N N . VAL B 167 ? 0.1145 0.4154 0.2343 -0.0253 0.0129 -0.0798 193 VAL B N 3858 C CA . VAL B 167 ? 0.1110 0.4028 0.2314 -0.0228 0.0103 -0.0801 193 VAL B CA 3859 C C . VAL B 167 ? 0.1913 0.4843 0.3108 -0.0100 0.0066 -0.0814 193 VAL B C 3860 O O . VAL B 167 ? 0.1958 0.4882 0.3152 -0.0070 0.0040 -0.0823 193 VAL B O 3861 C CB . VAL B 167 ? 0.1372 0.4097 0.2571 -0.0238 0.0110 -0.0756 193 VAL B CB 3862 C CG1 . VAL B 167 ? 0.1792 0.4449 0.2996 -0.0218 0.0084 -0.0769 193 VAL B CG1 3863 C CG2 . VAL B 167 ? 0.2076 0.4781 0.3292 -0.0365 0.0148 -0.0730 193 VAL B CG2 3864 N N . ASN B 168 ? 0.1347 0.4297 0.2536 -0.0027 0.0062 -0.0814 194 ASN B N 3865 C CA . ASN B 168 ? 0.1166 0.4125 0.2362 0.0090 0.0029 -0.0820 194 ASN B CA 3866 C C . ASN B 168 ? 0.1420 0.4206 0.2608 0.0158 0.0005 -0.0775 194 ASN B C 3867 O O . ASN B 168 ? 0.1614 0.4421 0.2807 0.0212 -0.0023 -0.0768 194 ASN B O 3868 C CB . ASN B 168 ? 0.2193 0.5332 0.3402 0.0090 0.0013 -0.0859 194 ASN B CB 3869 C CG . ASN B 168 ? 0.4289 0.7551 0.5517 0.0164 0.0003 -0.0887 194 ASN B CG 3870 O OD1 . ASN B 168 ? 0.4528 0.7810 0.5758 0.0170 0.0019 -0.0900 194 ASN B OD1 3871 N ND2 . ASN B 168 ? 0.5657 0.9016 0.6901 0.0223 -0.0025 -0.0898 194 ASN B ND2 3872 N N . THR B 169 ? 0.1067 0.3694 0.2242 0.0154 0.0016 -0.0739 195 THR B N 3873 C CA . THR B 169 ? 0.1165 0.3625 0.2333 0.0216 -0.0003 -0.0690 195 THR B CA 3874 C C . THR B 169 ? 0.1636 0.4020 0.2820 0.0310 -0.0016 -0.0671 195 THR B C 3875 O O . THR B 169 ? 0.1500 0.3944 0.2695 0.0320 -0.0006 -0.0703 195 THR B O 3876 C CB . THR B 169 ? 0.1429 0.3757 0.2581 0.0166 0.0015 -0.0660 195 THR B CB 3877 O OG1 . THR B 169 ? 0.1356 0.3623 0.2503 0.0172 0.0033 -0.0650 195 THR B OG1 3878 C CG2 . THR B 169 ? 0.1717 0.4117 0.2872 0.0056 0.0037 -0.0686 195 THR B CG2 3879 N N . PRO B 170 ? 0.1876 0.4132 0.3066 0.0375 -0.0037 -0.0620 196 PRO B N 3880 C CA . PRO B 170 ? 0.1952 0.4111 0.3171 0.0452 -0.0045 -0.0598 196 PRO B CA 3881 C C . PRO B 170 ? 0.1837 0.3864 0.3042 0.0434 -0.0028 -0.0585 196 PRO B C 3882 O O . PRO B 170 ? 0.2237 0.4173 0.3468 0.0489 -0.0034 -0.0572 196 PRO B O 3883 C CB . PRO B 170 ? 0.2110 0.4195 0.3348 0.0515 -0.0070 -0.0536 196 PRO B CB 3884 C CG . PRO B 170 ? 0.2822 0.4902 0.4016 0.0464 -0.0070 -0.0520 196 PRO B CG 3885 C CD . PRO B 170 ? 0.2498 0.4726 0.3675 0.0387 -0.0055 -0.0584 196 PRO B CD 3886 N N . SER B 171 ? 0.1318 0.3340 0.2488 0.0358 -0.0007 -0.0590 197 SER B N 3887 C CA . SER B 171 ? 0.0843 0.2749 0.1996 0.0341 0.0008 -0.0570 197 SER B CA 3888 C C . SER B 171 ? 0.0869 0.2828 0.2023 0.0335 0.0024 -0.0615 197 SER B C 3889 O O . SER B 171 ? 0.1172 0.3279 0.2324 0.0300 0.0036 -0.0659 197 SER B O 3890 C CB . SER B 171 ? 0.1079 0.2972 0.2206 0.0265 0.0027 -0.0555 197 SER B CB 3891 O OG . SER B 171 ? 0.1364 0.3216 0.2487 0.0273 0.0012 -0.0526 197 SER B OG 3892 N N . LYS B 172 ? 0.0864 0.2716 0.2020 0.0365 0.0022 -0.0606 198 LYS B N 3893 C CA . LYS B 172 ? 0.1008 0.2917 0.2154 0.0350 0.0038 -0.0653 198 LYS B CA 3894 C C . LYS B 172 ? 0.0852 0.2816 0.1960 0.0264 0.0068 -0.0640 198 LYS B C 3895 O O . LYS B 172 ? 0.1447 0.3324 0.2542 0.0234 0.0074 -0.0591 198 LYS B O 3896 C CB . LYS B 172 ? 0.1403 0.3188 0.2563 0.0396 0.0027 -0.0652 198 LYS B CB 3897 C CG . LYS B 172 ? 0.1843 0.3542 0.3055 0.0476 0.0000 -0.0643 198 LYS B CG 3898 C CD . LYS B 172 ? 0.2291 0.4104 0.3540 0.0519 -0.0008 -0.0707 198 LYS B CD 3899 C CE . LYS B 172 ? 0.3771 0.5499 0.5087 0.0602 -0.0032 -0.0690 198 LYS B CE 3900 N NZ . LYS B 172 ? 0.4192 0.5777 0.5534 0.0629 -0.0040 -0.0684 198 LYS B NZ 3901 N N . LEU B 173 ? 0.0888 0.3000 0.1981 0.0224 0.0088 -0.0681 199 LEU B N 3902 C CA . LEU B 173 ? 0.1228 0.3398 0.2291 0.0138 0.0121 -0.0654 199 LEU B CA 3903 C C . LEU B 173 ? 0.0879 0.3037 0.1917 0.0142 0.0130 -0.0660 199 LEU B C 3904 O O . LEU B 173 ? 0.1081 0.3320 0.2115 0.0172 0.0126 -0.0718 199 LEU B O 3905 C CB . LEU B 173 ? 0.0924 0.3279 0.1981 0.0076 0.0142 -0.0677 199 LEU B CB 3906 C CG . LEU B 173 ? 0.1066 0.3461 0.2150 0.0071 0.0130 -0.0685 199 LEU B CG 3907 C CD1 . LEU B 173 ? 0.1078 0.3667 0.2159 -0.0001 0.0153 -0.0708 199 LEU B CD1 3908 C CD2 . LEU B 173 ? 0.0881 0.3161 0.1976 0.0046 0.0126 -0.0638 199 LEU B CD2 3909 N N . TYR B 174 ? 0.0835 0.2903 0.1859 0.0114 0.0140 -0.0604 200 TYR B N 3910 C CA . TYR B 174 ? 0.0837 0.2903 0.1835 0.0114 0.0148 -0.0602 200 TYR B CA 3911 C C . TYR B 174 ? 0.1019 0.3187 0.1983 0.0028 0.0185 -0.0553 200 TYR B C 3912 O O . TYR B 174 ? 0.0978 0.3152 0.1950 -0.0035 0.0205 -0.0502 200 TYR B O 3913 C CB . TYR B 174 ? 0.0786 0.2680 0.1794 0.0152 0.0131 -0.0566 200 TYR B CB 3914 C CG . TYR B 174 ? 0.1501 0.3290 0.2537 0.0231 0.0098 -0.0604 200 TYR B CG 3915 C CD1 . TYR B 174 ? 0.0808 0.2553 0.1877 0.0277 0.0076 -0.0618 200 TYR B CD1 3916 C CD2 . TYR B 174 ? 0.0797 0.2534 0.1831 0.0254 0.0089 -0.0618 200 TYR B CD2 3917 C CE1 . TYR B 174 ? 0.1006 0.2649 0.2110 0.0343 0.0049 -0.0635 200 TYR B CE1 3918 C CE2 . TYR B 174 ? 0.0818 0.2454 0.1891 0.0314 0.0060 -0.0649 200 TYR B CE2 3919 C CZ . TYR B 174 ? 0.1556 0.3139 0.2665 0.0358 0.0042 -0.0652 200 TYR B CZ 3920 O OH . TYR B 174 ? 0.1102 0.2581 0.2259 0.0414 0.0016 -0.0670 200 TYR B OH 3921 N N . ILE B 175 ? 0.0883 0.3129 0.1809 0.0023 0.0193 -0.0566 201 ILE B N 3922 C CA . ILE B 175 ? 0.0901 0.3219 0.1788 -0.0048 0.0225 -0.0495 201 ILE B CA 3923 C C . ILE B 175 ? 0.0947 0.3175 0.1824 -0.0014 0.0214 -0.0476 201 ILE B C 3924 O O . ILE B 175 ? 0.0895 0.3079 0.1780 0.0052 0.0186 -0.0542 201 ILE B O 3925 C CB . ILE B 175 ? 0.1478 0.4008 0.2319 -0.0089 0.0244 -0.0516 201 ILE B CB 3926 C CG1 . ILE B 175 ? 0.1022 0.3627 0.1818 -0.0171 0.0278 -0.0416 201 ILE B CG1 3927 C CG2 . ILE B 175 ? 0.1016 0.3616 0.1842 -0.0022 0.0221 -0.0619 201 ILE B CG2 3928 C CD1 . ILE B 175 ? 0.1117 0.3931 0.1870 -0.0233 0.0301 -0.0406 201 ILE B CD1 3929 N N . ASN B 176 ? 0.0848 0.3044 0.1714 -0.0059 0.0234 -0.0385 202 ASN B N 3930 C CA . ASN B 176 ? 0.0808 0.2912 0.1671 -0.0026 0.0222 -0.0355 202 ASN B CA 3931 C C . ASN B 176 ? 0.1516 0.3727 0.2326 -0.0077 0.0247 -0.0278 202 ASN B C 3932 O O . ASN B 176 ? 0.1206 0.3490 0.1997 -0.0152 0.0279 -0.0203 202 ASN B O 3933 C CB . ASN B 176 ? 0.0744 0.2686 0.1654 -0.0014 0.0216 -0.0310 202 ASN B CB 3934 C CG . ASN B 176 ? 0.1483 0.3314 0.2402 0.0040 0.0193 -0.0297 202 ASN B CG 3935 O OD1 . ASN B 176 ? 0.2010 0.3808 0.2931 0.0093 0.0166 -0.0357 202 ASN B OD1 3936 N ND2 . ASN B 176 ? 0.1017 0.2718 0.1909 0.0024 0.0197 -0.0207 202 ASN B ND2 3937 N N . ASP B 177 ? 0.0846 0.3070 0.1630 -0.0042 0.0231 -0.0288 203 ASP B N 3938 C CA . ASP B 177 ? 0.0892 0.3224 0.1617 -0.0083 0.0251 -0.0199 203 ASP B CA 3939 C C . ASP B 177 ? 0.1118 0.3429 0.1834 -0.0035 0.0225 -0.0212 203 ASP B C 3940 O O . ASP B 177 ? 0.1157 0.3377 0.1912 0.0024 0.0193 -0.0301 203 ASP B O 3941 C CB . ASP B 177 ? 0.0982 0.3518 0.1645 -0.0125 0.0266 -0.0213 203 ASP B CB 3942 C CG . ASP B 177 ? 0.2089 0.4709 0.2701 -0.0203 0.0301 -0.0069 203 ASP B CG 3943 O OD1 . ASP B 177 ? 0.1454 0.4020 0.2053 -0.0206 0.0306 0.0031 203 ASP B OD1 3944 O OD2 . ASP B 177 ? 0.1650 0.4380 0.2235 -0.0261 0.0322 -0.0045 203 ASP B OD2 3945 N N . TYR B 178 ? 0.1431 0.3827 0.2095 -0.0062 0.0238 -0.0114 204 TYR B N 3946 C CA . TYR B 178 ? 0.0893 0.3310 0.1542 -0.0023 0.0213 -0.0119 204 TYR B CA 3947 C C . TYR B 178 ? 0.0978 0.3615 0.1545 -0.0045 0.0214 -0.0129 204 TYR B C 3948 O O . TYR B 178 ? 0.1152 0.3915 0.1671 -0.0093 0.0238 -0.0095 204 TYR B O 3949 C CB . TYR B 178 ? 0.0920 0.3142 0.1531 -0.0020 0.0204 0.0015 204 TYR B CB 3950 C CG . TYR B 178 ? 0.1296 0.3557 0.1837 -0.0076 0.0233 0.0162 204 TYR B CG 3951 C CD1 . TYR B 178 ? 0.1939 0.4096 0.2486 -0.0125 0.0258 0.0228 204 TYR B CD1 3952 C CD2 . TYR B 178 ? 0.1961 0.4373 0.2436 -0.0083 0.0232 0.0237 204 TYR B CD2 3953 C CE1 . TYR B 178 ? 0.2011 0.4186 0.2507 -0.0182 0.0285 0.0370 204 TYR B CE1 3954 C CE2 . TYR B 178 ? 0.1770 0.4214 0.2186 -0.0133 0.0259 0.0391 204 TYR B CE2 3955 C CZ . TYR B 178 ? 0.2694 0.5005 0.3125 -0.0184 0.0285 0.0458 204 TYR B CZ 3956 O OH . TYR B 178 ? 0.2841 0.5158 0.3228 -0.0241 0.0311 0.0616 204 TYR B OH 3957 N N . ASN B 179 ? 0.0979 0.3672 0.1531 -0.0012 0.0186 -0.0174 205 ASN B N 3958 C CA . ASN B 179 ? 0.1448 0.4371 0.1923 -0.0024 0.0178 -0.0209 205 ASN B CA 3959 C C . ASN B 179 ? 0.1750 0.4792 0.2211 -0.0029 0.0177 -0.0336 205 ASN B C 3960 O O . ASN B 179 ? 0.1197 0.4459 0.1585 -0.0054 0.0178 -0.0342 205 ASN B O 3961 C CB . ASN B 179 ? 0.2267 0.5321 0.2665 -0.0069 0.0202 -0.0042 205 ASN B CB 3962 C CG . ASN B 179 ? 0.2078 0.5098 0.2472 -0.0048 0.0193 0.0064 205 ASN B CG 3963 O OD1 . ASN B 179 ? 0.3145 0.6083 0.3588 -0.0004 0.0162 -0.0004 205 ASN B OD1 3964 N ND2 . ASN B 179 ? 0.2135 0.5205 0.2470 -0.0078 0.0215 0.0236 205 ASN B ND2 3965 N N . THR B 180 ? 0.1066 0.3968 0.1597 -0.0001 0.0170 -0.0432 206 THR B N 3966 C CA . THR B 180 ? 0.1111 0.4096 0.1646 0.0009 0.0165 -0.0557 206 THR B CA 3967 C C . THR B 180 ? 0.1655 0.4559 0.2254 0.0067 0.0130 -0.0710 206 THR B C 3968 O O . THR B 180 ? 0.1612 0.4540 0.2241 0.0091 0.0119 -0.0827 206 THR B O 3969 C CB . THR B 180 ? 0.1395 0.4290 0.1965 -0.0007 0.0186 -0.0531 206 THR B CB 3970 O OG1 . THR B 180 ? 0.1639 0.4301 0.2278 0.0017 0.0182 -0.0495 206 THR B OG1 3971 C CG2 . THR B 180 ? 0.1193 0.4195 0.1707 -0.0076 0.0222 -0.0398 206 THR B CG2 3972 N N . GLU B 181 ? 0.1057 0.3868 0.1686 0.0087 0.0111 -0.0705 207 GLU B N 3973 C CA . GLU B 181 ? 0.1800 0.4500 0.2510 0.0134 0.0077 -0.0832 207 GLU B CA 3974 C C . GLU B 181 ? 0.1781 0.4662 0.2480 0.0144 0.0056 -0.0986 207 GLU B C 3975 O O . GLU B 181 ? 0.1866 0.4695 0.2642 0.0181 0.0033 -0.1121 207 GLU B O 3976 C CB . GLU B 181 ? 0.1251 0.3804 0.2002 0.0145 0.0062 -0.0771 207 GLU B CB 3977 C CG . GLU B 181 ? 0.1453 0.3817 0.2230 0.0144 0.0076 -0.0640 207 GLU B CG 3978 C CD . GLU B 181 ? 0.2283 0.4724 0.2991 0.0104 0.0104 -0.0493 207 GLU B CD 3979 O OE1 . GLU B 181 ? 0.1807 0.4436 0.2444 0.0080 0.0109 -0.0470 207 GLU B OE1 3980 O OE2 . GLU B 181 ? 0.2083 0.4404 0.2809 0.0097 0.0121 -0.0398 207 GLU B OE2 3981 N N . GLY B 182 ? 0.1185 0.4286 0.1797 0.0114 0.0060 -0.0965 208 GLY B N 3982 C CA . GLY B 182 ? 0.1276 0.4594 0.1868 0.0119 0.0037 -0.1115 208 GLY B CA 3983 C C . GLY B 182 ? 0.1951 0.5466 0.2487 0.0101 0.0046 -0.1140 208 GLY B C 3984 O O . GLY B 182 ? 0.1513 0.4994 0.2024 0.0080 0.0075 -0.1033 208 GLY B O 3985 N N . ILE B 183 ? 0.1777 0.5511 0.2309 0.0106 0.0018 -0.1285 209 ILE B N 3986 C CA . ILE B 183 ? 0.1646 0.5620 0.2135 0.0087 0.0018 -0.1306 209 ILE B CA 3987 C C . ILE B 183 ? 0.2855 0.7056 0.3228 0.0036 0.0031 -0.1171 209 ILE B C 3988 O O . ILE B 183 ? 0.2433 0.6810 0.2774 0.0028 0.0006 -0.1200 209 ILE B O 3989 C CB . ILE B 183 ? 0.2484 0.6632 0.3048 0.0114 -0.0026 -0.1516 209 ILE B CB 3990 C CG1 . ILE B 183 ? 0.2595 0.6510 0.3294 0.0168 -0.0043 -0.1634 209 ILE B CG1 3991 C CG2 . ILE B 183 ? 0.2079 0.6509 0.2607 0.0093 -0.0026 -0.1526 209 ILE B CG2 3992 C CD1 . ILE B 183 ? 0.2884 0.6950 0.3702 0.0200 -0.0089 -0.1836 209 ILE B CD1 3993 N N . ASN B 184 ? 0.1535 0.5737 0.1857 0.0000 0.0066 -0.1020 210 ASN B N 3994 C CA . ASN B 184 ? 0.1609 0.5997 0.1840 -0.0051 0.0078 -0.0859 210 ASN B CA 3995 C C . ASN B 184 ? 0.2239 0.6674 0.2445 -0.0093 0.0110 -0.0754 210 ASN B C 3996 O O . ASN B 184 ? 0.1593 0.5944 0.1847 -0.0080 0.0120 -0.0821 210 ASN B O 3997 C CB . ASN B 184 ? 0.1517 0.5751 0.1726 -0.0057 0.0091 -0.0714 210 ASN B CB 3998 C CG . ASN B 184 ? 0.1421 0.5340 0.1685 -0.0050 0.0121 -0.0639 210 ASN B CG 3999 O OD1 . ASN B 184 ? 0.1631 0.5493 0.1907 -0.0071 0.0147 -0.0591 210 ASN B OD1 4000 N ND2 . ASN B 184 ? 0.1800 0.5528 0.2106 -0.0022 0.0115 -0.0630 210 ASN B ND2 4001 N N . ASN B 185 ? 0.1742 0.6312 0.1885 -0.0143 0.0126 -0.0585 211 ASN B N 4002 C CA . ASN B 185 ? 0.2331 0.6959 0.2457 -0.0195 0.0157 -0.0483 211 ASN B CA 4003 C C . ASN B 185 ? 0.2193 0.6535 0.2363 -0.0206 0.0193 -0.0418 211 ASN B C 4004 O O . ASN B 185 ? 0.1873 0.6229 0.2060 -0.0231 0.0213 -0.0419 211 ASN B O 4005 C CB . ASN B 185 ? 0.2885 0.7686 0.2949 -0.0248 0.0166 -0.0297 211 ASN B CB 4006 C CG . ASN B 185 ? 0.3850 0.9021 0.3884 -0.0257 0.0137 -0.0351 211 ASN B CG 4007 O OD1 . ASN B 185 ? 0.2450 0.7749 0.2512 -0.0218 0.0105 -0.0538 211 ASN B OD1 4008 N ND2 . ASN B 185 ? 0.5236 1.0583 0.5229 -0.0307 0.0147 -0.0187 211 ASN B ND2 4009 N N . LYS B 186 ? 0.1548 0.5650 0.1745 -0.0187 0.0200 -0.0366 212 LYS B N 4010 C CA . LYS B 186 ? 0.1508 0.5356 0.1761 -0.0197 0.0229 -0.0307 212 LYS B CA 4011 C C . LYS B 186 ? 0.1755 0.5494 0.2079 -0.0150 0.0219 -0.0467 212 LYS B C 4012 O O . LYS B 186 ? 0.1946 0.5628 0.2302 -0.0170 0.0238 -0.0458 212 LYS B O 4013 C CB . LYS B 186 ? 0.1402 0.5042 0.1675 -0.0186 0.0234 -0.0209 212 LYS B CB 4014 C CG . LYS B 186 ? 0.1365 0.4805 0.1682 -0.0222 0.0268 -0.0093 212 LYS B CG 4015 C CD . LYS B 186 ? 0.1633 0.4884 0.1976 -0.0207 0.0271 0.0003 212 LYS B CD 4016 C CE . LYS B 186 ? 0.1638 0.4712 0.2024 -0.0252 0.0304 0.0114 212 LYS B CE 4017 N NZ . LYS B 186 ? 0.1225 0.4117 0.1645 -0.0229 0.0305 0.0195 212 LYS B NZ 4018 N N . SER B 187 ? 0.1855 0.5566 0.2208 -0.0090 0.0186 -0.0611 213 SER B N 4019 C CA . SER B 187 ? 0.1359 0.4956 0.1787 -0.0040 0.0172 -0.0752 213 SER B CA 4020 C C . SER B 187 ? 0.1699 0.5497 0.2119 -0.0043 0.0167 -0.0844 213 SER B C 4021 O O . SER B 187 ? 0.1423 0.5143 0.1898 -0.0021 0.0169 -0.0900 213 SER B O 4022 C CB . SER B 187 ? 0.1331 0.4835 0.1808 0.0021 0.0138 -0.0878 213 SER B CB 4023 O OG . SER B 187 ? 0.1601 0.5323 0.2035 0.0022 0.0114 -0.0955 213 SER B OG 4024 N N . ASP B 188 ? 0.1528 0.5599 0.1886 -0.0067 0.0158 -0.0858 214 ASP B N 4025 C CA . ASP B 188 ? 0.1620 0.5916 0.1971 -0.0075 0.0154 -0.0932 214 ASP B CA 4026 C C . ASP B 188 ? 0.2201 0.6473 0.2550 -0.0124 0.0191 -0.0826 214 ASP B C 4027 O O . ASP B 188 ? 0.2197 0.6494 0.2585 -0.0107 0.0190 -0.0903 214 ASP B O 4028 C CB . ASP B 188 ? 0.1710 0.6329 0.1995 -0.0104 0.0138 -0.0930 214 ASP B CB 4029 C CG . ASP B 188 ? 0.3562 0.8274 0.3869 -0.0057 0.0094 -0.1080 214 ASP B CG 4030 O OD1 . ASP B 188 ? 0.2934 0.7482 0.3317 0.0000 0.0073 -0.1211 214 ASP B OD1 4031 O OD2 . ASP B 188 ? 0.3934 0.8898 0.4194 -0.0079 0.0077 -0.1065 214 ASP B OD2 4032 N N . ALA B 189 ? 0.1979 0.6204 0.2289 -0.0186 0.0221 -0.0651 215 ALA B N 4033 C CA . ALA B 189 ? 0.2251 0.6444 0.2569 -0.0246 0.0257 -0.0543 215 ALA B CA 4034 C C . ALA B 189 ? 0.2905 0.6857 0.3301 -0.0218 0.0263 -0.0580 215 ALA B C 4035 O O . ALA B 189 ? 0.1800 0.5785 0.2223 -0.0234 0.0274 -0.0601 215 ALA B O 4036 C CB . ALA B 189 ? 0.1644 0.5803 0.1923 -0.0315 0.0284 -0.0349 215 ALA B CB 4037 N N . LEU B 190 ? 0.1437 0.5161 0.1870 -0.0176 0.0253 -0.0584 216 LEU B N 4038 C CA . LEU B 190 ? 0.1353 0.4853 0.1862 -0.0141 0.0251 -0.0618 216 LEU B CA 4039 C C . LEU B 190 ? 0.2152 0.5696 0.2704 -0.0081 0.0227 -0.0772 216 LEU B C 4040 O O . LEU B 190 ? 0.1354 0.4847 0.1950 -0.0078 0.0232 -0.0786 216 LEU B O 4041 C CB . LEU B 190 ? 0.1262 0.4538 0.1806 -0.0100 0.0238 -0.0605 216 LEU B CB 4042 C CG . LEU B 190 ? 0.1176 0.4219 0.1801 -0.0061 0.0229 -0.0627 216 LEU B CG 4043 C CD1 . LEU B 190 ? 0.1160 0.4147 0.1800 -0.0121 0.0259 -0.0522 216 LEU B CD1 4044 C CD2 . LEU B 190 ? 0.1683 0.4540 0.2338 -0.0019 0.0211 -0.0619 216 LEU B CD2 4045 N N . LEU B 191 ? 0.1410 0.5056 0.1954 -0.0035 0.0198 -0.0889 217 LEU B N 4046 C CA . LEU B 191 ? 0.2508 0.6196 0.3104 0.0029 0.0170 -0.1044 217 LEU B CA 4047 C C . LEU B 191 ? 0.2814 0.6699 0.3399 0.0003 0.0182 -0.1060 217 LEU B C 4048 O O . LEU B 191 ? 0.1636 0.5480 0.2278 0.0041 0.0173 -0.1123 217 LEU B O 4049 C CB . LEU B 191 ? 0.2077 0.5876 0.2672 0.0069 0.0136 -0.1167 217 LEU B CB 4050 C CG . LEU B 191 ? 0.2550 0.6397 0.3218 0.0138 0.0100 -0.1338 217 LEU B CG 4051 C CD1 . LEU B 191 ? 0.2025 0.5611 0.2784 0.0195 0.0088 -0.1363 217 LEU B CD1 4052 C CD2 . LEU B 191 ? 0.2310 0.6270 0.2992 0.0166 0.0065 -0.1460 217 LEU B CD2 4053 N N . ALA B 192 ? 0.2569 0.6676 0.3083 -0.0062 0.0201 -0.0995 218 ALA B N 4054 C CA . ALA B 192 ? 0.2374 0.6690 0.2874 -0.0100 0.0215 -0.0993 218 ALA B CA 4055 C C . ALA B 192 ? 0.3016 0.7206 0.3551 -0.0133 0.0241 -0.0918 218 ALA B C 4056 O O . ALA B 192 ? 0.2031 0.6306 0.2597 -0.0122 0.0240 -0.0974 218 ALA B O 4057 C CB . ALA B 192 ? 0.1968 0.6526 0.2389 -0.0174 0.0232 -0.0903 218 ALA B CB 4058 N N . VAL B 193 ? 0.2226 0.6224 0.2762 -0.0173 0.0262 -0.0795 219 VAL B N 4059 C CA . VAL B 193 ? 0.2302 0.6186 0.2880 -0.0212 0.0284 -0.0728 219 VAL B CA 4060 C C . VAL B 193 ? 0.2006 0.5722 0.2657 -0.0134 0.0260 -0.0817 219 VAL B C 4061 O O . VAL B 193 ? 0.1890 0.5624 0.2577 -0.0139 0.0264 -0.0833 219 VAL B O 4062 C CB . VAL B 193 ? 0.2219 0.5948 0.2790 -0.0277 0.0310 -0.0578 219 VAL B CB 4063 C CG1 . VAL B 193 ? 0.2253 0.5845 0.2883 -0.0308 0.0324 -0.0537 219 VAL B CG1 4064 C CG2 . VAL B 193 ? 0.2414 0.6311 0.2920 -0.0364 0.0336 -0.0464 219 VAL B CG2 4065 N N . VAL B 194 ? 0.1386 0.4949 0.2060 -0.0064 0.0234 -0.0871 220 VAL B N 4066 C CA . VAL B 194 ? 0.1339 0.4741 0.2085 0.0014 0.0207 -0.0945 220 VAL B CA 4067 C C . VAL B 194 ? 0.1720 0.5271 0.2493 0.0065 0.0187 -0.1067 220 VAL B C 4068 O O . VAL B 194 ? 0.1403 0.4907 0.2228 0.0098 0.0178 -0.1094 220 VAL B O 4069 C CB . VAL B 194 ? 0.1289 0.4511 0.2059 0.0074 0.0181 -0.0978 220 VAL B CB 4070 C CG1 . VAL B 194 ? 0.1587 0.4671 0.2436 0.0158 0.0149 -0.1059 220 VAL B CG1 4071 C CG2 . VAL B 194 ? 0.1328 0.4383 0.2087 0.0035 0.0197 -0.0858 220 VAL B CG2 4072 N N . GLN B 195 ? 0.1489 0.5236 0.2229 0.0072 0.0179 -0.1139 221 GLN B N 4073 C CA . GLN B 195 ? 0.1572 0.5494 0.2342 0.0119 0.0160 -0.1260 221 GLN B CA 4074 C C . GLN B 195 ? 0.1606 0.5672 0.2367 0.0072 0.0183 -0.1224 221 GLN B C 4075 O O . GLN B 195 ? 0.1632 0.5728 0.2445 0.0121 0.0169 -0.1291 221 GLN B O 4076 C CB . GLN B 195 ? 0.1655 0.5795 0.2388 0.0122 0.0147 -0.1340 221 GLN B CB 4077 C CG . GLN B 195 ? 0.3472 0.7506 0.4246 0.0189 0.0111 -0.1436 221 GLN B CG 4078 C CD . GLN B 195 ? 0.4135 0.8408 0.4874 0.0182 0.0096 -0.1515 221 GLN B CD 4079 O OE1 . GLN B 195 ? 0.4365 0.8855 0.5028 0.0118 0.0116 -0.1458 221 GLN B OE1 4080 N NE2 . GLN B 195 ? 0.3494 0.7735 0.4296 0.0247 0.0057 -0.1643 221 GLN B NE2 4081 N N . SER B 196 ? 0.1615 0.5772 0.2317 -0.0023 0.0218 -0.1112 222 SER B N 4082 C CA . SER B 196 ? 0.1653 0.5942 0.2351 -0.0087 0.0243 -0.1062 222 SER B CA 4083 C C . SER B 196 ? 0.2106 0.6213 0.2862 -0.0078 0.0244 -0.1034 222 SER B C 4084 O O . SER B 196 ? 0.1616 0.5813 0.2406 -0.0065 0.0241 -0.1076 222 SER B O 4085 C CB . SER B 196 ? 0.1685 0.6065 0.2321 -0.0198 0.0279 -0.0930 222 SER B CB 4086 O OG . SER B 196 ? 0.1746 0.6276 0.2383 -0.0269 0.0303 -0.0887 222 SER B OG 4087 N N . MET B 197 ? 0.1495 0.5361 0.2265 -0.0081 0.0245 -0.0967 223 MET B N 4088 C CA . MET B 197 ? 0.1693 0.5399 0.2516 -0.0072 0.0242 -0.0940 223 MET B CA 4089 C C . MET B 197 ? 0.1424 0.5069 0.2306 0.0034 0.0205 -0.1041 223 MET B C 4090 O O . MET B 197 ? 0.1423 0.5070 0.2344 0.0047 0.0200 -0.1050 223 MET B O 4091 C CB . MET B 197 ? 0.1345 0.4824 0.2171 -0.0098 0.0249 -0.0848 223 MET B CB 4092 C CG . MET B 197 ? 0.2555 0.6069 0.3352 -0.0212 0.0286 -0.0731 223 MET B CG 4093 S SD . MET B 197 ? 0.2116 0.5369 0.2950 -0.0238 0.0290 -0.0642 223 MET B SD 4094 C CE . MET B 197 ? 0.1968 0.5067 0.2789 -0.0155 0.0267 -0.0665 223 MET B CE 4095 N N . LYS B 198 ? 0.1440 0.4203 0.2687 0.0446 0.0136 -0.0975 224 LYS B N 4096 C CA . LYS B 198 ? 0.1600 0.4316 0.2803 0.0488 0.0084 -0.1056 224 LYS B CA 4097 C C . LYS B 198 ? 0.1935 0.4745 0.3179 0.0509 0.0094 -0.1101 224 LYS B C 4098 O O . LYS B 198 ? 0.1388 0.4164 0.2655 0.0533 0.0064 -0.1142 224 LYS B O 4099 C CB . LYS B 198 ? 0.2021 0.4719 0.3151 0.0515 0.0056 -0.1097 224 LYS B CB 4100 C CG . LYS B 198 ? 0.3259 0.5868 0.4393 0.0557 0.0008 -0.1153 224 LYS B CG 4101 C CD . LYS B 198 ? 0.3591 0.6090 0.4737 0.0555 -0.0013 -0.1112 224 LYS B CD 4102 C CE . LYS B 198 ? 0.3911 0.6339 0.5079 0.0605 -0.0049 -0.1135 224 LYS B CE 4103 N NZ . LYS B 198 ? 0.4863 0.7355 0.6082 0.0639 -0.0051 -0.1187 224 LYS B NZ 4104 N N . ALA B 199 ? 0.1406 0.4350 0.2665 0.0503 0.0139 -0.1085 225 ALA B N 4105 C CA . ALA B 199 ? 0.1463 0.4511 0.2767 0.0521 0.0157 -0.1120 225 ALA B CA 4106 C C . ALA B 199 ? 0.1443 0.4469 0.2847 0.0504 0.0167 -0.1103 225 ALA B C 4107 O O . ALA B 199 ? 0.1481 0.4559 0.2925 0.0523 0.0165 -0.1146 225 ALA B O 4108 C CB . ALA B 199 ? 0.1515 0.4732 0.2818 0.0517 0.0213 -0.1082 225 ALA B CB 4109 N N . HIS B 200 ? 0.1388 0.4347 0.2844 0.0467 0.0177 -0.1047 226 HIS B N 4110 C CA . HIS B 200 ? 0.1374 0.4320 0.2940 0.0448 0.0181 -0.1048 226 HIS B CA 4111 C C . HIS B 200 ? 0.1339 0.4175 0.2868 0.0452 0.0122 -0.1084 226 HIS B C 4112 O O . HIS B 200 ? 0.1327 0.4152 0.2936 0.0430 0.0118 -0.1093 226 HIS B O 4113 C CB . HIS B 200 ? 0.1358 0.4343 0.3065 0.0402 0.0245 -0.0960 226 HIS B CB 4114 C CG . HIS B 200 ? 0.1555 0.4678 0.3328 0.0404 0.0313 -0.0904 226 HIS B CG 4115 N ND1 . HIS B 200 ? 0.2327 0.5520 0.4049 0.0407 0.0349 -0.0843 226 HIS B ND1 4116 C CD2 . HIS B 200 ? 0.1449 0.4671 0.3329 0.0409 0.0350 -0.0900 226 HIS B CD2 4117 C CE1 . HIS B 200 ? 0.1918 0.5254 0.3709 0.0414 0.0408 -0.0799 226 HIS B CE1 4118 N NE2 . HIS B 200 ? 0.1800 0.5149 0.3695 0.0414 0.0412 -0.0830 226 HIS B NE2 4119 N N . ASN B 201 ? 0.1333 0.4104 0.2752 0.0483 0.0079 -0.1108 227 ASN B N 4120 C CA . ASN B 201 ? 0.1313 0.4001 0.2690 0.0502 0.0028 -0.1127 227 ASN B CA 4121 C C . ASN B 201 ? 0.1266 0.3899 0.2666 0.0463 0.0028 -0.1098 227 ASN B C 4122 O O . ASN B 201 ? 0.1538 0.4152 0.2933 0.0471 -0.0007 -0.1124 227 ASN B O 4123 C CB . ASN B 201 ? 0.1351 0.4085 0.2760 0.0533 0.0001 -0.1175 227 ASN B CB 4124 C CG . ASN B 201 ? 0.2057 0.4827 0.3452 0.0579 -0.0006 -0.1206 227 ASN B CG 4125 O OD1 . ASN B 201 ? 0.2766 0.5486 0.4114 0.0608 -0.0022 -0.1205 227 ASN B OD1 4126 N ND2 . ASN B 201 ? 0.1848 0.4703 0.3304 0.0585 0.0007 -0.1238 227 ASN B ND2 4127 N N . LEU B 202 ? 0.1237 0.3859 0.2667 0.0424 0.0068 -0.1044 228 LEU B N 4128 C CA . LEU B 202 ? 0.1199 0.3775 0.2692 0.0382 0.0077 -0.1017 228 LEU B CA 4129 C C . LEU B 202 ? 0.1271 0.3750 0.2681 0.0379 0.0055 -0.0990 228 LEU B C 4130 O O . LEU B 202 ? 0.1378 0.3815 0.2830 0.0351 0.0052 -0.0984 228 LEU B O 4131 C CB . LEU B 202 ? 0.1195 0.3822 0.2823 0.0339 0.0145 -0.0950 228 LEU B CB 4132 C CG . LEU B 202 ? 0.1235 0.3958 0.2997 0.0332 0.0180 -0.0957 228 LEU B CG 4133 C CD1 . LEU B 202 ? 0.1235 0.4018 0.3145 0.0299 0.0258 -0.0851 228 LEU B CD1 4134 C CD2 . LEU B 202 ? 0.1245 0.3961 0.3087 0.0319 0.0151 -0.1027 228 LEU B CD2 4135 N N . VAL B 203 ? 0.1154 0.3604 0.2463 0.0408 0.0041 -0.0981 229 VAL B N 4136 C CA . VAL B 203 ? 0.1115 0.3476 0.2359 0.0405 0.0025 -0.0949 229 VAL B CA 4137 C C . VAL B 203 ? 0.1226 0.3540 0.2384 0.0457 -0.0018 -0.0973 229 VAL B C 4138 O O . VAL B 203 ? 0.1258 0.3611 0.2407 0.0490 -0.0023 -0.1005 229 VAL B O 4139 C CB . VAL B 203 ? 0.1097 0.3472 0.2345 0.0378 0.0067 -0.0891 229 VAL B CB 4140 C CG1 . VAL B 203 ? 0.1137 0.3573 0.2324 0.0409 0.0069 -0.0914 229 VAL B CG1 4141 C CG2 . VAL B 203 ? 0.1049 0.3332 0.2260 0.0362 0.0056 -0.0852 229 VAL B CG2 4142 N N . ASP B 204 ? 0.1105 0.3340 0.2223 0.0466 -0.0044 -0.0953 230 ASP B N 4143 C CA . ASP B 204 ? 0.1124 0.3311 0.2201 0.0519 -0.0076 -0.0950 230 ASP B CA 4144 C C . ASP B 204 ? 0.1571 0.3681 0.2614 0.0520 -0.0076 -0.0922 230 ASP B C 4145 O O . ASP B 204 ? 0.1127 0.3203 0.2175 0.0560 -0.0090 -0.0928 230 ASP B O 4146 C CB . ASP B 204 ? 0.1232 0.3411 0.2299 0.0543 -0.0103 -0.0936 230 ASP B CB 4147 C CG . ASP B 204 ? 0.1751 0.4022 0.2850 0.0549 -0.0110 -0.0978 230 ASP B CG 4148 O OD1 . ASP B 204 ? 0.2085 0.4404 0.3210 0.0573 -0.0108 -0.1003 230 ASP B OD1 4149 O OD2 . ASP B 204 ? 0.1682 0.3982 0.2790 0.0527 -0.0116 -0.0996 230 ASP B OD2 4150 N N . GLY B 205 ? 0.1055 0.3138 0.2087 0.0476 -0.0060 -0.0891 231 GLY B N 4151 C CA . GLY B 205 ? 0.1028 0.3035 0.2028 0.0476 -0.0066 -0.0861 231 GLY B CA 4152 C C . GLY B 205 ? 0.0995 0.3019 0.1995 0.0429 -0.0035 -0.0834 231 GLY B C 4153 O O . GLY B 205 ? 0.1047 0.3118 0.2092 0.0391 -0.0005 -0.0815 231 GLY B O 4154 N N . VAL B 206 ? 0.0989 0.2983 0.1958 0.0435 -0.0039 -0.0827 232 VAL B N 4155 C CA . VAL B 206 ? 0.0959 0.2974 0.1922 0.0396 -0.0012 -0.0785 232 VAL B CA 4156 C C . VAL B 206 ? 0.0918 0.2828 0.1861 0.0393 -0.0029 -0.0750 232 VAL B C 4157 O O . VAL B 206 ? 0.0932 0.2780 0.1858 0.0428 -0.0058 -0.0772 232 VAL B O 4158 C CB . VAL B 206 ? 0.1001 0.3124 0.1936 0.0405 0.0002 -0.0814 232 VAL B CB 4159 C CG1 . VAL B 206 ? 0.0976 0.3139 0.1900 0.0372 0.0028 -0.0753 232 VAL B CG1 4160 C CG2 . VAL B 206 ? 0.1076 0.3317 0.2034 0.0405 0.0026 -0.0834 232 VAL B CG2 4161 N N . GLY B 207 ? 0.0872 0.2759 0.1842 0.0350 -0.0008 -0.0692 233 GLY B N 4162 C CA . GLY B 207 ? 0.0831 0.2627 0.1787 0.0341 -0.0020 -0.0654 233 GLY B CA 4163 C C . GLY B 207 ? 0.0937 0.2774 0.1887 0.0318 0.0000 -0.0617 233 GLY B C 4164 O O . GLY B 207 ? 0.1185 0.3107 0.2176 0.0286 0.0039 -0.0573 233 GLY B O 4165 N N . PHE B 208 ? 0.0816 0.2605 0.1728 0.0338 -0.0025 -0.0629 234 PHE B N 4166 C CA . PHE B 208 ? 0.0808 0.2643 0.1704 0.0321 -0.0013 -0.0598 234 PHE B CA 4167 C C . PHE B 208 ? 0.0820 0.2549 0.1738 0.0295 -0.0018 -0.0536 234 PHE B C 4168 O O . PHE B 208 ? 0.0740 0.2361 0.1648 0.0318 -0.0049 -0.0549 234 PHE B O 4169 C CB . PHE B 208 ? 0.0855 0.2723 0.1714 0.0360 -0.0041 -0.0676 234 PHE B CB 4170 C CG . PHE B 208 ? 0.0920 0.2904 0.1762 0.0386 -0.0039 -0.0751 234 PHE B CG 4171 C CD1 . PHE B 208 ? 0.1384 0.3315 0.2250 0.0419 -0.0060 -0.0807 234 PHE B CD1 4172 C CD2 . PHE B 208 ? 0.0960 0.3120 0.1766 0.0379 -0.0015 -0.0753 234 PHE B CD2 4173 C CE1 . PHE B 208 ? 0.1241 0.3277 0.2104 0.0440 -0.0059 -0.0878 234 PHE B CE1 4174 C CE2 . PHE B 208 ? 0.1253 0.3534 0.2043 0.0404 -0.0015 -0.0826 234 PHE B CE2 4175 C CZ . PHE B 208 ? 0.1321 0.3530 0.2144 0.0432 -0.0038 -0.0894 234 PHE B CZ 4176 N N . GLN B 209 ? 0.0719 0.2478 0.1683 0.0248 0.0016 -0.0458 235 GLN B N 4177 C CA . GLN B 209 ? 0.0667 0.2321 0.1667 0.0220 0.0013 -0.0403 235 GLN B CA 4178 C C . GLN B 209 ? 0.0731 0.2338 0.1687 0.0235 -0.0016 -0.0405 235 GLN B C 4179 O O . GLN B 209 ? 0.0874 0.2366 0.1831 0.0241 -0.0039 -0.0397 235 GLN B O 4180 C CB . GLN B 209 ? 0.0644 0.2335 0.1744 0.0166 0.0060 -0.0313 235 GLN B CB 4181 C CG . GLN B 209 ? 0.0698 0.2397 0.1892 0.0147 0.0087 -0.0314 235 GLN B CG 4182 C CD . GLN B 209 ? 0.1185 0.2904 0.2536 0.0097 0.0138 -0.0215 235 GLN B CD 4183 O OE1 . GLN B 209 ? 0.1180 0.2871 0.2571 0.0072 0.0150 -0.0145 235 GLN B OE1 4184 N NE2 . GLN B 209 ? 0.1083 0.2849 0.2544 0.0083 0.0171 -0.0203 235 GLN B NE2 4185 N N . CYS B 210 ? 0.0689 0.2397 0.1606 0.0246 -0.0017 -0.0420 236 CYS B N 4186 C CA . CYS B 210 ? 0.0689 0.2365 0.1580 0.0261 -0.0049 -0.0439 236 CYS B CA 4187 C C . CYS B 210 ? 0.1411 0.3015 0.2335 0.0223 -0.0046 -0.0352 236 CYS B C 4188 O O . CYS B 210 ? 0.0682 0.2170 0.1611 0.0234 -0.0077 -0.0359 236 CYS B O 4189 C CB . CYS B 210 ? 0.0710 0.2271 0.1603 0.0309 -0.0089 -0.0515 236 CYS B CB 4190 S SG . CYS B 210 ? 0.1263 0.2903 0.2143 0.0357 -0.0101 -0.0631 236 CYS B SG 4191 N N . HIS B 211 ? 0.0616 0.2285 0.1582 0.0178 -0.0005 -0.0262 237 HIS B N 4192 C CA . HIS B 211 ? 0.0720 0.2345 0.1725 0.0140 0.0002 -0.0176 237 HIS B CA 4193 C C . HIS B 211 ? 0.1543 0.3292 0.2487 0.0149 -0.0008 -0.0163 237 HIS B C 4194 O O . HIS B 211 ? 0.1707 0.3598 0.2645 0.0133 0.0028 -0.0091 237 HIS B O 4195 C CB . HIS B 211 ? 0.0557 0.2179 0.1671 0.0089 0.0054 -0.0078 237 HIS B CB 4196 C CG . HIS B 211 ? 0.0528 0.2049 0.1716 0.0079 0.0060 -0.0104 237 HIS B CG 4197 N ND1 . HIS B 211 ? 0.0639 0.2033 0.1836 0.0075 0.0037 -0.0116 237 HIS B ND1 4198 C CD2 . HIS B 211 ? 0.0591 0.2140 0.1835 0.0075 0.0084 -0.0121 237 HIS B CD2 4199 C CE1 . HIS B 211 ? 0.0808 0.2171 0.2039 0.0072 0.0045 -0.0146 237 HIS B CE1 4200 N NE2 . HIS B 211 ? 0.0529 0.1979 0.1797 0.0072 0.0071 -0.0152 237 HIS B NE2 4201 N N . PHE B 212 ? 0.0620 0.2321 0.1526 0.0177 -0.0056 -0.0230 238 PHE B N 4202 C CA . PHE B 212 ? 0.0670 0.2504 0.1519 0.0192 -0.0076 -0.0258 238 PHE B CA 4203 C C . PHE B 212 ? 0.0643 0.2443 0.1506 0.0162 -0.0085 -0.0175 238 PHE B C 4204 O O . PHE B 212 ? 0.0582 0.2220 0.1503 0.0138 -0.0088 -0.0129 238 PHE B O 4205 C CB . PHE B 212 ? 0.1518 0.3318 0.2353 0.0242 -0.0125 -0.0409 238 PHE B CB 4206 C CG . PHE B 212 ? 0.0758 0.2612 0.1577 0.0277 -0.0120 -0.0501 238 PHE B CG 4207 C CD1 . PHE B 212 ? 0.1465 0.3529 0.2226 0.0283 -0.0091 -0.0507 238 PHE B CD1 4208 C CD2 . PHE B 212 ? 0.0759 0.2462 0.1624 0.0308 -0.0142 -0.0573 238 PHE B CD2 4209 C CE1 . PHE B 212 ? 0.1407 0.3520 0.2156 0.0314 -0.0088 -0.0596 238 PHE B CE1 4210 C CE2 . PHE B 212 ? 0.0805 0.2556 0.1665 0.0340 -0.0138 -0.0655 238 PHE B CE2 4211 C CZ . PHE B 212 ? 0.0849 0.2800 0.1651 0.0341 -0.0113 -0.0674 238 PHE B CZ 4212 N N . PHE B 213 ? 0.0697 0.2668 0.1503 0.0167 -0.0089 -0.0161 239 PHE B N 4213 C CA . PHE B 213 ? 0.0691 0.2641 0.1496 0.0150 -0.0113 -0.0115 239 PHE B CA 4214 C C . PHE B 213 ? 0.0777 0.2709 0.1566 0.0188 -0.0174 -0.0273 239 PHE B C 4215 O O . PHE B 213 ? 0.0804 0.2860 0.1553 0.0227 -0.0186 -0.0396 239 PHE B O 4216 C CB . PHE B 213 ? 0.0773 0.2928 0.1529 0.0136 -0.0079 0.0006 239 PHE B CB 4217 C CG . PHE B 213 ? 0.1087 0.3182 0.1864 0.0105 -0.0088 0.0103 239 PHE B CG 4218 C CD1 . PHE B 213 ? 0.1039 0.3155 0.1780 0.0123 -0.0143 0.0021 239 PHE B CD1 4219 C CD2 . PHE B 213 ? 0.1170 0.3158 0.2017 0.0057 -0.0041 0.0263 239 PHE B CD2 4220 C CE1 . PHE B 213 ? 0.1122 0.3172 0.1887 0.0094 -0.0153 0.0110 239 PHE B CE1 4221 C CE2 . PHE B 213 ? 0.1125 0.3036 0.1995 0.0029 -0.0047 0.0350 239 PHE B CE2 4222 C CZ . PHE B 213 ? 0.0910 0.2863 0.1733 0.0048 -0.0103 0.0283 239 PHE B CZ 4223 N N . VAL B 214 ? 0.0829 0.2600 0.1670 0.0178 -0.0209 -0.0276 240 VAL B N 4224 C CA . VAL B 214 ? 0.0748 0.2460 0.1623 0.0210 -0.0262 -0.0423 240 VAL B CA 4225 C C . VAL B 214 ? 0.0851 0.2796 0.1657 0.0235 -0.0278 -0.0523 240 VAL B C 4226 O O . VAL B 214 ? 0.0879 0.3005 0.1607 0.0221 -0.0261 -0.0442 240 VAL B O 4227 C CB . VAL B 214 ? 0.1193 0.2698 0.2124 0.0187 -0.0288 -0.0380 240 VAL B CB 4228 C CG1 . VAL B 214 ? 0.0964 0.2571 0.1847 0.0153 -0.0282 -0.0272 240 VAL B CG1 4229 C CG2 . VAL B 214 ? 0.1393 0.2826 0.2423 0.0222 -0.0338 -0.0531 240 VAL B CG2 4230 N N . GLY B 215 ? 0.0917 0.2871 0.1763 0.0276 -0.0304 -0.0700 241 GLY B N 4231 C CA . GLY B 215 ? 0.1029 0.3210 0.1828 0.0308 -0.0318 -0.0840 241 GLY B CA 4232 C C . GLY B 215 ? 0.1210 0.3663 0.1890 0.0326 -0.0278 -0.0829 241 GLY B C 4233 O O . GLY B 215 ? 0.1713 0.4413 0.2330 0.0360 -0.0279 -0.0933 241 GLY B O 4234 N N . GLU B 216 ? 0.1124 0.3549 0.1783 0.0309 -0.0239 -0.0707 242 GLU B N 4235 C CA . GLU B 216 ? 0.1061 0.3740 0.1622 0.0322 -0.0195 -0.0665 242 GLU B CA 4236 C C . GLU B 216 ? 0.1254 0.3880 0.1842 0.0338 -0.0178 -0.0715 242 GLU B C 4237 O O . GLU B 216 ? 0.1609 0.4343 0.2151 0.0330 -0.0133 -0.0618 242 GLU B O 4238 C CB . GLU B 216 ? 0.1880 0.4627 0.2401 0.0283 -0.0149 -0.0437 242 GLU B CB 4239 C CG . GLU B 216 ? 0.2004 0.4859 0.2482 0.0275 -0.0161 -0.0379 242 GLU B CG 4240 C CD . GLU B 216 ? 0.3582 0.6500 0.4048 0.0240 -0.0110 -0.0139 242 GLU B CD 4241 O OE1 . GLU B 216 ? 0.4836 0.7719 0.5338 0.0219 -0.0061 -0.0023 242 GLU B OE1 4242 O OE2 . GLU B 216 ? 0.5029 0.8018 0.5469 0.0232 -0.0117 -0.0067 242 GLU B OE2 4243 N N . LEU B 217 ? 0.1197 0.3657 0.1873 0.0361 -0.0212 -0.0861 243 LEU B N 4244 C CA . LEU B 217 ? 0.1052 0.3477 0.1755 0.0382 -0.0200 -0.0923 243 LEU B CA 4245 C C . LEU B 217 ? 0.1271 0.3976 0.1898 0.0419 -0.0193 -0.1042 243 LEU B C 4246 O O . LEU B 217 ? 0.1730 0.4609 0.2326 0.0444 -0.0211 -0.1151 243 LEU B O 4247 C CB . LEU B 217 ? 0.1380 0.3563 0.2216 0.0402 -0.0236 -0.1029 243 LEU B CB 4248 C CG . LEU B 217 ? 0.1390 0.3317 0.2283 0.0378 -0.0228 -0.0901 243 LEU B CG 4249 C CD1 . LEU B 217 ? 0.0938 0.2797 0.1821 0.0339 -0.0231 -0.0778 243 LEU B CD1 4250 C CD2 . LEU B 217 ? 0.1259 0.2981 0.2288 0.0407 -0.0256 -0.0982 243 LEU B CD2 4251 N N . PRO B 218 ? 0.1496 0.4259 0.2092 0.0425 -0.0166 -0.1023 244 PRO B N 4252 C CA . PRO B 218 ? 0.1274 0.4314 0.1797 0.0461 -0.0168 -0.1142 244 PRO B CA 4253 C C . PRO B 218 ? 0.1528 0.4538 0.2141 0.0497 -0.0221 -0.1382 244 PRO B C 4254 O O . PRO B 218 ? 0.2330 0.5084 0.3073 0.0496 -0.0244 -0.1425 244 PRO B O 4255 C CB . PRO B 218 ? 0.2100 0.5147 0.2604 0.0453 -0.0135 -0.1063 244 PRO B CB 4256 C CG . PRO B 218 ? 0.2245 0.4985 0.2839 0.0425 -0.0125 -0.0978 244 PRO B CG 4257 C CD . PRO B 218 ? 0.1913 0.4518 0.2538 0.0400 -0.0135 -0.0905 244 PRO B CD 4258 N N . PRO B 219 ? 0.1462 0.4714 0.2047 0.0526 -0.0238 -0.1506 245 PRO B N 4259 C CA . PRO B 219 ? 0.2817 0.6013 0.3570 0.0547 -0.0285 -0.1698 245 PRO B CA 4260 C C . PRO B 219 ? 0.2498 0.5656 0.3343 0.0551 -0.0310 -0.1772 245 PRO B C 4261 O O . PRO B 219 ? 0.3200 0.6259 0.4230 0.0558 -0.0352 -0.1910 245 PRO B O 4262 C CB . PRO B 219 ? 0.2839 0.6331 0.3550 0.0573 -0.0282 -0.1763 245 PRO B CB 4263 C CG . PRO B 219 ? 0.3763 0.7498 0.4295 0.0568 -0.0243 -0.1604 245 PRO B CG 4264 C CD . PRO B 219 ? 0.3247 0.6820 0.3703 0.0534 -0.0209 -0.1427 245 PRO B CD 4265 N N . ASP B 220 ? 0.1664 0.4907 0.2402 0.0546 -0.0281 -0.1677 246 ASP B N 4266 C CA . ASP B 220 ? 0.1548 0.4770 0.2361 0.0554 -0.0297 -0.1742 246 ASP B CA 4267 C C . ASP B 220 ? 0.1580 0.4555 0.2392 0.0537 -0.0272 -0.1636 246 ASP B C 4268 O O . ASP B 220 ? 0.1891 0.4879 0.2692 0.0540 -0.0252 -0.1606 246 ASP B O 4269 C CB . ASP B 220 ? 0.2246 0.5774 0.2972 0.0569 -0.0282 -0.1730 246 ASP B CB 4270 C CG . ASP B 220 ? 0.4115 0.7820 0.4658 0.0559 -0.0237 -0.1553 246 ASP B CG 4271 O OD1 . ASP B 220 ? 0.2966 0.6536 0.3443 0.0534 -0.0210 -0.1427 246 ASP B OD1 4272 O OD2 . ASP B 220 ? 0.5448 0.9447 0.5931 0.0577 -0.0229 -0.1534 246 ASP B OD2 4273 N N . LEU B 221 ? 0.1370 0.4099 0.2218 0.0523 -0.0257 -0.1550 247 LEU B N 4274 C CA . LEU B 221 ? 0.1283 0.3760 0.2167 0.0510 -0.0227 -0.1420 247 LEU B CA 4275 C C . LEU B 221 ? 0.1839 0.4204 0.2836 0.0528 -0.0242 -0.1485 247 LEU B C 4276 O O . LEU B 221 ? 0.1356 0.3700 0.2319 0.0526 -0.0214 -0.1412 247 LEU B O 4277 C CB . LEU B 221 ? 0.1539 0.3795 0.2483 0.0497 -0.0233 -0.1350 247 LEU B CB 4278 C CG . LEU B 221 ? 0.1547 0.3575 0.2521 0.0485 -0.0211 -0.1208 247 LEU B CG 4279 C CD1 . LEU B 221 ? 0.1528 0.3629 0.2390 0.0457 -0.0165 -0.1072 247 LEU B CD1 4280 C CD2 . LEU B 221 ? 0.1546 0.3384 0.2588 0.0476 -0.0226 -0.1150 247 LEU B CD2 4281 N N . GLU B 222 ? 0.1492 0.3787 0.2646 0.0542 -0.0285 -0.1615 248 GLU B N 4282 C CA . GLU B 222 ? 0.1621 0.3797 0.2913 0.0559 -0.0293 -0.1653 248 GLU B CA 4283 C C . GLU B 222 ? 0.1466 0.3835 0.2721 0.0570 -0.0291 -0.1727 248 GLU B C 4284 O O . GLU B 222 ? 0.1840 0.4138 0.3114 0.0580 -0.0271 -0.1680 248 GLU B O 4285 C CB . GLU B 222 ? 0.2876 0.4945 0.4387 0.0566 -0.0332 -0.1767 248 GLU B CB 4286 C CG . GLU B 222 ? 0.2340 0.4246 0.4020 0.0584 -0.0326 -0.1756 248 GLU B CG 4287 C CD . GLU B 222 ? 0.5088 0.7145 0.6834 0.0597 -0.0340 -0.1893 248 GLU B CD 4288 O OE1 . GLU B 222 ? 0.6724 0.8982 0.8507 0.0591 -0.0379 -0.2056 248 GLU B OE1 4289 O OE2 . GLU B 222 ? 0.4907 0.6904 0.6673 0.0615 -0.0316 -0.1840 248 GLU B OE2 4290 N N . GLN B 223 ? 0.1525 0.4158 0.2730 0.0571 -0.0315 -0.1836 249 GLN B N 4291 C CA . GLN B 223 ? 0.2289 0.5146 0.3454 0.0582 -0.0316 -0.1897 249 GLN B CA 4292 C C . GLN B 223 ? 0.1526 0.4394 0.2536 0.0574 -0.0260 -0.1737 249 GLN B C 4293 O O . GLN B 223 ? 0.1546 0.4432 0.2566 0.0583 -0.0246 -0.1738 249 GLN B O 4294 C CB . GLN B 223 ? 0.2556 0.5747 0.3688 0.0588 -0.0355 -0.2016 249 GLN B CB 4295 C CG . GLN B 223 ? 0.4282 0.7734 0.5393 0.0607 -0.0356 -0.2079 249 GLN B CG 4296 C CD . GLN B 223 ? 0.5629 0.9371 0.6735 0.0627 -0.0364 -0.2158 249 GLN B CD 4297 O OE1 . GLN B 223 ? 0.5637 0.9419 0.6702 0.0625 -0.0361 -0.2130 249 GLN B OE1 4298 N NE2 . GLN B 223 ? 0.6414 1.0374 0.7566 0.0649 -0.0376 -0.2260 249 GLN B NE2 4299 N N . ASN B 224 ? 0.1582 0.4435 0.2470 0.0554 -0.0226 -0.1599 250 ASN B N 4300 C CA . ASN B 224 ? 0.1404 0.4257 0.2196 0.0538 -0.0171 -0.1446 250 ASN B CA 4301 C C . ASN B 224 ? 0.1904 0.4514 0.2765 0.0536 -0.0158 -0.1384 250 ASN B C 4302 O O . ASN B 224 ? 0.2068 0.4703 0.2915 0.0535 -0.0134 -0.1346 250 ASN B O 4303 C CB . ASN B 224 ? 0.1346 0.4233 0.2040 0.0511 -0.0136 -0.1304 250 ASN B CB 4304 C CG . ASN B 224 ? 0.1303 0.4207 0.1946 0.0487 -0.0078 -0.1149 250 ASN B CG 4305 O OD1 . ASN B 224 ? 0.1468 0.4532 0.2082 0.0494 -0.0060 -0.1145 250 ASN B OD1 4306 N ND2 . ASN B 224 ? 0.1213 0.3953 0.1872 0.0457 -0.0052 -0.1023 250 ASN B ND2 4307 N N . PHE B 225 ? 0.2214 0.4608 0.3154 0.0538 -0.0174 -0.1370 251 PHE B N 4308 C CA . PHE B 225 ? 0.2232 0.4431 0.3238 0.0545 -0.0167 -0.1307 251 PHE B CA 4309 C C . PHE B 225 ? 0.1334 0.3561 0.2417 0.0572 -0.0177 -0.1391 251 PHE B C 4310 O O . PHE B 225 ? 0.1316 0.3510 0.2394 0.0576 -0.0158 -0.1336 251 PHE B O 4311 C CB . PHE B 225 ? 0.2034 0.4028 0.3132 0.0553 -0.0185 -0.1279 251 PHE B CB 4312 C CG . PHE B 225 ? 0.1387 0.3304 0.2421 0.0526 -0.0170 -0.1161 251 PHE B CG 4313 C CD1 . PHE B 225 ? 0.1111 0.3140 0.2034 0.0495 -0.0141 -0.1093 251 PHE B CD1 4314 C CD2 . PHE B 225 ? 0.1560 0.3297 0.2666 0.0533 -0.0183 -0.1107 251 PHE B CD2 4315 C CE1 . PHE B 225 ? 0.2062 0.4015 0.2954 0.0466 -0.0127 -0.0985 251 PHE B CE1 4316 C CE2 . PHE B 225 ? 0.1846 0.3517 0.2901 0.0507 -0.0172 -0.1004 251 PHE B CE2 4317 C CZ . PHE B 225 ? 0.1359 0.3136 0.2310 0.0472 -0.0146 -0.0950 251 PHE B CZ 4318 N N . ALA B 226 ? 0.1441 0.3740 0.2609 0.0588 -0.0209 -0.1533 252 ALA B N 4319 C CA . ALA B 226 ? 0.2052 0.4374 0.3329 0.0613 -0.0221 -0.1626 252 ALA B CA 4320 C C . ALA B 226 ? 0.2252 0.4744 0.3442 0.0613 -0.0201 -0.1631 252 ALA B C 4321 O O . ALA B 226 ? 0.2430 0.4886 0.3679 0.0630 -0.0193 -0.1635 252 ALA B O 4322 C CB . ALA B 226 ? 0.1664 0.4053 0.3075 0.0623 -0.0262 -0.1796 252 ALA B CB 4323 N N . ARG B 227 ? 0.1933 0.4622 0.2995 0.0596 -0.0189 -0.1620 253 ARG B N 4324 C CA . ARG B 227 ? 0.1964 0.4820 0.2961 0.0598 -0.0165 -0.1610 253 ARG B CA 4325 C C . ARG B 227 ? 0.2534 0.5287 0.3486 0.0582 -0.0123 -0.1467 253 ARG B C 4326 O O . ARG B 227 ? 0.1489 0.4308 0.2438 0.0587 -0.0104 -0.1461 253 ARG B O 4327 C CB . ARG B 227 ? 0.2395 0.5520 0.3283 0.0592 -0.0160 -0.1618 253 ARG B CB 4328 C CG . ARG B 227 ? 0.1973 0.5110 0.2749 0.0565 -0.0121 -0.1467 253 ARG B CG 4329 C CD . ARG B 227 ? 0.2314 0.5748 0.2996 0.0570 -0.0118 -0.1469 253 ARG B CD 4330 N NE . ARG B 227 ? 0.2555 0.5994 0.3155 0.0543 -0.0074 -0.1306 253 ARG B NE 4331 C CZ . ARG B 227 ? 0.1567 0.5229 0.2084 0.0541 -0.0038 -0.1204 253 ARG B CZ 4332 N NH1 . ARG B 227 ? 0.2004 0.5921 0.2490 0.0567 -0.0043 -0.1252 253 ARG B NH1 4333 N NH2 . ARG B 227 ? 0.1516 0.5151 0.1998 0.0513 0.0004 -0.1043 253 ARG B NH2 4334 N N . PHE B 228 ? 0.2000 0.4599 0.2933 0.0563 -0.0111 -0.1362 254 PHE B N 4335 C CA . PHE B 228 ? 0.1320 0.3825 0.2243 0.0547 -0.0082 -0.1251 254 PHE B CA 4336 C C . PHE B 228 ? 0.1329 0.3703 0.2339 0.0574 -0.0099 -0.1273 254 PHE B C 4337 O O . PHE B 228 ? 0.1327 0.3713 0.2345 0.0576 -0.0084 -0.1247 254 PHE B O 4338 C CB . PHE B 228 ? 0.1237 0.3637 0.2126 0.0517 -0.0068 -0.1143 254 PHE B CB 4339 C CG . PHE B 228 ? 0.1724 0.4251 0.2548 0.0484 -0.0028 -0.1063 254 PHE B CG 4340 C CD1 . PHE B 228 ? 0.1934 0.4586 0.2705 0.0482 -0.0029 -0.1075 254 PHE B CD1 4341 C CD2 . PHE B 228 ? 0.1468 0.4001 0.2305 0.0457 0.0011 -0.0972 254 PHE B CD2 4342 C CE1 . PHE B 228 ? 0.1241 0.4023 0.1966 0.0456 0.0015 -0.0972 254 PHE B CE1 4343 C CE2 . PHE B 228 ? 0.1177 0.3822 0.1998 0.0426 0.0057 -0.0877 254 PHE B CE2 4344 C CZ . PHE B 228 ? 0.2036 0.4805 0.2798 0.0427 0.0061 -0.0865 254 PHE B CZ 4345 N N . VAL B 229 ? 0.1588 0.3844 0.2680 0.0597 -0.0127 -0.1311 255 VAL B N 4346 C CA . VAL B 229 ? 0.1706 0.3856 0.2907 0.0632 -0.0137 -0.1316 255 VAL B CA 4347 C C . VAL B 229 ? 0.2457 0.4718 0.3703 0.0651 -0.0138 -0.1409 255 VAL B C 4348 O O . VAL B 229 ? 0.1820 0.4056 0.3109 0.0671 -0.0130 -0.1384 255 VAL B O 4349 C CB . VAL B 229 ? 0.1937 0.3954 0.3254 0.0655 -0.0158 -0.1336 255 VAL B CB 4350 C CG1 . VAL B 229 ? 0.1990 0.3928 0.3453 0.0698 -0.0158 -0.1335 255 VAL B CG1 4351 C CG2 . VAL B 229 ? 0.1319 0.3219 0.2595 0.0640 -0.0155 -0.1228 255 VAL B CG2 4352 N N . ALA B 230 ? 0.1744 0.4150 0.2979 0.0646 -0.0148 -0.1516 256 ALA B N 4353 C CA . ALA B 230 ? 0.1723 0.4262 0.3002 0.0664 -0.0152 -0.1619 256 ALA B CA 4354 C C . ALA B 230 ? 0.2429 0.5056 0.3629 0.0654 -0.0121 -0.1559 256 ALA B C 4355 O O . ALA B 230 ? 0.2263 0.4950 0.3513 0.0673 -0.0119 -0.1611 256 ALA B O 4356 C CB . ALA B 230 ? 0.1652 0.4377 0.2919 0.0659 -0.0174 -0.1744 256 ALA B CB 4357 N N . ALA B 231 ? 0.2108 0.4740 0.3206 0.0623 -0.0096 -0.1451 257 ALA B N 4358 C CA . ALA B 231 ? 0.2015 0.4721 0.3070 0.0609 -0.0062 -0.1390 257 ALA B CA 4359 C C . ALA B 231 ? 0.2300 0.4872 0.3401 0.0615 -0.0061 -0.1330 257 ALA B C 4360 O O . ALA B 231 ? 0.2675 0.5284 0.3762 0.0600 -0.0037 -0.1281 257 ALA B O 4361 C CB . ALA B 231 ? 0.1435 0.4215 0.2404 0.0571 -0.0028 -0.1299 257 ALA B CB 4362 N N . GLY B 232 ? 0.1702 0.4131 0.2867 0.0640 -0.0085 -0.1328 258 GLY B N 4363 C CA . GLY B 232 ? 0.1409 0.3749 0.2617 0.0659 -0.0087 -0.1271 258 GLY B CA 4364 C C . GLY B 232 ? 0.2009 0.4267 0.3171 0.0638 -0.0085 -0.1172 258 GLY B C 4365 O O . GLY B 232 ? 0.1836 0.4074 0.3013 0.0648 -0.0087 -0.1129 258 GLY B O 4366 N N . VAL B 233 ? 0.2298 0.4522 0.3408 0.0610 -0.0083 -0.1141 259 VAL B N 4367 C CA . VAL B 233 ? 0.1959 0.4102 0.3040 0.0591 -0.0084 -0.1057 259 VAL B CA 4368 C C . VAL B 233 ? 0.1758 0.3782 0.2866 0.0614 -0.0103 -0.1028 259 VAL B C 4369 O O . VAL B 233 ? 0.1567 0.3568 0.2716 0.0630 -0.0112 -0.1074 259 VAL B O 4370 C CB . VAL B 233 ? 0.1599 0.3781 0.2621 0.0539 -0.0060 -0.1019 259 VAL B CB 4371 C CG1 . VAL B 233 ? 0.2610 0.4901 0.3640 0.0516 -0.0031 -0.1020 259 VAL B CG1 4372 C CG2 . VAL B 233 ? 0.1592 0.3802 0.2582 0.0528 -0.0057 -0.1040 259 VAL B CG2 4373 N N . GLU B 234 ? 0.1422 0.3382 0.2520 0.0615 -0.0108 -0.0954 260 GLU B N 4374 C CA . GLU B 234 ? 0.1338 0.3193 0.2455 0.0630 -0.0119 -0.0902 260 GLU B CA 4375 C C . GLU B 234 ? 0.1100 0.2941 0.2149 0.0582 -0.0112 -0.0889 260 GLU B C 4376 O O . GLU B 234 ? 0.1074 0.2982 0.2076 0.0541 -0.0095 -0.0894 260 GLU B O 4377 C CB . GLU B 234 ? 0.1435 0.3259 0.2570 0.0660 -0.0126 -0.0822 260 GLU B CB 4378 C CG . GLU B 234 ? 0.1388 0.3248 0.2448 0.0624 -0.0125 -0.0797 260 GLU B CG 4379 C CD . GLU B 234 ? 0.2223 0.4088 0.3292 0.0661 -0.0137 -0.0731 260 GLU B CD 4380 O OE1 . GLU B 234 ? 0.1597 0.3510 0.2716 0.0708 -0.0141 -0.0718 260 GLU B OE1 4381 O OE2 . GLU B 234 ? 0.1226 0.3063 0.2256 0.0647 -0.0141 -0.0688 260 GLU B OE2 4382 N N . ILE B 235 ? 0.1087 0.2843 0.2152 0.0587 -0.0121 -0.0864 261 ILE B N 4383 C CA . ILE B 235 ? 0.1035 0.2777 0.2044 0.0545 -0.0114 -0.0843 261 ILE B CA 4384 C C . ILE B 235 ? 0.0999 0.2637 0.2015 0.0550 -0.0123 -0.0767 261 ILE B C 4385 O O . ILE B 235 ? 0.1200 0.2780 0.2274 0.0593 -0.0132 -0.0728 261 ILE B O 4386 C CB . ILE B 235 ? 0.1230 0.3008 0.2238 0.0537 -0.0116 -0.0907 261 ILE B CB 4387 C CG1 . ILE B 235 ? 0.1624 0.3308 0.2714 0.0571 -0.0137 -0.0927 261 ILE B CG1 4388 C CG2 . ILE B 235 ? 0.1419 0.3326 0.2421 0.0539 -0.0108 -0.0985 261 ILE B CG2 4389 C CD1 . ILE B 235 ? 0.1916 0.3642 0.3007 0.0560 -0.0146 -0.1004 261 ILE B CD1 4390 N N . ALA B 236 ? 0.0945 0.2569 0.1913 0.0509 -0.0114 -0.0734 262 ALA B N 4391 C CA . ALA B 236 ? 0.0909 0.2445 0.1876 0.0507 -0.0122 -0.0667 262 ALA B CA 4392 C C . ALA B 236 ? 0.0864 0.2390 0.1803 0.0463 -0.0112 -0.0657 262 ALA B C 4393 O O . ALA B 236 ? 0.0850 0.2453 0.1765 0.0426 -0.0092 -0.0672 262 ALA B O 4394 C CB . ALA B 236 ? 0.0891 0.2438 0.1836 0.0504 -0.0121 -0.0624 262 ALA B CB 4395 N N . VAL B 237 ? 0.0848 0.2285 0.1802 0.0470 -0.0124 -0.0619 263 VAL B N 4396 C CA . VAL B 237 ? 0.1242 0.2663 0.2175 0.0429 -0.0117 -0.0591 263 VAL B CA 4397 C C . VAL B 237 ? 0.0831 0.2225 0.1749 0.0404 -0.0108 -0.0533 263 VAL B C 4398 O O . VAL B 237 ? 0.1061 0.2401 0.1984 0.0430 -0.0120 -0.0493 263 VAL B O 4399 C CB . VAL B 237 ? 0.1154 0.2493 0.2122 0.0447 -0.0135 -0.0587 263 VAL B CB 4400 C CG1 . VAL B 237 ? 0.1175 0.2488 0.2123 0.0406 -0.0131 -0.0542 263 VAL B CG1 4401 C CG2 . VAL B 237 ? 0.1186 0.2573 0.2185 0.0467 -0.0146 -0.0679 263 VAL B CG2 4402 N N . THR B 238 ? 0.0723 0.2166 0.1639 0.0355 -0.0085 -0.0524 264 THR B N 4403 C CA . THR B 238 ? 0.0700 0.2137 0.1628 0.0331 -0.0077 -0.0504 264 THR B CA 4404 C C . THR B 238 ? 0.0769 0.2152 0.1718 0.0293 -0.0069 -0.0456 264 THR B C 4405 O O . THR B 238 ? 0.0665 0.2032 0.1621 0.0287 -0.0072 -0.0452 264 THR B O 4406 C CB . THR B 238 ? 0.0772 0.2293 0.1735 0.0301 -0.0052 -0.0531 264 THR B CB 4407 O OG1 . THR B 238 ? 0.0696 0.2265 0.1689 0.0267 -0.0023 -0.0507 264 THR B OG1 4408 C CG2 . THR B 238 ? 0.0756 0.2331 0.1700 0.0339 -0.0063 -0.0582 264 THR B CG2 4409 N N . GLU B 239 ? 0.0627 0.1999 0.1590 0.0268 -0.0059 -0.0424 265 GLU B N 4410 C CA . GLU B 239 ? 0.0583 0.1906 0.1582 0.0227 -0.0048 -0.0371 265 GLU B CA 4411 C C . GLU B 239 ? 0.0698 0.1979 0.1684 0.0229 -0.0061 -0.0337 265 GLU B C 4412 O O . GLU B 239 ? 0.0822 0.2116 0.1845 0.0188 -0.0043 -0.0289 265 GLU B O 4413 C CB . GLU B 239 ? 0.0568 0.1945 0.1652 0.0172 -0.0008 -0.0341 265 GLU B CB 4414 C CG . GLU B 239 ? 0.0594 0.2019 0.1719 0.0167 0.0005 -0.0383 265 GLU B CG 4415 C CD . GLU B 239 ? 0.1740 0.3206 0.2992 0.0115 0.0050 -0.0339 265 GLU B CD 4416 O OE1 . GLU B 239 ? 0.1360 0.2813 0.2674 0.0081 0.0073 -0.0262 265 GLU B OE1 4417 O OE2 . GLU B 239 ? 0.1925 0.3442 0.3231 0.0111 0.0064 -0.0372 265 GLU B OE2 4418 N N . LEU B 240 ? 0.0589 0.1823 0.1540 0.0276 -0.0091 -0.0358 266 LEU B N 4419 C CA . LEU B 240 ? 0.0589 0.1791 0.1542 0.0283 -0.0108 -0.0353 266 LEU B CA 4420 C C . LEU B 240 ? 0.0543 0.1677 0.1518 0.0252 -0.0109 -0.0289 266 LEU B C 4421 O O . LEU B 240 ? 0.0553 0.1614 0.1530 0.0258 -0.0113 -0.0257 266 LEU B O 4422 C CB . LEU B 240 ? 0.0635 0.1774 0.1595 0.0340 -0.0136 -0.0384 266 LEU B CB 4423 C CG . LEU B 240 ? 0.0773 0.1865 0.1765 0.0353 -0.0159 -0.0404 266 LEU B CG 4424 C CD1 . LEU B 240 ? 0.0673 0.1888 0.1651 0.0339 -0.0159 -0.0468 266 LEU B CD1 4425 C CD2 . LEU B 240 ? 0.0711 0.1725 0.1756 0.0406 -0.0175 -0.0422 266 LEU B CD2 4426 N N . ASP B 241 ? 0.0527 0.1706 0.1514 0.0221 -0.0104 -0.0268 267 ASP B N 4427 C CA . ASP B 241 ? 0.0496 0.1604 0.1505 0.0201 -0.0116 -0.0218 267 ASP B CA 4428 C C . ASP B 241 ? 0.0511 0.1707 0.1512 0.0191 -0.0125 -0.0224 267 ASP B C 4429 O O . ASP B 241 ? 0.0678 0.2012 0.1655 0.0185 -0.0106 -0.0239 267 ASP B O 4430 C CB . ASP B 241 ? 0.0447 0.1525 0.1501 0.0151 -0.0089 -0.0152 267 ASP B CB 4431 C CG . ASP B 241 ? 0.0628 0.1800 0.1728 0.0109 -0.0046 -0.0125 267 ASP B CG 4432 O OD1 . ASP B 241 ? 0.0924 0.2207 0.2019 0.0105 -0.0032 -0.0121 267 ASP B OD1 4433 O OD2 . ASP B 241 ? 0.1533 0.2673 0.2680 0.0081 -0.0024 -0.0105 267 ASP B OD2 4434 N N . ILE B 242 ? 0.0515 0.1631 0.1521 0.0191 -0.0152 -0.0213 268 ILE B N 4435 C CA . ILE B 242 ? 0.0556 0.1753 0.1532 0.0188 -0.0168 -0.0238 268 ILE B CA 4436 C C . ILE B 242 ? 0.0539 0.1672 0.1513 0.0145 -0.0168 -0.0150 268 ILE B C 4437 O O . ILE B 242 ? 0.0540 0.1529 0.1536 0.0150 -0.0193 -0.0146 268 ILE B O 4438 C CB . ILE B 242 ? 0.0606 0.1773 0.1613 0.0241 -0.0209 -0.0349 268 ILE B CB 4439 C CG1 . ILE B 242 ? 0.0635 0.1833 0.1644 0.0280 -0.0201 -0.0418 268 ILE B CG1 4440 C CG2 . ILE B 242 ? 0.0655 0.1961 0.1642 0.0241 -0.0231 -0.0412 268 ILE B CG2 4441 C CD1 . ILE B 242 ? 0.1026 0.2176 0.2095 0.0327 -0.0229 -0.0523 268 ILE B CD1 4442 N N . ARG B 243 ? 0.0569 0.1815 0.1537 0.0105 -0.0134 -0.0067 269 ARG B N 4443 C CA . ARG B 243 ? 0.0499 0.1681 0.1494 0.0059 -0.0121 0.0040 269 ARG B CA 4444 C C . ARG B 243 ? 0.1023 0.2289 0.1979 0.0057 -0.0144 0.0054 269 ARG B C 4445 O O . ARG B 243 ? 0.0589 0.2009 0.1498 0.0089 -0.0166 -0.0024 269 ARG B O 4446 C CB . ARG B 243 ? 0.0463 0.1714 0.1530 0.0017 -0.0064 0.0138 269 ARG B CB 4447 C CG . ARG B 243 ? 0.0508 0.1963 0.1553 0.0017 -0.0032 0.0174 269 ARG B CG 4448 C CD . ARG B 243 ? 0.0822 0.2241 0.1936 -0.0020 0.0030 0.0247 269 ARG B CD 4449 N NE . ARG B 243 ? 0.0736 0.2322 0.1832 -0.0021 0.0068 0.0327 269 ARG B NE 4450 C CZ . ARG B 243 ? 0.1558 0.3290 0.2629 0.0005 0.0082 0.0295 269 ARG B CZ 4451 N NH1 . ARG B 243 ? 0.1325 0.3043 0.2384 0.0032 0.0060 0.0178 269 ARG B NH1 4452 N NH2 . ARG B 243 ? 0.2044 0.3938 0.3095 0.0009 0.0117 0.0389 269 ARG B NH2 4453 N N . MET B 244 ? 0.0622 0.1806 0.1607 0.0021 -0.0141 0.0144 270 MET B N 4454 C CA . MET B 244 ? 0.0641 0.1901 0.1596 0.0019 -0.0168 0.0161 270 MET B CA 4455 C C . MET B 244 ? 0.1019 0.2233 0.2028 -0.0029 -0.0140 0.0307 270 MET B C 4456 O O . MET B 244 ? 0.0794 0.1844 0.1849 -0.0057 -0.0107 0.0352 270 MET B O 4457 C CB . MET B 244 ? 0.0576 0.1707 0.1531 0.0047 -0.0224 0.0052 270 MET B CB 4458 C CG . MET B 244 ? 0.0808 0.1680 0.1816 0.0032 -0.0226 0.0088 270 MET B CG 4459 S SD . MET B 244 ? 0.1229 0.1951 0.2293 0.0075 -0.0278 -0.0024 270 MET B SD 4460 C CE . MET B 244 ? 0.0774 0.1530 0.1847 0.0126 -0.0277 -0.0127 270 MET B CE 4461 N N . ASN B 245 ? 0.0604 0.1945 0.1588 -0.0034 -0.0149 0.0362 271 ASN B N 4462 C CA . ASN B 245 ? 0.1026 0.2257 0.2029 -0.0073 -0.0121 0.0486 271 ASN B CA 4463 C C . ASN B 245 ? 0.1397 0.2382 0.2432 -0.0088 -0.0146 0.0463 271 ASN B C 4464 O O . ASN B 245 ? 0.1025 0.1968 0.2071 -0.0064 -0.0199 0.0367 271 ASN B O 4465 C CB . ASN B 245 ? 0.1106 0.2539 0.2060 -0.0064 -0.0132 0.0545 271 ASN B CB 4466 C CG . ASN B 245 ? 0.2480 0.4129 0.3400 -0.0055 -0.0083 0.0638 271 ASN B CG 4467 O OD1 . ASN B 245 ? 0.2203 0.3804 0.3158 -0.0065 -0.0037 0.0680 271 ASN B OD1 4468 N ND2 . ASN B 245 ? 0.2652 0.4545 0.3500 -0.0030 -0.0094 0.0670 271 ASN B ND2 4469 N N . LEU B 246 ? 0.0830 0.1642 0.1880 -0.0119 -0.0107 0.0547 272 LEU B N 4470 C CA . LEU B 246 ? 0.1514 0.2097 0.2568 -0.0125 -0.0121 0.0538 272 LEU B CA 4471 C C . LEU B 246 ? 0.1093 0.1659 0.2140 -0.0135 -0.0131 0.0616 272 LEU B C 4472 O O . LEU B 246 ? 0.1665 0.2347 0.2710 -0.0140 -0.0112 0.0707 272 LEU B O 4473 C CB . LEU B 246 ? 0.1811 0.2232 0.2864 -0.0116 -0.0089 0.0532 272 LEU B CB 4474 C CG . LEU B 246 ? 0.1266 0.1705 0.2331 -0.0111 -0.0073 0.0462 272 LEU B CG 4475 C CD1 . LEU B 246 ? 0.1887 0.2216 0.2960 -0.0101 -0.0046 0.0444 272 LEU B CD1 4476 C CD2 . LEU B 246 ? 0.0492 0.0911 0.1561 -0.0090 -0.0111 0.0382 272 LEU B CD2 4477 N N . PRO B 247 ? 0.1060 0.1491 0.2110 -0.0131 -0.0163 0.0589 273 PRO B N 4478 C CA . PRO B 247 ? 0.1740 0.2049 0.2806 -0.0116 -0.0190 0.0500 273 PRO B CA 4479 C C . PRO B 247 ? 0.1556 0.2013 0.2646 -0.0093 -0.0238 0.0397 273 PRO B C 4480 O O . PRO B 247 ? 0.1167 0.1822 0.2248 -0.0088 -0.0263 0.0386 273 PRO B O 4481 C CB . PRO B 247 ? 0.2020 0.2211 0.3085 -0.0096 -0.0212 0.0508 273 PRO B CB 4482 C CG . PRO B 247 ? 0.1855 0.2134 0.2920 -0.0120 -0.0217 0.0591 273 PRO B CG 4483 C CD . PRO B 247 ? 0.1636 0.2038 0.2685 -0.0128 -0.0178 0.0654 273 PRO B CD 4484 N N . PRO B 248 ? 0.1266 0.2716 0.2048 0.0337 -0.0310 0.0026 274 PRO B N 4485 C CA . PRO B 248 ? 0.0842 0.2237 0.1571 0.0226 -0.0322 0.0019 274 PRO B CA 4486 C C . PRO B 248 ? 0.1144 0.2769 0.2005 0.0183 -0.0396 -0.0045 274 PRO B C 4487 O O . PRO B 248 ? 0.0994 0.2786 0.2032 0.0144 -0.0382 -0.0072 274 PRO B O 4488 C CB . PRO B 248 ? 0.1140 0.2453 0.1895 0.0119 -0.0241 0.0022 274 PRO B CB 4489 C CG . PRO B 248 ? 0.1499 0.2784 0.2252 0.0188 -0.0187 0.0033 274 PRO B CG 4490 C CD . PRO B 248 ? 0.1227 0.2680 0.2062 0.0306 -0.0227 0.0012 274 PRO B CD 4491 N N . SER B 249 ? 0.0884 0.2488 0.1647 0.0188 -0.0466 -0.0074 275 SER B N 4492 C CA . SER B 249 ? 0.0943 0.2674 0.1814 0.0131 -0.0539 -0.0163 275 SER B CA 4493 C C . SER B 249 ? 0.0979 0.2653 0.1976 -0.0024 -0.0516 -0.0205 275 SER B C 4494 O O . SER B 249 ? 0.0810 0.2341 0.1740 -0.0067 -0.0465 -0.0179 275 SER B O 4495 C CB . SER B 249 ? 0.1448 0.3172 0.2137 0.0209 -0.0621 -0.0196 275 SER B CB 4496 O OG . SER B 249 ? 0.1271 0.2871 0.1811 0.0188 -0.0602 -0.0198 275 SER B OG 4497 N N . GLN B 250 ? 0.0944 0.2703 0.2124 -0.0106 -0.0558 -0.0259 276 GLN B N 4498 C CA . GLN B 250 ? 0.2127 0.3790 0.3436 -0.0251 -0.0558 -0.0283 276 GLN B CA 4499 C C . GLN B 250 ? 0.1256 0.2754 0.2406 -0.0239 -0.0601 -0.0356 276 GLN B C 4500 O O . GLN B 250 ? 0.0996 0.2336 0.2166 -0.0315 -0.0571 -0.0350 276 GLN B O 4501 C CB . GLN B 250 ? 0.2324 0.4113 0.3856 -0.0337 -0.0616 -0.0326 276 GLN B CB 4502 C CG . GLN B 250 ? 0.3744 0.5720 0.5480 -0.0365 -0.0558 -0.0251 276 GLN B CG 4503 C CD . GLN B 250 ? 0.4669 0.6801 0.6657 -0.0473 -0.0614 -0.0280 276 GLN B CD 4504 O OE1 . GLN B 250 ? 0.5183 0.7285 0.7176 -0.0510 -0.0708 -0.0383 276 GLN B OE1 4505 N NE2 . GLN B 250 ? 0.4144 0.6454 0.6355 -0.0514 -0.0551 -0.0206 276 GLN B NE2 4506 N N . ALA B 251 ? 0.1112 0.2653 0.2089 -0.0128 -0.0664 -0.0419 277 ALA B N 4507 C CA . ALA B 251 ? 0.1197 0.2629 0.2015 -0.0098 -0.0695 -0.0500 277 ALA B CA 4508 C C . ALA B 251 ? 0.1411 0.2731 0.2093 -0.0076 -0.0619 -0.0432 277 ALA B C 4509 O O . ALA B 251 ? 0.1090 0.2274 0.1755 -0.0113 -0.0611 -0.0481 277 ALA B O 4510 C CB . ALA B 251 ? 0.1366 0.2912 0.2004 0.0028 -0.0763 -0.0563 277 ALA B CB 4511 N N . ASP B 252 ? 0.1003 0.2341 0.1589 -0.0013 -0.0556 -0.0313 278 ASP B N 4512 C CA . ASP B 252 ? 0.0957 0.2106 0.1397 -0.0002 -0.0452 -0.0219 278 ASP B CA 4513 C C . ASP B 252 ? 0.1771 0.2788 0.2333 -0.0101 -0.0389 -0.0191 278 ASP B C 4514 O O . ASP B 252 ? 0.0836 0.1709 0.1330 -0.0116 -0.0344 -0.0182 278 ASP B O 4515 C CB . ASP B 252 ? 0.1498 0.2633 0.1830 0.0084 -0.0404 -0.0098 278 ASP B CB 4516 C CG . ASP B 252 ? 0.2335 0.3526 0.2463 0.0191 -0.0434 -0.0064 278 ASP B CG 4517 O OD1 . ASP B 252 ? 0.2003 0.3267 0.2045 0.0206 -0.0480 -0.0149 278 ASP B OD1 4518 O OD2 . ASP B 252 ? 0.2441 0.3601 0.2488 0.0270 -0.0415 0.0050 278 ASP B OD2 4519 N N . ILE B 253 ? 0.0797 0.1894 0.1539 -0.0161 -0.0384 -0.0170 279 ILE B N 4520 C CA . ILE B 253 ? 0.0745 0.1749 0.1585 -0.0249 -0.0324 -0.0119 279 ILE B CA 4521 C C . ILE B 253 ? 0.1013 0.1878 0.1908 -0.0320 -0.0366 -0.0180 279 ILE B C 4522 O O . ILE B 253 ? 0.0809 0.1516 0.1659 -0.0336 -0.0323 -0.0139 279 ILE B O 4523 C CB . ILE B 253 ? 0.0962 0.2141 0.2000 -0.0307 -0.0303 -0.0076 279 ILE B CB 4524 C CG1 . ILE B 253 ? 0.1170 0.2456 0.2150 -0.0214 -0.0251 -0.0025 279 ILE B CG1 4525 C CG2 . ILE B 253 ? 0.0956 0.2062 0.2094 -0.0410 -0.0246 0.0000 279 ILE B CG2 4526 C CD1 . ILE B 253 ? 0.1787 0.3338 0.2974 -0.0241 -0.0236 -0.0010 279 ILE B CD1 4527 N N . GLU B 254 ? 0.0967 0.1890 0.1969 -0.0349 -0.0463 -0.0291 280 GLU B N 4528 C CA . GLU B 254 ? 0.1438 0.2197 0.2500 -0.0399 -0.0518 -0.0373 280 GLU B CA 4529 C C . GLU B 254 ? 0.1052 0.1720 0.1936 -0.0311 -0.0530 -0.0451 280 GLU B C 4530 O O . GLU B 254 ? 0.1102 0.1597 0.2001 -0.0325 -0.0530 -0.0467 280 GLU B O 4531 C CB . GLU B 254 ? 0.1200 0.2010 0.2358 -0.0429 -0.0600 -0.0471 280 GLU B CB 4532 C CG . GLU B 254 ? 0.6927 0.7833 0.8289 -0.0539 -0.0578 -0.0397 280 GLU B CG 4533 C CD . GLU B 254 ? 0.8065 0.8823 0.9530 -0.0639 -0.0504 -0.0283 280 GLU B CD 4534 O OE1 . GLU B 254 ? 0.8696 0.9242 1.0210 -0.0675 -0.0539 -0.0318 280 GLU B OE1 4535 O OE2 . GLU B 254 ? 0.7629 0.8480 0.9117 -0.0662 -0.0410 -0.0157 280 GLU B OE2 4536 N N . GLN B 255 ? 0.1049 0.1840 0.1750 -0.0210 -0.0529 -0.0479 281 GLN B N 4537 C CA . GLN B 255 ? 0.1092 0.1848 0.1606 -0.0126 -0.0506 -0.0523 281 GLN B CA 4538 C C . GLN B 255 ? 0.1119 0.1747 0.1575 -0.0132 -0.0401 -0.0410 281 GLN B C 4539 O O . GLN B 255 ? 0.1405 0.1959 0.1819 -0.0104 -0.0388 -0.0458 281 GLN B O 4540 C CB . GLN B 255 ? 0.1149 0.2082 0.1470 -0.0026 -0.0507 -0.0522 281 GLN B CB 4541 C CG . GLN B 255 ? 0.1237 0.2201 0.1366 0.0058 -0.0467 -0.0559 281 GLN B CG 4542 C CD . GLN B 255 ? 0.2273 0.3217 0.2446 0.0079 -0.0543 -0.0752 281 GLN B CD 4543 O OE1 . GLN B 255 ? 0.1874 0.2811 0.2143 0.0072 -0.0628 -0.0859 281 GLN B OE1 4544 N NE2 . GLN B 255 ? 0.1500 0.2390 0.1623 0.0109 -0.0484 -0.0769 281 GLN B NE2 4545 N N . GLN B 256 ? 0.0885 0.1508 0.1354 -0.0157 -0.0337 -0.0282 282 GLN B N 4546 C CA . GLN B 256 ? 0.0807 0.1330 0.1239 -0.0160 -0.0258 -0.0202 282 GLN B CA 4547 C C . GLN B 256 ? 0.1149 0.1536 0.1669 -0.0202 -0.0274 -0.0217 282 GLN B C 4548 O O . GLN B 256 ? 0.1062 0.1379 0.1539 -0.0174 -0.0248 -0.0221 282 GLN B O 4549 C CB . GLN B 256 ? 0.0726 0.1277 0.1171 -0.0166 -0.0207 -0.0100 282 GLN B CB 4550 C CG . GLN B 256 ? 0.1103 0.1569 0.1518 -0.0161 -0.0146 -0.0050 282 GLN B CG 4551 C CD . GLN B 256 ? 0.1154 0.1660 0.1589 -0.0152 -0.0110 0.0010 282 GLN B CD 4552 O OE1 . GLN B 256 ? 0.1082 0.1650 0.1593 -0.0183 -0.0108 0.0039 282 GLN B OE1 4553 N NE2 . GLN B 256 ? 0.1175 0.1655 0.1558 -0.0108 -0.0079 0.0025 282 GLN B NE2 4554 N N . ALA B 257 ? 0.1151 0.1507 0.1815 -0.0271 -0.0319 -0.0214 283 ALA B N 4555 C CA . ALA B 257 ? 0.0974 0.1166 0.1733 -0.0312 -0.0345 -0.0200 283 ALA B CA 4556 C C . ALA B 257 ? 0.1787 0.1886 0.2528 -0.0256 -0.0407 -0.0336 283 ALA B C 4557 O O . ALA B 257 ? 0.1892 0.1872 0.2619 -0.0222 -0.0404 -0.0328 283 ALA B O 4558 C CB . ALA B 257 ? 0.1291 0.1467 0.2249 -0.0419 -0.0383 -0.0162 283 ALA B CB 4559 N N . ARG B 258 ? 0.1162 0.1343 0.1896 -0.0226 -0.0468 -0.0472 284 ARG B N 4560 C CA . ARG B 258 ? 0.1257 0.1402 0.1960 -0.0147 -0.0525 -0.0633 284 ARG B CA 4561 C C . ARG B 258 ? 0.1308 0.1529 0.1856 -0.0062 -0.0445 -0.0623 284 ARG B C 4562 O O . ARG B 258 ? 0.1619 0.1779 0.2178 0.0000 -0.0465 -0.0705 284 ARG B O 4563 C CB . ARG B 258 ? 0.1449 0.1720 0.2132 -0.0108 -0.0596 -0.0781 284 ARG B CB 4564 C CG . ARG B 258 ? 0.2147 0.2316 0.3002 -0.0178 -0.0662 -0.0801 284 ARG B CG 4565 C CD . ARG B 258 ? 0.2693 0.2983 0.3520 -0.0115 -0.0732 -0.0958 284 ARG B CD 4566 N NE . ARG B 258 ? 0.3533 0.4047 0.4243 -0.0095 -0.0716 -0.0934 284 ARG B NE 4567 C CZ . ARG B 258 ? 0.3176 0.3773 0.3974 -0.0151 -0.0750 -0.0914 284 ARG B CZ 4568 N NH1 . ARG B 258 ? 0.3081 0.3570 0.4093 -0.0250 -0.0792 -0.0917 284 ARG B NH1 4569 N NH2 . ARG B 258 ? 0.1590 0.2390 0.2267 -0.0103 -0.0741 -0.0885 284 ARG B NH2 4570 N N . ASP B 259 ? 0.1162 0.1513 0.1595 -0.0059 -0.0360 -0.0525 285 ASP B N 4571 C CA . ASP B 259 ? 0.1705 0.2139 0.2034 -0.0010 -0.0275 -0.0495 285 ASP B CA 4572 C C . ASP B 259 ? 0.1345 0.1675 0.1733 -0.0020 -0.0247 -0.0441 285 ASP B C 4573 O O . ASP B 259 ? 0.1203 0.1573 0.1589 0.0033 -0.0227 -0.0496 285 ASP B O 4574 C CB . ASP B 259 ? 0.1477 0.2018 0.1709 -0.0020 -0.0204 -0.0384 285 ASP B CB 4575 C CG . ASP B 259 ? 0.2610 0.3300 0.2735 0.0025 -0.0228 -0.0425 285 ASP B CG 4576 O OD1 . ASP B 259 ? 0.2403 0.3170 0.2493 0.0083 -0.0279 -0.0565 285 ASP B OD1 4577 O OD2 . ASP B 259 ? 0.1775 0.2512 0.1843 0.0020 -0.0205 -0.0326 285 ASP B OD2 4578 N N . TYR B 260 ? 0.1182 0.1414 0.1620 -0.0076 -0.0245 -0.0340 286 TYR B N 4579 C CA . TYR B 260 ? 0.0920 0.1070 0.1388 -0.0065 -0.0238 -0.0296 286 TYR B CA 4580 C C . TYR B 260 ? 0.1196 0.1230 0.1731 -0.0018 -0.0310 -0.0377 286 TYR B C 4581 O O . TYR B 260 ? 0.1500 0.1543 0.2042 0.0043 -0.0309 -0.0408 286 TYR B O 4582 C CB . TYR B 260 ? 0.0846 0.0944 0.1330 -0.0117 -0.0225 -0.0175 286 TYR B CB 4583 C CG . TYR B 260 ? 0.1074 0.1261 0.1502 -0.0118 -0.0162 -0.0119 286 TYR B CG 4584 C CD1 . TYR B 260 ? 0.0964 0.1161 0.1378 -0.0085 -0.0148 -0.0114 286 TYR B CD1 4585 C CD2 . TYR B 260 ? 0.1278 0.1537 0.1685 -0.0141 -0.0132 -0.0089 286 TYR B CD2 4586 C CE1 . TYR B 260 ? 0.0970 0.1229 0.1363 -0.0085 -0.0109 -0.0096 286 TYR B CE1 4587 C CE2 . TYR B 260 ? 0.1134 0.1437 0.1514 -0.0130 -0.0090 -0.0055 286 TYR B CE2 4588 C CZ . TYR B 260 ? 0.2050 0.2344 0.2430 -0.0107 -0.0079 -0.0067 286 TYR B CZ 4589 O OH . TYR B 260 ? 0.1190 0.1509 0.1571 -0.0095 -0.0056 -0.0066 286 TYR B OH 4590 N N . ALA B 261 ? 0.1182 0.1108 0.1792 -0.0040 -0.0382 -0.0423 287 ALA B N 4591 C CA . ALA B 261 ? 0.1307 0.1074 0.2005 0.0015 -0.0469 -0.0512 287 ALA B CA 4592 C C . ALA B 261 ? 0.1926 0.1816 0.2588 0.0123 -0.0475 -0.0683 287 ALA B C 4593 O O . ALA B 261 ? 0.2003 0.1829 0.2714 0.0209 -0.0518 -0.0751 287 ALA B O 4594 C CB . ALA B 261 ? 0.1468 0.1078 0.2297 -0.0047 -0.0557 -0.0546 287 ALA B CB 4595 N N . THR B 262 ? 0.1699 0.1788 0.2272 0.0131 -0.0430 -0.0743 288 THR B N 4596 C CA . THR B 262 ? 0.2010 0.2286 0.2530 0.0235 -0.0409 -0.0887 288 THR B CA 4597 C C . THR B 262 ? 0.1657 0.2043 0.2178 0.0269 -0.0332 -0.0844 288 THR B C 4598 O O . THR B 262 ? 0.1305 0.1771 0.1870 0.0369 -0.0345 -0.0964 288 THR B O 4599 C CB . THR B 262 ? 0.2483 0.2979 0.2872 0.0236 -0.0357 -0.0907 288 THR B CB 4600 O OG1 . THR B 262 ? 0.1842 0.2281 0.2249 0.0229 -0.0454 -0.1003 288 THR B OG1 4601 C CG2 . THR B 262 ? 0.2316 0.3063 0.2630 0.0340 -0.0301 -0.1017 288 THR B CG2 4602 N N . VAL B 263 ? 0.1080 0.1489 0.1575 0.0193 -0.0260 -0.0693 289 VAL B N 4603 C CA . VAL B 263 ? 0.0996 0.1512 0.1531 0.0205 -0.0202 -0.0661 289 VAL B CA 4604 C C . VAL B 263 ? 0.1481 0.1871 0.2105 0.0267 -0.0280 -0.0689 289 VAL B C 4605 O O . VAL B 263 ? 0.1450 0.1965 0.2141 0.0341 -0.0276 -0.0765 289 VAL B O 4606 C CB . VAL B 263 ? 0.1096 0.1621 0.1607 0.0113 -0.0137 -0.0518 289 VAL B CB 4607 C CG1 . VAL B 263 ? 0.1018 0.1640 0.1614 0.0119 -0.0107 -0.0516 289 VAL B CG1 4608 C CG2 . VAL B 263 ? 0.0839 0.1476 0.1267 0.0068 -0.0063 -0.0468 289 VAL B CG2 4609 N N . VAL B 264 ? 0.1119 0.1278 0.1749 0.0241 -0.0348 -0.0616 290 VAL B N 4610 C CA . VAL B 264 ? 0.1239 0.1248 0.1930 0.0311 -0.0430 -0.0607 290 VAL B CA 4611 C C . VAL B 264 ? 0.1513 0.1493 0.2282 0.0431 -0.0504 -0.0771 290 VAL B C 4612 O O . VAL B 264 ? 0.1463 0.1481 0.2295 0.0537 -0.0542 -0.0827 290 VAL B O 4613 C CB . VAL B 264 ? 0.2159 0.1925 0.2842 0.0253 -0.0478 -0.0467 290 VAL B CB 4614 C CG1 . VAL B 264 ? 0.1788 0.1355 0.2530 0.0342 -0.0576 -0.0443 290 VAL B CG1 4615 C CG2 . VAL B 264 ? 0.1404 0.1236 0.2008 0.0177 -0.0411 -0.0324 290 VAL B CG2 4616 N N . ASN B 265 ? 0.2321 0.2259 0.3095 0.0429 -0.0533 -0.0871 291 ASN B N 4617 C CA . ASN B 265 ? 0.1764 0.1686 0.2607 0.0547 -0.0611 -0.1048 291 ASN B CA 4618 C C . ASN B 265 ? 0.2151 0.2399 0.2985 0.0632 -0.0546 -0.1151 291 ASN B C 4619 O O . ASN B 265 ? 0.2435 0.2711 0.3330 0.0725 -0.0602 -0.1222 291 ASN B O 4620 C CB . ASN B 265 ? 0.2567 0.2453 0.3403 0.0510 -0.0648 -0.1116 291 ASN B CB 4621 C CG . ASN B 265 ? 0.4052 0.3633 0.4963 0.0416 -0.0722 -0.1013 291 ASN B CG 4622 O OD1 . ASN B 265 ? 0.4448 0.3813 0.5414 0.0405 -0.0762 -0.0896 291 ASN B OD1 4623 N ND2 . ASN B 265 ? 0.3866 0.3454 0.4780 0.0348 -0.0734 -0.1041 291 ASN B ND2 4624 N N . ALA B 266 ? 0.1621 0.2122 0.2385 0.0590 -0.0426 -0.1146 292 ALA B N 4625 C CA . ALA B 266 ? 0.1923 0.2759 0.2694 0.0635 -0.0344 -0.1203 292 ALA B CA 4626 C C . ALA B 266 ? 0.1843 0.2725 0.2713 0.0660 -0.0347 -0.1170 292 ALA B C 4627 O O . ALA B 266 ? 0.1705 0.2765 0.2623 0.0724 -0.0347 -0.1246 292 ALA B O 4628 C CB . ALA B 266 ? 0.1684 0.2758 0.2366 0.0562 -0.0203 -0.1149 292 ALA B CB 4629 N N . CYS B 267 ? 0.2135 0.2873 0.3034 0.0616 -0.0360 -0.1061 293 CYS B N 4630 C CA A CYS B 267 ? 0.2217 0.2986 0.3190 0.0646 -0.0394 -0.1026 293 CYS B CA 4631 C CA B CYS B 267 ? 0.2420 0.3179 0.3392 0.0646 -0.0396 -0.1024 293 CYS B CA 4632 C C . CYS B 267 ? 0.2251 0.2849 0.3245 0.0756 -0.0520 -0.1076 293 CYS B C 4633 O O . CYS B 267 ? 0.2256 0.3007 0.3304 0.0822 -0.0535 -0.1151 293 CYS B O 4634 C CB A CYS B 267 ? 0.2830 0.3479 0.3774 0.0567 -0.0397 -0.0876 293 CYS B CB 4635 C CB B CYS B 267 ? 0.3027 0.3641 0.3959 0.0565 -0.0404 -0.0869 293 CYS B CB 4636 S SG A CYS B 267 ? 0.1797 0.2501 0.2811 0.0637 -0.0469 -0.0860 293 CYS B SG 4637 S SG B CYS B 267 ? 0.4222 0.5007 0.5121 0.0407 -0.0271 -0.0778 293 CYS B SG 4638 N N . LYS B 268 ? 0.1626 0.1906 0.2593 0.0767 -0.0608 -0.1029 294 LYS B N 4639 C CA . LYS B 268 ? 0.2712 0.2785 0.3709 0.0859 -0.0728 -0.1039 294 LYS B CA 4640 C C . LYS B 268 ? 0.3153 0.3345 0.4198 0.0945 -0.0761 -0.1209 294 LYS B C 4641 O O . LYS B 268 ? 0.3189 0.3321 0.4280 0.1045 -0.0844 -0.1250 294 LYS B O 4642 C CB . LYS B 268 ? 0.3538 0.3242 0.4520 0.0816 -0.0800 -0.0931 294 LYS B CB 4643 C CG . LYS B 268 ? 0.3632 0.3214 0.4560 0.0741 -0.0777 -0.0743 294 LYS B CG 4644 C CD . LYS B 268 ? 0.4278 0.3517 0.5210 0.0674 -0.0833 -0.0614 294 LYS B CD 4645 C CE . LYS B 268 ? 0.4914 0.3941 0.5882 0.0751 -0.0930 -0.0578 294 LYS B CE 4646 N NZ . LYS B 268 ? 0.4658 0.3372 0.5668 0.0659 -0.0969 -0.0446 294 LYS B NZ 4647 N N . ALA B 269 ? 0.1980 0.2360 0.3006 0.0921 -0.0697 -0.1305 295 ALA B N 4648 C CA . ALA B 269 ? 0.2493 0.3033 0.3553 0.1016 -0.0727 -0.1471 295 ALA B CA 4649 C C . ALA B 269 ? 0.2803 0.3628 0.3910 0.1079 -0.0689 -0.1531 295 ALA B C 4650 O O . ALA B 269 ? 0.2319 0.3274 0.3471 0.1181 -0.0729 -0.1668 295 ALA B O 4651 C CB . ALA B 269 ? 0.2184 0.2905 0.3181 0.0983 -0.0660 -0.1542 295 ALA B CB 4652 N N . GLN B 270 ? 0.2104 0.3033 0.3218 0.1017 -0.0618 -0.1435 296 GLN B N 4653 C CA . GLN B 270 ? 0.2227 0.3444 0.3413 0.1049 -0.0575 -0.1484 296 GLN B CA 4654 C C . GLN B 270 ? 0.2399 0.3493 0.3636 0.1136 -0.0682 -0.1476 296 GLN B C 4655 O O . GLN B 270 ? 0.2573 0.3889 0.3885 0.1166 -0.0666 -0.1519 296 GLN B O 4656 C CB . GLN B 270 ? 0.1689 0.3114 0.2885 0.0921 -0.0440 -0.1395 296 GLN B CB 4657 C CG . GLN B 270 ? 0.1763 0.3272 0.2883 0.0827 -0.0327 -0.1356 296 GLN B CG 4658 C CD . GLN B 270 ? 0.2674 0.4347 0.3751 0.0889 -0.0306 -0.1470 296 GLN B CD 4659 O OE1 . GLN B 270 ? 0.2564 0.4456 0.3700 0.0962 -0.0300 -0.1567 296 GLN B OE1 4660 N NE2 . GLN B 270 ? 0.2194 0.3781 0.3168 0.0869 -0.0300 -0.1467 296 GLN B NE2 4661 N N . GLY B 271 ? 0.2945 0.3686 0.4143 0.1172 -0.0789 -0.1405 297 GLY B N 4662 C CA . GLY B 271 ? 0.3012 0.3607 0.4225 0.1262 -0.0890 -0.1358 297 GLY B CA 4663 C C . GLY B 271 ? 0.2544 0.3282 0.3756 0.1222 -0.0854 -0.1279 297 GLY B C 4664 O O . GLY B 271 ? 0.2536 0.3299 0.3707 0.1110 -0.0782 -0.1189 297 GLY B O 4665 N N . ALA B 272 ? 0.2596 0.3440 0.3861 0.1321 -0.0913 -0.1329 298 ALA B N 4666 C CA . ALA B 272 ? 0.2475 0.3449 0.3745 0.1304 -0.0911 -0.1276 298 ALA B CA 4667 C C . ALA B 272 ? 0.2010 0.3306 0.3359 0.1179 -0.0787 -0.1322 298 ALA B C 4668 O O . ALA B 272 ? 0.2323 0.3706 0.3681 0.1126 -0.0775 -0.1279 298 ALA B O 4669 C CB . ALA B 272 ? 0.3155 0.4186 0.4475 0.1453 -0.1013 -0.1340 298 ALA B CB 4670 N N . ALA B 273 ? 0.1939 0.3405 0.3343 0.1132 -0.0695 -0.1402 299 ALA B N 4671 C CA . ALA B 273 ? 0.1757 0.3520 0.3252 0.1007 -0.0561 -0.1418 299 ALA B CA 4672 C C . ALA B 273 ? 0.1849 0.3530 0.3286 0.0862 -0.0483 -0.1298 299 ALA B C 4673 O O . ALA B 273 ? 0.1591 0.3449 0.3111 0.0748 -0.0394 -0.1274 299 ALA B O 4674 C CB . ALA B 273 ? 0.1805 0.3785 0.3348 0.1018 -0.0482 -0.1514 299 ALA B CB 4675 N N . CYS B 274 ? 0.1738 0.3147 0.3053 0.0864 -0.0517 -0.1222 300 CYS B N 4676 C CA . CYS B 274 ? 0.1342 0.2668 0.2605 0.0746 -0.0462 -0.1112 300 CYS B CA 4677 C C . CYS B 274 ? 0.1553 0.2712 0.2752 0.0775 -0.0553 -0.1030 300 CYS B C 4678 O O . CYS B 274 ? 0.2100 0.3022 0.3212 0.0860 -0.0643 -0.0976 300 CYS B O 4679 C CB . CYS B 274 ? 0.1306 0.2477 0.2483 0.0721 -0.0434 -0.1078 300 CYS B CB 4680 S SG . CYS B 274 ? 0.2617 0.3718 0.3748 0.0584 -0.0366 -0.0948 300 CYS B SG 4681 N N . VAL B 275 ? 0.1284 0.2559 0.2521 0.0707 -0.0531 -0.1013 301 VAL B N 4682 C CA . VAL B 275 ? 0.1367 0.2561 0.2531 0.0764 -0.0625 -0.0966 301 VAL B CA 4683 C C . VAL B 275 ? 0.1648 0.2690 0.2690 0.0713 -0.0626 -0.0846 301 VAL B C 4684 O O . VAL B 275 ? 0.1405 0.2357 0.2331 0.0780 -0.0704 -0.0776 301 VAL B O 4685 C CB . VAL B 275 ? 0.2783 0.4198 0.4055 0.0743 -0.0629 -0.1049 301 VAL B CB 4686 C CG1 . VAL B 275 ? 0.1489 0.3083 0.2887 0.0814 -0.0643 -0.1165 301 VAL B CG1 4687 C CG2 . VAL B 275 ? 0.1211 0.2736 0.2580 0.0585 -0.0525 -0.1051 301 VAL B CG2 4688 N N . GLY B 276 ? 0.1127 0.2161 0.2185 0.0602 -0.0539 -0.0816 302 GLY B N 4689 C CA . GLY B 276 ? 0.1064 0.1981 0.2019 0.0557 -0.0542 -0.0713 302 GLY B CA 4690 C C . GLY B 276 ? 0.1033 0.1966 0.2024 0.0430 -0.0444 -0.0691 302 GLY B C 4691 O O . GLY B 276 ? 0.0943 0.1992 0.2033 0.0360 -0.0357 -0.0739 302 GLY B O 4692 N N . ILE B 277 ? 0.0891 0.1668 0.1737 0.0386 -0.0436 -0.0586 303 ILE B N 4693 C CA . ILE B 277 ? 0.0793 0.1514 0.1602 0.0265 -0.0343 -0.0534 303 ILE B CA 4694 C C . ILE B 277 ? 0.1720 0.2442 0.2475 0.0230 -0.0348 -0.0509 303 ILE B C 4695 O O . ILE B 277 ? 0.1429 0.2109 0.2064 0.0296 -0.0408 -0.0464 303 ILE B O 4696 C CB . ILE B 277 ? 0.0835 0.1360 0.1523 0.0250 -0.0326 -0.0444 303 ILE B CB 4697 C CG1 . ILE B 277 ? 0.2060 0.2584 0.2807 0.0298 -0.0333 -0.0511 303 ILE B CG1 4698 C CG2 . ILE B 277 ? 0.0748 0.1237 0.1388 0.0146 -0.0248 -0.0388 303 ILE B CG2 4699 C CD1 . ILE B 277 ? 0.1939 0.2248 0.2613 0.0312 -0.0369 -0.0460 303 ILE B CD1 4700 N N . THR B 278 ? 0.0694 0.1466 0.1536 0.0137 -0.0287 -0.0535 304 THR B N 4701 C CA . THR B 278 ? 0.0698 0.1453 0.1513 0.0109 -0.0295 -0.0542 304 THR B CA 4702 C C . THR B 278 ? 0.1205 0.1847 0.1974 0.0029 -0.0217 -0.0465 304 THR B C 4703 O O . THR B 278 ? 0.1030 0.1675 0.1875 -0.0039 -0.0151 -0.0444 304 THR B O 4704 C CB . THR B 278 ? 0.0706 0.1593 0.1713 0.0078 -0.0321 -0.0664 304 THR B CB 4705 O OG1 . THR B 278 ? 0.0802 0.1775 0.1800 0.0169 -0.0392 -0.0728 304 THR B OG1 4706 C CG2 . THR B 278 ? 0.0749 0.1584 0.1748 0.0055 -0.0337 -0.0703 304 THR B CG2 4707 N N . THR B 279 ? 0.0858 0.1430 0.1500 0.0049 -0.0223 -0.0418 305 THR B N 4708 C CA . THR B 279 ? 0.0858 0.1347 0.1478 -0.0006 -0.0165 -0.0362 305 THR B CA 4709 C C . THR B 279 ? 0.1202 0.1693 0.1919 -0.0023 -0.0181 -0.0441 305 THR B C 4710 O O . THR B 279 ? 0.0782 0.1343 0.1517 0.0028 -0.0246 -0.0539 305 THR B O 4711 C CB . THR B 279 ? 0.0813 0.1254 0.1282 0.0021 -0.0155 -0.0276 305 THR B CB 4712 O OG1 . THR B 279 ? 0.0946 0.1454 0.1328 0.0093 -0.0198 -0.0293 305 THR B OG1 4713 C CG2 . THR B 279 ? 0.1285 0.1676 0.1709 0.0011 -0.0146 -0.0203 305 THR B CG2 4714 N N . TRP B 280 ? 0.1095 0.1503 0.1878 -0.0085 -0.0133 -0.0403 306 TRP B N 4715 C CA . TRP B 280 ? 0.0773 0.1130 0.1696 -0.0110 -0.0157 -0.0478 306 TRP B CA 4716 C C . TRP B 280 ? 0.1037 0.1352 0.1867 -0.0036 -0.0189 -0.0512 306 TRP B C 4717 O O . TRP B 280 ? 0.0969 0.1177 0.1819 -0.0043 -0.0169 -0.0475 306 TRP B O 4718 C CB . TRP B 280 ? 0.0814 0.1079 0.1861 -0.0205 -0.0093 -0.0397 306 TRP B CB 4719 C CG . TRP B 280 ? 0.0929 0.1138 0.2205 -0.0260 -0.0129 -0.0485 306 TRP B CG 4720 C CD1 . TRP B 280 ? 0.2011 0.2047 0.3381 -0.0279 -0.0142 -0.0482 306 TRP B CD1 4721 C CD2 . TRP B 280 ? 0.1698 0.2008 0.3126 -0.0283 -0.0168 -0.0592 306 TRP B CD2 4722 N NE1 . TRP B 280 ? 0.2106 0.2118 0.3669 -0.0318 -0.0184 -0.0573 306 TRP B NE1 4723 C CE2 . TRP B 280 ? 0.1298 0.1488 0.2879 -0.0317 -0.0195 -0.0635 306 TRP B CE2 4724 C CE3 . TRP B 280 ? 0.1105 0.1582 0.2517 -0.0254 -0.0183 -0.0640 306 TRP B CE3 4725 C CZ2 . TRP B 280 ? 0.1246 0.1501 0.2982 -0.0337 -0.0233 -0.0729 306 TRP B CZ2 4726 C CZ3 . TRP B 280 ? 0.1454 0.1996 0.3009 -0.0264 -0.0220 -0.0732 306 TRP B CZ3 4727 C CH2 . TRP B 280 ? 0.1825 0.2266 0.3547 -0.0313 -0.0242 -0.0777 306 TRP B CH2 4728 N N . GLY B 281 ? 0.0848 0.1273 0.1574 0.0049 -0.0238 -0.0580 307 GLY B N 4729 C CA . GLY B 281 ? 0.0914 0.1381 0.1525 0.0139 -0.0255 -0.0617 307 GLY B CA 4730 C C . GLY B 281 ? 0.1649 0.2232 0.2068 0.0193 -0.0233 -0.0529 307 GLY B C 4731 O O . GLY B 281 ? 0.1213 0.1792 0.1598 0.0159 -0.0216 -0.0440 307 GLY B O 4732 N N . ILE B 282 ? 0.1132 0.1822 0.1439 0.0279 -0.0233 -0.0553 308 ILE B N 4733 C CA . ILE B 282 ? 0.1585 0.2394 0.1726 0.0314 -0.0189 -0.0431 308 ILE B CA 4734 C C . ILE B 282 ? 0.1749 0.2560 0.1892 0.0289 -0.0120 -0.0343 308 ILE B C 4735 O O . ILE B 282 ? 0.1329 0.2099 0.1473 0.0218 -0.0077 -0.0211 308 ILE B O 4736 C CB . ILE B 282 ? 0.1473 0.2482 0.1467 0.0439 -0.0223 -0.0505 308 ILE B CB 4737 C CG1 . ILE B 282 ? 0.1187 0.2219 0.1177 0.0470 -0.0307 -0.0582 308 ILE B CG1 4738 C CG2 . ILE B 282 ? 0.1781 0.2938 0.1609 0.0466 -0.0150 -0.0339 308 ILE B CG2 4739 C CD1 . ILE B 282 ? 0.1374 0.2630 0.1190 0.0615 -0.0362 -0.0667 308 ILE B CD1 4740 N N . THR B 283 ? 0.1522 0.2383 0.1691 0.0354 -0.0123 -0.0436 309 THR B N 4741 C CA . THR B 283 ? 0.1353 0.2266 0.1540 0.0357 -0.0068 -0.0376 309 THR B CA 4742 C C . THR B 283 ? 0.0938 0.1677 0.1261 0.0335 -0.0089 -0.0411 309 THR B C 4743 O O . THR B 283 ? 0.1017 0.1623 0.1425 0.0350 -0.0144 -0.0521 309 THR B O 4744 C CB . THR B 283 ? 0.1079 0.2234 0.1185 0.0481 -0.0047 -0.0444 309 THR B CB 4745 O OG1 . THR B 283 ? 0.1898 0.3109 0.2077 0.0503 -0.0012 -0.0432 309 THR B OG1 4746 C CG2 . THR B 283 ? 0.1210 0.2369 0.1319 0.0590 -0.0126 -0.0656 309 THR B CG2 4747 N N . ASP B 284 ? 0.0908 0.1649 0.1259 0.0299 -0.0051 -0.0312 310 ASP B N 4748 C CA . ASP B 284 ? 0.1502 0.2110 0.1945 0.0303 -0.0070 -0.0310 310 ASP B CA 4749 C C . ASP B 284 ? 0.1029 0.1606 0.1533 0.0417 -0.0114 -0.0446 310 ASP B C 4750 O O . ASP B 284 ? 0.1561 0.1942 0.2159 0.0424 -0.0152 -0.0458 310 ASP B O 4751 C CB . ASP B 284 ? 0.1344 0.2061 0.1799 0.0291 -0.0037 -0.0215 310 ASP B CB 4752 C CG . ASP B 284 ? 0.1566 0.2275 0.1998 0.0181 -0.0015 -0.0107 310 ASP B CG 4753 O OD1 . ASP B 284 ? 0.1415 0.1992 0.1828 0.0122 -0.0026 -0.0094 310 ASP B OD1 4754 O OD2 . ASP B 284 ? 0.1503 0.2351 0.1959 0.0155 0.0008 -0.0049 310 ASP B OD2 4755 N N . LEU B 285 ? 0.1100 0.1874 0.1548 0.0514 -0.0111 -0.0544 311 LEU B N 4756 C CA . LEU B 285 ? 0.1367 0.2164 0.1869 0.0656 -0.0157 -0.0707 311 LEU B CA 4757 C C . LEU B 285 ? 0.1376 0.1903 0.1994 0.0658 -0.0243 -0.0827 311 LEU B C 4758 O O . LEU B 285 ? 0.1836 0.2227 0.2565 0.0741 -0.0298 -0.0919 311 LEU B O 4759 C CB . LEU B 285 ? 0.1946 0.3048 0.2332 0.0766 -0.0133 -0.0805 311 LEU B CB 4760 C CG . LEU B 285 ? 0.2404 0.3567 0.2789 0.0885 -0.0179 -0.0943 311 LEU B CG 4761 C CD1 . LEU B 285 ? 0.2316 0.3530 0.2766 0.0918 -0.0148 -0.0882 311 LEU B CD1 4762 C CD2 . LEU B 285 ? 0.2236 0.3691 0.2456 0.0950 -0.0163 -0.0988 311 LEU B CD2 4763 N N . TYR B 286 ? 0.1791 0.2241 0.2408 0.0565 -0.0259 -0.0828 312 TYR B N 4764 C CA . TYR B 286 ? 0.1463 0.1698 0.2233 0.0540 -0.0339 -0.0951 312 TYR B CA 4765 C C . TYR B 286 ? 0.2489 0.2520 0.3356 0.0381 -0.0316 -0.0808 312 TYR B C 4766 O O . TYR B 286 ? 0.2212 0.2091 0.3237 0.0317 -0.0364 -0.0874 312 TYR B O 4767 C CB . TYR B 286 ? 0.1517 0.1897 0.2242 0.0583 -0.0394 -0.1120 312 TYR B CB 4768 C CG . TYR B 286 ? 0.2245 0.2887 0.2821 0.0713 -0.0404 -0.1198 312 TYR B CG 4769 C CD1 . TYR B 286 ? 0.1975 0.2600 0.2604 0.0798 -0.0451 -0.1289 312 TYR B CD1 4770 C CD2 . TYR B 286 ? 0.2038 0.2950 0.2420 0.0754 -0.0367 -0.1168 312 TYR B CD2 4771 C CE1 . TYR B 286 ? 0.1918 0.2813 0.2417 0.0920 -0.0459 -0.1365 312 TYR B CE1 4772 C CE2 . TYR B 286 ? 0.1869 0.3043 0.2114 0.0868 -0.0366 -0.1210 312 TYR B CE2 4773 C CZ . TYR B 286 ? 0.2323 0.3500 0.2631 0.0950 -0.0411 -0.1318 312 TYR B CZ 4774 O OH . TYR B 286 ? 0.2259 0.3723 0.2441 0.1069 -0.0410 -0.1369 312 TYR B OH 4775 N N . SER B 287 ? 0.2048 0.2106 0.2832 0.0317 -0.0244 -0.0624 313 SER B N 4776 C CA . SER B 287 ? 0.1603 0.1528 0.2442 0.0190 -0.0209 -0.0490 313 SER B CA 4777 C C . SER B 287 ? 0.1569 0.1240 0.2574 0.0161 -0.0236 -0.0466 313 SER B C 4778 O O . SER B 287 ? 0.1516 0.1091 0.2554 0.0247 -0.0269 -0.0483 313 SER B O 4779 C CB . SER B 287 ? 0.1744 0.1749 0.2460 0.0161 -0.0146 -0.0330 313 SER B CB 4780 O OG . SER B 287 ? 0.1726 0.1634 0.2470 0.0066 -0.0111 -0.0211 313 SER B OG 4781 N N . TRP B 288 ? 0.1599 0.1168 0.2725 0.0041 -0.0218 -0.0414 314 TRP B N 4782 C CA . TRP B 288 ? 0.1626 0.0941 0.2925 -0.0018 -0.0224 -0.0334 314 TRP B CA 4783 C C . TRP B 288 ? 0.2243 0.1490 0.3437 -0.0004 -0.0174 -0.0126 314 TRP B C 4784 O O . TRP B 288 ? 0.1896 0.0915 0.3188 -0.0010 -0.0186 -0.0028 314 TRP B O 4785 C CB . TRP B 288 ? 0.2351 0.1644 0.3816 -0.0170 -0.0191 -0.0300 314 TRP B CB 4786 C CG . TRP B 288 ? 0.2290 0.1750 0.3621 -0.0234 -0.0096 -0.0156 314 TRP B CG 4787 C CD1 . TRP B 288 ? 0.1755 0.1432 0.2947 -0.0214 -0.0081 -0.0203 314 TRP B CD1 4788 C CD2 . TRP B 288 ? 0.3429 0.2853 0.4742 -0.0310 -0.0010 0.0052 314 TRP B CD2 4789 N NE1 . TRP B 288 ? 0.1667 0.1435 0.2778 -0.0269 -0.0001 -0.0069 314 TRP B NE1 4790 C CE2 . TRP B 288 ? 0.2718 0.2361 0.3886 -0.0324 0.0048 0.0085 314 TRP B CE2 4791 C CE3 . TRP B 288 ? 0.5045 0.4272 0.6441 -0.0358 0.0022 0.0222 314 TRP B CE3 4792 C CZ2 . TRP B 288 ? 0.4726 0.4437 0.5819 -0.0373 0.0137 0.0250 314 TRP B CZ2 4793 C CZ3 . TRP B 288 ? 0.6202 0.5504 0.7505 -0.0414 0.0121 0.0423 314 TRP B CZ3 4794 C CH2 . TRP B 288 ? 0.5974 0.5535 0.7121 -0.0416 0.0178 0.0421 314 TRP B CH2 4795 N N . ILE B 289 ? 0.1879 0.1315 0.2878 0.0018 -0.0128 -0.0058 315 ILE B N 4796 C CA . ILE B 289 ? 0.2564 0.1977 0.3457 0.0025 -0.0090 0.0127 315 ILE B CA 4797 C C . ILE B 289 ? 0.1716 0.1001 0.2610 0.0143 -0.0142 0.0167 315 ILE B C 4798 O O . ILE B 289 ? 0.2777 0.1884 0.3697 0.0135 -0.0136 0.0322 315 ILE B O 4799 C CB . ILE B 289 ? 0.2504 0.2151 0.3222 0.0024 -0.0052 0.0153 315 ILE B CB 4800 C CG1 . ILE B 289 ? 0.2011 0.1732 0.2734 -0.0084 0.0006 0.0176 315 ILE B CG1 4801 C CG2 . ILE B 289 ? 0.1577 0.1252 0.2173 0.0076 -0.0047 0.0285 315 ILE B CG2 4802 C CD1 . ILE B 289 ? 0.2500 0.2394 0.3150 -0.0086 0.0007 0.0089 315 ILE B CD1 4803 N N . PRO B 290 ? 0.2147 0.1528 0.3019 0.0260 -0.0191 0.0039 316 PRO B N 4804 C CA . PRO B 290 ? 0.3021 0.2310 0.3909 0.0393 -0.0246 0.0069 316 PRO B CA 4805 C C . PRO B 290 ? 0.3545 0.2496 0.4599 0.0414 -0.0299 0.0093 316 PRO B C 4806 O O . PRO B 290 ? 0.3511 0.2322 0.4565 0.0506 -0.0339 0.0198 316 PRO B O 4807 C CB . PRO B 290 ? 0.2522 0.2006 0.3409 0.0508 -0.0278 -0.0113 316 PRO B CB 4808 C CG . PRO B 290 ? 0.2668 0.2365 0.3484 0.0431 -0.0229 -0.0178 316 PRO B CG 4809 C CD . PRO B 290 ? 0.1982 0.1574 0.2820 0.0289 -0.0195 -0.0122 316 PRO B CD 4810 N N . SER B 291 ? 0.4067 0.2882 0.5277 0.0336 -0.0313 -0.0006 317 SER B N 4811 C CA . SER B 291 ? 0.4456 0.2978 0.5820 0.0328 -0.0362 -0.0001 317 SER B CA 4812 C C . SER B 291 ? 0.3721 0.2092 0.5109 0.0180 -0.0295 0.0230 317 SER B C 4813 O O . SER B 291 ? 0.5030 0.3179 0.6485 0.0165 -0.0313 0.0307 317 SER B O 4814 C CB . SER B 291 ? 0.4597 0.3133 0.6089 0.0309 -0.0414 -0.0240 317 SER B CB 4815 O OG . SER B 291 ? 0.4492 0.3135 0.6030 0.0174 -0.0373 -0.0272 317 SER B OG 4816 N N . THR B 292 ? 0.3413 0.1926 0.4739 0.0075 -0.0211 0.0341 318 THR B N 4817 C CA . THR B 292 ? 0.3709 0.2178 0.5011 -0.0052 -0.0124 0.0564 318 THR B CA 4818 C C . THR B 292 ? 0.4625 0.3132 0.5715 0.0018 -0.0091 0.0786 318 THR B C 4819 O O . THR B 292 ? 0.5331 0.3697 0.6369 0.0016 -0.0075 0.0956 318 THR B O 4820 C CB . THR B 292 ? 0.3907 0.2571 0.5245 -0.0194 -0.0043 0.0548 318 THR B CB 4821 O OG1 . THR B 292 ? 0.4925 0.3607 0.6431 -0.0228 -0.0096 0.0318 318 THR B OG1 4822 C CG2 . THR B 292 ? 0.2877 0.1541 0.4213 -0.0320 0.0053 0.0744 318 THR B CG2 4823 N N . TYR B 293 ? 0.3361 0.2109 0.4289 0.0084 -0.0085 0.0756 319 TYR B N 4824 C CA . TYR B 293 ? 0.3456 0.2316 0.4161 0.0172 -0.0079 0.0910 319 TYR B CA 4825 C C . TYR B 293 ? 0.3438 0.2352 0.4101 0.0342 -0.0173 0.0802 319 TYR B C 4826 O O . TYR B 293 ? 0.3438 0.2606 0.4032 0.0370 -0.0181 0.0662 319 TYR B O 4827 C CB . TYR B 293 ? 0.3751 0.2919 0.4280 0.0117 -0.0008 0.0911 319 TYR B CB 4828 C CG . TYR B 293 ? 0.4209 0.3422 0.4791 -0.0035 0.0091 0.0962 319 TYR B CG 4829 C CD1 . TYR B 293 ? 0.5566 0.4717 0.6125 -0.0098 0.0171 0.1196 319 TYR B CD1 4830 C CD2 . TYR B 293 ? 0.5035 0.4384 0.5688 -0.0108 0.0110 0.0787 319 TYR B CD2 4831 C CE1 . TYR B 293 ? 0.5446 0.4711 0.6063 -0.0234 0.0270 0.1214 319 TYR B CE1 4832 C CE2 . TYR B 293 ? 0.5984 0.5414 0.6708 -0.0233 0.0195 0.0818 319 TYR B CE2 4833 C CZ . TYR B 293 ? 0.6319 0.5717 0.7044 -0.0301 0.0282 0.1037 319 TYR B CZ 4834 O OH . TYR B 293 ? 0.6723 0.6265 0.7530 -0.0419 0.0373 0.1046 319 TYR B OH 4835 N N . PRO B 294 ? 0.4213 0.2894 0.4943 0.0455 -0.0246 0.0870 320 PRO B N 4836 C CA . PRO B 294 ? 0.4147 0.2913 0.4875 0.0631 -0.0337 0.0746 320 PRO B CA 4837 C C . PRO B 294 ? 0.3727 0.2822 0.4264 0.0691 -0.0338 0.0768 320 PRO B C 4838 O O . PRO B 294 ? 0.3963 0.3110 0.4339 0.0680 -0.0313 0.0944 320 PRO B O 4839 C CB . PRO B 294 ? 0.4844 0.3327 0.5579 0.0724 -0.0390 0.0828 320 PRO B CB 4840 C CG . PRO B 294 ? 0.4948 0.3248 0.5626 0.0588 -0.0319 0.1033 320 PRO B CG 4841 C CD . PRO B 294 ? 0.5025 0.3417 0.5783 0.0410 -0.0235 0.0998 320 PRO B CD 4842 N N . GLY B 295 ? 0.2936 0.2273 0.3499 0.0751 -0.0366 0.0583 321 GLY B N 4843 C CA . GLY B 295 ? 0.2759 0.2419 0.3207 0.0783 -0.0376 0.0572 321 GLY B CA 4844 C C . GLY B 295 ? 0.2637 0.2487 0.3007 0.0636 -0.0304 0.0533 321 GLY B C 4845 O O . GLY B 295 ? 0.1773 0.1870 0.2068 0.0639 -0.0318 0.0513 321 GLY B O 4846 N N . GLU B 296 ? 0.1821 0.1558 0.2228 0.0512 -0.0239 0.0510 322 GLU B N 4847 C CA . GLU B 296 ? 0.1588 0.1486 0.1941 0.0392 -0.0181 0.0456 322 GLU B CA 4848 C C . GLU B 296 ? 0.1498 0.1428 0.1952 0.0347 -0.0163 0.0303 322 GLU B C 4849 O O . GLU B 296 ? 0.1778 0.1574 0.2338 0.0385 -0.0183 0.0238 322 GLU B O 4850 C CB . GLU B 296 ? 0.1662 0.1474 0.1945 0.0294 -0.0116 0.0573 322 GLU B CB 4851 C CG . GLU B 296 ? 0.2101 0.1916 0.2237 0.0344 -0.0119 0.0750 322 GLU B CG 4852 C CD . GLU B 296 ? 0.3732 0.3523 0.3798 0.0247 -0.0030 0.0873 322 GLU B CD 4853 O OE1 . GLU B 296 ? 0.2942 0.2755 0.3082 0.0141 0.0025 0.0796 322 GLU B OE1 4854 O OE2 . GLU B 296 ? 0.4356 0.4133 0.4293 0.0287 -0.0014 0.1055 322 GLU B OE2 4855 N N . GLY B 297 ? 0.1345 0.1446 0.1764 0.0278 -0.0134 0.0242 323 GLY B N 4856 C CA . GLY B 297 ? 0.1293 0.1445 0.1771 0.0246 -0.0116 0.0127 323 GLY B CA 4857 C C . GLY B 297 ? 0.1267 0.1595 0.1706 0.0183 -0.0095 0.0100 323 GLY B C 4858 O O . GLY B 297 ? 0.0966 0.1317 0.1343 0.0130 -0.0087 0.0143 323 GLY B O 4859 N N . TYR B 298 ? 0.0920 0.1371 0.1397 0.0193 -0.0086 0.0031 324 TYR B N 4860 C CA . TYR B 298 ? 0.1320 0.1909 0.1790 0.0126 -0.0066 0.0029 324 TYR B CA 4861 C C . TYR B 298 ? 0.0847 0.1345 0.1268 0.0045 -0.0053 0.0042 324 TYR B C 4862 O O . TYR B 298 ? 0.1281 0.1825 0.1694 -0.0006 -0.0061 0.0055 324 TYR B O 4863 C CB . TYR B 298 ? 0.1046 0.1786 0.1551 0.0123 -0.0090 0.0054 324 TYR B CB 4864 C CG . TYR B 298 ? 0.0634 0.1535 0.1205 0.0059 -0.0067 0.0052 324 TYR B CG 4865 C CD1 . TYR B 298 ? 0.1169 0.2218 0.1788 0.0089 -0.0027 0.0040 324 TYR B CD1 4866 C CD2 . TYR B 298 ? 0.1521 0.2427 0.2115 -0.0029 -0.0085 0.0065 324 TYR B CD2 4867 C CE1 . TYR B 298 ? 0.2503 0.3709 0.3192 0.0015 0.0012 0.0081 324 TYR B CE1 4868 C CE2 . TYR B 298 ? 0.1423 0.2437 0.2113 -0.0106 -0.0065 0.0088 324 TYR B CE2 4869 C CZ . TYR B 298 ? 0.2591 0.3755 0.3327 -0.0092 -0.0009 0.0116 324 TYR B CZ 4870 O OH . TYR B 298 ? 0.2560 0.3835 0.3398 -0.0184 0.0026 0.0179 324 TYR B OH 4871 N N . ALA B 299 ? 0.1088 0.1469 0.1504 0.0038 -0.0042 0.0022 325 ALA B N 4872 C CA . ALA B 299 ? 0.0985 0.1309 0.1377 -0.0022 -0.0029 0.0029 325 ALA B CA 4873 C C . ALA B 299 ? 0.1166 0.1510 0.1557 -0.0048 -0.0028 -0.0011 325 ALA B C 4874 O O . ALA B 299 ? 0.0963 0.1289 0.1346 -0.0082 -0.0025 -0.0018 325 ALA B O 4875 C CB . ALA B 299 ? 0.0936 0.1144 0.1360 -0.0031 -0.0014 0.0047 325 ALA B CB 4876 N N . LEU B 300 ? 0.0630 0.1026 0.1021 -0.0015 -0.0031 -0.0040 326 LEU B N 4877 C CA . LEU B 300 ? 0.1000 0.1416 0.1366 -0.0016 -0.0038 -0.0064 326 LEU B CA 4878 C C . LEU B 300 ? 0.1641 0.2121 0.1979 -0.0037 -0.0030 0.0000 326 LEU B C 4879 O O . LEU B 300 ? 0.1292 0.1796 0.1660 -0.0070 -0.0025 0.0040 326 LEU B O 4880 C CB . LEU B 300 ? 0.0731 0.1182 0.1094 0.0046 -0.0053 -0.0140 326 LEU B CB 4881 C CG . LEU B 300 ? 0.1449 0.1800 0.1898 0.0038 -0.0074 -0.0211 326 LEU B CG 4882 C CD1 . LEU B 300 ? 0.1322 0.1692 0.1800 0.0108 -0.0111 -0.0324 326 LEU B CD1 4883 C CD2 . LEU B 300 ? 0.0813 0.1145 0.1301 -0.0007 -0.0084 -0.0230 326 LEU B CD2 4884 N N . LEU B 301 ? 0.1220 0.1726 0.1510 -0.0021 -0.0035 0.0019 327 LEU B N 4885 C CA . LEU B 301 ? 0.0927 0.1459 0.1212 -0.0058 -0.0022 0.0117 327 LEU B CA 4886 C C . LEU B 301 ? 0.0894 0.1595 0.1151 -0.0037 0.0025 0.0177 327 LEU B C 4887 O O . LEU B 301 ? 0.1193 0.1940 0.1482 -0.0091 0.0054 0.0285 327 LEU B O 4888 C CB . LEU B 301 ? 0.1011 0.1464 0.1255 -0.0047 -0.0055 0.0145 327 LEU B CB 4889 C CG . LEU B 301 ? 0.0876 0.1202 0.1172 -0.0066 -0.0094 0.0089 327 LEU B CG 4890 C CD1 . LEU B 301 ? 0.1471 0.1726 0.1742 -0.0029 -0.0138 0.0108 327 LEU B CD1 4891 C CD2 . LEU B 301 ? 0.1161 0.1439 0.1530 -0.0131 -0.0098 0.0103 327 LEU B CD2 4892 N N . PHE B 302 ? 0.0814 0.1618 0.1030 0.0041 0.0036 0.0104 328 PHE B N 4893 C CA . PHE B 302 ? 0.0851 0.1872 0.1028 0.0090 0.0089 0.0134 328 PHE B CA 4894 C C . PHE B 302 ? 0.1069 0.2160 0.1311 0.0140 0.0092 0.0044 328 PHE B C 4895 O O . PHE B 302 ? 0.1053 0.2025 0.1312 0.0181 0.0046 -0.0062 328 PHE B O 4896 C CB . PHE B 302 ? 0.1324 0.2446 0.1358 0.0183 0.0084 0.0105 328 PHE B CB 4897 C CG . PHE B 302 ? 0.1444 0.2501 0.1402 0.0160 0.0071 0.0212 328 PHE B CG 4898 C CD1 . PHE B 302 ? 0.1788 0.2949 0.1695 0.0132 0.0130 0.0385 328 PHE B CD1 4899 C CD2 . PHE B 302 ? 0.1332 0.2224 0.1288 0.0166 0.0000 0.0152 328 PHE B CD2 4900 C CE1 . PHE B 302 ? 0.2637 0.3694 0.2476 0.0121 0.0106 0.0506 328 PHE B CE1 4901 C CE2 . PHE B 302 ? 0.1544 0.2367 0.1439 0.0167 -0.0027 0.0245 328 PHE B CE2 4902 C CZ . PHE B 302 ? 0.2120 0.3002 0.1948 0.0150 0.0020 0.0427 328 PHE B CZ 4903 N N . ASP B 303 ? 0.1389 0.2671 0.1689 0.0137 0.0143 0.0091 329 ASP B N 4904 C CA . ASP B 303 ? 0.0957 0.2301 0.1335 0.0201 0.0132 0.0007 329 ASP B CA 4905 C C . ASP B 303 ? 0.1535 0.3021 0.1857 0.0343 0.0138 -0.0111 329 ASP B C 4906 O O . ASP B 303 ? 0.1228 0.2767 0.1432 0.0392 0.0142 -0.0142 329 ASP B O 4907 C CB . ASP B 303 ? 0.1675 0.3194 0.2184 0.0148 0.0168 0.0079 329 ASP B CB 4908 C CG . ASP B 303 ? 0.3401 0.5236 0.3927 0.0148 0.0259 0.0153 329 ASP B CG 4909 O OD1 . ASP B 303 ? 0.2446 0.4412 0.2851 0.0231 0.0298 0.0133 329 ASP B OD1 4910 O OD2 . ASP B 303 ? 0.3175 0.5140 0.3840 0.0062 0.0289 0.0230 329 ASP B OD2 4911 N N . ASP B 304 ? 0.1157 0.2721 0.1562 0.0426 0.0127 -0.0188 330 ASP B N 4912 C CA . ASP B 304 ? 0.1730 0.3413 0.2109 0.0585 0.0114 -0.0342 330 ASP B CA 4913 C C . ASP B 304 ? 0.2657 0.4615 0.2912 0.0629 0.0177 -0.0330 330 ASP B C 4914 O O . ASP B 304 ? 0.2632 0.4625 0.2795 0.0739 0.0139 -0.0461 330 ASP B O 4915 C CB . ASP B 304 ? 0.1805 0.3508 0.2298 0.0664 0.0086 -0.0402 330 ASP B CB 4916 C CG . ASP B 304 ? 0.2919 0.4307 0.3487 0.0672 0.0002 -0.0435 330 ASP B CG 4917 O OD1 . ASP B 304 ? 0.2445 0.3584 0.2973 0.0600 -0.0031 -0.0424 330 ASP B OD1 4918 O OD2 . ASP B 304 ? 0.2868 0.4253 0.3532 0.0746 -0.0032 -0.0456 330 ASP B OD2 4919 N N . ASN B 305 ? 0.1647 0.3767 0.1901 0.0531 0.0257 -0.0163 331 ASN B N 4920 C CA . ASN B 305 ? 0.1784 0.4138 0.1915 0.0552 0.0317 -0.0097 331 ASN B CA 4921 C C . ASN B 305 ? 0.2096 0.4424 0.2110 0.0488 0.0346 0.0038 331 ASN B C 4922 O O . ASN B 305 ? 0.2208 0.4705 0.2140 0.0477 0.0402 0.0158 331 ASN B O 4923 C CB . ASN B 305 ? 0.2635 0.5192 0.2874 0.0490 0.0386 0.0008 331 ASN B CB 4924 C CG . ASN B 305 ? 0.3449 0.6057 0.3794 0.0572 0.0354 -0.0120 331 ASN B CG 4925 O OD1 . ASN B 305 ? 0.4126 0.6735 0.4628 0.0506 0.0357 -0.0080 331 ASN B OD1 4926 N ND2 . ASN B 305 ? 0.3274 0.5916 0.3540 0.0724 0.0307 -0.0285 331 ASN B ND2 4927 N N . TYR B 306 ? 0.1618 0.3735 0.1631 0.0453 0.0305 0.0021 332 TYR B N 4928 C CA . TYR B 306 ? 0.2346 0.4337 0.2248 0.0392 0.0295 0.0137 332 TYR B CA 4929 C C . TYR B 306 ? 0.2472 0.4456 0.2446 0.0241 0.0359 0.0365 332 TYR B C 4930 O O . TYR B 306 ? 0.2413 0.4338 0.2292 0.0205 0.0367 0.0502 332 TYR B O 4931 C CB . TYR B 306 ? 0.2017 0.4180 0.1709 0.0517 0.0294 0.0104 332 TYR B CB 4932 C CG . TYR B 306 ? 0.2557 0.4656 0.2202 0.0646 0.0195 -0.0143 332 TYR B CG 4933 C CD1 . TYR B 306 ? 0.2744 0.4628 0.2358 0.0638 0.0104 -0.0206 332 TYR B CD1 4934 C CD2 . TYR B 306 ? 0.2585 0.4768 0.2273 0.0747 0.0158 -0.0310 332 TYR B CD2 4935 C CE1 . TYR B 306 ? 0.1462 0.3281 0.1090 0.0730 0.0004 -0.0440 332 TYR B CE1 4936 C CE2 . TYR B 306 ? 0.2579 0.4654 0.2277 0.0839 0.0048 -0.0533 332 TYR B CE2 4937 C CZ . TYR B 306 ? 0.2386 0.4291 0.2067 0.0826 -0.0023 -0.0600 332 TYR B CZ 4938 O OH . TYR B 306 ? 0.1964 0.3752 0.1719 0.0887 -0.0142 -0.0815 332 TYR B OH 4939 N N . VAL B 307 ? 0.2113 0.4147 0.2273 0.0158 0.0390 0.0399 333 VAL B N 4940 C CA . VAL B 307 ? 0.1901 0.3850 0.2196 -0.0005 0.0411 0.0566 333 VAL B CA 4941 C C . VAL B 307 ? 0.1638 0.3253 0.1988 -0.0075 0.0320 0.0531 333 VAL B C 4942 O O . VAL B 307 ? 0.1394 0.2899 0.1781 -0.0043 0.0259 0.0393 333 VAL B O 4943 C CB . VAL B 307 ? 0.2330 0.4404 0.2803 -0.0059 0.0435 0.0561 333 VAL B CB 4944 C CG1 . VAL B 307 ? 0.2599 0.4559 0.3234 -0.0228 0.0440 0.0696 333 VAL B CG1 4945 C CG2 . VAL B 307 ? 0.1738 0.4089 0.2143 0.0032 0.0498 0.0552 333 VAL B CG2 4946 N N . PRO B 308 ? 0.1545 0.2982 0.1891 -0.0159 0.0304 0.0653 334 PRO B N 4947 C CA . PRO B 308 ? 0.1358 0.2488 0.1745 -0.0201 0.0211 0.0592 334 PRO B CA 4948 C C . PRO B 308 ? 0.1108 0.2199 0.1676 -0.0280 0.0177 0.0533 334 PRO B C 4949 O O . PRO B 308 ? 0.1192 0.2434 0.1914 -0.0362 0.0219 0.0603 334 PRO B O 4950 C CB . PRO B 308 ? 0.2427 0.3408 0.2806 -0.0265 0.0205 0.0749 334 PRO B CB 4951 C CG . PRO B 308 ? 0.2830 0.4022 0.3077 -0.0220 0.0290 0.0893 334 PRO B CG 4952 C CD . PRO B 308 ? 0.1715 0.3226 0.2004 -0.0197 0.0371 0.0857 334 PRO B CD 4953 N N . HIS B 309 ? 0.1251 0.2183 0.1806 -0.0252 0.0107 0.0407 335 HIS B N 4954 C CA . HIS B 309 ? 0.0928 0.1800 0.1611 -0.0312 0.0055 0.0350 335 HIS B CA 4955 C C . HIS B 309 ? 0.1508 0.2245 0.2305 -0.0419 0.0021 0.0411 335 HIS B C 4956 O O . HIS B 309 ? 0.1603 0.2219 0.2348 -0.0426 0.0025 0.0491 335 HIS B O 4957 C CB . HIS B 309 ? 0.0855 0.1587 0.1460 -0.0255 0.0000 0.0235 335 HIS B CB 4958 C CG . HIS B 309 ? 0.1895 0.2687 0.2427 -0.0162 0.0014 0.0174 335 HIS B CG 4959 N ND1 . HIS B 309 ? 0.1888 0.2595 0.2389 -0.0127 -0.0019 0.0109 335 HIS B ND1 4960 C CD2 . HIS B 309 ? 0.2159 0.3078 0.2652 -0.0093 0.0055 0.0168 335 HIS B CD2 4961 C CE1 . HIS B 309 ? 0.2142 0.2881 0.2611 -0.0052 -0.0006 0.0076 335 HIS B CE1 4962 N NE2 . HIS B 309 ? 0.1909 0.2776 0.2374 -0.0022 0.0032 0.0089 335 HIS B NE2 4963 N N . PRO B 310 ? 0.1594 0.2336 0.2549 -0.0490 -0.0029 0.0360 336 PRO B N 4964 C CA . PRO B 310 ? 0.1284 0.1840 0.2365 -0.0578 -0.0095 0.0362 336 PRO B CA 4965 C C . PRO B 310 ? 0.1491 0.1818 0.2449 -0.0513 -0.0150 0.0292 336 PRO B C 4966 O O . PRO B 310 ? 0.1902 0.2038 0.2919 -0.0549 -0.0191 0.0325 336 PRO B O 4967 C CB . PRO B 310 ? 0.1462 0.2101 0.2693 -0.0621 -0.0160 0.0248 336 PRO B CB 4968 C CG . PRO B 310 ? 0.1391 0.2305 0.2642 -0.0596 -0.0097 0.0268 336 PRO B CG 4969 C CD . PRO B 310 ? 0.0952 0.1885 0.1997 -0.0484 -0.0042 0.0291 336 PRO B CD 4970 N N . ALA B 311 ? 0.0904 0.1253 0.1714 -0.0417 -0.0149 0.0202 337 ALA B N 4971 C CA . ALA B 311 ? 0.1486 0.1688 0.2193 -0.0350 -0.0180 0.0137 337 ALA B CA 4972 C C . ALA B 311 ? 0.1715 0.1821 0.2363 -0.0324 -0.0166 0.0226 337 ALA B C 4973 O O . ALA B 311 ? 0.1512 0.1487 0.2133 -0.0278 -0.0210 0.0179 337 ALA B O 4974 C CB . ALA B 311 ? 0.0786 0.1062 0.1374 -0.0275 -0.0158 0.0068 337 ALA B CB 4975 N N . PHE B 312 ? 0.1496 0.1699 0.2113 -0.0335 -0.0105 0.0348 338 PHE B N 4976 C CA . PHE B 312 ? 0.1508 0.1652 0.2038 -0.0296 -0.0096 0.0453 338 PHE B CA 4977 C C . PHE B 312 ? 0.1353 0.1293 0.1992 -0.0355 -0.0143 0.0541 338 PHE B C 4978 O O . PHE B 312 ? 0.1458 0.1241 0.2053 -0.0295 -0.0196 0.0542 338 PHE B O 4979 C CB . PHE B 312 ? 0.1176 0.1518 0.1627 -0.0283 -0.0013 0.0566 338 PHE B CB 4980 C CG . PHE B 312 ? 0.1602 0.1920 0.1936 -0.0235 -0.0003 0.0702 338 PHE B CG 4981 C CD1 . PHE B 312 ? 0.1798 0.2159 0.1970 -0.0116 -0.0024 0.0642 338 PHE B CD1 4982 C CD2 . PHE B 312 ? 0.2184 0.2447 0.2578 -0.0310 0.0023 0.0897 338 PHE B CD2 4983 C CE1 . PHE B 312 ? 0.1916 0.2283 0.1953 -0.0049 -0.0029 0.0766 338 PHE B CE1 4984 C CE2 . PHE B 312 ? 0.1908 0.2150 0.2162 -0.0251 0.0032 0.1057 338 PHE B CE2 4985 C CZ . PHE B 312 ? 0.2514 0.2819 0.2572 -0.0109 0.0001 0.0986 338 PHE B CZ 4986 N N . ASN B 313 ? 0.1433 0.1374 0.2238 -0.0472 -0.0132 0.0612 339 ASN B N 4987 C CA . ASN B 313 ? 0.2568 0.2267 0.3532 -0.0548 -0.0192 0.0684 339 ASN B CA 4988 C C . ASN B 313 ? 0.2287 0.1776 0.3293 -0.0495 -0.0304 0.0506 339 ASN B C 4989 O O . ASN B 313 ? 0.1894 0.1147 0.2932 -0.0465 -0.0369 0.0540 339 ASN B O 4990 C CB . ASN B 313 ? 0.2129 0.1897 0.3292 -0.0680 -0.0170 0.0718 339 ASN B CB 4991 C CG . ASN B 313 ? 0.3815 0.3731 0.4952 -0.0723 -0.0061 0.0916 339 ASN B CG 4992 O OD1 . ASN B 313 ? 0.4028 0.3963 0.5008 -0.0665 -0.0014 0.1058 339 ASN B OD1 4993 N ND2 . ASN B 313 ? 0.5149 0.5194 0.6432 -0.0814 -0.0023 0.0916 339 ASN B ND2 4994 N N . ALA B 314 ? 0.1908 0.1497 0.2906 -0.0469 -0.0327 0.0319 340 ALA B N 4995 C CA . ALA B 314 ? 0.2615 0.2082 0.3634 -0.0405 -0.0418 0.0133 340 ALA B CA 4996 C C . ALA B 314 ? 0.1934 0.1355 0.2813 -0.0277 -0.0425 0.0099 340 ALA B C 4997 O O . ALA B 314 ? 0.1819 0.1084 0.2742 -0.0214 -0.0504 0.0003 340 ALA B O 4998 C CB . ALA B 314 ? 0.1990 0.1631 0.2988 -0.0394 -0.0422 -0.0025 340 ALA B CB 4999 N N . THR B 315 ? 0.1388 0.0960 0.2119 -0.0233 -0.0353 0.0159 341 THR B N 5000 C CA . THR B 315 ? 0.2091 0.1663 0.2722 -0.0121 -0.0365 0.0119 341 THR B CA 5001 C C . THR B 315 ? 0.1599 0.0989 0.2238 -0.0079 -0.0416 0.0232 341 THR B C 5002 O O . THR B 315 ? 0.1685 0.0979 0.2339 0.0016 -0.0484 0.0153 341 THR B O 5003 C CB . THR B 315 ? 0.1817 0.1586 0.2322 -0.0092 -0.0294 0.0137 341 THR B CB 5004 O OG1 . THR B 315 ? 0.1590 0.1487 0.2095 -0.0123 -0.0254 0.0053 341 THR B OG1 5005 C CG2 . THR B 315 ? 0.1759 0.1560 0.2210 0.0013 -0.0320 0.0072 341 THR B CG2 5006 N N . ILE B 316 ? 0.1720 0.1082 0.2348 -0.0139 -0.0380 0.0426 342 ILE B N 5007 C CA . ILE B 316 ? 0.2569 0.1740 0.3192 -0.0106 -0.0424 0.0589 342 ILE B CA 5008 C C . ILE B 316 ? 0.2802 0.1673 0.3602 -0.0113 -0.0528 0.0540 342 ILE B C 5009 O O . ILE B 316 ? 0.2715 0.1409 0.3513 -0.0008 -0.0608 0.0550 342 ILE B O 5010 C CB . ILE B 316 ? 0.3263 0.2480 0.3865 -0.0198 -0.0345 0.0835 342 ILE B CB 5011 C CG1 . ILE B 316 ? 0.2762 0.2275 0.3171 -0.0151 -0.0257 0.0865 342 ILE B CG1 5012 C CG2 . ILE B 316 ? 0.3178 0.2154 0.3788 -0.0180 -0.0388 0.1051 342 ILE B CG2 5013 C CD1 . ILE B 316 ? 0.3121 0.2668 0.3349 -0.0007 -0.0290 0.0900 342 ILE B CD1 5014 N N . GLN B 317 ? 0.2221 0.1037 0.3190 -0.0226 -0.0541 0.0473 343 GLN B N 5015 C CA . GLN B 317 ? 0.2675 0.1270 0.3800 -0.0227 -0.0633 0.0376 343 GLN B CA 5016 C C . GLN B 317 ? 0.2607 0.1170 0.3718 -0.0082 -0.0716 0.0147 343 GLN B C 5017 O O . GLN B 317 ? 0.2813 0.1215 0.3972 -0.0006 -0.0790 0.0101 343 GLN B O 5018 C CB . GLN B 317 ? 0.2915 0.1568 0.4190 -0.0352 -0.0626 0.0298 343 GLN B CB 5019 C CG . GLN B 317 ? 0.5372 0.4071 0.6708 -0.0491 -0.0545 0.0506 343 GLN B CG 5020 C CD . GLN B 317 ? 0.7669 0.6149 0.9043 -0.0503 -0.0555 0.0683 343 GLN B CD 5021 O OE1 . GLN B 317 ? 0.7639 0.6162 0.8911 -0.0520 -0.0475 0.0907 343 GLN B OE1 5022 N NE2 . GLN B 317 ? 0.8213 0.6470 0.9723 -0.0486 -0.0653 0.0582 343 GLN B NE2 5023 N N . ALA B 318 ? 0.2359 0.1134 0.3386 -0.0040 -0.0683 0.0005 344 ALA B N 5024 C CA . ALA B 318 ? 0.2382 0.1217 0.3388 0.0097 -0.0729 -0.0212 344 ALA B CA 5025 C C . ALA B 318 ? 0.3193 0.2013 0.4126 0.0231 -0.0751 -0.0169 344 ALA B C 5026 O O . ALA B 318 ? 0.2458 0.1216 0.3441 0.0350 -0.0826 -0.0297 344 ALA B O 5027 C CB . ALA B 318 ? 0.2775 0.1915 0.3683 0.0092 -0.0648 -0.0332 344 ALA B CB 5028 N N . LEU B 319 ? 0.2388 0.1318 0.3194 0.0221 -0.0686 -0.0006 345 LEU B N 5029 C CA . LEU B 319 ? 0.2409 0.1338 0.3146 0.0355 -0.0728 0.0040 345 LEU B CA 5030 C C . LEU B 319 ? 0.2741 0.1352 0.3550 0.0412 -0.0830 0.0142 345 LEU B C 5031 O O . LEU B 319 ? 0.2694 0.1301 0.3493 0.0544 -0.0886 0.0078 345 LEU B O 5032 C CB . LEU B 319 ? 0.2056 0.1167 0.2634 0.0336 -0.0653 0.0189 345 LEU B CB 5033 C CG . LEU B 319 ? 0.1831 0.1241 0.2352 0.0310 -0.0570 0.0073 345 LEU B CG 5034 C CD1 . LEU B 319 ? 0.1913 0.1469 0.2296 0.0280 -0.0507 0.0198 345 LEU B CD1 5035 C CD2 . LEU B 319 ? 0.2218 0.1774 0.2774 0.0426 -0.0605 -0.0096 345 LEU B CD2 5036 N N . LEU B 320 ? 0.2711 0.1148 0.3572 0.0285 -0.0811 0.0291 346 LEU B N 5037 C CA . LEU B 320 ? 0.3709 0.1905 0.4606 0.0302 -0.0855 0.0408 346 LEU B CA 5038 C C . LEU B 320 ? 0.5257 0.3307 0.6307 0.0339 -0.0942 0.0214 346 LEU B C 5039 O O . LEU B 320 ? 0.5872 0.3730 0.6952 0.0414 -0.1005 0.0254 346 LEU B O 5040 C CB . LEU B 320 ? 0.3616 0.1718 0.4533 0.0144 -0.0787 0.0642 346 LEU B CB 5041 C CG . LEU B 320 ? 0.3695 0.1949 0.4429 0.0125 -0.0696 0.0874 346 LEU B CG 5042 C CD1 . LEU B 320 ? 0.4175 0.2385 0.4953 -0.0036 -0.0612 0.1079 346 LEU B CD1 5043 C CD2 . LEU B 320 ? 0.3720 0.1960 0.4283 0.0292 -0.0733 0.0971 346 LEU B CD2 # 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 PRO 1 27 ? ? ? A . n A 1 2 THR 2 28 ? ? ? A . n A 1 3 SER 3 29 ? ? ? A . n A 1 4 PRO 4 30 30 PRO PRO A . n A 1 5 PHE 5 31 31 PHE PHE A . n A 1 6 GLU 6 32 32 GLU GLU A . n A 1 7 THR 7 33 33 THR THR A . n A 1 8 LEU 8 34 34 LEU LEU A . n A 1 9 ARG 9 35 35 ARG ARG A . n A 1 10 ALA 10 36 36 ALA ALA A . n A 1 11 ALA 11 37 37 ALA ALA A . n A 1 12 ALA 12 38 38 ALA ALA A . n A 1 13 ALA 13 39 39 ALA ALA A . n A 1 14 PRO 14 40 40 PRO PRO A . n A 1 15 ARG 15 41 41 ARG ARG A . n A 1 16 TYR 16 42 42 TYR TYR A . n A 1 17 PHE 17 43 43 PHE PHE A . n A 1 18 GLY 18 44 44 GLY GLY A . n A 1 19 ALA 19 45 45 ALA ALA A . n A 1 20 ALA 20 46 46 ALA ALA A . n A 1 21 LEU 21 47 47 LEU LEU A . n A 1 22 GLY 22 48 48 GLY GLY A . n A 1 23 VAL 23 49 49 VAL VAL A . n A 1 24 PRO 24 50 50 PRO PRO A . n A 1 25 HIS 25 51 51 HIS HIS A . n A 1 26 LEU 26 52 52 LEU LEU A . n A 1 27 LEU 27 53 53 LEU LEU A . n A 1 28 ASN 28 54 54 ASN ASN A . n A 1 29 PHE 29 55 55 PHE PHE A . n A 1 30 THR 30 56 56 THR THR A . n A 1 31 HIS 31 57 57 HIS HIS A . n A 1 32 ASP 32 58 58 ASP ASP A . n A 1 33 PRO 33 59 59 PRO PRO A . n A 1 34 LEU 34 60 60 LEU LEU A . n A 1 35 PHE 35 61 61 PHE PHE A . n A 1 36 ASP 36 62 62 ASP ASP A . n A 1 37 VAL 37 63 63 VAL VAL A . n A 1 38 THR 38 64 64 THR THR A . n A 1 39 ALA 39 65 65 ALA ALA A . n A 1 40 VAL 40 66 66 VAL VAL A . n A 1 41 LEU 41 67 67 LEU LEU A . n A 1 42 GLN 42 68 68 GLN GLN A . n A 1 43 PHE 43 69 69 PHE PHE A . n A 1 44 ASN 44 70 70 ASN ASN A . n A 1 45 GLY 45 71 71 GLY GLY A . n A 1 46 ALA 46 72 72 ALA ALA A . n A 1 47 THR 47 73 73 THR THR A . n A 1 48 PRO 48 74 74 PRO PRO A . n A 1 49 GLU 49 75 75 GLU GLU A . n A 1 50 ASN 50 76 76 ASN ASN A . n A 1 51 GLU 51 77 77 GLU GLU A . n A 1 52 MET 52 78 78 MET MET A . n A 1 53 LYS 53 79 79 LYS LYS A . n A 1 54 TRP 54 80 80 TRP TRP A . n A 1 55 ALA 55 81 81 ALA ALA A . n A 1 56 TYR 56 82 82 TYR TYR A . n A 1 57 ILE 57 83 83 ILE ILE A . n A 1 58 GLU 58 84 84 GLU GLU A . n A 1 59 PRO 59 85 85 PRO PRO A . n A 1 60 GLU 60 86 86 GLU GLU A . n A 1 61 ARG 61 87 87 ARG ARG A . n A 1 62 ASN 62 88 88 ASN ASN A . n A 1 63 GLN 63 89 89 GLN GLN A . n A 1 64 PHE 64 90 90 PHE PHE A . n A 1 65 ASN 65 91 91 ASN ASN A . n A 1 66 PHE 66 92 92 PHE PHE A . n A 1 67 THR 67 93 93 THR THR A . n A 1 68 GLY 68 94 94 GLY GLY A . n A 1 69 GLY 69 95 95 GLY GLY A . n A 1 70 ASP 70 96 96 ASP ASP A . n A 1 71 ILE 71 97 97 ILE ILE A . n A 1 72 VAL 72 98 98 VAL VAL A . n A 1 73 ALA 73 99 99 ALA ALA A . n A 1 74 ALA 74 100 100 ALA ALA A . n A 1 75 PHE 75 101 101 PHE PHE A . n A 1 76 SER 76 102 102 SER SER A . n A 1 77 ALA 77 103 103 ALA ALA A . n A 1 78 ALA 78 104 104 ALA ALA A . n A 1 79 ASN 79 105 105 ASN ASN A . n A 1 80 ASP 80 106 106 ASP ASP A . n A 1 81 TYR 81 107 107 TYR TYR A . n A 1 82 VAL 82 108 108 VAL VAL A . n A 1 83 LEU 83 109 109 LEU LEU A . n A 1 84 ARG 84 110 110 ARG ARG A . n A 1 85 GLY 85 111 111 GLY GLY A . n A 1 86 HIS 86 112 112 HIS HIS A . n A 1 87 ASN 87 113 113 ASN ASN A . n A 1 88 LEU 88 114 114 LEU LEU A . n A 1 89 VAL 89 115 115 VAL VAL A . n A 1 90 TRP 90 116 116 TRP TRP A . n A 1 91 TYR 91 117 117 TYR TYR A . n A 1 92 GLN 92 118 118 GLN GLN A . n A 1 93 GLU 93 119 119 GLU GLU A . n A 1 94 LEU 94 120 120 LEU LEU A . n A 1 95 ALA 95 121 121 ALA ALA A . n A 1 96 PRO 96 122 122 PRO PRO A . n A 1 97 TRP 97 123 123 TRP TRP A . n A 1 98 VAL 98 124 124 VAL VAL A . n A 1 99 GLU 99 125 125 GLU GLU A . n A 1 100 THR 100 126 126 THR THR A . n A 1 101 LEU 101 127 127 LEU LEU A . n A 1 102 THR 102 128 128 THR THR A . n A 1 103 GLY 103 129 129 GLY GLY A . n A 1 104 GLU 104 130 130 GLU GLU A . n A 1 105 ASP 105 131 131 ASP ASP A . n A 1 106 LEU 106 132 132 LEU LEU A . n A 1 107 TRP 107 133 133 TRP TRP A . n A 1 108 ASN 108 134 134 ASN ASN A . n A 1 109 ALA 109 135 135 ALA ALA A . n A 1 110 THR 110 136 136 THR THR A . n A 1 111 VAL 111 137 137 VAL VAL A . n A 1 112 ASN 112 138 138 ASN ASN A . n A 1 113 HIS 113 139 139 HIS HIS A . n A 1 114 ILE 114 140 140 ILE ILE A . n A 1 115 THR 115 141 141 THR THR A . n A 1 116 THR 116 142 142 THR THR A . n A 1 117 VAL 117 143 143 VAL VAL A . n A 1 118 MET 118 144 144 MET MET A . n A 1 119 THR 119 145 145 THR THR A . n A 1 120 HIS 120 146 146 HIS HIS A . n A 1 121 TYR 121 147 147 TYR TYR A . n A 1 122 LYS 122 148 148 LYS LYS A . n A 1 123 GLU 123 149 149 GLU GLU A . n A 1 124 SER 124 150 150 SER SER A . n A 1 125 PHE 125 151 151 PHE PHE A . n A 1 126 ASN 126 152 152 ASN ASN A . n A 1 127 ILE 127 153 153 ILE ILE A . n A 1 128 TYR 128 154 154 TYR TYR A . n A 1 129 ALA 129 155 155 ALA ALA A . n A 1 130 TRP 130 156 156 TRP TRP A . n A 1 131 ASP 131 157 157 ASP ASP A . n A 1 132 VAL 132 158 158 VAL VAL A . n A 1 133 VAL 133 159 159 VAL VAL A . n A 1 134 ASN 134 160 160 ASN ASN A . n A 1 135 GLU 135 161 161 GLU GLU A . n A 1 136 ALA 136 162 162 ALA ALA A . n A 1 137 PHE 137 163 163 PHE PHE A . n A 1 138 ASN 138 164 164 ASN ASN A . n A 1 139 ASP 139 165 165 ASP ASP A . n A 1 140 ASN 140 166 166 ASN ASN A . n A 1 141 GLY 141 167 167 GLY GLY A . n A 1 142 THR 142 168 168 THR THR A . n A 1 143 TYR 143 169 169 TYR TYR A . n A 1 144 ARG 144 170 170 ARG ARG A . n A 1 145 GLU 145 171 171 GLU GLU A . n A 1 146 ASN 146 172 172 ASN ASN A . n A 1 147 VAL 147 173 173 VAL VAL A . n A 1 148 TRP 148 174 174 TRP TRP A . n A 1 149 TYR 149 175 175 TYR TYR A . n A 1 150 THR 150 176 176 THR THR A . n A 1 151 GLN 151 177 177 GLN GLN A . n A 1 152 LEU 152 178 178 LEU LEU A . n A 1 153 GLY 153 179 179 GLY GLY A . n A 1 154 PRO 154 180 180 PRO PRO A . n A 1 155 ASP 155 181 181 ASP ASP A . n A 1 156 TYR 156 182 182 TYR TYR A . n A 1 157 ILE 157 183 183 ILE ILE A . n A 1 158 PRO 158 184 184 PRO PRO A . n A 1 159 ASN 159 185 185 ASN ASN A . n A 1 160 ALA 160 186 186 ALA ALA A . n A 1 161 TYR 161 187 187 TYR TYR A . n A 1 162 ALA 162 188 188 ALA ALA A . n A 1 163 VAL 163 189 189 VAL VAL A . n A 1 164 ALA 164 190 190 ALA ALA A . n A 1 165 ARG 165 191 191 ARG ARG A . n A 1 166 SER 166 192 192 SER SER A . n A 1 167 VAL 167 193 193 VAL VAL A . n A 1 168 ASN 168 194 194 ASN ASN A . n A 1 169 THR 169 195 195 THR THR A . n A 1 170 PRO 170 196 196 PRO PRO A . n A 1 171 SER 171 197 197 SER SER A . n A 1 172 LYS 172 198 198 LYS LYS A . n A 1 173 LEU 173 199 199 LEU LEU A . n A 1 174 TYR 174 200 200 TYR TYR A . n A 1 175 ILE 175 201 201 ILE ILE A . n A 1 176 ASN 176 202 202 ASN ASN A . n A 1 177 ASP 177 203 203 ASP ASP A . n A 1 178 TYR 178 204 204 TYR TYR A . n A 1 179 ASN 179 205 205 ASN ASN A . n A 1 180 THR 180 206 206 THR THR A . n A 1 181 GLU 181 207 207 GLU GLU A . n A 1 182 GLY 182 208 208 GLY GLY A . n A 1 183 ILE 183 209 209 ILE ILE A . n A 1 184 ASN 184 210 210 ASN ASN A . n A 1 185 ASN 185 211 211 ASN ASN A . n A 1 186 LYS 186 212 212 LYS LYS A . n A 1 187 SER 187 213 213 SER SER A . n A 1 188 ASP 188 214 214 ASP ASP A . n A 1 189 ALA 189 215 215 ALA ALA A . n A 1 190 LEU 190 216 216 LEU LEU A . n A 1 191 LEU 191 217 217 LEU LEU A . n A 1 192 ALA 192 218 218 ALA ALA A . n A 1 193 VAL 193 219 219 VAL VAL A . n A 1 194 VAL 194 220 220 VAL VAL A . n A 1 195 GLN 195 221 221 GLN GLN A . n A 1 196 SER 196 222 222 SER SER A . n A 1 197 MET 197 223 223 MET MET A . n A 1 198 LYS 198 224 224 LYS LYS A . n A 1 199 ALA 199 225 225 ALA ALA A . n A 1 200 HIS 200 226 226 HIS HIS A . n A 1 201 ASN 201 227 227 ASN ASN A . n A 1 202 LEU 202 228 228 LEU LEU A . n A 1 203 VAL 203 229 229 VAL VAL A . n A 1 204 ASP 204 230 230 ASP ASP A . n A 1 205 GLY 205 231 231 GLY GLY A . n A 1 206 VAL 206 232 232 VAL VAL A . n A 1 207 GLY 207 233 233 GLY GLY A . n A 1 208 PHE 208 234 234 PHE PHE A . n A 1 209 GLN 209 235 235 GLN GLN A . n A 1 210 CYS 210 236 236 CYS CYS A . n A 1 211 HIS 211 237 237 HIS HIS A . n A 1 212 PHE 212 238 238 PHE PHE A . n A 1 213 PHE 213 239 239 PHE PHE A . n A 1 214 VAL 214 240 240 VAL VAL A . n A 1 215 GLY 215 241 241 GLY GLY A . n A 1 216 GLU 216 242 242 GLU GLU A . n A 1 217 LEU 217 243 243 LEU LEU A . n A 1 218 PRO 218 244 244 PRO PRO A . n A 1 219 PRO 219 245 245 PRO PRO A . n A 1 220 ASP 220 246 246 ASP ASP A . n A 1 221 LEU 221 247 247 LEU LEU A . n A 1 222 GLU 222 248 248 GLU GLU A . n A 1 223 GLN 223 249 249 GLN GLN A . n A 1 224 ASN 224 250 250 ASN ASN A . n A 1 225 PHE 225 251 251 PHE PHE A . n A 1 226 ALA 226 252 252 ALA ALA A . n A 1 227 ARG 227 253 253 ARG ARG A . n A 1 228 PHE 228 254 254 PHE PHE A . n A 1 229 VAL 229 255 255 VAL VAL A . n A 1 230 ALA 230 256 256 ALA ALA A . n A 1 231 ALA 231 257 257 ALA ALA A . n A 1 232 GLY 232 258 258 GLY GLY A . n A 1 233 VAL 233 259 259 VAL VAL A . n A 1 234 GLU 234 260 260 GLU GLU A . n A 1 235 ILE 235 261 261 ILE ILE A . n A 1 236 ALA 236 262 262 ALA ALA A . n A 1 237 VAL 237 263 263 VAL VAL A . n A 1 238 THR 238 264 264 THR THR A . n A 1 239 GLU 239 265 265 GLU GLU A . n A 1 240 LEU 240 266 266 LEU LEU A . n A 1 241 ASP 241 267 267 ASP ASP A . n A 1 242 ILE 242 268 268 ILE ILE A . n A 1 243 ARG 243 269 269 ARG ARG A . n A 1 244 MET 244 270 270 MET MET A . n A 1 245 ASN 245 271 271 ASN ASN A . n A 1 246 LEU 246 272 272 LEU LEU A . n A 1 247 PRO 247 273 273 PRO PRO A . n A 1 248 PRO 248 274 274 PRO PRO A . n A 1 249 SER 249 275 275 SER SER A . n A 1 250 GLN 250 276 276 GLN GLN A . n A 1 251 ALA 251 277 277 ALA ALA A . n A 1 252 ASP 252 278 278 ASP ASP A . n A 1 253 ILE 253 279 279 ILE ILE A . n A 1 254 GLU 254 280 280 GLU GLU A . n A 1 255 GLN 255 281 281 GLN GLN A . n A 1 256 GLN 256 282 282 GLN GLN A . n A 1 257 ALA 257 283 283 ALA ALA A . n A 1 258 ARG 258 284 284 ARG ARG A . n A 1 259 ASP 259 285 285 ASP ASP A . n A 1 260 TYR 260 286 286 TYR TYR A . n A 1 261 ALA 261 287 287 ALA ALA A . n A 1 262 THR 262 288 288 THR THR A . n A 1 263 VAL 263 289 289 VAL VAL A . n A 1 264 VAL 264 290 290 VAL VAL A . n A 1 265 ASN 265 291 291 ASN ASN A . n A 1 266 ALA 266 292 292 ALA ALA A . n A 1 267 CYS 267 293 293 CYS CYS A . n A 1 268 LYS 268 294 294 LYS LYS A . n A 1 269 ALA 269 295 295 ALA ALA A . n A 1 270 GLN 270 296 296 GLN GLN A . n A 1 271 GLY 271 297 297 GLY GLY A . n A 1 272 ALA 272 298 298 ALA ALA A . n A 1 273 ALA 273 299 299 ALA ALA A . n A 1 274 CYS 274 300 300 CYS CYS A . n A 1 275 VAL 275 301 301 VAL VAL A . n A 1 276 GLY 276 302 302 GLY GLY A . n A 1 277 ILE 277 303 303 ILE ILE A . n A 1 278 THR 278 304 304 THR THR A . n A 1 279 THR 279 305 305 THR THR A . n A 1 280 TRP 280 306 306 TRP TRP A . n A 1 281 GLY 281 307 307 GLY GLY A . n A 1 282 ILE 282 308 308 ILE ILE A . n A 1 283 THR 283 309 309 THR THR A . n A 1 284 ASP 284 310 310 ASP ASP A . n A 1 285 LEU 285 311 311 LEU LEU A . n A 1 286 TYR 286 312 312 TYR TYR A . n A 1 287 SER 287 313 313 SER SER A . n A 1 288 TRP 288 314 314 TRP TRP A . n A 1 289 ILE 289 315 315 ILE ILE A . n A 1 290 PRO 290 316 316 PRO PRO A . n A 1 291 SER 291 317 317 SER SER A . n A 1 292 THR 292 318 318 THR THR A . n A 1 293 TYR 293 319 319 TYR TYR A . n A 1 294 PRO 294 320 320 PRO PRO A . n A 1 295 GLY 295 321 321 GLY GLY A . n A 1 296 GLU 296 322 322 GLU GLU A . n A 1 297 GLY 297 323 323 GLY GLY A . n A 1 298 TYR 298 324 324 TYR TYR A . n A 1 299 ALA 299 325 325 ALA ALA A . n A 1 300 LEU 300 326 326 LEU LEU A . n A 1 301 LEU 301 327 327 LEU LEU A . n A 1 302 PHE 302 328 328 PHE PHE A . n A 1 303 ASP 303 329 329 ASP ASP A . n A 1 304 ASP 304 330 330 ASP ASP A . n A 1 305 ASN 305 331 331 ASN ASN A . n A 1 306 TYR 306 332 332 TYR TYR A . n A 1 307 VAL 307 333 333 VAL VAL A . n A 1 308 PRO 308 334 334 PRO PRO A . n A 1 309 HIS 309 335 335 HIS HIS A . n A 1 310 PRO 310 336 336 PRO PRO A . n A 1 311 ALA 311 337 337 ALA ALA A . n A 1 312 PHE 312 338 338 PHE PHE A . n A 1 313 ASN 313 339 339 ASN ASN A . n A 1 314 ALA 314 340 340 ALA ALA A . n A 1 315 THR 315 341 341 THR THR A . n A 1 316 ILE 316 342 342 ILE ILE A . n A 1 317 GLN 317 343 343 GLN GLN A . n A 1 318 ALA 318 344 344 ALA ALA A . n A 1 319 LEU 319 345 345 LEU LEU A . n A 1 320 LEU 320 346 346 LEU LEU A . n A 1 321 ALA 321 347 347 ALA ALA A . n B 1 1 PRO 1 27 27 PRO PRO B . n B 1 2 THR 2 28 28 THR THR B . n B 1 3 SER 3 29 29 SER SER B . n B 1 4 PRO 4 30 30 PRO PRO B . n B 1 5 PHE 5 31 31 PHE PHE B . n B 1 6 GLU 6 32 32 GLU GLU B . n B 1 7 THR 7 33 33 THR THR B . n B 1 8 LEU 8 34 34 LEU LEU B . n B 1 9 ARG 9 35 35 ARG ARG B . n B 1 10 ALA 10 36 36 ALA ALA B . n B 1 11 ALA 11 37 37 ALA ALA B . n B 1 12 ALA 12 38 38 ALA ALA B . n B 1 13 ALA 13 39 39 ALA ALA B . n B 1 14 PRO 14 40 40 PRO PRO B . n B 1 15 ARG 15 41 41 ARG ARG B . n B 1 16 TYR 16 42 42 TYR TYR B . n B 1 17 PHE 17 43 43 PHE PHE B . n B 1 18 GLY 18 44 44 GLY GLY B . n B 1 19 ALA 19 45 45 ALA ALA B . n B 1 20 ALA 20 46 46 ALA ALA B . n B 1 21 LEU 21 47 47 LEU LEU B . n B 1 22 GLY 22 48 48 GLY GLY B . n B 1 23 VAL 23 49 49 VAL VAL B . n B 1 24 PRO 24 50 50 PRO PRO B . n B 1 25 HIS 25 51 51 HIS HIS B . n B 1 26 LEU 26 52 52 LEU LEU B . n B 1 27 LEU 27 53 53 LEU LEU B . n B 1 28 ASN 28 54 54 ASN ASN B . n B 1 29 PHE 29 55 55 PHE PHE B . n B 1 30 THR 30 56 56 THR THR B . n B 1 31 HIS 31 57 57 HIS HIS B . n B 1 32 ASP 32 58 58 ASP ASP B . n B 1 33 PRO 33 59 59 PRO PRO B . n B 1 34 LEU 34 60 60 LEU LEU B . n B 1 35 PHE 35 61 61 PHE PHE B . n B 1 36 ASP 36 62 62 ASP ASP B . n B 1 37 VAL 37 63 63 VAL VAL B . n B 1 38 THR 38 64 64 THR THR B . n B 1 39 ALA 39 65 65 ALA ALA B . n B 1 40 VAL 40 66 66 VAL VAL B . n B 1 41 LEU 41 67 67 LEU LEU B . n B 1 42 GLN 42 68 68 GLN GLN B . n B 1 43 PHE 43 69 69 PHE PHE B . n B 1 44 ASN 44 70 70 ASN ASN B . n B 1 45 GLY 45 71 71 GLY GLY B . n B 1 46 ALA 46 72 72 ALA ALA B . n B 1 47 THR 47 73 73 THR THR B . n B 1 48 PRO 48 74 74 PRO PRO B . n B 1 49 GLU 49 75 75 GLU GLU B . n B 1 50 ASN 50 76 76 ASN ASN B . n B 1 51 GLU 51 77 77 GLU GLU B . n B 1 52 MET 52 78 78 MET MET B . n B 1 53 LYS 53 79 79 LYS LYS B . n B 1 54 TRP 54 80 80 TRP TRP B . n B 1 55 ALA 55 81 81 ALA ALA B . n B 1 56 TYR 56 82 82 TYR TYR B . n B 1 57 ILE 57 83 83 ILE ILE B . n B 1 58 GLU 58 84 84 GLU GLU B . n B 1 59 PRO 59 85 85 PRO PRO B . n B 1 60 GLU 60 86 86 GLU GLU B . n B 1 61 ARG 61 87 87 ARG ARG B . n B 1 62 ASN 62 88 88 ASN ASN B . n B 1 63 GLN 63 89 89 GLN GLN B . n B 1 64 PHE 64 90 90 PHE PHE B . n B 1 65 ASN 65 91 91 ASN ASN B . n B 1 66 PHE 66 92 92 PHE PHE B . n B 1 67 THR 67 93 93 THR THR B . n B 1 68 GLY 68 94 94 GLY GLY B . n B 1 69 GLY 69 95 95 GLY GLY B . n B 1 70 ASP 70 96 96 ASP ASP B . n B 1 71 ILE 71 97 97 ILE ILE B . n B 1 72 VAL 72 98 98 VAL VAL B . n B 1 73 ALA 73 99 99 ALA ALA B . n B 1 74 ALA 74 100 100 ALA ALA B . n B 1 75 PHE 75 101 101 PHE PHE B . n B 1 76 SER 76 102 102 SER SER B . n B 1 77 ALA 77 103 103 ALA ALA B . n B 1 78 ALA 78 104 104 ALA ALA B . n B 1 79 ASN 79 105 105 ASN ASN B . n B 1 80 ASP 80 106 106 ASP ASP B . n B 1 81 TYR 81 107 107 TYR TYR B . n B 1 82 VAL 82 108 108 VAL VAL B . n B 1 83 LEU 83 109 109 LEU LEU B . n B 1 84 ARG 84 110 110 ARG ARG B . n B 1 85 GLY 85 111 111 GLY GLY B . n B 1 86 HIS 86 112 112 HIS HIS B . n B 1 87 ASN 87 113 113 ASN ASN B . n B 1 88 LEU 88 114 114 LEU LEU B . n B 1 89 VAL 89 115 115 VAL VAL B . n B 1 90 TRP 90 116 116 TRP TRP B . n B 1 91 TYR 91 117 117 TYR TYR B . n B 1 92 GLN 92 118 118 GLN GLN B . n B 1 93 GLU 93 119 119 GLU GLU B . n B 1 94 LEU 94 120 120 LEU LEU B . n B 1 95 ALA 95 121 121 ALA ALA B . n B 1 96 PRO 96 122 122 PRO PRO B . n B 1 97 TRP 97 123 123 TRP TRP B . n B 1 98 VAL 98 124 124 VAL VAL B . n B 1 99 GLU 99 125 125 GLU GLU B . n B 1 100 THR 100 126 126 THR THR B . n B 1 101 LEU 101 127 127 LEU LEU B . n B 1 102 THR 102 128 128 THR THR B . n B 1 103 GLY 103 129 129 GLY GLY B . n B 1 104 GLU 104 130 130 GLU GLU B . n B 1 105 ASP 105 131 131 ASP ASP B . n B 1 106 LEU 106 132 132 LEU LEU B . n B 1 107 TRP 107 133 133 TRP TRP B . n B 1 108 ASN 108 134 134 ASN ASN B . n B 1 109 ALA 109 135 135 ALA ALA B . n B 1 110 THR 110 136 136 THR THR B . n B 1 111 VAL 111 137 137 VAL VAL B . n B 1 112 ASN 112 138 138 ASN ASN B . n B 1 113 HIS 113 139 139 HIS HIS B . n B 1 114 ILE 114 140 140 ILE ILE B . n B 1 115 THR 115 141 141 THR THR B . n B 1 116 THR 116 142 142 THR THR B . n B 1 117 VAL 117 143 143 VAL VAL B . n B 1 118 MET 118 144 144 MET MET B . n B 1 119 THR 119 145 145 THR THR B . n B 1 120 HIS 120 146 146 HIS HIS B . n B 1 121 TYR 121 147 147 TYR TYR B . n B 1 122 LYS 122 148 148 LYS LYS B . n B 1 123 GLU 123 149 149 GLU GLU B . n B 1 124 SER 124 150 150 SER SER B . n B 1 125 PHE 125 151 151 PHE PHE B . n B 1 126 ASN 126 152 152 ASN ASN B . n B 1 127 ILE 127 153 153 ILE ILE B . n B 1 128 TYR 128 154 154 TYR TYR B . n B 1 129 ALA 129 155 155 ALA ALA B . n B 1 130 TRP 130 156 156 TRP TRP B . n B 1 131 ASP 131 157 157 ASP ASP B . n B 1 132 VAL 132 158 158 VAL VAL B . n B 1 133 VAL 133 159 159 VAL VAL B . n B 1 134 ASN 134 160 160 ASN ASN B . n B 1 135 GLU 135 161 161 GLU GLU B . n B 1 136 ALA 136 162 162 ALA ALA B . n B 1 137 PHE 137 163 163 PHE PHE B . n B 1 138 ASN 138 164 164 ASN ASN B . n B 1 139 ASP 139 165 165 ASP ASP B . n B 1 140 ASN 140 166 166 ASN ASN B . n B 1 141 GLY 141 167 167 GLY GLY B . n B 1 142 THR 142 168 168 THR THR B . n B 1 143 TYR 143 169 169 TYR TYR B . n B 1 144 ARG 144 170 170 ARG ARG B . n B 1 145 GLU 145 171 171 GLU GLU B . n B 1 146 ASN 146 172 172 ASN ASN B . n B 1 147 VAL 147 173 173 VAL VAL B . n B 1 148 TRP 148 174 174 TRP TRP B . n B 1 149 TYR 149 175 175 TYR TYR B . n B 1 150 THR 150 176 176 THR THR B . n B 1 151 GLN 151 177 177 GLN GLN B . n B 1 152 LEU 152 178 178 LEU LEU B . n B 1 153 GLY 153 179 179 GLY GLY B . n B 1 154 PRO 154 180 180 PRO PRO B . n B 1 155 ASP 155 181 181 ASP ASP B . n B 1 156 TYR 156 182 182 TYR TYR B . n B 1 157 ILE 157 183 183 ILE ILE B . n B 1 158 PRO 158 184 184 PRO PRO B . n B 1 159 ASN 159 185 185 ASN ASN B . n B 1 160 ALA 160 186 186 ALA ALA B . n B 1 161 TYR 161 187 187 TYR TYR B . n B 1 162 ALA 162 188 188 ALA ALA B . n B 1 163 VAL 163 189 189 VAL VAL B . n B 1 164 ALA 164 190 190 ALA ALA B . n B 1 165 ARG 165 191 191 ARG ARG B . n B 1 166 SER 166 192 192 SER SER B . n B 1 167 VAL 167 193 193 VAL VAL B . n B 1 168 ASN 168 194 194 ASN ASN B . n B 1 169 THR 169 195 195 THR THR B . n B 1 170 PRO 170 196 196 PRO PRO B . n B 1 171 SER 171 197 197 SER SER B . n B 1 172 LYS 172 198 198 LYS LYS B . n B 1 173 LEU 173 199 199 LEU LEU B . n B 1 174 TYR 174 200 200 TYR TYR B . n B 1 175 ILE 175 201 201 ILE ILE B . n B 1 176 ASN 176 202 202 ASN ASN B . n B 1 177 ASP 177 203 203 ASP ASP B . n B 1 178 TYR 178 204 204 TYR TYR B . n B 1 179 ASN 179 205 205 ASN ASN B . n B 1 180 THR 180 206 206 THR THR B . n B 1 181 GLU 181 207 207 GLU GLU B . n B 1 182 GLY 182 208 208 GLY GLY B . n B 1 183 ILE 183 209 209 ILE ILE B . n B 1 184 ASN 184 210 210 ASN ASN B . n B 1 185 ASN 185 211 211 ASN ASN B . n B 1 186 LYS 186 212 212 LYS LYS B . n B 1 187 SER 187 213 213 SER SER B . n B 1 188 ASP 188 214 214 ASP ASP B . n B 1 189 ALA 189 215 215 ALA ALA B . n B 1 190 LEU 190 216 216 LEU LEU B . n B 1 191 LEU 191 217 217 LEU LEU B . n B 1 192 ALA 192 218 218 ALA ALA B . n B 1 193 VAL 193 219 219 VAL VAL B . n B 1 194 VAL 194 220 220 VAL VAL B . n B 1 195 GLN 195 221 221 GLN GLN B . n B 1 196 SER 196 222 222 SER SER B . n B 1 197 MET 197 223 223 MET MET B . n B 1 198 LYS 198 224 224 LYS LYS B . n B 1 199 ALA 199 225 225 ALA ALA B . n B 1 200 HIS 200 226 226 HIS HIS B . n B 1 201 ASN 201 227 227 ASN ASN B . n B 1 202 LEU 202 228 228 LEU LEU B . n B 1 203 VAL 203 229 229 VAL VAL B . n B 1 204 ASP 204 230 230 ASP ASP B . n B 1 205 GLY 205 231 231 GLY GLY B . n B 1 206 VAL 206 232 232 VAL VAL B . n B 1 207 GLY 207 233 233 GLY GLY B . n B 1 208 PHE 208 234 234 PHE PHE B . n B 1 209 GLN 209 235 235 GLN GLN B . n B 1 210 CYS 210 236 236 CYS CYS B . n B 1 211 HIS 211 237 237 HIS HIS B . n B 1 212 PHE 212 238 238 PHE PHE B . n B 1 213 PHE 213 239 239 PHE PHE B . n B 1 214 VAL 214 240 240 VAL VAL B . n B 1 215 GLY 215 241 241 GLY GLY B . n B 1 216 GLU 216 242 242 GLU GLU B . n B 1 217 LEU 217 243 243 LEU LEU B . n B 1 218 PRO 218 244 244 PRO PRO B . n B 1 219 PRO 219 245 245 PRO PRO B . n B 1 220 ASP 220 246 246 ASP ASP B . n B 1 221 LEU 221 247 247 LEU LEU B . n B 1 222 GLU 222 248 248 GLU GLU B . n B 1 223 GLN 223 249 249 GLN GLN B . n B 1 224 ASN 224 250 250 ASN ASN B . n B 1 225 PHE 225 251 251 PHE PHE B . n B 1 226 ALA 226 252 252 ALA ALA B . n B 1 227 ARG 227 253 253 ARG ARG B . n B 1 228 PHE 228 254 254 PHE PHE B . n B 1 229 VAL 229 255 255 VAL VAL B . n B 1 230 ALA 230 256 256 ALA ALA B . n B 1 231 ALA 231 257 257 ALA ALA B . n B 1 232 GLY 232 258 258 GLY GLY B . n B 1 233 VAL 233 259 259 VAL VAL B . n B 1 234 GLU 234 260 260 GLU GLU B . n B 1 235 ILE 235 261 261 ILE ILE B . n B 1 236 ALA 236 262 262 ALA ALA B . n B 1 237 VAL 237 263 263 VAL VAL B . n B 1 238 THR 238 264 264 THR THR B . n B 1 239 GLU 239 265 265 GLU GLU B . n B 1 240 LEU 240 266 266 LEU LEU B . n B 1 241 ASP 241 267 267 ASP ASP B . n B 1 242 ILE 242 268 268 ILE ILE B . n B 1 243 ARG 243 269 269 ARG ARG B . n B 1 244 MET 244 270 270 MET MET B . n B 1 245 ASN 245 271 271 ASN ASN B . n B 1 246 LEU 246 272 272 LEU LEU B . n B 1 247 PRO 247 273 273 PRO PRO B . n B 1 248 PRO 248 274 274 PRO PRO B . n B 1 249 SER 249 275 275 SER SER B . n B 1 250 GLN 250 276 276 GLN GLN B . n B 1 251 ALA 251 277 277 ALA ALA B . n B 1 252 ASP 252 278 278 ASP ASP B . n B 1 253 ILE 253 279 279 ILE ILE B . n B 1 254 GLU 254 280 280 GLU GLU B . n B 1 255 GLN 255 281 281 GLN GLN B . n B 1 256 GLN 256 282 282 GLN GLN B . n B 1 257 ALA 257 283 283 ALA ALA B . n B 1 258 ARG 258 284 284 ARG ARG B . n B 1 259 ASP 259 285 285 ASP ASP B . n B 1 260 TYR 260 286 286 TYR TYR B . n B 1 261 ALA 261 287 287 ALA ALA B . n B 1 262 THR 262 288 288 THR THR B . n B 1 263 VAL 263 289 289 VAL VAL B . n B 1 264 VAL 264 290 290 VAL VAL B . n B 1 265 ASN 265 291 291 ASN ASN B . n B 1 266 ALA 266 292 292 ALA ALA B . n B 1 267 CYS 267 293 293 CYS CYS B . n B 1 268 LYS 268 294 294 LYS LYS B . n B 1 269 ALA 269 295 295 ALA ALA B . n B 1 270 GLN 270 296 296 GLN GLN B . n B 1 271 GLY 271 297 297 GLY GLY B . n B 1 272 ALA 272 298 298 ALA ALA B . n B 1 273 ALA 273 299 299 ALA ALA B . n B 1 274 CYS 274 300 300 CYS CYS B . n B 1 275 VAL 275 301 301 VAL VAL B . n B 1 276 GLY 276 302 302 GLY GLY B . n B 1 277 ILE 277 303 303 ILE ILE B . n B 1 278 THR 278 304 304 THR THR B . n B 1 279 THR 279 305 305 THR THR B . n B 1 280 TRP 280 306 306 TRP TRP B . n B 1 281 GLY 281 307 307 GLY GLY B . n B 1 282 ILE 282 308 308 ILE ILE B . n B 1 283 THR 283 309 309 THR THR B . n B 1 284 ASP 284 310 310 ASP ASP B . n B 1 285 LEU 285 311 311 LEU LEU B . n B 1 286 TYR 286 312 312 TYR TYR B . n B 1 287 SER 287 313 313 SER SER B . n B 1 288 TRP 288 314 314 TRP TRP B . n B 1 289 ILE 289 315 315 ILE ILE B . n B 1 290 PRO 290 316 316 PRO PRO B . n B 1 291 SER 291 317 317 SER SER B . n B 1 292 THR 292 318 318 THR THR B . n B 1 293 TYR 293 319 319 TYR TYR B . n B 1 294 PRO 294 320 320 PRO PRO B . n B 1 295 GLY 295 321 321 GLY GLY B . n B 1 296 GLU 296 322 322 GLU GLU B . n B 1 297 GLY 297 323 323 GLY GLY B . n B 1 298 TYR 298 324 324 TYR TYR B . n B 1 299 ALA 299 325 325 ALA ALA B . n B 1 300 LEU 300 326 326 LEU LEU B . n B 1 301 LEU 301 327 327 LEU LEU B . n B 1 302 PHE 302 328 328 PHE PHE B . n B 1 303 ASP 303 329 329 ASP ASP B . n B 1 304 ASP 304 330 330 ASP ASP B . n B 1 305 ASN 305 331 331 ASN ASN B . n B 1 306 TYR 306 332 332 TYR TYR B . n B 1 307 VAL 307 333 333 VAL VAL B . n B 1 308 PRO 308 334 334 PRO PRO B . n B 1 309 HIS 309 335 335 HIS HIS B . n B 1 310 PRO 310 336 336 PRO PRO B . n B 1 311 ALA 311 337 337 ALA ALA B . n B 1 312 PHE 312 338 338 PHE PHE B . n B 1 313 ASN 313 339 339 ASN ASN B . n B 1 314 ALA 314 340 340 ALA ALA B . n B 1 315 THR 315 341 341 THR THR B . n B 1 316 ILE 316 342 342 ILE ILE B . n B 1 317 GLN 317 343 343 GLN GLN B . n B 1 318 ALA 318 344 344 ALA ALA B . n B 1 319 LEU 319 345 345 LEU LEU B . n B 1 320 LEU 320 346 346 LEU LEU B . n B 1 321 ALA 321 347 347 ALA ALA B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 UNX 1 401 2 UNX UNX A . D 3 NAG 1 402 401 NAG NAG A . E 3 NAG 2 403 402 NAG NAG A . F 4 BMA 3 404 403 BMA BMA A . G 5 MAN 4 405 404 MAN MAN A . H 5 MAN 5 406 405 MAN MAN A . I 5 MAN 6 407 406 MAN MAN A . J 5 MAN 7 408 407 MAN MAN A . K 5 MAN 8 409 408 MAN MAN A . L 3 NAG 1 410 409 NAG NAG A . M 3 NAG 2 411 410 NAG NAG A . N 4 BMA 3 412 411 BMA BMA A . O 5 MAN 4 413 412 MAN MAN A . P 5 MAN 5 414 413 MAN MAN A . Q 5 MAN 6 415 414 MAN MAN A . R 5 MAN 7 416 415 MAN MAN A . S 5 MAN 8 417 416 MAN MAN A . T 5 MAN 9 418 417 MAN MAN A . U 3 NAG 1 419 418 NAG NAG A . V 3 NAG 2 420 419 NAG NAG A . W 4 BMA 3 421 420 BMA BMA A . X 5 MAN 4 422 421 MAN MAN A . Y 3 NAG 1 423 422 NAG NAG A . Z 6 MG 1 424 423 MG MG A . AA 7 PEG 1 425 424 PEG PEG A . BA 8 P6G 1 426 425 P6G P6G A . CA 8 P6G 1 427 426 P6G P6G A . DA 9 GOL 1 428 427 GOL GOL A . EA 9 GOL 1 429 428 GOL GOL A . FA 9 GOL 1 430 429 GOL GOL A . GA 9 GOL 1 431 430 GOL GOL A . HA 2 UNX 1 401 1 UNX UNX B . IA 3 NAG 1 402 401 NAG NAG B . JA 3 NAG 2 403 402 NAG NAG B . KA 4 BMA 3 404 403 BMA BMA B . LA 5 MAN 4 405 404 MAN MAN B . MA 5 MAN 5 406 405 MAN MAN B . NA 5 MAN 6 407 406 MAN MAN B . OA 3 NAG 1 408 407 NAG NAG B . PA 3 NAG 2 409 408 NAG NAG B . QA 4 BMA 3 410 409 BMA BMA B . RA 5 MAN 4 411 410 MAN MAN B . SA 5 MAN 5 412 411 MAN MAN B . TA 5 MAN 6 413 412 MAN MAN B . UA 5 MAN 7 414 413 MAN MAN B . VA 5 MAN 8 415 414 MAN MAN B . WA 3 NAG 1 416 415 NAG NAG B . XA 3 NAG 1 417 416 NAG NAG B . YA 3 NAG 2 418 417 NAG NAG B . ZA 3 NAG 1 419 418 NAG NAG B . AB 6 MG 1 420 419 MG MG B . BB 10 CL 1 421 420 CL CL B . CB 7 PEG 1 422 421 PEG PEG B . DB 7 PEG 1 423 422 PEG PEG B . EB 9 GOL 1 424 423 GOL GOL B . FB 9 GOL 1 425 424 GOL GOL B . GB 9 GOL 1 426 425 GOL GOL B . HB 11 HOH 1 501 501 HOH HOH A . HB 11 HOH 2 502 782 HOH HOH A . HB 11 HOH 3 503 646 HOH HOH A . HB 11 HOH 4 504 502 HOH HOH A . HB 11 HOH 5 505 683 HOH HOH A . HB 11 HOH 6 506 682 HOH HOH A . HB 11 HOH 7 507 687 HOH HOH A . HB 11 HOH 8 508 503 HOH HOH A . HB 11 HOH 9 509 737 HOH HOH A . HB 11 HOH 10 510 575 HOH HOH A . HB 11 HOH 11 511 718 HOH HOH A . HB 11 HOH 12 512 504 HOH HOH A . HB 11 HOH 13 513 571 HOH HOH A . HB 11 HOH 14 514 642 HOH HOH A . HB 11 HOH 15 515 604 HOH HOH A . HB 11 HOH 16 516 663 HOH HOH A . HB 11 HOH 17 517 694 HOH HOH A . HB 11 HOH 18 518 569 HOH HOH A . HB 11 HOH 19 519 576 HOH HOH A . HB 11 HOH 20 520 595 HOH HOH A . HB 11 HOH 21 521 645 HOH HOH A . HB 11 HOH 22 522 630 HOH HOH A . HB 11 HOH 23 523 723 HOH HOH A . HB 11 HOH 24 524 620 HOH HOH A . HB 11 HOH 25 525 581 HOH HOH A . HB 11 HOH 26 526 577 HOH HOH A . HB 11 HOH 27 527 635 HOH HOH A . HB 11 HOH 28 528 566 HOH HOH A . HB 11 HOH 29 529 613 HOH HOH A . HB 11 HOH 30 530 762 HOH HOH A . HB 11 HOH 31 531 505 HOH HOH A . HB 11 HOH 32 532 627 HOH HOH A . HB 11 HOH 33 533 781 HOH HOH A . HB 11 HOH 34 534 623 HOH HOH A . HB 11 HOH 35 535 506 HOH HOH A . HB 11 HOH 36 536 621 HOH HOH A . HB 11 HOH 37 537 580 HOH HOH A . HB 11 HOH 38 538 750 HOH HOH A . HB 11 HOH 39 539 730 HOH HOH A . HB 11 HOH 40 540 590 HOH HOH A . HB 11 HOH 41 541 616 HOH HOH A . HB 11 HOH 42 542 601 HOH HOH A . HB 11 HOH 43 543 570 HOH HOH A . HB 11 HOH 44 544 602 HOH HOH A . HB 11 HOH 45 545 507 HOH HOH A . HB 11 HOH 46 546 508 HOH HOH A . HB 11 HOH 47 547 509 HOH HOH A . HB 11 HOH 48 548 675 HOH HOH A . HB 11 HOH 49 549 661 HOH HOH A . HB 11 HOH 50 550 510 HOH HOH A . HB 11 HOH 51 551 568 HOH HOH A . HB 11 HOH 52 552 614 HOH HOH A . HB 11 HOH 53 553 703 HOH HOH A . HB 11 HOH 54 554 671 HOH HOH A . HB 11 HOH 55 555 609 HOH HOH A . HB 11 HOH 56 556 612 HOH HOH A . HB 11 HOH 57 557 746 HOH HOH A . HB 11 HOH 58 558 722 HOH HOH A . HB 11 HOH 59 559 592 HOH HOH A . HB 11 HOH 60 560 740 HOH HOH A . HB 11 HOH 61 561 511 HOH HOH A . HB 11 HOH 62 562 512 HOH HOH A . HB 11 HOH 63 563 513 HOH HOH A . HB 11 HOH 64 564 514 HOH HOH A . HB 11 HOH 65 565 679 HOH HOH A . HB 11 HOH 66 566 585 HOH HOH A . HB 11 HOH 67 567 692 HOH HOH A . HB 11 HOH 68 568 515 HOH HOH A . HB 11 HOH 69 569 583 HOH HOH A . HB 11 HOH 70 570 678 HOH HOH A . HB 11 HOH 71 571 605 HOH HOH A . HB 11 HOH 72 572 676 HOH HOH A . HB 11 HOH 73 573 608 HOH HOH A . HB 11 HOH 74 574 636 HOH HOH A . HB 11 HOH 75 575 771 HOH HOH A . HB 11 HOH 76 576 720 HOH HOH A . HB 11 HOH 77 577 690 HOH HOH A . HB 11 HOH 78 578 693 HOH HOH A . HB 11 HOH 79 579 584 HOH HOH A . HB 11 HOH 80 580 578 HOH HOH A . HB 11 HOH 81 581 639 HOH HOH A . HB 11 HOH 82 582 586 HOH HOH A . HB 11 HOH 83 583 670 HOH HOH A . HB 11 HOH 84 584 603 HOH HOH A . HB 11 HOH 85 585 626 HOH HOH A . HB 11 HOH 86 586 516 HOH HOH A . HB 11 HOH 87 587 622 HOH HOH A . HB 11 HOH 88 588 594 HOH HOH A . HB 11 HOH 89 589 631 HOH HOH A . HB 11 HOH 90 590 640 HOH HOH A . HB 11 HOH 91 591 610 HOH HOH A . HB 11 HOH 92 592 517 HOH HOH A . HB 11 HOH 93 593 625 HOH HOH A . HB 11 HOH 94 594 684 HOH HOH A . HB 11 HOH 95 595 716 HOH HOH A . HB 11 HOH 96 596 518 HOH HOH A . HB 11 HOH 97 597 695 HOH HOH A . HB 11 HOH 98 598 579 HOH HOH A . HB 11 HOH 99 599 519 HOH HOH A . HB 11 HOH 100 600 600 HOH HOH A . HB 11 HOH 101 601 520 HOH HOH A . HB 11 HOH 102 602 615 HOH HOH A . HB 11 HOH 103 603 637 HOH HOH A . HB 11 HOH 104 604 521 HOH HOH A . HB 11 HOH 105 605 573 HOH HOH A . HB 11 HOH 106 606 659 HOH HOH A . HB 11 HOH 107 607 652 HOH HOH A . HB 11 HOH 108 608 618 HOH HOH A . HB 11 HOH 109 609 793 HOH HOH A . HB 11 HOH 110 610 522 HOH HOH A . HB 11 HOH 111 611 763 HOH HOH A . HB 11 HOH 112 612 632 HOH HOH A . HB 11 HOH 113 613 633 HOH HOH A . HB 11 HOH 114 614 758 HOH HOH A . HB 11 HOH 115 615 523 HOH HOH A . HB 11 HOH 116 616 651 HOH HOH A . HB 11 HOH 117 617 524 HOH HOH A . HB 11 HOH 118 618 666 HOH HOH A . HB 11 HOH 119 619 525 HOH HOH A . HB 11 HOH 120 620 708 HOH HOH A . HB 11 HOH 121 621 619 HOH HOH A . HB 11 HOH 122 622 660 HOH HOH A . HB 11 HOH 123 623 658 HOH HOH A . HB 11 HOH 124 624 649 HOH HOH A . HB 11 HOH 125 625 593 HOH HOH A . HB 11 HOH 126 626 526 HOH HOH A . HB 11 HOH 127 627 673 HOH HOH A . HB 11 HOH 128 628 527 HOH HOH A . HB 11 HOH 129 629 528 HOH HOH A . HB 11 HOH 130 630 587 HOH HOH A . HB 11 HOH 131 631 668 HOH HOH A . HB 11 HOH 132 632 529 HOH HOH A . HB 11 HOH 133 633 719 HOH HOH A . HB 11 HOH 134 634 629 HOH HOH A . HB 11 HOH 135 635 572 HOH HOH A . HB 11 HOH 136 636 743 HOH HOH A . HB 11 HOH 137 637 567 HOH HOH A . HB 11 HOH 138 638 611 HOH HOH A . HB 11 HOH 139 639 582 HOH HOH A . HB 11 HOH 140 640 706 HOH HOH A . HB 11 HOH 141 641 634 HOH HOH A . HB 11 HOH 142 642 530 HOH HOH A . HB 11 HOH 143 643 677 HOH HOH A . HB 11 HOH 144 644 531 HOH HOH A . HB 11 HOH 145 645 532 HOH HOH A . HB 11 HOH 146 646 705 HOH HOH A . HB 11 HOH 147 647 533 HOH HOH A . HB 11 HOH 148 648 667 HOH HOH A . HB 11 HOH 149 649 665 HOH HOH A . HB 11 HOH 150 650 617 HOH HOH A . HB 11 HOH 151 651 686 HOH HOH A . HB 11 HOH 152 652 638 HOH HOH A . HB 11 HOH 153 653 653 HOH HOH A . HB 11 HOH 154 654 534 HOH HOH A . HB 11 HOH 155 655 597 HOH HOH A . HB 11 HOH 156 656 774 HOH HOH A . HB 11 HOH 157 657 535 HOH HOH A . HB 11 HOH 158 658 574 HOH HOH A . HB 11 HOH 159 659 628 HOH HOH A . HB 11 HOH 160 660 662 HOH HOH A . HB 11 HOH 161 661 536 HOH HOH A . HB 11 HOH 162 662 689 HOH HOH A . HB 11 HOH 163 663 669 HOH HOH A . HB 11 HOH 164 664 772 HOH HOH A . HB 11 HOH 165 665 735 HOH HOH A . HB 11 HOH 166 666 588 HOH HOH A . HB 11 HOH 167 667 606 HOH HOH A . HB 11 HOH 168 668 721 HOH HOH A . HB 11 HOH 169 669 537 HOH HOH A . HB 11 HOH 170 670 765 HOH HOH A . HB 11 HOH 171 671 702 HOH HOH A . HB 11 HOH 172 672 538 HOH HOH A . HB 11 HOH 173 673 539 HOH HOH A . HB 11 HOH 174 674 540 HOH HOH A . HB 11 HOH 175 675 725 HOH HOH A . HB 11 HOH 176 676 596 HOH HOH A . HB 11 HOH 177 677 672 HOH HOH A . HB 11 HOH 178 678 599 HOH HOH A . HB 11 HOH 179 679 739 HOH HOH A . HB 11 HOH 180 680 648 HOH HOH A . HB 11 HOH 181 681 754 HOH HOH A . HB 11 HOH 182 682 541 HOH HOH A . HB 11 HOH 183 683 767 HOH HOH A . HB 11 HOH 184 684 734 HOH HOH A . HB 11 HOH 185 685 714 HOH HOH A . HB 11 HOH 186 686 745 HOH HOH A . HB 11 HOH 187 687 768 HOH HOH A . HB 11 HOH 188 688 700 HOH HOH A . HB 11 HOH 189 689 710 HOH HOH A . HB 11 HOH 190 690 761 HOH HOH A . HB 11 HOH 191 691 542 HOH HOH A . HB 11 HOH 192 692 543 HOH HOH A . HB 11 HOH 193 693 741 HOH HOH A . HB 11 HOH 194 694 544 HOH HOH A . HB 11 HOH 195 695 598 HOH HOH A . HB 11 HOH 196 696 641 HOH HOH A . HB 11 HOH 197 697 751 HOH HOH A . HB 11 HOH 198 698 624 HOH HOH A . HB 11 HOH 199 699 717 HOH HOH A . HB 11 HOH 200 700 712 HOH HOH A . HB 11 HOH 201 701 545 HOH HOH A . HB 11 HOH 202 702 738 HOH HOH A . HB 11 HOH 203 703 691 HOH HOH A . HB 11 HOH 204 704 657 HOH HOH A . HB 11 HOH 205 705 643 HOH HOH A . HB 11 HOH 206 706 674 HOH HOH A . HB 11 HOH 207 707 704 HOH HOH A . HB 11 HOH 208 708 546 HOH HOH A . HB 11 HOH 209 709 656 HOH HOH A . HB 11 HOH 210 710 547 HOH HOH A . HB 11 HOH 211 711 766 HOH HOH A . HB 11 HOH 212 712 744 HOH HOH A . HB 11 HOH 213 713 764 HOH HOH A . HB 11 HOH 214 714 548 HOH HOH A . HB 11 HOH 215 715 726 HOH HOH A . HB 11 HOH 216 716 549 HOH HOH A . HB 11 HOH 217 717 680 HOH HOH A . HB 11 HOH 218 718 550 HOH HOH A . HB 11 HOH 219 719 776 HOH HOH A . HB 11 HOH 220 720 755 HOH HOH A . HB 11 HOH 221 721 551 HOH HOH A . HB 11 HOH 222 722 552 HOH HOH A . HB 11 HOH 223 723 769 HOH HOH A . HB 11 HOH 224 724 607 HOH HOH A . HB 11 HOH 225 725 553 HOH HOH A . HB 11 HOH 226 726 685 HOH HOH A . HB 11 HOH 227 727 777 HOH HOH A . HB 11 HOH 228 728 688 HOH HOH A . HB 11 HOH 229 729 756 HOH HOH A . HB 11 HOH 230 730 733 HOH HOH A . HB 11 HOH 231 731 752 HOH HOH A . HB 11 HOH 232 732 711 HOH HOH A . HB 11 HOH 233 733 727 HOH HOH A . HB 11 HOH 234 734 770 HOH HOH A . HB 11 HOH 235 735 644 HOH HOH A . HB 11 HOH 236 736 554 HOH HOH A . HB 11 HOH 237 737 759 HOH HOH A . HB 11 HOH 238 738 742 HOH HOH A . HB 11 HOH 239 739 786 HOH HOH A . HB 11 HOH 240 740 785 HOH HOH A . HB 11 HOH 241 741 555 HOH HOH A . HB 11 HOH 242 742 647 HOH HOH A . HB 11 HOH 243 743 732 HOH HOH A . HB 11 HOH 244 744 736 HOH HOH A . HB 11 HOH 245 745 707 HOH HOH A . HB 11 HOH 246 746 760 HOH HOH A . HB 11 HOH 247 747 715 HOH HOH A . HB 11 HOH 248 748 655 HOH HOH A . HB 11 HOH 249 749 556 HOH HOH A . HB 11 HOH 250 750 557 HOH HOH A . HB 11 HOH 251 751 696 HOH HOH A . HB 11 HOH 252 752 753 HOH HOH A . HB 11 HOH 253 753 778 HOH HOH A . HB 11 HOH 254 754 780 HOH HOH A . HB 11 HOH 255 755 747 HOH HOH A . HB 11 HOH 256 756 787 HOH HOH A . HB 11 HOH 257 757 779 HOH HOH A . HB 11 HOH 258 758 792 HOH HOH A . HB 11 HOH 259 759 791 HOH HOH A . HB 11 HOH 260 760 558 HOH HOH A . HB 11 HOH 261 761 701 HOH HOH A . HB 11 HOH 262 762 559 HOH HOH A . HB 11 HOH 263 763 728 HOH HOH A . HB 11 HOH 264 764 681 HOH HOH A . HB 11 HOH 265 765 560 HOH HOH A . HB 11 HOH 266 766 561 HOH HOH A . HB 11 HOH 267 767 773 HOH HOH A . HB 11 HOH 268 768 654 HOH HOH A . HB 11 HOH 269 769 562 HOH HOH A . HB 11 HOH 270 770 713 HOH HOH A . HB 11 HOH 271 771 731 HOH HOH A . HB 11 HOH 272 772 563 HOH HOH A . HB 11 HOH 273 773 783 HOH HOH A . HB 11 HOH 274 774 729 HOH HOH A . HB 11 HOH 275 775 564 HOH HOH A . HB 11 HOH 276 776 709 HOH HOH A . HB 11 HOH 277 777 724 HOH HOH A . HB 11 HOH 278 778 697 HOH HOH A . HB 11 HOH 279 779 748 HOH HOH A . HB 11 HOH 280 780 757 HOH HOH A . HB 11 HOH 281 781 790 HOH HOH A . HB 11 HOH 282 782 784 HOH HOH A . HB 11 HOH 283 783 591 HOH HOH A . HB 11 HOH 284 784 565 HOH HOH A . HB 11 HOH 285 785 788 HOH HOH A . HB 11 HOH 286 786 775 HOH HOH A . HB 11 HOH 287 787 698 HOH HOH A . HB 11 HOH 288 788 789 HOH HOH A . HB 11 HOH 289 789 664 HOH HOH A . HB 11 HOH 290 790 699 HOH HOH A . HB 11 HOH 291 791 589 HOH HOH A . HB 11 HOH 292 792 749 HOH HOH A . HB 11 HOH 293 793 650 HOH HOH A . IB 11 HOH 1 501 757 HOH HOH B . IB 11 HOH 2 502 609 HOH HOH B . IB 11 HOH 3 503 614 HOH HOH B . IB 11 HOH 4 504 501 HOH HOH B . IB 11 HOH 5 505 765 HOH HOH B . IB 11 HOH 6 506 574 HOH HOH B . IB 11 HOH 7 507 502 HOH HOH B . IB 11 HOH 8 508 503 HOH HOH B . IB 11 HOH 9 509 587 HOH HOH B . IB 11 HOH 10 510 651 HOH HOH B . IB 11 HOH 11 511 709 HOH HOH B . IB 11 HOH 12 512 504 HOH HOH B . IB 11 HOH 13 513 714 HOH HOH B . IB 11 HOH 14 514 505 HOH HOH B . IB 11 HOH 15 515 634 HOH HOH B . IB 11 HOH 16 516 740 HOH HOH B . IB 11 HOH 17 517 506 HOH HOH B . IB 11 HOH 18 518 567 HOH HOH B . IB 11 HOH 19 519 507 HOH HOH B . IB 11 HOH 20 520 579 HOH HOH B . IB 11 HOH 21 521 642 HOH HOH B . IB 11 HOH 22 522 598 HOH HOH B . IB 11 HOH 23 523 784 HOH HOH B . IB 11 HOH 24 524 508 HOH HOH B . IB 11 HOH 25 525 783 HOH HOH B . IB 11 HOH 26 526 509 HOH HOH B . IB 11 HOH 27 527 617 HOH HOH B . IB 11 HOH 28 528 628 HOH HOH B . IB 11 HOH 29 529 780 HOH HOH B . IB 11 HOH 30 530 615 HOH HOH B . IB 11 HOH 31 531 597 HOH HOH B . IB 11 HOH 32 532 569 HOH HOH B . IB 11 HOH 33 533 644 HOH HOH B . IB 11 HOH 34 534 732 HOH HOH B . IB 11 HOH 35 535 580 HOH HOH B . IB 11 HOH 36 536 626 HOH HOH B . IB 11 HOH 37 537 562 HOH HOH B . IB 11 HOH 38 538 739 HOH HOH B . IB 11 HOH 39 539 636 HOH HOH B . IB 11 HOH 40 540 661 HOH HOH B . IB 11 HOH 41 541 573 HOH HOH B . IB 11 HOH 42 542 586 HOH HOH B . IB 11 HOH 43 543 602 HOH HOH B . IB 11 HOH 44 544 510 HOH HOH B . IB 11 HOH 45 545 676 HOH HOH B . IB 11 HOH 46 546 578 HOH HOH B . IB 11 HOH 47 547 511 HOH HOH B . IB 11 HOH 48 548 681 HOH HOH B . IB 11 HOH 49 549 572 HOH HOH B . IB 11 HOH 50 550 590 HOH HOH B . IB 11 HOH 51 551 652 HOH HOH B . IB 11 HOH 52 552 604 HOH HOH B . IB 11 HOH 53 553 512 HOH HOH B . IB 11 HOH 54 554 568 HOH HOH B . IB 11 HOH 55 555 653 HOH HOH B . IB 11 HOH 56 556 685 HOH HOH B . IB 11 HOH 57 557 513 HOH HOH B . IB 11 HOH 58 558 625 HOH HOH B . IB 11 HOH 59 559 566 HOH HOH B . IB 11 HOH 60 560 577 HOH HOH B . IB 11 HOH 61 561 643 HOH HOH B . IB 11 HOH 62 562 588 HOH HOH B . IB 11 HOH 63 563 514 HOH HOH B . IB 11 HOH 64 564 645 HOH HOH B . IB 11 HOH 65 565 624 HOH HOH B . IB 11 HOH 66 566 564 HOH HOH B . IB 11 HOH 67 567 576 HOH HOH B . IB 11 HOH 68 568 612 HOH HOH B . IB 11 HOH 69 569 583 HOH HOH B . IB 11 HOH 70 570 571 HOH HOH B . IB 11 HOH 71 571 589 HOH HOH B . IB 11 HOH 72 572 607 HOH HOH B . IB 11 HOH 73 573 606 HOH HOH B . IB 11 HOH 74 574 662 HOH HOH B . IB 11 HOH 75 575 735 HOH HOH B . IB 11 HOH 76 576 620 HOH HOH B . IB 11 HOH 77 577 591 HOH HOH B . IB 11 HOH 78 578 582 HOH HOH B . IB 11 HOH 79 579 515 HOH HOH B . IB 11 HOH 80 580 516 HOH HOH B . IB 11 HOH 81 581 563 HOH HOH B . IB 11 HOH 82 582 575 HOH HOH B . IB 11 HOH 83 583 675 HOH HOH B . IB 11 HOH 84 584 699 HOH HOH B . IB 11 HOH 85 585 613 HOH HOH B . IB 11 HOH 86 586 742 HOH HOH B . IB 11 HOH 87 587 639 HOH HOH B . IB 11 HOH 88 588 611 HOH HOH B . IB 11 HOH 89 589 565 HOH HOH B . IB 11 HOH 90 590 715 HOH HOH B . IB 11 HOH 91 591 561 HOH HOH B . IB 11 HOH 92 592 666 HOH HOH B . IB 11 HOH 93 593 585 HOH HOH B . IB 11 HOH 94 594 599 HOH HOH B . IB 11 HOH 95 595 517 HOH HOH B . IB 11 HOH 96 596 622 HOH HOH B . IB 11 HOH 97 597 654 HOH HOH B . IB 11 HOH 98 598 518 HOH HOH B . IB 11 HOH 99 599 719 HOH HOH B . IB 11 HOH 100 600 703 HOH HOH B . IB 11 HOH 101 601 737 HOH HOH B . IB 11 HOH 102 602 785 HOH HOH B . IB 11 HOH 103 603 631 HOH HOH B . IB 11 HOH 104 604 621 HOH HOH B . IB 11 HOH 105 605 649 HOH HOH B . IB 11 HOH 106 606 519 HOH HOH B . IB 11 HOH 107 607 671 HOH HOH B . IB 11 HOH 108 608 520 HOH HOH B . IB 11 HOH 109 609 619 HOH HOH B . IB 11 HOH 110 610 521 HOH HOH B . IB 11 HOH 111 611 522 HOH HOH B . IB 11 HOH 112 612 640 HOH HOH B . IB 11 HOH 113 613 725 HOH HOH B . IB 11 HOH 114 614 616 HOH HOH B . IB 11 HOH 115 615 610 HOH HOH B . IB 11 HOH 116 616 728 HOH HOH B . IB 11 HOH 117 617 584 HOH HOH B . IB 11 HOH 118 618 523 HOH HOH B . IB 11 HOH 119 619 726 HOH HOH B . IB 11 HOH 120 620 570 HOH HOH B . IB 11 HOH 121 621 601 HOH HOH B . IB 11 HOH 122 622 593 HOH HOH B . IB 11 HOH 123 623 698 HOH HOH B . IB 11 HOH 124 624 656 HOH HOH B . IB 11 HOH 125 625 710 HOH HOH B . IB 11 HOH 126 626 655 HOH HOH B . IB 11 HOH 127 627 594 HOH HOH B . IB 11 HOH 128 628 660 HOH HOH B . IB 11 HOH 129 629 674 HOH HOH B . IB 11 HOH 130 630 722 HOH HOH B . IB 11 HOH 131 631 524 HOH HOH B . IB 11 HOH 132 632 525 HOH HOH B . IB 11 HOH 133 633 630 HOH HOH B . IB 11 HOH 134 634 692 HOH HOH B . IB 11 HOH 135 635 623 HOH HOH B . IB 11 HOH 136 636 526 HOH HOH B . IB 11 HOH 137 637 527 HOH HOH B . IB 11 HOH 138 638 658 HOH HOH B . IB 11 HOH 139 639 638 HOH HOH B . IB 11 HOH 140 640 581 HOH HOH B . IB 11 HOH 141 641 664 HOH HOH B . IB 11 HOH 142 642 712 HOH HOH B . IB 11 HOH 143 643 647 HOH HOH B . IB 11 HOH 144 644 753 HOH HOH B . IB 11 HOH 145 645 718 HOH HOH B . IB 11 HOH 146 646 528 HOH HOH B . IB 11 HOH 147 647 629 HOH HOH B . IB 11 HOH 148 648 600 HOH HOH B . IB 11 HOH 149 649 595 HOH HOH B . IB 11 HOH 150 650 529 HOH HOH B . IB 11 HOH 151 651 530 HOH HOH B . IB 11 HOH 152 652 596 HOH HOH B . IB 11 HOH 153 653 730 HOH HOH B . IB 11 HOH 154 654 667 HOH HOH B . IB 11 HOH 155 655 668 HOH HOH B . IB 11 HOH 156 656 657 HOH HOH B . IB 11 HOH 157 657 531 HOH HOH B . IB 11 HOH 158 658 532 HOH HOH B . IB 11 HOH 159 659 637 HOH HOH B . IB 11 HOH 160 660 689 HOH HOH B . IB 11 HOH 161 661 533 HOH HOH B . IB 11 HOH 162 662 534 HOH HOH B . IB 11 HOH 163 663 650 HOH HOH B . IB 11 HOH 164 664 756 HOH HOH B . IB 11 HOH 165 665 727 HOH HOH B . IB 11 HOH 166 666 641 HOH HOH B . IB 11 HOH 167 667 767 HOH HOH B . IB 11 HOH 168 668 687 HOH HOH B . IB 11 HOH 169 669 731 HOH HOH B . IB 11 HOH 170 670 700 HOH HOH B . IB 11 HOH 171 671 697 HOH HOH B . IB 11 HOH 172 672 696 HOH HOH B . IB 11 HOH 173 673 688 HOH HOH B . IB 11 HOH 174 674 627 HOH HOH B . IB 11 HOH 175 675 751 HOH HOH B . IB 11 HOH 176 676 632 HOH HOH B . IB 11 HOH 177 677 669 HOH HOH B . IB 11 HOH 178 678 734 HOH HOH B . IB 11 HOH 179 679 786 HOH HOH B . IB 11 HOH 180 680 535 HOH HOH B . IB 11 HOH 181 681 536 HOH HOH B . IB 11 HOH 182 682 693 HOH HOH B . IB 11 HOH 183 683 755 HOH HOH B . IB 11 HOH 184 684 605 HOH HOH B . IB 11 HOH 185 685 759 HOH HOH B . IB 11 HOH 186 686 608 HOH HOH B . IB 11 HOH 187 687 764 HOH HOH B . IB 11 HOH 188 688 603 HOH HOH B . IB 11 HOH 189 689 673 HOH HOH B . IB 11 HOH 190 690 777 HOH HOH B . IB 11 HOH 191 691 748 HOH HOH B . IB 11 HOH 192 692 537 HOH HOH B . IB 11 HOH 193 693 729 HOH HOH B . IB 11 HOH 194 694 538 HOH HOH B . IB 11 HOH 195 695 646 HOH HOH B . IB 11 HOH 196 696 539 HOH HOH B . IB 11 HOH 197 697 736 HOH HOH B . IB 11 HOH 198 698 694 HOH HOH B . IB 11 HOH 199 699 749 HOH HOH B . IB 11 HOH 200 700 540 HOH HOH B . IB 11 HOH 201 701 747 HOH HOH B . IB 11 HOH 202 702 677 HOH HOH B . IB 11 HOH 203 703 635 HOH HOH B . IB 11 HOH 204 704 695 HOH HOH B . IB 11 HOH 205 705 713 HOH HOH B . IB 11 HOH 206 706 766 HOH HOH B . IB 11 HOH 207 707 541 HOH HOH B . IB 11 HOH 208 708 750 HOH HOH B . IB 11 HOH 209 709 542 HOH HOH B . IB 11 HOH 210 710 684 HOH HOH B . IB 11 HOH 211 711 680 HOH HOH B . IB 11 HOH 212 712 763 HOH HOH B . IB 11 HOH 213 713 746 HOH HOH B . IB 11 HOH 214 714 543 HOH HOH B . IB 11 HOH 215 715 706 HOH HOH B . IB 11 HOH 216 716 544 HOH HOH B . IB 11 HOH 217 717 545 HOH HOH B . IB 11 HOH 218 718 787 HOH HOH B . IB 11 HOH 219 719 744 HOH HOH B . IB 11 HOH 220 720 771 HOH HOH B . IB 11 HOH 221 721 760 HOH HOH B . IB 11 HOH 222 722 546 HOH HOH B . IB 11 HOH 223 723 704 HOH HOH B . IB 11 HOH 224 724 758 HOH HOH B . IB 11 HOH 225 725 720 HOH HOH B . IB 11 HOH 226 726 708 HOH HOH B . IB 11 HOH 227 727 592 HOH HOH B . IB 11 HOH 228 728 547 HOH HOH B . IB 11 HOH 229 729 686 HOH HOH B . IB 11 HOH 230 730 659 HOH HOH B . IB 11 HOH 231 731 548 HOH HOH B . IB 11 HOH 232 732 648 HOH HOH B . IB 11 HOH 233 733 672 HOH HOH B . IB 11 HOH 234 734 549 HOH HOH B . IB 11 HOH 235 735 741 HOH HOH B . IB 11 HOH 236 736 550 HOH HOH B . IB 11 HOH 237 737 551 HOH HOH B . IB 11 HOH 238 738 552 HOH HOH B . IB 11 HOH 239 739 776 HOH HOH B . IB 11 HOH 240 740 553 HOH HOH B . IB 11 HOH 241 741 554 HOH HOH B . IB 11 HOH 242 742 690 HOH HOH B . IB 11 HOH 243 743 678 HOH HOH B . IB 11 HOH 244 744 778 HOH HOH B . IB 11 HOH 245 745 762 HOH HOH B . IB 11 HOH 246 746 555 HOH HOH B . IB 11 HOH 247 747 701 HOH HOH B . IB 11 HOH 248 748 723 HOH HOH B . IB 11 HOH 249 749 556 HOH HOH B . IB 11 HOH 250 750 670 HOH HOH B . IB 11 HOH 251 751 782 HOH HOH B . IB 11 HOH 252 752 781 HOH HOH B . IB 11 HOH 253 753 770 HOH HOH B . IB 11 HOH 254 754 618 HOH HOH B . IB 11 HOH 255 755 683 HOH HOH B . IB 11 HOH 256 756 721 HOH HOH B . IB 11 HOH 257 757 788 HOH HOH B . IB 11 HOH 258 758 691 HOH HOH B . IB 11 HOH 259 759 745 HOH HOH B . IB 11 HOH 260 760 557 HOH HOH B . IB 11 HOH 261 761 702 HOH HOH B . IB 11 HOH 262 762 707 HOH HOH B . IB 11 HOH 263 763 633 HOH HOH B . IB 11 HOH 264 764 779 HOH HOH B . IB 11 HOH 265 765 724 HOH HOH B . IB 11 HOH 266 766 769 HOH HOH B . IB 11 HOH 267 767 558 HOH HOH B . IB 11 HOH 268 768 743 HOH HOH B . IB 11 HOH 269 769 775 HOH HOH B . IB 11 HOH 270 770 717 HOH HOH B . IB 11 HOH 271 771 559 HOH HOH B . IB 11 HOH 272 772 682 HOH HOH B . IB 11 HOH 273 773 768 HOH HOH B . IB 11 HOH 274 774 705 HOH HOH B . IB 11 HOH 275 775 663 HOH HOH B . IB 11 HOH 276 776 716 HOH HOH B . IB 11 HOH 277 777 738 HOH HOH B . IB 11 HOH 278 778 752 HOH HOH B . IB 11 HOH 279 779 733 HOH HOH B . IB 11 HOH 280 780 560 HOH HOH B . IB 11 HOH 281 781 774 HOH HOH B . IB 11 HOH 282 782 711 HOH HOH B . IB 11 HOH 283 783 761 HOH HOH B . IB 11 HOH 284 784 665 HOH HOH B . IB 11 HOH 285 785 772 HOH HOH B . IB 11 HOH 286 786 679 HOH HOH B . IB 11 HOH 287 787 754 HOH HOH B . IB 11 HOH 288 788 773 HOH HOH B . # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PISA monomeric 1 2 author_and_software_defined_assembly PISA monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HB 2 1 B,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,IB # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OD1 ? A ASP 80 ? A ASP 106 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? IB HOH . ? B HOH 551 ? 1_555 82.9 ? 2 OD1 ? A ASP 80 ? A ASP 106 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? IB HOH . ? B HOH 555 ? 1_555 94.5 ? 3 O ? IB HOH . ? B HOH 551 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? IB HOH . ? B HOH 555 ? 1_555 177.3 ? 4 OD1 ? A ASP 80 ? A ASP 106 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? IB HOH . ? B HOH 597 ? 1_555 90.2 ? 5 O ? IB HOH . ? B HOH 551 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? IB HOH . ? B HOH 597 ? 1_555 88.6 ? 6 O ? IB HOH . ? B HOH 555 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? IB HOH . ? B HOH 597 ? 1_555 90.8 ? 7 OD1 ? A ASP 80 ? A ASP 106 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 554 ? 1_555 87.0 ? 8 O ? IB HOH . ? B HOH 551 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 554 ? 1_555 98.1 ? 9 O ? IB HOH . ? B HOH 555 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 554 ? 1_555 82.4 ? 10 O ? IB HOH . ? B HOH 597 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 554 ? 1_555 172.4 ? 11 OD1 ? A ASP 80 ? A ASP 106 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 677 ? 1_555 173.8 ? 12 O ? IB HOH . ? B HOH 551 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 677 ? 1_555 91.1 ? 13 O ? IB HOH . ? B HOH 555 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 677 ? 1_555 91.5 ? 14 O ? IB HOH . ? B HOH 597 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 677 ? 1_555 90.9 ? 15 O ? HB HOH . ? A HOH 554 ? 1_555 MG ? Z MG . ? A MG 424 ? 1_555 O ? HB HOH . ? A HOH 677 ? 1_555 92.7 ? 16 O ? HB HOH . ? A HOH 536 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? IB HOH . ? B HOH 502 ? 1_555 80.7 ? 17 O ? HB HOH . ? A HOH 536 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? IB HOH . ? B HOH 572 ? 1_555 83.9 ? 18 O ? IB HOH . ? B HOH 502 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? IB HOH . ? B HOH 572 ? 1_555 92.5 ? 19 O ? HB HOH . ? A HOH 536 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? IB HOH . ? B HOH 686 ? 1_555 92.0 ? 20 O ? IB HOH . ? B HOH 502 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? IB HOH . ? B HOH 686 ? 1_555 172.1 ? 21 O ? IB HOH . ? B HOH 572 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? IB HOH . ? B HOH 686 ? 1_555 89.8 ? 22 O ? HB HOH . ? A HOH 536 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 587 ? 1_555 86.9 ? 23 O ? IB HOH . ? B HOH 502 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 587 ? 1_555 94.8 ? 24 O ? IB HOH . ? B HOH 572 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 587 ? 1_555 167.2 ? 25 O ? IB HOH . ? B HOH 686 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 587 ? 1_555 81.7 ? 26 O ? HB HOH . ? A HOH 536 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 524 ? 1_555 173.7 ? 27 O ? IB HOH . ? B HOH 502 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 524 ? 1_555 94.4 ? 28 O ? IB HOH . ? B HOH 572 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 524 ? 1_555 100.4 ? 29 O ? IB HOH . ? B HOH 686 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 524 ? 1_555 92.7 ? 30 O ? HB HOH . ? A HOH 587 ? 1_555 MG ? AB MG . ? B MG 420 ? 1_555 O ? HB HOH . ? A HOH 524 ? 1_555 89.6 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2015-02-11 2 'Structure model' 1 1 2015-04-01 3 'Structure model' 1 2 2015-04-22 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Atomic model' 2 3 'Structure model' 'Derived calculations' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -20.8534 13.1513 -37.4753 0.1370 0.0538 0.1607 -0.0019 0.0079 -0.0040 0.9928 1.4265 1.9049 0.5126 0.2897 0.4494 0.0074 0.0273 0.0387 -0.0665 0.0146 -0.1040 -0.1809 0.0509 -0.0089 'X-RAY DIFFRACTION' 2 ? refined -20.8011 24.6336 -26.3349 0.2639 0.0463 0.2292 -0.0139 0.0019 -0.0204 0.6713 1.0040 0.5923 -0.0588 -0.0118 0.3028 -0.0033 -0.0493 0.2122 0.0754 -0.0244 -0.0512 -0.2400 0.0641 0.0390 'X-RAY DIFFRACTION' 3 ? refined -28.0082 13.8818 -20.7658 0.1660 0.0768 0.1345 0.0232 0.0201 -0.0174 1.5468 3.6963 1.2505 -0.3928 0.1154 0.0173 -0.0497 -0.1728 0.0741 0.1997 0.0706 0.1570 -0.1260 -0.0457 -0.0121 'X-RAY DIFFRACTION' 4 ? refined -31.1801 0.2669 -24.1263 0.1433 0.0990 0.1273 -0.0422 0.0175 -0.0075 2.2839 3.5879 2.6135 -0.7289 -0.2034 0.3917 -0.0395 -0.1557 -0.1965 0.1606 0.0159 0.1897 0.2755 -0.1707 0.0004 'X-RAY DIFFRACTION' 5 ? refined -21.5731 5.9842 -64.4093 0.1034 0.1541 0.1339 -0.0019 -0.0083 0.0111 1.6733 0.9743 1.9765 0.4323 0.3824 0.4501 -0.0391 0.2403 0.2089 -0.0701 0.1000 -0.0210 -0.2460 0.1977 -0.0654 'X-RAY DIFFRACTION' 6 ? refined -12.7012 2.7281 -77.6581 0.0829 0.4351 0.1908 -0.0265 0.0402 -0.0552 1.9407 0.3265 1.2716 -0.0628 0.0668 0.0517 -0.0033 0.5510 0.0267 -0.0944 0.1106 -0.1199 -0.1255 0.4731 -0.0285 'X-RAY DIFFRACTION' 7 ? refined -24.5006 -4.4667 -78.7446 0.0695 0.3027 0.1762 0.0458 -0.0047 -0.0830 3.2530 0.4323 0.1626 -0.5288 -0.3159 0.0483 0.0530 0.4686 -0.1320 -0.0899 0.0537 -0.0651 0.0878 0.2257 -0.0176 'X-RAY DIFFRACTION' 8 ? refined -37.2048 -5.3226 -71.7845 0.0617 0.0928 0.0990 -0.0114 -0.0077 -0.0024 4.0792 1.9321 2.5279 -1.0469 0.6898 0.5000 0.0162 -0.0434 -0.1086 0.0248 0.0878 0.0058 0.0835 -0.0682 -0.0766 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESI 30:175' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESI 176:223' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESI 224:273' 'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESI 274:347' 'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? 'CHAIN B AND RESI 27:175' 'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? 'CHAIN B AND RESI 176:223' 'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? 'CHAIN B AND RESI 224:273' 'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? 'CHAIN B AND RESI 274:346' # 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 ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(PHENIX.REFINE: 1.9_1692)' 1 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? BALBES ? ? ? . 4 ? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 5 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A HOH 576 ? ? O A HOH 668 ? ? 1.99 2 1 O B HOH 599 ? ? O B HOH 645 ? ? 1.99 3 1 O A HOH 598 ? ? O A HOH 607 ? ? 2.08 4 1 O A HOH 608 ? ? O A HOH 769 ? ? 2.14 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 O _pdbx_validate_symm_contact.auth_asym_id_1 B _pdbx_validate_symm_contact.auth_comp_id_1 HOH _pdbx_validate_symm_contact.auth_seq_id_1 611 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 O _pdbx_validate_symm_contact.auth_asym_id_2 B _pdbx_validate_symm_contact.auth_comp_id_2 HOH _pdbx_validate_symm_contact.auth_seq_id_2 680 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 1_655 _pdbx_validate_symm_contact.dist 2.19 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 76 ? ? -138.88 -32.76 2 1 ASP A 106 ? ? 37.23 54.41 3 1 GLU A 265 ? ? -143.83 44.67 4 1 ILE A 308 ? ? -108.53 -60.17 5 1 LEU A 326 ? ? -100.75 -167.84 6 1 ASN B 76 ? ? -143.31 -28.80 7 1 ASN B 88 ? ? 59.15 19.10 8 1 HIS B 112 ? ? -163.90 117.82 9 1 GLU B 171 ? ? -78.10 38.92 10 1 GLU B 265 ? ? -142.56 43.84 11 1 ILE B 308 ? ? -105.14 -61.49 12 1 LEU B 326 ? ? -100.18 -167.19 # 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 ? B HOH 787 ? 5.85 . 2 1 O ? B HOH 788 ? 7.04 . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 N 1 A P6G 426 ? O1 ? BA P6G 1 O1 2 1 N 1 A P6G 427 ? O1 ? CA P6G 1 O1 3 1 N 1 A P6G 427 ? C2 ? CA P6G 1 C2 4 1 N 1 A P6G 427 ? C3 ? CA P6G 1 C3 5 1 N 1 A P6G 427 ? C17 ? CA P6G 1 C17 6 1 N 1 A P6G 427 ? C18 ? CA P6G 1 C18 7 1 N 1 A P6G 427 ? O19 ? CA P6G 1 O19 # 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 PRO 27 ? A PRO 1 2 1 Y 1 A THR 28 ? A THR 2 3 1 Y 1 A SER 29 ? A SER 3 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 'UNKNOWN ATOM OR ION' UNX 3 N-ACETYL-D-GLUCOSAMINE NAG 4 BETA-D-MANNOSE BMA 5 ALPHA-D-MANNOSE MAN 6 'MAGNESIUM ION' MG 7 'DI(HYDROXYETHYL)ETHER' PEG 8 'HEXAETHYLENE GLYCOL' P6G 9 GLYCEROL GOL 10 'CHLORIDE ION' CL 11 water HOH #