data_4X95 # _entry.id 4X95 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4X95 WWPDB D_1000205264 # loop_ _pdbx_database_related.db_name _pdbx_database_related.details _pdbx_database_related.db_id _pdbx_database_related.content_type PDB . 4X90 unspecified PDB . 4X91 unspecified PDB . 4X92 unspecified PDB . 4X93 unspecified PDB . 4X94 unspecified PDB . 4X96 unspecified PDB . 4X97 unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.entry_id 4X95 _pdbx_database_status.recvd_initial_deposition_date 2014-12-11 _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 'Glukhova, A.' 1 'Tesmer, J.J.G.' 2 # _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 UK _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'Nat Commun' _citation.journal_id_ASTM ? _citation.journal_id_CSD ? _citation.journal_id_ISSN 2041-1723 _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 6 _citation.language ? _citation.page_first 6250 _citation.page_last 6250 _citation.title 'Structure and function of lysosomal phospholipase A2 and lecithin:cholesterol acyltransferase.' _citation.year 2015 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1038/ncomms7250 _citation.pdbx_database_id_PubMed 25727495 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Glukhova, A.' 1 primary 'Hinkovska-Galcheva, V.' 2 primary 'Kelly, R.' 3 primary 'Abe, A.' 4 primary 'Shayman, J.A.' 5 primary 'Tesmer, J.J.' 6 # _cell.length_a 72.385 _cell.length_b 125.275 _cell.length_c 140.215 _cell.angle_alpha 90.000 _cell.angle_beta 90.000 _cell.angle_gamma 90.000 _cell.entry_id 4X95 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.space_group_name_H-M 'P 2 21 21' _symmetry.entry_id 4X95 _symmetry.Int_Tables_number 18 _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? # 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 'Group XV phospholipase A2' 43121.027 2 2.3.1.- ? 'UNP residues 34-412' ? 2 non-polymer syn N-ACETYL-D-GLUCOSAMINE 221.208 10 ? ? ? ? 3 non-polymer man BETA-D-MANNOSE 180.156 2 ? ? ? ? 4 non-polymer syn 'METHYL ARACHIDONYL FLUOROPHOSPHONATE' 370.482 2 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name '1-O-acylceramide synthase,ACS,LCAT-like lysophospholipase,LLPL,Lysophospholipase 3,Lysosomal phospholipase A2,LPLA2' # _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 ;GAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVD VRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPV VLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY NYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDP KICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP ; _entity_poly.pdbx_seq_one_letter_code_can ;GAGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVD VRVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPV VLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPY NYTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDP KICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 ALA n 1 3 GLY n 1 4 ARG n 1 5 HIS n 1 6 PRO n 1 7 PRO n 1 8 VAL n 1 9 VAL n 1 10 LEU n 1 11 VAL n 1 12 PRO n 1 13 GLY n 1 14 ASP n 1 15 LEU n 1 16 GLY n 1 17 ASN n 1 18 GLN n 1 19 LEU n 1 20 GLU n 1 21 ALA n 1 22 LYS n 1 23 LEU n 1 24 ASP n 1 25 LYS n 1 26 PRO n 1 27 THR n 1 28 VAL n 1 29 VAL n 1 30 HIS n 1 31 TYR n 1 32 LEU n 1 33 CYS n 1 34 SER n 1 35 LYS n 1 36 LYS n 1 37 THR n 1 38 GLU n 1 39 SER n 1 40 TYR n 1 41 PHE n 1 42 THR n 1 43 ILE n 1 44 TRP n 1 45 LEU n 1 46 ASN n 1 47 LEU n 1 48 GLU n 1 49 LEU n 1 50 LEU n 1 51 LEU n 1 52 PRO n 1 53 VAL n 1 54 ILE n 1 55 ILE n 1 56 ASP n 1 57 CYS n 1 58 TRP n 1 59 ILE n 1 60 ASP n 1 61 ASN n 1 62 ILE n 1 63 ARG n 1 64 LEU n 1 65 VAL n 1 66 TYR n 1 67 ASN n 1 68 LYS n 1 69 THR n 1 70 SER n 1 71 ARG n 1 72 ALA n 1 73 THR n 1 74 GLN n 1 75 PHE n 1 76 PRO n 1 77 ASP n 1 78 GLY n 1 79 VAL n 1 80 ASP n 1 81 VAL n 1 82 ARG n 1 83 VAL n 1 84 PRO n 1 85 GLY n 1 86 PHE n 1 87 GLY n 1 88 LYS n 1 89 THR n 1 90 PHE n 1 91 SER n 1 92 LEU n 1 93 GLU n 1 94 PHE n 1 95 LEU n 1 96 ASP n 1 97 PRO n 1 98 SER n 1 99 LYS n 1 100 SER n 1 101 SER n 1 102 VAL n 1 103 GLY n 1 104 SER n 1 105 TYR n 1 106 PHE n 1 107 HIS n 1 108 THR n 1 109 MET n 1 110 VAL n 1 111 GLU n 1 112 SER n 1 113 LEU n 1 114 VAL n 1 115 GLY n 1 116 TRP n 1 117 GLY n 1 118 TYR n 1 119 THR n 1 120 ARG n 1 121 GLY n 1 122 GLU n 1 123 ASP n 1 124 VAL n 1 125 ARG n 1 126 GLY n 1 127 ALA n 1 128 PRO n 1 129 TYR n 1 130 ASP n 1 131 TRP n 1 132 ARG n 1 133 ARG n 1 134 ALA n 1 135 PRO n 1 136 ASN n 1 137 GLU n 1 138 ASN n 1 139 GLY n 1 140 PRO n 1 141 TYR n 1 142 PHE n 1 143 LEU n 1 144 ALA n 1 145 LEU n 1 146 ARG n 1 147 GLU n 1 148 MET n 1 149 ILE n 1 150 GLU n 1 151 GLU n 1 152 MET n 1 153 TYR n 1 154 GLN n 1 155 LEU n 1 156 TYR n 1 157 GLY n 1 158 GLY n 1 159 PRO n 1 160 VAL n 1 161 VAL n 1 162 LEU n 1 163 VAL n 1 164 ALA n 1 165 HIS n 1 166 SER n 1 167 MET n 1 168 GLY n 1 169 ASN n 1 170 MET n 1 171 TYR n 1 172 THR n 1 173 LEU n 1 174 TYR n 1 175 PHE n 1 176 LEU n 1 177 GLN n 1 178 ARG n 1 179 GLN n 1 180 PRO n 1 181 GLN n 1 182 ALA n 1 183 TRP n 1 184 LYS n 1 185 ASP n 1 186 LYS n 1 187 TYR n 1 188 ILE n 1 189 ARG n 1 190 ALA n 1 191 PHE n 1 192 VAL n 1 193 SER n 1 194 LEU n 1 195 GLY n 1 196 ALA n 1 197 PRO n 1 198 TRP n 1 199 GLY n 1 200 GLY n 1 201 VAL n 1 202 ALA n 1 203 LYS n 1 204 THR n 1 205 LEU n 1 206 ARG n 1 207 VAL n 1 208 LEU n 1 209 ALA n 1 210 SER n 1 211 GLY n 1 212 ASP n 1 213 ASN n 1 214 ASN n 1 215 ARG n 1 216 ILE n 1 217 PRO n 1 218 VAL n 1 219 ILE n 1 220 GLY n 1 221 PRO n 1 222 LEU n 1 223 LYS n 1 224 ILE n 1 225 ARG n 1 226 GLU n 1 227 GLN n 1 228 GLN n 1 229 ARG n 1 230 SER n 1 231 ALA n 1 232 VAL n 1 233 SER n 1 234 THR n 1 235 SER n 1 236 TRP n 1 237 LEU n 1 238 LEU n 1 239 PRO n 1 240 TYR n 1 241 ASN n 1 242 TYR n 1 243 THR n 1 244 TRP n 1 245 SER n 1 246 PRO n 1 247 GLU n 1 248 LYS n 1 249 VAL n 1 250 PHE n 1 251 VAL n 1 252 GLN n 1 253 THR n 1 254 PRO n 1 255 THR n 1 256 ILE n 1 257 ASN n 1 258 TYR n 1 259 THR n 1 260 LEU n 1 261 ARG n 1 262 ASP n 1 263 TYR n 1 264 ARG n 1 265 LYS n 1 266 PHE n 1 267 PHE n 1 268 GLN n 1 269 ASP n 1 270 ILE n 1 271 GLY n 1 272 PHE n 1 273 GLU n 1 274 ASP n 1 275 GLY n 1 276 TRP n 1 277 LEU n 1 278 MET n 1 279 ARG n 1 280 GLN n 1 281 ASP n 1 282 THR n 1 283 GLU n 1 284 GLY n 1 285 LEU n 1 286 VAL n 1 287 GLU n 1 288 ALA n 1 289 THR n 1 290 MET n 1 291 PRO n 1 292 PRO n 1 293 GLY n 1 294 VAL n 1 295 GLN n 1 296 LEU n 1 297 HIS n 1 298 CYS n 1 299 LEU n 1 300 TYR n 1 301 GLY n 1 302 THR n 1 303 GLY n 1 304 VAL n 1 305 PRO n 1 306 THR n 1 307 PRO n 1 308 ASP n 1 309 SER n 1 310 PHE n 1 311 TYR n 1 312 TYR n 1 313 GLU n 1 314 SER n 1 315 PHE n 1 316 PRO n 1 317 ASP n 1 318 ARG n 1 319 ASP n 1 320 PRO n 1 321 LYS n 1 322 ILE n 1 323 CYS n 1 324 PHE n 1 325 GLY n 1 326 ASP n 1 327 GLY n 1 328 ASP n 1 329 GLY n 1 330 THR n 1 331 VAL n 1 332 ASN n 1 333 LEU n 1 334 LYS n 1 335 SER n 1 336 ALA n 1 337 LEU n 1 338 GLN n 1 339 CYS n 1 340 GLN n 1 341 ALA n 1 342 TRP n 1 343 GLN n 1 344 SER n 1 345 ARG n 1 346 GLN n 1 347 GLU n 1 348 HIS n 1 349 GLN n 1 350 VAL n 1 351 LEU n 1 352 LEU n 1 353 GLN n 1 354 GLU n 1 355 LEU n 1 356 PRO n 1 357 GLY n 1 358 SER n 1 359 GLU n 1 360 HIS n 1 361 ILE n 1 362 GLU n 1 363 MET n 1 364 LEU n 1 365 ALA n 1 366 ASN n 1 367 ALA n 1 368 THR n 1 369 THR n 1 370 LEU n 1 371 ALA n 1 372 TYR n 1 373 LEU n 1 374 LYS n 1 375 ARG n 1 376 VAL n 1 377 LEU n 1 378 LEU n 1 379 GLY n 1 380 PRO n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type 'Biological sequence' _entity_src_gen.pdbx_beg_seq_num 1 _entity_src_gen.pdbx_end_seq_num 380 _entity_src_gen.gene_src_common_name Human _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene 'PLA2G15, LYPLA3, UNQ341/PRO540' _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Homo sapiens' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _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 'Homo sapiens' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _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 HEK293T _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.db_code PAG15_HUMAN _struct_ref.db_name UNP _struct_ref.details ? _struct_ref.entity_id 1 _struct_ref.id 1 _struct_ref.seq_align ? _struct_ref.seq_dif ? _struct_ref.pdbx_db_accession Q8NCC3 _struct_ref.pdbx_db_isoform ? _struct_ref.pdbx_seq_one_letter_code ;AGRHPPVVLVPGDLGNQLEAKLDKPTVVHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDV RVPGFGKTFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREMIEEMYQLYGGPVV LVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVLASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYN YTWSPEKVFVQTPTINYTLRDYRKFFQDIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPK ICFGDGDGTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP ; _struct_ref.pdbx_align_begin 34 _struct_ref.pdbx_align_end ? # 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 4X95 A 2 ? 380 ? Q8NCC3 34 ? 412 ? 1 379 2 1 4X95 B 2 ? 380 ? Q8NCC3 34 ? 412 ? 1 379 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 4X95 GLY A 1 ? UNP Q8NCC3 ? ? 'cloning artifact' 0 1 2 4X95 GLY B 1 ? UNP Q8NCC3 ? ? 'cloning artifact' 0 2 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 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 MAY non-polymer . 'METHYL ARACHIDONYL FLUOROPHOSPHONATE' MAFP 'C21 H36 F O2 P' 370.482 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 4X95 _exptl.crystals_number 1 _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 3.70 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 66.77 _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, HANGING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH 3.5 _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 297 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '100 mM Na citrate pH 3.5-4, 20% PEG 3350, and 100 mM NaCl' _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 'MARMOSAIC 300 mm CCD' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2013-06-14 # _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 0.97933 _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 23-ID-D' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.97933 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline 23-ID-D _diffrn_source.pdbx_synchrotron_site APS # _reflns.d_resolution_high 3.08 _reflns.d_resolution_low 30.000 _reflns.pdbx_number_measured_all 61572 _reflns.number_obs 12079 _reflns.pdbx_Rmerge_I_obs 0.173 _reflns.pdbx_netI_over_av_sigmaI 11.100 _reflns.pdbx_netI_over_sigmaI 4.200 _reflns.pdbx_chi_squared 1.265 _reflns.pdbx_redundancy 5.100 _reflns.percent_possible_obs 49.400 _reflns.pdbx_Rrim_I_all 0.190 _reflns.pdbx_Rpim_I_all 0.076 _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4X95 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.number_all ? _reflns.pdbx_Rsym_value ? _reflns.B_iso_Wilson_estimate ? # loop_ _reflns_shell.pdbx_diffrn_id _reflns_shell.pdbx_ordinal _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.number_measured_obs _reflns_shell.number_measured_all _reflns_shell.number_unique_obs _reflns_shell.pdbx_rejects _reflns_shell.Rmerge_I_obs _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.pdbx_netI_over_sigmaI_obs _reflns_shell.number_possible _reflns_shell.number_unique_all _reflns_shell.Rmerge_F_all _reflns_shell.Rmerge_F_obs _reflns_shell.Rmerge_I_all _reflns_shell.meanI_over_sigI_all _reflns_shell.percent_possible_all _reflns_shell.pdbx_Rrim_I_all _reflns_shell.pdbx_Rpim_I_all _reflns_shell.pdbx_CC_half 1 1 3.100 3.150 ? ? ? 0 0.342 ? ? 0.215 2.600 ? ? ? 54 ? ? ? ? 4.500 0.423 0.244 0.783 1 2 3.150 3.210 ? ? ? 0 0.463 ? ? 0.255 4.000 ? ? ? 112 ? ? ? ? 9.300 0.532 0.252 0.827 1 3 3.210 3.270 ? ? ? 0 0.367 ? ? 0.354 4.600 ? ? ? 186 ? ? ? ? 15.700 0.409 0.177 0.875 1 4 3.270 3.340 ? ? ? 0 0.378 ? ? 0.441 5.100 ? ? ? 236 ? ? ? ? 19.700 0.419 0.175 0.836 1 5 3.340 3.410 ? ? ? 0 0.392 ? ? 0.381 5.400 ? ? ? 295 ? ? ? ? 24.900 0.432 0.177 0.869 1 6 3.410 3.490 ? ? ? 0 0.360 ? ? 0.605 5.600 ? ? ? 345 ? ? ? ? 28.300 0.394 0.157 0.873 1 7 3.490 3.580 ? ? ? 0 0.346 ? ? 0.642 5.800 ? ? ? 369 ? ? ? ? 30.900 0.378 0.149 0.927 1 8 3.580 3.670 ? ? ? 0 0.339 ? ? 0.705 5.900 ? ? ? 418 ? ? ? ? 34.300 0.369 0.143 0.950 1 9 3.670 3.780 ? ? ? 0 0.322 ? ? 0.835 5.900 ? ? ? 469 ? ? ? ? 39.500 0.351 0.137 0.909 1 10 3.780 3.900 ? ? ? 0 0.302 ? ? 1.106 5.900 ? ? ? 508 ? ? ? ? 41.300 0.330 0.129 0.942 1 11 3.900 4.040 ? ? ? 0 0.284 ? ? 1.208 5.800 ? ? ? 565 ? ? ? ? 46.800 0.310 0.122 0.965 1 12 4.040 4.210 ? ? ? 0 0.289 ? ? 1.452 5.800 ? ? ? 594 ? ? ? ? 49.600 0.315 0.123 0.964 1 13 4.210 4.400 ? ? ? 0 0.239 ? ? 1.392 5.600 ? ? ? 681 ? ? ? ? 55.500 0.262 0.104 0.968 1 14 4.400 4.630 ? ? ? 0 0.208 ? ? 1.438 5.400 ? ? ? 726 ? ? ? ? 59.300 0.227 0.090 0.987 1 15 4.630 4.920 ? ? ? 0 0.202 ? ? 1.564 5.100 ? ? ? 828 ? ? ? ? 67.900 0.222 0.089 0.983 1 16 4.920 5.290 ? ? ? 0 0.190 ? ? 1.370 5.000 ? ? ? 900 ? ? ? ? 73.100 0.208 0.083 0.988 1 17 5.290 5.820 ? ? ? 0 0.186 ? ? 1.417 4.700 ? ? ? 1049 ? ? ? ? 85.300 0.203 0.081 0.982 1 18 5.820 6.660 ? ? ? 0 0.158 ? ? 1.246 4.600 ? ? ? 1174 ? ? ? ? 93.000 0.173 0.069 0.987 1 19 6.660 8.360 ? ? ? 0 0.119 ? ? 1.494 4.600 ? ? ? 1251 ? ? ? ? 99.300 0.131 0.053 0.991 1 20 8.360 30.000 ? ? ? 0 0.074 ? ? 2.026 4.400 ? ? ? 1319 ? ? ? ? 98.200 0.082 0.035 0.994 # _refine.entry_id 4X95 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_d_res_high 3.0800 _refine.ls_d_res_low 30.0000 _refine.pdbx_ls_sigma_F 0.000 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_percent_reflns_obs 49.4900 _refine.ls_number_reflns_obs 11420 _refine.ls_number_reflns_all ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.ls_matrix_type ? _refine.pdbx_R_Free_selection_details RANDOM _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED' _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.2195 _refine.ls_R_factor_R_work 0.2177 _refine.ls_wR_factor_R_work ? _refine.ls_R_factor_R_free 0.2517 _refine.ls_wR_factor_R_free ? _refine.ls_percent_reflns_R_free 5.1000 _refine.ls_number_reflns_R_free 615 _refine.ls_number_reflns_R_work ? _refine.ls_R_factor_R_free_error ? _refine.B_iso_mean 150.0150 _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.pdbx_isotropic_thermal_model ? _refine.aniso_B[1][1] 42.7200 _refine.aniso_B[2][2] -17.6300 _refine.aniso_B[3][3] -25.0900 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.correlation_coeff_Fo_to_Fc 0.9280 _refine.correlation_coeff_Fo_to_Fc_free 0.8920 _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.overall_SU_R_free ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free 0.7360 _refine.overall_SU_ML 0.4070 _refine.overall_SU_B 54.6430 _refine.solvent_model_details MASK _refine.pdbx_solvent_vdw_probe_radii 1.2000 _refine.pdbx_solvent_ion_probe_radii 0.8000 _refine.pdbx_solvent_shrinkage_radii 0.8000 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.pdbx_starting_model 4X90 _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.overall_FOM_work_R_set ? _refine.B_iso_max 256.140 _refine.B_iso_min 103.970 _refine.pdbx_overall_phase_error ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_R_factor_R_free_error_details ? # _refine_hist.cycle_id final _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.d_res_high 3.0800 _refine_hist.d_res_low 30.0000 _refine_hist.pdbx_number_atoms_ligand 176 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 6217 _refine_hist.pdbx_number_residues_total 752 _refine_hist.pdbx_B_iso_mean_ligand 199.47 _refine_hist.pdbx_number_atoms_protein 6041 _refine_hist.pdbx_number_atoms_nucleic_acid 0 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' r_bond_refined_d 6408 0.005 0.019 ? ? 'X-RAY DIFFRACTION' r_bond_other_d 5943 0.002 0.020 ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 8750 1.020 1.991 ? ? 'X-RAY DIFFRACTION' r_angle_other_deg 13635 0.746 3.000 ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 750 4.998 5.000 ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 289 29.967 23.495 ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 998 14.549 15.000 ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 41 11.182 15.000 ? ? 'X-RAY DIFFRACTION' r_chiral_restr 967 0.073 0.200 ? ? 'X-RAY DIFFRACTION' r_gen_planes_refined 7078 0.004 0.021 ? ? 'X-RAY DIFFRACTION' r_gen_planes_other 1491 0.001 0.020 ? ? 'X-RAY DIFFRACTION' r_mcbond_it 3006 2.627 10.608 ? ? 'X-RAY DIFFRACTION' r_mcbond_other 3005 2.626 10.607 ? ? 'X-RAY DIFFRACTION' r_mcangle_it 3754 4.455 15.904 ? ? # loop_ _refine_ls_restr_ncs.pdbx_ordinal _refine_ls_restr_ncs.pdbx_refine_id _refine_ls_restr_ncs.pdbx_ens_id _refine_ls_restr_ncs.dom_id _refine_ls_restr_ncs.pdbx_type _refine_ls_restr_ncs.pdbx_auth_asym_id _refine_ls_restr_ncs.pdbx_number _refine_ls_restr_ncs.rms_dev_position _refine_ls_restr_ncs.weight_position _refine_ls_restr_ncs.ncs_model_details _refine_ls_restr_ncs.rms_dev_B_iso _refine_ls_restr_ncs.weight_B_iso 1 'X-RAY DIFFRACTION' 1 1 'interatomic distance' A 23133 0.060 0.050 ? ? ? 2 'X-RAY DIFFRACTION' 1 2 'interatomic distance' B 23133 0.060 0.050 ? ? ? # _refine_ls_shell.d_res_high 3.08 _refine_ls_shell.d_res_low 3.1580 _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.percent_reflns_obs 4.7100 _refine_ls_shell.number_reflns_R_work 80 _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_R_work 0.3620 _refine_ls_shell.R_factor_R_free 0.2620 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 3 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.number_reflns_all 83 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.R_factor_obs ? # loop_ _struct_ncs_dom.pdbx_ens_id _struct_ncs_dom.id _struct_ncs_dom.details 1 1 A 1 2 B # loop_ _struct_ncs_dom_lim.pdbx_ens_id _struct_ncs_dom_lim.dom_id _struct_ncs_dom_lim.pdbx_component_id _struct_ncs_dom_lim.pdbx_refine_code _struct_ncs_dom_lim.beg_auth_asym_id _struct_ncs_dom_lim.beg_auth_seq_id _struct_ncs_dom_lim.end_auth_asym_id _struct_ncs_dom_lim.end_auth_seq_id _struct_ncs_dom_lim.selection_details _struct_ncs_dom_lim.beg_label_asym_id _struct_ncs_dom_lim.beg_label_comp_id _struct_ncs_dom_lim.beg_label_seq_id _struct_ncs_dom_lim.beg_label_alt_id _struct_ncs_dom_lim.end_label_asym_id _struct_ncs_dom_lim.end_label_comp_id _struct_ncs_dom_lim.end_label_seq_id _struct_ncs_dom_lim.end_label_alt_id 1 1 0 0 A 4 A 377 ? ? ? ? ? ? ? ? ? 1 2 0 0 B 4 B 377 ? ? ? ? ? ? ? ? ? # _struct_ncs_ens.id 1 _struct_ncs_ens.details ? # _struct.entry_id 4X95 _struct.title 'Crystal structure of fully glycosylated Lysosomal Phospholipase A2 in complex with methyl arachidonyl fluorophosphonate (MAFP)' _struct.pdbx_descriptor 'Group XV phospholipase A2 (E.C.2.3.1.-)' _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 4X95 _struct_keywords.text 'hydrolase, phospholipase, MAFP, acyltransferase, TRANSFERASE' _struct_keywords.pdbx_keywords TRANSFERASE # 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 2 ? E N N 3 ? F N N 2 ? G N N 2 ? H N N 2 ? I N N 4 ? J N N 2 ? K N N 2 ? L N N 3 ? M N N 2 ? N N N 2 ? O N N 2 ? P N N 4 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 ASN A 46 ? LEU A 51 ? ASN A 45 LEU A 50 5 ? 6 HELX_P HELX_P2 AA2 VAL A 53 ? ARG A 63 ? VAL A 52 ARG A 62 1 ? 11 HELX_P HELX_P3 AA3 THR A 89 ? PHE A 94 ? THR A 88 PHE A 93 1 ? 6 HELX_P HELX_P4 AA4 SER A 100 ? SER A 104 ? SER A 99 SER A 103 5 ? 5 HELX_P HELX_P5 AA5 PHE A 106 ? TRP A 116 ? PHE A 105 TRP A 115 1 ? 11 HELX_P HELX_P6 AA6 ALA A 134 ? GLU A 137 ? ALA A 133 GLU A 136 5 ? 4 HELX_P HELX_P7 AA7 ASN A 138 ? GLY A 157 ? ASN A 137 GLY A 156 1 ? 20 HELX_P HELX_P8 AA8 SER A 166 ? ARG A 178 ? SER A 165 ARG A 177 1 ? 13 HELX_P HELX_P9 AA9 PRO A 180 ? TYR A 187 ? PRO A 179 TYR A 186 1 ? 8 HELX_P HELX_P10 AB1 ALA A 202 ? GLY A 211 ? ALA A 201 GLY A 210 1 ? 10 HELX_P HELX_P11 AB2 GLY A 220 ? ALA A 231 ? GLY A 219 ALA A 230 1 ? 12 HELX_P HELX_P12 AB3 ALA A 231 ? LEU A 237 ? ALA A 230 LEU A 236 1 ? 7 HELX_P HELX_P13 AB4 ASP A 262 ? ILE A 270 ? ASP A 261 ILE A 269 1 ? 9 HELX_P HELX_P14 AB5 PHE A 272 ? GLU A 283 ? PHE A 271 GLU A 282 1 ? 12 HELX_P HELX_P15 AB6 ASN A 332 ? SER A 335 ? ASN A 331 SER A 334 5 ? 4 HELX_P HELX_P16 AB7 ALA A 336 ? SER A 344 ? ALA A 335 SER A 343 1 ? 9 HELX_P HELX_P17 AB8 ILE A 361 ? ALA A 365 ? ILE A 360 ALA A 364 5 ? 5 HELX_P HELX_P18 AB9 ASN A 366 ? GLY A 379 ? ASN A 365 GLY A 378 1 ? 14 HELX_P HELX_P19 AC1 ASN B 46 ? LEU B 51 ? ASN B 45 LEU B 50 5 ? 6 HELX_P HELX_P20 AC2 VAL B 53 ? ARG B 63 ? VAL B 52 ARG B 62 1 ? 11 HELX_P HELX_P21 AC3 THR B 89 ? PHE B 94 ? THR B 88 PHE B 93 1 ? 6 HELX_P HELX_P22 AC4 SER B 100 ? SER B 104 ? SER B 99 SER B 103 5 ? 5 HELX_P HELX_P23 AC5 PHE B 106 ? TRP B 116 ? PHE B 105 TRP B 115 1 ? 11 HELX_P HELX_P24 AC6 ALA B 134 ? GLU B 137 ? ALA B 133 GLU B 136 5 ? 4 HELX_P HELX_P25 AC7 ASN B 138 ? GLY B 157 ? ASN B 137 GLY B 156 1 ? 20 HELX_P HELX_P26 AC8 SER B 166 ? ARG B 178 ? SER B 165 ARG B 177 1 ? 13 HELX_P HELX_P27 AC9 PRO B 180 ? TYR B 187 ? PRO B 179 TYR B 186 1 ? 8 HELX_P HELX_P28 AD1 ALA B 202 ? GLY B 211 ? ALA B 201 GLY B 210 1 ? 10 HELX_P HELX_P29 AD2 GLY B 220 ? ALA B 231 ? GLY B 219 ALA B 230 1 ? 12 HELX_P HELX_P30 AD3 ALA B 231 ? LEU B 237 ? ALA B 230 LEU B 236 1 ? 7 HELX_P HELX_P31 AD4 ASP B 262 ? ILE B 270 ? ASP B 261 ILE B 269 1 ? 9 HELX_P HELX_P32 AD5 PHE B 272 ? GLU B 283 ? PHE B 271 GLU B 282 1 ? 12 HELX_P HELX_P33 AD6 ASN B 332 ? SER B 335 ? ASN B 331 SER B 334 5 ? 4 HELX_P HELX_P34 AD7 ALA B 336 ? SER B 344 ? ALA B 335 SER B 343 1 ? 9 HELX_P HELX_P35 AD8 ILE B 361 ? ALA B 365 ? ILE B 360 ALA B 364 5 ? 5 HELX_P HELX_P36 AD9 ASN B 366 ? GLY B 379 ? ASN B 365 GLY B 378 1 ? 14 # _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 33 SG ? ? ? 1_555 A CYS 57 SG ? ? A CYS 32 A CYS 56 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? B CYS 33 SG ? ? ? 1_555 B CYS 57 SG ? ? B CYS 32 B CYS 56 1_555 ? ? ? ? ? ? ? 2.034 ? covale1 covale one ? A ASN 67 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 66 A NAG 401 1_555 ? ? ? ? ? ? ? 1.457 ? covale2 covale one ? A SER 166 OG ? ? ? 1_555 I MAY . P1 ? ? A SER 165 A MAY 407 1_555 ? ? ? ? ? ? ? 1.629 ? covale3 covale one ? A ASN 241 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 240 A NAG 404 1_555 ? ? ? ? ? ? ? 1.466 ? covale4 covale one ? A ASN 257 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 256 A NAG 405 1_555 ? ? ? ? ? ? ? 1.464 ? covale5 covale one ? A ASN 366 ND2 ? ? ? 1_555 H NAG . C1 ? ? A ASN 365 A NAG 406 1_555 ? ? ? ? ? ? ? 1.454 ? covale6 covale one ? B ASN 67 ND2 ? ? ? 1_555 J NAG . C1 ? ? B ASN 66 B NAG 401 1_555 ? ? ? ? ? ? ? 1.476 ? covale7 covale one ? B SER 166 OG ? ? ? 1_555 P MAY . P1 ? ? B SER 165 B MAY 407 1_555 ? ? ? ? ? ? ? 1.622 ? covale8 covale one ? B ASN 241 ND2 ? ? ? 1_555 M NAG . C1 ? ? B ASN 240 B NAG 404 1_555 ? ? ? ? ? ? ? 1.458 ? covale9 covale one ? B ASN 257 ND2 ? ? ? 1_555 N NAG . C1 ? ? B ASN 256 B NAG 405 1_555 ? ? ? ? ? ? ? 1.457 ? covale10 covale one ? B ASN 366 ND2 ? ? ? 1_555 O NAG . C1 ? ? B ASN 365 B NAG 406 1_555 ? ? ? ? ? ? ? 1.457 ? covale11 covale both ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 401 A NAG 402 1_555 ? ? ? ? ? ? ? 1.436 ? covale12 covale both ? D NAG . O4 ? ? ? 1_555 E BMA . C1 ? ? A NAG 402 A BMA 403 1_555 ? ? ? ? ? ? ? 1.431 ? covale13 covale both ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? B NAG 401 B NAG 402 1_555 ? ? ? ? ? ? ? 1.438 ? covale14 covale both ? K NAG . O4 ? ? ? 1_555 L BMA . C1 ? ? B NAG 402 B BMA 403 1_555 ? ? ? ? ? ? ? 1.445 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 TRP 44 A . ? TRP 43 A LEU 45 A ? LEU 44 A 1 -2.93 2 PHE 315 A . ? PHE 314 A PRO 316 A ? PRO 315 A 1 -6.58 3 TRP 44 B . ? TRP 43 B LEU 45 B ? LEU 44 B 1 -2.93 4 PHE 315 B . ? PHE 314 B PRO 316 B ? PRO 315 B 1 -6.60 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 6 ? AA2 ? 3 ? AA3 ? 2 ? AA4 ? 4 ? AA5 ? 6 ? AA6 ? 3 ? AA7 ? 2 ? AA8 ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? parallel AA1 2 3 ? parallel AA1 3 4 ? parallel AA1 4 5 ? parallel AA1 5 6 ? parallel AA2 1 2 ? anti-parallel AA2 2 3 ? anti-parallel AA3 1 2 ? anti-parallel AA4 1 2 ? anti-parallel AA4 2 3 ? parallel AA4 3 4 ? anti-parallel AA5 1 2 ? parallel AA5 2 3 ? parallel AA5 3 4 ? parallel AA5 4 5 ? parallel AA5 5 6 ? parallel AA6 1 2 ? anti-parallel AA6 2 3 ? anti-parallel AA7 1 2 ? anti-parallel AA8 1 2 ? anti-parallel AA8 2 3 ? parallel AA8 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 VAL A 124 ? GLY A 126 ? VAL A 123 GLY A 125 AA1 2 VAL A 8 ? VAL A 11 ? VAL A 7 VAL A 10 AA1 3 VAL A 160 ? HIS A 165 ? VAL A 159 HIS A 164 AA1 4 ILE A 188 ? LEU A 194 ? ILE A 187 LEU A 193 AA1 5 LEU A 296 ? THR A 302 ? LEU A 295 THR A 301 AA1 6 VAL A 350 ? PRO A 356 ? VAL A 349 PRO A 355 AA2 1 PHE A 41 ? TRP A 44 ? PHE A 40 TRP A 43 AA2 2 LEU A 19 ? LEU A 23 ? LEU A 18 LEU A 22 AA2 3 VAL A 79 ? ARG A 82 ? VAL A 78 ARG A 81 AA3 1 VAL A 65 ? ASN A 67 ? VAL A 64 ASN A 66 AA3 2 ALA A 72 ? GLN A 74 ? ALA A 71 GLN A 73 AA4 1 ASN A 257 ? THR A 259 ? ASN A 256 THR A 258 AA4 2 VAL A 249 ? GLN A 252 ? VAL A 248 GLN A 251 AA4 3 THR A 306 ? TYR A 311 ? THR A 305 TYR A 310 AA4 4 LYS A 321 ? GLY A 325 ? LYS A 320 GLY A 324 AA5 1 VAL B 124 ? GLY B 126 ? VAL B 123 GLY B 125 AA5 2 VAL B 8 ? VAL B 11 ? VAL B 7 VAL B 10 AA5 3 VAL B 160 ? HIS B 165 ? VAL B 159 HIS B 164 AA5 4 ILE B 188 ? LEU B 194 ? ILE B 187 LEU B 193 AA5 5 LEU B 296 ? THR B 302 ? LEU B 295 THR B 301 AA5 6 VAL B 350 ? PRO B 356 ? VAL B 349 PRO B 355 AA6 1 PHE B 41 ? TRP B 44 ? PHE B 40 TRP B 43 AA6 2 LEU B 19 ? LEU B 23 ? LEU B 18 LEU B 22 AA6 3 VAL B 79 ? ARG B 82 ? VAL B 78 ARG B 81 AA7 1 VAL B 65 ? ASN B 67 ? VAL B 64 ASN B 66 AA7 2 ALA B 72 ? GLN B 74 ? ALA B 71 GLN B 73 AA8 1 ASN B 257 ? THR B 259 ? ASN B 256 THR B 258 AA8 2 VAL B 249 ? GLN B 252 ? VAL B 248 GLN B 251 AA8 3 THR B 306 ? TYR B 311 ? THR B 305 TYR B 310 AA8 4 LYS B 321 ? GLY B 325 ? LYS B 320 GLY B 324 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA1 1 2 O ARG A 125 ? O ARG A 124 N LEU A 10 ? N LEU A 9 AA1 2 3 N VAL A 9 ? N VAL A 8 O VAL A 163 ? O VAL A 162 AA1 3 4 N LEU A 162 ? N LEU A 161 O VAL A 192 ? O VAL A 191 AA1 4 5 N SER A 193 ? N SER A 192 O HIS A 297 ? O HIS A 296 AA1 5 6 N LEU A 296 ? N LEU A 295 O LEU A 351 ? O LEU A 350 AA2 1 2 O PHE A 41 ? O PHE A 40 N ALA A 21 ? N ALA A 20 AA2 2 3 N GLU A 20 ? N GLU A 19 O ARG A 82 ? O ARG A 81 AA3 1 2 N VAL A 65 ? N VAL A 64 O GLN A 74 ? O GLN A 73 AA4 1 2 O TYR A 258 ? O TYR A 257 N PHE A 250 ? N PHE A 249 AA4 2 3 N PHE A 250 ? N PHE A 249 O PHE A 310 ? O PHE A 309 AA4 3 4 N ASP A 308 ? N ASP A 307 O CYS A 323 ? O CYS A 322 AA5 1 2 O ARG B 125 ? O ARG B 124 N LEU B 10 ? N LEU B 9 AA5 2 3 N VAL B 9 ? N VAL B 8 O VAL B 163 ? O VAL B 162 AA5 3 4 N LEU B 162 ? N LEU B 161 O VAL B 192 ? O VAL B 191 AA5 4 5 N SER B 193 ? N SER B 192 O HIS B 297 ? O HIS B 296 AA5 5 6 N LEU B 296 ? N LEU B 295 O LEU B 351 ? O LEU B 350 AA6 1 2 O PHE B 41 ? O PHE B 40 N ALA B 21 ? N ALA B 20 AA6 2 3 N GLU B 20 ? N GLU B 19 O ARG B 82 ? O ARG B 81 AA7 1 2 N VAL B 65 ? N VAL B 64 O GLN B 74 ? O GLN B 73 AA8 1 2 O TYR B 258 ? O TYR B 257 N PHE B 250 ? N PHE B 249 AA8 2 3 N PHE B 250 ? N PHE B 249 O PHE B 310 ? O PHE B 309 AA8 3 4 N ASP B 308 ? N ASP B 307 O CYS B 323 ? O CYS B 322 # 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 MAY 407 ? 5 'binding site for residue MAY A 407' AC2 Software B MAY 407 ? 6 'binding site for residue MAY B 407' AC3 Software A ASN 66 ? 3 'binding site for Poly-Saccharide residues NAG A 401 through BMA A 403 bound to ASN A 66' AC4 Software A NAG 404 ? 2 'binding site for Mono-Saccharide NAG A 404 bound to ASN A 240' AC5 Software A NAG 405 ? 2 'binding site for Mono-Saccharide NAG A 405 bound to ASN A 256' AC6 Software A NAG 406 ? 2 'binding site for Mono-Saccharide NAG A 406 bound to ASN A 365' AC7 Software B ASN 66 ? 3 'binding site for Poly-Saccharide residues NAG B 401 through BMA B 403 bound to ASN B 66' AC8 Software B NAG 404 ? 2 'binding site for Mono-Saccharide NAG B 404 bound to ASN B 240' AC9 Software B NAG 405 ? 3 'binding site for Mono-Saccharide NAG B 405 bound to ASN B 256' AD1 Software B NAG 406 ? 5 'binding site for Mono-Saccharide NAG B 406 bound to ASN B 365' # 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 5 GLY A 13 ? GLY A 12 . ? 1_555 ? 2 AC1 5 ASP A 14 ? ASP A 13 . ? 1_555 ? 3 AC1 5 MET A 167 ? MET A 166 . ? 1_555 ? 4 AC1 5 LYS A 203 ? LYS A 202 . ? 1_555 ? 5 AC1 5 HIS A 360 ? HIS A 359 . ? 1_555 ? 6 AC2 6 GLY B 13 ? GLY B 12 . ? 1_555 ? 7 AC2 6 ASP B 14 ? ASP B 13 . ? 1_555 ? 8 AC2 6 LEU B 15 ? LEU B 14 . ? 1_555 ? 9 AC2 6 MET B 167 ? MET B 166 . ? 1_555 ? 10 AC2 6 ARG B 215 ? ARG B 214 . ? 1_555 ? 11 AC2 6 HIS B 360 ? HIS B 359 . ? 1_555 ? 12 AC3 3 ASN A 67 ? ASN A 66 . ? 1_555 ? 13 AC3 3 THR A 69 ? THR A 68 . ? 1_555 ? 14 AC3 3 GLN A 74 ? GLN A 73 . ? 1_555 ? 15 AC4 2 ASN A 241 ? ASN A 240 . ? 1_555 ? 16 AC4 2 ARG A 261 ? ARG A 260 . ? 1_555 ? 17 AC5 2 THR A 253 ? THR A 252 . ? 1_555 ? 18 AC5 2 ASN A 257 ? ASN A 256 . ? 1_555 ? 19 AC6 2 PRO A 356 ? PRO A 355 . ? 1_555 ? 20 AC6 2 ASN A 366 ? ASN A 365 . ? 1_555 ? 21 AC7 3 ASN B 67 ? ASN B 66 . ? 1_555 ? 22 AC7 3 THR B 69 ? THR B 68 . ? 1_555 ? 23 AC7 3 GLN B 74 ? GLN B 73 . ? 1_555 ? 24 AC8 2 ASN B 241 ? ASN B 240 . ? 1_555 ? 25 AC8 2 GLU B 283 ? GLU B 282 . ? 1_555 ? 26 AC9 3 VAL B 249 ? VAL B 248 . ? 1_555 ? 27 AC9 3 THR B 255 ? THR B 254 . ? 1_555 ? 28 AC9 3 ASN B 257 ? ASN B 256 . ? 1_555 ? 29 AD1 5 LEU B 355 ? LEU B 354 . ? 1_555 ? 30 AD1 5 PRO B 356 ? PRO B 355 . ? 1_555 ? 31 AD1 5 GLU B 362 ? GLU B 361 . ? 1_555 ? 32 AD1 5 ASN B 366 ? ASN B 365 . ? 1_555 ? 33 AD1 5 THR B 368 ? THR B 367 . ? 1_555 ? # _atom_sites.entry_id 4X95 _atom_sites.fract_transf_matrix[1][1] 0.013815 _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] 0.007982 _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] 0.007132 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol C N O P S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . HIS A 1 5 ? -3.447 37.553 22.646 1.00 147.23 ? 4 HIS A N 1 ATOM 2 C CA . HIS A 1 5 ? -3.439 36.069 22.528 1.00 146.38 ? 4 HIS A CA 1 ATOM 3 C C . HIS A 1 5 ? -2.338 35.460 23.404 1.00 145.19 ? 4 HIS A C 1 ATOM 4 O O . HIS A 1 5 ? -1.201 35.916 23.379 1.00 145.68 ? 4 HIS A O 1 ATOM 5 C CB . HIS A 1 5 ? -3.290 35.637 21.059 1.00 148.79 ? 4 HIS A CB 1 ATOM 6 C CG . HIS A 1 5 ? -2.078 36.189 20.365 1.00 151.90 ? 4 HIS A CG 1 ATOM 7 N ND1 . HIS A 1 5 ? -2.141 37.257 19.494 1.00 156.03 ? 4 HIS A ND1 1 ATOM 8 C CD2 . HIS A 1 5 ? -0.779 35.803 20.389 1.00 150.93 ? 4 HIS A CD2 1 ATOM 9 C CE1 . HIS A 1 5 ? -0.932 37.515 19.025 1.00 155.18 ? 4 HIS A CE1 1 ATOM 10 N NE2 . HIS A 1 5 ? -0.088 36.647 19.553 1.00 153.89 ? 4 HIS A NE2 1 ATOM 11 N N . PRO A 1 6 ? -2.673 34.429 24.194 1.00 144.46 ? 5 PRO A N 1 ATOM 12 C CA . PRO A 1 6 ? -1.663 33.889 25.098 1.00 142.83 ? 5 PRO A CA 1 ATOM 13 C C . PRO A 1 6 ? -0.643 32.968 24.419 1.00 137.92 ? 5 PRO A C 1 ATOM 14 O O . PRO A 1 6 ? -0.923 32.406 23.360 1.00 138.59 ? 5 PRO A O 1 ATOM 15 C CB . PRO A 1 6 ? -2.495 33.103 26.111 1.00 144.11 ? 5 PRO A CB 1 ATOM 16 C CG . PRO A 1 6 ? -3.690 32.662 25.340 1.00 144.04 ? 5 PRO A CG 1 ATOM 17 C CD . PRO A 1 6 ? -3.977 33.760 24.356 1.00 144.92 ? 5 PRO A CD 1 ATOM 18 N N . PRO A 1 7 ? 0.540 32.808 25.031 1.00 134.41 ? 6 PRO A N 1 ATOM 19 C CA . PRO A 1 7 ? 1.559 31.899 24.492 1.00 132.70 ? 6 PRO A CA 1 ATOM 20 C C . PRO A 1 7 ? 1.115 30.431 24.452 1.00 131.30 ? 6 PRO A C 1 ATOM 21 O O . PRO A 1 7 ? 0.297 30.002 25.269 1.00 130.53 ? 6 PRO A O 1 ATOM 22 C CB . PRO A 1 7 ? 2.747 32.083 25.445 1.00 133.04 ? 6 PRO A CB 1 ATOM 23 C CG . PRO A 1 7 ? 2.193 32.735 26.665 1.00 134.75 ? 6 PRO A CG 1 ATOM 24 C CD . PRO A 1 7 ? 1.017 33.537 26.219 1.00 135.84 ? 6 PRO A CD 1 ATOM 25 N N . VAL A 1 8 ? 1.665 29.672 23.506 1.00 129.34 ? 7 VAL A N 1 ATOM 26 C CA . VAL A 1 8 ? 1.236 28.295 23.275 1.00 129.14 ? 7 VAL A CA 1 ATOM 27 C C . VAL A 1 8 ? 2.415 27.331 23.241 1.00 126.19 ? 7 VAL A C 1 ATOM 28 O O . VAL A 1 8 ? 3.430 27.603 22.596 1.00 126.49 ? 7 VAL A O 1 ATOM 29 C CB . VAL A 1 8 ? 0.472 28.171 21.941 1.00 129.87 ? 7 VAL A CB 1 ATOM 30 C CG1 . VAL A 1 8 ? 0.103 26.716 21.659 1.00 129.00 ? 7 VAL A CG1 1 ATOM 31 C CG2 . VAL A 1 8 ? -0.772 29.047 21.963 1.00 130.37 ? 7 VAL A CG2 1 ATOM 32 N N . VAL A 1 9 ? 2.254 26.202 23.928 1.00 120.85 ? 8 VAL A N 1 ATOM 33 C CA . VAL A 1 9 ? 3.231 25.124 23.903 1.00 118.52 ? 8 VAL A CA 1 ATOM 34 C C . VAL A 1 9 ? 2.580 23.883 23.298 1.00 119.20 ? 8 VAL A C 1 ATOM 35 O O . VAL A 1 9 ? 1.518 23.446 23.752 1.00 121.28 ? 8 VAL A O 1 ATOM 36 C CB . VAL A 1 9 ? 3.748 24.803 25.317 1.00 117.10 ? 8 VAL A CB 1 ATOM 37 C CG1 . VAL A 1 9 ? 4.912 23.824 25.250 1.00 113.54 ? 8 VAL A CG1 1 ATOM 38 C CG2 . VAL A 1 9 ? 4.163 26.088 26.026 1.00 120.85 ? 8 VAL A CG2 1 ATOM 39 N N . LEU A 1 10 ? 3.225 23.329 22.273 1.00 116.58 ? 9 LEU A N 1 ATOM 40 C CA . LEU A 1 10 ? 2.728 22.150 21.576 1.00 117.69 ? 9 LEU A CA 1 ATOM 41 C C . LEU A 1 10 ? 3.470 20.898 22.034 1.00 120.11 ? 9 LEU A C 1 ATOM 42 O O . LEU A 1 10 ? 4.699 20.871 22.042 1.00 121.35 ? 9 LEU A O 1 ATOM 43 C CB . LEU A 1 10 ? 2.904 22.320 20.068 1.00 120.27 ? 9 LEU A CB 1 ATOM 44 C CG . LEU A 1 10 ? 2.288 23.576 19.446 1.00 120.04 ? 9 LEU A CG 1 ATOM 45 C CD1 . LEU A 1 10 ? 2.502 23.560 17.940 1.00 118.84 ? 9 LEU A CD1 1 ATOM 46 C CD2 . LEU A 1 10 ? 0.807 23.692 19.775 1.00 120.79 ? 9 LEU A CD2 1 ATOM 47 N N . VAL A 1 11 ? 2.718 19.863 22.402 1.00 120.64 ? 10 VAL A N 1 ATOM 48 C CA . VAL A 1 11 ? 3.291 18.610 22.891 1.00 120.15 ? 10 VAL A CA 1 ATOM 49 C C . VAL A 1 11 ? 2.869 17.465 21.966 1.00 122.02 ? 10 VAL A C 1 ATOM 50 O O . VAL A 1 11 ? 1.678 17.179 21.841 1.00 121.19 ? 10 VAL A O 1 ATOM 51 C CB . VAL A 1 11 ? 2.829 18.305 24.333 1.00 120.14 ? 10 VAL A CB 1 ATOM 52 C CG1 . VAL A 1 11 ? 3.600 17.121 24.907 1.00 118.74 ? 10 VAL A CG1 1 ATOM 53 C CG2 . VAL A 1 11 ? 3.001 19.533 25.218 1.00 122.78 ? 10 VAL A CG2 1 ATOM 54 N N . PRO A 1 12 ? 3.846 16.805 21.317 1.00 126.32 ? 11 PRO A N 1 ATOM 55 C CA . PRO A 1 12 ? 3.549 15.711 20.389 1.00 126.22 ? 11 PRO A CA 1 ATOM 56 C C . PRO A 1 12 ? 3.225 14.385 21.070 1.00 124.64 ? 11 PRO A C 1 ATOM 57 O O . PRO A 1 12 ? 3.467 14.220 22.268 1.00 125.14 ? 11 PRO A O 1 ATOM 58 C CB . PRO A 1 12 ? 4.858 15.562 19.612 1.00 127.94 ? 11 PRO A CB 1 ATOM 59 C CG . PRO A 1 12 ? 5.901 15.946 20.604 1.00 128.17 ? 11 PRO A CG 1 ATOM 60 C CD . PRO A 1 12 ? 5.295 17.077 21.386 1.00 128.04 ? 11 PRO A CD 1 ATOM 61 N N . GLY A 1 13 ? 2.704 13.446 20.287 1.00 120.79 ? 12 GLY A N 1 ATOM 62 C CA . GLY A 1 13 ? 2.481 12.085 20.751 1.00 120.14 ? 12 GLY A CA 1 ATOM 63 C C . GLY A 1 13 ? 3.621 11.156 20.381 1.00 120.82 ? 12 GLY A C 1 ATOM 64 O O . GLY A 1 13 ? 4.692 11.603 19.967 1.00 115.56 ? 12 GLY A O 1 ATOM 65 N N . ASP A 1 14 ? 3.383 9.855 20.543 1.00 123.42 ? 13 ASP A N 1 ATOM 66 C CA . ASP A 1 14 ? 4.354 8.827 20.173 1.00 122.87 ? 13 ASP A CA 1 ATOM 67 C C . ASP A 1 14 ? 4.631 8.928 18.673 1.00 123.49 ? 13 ASP A C 1 ATOM 68 O O . ASP A 1 14 ? 3.722 9.153 17.876 1.00 124.62 ? 13 ASP A O 1 ATOM 69 C CB . ASP A 1 14 ? 3.818 7.432 20.531 1.00 125.30 ? 13 ASP A CB 1 ATOM 70 C CG . ASP A 1 14 ? 4.891 6.350 20.492 1.00 129.78 ? 13 ASP A CG 1 ATOM 71 O OD1 . ASP A 1 14 ? 6.022 6.625 20.037 1.00 135.12 ? 13 ASP A OD1 1 ATOM 72 O OD2 . ASP A 1 14 ? 4.600 5.211 20.920 1.00 127.56 ? 13 ASP A OD2 1 ATOM 73 N N . LEU A 1 15 ? 5.900 8.781 18.303 1.00 124.06 ? 14 LEU A N 1 ATOM 74 C CA . LEU A 1 15 ? 6.358 8.963 16.918 1.00 124.01 ? 14 LEU A CA 1 ATOM 75 C C . LEU A 1 15 ? 6.158 10.404 16.413 1.00 122.52 ? 14 LEU A C 1 ATOM 76 O O . LEU A 1 15 ? 6.274 10.666 15.215 1.00 121.30 ? 14 LEU A O 1 ATOM 77 C CB . LEU A 1 15 ? 5.645 7.982 15.973 1.00 123.87 ? 14 LEU A CB 1 ATOM 78 C CG . LEU A 1 15 ? 5.375 6.557 16.477 1.00 120.08 ? 14 LEU A CG 1 ATOM 79 C CD1 . LEU A 1 15 ? 3.970 6.102 16.100 1.00 120.23 ? 14 LEU A CD1 1 ATOM 80 N N . GLY A 1 16 ? 5.900 11.335 17.331 1.00 123.82 ? 15 GLY A N 1 ATOM 81 C CA . GLY A 1 16 ? 5.405 12.662 16.979 1.00 123.29 ? 15 GLY A CA 1 ATOM 82 C C . GLY A 1 16 ? 6.453 13.739 16.760 1.00 123.99 ? 15 GLY A C 1 ATOM 83 O O . GLY A 1 16 ? 6.107 14.855 16.368 1.00 128.19 ? 15 GLY A O 1 ATOM 84 N N . ASN A 1 17 ? 7.726 13.427 17.008 1.00 123.60 ? 16 ASN A N 1 ATOM 85 C CA . ASN A 1 17 ? 8.795 14.405 16.800 1.00 124.72 ? 16 ASN A CA 1 ATOM 86 C C . ASN A 1 17 ? 10.080 13.766 16.316 1.00 123.81 ? 16 ASN A C 1 ATOM 87 O O . ASN A 1 17 ? 10.336 12.593 16.579 1.00 121.67 ? 16 ASN A O 1 ATOM 88 C CB . ASN A 1 17 ? 9.040 15.251 18.060 1.00 126.08 ? 16 ASN A CB 1 ATOM 89 C CG . ASN A 1 17 ? 9.506 14.429 19.247 1.00 125.67 ? 16 ASN A CG 1 ATOM 90 O OD1 . ASN A 1 17 ? 10.702 14.192 19.428 1.00 125.03 ? 16 ASN A OD1 1 ATOM 91 N ND2 . ASN A 1 17 ? 8.559 14.006 20.074 1.00 125.73 ? 16 ASN A ND2 1 ATOM 92 N N . GLN A 1 18 ? 10.881 14.548 15.603 1.00 126.00 ? 17 GLN A N 1 ATOM 93 C CA . GLN A 1 18 ? 12.128 14.049 15.043 1.00 129.78 ? 17 GLN A CA 1 ATOM 94 C C . GLN A 1 18 ? 13.090 13.589 16.140 1.00 133.95 ? 17 GLN A C 1 ATOM 95 O O . GLN A 1 18 ? 13.026 14.073 17.273 1.00 137.52 ? 17 GLN A O 1 ATOM 96 C CB . GLN A 1 18 ? 12.799 15.125 14.184 1.00 132.10 ? 17 GLN A CB 1 ATOM 97 C CG . GLN A 1 18 ? 11.987 15.533 12.963 1.00 132.11 ? 17 GLN A CG 1 ATOM 98 C CD . GLN A 1 18 ? 12.783 16.341 11.951 1.00 134.60 ? 17 GLN A CD 1 ATOM 99 O OE1 . GLN A 1 18 ? 14.000 16.495 12.070 1.00 135.16 ? 17 GLN A OE1 1 ATOM 100 N NE2 . GLN A 1 18 ? 12.094 16.863 10.945 1.00 136.74 ? 17 GLN A NE2 1 ATOM 101 N N . LEU A 1 19 ? 13.971 12.650 15.789 1.00 135.92 ? 18 LEU A N 1 ATOM 102 C CA . LEU A 1 19 ? 15.048 12.191 16.676 1.00 137.41 ? 18 LEU A CA 1 ATOM 103 C C . LEU A 1 19 ? 16.353 12.088 15.883 1.00 137.00 ? 18 LEU A C 1 ATOM 104 O O . LEU A 1 19 ? 16.332 11.746 14.691 1.00 132.75 ? 18 LEU A O 1 ATOM 105 C CB . LEU A 1 19 ? 14.699 10.825 17.269 1.00 137.03 ? 18 LEU A CB 1 ATOM 106 C CG . LEU A 1 19 ? 13.491 10.778 18.208 1.00 138.22 ? 18 LEU A CG 1 ATOM 107 C CD1 . LEU A 1 19 ? 13.151 9.334 18.540 1.00 138.03 ? 18 LEU A CD1 1 ATOM 108 C CD2 . LEU A 1 19 ? 13.752 11.573 19.482 1.00 140.31 ? 18 LEU A CD2 1 ATOM 109 N N . GLU A 1 20 ? 17.473 12.383 16.547 1.00 136.15 ? 19 GLU A N 1 ATOM 110 C CA . GLU A 1 20 ? 18.792 12.387 15.909 1.00 134.99 ? 19 GLU A CA 1 ATOM 111 C C . GLU A 1 20 ? 19.753 11.471 16.648 1.00 131.61 ? 19 GLU A C 1 ATOM 112 O O . GLU A 1 20 ? 19.649 11.303 17.863 1.00 126.28 ? 19 GLU A O 1 ATOM 113 C CB . GLU A 1 20 ? 19.372 13.802 15.897 1.00 139.16 ? 19 GLU A CB 1 ATOM 114 C CG . GLU A 1 20 ? 18.733 14.731 14.877 1.00 144.98 ? 19 GLU A CG 1 ATOM 115 C CD . GLU A 1 20 ? 19.306 16.141 14.913 1.00 151.87 ? 19 GLU A CD 1 ATOM 116 O OE1 . GLU A 1 20 ? 20.212 16.415 15.732 1.00 154.72 ? 19 GLU A OE1 1 ATOM 117 O OE2 . GLU A 1 20 ? 18.847 16.984 14.112 1.00 155.81 ? 19 GLU A OE2 1 ATOM 118 N N . ALA A 1 21 ? 20.700 10.899 15.911 1.00 132.17 ? 20 ALA A N 1 ATOM 119 C CA . ALA A 1 21 ? 21.679 9.995 16.498 1.00 135.57 ? 20 ALA A CA 1 ATOM 120 C C . ALA A 1 21 ? 23.085 10.246 15.965 1.00 140.49 ? 20 ALA A C 1 ATOM 121 O O . ALA A 1 21 ? 23.256 10.778 14.872 1.00 141.57 ? 20 ALA A O 1 ATOM 122 C CB . ALA A 1 21 ? 21.274 8.551 16.251 1.00 134.18 ? 20 ALA A CB 1 ATOM 123 N N . LYS A 1 22 ? 24.083 9.865 16.761 1.00 145.28 ? 21 LYS A N 1 ATOM 124 C CA . LYS A 1 22 ? 25.494 9.922 16.364 1.00 148.69 ? 21 LYS A CA 1 ATOM 125 C C . LYS A 1 22 ? 26.103 8.550 16.675 1.00 144.43 ? 21 LYS A C 1 ATOM 126 O O . LYS A 1 22 ? 25.845 7.984 17.742 1.00 142.86 ? 21 LYS A O 1 ATOM 127 C CB . LYS A 1 22 ? 26.226 11.038 17.134 1.00 153.92 ? 21 LYS A CB 1 ATOM 128 C CG . LYS A 1 22 ? 27.447 11.618 16.429 1.00 159.58 ? 21 LYS A CG 1 ATOM 129 C CD . LYS A 1 22 ? 28.691 10.759 16.602 1.00 165.82 ? 21 LYS A CD 1 ATOM 130 C CE . LYS A 1 22 ? 29.930 11.467 16.076 1.00 170.36 ? 21 LYS A CE 1 ATOM 131 N NZ . LYS A 1 22 ? 31.069 10.527 15.878 1.00 173.63 ? 21 LYS A NZ 1 ATOM 132 N N . LEU A 1 23 ? 26.899 8.026 15.745 1.00 141.50 ? 22 LEU A N 1 ATOM 133 C CA . LEU A 1 23 ? 27.419 6.666 15.845 1.00 142.04 ? 22 LEU A CA 1 ATOM 134 C C . LEU A 1 23 ? 28.931 6.613 15.988 1.00 146.05 ? 22 LEU A C 1 ATOM 135 O O . LEU A 1 23 ? 29.657 7.325 15.284 1.00 146.60 ? 22 LEU A O 1 ATOM 136 C CB . LEU A 1 23 ? 27.056 5.876 14.589 1.00 142.28 ? 22 LEU A CB 1 ATOM 137 C CG . LEU A 1 23 ? 25.594 5.869 14.156 1.00 142.49 ? 22 LEU A CG 1 ATOM 138 C CD1 . LEU A 1 23 ? 25.432 4.968 12.938 1.00 143.55 ? 22 LEU A CD1 1 ATOM 139 C CD2 . LEU A 1 23 ? 24.691 5.415 15.294 1.00 141.68 ? 22 LEU A CD2 1 ATOM 140 N N . ASP A 1 24 ? 29.383 5.758 16.904 1.00 150.45 ? 23 ASP A N 1 ATOM 141 C CA . ASP A 1 24 ? 30.768 5.289 16.949 1.00 156.26 ? 23 ASP A CA 1 ATOM 142 C C . ASP A 1 24 ? 30.750 3.867 17.519 1.00 155.68 ? 23 ASP A C 1 ATOM 143 O O . ASP A 1 24 ? 31.192 3.618 18.645 1.00 154.22 ? 23 ASP A O 1 ATOM 144 C CB . ASP A 1 24 ? 31.636 6.216 17.806 1.00 162.09 ? 23 ASP A CB 1 ATOM 145 C CG . ASP A 1 24 ? 33.105 5.813 17.804 1.00 169.47 ? 23 ASP A CG 1 ATOM 146 O OD1 . ASP A 1 24 ? 33.568 5.214 16.807 1.00 171.60 ? 23 ASP A OD1 1 ATOM 147 O OD2 . ASP A 1 24 ? 33.800 6.099 18.802 1.00 177.24 ? 23 ASP A OD2 1 ATOM 148 N N . LYS A 1 25 ? 30.221 2.944 16.722 1.00 156.22 ? 24 LYS A N 1 ATOM 149 C CA . LYS A 1 25 ? 29.896 1.602 17.191 1.00 159.63 ? 24 LYS A CA 1 ATOM 150 C C . LYS A 1 25 ? 31.100 0.676 17.102 1.00 163.30 ? 24 LYS A C 1 ATOM 151 O O . LYS A 1 25 ? 31.883 0.771 16.159 1.00 162.75 ? 24 LYS A O 1 ATOM 152 C CB . LYS A 1 25 ? 28.761 1.011 16.355 1.00 160.17 ? 24 LYS A CB 1 ATOM 153 C CG . LYS A 1 25 ? 27.506 1.865 16.316 1.00 160.58 ? 24 LYS A CG 1 ATOM 154 C CD . LYS A 1 25 ? 26.387 1.188 15.541 1.00 160.34 ? 24 LYS A CD 1 ATOM 155 C CE . LYS A 1 25 ? 25.771 0.041 16.330 1.00 160.53 ? 24 LYS A CE 1 ATOM 156 N NZ . LYS A 1 25 ? 24.511 -0.463 15.718 1.00 159.91 ? 24 LYS A NZ 1 ATOM 157 N N . PRO A 1 26 ? 31.244 -0.234 18.081 1.00 167.17 ? 25 PRO A N 1 ATOM 158 C CA . PRO A 1 26 ? 32.323 -1.218 18.018 1.00 172.14 ? 25 PRO A CA 1 ATOM 159 C C . PRO A 1 26 ? 32.100 -2.262 16.920 1.00 175.71 ? 25 PRO A C 1 ATOM 160 O O . PRO A 1 26 ? 33.055 -2.667 16.256 1.00 182.49 ? 25 PRO A O 1 ATOM 161 C CB . PRO A 1 26 ? 32.297 -1.864 19.407 1.00 171.48 ? 25 PRO A CB 1 ATOM 162 C CG . PRO A 1 26 ? 30.907 -1.673 19.898 1.00 167.92 ? 25 PRO A CG 1 ATOM 163 C CD . PRO A 1 26 ? 30.402 -0.402 19.281 1.00 166.42 ? 25 PRO A CD 1 ATOM 164 N N . THR A 1 27 ? 30.852 -2.688 16.742 1.00 175.06 ? 26 THR A N 1 ATOM 165 C CA . THR A 1 27 ? 30.481 -3.629 15.680 1.00 174.18 ? 26 THR A CA 1 ATOM 166 C C . THR A 1 27 ? 29.007 -3.465 15.322 1.00 169.76 ? 26 THR A C 1 ATOM 167 O O . THR A 1 27 ? 28.240 -2.836 16.055 1.00 166.35 ? 26 THR A O 1 ATOM 168 C CB . THR A 1 27 ? 30.725 -5.103 16.085 1.00 176.26 ? 26 THR A CB 1 ATOM 169 O OG1 . THR A 1 27 ? 30.321 -5.306 17.445 1.00 177.96 ? 26 THR A OG1 1 ATOM 170 C CG2 . THR A 1 27 ? 32.196 -5.494 15.926 1.00 179.07 ? 26 THR A CG2 1 ATOM 171 N N . VAL A 1 28 ? 28.624 -4.050 14.191 1.00 169.59 ? 27 VAL A N 1 ATOM 172 C CA . VAL A 1 28 ? 27.253 -3.976 13.685 1.00 168.64 ? 27 VAL A CA 1 ATOM 173 C C . VAL A 1 28 ? 26.770 -5.352 13.245 1.00 171.08 ? 27 VAL A C 1 ATOM 174 O O . VAL A 1 28 ? 27.547 -6.308 13.186 1.00 176.71 ? 27 VAL A O 1 ATOM 175 C CB . VAL A 1 28 ? 27.138 -2.996 12.499 1.00 168.40 ? 27 VAL A CB 1 ATOM 176 C CG1 . VAL A 1 28 ? 27.147 -1.559 12.997 1.00 171.03 ? 27 VAL A CG1 1 ATOM 177 C CG2 . VAL A 1 28 ? 28.254 -3.231 11.487 1.00 170.33 ? 27 VAL A CG2 1 ATOM 178 N N . VAL A 1 29 ? 25.481 -5.443 12.938 1.00 169.41 ? 28 VAL A N 1 ATOM 179 C CA . VAL A 1 29 ? 24.867 -6.709 12.533 1.00 168.53 ? 28 VAL A CA 1 ATOM 180 C C . VAL A 1 29 ? 25.197 -7.134 11.097 1.00 167.23 ? 28 VAL A C 1 ATOM 181 O O . VAL A 1 29 ? 25.216 -8.331 10.801 1.00 172.16 ? 28 VAL A O 1 ATOM 182 C CB . VAL A 1 29 ? 23.334 -6.700 12.738 1.00 167.72 ? 28 VAL A CB 1 ATOM 183 C CG1 . VAL A 1 29 ? 22.998 -6.456 14.202 1.00 167.22 ? 28 VAL A CG1 1 ATOM 184 C CG2 . VAL A 1 29 ? 22.649 -5.668 11.847 1.00 167.99 ? 28 VAL A CG2 1 ATOM 185 N N . HIS A 1 30 ? 25.448 -6.164 10.216 1.00 163.93 ? 29 HIS A N 1 ATOM 186 C CA . HIS A 1 30 ? 25.807 -6.448 8.823 1.00 162.95 ? 29 HIS A CA 1 ATOM 187 C C . HIS A 1 30 ? 26.916 -5.514 8.370 1.00 159.34 ? 29 HIS A C 1 ATOM 188 O O . HIS A 1 30 ? 27.023 -4.386 8.855 1.00 156.64 ? 29 HIS A O 1 ATOM 189 C CB . HIS A 1 30 ? 24.592 -6.290 7.903 1.00 165.20 ? 29 HIS A CB 1 ATOM 190 C CG . HIS A 1 30 ? 23.537 -7.335 8.103 1.00 168.50 ? 29 HIS A CG 1 ATOM 191 N ND1 . HIS A 1 30 ? 23.775 -8.680 7.918 1.00 175.59 ? 29 HIS A ND1 1 ATOM 192 C CD2 . HIS A 1 30 ? 22.233 -7.230 8.456 1.00 167.32 ? 29 HIS A CD2 1 ATOM 193 C CE1 . HIS A 1 30 ? 22.668 -9.360 8.158 1.00 175.99 ? 29 HIS A CE1 1 ATOM 194 N NE2 . HIS A 1 30 ? 21.717 -8.503 8.487 1.00 171.05 ? 29 HIS A NE2 1 ATOM 195 N N . TYR A 1 31 ? 27.726 -5.988 7.428 1.00 158.36 ? 30 TYR A N 1 ATOM 196 C CA . TYR A 1 31 ? 28.860 -5.223 6.913 1.00 162.08 ? 30 TYR A CA 1 ATOM 197 C C . TYR A 1 31 ? 28.453 -3.887 6.291 1.00 164.73 ? 30 TYR A C 1 ATOM 198 O O . TYR A 1 31 ? 29.198 -2.910 6.360 1.00 168.98 ? 30 TYR A O 1 ATOM 199 C CB . TYR A 1 31 ? 29.638 -6.050 5.888 1.00 163.85 ? 30 TYR A CB 1 ATOM 200 C CG . TYR A 1 31 ? 30.538 -7.100 6.505 1.00 165.91 ? 30 TYR A CG 1 ATOM 201 C CD1 . TYR A 1 31 ? 30.057 -8.363 6.824 1.00 166.61 ? 30 TYR A CD1 1 ATOM 202 C CD2 . TYR A 1 31 ? 31.875 -6.823 6.773 1.00 168.20 ? 30 TYR A CD2 1 ATOM 203 C CE1 . TYR A 1 31 ? 30.884 -9.322 7.388 1.00 169.34 ? 30 TYR A CE1 1 ATOM 204 C CE2 . TYR A 1 31 ? 32.711 -7.777 7.333 1.00 169.48 ? 30 TYR A CE2 1 ATOM 205 C CZ . TYR A 1 31 ? 32.211 -9.024 7.638 1.00 170.72 ? 30 TYR A CZ 1 ATOM 206 O OH . TYR A 1 31 ? 33.037 -9.972 8.196 1.00 174.53 ? 30 TYR A OH 1 ATOM 207 N N . LEU A 1 32 ? 27.272 -3.841 5.689 1.00 165.74 ? 31 LEU A N 1 ATOM 208 C CA . LEU A 1 32 ? 26.806 -2.616 5.045 1.00 166.74 ? 31 LEU A CA 1 ATOM 209 C C . LEU A 1 32 ? 26.268 -1.562 6.023 1.00 164.73 ? 31 LEU A C 1 ATOM 210 O O . LEU A 1 32 ? 25.919 -0.459 5.602 1.00 166.20 ? 31 LEU A O 1 ATOM 211 C CB . LEU A 1 32 ? 25.764 -2.914 3.959 1.00 167.77 ? 31 LEU A CB 1 ATOM 212 C CG . LEU A 1 32 ? 24.549 -3.764 4.353 1.00 168.55 ? 31 LEU A CG 1 ATOM 213 C CD1 . LEU A 1 32 ? 23.265 -3.157 3.808 1.00 167.12 ? 31 LEU A CD1 1 ATOM 214 C CD2 . LEU A 1 32 ? 24.698 -5.217 3.907 1.00 170.64 ? 31 LEU A CD2 1 ATOM 215 N N . CYS A 1 33 ? 26.198 -1.886 7.315 1.00 163.50 ? 32 CYS A N 1 ATOM 216 C CA . CYS A 1 33 ? 25.808 -0.896 8.327 1.00 164.58 ? 32 CYS A CA 1 ATOM 217 C C . CYS A 1 33 ? 26.995 0.006 8.684 1.00 163.88 ? 32 CYS A C 1 ATOM 218 O O . CYS A 1 33 ? 28.126 -0.466 8.821 1.00 165.00 ? 32 CYS A O 1 ATOM 219 C CB . CYS A 1 33 ? 25.295 -1.575 9.604 1.00 165.57 ? 32 CYS A CB 1 ATOM 220 S SG . CYS A 1 33 ? 23.979 -2.802 9.396 1.00 162.67 ? 32 CYS A SG 1 ATOM 221 N N . SER A 1 34 ? 26.727 1.297 8.853 1.00 160.19 ? 33 SER A N 1 ATOM 222 C CA . SER A 1 34 ? 27.762 2.260 9.214 1.00 160.22 ? 33 SER A CA 1 ATOM 223 C C . SER A 1 34 ? 28.179 2.093 10.664 1.00 157.22 ? 33 SER A C 1 ATOM 224 O O . SER A 1 34 ? 27.332 1.984 11.554 1.00 151.05 ? 33 SER A O 1 ATOM 225 C CB . SER A 1 34 ? 27.276 3.695 8.998 1.00 161.97 ? 33 SER A CB 1 ATOM 226 O OG . SER A 1 34 ? 26.960 3.899 7.639 1.00 167.38 ? 33 SER A OG 1 ATOM 227 N N . LYS A 1 35 ? 29.491 2.077 10.885 1.00 159.51 ? 34 LYS A N 1 ATOM 228 C CA . LYS A 1 35 ? 30.064 2.038 12.233 1.00 161.73 ? 34 LYS A CA 1 ATOM 229 C C . LYS A 1 35 ? 30.076 3.425 12.857 1.00 158.73 ? 34 LYS A C 1 ATOM 230 O O . LYS A 1 35 ? 29.841 3.585 14.057 1.00 153.91 ? 34 LYS A O 1 ATOM 231 C CB . LYS A 1 35 ? 31.511 1.526 12.192 1.00 166.97 ? 34 LYS A CB 1 ATOM 232 C CG . LYS A 1 35 ? 31.678 0.034 12.427 1.00 167.88 ? 34 LYS A CG 1 ATOM 233 C CD . LYS A 1 35 ? 33.119 -0.290 12.797 1.00 171.78 ? 34 LYS A CD 1 ATOM 234 C CE . LYS A 1 35 ? 33.291 -1.746 13.193 1.00 173.99 ? 34 LYS A CE 1 ATOM 235 N NZ . LYS A 1 35 ? 33.300 -2.657 12.017 1.00 176.07 ? 34 LYS A NZ 1 ATOM 236 N N . LYS A 1 36 ? 30.380 4.420 12.032 1.00 159.51 ? 35 LYS A N 1 ATOM 237 C CA . LYS A 1 36 ? 30.625 5.761 12.513 1.00 163.15 ? 35 LYS A CA 1 ATOM 238 C C . LYS A 1 36 ? 29.923 6.789 11.643 1.00 162.03 ? 35 LYS A C 1 ATOM 239 O O . LYS A 1 36 ? 29.829 6.630 10.425 1.00 162.85 ? 35 LYS A O 1 ATOM 240 C CB . LYS A 1 36 ? 32.130 6.029 12.509 1.00 170.70 ? 35 LYS A CB 1 ATOM 241 C CG . LYS A 1 36 ? 32.536 7.298 13.234 1.00 177.74 ? 35 LYS A CG 1 ATOM 242 C CD . LYS A 1 36 ? 34.047 7.440 13.292 1.00 185.93 ? 35 LYS A CD 1 ATOM 243 C CE . LYS A 1 36 ? 34.460 8.629 14.146 1.00 191.22 ? 35 LYS A CE 1 ATOM 244 N NZ . LYS A 1 36 ? 34.151 8.445 15.591 1.00 192.42 ? 35 LYS A NZ 1 ATOM 245 N N . THR A 1 37 ? 29.424 7.841 12.284 1.00 160.68 ? 36 THR A N 1 ATOM 246 C CA . THR A 1 37 ? 28.962 9.033 11.580 1.00 158.80 ? 36 THR A CA 1 ATOM 247 C C . THR A 1 37 ? 29.803 10.218 12.040 1.00 158.90 ? 36 THR A C 1 ATOM 248 O O . THR A 1 37 ? 30.251 10.262 13.189 1.00 157.70 ? 36 THR A O 1 ATOM 249 C CB . THR A 1 37 ? 27.476 9.330 11.858 1.00 156.88 ? 36 THR A CB 1 ATOM 250 O OG1 . THR A 1 37 ? 27.250 9.411 13.271 1.00 155.70 ? 36 THR A OG1 1 ATOM 251 C CG2 . THR A 1 37 ? 26.596 8.245 11.261 1.00 155.99 ? 36 THR A CG2 1 ATOM 252 N N . GLU A 1 38 ? 30.015 11.171 11.139 1.00 158.21 ? 37 GLU A N 1 ATOM 253 C CA . GLU A 1 38 ? 30.808 12.363 11.440 1.00 161.06 ? 37 GLU A CA 1 ATOM 254 C C . GLU A 1 38 ? 30.059 13.347 12.340 1.00 159.95 ? 37 GLU A C 1 ATOM 255 O O . GLU A 1 38 ? 30.668 14.123 13.077 1.00 161.22 ? 37 GLU A O 1 ATOM 256 C CB . GLU A 1 38 ? 31.204 13.069 10.140 1.00 165.14 ? 37 GLU A CB 1 ATOM 257 C CG . GLU A 1 38 ? 32.128 12.248 9.255 1.00 169.11 ? 37 GLU A CG 1 ATOM 258 C CD . GLU A 1 38 ? 32.406 12.885 7.901 1.00 174.10 ? 37 GLU A CD 1 ATOM 259 O OE1 . GLU A 1 38 ? 31.989 14.043 7.671 1.00 174.87 ? 37 GLU A OE1 1 ATOM 260 O OE2 . GLU A 1 38 ? 33.054 12.221 7.060 1.00 176.13 ? 37 GLU A OE2 1 ATOM 261 N N . SER A 1 39 ? 28.734 13.315 12.268 1.00 158.07 ? 38 SER A N 1 ATOM 262 C CA . SER A 1 39 ? 27.894 14.215 13.044 1.00 158.96 ? 38 SER A CA 1 ATOM 263 C C . SER A 1 39 ? 26.593 13.509 13.406 1.00 156.01 ? 38 SER A C 1 ATOM 264 O O . SER A 1 39 ? 26.407 12.333 13.080 1.00 152.70 ? 38 SER A O 1 ATOM 265 C CB . SER A 1 39 ? 27.595 15.460 12.209 1.00 162.15 ? 38 SER A CB 1 ATOM 266 O OG . SER A 1 39 ? 27.084 15.095 10.935 1.00 163.64 ? 38 SER A OG 1 ATOM 267 N N . TYR A 1 40 ? 25.700 14.223 14.088 1.00 156.45 ? 39 TYR A N 1 ATOM 268 C CA . TYR A 1 40 ? 24.346 13.725 14.333 1.00 156.05 ? 39 TYR A CA 1 ATOM 269 C C . TYR A 1 40 ? 23.564 13.702 13.022 1.00 155.16 ? 39 TYR A C 1 ATOM 270 O O . TYR A 1 40 ? 23.750 14.578 12.176 1.00 153.11 ? 39 TYR A O 1 ATOM 271 C CB . TYR A 1 40 ? 23.615 14.603 15.358 1.00 155.73 ? 39 TYR A CB 1 ATOM 272 C CG . TYR A 1 40 ? 23.854 14.194 16.790 1.00 156.52 ? 39 TYR A CG 1 ATOM 273 C CD1 . TYR A 1 40 ? 24.955 14.665 17.495 1.00 157.76 ? 39 TYR A CD1 1 ATOM 274 C CD2 . TYR A 1 40 ? 22.973 13.332 17.441 1.00 156.09 ? 39 TYR A CD2 1 ATOM 275 C CE1 . TYR A 1 40 ? 25.174 14.290 18.808 1.00 158.27 ? 39 TYR A CE1 1 ATOM 276 C CE2 . TYR A 1 40 ? 23.184 12.951 18.756 1.00 155.86 ? 39 TYR A CE2 1 ATOM 277 C CZ . TYR A 1 40 ? 24.285 13.434 19.433 1.00 157.15 ? 39 TYR A CZ 1 ATOM 278 O OH . TYR A 1 40 ? 24.503 13.060 20.736 1.00 159.36 ? 39 TYR A OH 1 ATOM 279 N N . PHE A 1 41 ? 22.704 12.697 12.859 1.00 155.03 ? 40 PHE A N 1 ATOM 280 C CA . PHE A 1 41 ? 21.883 12.561 11.658 1.00 153.65 ? 40 PHE A CA 1 ATOM 281 C C . PHE A 1 41 ? 20.477 12.155 12.072 1.00 153.36 ? 40 PHE A C 1 ATOM 282 O O . PHE A 1 41 ? 20.272 11.670 13.183 1.00 150.47 ? 40 PHE A O 1 ATOM 283 C CB . PHE A 1 41 ? 22.486 11.530 10.695 1.00 150.33 ? 40 PHE A CB 1 ATOM 284 C CG . PHE A 1 41 ? 22.255 10.104 11.104 1.00 146.20 ? 40 PHE A CG 1 ATOM 285 C CD1 . PHE A 1 41 ? 23.030 9.518 12.092 1.00 144.37 ? 40 PHE A CD1 1 ATOM 286 C CD2 . PHE A 1 41 ? 21.265 9.346 10.495 1.00 145.32 ? 40 PHE A CD2 1 ATOM 287 C CE1 . PHE A 1 41 ? 22.821 8.204 12.472 1.00 144.37 ? 40 PHE A CE1 1 ATOM 288 C CE2 . PHE A 1 41 ? 21.051 8.030 10.869 1.00 146.23 ? 40 PHE A CE2 1 ATOM 289 C CZ . PHE A 1 41 ? 21.830 7.458 11.859 1.00 144.77 ? 40 PHE A CZ 1 ATOM 290 N N . THR A 1 42 ? 19.519 12.362 11.171 1.00 153.27 ? 41 THR A N 1 ATOM 291 C CA . THR A 1 42 ? 18.110 12.092 11.447 1.00 148.83 ? 41 THR A CA 1 ATOM 292 C C . THR A 1 42 ? 17.854 10.590 11.450 1.00 144.90 ? 41 THR A C 1 ATOM 293 O O . THR A 1 42 ? 18.002 9.935 10.417 1.00 141.07 ? 41 THR A O 1 ATOM 294 C CB . THR A 1 42 ? 17.197 12.733 10.371 1.00 148.46 ? 41 THR A CB 1 ATOM 295 O OG1 . THR A 1 42 ? 17.494 14.128 10.243 1.00 153.22 ? 41 THR A OG1 1 ATOM 296 C CG2 . THR A 1 42 ? 15.725 12.562 10.726 1.00 146.04 ? 41 THR A CG2 1 ATOM 297 N N . ILE A 1 43 ? 17.476 10.051 12.609 1.00 143.53 ? 42 ILE A N 1 ATOM 298 C CA . ILE A 1 43 ? 17.108 8.632 12.720 1.00 142.39 ? 42 ILE A CA 1 ATOM 299 C C . ILE A 1 43 ? 15.595 8.436 12.543 1.00 136.04 ? 42 ILE A C 1 ATOM 300 O O . ILE A 1 43 ? 15.149 7.421 11.993 1.00 127.63 ? 42 ILE A O 1 ATOM 301 C CB . ILE A 1 43 ? 17.614 8.007 14.048 1.00 146.35 ? 42 ILE A CB 1 ATOM 302 C CG1 . ILE A 1 43 ? 17.696 6.483 13.934 1.00 144.86 ? 42 ILE A CG1 1 ATOM 303 C CG2 . ILE A 1 43 ? 16.750 8.410 15.240 1.00 148.72 ? 42 ILE A CG2 1 ATOM 304 C CD1 . ILE A 1 43 ? 18.322 5.816 15.140 1.00 145.85 ? 42 ILE A CD1 1 ATOM 305 N N . TRP A 1 44 ? 14.820 9.421 12.999 1.00 133.53 ? 43 TRP A N 1 ATOM 306 C CA . TRP A 1 44 ? 13.374 9.425 12.816 1.00 131.69 ? 43 TRP A CA 1 ATOM 307 C C . TRP A 1 44 ? 12.919 10.831 12.418 1.00 132.53 ? 43 TRP A C 1 ATOM 308 O O . TRP A 1 44 ? 13.250 11.783 13.119 1.00 135.77 ? 43 TRP A O 1 ATOM 309 C CB . TRP A 1 44 ? 12.674 9.019 14.106 1.00 131.88 ? 43 TRP A CB 1 ATOM 310 C CG . TRP A 1 44 ? 11.194 8.987 13.972 1.00 131.76 ? 43 TRP A CG 1 ATOM 311 C CD1 . TRP A 1 44 ? 10.310 9.919 14.426 1.00 132.71 ? 43 TRP A CD1 1 ATOM 312 C CD2 . TRP A 1 44 ? 10.418 7.977 13.323 1.00 132.99 ? 43 TRP A CD2 1 ATOM 313 N NE1 . TRP A 1 44 ? 9.026 9.546 14.112 1.00 133.42 ? 43 TRP A NE1 1 ATOM 314 C CE2 . TRP A 1 44 ? 9.064 8.358 13.433 1.00 133.32 ? 43 TRP A CE2 1 ATOM 315 C CE3 . TRP A 1 44 ? 10.736 6.781 12.665 1.00 134.50 ? 43 TRP A CE3 1 ATOM 316 C CZ2 . TRP A 1 44 ? 8.025 7.588 12.908 1.00 135.59 ? 43 TRP A CZ2 1 ATOM 317 C CZ3 . TRP A 1 44 ? 9.703 6.014 12.146 1.00 135.97 ? 43 TRP A CZ3 1 ATOM 318 C CH2 . TRP A 1 44 ? 8.363 6.424 12.268 1.00 137.37 ? 43 TRP A CH2 1 ATOM 319 N N . LEU A 1 45 ? 12.188 10.995 11.310 1.00 130.44 ? 44 LEU A N 1 ATOM 320 C CA . LEU A 1 45 ? 11.818 9.924 10.376 1.00 129.46 ? 44 LEU A CA 1 ATOM 321 C C . LEU A 1 45 ? 12.734 9.962 9.155 1.00 128.80 ? 44 LEU A C 1 ATOM 322 O O . LEU A 1 45 ? 12.903 11.016 8.546 1.00 126.27 ? 44 LEU A O 1 ATOM 323 C CB . LEU A 1 45 ? 10.368 10.109 9.928 1.00 128.76 ? 44 LEU A CB 1 ATOM 324 C CG . LEU A 1 45 ? 9.867 9.210 8.795 1.00 130.40 ? 44 LEU A CG 1 ATOM 325 C CD1 . LEU A 1 45 ? 10.133 7.741 9.087 1.00 130.31 ? 44 LEU A CD1 1 ATOM 326 C CD2 . LEU A 1 45 ? 8.384 9.458 8.572 1.00 130.46 ? 44 LEU A CD2 1 ATOM 327 N N . ASN A 1 46 ? 13.331 8.821 8.815 1.00 128.13 ? 45 ASN A N 1 ATOM 328 C CA . ASN A 1 46 ? 14.092 8.698 7.579 1.00 129.89 ? 45 ASN A CA 1 ATOM 329 C C . ASN A 1 46 ? 13.654 7.448 6.838 1.00 128.36 ? 45 ASN A C 1 ATOM 330 O O . ASN A 1 46 ? 13.965 6.338 7.252 1.00 129.16 ? 45 ASN A O 1 ATOM 331 C CB . ASN A 1 46 ? 15.596 8.659 7.862 1.00 132.85 ? 45 ASN A CB 1 ATOM 332 C CG . ASN A 1 46 ? 16.431 8.933 6.621 1.00 137.74 ? 45 ASN A CG 1 ATOM 333 O OD1 . ASN A 1 46 ? 16.012 8.653 5.495 1.00 137.36 ? 45 ASN A OD1 1 ATOM 334 N ND2 . ASN A 1 46 ? 17.620 9.491 6.822 1.00 141.35 ? 45 ASN A ND2 1 ATOM 335 N N . LEU A 1 47 ? 12.940 7.646 5.735 1.00 129.33 ? 46 LEU A N 1 ATOM 336 C CA . LEU A 1 47 ? 12.349 6.545 4.979 1.00 131.94 ? 46 LEU A CA 1 ATOM 337 C C . LEU A 1 47 ? 13.395 5.651 4.337 1.00 132.66 ? 46 LEU A C 1 ATOM 338 O O . LEU A 1 47 ? 13.167 4.461 4.158 1.00 133.81 ? 46 LEU A O 1 ATOM 339 C CB . LEU A 1 47 ? 11.418 7.082 3.895 1.00 137.11 ? 46 LEU A CB 1 ATOM 340 C CG . LEU A 1 47 ? 10.228 7.896 4.403 1.00 140.39 ? 46 LEU A CG 1 ATOM 341 C CD1 . LEU A 1 47 ? 9.491 8.528 3.231 1.00 146.29 ? 46 LEU A CD1 1 ATOM 342 C CD2 . LEU A 1 47 ? 9.297 7.029 5.238 1.00 135.00 ? 46 LEU A CD2 1 ATOM 343 N N . GLU A 1 48 ? 14.546 6.217 3.997 1.00 136.37 ? 47 GLU A N 1 ATOM 344 C CA . GLU A 1 48 ? 15.614 5.442 3.370 1.00 141.53 ? 47 GLU A CA 1 ATOM 345 C C . GLU A 1 48 ? 16.186 4.366 4.302 1.00 141.34 ? 47 GLU A C 1 ATOM 346 O O . GLU A 1 48 ? 16.717 3.352 3.838 1.00 142.23 ? 47 GLU A O 1 ATOM 347 C CB . GLU A 1 48 ? 16.735 6.369 2.886 1.00 148.28 ? 47 GLU A CB 1 ATOM 348 C CG . GLU A 1 48 ? 16.316 7.312 1.763 1.00 155.53 ? 47 GLU A CG 1 ATOM 349 C CD . GLU A 1 48 ? 17.445 8.202 1.271 1.00 162.82 ? 47 GLU A CD 1 ATOM 350 O OE1 . GLU A 1 48 ? 18.238 8.695 2.104 1.00 166.01 ? 47 GLU A OE1 1 ATOM 351 O OE2 . GLU A 1 48 ? 17.535 8.418 0.043 1.00 163.78 ? 47 GLU A OE2 1 ATOM 352 N N . LEU A 1 49 ? 16.069 4.582 5.611 1.00 139.55 ? 48 LEU A N 1 ATOM 353 C CA . LEU A 1 49 ? 16.591 3.635 6.594 1.00 138.70 ? 48 LEU A CA 1 ATOM 354 C C . LEU A 1 49 ? 15.624 2.491 6.889 1.00 133.21 ? 48 LEU A C 1 ATOM 355 O O . LEU A 1 49 ? 16.002 1.528 7.564 1.00 133.75 ? 48 LEU A O 1 ATOM 356 C CB . LEU A 1 49 ? 16.933 4.357 7.899 1.00 142.17 ? 48 LEU A CB 1 ATOM 357 C CG . LEU A 1 49 ? 18.030 5.422 7.804 1.00 147.26 ? 48 LEU A CG 1 ATOM 358 C CD1 . LEU A 1 49 ? 18.140 6.192 9.111 1.00 149.87 ? 48 LEU A CD1 1 ATOM 359 C CD2 . LEU A 1 49 ? 19.369 4.797 7.438 1.00 149.46 ? 48 LEU A CD2 1 ATOM 360 N N . LEU A 1 50 ? 14.395 2.591 6.379 1.00 127.44 ? 49 LEU A N 1 ATOM 361 C CA . LEU A 1 50 ? 13.332 1.630 6.688 1.00 127.87 ? 49 LEU A CA 1 ATOM 362 C C . LEU A 1 50 ? 13.078 0.609 5.573 1.00 131.84 ? 49 LEU A C 1 ATOM 363 O O . LEU A 1 50 ? 12.166 -0.215 5.663 1.00 136.69 ? 49 LEU A O 1 ATOM 364 C CB . LEU A 1 50 ? 12.041 2.375 7.023 1.00 125.24 ? 49 LEU A CB 1 ATOM 365 C CG . LEU A 1 50 ? 12.176 3.459 8.100 1.00 125.59 ? 49 LEU A CG 1 ATOM 366 C CD1 . LEU A 1 50 ? 10.813 4.035 8.441 1.00 126.20 ? 49 LEU A CD1 1 ATOM 367 C CD2 . LEU A 1 50 ? 12.861 2.943 9.359 1.00 122.38 ? 49 LEU A CD2 1 ATOM 368 N N . LEU A 1 51 ? 13.915 0.629 4.545 1.00 132.96 ? 50 LEU A N 1 ATOM 369 C CA . LEU A 1 51 ? 13.812 -0.345 3.473 1.00 136.29 ? 50 LEU A CA 1 ATOM 370 C C . LEU A 1 51 ? 14.350 -1.700 3.961 1.00 138.31 ? 50 LEU A C 1 ATOM 371 O O . LEU A 1 51 ? 15.124 -1.765 4.928 1.00 136.71 ? 50 LEU A O 1 ATOM 372 C CB . LEU A 1 51 ? 14.595 0.139 2.255 1.00 140.56 ? 50 LEU A CB 1 ATOM 373 C CG . LEU A 1 51 ? 14.344 1.595 1.843 1.00 145.16 ? 50 LEU A CG 1 ATOM 374 C CD1 . LEU A 1 51 ? 15.242 1.994 0.677 1.00 150.85 ? 50 LEU A CD1 1 ATOM 375 C CD2 . LEU A 1 51 ? 12.870 1.814 1.527 1.00 146.09 ? 50 LEU A CD2 1 ATOM 376 N N . PRO A 1 52 ? 13.942 -2.797 3.299 1.00 140.93 ? 51 PRO A N 1 ATOM 377 C CA . PRO A 1 52 ? 14.516 -4.101 3.617 1.00 141.50 ? 51 PRO A CA 1 ATOM 378 C C . PRO A 1 52 ? 16.045 -4.092 3.657 1.00 143.85 ? 51 PRO A C 1 ATOM 379 O O . PRO A 1 52 ? 16.688 -3.327 2.930 1.00 141.76 ? 51 PRO A O 1 ATOM 380 C CB . PRO A 1 52 ? 14.007 -4.987 2.483 1.00 141.90 ? 51 PRO A CB 1 ATOM 381 C CG . PRO A 1 52 ? 12.690 -4.392 2.126 1.00 141.87 ? 51 PRO A CG 1 ATOM 382 C CD . PRO A 1 52 ? 12.830 -2.909 2.337 1.00 141.62 ? 51 PRO A CD 1 ATOM 383 N N . VAL A 1 53 ? 16.606 -4.952 4.507 1.00 147.50 ? 52 VAL A N 1 ATOM 384 C CA . VAL A 1 53 ? 18.055 -5.061 4.748 1.00 149.85 ? 52 VAL A CA 1 ATOM 385 C C . VAL A 1 53 ? 18.590 -3.903 5.595 1.00 148.15 ? 52 VAL A C 1 ATOM 386 O O . VAL A 1 53 ? 19.104 -4.117 6.702 1.00 146.03 ? 52 VAL A O 1 ATOM 387 C CB . VAL A 1 53 ? 18.891 -5.140 3.435 1.00 152.73 ? 52 VAL A CB 1 ATOM 388 C CG1 . VAL A 1 53 ? 20.299 -5.639 3.727 1.00 155.96 ? 52 VAL A CG1 1 ATOM 389 C CG2 . VAL A 1 53 ? 18.229 -6.012 2.369 1.00 154.81 ? 52 VAL A CG2 1 ATOM 390 N N . ILE A 1 54 ? 18.476 -2.683 5.069 1.00 143.94 ? 53 ILE A N 1 ATOM 391 C CA . ILE A 1 54 ? 18.946 -1.490 5.773 1.00 139.29 ? 53 ILE A CA 1 ATOM 392 C C . ILE A 1 54 ? 18.226 -1.362 7.115 1.00 133.67 ? 53 ILE A C 1 ATOM 393 O O . ILE A 1 54 ? 18.796 -0.867 8.091 1.00 129.37 ? 53 ILE A O 1 ATOM 394 C CB . ILE A 1 54 ? 18.745 -0.202 4.934 1.00 141.38 ? 53 ILE A CB 1 ATOM 395 C CG1 . ILE A 1 54 ? 19.555 -0.274 3.625 1.00 146.46 ? 53 ILE A CG1 1 ATOM 396 C CG2 . ILE A 1 54 ? 19.164 1.032 5.729 1.00 141.29 ? 53 ILE A CG2 1 ATOM 397 C CD1 . ILE A 1 54 ? 18.750 -0.638 2.390 1.00 149.74 ? 53 ILE A CD1 1 ATOM 398 N N . ILE A 1 55 ? 16.979 -1.825 7.158 1.00 129.65 ? 54 ILE A N 1 ATOM 399 C CA . ILE A 1 55 ? 16.200 -1.839 8.389 1.00 127.00 ? 54 ILE A CA 1 ATOM 400 C C . ILE A 1 55 ? 16.931 -2.467 9.575 1.00 123.00 ? 54 ILE A C 1 ATOM 401 O O . ILE A 1 55 ? 16.749 -2.028 10.710 1.00 122.15 ? 54 ILE A O 1 ATOM 402 C CB . ILE A 1 55 ? 14.857 -2.579 8.198 1.00 126.86 ? 54 ILE A CB 1 ATOM 403 C CG1 . ILE A 1 55 ? 13.985 -2.419 9.451 1.00 128.85 ? 54 ILE A CG1 1 ATOM 404 C CG2 . ILE A 1 55 ? 15.076 -4.052 7.868 1.00 126.36 ? 54 ILE A CG2 1 ATOM 405 C CD1 . ILE A 1 55 ? 13.242 -1.101 9.517 1.00 129.13 ? 54 ILE A CD1 1 ATOM 406 N N . ASP A 1 56 ? 17.737 -3.493 9.325 1.00 120.63 ? 55 ASP A N 1 ATOM 407 C CA . ASP A 1 56 ? 18.443 -4.156 10.419 1.00 124.01 ? 55 ASP A CA 1 ATOM 408 C C . ASP A 1 56 ? 19.435 -3.220 11.107 1.00 126.15 ? 55 ASP A C 1 ATOM 409 O O . ASP A 1 56 ? 19.570 -3.246 12.337 1.00 123.10 ? 55 ASP A O 1 ATOM 410 C CB . ASP A 1 56 ? 19.139 -5.428 9.934 1.00 127.67 ? 55 ASP A CB 1 ATOM 411 C CG . ASP A 1 56 ? 18.165 -6.566 9.666 1.00 127.39 ? 55 ASP A CG 1 ATOM 412 O OD1 . ASP A 1 56 ? 17.094 -6.614 10.313 1.00 123.61 ? 55 ASP A OD1 1 ATOM 413 O OD2 . ASP A 1 56 ? 18.475 -7.419 8.809 1.00 126.46 ? 55 ASP A OD2 1 ATOM 414 N N . CYS A 1 57 ? 20.108 -2.387 10.314 1.00 131.23 ? 56 CYS A N 1 ATOM 415 C CA . CYS A 1 57 ? 21.038 -1.393 10.860 1.00 136.92 ? 56 CYS A CA 1 ATOM 416 C C . CYS A 1 57 ? 20.285 -0.356 11.690 1.00 133.53 ? 56 CYS A C 1 ATOM 417 O O . CYS A 1 57 ? 20.715 0.014 12.780 1.00 131.92 ? 56 CYS A O 1 ATOM 418 C CB . CYS A 1 57 ? 21.806 -0.694 9.736 1.00 143.82 ? 56 CYS A CB 1 ATOM 419 S SG . CYS A 1 57 ? 22.466 -1.807 8.469 1.00 154.98 ? 56 CYS A SG 1 ATOM 420 N N . TRP A 1 58 ? 19.156 0.103 11.160 1.00 133.47 ? 57 TRP A N 1 ATOM 421 C CA . TRP A 1 58 ? 18.310 1.088 11.833 1.00 132.08 ? 57 TRP A CA 1 ATOM 422 C C . TRP A 1 58 ? 17.798 0.561 13.174 1.00 129.54 ? 57 TRP A C 1 ATOM 423 O O . TRP A 1 58 ? 17.907 1.240 14.199 1.00 129.22 ? 57 TRP A O 1 ATOM 424 C CB . TRP A 1 58 ? 17.136 1.459 10.919 1.00 131.02 ? 57 TRP A CB 1 ATOM 425 C CG . TRP A 1 58 ? 16.188 2.458 11.491 1.00 126.84 ? 57 TRP A CG 1 ATOM 426 C CD1 . TRP A 1 58 ? 16.361 3.809 11.562 1.00 128.96 ? 57 TRP A CD1 1 ATOM 427 C CD2 . TRP A 1 58 ? 14.902 2.188 12.053 1.00 120.74 ? 57 TRP A CD2 1 ATOM 428 N NE1 . TRP A 1 58 ? 15.264 4.398 12.143 1.00 127.59 ? 57 TRP A NE1 1 ATOM 429 C CE2 . TRP A 1 58 ? 14.353 3.423 12.454 1.00 121.94 ? 57 TRP A CE2 1 ATOM 430 C CE3 . TRP A 1 58 ? 14.160 1.022 12.259 1.00 116.05 ? 57 TRP A CE3 1 ATOM 431 C CZ2 . TRP A 1 58 ? 13.096 3.525 13.049 1.00 118.30 ? 57 TRP A CZ2 1 ATOM 432 C CZ3 . TRP A 1 58 ? 12.913 1.123 12.851 1.00 115.18 ? 57 TRP A CZ3 1 ATOM 433 C CH2 . TRP A 1 58 ? 12.394 2.365 13.241 1.00 116.00 ? 57 TRP A CH2 1 ATOM 434 N N . ILE A 1 59 ? 17.251 -0.653 13.161 1.00 127.84 ? 58 ILE A N 1 ATOM 435 C CA . ILE A 1 59 ? 16.769 -1.304 14.382 1.00 129.12 ? 58 ILE A CA 1 ATOM 436 C C . ILE A 1 59 ? 17.896 -1.403 15.407 1.00 128.35 ? 58 ILE A C 1 ATOM 437 O O . ILE A 1 59 ? 17.697 -1.127 16.588 1.00 122.78 ? 58 ILE A O 1 ATOM 438 C CB . ILE A 1 59 ? 16.207 -2.721 14.095 1.00 131.16 ? 58 ILE A CB 1 ATOM 439 C CG1 . ILE A 1 59 ? 14.885 -2.625 13.322 1.00 129.77 ? 58 ILE A CG1 1 ATOM 440 C CG2 . ILE A 1 59 ? 15.973 -3.486 15.397 1.00 133.36 ? 58 ILE A CG2 1 ATOM 441 C CD1 . ILE A 1 59 ? 14.406 -3.941 12.742 1.00 130.81 ? 58 ILE A CD1 1 ATOM 442 N N . ASP A 1 60 ? 19.079 -1.791 14.942 1.00 132.96 ? 59 ASP A N 1 ATOM 443 C CA . ASP A 1 60 ? 20.236 -1.951 15.817 1.00 138.13 ? 59 ASP A CA 1 ATOM 444 C C . ASP A 1 60 ? 20.610 -0.644 16.533 1.00 136.37 ? 59 ASP A C 1 ATOM 445 O O . ASP A 1 60 ? 21.127 -0.677 17.654 1.00 143.37 ? 59 ASP A O 1 ATOM 446 C CB . ASP A 1 60 ? 21.432 -2.476 15.004 1.00 143.93 ? 59 ASP A CB 1 ATOM 447 C CG . ASP A 1 60 ? 22.530 -3.076 15.873 1.00 148.70 ? 59 ASP A CG 1 ATOM 448 O OD1 . ASP A 1 60 ? 22.258 -3.455 17.032 1.00 149.19 ? 59 ASP A OD1 1 ATOM 449 O OD2 . ASP A 1 60 ? 23.675 -3.175 15.385 1.00 153.32 ? 59 ASP A OD2 1 ATOM 450 N N . ASN A 1 61 ? 20.339 0.491 15.888 1.00 130.07 ? 60 ASN A N 1 ATOM 451 C CA . ASN A 1 61 ? 20.655 1.811 16.438 1.00 130.07 ? 60 ASN A CA 1 ATOM 452 C C . ASN A 1 61 ? 19.530 2.406 17.295 1.00 131.53 ? 60 ASN A C 1 ATOM 453 O O . ASN A 1 61 ? 19.792 3.038 18.325 1.00 137.40 ? 60 ASN A O 1 ATOM 454 C CB . ASN A 1 61 ? 20.977 2.788 15.299 1.00 128.58 ? 60 ASN A CB 1 ATOM 455 C CG . ASN A 1 61 ? 22.127 2.318 14.423 1.00 130.47 ? 60 ASN A CG 1 ATOM 456 O OD1 . ASN A 1 61 ? 23.074 1.693 14.900 1.00 132.76 ? 60 ASN A OD1 1 ATOM 457 N ND2 . ASN A 1 61 ? 22.048 2.621 13.130 1.00 129.38 ? 60 ASN A ND2 1 ATOM 458 N N . ILE A 1 62 ? 18.285 2.213 16.862 1.00 128.27 ? 61 ILE A N 1 ATOM 459 C CA . ILE A 1 62 ? 17.134 2.868 17.499 1.00 125.34 ? 61 ILE A CA 1 ATOM 460 C C . ILE A 1 62 ? 16.531 2.092 18.667 1.00 123.51 ? 61 ILE A C 1 ATOM 461 O O . ILE A 1 62 ? 15.829 2.667 19.502 1.00 117.83 ? 61 ILE A O 1 ATOM 462 C CB . ILE A 1 62 ? 16.024 3.169 16.471 1.00 123.63 ? 61 ILE A CB 1 ATOM 463 C CG1 . ILE A 1 62 ? 15.059 4.224 17.022 1.00 124.07 ? 61 ILE A CG1 1 ATOM 464 C CG2 . ILE A 1 62 ? 15.277 1.900 16.069 1.00 122.63 ? 61 ILE A CG2 1 ATOM 465 C CD1 . ILE A 1 62 ? 14.134 4.801 15.976 1.00 127.18 ? 61 ILE A CD1 1 ATOM 466 N N . ARG A 1 63 ? 16.783 0.789 18.711 1.00 124.96 ? 62 ARG A N 1 ATOM 467 C CA . ARG A 1 63 ? 16.312 -0.038 19.816 1.00 130.78 ? 62 ARG A CA 1 ATOM 468 C C . ARG A 1 63 ? 16.876 0.458 21.149 1.00 130.63 ? 62 ARG A C 1 ATOM 469 O O . ARG A 1 63 ? 17.987 0.987 21.201 1.00 131.35 ? 62 ARG A O 1 ATOM 470 C CB . ARG A 1 63 ? 16.717 -1.500 19.601 1.00 136.23 ? 62 ARG A CB 1 ATOM 471 C CG . ARG A 1 63 ? 18.216 -1.752 19.681 1.00 141.93 ? 62 ARG A CG 1 ATOM 472 C CD . ARG A 1 63 ? 18.576 -3.137 19.175 1.00 147.43 ? 62 ARG A CD 1 ATOM 473 N NE . ARG A 1 63 ? 19.958 -3.486 19.498 1.00 154.72 ? 62 ARG A NE 1 ATOM 474 C CZ . ARG A 1 63 ? 20.384 -3.889 20.695 1.00 161.43 ? 62 ARG A CZ 1 ATOM 475 N NH1 . ARG A 1 63 ? 19.544 -4.000 21.722 1.00 162.88 ? 62 ARG A NH1 1 ATOM 476 N NH2 . ARG A 1 63 ? 21.669 -4.181 20.872 1.00 167.15 ? 62 ARG A NH2 1 ATOM 477 N N . LEU A 1 64 ? 16.092 0.297 22.212 1.00 127.85 ? 63 LEU A N 1 ATOM 478 C CA . LEU A 1 64 ? 16.559 0.543 23.577 1.00 127.58 ? 63 LEU A CA 1 ATOM 479 C C . LEU A 1 64 ? 16.969 -0.780 24.205 1.00 127.09 ? 63 LEU A C 1 ATOM 480 O O . LEU A 1 64 ? 16.317 -1.805 23.989 1.00 124.14 ? 63 LEU A O 1 ATOM 481 C CB . LEU A 1 64 ? 15.455 1.182 24.422 1.00 125.43 ? 63 LEU A CB 1 ATOM 482 C CG . LEU A 1 64 ? 15.064 2.611 24.048 1.00 124.33 ? 63 LEU A CG 1 ATOM 483 C CD1 . LEU A 1 64 ? 13.816 3.023 24.812 1.00 123.89 ? 63 LEU A CD1 1 ATOM 484 C CD2 . LEU A 1 64 ? 16.211 3.577 24.315 1.00 124.95 ? 63 LEU A CD2 1 ATOM 485 N N . VAL A 1 65 ? 18.050 -0.751 24.978 1.00 128.51 ? 64 VAL A N 1 ATOM 486 C CA . VAL A 1 65 ? 18.545 -1.942 25.659 1.00 130.50 ? 64 VAL A CA 1 ATOM 487 C C . VAL A 1 65 ? 18.064 -1.898 27.104 1.00 128.93 ? 64 VAL A C 1 ATOM 488 O O . VAL A 1 65 ? 18.353 -0.944 27.825 1.00 126.03 ? 64 VAL A O 1 ATOM 489 C CB . VAL A 1 65 ? 20.088 -2.006 25.636 1.00 135.10 ? 64 VAL A CB 1 ATOM 490 C CG1 . VAL A 1 65 ? 20.572 -3.376 26.095 1.00 137.73 ? 64 VAL A CG1 1 ATOM 491 C CG2 . VAL A 1 65 ? 20.614 -1.693 24.240 1.00 135.79 ? 64 VAL A CG2 1 ATOM 492 N N . TYR A 1 66 ? 17.325 -2.923 27.519 1.00 127.09 ? 65 TYR A N 1 ATOM 493 C CA . TYR A 1 66 ? 16.776 -2.966 28.862 1.00 129.51 ? 65 TYR A CA 1 ATOM 494 C C . TYR A 1 66 ? 17.748 -3.657 29.809 1.00 133.98 ? 65 TYR A C 1 ATOM 495 O O . TYR A 1 66 ? 18.149 -4.796 29.577 1.00 133.77 ? 65 TYR A O 1 ATOM 496 C CB . TYR A 1 66 ? 15.433 -3.691 28.870 1.00 129.95 ? 65 TYR A CB 1 ATOM 497 C CG . TYR A 1 66 ? 14.675 -3.519 30.165 1.00 133.21 ? 65 TYR A CG 1 ATOM 498 C CD1 . TYR A 1 66 ? 13.923 -2.372 30.405 1.00 131.40 ? 65 TYR A CD1 1 ATOM 499 C CD2 . TYR A 1 66 ? 14.714 -4.498 31.155 1.00 136.50 ? 65 TYR A CD2 1 ATOM 500 C CE1 . TYR A 1 66 ? 13.227 -2.206 31.591 1.00 131.12 ? 65 TYR A CE1 1 ATOM 501 C CE2 . TYR A 1 66 ? 14.020 -4.339 32.344 1.00 137.83 ? 65 TYR A CE2 1 ATOM 502 C CZ . TYR A 1 66 ? 13.279 -3.191 32.555 1.00 135.82 ? 65 TYR A CZ 1 ATOM 503 O OH . TYR A 1 66 ? 12.589 -3.026 33.731 1.00 138.35 ? 65 TYR A OH 1 ATOM 504 N N . ASN A 1 67 ? 18.126 -2.955 30.872 1.00 137.87 ? 66 ASN A N 1 ATOM 505 C CA . ASN A 1 67 ? 18.975 -3.516 31.916 1.00 144.56 ? 66 ASN A CA 1 ATOM 506 C C . ASN A 1 67 ? 18.060 -4.016 33.040 1.00 146.29 ? 66 ASN A C 1 ATOM 507 O O . ASN A 1 67 ? 17.460 -3.215 33.760 1.00 141.91 ? 66 ASN A O 1 ATOM 508 C CB . ASN A 1 67 ? 19.947 -2.433 32.422 1.00 150.18 ? 66 ASN A CB 1 ATOM 509 C CG . ASN A 1 67 ? 20.993 -2.970 33.392 1.00 158.01 ? 66 ASN A CG 1 ATOM 510 O OD1 . ASN A 1 67 ? 21.046 -4.171 33.675 1.00 164.96 ? 66 ASN A OD1 1 ATOM 511 N ND2 . ASN A 1 67 ? 21.831 -2.066 33.921 1.00 160.95 ? 66 ASN A ND2 1 ATOM 512 N N . LYS A 1 68 ? 17.943 -5.340 33.162 1.00 150.84 ? 67 LYS A N 1 ATOM 513 C CA . LYS A 1 68 ? 17.024 -5.969 34.121 1.00 153.18 ? 67 LYS A CA 1 ATOM 514 C C . LYS A 1 68 ? 17.395 -5.700 35.580 1.00 153.63 ? 67 LYS A C 1 ATOM 515 O O . LYS A 1 68 ? 16.515 -5.635 36.443 1.00 153.22 ? 67 LYS A O 1 ATOM 516 C CB . LYS A 1 68 ? 16.943 -7.490 33.898 1.00 157.14 ? 67 LYS A CB 1 ATOM 517 C CG . LYS A 1 68 ? 16.032 -7.937 32.758 1.00 158.31 ? 67 LYS A CG 1 ATOM 518 C CD . LYS A 1 68 ? 15.606 -9.393 32.930 1.00 159.93 ? 67 LYS A CD 1 ATOM 519 C CE . LYS A 1 68 ? 14.648 -9.856 31.841 1.00 157.26 ? 67 LYS A CE 1 ATOM 520 N NZ . LYS A 1 68 ? 15.346 -10.196 30.571 1.00 156.19 ? 67 LYS A NZ 1 ATOM 521 N N . THR A 1 69 ? 18.689 -5.553 35.855 1.00 154.26 ? 68 THR A N 1 ATOM 522 C CA . THR A 1 69 ? 19.159 -5.308 37.218 1.00 155.44 ? 68 THR A CA 1 ATOM 523 C C . THR A 1 69 ? 18.836 -3.882 37.666 1.00 154.23 ? 68 THR A C 1 ATOM 524 O O . THR A 1 69 ? 18.292 -3.679 38.749 1.00 156.34 ? 68 THR A O 1 ATOM 525 C CB . THR A 1 69 ? 20.669 -5.580 37.363 1.00 158.21 ? 68 THR A CB 1 ATOM 526 O OG1 . THR A 1 69 ? 21.398 -4.786 36.423 1.00 158.13 ? 68 THR A OG1 1 ATOM 527 C CG2 . THR A 1 69 ? 20.975 -7.053 37.120 1.00 159.88 ? 68 THR A CG2 1 ATOM 528 N N . SER A 1 70 ? 19.152 -2.897 36.829 1.00 152.24 ? 69 SER A N 1 ATOM 529 C CA . SER A 1 70 ? 18.858 -1.503 37.155 1.00 151.71 ? 69 SER A CA 1 ATOM 530 C C . SER A 1 70 ? 17.414 -1.090 36.850 1.00 149.31 ? 69 SER A C 1 ATOM 531 O O . SER A 1 70 ? 16.989 -0.011 37.263 1.00 148.04 ? 69 SER A O 1 ATOM 532 C CB . SER A 1 70 ? 19.825 -0.564 36.429 1.00 150.90 ? 69 SER A CB 1 ATOM 533 O OG . SER A 1 70 ? 19.634 -0.601 35.027 1.00 147.16 ? 69 SER A OG 1 ATOM 534 N N . ARG A 1 71 ? 16.668 -1.932 36.130 1.00 148.05 ? 70 ARG A N 1 ATOM 535 C CA . ARG A 1 71 ? 15.296 -1.609 35.718 1.00 146.50 ? 70 ARG A CA 1 ATOM 536 C C . ARG A 1 71 ? 15.271 -0.274 34.951 1.00 144.39 ? 70 ARG A C 1 ATOM 537 O O . ARG A 1 71 ? 14.456 0.607 35.235 1.00 143.04 ? 70 ARG A O 1 ATOM 538 C CB . ARG A 1 71 ? 14.334 -1.553 36.927 1.00 147.88 ? 70 ARG A CB 1 ATOM 539 C CG . ARG A 1 71 ? 14.006 -2.874 37.626 1.00 151.63 ? 70 ARG A CG 1 ATOM 540 C CD . ARG A 1 71 ? 13.199 -3.824 36.760 1.00 153.85 ? 70 ARG A CD 1 ATOM 541 N NE . ARG A 1 71 ? 12.300 -4.701 37.523 1.00 157.08 ? 70 ARG A NE 1 ATOM 542 C CZ . ARG A 1 71 ? 10.977 -4.551 37.653 1.00 159.17 ? 70 ARG A CZ 1 ATOM 543 N NH1 . ARG A 1 71 ? 10.328 -3.543 37.081 1.00 161.25 ? 70 ARG A NH1 1 ATOM 544 N NH2 . ARG A 1 71 ? 10.281 -5.428 38.371 1.00 160.42 ? 70 ARG A NH2 1 ATOM 545 N N . ALA A 1 72 ? 16.176 -0.134 33.983 1.00 142.60 ? 71 ALA A N 1 ATOM 546 C CA . ALA A 1 72 ? 16.291 1.096 33.198 1.00 138.10 ? 71 ALA A CA 1 ATOM 547 C C . ALA A 1 72 ? 16.842 0.781 31.815 1.00 134.58 ? 71 ALA A C 1 ATOM 548 O O . ALA A 1 72 ? 17.495 -0.244 31.626 1.00 136.34 ? 71 ALA A O 1 ATOM 549 C CB . ALA A 1 72 ? 17.199 2.085 33.908 1.00 140.80 ? 71 ALA A CB 1 ATOM 550 N N . THR A 1 73 ? 16.569 1.657 30.853 1.00 128.44 ? 72 THR A N 1 ATOM 551 C CA . THR A 1 73 ? 17.037 1.456 29.487 1.00 127.97 ? 72 THR A CA 1 ATOM 552 C C . THR A 1 73 ? 18.355 2.171 29.252 1.00 131.49 ? 72 THR A C 1 ATOM 553 O O . THR A 1 73 ? 18.681 3.141 29.934 1.00 131.00 ? 72 THR A O 1 ATOM 554 C CB . THR A 1 73 ? 16.027 1.981 28.454 1.00 124.66 ? 72 THR A CB 1 ATOM 555 O OG1 . THR A 1 73 ? 15.775 3.371 28.690 1.00 122.78 ? 72 THR A OG1 1 ATOM 556 C CG2 . THR A 1 73 ? 14.727 1.208 28.539 1.00 124.57 ? 72 THR A CG2 1 ATOM 557 N N . GLN A 1 74 ? 19.102 1.674 28.272 1.00 134.53 ? 73 GLN A N 1 ATOM 558 C CA . GLN A 1 74 ? 20.338 2.300 27.816 1.00 139.00 ? 73 GLN A CA 1 ATOM 559 C C . GLN A 1 74 ? 20.315 2.307 26.296 1.00 139.22 ? 73 GLN A C 1 ATOM 560 O O . GLN A 1 74 ? 19.578 1.535 25.671 1.00 134.51 ? 73 GLN A O 1 ATOM 561 C CB . GLN A 1 74 ? 21.558 1.494 28.280 1.00 145.24 ? 73 GLN A CB 1 ATOM 562 C CG . GLN A 1 74 ? 21.608 1.205 29.776 1.00 150.85 ? 73 GLN A CG 1 ATOM 563 C CD . GLN A 1 74 ? 22.787 0.330 30.174 1.00 154.34 ? 73 GLN A CD 1 ATOM 564 O OE1 . GLN A 1 74 ? 23.661 0.027 29.359 1.00 157.81 ? 73 GLN A OE1 1 ATOM 565 N NE2 . GLN A 1 74 ? 22.813 -0.084 31.436 1.00 153.99 ? 73 GLN A NE2 1 ATOM 566 N N . PHE A 1 75 ? 21.128 3.170 25.699 1.00 143.98 ? 74 PHE A N 1 ATOM 567 C CA . PHE A 1 75 ? 21.305 3.143 24.253 1.00 146.49 ? 74 PHE A CA 1 ATOM 568 C C . PHE A 1 75 ? 22.263 2.005 23.907 1.00 146.59 ? 74 PHE A C 1 ATOM 569 O O . PHE A 1 75 ? 23.062 1.587 24.748 1.00 144.83 ? 74 PHE A O 1 ATOM 570 C CB . PHE A 1 75 ? 21.869 4.468 23.731 1.00 150.42 ? 74 PHE A CB 1 ATOM 571 C CG . PHE A 1 75 ? 21.086 5.679 24.159 1.00 154.35 ? 74 PHE A CG 1 ATOM 572 C CD1 . PHE A 1 75 ? 19.695 5.680 24.127 1.00 154.88 ? 74 PHE A CD1 1 ATOM 573 C CD2 . PHE A 1 75 ? 21.744 6.830 24.579 1.00 159.55 ? 74 PHE A CD2 1 ATOM 574 C CE1 . PHE A 1 75 ? 18.980 6.800 24.518 1.00 157.60 ? 74 PHE A CE1 1 ATOM 575 C CE2 . PHE A 1 75 ? 21.033 7.953 24.968 1.00 161.02 ? 74 PHE A CE2 1 ATOM 576 C CZ . PHE A 1 75 ? 19.649 7.939 24.937 1.00 160.20 ? 74 PHE A CZ 1 ATOM 577 N N . PRO A 1 76 ? 22.184 1.490 22.669 1.00 147.45 ? 75 PRO A N 1 ATOM 578 C CA . PRO A 1 76 ? 23.172 0.502 22.238 1.00 151.34 ? 75 PRO A CA 1 ATOM 579 C C . PRO A 1 76 ? 24.600 1.040 22.327 1.00 157.55 ? 75 PRO A C 1 ATOM 580 O O . PRO A 1 76 ? 24.811 2.253 22.298 1.00 158.79 ? 75 PRO A O 1 ATOM 581 C CB . PRO A 1 76 ? 22.789 0.232 20.777 1.00 148.82 ? 75 PRO A CB 1 ATOM 582 C CG . PRO A 1 76 ? 21.345 0.586 20.686 1.00 146.21 ? 75 PRO A CG 1 ATOM 583 C CD . PRO A 1 76 ? 21.139 1.713 21.654 1.00 146.05 ? 75 PRO A CD 1 ATOM 584 N N . ASP A 1 77 ? 25.572 0.144 22.438 1.00 165.07 ? 76 ASP A N 1 ATOM 585 C CA . ASP A 1 77 ? 26.960 0.566 22.581 1.00 172.07 ? 76 ASP A CA 1 ATOM 586 C C . ASP A 1 77 ? 27.380 1.415 21.374 1.00 163.10 ? 76 ASP A C 1 ATOM 587 O O . ASP A 1 77 ? 27.118 1.051 20.226 1.00 156.09 ? 76 ASP A O 1 ATOM 588 C CB . ASP A 1 77 ? 27.884 -0.648 22.747 1.00 185.90 ? 76 ASP A CB 1 ATOM 589 C CG . ASP A 1 77 ? 29.217 -0.293 23.398 1.00 200.12 ? 76 ASP A CG 1 ATOM 590 O OD1 . ASP A 1 77 ? 29.350 0.821 23.951 1.00 210.39 ? 76 ASP A OD1 1 ATOM 591 O OD2 . ASP A 1 77 ? 30.137 -1.139 23.365 1.00 210.09 ? 76 ASP A OD2 1 ATOM 592 N N . GLY A 1 78 ? 28.012 2.553 21.651 1.00 158.69 ? 77 GLY A N 1 ATOM 593 C CA . GLY A 1 78 ? 28.485 3.469 20.611 1.00 155.65 ? 77 GLY A CA 1 ATOM 594 C C . GLY A 1 78 ? 27.419 4.321 19.936 1.00 151.60 ? 77 GLY A C 1 ATOM 595 O O . GLY A 1 78 ? 27.701 4.989 18.937 1.00 149.90 ? 77 GLY A O 1 ATOM 596 N N . VAL A 1 79 ? 26.202 4.319 20.475 1.00 148.86 ? 78 VAL A N 1 ATOM 597 C CA . VAL A 1 79 ? 25.097 5.064 19.879 1.00 146.18 ? 78 VAL A CA 1 ATOM 598 C C . VAL A 1 79 ? 24.632 6.130 20.858 1.00 144.46 ? 78 VAL A C 1 ATOM 599 O O . VAL A 1 79 ? 24.415 5.846 22.034 1.00 141.09 ? 78 VAL A O 1 ATOM 600 C CB . VAL A 1 79 ? 23.899 4.143 19.556 1.00 145.94 ? 78 VAL A CB 1 ATOM 601 C CG1 . VAL A 1 79 ? 22.756 4.941 18.935 1.00 142.95 ? 78 VAL A CG1 1 ATOM 602 C CG2 . VAL A 1 79 ? 24.329 3.003 18.638 1.00 147.50 ? 78 VAL A CG2 1 ATOM 603 N N . ASP A 1 80 ? 24.482 7.354 20.369 1.00 145.68 ? 79 ASP A N 1 ATOM 604 C CA . ASP A 1 80 ? 23.942 8.437 21.183 1.00 146.91 ? 79 ASP A CA 1 ATOM 605 C C . ASP A 1 80 ? 22.755 9.064 20.468 1.00 142.47 ? 79 ASP A C 1 ATOM 606 O O . ASP A 1 80 ? 22.752 9.181 19.245 1.00 140.69 ? 79 ASP A O 1 ATOM 607 C CB . ASP A 1 80 ? 25.019 9.487 21.455 1.00 151.91 ? 79 ASP A CB 1 ATOM 608 C CG . ASP A 1 80 ? 24.859 10.148 22.811 1.00 155.47 ? 79 ASP A CG 1 ATOM 609 O OD1 . ASP A 1 80 ? 23.710 10.419 23.223 1.00 153.38 ? 79 ASP A OD1 1 ATOM 610 O OD2 . ASP A 1 80 ? 25.890 10.390 23.469 1.00 162.60 ? 79 ASP A OD2 1 ATOM 611 N N . VAL A 1 81 ? 21.746 9.466 21.235 1.00 139.86 ? 80 VAL A N 1 ATOM 612 C CA . VAL A 1 81 ? 20.509 9.984 20.662 1.00 137.28 ? 80 VAL A CA 1 ATOM 613 C C . VAL A 1 81 ? 20.116 11.286 21.350 1.00 137.28 ? 80 VAL A C 1 ATOM 614 O O . VAL A 1 81 ? 20.187 11.394 22.577 1.00 134.98 ? 80 VAL A O 1 ATOM 615 C CB . VAL A 1 81 ? 19.360 8.963 20.807 1.00 134.77 ? 80 VAL A CB 1 ATOM 616 C CG1 . VAL A 1 81 ? 18.180 9.356 19.928 1.00 133.25 ? 80 VAL A CG1 1 ATOM 617 C CG2 . VAL A 1 81 ? 19.837 7.562 20.448 1.00 134.36 ? 80 VAL A CG2 1 ATOM 618 N N . ARG A 1 82 ? 19.703 12.273 20.558 1.00 137.07 ? 81 ARG A N 1 ATOM 619 C CA . ARG A 1 82 ? 19.201 13.531 21.108 1.00 138.51 ? 81 ARG A CA 1 ATOM 620 C C . ARG A 1 82 ? 17.889 13.948 20.448 1.00 133.19 ? 81 ARG A C 1 ATOM 621 O O . ARG A 1 82 ? 17.579 13.534 19.324 1.00 127.99 ? 81 ARG A O 1 ATOM 622 C CB . ARG A 1 82 ? 20.253 14.647 20.998 1.00 144.92 ? 81 ARG A CB 1 ATOM 623 C CG . ARG A 1 82 ? 20.471 15.206 19.597 1.00 148.93 ? 81 ARG A CG 1 ATOM 624 C CD . ARG A 1 82 ? 21.504 16.326 19.586 1.00 153.00 ? 81 ARG A CD 1 ATOM 625 N NE . ARG A 1 82 ? 21.646 16.914 18.254 1.00 158.02 ? 81 ARG A NE 1 ATOM 626 C CZ . ARG A 1 82 ? 22.574 17.804 17.905 1.00 164.56 ? 81 ARG A CZ 1 ATOM 627 N NH1 . ARG A 1 82 ? 23.472 18.237 18.787 1.00 169.15 ? 81 ARG A NH1 1 ATOM 628 N NH2 . ARG A 1 82 ? 22.607 18.267 16.658 1.00 164.93 ? 81 ARG A NH2 1 ATOM 629 N N . VAL A 1 83 ? 17.127 14.770 21.169 1.00 130.54 ? 82 VAL A N 1 ATOM 630 C CA . VAL A 1 83 ? 15.858 15.302 20.688 1.00 126.97 ? 82 VAL A CA 1 ATOM 631 C C . VAL A 1 83 ? 16.102 16.734 20.224 1.00 124.07 ? 82 VAL A C 1 ATOM 632 O O . VAL A 1 83 ? 16.328 17.626 21.047 1.00 123.10 ? 82 VAL A O 1 ATOM 633 C CB . VAL A 1 83 ? 14.784 15.311 21.798 1.00 127.92 ? 82 VAL A CB 1 ATOM 634 C CG1 . VAL A 1 83 ? 13.428 15.711 21.226 1.00 127.56 ? 82 VAL A CG1 1 ATOM 635 C CG2 . VAL A 1 83 ? 14.700 13.949 22.471 1.00 128.78 ? 82 VAL A CG2 1 ATOM 636 N N . PRO A 1 84 ? 16.069 16.961 18.904 1.00 119.01 ? 83 PRO A N 1 ATOM 637 C CA . PRO A 1 84 ? 16.295 18.297 18.397 1.00 121.65 ? 83 PRO A CA 1 ATOM 638 C C . PRO A 1 84 ? 15.018 19.125 18.446 1.00 124.45 ? 83 PRO A C 1 ATOM 639 O O . PRO A 1 84 ? 13.920 18.575 18.561 1.00 124.55 ? 83 PRO A O 1 ATOM 640 C CB . PRO A 1 84 ? 16.691 18.038 16.949 1.00 120.88 ? 83 PRO A CB 1 ATOM 641 C CG . PRO A 1 84 ? 15.870 16.853 16.571 1.00 118.00 ? 83 PRO A CG 1 ATOM 642 C CD . PRO A 1 84 ? 15.729 16.023 17.820 1.00 117.15 ? 83 PRO A CD 1 ATOM 643 N N . GLY A 1 85 ? 15.174 20.442 18.372 1.00 128.43 ? 84 GLY A N 1 ATOM 644 C CA . GLY A 1 85 ? 14.047 21.350 18.191 1.00 129.05 ? 84 GLY A CA 1 ATOM 645 C C . GLY A 1 85 ? 13.229 21.688 19.423 1.00 129.14 ? 84 GLY A C 1 ATOM 646 O O . GLY A 1 85 ? 12.097 22.153 19.293 1.00 128.12 ? 84 GLY A O 1 ATOM 647 N N . PHE A 1 86 ? 13.780 21.479 20.619 1.00 129.18 ? 85 PHE A N 1 ATOM 648 C CA . PHE A 1 86 ? 13.082 21.896 21.837 1.00 128.75 ? 85 PHE A CA 1 ATOM 649 C C . PHE A 1 86 ? 12.977 23.419 21.860 1.00 129.05 ? 85 PHE A C 1 ATOM 650 O O . PHE A 1 86 ? 13.971 24.119 21.673 1.00 129.20 ? 85 PHE A O 1 ATOM 651 C CB . PHE A 1 86 ? 13.786 21.393 23.100 1.00 129.24 ? 85 PHE A CB 1 ATOM 652 C CG . PHE A 1 86 ? 12.979 21.589 24.356 1.00 130.26 ? 85 PHE A CG 1 ATOM 653 C CD1 . PHE A 1 86 ? 13.071 22.769 25.086 1.00 131.90 ? 85 PHE A CD1 1 ATOM 654 C CD2 . PHE A 1 86 ? 12.114 20.598 24.804 1.00 131.80 ? 85 PHE A CD2 1 ATOM 655 C CE1 . PHE A 1 86 ? 12.323 22.954 26.240 1.00 133.33 ? 85 PHE A CE1 1 ATOM 656 C CE2 . PHE A 1 86 ? 11.364 20.775 25.958 1.00 133.73 ? 85 PHE A CE2 1 ATOM 657 C CZ . PHE A 1 86 ? 11.469 21.954 26.678 1.00 134.03 ? 85 PHE A CZ 1 ATOM 658 N N . GLY A 1 87 ? 11.765 23.925 22.067 1.00 128.67 ? 86 GLY A N 1 ATOM 659 C CA . GLY A 1 87 ? 11.517 25.362 22.033 1.00 131.32 ? 86 GLY A CA 1 ATOM 660 C C . GLY A 1 87 ? 11.243 25.895 20.638 1.00 134.15 ? 86 GLY A C 1 ATOM 661 O O . GLY A 1 87 ? 10.903 27.071 20.479 1.00 136.26 ? 86 GLY A O 1 ATOM 662 N N . LYS A 1 88 ? 11.400 25.037 19.631 1.00 137.15 ? 87 LYS A N 1 ATOM 663 C CA . LYS A 1 88 ? 11.067 25.364 18.247 1.00 143.94 ? 87 LYS A CA 1 ATOM 664 C C . LYS A 1 88 ? 9.925 24.442 17.828 1.00 144.01 ? 87 LYS A C 1 ATOM 665 O O . LYS A 1 88 ? 9.376 23.720 18.659 1.00 143.07 ? 87 LYS A O 1 ATOM 666 C CB . LYS A 1 88 ? 12.293 25.168 17.346 1.00 147.23 ? 87 LYS A CB 1 ATOM 667 C CG . LYS A 1 88 ? 13.463 26.081 17.679 1.00 150.70 ? 87 LYS A CG 1 ATOM 668 C CD . LYS A 1 88 ? 13.145 27.536 17.370 1.00 154.39 ? 87 LYS A CD 1 ATOM 669 C CE . LYS A 1 88 ? 14.359 28.425 17.579 1.00 160.34 ? 87 LYS A CE 1 ATOM 670 N NZ . LYS A 1 88 ? 14.069 29.846 17.240 1.00 163.03 ? 87 LYS A NZ 1 ATOM 671 N N . THR A 1 89 ? 9.543 24.479 16.559 1.00 144.20 ? 88 THR A N 1 ATOM 672 C CA . THR A 1 89 ? 8.417 23.680 16.101 1.00 141.71 ? 88 THR A CA 1 ATOM 673 C C . THR A 1 89 ? 8.710 22.792 14.898 1.00 141.29 ? 88 THR A C 1 ATOM 674 O O . THR A 1 89 ? 7.892 21.950 14.555 1.00 139.95 ? 88 THR A O 1 ATOM 675 C CB . THR A 1 89 ? 7.215 24.588 15.784 1.00 142.74 ? 88 THR A CB 1 ATOM 676 O OG1 . THR A 1 89 ? 7.604 25.587 14.833 1.00 142.75 ? 88 THR A OG1 1 ATOM 677 C CG2 . THR A 1 89 ? 6.716 25.275 17.049 1.00 142.29 ? 88 THR A CG2 1 ATOM 678 N N . PHE A 1 90 ? 9.865 22.954 14.259 1.00 141.66 ? 89 PHE A N 1 ATOM 679 C CA . PHE A 1 90 ? 10.155 22.196 13.037 1.00 141.82 ? 89 PHE A CA 1 ATOM 680 C C . PHE A 1 90 ? 10.075 20.672 13.216 1.00 137.51 ? 89 PHE A C 1 ATOM 681 O O . PHE A 1 90 ? 9.641 19.960 12.307 1.00 134.55 ? 89 PHE A O 1 ATOM 682 C CB . PHE A 1 90 ? 11.506 22.607 12.433 1.00 145.84 ? 89 PHE A CB 1 ATOM 683 C CG . PHE A 1 90 ? 12.692 22.292 13.302 1.00 148.46 ? 89 PHE A CG 1 ATOM 684 C CD1 . PHE A 1 90 ? 13.289 21.037 13.257 1.00 149.10 ? 89 PHE A CD1 1 ATOM 685 C CD2 . PHE A 1 90 ? 13.225 23.256 14.151 1.00 150.95 ? 89 PHE A CD2 1 ATOM 686 C CE1 . PHE A 1 90 ? 14.383 20.746 14.054 1.00 150.95 ? 89 PHE A CE1 1 ATOM 687 C CE2 . PHE A 1 90 ? 14.319 22.971 14.948 1.00 152.46 ? 89 PHE A CE2 1 ATOM 688 C CZ . PHE A 1 90 ? 14.900 21.714 14.899 1.00 151.99 ? 89 PHE A CZ 1 ATOM 689 N N . SER A 1 91 ? 10.480 20.183 14.386 1.00 133.11 ? 90 SER A N 1 ATOM 690 C CA . SER A 1 91 ? 10.530 18.742 14.661 1.00 128.69 ? 90 SER A CA 1 ATOM 691 C C . SER A 1 91 ? 9.147 18.115 14.867 1.00 125.70 ? 90 SER A C 1 ATOM 692 O O . SER A 1 91 ? 8.992 16.900 14.756 1.00 122.17 ? 90 SER A O 1 ATOM 693 C CB . SER A 1 91 ? 11.404 18.484 15.895 1.00 129.29 ? 90 SER A CB 1 ATOM 694 O OG . SER A 1 91 ? 11.019 19.309 16.984 1.00 131.10 ? 90 SER A OG 1 ATOM 695 N N . LEU A 1 92 ? 8.166 18.956 15.190 1.00 126.37 ? 91 LEU A N 1 ATOM 696 C CA . LEU A 1 92 ? 6.756 18.566 15.346 1.00 125.79 ? 91 LEU A CA 1 ATOM 697 C C . LEU A 1 92 ? 5.970 18.767 14.029 1.00 125.05 ? 91 LEU A C 1 ATOM 698 O O . LEU A 1 92 ? 5.023 18.033 13.744 1.00 123.40 ? 91 LEU A O 1 ATOM 699 C CB . LEU A 1 92 ? 6.098 19.443 16.443 1.00 127.72 ? 91 LEU A CB 1 ATOM 700 C CG . LEU A 1 92 ? 6.469 19.284 17.944 1.00 124.13 ? 91 LEU A CG 1 ATOM 701 C CD1 . LEU A 1 92 ? 7.880 19.798 18.208 1.00 125.84 ? 91 LEU A CD1 1 ATOM 702 C CD2 . LEU A 1 92 ? 5.505 19.956 18.923 1.00 118.82 ? 91 LEU A CD2 1 ATOM 703 N N . GLU A 1 93 ? 6.348 19.771 13.242 1.00 125.51 ? 92 GLU A N 1 ATOM 704 C CA . GLU A 1 93 ? 5.601 20.103 12.030 1.00 126.95 ? 92 GLU A CA 1 ATOM 705 C C . GLU A 1 93 ? 5.786 19.054 10.944 1.00 125.72 ? 92 GLU A C 1 ATOM 706 O O . GLU A 1 93 ? 4.826 18.696 10.272 1.00 122.06 ? 92 GLU A O 1 ATOM 707 C CB . GLU A 1 93 ? 6.002 21.480 11.493 1.00 129.94 ? 92 GLU A CB 1 ATOM 708 C CG . GLU A 1 93 ? 5.539 22.643 12.358 1.00 131.41 ? 92 GLU A CG 1 ATOM 709 C CD . GLU A 1 93 ? 5.977 23.988 11.809 1.00 133.14 ? 92 GLU A CD 1 ATOM 710 O OE1 . GLU A 1 93 ? 5.582 24.321 10.673 1.00 136.48 ? 92 GLU A OE1 1 ATOM 711 O OE2 . GLU A 1 93 ? 6.714 24.712 12.512 1.00 134.21 ? 92 GLU A OE2 1 ATOM 712 N N . PHE A 1 94 ? 7.024 18.590 10.767 1.00 129.23 ? 93 PHE A N 1 ATOM 713 C CA . PHE A 1 94 ? 7.369 17.590 9.745 1.00 131.96 ? 93 PHE A CA 1 ATOM 714 C C . PHE A 1 94 ? 8.227 16.483 10.360 1.00 137.61 ? 93 PHE A C 1 ATOM 715 O O . PHE A 1 94 ? 9.210 16.766 11.052 1.00 144.73 ? 93 PHE A O 1 ATOM 716 C CB . PHE A 1 94 ? 8.137 18.241 8.592 1.00 130.85 ? 93 PHE A CB 1 ATOM 717 C CG . PHE A 1 94 ? 7.268 18.997 7.628 1.00 131.07 ? 93 PHE A CG 1 ATOM 718 C CD1 . PHE A 1 94 ? 6.642 20.173 8.011 1.00 133.24 ? 93 PHE A CD1 1 ATOM 719 C CD2 . PHE A 1 94 ? 7.092 18.546 6.332 1.00 130.66 ? 93 PHE A CD2 1 ATOM 720 C CE1 . PHE A 1 94 ? 5.846 20.876 7.125 1.00 132.62 ? 93 PHE A CE1 1 ATOM 721 C CE2 . PHE A 1 94 ? 6.298 19.248 5.441 1.00 131.89 ? 93 PHE A CE2 1 ATOM 722 C CZ . PHE A 1 94 ? 5.674 20.412 5.838 1.00 132.37 ? 93 PHE A CZ 1 ATOM 723 N N . LEU A 1 95 ? 7.863 15.227 10.115 1.00 140.09 ? 94 LEU A N 1 ATOM 724 C CA . LEU A 1 95 ? 8.586 14.115 10.732 1.00 140.31 ? 94 LEU A CA 1 ATOM 725 C C . LEU A 1 95 ? 9.871 13.800 9.980 1.00 141.93 ? 94 LEU A C 1 ATOM 726 O O . LEU A 1 95 ? 10.884 13.439 10.590 1.00 142.59 ? 94 LEU A O 1 ATOM 727 C CB . LEU A 1 95 ? 7.720 12.853 10.837 1.00 139.74 ? 94 LEU A CB 1 ATOM 728 C CG . LEU A 1 95 ? 6.658 12.771 11.943 1.00 136.55 ? 94 LEU A CG 1 ATOM 729 C CD1 . LEU A 1 95 ? 7.157 13.313 13.275 1.00 133.63 ? 94 LEU A CD1 1 ATOM 730 C CD2 . LEU A 1 95 ? 5.384 13.482 11.530 1.00 138.18 ? 94 LEU A CD2 1 ATOM 731 N N . ASP A 1 96 ? 9.825 13.902 8.658 1.00 141.81 ? 95 ASP A N 1 ATOM 732 C CA . ASP A 1 96 ? 11.009 13.624 7.845 1.00 140.02 ? 95 ASP A CA 1 ATOM 733 C C . ASP A 1 96 ? 11.368 14.906 7.126 1.00 135.78 ? 95 ASP A C 1 ATOM 734 O O . ASP A 1 96 ? 10.734 15.244 6.136 1.00 122.27 ? 95 ASP A O 1 ATOM 735 C CB . ASP A 1 96 ? 10.744 12.484 6.851 1.00 141.60 ? 95 ASP A CB 1 ATOM 736 C CG . ASP A 1 96 ? 12.013 12.025 6.115 1.00 143.94 ? 95 ASP A CG 1 ATOM 737 O OD1 . ASP A 1 96 ? 13.012 12.780 6.077 1.00 146.47 ? 95 ASP A OD1 1 ATOM 738 O OD2 . ASP A 1 96 ? 12.011 10.895 5.578 1.00 140.16 ? 95 ASP A OD2 1 ATOM 739 N N . PRO A 1 97 ? 12.407 15.611 7.604 1.00 139.84 ? 96 PRO A N 1 ATOM 740 C CA . PRO A 1 97 ? 12.647 16.978 7.144 1.00 147.48 ? 96 PRO A CA 1 ATOM 741 C C . PRO A 1 97 ? 12.908 17.113 5.648 1.00 149.56 ? 96 PRO A C 1 ATOM 742 O O . PRO A 1 97 ? 12.510 18.109 5.034 1.00 152.19 ? 96 PRO A O 1 ATOM 743 C CB . PRO A 1 97 ? 13.876 17.408 7.952 1.00 148.62 ? 96 PRO A CB 1 ATOM 744 C CG . PRO A 1 97 ? 14.580 16.139 8.287 1.00 143.88 ? 96 PRO A CG 1 ATOM 745 C CD . PRO A 1 97 ? 13.508 15.106 8.447 1.00 140.15 ? 96 PRO A CD 1 ATOM 746 N N . SER A 1 98 ? 13.581 16.124 5.076 1.00 150.19 ? 97 SER A N 1 ATOM 747 C CA . SER A 1 98 ? 13.834 16.117 3.639 1.00 153.21 ? 97 SER A CA 1 ATOM 748 C C . SER A 1 98 ? 12.547 15.795 2.884 1.00 153.47 ? 97 SER A C 1 ATOM 749 O O . SER A 1 98 ? 12.336 16.248 1.757 1.00 153.66 ? 97 SER A O 1 ATOM 750 C CB . SER A 1 98 ? 14.921 15.090 3.297 1.00 154.73 ? 97 SER A CB 1 ATOM 751 O OG . SER A 1 98 ? 14.508 13.770 3.609 1.00 156.42 ? 97 SER A OG 1 ATOM 752 N N . LYS A 1 99 ? 11.691 15.007 3.515 1.00 159.49 ? 98 LYS A N 1 ATOM 753 C CA . LYS A 1 99 ? 10.558 14.431 2.814 1.00 168.20 ? 98 LYS A CA 1 ATOM 754 C C . LYS A 1 99 ? 9.382 15.226 3.290 1.00 171.16 ? 98 LYS A C 1 ATOM 755 O O . LYS A 1 99 ? 8.694 14.841 4.232 1.00 178.59 ? 98 LYS A O 1 ATOM 756 C CB . LYS A 1 99 ? 10.408 12.931 3.096 1.00 173.51 ? 98 LYS A CB 1 ATOM 757 C CG . LYS A 1 99 ? 11.584 12.065 2.643 1.00 173.92 ? 98 LYS A CG 1 ATOM 758 C CD . LYS A 1 99 ? 11.765 12.024 1.128 1.00 176.13 ? 98 LYS A CD 1 ATOM 759 C CE . LYS A 1 99 ? 12.816 13.012 0.636 1.00 179.46 ? 98 LYS A CE 1 ATOM 760 N NZ . LYS A 1 99 ? 13.119 12.861 -0.815 1.00 183.18 ? 98 LYS A NZ 1 ATOM 761 N N . SER A 1 100 ? 9.188 16.364 2.642 1.00 173.87 ? 99 SER A N 1 ATOM 762 C CA . SER A 1 100 ? 8.135 17.317 2.999 1.00 177.52 ? 99 SER A CA 1 ATOM 763 C C . SER A 1 100 ? 6.721 16.721 3.171 1.00 181.26 ? 99 SER A C 1 ATOM 764 O O . SER A 1 100 ? 6.363 16.354 4.288 1.00 201.57 ? 99 SER A O 1 ATOM 765 C CB . SER A 1 100 ? 8.127 18.496 2.015 1.00 177.67 ? 99 SER A CB 1 ATOM 766 O OG . SER A 1 100 ? 7.209 19.499 2.412 1.00 174.45 ? 99 SER A OG 1 ATOM 767 N N . SER A 1 101 ? 5.949 16.608 2.086 1.00 175.77 ? 100 SER A N 1 ATOM 768 C CA . SER A 1 101 ? 4.498 16.369 2.136 1.00 172.28 ? 100 SER A CA 1 ATOM 769 C C . SER A 1 101 ? 4.090 15.196 3.030 1.00 175.12 ? 100 SER A C 1 ATOM 770 O O . SER A 1 101 ? 3.197 15.292 3.900 1.00 192.40 ? 100 SER A O 1 ATOM 771 C CB . SER A 1 101 ? 3.997 16.078 0.717 1.00 168.11 ? 100 SER A CB 1 ATOM 772 O OG . SER A 1 101 ? 4.676 14.960 0.159 1.00 158.58 ? 100 SER A OG 1 ATOM 773 N N . VAL A 1 102 ? 4.778 14.089 2.804 1.00 161.99 ? 101 VAL A N 1 ATOM 774 C CA . VAL A 1 102 ? 4.398 12.827 3.424 1.00 148.84 ? 101 VAL A CA 1 ATOM 775 C C . VAL A 1 102 ? 4.500 12.867 4.951 1.00 141.04 ? 101 VAL A C 1 ATOM 776 O O . VAL A 1 102 ? 3.766 12.158 5.629 1.00 138.25 ? 101 VAL A O 1 ATOM 777 C CB . VAL A 1 102 ? 5.234 11.645 2.885 1.00 148.14 ? 101 VAL A CB 1 ATOM 778 C CG1 . VAL A 1 102 ? 4.493 10.335 3.119 1.00 147.77 ? 101 VAL A CG1 1 ATOM 779 C CG2 . VAL A 1 102 ? 5.558 11.818 1.398 1.00 150.49 ? 101 VAL A CG2 1 ATOM 780 N N . GLY A 1 103 ? 5.385 13.702 5.494 1.00 138.11 ? 102 GLY A N 1 ATOM 781 C CA . GLY A 1 103 ? 5.603 13.747 6.938 1.00 134.19 ? 102 GLY A CA 1 ATOM 782 C C . GLY A 1 103 ? 4.900 14.862 7.696 1.00 136.28 ? 102 GLY A C 1 ATOM 783 O O . GLY A 1 103 ? 5.254 15.134 8.848 1.00 130.99 ? 102 GLY A O 1 ATOM 784 N N . SER A 1 104 ? 3.908 15.509 7.079 1.00 144.95 ? 103 SER A N 1 ATOM 785 C CA . SER A 1 104 ? 3.217 16.631 7.741 1.00 145.53 ? 103 SER A CA 1 ATOM 786 C C . SER A 1 104 ? 2.404 16.186 8.970 1.00 134.82 ? 103 SER A C 1 ATOM 787 O O . SER A 1 104 ? 1.552 15.306 8.881 1.00 126.57 ? 103 SER A O 1 ATOM 788 C CB . SER A 1 104 ? 2.330 17.409 6.758 1.00 150.34 ? 103 SER A CB 1 ATOM 789 O OG . SER A 1 104 ? 1.312 16.589 6.214 1.00 159.29 ? 103 SER A OG 1 ATOM 790 N N . TYR A 1 105 ? 2.680 16.809 10.111 1.00 127.58 ? 104 TYR A N 1 ATOM 791 C CA . TYR A 1 105 ? 2.029 16.457 11.377 1.00 122.22 ? 104 TYR A CA 1 ATOM 792 C C . TYR A 1 105 ? 1.386 17.694 12.025 1.00 120.68 ? 104 TYR A C 1 ATOM 793 O O . TYR A 1 105 ? 0.191 17.921 11.849 1.00 121.88 ? 104 TYR A O 1 ATOM 794 C CB . TYR A 1 105 ? 3.053 15.780 12.293 1.00 118.78 ? 104 TYR A CB 1 ATOM 795 C CG . TYR A 1 105 ? 2.559 15.295 13.644 1.00 116.78 ? 104 TYR A CG 1 ATOM 796 C CD1 . TYR A 1 105 ? 1.496 14.402 13.746 1.00 116.23 ? 104 TYR A CD1 1 ATOM 797 C CD2 . TYR A 1 105 ? 3.201 15.676 14.819 1.00 115.93 ? 104 TYR A CD2 1 ATOM 798 C CE1 . TYR A 1 105 ? 1.062 13.937 14.981 1.00 113.57 ? 104 TYR A CE1 1 ATOM 799 C CE2 . TYR A 1 105 ? 2.777 15.217 16.056 1.00 114.73 ? 104 TYR A CE2 1 ATOM 800 C CZ . TYR A 1 105 ? 1.708 14.347 16.136 1.00 112.77 ? 104 TYR A CZ 1 ATOM 801 O OH . TYR A 1 105 ? 1.291 13.890 17.367 1.00 108.81 ? 104 TYR A OH 1 ATOM 802 N N . PHE A 1 106 ? 2.167 18.506 12.738 1.00 118.07 ? 105 PHE A N 1 ATOM 803 C CA . PHE A 1 106 ? 1.647 19.742 13.355 1.00 118.40 ? 105 PHE A CA 1 ATOM 804 C C . PHE A 1 106 ? 1.634 20.954 12.408 1.00 118.14 ? 105 PHE A C 1 ATOM 805 O O . PHE A 1 106 ? 1.135 22.027 12.778 1.00 115.01 ? 105 PHE A O 1 ATOM 806 C CB . PHE A 1 106 ? 2.472 20.117 14.599 1.00 117.09 ? 105 PHE A CB 1 ATOM 807 C CG . PHE A 1 106 ? 1.894 19.623 15.897 1.00 117.90 ? 105 PHE A CG 1 ATOM 808 C CD1 . PHE A 1 106 ? 0.813 20.272 16.480 1.00 119.29 ? 105 PHE A CD1 1 ATOM 809 C CD2 . PHE A 1 106 ? 2.452 18.535 16.556 1.00 116.16 ? 105 PHE A CD2 1 ATOM 810 C CE1 . PHE A 1 106 ? 0.288 19.834 17.685 1.00 118.54 ? 105 PHE A CE1 1 ATOM 811 C CE2 . PHE A 1 106 ? 1.932 18.092 17.760 1.00 116.78 ? 105 PHE A CE2 1 ATOM 812 C CZ . PHE A 1 106 ? 0.848 18.742 18.326 1.00 118.77 ? 105 PHE A CZ 1 ATOM 813 N N . HIS A 1 107 ? 2.187 20.795 11.205 1.00 118.88 ? 106 HIS A N 1 ATOM 814 C CA . HIS A 1 107 ? 2.352 21.919 10.275 1.00 123.00 ? 106 HIS A CA 1 ATOM 815 C C . HIS A 1 107 ? 1.107 22.781 10.072 1.00 122.60 ? 106 HIS A C 1 ATOM 816 O O . HIS A 1 107 ? 1.169 24.006 10.149 1.00 122.06 ? 106 HIS A O 1 ATOM 817 C CB . HIS A 1 107 ? 2.818 21.423 8.903 1.00 126.47 ? 106 HIS A CB 1 ATOM 818 C CG . HIS A 1 107 ? 2.783 22.479 7.839 1.00 130.20 ? 106 HIS A CG 1 ATOM 819 N ND1 . HIS A 1 107 ? 3.668 23.535 7.806 1.00 131.84 ? 106 HIS A ND1 1 ATOM 820 C CD2 . HIS A 1 107 ? 1.961 22.646 6.775 1.00 136.29 ? 106 HIS A CD2 1 ATOM 821 C CE1 . HIS A 1 107 ? 3.400 24.302 6.764 1.00 134.98 ? 106 HIS A CE1 1 ATOM 822 N NE2 . HIS A 1 107 ? 2.367 23.786 6.123 1.00 138.21 ? 106 HIS A NE2 1 ATOM 823 N N . THR A 1 108 ? -0.015 22.138 9.781 1.00 123.02 ? 107 THR A N 1 ATOM 824 C CA . THR A 1 108 ? -1.231 22.868 9.469 1.00 125.00 ? 107 THR A CA 1 ATOM 825 C C . THR A 1 108 ? -1.693 23.714 10.648 1.00 124.05 ? 107 THR A C 1 ATOM 826 O O . THR A 1 108 ? -2.087 24.864 10.466 1.00 123.21 ? 107 THR A O 1 ATOM 827 C CB . THR A 1 108 ? -2.361 21.917 9.048 1.00 127.55 ? 107 THR A CB 1 ATOM 828 O OG1 . THR A 1 108 ? -1.870 21.011 8.054 1.00 130.06 ? 107 THR A OG1 1 ATOM 829 C CG2 . THR A 1 108 ? -3.545 22.697 8.482 1.00 129.16 ? 107 THR A CG2 1 ATOM 830 N N . MET A 1 109 ? -1.641 23.149 11.852 1.00 121.89 ? 108 MET A N 1 ATOM 831 C CA . MET A 1 109 ? -2.053 23.884 13.052 1.00 121.79 ? 108 MET A CA 1 ATOM 832 C C . MET A 1 109 ? -1.155 25.094 13.277 1.00 123.07 ? 108 MET A C 1 ATOM 833 O O . MET A 1 109 ? -1.637 26.192 13.582 1.00 122.60 ? 108 MET A O 1 ATOM 834 C CB . MET A 1 109 ? -2.028 22.985 14.299 1.00 120.29 ? 108 MET A CB 1 ATOM 835 C CG . MET A 1 109 ? -2.577 23.659 15.557 1.00 118.90 ? 108 MET A CG 1 ATOM 836 S SD . MET A 1 109 ? -2.485 22.665 17.064 1.00 117.01 ? 108 MET A SD 1 ATOM 837 C CE . MET A 1 109 ? -3.583 21.311 16.648 1.00 118.70 ? 108 MET A CE 1 ATOM 838 N N . VAL A 1 110 ? 0.150 24.887 13.131 1.00 124.25 ? 109 VAL A N 1 ATOM 839 C CA . VAL A 1 110 ? 1.114 25.958 13.360 1.00 126.50 ? 109 VAL A CA 1 ATOM 840 C C . VAL A 1 110 ? 0.930 27.073 12.325 1.00 128.20 ? 109 VAL A C 1 ATOM 841 O O . VAL A 1 110 ? 0.953 28.257 12.664 1.00 128.14 ? 109 VAL A O 1 ATOM 842 C CB . VAL A 1 110 ? 2.567 25.433 13.335 1.00 126.82 ? 109 VAL A CB 1 ATOM 843 C CG1 . VAL A 1 110 ? 3.550 26.577 13.536 1.00 127.75 ? 109 VAL A CG1 1 ATOM 844 C CG2 . VAL A 1 110 ? 2.783 24.384 14.422 1.00 125.92 ? 109 VAL A CG2 1 ATOM 845 N N . GLU A 1 111 ? 0.735 26.692 11.068 1.00 131.28 ? 110 GLU A N 1 ATOM 846 C CA . GLU A 1 111 ? 0.482 27.676 10.025 1.00 138.03 ? 110 GLU A CA 1 ATOM 847 C C . GLU A 1 111 ? -0.744 28.529 10.326 1.00 141.81 ? 110 GLU A C 1 ATOM 848 O O . GLU A 1 111 ? -0.736 29.733 10.077 1.00 145.02 ? 110 GLU A O 1 ATOM 849 C CB . GLU A 1 111 ? 0.340 27.011 8.654 1.00 144.11 ? 110 GLU A CB 1 ATOM 850 C CG . GLU A 1 111 ? 1.654 26.894 7.898 1.00 147.66 ? 110 GLU A CG 1 ATOM 851 C CD . GLU A 1 111 ? 2.300 28.243 7.618 1.00 150.95 ? 110 GLU A CD 1 ATOM 852 O OE1 . GLU A 1 111 ? 1.591 29.275 7.630 1.00 148.80 ? 110 GLU A OE1 1 ATOM 853 O OE2 . GLU A 1 111 ? 3.526 28.270 7.390 1.00 155.76 ? 110 GLU A OE2 1 ATOM 854 N N . SER A 1 112 ? -1.789 27.904 10.861 1.00 143.81 ? 111 SER A N 1 ATOM 855 C CA . SER A 1 112 ? -2.993 28.633 11.257 1.00 146.81 ? 111 SER A CA 1 ATOM 856 C C . SER A 1 112 ? -2.704 29.612 12.398 1.00 144.11 ? 111 SER A C 1 ATOM 857 O O . SER A 1 112 ? -3.136 30.767 12.352 1.00 147.43 ? 111 SER A O 1 ATOM 858 C CB . SER A 1 112 ? -4.116 27.664 11.644 1.00 148.58 ? 111 SER A CB 1 ATOM 859 O OG . SER A 1 112 ? -4.576 26.940 10.512 1.00 150.79 ? 111 SER A OG 1 ATOM 860 N N . LEU A 1 113 ? -1.967 29.157 13.409 1.00 138.01 ? 112 LEU A N 1 ATOM 861 C CA . LEU A 1 113 ? -1.569 30.029 14.520 1.00 134.90 ? 112 LEU A CA 1 ATOM 862 C C . LEU A 1 113 ? -0.782 31.243 14.028 1.00 132.88 ? 112 LEU A C 1 ATOM 863 O O . LEU A 1 113 ? -1.036 32.371 14.455 1.00 132.80 ? 112 LEU A O 1 ATOM 864 C CB . LEU A 1 113 ? -0.740 29.252 15.542 1.00 134.87 ? 112 LEU A CB 1 ATOM 865 C CG . LEU A 1 113 ? -1.524 28.214 16.346 1.00 136.34 ? 112 LEU A CG 1 ATOM 866 C CD1 . LEU A 1 113 ? -0.587 27.212 17.003 1.00 135.92 ? 112 LEU A CD1 1 ATOM 867 C CD2 . LEU A 1 113 ? -2.403 28.891 17.388 1.00 137.74 ? 112 LEU A CD2 1 ATOM 868 N N . VAL A 1 114 ? 0.158 31.008 13.119 1.00 132.13 ? 113 VAL A N 1 ATOM 869 C CA . VAL A 1 114 ? 0.935 32.087 12.506 1.00 134.41 ? 113 VAL A CA 1 ATOM 870 C C . VAL A 1 114 ? 0.022 33.057 11.760 1.00 138.17 ? 113 VAL A C 1 ATOM 871 O O . VAL A 1 114 ? 0.194 34.275 11.855 1.00 137.94 ? 113 VAL A O 1 ATOM 872 C CB . VAL A 1 114 ? 2.003 31.534 11.537 1.00 135.57 ? 113 VAL A CB 1 ATOM 873 C CG1 . VAL A 1 114 ? 2.593 32.641 10.669 1.00 137.43 ? 113 VAL A CG1 1 ATOM 874 C CG2 . VAL A 1 114 ? 3.106 30.832 12.315 1.00 135.43 ? 113 VAL A CG2 1 ATOM 875 N N . GLY A 1 115 ? -0.944 32.518 11.020 1.00 141.08 ? 114 GLY A N 1 ATOM 876 C CA . GLY A 1 115 ? -1.953 33.341 10.355 1.00 146.98 ? 114 GLY A CA 1 ATOM 877 C C . GLY A 1 115 ? -2.732 34.238 11.308 1.00 149.54 ? 114 GLY A C 1 ATOM 878 O O . GLY A 1 115 ? -3.169 35.326 10.922 1.00 149.28 ? 114 GLY A O 1 ATOM 879 N N . TRP A 1 116 ? -2.907 33.782 12.550 1.00 151.03 ? 115 TRP A N 1 ATOM 880 C CA . TRP A 1 116 ? -3.590 34.570 13.582 1.00 153.09 ? 115 TRP A CA 1 ATOM 881 C C . TRP A 1 116 ? -2.650 35.492 14.367 1.00 150.20 ? 115 TRP A C 1 ATOM 882 O O . TRP A 1 116 ? -3.085 36.155 15.309 1.00 152.72 ? 115 TRP A O 1 ATOM 883 C CB . TRP A 1 116 ? -4.353 33.665 14.558 1.00 155.04 ? 115 TRP A CB 1 ATOM 884 C CG . TRP A 1 116 ? -5.233 32.636 13.898 1.00 159.41 ? 115 TRP A CG 1 ATOM 885 C CD1 . TRP A 1 116 ? -5.882 32.750 12.698 1.00 162.81 ? 115 TRP A CD1 1 ATOM 886 C CD2 . TRP A 1 116 ? -5.574 31.346 14.417 1.00 159.74 ? 115 TRP A CD2 1 ATOM 887 N NE1 . TRP A 1 116 ? -6.595 31.603 12.435 1.00 162.75 ? 115 TRP A NE1 1 ATOM 888 C CE2 . TRP A 1 116 ? -6.425 30.726 13.475 1.00 161.94 ? 115 TRP A CE2 1 ATOM 889 C CE3 . TRP A 1 116 ? -5.239 30.650 15.585 1.00 157.87 ? 115 TRP A CE3 1 ATOM 890 C CZ2 . TRP A 1 116 ? -6.945 29.441 13.667 1.00 161.50 ? 115 TRP A CZ2 1 ATOM 891 C CZ3 . TRP A 1 116 ? -5.756 29.375 15.776 1.00 157.53 ? 115 TRP A CZ3 1 ATOM 892 C CH2 . TRP A 1 116 ? -6.599 28.784 14.821 1.00 159.10 ? 115 TRP A CH2 1 ATOM 893 N N . GLY A 1 117 ? -1.371 35.530 13.992 1.00 146.54 ? 116 GLY A N 1 ATOM 894 C CA . GLY A 1 117 ? -0.427 36.499 14.554 1.00 146.40 ? 116 GLY A CA 1 ATOM 895 C C . GLY A 1 117 ? 0.685 35.945 15.428 1.00 143.61 ? 116 GLY A C 1 ATOM 896 O O . GLY A 1 117 ? 1.448 36.716 16.012 1.00 142.48 ? 116 GLY A O 1 ATOM 897 N N . TYR A 1 118 ? 0.785 34.620 15.527 1.00 143.68 ? 117 TYR A N 1 ATOM 898 C CA . TYR A 1 118 ? 1.852 33.986 16.306 1.00 143.41 ? 117 TYR A CA 1 ATOM 899 C C . TYR A 1 118 ? 3.154 33.951 15.513 1.00 142.74 ? 117 TYR A C 1 ATOM 900 O O . TYR A 1 118 ? 3.154 34.169 14.297 1.00 142.81 ? 117 TYR A O 1 ATOM 901 C CB . TYR A 1 118 ? 1.452 32.572 16.738 1.00 142.20 ? 117 TYR A CB 1 ATOM 902 C CG . TYR A 1 118 ? 0.498 32.550 17.909 1.00 142.07 ? 117 TYR A CG 1 ATOM 903 C CD1 . TYR A 1 118 ? -0.815 32.988 17.773 1.00 145.29 ? 117 TYR A CD1 1 ATOM 904 C CD2 . TYR A 1 118 ? 0.909 32.094 19.155 1.00 141.49 ? 117 TYR A CD2 1 ATOM 905 C CE1 . TYR A 1 118 ? -1.691 32.972 18.845 1.00 146.35 ? 117 TYR A CE1 1 ATOM 906 C CE2 . TYR A 1 118 ? 0.043 32.075 20.233 1.00 142.40 ? 117 TYR A CE2 1 ATOM 907 C CZ . TYR A 1 118 ? -1.257 32.512 20.073 1.00 143.73 ? 117 TYR A CZ 1 ATOM 908 O OH . TYR A 1 118 ? -2.123 32.492 21.141 1.00 141.69 ? 117 TYR A OH 1 ATOM 909 N N . THR A 1 119 ? 4.250 33.667 16.215 1.00 140.02 ? 118 THR A N 1 ATOM 910 C CA . THR A 1 119 ? 5.589 33.637 15.626 1.00 141.28 ? 118 THR A CA 1 ATOM 911 C C . THR A 1 119 ? 6.361 32.400 16.083 1.00 140.62 ? 118 THR A C 1 ATOM 912 O O . THR A 1 119 ? 6.431 32.108 17.277 1.00 139.43 ? 118 THR A O 1 ATOM 913 C CB . THR A 1 119 ? 6.380 34.895 16.019 1.00 144.11 ? 118 THR A CB 1 ATOM 914 O OG1 . THR A 1 119 ? 5.630 36.063 15.659 1.00 147.20 ? 118 THR A OG1 1 ATOM 915 C CG2 . THR A 1 119 ? 7.738 34.924 15.325 1.00 146.43 ? 118 THR A CG2 1 ATOM 916 N N . ARG A 1 120 ? 6.940 31.677 15.127 1.00 143.35 ? 119 ARG A N 1 ATOM 917 C CA . ARG A 1 120 ? 7.650 30.427 15.424 1.00 146.88 ? 119 ARG A CA 1 ATOM 918 C C . ARG A 1 120 ? 8.802 30.649 16.396 1.00 146.55 ? 119 ARG A C 1 ATOM 919 O O . ARG A 1 120 ? 9.616 31.555 16.203 1.00 142.98 ? 119 ARG A O 1 ATOM 920 C CB . ARG A 1 120 ? 8.203 29.800 14.142 1.00 152.81 ? 119 ARG A CB 1 ATOM 921 C CG . ARG A 1 120 ? 7.141 29.230 13.219 1.00 155.14 ? 119 ARG A CG 1 ATOM 922 C CD . ARG A 1 120 ? 7.762 28.520 12.028 1.00 156.45 ? 119 ARG A CD 1 ATOM 923 N NE . ARG A 1 120 ? 6.789 27.678 11.327 1.00 156.43 ? 119 ARG A NE 1 ATOM 924 C CZ . ARG A 1 120 ? 5.881 28.119 10.455 1.00 160.67 ? 119 ARG A CZ 1 ATOM 925 N NH1 . ARG A 1 120 ? 5.803 29.409 10.146 1.00 164.80 ? 119 ARG A NH1 1 ATOM 926 N NH2 . ARG A 1 120 ? 5.040 27.263 9.883 1.00 157.31 ? 119 ARG A NH2 1 ATOM 927 N N . GLY A 1 121 ? 8.854 29.827 17.444 1.00 145.91 ? 120 GLY A N 1 ATOM 928 C CA . GLY A 1 121 ? 9.927 29.898 18.433 1.00 145.61 ? 120 GLY A CA 1 ATOM 929 C C . GLY A 1 121 ? 9.755 31.012 19.451 1.00 144.76 ? 120 GLY A C 1 ATOM 930 O O . GLY A 1 121 ? 10.581 31.159 20.353 1.00 148.23 ? 120 GLY A O 1 ATOM 931 N N . GLU A 1 122 ? 8.684 31.790 19.313 1.00 142.78 ? 121 GLU A N 1 ATOM 932 C CA . GLU A 1 122 ? 8.434 32.930 20.177 1.00 145.46 ? 121 GLU A CA 1 ATOM 933 C C . GLU A 1 122 ? 7.125 32.718 20.928 1.00 144.41 ? 121 GLU A C 1 ATOM 934 O O . GLU A 1 122 ? 7.147 32.204 22.041 1.00 145.06 ? 121 GLU A O 1 ATOM 935 C CB . GLU A 1 122 ? 8.417 34.225 19.366 1.00 151.15 ? 121 GLU A CB 1 ATOM 936 C CG . GLU A 1 122 ? 9.784 34.631 18.838 1.00 153.61 ? 121 GLU A CG 1 ATOM 937 C CD . GLU A 1 122 ? 9.791 36.015 18.216 1.00 155.44 ? 121 GLU A CD 1 ATOM 938 O OE1 . GLU A 1 122 ? 9.067 36.905 18.712 1.00 153.54 ? 121 GLU A OE1 1 ATOM 939 O OE2 . GLU A 1 122 ? 10.532 36.215 17.230 1.00 160.24 ? 121 GLU A OE2 1 ATOM 940 N N . ASP A 1 123 ? 5.995 33.081 20.317 1.00 145.24 ? 122 ASP A N 1 ATOM 941 C CA . ASP A 1 123 ? 4.671 32.919 20.938 1.00 146.66 ? 122 ASP A CA 1 ATOM 942 C C . ASP A 1 123 ? 4.259 31.451 21.002 1.00 145.33 ? 122 ASP A C 1 ATOM 943 O O . ASP A 1 123 ? 3.567 31.034 21.936 1.00 141.73 ? 122 ASP A O 1 ATOM 944 C CB . ASP A 1 123 ? 3.591 33.649 20.128 1.00 149.05 ? 122 ASP A CB 1 ATOM 945 C CG . ASP A 1 123 ? 3.888 35.116 19.925 1.00 155.28 ? 122 ASP A CG 1 ATOM 946 O OD1 . ASP A 1 123 ? 4.304 35.783 20.895 1.00 162.01 ? 122 ASP A OD1 1 ATOM 947 O OD2 . ASP A 1 123 ? 3.686 35.601 18.790 1.00 157.95 ? 122 ASP A OD2 1 ATOM 948 N N . VAL A 1 124 ? 4.685 30.695 19.990 1.00 143.86 ? 123 VAL A N 1 ATOM 949 C CA . VAL A 1 124 ? 4.422 29.267 19.907 1.00 142.86 ? 123 VAL A CA 1 ATOM 950 C C . VAL A 1 124 ? 5.743 28.501 19.888 1.00 141.78 ? 123 VAL A C 1 ATOM 951 O O . VAL A 1 124 ? 6.646 28.806 19.092 1.00 140.59 ? 123 VAL A O 1 ATOM 952 C CB . VAL A 1 124 ? 3.552 28.905 18.677 1.00 142.71 ? 123 VAL A CB 1 ATOM 953 C CG1 . VAL A 1 124 ? 4.296 29.130 17.363 1.00 141.73 ? 123 VAL A CG1 1 ATOM 954 C CG2 . VAL A 1 124 ? 3.056 27.469 18.778 1.00 143.20 ? 123 VAL A CG2 1 ATOM 955 N N . ARG A 1 125 ? 5.847 27.524 20.788 1.00 138.66 ? 124 ARG A N 1 ATOM 956 C CA . ARG A 1 125 ? 7.034 26.680 20.898 1.00 137.36 ? 124 ARG A CA 1 ATOM 957 C C . ARG A 1 125 ? 6.646 25.225 21.111 1.00 135.69 ? 124 ARG A C 1 ATOM 958 O O . ARG A 1 125 ? 5.631 24.929 21.741 1.00 134.43 ? 124 ARG A O 1 ATOM 959 C CB . ARG A 1 125 ? 7.901 27.136 22.067 1.00 138.37 ? 124 ARG A CB 1 ATOM 960 C CG . ARG A 1 125 ? 8.332 28.588 21.991 1.00 141.48 ? 124 ARG A CG 1 ATOM 961 C CD . ARG A 1 125 ? 9.333 28.906 23.085 1.00 144.34 ? 124 ARG A CD 1 ATOM 962 N NE . ARG A 1 125 ? 9.483 30.343 23.296 1.00 149.00 ? 124 ARG A NE 1 ATOM 963 C CZ . ARG A 1 125 ? 10.311 30.893 24.182 1.00 154.42 ? 124 ARG A CZ 1 ATOM 964 N NH1 . ARG A 1 125 ? 11.082 30.130 24.953 1.00 157.06 ? 124 ARG A NH1 1 ATOM 965 N NH2 . ARG A 1 125 ? 10.372 32.216 24.297 1.00 156.66 ? 124 ARG A NH2 1 ATOM 966 N N . GLY A 1 126 ? 7.465 24.321 20.585 1.00 134.48 ? 125 GLY A N 1 ATOM 967 C CA . GLY A 1 126 ? 7.246 22.889 20.759 1.00 131.72 ? 125 GLY A CA 1 ATOM 968 C C . GLY A 1 126 ? 7.987 22.321 21.955 1.00 128.70 ? 125 GLY A C 1 ATOM 969 O O . GLY A 1 126 ? 9.035 22.837 22.366 1.00 130.35 ? 125 GLY A O 1 ATOM 970 N N . ALA A 1 127 ? 7.439 21.240 22.503 1.00 124.88 ? 126 ALA A N 1 ATOM 971 C CA . ALA A 1 127 ? 8.065 20.505 23.596 1.00 123.04 ? 126 ALA A CA 1 ATOM 972 C C . ALA A 1 127 ? 8.238 19.032 23.202 1.00 123.61 ? 126 ALA A C 1 ATOM 973 O O . ALA A 1 127 ? 7.596 18.151 23.777 1.00 122.38 ? 126 ALA A O 1 ATOM 974 C CB . ALA A 1 127 ? 7.227 20.632 24.860 1.00 120.78 ? 126 ALA A CB 1 ATOM 975 N N . PRO A 1 128 ? 9.112 18.758 22.213 1.00 123.14 ? 127 PRO A N 1 ATOM 976 C CA . PRO A 1 128 ? 9.402 17.371 21.844 1.00 121.91 ? 127 PRO A CA 1 ATOM 977 C C . PRO A 1 128 ? 10.219 16.638 22.913 1.00 121.00 ? 127 PRO A C 1 ATOM 978 O O . PRO A 1 128 ? 10.900 17.267 23.729 1.00 119.87 ? 127 PRO A O 1 ATOM 979 C CB . PRO A 1 128 ? 10.211 17.517 20.552 1.00 123.76 ? 127 PRO A CB 1 ATOM 980 C CG . PRO A 1 128 ? 10.900 18.826 20.700 1.00 124.98 ? 127 PRO A CG 1 ATOM 981 C CD . PRO A 1 128 ? 9.939 19.709 21.449 1.00 124.23 ? 127 PRO A CD 1 ATOM 982 N N . TYR A 1 129 ? 10.143 15.312 22.899 1.00 118.84 ? 128 TYR A N 1 ATOM 983 C CA . TYR A 1 129 ? 10.827 14.478 23.883 1.00 118.77 ? 128 TYR A CA 1 ATOM 984 C C . TYR A 1 129 ? 11.175 13.118 23.283 1.00 117.34 ? 128 TYR A C 1 ATOM 985 O O . TYR A 1 129 ? 10.762 12.797 22.168 1.00 109.71 ? 128 TYR A O 1 ATOM 986 C CB . TYR A 1 129 ? 9.931 14.284 25.110 1.00 118.42 ? 128 TYR A CB 1 ATOM 987 C CG . TYR A 1 129 ? 8.543 13.770 24.781 1.00 118.07 ? 128 TYR A CG 1 ATOM 988 C CD1 . TYR A 1 129 ? 7.553 14.632 24.313 1.00 116.96 ? 128 TYR A CD1 1 ATOM 989 C CD2 . TYR A 1 129 ? 8.218 12.425 24.940 1.00 117.76 ? 128 TYR A CD2 1 ATOM 990 C CE1 . TYR A 1 129 ? 6.283 14.171 24.011 1.00 114.68 ? 128 TYR A CE1 1 ATOM 991 C CE2 . TYR A 1 129 ? 6.950 11.953 24.641 1.00 115.63 ? 128 TYR A CE2 1 ATOM 992 C CZ . TYR A 1 129 ? 5.986 12.831 24.178 1.00 114.76 ? 128 TYR A CZ 1 ATOM 993 O OH . TYR A 1 129 ? 4.724 12.374 23.882 1.00 113.05 ? 128 TYR A OH 1 ATOM 994 N N . ASP A 1 130 ? 11.943 12.328 24.031 1.00 119.62 ? 129 ASP A N 1 ATOM 995 C CA . ASP A 1 130 ? 12.258 10.959 23.626 1.00 119.18 ? 129 ASP A CA 1 ATOM 996 C C . ASP A 1 130 ? 11.043 10.083 23.926 1.00 117.01 ? 129 ASP A C 1 ATOM 997 O O . ASP A 1 130 ? 10.909 9.517 25.016 1.00 115.01 ? 129 ASP A O 1 ATOM 998 C CB . ASP A 1 130 ? 13.510 10.441 24.351 1.00 120.98 ? 129 ASP A CB 1 ATOM 999 C CG . ASP A 1 130 ? 14.109 9.204 23.688 1.00 120.42 ? 129 ASP A CG 1 ATOM 1000 O OD1 . ASP A 1 130 ? 13.402 8.523 22.913 1.00 116.13 ? 129 ASP A OD1 1 ATOM 1001 O OD2 . ASP A 1 130 ? 15.297 8.913 23.948 1.00 122.41 ? 129 ASP A OD2 1 ATOM 1002 N N . TRP A 1 131 ? 10.162 9.986 22.937 1.00 115.82 ? 130 TRP A N 1 ATOM 1003 C CA . TRP A 1 131 ? 8.898 9.258 23.069 1.00 115.57 ? 130 TRP A CA 1 ATOM 1004 C C . TRP A 1 131 ? 9.051 7.738 23.143 1.00 116.32 ? 130 TRP A C 1 ATOM 1005 O O . TRP A 1 131 ? 8.065 7.031 23.346 1.00 115.88 ? 130 TRP A O 1 ATOM 1006 C CB . TRP A 1 131 ? 7.937 9.626 21.931 1.00 115.54 ? 130 TRP A CB 1 ATOM 1007 C CG . TRP A 1 131 ? 8.583 9.706 20.586 1.00 115.60 ? 130 TRP A CG 1 ATOM 1008 C CD1 . TRP A 1 131 ? 8.872 10.837 19.894 1.00 115.53 ? 130 TRP A CD1 1 ATOM 1009 C CD2 . TRP A 1 131 ? 9.036 8.614 19.777 1.00 120.50 ? 130 TRP A CD2 1 ATOM 1010 N NE1 . TRP A 1 131 ? 9.469 10.528 18.698 1.00 119.42 ? 130 TRP A NE1 1 ATOM 1011 C CE2 . TRP A 1 131 ? 9.578 9.167 18.599 1.00 121.13 ? 130 TRP A CE2 1 ATOM 1012 C CE3 . TRP A 1 131 ? 9.024 7.221 19.924 1.00 124.45 ? 130 TRP A CE3 1 ATOM 1013 C CZ2 . TRP A 1 131 ? 10.108 8.378 17.574 1.00 122.25 ? 130 TRP A CZ2 1 ATOM 1014 C CZ3 . TRP A 1 131 ? 9.551 6.438 18.905 1.00 123.99 ? 130 TRP A CZ3 1 ATOM 1015 C CH2 . TRP A 1 131 ? 10.086 7.020 17.745 1.00 122.08 ? 130 TRP A CH2 1 ATOM 1016 N N . ARG A 1 132 ? 10.273 7.235 22.967 1.00 117.11 ? 131 ARG A N 1 ATOM 1017 C CA . ARG A 1 132 ? 10.560 5.813 23.159 1.00 119.42 ? 131 ARG A CA 1 ATOM 1018 C C . ARG A 1 132 ? 10.461 5.427 24.636 1.00 121.16 ? 131 ARG A C 1 ATOM 1019 O O . ARG A 1 132 ? 10.192 4.266 24.965 1.00 124.76 ? 131 ARG A O 1 ATOM 1020 C CB . ARG A 1 132 ? 11.970 5.478 22.667 1.00 120.79 ? 131 ARG A CB 1 ATOM 1021 C CG . ARG A 1 132 ? 12.218 5.729 21.189 1.00 121.40 ? 131 ARG A CG 1 ATOM 1022 C CD . ARG A 1 132 ? 13.623 5.292 20.796 1.00 124.74 ? 131 ARG A CD 1 ATOM 1023 N NE . ARG A 1 132 ? 14.658 6.084 21.464 1.00 126.47 ? 131 ARG A NE 1 ATOM 1024 C CZ . ARG A 1 132 ? 15.964 5.811 21.442 1.00 128.71 ? 131 ARG A CZ 1 ATOM 1025 N NH1 . ARG A 1 132 ? 16.437 4.752 20.785 1.00 126.58 ? 131 ARG A NH1 1 ATOM 1026 N NH2 . ARG A 1 132 ? 16.810 6.607 22.088 1.00 129.53 ? 131 ARG A NH2 1 ATOM 1027 N N . ARG A 1 133 ? 10.695 6.403 25.510 1.00 122.69 ? 132 ARG A N 1 ATOM 1028 C CA . ARG A 1 133 ? 10.723 6.182 26.948 1.00 127.85 ? 132 ARG A CA 1 ATOM 1029 C C . ARG A 1 133 ? 9.475 6.710 27.637 1.00 126.85 ? 132 ARG A C 1 ATOM 1030 O O . ARG A 1 133 ? 8.655 7.404 27.033 1.00 122.53 ? 132 ARG A O 1 ATOM 1031 C CB . ARG A 1 133 ? 11.962 6.850 27.546 1.00 132.35 ? 132 ARG A CB 1 ATOM 1032 C CG . ARG A 1 133 ? 13.261 6.214 27.091 1.00 135.80 ? 132 ARG A CG 1 ATOM 1033 C CD . ARG A 1 133 ? 14.470 6.945 27.642 1.00 138.78 ? 132 ARG A CD 1 ATOM 1034 N NE . ARG A 1 133 ? 15.650 6.083 27.661 1.00 143.53 ? 132 ARG A NE 1 ATOM 1035 C CZ . ARG A 1 133 ? 16.858 6.461 28.070 1.00 149.31 ? 132 ARG A CZ 1 ATOM 1036 N NH1 . ARG A 1 133 ? 17.072 7.703 28.497 1.00 150.61 ? 132 ARG A NH1 1 ATOM 1037 N NH2 . ARG A 1 133 ? 17.864 5.591 28.047 1.00 153.66 ? 132 ARG A NH2 1 ATOM 1038 N N . ALA A 1 134 ? 9.352 6.368 28.916 1.00 128.79 ? 133 ALA A N 1 ATOM 1039 C CA . ALA A 1 134 ? 8.267 6.849 29.766 1.00 129.42 ? 133 ALA A CA 1 ATOM 1040 C C . ALA A 1 134 ? 8.742 8.104 30.495 1.00 130.86 ? 133 ALA A C 1 ATOM 1041 O O . ALA A 1 134 ? 9.930 8.410 30.486 1.00 133.11 ? 133 ALA A O 1 ATOM 1042 C CB . ALA A 1 134 ? 7.871 5.771 30.767 1.00 130.43 ? 133 ALA A CB 1 ATOM 1043 N N . PRO A 1 135 ? 7.816 8.839 31.131 1.00 130.43 ? 134 PRO A N 1 ATOM 1044 C CA . PRO A 1 135 ? 8.191 10.057 31.851 1.00 132.55 ? 134 PRO A CA 1 ATOM 1045 C C . PRO A 1 135 ? 9.293 9.906 32.902 1.00 133.94 ? 134 PRO A C 1 ATOM 1046 O O . PRO A 1 135 ? 10.033 10.859 33.158 1.00 136.63 ? 134 PRO A O 1 ATOM 1047 C CB . PRO A 1 135 ? 6.884 10.468 32.525 1.00 133.34 ? 134 PRO A CB 1 ATOM 1048 C CG . PRO A 1 135 ? 5.826 9.968 31.609 1.00 132.16 ? 134 PRO A CG 1 ATOM 1049 C CD . PRO A 1 135 ? 6.352 8.682 31.046 1.00 130.14 ? 134 PRO A CD 1 ATOM 1050 N N . ASN A 1 136 ? 9.391 8.724 33.505 1.00 133.57 ? 135 ASN A N 1 ATOM 1051 C CA . ASN A 1 136 ? 10.424 8.433 34.502 1.00 136.57 ? 135 ASN A CA 1 ATOM 1052 C C . ASN A 1 136 ? 11.854 8.659 34.002 1.00 136.72 ? 135 ASN A C 1 ATOM 1053 O O . ASN A 1 136 ? 12.747 8.964 34.792 1.00 141.91 ? 135 ASN A O 1 ATOM 1054 C CB . ASN A 1 136 ? 10.284 6.990 35.001 1.00 136.19 ? 135 ASN A CB 1 ATOM 1055 C CG . ASN A 1 136 ? 10.445 5.964 33.889 1.00 134.75 ? 135 ASN A CG 1 ATOM 1056 O OD1 . ASN A 1 136 ? 10.366 6.295 32.703 1.00 131.15 ? 135 ASN A OD1 1 ATOM 1057 N ND2 . ASN A 1 136 ? 10.657 4.709 34.269 1.00 134.80 ? 135 ASN A ND2 1 ATOM 1058 N N . GLU A 1 137 ? 12.064 8.499 32.697 1.00 133.01 ? 136 GLU A N 1 ATOM 1059 C CA . GLU A 1 137 ? 13.386 8.670 32.097 1.00 133.67 ? 136 GLU A CA 1 ATOM 1060 C C . GLU A 1 137 ? 13.476 9.905 31.196 1.00 131.27 ? 136 GLU A C 1 ATOM 1061 O O . GLU A 1 137 ? 14.325 9.969 30.307 1.00 134.15 ? 136 GLU A O 1 ATOM 1062 C CB . GLU A 1 137 ? 13.753 7.421 31.298 1.00 136.50 ? 136 GLU A CB 1 ATOM 1063 C CG . GLU A 1 137 ? 13.919 6.169 32.141 1.00 140.02 ? 136 GLU A CG 1 ATOM 1064 C CD . GLU A 1 137 ? 14.141 4.932 31.294 1.00 144.58 ? 136 GLU A CD 1 ATOM 1065 O OE1 . GLU A 1 137 ? 15.140 4.219 31.530 1.00 149.07 ? 136 GLU A OE1 1 ATOM 1066 O OE2 . GLU A 1 137 ? 13.319 4.681 30.383 1.00 144.26 ? 136 GLU A OE2 1 ATOM 1067 N N . ASN A 1 138 ? 12.601 10.880 31.419 1.00 127.85 ? 137 ASN A N 1 ATOM 1068 C CA . ASN A 1 138 ? 12.677 12.159 30.718 1.00 126.13 ? 137 ASN A CA 1 ATOM 1069 C C . ASN A 1 138 ? 12.575 13.311 31.713 1.00 126.11 ? 137 ASN A C 1 ATOM 1070 O O . ASN A 1 138 ? 11.945 14.336 31.446 1.00 124.76 ? 137 ASN A O 1 ATOM 1071 C CB . ASN A 1 138 ? 11.597 12.245 29.632 1.00 125.16 ? 137 ASN A CB 1 ATOM 1072 C CG . ASN A 1 138 ? 12.035 11.608 28.323 1.00 125.08 ? 137 ASN A CG 1 ATOM 1073 O OD1 . ASN A 1 138 ? 12.947 12.101 27.656 1.00 126.05 ? 137 ASN A OD1 1 ATOM 1074 N ND2 . ASN A 1 138 ? 11.383 10.513 27.945 1.00 122.68 ? 137 ASN A ND2 1 ATOM 1075 N N . GLY A 1 139 ? 13.223 13.135 32.863 1.00 126.56 ? 138 GLY A N 1 ATOM 1076 C CA . GLY A 1 139 ? 13.294 14.172 33.889 1.00 128.30 ? 138 GLY A CA 1 ATOM 1077 C C . GLY A 1 139 ? 13.767 15.513 33.357 1.00 127.74 ? 138 GLY A C 1 ATOM 1078 O O . GLY A 1 139 ? 13.136 16.536 33.620 1.00 126.89 ? 138 GLY A O 1 ATOM 1079 N N . PRO A 1 140 ? 14.876 15.520 32.595 1.00 126.90 ? 139 PRO A N 1 ATOM 1080 C CA . PRO A 1 140 ? 15.393 16.767 32.029 1.00 127.36 ? 139 PRO A CA 1 ATOM 1081 C C . PRO A 1 140 ? 14.382 17.508 31.161 1.00 125.71 ? 139 PRO A C 1 ATOM 1082 O O . PRO A 1 140 ? 14.310 18.736 31.211 1.00 124.03 ? 139 PRO A O 1 ATOM 1083 C CB . PRO A 1 140 ? 16.576 16.303 31.176 1.00 127.61 ? 139 PRO A CB 1 ATOM 1084 C CG . PRO A 1 140 ? 16.995 15.010 31.779 1.00 128.78 ? 139 PRO A CG 1 ATOM 1085 C CD . PRO A 1 140 ? 15.728 14.368 32.246 1.00 127.17 ? 139 PRO A CD 1 ATOM 1086 N N . TYR A 1 141 ? 13.618 16.760 30.372 1.00 124.73 ? 140 TYR A N 1 ATOM 1087 C CA . TYR A 1 141 ? 12.555 17.334 29.550 1.00 125.12 ? 140 TYR A CA 1 ATOM 1088 C C . TYR A 1 141 ? 11.582 18.162 30.391 1.00 123.75 ? 140 TYR A C 1 ATOM 1089 O O . TYR A 1 141 ? 11.254 19.295 30.035 1.00 121.80 ? 140 TYR A O 1 ATOM 1090 C CB . TYR A 1 141 ? 11.808 16.218 28.805 1.00 125.35 ? 140 TYR A CB 1 ATOM 1091 C CG . TYR A 1 141 ? 10.479 16.626 28.208 1.00 124.71 ? 140 TYR A CG 1 ATOM 1092 C CD1 . TYR A 1 141 ? 10.421 17.343 27.018 1.00 122.98 ? 140 TYR A CD1 1 ATOM 1093 C CD2 . TYR A 1 141 ? 9.277 16.281 28.828 1.00 124.26 ? 140 TYR A CD2 1 ATOM 1094 C CE1 . TYR A 1 141 ? 9.207 17.713 26.465 1.00 121.19 ? 140 TYR A CE1 1 ATOM 1095 C CE2 . TYR A 1 141 ? 8.056 16.648 28.283 1.00 123.25 ? 140 TYR A CE2 1 ATOM 1096 C CZ . TYR A 1 141 ? 8.025 17.365 27.100 1.00 121.66 ? 140 TYR A CZ 1 ATOM 1097 O OH . TYR A 1 141 ? 6.815 17.732 26.554 1.00 117.69 ? 140 TYR A OH 1 ATOM 1098 N N . PHE A 1 142 ? 11.141 17.599 31.513 1.00 122.72 ? 141 PHE A N 1 ATOM 1099 C CA . PHE A 1 142 ? 10.174 18.276 32.375 1.00 124.59 ? 141 PHE A CA 1 ATOM 1100 C C . PHE A 1 142 ? 10.746 19.520 33.045 1.00 128.33 ? 141 PHE A C 1 ATOM 1101 O O . PHE A 1 142 ? 10.028 20.498 33.251 1.00 128.87 ? 141 PHE A O 1 ATOM 1102 C CB . PHE A 1 142 ? 9.612 17.316 33.425 1.00 124.62 ? 141 PHE A CB 1 ATOM 1103 C CG . PHE A 1 142 ? 8.803 16.192 32.840 1.00 124.07 ? 141 PHE A CG 1 ATOM 1104 C CD1 . PHE A 1 142 ? 7.689 16.459 32.053 1.00 123.93 ? 141 PHE A CD1 1 ATOM 1105 C CD2 . PHE A 1 142 ? 9.149 14.869 33.077 1.00 124.32 ? 141 PHE A CD2 1 ATOM 1106 C CE1 . PHE A 1 142 ? 6.941 15.430 31.510 1.00 124.40 ? 141 PHE A CE1 1 ATOM 1107 C CE2 . PHE A 1 142 ? 8.403 13.837 32.536 1.00 123.70 ? 141 PHE A CE2 1 ATOM 1108 C CZ . PHE A 1 142 ? 7.298 14.117 31.753 1.00 123.68 ? 141 PHE A CZ 1 ATOM 1109 N N . LEU A 1 143 ? 12.031 19.486 33.387 1.00 133.53 ? 142 LEU A N 1 ATOM 1110 C CA . LEU A 1 143 ? 12.705 20.666 33.928 1.00 139.63 ? 142 LEU A CA 1 ATOM 1111 C C . LEU A 1 143 ? 12.724 21.773 32.883 1.00 137.53 ? 142 LEU A C 1 ATOM 1112 O O . LEU A 1 143 ? 12.402 22.925 33.177 1.00 135.13 ? 142 LEU A O 1 ATOM 1113 C CB . LEU A 1 143 ? 14.140 20.334 34.345 1.00 146.08 ? 142 LEU A CB 1 ATOM 1114 C CG . LEU A 1 143 ? 14.294 19.358 35.515 1.00 152.86 ? 142 LEU A CG 1 ATOM 1115 C CD1 . LEU A 1 143 ? 15.739 18.891 35.637 1.00 157.60 ? 142 LEU A CD1 1 ATOM 1116 C CD2 . LEU A 1 143 ? 13.812 19.978 36.820 1.00 153.26 ? 142 LEU A CD2 1 ATOM 1117 N N . ALA A 1 144 ? 13.104 21.409 31.661 1.00 135.44 ? 143 ALA A N 1 ATOM 1118 C CA . ALA A 1 144 ? 13.148 22.349 30.546 1.00 135.93 ? 143 ALA A CA 1 ATOM 1119 C C . ALA A 1 144 ? 11.763 22.900 30.227 1.00 132.80 ? 143 ALA A C 1 ATOM 1120 O O . ALA A 1 144 ? 11.618 24.080 29.915 1.00 131.70 ? 143 ALA A O 1 ATOM 1121 C CB . ALA A 1 144 ? 13.735 21.674 29.317 1.00 137.25 ? 143 ALA A CB 1 ATOM 1122 N N . LEU A 1 145 ? 10.755 22.036 30.299 1.00 128.37 ? 144 LEU A N 1 ATOM 1123 C CA . LEU A 1 145 ? 9.376 22.436 30.055 1.00 127.57 ? 144 LEU A CA 1 ATOM 1124 C C . LEU A 1 145 ? 8.923 23.481 31.067 1.00 128.96 ? 144 LEU A C 1 ATOM 1125 O O . LEU A 1 145 ? 8.368 24.514 30.690 1.00 130.86 ? 144 LEU A O 1 ATOM 1126 C CB . LEU A 1 145 ? 8.454 21.216 30.123 1.00 128.52 ? 144 LEU A CB 1 ATOM 1127 C CG . LEU A 1 145 ? 6.957 21.449 29.895 1.00 128.98 ? 144 LEU A CG 1 ATOM 1128 C CD1 . LEU A 1 145 ? 6.729 22.269 28.634 1.00 128.18 ? 144 LEU A CD1 1 ATOM 1129 C CD2 . LEU A 1 145 ? 6.205 20.124 29.824 1.00 128.58 ? 144 LEU A CD2 1 ATOM 1130 N N . ARG A 1 146 ? 9.166 23.211 32.348 1.00 128.37 ? 145 ARG A N 1 ATOM 1131 C CA . ARG A 1 146 ? 8.813 24.155 33.409 1.00 130.62 ? 145 ARG A CA 1 ATOM 1132 C C . ARG A 1 146 ? 9.497 25.501 33.182 1.00 136.09 ? 145 ARG A C 1 ATOM 1133 O O . ARG A 1 146 ? 8.863 26.552 33.254 1.00 137.43 ? 145 ARG A O 1 ATOM 1134 C CB . ARG A 1 146 ? 9.217 23.624 34.784 1.00 131.65 ? 145 ARG A CB 1 ATOM 1135 C CG . ARG A 1 146 ? 8.506 24.320 35.938 1.00 134.04 ? 145 ARG A CG 1 ATOM 1136 C CD . ARG A 1 146 ? 9.476 24.790 37.015 1.00 136.62 ? 145 ARG A CD 1 ATOM 1137 N NE . ARG A 1 146 ? 8.773 25.302 38.179 1.00 142.28 ? 145 ARG A NE 1 ATOM 1138 C CZ . ARG A 1 146 ? 8.374 24.567 39.215 1.00 145.41 ? 145 ARG A CZ 1 ATOM 1139 N NH1 . ARG A 1 146 ? 8.603 23.257 39.257 1.00 146.53 ? 145 ARG A NH1 1 ATOM 1140 N NH2 . ARG A 1 146 ? 7.736 25.153 40.221 1.00 146.28 ? 145 ARG A NH2 1 ATOM 1141 N N . GLU A 1 147 ? 10.795 25.463 32.908 1.00 139.69 ? 146 GLU A N 1 ATOM 1142 C CA . GLU A 1 147 ? 11.551 26.687 32.682 1.00 141.94 ? 146 GLU A CA 1 ATOM 1143 C C . GLU A 1 147 ? 11.084 27.440 31.443 1.00 132.84 ? 146 GLU A C 1 ATOM 1144 O O . GLU A 1 147 ? 11.013 28.665 31.462 1.00 131.76 ? 146 GLU A O 1 ATOM 1145 C CB . GLU A 1 147 ? 13.050 26.397 32.592 1.00 152.25 ? 146 GLU A CB 1 ATOM 1146 C CG . GLU A 1 147 ? 13.682 26.048 33.934 1.00 161.66 ? 146 GLU A CG 1 ATOM 1147 C CD . GLU A 1 147 ? 15.200 26.102 33.906 1.00 170.08 ? 146 GLU A CD 1 ATOM 1148 O OE1 . GLU A 1 147 ? 15.801 25.610 32.923 1.00 177.24 ? 146 GLU A OE1 1 ATOM 1149 O OE2 . GLU A 1 147 ? 15.793 26.631 34.874 1.00 172.98 ? 146 GLU A OE2 1 ATOM 1150 N N . MET A 1 148 ? 10.769 26.712 30.375 1.00 125.15 ? 147 MET A N 1 ATOM 1151 C CA . MET A 1 148 ? 10.295 27.331 29.139 1.00 123.47 ? 147 MET A CA 1 ATOM 1152 C C . MET A 1 148 ? 8.956 28.030 29.356 1.00 121.55 ? 147 MET A C 1 ATOM 1153 O O . MET A 1 148 ? 8.745 29.139 28.870 1.00 115.96 ? 147 MET A O 1 ATOM 1154 C CB . MET A 1 148 ? 10.162 26.293 28.022 1.00 123.01 ? 147 MET A CB 1 ATOM 1155 C CG . MET A 1 148 ? 9.821 26.899 26.666 1.00 123.81 ? 147 MET A CG 1 ATOM 1156 S SD . MET A 1 148 ? 9.962 25.740 25.292 1.00 124.09 ? 147 MET A SD 1 ATOM 1157 C CE . MET A 1 148 ? 8.522 24.707 25.553 1.00 123.01 ? 147 MET A CE 1 ATOM 1158 N N . ILE A 1 149 ? 8.060 27.380 30.090 1.00 124.36 ? 148 ILE A N 1 ATOM 1159 C CA . ILE A 1 149 ? 6.759 27.967 30.407 1.00 129.83 ? 148 ILE A CA 1 ATOM 1160 C C . ILE A 1 149 ? 6.929 29.258 31.212 1.00 134.47 ? 148 ILE A C 1 ATOM 1161 O O . ILE A 1 149 ? 6.285 30.266 30.914 1.00 135.63 ? 148 ILE A O 1 ATOM 1162 C CB . ILE A 1 149 ? 5.859 26.972 31.176 1.00 131.36 ? 148 ILE A CB 1 ATOM 1163 C CG1 . ILE A 1 149 ? 5.433 25.829 30.247 1.00 130.95 ? 148 ILE A CG1 1 ATOM 1164 C CG2 . ILE A 1 149 ? 4.617 27.668 31.730 1.00 133.07 ? 148 ILE A CG2 1 ATOM 1165 C CD1 . ILE A 1 149 ? 4.974 24.585 30.978 1.00 132.62 ? 148 ILE A CD1 1 ATOM 1166 N N . GLU A 1 150 ? 7.794 29.227 32.223 1.00 136.37 ? 149 GLU A N 1 ATOM 1167 C CA . GLU A 1 150 ? 8.070 30.418 33.026 1.00 140.54 ? 149 GLU A CA 1 ATOM 1168 C C . GLU A 1 150 ? 8.642 31.558 32.175 1.00 146.16 ? 149 GLU A C 1 ATOM 1169 O O . GLU A 1 150 ? 8.249 32.714 32.336 1.00 150.66 ? 149 GLU A O 1 ATOM 1170 C CB . GLU A 1 150 ? 9.012 30.084 34.187 1.00 140.64 ? 149 GLU A CB 1 ATOM 1171 C CG . GLU A 1 150 ? 8.370 29.223 35.267 1.00 139.86 ? 149 GLU A CG 1 ATOM 1172 C CD . GLU A 1 150 ? 9.344 28.789 36.348 1.00 141.74 ? 149 GLU A CD 1 ATOM 1173 O OE1 . GLU A 1 150 ? 10.502 29.255 36.346 1.00 143.70 ? 149 GLU A OE1 1 ATOM 1174 O OE2 . GLU A 1 150 ? 8.950 27.977 37.210 1.00 141.77 ? 149 GLU A OE2 1 ATOM 1175 N N . GLU A 1 151 ? 9.553 31.227 31.261 1.00 149.58 ? 150 GLU A N 1 ATOM 1176 C CA . GLU A 1 151 ? 10.143 32.222 30.359 1.00 153.87 ? 150 GLU A CA 1 ATOM 1177 C C . GLU A 1 151 ? 9.077 32.852 29.459 1.00 149.94 ? 150 GLU A C 1 ATOM 1178 O O . GLU A 1 151 ? 9.049 34.067 29.277 1.00 156.08 ? 150 GLU A O 1 ATOM 1179 C CB . GLU A 1 151 ? 11.237 31.589 29.488 1.00 160.78 ? 150 GLU A CB 1 ATOM 1180 C CG . GLU A 1 151 ? 12.116 32.603 28.761 1.00 170.20 ? 150 GLU A CG 1 ATOM 1181 C CD . GLU A 1 151 ? 12.959 31.990 27.654 1.00 177.61 ? 150 GLU A CD 1 ATOM 1182 O OE1 . GLU A 1 151 ? 13.334 32.732 26.717 1.00 185.75 ? 150 GLU A OE1 1 ATOM 1183 O OE2 . GLU A 1 151 ? 13.251 30.775 27.711 1.00 179.89 ? 150 GLU A OE2 1 ATOM 1184 N N . MET A 1 152 ? 8.212 32.021 28.889 1.00 142.12 ? 151 MET A N 1 ATOM 1185 C CA . MET A 1 152 ? 7.173 32.510 27.987 1.00 137.96 ? 151 MET A CA 1 ATOM 1186 C C . MET A 1 152 ? 6.180 33.405 28.732 1.00 135.12 ? 151 MET A C 1 ATOM 1187 O O . MET A 1 152 ? 5.726 34.414 28.195 1.00 129.87 ? 151 MET A O 1 ATOM 1188 C CB . MET A 1 152 ? 6.458 31.340 27.299 1.00 137.77 ? 151 MET A CB 1 ATOM 1189 C CG . MET A 1 152 ? 7.342 30.577 26.315 1.00 139.32 ? 151 MET A CG 1 ATOM 1190 S SD . MET A 1 152 ? 6.627 29.037 25.692 1.00 137.26 ? 151 MET A SD 1 ATOM 1191 C CE . MET A 1 152 ? 5.592 29.661 24.370 1.00 138.50 ? 151 MET A CE 1 ATOM 1192 N N . TYR A 1 153 ? 5.858 33.042 29.971 1.00 135.63 ? 152 TYR A N 1 ATOM 1193 C CA . TYR A 1 153 ? 4.992 33.869 30.818 1.00 139.32 ? 152 TYR A CA 1 ATOM 1194 C C . TYR A 1 153 ? 5.593 35.256 31.022 1.00 140.73 ? 152 TYR A C 1 ATOM 1195 O O . TYR A 1 153 ? 4.894 36.257 30.921 1.00 138.63 ? 152 TYR A O 1 ATOM 1196 C CB . TYR A 1 153 ? 4.758 33.202 32.183 1.00 142.35 ? 152 TYR A CB 1 ATOM 1197 C CG . TYR A 1 153 ? 3.982 34.050 33.183 1.00 143.56 ? 152 TYR A CG 1 ATOM 1198 C CD1 . TYR A 1 153 ? 4.635 34.963 34.010 1.00 146.05 ? 152 TYR A CD1 1 ATOM 1199 C CD2 . TYR A 1 153 ? 2.600 33.927 33.309 1.00 143.18 ? 152 TYR A CD2 1 ATOM 1200 C CE1 . TYR A 1 153 ? 3.932 35.735 34.922 1.00 149.13 ? 152 TYR A CE1 1 ATOM 1201 C CE2 . TYR A 1 153 ? 1.890 34.694 34.221 1.00 145.14 ? 152 TYR A CE2 1 ATOM 1202 C CZ . TYR A 1 153 ? 2.560 35.597 35.025 1.00 147.95 ? 152 TYR A CZ 1 ATOM 1203 O OH . TYR A 1 153 ? 1.862 36.366 35.928 1.00 148.67 ? 152 TYR A OH 1 ATOM 1204 N N . GLN A 1 154 ? 6.887 35.300 31.324 1.00 144.54 ? 153 GLN A N 1 ATOM 1205 C CA . GLN A 1 154 ? 7.584 36.559 31.573 1.00 151.14 ? 153 GLN A CA 1 ATOM 1206 C C . GLN A 1 154 ? 7.722 37.393 30.301 1.00 147.36 ? 153 GLN A C 1 ATOM 1207 O O . GLN A 1 154 ? 7.487 38.602 30.322 1.00 149.87 ? 153 GLN A O 1 ATOM 1208 C CB . GLN A 1 154 ? 8.974 36.297 32.171 1.00 160.40 ? 153 GLN A CB 1 ATOM 1209 C CG . GLN A 1 154 ? 8.986 35.689 33.572 1.00 169.32 ? 153 GLN A CG 1 ATOM 1210 C CD . GLN A 1 154 ? 8.261 36.522 34.621 1.00 178.99 ? 153 GLN A CD 1 ATOM 1211 O OE1 . GLN A 1 154 ? 8.183 37.749 34.525 1.00 186.70 ? 153 GLN A OE1 1 ATOM 1212 N NE2 . GLN A 1 154 ? 7.732 35.852 35.641 1.00 183.57 ? 153 GLN A NE2 1 ATOM 1213 N N . LEU A 1 155 ? 8.105 36.744 29.203 1.00 141.99 ? 154 LEU A N 1 ATOM 1214 C CA . LEU A 1 155 ? 8.298 37.429 27.920 1.00 141.59 ? 154 LEU A CA 1 ATOM 1215 C C . LEU A 1 155 ? 6.996 38.001 27.360 1.00 141.10 ? 154 LEU A C 1 ATOM 1216 O O . LEU A 1 155 ? 6.948 39.169 26.963 1.00 146.31 ? 154 LEU A O 1 ATOM 1217 C CB . LEU A 1 155 ? 8.951 36.500 26.876 1.00 138.76 ? 154 LEU A CB 1 ATOM 1218 C CG . LEU A 1 155 ? 10.450 36.697 26.605 1.00 139.36 ? 154 LEU A CG 1 ATOM 1219 C CD1 . LEU A 1 155 ? 11.078 35.469 25.963 1.00 135.21 ? 154 LEU A CD1 1 ATOM 1220 C CD2 . LEU A 1 155 ? 10.678 37.920 25.728 1.00 141.34 ? 154 LEU A CD2 1 ATOM 1221 N N . TYR A 1 156 ? 5.947 37.185 27.341 1.00 135.54 ? 155 TYR A N 1 ATOM 1222 C CA . TYR A 1 156 ? 4.710 37.546 26.652 1.00 134.94 ? 155 TYR A CA 1 ATOM 1223 C C . TYR A 1 156 ? 3.592 38.008 27.577 1.00 137.02 ? 155 TYR A C 1 ATOM 1224 O O . TYR A 1 156 ? 2.500 38.338 27.116 1.00 139.00 ? 155 TYR A O 1 ATOM 1225 C CB . TYR A 1 156 ? 4.277 36.397 25.747 1.00 131.58 ? 155 TYR A CB 1 ATOM 1226 C CG . TYR A 1 156 ? 5.451 35.905 24.936 1.00 130.81 ? 155 TYR A CG 1 ATOM 1227 C CD1 . TYR A 1 156 ? 6.129 36.767 24.079 1.00 130.31 ? 155 TYR A CD1 1 ATOM 1228 C CD2 . TYR A 1 156 ? 5.921 34.603 25.063 1.00 131.96 ? 155 TYR A CD2 1 ATOM 1229 C CE1 . TYR A 1 156 ? 7.224 36.342 23.352 1.00 130.33 ? 155 TYR A CE1 1 ATOM 1230 C CE2 . TYR A 1 156 ? 7.016 34.167 24.336 1.00 131.51 ? 155 TYR A CE2 1 ATOM 1231 C CZ . TYR A 1 156 ? 7.663 35.043 23.482 1.00 131.13 ? 155 TYR A CZ 1 ATOM 1232 O OH . TYR A 1 156 ? 8.751 34.626 22.754 1.00 133.76 ? 155 TYR A OH 1 ATOM 1233 N N . GLY A 1 157 ? 3.872 38.044 28.877 1.00 139.46 ? 156 GLY A N 1 ATOM 1234 C CA . GLY A 1 157 ? 3.013 38.726 29.844 1.00 145.10 ? 156 GLY A CA 1 ATOM 1235 C C . GLY A 1 157 ? 1.757 37.992 30.277 1.00 145.89 ? 156 GLY A C 1 ATOM 1236 O O . GLY A 1 157 ? 0.836 38.612 30.810 1.00 152.99 ? 156 GLY A O 1 ATOM 1237 N N . GLY A 1 158 ? 1.712 36.680 30.070 1.00 143.40 ? 157 GLY A N 1 ATOM 1238 C CA . GLY A 1 158 ? 0.512 35.916 30.386 1.00 141.52 ? 157 GLY A CA 1 ATOM 1239 C C . GLY A 1 158 ? 0.728 34.418 30.420 1.00 137.69 ? 157 GLY A C 1 ATOM 1240 O O . GLY A 1 158 ? 1.723 33.920 29.889 1.00 132.72 ? 157 GLY A O 1 ATOM 1241 N N . PRO A 1 159 ? -0.207 33.690 31.054 1.00 137.45 ? 158 PRO A N 1 ATOM 1242 C CA . PRO A 1 159 ? -0.121 32.238 31.185 1.00 137.41 ? 158 PRO A CA 1 ATOM 1243 C C . PRO A 1 159 ? -0.269 31.518 29.850 1.00 137.23 ? 158 PRO A C 1 ATOM 1244 O O . PRO A 1 159 ? -0.863 32.064 28.913 1.00 139.76 ? 158 PRO A O 1 ATOM 1245 C CB . PRO A 1 159 ? -1.278 31.897 32.128 1.00 139.45 ? 158 PRO A CB 1 ATOM 1246 C CG . PRO A 1 159 ? -2.242 33.021 31.987 1.00 139.90 ? 158 PRO A CG 1 ATOM 1247 C CD . PRO A 1 159 ? -1.427 34.236 31.679 1.00 139.34 ? 158 PRO A CD 1 ATOM 1248 N N . VAL A 1 160 ? 0.264 30.298 29.785 1.00 137.01 ? 159 VAL A N 1 ATOM 1249 C CA . VAL A 1 160 ? 0.362 29.545 28.531 1.00 137.37 ? 159 VAL A CA 1 ATOM 1250 C C . VAL A 1 160 ? -0.786 28.560 28.327 1.00 136.28 ? 159 VAL A C 1 ATOM 1251 O O . VAL A 1 160 ? -1.379 28.049 29.287 1.00 138.86 ? 159 VAL A O 1 ATOM 1252 C CB . VAL A 1 160 ? 1.693 28.759 28.416 1.00 138.72 ? 159 VAL A CB 1 ATOM 1253 C CG1 . VAL A 1 160 ? 2.888 29.660 28.700 1.00 139.47 ? 159 VAL A CG1 1 ATOM 1254 C CG2 . VAL A 1 160 ? 1.703 27.537 29.332 1.00 140.68 ? 159 VAL A CG2 1 ATOM 1255 N N . VAL A 1 161 ? -1.085 28.299 27.061 1.00 134.50 ? 160 VAL A N 1 ATOM 1256 C CA . VAL A 1 161 ? -2.027 27.259 26.693 1.00 133.04 ? 160 VAL A CA 1 ATOM 1257 C C . VAL A 1 161 ? -1.216 26.079 26.200 1.00 130.15 ? 160 VAL A C 1 ATOM 1258 O O . VAL A 1 161 ? -0.411 26.223 25.278 1.00 126.66 ? 160 VAL A O 1 ATOM 1259 C CB . VAL A 1 161 ? -2.970 27.714 25.566 1.00 136.17 ? 160 VAL A CB 1 ATOM 1260 C CG1 . VAL A 1 161 ? -4.001 26.631 25.266 1.00 136.08 ? 160 VAL A CG1 1 ATOM 1261 C CG2 . VAL A 1 161 ? -3.649 29.022 25.945 1.00 141.13 ? 160 VAL A CG2 1 ATOM 1262 N N . LEU A 1 162 ? -1.421 24.926 26.828 1.00 130.66 ? 161 LEU A N 1 ATOM 1263 C CA . LEU A 1 162 ? -0.810 23.680 26.380 1.00 131.33 ? 161 LEU A CA 1 ATOM 1264 C C . LEU A 1 162 ? -1.743 23.007 25.393 1.00 125.81 ? 161 LEU A C 1 ATOM 1265 O O . LEU A 1 162 ? -2.938 22.887 25.650 1.00 123.96 ? 161 LEU A O 1 ATOM 1266 C CB . LEU A 1 162 ? -0.574 22.738 27.561 1.00 137.55 ? 161 LEU A CB 1 ATOM 1267 C CG . LEU A 1 162 ? 0.275 23.291 28.704 1.00 142.58 ? 161 LEU A CG 1 ATOM 1268 C CD1 . LEU A 1 162 ? 0.448 22.231 29.781 1.00 143.83 ? 161 LEU A CD1 1 ATOM 1269 C CD2 . LEU A 1 162 ? 1.628 23.760 28.191 1.00 144.88 ? 161 LEU A CD2 1 ATOM 1270 N N . VAL A 1 163 ? -1.194 22.578 24.266 1.00 121.34 ? 162 VAL A N 1 ATOM 1271 C CA . VAL A 1 163 ? -1.950 21.822 23.284 1.00 119.45 ? 162 VAL A CA 1 ATOM 1272 C C . VAL A 1 163 ? -1.186 20.527 23.077 1.00 120.95 ? 162 VAL A C 1 ATOM 1273 O O . VAL A 1 163 ? -0.056 20.551 22.597 1.00 120.22 ? 162 VAL A O 1 ATOM 1274 C CB . VAL A 1 163 ? -2.057 22.590 21.954 1.00 117.50 ? 162 VAL A CB 1 ATOM 1275 C CG1 . VAL A 1 163 ? -2.981 21.858 20.988 1.00 117.92 ? 162 VAL A CG1 1 ATOM 1276 C CG2 . VAL A 1 163 ? -2.545 24.010 22.205 1.00 117.40 ? 162 VAL A CG2 1 ATOM 1277 N N . ALA A 1 164 ? -1.795 19.404 23.453 1.00 125.65 ? 163 ALA A N 1 ATOM 1278 C CA . ALA A 1 164 ? -1.126 18.100 23.399 1.00 127.20 ? 163 ALA A CA 1 ATOM 1279 C C . ALA A 1 164 ? -1.914 17.100 22.560 1.00 125.51 ? 163 ALA A C 1 ATOM 1280 O O . ALA A 1 164 ? -3.143 17.141 22.513 1.00 123.67 ? 163 ALA A O 1 ATOM 1281 C CB . ALA A 1 164 ? -0.922 17.559 24.806 1.00 127.24 ? 163 ALA A CB 1 ATOM 1282 N N . HIS A 1 165 ? -1.191 16.199 21.903 1.00 124.30 ? 164 HIS A N 1 ATOM 1283 C CA . HIS A 1 165 ? -1.797 15.195 21.044 1.00 123.80 ? 164 HIS A CA 1 ATOM 1284 C C . HIS A 1 165 ? -1.405 13.794 21.504 1.00 121.57 ? 164 HIS A C 1 ATOM 1285 O O . HIS A 1 165 ? -0.248 13.552 21.842 1.00 117.25 ? 164 HIS A O 1 ATOM 1286 C CB . HIS A 1 165 ? -1.359 15.411 19.597 1.00 122.07 ? 164 HIS A CB 1 ATOM 1287 C CG . HIS A 1 165 ? -1.892 14.381 18.653 1.00 124.70 ? 164 HIS A CG 1 ATOM 1288 N ND1 . HIS A 1 165 ? -1.104 13.392 18.105 1.00 123.70 ? 164 HIS A ND1 1 ATOM 1289 C CD2 . HIS A 1 165 ? -3.144 14.168 18.183 1.00 126.27 ? 164 HIS A CD2 1 ATOM 1290 C CE1 . HIS A 1 165 ? -1.843 12.625 17.324 1.00 124.42 ? 164 HIS A CE1 1 ATOM 1291 N NE2 . HIS A 1 165 ? -3.085 13.074 17.355 1.00 125.32 ? 164 HIS A NE2 1 ATOM 1292 N N . SER A 1 166 ? -2.380 12.887 21.517 1.00 120.95 ? 165 SER A N 1 ATOM 1293 C CA . SER A 1 166 ? -2.153 11.481 21.847 1.00 126.02 ? 165 SER A CA 1 ATOM 1294 C C . SER A 1 166 ? -1.363 11.325 23.155 1.00 120.16 ? 165 SER A C 1 ATOM 1295 O O . SER A 1 166 ? -1.729 11.918 24.169 1.00 116.79 ? 165 SER A O 1 ATOM 1296 C CB . SER A 1 166 ? -1.479 10.771 20.666 1.00 135.60 ? 165 SER A CB 1 ATOM 1297 O OG . SER A 1 166 ? -1.418 9.359 20.847 1.00 149.46 ? 165 SER A OG 1 ATOM 1298 N N . MET A 1 167 ? -0.273 10.558 23.127 1.00 116.58 ? 166 MET A N 1 ATOM 1299 C CA . MET A 1 167 ? 0.544 10.307 24.314 1.00 115.36 ? 166 MET A CA 1 ATOM 1300 C C . MET A 1 167 ? 1.067 11.581 24.975 1.00 112.66 ? 166 MET A C 1 ATOM 1301 O O . MET A 1 167 ? 1.342 11.583 26.172 1.00 108.06 ? 166 MET A O 1 ATOM 1302 C CB . MET A 1 167 ? 1.725 9.401 23.952 1.00 118.59 ? 166 MET A CB 1 ATOM 1303 C CG . MET A 1 167 ? 2.500 8.866 25.147 1.00 121.02 ? 166 MET A CG 1 ATOM 1304 S SD . MET A 1 167 ? 3.784 7.694 24.663 1.00 126.38 ? 166 MET A SD 1 ATOM 1305 C CE . MET A 1 167 ? 4.929 8.780 23.817 1.00 125.82 ? 166 MET A CE 1 ATOM 1306 N N . GLY A 1 168 ? 1.205 12.658 24.202 1.00 110.88 ? 167 GLY A N 1 ATOM 1307 C CA . GLY A 1 168 ? 1.600 13.950 24.753 1.00 110.85 ? 167 GLY A CA 1 ATOM 1308 C C . GLY A 1 168 ? 0.729 14.354 25.931 1.00 112.62 ? 167 GLY A C 1 ATOM 1309 O O . GLY A 1 168 ? 1.191 15.013 26.861 1.00 114.71 ? 167 GLY A O 1 ATOM 1310 N N . ASN A 1 169 ? -0.539 13.959 25.891 1.00 112.37 ? 168 ASN A N 1 ATOM 1311 C CA . ASN A 1 169 ? -1.468 14.276 26.967 1.00 113.88 ? 168 ASN A CA 1 ATOM 1312 C C . ASN A 1 169 ? -1.126 13.570 28.268 1.00 114.57 ? 168 ASN A C 1 ATOM 1313 O O . ASN A 1 169 ? -1.243 14.157 29.342 1.00 111.42 ? 168 ASN A O 1 ATOM 1314 C CB . ASN A 1 169 ? -2.893 13.927 26.546 1.00 113.88 ? 168 ASN A CB 1 ATOM 1315 C CG . ASN A 1 169 ? -3.385 14.794 25.405 1.00 112.79 ? 168 ASN A CG 1 ATOM 1316 O OD1 . ASN A 1 169 ? -3.761 15.945 25.614 1.00 107.40 ? 168 ASN A OD1 1 ATOM 1317 N ND2 . ASN A 1 169 ? -3.392 14.245 24.192 1.00 111.06 ? 168 ASN A ND2 1 ATOM 1318 N N . MET A 1 170 ? -0.705 12.313 28.164 1.00 117.99 ? 169 MET A N 1 ATOM 1319 C CA . MET A 1 170 ? -0.301 11.530 29.332 1.00 126.14 ? 169 MET A CA 1 ATOM 1320 C C . MET A 1 170 ? 0.987 12.080 29.938 1.00 124.52 ? 169 MET A C 1 ATOM 1321 O O . MET A 1 170 ? 1.115 12.178 31.161 1.00 122.69 ? 169 MET A O 1 ATOM 1322 C CB . MET A 1 170 ? -0.091 10.061 28.949 1.00 136.96 ? 169 MET A CB 1 ATOM 1323 C CG . MET A 1 170 ? -1.377 9.296 28.661 1.00 151.39 ? 169 MET A CG 1 ATOM 1324 S SD . MET A 1 170 ? -2.033 8.349 30.062 1.00 174.66 ? 169 MET A SD 1 ATOM 1325 C CE . MET A 1 170 ? -1.287 6.735 29.812 1.00 168.94 ? 169 MET A CE 1 ATOM 1326 N N . TYR A 1 171 ? 1.940 12.420 29.072 1.00 122.92 ? 170 TYR A N 1 ATOM 1327 C CA . TYR A 1 171 ? 3.180 13.081 29.493 1.00 119.58 ? 170 TYR A CA 1 ATOM 1328 C C . TYR A 1 171 ? 2.884 14.376 30.231 1.00 114.52 ? 170 TYR A C 1 ATOM 1329 O O . TYR A 1 171 ? 3.415 14.619 31.319 1.00 112.89 ? 170 TYR A O 1 ATOM 1330 C CB . TYR A 1 171 ? 4.091 13.375 28.288 1.00 118.92 ? 170 TYR A CB 1 ATOM 1331 C CG . TYR A 1 171 ? 5.275 12.441 28.174 1.00 120.05 ? 170 TYR A CG 1 ATOM 1332 C CD1 . TYR A 1 171 ? 5.134 11.168 27.629 1.00 120.67 ? 170 TYR A CD1 1 ATOM 1333 C CD2 . TYR A 1 171 ? 6.537 12.828 28.616 1.00 120.12 ? 170 TYR A CD2 1 ATOM 1334 C CE1 . TYR A 1 171 ? 6.216 10.308 27.527 1.00 121.66 ? 170 TYR A CE1 1 ATOM 1335 C CE2 . TYR A 1 171 ? 7.625 11.976 28.519 1.00 121.02 ? 170 TYR A CE2 1 ATOM 1336 C CZ . TYR A 1 171 ? 7.460 10.718 27.973 1.00 121.68 ? 170 TYR A CZ 1 ATOM 1337 O OH . TYR A 1 171 ? 8.537 9.868 27.872 1.00 123.31 ? 170 TYR A OH 1 ATOM 1338 N N . THR A 1 172 ? 2.031 15.205 29.639 1.00 111.49 ? 171 THR A N 1 ATOM 1339 C CA . THR A 1 172 ? 1.732 16.497 30.232 1.00 112.62 ? 171 THR A CA 1 ATOM 1340 C C . THR A 1 172 ? 0.867 16.362 31.499 1.00 113.30 ? 171 THR A C 1 ATOM 1341 O O . THR A 1 172 ? 1.056 17.125 32.438 1.00 113.08 ? 171 THR A O 1 ATOM 1342 C CB . THR A 1 172 ? 1.240 17.532 29.184 1.00 111.80 ? 171 THR A CB 1 ATOM 1343 O OG1 . THR A 1 172 ? 2.378 18.177 28.584 1.00 103.97 ? 171 THR A OG1 1 ATOM 1344 C CG2 . THR A 1 172 ? 0.364 18.609 29.809 1.00 115.22 ? 171 THR A CG2 1 ATOM 1345 N N . LEU A 1 173 ? -0.034 15.383 31.558 1.00 113.33 ? 172 LEU A N 1 ATOM 1346 C CA . LEU A 1 173 ? -0.780 15.112 32.797 1.00 118.09 ? 172 LEU A CA 1 ATOM 1347 C C . LEU A 1 173 ? 0.158 14.727 33.944 1.00 121.47 ? 172 LEU A C 1 ATOM 1348 O O . LEU A 1 173 ? 0.027 15.225 35.062 1.00 124.17 ? 172 LEU A O 1 ATOM 1349 C CB . LEU A 1 173 ? -1.801 13.992 32.590 1.00 119.37 ? 172 LEU A CB 1 ATOM 1350 C CG . LEU A 1 173 ? -2.488 13.486 33.869 1.00 121.55 ? 172 LEU A CG 1 ATOM 1351 C CD1 . LEU A 1 173 ? -3.247 14.602 34.572 1.00 123.62 ? 172 LEU A CD1 1 ATOM 1352 C CD2 . LEU A 1 173 ? -3.425 12.332 33.554 1.00 123.31 ? 172 LEU A CD2 1 ATOM 1353 N N . TYR A 1 174 ? 1.089 13.825 33.664 1.00 121.85 ? 173 TYR A N 1 ATOM 1354 C CA . TYR A 1 174 ? 2.124 13.462 34.633 1.00 125.00 ? 173 TYR A CA 1 ATOM 1355 C C . TYR A 1 174 ? 2.827 14.719 35.142 1.00 126.42 ? 173 TYR A C 1 ATOM 1356 O O . TYR A 1 174 ? 2.972 14.917 36.345 1.00 126.96 ? 173 TYR A O 1 ATOM 1357 C CB . TYR A 1 174 ? 3.132 12.520 33.968 1.00 127.47 ? 173 TYR A CB 1 ATOM 1358 C CG . TYR A 1 174 ? 4.401 12.227 34.749 1.00 131.84 ? 173 TYR A CG 1 ATOM 1359 C CD1 . TYR A 1 174 ? 4.451 11.187 35.673 1.00 134.56 ? 173 TYR A CD1 1 ATOM 1360 C CD2 . TYR A 1 174 ? 5.566 12.962 34.527 1.00 132.50 ? 173 TYR A CD2 1 ATOM 1361 C CE1 . TYR A 1 174 ? 5.615 10.902 36.370 1.00 134.86 ? 173 TYR A CE1 1 ATOM 1362 C CE2 . TYR A 1 174 ? 6.735 12.684 35.219 1.00 133.36 ? 173 TYR A CE2 1 ATOM 1363 C CZ . TYR A 1 174 ? 6.756 11.651 36.137 1.00 134.65 ? 173 TYR A CZ 1 ATOM 1364 O OH . TYR A 1 174 ? 7.913 11.372 36.826 1.00 135.76 ? 173 TYR A OH 1 ATOM 1365 N N . PHE A 1 175 ? 3.253 15.565 34.210 1.00 125.73 ? 174 PHE A N 1 ATOM 1366 C CA . PHE A 1 175 ? 3.908 16.832 34.533 1.00 126.70 ? 174 PHE A CA 1 ATOM 1367 C C . PHE A 1 175 ? 3.053 17.694 35.463 1.00 126.04 ? 174 PHE A C 1 ATOM 1368 O O . PHE A 1 175 ? 3.514 18.117 36.521 1.00 124.94 ? 174 PHE A O 1 ATOM 1369 C CB . PHE A 1 175 ? 4.217 17.594 33.235 1.00 127.77 ? 174 PHE A CB 1 ATOM 1370 C CG . PHE A 1 175 ? 4.648 19.019 33.444 1.00 128.82 ? 174 PHE A CG 1 ATOM 1371 C CD1 . PHE A 1 175 ? 5.862 19.310 34.050 1.00 128.85 ? 174 PHE A CD1 1 ATOM 1372 C CD2 . PHE A 1 175 ? 3.846 20.070 33.015 1.00 129.33 ? 174 PHE A CD2 1 ATOM 1373 C CE1 . PHE A 1 175 ? 6.264 20.620 34.237 1.00 131.19 ? 174 PHE A CE1 1 ATOM 1374 C CE2 . PHE A 1 175 ? 4.243 21.383 33.199 1.00 131.47 ? 174 PHE A CE2 1 ATOM 1375 C CZ . PHE A 1 175 ? 5.454 21.660 33.810 1.00 132.72 ? 174 PHE A CZ 1 ATOM 1376 N N . LEU A 1 176 ? 1.809 17.938 35.058 1.00 123.85 ? 175 LEU A N 1 ATOM 1377 C CA . LEU A 1 176 ? 0.882 18.796 35.809 1.00 124.16 ? 175 LEU A CA 1 ATOM 1378 C C . LEU A 1 176 ? 0.562 18.259 37.196 1.00 122.93 ? 175 LEU A C 1 ATOM 1379 O O . LEU A 1 176 ? 0.465 19.021 38.153 1.00 118.14 ? 175 LEU A O 1 ATOM 1380 C CB . LEU A 1 176 ? -0.435 18.961 35.043 1.00 124.02 ? 175 LEU A CB 1 ATOM 1381 C CG . LEU A 1 176 ? -0.401 19.831 33.787 1.00 123.66 ? 175 LEU A CG 1 ATOM 1382 C CD1 . LEU A 1 176 ? -1.665 19.619 32.962 1.00 123.29 ? 175 LEU A CD1 1 ATOM 1383 C CD2 . LEU A 1 176 ? -0.228 21.298 34.153 1.00 124.71 ? 175 LEU A CD2 1 ATOM 1384 N N . GLN A 1 177 ? 0.382 16.947 37.297 1.00 125.95 ? 176 GLN A N 1 ATOM 1385 C CA . GLN A 1 177 ? 0.131 16.312 38.587 1.00 133.78 ? 176 GLN A CA 1 ATOM 1386 C C . GLN A 1 177 ? 1.255 16.561 39.593 1.00 137.11 ? 176 GLN A C 1 ATOM 1387 O O . GLN A 1 177 ? 1.019 16.577 40.799 1.00 135.51 ? 176 GLN A O 1 ATOM 1388 C CB . GLN A 1 177 ? -0.068 14.808 38.412 1.00 136.08 ? 176 GLN A CB 1 ATOM 1389 C CG . GLN A 1 177 ? -1.433 14.434 37.865 1.00 138.95 ? 176 GLN A CG 1 ATOM 1390 C CD . GLN A 1 177 ? -1.656 12.939 37.848 1.00 143.28 ? 176 GLN A CD 1 ATOM 1391 O OE1 . GLN A 1 177 ? -0.712 12.157 37.973 1.00 146.05 ? 176 GLN A OE1 1 ATOM 1392 N NE2 . GLN A 1 177 ? -2.911 12.530 37.689 1.00 147.60 ? 176 GLN A NE2 1 ATOM 1393 N N . ARG A 1 178 ? 2.471 16.752 39.087 1.00 140.27 ? 177 ARG A N 1 ATOM 1394 C CA . ARG A 1 178 ? 3.651 16.945 39.927 1.00 143.11 ? 177 ARG A CA 1 ATOM 1395 C C . ARG A 1 178 ? 3.987 18.410 40.244 1.00 140.61 ? 177 ARG A C 1 ATOM 1396 O O . ARG A 1 178 ? 4.910 18.674 41.011 1.00 139.00 ? 177 ARG A O 1 ATOM 1397 C CB . ARG A 1 178 ? 4.853 16.268 39.269 1.00 146.33 ? 177 ARG A CB 1 ATOM 1398 C CG . ARG A 1 178 ? 4.651 14.779 39.036 1.00 147.87 ? 177 ARG A CG 1 ATOM 1399 C CD . ARG A 1 178 ? 5.732 14.197 38.144 1.00 149.00 ? 177 ARG A CD 1 ATOM 1400 N NE . ARG A 1 178 ? 6.936 13.860 38.904 1.00 150.34 ? 177 ARG A NE 1 ATOM 1401 C CZ . ARG A 1 178 ? 7.095 12.756 39.634 1.00 150.02 ? 177 ARG A CZ 1 ATOM 1402 N NH1 . ARG A 1 178 ? 6.126 11.847 39.724 1.00 148.86 ? 177 ARG A NH1 1 ATOM 1403 N NH2 . ARG A 1 178 ? 8.237 12.557 40.285 1.00 151.87 ? 177 ARG A NH2 1 ATOM 1404 N N . GLN A 1 179 ? 3.250 19.358 39.667 1.00 136.99 ? 178 GLN A N 1 ATOM 1405 C CA . GLN A 1 179 ? 3.465 20.772 39.963 1.00 136.44 ? 178 GLN A CA 1 ATOM 1406 C C . GLN A 1 179 ? 2.485 21.226 41.037 1.00 138.30 ? 178 GLN A C 1 ATOM 1407 O O . GLN A 1 179 ? 1.329 20.801 41.037 1.00 138.27 ? 178 GLN A O 1 ATOM 1408 C CB . GLN A 1 179 ? 3.267 21.623 38.706 1.00 134.46 ? 178 GLN A CB 1 ATOM 1409 C CG . GLN A 1 179 ? 4.145 21.219 37.535 1.00 132.82 ? 178 GLN A CG 1 ATOM 1410 C CD . GLN A 1 179 ? 5.606 21.084 37.921 1.00 132.31 ? 178 GLN A CD 1 ATOM 1411 O OE1 . GLN A 1 179 ? 6.187 21.996 38.510 1.00 132.24 ? 178 GLN A OE1 1 ATOM 1412 N NE2 . GLN A 1 179 ? 6.208 19.945 37.590 1.00 130.78 ? 178 GLN A NE2 1 ATOM 1413 N N . PRO A 1 180 ? 2.937 22.097 41.955 1.00 139.01 ? 179 PRO A N 1 ATOM 1414 C CA . PRO A 1 180 ? 2.013 22.599 42.968 1.00 139.93 ? 179 PRO A CA 1 ATOM 1415 C C . PRO A 1 180 ? 0.871 23.408 42.353 1.00 139.09 ? 179 PRO A C 1 ATOM 1416 O O . PRO A 1 180 ? 1.035 24.027 41.295 1.00 134.87 ? 179 PRO A O 1 ATOM 1417 C CB . PRO A 1 180 ? 2.897 23.475 43.860 1.00 141.57 ? 179 PRO A CB 1 ATOM 1418 C CG . PRO A 1 180 ? 4.059 23.847 43.011 1.00 140.71 ? 179 PRO A CG 1 ATOM 1419 C CD . PRO A 1 180 ? 4.277 22.697 42.078 1.00 139.41 ? 179 PRO A CD 1 ATOM 1420 N N . GLN A 1 181 ? -0.277 23.389 43.023 1.00 141.97 ? 180 GLN A N 1 ATOM 1421 C CA . GLN A 1 181 ? -1.485 24.044 42.521 1.00 140.14 ? 180 GLN A CA 1 ATOM 1422 C C . GLN A 1 181 ? -1.251 25.525 42.237 1.00 136.45 ? 180 GLN A C 1 ATOM 1423 O O . GLN A 1 181 ? -1.721 26.045 41.229 1.00 130.18 ? 180 GLN A O 1 ATOM 1424 C CB . GLN A 1 181 ? -2.644 23.875 43.517 1.00 143.99 ? 180 GLN A CB 1 ATOM 1425 C CG . GLN A 1 181 ? -4.022 24.181 42.943 1.00 143.87 ? 180 GLN A CG 1 ATOM 1426 C CD . GLN A 1 181 ? -4.453 23.187 41.879 1.00 141.53 ? 180 GLN A CD 1 ATOM 1427 O OE1 . GLN A 1 181 ? -4.378 21.972 42.078 1.00 142.43 ? 180 GLN A OE1 1 ATOM 1428 N NE2 . GLN A 1 181 ? -4.899 23.697 40.738 1.00 140.04 ? 180 GLN A NE2 1 ATOM 1429 N N . ALA A 1 182 ? -0.515 26.194 43.122 1.00 137.23 ? 181 ALA A N 1 ATOM 1430 C CA . ALA A 1 182 ? -0.215 27.617 42.961 1.00 138.16 ? 181 ALA A CA 1 ATOM 1431 C C . ALA A 1 182 ? 0.526 27.911 41.654 1.00 137.74 ? 181 ALA A C 1 ATOM 1432 O O . ALA A 1 182 ? 0.263 28.925 41.003 1.00 137.30 ? 181 ALA A O 1 ATOM 1433 C CB . ALA A 1 182 ? 0.594 28.118 44.148 1.00 137.81 ? 181 ALA A CB 1 ATOM 1434 N N . TRP A 1 183 ? 1.447 27.024 41.278 1.00 137.39 ? 182 TRP A N 1 ATOM 1435 C CA . TRP A 1 183 ? 2.203 27.179 40.036 1.00 134.70 ? 182 TRP A CA 1 ATOM 1436 C C . TRP A 1 183 ? 1.283 27.044 38.833 1.00 132.66 ? 182 TRP A C 1 ATOM 1437 O O . TRP A 1 183 ? 1.333 27.858 37.913 1.00 130.33 ? 182 TRP A O 1 ATOM 1438 C CB . TRP A 1 183 ? 3.330 26.145 39.943 1.00 134.59 ? 182 TRP A CB 1 ATOM 1439 C CG . TRP A 1 183 ? 4.230 26.347 38.757 1.00 135.01 ? 182 TRP A CG 1 ATOM 1440 C CD1 . TRP A 1 183 ? 5.361 27.108 38.709 1.00 136.19 ? 182 TRP A CD1 1 ATOM 1441 C CD2 . TRP A 1 183 ? 4.072 25.781 37.448 1.00 136.01 ? 182 TRP A CD2 1 ATOM 1442 N NE1 . TRP A 1 183 ? 5.917 27.053 37.453 1.00 137.35 ? 182 TRP A NE1 1 ATOM 1443 C CE2 . TRP A 1 183 ? 5.146 26.245 36.659 1.00 136.72 ? 182 TRP A CE2 1 ATOM 1444 C CE3 . TRP A 1 183 ? 3.125 24.929 36.866 1.00 135.97 ? 182 TRP A CE3 1 ATOM 1445 C CZ2 . TRP A 1 183 ? 5.303 25.883 35.314 1.00 135.99 ? 182 TRP A CZ2 1 ATOM 1446 C CZ3 . TRP A 1 183 ? 3.281 24.570 35.527 1.00 136.17 ? 182 TRP A CZ3 1 ATOM 1447 C CH2 . TRP A 1 183 ? 4.363 25.048 34.768 1.00 135.22 ? 182 TRP A CH2 1 ATOM 1448 N N . LYS A 1 184 ? 0.445 26.012 38.842 1.00 135.44 ? 183 LYS A N 1 ATOM 1449 C CA . LYS A 1 184 ? -0.473 25.754 37.727 1.00 135.87 ? 183 LYS A CA 1 ATOM 1450 C C . LYS A 1 184 ? -1.456 26.905 37.539 1.00 132.33 ? 183 LYS A C 1 ATOM 1451 O O . LYS A 1 184 ? -1.725 27.330 36.410 1.00 125.01 ? 183 LYS A O 1 ATOM 1452 C CB . LYS A 1 184 ? -1.256 24.456 37.958 1.00 140.51 ? 183 LYS A CB 1 ATOM 1453 C CG . LYS A 1 184 ? -0.420 23.188 37.869 1.00 142.41 ? 183 LYS A CG 1 ATOM 1454 C CD . LYS A 1 184 ? -1.275 21.939 38.028 1.00 144.41 ? 183 LYS A CD 1 ATOM 1455 C CE . LYS A 1 184 ? -1.727 21.740 39.468 1.00 148.91 ? 183 LYS A CE 1 ATOM 1456 N NZ . LYS A 1 184 ? -2.400 20.427 39.673 1.00 152.85 ? 183 LYS A NZ 1 ATOM 1457 N N . ASP A 1 185 ? -1.984 27.397 38.658 1.00 133.39 ? 184 ASP A N 1 ATOM 1458 C CA . ASP A 1 185 ? -2.944 28.498 38.648 1.00 135.97 ? 184 ASP A CA 1 ATOM 1459 C C . ASP A 1 185 ? -2.339 29.759 38.022 1.00 136.98 ? 184 ASP A C 1 ATOM 1460 O O . ASP A 1 185 ? -3.031 30.498 37.321 1.00 140.84 ? 184 ASP A O 1 ATOM 1461 C CB . ASP A 1 185 ? -3.439 28.806 40.074 1.00 140.10 ? 184 ASP A CB 1 ATOM 1462 C CG . ASP A 1 185 ? -4.322 27.697 40.656 1.00 141.40 ? 184 ASP A CG 1 ATOM 1463 O OD1 . ASP A 1 185 ? -4.399 26.598 40.062 1.00 141.63 ? 184 ASP A OD1 1 ATOM 1464 O OD2 . ASP A 1 185 ? -4.939 27.928 41.720 1.00 138.64 ? 184 ASP A OD2 1 ATOM 1465 N N . LYS A 1 186 ? -1.052 29.998 38.269 1.00 137.16 ? 185 LYS A N 1 ATOM 1466 C CA . LYS A 1 186 ? -0.371 31.178 37.732 1.00 138.79 ? 185 LYS A CA 1 ATOM 1467 C C . LYS A 1 186 ? 0.021 31.027 36.263 1.00 135.26 ? 185 LYS A C 1 ATOM 1468 O O . LYS A 1 186 ? -0.244 31.912 35.450 1.00 134.84 ? 185 LYS A O 1 ATOM 1469 C CB . LYS A 1 186 ? 0.882 31.503 38.557 1.00 142.92 ? 185 LYS A CB 1 ATOM 1470 C CG . LYS A 1 186 ? 1.774 32.571 37.935 1.00 147.45 ? 185 LYS A CG 1 ATOM 1471 C CD . LYS A 1 186 ? 2.773 33.144 38.926 1.00 153.46 ? 185 LYS A CD 1 ATOM 1472 C CE . LYS A 1 186 ? 3.607 34.241 38.280 1.00 157.82 ? 185 LYS A CE 1 ATOM 1473 N NZ . LYS A 1 186 ? 4.410 35.012 39.270 1.00 162.56 ? 185 LYS A NZ 1 ATOM 1474 N N . TYR A 1 187 ? 0.658 29.908 35.934 1.00 132.05 ? 186 TYR A N 1 ATOM 1475 C CA . TYR A 1 187 ? 1.365 29.772 34.664 1.00 132.07 ? 186 TYR A CA 1 ATOM 1476 C C . TYR A 1 187 ? 0.587 29.097 33.540 1.00 136.34 ? 186 TYR A C 1 ATOM 1477 O O . TYR A 1 187 ? 0.957 29.246 32.374 1.00 136.61 ? 186 TYR A O 1 ATOM 1478 C CB . TYR A 1 187 ? 2.689 29.038 34.879 1.00 132.28 ? 186 TYR A CB 1 ATOM 1479 C CG . TYR A 1 187 ? 3.735 29.877 35.567 1.00 134.09 ? 186 TYR A CG 1 ATOM 1480 C CD1 . TYR A 1 187 ? 4.542 30.742 34.840 1.00 135.24 ? 186 TYR A CD1 1 ATOM 1481 C CD2 . TYR A 1 187 ? 3.918 29.809 36.945 1.00 137.22 ? 186 TYR A CD2 1 ATOM 1482 C CE1 . TYR A 1 187 ? 5.503 31.518 35.465 1.00 140.21 ? 186 TYR A CE1 1 ATOM 1483 C CE2 . TYR A 1 187 ? 4.876 30.580 37.580 1.00 139.97 ? 186 TYR A CE2 1 ATOM 1484 C CZ . TYR A 1 187 ? 5.666 31.433 36.836 1.00 141.88 ? 186 TYR A CZ 1 ATOM 1485 O OH . TYR A 1 187 ? 6.621 32.203 37.459 1.00 145.58 ? 186 TYR A OH 1 ATOM 1486 N N . ILE A 1 188 ? -0.468 28.353 33.876 1.00 138.60 ? 187 ILE A N 1 ATOM 1487 C CA . ILE A 1 188 ? -1.255 27.642 32.871 1.00 140.05 ? 187 ILE A CA 1 ATOM 1488 C C . ILE A 1 188 ? -2.616 28.295 32.690 1.00 139.78 ? 187 ILE A C 1 ATOM 1489 O O . ILE A 1 188 ? -3.396 28.396 33.639 1.00 134.81 ? 187 ILE A O 1 ATOM 1490 C CB . ILE A 1 188 ? -1.462 26.161 33.248 1.00 145.35 ? 187 ILE A CB 1 ATOM 1491 C CG1 . ILE A 1 188 ? -0.114 25.474 33.519 1.00 146.69 ? 187 ILE A CG1 1 ATOM 1492 C CG2 . ILE A 1 188 ? -2.229 25.430 32.148 1.00 146.15 ? 187 ILE A CG2 1 ATOM 1493 C CD1 . ILE A 1 188 ? 0.842 25.468 32.342 1.00 144.66 ? 187 ILE A CD1 1 ATOM 1494 N N . ARG A 1 189 ? -2.885 28.733 31.461 1.00 144.24 ? 188 ARG A N 1 ATOM 1495 C CA . ARG A 1 189 ? -4.178 29.312 31.093 1.00 150.14 ? 188 ARG A CA 1 ATOM 1496 C C . ARG A 1 189 ? -5.178 28.191 30.828 1.00 148.99 ? 188 ARG A C 1 ATOM 1497 O O . ARG A 1 189 ? -6.290 28.201 31.359 1.00 150.92 ? 188 ARG A O 1 ATOM 1498 C CB . ARG A 1 189 ? -4.021 30.212 29.853 1.00 153.98 ? 188 ARG A CB 1 ATOM 1499 C CG . ARG A 1 189 ? -5.264 30.403 28.992 1.00 157.16 ? 188 ARG A CG 1 ATOM 1500 C CD . ARG A 1 189 ? -6.381 31.144 29.707 1.00 161.52 ? 188 ARG A CD 1 ATOM 1501 N NE . ARG A 1 189 ? -7.535 31.312 28.825 1.00 168.32 ? 188 ARG A NE 1 ATOM 1502 C CZ . ARG A 1 189 ? -8.698 31.855 29.181 1.00 176.59 ? 188 ARG A CZ 1 ATOM 1503 N NH1 . ARG A 1 189 ? -8.891 32.295 30.423 1.00 179.49 ? 188 ARG A NH1 1 ATOM 1504 N NH2 . ARG A 1 189 ? -9.678 31.958 28.286 1.00 179.79 ? 188 ARG A NH2 1 ATOM 1505 N N . ALA A 1 190 ? -4.778 27.233 29.997 1.00 146.09 ? 189 ALA A N 1 ATOM 1506 C CA . ALA A 1 190 ? -5.645 26.114 29.656 1.00 144.65 ? 189 ALA A CA 1 ATOM 1507 C C . ALA A 1 190 ? -4.829 24.956 29.110 1.00 138.99 ? 189 ALA A C 1 ATOM 1508 O O . ALA A 1 190 ? -3.671 25.129 28.720 1.00 136.26 ? 189 ALA A O 1 ATOM 1509 C CB . ALA A 1 190 ? -6.685 26.551 28.636 1.00 147.13 ? 189 ALA A CB 1 ATOM 1510 N N . PHE A 1 191 ? -5.456 23.784 29.095 1.00 133.19 ? 190 PHE A N 1 ATOM 1511 C CA . PHE A 1 191 ? -4.860 22.561 28.582 1.00 128.76 ? 190 PHE A CA 1 ATOM 1512 C C . PHE A 1 191 ? -5.851 22.004 27.568 1.00 125.73 ? 190 PHE A C 1 ATOM 1513 O O . PHE A 1 191 ? -6.963 21.609 27.923 1.00 125.85 ? 190 PHE A O 1 ATOM 1514 C CB . PHE A 1 191 ? -4.616 21.588 29.751 1.00 129.12 ? 190 PHE A CB 1 ATOM 1515 C CG . PHE A 1 191 ? -4.200 20.191 29.345 1.00 127.81 ? 190 PHE A CG 1 ATOM 1516 C CD1 . PHE A 1 191 ? -3.543 19.938 28.141 1.00 127.61 ? 190 PHE A CD1 1 ATOM 1517 C CD2 . PHE A 1 191 ? -4.433 19.124 30.210 1.00 126.74 ? 190 PHE A CD2 1 ATOM 1518 C CE1 . PHE A 1 191 ? -3.166 18.647 27.800 1.00 129.23 ? 190 PHE A CE1 1 ATOM 1519 C CE2 . PHE A 1 191 ? -4.052 17.835 29.875 1.00 126.37 ? 190 PHE A CE2 1 ATOM 1520 C CZ . PHE A 1 191 ? -3.418 17.594 28.668 1.00 128.85 ? 190 PHE A CZ 1 ATOM 1521 N N . VAL A 1 192 ? -5.443 22.022 26.303 1.00 121.66 ? 191 VAL A N 1 ATOM 1522 C CA . VAL A 1 192 ? -6.236 21.497 25.205 1.00 119.65 ? 191 VAL A CA 1 ATOM 1523 C C . VAL A 1 192 ? -5.724 20.100 24.898 1.00 120.70 ? 191 VAL A C 1 ATOM 1524 O O . VAL A 1 192 ? -4.579 19.931 24.479 1.00 118.16 ? 191 VAL A O 1 ATOM 1525 C CB . VAL A 1 192 ? -6.076 22.371 23.952 1.00 118.20 ? 191 VAL A CB 1 ATOM 1526 C CG1 . VAL A 1 192 ? -6.927 21.830 22.810 1.00 118.89 ? 191 VAL A CG1 1 ATOM 1527 C CG2 . VAL A 1 192 ? -6.435 23.813 24.275 1.00 119.38 ? 191 VAL A CG2 1 ATOM 1528 N N . SER A 1 193 ? -6.585 19.109 25.117 1.00 123.68 ? 192 SER A N 1 ATOM 1529 C CA . SER A 1 193 ? -6.227 17.705 24.984 1.00 123.33 ? 192 SER A CA 1 ATOM 1530 C C . SER A 1 193 ? -6.815 17.136 23.695 1.00 125.23 ? 192 SER A C 1 ATOM 1531 O O . SER A 1 193 ? -8.031 17.120 23.522 1.00 128.34 ? 192 SER A O 1 ATOM 1532 C CB . SER A 1 193 ? -6.757 16.929 26.192 1.00 121.77 ? 192 SER A CB 1 ATOM 1533 O OG . SER A 1 193 ? -6.430 15.557 26.109 1.00 119.84 ? 192 SER A OG 1 ATOM 1534 N N . LEU A 1 194 ? -5.948 16.667 22.803 1.00 124.29 ? 193 LEU A N 1 ATOM 1535 C CA . LEU A 1 194 ? -6.371 16.164 21.497 1.00 127.39 ? 193 LEU A CA 1 ATOM 1536 C C . LEU A 1 194 ? -6.107 14.667 21.370 1.00 126.64 ? 193 LEU A C 1 ATOM 1537 O O . LEU A 1 194 ? -4.959 14.238 21.280 1.00 125.32 ? 193 LEU A O 1 ATOM 1538 C CB . LEU A 1 194 ? -5.625 16.910 20.390 1.00 130.92 ? 193 LEU A CB 1 ATOM 1539 C CG . LEU A 1 194 ? -5.650 18.438 20.491 1.00 136.57 ? 193 LEU A CG 1 ATOM 1540 C CD1 . LEU A 1 194 ? -4.826 19.055 19.372 1.00 139.42 ? 193 LEU A CD1 1 ATOM 1541 C CD2 . LEU A 1 194 ? -7.078 18.961 20.459 1.00 138.88 ? 193 LEU A CD2 1 ATOM 1542 N N . GLY A 1 195 ? -7.173 13.872 21.371 1.00 128.53 ? 194 GLY A N 1 ATOM 1543 C CA . GLY A 1 195 ? -7.059 12.424 21.185 1.00 127.25 ? 194 GLY A CA 1 ATOM 1544 C C . GLY A 1 195 ? -6.251 11.724 22.264 1.00 125.11 ? 194 GLY A C 1 ATOM 1545 O O . GLY A 1 195 ? -5.403 10.882 21.966 1.00 126.07 ? 194 GLY A O 1 ATOM 1546 N N . ALA A 1 196 ? -6.519 12.069 23.519 1.00 120.17 ? 195 ALA A N 1 ATOM 1547 C CA . ALA A 1 196 ? -5.753 11.538 24.643 1.00 117.55 ? 195 ALA A CA 1 ATOM 1548 C C . ALA A 1 196 ? -6.161 10.103 24.980 1.00 117.35 ? 195 ALA A C 1 ATOM 1549 O O . ALA A 1 196 ? -7.340 9.843 25.229 1.00 118.09 ? 195 ALA A O 1 ATOM 1550 C CB . ALA A 1 196 ? -5.934 12.426 25.855 1.00 118.06 ? 195 ALA A CB 1 ATOM 1551 N N . PRO A 1 197 ? -5.184 9.170 25.011 1.00 115.30 ? 196 PRO A N 1 ATOM 1552 C CA . PRO A 1 197 ? -5.449 7.762 25.296 1.00 115.25 ? 196 PRO A CA 1 ATOM 1553 C C . PRO A 1 197 ? -5.484 7.464 26.791 1.00 116.46 ? 196 PRO A C 1 ATOM 1554 O O . PRO A 1 197 ? -4.676 6.671 27.289 1.00 113.68 ? 196 PRO A O 1 ATOM 1555 C CB . PRO A 1 197 ? -4.265 7.060 24.631 1.00 114.55 ? 196 PRO A CB 1 ATOM 1556 C CG . PRO A 1 197 ? -3.144 8.020 24.816 1.00 114.06 ? 196 PRO A CG 1 ATOM 1557 C CD . PRO A 1 197 ? -3.756 9.394 24.709 1.00 114.22 ? 196 PRO A CD 1 ATOM 1558 N N . TRP A 1 198 ? -6.420 8.096 27.497 1.00 121.58 ? 197 TRP A N 1 ATOM 1559 C CA . TRP A 1 198 ? -6.530 7.918 28.945 1.00 126.75 ? 197 TRP A CA 1 ATOM 1560 C C . TRP A 1 198 ? -6.859 6.455 29.233 1.00 131.15 ? 197 TRP A C 1 ATOM 1561 O O . TRP A 1 198 ? -7.878 5.939 28.769 1.00 132.04 ? 197 TRP A O 1 ATOM 1562 C CB . TRP A 1 198 ? -7.618 8.816 29.549 1.00 125.75 ? 197 TRP A CB 1 ATOM 1563 C CG . TRP A 1 198 ? -7.535 10.270 29.179 1.00 124.90 ? 197 TRP A CG 1 ATOM 1564 C CD1 . TRP A 1 198 ? -8.471 10.988 28.497 1.00 128.45 ? 197 TRP A CD1 1 ATOM 1565 C CD2 . TRP A 1 198 ? -6.469 11.184 29.480 1.00 123.53 ? 197 TRP A CD2 1 ATOM 1566 N NE1 . TRP A 1 198 ? -8.059 12.291 28.353 1.00 130.57 ? 197 TRP A NE1 1 ATOM 1567 C CE2 . TRP A 1 198 ? -6.834 12.439 28.949 1.00 126.26 ? 197 TRP A CE2 1 ATOM 1568 C CE3 . TRP A 1 198 ? -5.244 11.066 30.146 1.00 121.02 ? 197 TRP A CE3 1 ATOM 1569 C CZ2 . TRP A 1 198 ? -6.013 13.567 29.055 1.00 122.92 ? 197 TRP A CZ2 1 ATOM 1570 C CZ3 . TRP A 1 198 ? -4.430 12.190 30.254 1.00 118.77 ? 197 TRP A CZ3 1 ATOM 1571 C CH2 . TRP A 1 198 ? -4.820 13.422 29.711 1.00 120.35 ? 197 TRP A CH2 1 ATOM 1572 N N . GLY A 1 199 ? -5.982 5.790 29.981 1.00 133.51 ? 198 GLY A N 1 ATOM 1573 C CA . GLY A 1 199 ? -6.168 4.384 30.315 1.00 135.10 ? 198 GLY A CA 1 ATOM 1574 C C . GLY A 1 199 ? -5.826 3.429 29.186 1.00 134.44 ? 198 GLY A C 1 ATOM 1575 O O . GLY A 1 199 ? -6.357 2.321 29.129 1.00 136.19 ? 198 GLY A O 1 ATOM 1576 N N . GLY A 1 200 ? -4.944 3.855 28.284 1.00 133.16 ? 199 GLY A N 1 ATOM 1577 C CA . GLY A 1 200 ? -4.374 2.963 27.279 1.00 132.61 ? 199 GLY A CA 1 ATOM 1578 C C . GLY A 1 200 ? -5.289 2.654 26.113 1.00 131.48 ? 199 GLY A C 1 ATOM 1579 O O . GLY A 1 200 ? -6.428 3.113 26.063 1.00 129.31 ? 199 GLY A O 1 ATOM 1580 N N . VAL A 1 201 ? -4.775 1.872 25.169 1.00 131.34 ? 200 VAL A N 1 ATOM 1581 C CA . VAL A 1 201 ? -5.503 1.552 23.946 1.00 133.76 ? 200 VAL A CA 1 ATOM 1582 C C . VAL A 1 201 ? -5.321 0.092 23.545 1.00 135.61 ? 200 VAL A C 1 ATOM 1583 O O . VAL A 1 201 ? -4.279 -0.518 23.792 1.00 133.90 ? 200 VAL A O 1 ATOM 1584 C CB . VAL A 1 201 ? -5.080 2.459 22.772 1.00 133.10 ? 200 VAL A CB 1 ATOM 1585 C CG1 . VAL A 1 201 ? -5.529 3.890 23.023 1.00 134.07 ? 200 VAL A CG1 1 ATOM 1586 C CG2 . VAL A 1 201 ? -3.575 2.396 22.536 1.00 131.51 ? 200 VAL A CG2 1 ATOM 1587 N N . ALA A 1 202 ? -6.344 -0.453 22.901 1.00 136.41 ? 201 ALA A N 1 ATOM 1588 C CA . ALA A 1 202 ? -6.361 -1.863 22.545 1.00 135.03 ? 201 ALA A CA 1 ATOM 1589 C C . ALA A 1 202 ? -5.257 -2.239 21.569 1.00 132.23 ? 201 ALA A C 1 ATOM 1590 O O . ALA A 1 202 ? -4.723 -3.338 21.647 1.00 127.70 ? 201 ALA A O 1 ATOM 1591 C CB . ALA A 1 202 ? -7.716 -2.242 21.971 1.00 137.54 ? 201 ALA A CB 1 ATOM 1592 N N . LYS A 1 203 ? -4.906 -1.335 20.656 1.00 133.40 ? 202 LYS A N 1 ATOM 1593 C CA . LYS A 1 203 ? -3.944 -1.660 19.593 1.00 133.67 ? 202 LYS A CA 1 ATOM 1594 C C . LYS A 1 203 ? -2.570 -2.127 20.098 1.00 128.24 ? 202 LYS A C 1 ATOM 1595 O O . LYS A 1 203 ? -1.849 -2.840 19.393 1.00 126.07 ? 202 LYS A O 1 ATOM 1596 C CB . LYS A 1 203 ? -3.773 -0.480 18.617 1.00 138.81 ? 202 LYS A CB 1 ATOM 1597 C CG . LYS A 1 203 ? -3.067 0.752 19.184 1.00 144.57 ? 202 LYS A CG 1 ATOM 1598 C CD . LYS A 1 203 ? -2.125 1.399 18.168 1.00 151.27 ? 202 LYS A CD 1 ATOM 1599 C CE . LYS A 1 203 ? -1.192 2.418 18.819 1.00 156.99 ? 202 LYS A CE 1 ATOM 1600 N NZ . LYS A 1 203 ? -0.162 2.959 17.884 1.00 157.84 ? 202 LYS A NZ 1 ATOM 1601 N N . THR A 1 204 ? -2.221 -1.707 21.313 1.00 122.92 ? 203 THR A N 1 ATOM 1602 C CA . THR A 1 204 ? -0.981 -2.098 21.981 1.00 119.77 ? 203 THR A CA 1 ATOM 1603 C C . THR A 1 204 ? -0.749 -3.610 21.981 1.00 118.01 ? 203 THR A C 1 ATOM 1604 O O . THR A 1 204 ? 0.367 -4.086 21.765 1.00 114.32 ? 203 THR A O 1 ATOM 1605 C CB . THR A 1 204 ? -1.022 -1.640 23.451 1.00 122.36 ? 203 THR A CB 1 ATOM 1606 O OG1 . THR A 1 204 ? -1.528 -0.301 23.531 1.00 122.35 ? 203 THR A OG1 1 ATOM 1607 C CG2 . THR A 1 204 ? 0.354 -1.699 24.079 1.00 124.78 ? 203 THR A CG2 1 ATOM 1608 N N . LEU A 1 205 ? -1.814 -4.359 22.224 1.00 117.37 ? 204 LEU A N 1 ATOM 1609 C CA . LEU A 1 205 ? -1.712 -5.805 22.326 1.00 119.98 ? 204 LEU A CA 1 ATOM 1610 C C . LEU A 1 205 ? -1.261 -6.421 21.005 1.00 118.47 ? 204 LEU A C 1 ATOM 1611 O O . LEU A 1 205 ? -0.406 -7.305 20.989 1.00 116.65 ? 204 LEU A O 1 ATOM 1612 C CB . LEU A 1 205 ? -3.050 -6.415 22.763 1.00 124.95 ? 204 LEU A CB 1 ATOM 1613 C CG . LEU A 1 205 ? -3.450 -6.282 24.239 1.00 128.03 ? 204 LEU A CG 1 ATOM 1614 C CD1 . LEU A 1 205 ? -2.429 -6.953 25.145 1.00 129.75 ? 204 LEU A CD1 1 ATOM 1615 C CD2 . LEU A 1 205 ? -3.675 -4.836 24.661 1.00 127.52 ? 204 LEU A CD2 1 ATOM 1616 N N . ARG A 1 206 ? -1.844 -5.959 19.903 1.00 118.50 ? 205 ARG A N 1 ATOM 1617 C CA . ARG A 1 206 ? -1.507 -6.488 18.585 1.00 121.33 ? 205 ARG A CA 1 ATOM 1618 C C . ARG A 1 206 ? -0.064 -6.160 18.235 1.00 122.22 ? 205 ARG A C 1 ATOM 1619 O O . ARG A 1 206 ? 0.668 -7.003 17.718 1.00 120.51 ? 205 ARG A O 1 ATOM 1620 C CB . ARG A 1 206 ? -2.428 -5.899 17.514 1.00 123.04 ? 205 ARG A CB 1 ATOM 1621 C CG . ARG A 1 206 ? -2.295 -6.571 16.152 1.00 125.69 ? 205 ARG A CG 1 ATOM 1622 C CD . ARG A 1 206 ? -2.325 -5.576 15.003 1.00 125.18 ? 205 ARG A CD 1 ATOM 1623 N NE . ARG A 1 206 ? -1.685 -6.132 13.815 1.00 126.25 ? 205 ARG A NE 1 ATOM 1624 C CZ . ARG A 1 206 ? -1.382 -5.439 12.720 1.00 128.04 ? 205 ARG A CZ 1 ATOM 1625 N NH1 . ARG A 1 206 ? -1.666 -4.142 12.634 1.00 125.09 ? 205 ARG A NH1 1 ATOM 1626 N NH2 . ARG A 1 206 ? -0.791 -6.052 11.699 1.00 131.11 ? 205 ARG A NH2 1 ATOM 1627 N N . VAL A 1 207 ? 0.328 -4.921 18.511 1.00 125.22 ? 206 VAL A N 1 ATOM 1628 C CA . VAL A 1 207 ? 1.684 -4.458 18.235 1.00 126.50 ? 206 VAL A CA 1 ATOM 1629 C C . VAL A 1 207 ? 2.697 -5.374 18.916 1.00 126.04 ? 206 VAL A C 1 ATOM 1630 O O . VAL A 1 207 ? 3.622 -5.871 18.271 1.00 124.54 ? 206 VAL A O 1 ATOM 1631 C CB . VAL A 1 207 ? 1.884 -2.999 18.715 1.00 127.68 ? 206 VAL A CB 1 ATOM 1632 C CG1 . VAL A 1 207 ? 3.353 -2.592 18.647 1.00 127.34 ? 206 VAL A CG1 1 ATOM 1633 C CG2 . VAL A 1 207 ? 1.024 -2.041 17.894 1.00 129.21 ? 206 VAL A CG2 1 ATOM 1634 N N . LEU A 1 208 ? 2.501 -5.604 20.211 1.00 124.84 ? 207 LEU A N 1 ATOM 1635 C CA . LEU A 1 208 ? 3.419 -6.419 21.001 1.00 128.70 ? 207 LEU A CA 1 ATOM 1636 C C . LEU A 1 208 ? 3.414 -7.883 20.573 1.00 127.83 ? 207 LEU A C 1 ATOM 1637 O O . LEU A 1 208 ? 4.463 -8.524 20.521 1.00 128.07 ? 207 LEU A O 1 ATOM 1638 C CB . LEU A 1 208 ? 3.067 -6.318 22.485 1.00 133.79 ? 207 LEU A CB 1 ATOM 1639 C CG . LEU A 1 208 ? 3.265 -4.932 23.108 1.00 138.35 ? 207 LEU A CG 1 ATOM 1640 C CD1 . LEU A 1 208 ? 2.420 -4.776 24.363 1.00 139.88 ? 207 LEU A CD1 1 ATOM 1641 C CD2 . LEU A 1 208 ? 4.735 -4.666 23.409 1.00 141.03 ? 207 LEU A CD2 1 ATOM 1642 N N . ALA A 1 209 ? 2.233 -8.407 20.269 1.00 125.41 ? 208 ALA A N 1 ATOM 1643 C CA . ALA A 1 209 ? 2.099 -9.809 19.908 1.00 127.31 ? 208 ALA A CA 1 ATOM 1644 C C . ALA A 1 209 ? 2.709 -10.104 18.539 1.00 128.08 ? 208 ALA A C 1 ATOM 1645 O O . ALA A 1 209 ? 3.614 -10.932 18.427 1.00 128.33 ? 208 ALA A O 1 ATOM 1646 C CB . ALA A 1 209 ? 0.637 -10.222 19.941 1.00 129.06 ? 208 ALA A CB 1 ATOM 1647 N N . SER A 1 210 ? 2.222 -9.416 17.508 1.00 126.83 ? 209 SER A N 1 ATOM 1648 C CA . SER A 1 210 ? 2.551 -9.765 16.121 1.00 130.41 ? 209 SER A CA 1 ATOM 1649 C C . SER A 1 210 ? 3.120 -8.633 15.261 1.00 127.90 ? 209 SER A C 1 ATOM 1650 O O . SER A 1 210 ? 3.321 -8.822 14.058 1.00 129.41 ? 209 SER A O 1 ATOM 1651 C CB . SER A 1 210 ? 1.307 -10.320 15.424 1.00 135.19 ? 209 SER A CB 1 ATOM 1652 O OG . SER A 1 210 ? 0.429 -9.276 15.032 1.00 138.06 ? 209 SER A OG 1 ATOM 1653 N N . GLY A 1 211 ? 3.369 -7.470 15.858 1.00 123.93 ? 210 GLY A N 1 ATOM 1654 C CA . GLY A 1 211 ? 3.870 -6.317 15.116 1.00 123.04 ? 210 GLY A CA 1 ATOM 1655 C C . GLY A 1 211 ? 2.769 -5.574 14.381 1.00 126.21 ? 210 GLY A C 1 ATOM 1656 O O . GLY A 1 211 ? 1.689 -6.116 14.143 1.00 128.91 ? 210 GLY A O 1 ATOM 1657 N N . ASP A 1 212 ? 3.050 -4.329 14.015 1.00 126.09 ? 211 ASP A N 1 ATOM 1658 C CA . ASP A 1 212 ? 2.059 -3.460 13.385 1.00 127.75 ? 211 ASP A CA 1 ATOM 1659 C C . ASP A 1 212 ? 2.766 -2.601 12.342 1.00 126.27 ? 211 ASP A C 1 ATOM 1660 O O . ASP A 1 212 ? 3.500 -1.677 12.690 1.00 127.08 ? 211 ASP A O 1 ATOM 1661 C CB . ASP A 1 212 ? 1.396 -2.585 14.461 1.00 132.40 ? 211 ASP A CB 1 ATOM 1662 C CG . ASP A 1 212 ? 0.144 -1.873 13.965 1.00 137.91 ? 211 ASP A CG 1 ATOM 1663 O OD1 . ASP A 1 212 ? 0.212 -1.173 12.931 1.00 142.28 ? 211 ASP A OD1 1 ATOM 1664 O OD2 . ASP A 1 212 ? -0.907 -1.994 14.633 1.00 140.15 ? 211 ASP A OD2 1 ATOM 1665 N N . ASN A 1 213 ? 2.550 -2.910 11.068 1.00 129.02 ? 212 ASN A N 1 ATOM 1666 C CA . ASN A 1 213 ? 3.244 -2.213 9.987 1.00 135.91 ? 212 ASN A CA 1 ATOM 1667 C C . ASN A 1 213 ? 2.317 -1.360 9.119 1.00 143.59 ? 212 ASN A C 1 ATOM 1668 O O . ASN A 1 213 ? 2.666 -1.018 7.983 1.00 140.13 ? 212 ASN A O 1 ATOM 1669 C CB . ASN A 1 213 ? 4.020 -3.215 9.125 1.00 136.08 ? 212 ASN A CB 1 ATOM 1670 C CG . ASN A 1 213 ? 3.113 -4.148 8.346 1.00 136.64 ? 212 ASN A CG 1 ATOM 1671 O OD1 . ASN A 1 213 ? 1.951 -4.346 8.700 1.00 137.58 ? 212 ASN A OD1 1 ATOM 1672 N ND2 . ASN A 1 213 ? 3.644 -4.731 7.278 1.00 137.51 ? 212 ASN A ND2 1 ATOM 1673 N N . ASN A 1 214 ? 1.165 -0.978 9.674 1.00 153.82 ? 213 ASN A N 1 ATOM 1674 C CA . ASN A 1 214 ? 0.149 -0.187 8.952 1.00 160.95 ? 213 ASN A CA 1 ATOM 1675 C C . ASN A 1 214 ? 0.724 1.012 8.206 1.00 162.28 ? 213 ASN A C 1 ATOM 1676 O O . ASN A 1 214 ? 0.262 1.370 7.122 1.00 165.45 ? 213 ASN A O 1 ATOM 1677 C CB . ASN A 1 214 ? -0.911 0.338 9.929 1.00 164.88 ? 213 ASN A CB 1 ATOM 1678 C CG . ASN A 1 214 ? -1.900 -0.728 10.360 1.00 168.68 ? 213 ASN A CG 1 ATOM 1679 O OD1 . ASN A 1 214 ? -1.893 -1.848 9.850 1.00 166.77 ? 213 ASN A OD1 1 ATOM 1680 N ND2 . ASN A 1 214 ? -2.765 -0.377 11.306 1.00 172.88 ? 213 ASN A ND2 1 ATOM 1681 N N . ARG A 1 215 ? 1.725 1.639 8.805 1.00 161.51 ? 214 ARG A N 1 ATOM 1682 C CA . ARG A 1 215 ? 2.323 2.837 8.224 1.00 158.94 ? 214 ARG A CA 1 ATOM 1683 C C . ARG A 1 215 ? 3.470 2.446 7.297 1.00 151.93 ? 214 ARG A C 1 ATOM 1684 O O . ARG A 1 215 ? 3.787 3.162 6.352 1.00 150.13 ? 214 ARG A O 1 ATOM 1685 C CB . ARG A 1 215 ? 2.826 3.776 9.327 1.00 161.76 ? 214 ARG A CB 1 ATOM 1686 C CG . ARG A 1 215 ? 1.817 3.995 10.452 1.00 167.04 ? 214 ARG A CG 1 ATOM 1687 C CD . ARG A 1 215 ? 0.978 5.244 10.239 1.00 172.56 ? 214 ARG A CD 1 ATOM 1688 N NE . ARG A 1 215 ? -0.263 5.179 11.012 1.00 179.77 ? 214 ARG A NE 1 ATOM 1689 C CZ . ARG A 1 215 ? -1.140 6.176 11.130 1.00 179.50 ? 214 ARG A CZ 1 ATOM 1690 N NH1 . ARG A 1 215 ? -0.923 7.354 10.548 1.00 176.43 ? 214 ARG A NH1 1 ATOM 1691 N NH2 . ARG A 1 215 ? -2.242 5.993 11.852 1.00 181.84 ? 214 ARG A NH2 1 ATOM 1692 N N . ILE A 1 216 ? 4.077 1.294 7.561 1.00 146.21 ? 215 ILE A N 1 ATOM 1693 C CA . ILE A 1 216 ? 5.313 0.909 6.906 1.00 147.64 ? 215 ILE A CA 1 ATOM 1694 C C . ILE A 1 216 ? 5.080 -0.437 6.232 1.00 147.72 ? 215 ILE A C 1 ATOM 1695 O O . ILE A 1 216 ? 5.718 -1.434 6.587 1.00 155.31 ? 215 ILE A O 1 ATOM 1696 C CB . ILE A 1 216 ? 6.479 0.820 7.921 1.00 150.82 ? 215 ILE A CB 1 ATOM 1697 C CG1 . ILE A 1 216 ? 6.243 1.760 9.112 1.00 155.68 ? 215 ILE A CG1 1 ATOM 1698 C CG2 . ILE A 1 216 ? 7.796 1.155 7.233 1.00 153.01 ? 215 ILE A CG2 1 ATOM 1699 C CD1 . ILE A 1 216 ? 7.276 1.633 10.210 1.00 157.49 ? 215 ILE A CD1 1 ATOM 1700 N N . PRO A 1 217 ? 4.160 -0.469 5.249 1.00 143.35 ? 216 PRO A N 1 ATOM 1701 C CA . PRO A 1 217 ? 3.747 -1.731 4.621 1.00 143.56 ? 216 PRO A CA 1 ATOM 1702 C C . PRO A 1 217 ? 4.849 -2.452 3.835 1.00 143.46 ? 216 PRO A C 1 ATOM 1703 O O . PRO A 1 217 ? 4.740 -3.653 3.587 1.00 142.48 ? 216 PRO A O 1 ATOM 1704 C CB . PRO A 1 217 ? 2.641 -1.289 3.668 1.00 145.89 ? 216 PRO A CB 1 ATOM 1705 C CG . PRO A 1 217 ? 3.055 0.080 3.264 1.00 146.12 ? 216 PRO A CG 1 ATOM 1706 C CD . PRO A 1 217 ? 3.622 0.690 4.512 1.00 144.46 ? 216 PRO A CD 1 ATOM 1707 N N . VAL A 1 218 ? 5.890 -1.722 3.444 1.00 144.23 ? 217 VAL A N 1 ATOM 1708 C CA . VAL A 1 218 ? 7.039 -2.313 2.767 1.00 148.26 ? 217 VAL A CA 1 ATOM 1709 C C . VAL A 1 218 ? 7.844 -3.246 3.681 1.00 147.81 ? 217 VAL A C 1 ATOM 1710 O O . VAL A 1 218 ? 8.598 -4.096 3.195 1.00 144.78 ? 217 VAL A O 1 ATOM 1711 C CB . VAL A 1 218 ? 7.971 -1.217 2.193 1.00 153.31 ? 217 VAL A CB 1 ATOM 1712 C CG1 . VAL A 1 218 ? 8.726 -0.485 3.303 1.00 153.86 ? 217 VAL A CG1 1 ATOM 1713 C CG2 . VAL A 1 218 ? 8.936 -1.805 1.171 1.00 155.92 ? 217 VAL A CG2 1 ATOM 1714 N N . ILE A 1 219 ? 7.692 -3.088 4.995 1.00 150.21 ? 218 ILE A N 1 ATOM 1715 C CA . ILE A 1 219 ? 8.389 -3.969 5.932 1.00 154.82 ? 218 ILE A CA 1 ATOM 1716 C C . ILE A 1 219 ? 7.475 -4.962 6.657 1.00 153.18 ? 218 ILE A C 1 ATOM 1717 O O . ILE A 1 219 ? 6.361 -4.628 7.069 1.00 149.84 ? 218 ILE A O 1 ATOM 1718 C CB . ILE A 1 219 ? 9.279 -3.199 6.930 1.00 157.37 ? 218 ILE A CB 1 ATOM 1719 C CG1 . ILE A 1 219 ? 9.993 -4.188 7.855 1.00 164.61 ? 218 ILE A CG1 1 ATOM 1720 C CG2 . ILE A 1 219 ? 8.473 -2.193 7.738 1.00 156.43 ? 218 ILE A CG2 1 ATOM 1721 C CD1 . ILE A 1 219 ? 11.230 -3.635 8.503 1.00 167.11 ? 218 ILE A CD1 1 ATOM 1722 N N . GLY A 1 220 ? 7.976 -6.187 6.808 1.00 151.26 ? 219 GLY A N 1 ATOM 1723 C CA . GLY A 1 220 ? 7.265 -7.249 7.511 1.00 152.20 ? 219 GLY A CA 1 ATOM 1724 C C . GLY A 1 220 ? 6.967 -6.937 8.974 1.00 149.47 ? 219 GLY A C 1 ATOM 1725 O O . GLY A 1 220 ? 7.806 -6.360 9.675 1.00 148.62 ? 219 GLY A O 1 ATOM 1726 N N . PRO A 1 221 ? 5.769 -7.325 9.449 1.00 144.28 ? 220 PRO A N 1 ATOM 1727 C CA . PRO A 1 221 ? 5.368 -6.946 10.800 1.00 139.99 ? 220 PRO A CA 1 ATOM 1728 C C . PRO A 1 221 ? 6.244 -7.562 11.878 1.00 138.87 ? 220 PRO A C 1 ATOM 1729 O O . PRO A 1 221 ? 6.511 -6.922 12.889 1.00 136.59 ? 220 PRO A O 1 ATOM 1730 C CB . PRO A 1 221 ? 3.933 -7.484 10.924 1.00 140.22 ? 220 PRO A CB 1 ATOM 1731 C CG . PRO A 1 221 ? 3.534 -7.935 9.564 1.00 143.32 ? 220 PRO A CG 1 ATOM 1732 C CD . PRO A 1 221 ? 4.799 -8.245 8.833 1.00 145.44 ? 220 PRO A CD 1 ATOM 1733 N N . LEU A 1 222 ? 6.692 -8.793 11.660 1.00 138.31 ? 221 LEU A N 1 ATOM 1734 C CA . LEU A 1 222 ? 7.483 -9.499 12.664 1.00 139.73 ? 221 LEU A CA 1 ATOM 1735 C C . LEU A 1 222 ? 8.878 -8.890 12.822 1.00 138.42 ? 221 LEU A C 1 ATOM 1736 O O . LEU A 1 222 ? 9.486 -8.992 13.891 1.00 138.36 ? 221 LEU A O 1 ATOM 1737 C CB . LEU A 1 222 ? 7.578 -10.988 12.322 1.00 142.86 ? 221 LEU A CB 1 ATOM 1738 C CG . LEU A 1 222 ? 6.246 -11.745 12.212 1.00 142.40 ? 221 LEU A CG 1 ATOM 1739 C CD1 . LEU A 1 222 ? 6.480 -13.189 11.794 1.00 143.76 ? 221 LEU A CD1 1 ATOM 1740 C CD2 . LEU A 1 222 ? 5.461 -11.687 13.514 1.00 138.98 ? 221 LEU A CD2 1 ATOM 1741 N N . LYS A 1 223 ? 9.372 -8.250 11.763 1.00 137.22 ? 222 LYS A N 1 ATOM 1742 C CA . LYS A 1 223 ? 10.669 -7.581 11.811 1.00 135.25 ? 222 LYS A CA 1 ATOM 1743 C C . LYS A 1 223 ? 10.572 -6.298 12.626 1.00 129.01 ? 222 LYS A C 1 ATOM 1744 O O . LYS A 1 223 ? 11.346 -6.088 13.556 1.00 126.02 ? 222 LYS A O 1 ATOM 1745 C CB . LYS A 1 223 ? 11.182 -7.272 10.400 1.00 137.97 ? 222 LYS A CB 1 ATOM 1746 C CG . LYS A 1 223 ? 12.698 -7.282 10.291 1.00 143.02 ? 222 LYS A CG 1 ATOM 1747 C CD . LYS A 1 223 ? 13.229 -8.710 10.257 1.00 153.53 ? 222 LYS A CD 1 ATOM 1748 C CE . LYS A 1 223 ? 14.727 -8.775 10.505 1.00 158.66 ? 222 LYS A CE 1 ATOM 1749 N NZ . LYS A 1 223 ? 15.204 -10.182 10.648 1.00 161.35 ? 222 LYS A NZ 1 ATOM 1750 N N . ILE A 1 224 ? 9.608 -5.449 12.279 1.00 126.02 ? 223 ILE A N 1 ATOM 1751 C CA . ILE A 1 224 ? 9.405 -4.178 12.985 1.00 125.42 ? 223 ILE A CA 1 ATOM 1752 C C . ILE A 1 224 ? 9.004 -4.368 14.453 1.00 125.38 ? 223 ILE A C 1 ATOM 1753 O O . ILE A 1 224 ? 9.298 -3.519 15.302 1.00 123.76 ? 223 ILE A O 1 ATOM 1754 C CB . ILE A 1 224 ? 8.364 -3.284 12.255 1.00 126.55 ? 223 ILE A CB 1 ATOM 1755 C CG1 . ILE A 1 224 ? 8.387 -1.844 12.778 1.00 127.26 ? 223 ILE A CG1 1 ATOM 1756 C CG2 . ILE A 1 224 ? 6.952 -3.847 12.367 1.00 126.48 ? 223 ILE A CG2 1 ATOM 1757 C CD1 . ILE A 1 224 ? 9.693 -1.118 12.542 1.00 128.15 ? 223 ILE A CD1 1 ATOM 1758 N N . ARG A 1 225 ? 8.332 -5.481 14.741 1.00 126.97 ? 224 ARG A N 1 ATOM 1759 C CA . ARG A 1 225 ? 7.907 -5.814 16.100 1.00 128.38 ? 224 ARG A CA 1 ATOM 1760 C C . ARG A 1 225 ? 9.064 -5.728 17.091 1.00 127.88 ? 224 ARG A C 1 ATOM 1761 O O . ARG A 1 225 ? 8.883 -5.305 18.236 1.00 125.03 ? 224 ARG A O 1 ATOM 1762 C CB . ARG A 1 225 ? 7.310 -7.220 16.125 1.00 131.50 ? 224 ARG A CB 1 ATOM 1763 C CG . ARG A 1 225 ? 6.757 -7.642 17.475 1.00 133.89 ? 224 ARG A CG 1 ATOM 1764 C CD . ARG A 1 225 ? 6.189 -9.047 17.415 1.00 136.19 ? 224 ARG A CD 1 ATOM 1765 N NE . ARG A 1 225 ? 7.216 -10.042 17.118 1.00 137.46 ? 224 ARG A NE 1 ATOM 1766 C CZ . ARG A 1 225 ? 6.999 -11.354 17.053 1.00 142.09 ? 224 ARG A CZ 1 ATOM 1767 N NH1 . ARG A 1 225 ? 5.787 -11.858 17.269 1.00 141.99 ? 224 ARG A NH1 1 ATOM 1768 N NH2 . ARG A 1 225 ? 8.005 -12.174 16.774 1.00 148.08 ? 224 ARG A NH2 1 ATOM 1769 N N . GLU A 1 226 ? 10.247 -6.133 16.639 1.00 130.79 ? 225 GLU A N 1 ATOM 1770 C CA . GLU A 1 226 ? 11.452 -6.120 17.468 1.00 134.52 ? 225 GLU A CA 1 ATOM 1771 C C . GLU A 1 226 ? 11.716 -4.732 18.055 1.00 129.46 ? 225 GLU A C 1 ATOM 1772 O O . GLU A 1 226 ? 11.951 -4.581 19.260 1.00 132.30 ? 225 GLU A O 1 ATOM 1773 C CB . GLU A 1 226 ? 12.654 -6.589 16.642 1.00 140.28 ? 225 GLU A CB 1 ATOM 1774 C CG . GLU A 1 226 ? 12.588 -8.060 16.239 1.00 145.43 ? 225 GLU A CG 1 ATOM 1775 C CD . GLU A 1 226 ? 13.287 -8.357 14.924 1.00 150.99 ? 225 GLU A CD 1 ATOM 1776 O OE1 . GLU A 1 226 ? 14.306 -7.700 14.619 1.00 153.68 ? 225 GLU A OE1 1 ATOM 1777 O OE2 . GLU A 1 226 ? 12.818 -9.257 14.195 1.00 154.24 ? 225 GLU A OE2 1 ATOM 1778 N N . GLN A 1 227 ? 11.661 -3.717 17.202 1.00 122.90 ? 226 GLN A N 1 ATOM 1779 C CA . GLN A 1 227 ? 11.856 -2.335 17.641 1.00 120.89 ? 226 GLN A CA 1 ATOM 1780 C C . GLN A 1 227 ? 10.717 -1.867 18.544 1.00 115.96 ? 226 GLN A C 1 ATOM 1781 O O . GLN A 1 227 ? 10.946 -1.236 19.581 1.00 114.35 ? 226 GLN A O 1 ATOM 1782 C CB . GLN A 1 227 ? 11.954 -1.408 16.421 1.00 120.21 ? 226 GLN A CB 1 ATOM 1783 C CG . GLN A 1 227 ? 11.993 0.082 16.748 1.00 119.87 ? 226 GLN A CG 1 ATOM 1784 C CD . GLN A 1 227 ? 10.628 0.665 17.079 1.00 118.23 ? 226 GLN A CD 1 ATOM 1785 O OE1 . GLN A 1 227 ? 10.431 1.234 18.155 1.00 117.18 ? 226 GLN A OE1 1 ATOM 1786 N NE2 . GLN A 1 227 ? 9.674 0.512 16.164 1.00 115.57 ? 226 GLN A NE2 1 ATOM 1787 N N . GLN A 1 228 ? 9.492 -2.170 18.132 1.00 113.16 ? 227 GLN A N 1 ATOM 1788 C CA . GLN A 1 228 ? 8.304 -1.703 18.837 1.00 111.70 ? 227 GLN A CA 1 ATOM 1789 C C . GLN A 1 228 ? 8.276 -2.208 20.278 1.00 115.82 ? 227 GLN A C 1 ATOM 1790 O O . GLN A 1 228 ? 7.929 -1.464 21.195 1.00 119.77 ? 227 GLN A O 1 ATOM 1791 C CB . GLN A 1 228 ? 7.041 -2.143 18.094 1.00 110.52 ? 227 GLN A CB 1 ATOM 1792 C CG . GLN A 1 228 ? 6.871 -1.486 16.730 1.00 110.68 ? 227 GLN A CG 1 ATOM 1793 C CD . GLN A 1 228 ? 5.822 -2.164 15.861 1.00 112.61 ? 227 GLN A CD 1 ATOM 1794 O OE1 . GLN A 1 228 ? 5.610 -3.374 15.941 1.00 116.65 ? 227 GLN A OE1 1 ATOM 1795 N NE2 . GLN A 1 228 ? 5.170 -1.382 15.012 1.00 113.10 ? 227 GLN A NE2 1 ATOM 1796 N N . ARG A 1 229 ? 8.651 -3.468 20.474 1.00 117.70 ? 228 ARG A N 1 ATOM 1797 C CA . ARG A 1 229 ? 8.728 -4.043 21.817 1.00 121.96 ? 228 ARG A CA 1 ATOM 1798 C C . ARG A 1 229 ? 9.722 -3.307 22.717 1.00 123.65 ? 228 ARG A C 1 ATOM 1799 O O . ARG A 1 229 ? 9.483 -3.148 23.922 1.00 121.20 ? 228 ARG A O 1 ATOM 1800 C CB . ARG A 1 229 ? 9.105 -5.526 21.741 1.00 125.05 ? 228 ARG A CB 1 ATOM 1801 C CG . ARG A 1 229 ? 7.981 -6.417 21.246 1.00 128.41 ? 228 ARG A CG 1 ATOM 1802 C CD . ARG A 1 229 ? 8.402 -7.875 21.203 1.00 131.71 ? 228 ARG A CD 1 ATOM 1803 N NE . ARG A 1 229 ? 7.291 -8.751 20.835 1.00 134.00 ? 228 ARG A NE 1 ATOM 1804 C CZ . ARG A 1 229 ? 7.358 -10.080 20.787 1.00 138.24 ? 228 ARG A CZ 1 ATOM 1805 N NH1 . ARG A 1 229 ? 8.491 -10.711 21.083 1.00 141.53 ? 228 ARG A NH1 1 ATOM 1806 N NH2 . ARG A 1 229 ? 6.285 -10.787 20.444 1.00 139.86 ? 228 ARG A NH2 1 ATOM 1807 N N . SER A 1 230 ? 10.829 -2.863 22.121 1.00 124.43 ? 229 SER A N 1 ATOM 1808 C CA . SER A 1 230 ? 11.926 -2.227 22.856 1.00 126.85 ? 229 SER A CA 1 ATOM 1809 C C . SER A 1 230 ? 11.559 -0.880 23.479 1.00 126.40 ? 229 SER A C 1 ATOM 1810 O O . SER A 1 230 ? 12.155 -0.479 24.486 1.00 126.85 ? 229 SER A O 1 ATOM 1811 C CB . SER A 1 230 ? 13.145 -2.037 21.946 1.00 125.78 ? 229 SER A CB 1 ATOM 1812 O OG . SER A 1 230 ? 13.001 -0.884 21.131 1.00 124.03 ? 229 SER A OG 1 ATOM 1813 N N . ALA A 1 231 ? 10.597 -0.185 22.873 1.00 124.17 ? 230 ALA A N 1 ATOM 1814 C CA . ALA A 1 231 ? 10.142 1.115 23.375 1.00 123.50 ? 230 ALA A CA 1 ATOM 1815 C C . ALA A 1 231 ? 9.241 0.965 24.605 1.00 122.13 ? 230 ALA A C 1 ATOM 1816 O O . ALA A 1 231 ? 8.164 0.370 24.530 1.00 122.15 ? 230 ALA A O 1 ATOM 1817 C CB . ALA A 1 231 ? 9.414 1.876 22.279 1.00 123.79 ? 230 ALA A CB 1 ATOM 1818 N N . VAL A 1 232 ? 9.689 1.519 25.728 1.00 121.83 ? 231 VAL A N 1 ATOM 1819 C CA . VAL A 1 232 ? 8.943 1.455 26.992 1.00 122.38 ? 231 VAL A CA 1 ATOM 1820 C C . VAL A 1 232 ? 7.546 2.051 26.838 1.00 119.12 ? 231 VAL A C 1 ATOM 1821 O O . VAL A 1 232 ? 6.582 1.558 27.425 1.00 118.32 ? 231 VAL A O 1 ATOM 1822 C CB . VAL A 1 232 ? 9.681 2.210 28.124 1.00 124.43 ? 231 VAL A CB 1 ATOM 1823 C CG1 . VAL A 1 232 ? 8.839 2.252 29.397 1.00 124.03 ? 231 VAL A CG1 1 ATOM 1824 C CG2 . VAL A 1 232 ? 11.034 1.566 28.403 1.00 127.95 ? 231 VAL A CG2 1 ATOM 1825 N N . SER A 1 233 ? 7.450 3.110 26.043 1.00 117.41 ? 232 SER A N 1 ATOM 1826 C CA . SER A 1 233 ? 6.181 3.778 25.777 1.00 119.04 ? 232 SER A CA 1 ATOM 1827 C C . SER A 1 233 ? 5.096 2.831 25.264 1.00 120.88 ? 232 SER A C 1 ATOM 1828 O O . SER A 1 233 ? 3.914 3.039 25.525 1.00 122.81 ? 232 SER A O 1 ATOM 1829 C CB . SER A 1 233 ? 6.390 4.904 24.764 1.00 117.69 ? 232 SER A CB 1 ATOM 1830 O OG . SER A 1 233 ? 7.034 4.426 23.593 1.00 115.57 ? 232 SER A OG 1 ATOM 1831 N N . THR A 1 234 ? 5.493 1.798 24.529 1.00 121.05 ? 233 THR A N 1 ATOM 1832 C CA . THR A 1 234 ? 4.543 0.807 24.024 1.00 125.57 ? 233 THR A CA 1 ATOM 1833 C C . THR A 1 234 ? 3.830 0.071 25.163 1.00 128.94 ? 233 THR A C 1 ATOM 1834 O O . THR A 1 234 ? 2.597 0.034 25.221 1.00 134.45 ? 233 THR A O 1 ATOM 1835 C CB . THR A 1 234 ? 5.254 -0.236 23.139 1.00 126.45 ? 233 THR A CB 1 ATOM 1836 O OG1 . THR A 1 234 ? 6.184 0.424 22.273 1.00 127.76 ? 233 THR A OG1 1 ATOM 1837 C CG2 . THR A 1 234 ? 4.246 -1.018 22.304 1.00 125.33 ? 233 THR A CG2 1 ATOM 1838 N N . SER A 1 235 ? 4.614 -0.499 26.070 1.00 128.26 ? 234 SER A N 1 ATOM 1839 C CA . SER A 1 235 ? 4.078 -1.233 27.214 1.00 131.99 ? 234 SER A CA 1 ATOM 1840 C C . SER A 1 235 ? 3.308 -0.320 28.177 1.00 130.56 ? 234 SER A C 1 ATOM 1841 O O . SER A 1 235 ? 2.341 -0.744 28.811 1.00 128.16 ? 234 SER A O 1 ATOM 1842 C CB . SER A 1 235 ? 5.219 -1.939 27.949 1.00 136.78 ? 234 SER A CB 1 ATOM 1843 O OG . SER A 1 235 ? 6.084 -2.587 27.027 1.00 139.23 ? 234 SER A OG 1 ATOM 1844 N N . TRP A 1 236 ? 3.742 0.934 28.276 1.00 131.43 ? 235 TRP A N 1 ATOM 1845 C CA . TRP A 1 236 ? 3.074 1.931 29.109 1.00 135.28 ? 235 TRP A CA 1 ATOM 1846 C C . TRP A 1 236 ? 1.629 2.206 28.673 1.00 134.45 ? 235 TRP A C 1 ATOM 1847 O O . TRP A 1 236 ? 0.782 2.551 29.500 1.00 135.28 ? 235 TRP A O 1 ATOM 1848 C CB . TRP A 1 236 ? 3.883 3.231 29.093 1.00 136.87 ? 235 TRP A CB 1 ATOM 1849 C CG . TRP A 1 236 ? 3.344 4.303 29.982 1.00 138.47 ? 235 TRP A CG 1 ATOM 1850 C CD1 . TRP A 1 236 ? 2.773 4.141 31.212 1.00 139.46 ? 235 TRP A CD1 1 ATOM 1851 C CD2 . TRP A 1 236 ? 3.352 5.708 29.724 1.00 139.45 ? 235 TRP A CD2 1 ATOM 1852 N NE1 . TRP A 1 236 ? 2.412 5.360 31.731 1.00 140.46 ? 235 TRP A NE1 1 ATOM 1853 C CE2 . TRP A 1 236 ? 2.759 6.341 30.838 1.00 142.29 ? 235 TRP A CE2 1 ATOM 1854 C CE3 . TRP A 1 236 ? 3.802 6.498 28.656 1.00 136.97 ? 235 TRP A CE3 1 ATOM 1855 C CZ2 . TRP A 1 236 ? 2.602 7.728 30.914 1.00 144.35 ? 235 TRP A CZ2 1 ATOM 1856 C CZ3 . TRP A 1 236 ? 3.644 7.876 28.732 1.00 136.46 ? 235 TRP A CZ3 1 ATOM 1857 C CH2 . TRP A 1 236 ? 3.048 8.476 29.853 1.00 139.92 ? 235 TRP A CH2 1 ATOM 1858 N N . LEU A 1 237 ? 1.352 2.047 27.381 1.00 132.37 ? 236 LEU A N 1 ATOM 1859 C CA . LEU A 1 237 ? 0.023 2.322 26.827 1.00 134.61 ? 236 LEU A CA 1 ATOM 1860 C C . LEU A 1 237 ? -0.934 1.121 26.787 1.00 136.81 ? 236 LEU A C 1 ATOM 1861 O O . LEU A 1 237 ? -2.007 1.211 26.183 1.00 140.88 ? 236 LEU A O 1 ATOM 1862 C CB . LEU A 1 237 ? 0.159 2.905 25.416 1.00 135.18 ? 236 LEU A CB 1 ATOM 1863 C CG . LEU A 1 237 ? 0.778 4.299 25.313 1.00 136.72 ? 236 LEU A CG 1 ATOM 1864 C CD1 . LEU A 1 237 ? 0.999 4.658 23.850 1.00 138.91 ? 236 LEU A CD1 1 ATOM 1865 C CD2 . LEU A 1 237 ? -0.099 5.336 26.001 1.00 136.84 ? 236 LEU A CD2 1 ATOM 1866 N N . LEU A 1 238 ? -0.563 0.004 27.409 1.00 135.25 ? 237 LEU A N 1 ATOM 1867 C CA . LEU A 1 238 ? -1.496 -1.113 27.559 1.00 132.40 ? 237 LEU A CA 1 ATOM 1868 C C . LEU A 1 238 ? -2.712 -0.658 28.374 1.00 131.90 ? 237 LEU A C 1 ATOM 1869 O O . LEU A 1 238 ? -2.580 0.198 29.252 1.00 129.88 ? 237 LEU A O 1 ATOM 1870 C CB . LEU A 1 238 ? -0.819 -2.301 28.248 1.00 131.91 ? 237 LEU A CB 1 ATOM 1871 C CG . LEU A 1 238 ? 0.160 -3.098 27.386 1.00 129.63 ? 237 LEU A CG 1 ATOM 1872 C CD1 . LEU A 1 238 ? 1.090 -3.928 28.256 1.00 129.68 ? 237 LEU A CD1 1 ATOM 1873 C CD2 . LEU A 1 238 ? -0.596 -3.981 26.407 1.00 129.45 ? 237 LEU A CD2 1 ATOM 1874 N N . PRO A 1 239 ? -3.898 -1.216 28.074 1.00 131.25 ? 238 PRO A N 1 ATOM 1875 C CA . PRO A 1 239 ? -5.134 -0.886 28.786 1.00 132.95 ? 238 PRO A CA 1 ATOM 1876 C C . PRO A 1 239 ? -5.027 -0.925 30.313 1.00 136.62 ? 238 PRO A C 1 ATOM 1877 O O . PRO A 1 239 ? -4.386 -1.823 30.866 1.00 133.83 ? 238 PRO A O 1 ATOM 1878 C CB . PRO A 1 239 ? -6.104 -1.958 28.299 1.00 133.99 ? 238 PRO A CB 1 ATOM 1879 C CG . PRO A 1 239 ? -5.643 -2.266 26.920 1.00 133.90 ? 238 PRO A CG 1 ATOM 1880 C CD . PRO A 1 239 ? -4.150 -2.116 26.934 1.00 131.35 ? 238 PRO A CD 1 ATOM 1881 N N . TYR A 1 240 ? -5.658 0.048 30.973 1.00 143.45 ? 239 TYR A N 1 ATOM 1882 C CA . TYR A 1 240 ? -5.692 0.141 32.440 1.00 148.62 ? 239 TYR A CA 1 ATOM 1883 C C . TYR A 1 240 ? -7.105 -0.137 32.974 1.00 153.13 ? 239 TYR A C 1 ATOM 1884 O O . TYR A 1 240 ? -8.102 0.172 32.317 1.00 150.08 ? 239 TYR A O 1 ATOM 1885 C CB . TYR A 1 240 ? -5.249 1.533 32.897 1.00 149.71 ? 239 TYR A CB 1 ATOM 1886 C CG . TYR A 1 240 ? -3.782 1.851 32.673 1.00 150.66 ? 239 TYR A CG 1 ATOM 1887 C CD1 . TYR A 1 240 ? -3.337 2.377 31.459 1.00 150.21 ? 239 TYR A CD1 1 ATOM 1888 C CD2 . TYR A 1 240 ? -2.843 1.654 33.684 1.00 151.62 ? 239 TYR A CD2 1 ATOM 1889 C CE1 . TYR A 1 240 ? -2.001 2.683 31.256 1.00 150.06 ? 239 TYR A CE1 1 ATOM 1890 C CE2 . TYR A 1 240 ? -1.505 1.958 33.490 1.00 151.20 ? 239 TYR A CE2 1 ATOM 1891 C CZ . TYR A 1 240 ? -1.091 2.472 32.277 1.00 151.16 ? 239 TYR A CZ 1 ATOM 1892 O OH . TYR A 1 240 ? 0.235 2.771 32.085 1.00 151.26 ? 239 TYR A OH 1 ATOM 1893 N N . ASN A 1 241 ? -7.171 -0.699 34.180 1.00 162.41 ? 240 ASN A N 1 ATOM 1894 C CA . ASN A 1 241 ? -8.426 -1.210 34.750 1.00 170.72 ? 240 ASN A CA 1 ATOM 1895 C C . ASN A 1 241 ? -9.445 -0.167 35.190 1.00 170.84 ? 240 ASN A C 1 ATOM 1896 O O . ASN A 1 241 ? -10.608 -0.488 35.434 1.00 168.16 ? 240 ASN A O 1 ATOM 1897 C CB . ASN A 1 241 ? -8.129 -2.145 35.930 1.00 178.48 ? 240 ASN A CB 1 ATOM 1898 C CG . ASN A 1 241 ? -7.481 -1.432 37.111 1.00 185.80 ? 240 ASN A CG 1 ATOM 1899 O OD1 . ASN A 1 241 ? -7.525 -0.203 37.225 1.00 185.61 ? 240 ASN A OD1 1 ATOM 1900 N ND2 . ASN A 1 241 ? -6.895 -2.220 38.023 1.00 195.37 ? 240 ASN A ND2 1 ATOM 1901 N N . TYR A 1 242 ? -9.006 1.074 35.330 1.00 174.58 ? 241 TYR A N 1 ATOM 1902 C CA . TYR A 1 242 ? -9.911 2.138 35.736 1.00 183.00 ? 241 TYR A CA 1 ATOM 1903 C C . TYR A 1 242 ? -10.745 2.668 34.563 1.00 174.96 ? 241 TYR A C 1 ATOM 1904 O O . TYR A 1 242 ? -11.779 3.307 34.779 1.00 180.37 ? 241 TYR A O 1 ATOM 1905 C CB . TYR A 1 242 ? -9.147 3.276 36.433 1.00 192.73 ? 241 TYR A CB 1 ATOM 1906 C CG . TYR A 1 242 ? -8.083 3.965 35.591 1.00 202.57 ? 241 TYR A CG 1 ATOM 1907 C CD1 . TYR A 1 242 ? -8.420 4.989 34.705 1.00 206.16 ? 241 TYR A CD1 1 ATOM 1908 C CD2 . TYR A 1 242 ? -6.737 3.611 35.701 1.00 207.29 ? 241 TYR A CD2 1 ATOM 1909 C CE1 . TYR A 1 242 ? -7.453 5.628 33.942 1.00 206.17 ? 241 TYR A CE1 1 ATOM 1910 C CE2 . TYR A 1 242 ? -5.763 4.246 34.941 1.00 209.04 ? 241 TYR A CE2 1 ATOM 1911 C CZ . TYR A 1 242 ? -6.125 5.254 34.062 1.00 207.40 ? 241 TYR A CZ 1 ATOM 1912 O OH . TYR A 1 242 ? -5.165 5.891 33.304 1.00 203.42 ? 241 TYR A OH 1 ATOM 1913 N N . THR A 1 243 ? -10.293 2.403 33.335 1.00 162.79 ? 242 THR A N 1 ATOM 1914 C CA . THR A 1 243 ? -11.016 2.816 32.122 1.00 157.51 ? 242 THR A CA 1 ATOM 1915 C C . THR A 1 243 ? -11.713 1.638 31.451 1.00 155.11 ? 242 THR A C 1 ATOM 1916 O O . THR A 1 243 ? -12.864 1.750 31.029 1.00 154.24 ? 242 THR A O 1 ATOM 1917 C CB . THR A 1 243 ? -10.073 3.466 31.091 1.00 152.79 ? 242 THR A CB 1 ATOM 1918 O OG1 . THR A 1 243 ? -9.438 4.607 31.678 1.00 156.66 ? 242 THR A OG1 1 ATOM 1919 C CG2 . THR A 1 243 ? -10.843 3.909 29.848 1.00 150.09 ? 242 THR A CG2 1 ATOM 1920 N N . TRP A 1 244 ? -11.001 0.522 31.345 1.00 152.53 ? 243 TRP A N 1 ATOM 1921 C CA . TRP A 1 244 ? -11.543 -0.700 30.761 1.00 151.74 ? 243 TRP A CA 1 ATOM 1922 C C . TRP A 1 244 ? -12.055 -1.622 31.861 1.00 153.68 ? 243 TRP A C 1 ATOM 1923 O O . TRP A 1 244 ? -11.632 -1.519 33.015 1.00 157.83 ? 243 TRP A O 1 ATOM 1924 C CB . TRP A 1 244 ? -10.459 -1.401 29.948 1.00 148.21 ? 243 TRP A CB 1 ATOM 1925 C CG . TRP A 1 244 ? -9.918 -0.541 28.850 1.00 145.12 ? 243 TRP A CG 1 ATOM 1926 C CD1 . TRP A 1 244 ? -8.914 0.379 28.944 1.00 143.47 ? 243 TRP A CD1 1 ATOM 1927 C CD2 . TRP A 1 244 ? -10.363 -0.512 27.492 1.00 144.67 ? 243 TRP A CD2 1 ATOM 1928 N NE1 . TRP A 1 244 ? -8.701 0.975 27.724 1.00 142.44 ? 243 TRP A NE1 1 ATOM 1929 C CE2 . TRP A 1 244 ? -9.578 0.445 26.814 1.00 142.38 ? 243 TRP A CE2 1 ATOM 1930 C CE3 . TRP A 1 244 ? -11.346 -1.206 26.779 1.00 145.85 ? 243 TRP A CE3 1 ATOM 1931 C CZ2 . TRP A 1 244 ? -9.749 0.726 25.458 1.00 141.88 ? 243 TRP A CZ2 1 ATOM 1932 C CZ3 . TRP A 1 244 ? -11.514 -0.927 25.432 1.00 144.69 ? 243 TRP A CZ3 1 ATOM 1933 C CH2 . TRP A 1 244 ? -10.722 0.032 24.787 1.00 142.04 ? 243 TRP A CH2 1 ATOM 1934 N N . SER A 1 245 ? -12.975 -2.513 31.507 1.00 153.42 ? 244 SER A N 1 ATOM 1935 C CA . SER A 1 245 ? -13.514 -3.468 32.472 1.00 157.66 ? 244 SER A CA 1 ATOM 1936 C C . SER A 1 245 ? -12.415 -4.450 32.885 1.00 156.61 ? 244 SER A C 1 ATOM 1937 O O . SER A 1 245 ? -11.690 -4.955 32.028 1.00 150.33 ? 244 SER A O 1 ATOM 1938 C CB . SER A 1 245 ? -14.696 -4.231 31.872 1.00 160.77 ? 244 SER A CB 1 ATOM 1939 O OG . SER A 1 245 ? -15.334 -5.032 32.853 1.00 165.26 ? 244 SER A OG 1 ATOM 1940 N N . PRO A 1 246 ? -12.279 -4.721 34.199 1.00 159.38 ? 245 PRO A N 1 ATOM 1941 C CA . PRO A 1 246 ? -11.274 -5.699 34.642 1.00 154.04 ? 245 PRO A CA 1 ATOM 1942 C C . PRO A 1 246 ? -11.420 -7.098 34.027 1.00 146.63 ? 245 PRO A C 1 ATOM 1943 O O . PRO A 1 246 ? -10.444 -7.847 33.950 1.00 140.50 ? 245 PRO A O 1 ATOM 1944 C CB . PRO A 1 246 ? -11.488 -5.762 36.157 1.00 156.90 ? 245 PRO A CB 1 ATOM 1945 C CG . PRO A 1 246 ? -12.113 -4.460 36.526 1.00 159.34 ? 245 PRO A CG 1 ATOM 1946 C CD . PRO A 1 246 ? -12.926 -4.034 35.338 1.00 160.82 ? 245 PRO A CD 1 ATOM 1947 N N . GLU A 1 247 ? -12.631 -7.429 33.592 1.00 144.95 ? 246 GLU A N 1 ATOM 1948 C CA . GLU A 1 247 ? -12.933 -8.741 33.030 1.00 145.86 ? 246 GLU A CA 1 ATOM 1949 C C . GLU A 1 247 ? -12.960 -8.749 31.492 1.00 142.88 ? 246 GLU A C 1 ATOM 1950 O O . GLU A 1 247 ? -13.243 -9.779 30.886 1.00 142.49 ? 246 GLU A O 1 ATOM 1951 C CB . GLU A 1 247 ? -14.289 -9.228 33.565 1.00 151.17 ? 246 GLU A CB 1 ATOM 1952 C CG . GLU A 1 247 ? -14.336 -9.527 35.064 1.00 156.29 ? 246 GLU A CG 1 ATOM 1953 C CD . GLU A 1 247 ? -14.162 -8.298 35.955 1.00 158.99 ? 246 GLU A CD 1 ATOM 1954 O OE1 . GLU A 1 247 ? -14.499 -7.172 35.525 1.00 158.29 ? 246 GLU A OE1 1 ATOM 1955 O OE2 . GLU A 1 247 ? -13.698 -8.460 37.103 1.00 160.30 ? 246 GLU A OE2 1 ATOM 1956 N N . LYS A 1 248 ? -12.670 -7.618 30.855 1.00 139.94 ? 247 LYS A N 1 ATOM 1957 C CA . LYS A 1 248 ? -12.771 -7.527 29.403 1.00 140.77 ? 247 LYS A CA 1 ATOM 1958 C C . LYS A 1 248 ? -11.692 -8.363 28.722 1.00 139.87 ? 247 LYS A C 1 ATOM 1959 O O . LYS A 1 248 ? -10.510 -8.237 29.036 1.00 137.20 ? 247 LYS A O 1 ATOM 1960 C CB . LYS A 1 248 ? -12.663 -6.067 28.945 1.00 139.75 ? 247 LYS A CB 1 ATOM 1961 C CG . LYS A 1 248 ? -12.718 -5.856 27.435 1.00 141.09 ? 247 LYS A CG 1 ATOM 1962 C CD . LYS A 1 248 ? -14.085 -6.180 26.848 1.00 144.57 ? 247 LYS A CD 1 ATOM 1963 C CE . LYS A 1 248 ? -14.037 -6.241 25.328 1.00 145.28 ? 247 LYS A CE 1 ATOM 1964 N NZ . LYS A 1 248 ? -13.491 -4.995 24.721 1.00 142.11 ? 247 LYS A NZ 1 ATOM 1965 N N . VAL A 1 249 ? -12.112 -9.206 27.782 1.00 141.83 ? 248 VAL A N 1 ATOM 1966 C CA . VAL A 1 249 ? -11.193 -10.049 27.016 1.00 142.92 ? 248 VAL A CA 1 ATOM 1967 C C . VAL A 1 249 ? -10.707 -9.264 25.799 1.00 141.09 ? 248 VAL A C 1 ATOM 1968 O O . VAL A 1 249 ? -11.512 -8.863 24.957 1.00 139.81 ? 248 VAL A O 1 ATOM 1969 C CB . VAL A 1 249 ? -11.891 -11.342 26.529 1.00 146.44 ? 248 VAL A CB 1 ATOM 1970 C CG1 . VAL A 1 249 ? -10.892 -12.265 25.840 1.00 145.87 ? 248 VAL A CG1 1 ATOM 1971 C CG2 . VAL A 1 249 ? -12.572 -12.059 27.691 1.00 149.46 ? 248 VAL A CG2 1 ATOM 1972 N N . PHE A 1 250 ? -9.399 -9.041 25.713 1.00 138.91 ? 249 PHE A N 1 ATOM 1973 C CA . PHE A 1 250 ? -8.818 -8.290 24.600 1.00 135.68 ? 249 PHE A CA 1 ATOM 1974 C C . PHE A 1 250 ? -8.287 -9.208 23.511 1.00 134.02 ? 249 PHE A C 1 ATOM 1975 O O . PHE A 1 250 ? -8.378 -8.888 22.326 1.00 134.62 ? 249 PHE A O 1 ATOM 1976 C CB . PHE A 1 250 ? -7.686 -7.394 25.094 1.00 135.38 ? 249 PHE A CB 1 ATOM 1977 C CG . PHE A 1 250 ? -8.150 -6.248 25.938 1.00 137.61 ? 249 PHE A CG 1 ATOM 1978 C CD1 . PHE A 1 250 ? -8.580 -5.069 25.348 1.00 135.90 ? 249 PHE A CD1 1 ATOM 1979 C CD2 . PHE A 1 250 ? -8.156 -6.347 27.324 1.00 142.65 ? 249 PHE A CD2 1 ATOM 1980 C CE1 . PHE A 1 250 ? -9.008 -4.007 26.123 1.00 138.72 ? 249 PHE A CE1 1 ATOM 1981 C CE2 . PHE A 1 250 ? -8.582 -5.290 28.107 1.00 145.18 ? 249 PHE A CE2 1 ATOM 1982 C CZ . PHE A 1 250 ? -9.009 -4.116 27.505 1.00 144.01 ? 249 PHE A CZ 1 ATOM 1983 N N . VAL A 1 251 ? -7.713 -10.337 23.918 1.00 131.44 ? 250 VAL A N 1 ATOM 1984 C CA . VAL A 1 251 ? -7.081 -11.256 22.977 1.00 131.76 ? 250 VAL A CA 1 ATOM 1985 C C . VAL A 1 251 ? -7.519 -12.688 23.235 1.00 136.64 ? 250 VAL A C 1 ATOM 1986 O O . VAL A 1 251 ? -7.427 -13.185 24.363 1.00 139.52 ? 250 VAL A O 1 ATOM 1987 C CB . VAL A 1 251 ? -5.541 -11.179 23.046 1.00 128.92 ? 250 VAL A CB 1 ATOM 1988 C CG1 . VAL A 1 251 ? -4.905 -12.193 22.098 1.00 127.34 ? 250 VAL A CG1 1 ATOM 1989 C CG2 . VAL A 1 251 ? -5.069 -9.769 22.722 1.00 128.33 ? 250 VAL A CG2 1 ATOM 1990 N N . GLN A 1 252 ? -7.997 -13.337 22.175 1.00 139.04 ? 251 GLN A N 1 ATOM 1991 C CA . GLN A 1 252 ? -8.354 -14.749 22.212 1.00 142.15 ? 251 GLN A CA 1 ATOM 1992 C C . GLN A 1 252 ? -7.410 -15.529 21.298 1.00 142.63 ? 251 GLN A C 1 ATOM 1993 O O . GLN A 1 252 ? -7.114 -15.094 20.184 1.00 139.74 ? 251 GLN A O 1 ATOM 1994 C CB . GLN A 1 252 ? -9.806 -14.950 21.759 1.00 145.35 ? 251 GLN A CB 1 ATOM 1995 C CG . GLN A 1 252 ? -10.862 -14.458 22.746 1.00 147.48 ? 251 GLN A CG 1 ATOM 1996 C CD . GLN A 1 252 ? -11.351 -13.044 22.472 1.00 147.80 ? 251 GLN A CD 1 ATOM 1997 O OE1 . GLN A 1 252 ? -10.606 -12.197 21.980 1.00 148.57 ? 251 GLN A OE1 1 ATOM 1998 N NE2 . GLN A 1 252 ? -12.611 -12.781 22.805 1.00 148.30 ? 251 GLN A NE2 1 ATOM 1999 N N . THR A 1 253 ? -6.929 -16.671 21.787 1.00 146.33 ? 252 THR A N 1 ATOM 2000 C CA . THR A 1 253 ? -6.068 -17.569 21.010 1.00 146.81 ? 252 THR A CA 1 ATOM 2001 C C . THR A 1 253 ? -6.711 -18.953 21.066 1.00 148.32 ? 252 THR A C 1 ATOM 2002 O O . THR A 1 253 ? -7.709 -19.132 21.765 1.00 148.57 ? 252 THR A O 1 ATOM 2003 C CB . THR A 1 253 ? -4.636 -17.627 21.599 1.00 149.21 ? 252 THR A CB 1 ATOM 2004 O OG1 . THR A 1 253 ? -4.609 -18.478 22.752 1.00 150.43 ? 252 THR A OG1 1 ATOM 2005 C CG2 . THR A 1 253 ? -4.147 -16.235 21.981 1.00 150.97 ? 252 THR A CG2 1 ATOM 2006 N N . PRO A 1 254 ? -6.145 -19.941 20.345 1.00 148.97 ? 253 PRO A N 1 ATOM 2007 C CA . PRO A 1 254 ? -6.757 -21.271 20.366 1.00 151.73 ? 253 PRO A CA 1 ATOM 2008 C C . PRO A 1 254 ? -6.767 -21.934 21.745 1.00 156.07 ? 253 PRO A C 1 ATOM 2009 O O . PRO A 1 254 ? -7.628 -22.771 22.012 1.00 157.85 ? 253 PRO A O 1 ATOM 2010 C CB . PRO A 1 254 ? -5.889 -22.081 19.389 1.00 150.37 ? 253 PRO A CB 1 ATOM 2011 C CG . PRO A 1 254 ? -5.143 -21.072 18.585 1.00 147.56 ? 253 PRO A CG 1 ATOM 2012 C CD . PRO A 1 254 ? -4.929 -19.922 19.515 1.00 146.64 ? 253 PRO A CD 1 ATOM 2013 N N . THR A 1 255 ? -5.825 -21.556 22.609 1.00 160.44 ? 254 THR A N 1 ATOM 2014 C CA . THR A 1 255 ? -5.656 -22.192 23.915 1.00 167.58 ? 254 THR A CA 1 ATOM 2015 C C . THR A 1 255 ? -6.118 -21.351 25.112 1.00 168.00 ? 254 THR A C 1 ATOM 2016 O O . THR A 1 255 ? -6.556 -21.906 26.122 1.00 168.66 ? 254 THR A O 1 ATOM 2017 C CB . THR A 1 255 ? -4.176 -22.567 24.141 1.00 170.41 ? 254 THR A CB 1 ATOM 2018 O OG1 . THR A 1 255 ? -3.357 -21.394 24.036 1.00 171.41 ? 254 THR A OG1 1 ATOM 2019 C CG2 . THR A 1 255 ? -3.718 -23.597 23.114 1.00 170.77 ? 254 THR A CG2 1 ATOM 2020 N N . ILE A 1 256 ? -6.024 -20.027 25.011 1.00 169.20 ? 255 ILE A N 1 ATOM 2021 C CA . ILE A 1 256 ? -6.223 -19.175 26.182 1.00 172.31 ? 255 ILE A CA 1 ATOM 2022 C C . ILE A 1 256 ? -6.756 -17.780 25.824 1.00 164.32 ? 255 ILE A C 1 ATOM 2023 O O . ILE A 1 256 ? -6.637 -17.326 24.682 1.00 157.24 ? 255 ILE A O 1 ATOM 2024 C CB . ILE A 1 256 ? -4.899 -19.068 26.989 1.00 177.75 ? 255 ILE A CB 1 ATOM 2025 C CG1 . ILE A 1 256 ? -5.152 -18.654 28.445 1.00 181.94 ? 255 ILE A CG1 1 ATOM 2026 C CG2 . ILE A 1 256 ? -3.912 -18.128 26.309 1.00 175.17 ? 255 ILE A CG2 1 ATOM 2027 C CD1 . ILE A 1 256 ? -3.915 -18.706 29.316 1.00 182.09 ? 255 ILE A CD1 1 ATOM 2028 N N . ASN A 1 257 ? -7.371 -17.133 26.814 1.00 161.79 ? 256 ASN A N 1 ATOM 2029 C CA . ASN A 1 257 ? -7.771 -15.728 26.734 1.00 157.86 ? 256 ASN A CA 1 ATOM 2030 C C . ASN A 1 257 ? -6.747 -14.825 27.399 1.00 151.12 ? 256 ASN A C 1 ATOM 2031 O O . ASN A 1 257 ? -5.901 -15.282 28.172 1.00 155.32 ? 256 ASN A O 1 ATOM 2032 C CB . ASN A 1 257 ? -9.097 -15.515 27.462 1.00 162.57 ? 256 ASN A CB 1 ATOM 2033 C CG . ASN A 1 257 ? -10.276 -16.094 26.719 1.00 170.32 ? 256 ASN A CG 1 ATOM 2034 O OD1 . ASN A 1 257 ? -10.277 -16.167 25.489 1.00 168.54 ? 256 ASN A OD1 1 ATOM 2035 N ND2 . ASN A 1 257 ? -11.324 -16.464 27.472 1.00 181.31 ? 256 ASN A ND2 1 ATOM 2036 N N . TYR A 1 258 ? -6.844 -13.534 27.105 1.00 141.73 ? 257 TYR A N 1 ATOM 2037 C CA . TYR A 1 258 ? -6.053 -12.527 27.796 1.00 136.51 ? 257 TYR A CA 1 ATOM 2038 C C . TYR A 1 258 ? -6.900 -11.300 28.110 1.00 137.53 ? 257 TYR A C 1 ATOM 2039 O O . TYR A 1 258 ? -7.440 -10.645 27.202 1.00 133.60 ? 257 TYR A O 1 ATOM 2040 C CB . TYR A 1 258 ? -4.833 -12.133 26.971 1.00 132.84 ? 257 TYR A CB 1 ATOM 2041 C CG . TYR A 1 258 ? -3.843 -13.258 26.792 1.00 133.91 ? 257 TYR A CG 1 ATOM 2042 C CD1 . TYR A 1 258 ? -2.984 -13.627 27.823 1.00 134.26 ? 257 TYR A CD1 1 ATOM 2043 C CD2 . TYR A 1 258 ? -3.765 -13.959 25.590 1.00 136.28 ? 257 TYR A CD2 1 ATOM 2044 C CE1 . TYR A 1 258 ? -2.074 -14.661 27.663 1.00 138.03 ? 257 TYR A CE1 1 ATOM 2045 C CE2 . TYR A 1 258 ? -2.858 -14.993 25.420 1.00 138.14 ? 257 TYR A CE2 1 ATOM 2046 C CZ . TYR A 1 258 ? -2.014 -15.340 26.458 1.00 139.30 ? 257 TYR A CZ 1 ATOM 2047 O OH . TYR A 1 258 ? -1.120 -16.372 26.289 1.00 140.76 ? 257 TYR A OH 1 ATOM 2048 N N . THR A 1 259 ? -7.036 -11.032 29.410 1.00 141.37 ? 258 THR A N 1 ATOM 2049 C CA . THR A 1 259 ? -7.599 -9.784 29.927 1.00 142.48 ? 258 THR A CA 1 ATOM 2050 C C . THR A 1 259 ? -6.449 -8.912 30.426 1.00 143.03 ? 258 THR A C 1 ATOM 2051 O O . THR A 1 259 ? -5.289 -9.328 30.424 1.00 143.90 ? 258 THR A O 1 ATOM 2052 C CB . THR A 1 259 ? -8.567 -10.034 31.107 1.00 143.52 ? 258 THR A CB 1 ATOM 2053 O OG1 . THR A 1 259 ? -7.849 -10.573 32.223 1.00 140.76 ? 258 THR A OG1 1 ATOM 2054 C CG2 . THR A 1 259 ? -9.678 -10.992 30.710 1.00 146.33 ? 258 THR A CG2 1 ATOM 2055 N N . LEU A 1 260 ? -6.777 -7.703 30.863 1.00 142.75 ? 259 LEU A N 1 ATOM 2056 C CA . LEU A 1 260 ? -5.780 -6.796 31.426 1.00 142.67 ? 259 LEU A CA 1 ATOM 2057 C C . LEU A 1 260 ? -5.101 -7.320 32.702 1.00 141.53 ? 259 LEU A C 1 ATOM 2058 O O . LEU A 1 260 ? -4.053 -6.817 33.109 1.00 136.09 ? 259 LEU A O 1 ATOM 2059 C CB . LEU A 1 260 ? -6.409 -5.422 31.679 1.00 146.41 ? 259 LEU A CB 1 ATOM 2060 C CG . LEU A 1 260 ? -7.628 -5.337 32.614 1.00 151.37 ? 259 LEU A CG 1 ATOM 2061 C CD1 . LEU A 1 260 ? -7.213 -5.152 34.069 1.00 153.43 ? 259 LEU A CD1 1 ATOM 2062 C CD2 . LEU A 1 260 ? -8.546 -4.201 32.180 1.00 151.63 ? 259 LEU A CD2 1 ATOM 2063 N N . ARG A 1 261 ? -5.701 -8.325 33.330 1.00 144.71 ? 260 ARG A N 1 ATOM 2064 C CA . ARG A 1 261 ? -5.108 -8.960 34.501 1.00 150.11 ? 260 ARG A CA 1 ATOM 2065 C C . ARG A 1 261 ? -4.160 -10.108 34.140 1.00 148.46 ? 260 ARG A C 1 ATOM 2066 O O . ARG A 1 261 ? -3.585 -10.730 35.033 1.00 150.58 ? 260 ARG A O 1 ATOM 2067 C CB . ARG A 1 261 ? -6.215 -9.460 35.437 1.00 157.63 ? 260 ARG A CB 1 ATOM 2068 C CG . ARG A 1 261 ? -7.169 -8.361 35.891 1.00 161.95 ? 260 ARG A CG 1 ATOM 2069 C CD . ARG A 1 261 ? -8.081 -8.795 37.011 1.00 165.29 ? 260 ARG A CD 1 ATOM 2070 N NE . ARG A 1 261 ? -8.828 -7.689 37.619 1.00 167.32 ? 260 ARG A NE 1 ATOM 2071 C CZ . ARG A 1 261 ? -9.907 -7.835 38.389 1.00 169.44 ? 260 ARG A CZ 1 ATOM 2072 N NH1 . ARG A 1 261 ? -10.405 -9.041 38.647 1.00 171.71 ? 260 ARG A NH1 1 ATOM 2073 N NH2 . ARG A 1 261 ? -10.502 -6.764 38.900 1.00 169.87 ? 260 ARG A NH2 1 ATOM 2074 N N . ASP A 1 262 ? -3.991 -10.382 32.845 1.00 146.97 ? 261 ASP A N 1 ATOM 2075 C CA . ASP A 1 262 ? -3.179 -11.515 32.378 1.00 146.98 ? 261 ASP A CA 1 ATOM 2076 C C . ASP A 1 262 ? -1.902 -11.080 31.634 1.00 145.86 ? 261 ASP A C 1 ATOM 2077 O O . ASP A 1 262 ? -1.355 -11.835 30.818 1.00 147.87 ? 261 ASP A O 1 ATOM 2078 C CB . ASP A 1 262 ? -4.024 -12.423 31.469 1.00 146.82 ? 261 ASP A CB 1 ATOM 2079 C CG . ASP A 1 262 ? -5.168 -13.102 32.209 1.00 149.14 ? 261 ASP A CG 1 ATOM 2080 O OD1 . ASP A 1 262 ? -4.932 -13.673 33.295 1.00 148.51 ? 261 ASP A OD1 1 ATOM 2081 O OD2 . ASP A 1 262 ? -6.304 -13.082 31.691 1.00 150.12 ? 261 ASP A OD2 1 ATOM 2082 N N . TYR A 1 263 ? -1.413 -9.877 31.927 1.00 142.95 ? 262 TYR A N 1 ATOM 2083 C CA . TYR A 1 263 ? -0.241 -9.350 31.233 1.00 138.99 ? 262 TYR A CA 1 ATOM 2084 C C . TYR A 1 263 ? 1.025 -10.182 31.480 1.00 137.28 ? 262 TYR A C 1 ATOM 2085 O O . TYR A 1 263 ? 1.842 -10.354 30.574 1.00 133.65 ? 262 TYR A O 1 ATOM 2086 C CB . TYR A 1 263 ? 0.008 -7.880 31.603 1.00 138.84 ? 262 TYR A CB 1 ATOM 2087 C CG . TYR A 1 263 ? -1.007 -6.877 31.053 1.00 136.31 ? 262 TYR A CG 1 ATOM 2088 C CD1 . TYR A 1 263 ? -1.477 -6.959 29.739 1.00 133.38 ? 262 TYR A CD1 1 ATOM 2089 C CD2 . TYR A 1 263 ? -1.461 -5.818 31.840 1.00 135.06 ? 262 TYR A CD2 1 ATOM 2090 C CE1 . TYR A 1 263 ? -2.386 -6.035 29.242 1.00 130.07 ? 262 TYR A CE1 1 ATOM 2091 C CE2 . TYR A 1 263 ? -2.368 -4.890 31.347 1.00 131.35 ? 262 TYR A CE2 1 ATOM 2092 C CZ . TYR A 1 263 ? -2.828 -5.004 30.049 1.00 129.31 ? 262 TYR A CZ 1 ATOM 2093 O OH . TYR A 1 263 ? -3.725 -4.085 29.559 1.00 127.18 ? 262 TYR A OH 1 ATOM 2094 N N . ARG A 1 264 ? 1.194 -10.705 32.692 1.00 139.20 ? 263 ARG A N 1 ATOM 2095 C CA . ARG A 1 264 ? 2.373 -11.518 32.977 1.00 142.76 ? 263 ARG A CA 1 ATOM 2096 C C . ARG A 1 264 ? 2.412 -12.749 32.071 1.00 145.46 ? 263 ARG A C 1 ATOM 2097 O O . ARG A 1 264 ? 3.451 -13.045 31.479 1.00 143.06 ? 263 ARG A O 1 ATOM 2098 C CB . ARG A 1 264 ? 2.441 -11.924 34.450 1.00 145.98 ? 263 ARG A CB 1 ATOM 2099 C CG . ARG A 1 264 ? 3.813 -12.435 34.864 1.00 150.46 ? 263 ARG A CG 1 ATOM 2100 C CD . ARG A 1 264 ? 3.962 -12.497 36.374 1.00 160.53 ? 263 ARG A CD 1 ATOM 2101 N NE . ARG A 1 264 ? 3.077 -13.495 36.981 1.00 173.89 ? 263 ARG A NE 1 ATOM 2102 C CZ . ARG A 1 264 ? 3.330 -14.804 37.061 1.00 180.76 ? 263 ARG A CZ 1 ATOM 2103 N NH1 . ARG A 1 264 ? 4.453 -15.319 36.565 1.00 184.06 ? 263 ARG A NH1 1 ATOM 2104 N NH2 . ARG A 1 264 ? 2.446 -15.611 37.641 1.00 182.50 ? 263 ARG A NH2 1 ATOM 2105 N N . LYS A 1 265 ? 1.277 -13.448 31.961 1.00 151.91 ? 264 LYS A N 1 ATOM 2106 C CA . LYS A 1 265 ? 1.123 -14.591 31.039 1.00 154.82 ? 264 LYS A CA 1 ATOM 2107 C C . LYS A 1 265 ? 1.430 -14.201 29.600 1.00 148.61 ? 264 LYS A C 1 ATOM 2108 O O . LYS A 1 265 ? 2.147 -14.911 28.898 1.00 143.54 ? 264 LYS A O 1 ATOM 2109 C CB . LYS A 1 265 ? -0.315 -15.131 31.057 1.00 160.03 ? 264 LYS A CB 1 ATOM 2110 C CG . LYS A 1 265 ? -0.681 -16.010 32.234 1.00 167.78 ? 264 LYS A CG 1 ATOM 2111 C CD . LYS A 1 265 ? -2.054 -16.625 32.010 1.00 174.33 ? 264 LYS A CD 1 ATOM 2112 C CE . LYS A 1 265 ? -2.491 -17.471 33.196 1.00 184.23 ? 264 LYS A CE 1 ATOM 2113 N NZ . LYS A 1 265 ? -3.833 -18.084 32.990 1.00 188.12 ? 264 LYS A NZ 1 ATOM 2114 N N . PHE A 1 266 ? 0.845 -13.084 29.173 1.00 143.80 ? 265 PHE A N 1 ATOM 2115 C CA . PHE A 1 266 ? 1.017 -12.574 27.818 1.00 142.80 ? 265 PHE A CA 1 ATOM 2116 C C . PHE A 1 266 ? 2.494 -12.408 27.479 1.00 143.28 ? 265 PHE A C 1 ATOM 2117 O O . PHE A 1 266 ? 2.972 -12.936 26.474 1.00 141.60 ? 265 PHE A O 1 ATOM 2118 C CB . PHE A 1 266 ? 0.284 -11.234 27.663 1.00 142.36 ? 265 PHE A CB 1 ATOM 2119 C CG . PHE A 1 266 ? 0.560 -10.530 26.361 1.00 142.90 ? 265 PHE A CG 1 ATOM 2120 C CD1 . PHE A 1 266 ? -0.128 -10.881 25.207 1.00 145.96 ? 265 PHE A CD1 1 ATOM 2121 C CD2 . PHE A 1 266 ? 1.501 -9.509 26.290 1.00 141.02 ? 265 PHE A CD2 1 ATOM 2122 C CE1 . PHE A 1 266 ? 0.122 -10.233 24.005 1.00 144.73 ? 265 PHE A CE1 1 ATOM 2123 C CE2 . PHE A 1 266 ? 1.756 -8.859 25.092 1.00 140.11 ? 265 PHE A CE2 1 ATOM 2124 C CZ . PHE A 1 266 ? 1.065 -9.220 23.948 1.00 141.31 ? 265 PHE A CZ 1 ATOM 2125 N N . PHE A 1 267 ? 3.216 -11.691 28.335 1.00 146.94 ? 266 PHE A N 1 ATOM 2126 C CA . PHE A 1 267 ? 4.632 -11.420 28.087 1.00 151.48 ? 266 PHE A CA 1 ATOM 2127 C C . PHE A 1 267 ? 5.476 -12.687 28.084 1.00 153.42 ? 266 PHE A C 1 ATOM 2128 O O . PHE A 1 267 ? 6.394 -12.823 27.272 1.00 154.23 ? 266 PHE A O 1 ATOM 2129 C CB . PHE A 1 267 ? 5.199 -10.413 29.096 1.00 155.25 ? 266 PHE A CB 1 ATOM 2130 C CG . PHE A 1 267 ? 4.888 -8.979 28.762 1.00 155.26 ? 266 PHE A CG 1 ATOM 2131 C CD1 . PHE A 1 267 ? 5.338 -8.419 27.573 1.00 156.58 ? 266 PHE A CD1 1 ATOM 2132 C CD2 . PHE A 1 267 ? 4.154 -8.186 29.636 1.00 154.32 ? 266 PHE A CD2 1 ATOM 2133 C CE1 . PHE A 1 267 ? 5.051 -7.101 27.258 1.00 155.95 ? 266 PHE A CE1 1 ATOM 2134 C CE2 . PHE A 1 267 ? 3.870 -6.866 29.328 1.00 152.31 ? 266 PHE A CE2 1 ATOM 2135 C CZ . PHE A 1 267 ? 4.320 -6.322 28.139 1.00 153.54 ? 266 PHE A CZ 1 ATOM 2136 N N . GLN A 1 268 ? 5.171 -13.608 28.992 1.00 155.46 ? 267 GLN A N 1 ATOM 2137 C CA . GLN A 1 268 ? 5.868 -14.887 29.021 1.00 157.70 ? 267 GLN A CA 1 ATOM 2138 C C . GLN A 1 268 ? 5.571 -15.691 27.759 1.00 155.88 ? 267 GLN A C 1 ATOM 2139 O O . GLN A 1 268 ? 6.485 -16.246 27.151 1.00 156.93 ? 267 GLN A O 1 ATOM 2140 C CB . GLN A 1 268 ? 5.523 -15.677 30.286 1.00 162.22 ? 267 GLN A CB 1 ATOM 2141 C CG . GLN A 1 268 ? 6.149 -15.083 31.540 1.00 166.09 ? 267 GLN A CG 1 ATOM 2142 C CD . GLN A 1 268 ? 5.875 -15.891 32.796 1.00 174.13 ? 267 GLN A CD 1 ATOM 2143 O OE1 . GLN A 1 268 ? 5.279 -16.968 32.746 1.00 180.38 ? 267 GLN A OE1 1 ATOM 2144 N NE2 . GLN A 1 268 ? 6.315 -15.369 33.935 1.00 177.10 ? 267 GLN A NE2 1 ATOM 2145 N N . ASP A 1 269 ? 4.304 -15.711 27.349 1.00 153.42 ? 268 ASP A N 1 ATOM 2146 C CA . ASP A 1 269 ? 3.858 -16.533 26.221 1.00 154.03 ? 268 ASP A CA 1 ATOM 2147 C C . ASP A 1 269 ? 4.358 -16.045 24.861 1.00 151.04 ? 268 ASP A C 1 ATOM 2148 O O . ASP A 1 269 ? 4.576 -16.854 23.954 1.00 153.01 ? 268 ASP A O 1 ATOM 2149 C CB . ASP A 1 269 ? 2.326 -16.637 26.201 1.00 156.09 ? 268 ASP A CB 1 ATOM 2150 C CG . ASP A 1 269 ? 1.776 -17.485 27.342 1.00 160.75 ? 268 ASP A CG 1 ATOM 2151 O OD1 . ASP A 1 269 ? 2.511 -17.731 28.321 1.00 164.95 ? 268 ASP A OD1 1 ATOM 2152 O OD2 . ASP A 1 269 ? 0.603 -17.905 27.262 1.00 162.86 ? 268 ASP A OD2 1 ATOM 2153 N N . ILE A 1 270 ? 4.531 -14.733 24.714 1.00 148.04 ? 269 ILE A N 1 ATOM 2154 C CA . ILE A 1 270 ? 5.051 -14.167 23.462 1.00 145.65 ? 269 ILE A CA 1 ATOM 2155 C C . ILE A 1 270 ? 6.578 -14.072 23.431 1.00 146.17 ? 269 ILE A C 1 ATOM 2156 O O . ILE A 1 270 ? 7.154 -13.680 22.415 1.00 140.29 ? 269 ILE A O 1 ATOM 2157 C CB . ILE A 1 270 ? 4.413 -12.796 23.121 1.00 140.85 ? 269 ILE A CB 1 ATOM 2158 C CG1 . ILE A 1 270 ? 4.752 -11.725 24.169 1.00 139.10 ? 269 ILE A CG1 1 ATOM 2159 C CG2 . ILE A 1 270 ? 2.908 -12.936 22.956 1.00 140.37 ? 269 ILE A CG2 1 ATOM 2160 C CD1 . ILE A 1 270 ? 5.650 -10.624 23.651 1.00 137.96 ? 269 ILE A CD1 1 ATOM 2161 N N . GLY A 1 271 ? 7.224 -14.437 24.539 1.00 148.97 ? 270 GLY A N 1 ATOM 2162 C CA . GLY A 1 271 ? 8.683 -14.486 24.614 1.00 150.82 ? 270 GLY A CA 1 ATOM 2163 C C . GLY A 1 271 ? 9.335 -13.124 24.785 1.00 149.84 ? 270 GLY A C 1 ATOM 2164 O O . GLY A 1 271 ? 10.371 -12.844 24.176 1.00 150.48 ? 270 GLY A O 1 ATOM 2165 N N . PHE A 1 272 ? 8.736 -12.279 25.621 1.00 147.06 ? 271 PHE A N 1 ATOM 2166 C CA . PHE A 1 272 ? 9.291 -10.959 25.905 1.00 141.79 ? 271 PHE A CA 1 ATOM 2167 C C . PHE A 1 272 ? 9.078 -10.607 27.373 1.00 138.35 ? 271 PHE A C 1 ATOM 2168 O O . PHE A 1 272 ? 8.265 -9.749 27.713 1.00 130.97 ? 271 PHE A O 1 ATOM 2169 C CB . PHE A 1 272 ? 8.662 -9.909 24.985 1.00 140.51 ? 271 PHE A CB 1 ATOM 2170 C CG . PHE A 1 272 ? 9.357 -8.575 25.016 1.00 143.37 ? 271 PHE A CG 1 ATOM 2171 C CD1 . PHE A 1 272 ? 10.693 -8.463 24.651 1.00 147.08 ? 271 PHE A CD1 1 ATOM 2172 C CD2 . PHE A 1 272 ? 8.672 -7.426 25.391 1.00 142.62 ? 271 PHE A CD2 1 ATOM 2173 C CE1 . PHE A 1 272 ? 11.335 -7.233 24.672 1.00 145.98 ? 271 PHE A CE1 1 ATOM 2174 C CE2 . PHE A 1 272 ? 9.309 -6.195 25.415 1.00 141.43 ? 271 PHE A CE2 1 ATOM 2175 C CZ . PHE A 1 272 ? 10.642 -6.099 25.055 1.00 141.97 ? 271 PHE A CZ 1 ATOM 2176 N N . GLU A 1 273 ? 9.830 -11.278 28.241 1.00 142.03 ? 272 GLU A N 1 ATOM 2177 C CA . GLU A 1 273 ? 9.720 -11.069 29.687 1.00 146.89 ? 272 GLU A CA 1 ATOM 2178 C C . GLU A 1 273 ? 10.076 -9.641 30.107 1.00 141.48 ? 272 GLU A C 1 ATOM 2179 O O . GLU A 1 273 ? 9.534 -9.132 31.084 1.00 139.48 ? 272 GLU A O 1 ATOM 2180 C CB . GLU A 1 273 ? 10.587 -12.078 30.454 1.00 156.07 ? 272 GLU A CB 1 ATOM 2181 C CG . GLU A 1 273 ? 10.152 -13.530 30.279 1.00 165.84 ? 272 GLU A CG 1 ATOM 2182 C CD . GLU A 1 273 ? 10.757 -14.475 31.310 1.00 175.19 ? 272 GLU A CD 1 ATOM 2183 O OE1 . GLU A 1 273 ? 10.652 -14.191 32.523 1.00 181.48 ? 272 GLU A OE1 1 ATOM 2184 O OE2 . GLU A 1 273 ? 11.324 -15.518 30.909 1.00 177.90 ? 272 GLU A OE2 1 ATOM 2185 N N . ASP A 1 274 ? 10.972 -8.996 29.361 1.00 138.37 ? 273 ASP A N 1 ATOM 2186 C CA . ASP A 1 274 ? 11.352 -7.604 29.624 1.00 135.76 ? 273 ASP A CA 1 ATOM 2187 C C . ASP A 1 274 ? 10.141 -6.676 29.646 1.00 132.01 ? 273 ASP A C 1 ATOM 2188 O O . ASP A 1 274 ? 10.089 -5.722 30.419 1.00 129.66 ? 273 ASP A O 1 ATOM 2189 C CB . ASP A 1 274 ? 12.326 -7.101 28.552 1.00 137.60 ? 273 ASP A CB 1 ATOM 2190 C CG . ASP A 1 274 ? 13.636 -7.865 28.540 1.00 142.80 ? 273 ASP A CG 1 ATOM 2191 O OD1 . ASP A 1 274 ? 13.612 -9.099 28.732 1.00 149.75 ? 273 ASP A OD1 1 ATOM 2192 O OD2 . ASP A 1 274 ? 14.689 -7.232 28.322 1.00 144.72 ? 273 ASP A OD2 1 ATOM 2193 N N . GLY A 1 275 ? 9.172 -6.956 28.783 1.00 131.70 ? 274 GLY A N 1 ATOM 2194 C CA . GLY A 1 275 ? 7.979 -6.130 28.689 1.00 132.24 ? 274 GLY A CA 1 ATOM 2195 C C . GLY A 1 275 ? 7.158 -6.106 29.963 1.00 134.67 ? 274 GLY A C 1 ATOM 2196 O O . GLY A 1 275 ? 6.569 -5.080 30.303 1.00 138.10 ? 274 GLY A O 1 ATOM 2197 N N . TRP A 1 276 ? 7.109 -7.237 30.664 1.00 136.01 ? 275 TRP A N 1 ATOM 2198 C CA . TRP A 1 276 ? 6.411 -7.329 31.953 1.00 137.74 ? 275 TRP A CA 1 ATOM 2199 C C . TRP A 1 276 ? 7.092 -6.420 32.972 1.00 135.32 ? 275 TRP A C 1 ATOM 2200 O O . TRP A 1 276 ? 6.431 -5.699 33.722 1.00 134.14 ? 275 TRP A O 1 ATOM 2201 C CB . TRP A 1 276 ? 6.396 -8.789 32.435 1.00 142.05 ? 275 TRP A CB 1 ATOM 2202 C CG . TRP A 1 276 ? 5.821 -9.034 33.812 1.00 144.99 ? 275 TRP A CG 1 ATOM 2203 C CD1 . TRP A 1 276 ? 6.418 -9.719 34.831 1.00 148.89 ? 275 TRP A CD1 1 ATOM 2204 C CD2 . TRP A 1 276 ? 4.538 -8.623 34.306 1.00 145.43 ? 275 TRP A CD2 1 ATOM 2205 N NE1 . TRP A 1 276 ? 5.594 -9.755 35.927 1.00 150.23 ? 275 TRP A NE1 1 ATOM 2206 C CE2 . TRP A 1 276 ? 4.435 -9.088 35.634 1.00 147.23 ? 275 TRP A CE2 1 ATOM 2207 C CE3 . TRP A 1 276 ? 3.469 -7.904 33.759 1.00 145.63 ? 275 TRP A CE3 1 ATOM 2208 C CZ2 . TRP A 1 276 ? 3.305 -8.858 36.424 1.00 147.22 ? 275 TRP A CZ2 1 ATOM 2209 C CZ3 . TRP A 1 276 ? 2.345 -7.675 34.548 1.00 147.12 ? 275 TRP A CZ3 1 ATOM 2210 C CH2 . TRP A 1 276 ? 2.275 -8.152 35.865 1.00 146.91 ? 275 TRP A CH2 1 ATOM 2211 N N . LEU A 1 277 ? 8.421 -6.441 32.962 1.00 135.45 ? 276 LEU A N 1 ATOM 2212 C CA . LEU A 1 277 ? 9.213 -5.599 33.849 1.00 136.35 ? 276 LEU A CA 1 ATOM 2213 C C . LEU A 1 277 ? 8.970 -4.122 33.520 1.00 132.38 ? 276 LEU A C 1 ATOM 2214 O O . LEU A 1 277 ? 8.784 -3.304 34.426 1.00 129.50 ? 276 LEU A O 1 ATOM 2215 C CB . LEU A 1 277 ? 10.705 -5.956 33.743 1.00 139.68 ? 276 LEU A CB 1 ATOM 2216 C CG . LEU A 1 277 ? 11.084 -7.433 33.961 1.00 143.47 ? 276 LEU A CG 1 ATOM 2217 C CD1 . LEU A 1 277 ? 12.552 -7.667 33.644 1.00 145.52 ? 276 LEU A CD1 1 ATOM 2218 C CD2 . LEU A 1 277 ? 10.769 -7.900 35.374 1.00 144.29 ? 276 LEU A CD2 1 ATOM 2219 N N . MET A 1 278 ? 8.940 -3.798 32.226 1.00 127.63 ? 277 MET A N 1 ATOM 2220 C CA . MET A 1 278 ? 8.608 -2.447 31.759 1.00 128.77 ? 277 MET A CA 1 ATOM 2221 C C . MET A 1 278 ? 7.238 -1.983 32.264 1.00 129.87 ? 277 MET A C 1 ATOM 2222 O O . MET A 1 278 ? 7.086 -0.853 32.745 1.00 133.09 ? 277 MET A O 1 ATOM 2223 C CB . MET A 1 278 ? 8.599 -2.396 30.224 1.00 131.12 ? 277 MET A CB 1 ATOM 2224 C CG . MET A 1 278 ? 9.965 -2.449 29.558 1.00 136.17 ? 277 MET A CG 1 ATOM 2225 S SD . MET A 1 278 ? 9.835 -2.357 27.755 1.00 146.23 ? 277 MET A SD 1 ATOM 2226 C CE . MET A 1 278 ? 11.560 -2.290 27.273 1.00 146.92 ? 277 MET A CE 1 ATOM 2227 N N . ARG A 1 279 ? 6.241 -2.853 32.138 1.00 131.02 ? 278 ARG A N 1 ATOM 2228 C CA . ARG A 1 279 ? 4.884 -2.526 32.577 1.00 133.85 ? 278 ARG A CA 1 ATOM 2229 C C . ARG A 1 279 ? 4.838 -2.287 34.083 1.00 132.82 ? 278 ARG A C 1 ATOM 2230 O O . ARG A 1 279 ? 4.223 -1.320 34.545 1.00 138.15 ? 278 ARG A O 1 ATOM 2231 C CB . ARG A 1 279 ? 3.906 -3.642 32.191 1.00 138.78 ? 278 ARG A CB 1 ATOM 2232 C CG . ARG A 1 279 ? 2.461 -3.419 32.630 1.00 141.10 ? 278 ARG A CG 1 ATOM 2233 C CD . ARG A 1 279 ? 1.822 -2.202 31.972 1.00 138.17 ? 278 ARG A CD 1 ATOM 2234 N NE . ARG A 1 279 ? 0.386 -2.127 32.255 1.00 138.61 ? 278 ARG A NE 1 ATOM 2235 C CZ . ARG A 1 279 ? -0.445 -1.215 31.753 1.00 138.79 ? 278 ARG A CZ 1 ATOM 2236 N NH1 . ARG A 1 279 ? 0.002 -0.272 30.927 1.00 139.57 ? 278 ARG A NH1 1 ATOM 2237 N NH2 . ARG A 1 279 ? -1.734 -1.246 32.078 1.00 139.54 ? 278 ARG A NH2 1 ATOM 2238 N N . GLN A 1 280 ? 5.487 -3.164 34.845 1.00 130.48 ? 279 GLN A N 1 ATOM 2239 C CA . GLN A 1 280 ? 5.566 -2.989 36.290 1.00 133.08 ? 279 GLN A CA 1 ATOM 2240 C C . GLN A 1 280 ? 6.221 -1.667 36.663 1.00 132.01 ? 279 GLN A C 1 ATOM 2241 O O . GLN A 1 280 ? 5.780 -1.012 37.607 1.00 134.98 ? 279 GLN A O 1 ATOM 2242 C CB . GLN A 1 280 ? 6.316 -4.147 36.945 1.00 139.82 ? 279 GLN A CB 1 ATOM 2243 C CG . GLN A 1 280 ? 5.519 -5.438 36.978 1.00 145.42 ? 279 GLN A CG 1 ATOM 2244 C CD . GLN A 1 280 ? 6.321 -6.612 37.507 1.00 151.67 ? 279 GLN A CD 1 ATOM 2245 O OE1 . GLN A 1 280 ? 7.448 -6.860 37.074 1.00 152.90 ? 279 GLN A OE1 1 ATOM 2246 N NE2 . GLN A 1 280 ? 5.738 -7.346 38.448 1.00 157.11 ? 279 GLN A NE2 1 ATOM 2247 N N . ASP A 1 281 ? 7.260 -1.276 35.922 1.00 130.82 ? 280 ASP A N 1 ATOM 2248 C CA . ASP A 1 281 ? 7.947 0.001 36.158 1.00 132.77 ? 280 ASP A CA 1 ATOM 2249 C C . ASP A 1 281 ? 7.021 1.204 35.981 1.00 130.98 ? 280 ASP A C 1 ATOM 2250 O O . ASP A 1 281 ? 7.112 2.187 36.721 1.00 127.37 ? 280 ASP A O 1 ATOM 2251 C CB . ASP A 1 281 ? 9.128 0.183 35.185 1.00 134.54 ? 280 ASP A CB 1 ATOM 2252 C CG . ASP A 1 281 ? 10.245 -0.819 35.405 1.00 136.35 ? 280 ASP A CG 1 ATOM 2253 O OD1 . ASP A 1 281 ? 10.509 -1.184 36.569 1.00 138.14 ? 280 ASP A OD1 1 ATOM 2254 O OD2 . ASP A 1 281 ? 10.873 -1.234 34.407 1.00 135.29 ? 280 ASP A OD2 1 ATOM 2255 N N . THR A 1 282 ? 6.136 1.126 34.992 1.00 133.73 ? 281 THR A N 1 ATOM 2256 C CA . THR A 1 282 ? 5.465 2.318 34.490 1.00 136.50 ? 281 THR A CA 1 ATOM 2257 C C . THR A 1 282 ? 3.968 2.457 34.805 1.00 138.69 ? 281 THR A C 1 ATOM 2258 O O . THR A 1 282 ? 3.437 3.572 34.765 1.00 134.69 ? 281 THR A O 1 ATOM 2259 C CB . THR A 1 282 ? 5.723 2.485 32.983 1.00 137.12 ? 281 THR A CB 1 ATOM 2260 O OG1 . THR A 1 282 ? 5.319 3.793 32.574 1.00 144.82 ? 281 THR A OG1 1 ATOM 2261 C CG2 . THR A 1 282 ? 5.003 1.420 32.167 1.00 136.62 ? 281 THR A CG2 1 ATOM 2262 N N . GLU A 1 283 ? 3.294 1.354 35.137 1.00 146.27 ? 282 GLU A N 1 ATOM 2263 C CA . GLU A 1 283 ? 1.835 1.390 35.299 1.00 151.79 ? 282 GLU A CA 1 ATOM 2264 C C . GLU A 1 283 ? 1.363 2.286 36.445 1.00 148.47 ? 282 GLU A C 1 ATOM 2265 O O . GLU A 1 283 ? 0.231 2.767 36.429 1.00 147.94 ? 282 GLU A O 1 ATOM 2266 C CB . GLU A 1 283 ? 1.235 -0.020 35.414 1.00 161.01 ? 282 GLU A CB 1 ATOM 2267 C CG . GLU A 1 283 ? 1.456 -0.742 36.737 1.00 169.37 ? 282 GLU A CG 1 ATOM 2268 C CD . GLU A 1 283 ? 0.623 -2.010 36.848 1.00 177.08 ? 282 GLU A CD 1 ATOM 2269 O OE1 . GLU A 1 283 ? 0.504 -2.741 35.842 1.00 177.44 ? 282 GLU A OE1 1 ATOM 2270 O OE2 . GLU A 1 283 ? 0.084 -2.280 37.943 1.00 186.81 ? 282 GLU A OE2 1 ATOM 2271 N N . GLY A 1 284 ? 2.231 2.517 37.428 1.00 145.91 ? 283 GLY A N 1 ATOM 2272 C CA . GLY A 1 284 ? 1.887 3.353 38.572 1.00 148.80 ? 283 GLY A CA 1 ATOM 2273 C C . GLY A 1 284 ? 2.301 4.815 38.480 1.00 150.09 ? 283 GLY A C 1 ATOM 2274 O O . GLY A 1 284 ? 2.070 5.574 39.422 1.00 154.86 ? 283 GLY A O 1 ATOM 2275 N N . LEU A 1 285 ? 2.894 5.227 37.360 1.00 147.83 ? 284 LEU A N 1 ATOM 2276 C CA . LEU A 1 285 ? 3.454 6.579 37.239 1.00 145.62 ? 284 LEU A CA 1 ATOM 2277 C C . LEU A 1 285 ? 2.415 7.682 37.385 1.00 143.34 ? 284 LEU A C 1 ATOM 2278 O O . LEU A 1 285 ? 2.603 8.625 38.157 1.00 143.75 ? 284 LEU A O 1 ATOM 2279 C CB . LEU A 1 285 ? 4.192 6.753 35.907 1.00 141.98 ? 284 LEU A CB 1 ATOM 2280 C CG . LEU A 1 285 ? 5.637 6.247 35.858 1.00 143.74 ? 284 LEU A CG 1 ATOM 2281 C CD1 . LEU A 1 285 ? 6.199 6.386 34.452 1.00 142.75 ? 284 LEU A CD1 1 ATOM 2282 C CD2 . LEU A 1 285 ? 6.520 6.989 36.854 1.00 146.84 ? 284 LEU A CD2 1 ATOM 2283 N N . VAL A 1 286 ? 1.329 7.562 36.633 1.00 141.51 ? 285 VAL A N 1 ATOM 2284 C CA . VAL A 1 286 ? 0.269 8.563 36.653 1.00 144.49 ? 285 VAL A CA 1 ATOM 2285 C C . VAL A 1 286 ? -0.840 8.113 37.600 1.00 153.06 ? 285 VAL A C 1 ATOM 2286 O O . VAL A 1 286 ? -1.381 7.020 37.446 1.00 159.93 ? 285 VAL A O 1 ATOM 2287 C CB . VAL A 1 286 ? -0.311 8.776 35.240 1.00 140.74 ? 285 VAL A CB 1 ATOM 2288 C CG1 . VAL A 1 286 ? -1.336 9.903 35.239 1.00 140.35 ? 285 VAL A CG1 1 ATOM 2289 C CG2 . VAL A 1 286 ? 0.810 9.072 34.252 1.00 140.29 ? 285 VAL A CG2 1 ATOM 2290 N N . GLU A 1 287 ? -1.172 8.945 38.585 1.00 159.43 ? 286 GLU A N 1 ATOM 2291 C CA . GLU A 1 287 ? -2.285 8.648 39.491 1.00 166.04 ? 286 GLU A CA 1 ATOM 2292 C C . GLU A 1 287 ? -3.600 8.700 38.720 1.00 167.37 ? 286 GLU A C 1 ATOM 2293 O O . GLU A 1 287 ? -3.987 9.753 38.222 1.00 160.51 ? 286 GLU A O 1 ATOM 2294 C CB . GLU A 1 287 ? -2.322 9.639 40.659 1.00 170.09 ? 286 GLU A CB 1 ATOM 2295 C CG . GLU A 1 287 ? -1.177 9.463 41.643 1.00 174.94 ? 286 GLU A CG 1 ATOM 2296 C CD . GLU A 1 287 ? -1.111 10.569 42.679 1.00 180.59 ? 286 GLU A CD 1 ATOM 2297 O OE1 . GLU A 1 287 ? -1.073 11.755 42.287 1.00 179.13 ? 286 GLU A OE1 1 ATOM 2298 O OE2 . GLU A 1 287 ? -1.083 10.253 43.889 1.00 187.03 ? 286 GLU A OE2 1 ATOM 2299 N N . ALA A 1 288 ? -4.281 7.559 38.637 1.00 172.93 ? 287 ALA A N 1 ATOM 2300 C CA . ALA A 1 288 ? -5.450 7.390 37.766 1.00 173.31 ? 287 ALA A CA 1 ATOM 2301 C C . ALA A 1 288 ? -6.554 8.426 37.986 1.00 169.26 ? 287 ALA A C 1 ATOM 2302 O O . ALA A 1 288 ? -7.152 8.914 37.024 1.00 163.65 ? 287 ALA A O 1 ATOM 2303 C CB . ALA A 1 288 ? -6.016 5.986 37.927 1.00 177.94 ? 287 ALA A CB 1 ATOM 2304 N N . THR A 1 289 ? -6.806 8.764 39.249 1.00 167.39 ? 288 THR A N 1 ATOM 2305 C CA . THR A 1 289 ? -7.963 9.578 39.626 1.00 166.70 ? 288 THR A CA 1 ATOM 2306 C C . THR A 1 289 ? -7.688 11.080 39.787 1.00 167.61 ? 288 THR A C 1 ATOM 2307 O O . THR A 1 289 ? -8.618 11.882 39.691 1.00 173.24 ? 288 THR A O 1 ATOM 2308 C CB . THR A 1 289 ? -8.602 9.053 40.930 1.00 165.97 ? 288 THR A CB 1 ATOM 2309 O OG1 . THR A 1 289 ? -7.590 8.879 41.929 1.00 163.74 ? 288 THR A OG1 1 ATOM 2310 C CG2 . THR A 1 289 ? -9.308 7.722 40.690 1.00 164.69 ? 288 THR A CG2 1 ATOM 2311 N N . MET A 1 290 ? -6.429 11.456 40.015 1.00 163.95 ? 289 MET A N 1 ATOM 2312 C CA . MET A 1 290 ? -6.066 12.861 40.233 1.00 160.39 ? 289 MET A CA 1 ATOM 2313 C C . MET A 1 290 ? -6.191 13.672 38.941 1.00 149.78 ? 289 MET A C 1 ATOM 2314 O O . MET A 1 290 ? -5.503 13.374 37.967 1.00 144.43 ? 289 MET A O 1 ATOM 2315 C CB . MET A 1 290 ? -4.633 12.964 40.761 1.00 167.37 ? 289 MET A CB 1 ATOM 2316 C CG . MET A 1 290 ? -4.410 12.292 42.107 1.00 178.71 ? 289 MET A CG 1 ATOM 2317 S SD . MET A 1 290 ? -5.452 12.942 43.430 1.00 201.34 ? 289 MET A SD 1 ATOM 2318 C CE . MET A 1 290 ? -4.828 14.617 43.578 1.00 201.90 ? 289 MET A CE 1 ATOM 2319 N N . PRO A 1 291 ? -7.071 14.698 38.923 1.00 145.91 ? 290 PRO A N 1 ATOM 2320 C CA . PRO A 1 291 ? -7.181 15.538 37.725 1.00 142.44 ? 290 PRO A CA 1 ATOM 2321 C C . PRO A 1 291 ? -5.980 16.470 37.577 1.00 139.02 ? 290 PRO A C 1 ATOM 2322 O O . PRO A 1 291 ? -5.233 16.666 38.535 1.00 139.58 ? 290 PRO A O 1 ATOM 2323 C CB . PRO A 1 291 ? -8.468 16.349 37.957 1.00 144.68 ? 290 PRO A CB 1 ATOM 2324 C CG . PRO A 1 291 ? -9.075 15.842 39.223 1.00 147.57 ? 290 PRO A CG 1 ATOM 2325 C CD . PRO A 1 291 ? -7.998 15.134 39.981 1.00 147.71 ? 290 PRO A CD 1 ATOM 2326 N N . PRO A 1 292 ? -5.788 17.046 36.383 1.00 135.08 ? 291 PRO A N 1 ATOM 2327 C CA . PRO A 1 292 ? -4.664 17.962 36.191 1.00 134.82 ? 291 PRO A CA 1 ATOM 2328 C C . PRO A 1 292 ? -4.779 19.263 36.988 1.00 136.86 ? 291 PRO A C 1 ATOM 2329 O O . PRO A 1 292 ? -3.763 19.892 37.286 1.00 136.68 ? 291 PRO A O 1 ATOM 2330 C CB . PRO A 1 292 ? -4.682 18.238 34.684 1.00 132.74 ? 291 PRO A CB 1 ATOM 2331 C CG . PRO A 1 292 ? -6.071 17.931 34.247 1.00 132.64 ? 291 PRO A CG 1 ATOM 2332 C CD . PRO A 1 292 ? -6.551 16.831 35.142 1.00 133.16 ? 291 PRO A CD 1 ATOM 2333 N N . GLY A 1 293 ? -6.002 19.660 37.332 1.00 140.24 ? 292 GLY A N 1 ATOM 2334 C CA . GLY A 1 293 ? -6.218 20.838 38.170 1.00 142.25 ? 292 GLY A CA 1 ATOM 2335 C C . GLY A 1 293 ? -6.143 22.152 37.416 1.00 139.35 ? 292 GLY A C 1 ATOM 2336 O O . GLY A 1 293 ? -5.843 23.191 38.010 1.00 136.39 ? 292 GLY A O 1 ATOM 2337 N N . VAL A 1 294 ? -6.413 22.104 36.111 1.00 138.53 ? 293 VAL A N 1 ATOM 2338 C CA . VAL A 1 294 ? -6.432 23.298 35.258 1.00 140.08 ? 293 VAL A CA 1 ATOM 2339 C C . VAL A 1 294 ? -7.600 23.229 34.281 1.00 141.24 ? 293 VAL A C 1 ATOM 2340 O O . VAL A 1 294 ? -8.186 22.166 34.087 1.00 140.24 ? 293 VAL A O 1 ATOM 2341 C CB . VAL A 1 294 ? -5.122 23.458 34.454 1.00 137.42 ? 293 VAL A CB 1 ATOM 2342 C CG1 . VAL A 1 294 ? -3.953 23.727 35.389 1.00 139.61 ? 293 VAL A CG1 1 ATOM 2343 C CG2 . VAL A 1 294 ? -4.852 22.235 33.589 1.00 135.41 ? 293 VAL A CG2 1 ATOM 2344 N N . GLN A 1 295 ? -7.932 24.365 33.672 1.00 146.83 ? 294 GLN A N 1 ATOM 2345 C CA . GLN A 1 295 ? -9.012 24.416 32.688 1.00 151.06 ? 294 GLN A CA 1 ATOM 2346 C C . GLN A 1 295 ? -8.676 23.463 31.553 1.00 148.83 ? 294 GLN A C 1 ATOM 2347 O O . GLN A 1 295 ? -7.612 23.575 30.938 1.00 145.39 ? 294 GLN A O 1 ATOM 2348 C CB . GLN A 1 295 ? -9.202 25.830 32.133 1.00 154.89 ? 294 GLN A CB 1 ATOM 2349 C CG . GLN A 1 295 ? -10.444 25.976 31.258 1.00 157.16 ? 294 GLN A CG 1 ATOM 2350 C CD . GLN A 1 295 ? -10.493 27.283 30.488 1.00 159.96 ? 294 GLN A CD 1 ATOM 2351 O OE1 . GLN A 1 295 ? -11.141 27.372 29.444 1.00 160.03 ? 294 GLN A OE1 1 ATOM 2352 N NE2 . GLN A 1 295 ? -9.810 28.304 30.996 1.00 162.07 ? 294 GLN A NE2 1 ATOM 2353 N N . LEU A 1 296 ? -9.588 22.533 31.288 1.00 149.57 ? 295 LEU A N 1 ATOM 2354 C CA . LEU A 1 296 ? -9.326 21.423 30.387 1.00 147.94 ? 295 LEU A CA 1 ATOM 2355 C C . LEU A 1 296 ? -10.362 21.360 29.278 1.00 145.18 ? 295 LEU A C 1 ATOM 2356 O O . LEU A 1 296 ? -11.565 21.451 29.531 1.00 144.35 ? 295 LEU A O 1 ATOM 2357 C CB . LEU A 1 296 ? -9.339 20.114 31.178 1.00 150.09 ? 295 LEU A CB 1 ATOM 2358 C CG . LEU A 1 296 ? -9.206 18.808 30.392 1.00 152.17 ? 295 LEU A CG 1 ATOM 2359 C CD1 . LEU A 1 296 ? -7.944 18.804 29.538 1.00 150.35 ? 295 LEU A CD1 1 ATOM 2360 C CD2 . LEU A 1 296 ? -9.220 17.634 31.361 1.00 156.47 ? 295 LEU A CD2 1 ATOM 2361 N N . HIS A 1 297 ? -9.878 21.206 28.051 1.00 142.18 ? 296 HIS A N 1 ATOM 2362 C CA . HIS A 1 297 ? -10.737 20.990 26.904 1.00 141.67 ? 296 HIS A CA 1 ATOM 2363 C C . HIS A 1 297 ? -10.366 19.653 26.289 1.00 136.47 ? 296 HIS A C 1 ATOM 2364 O O . HIS A 1 297 ? -9.281 19.504 25.734 1.00 132.82 ? 296 HIS A O 1 ATOM 2365 C CB . HIS A 1 297 ? -10.572 22.131 25.909 1.00 144.64 ? 296 HIS A CB 1 ATOM 2366 C CG . HIS A 1 297 ? -10.943 23.468 26.472 1.00 151.54 ? 296 HIS A CG 1 ATOM 2367 N ND1 . HIS A 1 297 ? -12.163 24.064 26.232 1.00 157.26 ? 296 HIS A ND1 1 ATOM 2368 C CD2 . HIS A 1 297 ? -10.263 24.314 27.281 1.00 153.45 ? 296 HIS A CD2 1 ATOM 2369 C CE1 . HIS A 1 297 ? -12.213 25.226 26.859 1.00 158.94 ? 296 HIS A CE1 1 ATOM 2370 N NE2 . HIS A 1 297 ? -11.073 25.401 27.503 1.00 156.83 ? 296 HIS A NE2 1 ATOM 2371 N N . CYS A 1 298 ? -11.259 18.676 26.418 1.00 136.31 ? 297 CYS A N 1 ATOM 2372 C CA . CYS A 1 298 ? -11.003 17.324 25.922 1.00 137.87 ? 297 CYS A CA 1 ATOM 2373 C C . CYS A 1 298 ? -11.681 17.074 24.585 1.00 137.63 ? 297 CYS A C 1 ATOM 2374 O O . CYS A 1 298 ? -12.900 16.929 24.504 1.00 137.40 ? 297 CYS A O 1 ATOM 2375 C CB . CYS A 1 298 ? -11.448 16.282 26.944 1.00 141.72 ? 297 CYS A CB 1 ATOM 2376 S SG . CYS A 1 298 ? -10.360 16.199 28.384 1.00 147.88 ? 297 CYS A SG 1 ATOM 2377 N N . LEU A 1 299 ? -10.869 17.027 23.535 1.00 137.82 ? 298 LEU A N 1 ATOM 2378 C CA . LEU A 1 299 ? -11.349 16.764 22.184 1.00 137.82 ? 298 LEU A CA 1 ATOM 2379 C C . LEU A 1 299 ? -11.065 15.316 21.814 1.00 132.77 ? 298 LEU A C 1 ATOM 2380 O O . LEU A 1 299 ? -9.939 14.840 21.959 1.00 128.04 ? 298 LEU A O 1 ATOM 2381 C CB . LEU A 1 299 ? -10.668 17.695 21.178 1.00 140.69 ? 298 LEU A CB 1 ATOM 2382 C CG . LEU A 1 299 ? -11.248 19.108 21.069 1.00 144.15 ? 298 LEU A CG 1 ATOM 2383 C CD1 . LEU A 1 299 ? -11.268 19.808 22.422 1.00 145.09 ? 298 LEU A CD1 1 ATOM 2384 C CD2 . LEU A 1 299 ? -10.471 19.925 20.046 1.00 143.89 ? 298 LEU A CD2 1 ATOM 2385 N N . TYR A 1 300 ? -12.089 14.623 21.330 1.00 132.56 ? 299 TYR A N 1 ATOM 2386 C CA . TYR A 1 300 ? -11.955 13.221 20.951 1.00 134.43 ? 299 TYR A CA 1 ATOM 2387 C C . TYR A 1 300 ? -12.657 12.936 19.628 1.00 133.13 ? 299 TYR A C 1 ATOM 2388 O O . TYR A 1 300 ? -13.750 13.439 19.379 1.00 137.47 ? 299 TYR A O 1 ATOM 2389 C CB . TYR A 1 300 ? -12.510 12.315 22.056 1.00 138.48 ? 299 TYR A CB 1 ATOM 2390 C CG . TYR A 1 300 ? -13.961 12.566 22.413 1.00 142.31 ? 299 TYR A CG 1 ATOM 2391 C CD1 . TYR A 1 300 ? -14.310 13.509 23.374 1.00 144.31 ? 299 TYR A CD1 1 ATOM 2392 C CD2 . TYR A 1 300 ? -14.984 11.852 21.796 1.00 145.59 ? 299 TYR A CD2 1 ATOM 2393 C CE1 . TYR A 1 300 ? -15.636 13.737 23.703 1.00 147.26 ? 299 TYR A CE1 1 ATOM 2394 C CE2 . TYR A 1 300 ? -16.313 12.075 22.118 1.00 146.94 ? 299 TYR A CE2 1 ATOM 2395 C CZ . TYR A 1 300 ? -16.634 13.016 23.072 1.00 147.26 ? 299 TYR A CZ 1 ATOM 2396 O OH . TYR A 1 300 ? -17.954 13.235 23.394 1.00 149.64 ? 299 TYR A OH 1 ATOM 2397 N N . GLY A 1 301 ? -12.018 12.137 18.779 1.00 127.66 ? 300 GLY A N 1 ATOM 2398 C CA . GLY A 1 301 ? -12.608 11.732 17.505 1.00 124.87 ? 300 GLY A CA 1 ATOM 2399 C C . GLY A 1 301 ? -13.502 10.515 17.664 1.00 124.40 ? 300 GLY A C 1 ATOM 2400 O O . GLY A 1 301 ? -13.223 9.629 18.482 1.00 122.36 ? 300 GLY A O 1 ATOM 2401 N N . THR A 1 302 ? -14.582 10.475 16.884 1.00 125.87 ? 301 THR A N 1 ATOM 2402 C CA . THR A 1 302 ? -15.519 9.350 16.900 1.00 127.57 ? 301 THR A CA 1 ATOM 2403 C C . THR A 1 302 ? -15.922 8.976 15.477 1.00 128.45 ? 301 THR A C 1 ATOM 2404 O O . THR A 1 302 ? -15.612 9.697 14.521 1.00 125.92 ? 301 THR A O 1 ATOM 2405 C CB . THR A 1 302 ? -16.792 9.671 17.718 1.00 129.46 ? 301 THR A CB 1 ATOM 2406 O OG1 . THR A 1 302 ? -17.539 10.715 17.081 1.00 131.99 ? 301 THR A OG1 1 ATOM 2407 C CG2 . THR A 1 302 ? -16.434 10.094 19.134 1.00 128.43 ? 301 THR A CG2 1 ATOM 2408 N N . GLY A 1 303 ? -16.613 7.846 15.352 1.00 130.59 ? 302 GLY A N 1 ATOM 2409 C CA . GLY A 1 303 ? -17.142 7.383 14.073 1.00 133.30 ? 302 GLY A CA 1 ATOM 2410 C C . GLY A 1 303 ? -16.114 6.726 13.169 1.00 133.67 ? 302 GLY A C 1 ATOM 2411 O O . GLY A 1 303 ? -16.370 6.542 11.978 1.00 138.22 ? 302 GLY A O 1 ATOM 2412 N N . VAL A 1 304 ? -14.958 6.368 13.725 1.00 129.97 ? 303 VAL A N 1 ATOM 2413 C CA . VAL A 1 304 ? -13.880 5.753 12.949 1.00 126.93 ? 303 VAL A CA 1 ATOM 2414 C C . VAL A 1 304 ? -13.608 4.362 13.517 1.00 124.46 ? 303 VAL A C 1 ATOM 2415 O O . VAL A 1 304 ? -13.374 4.226 14.715 1.00 122.85 ? 303 VAL A O 1 ATOM 2416 C CB . VAL A 1 304 ? -12.582 6.590 13.028 1.00 124.04 ? 303 VAL A CB 1 ATOM 2417 C CG1 . VAL A 1 304 ? -11.503 6.013 12.118 1.00 121.87 ? 303 VAL A CG1 1 ATOM 2418 C CG2 . VAL A 1 304 ? -12.860 8.044 12.667 1.00 124.44 ? 303 VAL A CG2 1 ATOM 2419 N N . PRO A 1 305 ? -13.624 3.326 12.660 1.00 125.68 ? 304 PRO A N 1 ATOM 2420 C CA . PRO A 1 305 ? -13.404 1.982 13.191 1.00 125.72 ? 304 PRO A CA 1 ATOM 2421 C C . PRO A 1 305 ? -12.058 1.886 13.899 1.00 121.77 ? 304 PRO A C 1 ATOM 2422 O O . PRO A 1 305 ? -11.035 2.207 13.303 1.00 116.78 ? 304 PRO A O 1 ATOM 2423 C CB . PRO A 1 305 ? -13.421 1.098 11.937 1.00 128.94 ? 304 PRO A CB 1 ATOM 2424 C CG . PRO A 1 305 ? -13.064 2.011 10.815 1.00 128.39 ? 304 PRO A CG 1 ATOM 2425 C CD . PRO A 1 305 ? -13.664 3.334 11.185 1.00 127.94 ? 304 PRO A CD 1 ATOM 2426 N N . THR A 1 306 ? -12.075 1.459 15.159 1.00 122.14 ? 305 THR A N 1 ATOM 2427 C CA . THR A 1 306 ? -10.869 1.389 15.982 1.00 122.35 ? 305 THR A CA 1 ATOM 2428 C C . THR A 1 306 ? -10.716 -0.034 16.526 1.00 127.86 ? 305 THR A C 1 ATOM 2429 O O . THR A 1 306 ? -11.675 -0.595 17.047 1.00 131.78 ? 305 THR A O 1 ATOM 2430 C CB . THR A 1 306 ? -10.979 2.354 17.178 1.00 121.94 ? 305 THR A CB 1 ATOM 2431 O OG1 . THR A 1 306 ? -11.451 3.631 16.728 1.00 122.23 ? 305 THR A OG1 1 ATOM 2432 C CG2 . THR A 1 306 ? -9.634 2.521 17.872 1.00 121.38 ? 305 THR A CG2 1 ATOM 2433 N N . PRO A 1 307 ? -9.510 -0.625 16.420 1.00 132.40 ? 306 PRO A N 1 ATOM 2434 C CA . PRO A 1 307 ? -9.344 -1.996 16.926 1.00 133.65 ? 306 PRO A CA 1 ATOM 2435 C C . PRO A 1 307 ? -9.760 -2.122 18.392 1.00 133.37 ? 306 PRO A C 1 ATOM 2436 O O . PRO A 1 307 ? -9.339 -1.311 19.218 1.00 129.90 ? 306 PRO A O 1 ATOM 2437 C CB . PRO A 1 307 ? -7.841 -2.262 16.756 1.00 133.35 ? 306 PRO A CB 1 ATOM 2438 C CG . PRO A 1 307 ? -7.211 -0.921 16.582 1.00 132.83 ? 306 PRO A CG 1 ATOM 2439 C CD . PRO A 1 307 ? -8.244 -0.076 15.904 1.00 132.26 ? 306 PRO A CD 1 ATOM 2440 N N . ASP A 1 308 ? -10.592 -3.123 18.684 1.00 137.10 ? 307 ASP A N 1 ATOM 2441 C CA . ASP A 1 308 ? -11.175 -3.338 20.016 1.00 140.84 ? 307 ASP A CA 1 ATOM 2442 C C . ASP A 1 308 ? -10.670 -4.634 20.659 1.00 140.37 ? 307 ASP A C 1 ATOM 2443 O O . ASP A 1 308 ? -10.304 -4.649 21.837 1.00 139.08 ? 307 ASP A O 1 ATOM 2444 C CB . ASP A 1 308 ? -12.705 -3.380 19.905 1.00 146.41 ? 307 ASP A CB 1 ATOM 2445 C CG . ASP A 1 308 ? -13.386 -3.706 21.227 1.00 151.05 ? 307 ASP A CG 1 ATOM 2446 O OD1 . ASP A 1 308 ? -12.962 -3.173 22.275 1.00 151.11 ? 307 ASP A OD1 1 ATOM 2447 O OD2 . ASP A 1 308 ? -14.357 -4.495 21.214 1.00 157.08 ? 307 ASP A OD2 1 ATOM 2448 N N . SER A 1 309 ? -10.677 -5.721 19.889 1.00 140.26 ? 308 SER A N 1 ATOM 2449 C CA . SER A 1 309 ? -10.176 -7.010 20.366 1.00 139.71 ? 308 SER A CA 1 ATOM 2450 C C . SER A 1 309 ? -9.647 -7.830 19.196 1.00 135.91 ? 308 SER A C 1 ATOM 2451 O O . SER A 1 309 ? -9.921 -7.509 18.038 1.00 130.49 ? 308 SER A O 1 ATOM 2452 C CB . SER A 1 309 ? -11.271 -7.776 21.115 1.00 144.77 ? 308 SER A CB 1 ATOM 2453 O OG . SER A 1 309 ? -12.459 -7.863 20.348 1.00 148.76 ? 308 SER A OG 1 ATOM 2454 N N . PHE A 1 310 ? -8.894 -8.884 19.512 1.00 135.88 ? 309 PHE A N 1 ATOM 2455 C CA . PHE A 1 310 ? -8.170 -9.656 18.505 1.00 138.95 ? 309 PHE A CA 1 ATOM 2456 C C . PHE A 1 310 ? -8.332 -11.154 18.686 1.00 144.92 ? 309 PHE A C 1 ATOM 2457 O O . PHE A 1 310 ? -8.315 -11.656 19.810 1.00 146.97 ? 309 PHE A O 1 ATOM 2458 C CB . PHE A 1 310 ? -6.684 -9.321 18.571 1.00 136.99 ? 309 PHE A CB 1 ATOM 2459 C CG . PHE A 1 310 ? -6.398 -7.856 18.480 1.00 137.38 ? 309 PHE A CG 1 ATOM 2460 C CD1 . PHE A 1 310 ? -6.384 -7.220 17.248 1.00 138.98 ? 309 PHE A CD1 1 ATOM 2461 C CD2 . PHE A 1 310 ? -6.160 -7.108 19.622 1.00 137.13 ? 309 PHE A CD2 1 ATOM 2462 C CE1 . PHE A 1 310 ? -6.125 -5.863 17.153 1.00 137.63 ? 309 PHE A CE1 1 ATOM 2463 C CE2 . PHE A 1 310 ? -5.900 -5.751 19.536 1.00 137.06 ? 309 PHE A CE2 1 ATOM 2464 C CZ . PHE A 1 310 ? -5.884 -5.126 18.300 1.00 137.40 ? 309 PHE A CZ 1 ATOM 2465 N N . TYR A 1 311 ? -8.479 -11.862 17.568 1.00 148.91 ? 310 TYR A N 1 ATOM 2466 C CA . TYR A 1 311 ? -8.417 -13.317 17.576 1.00 154.55 ? 310 TYR A CA 1 ATOM 2467 C C . TYR A 1 311 ? -7.175 -13.777 16.827 1.00 147.13 ? 310 TYR A C 1 ATOM 2468 O O . TYR A 1 311 ? -6.986 -13.440 15.655 1.00 144.35 ? 310 TYR A O 1 ATOM 2469 C CB . TYR A 1 311 ? -9.658 -13.940 16.939 1.00 166.87 ? 310 TYR A CB 1 ATOM 2470 C CG . TYR A 1 311 ? -9.564 -15.453 16.841 1.00 181.29 ? 310 TYR A CG 1 ATOM 2471 C CD1 . TYR A 1 311 ? -9.712 -16.257 17.971 1.00 186.41 ? 310 TYR A CD1 1 ATOM 2472 C CD2 . TYR A 1 311 ? -9.305 -16.080 15.622 1.00 187.70 ? 310 TYR A CD2 1 ATOM 2473 C CE1 . TYR A 1 311 ? -9.618 -17.638 17.889 1.00 190.32 ? 310 TYR A CE1 1 ATOM 2474 C CE2 . TYR A 1 311 ? -9.209 -17.460 15.529 1.00 191.45 ? 310 TYR A CE2 1 ATOM 2475 C CZ . TYR A 1 311 ? -9.366 -18.234 16.664 1.00 193.68 ? 310 TYR A CZ 1 ATOM 2476 O OH . TYR A 1 311 ? -9.272 -19.604 16.575 1.00 199.18 ? 310 TYR A OH 1 ATOM 2477 N N . TYR A 1 312 ? -6.342 -14.558 17.510 1.00 142.24 ? 311 TYR A N 1 ATOM 2478 C CA . TYR A 1 312 ? -5.154 -15.149 16.906 1.00 139.86 ? 311 TYR A CA 1 ATOM 2479 C C . TYR A 1 312 ? -5.402 -16.606 16.556 1.00 142.87 ? 311 TYR A C 1 ATOM 2480 O O . TYR A 1 312 ? -5.694 -17.419 17.431 1.00 145.77 ? 311 TYR A O 1 ATOM 2481 C CB . TYR A 1 312 ? -3.963 -15.037 17.855 1.00 137.94 ? 311 TYR A CB 1 ATOM 2482 C CG . TYR A 1 312 ? -3.270 -13.705 17.764 1.00 135.72 ? 311 TYR A CG 1 ATOM 2483 C CD1 . TYR A 1 312 ? -2.259 -13.497 16.835 1.00 136.44 ? 311 TYR A CD1 1 ATOM 2484 C CD2 . TYR A 1 312 ? -3.631 -12.648 18.593 1.00 131.90 ? 311 TYR A CD2 1 ATOM 2485 C CE1 . TYR A 1 312 ? -1.619 -12.276 16.736 1.00 133.38 ? 311 TYR A CE1 1 ATOM 2486 C CE2 . TYR A 1 312 ? -2.995 -11.423 18.501 1.00 131.61 ? 311 TYR A CE2 1 ATOM 2487 C CZ . TYR A 1 312 ? -1.987 -11.244 17.570 1.00 132.15 ? 311 TYR A CZ 1 ATOM 2488 O OH . TYR A 1 312 ? -1.345 -10.031 17.459 1.00 133.70 ? 311 TYR A OH 1 ATOM 2489 N N . GLU A 1 313 ? -5.296 -16.922 15.268 1.00 143.27 ? 312 GLU A N 1 ATOM 2490 C CA . GLU A 1 313 ? -5.382 -18.298 14.791 1.00 145.99 ? 312 GLU A CA 1 ATOM 2491 C C . GLU A 1 313 ? -4.109 -19.041 15.189 1.00 146.47 ? 312 GLU A C 1 ATOM 2492 O O . GLU A 1 313 ? -4.141 -20.232 15.518 1.00 150.44 ? 312 GLU A O 1 ATOM 2493 C CB . GLU A 1 313 ? -5.528 -18.308 13.267 1.00 148.37 ? 312 GLU A CB 1 ATOM 2494 C CG . GLU A 1 313 ? -5.692 -19.693 12.650 1.00 152.20 ? 312 GLU A CG 1 ATOM 2495 C CD . GLU A 1 313 ? -5.427 -19.716 11.155 1.00 152.84 ? 312 GLU A CD 1 ATOM 2496 O OE1 . GLU A 1 313 ? -4.887 -18.724 10.617 1.00 149.62 ? 312 GLU A OE1 1 ATOM 2497 O OE2 . GLU A 1 313 ? -5.747 -20.743 10.517 1.00 155.84 ? 312 GLU A OE2 1 ATOM 2498 N N . SER A 1 314 ? -2.988 -18.327 15.126 1.00 144.28 ? 313 SER A N 1 ATOM 2499 C CA . SER A 1 314 ? -1.702 -18.836 15.588 1.00 144.40 ? 313 SER A CA 1 ATOM 2500 C C . SER A 1 314 ? -0.963 -17.738 16.342 1.00 139.72 ? 313 SER A C 1 ATOM 2501 O O . SER A 1 314 ? -0.845 -16.609 15.867 1.00 140.11 ? 313 SER A O 1 ATOM 2502 C CB . SER A 1 314 ? -0.860 -19.323 14.413 1.00 147.83 ? 313 SER A CB 1 ATOM 2503 O OG . SER A 1 314 ? 0.388 -19.820 14.864 1.00 149.78 ? 313 SER A OG 1 ATOM 2504 N N . PHE A 1 315 ? -0.454 -18.090 17.515 1.00 138.77 ? 314 PHE A N 1 ATOM 2505 C CA . PHE A 1 315 ? 0.098 -17.125 18.454 1.00 135.90 ? 314 PHE A CA 1 ATOM 2506 C C . PHE A 1 315 ? 1.612 -17.332 18.571 1.00 136.78 ? 314 PHE A C 1 ATOM 2507 O O . PHE A 1 315 ? 2.047 -18.472 18.737 1.00 141.81 ? 314 PHE A O 1 ATOM 2508 C CB . PHE A 1 315 ? -0.566 -17.359 19.813 1.00 136.29 ? 314 PHE A CB 1 ATOM 2509 C CG . PHE A 1 315 ? -0.520 -16.175 20.727 1.00 134.65 ? 314 PHE A CG 1 ATOM 2510 C CD1 . PHE A 1 315 ? -1.171 -15.001 20.388 1.00 133.89 ? 314 PHE A CD1 1 ATOM 2511 C CD2 . PHE A 1 315 ? 0.148 -16.243 21.942 1.00 137.02 ? 314 PHE A CD2 1 ATOM 2512 C CE1 . PHE A 1 315 ? -1.144 -13.906 21.234 1.00 133.68 ? 314 PHE A CE1 1 ATOM 2513 C CE2 . PHE A 1 315 ? 0.178 -15.153 22.794 1.00 136.37 ? 314 PHE A CE2 1 ATOM 2514 C CZ . PHE A 1 315 ? -0.468 -13.981 22.439 1.00 134.37 ? 314 PHE A CZ 1 ATOM 2515 N N . PRO A 1 316 ? 2.426 -16.276 18.461 1.00 132.70 ? 315 PRO A N 1 ATOM 2516 C CA . PRO A 1 316 ? 2.011 -14.920 18.098 1.00 131.98 ? 315 PRO A CA 1 ATOM 2517 C C . PRO A 1 316 ? 2.576 -14.463 16.742 1.00 132.12 ? 315 PRO A C 1 ATOM 2518 O O . PRO A 1 316 ? 2.607 -13.263 16.460 1.00 132.56 ? 315 PRO A O 1 ATOM 2519 C CB . PRO A 1 316 ? 2.605 -14.087 19.231 1.00 131.08 ? 315 PRO A CB 1 ATOM 2520 C CG . PRO A 1 316 ? 3.873 -14.797 19.570 1.00 131.46 ? 315 PRO A CG 1 ATOM 2521 C CD . PRO A 1 316 ? 3.643 -16.262 19.296 1.00 132.34 ? 315 PRO A CD 1 ATOM 2522 N N . ASP A 1 317 ? 2.987 -15.409 15.900 1.00 135.79 ? 316 ASP A N 1 ATOM 2523 C CA . ASP A 1 317 ? 3.709 -15.094 14.661 1.00 140.38 ? 316 ASP A CA 1 ATOM 2524 C C . ASP A 1 317 ? 2.821 -14.922 13.423 1.00 143.32 ? 316 ASP A C 1 ATOM 2525 O O . ASP A 1 317 ? 3.329 -14.705 12.319 1.00 143.66 ? 316 ASP A O 1 ATOM 2526 C CB . ASP A 1 317 ? 4.743 -16.189 14.374 1.00 145.03 ? 316 ASP A CB 1 ATOM 2527 C CG . ASP A 1 317 ? 5.721 -16.388 15.519 1.00 147.00 ? 316 ASP A CG 1 ATOM 2528 O OD1 . ASP A 1 317 ? 6.243 -15.376 16.042 1.00 141.79 ? 316 ASP A OD1 1 ATOM 2529 O OD2 . ASP A 1 317 ? 5.970 -17.559 15.887 1.00 150.34 ? 316 ASP A OD2 1 ATOM 2530 N N . ARG A 1 318 ? 1.506 -15.024 13.605 1.00 146.09 ? 317 ARG A N 1 ATOM 2531 C CA . ARG A 1 318 ? 0.547 -14.913 12.512 1.00 150.66 ? 317 ARG A CA 1 ATOM 2532 C C . ARG A 1 318 ? -0.362 -13.718 12.806 1.00 145.16 ? 317 ARG A C 1 ATOM 2533 O O . ARG A 1 318 ? -0.757 -13.513 13.949 1.00 142.68 ? 317 ARG A O 1 ATOM 2534 C CB . ARG A 1 318 ? -0.251 -16.215 12.431 1.00 158.79 ? 317 ARG A CB 1 ATOM 2535 C CG . ARG A 1 318 ? -1.030 -16.423 11.153 1.00 166.27 ? 317 ARG A CG 1 ATOM 2536 C CD . ARG A 1 318 ? -0.134 -16.740 9.959 1.00 172.28 ? 317 ARG A CD 1 ATOM 2537 N NE . ARG A 1 318 ? -0.915 -17.086 8.774 1.00 184.03 ? 317 ARG A NE 1 ATOM 2538 C CZ . ARG A 1 318 ? -1.578 -16.214 8.013 1.00 195.09 ? 317 ARG A CZ 1 ATOM 2539 N NH1 . ARG A 1 318 ? -1.577 -14.912 8.298 1.00 199.79 ? 317 ARG A NH1 1 ATOM 2540 N NH2 . ARG A 1 318 ? -2.255 -16.649 6.955 1.00 201.31 ? 317 ARG A NH2 1 ATOM 2541 N N . ASP A 1 319 ? -0.665 -12.915 11.788 1.00 142.91 ? 318 ASP A N 1 ATOM 2542 C CA . ASP A 1 319 ? -1.482 -11.718 11.991 1.00 143.62 ? 318 ASP A CA 1 ATOM 2543 C C . ASP A 1 319 ? -2.904 -12.087 12.413 1.00 142.48 ? 318 ASP A C 1 ATOM 2544 O O . ASP A 1 319 ? -3.470 -13.054 11.907 1.00 142.64 ? 318 ASP A O 1 ATOM 2545 C CB . ASP A 1 319 ? -1.507 -10.848 10.734 1.00 147.36 ? 318 ASP A CB 1 ATOM 2546 C CG . ASP A 1 319 ? -0.194 -10.126 10.499 1.00 149.95 ? 318 ASP A CG 1 ATOM 2547 O OD1 . ASP A 1 319 ? 0.418 -9.642 11.480 1.00 146.55 ? 318 ASP A OD1 1 ATOM 2548 O OD2 . ASP A 1 319 ? 0.224 -10.038 9.325 1.00 155.94 ? 318 ASP A OD2 1 ATOM 2549 N N . PRO A 1 320 ? -3.484 -11.318 13.351 1.00 140.07 ? 319 PRO A N 1 ATOM 2550 C CA . PRO A 1 320 ? -4.777 -11.686 13.907 1.00 140.86 ? 319 PRO A CA 1 ATOM 2551 C C . PRO A 1 320 ? -5.957 -11.110 13.143 1.00 140.64 ? 319 PRO A C 1 ATOM 2552 O O . PRO A 1 320 ? -5.796 -10.198 12.332 1.00 134.36 ? 319 PRO A O 1 ATOM 2553 C CB . PRO A 1 320 ? -4.728 -11.056 15.294 1.00 139.48 ? 319 PRO A CB 1 ATOM 2554 C CG . PRO A 1 320 ? -3.962 -9.795 15.072 1.00 138.31 ? 319 PRO A CG 1 ATOM 2555 C CD . PRO A 1 320 ? -2.972 -10.080 13.969 1.00 138.03 ? 319 PRO A CD 1 ATOM 2556 N N . LYS A 1 321 ? -7.139 -11.643 13.427 1.00 144.80 ? 320 LYS A N 1 ATOM 2557 C CA . LYS A 1 321 ? -8.376 -11.061 12.926 1.00 148.96 ? 320 LYS A CA 1 ATOM 2558 C C . LYS A 1 321 ? -8.766 -10.002 13.940 1.00 145.34 ? 320 LYS A C 1 ATOM 2559 O O . LYS A 1 321 ? -8.539 -10.179 15.136 1.00 143.15 ? 320 LYS A O 1 ATOM 2560 C CB . LYS A 1 321 ? -9.470 -12.123 12.791 1.00 158.57 ? 320 LYS A CB 1 ATOM 2561 C CG . LYS A 1 321 ? -10.748 -11.639 12.123 1.00 166.12 ? 320 LYS A CG 1 ATOM 2562 C CD . LYS A 1 321 ? -11.225 -12.618 11.058 1.00 173.05 ? 320 LYS A CD 1 ATOM 2563 C CE . LYS A 1 321 ? -12.643 -12.307 10.607 1.00 177.63 ? 320 LYS A CE 1 ATOM 2564 N NZ . LYS A 1 321 ? -13.219 -13.396 9.769 1.00 180.62 ? 320 LYS A NZ 1 ATOM 2565 N N . ILE A 1 322 ? -9.330 -8.899 13.461 1.00 144.83 ? 321 ILE A N 1 ATOM 2566 C CA . ILE A 1 322 ? -9.565 -7.733 14.306 1.00 144.81 ? 321 ILE A CA 1 ATOM 2567 C C . ILE A 1 322 ? -11.052 -7.414 14.406 1.00 147.52 ? 321 ILE A C 1 ATOM 2568 O O . ILE A 1 322 ? -11.744 -7.343 13.391 1.00 152.02 ? 321 ILE A O 1 ATOM 2569 C CB . ILE A 1 322 ? -8.837 -6.488 13.747 1.00 143.53 ? 321 ILE A CB 1 ATOM 2570 C CG1 . ILE A 1 322 ? -7.341 -6.781 13.558 1.00 143.42 ? 321 ILE A CG1 1 ATOM 2571 C CG2 . ILE A 1 322 ? -9.042 -5.291 14.671 1.00 142.28 ? 321 ILE A CG2 1 ATOM 2572 C CD1 . ILE A 1 322 ? -6.582 -5.701 12.815 1.00 142.45 ? 321 ILE A CD1 1 ATOM 2573 N N . CYS A 1 323 ? -11.528 -7.225 15.635 1.00 149.25 ? 322 CYS A N 1 ATOM 2574 C CA . CYS A 1 323 ? -12.877 -6.715 15.890 1.00 152.60 ? 322 CYS A CA 1 ATOM 2575 C C . CYS A 1 323 ? -12.773 -5.225 16.213 1.00 147.81 ? 322 CYS A C 1 ATOM 2576 O O . CYS A 1 323 ? -11.892 -4.808 16.966 1.00 143.18 ? 322 CYS A O 1 ATOM 2577 C CB . CYS A 1 323 ? -13.521 -7.463 17.059 1.00 157.61 ? 322 CYS A CB 1 ATOM 2578 S SG . CYS A 1 323 ? -15.245 -7.014 17.378 1.00 166.68 ? 322 CYS A SG 1 ATOM 2579 N N . PHE A 1 324 ? -13.673 -4.426 15.644 1.00 146.18 ? 323 PHE A N 1 ATOM 2580 C CA . PHE A 1 324 ? -13.579 -2.973 15.744 1.00 142.53 ? 323 PHE A CA 1 ATOM 2581 C C . PHE A 1 324 ? -14.663 -2.358 16.616 1.00 144.32 ? 323 PHE A C 1 ATOM 2582 O O . PHE A 1 324 ? -15.806 -2.819 16.632 1.00 146.92 ? 323 PHE A O 1 ATOM 2583 C CB . PHE A 1 324 ? -13.624 -2.348 14.353 1.00 141.96 ? 323 PHE A CB 1 ATOM 2584 C CG . PHE A 1 324 ? -12.414 -2.649 13.522 1.00 141.18 ? 323 PHE A CG 1 ATOM 2585 C CD1 . PHE A 1 324 ? -12.326 -3.835 12.805 1.00 141.47 ? 323 PHE A CD1 1 ATOM 2586 C CD2 . PHE A 1 324 ? -11.359 -1.751 13.461 1.00 139.45 ? 323 PHE A CD2 1 ATOM 2587 C CE1 . PHE A 1 324 ? -11.210 -4.117 12.038 1.00 139.96 ? 323 PHE A CE1 1 ATOM 2588 C CE2 . PHE A 1 324 ? -10.239 -2.026 12.695 1.00 138.96 ? 323 PHE A CE2 1 ATOM 2589 C CZ . PHE A 1 324 ? -10.165 -3.211 11.982 1.00 138.66 ? 323 PHE A CZ 1 ATOM 2590 N N . GLY A 1 325 ? -14.279 -1.313 17.342 1.00 144.87 ? 324 GLY A N 1 ATOM 2591 C CA . GLY A 1 325 ? -15.204 -0.497 18.119 1.00 146.06 ? 324 GLY A CA 1 ATOM 2592 C C . GLY A 1 325 ? -15.086 0.959 17.707 1.00 143.29 ? 324 GLY A C 1 ATOM 2593 O O . GLY A 1 325 ? -14.527 1.275 16.653 1.00 139.88 ? 324 GLY A O 1 ATOM 2594 N N . ASP A 1 326 ? -15.610 1.850 18.541 1.00 143.66 ? 325 ASP A N 1 ATOM 2595 C CA . ASP A 1 326 ? -15.644 3.268 18.209 1.00 143.97 ? 325 ASP A CA 1 ATOM 2596 C C . ASP A 1 326 ? -14.392 3.981 18.707 1.00 136.91 ? 325 ASP A C 1 ATOM 2597 O O . ASP A 1 326 ? -13.709 3.503 19.615 1.00 130.85 ? 325 ASP A O 1 ATOM 2598 C CB . ASP A 1 326 ? -16.902 3.925 18.792 1.00 149.64 ? 325 ASP A CB 1 ATOM 2599 C CG . ASP A 1 326 ? -17.366 5.136 17.986 1.00 152.07 ? 325 ASP A CG 1 ATOM 2600 O OD1 . ASP A 1 326 ? -16.619 5.603 17.098 1.00 148.93 ? 325 ASP A OD1 1 ATOM 2601 O OD2 . ASP A 1 326 ? -18.489 5.622 18.244 1.00 157.59 ? 325 ASP A OD2 1 ATOM 2602 N N . GLY A 1 327 ? -14.107 5.126 18.092 1.00 131.87 ? 326 GLY A N 1 ATOM 2603 C CA . GLY A 1 327 ? -12.933 5.931 18.411 1.00 127.45 ? 326 GLY A CA 1 ATOM 2604 C C . GLY A 1 327 ? -12.501 6.728 17.197 1.00 125.26 ? 326 GLY A C 1 ATOM 2605 O O . GLY A 1 327 ? -13.322 7.051 16.328 1.00 124.87 ? 326 GLY A O 1 ATOM 2606 N N . ASP A 1 328 ? -11.206 7.026 17.131 1.00 124.57 ? 327 ASP A N 1 ATOM 2607 C CA . ASP A 1 328 ? -10.636 7.845 16.053 1.00 126.37 ? 327 ASP A CA 1 ATOM 2608 C C . ASP A 1 328 ? -9.743 7.050 15.090 1.00 127.10 ? 327 ASP A C 1 ATOM 2609 O O . ASP A 1 328 ? -9.047 7.639 14.259 1.00 127.56 ? 327 ASP A O 1 ATOM 2610 C CB . ASP A 1 328 ? -9.862 9.037 16.644 1.00 124.11 ? 327 ASP A CB 1 ATOM 2611 C CG . ASP A 1 328 ? -8.741 8.613 17.588 1.00 121.73 ? 327 ASP A CG 1 ATOM 2612 O OD1 . ASP A 1 328 ? -8.371 7.419 17.603 1.00 120.74 ? 327 ASP A OD1 1 ATOM 2613 O OD2 . ASP A 1 328 ? -8.226 9.482 18.319 1.00 119.53 ? 327 ASP A OD2 1 ATOM 2614 N N . GLY A 1 329 ? -9.780 5.722 15.190 1.00 129.61 ? 328 GLY A N 1 ATOM 2615 C CA . GLY A 1 329 ? -8.931 4.857 14.371 1.00 131.30 ? 328 GLY A CA 1 ATOM 2616 C C . GLY A 1 329 ? -7.768 4.268 15.146 1.00 131.25 ? 328 GLY A C 1 ATOM 2617 O O . GLY A 1 329 ? -7.250 3.210 14.784 1.00 133.38 ? 328 GLY A O 1 ATOM 2618 N N . THR A 1 330 ? -7.359 4.953 16.211 1.00 129.65 ? 329 THR A N 1 ATOM 2619 C CA . THR A 1 330 ? -6.261 4.501 17.055 1.00 128.85 ? 329 THR A CA 1 ATOM 2620 C C . THR A 1 330 ? -6.706 4.466 18.521 1.00 124.83 ? 329 THR A C 1 ATOM 2621 O O . THR A 1 330 ? -6.670 3.411 19.165 1.00 122.87 ? 329 THR A O 1 ATOM 2622 C CB . THR A 1 330 ? -5.028 5.416 16.875 1.00 132.12 ? 329 THR A CB 1 ATOM 2623 O OG1 . THR A 1 330 ? -4.654 5.454 15.486 1.00 135.91 ? 329 THR A OG1 1 ATOM 2624 C CG2 . THR A 1 330 ? -3.852 4.920 17.711 1.00 131.54 ? 329 THR A CG2 1 ATOM 2625 N N . VAL A 1 331 ? -7.127 5.619 19.034 1.00 122.57 ? 330 VAL A N 1 ATOM 2626 C CA . VAL A 1 331 ? -7.581 5.743 20.419 1.00 124.93 ? 330 VAL A CA 1 ATOM 2627 C C . VAL A 1 331 ? -9.049 5.352 20.569 1.00 127.21 ? 330 VAL A C 1 ATOM 2628 O O . VAL A 1 331 ? -9.928 5.898 19.898 1.00 127.03 ? 330 VAL A O 1 ATOM 2629 C CB . VAL A 1 331 ? -7.384 7.176 20.956 1.00 125.11 ? 330 VAL A CB 1 ATOM 2630 C CG1 . VAL A 1 331 ? -7.970 7.316 22.358 1.00 125.07 ? 330 VAL A CG1 1 ATOM 2631 C CG2 . VAL A 1 331 ? -5.906 7.540 20.956 1.00 124.03 ? 330 VAL A CG2 1 ATOM 2632 N N . ASN A 1 332 ? -9.299 4.418 21.477 1.00 131.10 ? 331 ASN A N 1 ATOM 2633 C CA . ASN A 1 332 ? -10.638 3.906 21.691 1.00 133.86 ? 331 ASN A CA 1 ATOM 2634 C C . ASN A 1 332 ? -11.490 4.971 22.347 1.00 132.75 ? 331 ASN A C 1 ATOM 2635 O O . ASN A 1 332 ? -11.014 5.726 23.189 1.00 127.02 ? 331 ASN A O 1 ATOM 2636 C CB . ASN A 1 332 ? -10.593 2.648 22.558 1.00 134.79 ? 331 ASN A CB 1 ATOM 2637 C CG . ASN A 1 332 ? -9.760 1.547 21.932 1.00 136.64 ? 331 ASN A CG 1 ATOM 2638 O OD1 . ASN A 1 332 ? -8.698 1.191 22.441 1.00 137.92 ? 331 ASN A OD1 1 ATOM 2639 N ND2 . ASN A 1 332 ? -10.227 1.015 20.810 1.00 139.37 ? 331 ASN A ND2 1 ATOM 2640 N N . LEU A 1 333 ? -12.754 5.027 21.948 1.00 135.36 ? 332 LEU A N 1 ATOM 2641 C CA . LEU A 1 333 ? -13.721 5.946 22.541 1.00 137.23 ? 332 LEU A CA 1 ATOM 2642 C C . LEU A 1 333 ? -13.751 5.848 24.067 1.00 136.40 ? 332 LEU A C 1 ATOM 2643 O O . LEU A 1 333 ? -13.880 6.855 24.761 1.00 138.46 ? 332 LEU A O 1 ATOM 2644 C CB . LEU A 1 333 ? -15.118 5.650 21.992 1.00 141.37 ? 332 LEU A CB 1 ATOM 2645 C CG . LEU A 1 333 ? -16.285 6.414 22.624 1.00 144.89 ? 332 LEU A CG 1 ATOM 2646 C CD1 . LEU A 1 333 ? -16.100 7.915 22.455 1.00 144.30 ? 332 LEU A CD1 1 ATOM 2647 C CD2 . LEU A 1 333 ? -17.603 5.954 22.019 1.00 148.23 ? 332 LEU A CD2 1 ATOM 2648 N N . LYS A 1 334 ? -13.631 4.633 24.589 1.00 134.18 ? 333 LYS A N 1 ATOM 2649 C CA . LYS A 1 334 ? -13.704 4.410 26.028 1.00 134.17 ? 333 LYS A CA 1 ATOM 2650 C C . LYS A 1 334 ? -12.685 5.224 26.833 1.00 132.98 ? 333 LYS A C 1 ATOM 2651 O O . LYS A 1 334 ? -12.875 5.440 28.026 1.00 130.90 ? 333 LYS A O 1 ATOM 2652 C CB . LYS A 1 334 ? -13.574 2.918 26.326 1.00 133.67 ? 333 LYS A CB 1 ATOM 2653 C CG . LYS A 1 334 ? -14.757 2.117 25.802 1.00 137.53 ? 333 LYS A CG 1 ATOM 2654 C CD . LYS A 1 334 ? -14.358 0.741 25.302 1.00 140.02 ? 333 LYS A CD 1 ATOM 2655 C CE . LYS A 1 334 ? -15.531 0.045 24.628 1.00 143.99 ? 333 LYS A CE 1 ATOM 2656 N NZ . LYS A 1 334 ? -15.330 -1.428 24.512 1.00 146.43 ? 333 LYS A NZ 1 ATOM 2657 N N . SER A 1 335 ? -11.617 5.676 26.175 1.00 132.40 ? 334 SER A N 1 ATOM 2658 C CA . SER A 1 335 ? -10.639 6.579 26.785 1.00 127.99 ? 334 SER A CA 1 ATOM 2659 C C . SER A 1 335 ? -11.254 7.892 27.280 1.00 124.19 ? 334 SER A C 1 ATOM 2660 O O . SER A 1 335 ? -10.854 8.404 28.325 1.00 125.97 ? 334 SER A O 1 ATOM 2661 C CB . SER A 1 335 ? -9.514 6.887 25.792 1.00 127.73 ? 334 SER A CB 1 ATOM 2662 O OG . SER A 1 335 ? -8.938 5.693 25.282 1.00 131.27 ? 334 SER A OG 1 ATOM 2663 N N . ALA A 1 336 ? -12.233 8.421 26.546 1.00 120.15 ? 335 ALA A N 1 ATOM 2664 C CA . ALA A 1 336 ? -12.861 9.707 26.888 1.00 119.51 ? 335 ALA A CA 1 ATOM 2665 C C . ALA A 1 336 ? -13.685 9.702 28.188 1.00 121.13 ? 335 ALA A C 1 ATOM 2666 O O . ALA A 1 336 ? -14.156 10.753 28.624 1.00 116.04 ? 335 ALA A O 1 ATOM 2667 C CB . ALA A 1 336 ? -13.717 10.197 25.731 1.00 118.52 ? 335 ALA A CB 1 ATOM 2668 N N . LEU A 1 337 ? -13.859 8.532 28.800 1.00 125.54 ? 336 LEU A N 1 ATOM 2669 C CA . LEU A 1 337 ? -14.544 8.419 30.089 1.00 132.31 ? 336 LEU A CA 1 ATOM 2670 C C . LEU A 1 337 ? -13.829 9.165 31.212 1.00 134.99 ? 336 LEU A C 1 ATOM 2671 O O . LEU A 1 337 ? -14.473 9.672 32.127 1.00 134.00 ? 336 LEU A O 1 ATOM 2672 C CB . LEU A 1 337 ? -14.670 6.950 30.497 1.00 135.81 ? 336 LEU A CB 1 ATOM 2673 C CG . LEU A 1 337 ? -15.569 6.075 29.627 1.00 140.31 ? 336 LEU A CG 1 ATOM 2674 C CD1 . LEU A 1 337 ? -15.422 4.616 30.034 1.00 141.67 ? 336 LEU A CD1 1 ATOM 2675 C CD2 . LEU A 1 337 ? -17.019 6.530 29.715 1.00 143.99 ? 336 LEU A CD2 1 ATOM 2676 N N . GLN A 1 338 ? -12.500 9.207 31.155 1.00 138.25 ? 337 GLN A N 1 ATOM 2677 C CA . GLN A 1 338 ? -11.699 9.841 32.207 1.00 139.31 ? 337 GLN A CA 1 ATOM 2678 C C . GLN A 1 338 ? -12.008 11.330 32.317 1.00 137.63 ? 337 GLN A C 1 ATOM 2679 O O . GLN A 1 338 ? -12.126 11.866 33.421 1.00 136.34 ? 337 GLN A O 1 ATOM 2680 C CB . GLN A 1 338 ? -10.202 9.628 31.944 1.00 140.61 ? 337 GLN A CB 1 ATOM 2681 C CG . GLN A 1 338 ? -9.274 10.133 33.044 1.00 140.64 ? 337 GLN A CG 1 ATOM 2682 C CD . GLN A 1 338 ? -9.474 9.425 34.372 1.00 143.64 ? 337 GLN A CD 1 ATOM 2683 O OE1 . GLN A 1 338 ? -9.990 8.307 34.426 1.00 148.35 ? 337 GLN A OE1 1 ATOM 2684 N NE2 . GLN A 1 338 ? -9.058 10.073 35.454 1.00 143.67 ? 337 GLN A NE2 1 ATOM 2685 N N . CYS A 1 339 ? -12.135 11.989 31.169 1.00 135.95 ? 338 CYS A N 1 ATOM 2686 C CA . CYS A 1 339 ? -12.532 13.394 31.125 1.00 138.34 ? 338 CYS A CA 1 ATOM 2687 C C . CYS A 1 339 ? -13.925 13.546 31.717 1.00 139.43 ? 338 CYS A C 1 ATOM 2688 O O . CYS A 1 339 ? -14.188 14.468 32.491 1.00 138.98 ? 338 CYS A O 1 ATOM 2689 C CB . CYS A 1 339 ? -12.535 13.891 29.682 1.00 138.69 ? 338 CYS A CB 1 ATOM 2690 S SG . CYS A 1 339 ? -11.116 13.325 28.720 1.00 141.93 ? 338 CYS A SG 1 ATOM 2691 N N . GLN A 1 340 ? -14.805 12.622 31.339 1.00 140.56 ? 339 GLN A N 1 ATOM 2692 C CA . GLN A 1 340 ? -16.163 12.563 31.866 1.00 144.66 ? 339 GLN A CA 1 ATOM 2693 C C . GLN A 1 340 ? -16.113 12.459 33.393 1.00 142.61 ? 339 GLN A C 1 ATOM 2694 O O . GLN A 1 340 ? -16.818 13.177 34.094 1.00 139.92 ? 339 GLN A O 1 ATOM 2695 C CB . GLN A 1 340 ? -16.904 11.356 31.270 1.00 151.14 ? 339 GLN A CB 1 ATOM 2696 C CG . GLN A 1 340 ? -18.395 11.557 31.051 1.00 158.34 ? 339 GLN A CG 1 ATOM 2697 C CD . GLN A 1 340 ? -19.028 10.411 30.275 1.00 163.42 ? 339 GLN A CD 1 ATOM 2698 O OE1 . GLN A 1 340 ? -18.470 9.317 30.192 1.00 160.73 ? 339 GLN A OE1 1 ATOM 2699 N NE2 . GLN A 1 340 ? -20.200 10.662 29.699 1.00 168.01 ? 339 GLN A NE2 1 ATOM 2700 N N . ALA A 1 341 ? -15.263 11.571 33.897 1.00 141.75 ? 340 ALA A N 1 ATOM 2701 C CA . ALA A 1 341 ? -15.117 11.373 35.337 1.00 141.51 ? 340 ALA A CA 1 ATOM 2702 C C . ALA A 1 341 ? -14.567 12.614 36.040 1.00 138.83 ? 340 ALA A C 1 ATOM 2703 O O . ALA A 1 341 ? -14.959 12.915 37.161 1.00 136.95 ? 340 ALA A O 1 ATOM 2704 C CB . ALA A 1 341 ? -14.230 10.168 35.619 1.00 142.04 ? 340 ALA A CB 1 ATOM 2705 N N . TRP A 1 342 ? -13.652 13.325 35.389 1.00 137.97 ? 341 TRP A N 1 ATOM 2706 C CA . TRP A 1 342 ? -13.080 14.550 35.973 1.00 140.97 ? 341 TRP A CA 1 ATOM 2707 C C . TRP A 1 342 ? -14.104 15.694 36.042 1.00 141.14 ? 341 TRP A C 1 ATOM 2708 O O . TRP A 1 342 ? -14.048 16.544 36.930 1.00 142.63 ? 341 TRP A O 1 ATOM 2709 C CB . TRP A 1 342 ? -11.850 15.017 35.175 1.00 142.12 ? 341 TRP A CB 1 ATOM 2710 C CG . TRP A 1 342 ? -10.583 14.205 35.384 1.00 144.12 ? 341 TRP A CG 1 ATOM 2711 C CD1 . TRP A 1 342 ? -10.165 13.613 36.541 1.00 147.80 ? 341 TRP A CD1 1 ATOM 2712 C CD2 . TRP A 1 342 ? -9.558 13.942 34.411 1.00 143.40 ? 341 TRP A CD2 1 ATOM 2713 N NE1 . TRP A 1 342 ? -8.959 12.980 36.344 1.00 147.92 ? 341 TRP A NE1 1 ATOM 2714 C CE2 . TRP A 1 342 ? -8.563 13.169 35.047 1.00 144.62 ? 341 TRP A CE2 1 ATOM 2715 C CE3 . TRP A 1 342 ? -9.390 14.277 33.063 1.00 141.64 ? 341 TRP A CE3 1 ATOM 2716 C CZ2 . TRP A 1 342 ? -7.414 12.724 34.379 1.00 143.70 ? 341 TRP A CZ2 1 ATOM 2717 C CZ3 . TRP A 1 342 ? -8.245 13.835 32.398 1.00 140.45 ? 341 TRP A CZ3 1 ATOM 2718 C CH2 . TRP A 1 342 ? -7.274 13.067 33.058 1.00 141.18 ? 341 TRP A CH2 1 ATOM 2719 N N . GLN A 1 343 ? -15.038 15.709 35.101 1.00 142.33 ? 342 GLN A N 1 ATOM 2720 C CA . GLN A 1 343 ? -16.086 16.727 35.059 1.00 145.84 ? 342 GLN A CA 1 ATOM 2721 C C . GLN A 1 343 ? -16.858 16.830 36.382 1.00 152.03 ? 342 GLN A C 1 ATOM 2722 O O . GLN A 1 343 ? -17.221 17.920 36.819 1.00 154.07 ? 342 GLN A O 1 ATOM 2723 C CB . GLN A 1 343 ? -17.068 16.396 33.940 1.00 148.58 ? 342 GLN A CB 1 ATOM 2724 C CG . GLN A 1 343 ? -17.889 17.574 33.454 1.00 151.82 ? 342 GLN A CG 1 ATOM 2725 C CD . GLN A 1 343 ? -18.678 17.253 32.198 1.00 154.92 ? 342 GLN A CD 1 ATOM 2726 O OE1 . GLN A 1 343 ? -18.928 16.086 31.886 1.00 155.25 ? 342 GLN A OE1 1 ATOM 2727 N NE2 . GLN A 1 343 ? -19.080 18.290 31.470 1.00 158.22 ? 342 GLN A NE2 1 ATOM 2728 N N . SER A 1 344 ? -17.098 15.696 37.030 1.00 158.59 ? 343 SER A N 1 ATOM 2729 C CA . SER A 1 344 ? -17.856 15.668 38.278 1.00 168.08 ? 343 SER A CA 1 ATOM 2730 C C . SER A 1 344 ? -17.026 16.046 39.507 1.00 173.86 ? 343 SER A C 1 ATOM 2731 O O . SER A 1 344 ? -17.569 16.228 40.594 1.00 178.13 ? 343 SER A O 1 ATOM 2732 C CB . SER A 1 344 ? -18.451 14.277 38.491 1.00 170.85 ? 343 SER A CB 1 ATOM 2733 O OG . SER A 1 344 ? -17.430 13.290 38.484 1.00 169.60 ? 343 SER A OG 1 ATOM 2734 N N . ARG A 1 345 ? -15.713 16.166 39.332 1.00 178.52 ? 344 ARG A N 1 ATOM 2735 C CA . ARG A 1 345 ? -14.802 16.449 40.429 1.00 186.15 ? 344 ARG A CA 1 ATOM 2736 C C . ARG A 1 345 ? -14.165 17.810 40.176 1.00 184.31 ? 344 ARG A C 1 ATOM 2737 O O . ARG A 1 345 ? -12.950 17.965 40.288 1.00 187.53 ? 344 ARG A O 1 ATOM 2738 C CB . ARG A 1 345 ? -13.727 15.362 40.461 1.00 192.41 ? 344 ARG A CB 1 ATOM 2739 C CG . ARG A 1 345 ? -14.284 13.947 40.346 1.00 200.01 ? 344 ARG A CG 1 ATOM 2740 C CD . ARG A 1 345 ? -15.029 13.505 41.596 1.00 210.50 ? 344 ARG A CD 1 ATOM 2741 N NE . ARG A 1 345 ? -14.173 13.373 42.777 1.00 220.10 ? 344 ARG A NE 1 ATOM 2742 C CZ . ARG A 1 345 ? -14.346 12.485 43.758 1.00 231.25 ? 344 ARG A CZ 1 ATOM 2743 N NH1 . ARG A 1 345 ? -15.332 11.589 43.714 1.00 237.71 ? 344 ARG A NH1 1 ATOM 2744 N NH2 . ARG A 1 345 ? -13.505 12.476 44.788 1.00 234.22 ? 344 ARG A NH2 1 ATOM 2745 N N . GLN A 1 346 ? -14.992 18.795 39.836 1.00 183.31 ? 345 GLN A N 1 ATOM 2746 C CA . GLN A 1 346 ? -14.516 19.987 39.168 1.00 181.73 ? 345 GLN A CA 1 ATOM 2747 C C . GLN A 1 346 ? -14.418 21.166 40.090 1.00 174.99 ? 345 GLN A C 1 ATOM 2748 O O . GLN A 1 346 ? -15.427 21.622 40.579 1.00 171.12 ? 345 GLN A O 1 ATOM 2749 C CB . GLN A 1 346 ? -15.496 20.395 38.059 1.00 187.01 ? 345 GLN A CB 1 ATOM 2750 C CG . GLN A 1 346 ? -15.192 19.840 36.691 1.00 188.51 ? 345 GLN A CG 1 ATOM 2751 C CD . GLN A 1 346 ? -16.077 20.482 35.634 1.00 191.46 ? 345 GLN A CD 1 ATOM 2752 O OE1 . GLN A 1 346 ? -15.606 21.208 34.761 1.00 188.54 ? 345 GLN A OE1 1 ATOM 2753 N NE2 . GLN A 1 346 ? -17.378 20.243 35.739 1.00 195.24 ? 345 GLN A NE2 1 ATOM 2754 N N . GLU A 1 347 ? -13.200 21.630 40.328 1.00 167.50 ? 346 GLU A N 1 ATOM 2755 C CA . GLU A 1 347 ? -12.969 23.012 40.698 1.00 163.14 ? 346 GLU A CA 1 ATOM 2756 C C . GLU A 1 347 ? -12.816 23.758 39.375 1.00 160.53 ? 346 GLU A C 1 ATOM 2757 O O . GLU A 1 347 ? -13.629 24.606 39.006 1.00 159.80 ? 346 GLU A O 1 ATOM 2758 C CB . GLU A 1 347 ? -11.729 23.102 41.584 1.00 161.54 ? 346 GLU A CB 1 ATOM 2759 C CG . GLU A 1 347 ? -11.863 22.231 42.827 1.00 162.25 ? 346 GLU A CG 1 ATOM 2760 C CD . GLU A 1 347 ? -10.712 22.380 43.796 1.00 162.23 ? 346 GLU A CD 1 ATOM 2761 O OE1 . GLU A 1 347 ? -9.612 22.807 43.375 1.00 160.98 ? 346 GLU A OE1 1 ATOM 2762 O OE2 . GLU A 1 347 ? -10.906 22.060 44.990 1.00 161.56 ? 346 GLU A OE2 1 ATOM 2763 N N . HIS A 1 348 ? -11.787 23.400 38.634 1.00 160.41 ? 347 HIS A N 1 ATOM 2764 C CA . HIS A 1 348 ? -11.567 24.016 37.338 1.00 164.45 ? 347 HIS A CA 1 ATOM 2765 C C . HIS A 1 348 ? -12.531 23.477 36.297 1.00 163.95 ? 347 HIS A C 1 ATOM 2766 O O . HIS A 1 348 ? -13.000 22.354 36.407 1.00 162.33 ? 347 HIS A O 1 ATOM 2767 C CB . HIS A 1 348 ? -10.131 23.792 36.908 1.00 165.61 ? 347 HIS A CB 1 ATOM 2768 C CG . HIS A 1 348 ? -9.155 24.560 37.740 1.00 169.55 ? 347 HIS A CG 1 ATOM 2769 N ND1 . HIS A 1 348 ? -8.840 24.202 39.033 1.00 170.25 ? 347 HIS A ND1 1 ATOM 2770 C CD2 . HIS A 1 348 ? -8.464 25.694 37.484 1.00 172.42 ? 347 HIS A CD2 1 ATOM 2771 C CE1 . HIS A 1 348 ? -7.976 25.069 39.529 1.00 172.58 ? 347 HIS A CE1 1 ATOM 2772 N NE2 . HIS A 1 348 ? -7.731 25.984 38.609 1.00 173.19 ? 347 HIS A NE2 1 ATOM 2773 N N . GLN A 1 349 ? -12.803 24.277 35.271 1.00 165.39 ? 348 GLN A N 1 ATOM 2774 C CA . GLN A 1 349 ? -13.719 23.876 34.195 1.00 167.69 ? 348 GLN A CA 1 ATOM 2775 C C . GLN A 1 349 ? -13.182 22.720 33.361 1.00 165.70 ? 348 GLN A C 1 ATOM 2776 O O . GLN A 1 349 ? -11.982 22.642 33.102 1.00 164.05 ? 348 GLN A O 1 ATOM 2777 C CB . GLN A 1 349 ? -13.986 25.044 33.251 1.00 172.86 ? 348 GLN A CB 1 ATOM 2778 C CG . GLN A 1 349 ? -14.746 26.200 33.871 1.00 179.78 ? 348 GLN A CG 1 ATOM 2779 C CD . GLN A 1 349 ? -15.111 27.260 32.849 1.00 186.32 ? 348 GLN A CD 1 ATOM 2780 O OE1 . GLN A 1 349 ? -14.766 27.150 31.667 1.00 188.56 ? 348 GLN A OE1 1 ATOM 2781 N NE2 . GLN A 1 349 ? -15.816 28.292 33.297 1.00 191.17 ? 348 GLN A NE2 1 ATOM 2782 N N . VAL A 1 350 ? -14.087 21.843 32.931 1.00 168.76 ? 349 VAL A N 1 ATOM 2783 C CA . VAL A 1 350 ? -13.751 20.709 32.064 1.00 168.32 ? 349 VAL A CA 1 ATOM 2784 C C . VAL A 1 350 ? -14.764 20.687 30.925 1.00 168.75 ? 349 VAL A C 1 ATOM 2785 O O . VAL A 1 350 ? -15.949 20.459 31.163 1.00 173.00 ? 349 VAL A O 1 ATOM 2786 C CB . VAL A 1 350 ? -13.833 19.366 32.831 1.00 168.06 ? 349 VAL A CB 1 ATOM 2787 C CG1 . VAL A 1 350 ? -13.374 18.209 31.953 1.00 163.15 ? 349 VAL A CG1 1 ATOM 2788 C CG2 . VAL A 1 350 ? -13.003 19.431 34.105 1.00 171.57 ? 349 VAL A CG2 1 ATOM 2789 N N . LEU A 1 351 ? -14.307 20.937 29.701 1.00 167.02 ? 350 LEU A N 1 ATOM 2790 C CA . LEU A 1 351 ? -15.200 20.966 28.545 1.00 169.02 ? 350 LEU A CA 1 ATOM 2791 C C . LEU A 1 351 ? -14.902 19.769 27.649 1.00 164.83 ? 350 LEU A C 1 ATOM 2792 O O . LEU A 1 351 ? -13.755 19.531 27.296 1.00 160.64 ? 350 LEU A O 1 ATOM 2793 C CB . LEU A 1 351 ? -15.042 22.282 27.773 1.00 172.54 ? 350 LEU A CB 1 ATOM 2794 C CG . LEU A 1 351 ? -15.551 23.556 28.472 1.00 176.28 ? 350 LEU A CG 1 ATOM 2795 C CD1 . LEU A 1 351 ? -14.546 24.084 29.492 1.00 175.35 ? 350 LEU A CD1 1 ATOM 2796 C CD2 . LEU A 1 351 ? -15.892 24.637 27.453 1.00 177.54 ? 350 LEU A CD2 1 ATOM 2797 N N . LEU A 1 352 ? -15.933 19.005 27.304 1.00 163.12 ? 351 LEU A N 1 ATOM 2798 C CA . LEU A 1 352 ? -15.777 17.861 26.406 1.00 160.79 ? 351 LEU A CA 1 ATOM 2799 C C . LEU A 1 352 ? -16.264 18.232 25.016 1.00 159.39 ? 351 LEU A C 1 ATOM 2800 O O . LEU A 1 352 ? -17.265 18.934 24.868 1.00 164.07 ? 351 LEU A O 1 ATOM 2801 C CB . LEU A 1 352 ? -16.541 16.644 26.932 1.00 163.33 ? 351 LEU A CB 1 ATOM 2802 C CG . LEU A 1 352 ? -15.762 15.737 27.889 1.00 164.84 ? 351 LEU A CG 1 ATOM 2803 C CD1 . LEU A 1 352 ? -15.054 16.532 28.977 1.00 166.23 ? 351 LEU A CD1 1 ATOM 2804 C CD2 . LEU A 1 352 ? -16.687 14.694 28.497 1.00 167.52 ? 351 LEU A CD2 1 ATOM 2805 N N . GLN A 1 353 ? -15.554 17.765 23.996 1.00 153.80 ? 352 GLN A N 1 ATOM 2806 C CA . GLN A 1 353 ? -15.910 18.089 22.618 1.00 150.74 ? 352 GLN A CA 1 ATOM 2807 C C . GLN A 1 353 ? -15.721 16.903 21.677 1.00 147.35 ? 352 GLN A C 1 ATOM 2808 O O . GLN A 1 353 ? -14.594 16.492 21.395 1.00 144.76 ? 352 GLN A O 1 ATOM 2809 C CB . GLN A 1 353 ? -15.082 19.283 22.133 1.00 150.16 ? 352 GLN A CB 1 ATOM 2810 C CG . GLN A 1 353 ? -15.481 19.834 20.770 1.00 150.04 ? 352 GLN A CG 1 ATOM 2811 C CD . GLN A 1 353 ? -16.844 20.499 20.774 1.00 151.68 ? 352 GLN A CD 1 ATOM 2812 O OE1 . GLN A 1 353 ? -16.948 21.724 20.847 1.00 153.18 ? 352 GLN A OE1 1 ATOM 2813 N NE2 . GLN A 1 353 ? -17.897 19.695 20.703 1.00 151.74 ? 352 GLN A NE2 1 ATOM 2814 N N . GLU A 1 354 ? -16.834 16.366 21.187 1.00 147.01 ? 353 GLU A N 1 ATOM 2815 C CA . GLU A 1 354 ? -16.805 15.289 20.194 1.00 145.89 ? 353 GLU A CA 1 ATOM 2816 C C . GLU A 1 354 ? -16.400 15.834 18.820 1.00 145.70 ? 353 GLU A C 1 ATOM 2817 O O . GLU A 1 354 ? -16.765 16.953 18.449 1.00 146.31 ? 353 GLU A O 1 ATOM 2818 C CB . GLU A 1 354 ? -18.179 14.607 20.103 1.00 146.36 ? 353 GLU A CB 1 ATOM 2819 C CG . GLU A 1 354 ? -18.209 13.351 19.236 1.00 144.81 ? 353 GLU A CG 1 ATOM 2820 C CD . GLU A 1 354 ? -19.580 12.693 19.169 1.00 146.27 ? 353 GLU A CD 1 ATOM 2821 O OE1 . GLU A 1 354 ? -20.360 12.808 20.138 1.00 148.14 ? 353 GLU A OE1 1 ATOM 2822 O OE2 . GLU A 1 354 ? -19.882 12.051 18.142 1.00 145.26 ? 353 GLU A OE2 1 ATOM 2823 N N . LEU A 1 355 ? -15.641 15.032 18.078 1.00 143.58 ? 354 LEU A N 1 ATOM 2824 C CA . LEU A 1 355 ? -15.234 15.359 16.711 1.00 143.50 ? 354 LEU A CA 1 ATOM 2825 C C . LEU A 1 355 ? -15.652 14.224 15.776 1.00 144.63 ? 354 LEU A C 1 ATOM 2826 O O . LEU A 1 355 ? -14.840 13.355 15.439 1.00 144.26 ? 354 LEU A O 1 ATOM 2827 C CB . LEU A 1 355 ? -13.723 15.567 16.649 1.00 141.80 ? 354 LEU A CB 1 ATOM 2828 C CG . LEU A 1 355 ? -13.224 16.857 17.295 1.00 141.70 ? 354 LEU A CG 1 ATOM 2829 C CD1 . LEU A 1 355 ? -11.764 16.730 17.701 1.00 139.62 ? 354 LEU A CD1 1 ATOM 2830 C CD2 . LEU A 1 355 ? -13.425 18.027 16.343 1.00 143.18 ? 354 LEU A CD2 1 ATOM 2831 N N . PRO A 1 356 ? -16.925 14.229 15.351 1.00 147.11 ? 355 PRO A N 1 ATOM 2832 C CA . PRO A 1 356 ? -17.434 13.098 14.586 1.00 148.44 ? 355 PRO A CA 1 ATOM 2833 C C . PRO A 1 356 ? -16.788 12.980 13.212 1.00 148.90 ? 355 PRO A C 1 ATOM 2834 O O . PRO A 1 356 ? -16.746 13.958 12.466 1.00 150.28 ? 355 PRO A O 1 ATOM 2835 C CB . PRO A 1 356 ? -18.927 13.405 14.457 1.00 151.01 ? 355 PRO A CB 1 ATOM 2836 C CG . PRO A 1 356 ? -19.010 14.889 14.519 1.00 152.13 ? 355 PRO A CG 1 ATOM 2837 C CD . PRO A 1 356 ? -17.906 15.326 15.439 1.00 149.27 ? 355 PRO A CD 1 ATOM 2838 N N . GLY A 1 357 ? -16.282 11.789 12.898 1.00 149.00 ? 356 GLY A N 1 ATOM 2839 C CA . GLY A 1 357 ? -15.669 11.519 11.602 1.00 148.05 ? 356 GLY A CA 1 ATOM 2840 C C . GLY A 1 357 ? -14.238 12.010 11.462 1.00 145.31 ? 356 GLY A C 1 ATOM 2841 O O . GLY A 1 357 ? -13.677 11.972 10.367 1.00 141.85 ? 356 GLY A O 1 ATOM 2842 N N . SER A 1 358 ? -13.634 12.466 12.559 1.00 143.82 ? 357 SER A N 1 ATOM 2843 C CA . SER A 1 358 ? -12.257 12.950 12.512 1.00 141.56 ? 357 SER A CA 1 ATOM 2844 C C . SER A 1 358 ? -11.287 11.841 12.925 1.00 135.86 ? 357 SER A C 1 ATOM 2845 O O . SER A 1 358 ? -11.382 11.281 14.024 1.00 128.10 ? 357 SER A O 1 ATOM 2846 C CB . SER A 1 358 ? -12.076 14.181 13.404 1.00 143.07 ? 357 SER A CB 1 ATOM 2847 O OG . SER A 1 358 ? -12.010 13.815 14.768 1.00 146.23 ? 357 SER A OG 1 ATOM 2848 N N . GLU A 1 359 ? -10.352 11.533 12.031 1.00 135.55 ? 358 GLU A N 1 ATOM 2849 C CA . GLU A 1 359 ? -9.323 10.528 12.300 1.00 134.05 ? 358 GLU A CA 1 ATOM 2850 C C . GLU A 1 359 ? -8.278 11.060 13.283 1.00 131.55 ? 358 GLU A C 1 ATOM 2851 O O . GLU A 1 359 ? -8.044 12.272 13.392 1.00 134.43 ? 358 GLU A O 1 ATOM 2852 C CB . GLU A 1 359 ? -8.647 10.091 10.992 1.00 136.26 ? 358 GLU A CB 1 ATOM 2853 C CG . GLU A 1 359 ? -7.917 8.748 11.050 1.00 137.52 ? 358 GLU A CG 1 ATOM 2854 C CD . GLU A 1 359 ? -6.441 8.853 11.412 1.00 137.57 ? 358 GLU A CD 1 ATOM 2855 O OE1 . GLU A 1 359 ? -5.780 9.834 11.008 1.00 136.41 ? 358 GLU A OE1 1 ATOM 2856 O OE2 . GLU A 1 359 ? -5.934 7.939 12.103 1.00 141.09 ? 358 GLU A OE2 1 ATOM 2857 N N . HIS A 1 360 ? -7.651 10.126 13.985 1.00 130.02 ? 359 HIS A N 1 ATOM 2858 C CA . HIS A 1 360 ? -6.687 10.413 15.042 1.00 130.91 ? 359 HIS A CA 1 ATOM 2859 C C . HIS A 1 360 ? -5.631 11.477 14.687 1.00 131.98 ? 359 HIS A C 1 ATOM 2860 O O . HIS A 1 360 ? -5.388 12.398 15.468 1.00 138.58 ? 359 HIS A O 1 ATOM 2861 C CB . HIS A 1 360 ? -6.020 9.103 15.466 1.00 128.94 ? 359 HIS A CB 1 ATOM 2862 C CG . HIS A 1 360 ? -5.119 9.241 16.648 1.00 127.02 ? 359 HIS A CG 1 ATOM 2863 N ND1 . HIS A 1 360 ? -5.479 9.934 17.785 1.00 127.42 ? 359 HIS A ND1 1 ATOM 2864 C CD2 . HIS A 1 360 ? -3.879 8.757 16.879 1.00 126.47 ? 359 HIS A CD2 1 ATOM 2865 C CE1 . HIS A 1 360 ? -4.491 9.882 18.659 1.00 126.73 ? 359 HIS A CE1 1 ATOM 2866 N NE2 . HIS A 1 360 ? -3.511 9.172 18.134 1.00 126.24 ? 359 HIS A NE2 1 ATOM 2867 N N . ILE A 1 361 ? -5.017 11.359 13.515 1.00 128.68 ? 360 ILE A N 1 ATOM 2868 C CA . ILE A 1 361 ? -4.000 12.316 13.083 1.00 130.02 ? 360 ILE A CA 1 ATOM 2869 C C . ILE A 1 361 ? -4.631 13.506 12.356 1.00 132.52 ? 360 ILE A C 1 ATOM 2870 O O . ILE A 1 361 ? -4.220 14.647 12.550 1.00 130.08 ? 360 ILE A O 1 ATOM 2871 C CB . ILE A 1 361 ? -2.951 11.647 12.169 1.00 131.79 ? 360 ILE A CB 1 ATOM 2872 C CG1 . ILE A 1 361 ? -2.161 10.587 12.950 1.00 133.76 ? 360 ILE A CG1 1 ATOM 2873 C CG2 . ILE A 1 361 ? -1.994 12.682 11.590 1.00 132.49 ? 360 ILE A CG2 1 ATOM 2874 C CD1 . ILE A 1 361 ? -2.797 9.213 12.968 1.00 139.11 ? 360 ILE A CD1 1 ATOM 2875 N N . GLU A 1 362 ? -5.631 13.233 11.523 1.00 135.49 ? 361 GLU A N 1 ATOM 2876 C CA . GLU A 1 362 ? -6.285 14.276 10.731 1.00 136.33 ? 361 GLU A CA 1 ATOM 2877 C C . GLU A 1 362 ? -6.890 15.381 11.589 1.00 128.28 ? 361 GLU A C 1 ATOM 2878 O O . GLU A 1 362 ? -7.015 16.513 11.137 1.00 125.00 ? 361 GLU A O 1 ATOM 2879 C CB . GLU A 1 362 ? -7.373 13.669 9.840 1.00 148.02 ? 361 GLU A CB 1 ATOM 2880 C CG . GLU A 1 362 ? -6.843 12.760 8.737 1.00 158.48 ? 361 GLU A CG 1 ATOM 2881 C CD . GLU A 1 362 ? -7.941 12.001 8.007 1.00 168.45 ? 361 GLU A CD 1 ATOM 2882 O OE1 . GLU A 1 362 ? -9.081 12.515 7.926 1.00 177.59 ? 361 GLU A OE1 1 ATOM 2883 O OE2 . GLU A 1 362 ? -7.661 10.889 7.506 1.00 171.26 ? 361 GLU A OE2 1 ATOM 2884 N N . MET A 1 363 ? -7.251 15.059 12.827 1.00 124.04 ? 362 MET A N 1 ATOM 2885 C CA . MET A 1 363 ? -7.839 16.048 13.726 1.00 126.44 ? 362 MET A CA 1 ATOM 2886 C C . MET A 1 363 ? -6.930 17.262 13.951 1.00 127.78 ? 362 MET A C 1 ATOM 2887 O O . MET A 1 363 ? -7.421 18.356 14.219 1.00 129.19 ? 362 MET A O 1 ATOM 2888 C CB . MET A 1 363 ? -8.198 15.410 15.074 1.00 125.52 ? 362 MET A CB 1 ATOM 2889 C CG . MET A 1 363 ? -7.032 15.273 16.047 1.00 123.62 ? 362 MET A CG 1 ATOM 2890 S SD . MET A 1 363 ? -7.467 14.519 17.629 1.00 121.70 ? 362 MET A SD 1 ATOM 2891 C CE . MET A 1 363 ? -8.519 13.160 17.128 1.00 123.89 ? 362 MET A CE 1 ATOM 2892 N N . LEU A 1 364 ? -5.614 17.063 13.852 1.00 126.44 ? 363 LEU A N 1 ATOM 2893 C CA . LEU A 1 364 ? -4.639 18.145 14.051 1.00 124.19 ? 363 LEU A CA 1 ATOM 2894 C C . LEU A 1 364 ? -4.633 19.202 12.952 1.00 122.56 ? 363 LEU A C 1 ATOM 2895 O O . LEU A 1 364 ? -4.142 20.306 13.167 1.00 117.62 ? 363 LEU A O 1 ATOM 2896 C CB . LEU A 1 364 ? -3.221 17.581 14.187 1.00 123.32 ? 363 LEU A CB 1 ATOM 2897 C CG . LEU A 1 364 ? -2.893 16.815 15.469 1.00 123.26 ? 363 LEU A CG 1 ATOM 2898 C CD1 . LEU A 1 364 ? -1.473 16.274 15.393 1.00 123.86 ? 363 LEU A CD1 1 ATOM 2899 C CD2 . LEU A 1 364 ? -3.062 17.699 16.696 1.00 121.12 ? 363 LEU A CD2 1 ATOM 2900 N N . ALA A 1 365 ? -5.150 18.855 11.778 1.00 126.61 ? 364 ALA A N 1 ATOM 2901 C CA . ALA A 1 365 ? -5.219 19.778 10.654 1.00 130.72 ? 364 ALA A CA 1 ATOM 2902 C C . ALA A 1 365 ? -6.668 20.066 10.264 1.00 135.41 ? 364 ALA A C 1 ATOM 2903 O O . ALA A 1 365 ? -6.928 20.642 9.208 1.00 140.71 ? 364 ALA A O 1 ATOM 2904 C CB . ALA A 1 365 ? -4.461 19.196 9.472 1.00 132.09 ? 364 ALA A CB 1 ATOM 2905 N N . ASN A 1 366 ? -7.608 19.680 11.122 1.00 138.14 ? 365 ASN A N 1 ATOM 2906 C CA . ASN A 1 366 ? -9.022 19.818 10.814 1.00 145.21 ? 365 ASN A CA 1 ATOM 2907 C C . ASN A 1 366 ? -9.526 21.215 11.167 1.00 142.80 ? 365 ASN A C 1 ATOM 2908 O O . ASN A 1 366 ? -9.228 21.738 12.241 1.00 140.97 ? 365 ASN A O 1 ATOM 2909 C CB . ASN A 1 366 ? -9.837 18.752 11.552 1.00 152.87 ? 365 ASN A CB 1 ATOM 2910 C CG . ASN A 1 366 ? -11.270 18.689 11.069 1.00 166.23 ? 365 ASN A CG 1 ATOM 2911 O OD1 . ASN A 1 366 ? -11.949 19.716 10.998 1.00 170.64 ? 365 ASN A OD1 1 ATOM 2912 N ND2 . ASN A 1 366 ? -11.721 17.498 10.670 1.00 177.51 ? 365 ASN A ND2 1 ATOM 2913 N N . ALA A 1 367 ? -10.304 21.800 10.260 1.00 143.18 ? 366 ALA A N 1 ATOM 2914 C CA . ALA A 1 367 ? -10.807 23.166 10.416 1.00 143.17 ? 366 ALA A CA 1 ATOM 2915 C C . ALA A 1 367 ? -11.659 23.357 11.671 1.00 141.43 ? 366 ALA A C 1 ATOM 2916 O O . ALA A 1 367 ? -11.643 24.430 12.276 1.00 147.30 ? 366 ALA A O 1 ATOM 2917 C CB . ALA A 1 367 ? -11.593 23.579 9.181 1.00 145.61 ? 366 ALA A CB 1 ATOM 2918 N N . THR A 1 368 ? -12.408 22.327 12.055 1.00 135.99 ? 367 THR A N 1 ATOM 2919 C CA . THR A 1 368 ? -13.221 22.385 13.268 1.00 132.64 ? 367 THR A CA 1 ATOM 2920 C C . THR A 1 368 ? -12.341 22.419 14.513 1.00 126.46 ? 367 THR A C 1 ATOM 2921 O O . THR A 1 368 ? -12.631 23.142 15.462 1.00 127.47 ? 367 THR A O 1 ATOM 2922 C CB . THR A 1 368 ? -14.189 21.190 13.369 1.00 135.97 ? 367 THR A CB 1 ATOM 2923 O OG1 . THR A 1 368 ? -13.455 19.961 13.286 1.00 137.57 ? 367 THR A OG1 1 ATOM 2924 C CG2 . THR A 1 368 ? -15.223 21.240 12.252 1.00 139.59 ? 367 THR A CG2 1 ATOM 2925 N N . THR A 1 369 ? -11.267 21.635 14.505 1.00 122.42 ? 368 THR A N 1 ATOM 2926 C CA . THR A 1 369 ? -10.307 21.641 15.608 1.00 121.59 ? 368 THR A CA 1 ATOM 2927 C C . THR A 1 369 ? -9.683 23.021 15.757 1.00 124.43 ? 368 THR A C 1 ATOM 2928 O O . THR A 1 369 ? -9.565 23.549 16.864 1.00 121.04 ? 368 THR A O 1 ATOM 2929 C CB . THR A 1 369 ? -9.171 20.626 15.371 1.00 119.91 ? 368 THR A CB 1 ATOM 2930 O OG1 . THR A 1 369 ? -9.726 19.345 15.044 1.00 121.72 ? 368 THR A OG1 1 ATOM 2931 C CG2 . THR A 1 369 ? -8.284 20.502 16.607 1.00 117.54 ? 368 THR A CG2 1 ATOM 2932 N N . LEU A 1 370 ? -9.293 23.601 14.626 1.00 129.48 ? 369 LEU A N 1 ATOM 2933 C CA . LEU A 1 370 ? -8.655 24.916 14.608 1.00 134.84 ? 369 LEU A CA 1 ATOM 2934 C C . LEU A 1 370 ? -9.618 26.016 15.065 1.00 137.90 ? 369 LEU A C 1 ATOM 2935 O O . LEU A 1 370 ? -9.221 26.951 15.763 1.00 136.44 ? 369 LEU A O 1 ATOM 2936 C CB . LEU A 1 370 ? -8.133 25.233 13.199 1.00 136.81 ? 369 LEU A CB 1 ATOM 2937 C CG . LEU A 1 370 ? -7.091 24.281 12.595 1.00 134.09 ? 369 LEU A CG 1 ATOM 2938 C CD1 . LEU A 1 370 ? -6.944 24.524 11.098 1.00 135.97 ? 369 LEU A CD1 1 ATOM 2939 C CD2 . LEU A 1 370 ? -5.748 24.412 13.297 1.00 131.53 ? 369 LEU A CD2 1 ATOM 2940 N N . ALA A 1 371 ? -10.882 25.903 14.663 1.00 141.51 ? 370 ALA A N 1 ATOM 2941 C CA . ALA A 1 371 ? -11.912 26.851 15.083 1.00 143.54 ? 370 ALA A CA 1 ATOM 2942 C C . ALA A 1 371 ? -12.119 26.811 16.599 1.00 142.47 ? 370 ALA A C 1 ATOM 2943 O O . ALA A 1 371 ? -12.327 27.848 17.229 1.00 143.44 ? 370 ALA A O 1 ATOM 2944 C CB . ALA A 1 371 ? -13.220 26.561 14.363 1.00 145.77 ? 370 ALA A CB 1 ATOM 2945 N N . TYR A 1 372 ? -12.062 25.616 17.181 1.00 139.30 ? 371 TYR A N 1 ATOM 2946 C CA . TYR A 1 372 ? -12.180 25.483 18.631 1.00 141.31 ? 371 TYR A CA 1 ATOM 2947 C C . TYR A 1 372 ? -10.977 26.109 19.327 1.00 139.04 ? 371 TYR A C 1 ATOM 2948 O O . TYR A 1 372 ? -11.120 26.805 20.324 1.00 138.96 ? 371 TYR A O 1 ATOM 2949 C CB . TYR A 1 372 ? -12.317 24.020 19.046 1.00 143.62 ? 371 TYR A CB 1 ATOM 2950 C CG . TYR A 1 372 ? -12.845 23.854 20.455 1.00 149.86 ? 371 TYR A CG 1 ATOM 2951 C CD1 . TYR A 1 372 ? -14.214 23.838 20.708 1.00 155.50 ? 371 TYR A CD1 1 ATOM 2952 C CD2 . TYR A 1 372 ? -11.977 23.728 21.537 1.00 151.48 ? 371 TYR A CD2 1 ATOM 2953 C CE1 . TYR A 1 372 ? -14.705 23.692 21.998 1.00 158.03 ? 371 TYR A CE1 1 ATOM 2954 C CE2 . TYR A 1 372 ? -12.459 23.583 22.830 1.00 152.29 ? 371 TYR A CE2 1 ATOM 2955 C CZ . TYR A 1 372 ? -13.822 23.565 23.055 1.00 155.00 ? 371 TYR A CZ 1 ATOM 2956 O OH . TYR A 1 372 ? -14.302 23.423 24.336 1.00 153.78 ? 371 TYR A OH 1 ATOM 2957 N N . LEU A 1 373 ? -9.787 25.857 18.799 1.00 138.76 ? 372 LEU A N 1 ATOM 2958 C CA . LEU A 1 373 ? -8.569 26.459 19.330 1.00 140.71 ? 372 LEU A CA 1 ATOM 2959 C C . LEU A 1 373 ? -8.650 27.988 19.310 1.00 140.74 ? 372 LEU A C 1 ATOM 2960 O O . LEU A 1 373 ? -8.279 28.652 20.275 1.00 141.00 ? 372 LEU A O 1 ATOM 2961 C CB . LEU A 1 373 ? -7.366 25.991 18.509 1.00 145.22 ? 372 LEU A CB 1 ATOM 2962 C CG . LEU A 1 373 ? -5.983 26.149 19.140 1.00 149.04 ? 372 LEU A CG 1 ATOM 2963 C CD1 . LEU A 1 373 ? -5.866 25.322 20.413 1.00 149.43 ? 372 LEU A CD1 1 ATOM 2964 C CD2 . LEU A 1 373 ? -4.914 25.738 18.137 1.00 151.86 ? 372 LEU A CD2 1 ATOM 2965 N N . LYS A 1 374 ? -9.132 28.536 18.200 1.00 141.39 ? 373 LYS A N 1 ATOM 2966 C CA . LYS A 1 374 ? -9.380 29.978 18.082 1.00 144.57 ? 373 LYS A CA 1 ATOM 2967 C C . LYS A 1 374 ? -10.207 30.527 19.254 1.00 142.63 ? 373 LYS A C 1 ATOM 2968 O O . LYS A 1 374 ? -9.875 31.572 19.826 1.00 140.71 ? 373 LYS A O 1 ATOM 2969 C CB . LYS A 1 374 ? -10.125 30.264 16.769 1.00 149.91 ? 373 LYS A CB 1 ATOM 2970 C CG . LYS A 1 374 ? -9.284 30.872 15.654 1.00 153.32 ? 373 LYS A CG 1 ATOM 2971 C CD . LYS A 1 374 ? -9.605 32.349 15.472 1.00 158.82 ? 373 LYS A CD 1 ATOM 2972 C CE . LYS A 1 374 ? -8.941 32.935 14.237 1.00 160.97 ? 373 LYS A CE 1 ATOM 2973 N NZ . LYS A 1 374 ? -9.519 34.257 13.861 1.00 165.05 ? 373 LYS A NZ 1 ATOM 2974 N N . ARG A 1 375 ? -11.295 29.819 19.561 1.00 145.96 ? 374 ARG A N 1 ATOM 2975 C CA . ARG A 1 375 ? -12.182 30.097 20.703 1.00 154.50 ? 374 ARG A CA 1 ATOM 2976 C C . ARG A 1 375 ? -11.422 30.195 22.026 1.00 153.07 ? 374 ARG A C 1 ATOM 2977 O O . ARG A 1 375 ? -11.609 31.125 22.823 1.00 155.21 ? 374 ARG A O 1 ATOM 2978 C CB . ARG A 1 375 ? -13.229 28.958 20.840 1.00 163.89 ? 374 ARG A CB 1 ATOM 2979 C CG . ARG A 1 375 ? -14.629 29.297 20.367 1.00 175.21 ? 374 ARG A CG 1 ATOM 2980 C CD . ARG A 1 375 ? -15.664 28.449 21.101 1.00 184.46 ? 374 ARG A CD 1 ATOM 2981 N NE . ARG A 1 375 ? -16.741 28.003 20.212 1.00 193.97 ? 374 ARG A NE 1 ATOM 2982 C CZ . ARG A 1 375 ? -17.743 28.773 19.781 1.00 204.24 ? 374 ARG A CZ 1 ATOM 2983 N NH1 . ARG A 1 375 ? -18.670 28.255 18.978 1.00 208.33 ? 374 ARG A NH1 1 ATOM 2984 N NH2 . ARG A 1 375 ? -17.825 30.057 20.126 1.00 207.69 ? 374 ARG A NH2 1 ATOM 2985 N N . VAL A 1 376 ? -10.573 29.206 22.256 1.00 150.46 ? 375 VAL A N 1 ATOM 2986 C CA . VAL A 1 376 ? -9.808 29.135 23.491 1.00 150.99 ? 375 VAL A CA 1 ATOM 2987 C C . VAL A 1 376 ? -8.822 30.298 23.595 1.00 150.92 ? 375 VAL A C 1 ATOM 2988 O O . VAL A 1 376 ? -8.711 30.931 24.645 1.00 150.63 ? 375 VAL A O 1 ATOM 2989 C CB . VAL A 1 376 ? -9.063 27.791 23.600 1.00 151.48 ? 375 VAL A CB 1 ATOM 2990 C CG1 . VAL A 1 376 ? -8.126 27.785 24.802 1.00 150.21 ? 375 VAL A CG1 1 ATOM 2991 C CG2 . VAL A 1 376 ? -10.063 26.644 23.698 1.00 152.65 ? 375 VAL A CG2 1 ATOM 2992 N N . LEU A 1 377 ? -8.132 30.586 22.494 1.00 152.16 ? 376 LEU A N 1 ATOM 2993 C CA . LEU A 1 377 ? -7.066 31.588 22.476 1.00 156.44 ? 376 LEU A CA 1 ATOM 2994 C C . LEU A 1 377 ? -7.560 33.032 22.473 1.00 161.43 ? 376 LEU A C 1 ATOM 2995 O O . LEU A 1 377 ? -7.023 33.880 23.196 1.00 162.40 ? 376 LEU A O 1 ATOM 2996 C CB . LEU A 1 377 ? -6.176 31.381 21.249 1.00 156.55 ? 376 LEU A CB 1 ATOM 2997 C CG . LEU A 1 377 ? -5.455 30.038 21.154 1.00 157.24 ? 376 LEU A CG 1 ATOM 2998 C CD1 . LEU A 1 377 ? -4.798 29.903 19.788 1.00 159.84 ? 376 LEU A CD1 1 ATOM 2999 C CD2 . LEU A 1 377 ? -4.433 29.885 22.270 1.00 155.91 ? 376 LEU A CD2 1 ATOM 3000 N N . LEU A 1 378 ? -8.560 33.313 21.639 1.00 165.65 ? 377 LEU A N 1 ATOM 3001 C CA . LEU A 1 378 ? -9.030 34.681 21.436 1.00 166.79 ? 377 LEU A CA 1 ATOM 3002 C C . LEU A 1 378 ? -10.277 35.024 22.259 1.00 166.16 ? 377 LEU A C 1 ATOM 3003 O O . LEU A 1 378 ? -10.572 36.195 22.475 1.00 168.90 ? 377 LEU A O 1 ATOM 3004 C CB . LEU A 1 378 ? -9.256 34.944 19.943 1.00 168.59 ? 377 LEU A CB 1 ATOM 3005 C CG . LEU A 1 378 ? -8.098 34.548 19.008 1.00 169.51 ? 377 LEU A CG 1 ATOM 3006 C CD1 . LEU A 1 378 ? -8.343 35.068 17.598 1.00 173.18 ? 377 LEU A CD1 1 ATOM 3007 C CD2 . LEU A 1 378 ? -6.751 35.043 19.519 1.00 167.43 ? 377 LEU A CD2 1 ATOM 3008 N N . GLY A 1 379 ? -10.997 34.011 22.733 1.00 162.98 ? 378 GLY A N 1 ATOM 3009 C CA . GLY A 1 379 ? -12.141 34.229 23.618 1.00 161.70 ? 378 GLY A CA 1 ATOM 3010 C C . GLY A 1 379 ? -11.699 34.307 25.064 1.00 158.67 ? 378 GLY A C 1 ATOM 3011 O O . GLY A 1 379 ? -10.560 33.975 25.387 1.00 151.32 ? 378 GLY A O 1 ATOM 3012 N N . ARG B 1 4 ? -6.588 36.770 -7.609 1.00 175.75 ? 3 ARG B N 1 ATOM 3013 C CA . ARG B 1 4 ? -5.810 36.329 -8.801 1.00 173.78 ? 3 ARG B CA 1 ATOM 3014 C C . ARG B 1 4 ? -4.318 36.618 -8.613 1.00 168.50 ? 3 ARG B C 1 ATOM 3015 O O . ARG B 1 4 ? -3.879 37.760 -8.764 1.00 169.55 ? 3 ARG B O 1 ATOM 3016 C CB . ARG B 1 4 ? -6.329 37.033 -10.063 1.00 177.58 ? 3 ARG B CB 1 ATOM 3017 C CG . ARG B 1 4 ? -5.654 36.587 -11.354 1.00 178.64 ? 3 ARG B CG 1 ATOM 3018 C CD . ARG B 1 4 ? -6.107 35.196 -11.777 1.00 180.54 ? 3 ARG B CD 1 ATOM 3019 N NE . ARG B 1 4 ? -5.020 34.422 -12.383 1.00 178.79 ? 3 ARG B NE 1 ATOM 3020 C CZ . ARG B 1 4 ? -4.249 33.538 -11.745 1.00 174.77 ? 3 ARG B CZ 1 ATOM 3021 N NH1 . ARG B 1 4 ? -4.417 33.274 -10.451 1.00 172.33 ? 3 ARG B NH1 1 ATOM 3022 N NH2 . ARG B 1 4 ? -3.294 32.902 -12.416 1.00 173.64 ? 3 ARG B NH2 1 ATOM 3023 N N . HIS B 1 5 ? -3.549 35.579 -8.286 1.00 161.15 ? 4 HIS B N 1 ATOM 3024 C CA . HIS B 1 5 ? -2.099 35.703 -8.110 1.00 156.19 ? 4 HIS B CA 1 ATOM 3025 C C . HIS B 1 5 ? -1.358 34.605 -8.885 1.00 147.44 ? 4 HIS B C 1 ATOM 3026 O O . HIS B 1 5 ? -1.715 33.434 -8.803 1.00 145.59 ? 4 HIS B O 1 ATOM 3027 C CB . HIS B 1 5 ? -1.719 35.677 -6.620 1.00 158.84 ? 4 HIS B CB 1 ATOM 3028 C CG . HIS B 1 5 ? -2.205 34.467 -5.877 1.00 162.50 ? 4 HIS B CG 1 ATOM 3029 N ND1 . HIS B 1 5 ? -3.321 34.490 -5.068 1.00 165.69 ? 4 HIS B ND1 1 ATOM 3030 C CD2 . HIS B 1 5 ? -1.712 33.207 -5.800 1.00 162.84 ? 4 HIS B CD2 1 ATOM 3031 C CE1 . HIS B 1 5 ? -3.501 33.295 -4.534 1.00 165.43 ? 4 HIS B CE1 1 ATOM 3032 N NE2 . HIS B 1 5 ? -2.539 32.498 -4.963 1.00 163.25 ? 4 HIS B NE2 1 ATOM 3033 N N . PRO B 1 6 ? -0.323 34.979 -9.651 1.00 139.98 ? 5 PRO B N 1 ATOM 3034 C CA . PRO B 1 6 ? 0.335 33.965 -10.463 1.00 136.63 ? 5 PRO B CA 1 ATOM 3035 C C . PRO B 1 6 ? 1.305 33.067 -9.685 1.00 132.31 ? 5 PRO B C 1 ATOM 3036 O O . PRO B 1 6 ? 1.799 33.456 -8.629 1.00 128.48 ? 5 PRO B O 1 ATOM 3037 C CB . PRO B 1 6 ? 1.095 34.795 -11.499 1.00 136.17 ? 5 PRO B CB 1 ATOM 3038 C CG . PRO B 1 6 ? 1.404 36.066 -10.792 1.00 136.52 ? 5 PRO B CG 1 ATOM 3039 C CD . PRO B 1 6 ? 0.245 36.321 -9.871 1.00 138.20 ? 5 PRO B CD 1 ATOM 3040 N N . PRO B 1 7 ? 1.584 31.867 -10.215 1.00 128.40 ? 6 PRO B N 1 ATOM 3041 C CA . PRO B 1 7 ? 2.551 30.965 -9.582 1.00 125.13 ? 6 PRO B CA 1 ATOM 3042 C C . PRO B 1 7 ? 3.974 31.530 -9.516 1.00 121.48 ? 6 PRO B C 1 ATOM 3043 O O . PRO B 1 7 ? 4.372 32.327 -10.368 1.00 118.98 ? 6 PRO B O 1 ATOM 3044 C CB . PRO B 1 7 ? 2.505 29.709 -10.465 1.00 126.78 ? 6 PRO B CB 1 ATOM 3045 C CG . PRO B 1 7 ? 1.862 30.131 -11.741 1.00 128.60 ? 6 PRO B CG 1 ATOM 3046 C CD . PRO B 1 7 ? 0.951 31.262 -11.401 1.00 129.52 ? 6 PRO B CD 1 ATOM 3047 N N . VAL B 1 8 ? 4.731 31.104 -8.510 1.00 120.26 ? 7 VAL B N 1 ATOM 3048 C CA . VAL B 1 8 ? 6.059 31.652 -8.255 1.00 119.91 ? 7 VAL B CA 1 ATOM 3049 C C . VAL B 1 8 ? 7.110 30.559 -8.109 1.00 116.49 ? 7 VAL B C 1 ATOM 3050 O O . VAL B 1 8 ? 6.894 29.569 -7.408 1.00 112.57 ? 7 VAL B O 1 ATOM 3051 C CB . VAL B 1 8 ? 6.066 32.504 -6.971 1.00 122.35 ? 7 VAL B CB 1 ATOM 3052 C CG1 . VAL B 1 8 ? 7.474 33.008 -6.658 1.00 123.32 ? 7 VAL B CG1 1 ATOM 3053 C CG2 . VAL B 1 8 ? 5.097 33.669 -7.106 1.00 124.93 ? 7 VAL B CG2 1 ATOM 3054 N N . VAL B 1 9 ? 8.250 30.768 -8.762 1.00 115.03 ? 8 VAL B N 1 ATOM 3055 C CA . VAL B 1 9 ? 9.405 29.888 -8.634 1.00 113.48 ? 8 VAL B CA 1 ATOM 3056 C C . VAL B 1 9 ? 10.567 30.673 -8.026 1.00 113.22 ? 8 VAL B C 1 ATOM 3057 O O . VAL B 1 9 ? 10.937 31.739 -8.528 1.00 113.78 ? 8 VAL B O 1 ATOM 3058 C CB . VAL B 1 9 ? 9.822 29.312 -9.998 1.00 113.61 ? 8 VAL B CB 1 ATOM 3059 C CG1 . VAL B 1 9 ? 10.888 28.237 -9.818 1.00 114.07 ? 8 VAL B CG1 1 ATOM 3060 C CG2 . VAL B 1 9 ? 8.607 28.749 -10.726 1.00 113.42 ? 8 VAL B CG2 1 ATOM 3061 N N . LEU B 1 10 ? 11.125 30.141 -6.940 1.00 113.01 ? 9 LEU B N 1 ATOM 3062 C CA . LEU B 1 10 ? 12.230 30.778 -6.229 1.00 116.69 ? 9 LEU B CA 1 ATOM 3063 C C . LEU B 1 10 ? 13.554 30.113 -6.590 1.00 118.57 ? 9 LEU B C 1 ATOM 3064 O O . LEU B 1 10 ? 13.678 28.893 -6.519 1.00 118.73 ? 9 LEU B O 1 ATOM 3065 C CB . LEU B 1 10 ? 12.010 30.681 -4.720 1.00 118.70 ? 9 LEU B CB 1 ATOM 3066 C CG . LEU B 1 10 ? 10.683 31.229 -4.187 1.00 120.31 ? 9 LEU B CG 1 ATOM 3067 C CD1 . LEU B 1 10 ? 10.647 31.109 -2.671 1.00 120.31 ? 9 LEU B CD1 1 ATOM 3068 C CD2 . LEU B 1 10 ? 10.466 32.675 -4.614 1.00 121.30 ? 9 LEU B CD2 1 ATOM 3069 N N . VAL B 1 11 ? 14.541 30.924 -6.965 1.00 123.49 ? 10 VAL B N 1 ATOM 3070 C CA . VAL B 1 11 ? 15.855 30.426 -7.371 1.00 127.05 ? 10 VAL B CA 1 ATOM 3071 C C . VAL B 1 11 ? 16.923 30.996 -6.432 1.00 129.85 ? 10 VAL B C 1 ATOM 3072 O O . VAL B 1 11 ? 17.108 32.213 -6.371 1.00 134.28 ? 10 VAL B O 1 ATOM 3073 C CB . VAL B 1 11 ? 16.182 30.825 -8.829 1.00 128.37 ? 10 VAL B CB 1 ATOM 3074 C CG1 . VAL B 1 11 ? 17.449 30.121 -9.304 1.00 129.53 ? 10 VAL B CG1 1 ATOM 3075 C CG2 . VAL B 1 11 ? 15.010 30.499 -9.747 1.00 127.43 ? 10 VAL B CG2 1 ATOM 3076 N N . PRO B 1 12 ? 17.629 30.119 -5.696 1.00 129.96 ? 11 PRO B N 1 ATOM 3077 C CA . PRO B 1 12 ? 18.651 30.558 -4.747 1.00 130.96 ? 11 PRO B CA 1 ATOM 3078 C C . PRO B 1 12 ? 19.977 30.946 -5.396 1.00 133.21 ? 11 PRO B C 1 ATOM 3079 O O . PRO B 1 12 ? 20.214 30.649 -6.567 1.00 130.36 ? 11 PRO B O 1 ATOM 3080 C CB . PRO B 1 12 ? 18.865 29.316 -3.883 1.00 131.35 ? 11 PRO B CB 1 ATOM 3081 C CG . PRO B 1 12 ? 18.614 28.191 -4.824 1.00 131.88 ? 11 PRO B CG 1 ATOM 3082 C CD . PRO B 1 12 ? 17.476 28.652 -5.686 1.00 130.93 ? 11 PRO B CD 1 ATOM 3083 N N . GLY B 1 13 ? 20.837 31.589 -4.610 1.00 135.63 ? 12 GLY B N 1 ATOM 3084 C CA . GLY B 1 13 ? 22.197 31.898 -5.033 1.00 137.40 ? 12 GLY B CA 1 ATOM 3085 C C . GLY B 1 13 ? 23.191 30.859 -4.557 1.00 137.76 ? 12 GLY B C 1 ATOM 3086 O O . GLY B 1 13 ? 22.811 29.780 -4.092 1.00 135.24 ? 12 GLY B O 1 ATOM 3087 N N . ASP B 1 14 ? 24.474 31.192 -4.676 1.00 139.59 ? 13 ASP B N 1 ATOM 3088 C CA . ASP B 1 14 ? 25.553 30.326 -4.199 1.00 140.78 ? 13 ASP B CA 1 ATOM 3089 C C . ASP B 1 14 ? 25.404 30.127 -2.688 1.00 138.27 ? 13 ASP B C 1 ATOM 3090 O O . ASP B 1 14 ? 25.075 31.064 -1.960 1.00 139.16 ? 13 ASP B O 1 ATOM 3091 C CB . ASP B 1 14 ? 26.920 30.948 -4.533 1.00 145.50 ? 13 ASP B CB 1 ATOM 3092 C CG . ASP B 1 14 ? 28.078 29.965 -4.385 1.00 148.18 ? 13 ASP B CG 1 ATOM 3093 O OD1 . ASP B 1 14 ? 27.872 28.847 -3.868 1.00 146.58 ? 13 ASP B OD1 1 ATOM 3094 O OD2 . ASP B 1 14 ? 29.208 30.320 -4.790 1.00 152.27 ? 13 ASP B OD2 1 ATOM 3095 N N . LEU B 1 15 ? 25.631 28.895 -2.233 1.00 135.21 ? 14 LEU B N 1 ATOM 3096 C CA . LEU B 1 15 ? 25.423 28.502 -0.832 1.00 133.63 ? 14 LEU B CA 1 ATOM 3097 C C . LEU B 1 15 ? 23.951 28.605 -0.401 1.00 130.17 ? 14 LEU B C 1 ATOM 3098 O O . LEU B 1 15 ? 23.644 28.547 0.789 1.00 125.68 ? 14 LEU B O 1 ATOM 3099 C CB . LEU B 1 15 ? 26.295 29.355 0.104 1.00 136.82 ? 14 LEU B CB 1 ATOM 3100 C CG . LEU B 1 15 ? 27.719 29.703 -0.356 1.00 139.94 ? 14 LEU B CG 1 ATOM 3101 C CD1 . LEU B 1 15 ? 28.055 31.158 -0.041 1.00 142.18 ? 14 LEU B CD1 1 ATOM 3102 C CD2 . LEU B 1 15 ? 28.738 28.750 0.250 1.00 141.44 ? 14 LEU B CD2 1 ATOM 3103 N N . GLY B 1 16 ? 23.049 28.737 -1.373 1.00 128.44 ? 15 GLY B N 1 ATOM 3104 C CA . GLY B 1 16 ? 21.675 29.152 -1.108 1.00 127.61 ? 15 GLY B CA 1 ATOM 3105 C C . GLY B 1 16 ? 20.673 28.040 -0.869 1.00 125.68 ? 15 GLY B C 1 ATOM 3106 O O . GLY B 1 16 ? 19.516 28.321 -0.544 1.00 125.13 ? 15 GLY B O 1 ATOM 3107 N N . ASN B 1 17 ? 21.097 26.785 -1.021 1.00 125.33 ? 16 ASN B N 1 ATOM 3108 C CA . ASN B 1 17 ? 20.196 25.657 -0.787 1.00 126.13 ? 16 ASN B CA 1 ATOM 3109 C C . ASN B 1 17 ? 20.909 24.456 -0.200 1.00 126.11 ? 16 ASN B C 1 ATOM 3110 O O . ASN B 1 17 ? 22.108 24.283 -0.396 1.00 126.02 ? 16 ASN B O 1 ATOM 3111 C CB . ASN B 1 17 ? 19.431 25.272 -2.063 1.00 125.15 ? 16 ASN B CB 1 ATOM 3112 C CG . ASN B 1 17 ? 20.340 24.806 -3.183 1.00 124.58 ? 16 ASN B CG 1 ATOM 3113 O OD1 . ASN B 1 17 ? 20.674 23.622 -3.281 1.00 122.85 ? 16 ASN B OD1 1 ATOM 3114 N ND2 . ASN B 1 17 ? 20.728 25.734 -4.049 1.00 123.83 ? 16 ASN B ND2 1 ATOM 3115 N N . GLN B 1 18 ? 20.157 23.637 0.524 1.00 125.23 ? 17 GLN B N 1 ATOM 3116 C CA . GLN B 1 18 ? 20.723 22.470 1.180 1.00 127.81 ? 17 GLN B CA 1 ATOM 3117 C C . GLN B 1 18 ? 21.306 21.485 0.165 1.00 129.96 ? 17 GLN B C 1 ATOM 3118 O O . GLN B 1 18 ? 20.872 21.445 -0.989 1.00 130.24 ? 17 GLN B O 1 ATOM 3119 C CB . GLN B 1 18 ? 19.664 21.768 2.034 1.00 128.29 ? 17 GLN B CB 1 ATOM 3120 C CG . GLN B 1 18 ? 19.136 22.615 3.185 1.00 128.70 ? 17 GLN B CG 1 ATOM 3121 C CD . GLN B 1 18 ? 18.341 21.818 4.206 1.00 128.65 ? 17 GLN B CD 1 ATOM 3122 O OE1 . GLN B 1 18 ? 18.293 20.587 4.159 1.00 128.71 ? 17 GLN B OE1 1 ATOM 3123 N NE2 . GLN B 1 18 ? 17.721 22.524 5.148 1.00 128.65 ? 17 GLN B NE2 1 ATOM 3124 N N . LEU B 1 19 ? 22.293 20.704 0.606 1.00 133.39 ? 18 LEU B N 1 ATOM 3125 C CA . LEU B 1 19 ? 22.877 19.620 -0.194 1.00 137.79 ? 18 LEU B CA 1 ATOM 3126 C C . LEU B 1 19 ? 23.045 18.380 0.682 1.00 140.94 ? 18 LEU B C 1 ATOM 3127 O O . LEU B 1 19 ? 23.327 18.498 1.883 1.00 140.12 ? 18 LEU B O 1 ATOM 3128 C CB . LEU B 1 19 ? 24.239 20.041 -0.749 1.00 140.26 ? 18 LEU B CB 1 ATOM 3129 C CG . LEU B 1 19 ? 24.236 21.191 -1.758 1.00 143.95 ? 18 LEU B CG 1 ATOM 3130 C CD1 . LEU B 1 19 ? 25.663 21.630 -2.050 1.00 146.95 ? 18 LEU B CD1 1 ATOM 3131 C CD2 . LEU B 1 19 ? 23.524 20.794 -3.044 1.00 143.49 ? 18 LEU B CD2 1 ATOM 3132 N N . GLU B 1 20 ? 22.872 17.203 0.076 1.00 142.57 ? 19 GLU B N 1 ATOM 3133 C CA . GLU B 1 20 ? 22.941 15.930 0.793 1.00 142.11 ? 19 GLU B CA 1 ATOM 3134 C C . GLU B 1 20 ? 23.964 15.006 0.150 1.00 138.60 ? 19 GLU B C 1 ATOM 3135 O O . GLU B 1 20 ? 24.177 15.051 -1.064 1.00 133.64 ? 19 GLU B O 1 ATOM 3136 C CB . GLU B 1 20 ? 21.575 15.241 0.782 1.00 147.48 ? 19 GLU B CB 1 ATOM 3137 C CG . GLU B 1 20 ? 20.552 15.859 1.723 1.00 152.11 ? 19 GLU B CG 1 ATOM 3138 C CD . GLU B 1 20 ? 19.194 15.172 1.670 1.00 157.21 ? 19 GLU B CD 1 ATOM 3139 O OE1 . GLU B 1 20 ? 19.028 14.200 0.897 1.00 160.68 ? 19 GLU B OE1 1 ATOM 3140 O OE2 . GLU B 1 20 ? 18.284 15.607 2.408 1.00 160.06 ? 19 GLU B OE2 1 ATOM 3141 N N . ALA B 1 21 ? 24.573 14.151 0.964 1.00 137.96 ? 20 ALA B N 1 ATOM 3142 C CA . ALA B 1 21 ? 25.576 13.214 0.473 1.00 139.46 ? 20 ALA B CA 1 ATOM 3143 C C . ALA B 1 21 ? 25.408 11.823 1.074 1.00 141.33 ? 20 ALA B C 1 ATOM 3144 O O . ALA B 1 21 ? 24.837 11.672 2.152 1.00 143.83 ? 20 ALA B O 1 ATOM 3145 C CB . ALA B 1 21 ? 26.970 13.748 0.756 1.00 140.53 ? 20 ALA B CB 1 ATOM 3146 N N . LYS B 1 22 ? 25.901 10.814 0.356 1.00 142.09 ? 21 LYS B N 1 ATOM 3147 C CA . LYS B 1 22 ? 25.934 9.427 0.833 1.00 143.78 ? 21 LYS B CA 1 ATOM 3148 C C . LYS B 1 22 ? 27.359 8.912 0.616 1.00 147.06 ? 21 LYS B C 1 ATOM 3149 O O . LYS B 1 22 ? 27.960 9.161 -0.433 1.00 148.91 ? 21 LYS B O 1 ATOM 3150 C CB . LYS B 1 22 ? 24.921 8.568 0.060 1.00 143.08 ? 21 LYS B CB 1 ATOM 3151 C CG . LYS B 1 22 ? 24.407 7.344 0.805 1.00 143.36 ? 21 LYS B CG 1 ATOM 3152 C CD . LYS B 1 22 ? 25.368 6.167 0.738 1.00 145.74 ? 21 LYS B CD 1 ATOM 3153 C CE . LYS B 1 22 ? 24.734 4.905 1.303 1.00 146.30 ? 21 LYS B CE 1 ATOM 3154 N NZ . LYS B 1 22 ? 25.748 3.857 1.609 1.00 146.54 ? 21 LYS B NZ 1 ATOM 3155 N N . LEU B 1 23 ? 27.897 8.212 1.613 1.00 149.37 ? 22 LEU B N 1 ATOM 3156 C CA . LEU B 1 23 ? 29.299 7.801 1.604 1.00 153.01 ? 22 LEU B CA 1 ATOM 3157 C C . LEU B 1 23 ? 29.478 6.291 1.552 1.00 155.58 ? 22 LEU B C 1 ATOM 3158 O O . LEU B 1 23 ? 28.791 5.551 2.267 1.00 159.58 ? 22 LEU B O 1 ATOM 3159 C CB . LEU B 1 23 ? 29.995 8.303 2.872 1.00 154.82 ? 22 LEU B CB 1 ATOM 3160 C CG . LEU B 1 23 ? 29.870 9.785 3.219 1.00 154.35 ? 22 LEU B CG 1 ATOM 3161 C CD1 . LEU B 1 23 ? 30.693 10.088 4.463 1.00 156.38 ? 22 LEU B CD1 1 ATOM 3162 C CD2 . LEU B 1 23 ? 30.309 10.658 2.051 1.00 154.18 ? 22 LEU B CD2 1 ATOM 3163 N N . ASP B 1 24 ? 30.411 5.858 0.705 1.00 155.87 ? 23 ASP B N 1 ATOM 3164 C CA . ASP B 1 24 ? 30.991 4.512 0.767 1.00 157.91 ? 23 ASP B CA 1 ATOM 3165 C C . ASP B 1 24 ? 32.435 4.615 0.264 1.00 157.60 ? 23 ASP B C 1 ATOM 3166 O O . ASP B 1 24 ? 32.775 4.133 -0.819 1.00 155.45 ? 23 ASP B O 1 ATOM 3167 C CB . ASP B 1 24 ? 30.180 3.521 -0.076 1.00 158.76 ? 23 ASP B CB 1 ATOM 3168 C CG . ASP B 1 24 ? 30.697 2.090 0.035 1.00 162.29 ? 23 ASP B CG 1 ATOM 3169 O OD1 . ASP B 1 24 ? 31.280 1.735 1.084 1.00 163.01 ? 23 ASP B OD1 1 ATOM 3170 O OD2 . ASP B 1 24 ? 30.520 1.319 -0.930 1.00 164.30 ? 23 ASP B OD2 1 ATOM 3171 N N . LYS B 1 25 ? 33.272 5.265 1.068 1.00 157.71 ? 24 LYS B N 1 ATOM 3172 C CA . LYS B 1 25 ? 34.604 5.674 0.643 1.00 159.45 ? 24 LYS B CA 1 ATOM 3173 C C . LYS B 1 25 ? 35.615 4.559 0.848 1.00 160.55 ? 24 LYS B C 1 ATOM 3174 O O . LYS B 1 25 ? 35.535 3.826 1.834 1.00 159.40 ? 24 LYS B O 1 ATOM 3175 C CB . LYS B 1 25 ? 35.061 6.899 1.435 1.00 162.05 ? 24 LYS B CB 1 ATOM 3176 C CG . LYS B 1 25 ? 34.111 8.083 1.358 1.00 161.91 ? 24 LYS B CG 1 ATOM 3177 C CD . LYS B 1 25 ? 34.659 9.296 2.093 1.00 164.15 ? 24 LYS B CD 1 ATOM 3178 C CE . LYS B 1 25 ? 35.793 9.956 1.324 1.00 166.52 ? 24 LYS B CE 1 ATOM 3179 N NZ . LYS B 1 25 ? 36.167 11.287 1.881 1.00 167.81 ? 24 LYS B NZ 1 ATOM 3180 N N . PRO B 1 26 ? 36.581 4.437 -0.075 1.00 163.15 ? 25 PRO B N 1 ATOM 3181 C CA . PRO B 1 26 ? 37.640 3.447 0.101 1.00 169.46 ? 25 PRO B CA 1 ATOM 3182 C C . PRO B 1 26 ? 38.606 3.811 1.233 1.00 174.79 ? 25 PRO B C 1 ATOM 3183 O O . PRO B 1 26 ? 39.052 2.929 1.972 1.00 177.91 ? 25 PRO B O 1 ATOM 3184 C CB . PRO B 1 26 ? 38.354 3.448 -1.255 1.00 169.91 ? 25 PRO B CB 1 ATOM 3185 C CG . PRO B 1 26 ? 38.080 4.788 -1.840 1.00 166.39 ? 25 PRO B CG 1 ATOM 3186 C CD . PRO B 1 26 ? 36.744 5.219 -1.315 1.00 162.34 ? 25 PRO B CD 1 ATOM 3187 N N . THR B 1 27 ? 38.925 5.097 1.356 1.00 177.32 ? 26 THR B N 1 ATOM 3188 C CA . THR B 1 27 ? 39.778 5.597 2.438 1.00 180.71 ? 26 THR B CA 1 ATOM 3189 C C . THR B 1 27 ? 39.482 7.069 2.697 1.00 177.35 ? 26 THR B C 1 ATOM 3190 O O . THR B 1 27 ? 38.834 7.741 1.890 1.00 173.30 ? 26 THR B O 1 ATOM 3191 C CB . THR B 1 27 ? 41.286 5.449 2.118 1.00 185.99 ? 26 THR B CB 1 ATOM 3192 O OG1 . THR B 1 27 ? 41.527 5.794 0.748 1.00 188.78 ? 26 THR B OG1 1 ATOM 3193 C CG2 . THR B 1 27 ? 41.781 4.025 2.383 1.00 188.12 ? 26 THR B CG2 1 ATOM 3194 N N . VAL B 1 28 ? 39.976 7.560 3.829 1.00 178.57 ? 27 VAL B N 1 ATOM 3195 C CA . VAL B 1 28 ? 39.770 8.946 4.243 1.00 179.23 ? 27 VAL B CA 1 ATOM 3196 C C . VAL B 1 28 ? 41.081 9.559 4.715 1.00 180.78 ? 27 VAL B C 1 ATOM 3197 O O . VAL B 1 28 ? 42.086 8.865 4.870 1.00 181.54 ? 27 VAL B O 1 ATOM 3198 C CB . VAL B 1 28 ? 38.721 9.054 5.371 1.00 180.09 ? 27 VAL B CB 1 ATOM 3199 C CG1 . VAL B 1 28 ? 37.317 8.905 4.804 1.00 178.91 ? 27 VAL B CG1 1 ATOM 3200 C CG2 . VAL B 1 28 ? 38.983 8.023 6.463 1.00 181.79 ? 27 VAL B CG2 1 ATOM 3201 N N . VAL B 1 29 ? 41.058 10.866 4.944 1.00 181.35 ? 28 VAL B N 1 ATOM 3202 C CA . VAL B 1 29 ? 42.250 11.596 5.371 1.00 187.43 ? 28 VAL B CA 1 ATOM 3203 C C . VAL B 1 29 ? 42.623 11.383 6.845 1.00 191.37 ? 28 VAL B C 1 ATOM 3204 O O . VAL B 1 29 ? 43.802 11.482 7.202 1.00 194.71 ? 28 VAL B O 1 ATOM 3205 C CB . VAL B 1 29 ? 42.135 13.110 5.067 1.00 187.87 ? 28 VAL B CB 1 ATOM 3206 C CG1 . VAL B 1 29 ? 41.942 13.338 3.574 1.00 186.56 ? 28 VAL B CG1 1 ATOM 3207 C CG2 . VAL B 1 29 ? 41.010 13.767 5.862 1.00 185.90 ? 28 VAL B CG2 1 ATOM 3208 N N . HIS B 1 30 ? 41.628 11.109 7.692 1.00 192.37 ? 29 HIS B N 1 ATOM 3209 C CA . HIS B 1 30 ? 41.862 10.854 9.119 1.00 195.27 ? 29 HIS B CA 1 ATOM 3210 C C . HIS B 1 30 ? 40.979 9.707 9.596 1.00 193.08 ? 29 HIS B C 1 ATOM 3211 O O . HIS B 1 30 ? 39.893 9.492 9.063 1.00 188.95 ? 29 HIS B O 1 ATOM 3212 C CB . HIS B 1 30 ? 41.571 12.109 9.952 1.00 195.73 ? 29 HIS B CB 1 ATOM 3213 C CG . HIS B 1 30 ? 42.549 13.224 9.738 1.00 197.46 ? 29 HIS B CG 1 ATOM 3214 N ND1 . HIS B 1 30 ? 43.895 13.098 10.009 1.00 201.03 ? 29 HIS B ND1 1 ATOM 3215 C CD2 . HIS B 1 30 ? 42.371 14.493 9.299 1.00 195.93 ? 29 HIS B CD2 1 ATOM 3216 C CE1 . HIS B 1 30 ? 44.506 14.237 9.734 1.00 201.20 ? 29 HIS B CE1 1 ATOM 3217 N NE2 . HIS B 1 30 ? 43.603 15.100 9.302 1.00 198.75 ? 29 HIS B NE2 1 ATOM 3218 N N . TYR B 1 31 ? 41.452 8.990 10.612 1.00 194.18 ? 30 TYR B N 1 ATOM 3219 C CA . TYR B 1 31 ? 40.734 7.835 11.161 1.00 193.41 ? 30 TYR B CA 1 ATOM 3220 C C . TYR B 1 31 ? 39.342 8.183 11.682 1.00 187.92 ? 30 TYR B C 1 ATOM 3221 O O . TYR B 1 31 ? 38.425 7.370 11.616 1.00 185.07 ? 30 TYR B O 1 ATOM 3222 C CB . TYR B 1 31 ? 41.548 7.187 12.286 1.00 198.77 ? 30 TYR B CB 1 ATOM 3223 C CG . TYR B 1 31 ? 42.695 6.331 11.803 1.00 203.72 ? 30 TYR B CG 1 ATOM 3224 C CD1 . TYR B 1 31 ? 43.943 6.889 11.532 1.00 207.47 ? 30 TYR B CD1 1 ATOM 3225 C CD2 . TYR B 1 31 ? 42.535 4.961 11.623 1.00 204.49 ? 30 TYR B CD2 1 ATOM 3226 C CE1 . TYR B 1 31 ? 44.996 6.105 11.091 1.00 210.75 ? 30 TYR B CE1 1 ATOM 3227 C CE2 . TYR B 1 31 ? 43.581 4.169 11.182 1.00 208.15 ? 30 TYR B CE2 1 ATOM 3228 C CZ . TYR B 1 31 ? 44.809 4.746 10.918 1.00 211.51 ? 30 TYR B CZ 1 ATOM 3229 O OH . TYR B 1 31 ? 45.851 3.962 10.481 1.00 216.54 ? 30 TYR B OH 1 ATOM 3230 N N . LEU B 1 32 ? 39.186 9.393 12.203 1.00 185.68 ? 31 LEU B N 1 ATOM 3231 C CA . LEU B 1 32 ? 37.901 9.809 12.757 1.00 182.11 ? 31 LEU B CA 1 ATOM 3232 C C . LEU B 1 32 ? 36.868 10.212 11.697 1.00 176.81 ? 31 LEU B C 1 ATOM 3233 O O . LEU B 1 32 ? 35.724 10.511 12.041 1.00 170.05 ? 31 LEU B O 1 ATOM 3234 C CB . LEU B 1 32 ? 38.075 10.933 13.787 1.00 184.38 ? 31 LEU B CB 1 ATOM 3235 C CG . LEU B 1 32 ? 38.865 12.179 13.366 1.00 187.50 ? 31 LEU B CG 1 ATOM 3236 C CD1 . LEU B 1 32 ? 38.153 13.450 13.805 1.00 186.42 ? 31 LEU B CD1 1 ATOM 3237 C CD2 . LEU B 1 32 ? 40.299 12.156 13.891 1.00 192.09 ? 31 LEU B CD2 1 ATOM 3238 N N . CYS B 1 33 ? 37.257 10.224 10.420 1.00 177.27 ? 32 CYS B N 1 ATOM 3239 C CA . CYS B 1 33 ? 36.301 10.476 9.337 1.00 176.45 ? 32 CYS B CA 1 ATOM 3240 C C . CYS B 1 33 ? 35.514 9.206 9.014 1.00 174.43 ? 32 CYS B C 1 ATOM 3241 O O . CYS B 1 33 ? 36.071 8.108 8.975 1.00 177.35 ? 32 CYS B O 1 ATOM 3242 C CB . CYS B 1 33 ? 37.010 10.958 8.065 1.00 180.64 ? 32 CYS B CB 1 ATOM 3243 S SG . CYS B 1 33 ? 38.126 12.370 8.249 1.00 187.99 ? 32 CYS B SG 1 ATOM 3244 N N . SER B 1 34 ? 34.219 9.363 8.767 1.00 170.16 ? 33 SER B N 1 ATOM 3245 C CA . SER B 1 34 ? 33.355 8.236 8.434 1.00 167.57 ? 33 SER B CA 1 ATOM 3246 C C . SER B 1 34 ? 33.634 7.732 7.021 1.00 165.80 ? 33 SER B C 1 ATOM 3247 O O . SER B 1 34 ? 33.733 8.523 6.084 1.00 162.57 ? 33 SER B O 1 ATOM 3248 C CB . SER B 1 34 ? 31.891 8.652 8.557 1.00 163.99 ? 33 SER B CB 1 ATOM 3249 O OG . SER B 1 34 ? 31.019 7.558 8.342 1.00 162.30 ? 33 SER B OG 1 ATOM 3250 N N . LYS B 1 35 ? 33.768 6.412 6.886 1.00 166.07 ? 34 LYS B N 1 ATOM 3251 C CA . LYS B 1 35 ? 33.928 5.755 5.581 1.00 164.56 ? 34 LYS B CA 1 ATOM 3252 C C . LYS B 1 35 ? 32.583 5.582 4.894 1.00 162.44 ? 34 LYS B C 1 ATOM 3253 O O . LYS B 1 35 ? 32.466 5.740 3.675 1.00 161.55 ? 34 LYS B O 1 ATOM 3254 C CB . LYS B 1 35 ? 34.548 4.358 5.737 1.00 165.47 ? 34 LYS B CB 1 ATOM 3255 C CG . LYS B 1 35 ? 36.057 4.296 5.579 1.00 167.14 ? 34 LYS B CG 1 ATOM 3256 C CD . LYS B 1 35 ? 36.509 2.867 5.312 1.00 168.69 ? 34 LYS B CD 1 ATOM 3257 C CE . LYS B 1 35 ? 37.994 2.789 4.997 1.00 170.94 ? 34 LYS B CE 1 ATOM 3258 N NZ . LYS B 1 35 ? 38.841 2.918 6.213 1.00 173.10 ? 34 LYS B NZ 1 ATOM 3259 N N . LYS B 1 36 ? 31.574 5.241 5.689 1.00 161.67 ? 35 LYS B N 1 ATOM 3260 C CA . LYS B 1 36 ? 30.282 4.861 5.162 1.00 159.99 ? 35 LYS B CA 1 ATOM 3261 C C . LYS B 1 36 ? 29.158 5.529 5.941 1.00 157.27 ? 35 LYS B C 1 ATOM 3262 O O . LYS B 1 36 ? 29.245 5.704 7.157 1.00 157.32 ? 35 LYS B O 1 ATOM 3263 C CB . LYS B 1 36 ? 30.132 3.343 5.242 1.00 161.70 ? 35 LYS B CB 1 ATOM 3264 C CG . LYS B 1 36 ? 28.938 2.799 4.484 1.00 162.65 ? 35 LYS B CG 1 ATOM 3265 C CD . LYS B 1 36 ? 28.919 1.282 4.509 1.00 167.60 ? 35 LYS B CD 1 ATOM 3266 C CE . LYS B 1 36 ? 27.812 0.729 3.627 1.00 170.55 ? 35 LYS B CE 1 ATOM 3267 N NZ . LYS B 1 36 ? 28.045 0.970 2.176 1.00 172.85 ? 35 LYS B NZ 1 ATOM 3268 N N . THR B 1 37 ? 28.106 5.909 5.222 1.00 154.06 ? 36 THR B N 1 ATOM 3269 C CA . THR B 1 37 ? 26.847 6.317 5.839 1.00 151.90 ? 36 THR B CA 1 ATOM 3270 C C . THR B 1 37 ? 25.754 5.362 5.372 1.00 153.87 ? 36 THR B C 1 ATOM 3271 O O . THR B 1 37 ? 25.808 4.842 4.256 1.00 150.88 ? 36 THR B O 1 ATOM 3272 C CB . THR B 1 37 ? 26.454 7.755 5.463 1.00 148.89 ? 36 THR B CB 1 ATOM 3273 O OG1 . THR B 1 37 ? 26.428 7.895 4.038 1.00 146.31 ? 36 THR B OG1 1 ATOM 3274 C CG2 . THR B 1 37 ? 27.438 8.749 6.057 1.00 149.69 ? 36 THR B CG2 1 ATOM 3275 N N . GLU B 1 38 ? 24.775 5.122 6.240 1.00 158.40 ? 37 GLU B N 1 ATOM 3276 C CA . GLU B 1 38 ? 23.663 4.216 5.932 1.00 159.86 ? 37 GLU B CA 1 ATOM 3277 C C . GLU B 1 38 ? 22.672 4.837 4.948 1.00 154.18 ? 37 GLU B C 1 ATOM 3278 O O . GLU B 1 38 ? 21.987 4.129 4.211 1.00 153.99 ? 37 GLU B O 1 ATOM 3279 C CB . GLU B 1 38 ? 22.915 3.836 7.218 1.00 163.87 ? 37 GLU B CB 1 ATOM 3280 C CG . GLU B 1 38 ? 23.745 3.026 8.198 1.00 168.05 ? 37 GLU B CG 1 ATOM 3281 C CD . GLU B 1 38 ? 23.052 2.773 9.529 1.00 171.68 ? 37 GLU B CD 1 ATOM 3282 O OE1 . GLU B 1 38 ? 21.861 3.126 9.676 1.00 172.14 ? 37 GLU B OE1 1 ATOM 3283 O OE2 . GLU B 1 38 ? 23.706 2.215 10.439 1.00 174.29 ? 37 GLU B OE2 1 ATOM 3284 N N . SER B 1 39 ? 22.597 6.163 4.949 1.00 148.15 ? 38 SER B N 1 ATOM 3285 C CA . SER B 1 39 ? 21.676 6.884 4.089 1.00 144.79 ? 38 SER B CA 1 ATOM 3286 C C . SER B 1 39 ? 22.302 8.216 3.688 1.00 142.38 ? 38 SER B C 1 ATOM 3287 O O . SER B 1 39 ? 23.443 8.511 4.055 1.00 144.18 ? 38 SER B O 1 ATOM 3288 C CB . SER B 1 39 ? 20.370 7.125 4.850 1.00 143.66 ? 38 SER B CB 1 ATOM 3289 O OG . SER B 1 39 ? 20.627 7.729 6.108 1.00 141.65 ? 38 SER B OG 1 ATOM 3290 N N . TYR B 1 40 ? 21.559 9.013 2.924 1.00 136.49 ? 39 TYR B N 1 ATOM 3291 C CA . TYR B 1 40 ? 21.965 10.384 2.626 1.00 134.04 ? 39 TYR B CA 1 ATOM 3292 C C . TYR B 1 40 ? 21.861 11.240 3.887 1.00 135.66 ? 39 TYR B C 1 ATOM 3293 O O . TYR B 1 40 ? 20.964 11.026 4.706 1.00 135.63 ? 39 TYR B O 1 ATOM 3294 C CB . TYR B 1 40 ? 21.087 10.981 1.523 1.00 131.03 ? 39 TYR B CB 1 ATOM 3295 C CG . TYR B 1 40 ? 21.578 10.684 0.127 1.00 129.93 ? 39 TYR B CG 1 ATOM 3296 C CD1 . TYR B 1 40 ? 22.490 11.527 -0.501 1.00 131.06 ? 39 TYR B CD1 1 ATOM 3297 C CD2 . TYR B 1 40 ? 21.132 9.565 -0.568 1.00 128.81 ? 39 TYR B CD2 1 ATOM 3298 C CE1 . TYR B 1 40 ? 22.946 11.264 -1.783 1.00 131.73 ? 39 TYR B CE1 1 ATOM 3299 C CE2 . TYR B 1 40 ? 21.582 9.293 -1.850 1.00 128.60 ? 39 TYR B CE2 1 ATOM 3300 C CZ . TYR B 1 40 ? 22.488 10.144 -2.453 1.00 130.24 ? 39 TYR B CZ 1 ATOM 3301 O OH . TYR B 1 40 ? 22.938 9.882 -3.726 1.00 132.65 ? 39 TYR B OH 1 ATOM 3302 N N . PHE B 1 41 ? 22.785 12.189 4.044 1.00 137.82 ? 40 PHE B N 1 ATOM 3303 C CA . PHE B 1 41 ? 22.796 13.082 5.202 1.00 138.75 ? 40 PHE B CA 1 ATOM 3304 C C . PHE B 1 41 ? 23.110 14.489 4.725 1.00 136.77 ? 40 PHE B C 1 ATOM 3305 O O . PHE B 1 41 ? 23.636 14.668 3.627 1.00 136.21 ? 40 PHE B O 1 ATOM 3306 C CB . PHE B 1 41 ? 23.827 12.619 6.244 1.00 140.78 ? 40 PHE B CB 1 ATOM 3307 C CG . PHE B 1 41 ? 25.249 12.945 5.884 1.00 140.65 ? 40 PHE B CG 1 ATOM 3308 C CD1 . PHE B 1 41 ? 25.940 12.164 4.971 1.00 142.19 ? 40 PHE B CD1 1 ATOM 3309 C CD2 . PHE B 1 41 ? 25.900 14.026 6.464 1.00 139.65 ? 40 PHE B CD2 1 ATOM 3310 C CE1 . PHE B 1 41 ? 27.250 12.458 4.635 1.00 143.06 ? 40 PHE B CE1 1 ATOM 3311 C CE2 . PHE B 1 41 ? 27.211 14.325 6.133 1.00 140.60 ? 40 PHE B CE2 1 ATOM 3312 C CZ . PHE B 1 41 ? 27.887 13.541 5.217 1.00 141.73 ? 40 PHE B CZ 1 ATOM 3313 N N . THR B 1 42 ? 22.787 15.475 5.558 1.00 136.84 ? 41 THR B N 1 ATOM 3314 C CA . THR B 1 42 ? 22.965 16.882 5.208 1.00 137.58 ? 41 THR B CA 1 ATOM 3315 C C . THR B 1 42 ? 24.441 17.263 5.251 1.00 140.12 ? 41 THR B C 1 ATOM 3316 O O . THR B 1 42 ? 25.059 17.228 6.317 1.00 140.49 ? 41 THR B O 1 ATOM 3317 C CB . THR B 1 42 ? 22.208 17.799 6.199 1.00 136.91 ? 41 THR B CB 1 ATOM 3318 O OG1 . THR B 1 42 ? 20.835 17.400 6.285 1.00 136.54 ? 41 THR B OG1 1 ATOM 3319 C CG2 . THR B 1 42 ? 22.282 19.259 5.764 1.00 136.26 ? 41 THR B CG2 1 ATOM 3320 N N . ILE B 1 43 ? 25.001 17.619 4.094 1.00 142.40 ? 42 ILE B N 1 ATOM 3321 C CA . ILE B 1 43 ? 26.391 18.094 4.019 1.00 146.84 ? 42 ILE B CA 1 ATOM 3322 C C . ILE B 1 43 ? 26.462 19.624 4.111 1.00 145.38 ? 42 ILE B C 1 ATOM 3323 O O . ILE B 1 43 ? 27.414 20.182 4.677 1.00 142.97 ? 42 ILE B O 1 ATOM 3324 C CB . ILE B 1 43 ? 27.114 17.563 2.751 1.00 151.33 ? 42 ILE B CB 1 ATOM 3325 C CG1 . ILE B 1 43 ? 28.637 17.612 2.935 1.00 156.50 ? 42 ILE B CG1 1 ATOM 3326 C CG2 . ILE B 1 43 ? 26.704 18.322 1.494 1.00 150.25 ? 42 ILE B CG2 1 ATOM 3327 C CD1 . ILE B 1 43 ? 29.410 16.973 1.798 1.00 157.80 ? 42 ILE B CD1 1 ATOM 3328 N N . TRP B 1 44 ? 25.443 20.289 3.571 1.00 144.20 ? 43 TRP B N 1 ATOM 3329 C CA . TRP B 1 44 ? 25.321 21.737 3.665 1.00 144.04 ? 43 TRP B CA 1 ATOM 3330 C C . TRP B 1 44 ? 23.866 22.101 3.979 1.00 142.37 ? 43 TRP B C 1 ATOM 3331 O O . TRP B 1 44 ? 22.977 21.653 3.263 1.00 143.97 ? 43 TRP B O 1 ATOM 3332 C CB . TRP B 1 44 ? 25.732 22.392 2.352 1.00 145.18 ? 43 TRP B CB 1 ATOM 3333 C CG . TRP B 1 44 ? 25.641 23.877 2.397 1.00 145.74 ? 43 TRP B CG 1 ATOM 3334 C CD1 . TRP B 1 44 ? 24.665 24.654 1.852 1.00 145.75 ? 43 TRP B CD1 1 ATOM 3335 C CD2 . TRP B 1 44 ? 26.554 24.769 3.042 1.00 146.78 ? 43 TRP B CD2 1 ATOM 3336 N NE1 . TRP B 1 44 ? 24.919 25.981 2.104 1.00 146.95 ? 43 TRP B NE1 1 ATOM 3337 C CE2 . TRP B 1 44 ? 26.073 26.080 2.835 1.00 145.85 ? 43 TRP B CE2 1 ATOM 3338 C CE3 . TRP B 1 44 ? 27.736 24.590 3.769 1.00 147.65 ? 43 TRP B CE3 1 ATOM 3339 C CZ2 . TRP B 1 44 ? 26.732 27.205 3.330 1.00 144.00 ? 43 TRP B CZ2 1 ATOM 3340 C CZ3 . TRP B 1 44 ? 28.393 25.710 4.258 1.00 146.51 ? 43 TRP B CZ3 1 ATOM 3341 C CH2 . TRP B 1 44 ? 27.886 27.001 4.038 1.00 144.71 ? 43 TRP B CH2 1 ATOM 3342 N N . LEU B 1 45 ? 23.596 22.876 5.034 1.00 141.21 ? 44 LEU B N 1 ATOM 3343 C CA . LEU B 1 45 ? 24.590 23.382 5.989 1.00 143.64 ? 44 LEU B CA 1 ATOM 3344 C C . LEU B 1 45 ? 24.565 22.537 7.259 1.00 144.18 ? 44 LEU B C 1 ATOM 3345 O O . LEU B 1 45 ? 23.500 22.319 7.835 1.00 144.04 ? 44 LEU B O 1 ATOM 3346 C CB . LEU B 1 45 ? 24.272 24.835 6.342 1.00 146.10 ? 44 LEU B CB 1 ATOM 3347 C CG . LEU B 1 45 ? 25.074 25.471 7.480 1.00 150.27 ? 44 LEU B CG 1 ATOM 3348 C CD1 . LEU B 1 45 ? 26.572 25.310 7.266 1.00 152.22 ? 44 LEU B CD1 1 ATOM 3349 C CD2 . LEU B 1 45 ? 24.702 26.940 7.605 1.00 151.20 ? 44 LEU B CD2 1 ATOM 3350 N N . ASN B 1 46 ? 25.732 22.057 7.683 1.00 145.66 ? 45 ASN B N 1 ATOM 3351 C CA . ASN B 1 46 ? 25.856 21.380 8.968 1.00 148.76 ? 45 ASN B CA 1 ATOM 3352 C C . ASN B 1 46 ? 27.033 21.956 9.735 1.00 149.58 ? 45 ASN B C 1 ATOM 3353 O O . ASN B 1 46 ? 28.183 21.716 9.385 1.00 147.86 ? 45 ASN B O 1 ATOM 3354 C CB . ASN B 1 46 ? 26.025 19.871 8.778 1.00 151.73 ? 45 ASN B CB 1 ATOM 3355 C CG . ASN B 1 46 ? 25.762 19.087 10.056 1.00 155.23 ? 45 ASN B CG 1 ATOM 3356 O OD1 . ASN B 1 46 ? 25.963 19.586 11.166 1.00 155.97 ? 45 ASN B OD1 1 ATOM 3357 N ND2 . ASN B 1 46 ? 25.307 17.848 9.902 1.00 157.34 ? 45 ASN B ND2 1 ATOM 3358 N N . LEU B 1 47 ? 26.727 22.708 10.787 1.00 151.01 ? 46 LEU B N 1 ATOM 3359 C CA . LEU B 1 47 ? 27.739 23.429 11.551 1.00 155.08 ? 46 LEU B CA 1 ATOM 3360 C C . LEU B 1 47 ? 28.685 22.502 12.288 1.00 155.05 ? 46 LEU B C 1 ATOM 3361 O O . LEU B 1 47 ? 29.844 22.839 12.498 1.00 155.56 ? 46 LEU B O 1 ATOM 3362 C CB . LEU B 1 47 ? 27.077 24.368 12.556 1.00 158.85 ? 46 LEU B CB 1 ATOM 3363 C CG . LEU B 1 47 ? 26.201 25.461 11.944 1.00 160.10 ? 46 LEU B CG 1 ATOM 3364 C CD1 . LEU B 1 47 ? 25.462 26.211 13.041 1.00 162.32 ? 46 LEU B CD1 1 ATOM 3365 C CD2 . LEU B 1 47 ? 27.032 26.409 11.090 1.00 160.42 ? 46 LEU B CD2 1 ATOM 3366 N N . GLU B 1 48 ? 28.200 21.328 12.672 1.00 154.55 ? 47 GLU B N 1 ATOM 3367 C CA . GLU B 1 48 ? 29.035 20.370 13.390 1.00 157.46 ? 47 GLU B CA 1 ATOM 3368 C C . GLU B 1 48 ? 30.194 19.841 12.538 1.00 155.80 ? 47 GLU B C 1 ATOM 3369 O O . GLU B 1 48 ? 31.223 19.426 13.075 1.00 155.41 ? 47 GLU B O 1 ATOM 3370 C CB . GLU B 1 48 ? 28.191 19.195 13.897 1.00 161.19 ? 47 GLU B CB 1 ATOM 3371 C CG . GLU B 1 48 ? 27.171 19.575 14.961 1.00 164.47 ? 47 GLU B CG 1 ATOM 3372 C CD . GLU B 1 48 ? 26.383 18.382 15.482 1.00 167.83 ? 47 GLU B CD 1 ATOM 3373 O OE1 . GLU B 1 48 ? 25.990 17.514 14.672 1.00 166.98 ? 47 GLU B OE1 1 ATOM 3374 O OE2 . GLU B 1 48 ? 26.145 18.315 16.708 1.00 172.84 ? 47 GLU B OE2 1 ATOM 3375 N N . LEU B 1 49 ? 30.026 19.863 11.218 1.00 154.06 ? 48 LEU B N 1 ATOM 3376 C CA . LEU B 1 49 ? 31.053 19.365 10.309 1.00 156.24 ? 48 LEU B CA 1 ATOM 3377 C C . LEU B 1 49 ? 32.131 20.400 10.005 1.00 158.79 ? 48 LEU B C 1 ATOM 3378 O O . LEU B 1 49 ? 33.147 20.069 9.392 1.00 159.05 ? 48 LEU B O 1 ATOM 3379 C CB . LEU B 1 49 ? 30.420 18.893 8.998 1.00 156.10 ? 48 LEU B CB 1 ATOM 3380 C CG . LEU B 1 49 ? 29.444 17.719 9.112 1.00 157.10 ? 48 LEU B CG 1 ATOM 3381 C CD1 . LEU B 1 49 ? 28.744 17.470 7.784 1.00 157.03 ? 48 LEU B CD1 1 ATOM 3382 C CD2 . LEU B 1 49 ? 30.155 16.459 9.585 1.00 159.27 ? 48 LEU B CD2 1 ATOM 3383 N N . LEU B 1 50 ? 31.912 21.643 10.432 1.00 162.65 ? 49 LEU B N 1 ATOM 3384 C CA . LEU B 1 50 ? 32.801 22.761 10.094 1.00 167.38 ? 49 LEU B CA 1 ATOM 3385 C C . LEU B 1 50 ? 33.753 23.160 11.227 1.00 170.76 ? 49 LEU B C 1 ATOM 3386 O O . LEU B 1 50 ? 34.498 24.135 11.117 1.00 171.06 ? 49 LEU B O 1 ATOM 3387 C CB . LEU B 1 50 ? 31.968 23.968 9.653 1.00 167.28 ? 49 LEU B CB 1 ATOM 3388 C CG . LEU B 1 50 ? 30.943 23.683 8.547 1.00 165.97 ? 49 LEU B CG 1 ATOM 3389 C CD1 . LEU B 1 50 ? 30.276 24.974 8.103 1.00 165.55 ? 49 LEU B CD1 1 ATOM 3390 C CD2 . LEU B 1 50 ? 31.569 22.974 7.352 1.00 166.63 ? 49 LEU B CD2 1 ATOM 3391 N N . LEU B 1 51 ? 33.750 22.388 12.305 1.00 173.00 ? 50 LEU B N 1 ATOM 3392 C CA . LEU B 1 51 ? 34.653 22.641 13.415 1.00 177.60 ? 50 LEU B CA 1 ATOM 3393 C C . LEU B 1 51 ? 36.063 22.187 13.020 1.00 178.08 ? 50 LEU B C 1 ATOM 3394 O O . LEU B 1 51 ? 36.231 21.366 12.106 1.00 175.63 ? 50 LEU B O 1 ATOM 3395 C CB . LEU B 1 51 ? 34.173 21.897 14.663 1.00 181.00 ? 50 LEU B CB 1 ATOM 3396 C CG . LEU B 1 51 ? 32.683 22.052 14.998 1.00 181.27 ? 50 LEU B CG 1 ATOM 3397 C CD1 . LEU B 1 51 ? 32.303 21.197 16.201 1.00 181.43 ? 50 LEU B CD1 1 ATOM 3398 C CD2 . LEU B 1 51 ? 32.333 23.520 15.208 1.00 182.29 ? 50 LEU B CD2 1 ATOM 3399 N N . PRO B 1 52 ? 37.090 22.722 13.703 1.00 179.97 ? 51 PRO B N 1 ATOM 3400 C CA . PRO B 1 52 ? 38.447 22.236 13.474 1.00 182.64 ? 51 PRO B CA 1 ATOM 3401 C C . PRO B 1 52 ? 38.559 20.705 13.530 1.00 182.48 ? 51 PRO B C 1 ATOM 3402 O O . PRO B 1 52 ? 37.813 20.053 14.262 1.00 180.50 ? 51 PRO B O 1 ATOM 3403 C CB . PRO B 1 52 ? 39.238 22.886 14.608 1.00 184.90 ? 51 PRO B CB 1 ATOM 3404 C CG . PRO B 1 52 ? 38.525 24.172 14.855 1.00 183.60 ? 51 PRO B CG 1 ATOM 3405 C CD . PRO B 1 52 ? 37.070 23.898 14.593 1.00 180.14 ? 51 PRO B CD 1 ATOM 3406 N N . VAL B 1 53 ? 39.502 20.160 12.762 1.00 182.79 ? 52 VAL B N 1 ATOM 3407 C CA . VAL B 1 53 ? 39.744 18.707 12.613 1.00 181.04 ? 52 VAL B CA 1 ATOM 3408 C C . VAL B 1 53 ? 38.663 18.025 11.760 1.00 179.88 ? 52 VAL B C 1 ATOM 3409 O O . VAL B 1 53 ? 38.957 17.489 10.677 1.00 176.69 ? 52 VAL B O 1 ATOM 3410 C CB . VAL B 1 53 ? 40.118 17.957 13.933 1.00 180.04 ? 52 VAL B CB 1 ATOM 3411 C CG1 . VAL B 1 53 ? 40.760 18.894 14.948 1.00 182.46 ? 52 VAL B CG1 1 ATOM 3412 C CG2 . VAL B 1 53 ? 38.953 17.203 14.554 1.00 176.12 ? 52 VAL B CG2 1 ATOM 3413 N N . ILE B 1 54 ? 37.414 18.091 12.217 1.00 182.84 ? 53 ILE B N 1 ATOM 3414 C CA . ILE B 1 54 ? 36.293 17.495 11.490 1.00 184.53 ? 53 ILE B CA 1 ATOM 3415 C C . ILE B 1 54 ? 36.173 18.124 10.102 1.00 181.93 ? 53 ILE B C 1 ATOM 3416 O O . ILE B 1 54 ? 35.768 17.462 9.141 1.00 180.74 ? 53 ILE B O 1 ATOM 3417 C CB . ILE B 1 54 ? 34.953 17.641 12.259 1.00 186.71 ? 53 ILE B CB 1 ATOM 3418 C CG1 . ILE B 1 54 ? 35.022 16.921 13.620 1.00 191.09 ? 53 ILE B CG1 1 ATOM 3419 C CG2 . ILE B 1 54 ? 33.796 17.076 11.440 1.00 183.80 ? 53 ILE B CG2 1 ATOM 3420 C CD1 . ILE B 1 54 ? 35.269 17.820 14.817 1.00 192.55 ? 53 ILE B CD1 1 ATOM 3421 N N . ILE B 1 55 ? 36.537 19.401 10.001 1.00 180.75 ? 54 ILE B N 1 ATOM 3422 C CA . ILE B 1 55 ? 36.546 20.105 8.723 1.00 179.43 ? 54 ILE B CA 1 ATOM 3423 C C . ILE B 1 55 ? 37.285 19.361 7.611 1.00 176.58 ? 54 ILE B C 1 ATOM 3424 O O . ILE B 1 55 ? 36.889 19.438 6.449 1.00 172.39 ? 54 ILE B O 1 ATOM 3425 C CB . ILE B 1 55 ? 37.173 21.513 8.856 1.00 181.91 ? 54 ILE B CB 1 ATOM 3426 C CG1 . ILE B 1 55 ? 37.007 22.293 7.545 1.00 182.70 ? 54 ILE B CG1 1 ATOM 3427 C CG2 . ILE B 1 55 ? 38.642 21.433 9.263 1.00 184.10 ? 54 ILE B CG2 1 ATOM 3428 C CD1 . ILE B 1 55 ? 35.641 22.920 7.377 1.00 181.75 ? 54 ILE B CD1 1 ATOM 3429 N N . ASP B 1 56 ? 38.358 18.655 7.956 1.00 175.34 ? 55 ASP B N 1 ATOM 3430 C CA . ASP B 1 56 ? 39.125 17.937 6.939 1.00 174.09 ? 55 ASP B CA 1 ATOM 3431 C C . ASP B 1 56 ? 38.299 16.835 6.276 1.00 173.17 ? 55 ASP B C 1 ATOM 3432 O O . ASP B 1 56 ? 38.395 16.627 5.059 1.00 169.27 ? 55 ASP B O 1 ATOM 3433 C CB . ASP B 1 56 ? 40.421 17.373 7.523 1.00 176.09 ? 55 ASP B CB 1 ATOM 3434 C CG . ASP B 1 56 ? 41.463 18.451 7.781 1.00 177.22 ? 55 ASP B CG 1 ATOM 3435 O OD1 . ASP B 1 56 ? 41.459 19.485 7.075 1.00 173.68 ? 55 ASP B OD1 1 ATOM 3436 O OD2 . ASP B 1 56 ? 42.300 18.254 8.686 1.00 181.67 ? 55 ASP B OD2 1 ATOM 3437 N N . CYS B 1 57 ? 37.483 16.145 7.073 1.00 175.87 ? 56 CYS B N 1 ATOM 3438 C CA . CYS B 1 57 ? 36.588 15.112 6.545 1.00 177.13 ? 56 CYS B CA 1 ATOM 3439 C C . CYS B 1 57 ? 35.538 15.729 5.623 1.00 173.26 ? 56 CYS B C 1 ATOM 3440 O O . CYS B 1 57 ? 35.255 15.205 4.546 1.00 175.45 ? 56 CYS B O 1 ATOM 3441 C CB . CYS B 1 57 ? 35.893 14.358 7.680 1.00 179.17 ? 56 CYS B CB 1 ATOM 3442 S SG . CYS B 1 57 ? 36.981 13.857 9.033 1.00 186.60 ? 56 CYS B SG 1 ATOM 3443 N N . TRP B 1 58 ? 34.970 16.848 6.061 1.00 168.16 ? 57 TRP B N 1 ATOM 3444 C CA . TRP B 1 58 ? 33.958 17.569 5.295 1.00 162.76 ? 57 TRP B CA 1 ATOM 3445 C C . TRP B 1 58 ? 34.509 18.040 3.947 1.00 160.73 ? 57 TRP B C 1 ATOM 3446 O O . TRP B 1 58 ? 33.892 17.815 2.903 1.00 156.59 ? 57 TRP B O 1 ATOM 3447 C CB . TRP B 1 58 ? 33.457 18.759 6.116 1.00 161.83 ? 57 TRP B CB 1 ATOM 3448 C CG . TRP B 1 58 ? 32.412 19.588 5.447 1.00 158.40 ? 57 TRP B CG 1 ATOM 3449 C CD1 . TRP B 1 58 ? 31.083 19.303 5.333 1.00 156.36 ? 57 TRP B CD1 1 ATOM 3450 C CD2 . TRP B 1 58 ? 32.607 20.855 4.818 1.00 157.29 ? 57 TRP B CD2 1 ATOM 3451 N NE1 . TRP B 1 58 ? 30.438 20.313 4.662 1.00 152.89 ? 57 TRP B NE1 1 ATOM 3452 C CE2 . TRP B 1 58 ? 31.352 21.279 4.333 1.00 154.80 ? 57 TRP B CE2 1 ATOM 3453 C CE3 . TRP B 1 58 ? 33.723 21.673 4.612 1.00 159.52 ? 57 TRP B CE3 1 ATOM 3454 C CZ2 . TRP B 1 58 ? 31.182 22.485 3.655 1.00 155.01 ? 57 TRP B CZ2 1 ATOM 3455 C CZ3 . TRP B 1 58 ? 33.554 22.873 3.937 1.00 158.87 ? 57 TRP B CZ3 1 ATOM 3456 C CH2 . TRP B 1 58 ? 32.292 23.267 3.467 1.00 156.32 ? 57 TRP B CH2 1 ATOM 3457 N N . ILE B 1 59 ? 35.675 18.683 3.978 1.00 162.04 ? 58 ILE B N 1 ATOM 3458 C CA . ILE B 1 59 ? 36.346 19.142 2.759 1.00 163.89 ? 58 ILE B CA 1 ATOM 3459 C C . ILE B 1 59 ? 36.584 17.967 1.813 1.00 161.35 ? 58 ILE B C 1 ATOM 3460 O O . ILE B 1 59 ? 36.350 18.071 0.612 1.00 157.56 ? 58 ILE B O 1 ATOM 3461 C CB . ILE B 1 59 ? 37.699 19.835 3.069 1.00 170.01 ? 58 ILE B CB 1 ATOM 3462 C CG1 . ILE B 1 59 ? 37.465 21.189 3.752 1.00 171.08 ? 58 ILE B CG1 1 ATOM 3463 C CG2 . ILE B 1 59 ? 38.506 20.052 1.789 1.00 171.90 ? 58 ILE B CG2 1 ATOM 3464 C CD1 . ILE B 1 59 ? 38.711 21.805 4.357 1.00 174.35 ? 58 ILE B CD1 1 ATOM 3465 N N . ASP B 1 60 ? 37.039 16.848 2.368 1.00 161.12 ? 59 ASP B N 1 ATOM 3466 C CA . ASP B 1 60 ? 37.330 15.656 1.573 1.00 161.57 ? 59 ASP B CA 1 ATOM 3467 C C . ASP B 1 60 ? 36.091 15.140 0.824 1.00 159.16 ? 59 ASP B C 1 ATOM 3468 O O . ASP B 1 60 ? 36.218 14.560 -0.256 1.00 157.80 ? 59 ASP B O 1 ATOM 3469 C CB . ASP B 1 60 ? 37.901 14.554 2.484 1.00 164.31 ? 59 ASP B CB 1 ATOM 3470 C CG . ASP B 1 60 ? 38.623 13.456 1.715 1.00 165.85 ? 59 ASP B CG 1 ATOM 3471 O OD1 . ASP B 1 60 ? 39.040 13.689 0.560 1.00 165.76 ? 59 ASP B OD1 1 ATOM 3472 O OD2 . ASP B 1 60 ? 38.784 12.352 2.283 1.00 166.78 ? 59 ASP B OD2 1 ATOM 3473 N N . ASN B 1 61 ? 34.907 15.356 1.401 1.00 157.78 ? 60 ASN B N 1 ATOM 3474 C CA . ASN B 1 61 ? 33.640 14.903 0.816 1.00 155.99 ? 60 ASN B CA 1 ATOM 3475 C C . ASN B 1 61 ? 33.001 15.925 -0.132 1.00 151.48 ? 60 ASN B C 1 ATOM 3476 O O . ASN B 1 61 ? 32.443 15.554 -1.168 1.00 149.61 ? 60 ASN B O 1 ATOM 3477 C CB . ASN B 1 61 ? 32.638 14.569 1.931 1.00 156.51 ? 60 ASN B CB 1 ATOM 3478 C CG . ASN B 1 61 ? 33.154 13.513 2.897 1.00 160.08 ? 60 ASN B CG 1 ATOM 3479 O OD1 . ASN B 1 61 ? 33.871 12.591 2.508 1.00 162.01 ? 60 ASN B OD1 1 ATOM 3480 N ND2 . ASN B 1 61 ? 32.783 13.642 4.167 1.00 160.58 ? 60 ASN B ND2 1 ATOM 3481 N N . ILE B 1 62 ? 33.076 17.204 0.232 1.00 147.83 ? 61 ILE B N 1 ATOM 3482 C CA . ILE B 1 62 ? 32.368 18.263 -0.502 1.00 145.13 ? 61 ILE B CA 1 ATOM 3483 C C . ILE B 1 62 ? 33.152 18.862 -1.670 1.00 144.59 ? 61 ILE B C 1 ATOM 3484 O O . ILE B 1 62 ? 32.565 19.467 -2.570 1.00 139.90 ? 61 ILE B O 1 ATOM 3485 C CB . ILE B 1 62 ? 31.934 19.406 0.444 1.00 144.50 ? 61 ILE B CB 1 ATOM 3486 C CG1 . ILE B 1 62 ? 30.833 20.252 -0.208 1.00 141.94 ? 61 ILE B CG1 1 ATOM 3487 C CG2 . ILE B 1 62 ? 33.122 20.272 0.851 1.00 145.53 ? 61 ILE B CG2 1 ATOM 3488 C CD1 . ILE B 1 62 ? 30.137 21.186 0.755 1.00 140.39 ? 61 ILE B CD1 1 ATOM 3489 N N . ARG B 1 63 ? 34.472 18.711 -1.645 1.00 146.32 ? 62 ARG B N 1 ATOM 3490 C CA . ARG B 1 63 ? 35.314 19.179 -2.741 1.00 146.26 ? 62 ARG B CA 1 ATOM 3491 C C . ARG B 1 63 ? 34.927 18.501 -4.052 1.00 143.32 ? 62 ARG B C 1 ATOM 3492 O O . ARG B 1 63 ? 34.487 17.349 -4.056 1.00 141.12 ? 62 ARG B O 1 ATOM 3493 C CB . ARG B 1 63 ? 36.791 18.902 -2.440 1.00 150.15 ? 62 ARG B CB 1 ATOM 3494 C CG . ARG B 1 63 ? 37.160 17.424 -2.412 1.00 151.73 ? 62 ARG B CG 1 ATOM 3495 C CD . ARG B 1 63 ? 38.542 17.200 -1.825 1.00 154.30 ? 62 ARG B CD 1 ATOM 3496 N NE . ARG B 1 63 ? 39.010 15.832 -2.047 1.00 155.32 ? 62 ARG B NE 1 ATOM 3497 C CZ . ARG B 1 63 ? 39.504 15.369 -3.197 1.00 156.66 ? 62 ARG B CZ 1 ATOM 3498 N NH1 . ARG B 1 63 ? 39.601 16.156 -4.267 1.00 157.34 ? 62 ARG B NH1 1 ATOM 3499 N NH2 . ARG B 1 63 ? 39.903 14.104 -3.280 1.00 157.15 ? 62 ARG B NH2 1 ATOM 3500 N N . LEU B 1 64 ? 35.078 19.231 -5.152 1.00 142.99 ? 63 LEU B N 1 ATOM 3501 C CA . LEU B 1 64 ? 34.936 18.664 -6.490 1.00 144.74 ? 63 LEU B CA 1 ATOM 3502 C C . LEU B 1 64 ? 36.316 18.324 -7.034 1.00 147.28 ? 63 LEU B C 1 ATOM 3503 O O . LEU B 1 64 ? 37.274 19.067 -6.819 1.00 148.50 ? 63 LEU B O 1 ATOM 3504 C CB . LEU B 1 64 ? 34.250 19.660 -7.428 1.00 144.69 ? 63 LEU B CB 1 ATOM 3505 C CG . LEU B 1 64 ? 32.778 19.957 -7.142 1.00 142.68 ? 63 LEU B CG 1 ATOM 3506 C CD1 . LEU B 1 64 ? 32.303 21.120 -8.002 1.00 141.39 ? 63 LEU B CD1 1 ATOM 3507 C CD2 . LEU B 1 64 ? 31.918 18.722 -7.379 1.00 142.18 ? 63 LEU B CD2 1 ATOM 3508 N N . VAL B 1 65 ? 36.408 17.199 -7.738 1.00 148.85 ? 64 VAL B N 1 ATOM 3509 C CA . VAL B 1 65 ? 37.666 16.765 -8.339 1.00 153.19 ? 64 VAL B CA 1 ATOM 3510 C C . VAL B 1 65 ? 37.651 17.159 -9.813 1.00 154.96 ? 64 VAL B C 1 ATOM 3511 O O . VAL B 1 65 ? 36.757 16.754 -10.554 1.00 152.15 ? 64 VAL B O 1 ATOM 3512 C CB . VAL B 1 65 ? 37.850 15.236 -8.219 1.00 153.75 ? 64 VAL B CB 1 ATOM 3513 C CG1 . VAL B 1 65 ? 39.273 14.839 -8.591 1.00 156.34 ? 64 VAL B CG1 1 ATOM 3514 C CG2 . VAL B 1 65 ? 37.511 14.768 -6.809 1.00 153.08 ? 64 VAL B CG2 1 ATOM 3515 N N . TYR B 1 66 ? 38.632 17.955 -10.233 1.00 158.72 ? 65 TYR B N 1 ATOM 3516 C CA . TYR B 1 66 ? 38.692 18.427 -11.610 1.00 159.89 ? 65 TYR B CA 1 ATOM 3517 C C . TYR B 1 66 ? 39.501 17.461 -12.467 1.00 164.30 ? 65 TYR B C 1 ATOM 3518 O O . TYR B 1 66 ? 40.656 17.169 -12.163 1.00 167.63 ? 65 TYR B O 1 ATOM 3519 C CB . TYR B 1 66 ? 39.309 19.823 -11.675 1.00 160.02 ? 65 TYR B CB 1 ATOM 3520 C CG . TYR B 1 66 ? 39.134 20.487 -13.021 1.00 159.69 ? 65 TYR B CG 1 ATOM 3521 C CD1 . TYR B 1 66 ? 37.942 21.125 -13.352 1.00 156.54 ? 65 TYR B CD1 1 ATOM 3522 C CD2 . TYR B 1 66 ? 40.154 20.470 -13.968 1.00 162.00 ? 65 TYR B CD2 1 ATOM 3523 C CE1 . TYR B 1 66 ? 37.773 21.734 -14.584 1.00 155.72 ? 65 TYR B CE1 1 ATOM 3524 C CE2 . TYR B 1 66 ? 39.993 21.077 -15.203 1.00 161.20 ? 65 TYR B CE2 1 ATOM 3525 C CZ . TYR B 1 66 ? 38.802 21.707 -15.505 1.00 157.86 ? 65 TYR B CZ 1 ATOM 3526 O OH . TYR B 1 66 ? 38.638 22.309 -16.727 1.00 156.74 ? 65 TYR B OH 1 ATOM 3527 N N . ASN B 1 67 ? 38.880 16.966 -13.534 1.00 166.07 ? 66 ASN B N 1 ATOM 3528 C CA . ASN B 1 67 ? 39.551 16.106 -14.504 1.00 171.60 ? 66 ASN B CA 1 ATOM 3529 C C . ASN B 1 67 ? 40.024 16.991 -15.661 1.00 173.84 ? 66 ASN B C 1 ATOM 3530 O O . ASN B 1 67 ? 39.211 17.481 -16.447 1.00 172.56 ? 66 ASN B O 1 ATOM 3531 C CB . ASN B 1 67 ? 38.575 15.020 -14.993 1.00 173.08 ? 66 ASN B CB 1 ATOM 3532 C CG . ASN B 1 67 ? 39.241 13.962 -15.871 1.00 179.45 ? 66 ASN B CG 1 ATOM 3533 O OD1 . ASN B 1 67 ? 40.451 13.996 -16.099 1.00 186.50 ? 66 ASN B OD1 1 ATOM 3534 N ND2 . ASN B 1 67 ? 38.436 12.999 -16.368 1.00 180.16 ? 66 ASN B ND2 1 ATOM 3535 N N . LYS B 1 68 ? 41.338 17.209 -15.739 1.00 178.57 ? 67 LYS B N 1 ATOM 3536 C CA . LYS B 1 68 ? 41.931 18.119 -16.728 1.00 181.78 ? 67 LYS B CA 1 ATOM 3537 C C . LYS B 1 68 ? 41.753 17.642 -18.173 1.00 181.54 ? 67 LYS B C 1 ATOM 3538 O O . LYS B 1 68 ? 41.661 18.461 -19.091 1.00 180.89 ? 67 LYS B O 1 ATOM 3539 C CB . LYS B 1 68 ? 43.431 18.338 -16.450 1.00 186.12 ? 67 LYS B CB 1 ATOM 3540 C CG . LYS B 1 68 ? 43.756 19.347 -15.350 1.00 185.02 ? 67 LYS B CG 1 ATOM 3541 C CD . LYS B 1 68 ? 45.180 19.878 -15.491 1.00 187.12 ? 67 LYS B CD 1 ATOM 3542 C CE . LYS B 1 68 ? 45.517 20.934 -14.447 1.00 186.04 ? 67 LYS B CE 1 ATOM 3543 N NZ . LYS B 1 68 ? 45.856 20.341 -13.124 1.00 186.18 ? 67 LYS B NZ 1 ATOM 3544 N N . THR B 1 69 ? 41.718 16.326 -18.372 1.00 180.05 ? 68 THR B N 1 ATOM 3545 C CA . THR B 1 69 ? 41.571 15.757 -19.711 1.00 179.88 ? 68 THR B CA 1 ATOM 3546 C C . THR B 1 69 ? 40.145 15.938 -20.235 1.00 177.40 ? 68 THR B C 1 ATOM 3547 O O . THR B 1 69 ? 39.947 16.400 -21.355 1.00 177.40 ? 68 THR B O 1 ATOM 3548 C CB . THR B 1 69 ? 41.969 14.266 -19.750 1.00 179.92 ? 68 THR B CB 1 ATOM 3549 O OG1 . THR B 1 69 ? 41.197 13.531 -18.795 1.00 176.96 ? 68 THR B OG1 1 ATOM 3550 C CG2 . THR B 1 69 ? 43.451 14.095 -19.435 1.00 182.20 ? 68 THR B CG2 1 ATOM 3551 N N . SER B 1 70 ? 39.155 15.591 -19.418 1.00 175.45 ? 69 SER B N 1 ATOM 3552 C CA . SER B 1 70 ? 37.760 15.747 -19.815 1.00 173.37 ? 69 SER B CA 1 ATOM 3553 C C . SER B 1 70 ? 37.220 17.167 -19.611 1.00 172.23 ? 69 SER B C 1 ATOM 3554 O O . SER B 1 70 ? 36.131 17.478 -20.092 1.00 169.07 ? 69 SER B O 1 ATOM 3555 C CB . SER B 1 70 ? 36.873 14.750 -19.064 1.00 171.01 ? 69 SER B CB 1 ATOM 3556 O OG . SER B 1 70 ? 36.839 15.027 -17.675 1.00 167.68 ? 69 SER B OG 1 ATOM 3557 N N . ARG B 1 71 ? 37.966 18.017 -18.903 1.00 174.30 ? 70 ARG B N 1 ATOM 3558 C CA . ARG B 1 71 ? 37.510 19.373 -18.583 1.00 173.50 ? 70 ARG B CA 1 ATOM 3559 C C . ARG B 1 71 ? 36.156 19.345 -17.875 1.00 168.89 ? 70 ARG B C 1 ATOM 3560 O O . ARG B 1 71 ? 35.231 20.073 -18.244 1.00 166.15 ? 70 ARG B O 1 ATOM 3561 C CB . ARG B 1 71 ? 37.435 20.237 -19.848 1.00 175.88 ? 70 ARG B CB 1 ATOM 3562 C CG . ARG B 1 71 ? 38.785 20.455 -20.501 1.00 180.96 ? 70 ARG B CG 1 ATOM 3563 C CD . ARG B 1 71 ? 38.718 21.664 -21.437 1.00 183.34 ? 70 ARG B CD 1 ATOM 3564 N NE . ARG B 1 71 ? 39.009 22.905 -20.719 1.00 183.56 ? 70 ARG B NE 1 ATOM 3565 C CZ . ARG B 1 71 ? 40.225 23.428 -20.571 1.00 186.11 ? 70 ARG B CZ 1 ATOM 3566 N NH1 . ARG B 1 71 ? 41.295 22.834 -21.090 1.00 190.16 ? 70 ARG B NH1 1 ATOM 3567 N NH2 . ARG B 1 71 ? 40.375 24.560 -19.900 1.00 184.59 ? 70 ARG B NH2 1 ATOM 3568 N N . ALA B 1 72 ? 36.050 18.490 -16.862 1.00 166.43 ? 71 ALA B N 1 ATOM 3569 C CA . ALA B 1 72 ? 34.804 18.322 -16.125 1.00 163.33 ? 71 ALA B CA 1 ATOM 3570 C C . ALA B 1 72 ? 35.104 17.887 -14.699 1.00 163.28 ? 71 ALA B C 1 ATOM 3571 O O . ALA B 1 72 ? 36.167 17.330 -14.430 1.00 166.86 ? 71 ALA B O 1 ATOM 3572 C CB . ALA B 1 72 ? 33.922 17.295 -16.816 1.00 161.95 ? 71 ALA B CB 1 ATOM 3573 N N . THR B 1 73 ? 34.169 18.143 -13.791 1.00 159.33 ? 72 THR B N 1 ATOM 3574 C CA . THR B 1 73 ? 34.343 17.771 -12.393 1.00 157.03 ? 72 THR B CA 1 ATOM 3575 C C . THR B 1 73 ? 33.726 16.413 -12.107 1.00 155.02 ? 72 THR B C 1 ATOM 3576 O O . THR B 1 73 ? 32.819 15.966 -12.806 1.00 153.34 ? 72 THR B O 1 ATOM 3577 C CB . THR B 1 73 ? 33.690 18.793 -11.449 1.00 155.31 ? 72 THR B CB 1 ATOM 3578 O OG1 . THR B 1 73 ? 32.296 18.913 -11.758 1.00 153.40 ? 72 THR B OG1 1 ATOM 3579 C CG2 . THR B 1 73 ? 34.361 20.144 -11.583 1.00 157.05 ? 72 THR B CG2 1 ATOM 3580 N N . GLN B 1 74 ? 34.235 15.768 -11.064 1.00 154.96 ? 73 GLN B N 1 ATOM 3581 C CA . GLN B 1 74 ? 33.688 14.511 -10.559 1.00 154.17 ? 73 GLN B CA 1 ATOM 3582 C C . GLN B 1 74 ? 33.603 14.622 -9.042 1.00 151.78 ? 73 GLN B C 1 ATOM 3583 O O . GLN B 1 74 ? 34.281 15.457 -8.432 1.00 151.00 ? 73 GLN B O 1 ATOM 3584 C CB . GLN B 1 74 ? 34.612 13.336 -10.910 1.00 156.69 ? 73 GLN B CB 1 ATOM 3585 C CG . GLN B 1 74 ? 34.985 13.221 -12.383 1.00 158.01 ? 73 GLN B CG 1 ATOM 3586 C CD . GLN B 1 74 ? 35.979 12.102 -12.660 1.00 159.65 ? 73 GLN B CD 1 ATOM 3587 O OE1 . GLN B 1 74 ? 36.313 11.310 -11.776 1.00 158.89 ? 73 GLN B OE1 1 ATOM 3588 N NE2 . GLN B 1 74 ? 36.453 12.031 -13.897 1.00 160.99 ? 73 GLN B NE2 1 ATOM 3589 N N . PHE B 1 75 ? 32.780 13.778 -8.434 1.00 150.09 ? 74 PHE B N 1 ATOM 3590 C CA . PHE B 1 75 ? 32.744 13.695 -6.982 1.00 151.55 ? 74 PHE B CA 1 ATOM 3591 C C . PHE B 1 75 ? 33.931 12.852 -6.530 1.00 154.01 ? 74 PHE B C 1 ATOM 3592 O O . PHE B 1 75 ? 34.451 12.043 -7.302 1.00 152.21 ? 74 PHE B O 1 ATOM 3593 C CB . PHE B 1 75 ? 31.442 13.060 -6.486 1.00 151.84 ? 74 PHE B CB 1 ATOM 3594 C CG . PHE B 1 75 ? 30.196 13.719 -7.014 1.00 151.35 ? 74 PHE B CG 1 ATOM 3595 C CD1 . PHE B 1 75 ? 30.084 15.103 -7.066 1.00 149.26 ? 74 PHE B CD1 1 ATOM 3596 C CD2 . PHE B 1 75 ? 29.121 12.947 -7.440 1.00 153.10 ? 74 PHE B CD2 1 ATOM 3597 C CE1 . PHE B 1 75 ? 28.932 15.701 -7.548 1.00 148.36 ? 74 PHE B CE1 1 ATOM 3598 C CE2 . PHE B 1 75 ? 27.965 13.541 -7.921 1.00 151.98 ? 74 PHE B CE2 1 ATOM 3599 C CZ . PHE B 1 75 ? 27.871 14.920 -7.975 1.00 149.43 ? 74 PHE B CZ 1 ATOM 3600 N N . PRO B 1 76 ? 34.377 13.042 -5.278 1.00 155.84 ? 75 PRO B N 1 ATOM 3601 C CA . PRO B 1 76 ? 35.420 12.166 -4.749 1.00 159.18 ? 75 PRO B CA 1 ATOM 3602 C C . PRO B 1 76 ? 35.003 10.695 -4.776 1.00 160.14 ? 75 PRO B C 1 ATOM 3603 O O . PRO B 1 76 ? 33.810 10.388 -4.786 1.00 158.29 ? 75 PRO B O 1 ATOM 3604 C CB . PRO B 1 76 ? 35.589 12.653 -3.305 1.00 158.76 ? 75 PRO B CB 1 ATOM 3605 C CG . PRO B 1 76 ? 35.121 14.067 -3.317 1.00 156.58 ? 75 PRO B CG 1 ATOM 3606 C CD . PRO B 1 76 ? 34.028 14.125 -4.341 1.00 154.43 ? 75 PRO B CD 1 ATOM 3607 N N . ASP B 1 77 ? 35.978 9.795 -4.792 1.00 163.77 ? 76 ASP B N 1 ATOM 3608 C CA . ASP B 1 77 ? 35.675 8.372 -4.868 1.00 166.97 ? 76 ASP B CA 1 ATOM 3609 C C . ASP B 1 77 ? 34.804 7.957 -3.676 1.00 166.73 ? 76 ASP B C 1 ATOM 3610 O O . ASP B 1 77 ? 35.087 8.313 -2.528 1.00 169.45 ? 76 ASP B O 1 ATOM 3611 C CB . ASP B 1 77 ? 36.965 7.543 -4.917 1.00 172.65 ? 76 ASP B CB 1 ATOM 3612 C CG . ASP B 1 77 ? 36.750 6.151 -5.497 1.00 176.47 ? 76 ASP B CG 1 ATOM 3613 O OD1 . ASP B 1 77 ? 35.680 5.896 -6.092 1.00 177.24 ? 76 ASP B OD1 1 ATOM 3614 O OD2 . ASP B 1 77 ? 37.663 5.307 -5.366 1.00 180.49 ? 76 ASP B OD2 1 ATOM 3615 N N . GLY B 1 78 ? 33.734 7.219 -3.963 1.00 165.78 ? 77 GLY B N 1 ATOM 3616 C CA . GLY B 1 78 ? 32.806 6.735 -2.937 1.00 164.45 ? 77 GLY B CA 1 ATOM 3617 C C . GLY B 1 78 ? 31.842 7.766 -2.364 1.00 160.72 ? 77 GLY B C 1 ATOM 3618 O O . GLY B 1 78 ? 31.148 7.487 -1.380 1.00 158.03 ? 77 GLY B O 1 ATOM 3619 N N . VAL B 1 79 ? 31.774 8.947 -2.975 1.00 157.20 ? 78 VAL B N 1 ATOM 3620 C CA . VAL B 1 79 ? 30.916 10.019 -2.477 1.00 153.03 ? 78 VAL B CA 1 ATOM 3621 C C . VAL B 1 79 ? 29.864 10.340 -3.526 1.00 147.76 ? 78 VAL B C 1 ATOM 3622 O O . VAL B 1 79 ? 30.186 10.514 -4.698 1.00 148.97 ? 78 VAL B O 1 ATOM 3623 C CB . VAL B 1 79 ? 31.724 11.305 -2.188 1.00 154.34 ? 78 VAL B CB 1 ATOM 3624 C CG1 . VAL B 1 79 ? 30.809 12.413 -1.672 1.00 152.46 ? 78 VAL B CG1 1 ATOM 3625 C CG2 . VAL B 1 79 ? 32.846 11.022 -1.198 1.00 156.42 ? 78 VAL B CG2 1 ATOM 3626 N N . ASP B 1 80 ? 28.610 10.416 -3.101 1.00 142.65 ? 79 ASP B N 1 ATOM 3627 C CA . ASP B 1 80 ? 27.530 10.817 -3.991 1.00 141.27 ? 79 ASP B CA 1 ATOM 3628 C C . ASP B 1 80 ? 26.775 11.989 -3.380 1.00 134.74 ? 79 ASP B C 1 ATOM 3629 O O . ASP B 1 80 ? 26.600 12.054 -2.166 1.00 132.13 ? 79 ASP B O 1 ATOM 3630 C CB . ASP B 1 80 ? 26.587 9.639 -4.240 1.00 144.81 ? 79 ASP B CB 1 ATOM 3631 C CG . ASP B 1 80 ? 25.988 9.658 -5.630 1.00 147.78 ? 79 ASP B CG 1 ATOM 3632 O OD1 . ASP B 1 80 ? 25.638 10.758 -6.129 1.00 146.52 ? 79 ASP B OD1 1 ATOM 3633 O OD2 . ASP B 1 80 ? 25.870 8.565 -6.225 1.00 148.15 ? 79 ASP B OD2 1 ATOM 3634 N N . VAL B 1 81 ? 26.328 12.915 -4.224 1.00 133.25 ? 80 VAL B N 1 ATOM 3635 C CA . VAL B 1 81 ? 25.686 14.139 -3.750 1.00 134.71 ? 80 VAL B CA 1 ATOM 3636 C C . VAL B 1 81 ? 24.391 14.388 -4.511 1.00 132.39 ? 80 VAL B C 1 ATOM 3637 O O . VAL B 1 81 ? 24.346 14.232 -5.734 1.00 130.12 ? 80 VAL B O 1 ATOM 3638 C CB . VAL B 1 81 ? 26.620 15.357 -3.922 1.00 138.39 ? 80 VAL B CB 1 ATOM 3639 C CG1 . VAL B 1 81 ? 26.095 16.552 -3.135 1.00 138.57 ? 80 VAL B CG1 1 ATOM 3640 C CG2 . VAL B 1 81 ? 28.037 15.017 -3.475 1.00 141.48 ? 80 VAL B CG2 1 ATOM 3641 N N . ARG B 1 82 ? 23.341 14.767 -3.786 1.00 131.17 ? 81 ARG B N 1 ATOM 3642 C CA . ARG B 1 82 ? 22.073 15.125 -4.415 1.00 131.16 ? 81 ARG B CA 1 ATOM 3643 C C . ARG B 1 82 ? 21.522 16.428 -3.852 1.00 126.87 ? 81 ARG B C 1 ATOM 3644 O O . ARG B 1 82 ? 21.861 16.838 -2.736 1.00 121.77 ? 81 ARG B O 1 ATOM 3645 C CB . ARG B 1 82 ? 21.042 13.992 -4.284 1.00 136.79 ? 81 ARG B CB 1 ATOM 3646 C CG . ARG B 1 82 ? 20.436 13.814 -2.896 1.00 140.15 ? 81 ARG B CG 1 ATOM 3647 C CD . ARG B 1 82 ? 19.405 12.688 -2.862 1.00 142.90 ? 81 ARG B CD 1 ATOM 3648 N NE . ARG B 1 82 ? 18.764 12.579 -1.548 1.00 145.64 ? 81 ARG B NE 1 ATOM 3649 C CZ . ARG B 1 82 ? 17.941 11.597 -1.173 1.00 147.15 ? 81 ARG B CZ 1 ATOM 3650 N NH1 . ARG B 1 82 ? 17.638 10.605 -2.006 1.00 149.50 ? 81 ARG B NH1 1 ATOM 3651 N NH2 . ARG B 1 82 ? 17.419 11.606 0.051 1.00 145.16 ? 81 ARG B NH2 1 ATOM 3652 N N . VAL B 1 83 ? 20.674 17.074 -4.650 1.00 128.46 ? 82 VAL B N 1 ATOM 3653 C CA . VAL B 1 83 ? 20.026 18.324 -4.269 1.00 129.35 ? 82 VAL B CA 1 ATOM 3654 C C . VAL B 1 83 ? 18.598 17.996 -3.847 1.00 127.16 ? 82 VAL B C 1 ATOM 3655 O O . VAL B 1 83 ? 17.769 17.650 -4.688 1.00 125.73 ? 82 VAL B O 1 ATOM 3656 C CB . VAL B 1 83 ? 19.983 19.329 -5.444 1.00 130.71 ? 82 VAL B CB 1 ATOM 3657 C CG1 . VAL B 1 83 ? 19.455 20.679 -4.971 1.00 130.58 ? 82 VAL B CG1 1 ATOM 3658 C CG2 . VAL B 1 83 ? 21.365 19.483 -6.065 1.00 132.79 ? 82 VAL B CG2 1 ATOM 3659 N N . PRO B 1 84 ? 18.308 18.091 -2.541 1.00 125.41 ? 83 PRO B N 1 ATOM 3660 C CA . PRO B 1 84 ? 16.973 17.787 -2.075 1.00 124.65 ? 83 PRO B CA 1 ATOM 3661 C C . PRO B 1 84 ? 16.052 18.986 -2.237 1.00 125.10 ? 83 PRO B C 1 ATOM 3662 O O . PRO B 1 84 ? 16.520 20.118 -2.394 1.00 121.15 ? 83 PRO B O 1 ATOM 3663 C CB . PRO B 1 84 ? 17.196 17.501 -0.594 1.00 123.94 ? 83 PRO B CB 1 ATOM 3664 C CG . PRO B 1 84 ? 18.293 18.437 -0.222 1.00 123.83 ? 83 PRO B CG 1 ATOM 3665 C CD . PRO B 1 84 ? 19.167 18.569 -1.442 1.00 124.70 ? 83 PRO B CD 1 ATOM 3666 N N . GLY B 1 85 ? 14.750 18.723 -2.204 1.00 127.54 ? 84 GLY B N 1 ATOM 3667 C CA . GLY B 1 85 ? 13.751 19.778 -2.124 1.00 129.01 ? 84 GLY B CA 1 ATOM 3668 C C . GLY B 1 85 ? 13.409 20.490 -3.416 1.00 129.59 ? 84 GLY B C 1 ATOM 3669 O O . GLY B 1 85 ? 12.852 21.587 -3.375 1.00 133.52 ? 84 GLY B O 1 ATOM 3670 N N . PHE B 1 86 ? 13.719 19.890 -4.565 1.00 128.47 ? 85 PHE B N 1 ATOM 3671 C CA . PHE B 1 86 ? 13.309 20.480 -5.838 1.00 128.17 ? 85 PHE B CA 1 ATOM 3672 C C . PHE B 1 86 ? 11.783 20.456 -5.928 1.00 128.46 ? 85 PHE B C 1 ATOM 3673 O O . PHE B 1 86 ? 11.154 19.421 -5.703 1.00 130.24 ? 85 PHE B O 1 ATOM 3674 C CB . PHE B 1 86 ? 13.927 19.747 -7.027 1.00 128.99 ? 85 PHE B CB 1 ATOM 3675 C CG . PHE B 1 86 ? 13.726 20.456 -8.336 1.00 129.91 ? 85 PHE B CG 1 ATOM 3676 C CD1 . PHE B 1 86 ? 12.588 20.222 -9.102 1.00 130.79 ? 85 PHE B CD1 1 ATOM 3677 C CD2 . PHE B 1 86 ? 14.664 21.367 -8.799 1.00 129.71 ? 85 PHE B CD2 1 ATOM 3678 C CE1 . PHE B 1 86 ? 12.394 20.876 -10.306 1.00 131.01 ? 85 PHE B CE1 1 ATOM 3679 C CE2 . PHE B 1 86 ? 14.476 22.025 -10.003 1.00 131.19 ? 85 PHE B CE2 1 ATOM 3680 C CZ . PHE B 1 86 ? 13.340 21.779 -10.759 1.00 131.53 ? 85 PHE B CZ 1 ATOM 3681 N N . GLY B 1 87 ? 11.190 21.608 -6.226 1.00 127.53 ? 86 GLY B N 1 ATOM 3682 C CA . GLY B 1 87 ? 9.735 21.737 -6.259 1.00 128.58 ? 86 GLY B CA 1 ATOM 3683 C C . GLY B 1 87 ? 9.118 22.049 -4.904 1.00 129.87 ? 86 GLY B C 1 ATOM 3684 O O . GLY B 1 87 ? 7.915 22.302 -4.811 1.00 130.44 ? 86 GLY B O 1 ATOM 3685 N N . LYS B 1 88 ? 9.940 22.027 -3.854 1.00 130.70 ? 87 LYS B N 1 ATOM 3686 C CA . LYS B 1 88 ? 9.527 22.413 -2.506 1.00 129.95 ? 87 LYS B CA 1 ATOM 3687 C C . LYS B 1 88 ? 10.335 23.650 -2.121 1.00 124.42 ? 87 LYS B C 1 ATOM 3688 O O . LYS B 1 88 ? 11.052 24.206 -2.954 1.00 119.92 ? 87 LYS B O 1 ATOM 3689 C CB . LYS B 1 88 ? 9.775 21.263 -1.525 1.00 134.03 ? 87 LYS B CB 1 ATOM 3690 C CG . LYS B 1 88 ? 8.976 20.003 -1.826 1.00 138.41 ? 87 LYS B CG 1 ATOM 3691 C CD . LYS B 1 88 ? 7.488 20.216 -1.596 1.00 142.63 ? 87 LYS B CD 1 ATOM 3692 C CE . LYS B 1 88 ? 6.712 18.922 -1.773 1.00 147.77 ? 87 LYS B CE 1 ATOM 3693 N NZ . LYS B 1 88 ? 5.260 19.113 -1.509 1.00 150.98 ? 87 LYS B NZ 1 ATOM 3694 N N . THR B 1 89 ? 10.204 24.104 -0.881 1.00 121.78 ? 88 THR B N 1 ATOM 3695 C CA . THR B 1 89 ? 10.888 25.318 -0.461 1.00 120.63 ? 88 THR B CA 1 ATOM 3696 C C . THR B 1 89 ? 11.739 25.171 0.789 1.00 121.28 ? 88 THR B C 1 ATOM 3697 O O . THR B 1 89 ? 12.501 26.075 1.110 1.00 123.79 ? 88 THR B O 1 ATOM 3698 C CB . THR B 1 89 ? 9.882 26.465 -0.256 1.00 119.80 ? 88 THR B CB 1 ATOM 3699 O OG1 . THR B 1 89 ? 8.874 26.062 0.679 1.00 121.03 ? 88 THR B OG1 1 ATOM 3700 C CG2 . THR B 1 89 ? 9.223 26.828 -1.576 1.00 119.61 ? 88 THR B CG2 1 ATOM 3701 N N . PHE B 1 90 ? 11.639 24.047 1.491 1.00 120.33 ? 89 PHE B N 1 ATOM 3702 C CA . PHE B 1 90 ? 12.361 23.896 2.754 1.00 123.84 ? 89 PHE B CA 1 ATOM 3703 C C . PHE B 1 90 ? 13.878 24.087 2.623 1.00 120.11 ? 89 PHE B C 1 ATOM 3704 O O . PHE B 1 90 ? 14.517 24.635 3.527 1.00 120.21 ? 89 PHE B O 1 ATOM 3705 C CB . PHE B 1 90 ? 12.035 22.556 3.425 1.00 131.65 ? 89 PHE B CB 1 ATOM 3706 C CG . PHE B 1 90 ? 12.481 21.351 2.641 1.00 137.45 ? 89 PHE B CG 1 ATOM 3707 C CD1 . PHE B 1 90 ? 13.777 20.864 2.765 1.00 140.51 ? 89 PHE B CD1 1 ATOM 3708 C CD2 . PHE B 1 90 ? 11.600 20.691 1.792 1.00 140.85 ? 89 PHE B CD2 1 ATOM 3709 C CE1 . PHE B 1 90 ? 14.192 19.754 2.048 1.00 142.79 ? 89 PHE B CE1 1 ATOM 3710 C CE2 . PHE B 1 90 ? 12.009 19.579 1.073 1.00 142.83 ? 89 PHE B CE2 1 ATOM 3711 C CZ . PHE B 1 90 ? 13.307 19.110 1.201 1.00 143.99 ? 89 PHE B CZ 1 ATOM 3712 N N . SER B 1 91 ? 14.446 23.653 1.499 1.00 115.89 ? 90 SER B N 1 ATOM 3713 C CA . SER B 1 91 ? 15.898 23.707 1.278 1.00 115.73 ? 90 SER B CA 1 ATOM 3714 C C . SER B 1 91 ? 16.430 25.121 1.012 1.00 118.05 ? 90 SER B C 1 ATOM 3715 O O . SER B 1 91 ? 17.626 25.382 1.161 1.00 118.58 ? 90 SER B O 1 ATOM 3716 C CB . SER B 1 91 ? 16.283 22.787 0.110 1.00 113.96 ? 90 SER B CB 1 ATOM 3717 O OG . SER B 1 91 ? 15.485 23.044 -1.036 1.00 110.26 ? 90 SER B OG 1 ATOM 3718 N N . LEU B 1 92 ? 15.531 26.011 0.596 1.00 119.02 ? 91 LEU B N 1 ATOM 3719 C CA . LEU B 1 92 ? 15.819 27.437 0.382 1.00 118.83 ? 91 LEU B CA 1 ATOM 3720 C C . LEU B 1 92 ? 15.505 28.287 1.634 1.00 119.71 ? 91 LEU B C 1 ATOM 3721 O O . LEU B 1 92 ? 16.151 29.305 1.883 1.00 115.99 ? 91 LEU B O 1 ATOM 3722 C CB . LEU B 1 92 ? 14.930 27.952 -0.770 1.00 116.88 ? 91 LEU B CB 1 ATOM 3723 C CG . LEU B 1 92 ? 15.068 27.361 -2.173 1.00 114.94 ? 91 LEU B CG 1 ATOM 3724 C CD1 . LEU B 1 92 ? 14.406 28.228 -3.239 1.00 112.16 ? 91 LEU B CD1 1 ATOM 3725 C CD2 . LEU B 1 92 ? 16.529 27.171 -2.483 1.00 115.47 ? 91 LEU B CD2 1 ATOM 3726 N N . GLU B 1 93 ? 14.497 27.880 2.401 1.00 123.71 ? 92 GLU B N 1 ATOM 3727 C CA . GLU B 1 93 ? 14.058 28.670 3.547 1.00 127.68 ? 92 GLU B CA 1 ATOM 3728 C C . GLU B 1 93 ? 15.067 28.631 4.682 1.00 131.07 ? 92 GLU B C 1 ATOM 3729 O O . GLU B 1 93 ? 15.322 29.655 5.306 1.00 131.32 ? 92 GLU B O 1 ATOM 3730 C CB . GLU B 1 93 ? 12.698 28.191 4.056 1.00 128.75 ? 92 GLU B CB 1 ATOM 3731 C CG . GLU B 1 93 ? 11.545 28.506 3.121 1.00 128.56 ? 92 GLU B CG 1 ATOM 3732 C CD . GLU B 1 93 ? 10.223 27.992 3.648 1.00 127.85 ? 92 GLU B CD 1 ATOM 3733 O OE1 . GLU B 1 93 ? 9.808 28.433 4.743 1.00 129.72 ? 92 GLU B OE1 1 ATOM 3734 O OE2 . GLU B 1 93 ? 9.584 27.161 2.965 1.00 122.19 ? 92 GLU B OE2 1 ATOM 3735 N N . PHE B 1 94 ? 15.613 27.445 4.954 1.00 135.19 ? 93 PHE B N 1 ATOM 3736 C CA . PHE B 1 94 ? 16.585 27.239 6.033 1.00 139.97 ? 93 PHE B CA 1 ATOM 3737 C C . PHE B 1 94 ? 17.780 26.437 5.520 1.00 140.81 ? 93 PHE B C 1 ATOM 3738 O O . PHE B 1 94 ? 17.606 25.393 4.878 1.00 141.98 ? 93 PHE B O 1 ATOM 3739 C CB . PHE B 1 94 ? 15.940 26.491 7.203 1.00 144.21 ? 93 PHE B CB 1 ATOM 3740 C CG . PHE B 1 94 ? 15.075 27.355 8.078 1.00 147.16 ? 93 PHE B CG 1 ATOM 3741 C CD1 . PHE B 1 94 ? 13.876 27.866 7.608 1.00 145.87 ? 93 PHE B CD1 1 ATOM 3742 C CD2 . PHE B 1 94 ? 15.452 27.644 9.377 1.00 150.95 ? 93 PHE B CD2 1 ATOM 3743 C CE1 . PHE B 1 94 ? 13.078 28.659 8.413 1.00 146.56 ? 93 PHE B CE1 1 ATOM 3744 C CE2 . PHE B 1 94 ? 14.654 28.438 10.186 1.00 152.08 ? 93 PHE B CE2 1 ATOM 3745 C CZ . PHE B 1 94 ? 13.466 28.947 9.704 1.00 148.62 ? 93 PHE B CZ 1 ATOM 3746 N N . LEU B 1 95 ? 18.989 26.918 5.794 1.00 141.07 ? 94 LEU B N 1 ATOM 3747 C CA . LEU B 1 95 ? 20.182 26.248 5.272 1.00 140.56 ? 94 LEU B CA 1 ATOM 3748 C C . LEU B 1 95 ? 20.564 25.037 6.110 1.00 137.67 ? 94 LEU B C 1 ATOM 3749 O O . LEU B 1 95 ? 21.029 24.021 5.577 1.00 135.56 ? 94 LEU B O 1 ATOM 3750 C CB . LEU B 1 95 ? 21.378 27.202 5.163 1.00 143.42 ? 94 LEU B CB 1 ATOM 3751 C CG . LEU B 1 95 ? 21.429 28.200 3.995 1.00 143.79 ? 94 LEU B CG 1 ATOM 3752 C CD1 . LEU B 1 95 ? 20.988 27.584 2.673 1.00 141.82 ? 94 LEU B CD1 1 ATOM 3753 C CD2 . LEU B 1 95 ? 20.606 29.437 4.300 1.00 144.68 ? 94 LEU B CD2 1 ATOM 3754 N N . ASP B 1 96 ? 20.401 25.150 7.419 1.00 137.28 ? 95 ASP B N 1 ATOM 3755 C CA . ASP B 1 96 ? 20.726 24.039 8.303 1.00 141.28 ? 95 ASP B CA 1 ATOM 3756 C C . ASP B 1 96 ? 19.440 23.621 8.986 1.00 143.28 ? 95 ASP B C 1 ATOM 3757 O O . ASP B 1 96 ? 19.008 24.280 9.924 1.00 146.85 ? 95 ASP B O 1 ATOM 3758 C CB . ASP B 1 96 ? 21.790 24.447 9.329 1.00 144.72 ? 95 ASP B CB 1 ATOM 3759 C CG . ASP B 1 96 ? 22.308 23.263 10.160 1.00 146.50 ? 95 ASP B CG 1 ATOM 3760 O OD1 . ASP B 1 96 ? 21.633 22.211 10.228 1.00 144.24 ? 95 ASP B OD1 1 ATOM 3761 O OD2 . ASP B 1 96 ? 23.407 23.385 10.746 1.00 147.66 ? 95 ASP B OD2 1 ATOM 3762 N N . PRO B 1 97 ? 18.839 22.502 8.547 1.00 143.82 ? 96 PRO B N 1 ATOM 3763 C CA . PRO B 1 97 ? 17.477 22.180 8.966 1.00 145.77 ? 96 PRO B CA 1 ATOM 3764 C C . PRO B 1 97 ? 17.297 21.988 10.468 1.00 149.58 ? 96 PRO B C 1 ATOM 3765 O O . PRO B 1 97 ? 16.246 22.334 11.017 1.00 154.29 ? 96 PRO B O 1 ATOM 3766 C CB . PRO B 1 97 ? 17.179 20.876 8.218 1.00 145.09 ? 96 PRO B CB 1 ATOM 3767 C CG . PRO B 1 97 ? 18.512 20.257 7.981 1.00 145.13 ? 96 PRO B CG 1 ATOM 3768 C CD . PRO B 1 97 ? 19.468 21.397 7.800 1.00 144.30 ? 96 PRO B CD 1 ATOM 3769 N N . SER B 1 98 ? 18.310 21.433 11.119 1.00 151.49 ? 97 SER B N 1 ATOM 3770 C CA . SER B 1 98 ? 18.273 21.274 12.569 1.00 157.28 ? 97 SER B CA 1 ATOM 3771 C C . SER B 1 98 ? 18.434 22.630 13.253 1.00 165.46 ? 97 SER B C 1 ATOM 3772 O O . SER B 1 98 ? 17.911 22.865 14.350 1.00 165.89 ? 97 SER B O 1 ATOM 3773 C CB . SER B 1 98 ? 19.391 20.335 13.027 1.00 158.81 ? 97 SER B CB 1 ATOM 3774 O OG . SER B 1 98 ? 19.334 20.102 14.425 1.00 163.57 ? 97 SER B OG 1 ATOM 3775 N N . LYS B 1 99 ? 19.184 23.507 12.602 1.00 175.15 ? 98 LYS B N 1 ATOM 3776 C CA . LYS B 1 99 ? 19.642 24.722 13.258 1.00 180.36 ? 98 LYS B CA 1 ATOM 3777 C C . LYS B 1 99 ? 18.784 25.798 12.677 1.00 183.01 ? 98 LYS B C 1 ATOM 3778 O O . LYS B 1 99 ? 19.161 26.457 11.715 1.00 187.23 ? 98 LYS B O 1 ATOM 3779 C CB . LYS B 1 99 ? 21.137 24.972 13.034 1.00 182.25 ? 98 LYS B CB 1 ATOM 3780 C CG . LYS B 1 99 ? 22.064 23.895 13.600 1.00 184.27 ? 98 LYS B CG 1 ATOM 3781 C CD . LYS B 1 99 ? 22.045 23.813 15.126 1.00 187.07 ? 98 LYS B CD 1 ATOM 3782 C CE . LYS B 1 99 ? 21.117 22.721 15.645 1.00 186.87 ? 98 LYS B CE 1 ATOM 3783 N NZ . LYS B 1 99 ? 21.221 22.522 17.118 1.00 187.17 ? 98 LYS B NZ 1 ATOM 3784 N N . SER B 1 100 ? 17.603 25.936 13.262 1.00 185.01 ? 99 SER B N 1 ATOM 3785 C CA . SER B 1 100 ? 16.594 26.893 12.804 1.00 187.53 ? 99 SER B CA 1 ATOM 3786 C C . SER B 1 100 ? 17.094 28.338 12.575 1.00 192.94 ? 99 SER B C 1 ATOM 3787 O O . SER B 1 100 ? 17.484 28.660 11.457 1.00 207.23 ? 99 SER B O 1 ATOM 3788 C CB . SER B 1 100 ? 15.375 26.866 13.736 1.00 187.21 ? 99 SER B CB 1 ATOM 3789 O OG . SER B 1 100 ? 14.326 27.681 13.246 1.00 184.83 ? 99 SER B OG 1 ATOM 3790 N N . SER B 1 101 ? 17.098 29.176 13.616 1.00 187.46 ? 100 SER B N 1 ATOM 3791 C CA . SER B 1 101 ? 17.226 30.634 13.487 1.00 183.57 ? 100 SER B CA 1 ATOM 3792 C C . SER B 1 101 ? 18.405 31.077 12.623 1.00 183.66 ? 100 SER B C 1 ATOM 3793 O O . SER B 1 101 ? 18.293 31.913 11.702 1.00 187.33 ? 100 SER B O 1 ATOM 3794 C CB . SER B 1 101 ? 17.409 31.236 14.887 1.00 181.83 ? 100 SER B CB 1 ATOM 3795 O OG . SER B 1 101 ? 18.541 30.673 15.540 1.00 175.47 ? 100 SER B OG 1 ATOM 3796 N N . VAL B 1 102 ? 19.543 30.486 12.947 1.00 178.90 ? 101 VAL B N 1 ATOM 3797 C CA . VAL B 1 102 ? 20.808 30.920 12.374 1.00 173.86 ? 101 VAL B CA 1 ATOM 3798 C C . VAL B 1 102 ? 20.858 30.726 10.848 1.00 170.63 ? 101 VAL B C 1 ATOM 3799 O O . VAL B 1 102 ? 21.541 31.476 10.154 1.00 173.28 ? 101 VAL B O 1 ATOM 3800 C CB . VAL B 1 102 ? 22.017 30.268 13.090 1.00 171.91 ? 101 VAL B CB 1 ATOM 3801 C CG1 . VAL B 1 102 ? 21.921 30.433 14.608 1.00 169.62 ? 101 VAL B CG1 1 ATOM 3802 C CG2 . VAL B 1 102 ? 22.135 28.798 12.718 1.00 172.69 ? 101 VAL B CG2 1 ATOM 3803 N N . GLY B 1 103 ? 20.107 29.758 10.321 1.00 164.92 ? 102 GLY B N 1 ATOM 3804 C CA . GLY B 1 103 ? 20.144 29.461 8.891 1.00 159.87 ? 102 GLY B CA 1 ATOM 3805 C C . GLY B 1 103 ? 19.014 30.031 8.046 1.00 155.32 ? 102 GLY B C 1 ATOM 3806 O O . GLY B 1 103 ? 18.827 29.592 6.900 1.00 154.61 ? 102 GLY B O 1 ATOM 3807 N N . SER B 1 104 ? 18.273 31.009 8.574 1.00 150.23 ? 103 SER B N 1 ATOM 3808 C CA . SER B 1 104 ? 17.141 31.573 7.823 1.00 143.01 ? 103 SER B CA 1 ATOM 3809 C C . SER B 1 104 ? 17.576 32.342 6.565 1.00 134.54 ? 103 SER B C 1 ATOM 3810 O O . SER B 1 104 ? 18.383 33.261 6.632 1.00 130.98 ? 103 SER B O 1 ATOM 3811 C CB . SER B 1 104 ? 16.261 32.456 8.713 1.00 145.45 ? 103 SER B CB 1 ATOM 3812 O OG . SER B 1 104 ? 16.982 33.560 9.228 1.00 148.99 ? 103 SER B OG 1 ATOM 3813 N N . TYR B 1 105 ? 17.029 31.950 5.419 1.00 130.41 ? 104 TYR B N 1 ATOM 3814 C CA . TYR B 1 105 ? 17.387 32.554 4.130 1.00 128.51 ? 104 TYR B CA 1 ATOM 3815 C C . TYR B 1 105 ? 16.133 33.057 3.394 1.00 127.86 ? 104 TYR B C 1 ATOM 3816 O O . TYR B 1 105 ? 15.812 34.242 3.477 1.00 125.15 ? 104 TYR B O 1 ATOM 3817 C CB . TYR B 1 105 ? 18.181 31.536 3.304 1.00 127.70 ? 104 TYR B CB 1 ATOM 3818 C CG . TYR B 1 105 ? 18.687 31.986 1.942 1.00 128.06 ? 104 TYR B CG 1 ATOM 3819 C CD1 . TYR B 1 105 ? 19.498 33.110 1.808 1.00 130.31 ? 104 TYR B CD1 1 ATOM 3820 C CD2 . TYR B 1 105 ? 18.409 31.244 0.792 1.00 127.71 ? 104 TYR B CD2 1 ATOM 3821 C CE1 . TYR B 1 105 ? 19.982 33.505 0.565 1.00 130.93 ? 104 TYR B CE1 1 ATOM 3822 C CE2 . TYR B 1 105 ? 18.889 31.629 -0.450 1.00 128.08 ? 104 TYR B CE2 1 ATOM 3823 C CZ . TYR B 1 105 ? 19.675 32.759 -0.562 1.00 129.49 ? 104 TYR B CZ 1 ATOM 3824 O OH . TYR B 1 105 ? 20.152 33.137 -1.799 1.00 128.15 ? 104 TYR B OH 1 ATOM 3825 N N . PHE B 1 106 ? 15.419 32.172 2.694 1.00 128.76 ? 105 PHE B N 1 ATOM 3826 C CA . PHE B 1 106 ? 14.177 32.553 1.991 1.00 130.71 ? 105 PHE B CA 1 ATOM 3827 C C . PHE B 1 106 ? 12.927 32.525 2.886 1.00 130.03 ? 105 PHE B C 1 ATOM 3828 O O . PHE B 1 106 ? 11.837 32.915 2.443 1.00 129.90 ? 105 PHE B O 1 ATOM 3829 C CB . PHE B 1 106 ? 13.923 31.629 0.790 1.00 132.24 ? 105 PHE B CB 1 ATOM 3830 C CG . PHE B 1 106 ? 14.424 32.167 -0.521 1.00 135.42 ? 105 PHE B CG 1 ATOM 3831 C CD1 . PHE B 1 106 ? 13.720 33.157 -1.196 1.00 136.72 ? 105 PHE B CD1 1 ATOM 3832 C CD2 . PHE B 1 106 ? 15.579 31.659 -1.101 1.00 138.55 ? 105 PHE B CD2 1 ATOM 3833 C CE1 . PHE B 1 106 ? 14.170 33.644 -2.415 1.00 138.00 ? 105 PHE B CE1 1 ATOM 3834 C CE2 . PHE B 1 106 ? 16.033 32.141 -2.319 1.00 140.35 ? 105 PHE B CE2 1 ATOM 3835 C CZ . PHE B 1 106 ? 15.328 33.135 -2.978 1.00 138.85 ? 105 PHE B CZ 1 ATOM 3836 N N . HIS B 1 107 ? 13.076 32.057 4.127 1.00 129.66 ? 106 HIS B N 1 ATOM 3837 C CA . HIS B 1 107 ? 11.930 31.863 5.022 1.00 127.66 ? 106 HIS B CA 1 ATOM 3838 C C . HIS B 1 107 ? 10.971 33.048 5.113 1.00 126.88 ? 106 HIS B C 1 ATOM 3839 O O . HIS B 1 107 ? 9.759 32.887 4.992 1.00 123.75 ? 106 HIS B O 1 ATOM 3840 C CB . HIS B 1 107 ? 12.403 31.529 6.437 1.00 128.84 ? 106 HIS B CB 1 ATOM 3841 C CG . HIS B 1 107 ? 11.307 31.549 7.459 1.00 130.33 ? 106 HIS B CG 1 ATOM 3842 N ND1 . HIS B 1 107 ? 10.323 30.585 7.515 1.00 131.46 ? 106 HIS B ND1 1 ATOM 3843 C CD2 . HIS B 1 107 ? 11.040 32.415 8.465 1.00 130.67 ? 106 HIS B CD2 1 ATOM 3844 C CE1 . HIS B 1 107 ? 9.500 30.853 8.513 1.00 129.52 ? 106 HIS B CE1 1 ATOM 3845 N NE2 . HIS B 1 107 ? 9.913 31.958 9.106 1.00 130.20 ? 106 HIS B NE2 1 ATOM 3846 N N . THR B 1 108 ? 11.513 34.234 5.352 1.00 128.26 ? 107 THR B N 1 ATOM 3847 C CA . THR B 1 108 ? 10.680 35.406 5.550 1.00 129.01 ? 107 THR B CA 1 ATOM 3848 C C . THR B 1 108 ? 9.854 35.729 4.315 1.00 125.06 ? 107 THR B C 1 ATOM 3849 O O . THR B 1 108 ? 8.669 36.036 4.429 1.00 123.93 ? 107 THR B O 1 ATOM 3850 C CB . THR B 1 108 ? 11.521 36.632 5.932 1.00 132.10 ? 107 THR B CB 1 ATOM 3851 O OG1 . THR B 1 108 ? 12.420 36.279 6.990 1.00 135.57 ? 107 THR B OG1 1 ATOM 3852 C CG2 . THR B 1 108 ? 10.623 37.780 6.390 1.00 134.82 ? 107 THR B CG2 1 ATOM 3853 N N . MET B 1 109 ? 10.472 35.649 3.140 1.00 122.68 ? 108 MET B N 1 ATOM 3854 C CA . MET B 1 109 ? 9.759 35.923 1.888 1.00 122.34 ? 108 MET B CA 1 ATOM 3855 C C . MET B 1 109 ? 8.635 34.915 1.665 1.00 120.79 ? 108 MET B C 1 ATOM 3856 O O . MET B 1 109 ? 7.513 35.286 1.295 1.00 118.75 ? 108 MET B O 1 ATOM 3857 C CB . MET B 1 109 ? 10.709 35.893 0.686 1.00 122.42 ? 108 MET B CB 1 ATOM 3858 C CG . MET B 1 109 ? 10.047 36.303 -0.628 1.00 123.98 ? 108 MET B CG 1 ATOM 3859 S SD . MET B 1 109 ? 11.110 36.200 -2.085 1.00 124.22 ? 108 MET B SD 1 ATOM 3860 C CE . MET B 1 109 ? 12.350 37.432 -1.693 1.00 125.54 ? 108 MET B CE 1 ATOM 3861 N N . VAL B 1 110 ? 8.938 33.642 1.904 1.00 119.12 ? 109 VAL B N 1 ATOM 3862 C CA . VAL B 1 110 ? 7.954 32.585 1.704 1.00 117.51 ? 109 VAL B CA 1 ATOM 3863 C C . VAL B 1 110 ? 6.785 32.744 2.685 1.00 118.45 ? 109 VAL B C 1 ATOM 3864 O O . VAL B 1 110 ? 5.619 32.600 2.308 1.00 118.52 ? 109 VAL B O 1 ATOM 3865 C CB . VAL B 1 110 ? 8.585 31.181 1.847 1.00 115.85 ? 109 VAL B CB 1 ATOM 3866 C CG1 . VAL B 1 110 ? 7.529 30.099 1.668 1.00 115.95 ? 109 VAL B CG1 1 ATOM 3867 C CG2 . VAL B 1 110 ? 9.693 30.983 0.819 1.00 114.86 ? 109 VAL B CG2 1 ATOM 3868 N N . GLU B 1 111 ? 7.097 33.047 3.940 1.00 119.62 ? 110 GLU B N 1 ATOM 3869 C CA . GLU B 1 111 ? 6.053 33.282 4.931 1.00 122.01 ? 110 GLU B CA 1 ATOM 3870 C C . GLU B 1 111 ? 5.119 34.410 4.519 1.00 122.12 ? 110 GLU B C 1 ATOM 3871 O O . GLU B 1 111 ? 3.912 34.317 4.722 1.00 121.05 ? 110 GLU B O 1 ATOM 3872 C CB . GLU B 1 111 ? 6.645 33.564 6.314 1.00 125.21 ? 110 GLU B CB 1 ATOM 3873 C CG . GLU B 1 111 ? 6.833 32.315 7.160 1.00 129.13 ? 110 GLU B CG 1 ATOM 3874 C CD . GLU B 1 111 ? 5.529 31.580 7.435 1.00 132.26 ? 110 GLU B CD 1 ATOM 3875 O OE1 . GLU B 1 111 ? 4.445 32.202 7.339 1.00 137.49 ? 110 GLU B OE1 1 ATOM 3876 O OE2 . GLU B 1 111 ? 5.589 30.372 7.744 1.00 129.31 ? 110 GLU B OE2 1 ATOM 3877 N N . SER B 1 112 ? 5.680 35.468 3.942 1.00 123.72 ? 111 SER B N 1 ATOM 3878 C CA . SER B 1 112 ? 4.875 36.579 3.441 1.00 125.83 ? 111 SER B CA 1 ATOM 3879 C C . SER B 1 112 ? 3.973 36.137 2.284 1.00 125.46 ? 111 SER B C 1 ATOM 3880 O O . SER B 1 112 ? 2.784 36.474 2.258 1.00 128.81 ? 111 SER B O 1 ATOM 3881 C CB . SER B 1 112 ? 5.767 37.751 3.019 1.00 126.10 ? 111 SER B CB 1 ATOM 3882 O OG . SER B 1 112 ? 6.400 38.336 4.145 1.00 125.52 ? 111 SER B OG 1 ATOM 3883 N N . LEU B 1 113 ? 4.530 35.379 1.340 1.00 121.84 ? 112 LEU B N 1 ATOM 3884 C CA . LEU B 1 113 ? 3.741 34.845 0.225 1.00 120.73 ? 112 LEU B CA 1 ATOM 3885 C C . LEU B 1 113 ? 2.570 33.998 0.722 1.00 122.14 ? 112 LEU B C 1 ATOM 3886 O O . LEU B 1 113 ? 1.444 34.131 0.236 1.00 121.30 ? 112 LEU B O 1 ATOM 3887 C CB . LEU B 1 113 ? 4.624 34.020 -0.709 1.00 118.08 ? 112 LEU B CB 1 ATOM 3888 C CG . LEU B 1 113 ? 5.631 34.835 -1.520 1.00 117.57 ? 112 LEU B CG 1 ATOM 3889 C CD1 . LEU B 1 113 ? 6.730 33.945 -2.077 1.00 116.19 ? 112 LEU B CD1 1 ATOM 3890 C CD2 . LEU B 1 113 ? 4.930 35.586 -2.640 1.00 119.14 ? 112 LEU B CD2 1 ATOM 3891 N N . VAL B 1 114 ? 2.840 33.141 1.701 1.00 125.59 ? 113 VAL B N 1 ATOM 3892 C CA . VAL B 1 114 ? 1.798 32.316 2.321 1.00 130.46 ? 113 VAL B CA 1 ATOM 3893 C C . VAL B 1 114 ? 0.721 33.189 2.967 1.00 133.39 ? 113 VAL B C 1 ATOM 3894 O O . VAL B 1 114 ? -0.473 32.910 2.839 1.00 133.85 ? 113 VAL B O 1 ATOM 3895 C CB . VAL B 1 114 ? 2.391 31.355 3.379 1.00 131.11 ? 113 VAL B CB 1 ATOM 3896 C CG1 . VAL B 1 114 ? 1.296 30.731 4.239 1.00 132.94 ? 113 VAL B CG1 1 ATOM 3897 C CG2 . VAL B 1 114 ? 3.211 30.267 2.702 1.00 129.57 ? 113 VAL B CG2 1 ATOM 3898 N N . GLY B 1 115 ? 1.147 34.242 3.661 1.00 135.80 ? 114 GLY B N 1 ATOM 3899 C CA . GLY B 1 115 ? 0.222 35.220 4.233 1.00 139.10 ? 114 GLY B CA 1 ATOM 3900 C C . GLY B 1 115 ? -0.690 35.862 3.200 1.00 140.64 ? 114 GLY B C 1 ATOM 3901 O O . GLY B 1 115 ? -1.826 36.226 3.512 1.00 140.29 ? 114 GLY B O 1 ATOM 3902 N N . TRP B 1 116 ? -0.196 35.995 1.969 1.00 142.46 ? 115 TRP B N 1 ATOM 3903 C CA . TRP B 1 116 ? -0.990 36.547 0.872 1.00 147.68 ? 115 TRP B CA 1 ATOM 3904 C C . TRP B 1 116 ? -1.807 35.491 0.116 1.00 147.62 ? 115 TRP B C 1 ATOM 3905 O O . TRP B 1 116 ? -2.460 35.813 -0.876 1.00 150.93 ? 115 TRP B O 1 ATOM 3906 C CB . TRP B 1 116 ? -0.105 37.314 -0.117 1.00 150.85 ? 115 TRP B CB 1 ATOM 3907 C CG . TRP B 1 116 ? 0.820 38.310 0.518 1.00 153.73 ? 115 TRP B CG 1 ATOM 3908 C CD1 . TRP B 1 116 ? 0.606 39.020 1.668 1.00 157.59 ? 115 TRP B CD1 1 ATOM 3909 C CD2 . TRP B 1 116 ? 2.101 38.721 0.024 1.00 153.78 ? 115 TRP B CD2 1 ATOM 3910 N NE1 . TRP B 1 116 ? 1.682 39.837 1.926 1.00 159.42 ? 115 TRP B NE1 1 ATOM 3911 C CE2 . TRP B 1 116 ? 2.612 39.674 0.931 1.00 157.18 ? 115 TRP B CE2 1 ATOM 3912 C CE3 . TRP B 1 116 ? 2.870 38.372 -1.095 1.00 151.18 ? 115 TRP B CE3 1 ATOM 3913 C CZ2 . TRP B 1 116 ? 3.858 40.283 0.752 1.00 157.17 ? 115 TRP B CZ2 1 ATOM 3914 C CZ3 . TRP B 1 116 ? 4.108 38.978 -1.271 1.00 150.64 ? 115 TRP B CZ3 1 ATOM 3915 C CH2 . TRP B 1 116 ? 4.589 39.921 -0.352 1.00 153.62 ? 115 TRP B CH2 1 ATOM 3916 N N . GLY B 1 117 ? -1.760 34.238 0.562 1.00 146.74 ? 116 GLY B N 1 ATOM 3917 C CA . GLY B 1 117 ? -2.620 33.186 0.013 1.00 145.71 ? 116 GLY B CA 1 ATOM 3918 C C . GLY B 1 117 ? -1.935 32.075 -0.770 1.00 142.07 ? 116 GLY B C 1 ATOM 3919 O O . GLY B 1 117 ? -2.615 31.214 -1.332 1.00 144.05 ? 116 GLY B O 1 ATOM 3920 N N . TYR B 1 118 ? -0.602 32.078 -0.810 1.00 136.07 ? 117 TYR B N 1 ATOM 3921 C CA . TYR B 1 118 ? 0.149 31.019 -1.492 1.00 130.57 ? 117 TYR B CA 1 ATOM 3922 C C . TYR B 1 118 ? 0.252 29.777 -0.615 1.00 129.13 ? 117 TYR B C 1 ATOM 3923 O O . TYR B 1 118 ? -0.020 29.831 0.591 1.00 129.23 ? 117 TYR B O 1 ATOM 3924 C CB . TYR B 1 118 ? 1.545 31.502 -1.886 1.00 126.79 ? 117 TYR B CB 1 ATOM 3925 C CG . TYR B 1 118 ? 1.542 32.378 -3.110 1.00 124.49 ? 117 TYR B CG 1 ATOM 3926 C CD1 . TYR B 1 118 ? 0.995 33.653 -3.074 1.00 123.89 ? 117 TYR B CD1 1 ATOM 3927 C CD2 . TYR B 1 118 ? 2.080 31.928 -4.310 1.00 122.60 ? 117 TYR B CD2 1 ATOM 3928 C CE1 . TYR B 1 118 ? 0.986 34.455 -4.200 1.00 124.37 ? 117 TYR B CE1 1 ATOM 3929 C CE2 . TYR B 1 118 ? 2.076 32.721 -5.441 1.00 122.43 ? 117 TYR B CE2 1 ATOM 3930 C CZ . TYR B 1 118 ? 1.529 33.985 -5.380 1.00 123.26 ? 117 TYR B CZ 1 ATOM 3931 O OH . TYR B 1 118 ? 1.521 34.778 -6.501 1.00 121.90 ? 117 TYR B OH 1 ATOM 3932 N N . THR B 1 119 ? 0.649 28.667 -1.236 1.00 125.65 ? 118 THR B N 1 ATOM 3933 C CA . THR B 1 119 ? 0.755 27.372 -0.564 1.00 125.61 ? 118 THR B CA 1 ATOM 3934 C C . THR B 1 119 ? 2.073 26.678 -0.923 1.00 123.86 ? 118 THR B C 1 ATOM 3935 O O . THR B 1 119 ? 2.416 26.548 -2.093 1.00 125.21 ? 118 THR B O 1 ATOM 3936 C CB . THR B 1 119 ? -0.423 26.459 -0.952 1.00 126.81 ? 118 THR B CB 1 ATOM 3937 O OG1 . THR B 1 119 ? -1.662 27.134 -0.689 1.00 126.37 ? 118 THR B OG1 1 ATOM 3938 C CG2 . THR B 1 119 ? -0.378 25.147 -0.169 1.00 127.96 ? 118 THR B CG2 1 ATOM 3939 N N . ARG B 1 120 ? 2.797 26.222 0.095 1.00 122.13 ? 119 ARG B N 1 ATOM 3940 C CA . ARG B 1 120 ? 4.107 25.589 -0.100 1.00 120.16 ? 119 ARG B CA 1 ATOM 3941 C C . ARG B 1 120 ? 4.014 24.362 -1.004 1.00 119.06 ? 119 ARG B C 1 ATOM 3942 O O . ARG B 1 120 ? 3.167 23.490 -0.792 1.00 119.14 ? 119 ARG B O 1 ATOM 3943 C CB . ARG B 1 120 ? 4.707 25.166 1.245 1.00 121.47 ? 119 ARG B CB 1 ATOM 3944 C CG . ARG B 1 120 ? 5.134 26.321 2.138 1.00 121.85 ? 119 ARG B CG 1 ATOM 3945 C CD . ARG B 1 120 ? 5.699 25.828 3.466 1.00 122.72 ? 119 ARG B CD 1 ATOM 3946 N NE . ARG B 1 120 ? 5.489 26.797 4.544 1.00 124.36 ? 119 ARG B NE 1 ATOM 3947 C CZ . ARG B 1 120 ? 6.237 27.879 4.757 1.00 124.41 ? 119 ARG B CZ 1 ATOM 3948 N NH1 . ARG B 1 120 ? 7.265 28.159 3.968 1.00 123.53 ? 119 ARG B NH1 1 ATOM 3949 N NH2 . ARG B 1 120 ? 5.956 28.695 5.768 1.00 123.61 ? 119 ARG B NH2 1 ATOM 3950 N N . GLY B 1 121 ? 4.880 24.308 -2.015 1.00 117.44 ? 120 GLY B N 1 ATOM 3951 C CA . GLY B 1 121 ? 4.934 23.169 -2.931 1.00 116.75 ? 120 GLY B CA 1 ATOM 3952 C C . GLY B 1 121 ? 3.858 23.189 -4.001 1.00 117.37 ? 120 GLY B C 1 ATOM 3953 O O . GLY B 1 121 ? 3.817 22.302 -4.853 1.00 116.74 ? 120 GLY B O 1 ATOM 3954 N N . GLU B 1 122 ? 2.994 24.202 -3.961 1.00 118.33 ? 121 GLU B N 1 ATOM 3955 C CA . GLU B 1 122 ? 1.878 24.309 -4.882 1.00 120.22 ? 121 GLU B CA 1 ATOM 3956 C C . GLU B 1 122 ? 2.020 25.579 -5.710 1.00 120.43 ? 121 GLU B C 1 ATOM 3957 O O . GLU B 1 122 ? 2.585 25.533 -6.794 1.00 117.82 ? 121 GLU B O 1 ATOM 3958 C CB . GLU B 1 122 ? 0.552 24.272 -4.122 1.00 121.92 ? 121 GLU B CB 1 ATOM 3959 C CG . GLU B 1 122 ? 0.233 22.914 -3.519 1.00 123.81 ? 121 GLU B CG 1 ATOM 3960 C CD . GLU B 1 122 ? -1.173 22.833 -2.951 1.00 126.51 ? 121 GLU B CD 1 ATOM 3961 O OE1 . GLU B 1 122 ? -2.095 23.446 -3.532 1.00 129.27 ? 121 GLU B OE1 1 ATOM 3962 O OE2 . GLU B 1 122 ? -1.361 22.142 -1.927 1.00 125.79 ? 121 GLU B OE2 1 ATOM 3963 N N . ASP B 1 123 ? 1.543 26.711 -5.190 1.00 122.90 ? 122 ASP B N 1 ATOM 3964 C CA . ASP B 1 123 ? 1.632 28.002 -5.887 1.00 125.77 ? 122 ASP B CA 1 ATOM 3965 C C . ASP B 1 123 ? 3.063 28.529 -5.920 1.00 125.32 ? 122 ASP B C 1 ATOM 3966 O O . ASP B 1 123 ? 3.462 29.196 -6.876 1.00 125.01 ? 122 ASP B O 1 ATOM 3967 C CB . ASP B 1 123 ? 0.787 29.069 -5.175 1.00 128.75 ? 122 ASP B CB 1 ATOM 3968 C CG . ASP B 1 123 ? -0.658 28.671 -5.009 1.00 131.94 ? 122 ASP B CG 1 ATOM 3969 O OD1 . ASP B 1 123 ? -1.245 28.143 -5.976 1.00 134.74 ? 122 ASP B OD1 1 ATOM 3970 O OD2 . ASP B 1 123 ? -1.208 28.904 -3.911 1.00 132.20 ? 122 ASP B OD2 1 ATOM 3971 N N . VAL B 1 124 ? 3.805 28.231 -4.853 1.00 124.57 ? 123 VAL B N 1 ATOM 3972 C CA . VAL B 1 124 ? 5.202 28.615 -4.730 1.00 123.36 ? 123 VAL B CA 1 ATOM 3973 C C . VAL B 1 124 ? 6.067 27.362 -4.594 1.00 120.89 ? 123 VAL B C 1 ATOM 3974 O O . VAL B 1 124 ? 5.798 26.488 -3.756 1.00 118.03 ? 123 VAL B O 1 ATOM 3975 C CB . VAL B 1 124 ? 5.440 29.585 -3.546 1.00 123.87 ? 123 VAL B CB 1 ATOM 3976 C CG1 . VAL B 1 124 ? 5.215 28.909 -2.196 1.00 124.41 ? 123 VAL B CG1 1 ATOM 3977 C CG2 . VAL B 1 124 ? 6.836 30.189 -3.623 1.00 123.44 ? 123 VAL B CG2 1 ATOM 3978 N N . ARG B 1 125 ? 7.086 27.282 -5.446 1.00 120.49 ? 124 ARG B N 1 ATOM 3979 C CA . ARG B 1 125 ? 8.023 26.162 -5.447 1.00 119.96 ? 124 ARG B CA 1 ATOM 3980 C C . ARG B 1 125 ? 9.453 26.654 -5.627 1.00 121.44 ? 124 ARG B C 1 ATOM 3981 O O . ARG B 1 125 ? 9.698 27.649 -6.310 1.00 122.95 ? 124 ARG B O 1 ATOM 3982 C CB . ARG B 1 125 ? 7.687 25.191 -6.576 1.00 119.49 ? 124 ARG B CB 1 ATOM 3983 C CG . ARG B 1 125 ? 6.271 24.649 -6.529 1.00 119.54 ? 124 ARG B CG 1 ATOM 3984 C CD . ARG B 1 125 ? 6.080 23.563 -7.569 1.00 120.19 ? 124 ARG B CD 1 ATOM 3985 N NE . ARG B 1 125 ? 4.671 23.286 -7.822 1.00 121.80 ? 124 ARG B NE 1 ATOM 3986 C CZ . ARG B 1 125 ? 4.227 22.361 -8.670 1.00 125.96 ? 124 ARG B CZ 1 ATOM 3987 N NH1 . ARG B 1 125 ? 5.081 21.605 -9.359 1.00 127.03 ? 124 ARG B NH1 1 ATOM 3988 N NH2 . ARG B 1 125 ? 2.920 22.185 -8.830 1.00 128.48 ? 124 ARG B NH2 1 ATOM 3989 N N . GLY B 1 126 ? 10.396 25.945 -5.017 1.00 123.37 ? 125 GLY B N 1 ATOM 3990 C CA . GLY B 1 126 ? 11.813 26.268 -5.149 1.00 124.19 ? 125 GLY B CA 1 ATOM 3991 C C . GLY B 1 126 ? 12.489 25.503 -6.274 1.00 124.51 ? 125 GLY B C 1 ATOM 3992 O O . GLY B 1 126 ? 12.070 24.396 -6.640 1.00 124.02 ? 125 GLY B O 1 ATOM 3993 N N . ALA B 1 127 ? 13.546 26.103 -6.816 1.00 125.36 ? 126 ALA B N 1 ATOM 3994 C CA . ALA B 1 127 ? 14.373 25.475 -7.842 1.00 125.81 ? 126 ALA B CA 1 ATOM 3995 C C . ALA B 1 127 ? 15.835 25.449 -7.383 1.00 126.05 ? 126 ALA B C 1 ATOM 3996 O O . ALA B 1 127 ? 16.689 26.126 -7.963 1.00 125.87 ? 126 ALA B O 1 ATOM 3997 C CB . ALA B 1 127 ? 14.236 26.224 -9.161 1.00 126.32 ? 126 ALA B CB 1 ATOM 3998 N N . PRO B 1 128 ? 16.131 24.662 -6.333 1.00 125.68 ? 127 PRO B N 1 ATOM 3999 C CA . PRO B 1 128 ? 17.517 24.512 -5.894 1.00 126.00 ? 127 PRO B CA 1 ATOM 4000 C C . PRO B 1 128 ? 18.360 23.696 -6.883 1.00 127.24 ? 127 PRO B C 1 ATOM 4001 O O . PRO B 1 128 ? 17.825 22.918 -7.678 1.00 128.69 ? 127 PRO B O 1 ATOM 4002 C CB . PRO B 1 128 ? 17.376 23.776 -4.560 1.00 126.41 ? 127 PRO B CB 1 ATOM 4003 C CG . PRO B 1 128 ? 16.136 22.971 -4.717 1.00 125.93 ? 127 PRO B CG 1 ATOM 4004 C CD . PRO B 1 128 ? 15.215 23.805 -5.558 1.00 125.28 ? 127 PRO B CD 1 ATOM 4005 N N . TYR B 1 129 ? 19.674 23.883 -6.826 1.00 127.42 ? 128 TYR B N 1 ATOM 4006 C CA . TYR B 1 129 ? 20.604 23.210 -7.734 1.00 128.25 ? 128 TYR B CA 1 ATOM 4007 C C . TYR B 1 129 ? 21.961 23.005 -7.063 1.00 129.35 ? 128 TYR B C 1 ATOM 4008 O O . TYR B 1 129 ? 22.199 23.510 -5.961 1.00 128.77 ? 128 TYR B O 1 ATOM 4009 C CB . TYR B 1 129 ? 20.782 24.043 -9.007 1.00 126.88 ? 128 TYR B CB 1 ATOM 4010 C CG . TYR B 1 129 ? 21.169 25.484 -8.747 1.00 126.15 ? 128 TYR B CG 1 ATOM 4011 C CD1 . TYR B 1 129 ? 20.212 26.425 -8.377 1.00 125.03 ? 128 TYR B CD1 1 ATOM 4012 C CD2 . TYR B 1 129 ? 22.491 25.907 -8.870 1.00 127.28 ? 128 TYR B CD2 1 ATOM 4013 C CE1 . TYR B 1 129 ? 20.559 27.745 -8.136 1.00 125.53 ? 128 TYR B CE1 1 ATOM 4014 C CE2 . TYR B 1 129 ? 22.848 27.227 -8.633 1.00 126.48 ? 128 TYR B CE2 1 ATOM 4015 C CZ . TYR B 1 129 ? 21.879 28.142 -8.266 1.00 125.75 ? 128 TYR B CZ 1 ATOM 4016 O OH . TYR B 1 129 ? 22.224 29.453 -8.023 1.00 124.86 ? 128 TYR B OH 1 ATOM 4017 N N . ASP B 1 130 ? 22.844 22.262 -7.730 1.00 129.85 ? 129 ASP B N 1 ATOM 4018 C CA . ASP B 1 130 ? 24.212 22.083 -7.251 1.00 131.02 ? 129 ASP B CA 1 ATOM 4019 C C . ASP B 1 130 ? 25.007 23.343 -7.586 1.00 133.67 ? 129 ASP B C 1 ATOM 4020 O O . ASP B 1 130 ? 25.609 23.460 -8.656 1.00 132.68 ? 129 ASP B O 1 ATOM 4021 C CB . ASP B 1 130 ? 24.860 20.838 -7.873 1.00 131.63 ? 129 ASP B CB 1 ATOM 4022 C CG . ASP B 1 130 ? 26.113 20.386 -7.125 1.00 132.46 ? 129 ASP B CG 1 ATOM 4023 O OD1 . ASP B 1 130 ? 26.699 21.192 -6.367 1.00 132.05 ? 129 ASP B OD1 1 ATOM 4024 O OD2 . ASP B 1 130 ? 26.511 19.214 -7.295 1.00 130.64 ? 129 ASP B OD2 1 ATOM 4025 N N . TRP B 1 131 ? 24.993 24.284 -6.648 1.00 136.77 ? 130 TRP B N 1 ATOM 4026 C CA . TRP B 1 131 ? 25.625 25.597 -6.827 1.00 140.08 ? 130 TRP B CA 1 ATOM 4027 C C . TRP B 1 131 ? 27.155 25.568 -6.835 1.00 138.81 ? 130 TRP B C 1 ATOM 4028 O O . TRP B 1 131 ? 27.789 26.595 -7.068 1.00 138.52 ? 130 TRP B O 1 ATOM 4029 C CB . TRP B 1 131 ? 25.128 26.593 -5.764 1.00 143.66 ? 130 TRP B CB 1 ATOM 4030 C CG . TRP B 1 131 ? 25.037 26.025 -4.377 1.00 145.01 ? 130 TRP B CG 1 ATOM 4031 C CD1 . TRP B 1 131 ? 23.899 25.689 -3.712 1.00 144.44 ? 130 TRP B CD1 1 ATOM 4032 C CD2 . TRP B 1 131 ? 26.122 25.712 -3.497 1.00 146.98 ? 130 TRP B CD2 1 ATOM 4033 N NE1 . TRP B 1 131 ? 24.199 25.192 -2.470 1.00 145.52 ? 130 TRP B NE1 1 ATOM 4034 C CE2 . TRP B 1 131 ? 25.559 25.197 -2.311 1.00 146.84 ? 130 TRP B CE2 1 ATOM 4035 C CE3 . TRP B 1 131 ? 27.515 25.828 -3.591 1.00 148.56 ? 130 TRP B CE3 1 ATOM 4036 C CZ2 . TRP B 1 131 ? 26.337 24.793 -1.229 1.00 147.90 ? 130 TRP B CZ2 1 ATOM 4037 C CZ3 . TRP B 1 131 ? 28.287 25.426 -2.516 1.00 150.62 ? 130 TRP B CZ3 1 ATOM 4038 C CH2 . TRP B 1 131 ? 27.694 24.914 -1.349 1.00 150.58 ? 130 TRP B CH2 1 ATOM 4039 N N . ARG B 1 132 ? 27.745 24.407 -6.562 1.00 138.03 ? 131 ARG B N 1 ATOM 4040 C CA . ARG B 1 132 ? 29.193 24.229 -6.676 1.00 140.64 ? 131 ARG B CA 1 ATOM 4041 C C . ARG B 1 132 ? 29.637 24.271 -8.138 1.00 138.28 ? 131 ARG B C 1 ATOM 4042 O O . ARG B 1 132 ? 30.788 24.611 -8.434 1.00 138.99 ? 131 ARG B O 1 ATOM 4043 C CB . ARG B 1 132 ? 29.614 22.882 -6.081 1.00 145.74 ? 131 ARG B CB 1 ATOM 4044 C CG . ARG B 1 132 ? 29.313 22.701 -4.601 1.00 147.96 ? 131 ARG B CG 1 ATOM 4045 C CD . ARG B 1 132 ? 29.841 21.362 -4.102 1.00 150.63 ? 131 ARG B CD 1 ATOM 4046 N NE . ARG B 1 132 ? 29.165 20.230 -4.740 1.00 152.04 ? 131 ARG B NE 1 ATOM 4047 C CZ . ARG B 1 132 ? 29.536 18.955 -4.627 1.00 155.12 ? 131 ARG B CZ 1 ATOM 4048 N NH1 . ARG B 1 132 ? 30.593 18.611 -3.896 1.00 158.06 ? 131 ARG B NH1 1 ATOM 4049 N NH2 . ARG B 1 132 ? 28.842 18.011 -5.255 1.00 154.36 ? 131 ARG B NH2 1 ATOM 4050 N N . ARG B 1 133 ? 28.722 23.905 -9.036 1.00 134.67 ? 132 ARG B N 1 ATOM 4051 C CA . ARG B 1 133 ? 29.010 23.807 -10.459 1.00 134.95 ? 132 ARG B CA 1 ATOM 4052 C C . ARG B 1 133 ? 28.413 24.962 -11.242 1.00 133.38 ? 132 ARG B C 1 ATOM 4053 O O . ARG B 1 133 ? 27.630 25.756 -10.718 1.00 131.46 ? 132 ARG B O 1 ATOM 4054 C CB . ARG B 1 133 ? 28.470 22.485 -11.002 1.00 135.38 ? 132 ARG B CB 1 ATOM 4055 C CG . ARG B 1 133 ? 29.189 21.274 -10.441 1.00 137.09 ? 132 ARG B CG 1 ATOM 4056 C CD . ARG B 1 133 ? 28.584 19.978 -10.945 1.00 138.65 ? 132 ARG B CD 1 ATOM 4057 N NE . ARG B 1 133 ? 29.538 18.874 -10.857 1.00 143.17 ? 132 ARG B NE 1 ATOM 4058 C CZ . ARG B 1 133 ? 29.278 17.616 -11.208 1.00 144.90 ? 132 ARG B CZ 1 ATOM 4059 N NH1 . ARG B 1 133 ? 28.079 17.276 -11.672 1.00 144.99 ? 132 ARG B NH1 1 ATOM 4060 N NH2 . ARG B 1 133 ? 30.224 16.689 -11.087 1.00 146.37 ? 132 ARG B NH2 1 ATOM 4061 N N . ALA B 1 134 ? 28.802 25.037 -12.509 1.00 133.93 ? 133 ALA B N 1 ATOM 4062 C CA . ALA B 1 134 ? 28.272 26.026 -13.443 1.00 132.66 ? 133 ALA B CA 1 ATOM 4063 C C . ALA B 1 134 ? 27.090 25.409 -14.187 1.00 130.38 ? 133 ALA B C 1 ATOM 4064 O O . ALA B 1 134 ? 26.881 24.202 -14.120 1.00 132.59 ? 133 ALA B O 1 ATOM 4065 C CB . ALA B 1 134 ? 29.359 26.448 -14.424 1.00 136.24 ? 133 ALA B CB 1 ATOM 4066 N N . PRO B 1 135 ? 26.308 26.231 -14.903 1.00 127.84 ? 134 PRO B N 1 ATOM 4067 C CA . PRO B 1 135 ? 25.163 25.714 -15.652 1.00 128.73 ? 134 PRO B CA 1 ATOM 4068 C C . PRO B 1 135 ? 25.449 24.570 -16.632 1.00 133.77 ? 134 PRO B C 1 ATOM 4069 O O . PRO B 1 135 ? 24.568 23.737 -16.877 1.00 135.03 ? 134 PRO B O 1 ATOM 4070 C CB . PRO B 1 135 ? 24.677 26.939 -16.422 1.00 127.26 ? 134 PRO B CB 1 ATOM 4071 C CG . PRO B 1 135 ? 25.048 28.087 -15.557 1.00 127.60 ? 134 PRO B CG 1 ATOM 4072 C CD . PRO B 1 135 ? 26.346 27.704 -14.910 1.00 128.61 ? 134 PRO B CD 1 ATOM 4073 N N . ASN B 1 136 ? 26.660 24.535 -17.183 1.00 137.82 ? 135 ASN B N 1 ATOM 4074 C CA . ASN B 1 136 ? 27.078 23.474 -18.100 1.00 141.36 ? 135 ASN B CA 1 ATOM 4075 C C . ASN B 1 136 ? 26.943 22.065 -17.517 1.00 144.93 ? 135 ASN B C 1 ATOM 4076 O O . ASN B 1 136 ? 26.748 21.101 -18.259 1.00 150.72 ? 135 ASN B O 1 ATOM 4077 C CB . ASN B 1 136 ? 28.526 23.702 -18.549 1.00 142.53 ? 135 ASN B CB 1 ATOM 4078 C CG . ASN B 1 136 ? 29.510 23.705 -17.389 1.00 143.79 ? 135 ASN B CG 1 ATOM 4079 O OD1 . ASN B 1 136 ? 29.121 23.816 -16.223 1.00 141.71 ? 135 ASN B OD1 1 ATOM 4080 N ND2 . ASN B 1 136 ? 30.794 23.575 -17.705 1.00 146.42 ? 135 ASN B ND2 1 ATOM 4081 N N . GLU B 1 137 ? 27.060 21.950 -16.195 1.00 145.84 ? 136 GLU B N 1 ATOM 4082 C CA . GLU B 1 137 ? 26.970 20.658 -15.516 1.00 147.80 ? 136 GLU B CA 1 ATOM 4083 C C . GLU B 1 137 ? 25.708 20.520 -14.658 1.00 147.04 ? 136 GLU B C 1 ATOM 4084 O O . GLU B 1 137 ? 25.672 19.719 -13.722 1.00 149.01 ? 136 GLU B O 1 ATOM 4085 C CB . GLU B 1 137 ? 28.210 20.442 -14.647 1.00 149.49 ? 136 GLU B CB 1 ATOM 4086 C CG . GLU B 1 137 ? 29.508 20.327 -15.425 1.00 152.14 ? 136 GLU B CG 1 ATOM 4087 C CD . GLU B 1 137 ? 30.720 20.257 -14.516 1.00 153.58 ? 136 GLU B CD 1 ATOM 4088 O OE1 . GLU B 1 137 ? 31.520 19.306 -14.658 1.00 153.78 ? 136 GLU B OE1 1 ATOM 4089 O OE2 . GLU B 1 137 ? 30.867 21.150 -13.655 1.00 153.50 ? 136 GLU B OE2 1 ATOM 4090 N N . ASN B 1 138 ? 24.674 21.291 -14.979 1.00 144.64 ? 137 ASN B N 1 ATOM 4091 C CA . ASN B 1 138 ? 23.374 21.146 -14.331 1.00 141.79 ? 137 ASN B CA 1 ATOM 4092 C C . ASN B 1 138 ? 22.261 21.093 -15.379 1.00 138.16 ? 137 ASN B C 1 ATOM 4093 O O . ASN B 1 138 ? 21.176 21.647 -15.191 1.00 139.06 ? 137 ASN B O 1 ATOM 4094 C CB . ASN B 1 138 ? 23.152 22.277 -13.316 1.00 141.18 ? 137 ASN B CB 1 ATOM 4095 C CG . ASN B 1 138 ? 23.764 21.971 -11.960 1.00 141.27 ? 137 ASN B CG 1 ATOM 4096 O OD1 . ASN B 1 138 ? 23.316 21.062 -11.259 1.00 139.42 ? 137 ASN B OD1 1 ATOM 4097 N ND2 . ASN B 1 138 ? 24.785 22.733 -11.581 1.00 142.36 ? 137 ASN B ND2 1 ATOM 4098 N N . GLY B 1 139 ? 22.539 20.394 -16.478 1.00 133.81 ? 138 GLY B N 1 ATOM 4099 C CA . GLY B 1 139 ? 21.553 20.178 -17.535 1.00 131.80 ? 138 GLY B CA 1 ATOM 4100 C C . GLY B 1 139 ? 20.230 19.626 -17.028 1.00 129.85 ? 138 GLY B C 1 ATOM 4101 O O . GLY B 1 139 ? 19.170 20.147 -17.369 1.00 129.12 ? 138 GLY B O 1 ATOM 4102 N N . PRO B 1 140 ? 20.277 18.566 -16.203 1.00 130.38 ? 139 PRO B N 1 ATOM 4103 C CA . PRO B 1 140 ? 19.051 17.981 -15.655 1.00 129.48 ? 139 PRO B CA 1 ATOM 4104 C C . PRO B 1 140 ? 18.196 18.976 -14.877 1.00 125.08 ? 139 PRO B C 1 ATOM 4105 O O . PRO B 1 140 ? 16.969 18.941 -14.971 1.00 124.59 ? 139 PRO B O 1 ATOM 4106 C CB . PRO B 1 140 ? 19.572 16.890 -14.715 1.00 131.68 ? 139 PRO B CB 1 ATOM 4107 C CG . PRO B 1 140 ? 20.919 16.545 -15.245 1.00 133.63 ? 139 PRO B CG 1 ATOM 4108 C CD . PRO B 1 140 ? 21.477 17.835 -15.760 1.00 133.05 ? 139 PRO B CD 1 ATOM 4109 N N . TYR B 1 141 ? 18.845 19.845 -14.109 1.00 121.67 ? 140 TYR B N 1 ATOM 4110 C CA . TYR B 1 141 ? 18.152 20.903 -13.376 1.00 121.46 ? 140 TYR B CA 1 ATOM 4111 C C . TYR B 1 141 ? 17.283 21.748 -14.310 1.00 122.15 ? 140 TYR B C 1 ATOM 4112 O O . TYR B 1 141 ? 16.113 22.005 -14.018 1.00 121.59 ? 140 TYR B O 1 ATOM 4113 C CB . TYR B 1 141 ? 19.171 21.786 -12.638 1.00 120.69 ? 140 TYR B CB 1 ATOM 4114 C CG . TYR B 1 141 ? 18.632 23.112 -12.144 1.00 118.55 ? 140 TYR B CG 1 ATOM 4115 C CD1 . TYR B 1 141 ? 17.856 23.183 -10.993 1.00 117.96 ? 140 TYR B CD1 1 ATOM 4116 C CD2 . TYR B 1 141 ? 18.911 24.298 -12.823 1.00 118.42 ? 140 TYR B CD2 1 ATOM 4117 C CE1 . TYR B 1 141 ? 17.365 24.395 -10.533 1.00 116.50 ? 140 TYR B CE1 1 ATOM 4118 C CE2 . TYR B 1 141 ? 18.422 25.518 -12.371 1.00 118.12 ? 140 TYR B CE2 1 ATOM 4119 C CZ . TYR B 1 141 ? 17.650 25.563 -11.225 1.00 116.29 ? 140 TYR B CZ 1 ATOM 4120 O OH . TYR B 1 141 ? 17.163 26.772 -10.772 1.00 111.59 ? 140 TYR B OH 1 ATOM 4121 N N . PHE B 1 142 ? 17.856 22.166 -15.433 1.00 124.51 ? 141 PHE B N 1 ATOM 4122 C CA . PHE B 1 142 ? 17.141 23.020 -16.381 1.00 127.47 ? 141 PHE B CA 1 ATOM 4123 C C . PHE B 1 142 ? 15.972 22.305 -17.062 1.00 128.35 ? 141 PHE B C 1 ATOM 4124 O O . PHE B 1 142 ? 14.949 22.924 -17.350 1.00 126.45 ? 141 PHE B O 1 ATOM 4125 C CB . PHE B 1 142 ? 18.104 23.601 -17.424 1.00 129.13 ? 141 PHE B CB 1 ATOM 4126 C CG . PHE B 1 142 ? 19.137 24.536 -16.845 1.00 128.07 ? 141 PHE B CG 1 ATOM 4127 C CD1 . PHE B 1 142 ? 18.749 25.670 -16.139 1.00 126.91 ? 141 PHE B CD1 1 ATOM 4128 C CD2 . PHE B 1 142 ? 20.494 24.289 -17.008 1.00 128.39 ? 141 PHE B CD2 1 ATOM 4129 C CE1 . PHE B 1 142 ? 19.691 26.531 -15.603 1.00 126.59 ? 141 PHE B CE1 1 ATOM 4130 C CE2 . PHE B 1 142 ? 21.440 25.148 -16.474 1.00 128.21 ? 141 PHE B CE2 1 ATOM 4131 C CZ . PHE B 1 142 ? 21.039 26.271 -15.772 1.00 127.30 ? 141 PHE B CZ 1 ATOM 4132 N N . LEU B 1 143 ? 16.120 21.007 -17.316 1.00 131.67 ? 142 LEU B N 1 ATOM 4133 C CA . LEU B 1 143 ? 15.020 20.203 -17.853 1.00 134.77 ? 142 LEU B CA 1 ATOM 4134 C C . LEU B 1 143 ? 13.875 20.153 -16.852 1.00 130.67 ? 142 LEU B C 1 ATOM 4135 O O . LEU B 1 143 ? 12.717 20.364 -17.208 1.00 129.49 ? 142 LEU B O 1 ATOM 4136 C CB . LEU B 1 143 ? 15.486 18.776 -18.162 1.00 140.02 ? 142 LEU B CB 1 ATOM 4137 C CG . LEU B 1 143 ? 16.521 18.630 -19.283 1.00 146.73 ? 142 LEU B CG 1 ATOM 4138 C CD1 . LEU B 1 143 ? 17.107 17.226 -19.294 1.00 148.44 ? 142 LEU B CD1 1 ATOM 4139 C CD2 . LEU B 1 143 ? 15.918 18.976 -20.639 1.00 149.18 ? 142 LEU B CD2 1 ATOM 4140 N N . ALA B 1 144 ? 14.217 19.882 -15.596 1.00 128.18 ? 143 ALA B N 1 ATOM 4141 C CA . ALA B 1 144 ? 13.239 19.833 -14.514 1.00 127.17 ? 143 ALA B CA 1 ATOM 4142 C C . ALA B 1 144 ? 12.566 21.185 -14.306 1.00 125.76 ? 143 ALA B C 1 ATOM 4143 O O . ALA B 1 144 ? 11.366 21.253 -14.049 1.00 126.88 ? 143 ALA B O 1 ATOM 4144 C CB . ALA B 1 144 ? 13.908 19.383 -13.226 1.00 127.04 ? 143 ALA B CB 1 ATOM 4145 N N . LEU B 1 145 ? 13.348 22.256 -14.413 1.00 122.66 ? 144 LEU B N 1 ATOM 4146 C CA . LEU B 1 145 ? 12.828 23.609 -14.271 1.00 118.93 ? 144 LEU B CA 1 ATOM 4147 C C . LEU B 1 145 ? 11.794 23.911 -15.347 1.00 117.72 ? 144 LEU B C 1 ATOM 4148 O O . LEU B 1 145 ? 10.709 24.405 -15.046 1.00 113.71 ? 144 LEU B O 1 ATOM 4149 C CB . LEU B 1 145 ? 13.975 24.621 -14.353 1.00 119.93 ? 144 LEU B CB 1 ATOM 4150 C CG . LEU B 1 145 ? 13.617 26.105 -14.227 1.00 123.02 ? 144 LEU B CG 1 ATOM 4151 C CD1 . LEU B 1 145 ? 12.727 26.344 -13.015 1.00 123.54 ? 144 LEU B CD1 1 ATOM 4152 C CD2 . LEU B 1 145 ? 14.874 26.968 -14.155 1.00 124.94 ? 144 LEU B CD2 1 ATOM 4153 N N . ARG B 1 146 ? 12.136 23.610 -16.597 1.00 120.80 ? 145 ARG B N 1 ATOM 4154 C CA . ARG B 1 146 ? 11.213 23.821 -17.713 1.00 125.50 ? 145 ARG B CA 1 ATOM 4155 C C . ARG B 1 146 ? 9.919 23.045 -17.493 1.00 125.28 ? 145 ARG B C 1 ATOM 4156 O O . ARG B 1 146 ? 8.827 23.585 -17.642 1.00 123.62 ? 145 ARG B O 1 ATOM 4157 C CB . ARG B 1 146 ? 11.830 23.380 -19.045 1.00 131.83 ? 145 ARG B CB 1 ATOM 4158 C CG . ARG B 1 146 ? 11.133 23.985 -20.263 1.00 139.39 ? 145 ARG B CG 1 ATOM 4159 C CD . ARG B 1 146 ? 10.699 22.966 -21.310 1.00 146.69 ? 145 ARG B CD 1 ATOM 4160 N NE . ARG B 1 146 ? 11.790 22.190 -21.917 1.00 154.64 ? 145 ARG B NE 1 ATOM 4161 C CZ . ARG B 1 146 ? 12.133 20.938 -21.588 1.00 164.37 ? 145 ARG B CZ 1 ATOM 4162 N NH1 . ARG B 1 146 ? 11.489 20.252 -20.639 1.00 165.77 ? 145 ARG B NH1 1 ATOM 4163 N NH2 . ARG B 1 146 ? 13.145 20.354 -22.227 1.00 170.15 ? 145 ARG B NH2 1 ATOM 4164 N N . GLU B 1 147 ? 10.049 21.772 -17.139 1.00 128.04 ? 146 GLU B N 1 ATOM 4165 C CA . GLU B 1 147 ? 8.882 20.934 -16.909 1.00 130.96 ? 146 GLU B CA 1 ATOM 4166 C C . GLU B 1 147 ? 8.041 21.417 -15.732 1.00 126.28 ? 146 GLU B C 1 ATOM 4167 O O . GLU B 1 147 ? 6.815 21.383 -15.796 1.00 125.44 ? 146 GLU B O 1 ATOM 4168 C CB . GLU B 1 147 ? 9.289 19.471 -16.711 1.00 136.60 ? 146 GLU B CB 1 ATOM 4169 C CG . GLU B 1 147 ? 9.751 18.787 -17.991 1.00 143.45 ? 146 GLU B CG 1 ATOM 4170 C CD . GLU B 1 147 ? 9.836 17.273 -17.863 1.00 150.44 ? 146 GLU B CD 1 ATOM 4171 O OE1 . GLU B 1 147 ? 10.318 16.779 -16.820 1.00 154.12 ? 146 GLU B OE1 1 ATOM 4172 O OE2 . GLU B 1 147 ? 9.420 16.573 -18.811 1.00 153.21 ? 146 GLU B OE2 1 ATOM 4173 N N . MET B 1 148 ? 8.696 21.858 -14.661 1.00 123.35 ? 147 MET B N 1 ATOM 4174 C CA . MET B 1 148 ? 7.986 22.355 -13.481 1.00 123.40 ? 147 MET B CA 1 ATOM 4175 C C . MET B 1 148 ? 7.192 23.614 -13.811 1.00 122.73 ? 147 MET B C 1 ATOM 4176 O O . MET B 1 148 ? 6.050 23.763 -13.379 1.00 120.19 ? 147 MET B O 1 ATOM 4177 C CB . MET B 1 148 ? 8.962 22.641 -12.337 1.00 122.51 ? 147 MET B CB 1 ATOM 4178 C CG . MET B 1 148 ? 8.272 23.015 -11.033 1.00 121.92 ? 147 MET B CG 1 ATOM 4179 S SD . MET B 1 148 ? 9.379 23.051 -9.613 1.00 121.16 ? 147 MET B SD 1 ATOM 4180 C CE . MET B 1 148 ? 10.305 24.554 -9.926 1.00 121.56 ? 147 MET B CE 1 ATOM 4181 N N . ILE B 1 149 ? 7.800 24.514 -14.577 1.00 124.69 ? 148 ILE B N 1 ATOM 4182 C CA . ILE B 1 149 ? 7.126 25.742 -14.998 1.00 127.28 ? 148 ILE B CA 1 ATOM 4183 C C . ILE B 1 149 ? 5.889 25.419 -15.835 1.00 126.21 ? 148 ILE B C 1 ATOM 4184 O O . ILE B 1 149 ? 4.823 25.996 -15.617 1.00 123.29 ? 148 ILE B O 1 ATOM 4185 C CB . ILE B 1 149 ? 8.080 26.674 -15.784 1.00 130.45 ? 148 ILE B CB 1 ATOM 4186 C CG1 . ILE B 1 149 ? 9.146 27.248 -14.840 1.00 131.10 ? 148 ILE B CG1 1 ATOM 4187 C CG2 . ILE B 1 149 ? 7.313 27.819 -16.442 1.00 130.77 ? 148 ILE B CG2 1 ATOM 4188 C CD1 . ILE B 1 149 ? 10.381 27.761 -15.550 1.00 132.38 ? 148 ILE B CD1 1 ATOM 4189 N N . GLU B 1 150 ? 6.031 24.498 -16.784 1.00 126.76 ? 149 GLU B N 1 ATOM 4190 C CA . GLU B 1 150 ? 4.902 24.077 -17.610 1.00 128.53 ? 149 GLU B CA 1 ATOM 4191 C C . GLU B 1 150 ? 3.775 23.467 -16.765 1.00 129.89 ? 149 GLU B C 1 ATOM 4192 O O . GLU B 1 150 ? 2.601 23.755 -16.996 1.00 131.06 ? 149 GLU B O 1 ATOM 4193 C CB . GLU B 1 150 ? 5.359 23.095 -18.692 1.00 129.22 ? 149 GLU B CB 1 ATOM 4194 C CG . GLU B 1 150 ? 6.214 23.735 -19.776 1.00 130.63 ? 149 GLU B CG 1 ATOM 4195 C CD . GLU B 1 150 ? 6.769 22.734 -20.774 1.00 134.14 ? 149 GLU B CD 1 ATOM 4196 O OE1 . GLU B 1 150 ? 6.393 21.543 -20.719 1.00 139.82 ? 149 GLU B OE1 1 ATOM 4197 O OE2 . GLU B 1 150 ? 7.589 23.139 -21.624 1.00 134.12 ? 149 GLU B OE2 1 ATOM 4198 N N . GLU B 1 151 ? 4.136 22.644 -15.782 1.00 130.29 ? 150 GLU B N 1 ATOM 4199 C CA . GLU B 1 151 ? 3.151 22.032 -14.881 1.00 132.51 ? 150 GLU B CA 1 ATOM 4200 C C . GLU B 1 151 ? 2.401 23.095 -14.080 1.00 130.35 ? 150 GLU B C 1 ATOM 4201 O O . GLU B 1 151 ? 1.178 23.037 -13.950 1.00 129.28 ? 150 GLU B O 1 ATOM 4202 C CB . GLU B 1 151 ? 3.831 21.050 -13.915 1.00 137.05 ? 150 GLU B CB 1 ATOM 4203 C CG . GLU B 1 151 ? 2.862 20.138 -13.167 1.00 141.33 ? 150 GLU B CG 1 ATOM 4204 C CD . GLU B 1 151 ? 3.491 19.416 -11.985 1.00 143.52 ? 150 GLU B CD 1 ATOM 4205 O OE1 . GLU B 1 151 ? 2.741 19.039 -11.057 1.00 144.04 ? 150 GLU B OE1 1 ATOM 4206 O OE2 . GLU B 1 151 ? 4.726 19.218 -11.981 1.00 145.70 ? 150 GLU B OE2 1 ATOM 4207 N N . MET B 1 152 ? 3.139 24.057 -13.537 1.00 128.81 ? 151 MET B N 1 ATOM 4208 C CA . MET B 1 152 ? 2.532 25.108 -12.726 1.00 129.20 ? 151 MET B CA 1 ATOM 4209 C C . MET B 1 152 ? 1.595 25.978 -13.566 1.00 128.86 ? 151 MET B C 1 ATOM 4210 O O . MET B 1 152 ? 0.530 26.384 -13.098 1.00 127.67 ? 151 MET B O 1 ATOM 4211 C CB . MET B 1 152 ? 3.613 25.959 -12.043 1.00 129.24 ? 151 MET B CB 1 ATOM 4212 C CG . MET B 1 152 ? 4.402 25.204 -10.976 1.00 127.26 ? 151 MET B CG 1 ATOM 4213 S SD . MET B 1 152 ? 5.850 26.082 -10.345 1.00 123.76 ? 151 MET B SD 1 ATOM 4214 C CE . MET B 1 152 ? 5.092 27.144 -9.119 1.00 122.70 ? 151 MET B CE 1 ATOM 4215 N N . TYR B 1 153 ? 1.985 26.253 -14.808 1.00 128.82 ? 152 TYR B N 1 ATOM 4216 C CA . TYR B 1 153 ? 1.129 26.998 -15.737 1.00 131.93 ? 152 TYR B CA 1 ATOM 4217 C C . TYR B 1 153 ? -0.201 26.281 -15.951 1.00 133.42 ? 152 TYR B C 1 ATOM 4218 O O . TYR B 1 153 ? -1.259 26.903 -15.935 1.00 135.64 ? 152 TYR B O 1 ATOM 4219 C CB . TYR B 1 153 ? 1.831 27.198 -17.088 1.00 133.65 ? 152 TYR B CB 1 ATOM 4220 C CG . TYR B 1 153 ? 0.964 27.834 -18.164 1.00 136.80 ? 152 TYR B CG 1 ATOM 4221 C CD1 . TYR B 1 153 ? 0.137 27.056 -18.978 1.00 138.25 ? 152 TYR B CD1 1 ATOM 4222 C CD2 . TYR B 1 153 ? 0.981 29.209 -18.377 1.00 139.24 ? 152 TYR B CD2 1 ATOM 4223 C CE1 . TYR B 1 153 ? -0.652 27.631 -19.960 1.00 140.42 ? 152 TYR B CE1 1 ATOM 4224 C CE2 . TYR B 1 153 ? 0.198 29.793 -19.359 1.00 141.69 ? 152 TYR B CE2 1 ATOM 4225 C CZ . TYR B 1 153 ? -0.617 28.999 -20.146 1.00 142.86 ? 152 TYR B CZ 1 ATOM 4226 O OH . TYR B 1 153 ? -1.396 29.574 -21.124 1.00 147.94 ? 152 TYR B OH 1 ATOM 4227 N N . GLN B 1 154 ? -0.136 24.971 -16.167 1.00 132.62 ? 153 GLN B N 1 ATOM 4228 C CA . GLN B 1 154 ? -1.335 24.172 -16.415 1.00 131.95 ? 153 GLN B CA 1 ATOM 4229 C C . GLN B 1 154 ? -2.206 24.040 -15.174 1.00 129.08 ? 153 GLN B C 1 ATOM 4230 O O . GLN B 1 154 ? -3.425 24.175 -15.255 1.00 126.46 ? 153 GLN B O 1 ATOM 4231 C CB . GLN B 1 154 ? -0.949 22.789 -16.936 1.00 133.65 ? 153 GLN B CB 1 ATOM 4232 C CG . GLN B 1 154 ? -0.403 22.823 -18.356 1.00 135.18 ? 153 GLN B CG 1 ATOM 4233 C CD . GLN B 1 154 ? -0.171 21.436 -18.920 1.00 136.34 ? 153 GLN B CD 1 ATOM 4234 O OE1 . GLN B 1 154 ? 0.073 20.488 -18.176 1.00 135.39 ? 153 GLN B OE1 1 ATOM 4235 N NE2 . GLN B 1 154 ? -0.253 21.309 -20.240 1.00 139.43 ? 153 GLN B NE2 1 ATOM 4236 N N . LEU B 1 155 ? -1.572 23.773 -14.033 1.00 127.78 ? 154 LEU B N 1 ATOM 4237 C CA . LEU B 1 155 ? -2.291 23.602 -12.765 1.00 127.58 ? 154 LEU B CA 1 ATOM 4238 C C . LEU B 1 155 ? -2.986 24.886 -12.312 1.00 128.36 ? 154 LEU B C 1 ATOM 4239 O O . LEU B 1 155 ? -4.167 24.863 -11.960 1.00 130.31 ? 154 LEU B O 1 ATOM 4240 C CB . LEU B 1 155 ? -1.355 23.089 -11.648 1.00 123.92 ? 154 LEU B CB 1 ATOM 4241 C CG . LEU B 1 155 ? -1.443 21.596 -11.285 1.00 121.64 ? 154 LEU B CG 1 ATOM 4242 C CD1 . LEU B 1 155 ? -0.195 21.110 -10.561 1.00 118.45 ? 154 LEU B CD1 1 ATOM 4243 C CD2 . LEU B 1 155 ? -2.676 21.328 -10.439 1.00 120.89 ? 154 LEU B CD2 1 ATOM 4244 N N . TYR B 1 156 ? -2.255 25.999 -12.332 1.00 127.30 ? 155 TYR B N 1 ATOM 4245 C CA . TYR B 1 156 ? -2.737 27.245 -11.734 1.00 126.40 ? 155 TYR B CA 1 ATOM 4246 C C . TYR B 1 156 ? -3.255 28.264 -12.740 1.00 128.04 ? 155 TYR B C 1 ATOM 4247 O O . TYR B 1 156 ? -3.688 29.348 -12.359 1.00 125.66 ? 155 TYR B O 1 ATOM 4248 C CB . TYR B 1 156 ? -1.656 27.825 -10.823 1.00 123.32 ? 155 TYR B CB 1 ATOM 4249 C CG . TYR B 1 156 ? -1.101 26.750 -9.921 1.00 121.72 ? 155 TYR B CG 1 ATOM 4250 C CD1 . TYR B 1 156 ? -1.942 26.059 -9.052 1.00 123.27 ? 155 TYR B CD1 1 ATOM 4251 C CD2 . TYR B 1 156 ? 0.237 26.381 -9.971 1.00 119.64 ? 155 TYR B CD2 1 ATOM 4252 C CE1 . TYR B 1 156 ? -1.463 25.049 -8.240 1.00 122.91 ? 155 TYR B CE1 1 ATOM 4253 C CE2 . TYR B 1 156 ? 0.727 25.371 -9.161 1.00 120.15 ? 155 TYR B CE2 1 ATOM 4254 C CZ . TYR B 1 156 ? -0.128 24.709 -8.296 1.00 121.17 ? 155 TYR B CZ 1 ATOM 4255 O OH . TYR B 1 156 ? 0.334 23.700 -7.486 1.00 118.41 ? 155 TYR B OH 1 ATOM 4256 N N . GLY B 1 157 ? -3.216 27.906 -14.022 1.00 131.47 ? 156 GLY B N 1 ATOM 4257 C CA . GLY B 1 157 ? -3.923 28.650 -15.063 1.00 133.45 ? 156 GLY B CA 1 ATOM 4258 C C . GLY B 1 157 ? -3.273 29.931 -15.547 1.00 133.17 ? 156 GLY B C 1 ATOM 4259 O O . GLY B 1 157 ? -3.943 30.772 -16.146 1.00 136.34 ? 156 GLY B O 1 ATOM 4260 N N . GLY B 1 158 ? -1.973 30.085 -15.310 1.00 131.90 ? 157 GLY B N 1 ATOM 4261 C CA . GLY B 1 158 ? -1.288 31.314 -15.686 1.00 133.22 ? 157 GLY B CA 1 ATOM 4262 C C . GLY B 1 158 ? 0.224 31.214 -15.654 1.00 131.55 ? 157 GLY B C 1 ATOM 4263 O O . GLY B 1 158 ? 0.776 30.302 -15.033 1.00 130.00 ? 157 GLY B O 1 ATOM 4264 N N . PRO B 1 159 ? 0.905 32.161 -16.326 1.00 130.16 ? 158 PRO B N 1 ATOM 4265 C CA . PRO B 1 159 ? 2.367 32.193 -16.388 1.00 127.63 ? 158 PRO B CA 1 ATOM 4266 C C . PRO B 1 159 ? 3.015 32.486 -15.037 1.00 125.93 ? 158 PRO B C 1 ATOM 4267 O O . PRO B 1 159 ? 2.380 33.084 -14.158 1.00 124.69 ? 158 PRO B O 1 ATOM 4268 C CB . PRO B 1 159 ? 2.657 33.311 -17.390 1.00 128.34 ? 158 PRO B CB 1 ATOM 4269 C CG . PRO B 1 159 ? 1.454 34.185 -17.356 1.00 130.83 ? 158 PRO B CG 1 ATOM 4270 C CD . PRO B 1 159 ? 0.293 33.294 -17.045 1.00 130.93 ? 158 PRO B CD 1 ATOM 4271 N N . VAL B 1 160 ? 4.270 32.061 -14.891 1.00 124.75 ? 159 VAL B N 1 ATOM 4272 C CA . VAL B 1 160 ? 4.972 32.100 -13.605 1.00 124.38 ? 159 VAL B CA 1 ATOM 4273 C C . VAL B 1 160 ? 5.851 33.337 -13.438 1.00 123.76 ? 159 VAL B C 1 ATOM 4274 O O . VAL B 1 160 ? 6.357 33.905 -14.413 1.00 121.18 ? 159 VAL B O 1 ATOM 4275 C CB . VAL B 1 160 ? 5.854 30.846 -13.373 1.00 125.58 ? 159 VAL B CB 1 ATOM 4276 C CG1 . VAL B 1 160 ? 5.064 29.565 -13.611 1.00 127.07 ? 159 VAL B CG1 1 ATOM 4277 C CG2 . VAL B 1 160 ? 7.112 30.878 -14.238 1.00 127.04 ? 159 VAL B CG2 1 ATOM 4278 N N . VAL B 1 161 ? 6.029 33.736 -12.184 1.00 124.08 ? 160 VAL B N 1 ATOM 4279 C CA . VAL B 1 161 ? 6.976 34.778 -11.836 1.00 124.55 ? 160 VAL B CA 1 ATOM 4280 C C . VAL B 1 161 ? 8.199 34.096 -11.246 1.00 123.51 ? 160 VAL B C 1 ATOM 4281 O O . VAL B 1 161 ? 8.081 33.339 -10.279 1.00 121.15 ? 160 VAL B O 1 ATOM 4282 C CB . VAL B 1 161 ? 6.399 35.746 -10.788 1.00 126.44 ? 160 VAL B CB 1 ATOM 4283 C CG1 . VAL B 1 161 ? 7.383 36.878 -10.513 1.00 127.54 ? 160 VAL B CG1 1 ATOM 4284 C CG2 . VAL B 1 161 ? 5.058 36.289 -11.260 1.00 128.03 ? 160 VAL B CG2 1 ATOM 4285 N N . LEU B 1 162 ? 9.360 34.352 -11.844 1.00 122.85 ? 161 LEU B N 1 ATOM 4286 C CA . LEU B 1 162 ? 10.631 33.874 -11.309 1.00 121.70 ? 161 LEU B CA 1 ATOM 4287 C C . LEU B 1 162 ? 11.185 34.919 -10.358 1.00 120.81 ? 161 LEU B C 1 ATOM 4288 O O . LEU B 1 162 ? 11.220 36.101 -10.686 1.00 119.75 ? 161 LEU B O 1 ATOM 4289 C CB . LEU B 1 162 ? 11.637 33.642 -12.434 1.00 122.00 ? 161 LEU B CB 1 ATOM 4290 C CG . LEU B 1 162 ? 11.204 32.684 -13.540 1.00 123.10 ? 161 LEU B CG 1 ATOM 4291 C CD1 . LEU B 1 162 ? 12.319 32.532 -14.562 1.00 124.49 ? 161 LEU B CD1 1 ATOM 4292 C CD2 . LEU B 1 162 ? 10.823 31.332 -12.959 1.00 123.42 ? 161 LEU B CD2 1 ATOM 4293 N N . VAL B 1 163 ? 11.606 34.480 -9.180 1.00 120.63 ? 162 VAL B N 1 ATOM 4294 C CA . VAL B 1 163 ? 12.257 35.358 -8.219 1.00 123.05 ? 162 VAL B CA 1 ATOM 4295 C C . VAL B 1 163 ? 13.600 34.720 -7.909 1.00 126.94 ? 162 VAL B C 1 ATOM 4296 O O . VAL B 1 163 ? 13.645 33.619 -7.362 1.00 127.80 ? 162 VAL B O 1 ATOM 4297 C CB . VAL B 1 163 ? 11.426 35.484 -6.928 1.00 121.40 ? 162 VAL B CB 1 ATOM 4298 C CG1 . VAL B 1 163 ? 12.039 36.521 -5.997 1.00 120.78 ? 162 VAL B CG1 1 ATOM 4299 C CG2 . VAL B 1 163 ? 9.983 35.836 -7.266 1.00 121.49 ? 162 VAL B CG2 1 ATOM 4300 N N . ALA B 1 164 ? 14.687 35.395 -8.280 1.00 130.02 ? 163 ALA B N 1 ATOM 4301 C CA . ALA B 1 164 ? 16.034 34.837 -8.135 1.00 131.35 ? 163 ALA B CA 1 ATOM 4302 C C . ALA B 1 164 ? 16.931 35.754 -7.313 1.00 131.29 ? 163 ALA B C 1 ATOM 4303 O O . ALA B 1 164 ? 16.790 36.975 -7.349 1.00 128.85 ? 163 ALA B O 1 ATOM 4304 C CB . ALA B 1 164 ? 16.650 34.589 -9.505 1.00 132.25 ? 163 ALA B CB 1 ATOM 4305 N N . HIS B 1 165 ? 17.860 35.150 -6.580 1.00 133.26 ? 164 HIS B N 1 ATOM 4306 C CA . HIS B 1 165 ? 18.773 35.889 -5.725 1.00 136.44 ? 164 HIS B CA 1 ATOM 4307 C C . HIS B 1 165 ? 20.217 35.582 -6.102 1.00 138.07 ? 164 HIS B C 1 ATOM 4308 O O . HIS B 1 165 ? 20.566 34.429 -6.352 1.00 136.08 ? 164 HIS B O 1 ATOM 4309 C CB . HIS B 1 165 ? 18.529 35.526 -4.263 1.00 137.94 ? 164 HIS B CB 1 ATOM 4310 C CG . HIS B 1 165 ? 19.468 36.199 -3.314 1.00 140.53 ? 164 HIS B CG 1 ATOM 4311 N ND1 . HIS B 1 165 ? 20.485 35.526 -2.673 1.00 141.99 ? 164 HIS B ND1 1 ATOM 4312 C CD2 . HIS B 1 165 ? 19.556 37.489 -2.915 1.00 142.13 ? 164 HIS B CD2 1 ATOM 4313 C CE1 . HIS B 1 165 ? 21.151 36.371 -1.907 1.00 144.57 ? 164 HIS B CE1 1 ATOM 4314 N NE2 . HIS B 1 165 ? 20.609 37.569 -2.037 1.00 144.76 ? 164 HIS B NE2 1 ATOM 4315 N N . SER B 1 166 ? 21.045 36.623 -6.136 1.00 141.89 ? 165 SER B N 1 ATOM 4316 C CA . SER B 1 166 ? 22.478 36.490 -6.391 1.00 146.68 ? 165 SER B CA 1 ATOM 4317 C C . SER B 1 166 ? 22.754 35.635 -7.639 1.00 141.60 ? 165 SER B C 1 ATOM 4318 O O . SER B 1 166 ? 22.181 35.890 -8.700 1.00 137.85 ? 165 SER B O 1 ATOM 4319 C CB . SER B 1 166 ? 23.190 35.948 -5.139 1.00 154.56 ? 165 SER B CB 1 ATOM 4320 O OG . SER B 1 166 ? 24.606 36.011 -5.281 1.00 169.48 ? 165 SER B OG 1 ATOM 4321 N N . MET B 1 167 ? 23.603 34.617 -7.509 1.00 139.91 ? 166 MET B N 1 ATOM 4322 C CA . MET B 1 167 ? 23.974 33.754 -8.629 1.00 141.59 ? 166 MET B CA 1 ATOM 4323 C C . MET B 1 167 ? 22.776 33.086 -9.304 1.00 139.57 ? 166 MET B C 1 ATOM 4324 O O . MET B 1 167 ? 22.852 32.739 -10.484 1.00 137.39 ? 166 MET B O 1 ATOM 4325 C CB . MET B 1 167 ? 24.958 32.677 -8.159 1.00 143.59 ? 166 MET B CB 1 ATOM 4326 C CG . MET B 1 167 ? 25.607 31.879 -9.281 1.00 145.46 ? 166 MET B CG 1 ATOM 4327 S SD . MET B 1 167 ? 26.856 30.729 -8.673 1.00 148.22 ? 166 MET B SD 1 ATOM 4328 C CE . MET B 1 167 ? 25.824 29.549 -7.800 1.00 147.02 ? 166 MET B CE 1 ATOM 4329 N N . GLY B 1 168 ? 21.676 32.909 -8.568 1.00 137.16 ? 167 GLY B N 1 ATOM 4330 C CA . GLY B 1 168 ? 20.442 32.378 -9.144 1.00 134.68 ? 167 GLY B CA 1 ATOM 4331 C C . GLY B 1 168 ? 20.021 33.141 -10.391 1.00 134.92 ? 167 GLY B C 1 ATOM 4332 O O . GLY B 1 168 ? 19.448 32.570 -11.318 1.00 136.00 ? 167 GLY B O 1 ATOM 4333 N N . ASN B 1 169 ? 20.313 34.438 -10.417 1.00 133.19 ? 168 ASN B N 1 ATOM 4334 C CA . ASN B 1 169 ? 19.976 35.268 -11.564 1.00 132.98 ? 168 ASN B CA 1 ATOM 4335 C C . ASN B 1 169 ? 20.763 34.902 -12.814 1.00 135.56 ? 168 ASN B C 1 ATOM 4336 O O . ASN B 1 169 ? 20.218 34.905 -13.917 1.00 134.41 ? 168 ASN B O 1 ATOM 4337 C CB . ASN B 1 169 ? 20.194 36.742 -11.227 1.00 131.92 ? 168 ASN B CB 1 ATOM 4338 C CG . ASN B 1 169 ? 19.243 37.236 -10.157 1.00 129.90 ? 168 ASN B CG 1 ATOM 4339 O OD1 . ASN B 1 169 ? 18.076 37.498 -10.433 1.00 127.71 ? 168 ASN B OD1 1 ATOM 4340 N ND2 . ASN B 1 169 ? 19.734 37.360 -8.928 1.00 129.21 ? 168 ASN B ND2 1 ATOM 4341 N N . MET B 1 170 ? 22.044 34.591 -12.634 1.00 139.45 ? 169 MET B N 1 ATOM 4342 C CA . MET B 1 170 ? 22.910 34.183 -13.742 1.00 144.94 ? 169 MET B CA 1 ATOM 4343 C C . MET B 1 170 ? 22.494 32.820 -14.286 1.00 138.17 ? 169 MET B C 1 ATOM 4344 O O . MET B 1 170 ? 22.459 32.612 -15.500 1.00 135.17 ? 169 MET B O 1 ATOM 4345 C CB . MET B 1 170 ? 24.375 34.119 -13.289 1.00 158.13 ? 169 MET B CB 1 ATOM 4346 C CG . MET B 1 170 ? 25.025 35.478 -13.052 1.00 173.25 ? 169 MET B CG 1 ATOM 4347 S SD . MET B 1 170 ? 25.977 36.122 -14.455 1.00 198.15 ? 169 MET B SD 1 ATOM 4348 C CE . MET B 1 170 ? 27.632 35.527 -14.094 1.00 200.05 ? 169 MET B CE 1 ATOM 4349 N N . TYR B 1 171 ? 22.194 31.898 -13.375 1.00 134.82 ? 170 TYR B N 1 ATOM 4350 C CA . TYR B 1 171 ? 21.649 30.588 -13.741 1.00 133.92 ? 170 TYR B CA 1 ATOM 4351 C C . TYR B 1 171 ? 20.362 30.731 -14.548 1.00 131.72 ? 170 TYR B C 1 ATOM 4352 O O . TYR B 1 171 ? 20.207 30.113 -15.606 1.00 131.83 ? 170 TYR B O 1 ATOM 4353 C CB . TYR B 1 171 ? 21.378 29.731 -12.493 1.00 133.51 ? 170 TYR B CB 1 ATOM 4354 C CG . TYR B 1 171 ? 22.400 28.638 -12.268 1.00 133.19 ? 170 TYR B CG 1 ATOM 4355 C CD1 . TYR B 1 171 ? 23.632 28.916 -11.683 1.00 133.50 ? 170 TYR B CD1 1 ATOM 4356 C CD2 . TYR B 1 171 ? 22.134 27.325 -12.644 1.00 132.39 ? 170 TYR B CD2 1 ATOM 4357 C CE1 . TYR B 1 171 ? 24.571 27.916 -11.479 1.00 132.27 ? 170 TYR B CE1 1 ATOM 4358 C CE2 . TYR B 1 171 ? 23.065 26.319 -12.444 1.00 132.19 ? 170 TYR B CE2 1 ATOM 4359 C CZ . TYR B 1 171 ? 24.281 26.621 -11.862 1.00 131.52 ? 170 TYR B CZ 1 ATOM 4360 O OH . TYR B 1 171 ? 25.206 25.624 -11.661 1.00 131.01 ? 170 TYR B OH 1 ATOM 4361 N N . THR B 1 172 ? 19.442 31.547 -14.045 1.00 127.66 ? 171 THR B N 1 ATOM 4362 C CA . THR B 1 172 ? 18.153 31.701 -14.704 1.00 123.71 ? 171 THR B CA 1 ATOM 4363 C C . THR B 1 172 ? 18.274 32.491 -16.017 1.00 124.16 ? 171 THR B C 1 ATOM 4364 O O . THR B 1 172 ? 17.573 32.180 -16.968 1.00 123.45 ? 171 THR B O 1 ATOM 4365 C CB . THR B 1 172 ? 17.039 32.172 -13.731 1.00 120.61 ? 171 THR B CB 1 ATOM 4366 O OG1 . THR B 1 172 ? 16.463 31.023 -13.085 1.00 113.24 ? 171 THR B OG1 1 ATOM 4367 C CG2 . THR B 1 172 ? 15.925 32.916 -14.451 1.00 121.92 ? 171 THR B CG2 1 ATOM 4368 N N . LEU B 1 173 ? 19.179 33.467 -16.098 1.00 123.77 ? 172 LEU B N 1 ATOM 4369 C CA . LEU B 1 173 ? 19.447 34.155 -17.371 1.00 124.75 ? 172 LEU B CA 1 ATOM 4370 C C . LEU B 1 173 ? 19.955 33.183 -18.436 1.00 124.14 ? 172 LEU B C 1 ATOM 4371 O O . LEU B 1 173 ? 19.500 33.200 -19.579 1.00 123.57 ? 172 LEU B O 1 ATOM 4372 C CB . LEU B 1 173 ? 20.475 35.272 -17.185 1.00 128.00 ? 172 LEU B CB 1 ATOM 4373 C CG . LEU B 1 173 ? 20.983 35.916 -18.484 1.00 132.30 ? 172 LEU B CG 1 ATOM 4374 C CD1 . LEU B 1 173 ? 19.843 36.536 -19.280 1.00 133.03 ? 172 LEU B CD1 1 ATOM 4375 C CD2 . LEU B 1 173 ? 22.047 36.958 -18.186 1.00 134.66 ? 172 LEU B CD2 1 ATOM 4376 N N . TYR B 1 174 ? 20.916 32.348 -18.061 1.00 123.00 ? 173 TYR B N 1 ATOM 4377 C CA . TYR B 1 174 ? 21.404 31.288 -18.947 1.00 122.81 ? 173 TYR B CA 1 ATOM 4378 C C . TYR B 1 174 ? 20.229 30.454 -19.456 1.00 119.28 ? 173 TYR B C 1 ATOM 4379 O O . TYR B 1 174 ? 20.098 30.219 -20.652 1.00 116.65 ? 173 TYR B O 1 ATOM 4380 C CB . TYR B 1 174 ? 22.398 30.407 -18.184 1.00 123.38 ? 173 TYR B CB 1 ATOM 4381 C CG . TYR B 1 174 ? 22.826 29.125 -18.868 1.00 122.97 ? 173 TYR B CG 1 ATOM 4382 C CD1 . TYR B 1 174 ? 23.908 29.107 -19.746 1.00 124.37 ? 173 TYR B CD1 1 ATOM 4383 C CD2 . TYR B 1 174 ? 22.179 27.922 -18.598 1.00 122.43 ? 173 TYR B CD2 1 ATOM 4384 C CE1 . TYR B 1 174 ? 24.317 27.931 -20.354 1.00 126.15 ? 173 TYR B CE1 1 ATOM 4385 C CE2 . TYR B 1 174 ? 22.580 26.741 -19.201 1.00 124.37 ? 173 TYR B CE2 1 ATOM 4386 C CZ . TYR B 1 174 ? 23.650 26.749 -20.075 1.00 126.48 ? 173 TYR B CZ 1 ATOM 4387 O OH . TYR B 1 174 ? 24.048 25.574 -20.675 1.00 128.13 ? 173 TYR B OH 1 ATOM 4388 N N . PHE B 1 175 ? 19.378 30.023 -18.531 1.00 116.99 ? 174 PHE B N 1 ATOM 4389 C CA . PHE B 1 175 ? 18.185 29.248 -18.859 1.00 117.90 ? 174 PHE B CA 1 ATOM 4390 C C . PHE B 1 175 ? 17.300 29.965 -19.874 1.00 117.39 ? 174 PHE B C 1 ATOM 4391 O O . PHE B 1 175 ? 16.961 29.407 -20.914 1.00 116.12 ? 174 PHE B O 1 ATOM 4392 C CB . PHE B 1 175 ? 17.394 28.960 -17.577 1.00 118.75 ? 174 PHE B CB 1 ATOM 4393 C CG . PHE B 1 175 ? 16.017 28.403 -17.815 1.00 120.72 ? 174 PHE B CG 1 ATOM 4394 C CD1 . PHE B 1 175 ? 15.849 27.132 -18.351 1.00 120.96 ? 174 PHE B CD1 1 ATOM 4395 C CD2 . PHE B 1 175 ? 14.888 29.140 -17.482 1.00 121.23 ? 174 PHE B CD2 1 ATOM 4396 C CE1 . PHE B 1 175 ? 14.581 26.611 -18.562 1.00 120.80 ? 174 PHE B CE1 1 ATOM 4397 C CE2 . PHE B 1 175 ? 13.618 28.623 -17.691 1.00 121.26 ? 174 PHE B CE2 1 ATOM 4398 C CZ . PHE B 1 175 ? 13.464 27.357 -18.231 1.00 120.25 ? 174 PHE B CZ 1 ATOM 4399 N N . LEU B 1 176 ? 16.939 31.204 -19.561 1.00 118.99 ? 175 LEU B N 1 ATOM 4400 C CA . LEU B 1 176 ? 16.049 32.009 -20.404 1.00 122.96 ? 175 LEU B CA 1 ATOM 4401 C C . LEU B 1 176 ? 16.621 32.287 -21.787 1.00 128.54 ? 175 LEU B C 1 ATOM 4402 O O . LEU B 1 176 ? 15.894 32.263 -22.780 1.00 130.50 ? 175 LEU B O 1 ATOM 4403 C CB . LEU B 1 176 ? 15.743 33.353 -19.735 1.00 121.72 ? 175 LEU B CB 1 ATOM 4404 C CG . LEU B 1 176 ? 14.822 33.326 -18.516 1.00 119.35 ? 175 LEU B CG 1 ATOM 4405 C CD1 . LEU B 1 176 ? 14.897 34.652 -17.772 1.00 118.71 ? 175 LEU B CD1 1 ATOM 4406 C CD2 . LEU B 1 176 ? 13.389 33.011 -18.924 1.00 118.38 ? 175 LEU B CD2 1 ATOM 4407 N N . GLN B 1 177 ? 17.918 32.572 -21.848 1.00 133.18 ? 176 GLN B N 1 ATOM 4408 C CA . GLN B 1 177 ? 18.590 32.796 -23.126 1.00 138.53 ? 176 GLN B CA 1 ATOM 4409 C C . GLN B 1 177 ? 18.474 31.594 -24.062 1.00 140.97 ? 176 GLN B C 1 ATOM 4410 O O . GLN B 1 177 ? 18.489 31.752 -25.281 1.00 143.16 ? 176 GLN B O 1 ATOM 4411 C CB . GLN B 1 177 ? 20.065 33.123 -22.906 1.00 140.96 ? 176 GLN B CB 1 ATOM 4412 C CG . GLN B 1 177 ? 20.311 34.542 -22.432 1.00 143.01 ? 176 GLN B CG 1 ATOM 4413 C CD . GLN B 1 177 ? 21.785 34.886 -22.365 1.00 147.29 ? 176 GLN B CD 1 ATOM 4414 O OE1 . GLN B 1 177 ? 22.643 34.003 -22.404 1.00 150.28 ? 176 GLN B OE1 1 ATOM 4415 N NE2 . GLN B 1 177 ? 22.089 36.177 -22.275 1.00 150.37 ? 176 GLN B NE2 1 ATOM 4416 N N . ARG B 1 178 ? 18.356 30.401 -23.484 1.00 142.15 ? 177 ARG B N 1 ATOM 4417 C CA . ARG B 1 178 ? 18.292 29.161 -24.250 1.00 147.13 ? 177 ARG B CA 1 ATOM 4418 C C . ARG B 1 178 ? 16.874 28.689 -24.601 1.00 146.15 ? 177 ARG B C 1 ATOM 4419 O O . ARG B 1 178 ? 16.720 27.702 -25.321 1.00 150.02 ? 177 ARG B O 1 ATOM 4420 C CB . ARG B 1 178 ? 19.030 28.058 -23.493 1.00 149.70 ? 177 ARG B CB 1 ATOM 4421 C CG . ARG B 1 178 ? 20.487 28.394 -23.219 1.00 154.07 ? 177 ARG B CG 1 ATOM 4422 C CD . ARG B 1 178 ? 21.113 27.421 -22.238 1.00 157.96 ? 177 ARG B CD 1 ATOM 4423 N NE . ARG B 1 178 ? 21.575 26.202 -22.901 1.00 162.66 ? 177 ARG B NE 1 ATOM 4424 C CZ . ARG B 1 178 ? 22.720 26.085 -23.577 1.00 168.10 ? 177 ARG B CZ 1 ATOM 4425 N NH1 . ARG B 1 178 ? 23.552 27.118 -23.700 1.00 171.97 ? 177 ARG B NH1 1 ATOM 4426 N NH2 . ARG B 1 178 ? 23.037 24.923 -24.141 1.00 170.10 ? 177 ARG B NH2 1 ATOM 4427 N N . GLN B 1 179 ? 15.845 29.379 -24.112 1.00 141.08 ? 178 GLN B N 1 ATOM 4428 C CA . GLN B 1 179 ? 14.467 29.026 -24.448 1.00 138.07 ? 178 GLN B CA 1 ATOM 4429 C C . GLN B 1 179 ? 13.982 29.891 -25.601 1.00 135.98 ? 178 GLN B C 1 ATOM 4430 O O . GLN B 1 179 ? 14.312 31.072 -25.664 1.00 135.93 ? 178 GLN B O 1 ATOM 4431 C CB . GLN B 1 179 ? 13.547 29.229 -23.242 1.00 136.54 ? 178 GLN B CB 1 ATOM 4432 C CG . GLN B 1 179 ? 13.967 28.464 -21.999 1.00 136.35 ? 178 GLN B CG 1 ATOM 4433 C CD . GLN B 1 179 ? 14.228 26.997 -22.278 1.00 138.19 ? 178 GLN B CD 1 ATOM 4434 O OE1 . GLN B 1 179 ? 13.392 26.307 -22.865 1.00 139.77 ? 178 GLN B OE1 1 ATOM 4435 N NE2 . GLN B 1 179 ? 15.399 26.514 -21.869 1.00 139.03 ? 178 GLN B NE2 1 ATOM 4436 N N . PRO B 1 180 ? 13.192 29.309 -26.518 1.00 134.58 ? 179 PRO B N 1 ATOM 4437 C CA . PRO B 1 180 ? 12.666 30.119 -27.610 1.00 136.32 ? 179 PRO B CA 1 ATOM 4438 C C . PRO B 1 180 ? 11.741 31.223 -27.105 1.00 134.52 ? 179 PRO B C 1 ATOM 4439 O O . PRO B 1 180 ? 11.088 31.074 -26.064 1.00 128.13 ? 179 PRO B O 1 ATOM 4440 C CB . PRO B 1 180 ? 11.905 29.109 -28.477 1.00 138.59 ? 179 PRO B CB 1 ATOM 4441 C CG . PRO B 1 180 ? 11.591 27.976 -27.567 1.00 137.53 ? 179 PRO B CG 1 ATOM 4442 C CD . PRO B 1 180 ? 12.713 27.917 -26.576 1.00 135.49 ? 179 PRO B CD 1 ATOM 4443 N N . GLN B 1 181 ? 11.699 32.322 -27.850 1.00 137.33 ? 180 GLN B N 1 ATOM 4444 C CA . GLN B 1 181 ? 10.927 33.497 -27.458 1.00 138.19 ? 180 GLN B CA 1 ATOM 4445 C C . GLN B 1 181 ? 9.454 33.157 -27.216 1.00 134.92 ? 180 GLN B C 1 ATOM 4446 O O . GLN B 1 181 ? 8.853 33.649 -26.264 1.00 133.35 ? 180 GLN B O 1 ATOM 4447 C CB . GLN B 1 181 ? 11.048 34.597 -28.522 1.00 142.52 ? 180 GLN B CB 1 ATOM 4448 C CG . GLN B 1 181 ? 10.609 35.974 -28.052 1.00 144.62 ? 180 GLN B CG 1 ATOM 4449 C CD . GLN B 1 181 ? 11.519 36.541 -26.976 1.00 145.13 ? 180 GLN B CD 1 ATOM 4450 O OE1 . GLN B 1 181 ? 12.742 36.566 -27.128 1.00 147.30 ? 180 GLN B OE1 1 ATOM 4451 N NE2 . GLN B 1 181 ? 10.922 37.024 -25.891 1.00 143.66 ? 180 GLN B NE2 1 ATOM 4452 N N . ALA B 1 182 ? 8.885 32.312 -28.075 1.00 130.82 ? 181 ALA B N 1 ATOM 4453 C CA . ALA B 1 182 ? 7.487 31.910 -27.949 1.00 126.70 ? 181 ALA B CA 1 ATOM 4454 C C . ALA B 1 182 ? 7.197 31.237 -26.609 1.00 125.03 ? 181 ALA B C 1 ATOM 4455 O O . ALA B 1 182 ? 6.137 31.458 -26.014 1.00 124.58 ? 181 ALA B O 1 ATOM 4456 C CB . ALA B 1 182 ? 7.104 30.985 -29.093 1.00 125.33 ? 181 ALA B CB 1 ATOM 4457 N N . TRP B 1 183 ? 8.139 30.421 -26.140 1.00 124.83 ? 182 TRP B N 1 ATOM 4458 C CA . TRP B 1 183 ? 7.989 29.736 -24.856 1.00 125.18 ? 182 TRP B CA 1 ATOM 4459 C C . TRP B 1 183 ? 7.997 30.738 -23.708 1.00 125.77 ? 182 TRP B C 1 ATOM 4460 O O . TRP B 1 183 ? 7.145 30.679 -22.820 1.00 123.04 ? 182 TRP B O 1 ATOM 4461 C CB . TRP B 1 183 ? 9.104 28.705 -24.647 1.00 123.96 ? 182 TRP B CB 1 ATOM 4462 C CG . TRP B 1 183 ? 8.922 27.867 -23.412 1.00 120.84 ? 182 TRP B CG 1 ATOM 4463 C CD1 . TRP B 1 183 ? 8.252 26.683 -23.319 1.00 120.38 ? 182 TRP B CD1 1 ATOM 4464 C CD2 . TRP B 1 183 ? 9.412 28.155 -22.098 1.00 119.40 ? 182 TRP B CD2 1 ATOM 4465 N NE1 . TRP B 1 183 ? 8.296 26.212 -22.029 1.00 118.76 ? 182 TRP B NE1 1 ATOM 4466 C CE2 . TRP B 1 183 ? 9.001 27.098 -21.259 1.00 118.53 ? 182 TRP B CE2 1 ATOM 4467 C CE3 . TRP B 1 183 ? 10.157 29.206 -21.548 1.00 119.71 ? 182 TRP B CE3 1 ATOM 4468 C CZ2 . TRP B 1 183 ? 9.309 27.059 -19.896 1.00 117.86 ? 182 TRP B CZ2 1 ATOM 4469 C CZ3 . TRP B 1 183 ? 10.465 29.166 -20.191 1.00 118.46 ? 182 TRP B CZ3 1 ATOM 4470 C CH2 . TRP B 1 183 ? 10.041 28.099 -19.382 1.00 116.76 ? 182 TRP B CH2 1 ATOM 4471 N N . LYS B 1 184 ? 8.959 31.655 -23.733 1.00 127.85 ? 183 LYS B N 1 ATOM 4472 C CA . LYS B 1 184 ? 9.090 32.658 -22.675 1.00 127.53 ? 183 LYS B CA 1 ATOM 4473 C C . LYS B 1 184 ? 7.855 33.550 -22.600 1.00 127.47 ? 183 LYS B C 1 ATOM 4474 O O . LYS B 1 184 ? 7.358 33.856 -21.509 1.00 124.29 ? 183 LYS B O 1 ATOM 4475 C CB . LYS B 1 184 ? 10.328 33.529 -22.909 1.00 130.23 ? 183 LYS B CB 1 ATOM 4476 C CG . LYS B 1 184 ? 11.655 32.809 -22.716 1.00 130.61 ? 183 LYS B CG 1 ATOM 4477 C CD . LYS B 1 184 ? 12.838 33.754 -22.886 1.00 132.03 ? 183 LYS B CD 1 ATOM 4478 C CE . LYS B 1 184 ? 13.068 34.129 -24.344 1.00 134.44 ? 183 LYS B CE 1 ATOM 4479 N NZ . LYS B 1 184 ? 14.329 34.896 -24.543 1.00 135.85 ? 183 LYS B NZ 1 ATOM 4480 N N . ASP B 1 185 ? 7.372 33.963 -23.771 1.00 129.78 ? 184 ASP B N 1 ATOM 4481 C CA . ASP B 1 185 ? 6.200 34.832 -23.869 1.00 131.68 ? 184 ASP B CA 1 ATOM 4482 C C . ASP B 1 185 ? 4.963 34.171 -23.255 1.00 131.39 ? 184 ASP B C 1 ATOM 4483 O O . ASP B 1 185 ? 4.143 34.845 -22.631 1.00 133.89 ? 184 ASP B O 1 ATOM 4484 C CB . ASP B 1 185 ? 5.919 35.209 -25.337 1.00 133.48 ? 184 ASP B CB 1 ATOM 4485 C CG . ASP B 1 185 ? 6.980 36.141 -25.934 1.00 132.43 ? 184 ASP B CG 1 ATOM 4486 O OD1 . ASP B 1 185 ? 8.039 36.348 -25.303 1.00 129.96 ? 184 ASP B OD1 1 ATOM 4487 O OD2 . ASP B 1 185 ? 6.751 36.660 -27.050 1.00 131.40 ? 184 ASP B OD2 1 ATOM 4488 N N . LYS B 1 186 ? 4.838 32.856 -23.423 1.00 130.04 ? 185 LYS B N 1 ATOM 4489 C CA . LYS B 1 186 ? 3.692 32.119 -22.886 1.00 130.47 ? 185 LYS B CA 1 ATOM 4490 C C . LYS B 1 186 ? 3.808 31.833 -21.391 1.00 124.68 ? 185 LYS B C 1 ATOM 4491 O O . LYS B 1 186 ? 2.866 32.075 -20.632 1.00 122.38 ? 185 LYS B O 1 ATOM 4492 C CB . LYS B 1 186 ? 3.502 30.791 -23.635 1.00 134.96 ? 185 LYS B CB 1 ATOM 4493 C CG . LYS B 1 186 ? 2.477 29.857 -22.993 1.00 138.36 ? 185 LYS B CG 1 ATOM 4494 C CD . LYS B 1 186 ? 2.024 28.750 -23.932 1.00 142.45 ? 185 LYS B CD 1 ATOM 4495 C CE . LYS B 1 186 ? 0.968 27.870 -23.274 1.00 144.27 ? 185 LYS B CE 1 ATOM 4496 N NZ . LYS B 1 186 ? 0.307 26.944 -24.235 1.00 147.28 ? 185 LYS B NZ 1 ATOM 4497 N N . TYR B 1 187 ? 4.959 31.309 -20.978 1.00 120.06 ? 186 TYR B N 1 ATOM 4498 C CA . TYR B 1 187 ? 5.094 30.696 -19.658 1.00 116.97 ? 186 TYR B CA 1 ATOM 4499 C C . TYR B 1 187 ? 5.654 31.595 -18.561 1.00 118.68 ? 186 TYR B C 1 ATOM 4500 O O . TYR B 1 187 ? 5.482 31.289 -17.382 1.00 116.03 ? 186 TYR B O 1 ATOM 4501 C CB . TYR B 1 187 ? 5.939 29.429 -19.756 1.00 114.37 ? 186 TYR B CB 1 ATOM 4502 C CG . TYR B 1 187 ? 5.213 28.276 -20.403 1.00 115.09 ? 186 TYR B CG 1 ATOM 4503 C CD1 . TYR B 1 187 ? 4.382 27.447 -19.657 1.00 114.71 ? 186 TYR B CD1 1 ATOM 4504 C CD2 . TYR B 1 187 ? 5.355 28.012 -21.762 1.00 117.04 ? 186 TYR B CD2 1 ATOM 4505 C CE1 . TYR B 1 187 ? 3.712 26.387 -20.245 1.00 116.35 ? 186 TYR B CE1 1 ATOM 4506 C CE2 . TYR B 1 187 ? 4.690 26.954 -22.360 1.00 118.42 ? 186 TYR B CE2 1 ATOM 4507 C CZ . TYR B 1 187 ? 3.870 26.144 -21.597 1.00 118.89 ? 186 TYR B CZ 1 ATOM 4508 O OH . TYR B 1 187 ? 3.207 25.091 -22.186 1.00 121.91 ? 186 TYR B OH 1 ATOM 4509 N N . ILE B 1 188 ? 6.326 32.684 -18.936 1.00 122.71 ? 187 ILE B N 1 ATOM 4510 C CA . ILE B 1 188 ? 6.927 33.590 -17.959 1.00 124.18 ? 187 ILE B CA 1 ATOM 4511 C C . ILE B 1 188 ? 6.155 34.902 -17.892 1.00 125.51 ? 187 ILE B C 1 ATOM 4512 O O . ILE B 1 188 ? 6.037 35.613 -18.893 1.00 123.48 ? 187 ILE B O 1 ATOM 4513 C CB . ILE B 1 188 ? 8.404 33.895 -18.293 1.00 126.17 ? 187 ILE B CB 1 ATOM 4514 C CG1 . ILE B 1 188 ? 9.208 32.596 -18.449 1.00 126.12 ? 187 ILE B CG1 1 ATOM 4515 C CG2 . ILE B 1 188 ? 9.022 34.784 -17.219 1.00 127.35 ? 187 ILE B CG2 1 ATOM 4516 C CD1 . ILE B 1 188 ? 9.238 31.720 -17.213 1.00 124.93 ? 187 ILE B CD1 1 ATOM 4517 N N . ARG B 1 189 ? 5.641 35.208 -16.700 1.00 127.24 ? 188 ARG B N 1 ATOM 4518 C CA . ARG B 1 189 ? 4.944 36.471 -16.438 1.00 129.01 ? 188 ARG B CA 1 ATOM 4519 C C . ARG B 1 189 ? 5.965 37.573 -16.193 1.00 128.38 ? 188 ARG B C 1 ATOM 4520 O O . ARG B 1 189 ? 5.888 38.644 -16.793 1.00 130.51 ? 188 ARG B O 1 ATOM 4521 C CB . ARG B 1 189 ? 4.009 36.317 -15.225 1.00 130.23 ? 188 ARG B CB 1 ATOM 4522 C CG . ARG B 1 189 ? 3.682 37.588 -14.452 1.00 131.97 ? 188 ARG B CG 1 ATOM 4523 C CD . ARG B 1 189 ? 2.876 38.588 -15.259 1.00 136.87 ? 188 ARG B CD 1 ATOM 4524 N NE . ARG B 1 189 ? 2.557 39.765 -14.452 1.00 144.89 ? 188 ARG B NE 1 ATOM 4525 C CZ . ARG B 1 189 ? 1.940 40.859 -14.900 1.00 155.33 ? 188 ARG B CZ 1 ATOM 4526 N NH1 . ARG B 1 189 ? 1.554 40.952 -16.172 1.00 160.35 ? 188 ARG B NH1 1 ATOM 4527 N NH2 . ARG B 1 189 ? 1.706 41.873 -14.068 1.00 156.30 ? 188 ARG B NH2 1 ATOM 4528 N N . ALA B 1 190 ? 6.917 37.305 -15.305 1.00 127.17 ? 189 ALA B N 1 ATOM 4529 C CA . ALA B 1 190 ? 7.951 38.276 -14.977 1.00 128.08 ? 189 ALA B CA 1 ATOM 4530 C C . ALA B 1 190 ? 9.150 37.594 -14.336 1.00 127.82 ? 189 ALA B C 1 ATOM 4531 O O . ALA B 1 190 ? 9.057 36.454 -13.878 1.00 125.94 ? 189 ALA B O 1 ATOM 4532 C CB . ALA B 1 190 ? 7.391 39.338 -14.045 1.00 128.63 ? 189 ALA B CB 1 ATOM 4533 N N . PHE B 1 191 ? 10.268 38.312 -14.320 1.00 129.96 ? 190 PHE B N 1 ATOM 4534 C CA . PHE B 1 191 ? 11.516 37.850 -13.722 1.00 130.32 ? 190 PHE B CA 1 ATOM 4535 C C . PHE B 1 191 ? 11.954 38.945 -12.756 1.00 129.09 ? 190 PHE B C 1 ATOM 4536 O O . PHE B 1 191 ? 12.270 40.061 -13.168 1.00 130.81 ? 190 PHE B O 1 ATOM 4537 C CB . PHE B 1 191 ? 12.556 37.612 -14.835 1.00 132.97 ? 190 PHE B CB 1 ATOM 4538 C CG . PHE B 1 191 ? 13.965 37.340 -14.348 1.00 136.07 ? 190 PHE B CG 1 ATOM 4539 C CD1 . PHE B 1 191 ? 14.219 36.787 -13.094 1.00 136.94 ? 190 PHE B CD1 1 ATOM 4540 C CD2 . PHE B 1 191 ? 15.048 37.605 -15.184 1.00 138.55 ? 190 PHE B CD2 1 ATOM 4541 C CE1 . PHE B 1 191 ? 15.520 36.540 -12.681 1.00 138.32 ? 190 PHE B CE1 1 ATOM 4542 C CE2 . PHE B 1 191 ? 16.349 37.355 -14.775 1.00 139.33 ? 190 PHE B CE2 1 ATOM 4543 C CZ . PHE B 1 191 ? 16.586 36.822 -13.522 1.00 139.18 ? 190 PHE B CZ 1 ATOM 4544 N N . VAL B 1 192 ? 11.915 38.620 -11.469 1.00 126.09 ? 191 VAL B N 1 ATOM 4545 C CA . VAL B 1 192 ? 12.325 39.524 -10.407 1.00 127.50 ? 191 VAL B CA 1 ATOM 4546 C C . VAL B 1 192 ? 13.746 39.149 -10.017 1.00 128.73 ? 191 VAL B C 1 ATOM 4547 O O . VAL B 1 192 ? 13.985 38.050 -9.515 1.00 129.06 ? 191 VAL B O 1 ATOM 4548 C CB . VAL B 1 192 ? 11.407 39.374 -9.180 1.00 128.10 ? 191 VAL B CB 1 ATOM 4549 C CG1 . VAL B 1 192 ? 11.827 40.335 -8.075 1.00 128.67 ? 191 VAL B CG1 1 ATOM 4550 C CG2 . VAL B 1 192 ? 9.955 39.591 -9.580 1.00 128.79 ? 191 VAL B CG2 1 ATOM 4551 N N . SER B 1 193 ? 14.674 40.072 -10.252 1.00 131.19 ? 192 SER B N 1 ATOM 4552 C CA . SER B 1 193 ? 16.095 39.842 -10.040 1.00 133.97 ? 192 SER B CA 1 ATOM 4553 C C . SER B 1 193 ? 16.557 40.557 -8.775 1.00 135.51 ? 192 SER B C 1 ATOM 4554 O O . SER B 1 193 ? 16.467 41.777 -8.679 1.00 136.14 ? 192 SER B O 1 ATOM 4555 C CB . SER B 1 193 ? 16.879 40.357 -11.247 1.00 136.68 ? 192 SER B CB 1 ATOM 4556 O OG . SER B 1 193 ? 18.269 40.152 -11.087 1.00 139.23 ? 192 SER B OG 1 ATOM 4557 N N . LEU B 1 194 ? 17.053 39.789 -7.810 1.00 135.63 ? 193 LEU B N 1 ATOM 4558 C CA . LEU B 1 194 ? 17.461 40.333 -6.516 1.00 138.68 ? 193 LEU B CA 1 ATOM 4559 C C . LEU B 1 194 ? 18.969 40.202 -6.322 1.00 140.64 ? 193 LEU B C 1 ATOM 4560 O O . LEU B 1 194 ? 19.484 39.100 -6.132 1.00 143.31 ? 193 LEU B O 1 ATOM 4561 C CB . LEU B 1 194 ? 16.730 39.596 -5.389 1.00 139.24 ? 193 LEU B CB 1 ATOM 4562 C CG . LEU B 1 194 ? 15.211 39.486 -5.547 1.00 139.93 ? 193 LEU B CG 1 ATOM 4563 C CD1 . LEU B 1 194 ? 14.614 38.685 -4.401 1.00 140.04 ? 193 LEU B CD1 1 ATOM 4564 C CD2 . LEU B 1 194 ? 14.575 40.865 -5.630 1.00 141.45 ? 193 LEU B CD2 1 ATOM 4565 N N . GLY B 1 195 ? 19.677 41.329 -6.364 1.00 140.95 ? 194 GLY B N 1 ATOM 4566 C CA . GLY B 1 195 ? 21.119 41.346 -6.110 1.00 141.34 ? 194 GLY B CA 1 ATOM 4567 C C . GLY B 1 195 ? 21.929 40.529 -7.100 1.00 140.02 ? 194 GLY B C 1 ATOM 4568 O O . GLY B 1 195 ? 22.821 39.771 -6.712 1.00 137.41 ? 194 GLY B O 1 ATOM 4569 N N . ALA B 1 196 ? 21.619 40.687 -8.382 1.00 139.59 ? 195 ALA B N 1 ATOM 4570 C CA . ALA B 1 196 ? 22.258 39.896 -9.430 1.00 139.70 ? 195 ALA B CA 1 ATOM 4571 C C . ALA B 1 196 ? 23.671 40.397 -9.737 1.00 142.67 ? 195 ALA B C 1 ATOM 4572 O O . ALA B 1 196 ? 23.849 41.577 -10.051 1.00 143.49 ? 195 ALA B O 1 ATOM 4573 C CB . ALA B 1 196 ? 21.415 39.928 -10.684 1.00 139.86 ? 195 ALA B CB 1 ATOM 4574 N N . PRO B 1 197 ? 24.679 39.499 -9.664 1.00 144.27 ? 196 PRO B N 1 ATOM 4575 C CA . PRO B 1 197 ? 26.074 39.860 -9.910 1.00 148.14 ? 196 PRO B CA 1 ATOM 4576 C C . PRO B 1 197 ? 26.436 39.821 -11.396 1.00 149.60 ? 196 PRO B C 1 ATOM 4577 O O . PRO B 1 197 ? 27.313 39.054 -11.804 1.00 150.21 ? 196 PRO B O 1 ATOM 4578 C CB . PRO B 1 197 ? 26.838 38.783 -9.137 1.00 146.88 ? 196 PRO B CB 1 ATOM 4579 C CG . PRO B 1 197 ? 25.980 37.579 -9.286 1.00 144.40 ? 196 PRO B CG 1 ATOM 4580 C CD . PRO B 1 197 ? 24.558 38.081 -9.275 1.00 143.25 ? 196 PRO B CD 1 ATOM 4581 N N . TRP B 1 198 ? 25.767 40.656 -12.188 1.00 150.18 ? 197 TRP B N 1 ATOM 4582 C CA . TRP B 1 198 ? 25.999 40.690 -13.628 1.00 152.51 ? 197 TRP B CA 1 ATOM 4583 C C . TRP B 1 198 ? 27.442 41.123 -13.876 1.00 157.48 ? 197 TRP B C 1 ATOM 4584 O O . TRP B 1 198 ? 27.854 42.210 -13.459 1.00 159.25 ? 197 TRP B O 1 ATOM 4585 C CB . TRP B 1 198 ? 25.045 41.662 -14.333 1.00 153.26 ? 197 TRP B CB 1 ATOM 4586 C CG . TRP B 1 198 ? 23.581 41.487 -14.015 1.00 149.93 ? 197 TRP B CG 1 ATOM 4587 C CD1 . TRP B 1 198 ? 22.760 42.404 -13.423 1.00 150.00 ? 197 TRP B CD1 1 ATOM 4588 C CD2 . TRP B 1 198 ? 22.770 40.338 -14.280 1.00 147.11 ? 197 TRP B CD2 1 ATOM 4589 N NE1 . TRP B 1 198 ? 21.490 41.898 -13.303 1.00 146.67 ? 197 TRP B NE1 1 ATOM 4590 C CE2 . TRP B 1 198 ? 21.466 40.632 -13.823 1.00 146.00 ? 197 TRP B CE2 1 ATOM 4591 C CE3 . TRP B 1 198 ? 23.016 39.089 -14.859 1.00 147.94 ? 197 TRP B CE3 1 ATOM 4592 C CZ2 . TRP B 1 198 ? 20.413 39.718 -13.919 1.00 145.83 ? 197 TRP B CZ2 1 ATOM 4593 C CZ3 . TRP B 1 198 ? 21.964 38.180 -14.957 1.00 147.62 ? 197 TRP B CZ3 1 ATOM 4594 C CH2 . TRP B 1 198 ? 20.681 38.501 -14.489 1.00 146.10 ? 197 TRP B CH2 1 ATOM 4595 N N . GLY B 1 199 ? 28.209 40.261 -14.536 1.00 159.77 ? 198 GLY B N 1 ATOM 4596 C CA . GLY B 1 199 ? 29.611 40.544 -14.820 1.00 163.92 ? 198 GLY B CA 1 ATOM 4597 C C . GLY B 1 199 ? 30.537 40.353 -13.631 1.00 164.96 ? 198 GLY B C 1 ATOM 4598 O O . GLY B 1 199 ? 31.597 40.977 -13.564 1.00 167.92 ? 198 GLY B O 1 ATOM 4599 N N . GLY B 1 200 ? 30.141 39.496 -12.691 1.00 162.49 ? 199 GLY B N 1 ATOM 4600 C CA . GLY B 1 200 ? 31.029 39.063 -11.617 1.00 161.49 ? 199 GLY B CA 1 ATOM 4601 C C . GLY B 1 200 ? 31.209 40.069 -10.500 1.00 160.05 ? 199 GLY B C 1 ATOM 4602 O O . GLY B 1 200 ? 30.663 41.170 -10.547 1.00 155.12 ? 199 GLY B O 1 ATOM 4603 N N . VAL B 1 201 ? 31.986 39.682 -9.493 1.00 161.13 ? 200 VAL B N 1 ATOM 4604 C CA . VAL B 1 201 ? 32.191 40.510 -8.309 1.00 163.73 ? 200 VAL B CA 1 ATOM 4605 C C . VAL B 1 201 ? 33.640 40.472 -7.835 1.00 166.97 ? 200 VAL B C 1 ATOM 4606 O O . VAL B 1 201 ? 34.343 39.471 -7.990 1.00 167.15 ? 200 VAL B O 1 ATOM 4607 C CB . VAL B 1 201 ? 31.268 40.087 -7.148 1.00 163.04 ? 200 VAL B CB 1 ATOM 4608 C CG1 . VAL B 1 201 ? 29.821 40.403 -7.486 1.00 161.96 ? 200 VAL B CG1 1 ATOM 4609 C CG2 . VAL B 1 201 ? 31.439 38.608 -6.814 1.00 161.78 ? 200 VAL B CG2 1 ATOM 4610 N N . ALA B 1 202 ? 34.072 41.575 -7.237 1.00 169.84 ? 201 ALA B N 1 ATOM 4611 C CA . ALA B 1 202 ? 35.458 41.729 -6.827 1.00 171.52 ? 201 ALA B CA 1 ATOM 4612 C C . ALA B 1 202 ? 35.875 40.718 -5.768 1.00 169.82 ? 201 ALA B C 1 ATOM 4613 O O . ALA B 1 202 ? 37.020 40.275 -5.767 1.00 170.93 ? 201 ALA B O 1 ATOM 4614 C CB . ALA B 1 202 ? 35.706 43.144 -6.326 1.00 173.65 ? 201 ALA B CB 1 ATOM 4615 N N . LYS B 1 203 ? 34.959 40.348 -4.872 1.00 166.94 ? 202 LYS B N 1 ATOM 4616 C CA . LYS B 1 203 ? 35.305 39.481 -3.731 1.00 167.01 ? 202 LYS B CA 1 ATOM 4617 C C . LYS B 1 203 ? 35.902 38.121 -4.127 1.00 164.16 ? 202 LYS B C 1 ATOM 4618 O O . LYS B 1 203 ? 36.643 37.507 -3.352 1.00 162.98 ? 202 LYS B O 1 ATOM 4619 C CB . LYS B 1 203 ? 34.100 39.276 -2.798 1.00 166.44 ? 202 LYS B CB 1 ATOM 4620 C CG . LYS B 1 203 ? 32.958 38.439 -3.374 1.00 166.71 ? 202 LYS B CG 1 ATOM 4621 C CD . LYS B 1 203 ? 32.342 37.511 -2.331 1.00 167.74 ? 202 LYS B CD 1 ATOM 4622 C CE . LYS B 1 203 ? 31.432 36.464 -2.970 1.00 166.67 ? 202 LYS B CE 1 ATOM 4623 N NZ . LYS B 1 203 ? 30.930 35.449 -1.997 1.00 166.20 ? 202 LYS B NZ 1 ATOM 4624 N N . THR B 1 204 ? 35.568 37.668 -5.335 1.00 161.58 ? 203 THR B N 1 ATOM 4625 C CA . THR B 1 204 ? 36.093 36.428 -5.908 1.00 159.87 ? 203 THR B CA 1 ATOM 4626 C C . THR B 1 204 ? 37.621 36.324 -5.828 1.00 162.00 ? 203 THR B C 1 ATOM 4627 O O . THR B 1 204 ? 38.175 35.264 -5.526 1.00 161.50 ? 203 THR B O 1 ATOM 4628 C CB . THR B 1 204 ? 35.702 36.340 -7.398 1.00 158.19 ? 203 THR B CB 1 ATOM 4629 O OG1 . THR B 1 204 ? 34.333 36.728 -7.564 1.00 155.06 ? 203 THR B OG1 1 ATOM 4630 C CG2 . THR B 1 204 ? 35.902 34.938 -7.933 1.00 157.12 ? 203 THR B CG2 1 ATOM 4631 N N . LEU B 1 205 ? 38.295 37.433 -6.105 1.00 162.86 ? 204 LEU B N 1 ATOM 4632 C CA . LEU B 1 205 ? 39.750 37.444 -6.144 1.00 165.48 ? 204 LEU B CA 1 ATOM 4633 C C . LEU B 1 205 ? 40.338 37.130 -4.774 1.00 166.62 ? 204 LEU B C 1 ATOM 4634 O O . LEU B 1 205 ? 41.283 36.348 -4.665 1.00 166.18 ? 204 LEU B O 1 ATOM 4635 C CB . LEU B 1 205 ? 40.271 38.796 -6.640 1.00 168.39 ? 204 LEU B CB 1 ATOM 4636 C CG . LEU B 1 205 ? 40.175 39.093 -8.143 1.00 170.02 ? 204 LEU B CG 1 ATOM 4637 C CD1 . LEU B 1 205 ? 40.965 38.075 -8.954 1.00 171.20 ? 204 LEU B CD1 1 ATOM 4638 C CD2 . LEU B 1 205 ? 38.737 39.174 -8.640 1.00 167.15 ? 204 LEU B CD2 1 ATOM 4639 N N . ARG B 1 206 ? 39.774 37.735 -3.732 1.00 168.13 ? 205 ARG B N 1 ATOM 4640 C CA . ARG B 1 206 ? 40.259 37.514 -2.369 1.00 172.82 ? 205 ARG B CA 1 ATOM 4641 C C . ARG B 1 206 ? 40.028 36.072 -1.937 1.00 171.72 ? 205 ARG B C 1 ATOM 4642 O O . ARG B 1 206 ? 40.905 35.441 -1.345 1.00 172.71 ? 205 ARG B O 1 ATOM 4643 C CB . ARG B 1 206 ? 39.550 38.445 -1.383 1.00 174.14 ? 205 ARG B CB 1 ATOM 4644 C CG . ARG B 1 206 ? 40.166 38.444 0.011 1.00 176.91 ? 205 ARG B CG 1 ATOM 4645 C CD . ARG B 1 206 ? 39.120 38.460 1.114 1.00 175.78 ? 205 ARG B CD 1 ATOM 4646 N NE . ARG B 1 206 ? 39.669 37.937 2.363 1.00 179.41 ? 205 ARG B NE 1 ATOM 4647 C CZ . ARG B 1 206 ? 38.951 37.640 3.444 1.00 180.30 ? 205 ARG B CZ 1 ATOM 4648 N NH1 . ARG B 1 206 ? 37.633 37.818 3.457 1.00 179.32 ? 205 ARG B NH1 1 ATOM 4649 N NH2 . ARG B 1 206 ? 39.558 37.160 4.525 1.00 181.36 ? 205 ARG B NH2 1 ATOM 4650 N N . VAL B 1 207 ? 38.839 35.563 -2.239 1.00 169.84 ? 206 VAL B N 1 ATOM 4651 C CA . VAL B 1 207 ? 38.477 34.191 -1.901 1.00 168.80 ? 206 VAL B CA 1 ATOM 4652 C C . VAL B 1 207 ? 39.507 33.217 -2.481 1.00 168.78 ? 206 VAL B C 1 ATOM 4653 O O . VAL B 1 207 ? 40.046 32.375 -1.760 1.00 167.71 ? 206 VAL B O 1 ATOM 4654 C CB . VAL B 1 207 ? 37.066 33.844 -2.429 1.00 168.09 ? 206 VAL B CB 1 ATOM 4655 C CG1 . VAL B 1 207 ? 36.778 32.351 -2.289 1.00 168.27 ? 206 VAL B CG1 1 ATOM 4656 C CG2 . VAL B 1 207 ? 36.002 34.669 -1.708 1.00 167.01 ? 206 VAL B CG2 1 ATOM 4657 N N . LEU B 1 208 ? 39.783 33.354 -3.776 1.00 168.14 ? 207 LEU B N 1 ATOM 4658 C CA . LEU B 1 208 ? 40.706 32.458 -4.477 1.00 168.93 ? 207 LEU B CA 1 ATOM 4659 C C . LEU B 1 208 ? 42.144 32.610 -3.989 1.00 170.93 ? 207 LEU B C 1 ATOM 4660 O O . LEU B 1 208 ? 42.864 31.623 -3.842 1.00 171.54 ? 207 LEU B O 1 ATOM 4661 C CB . LEU B 1 208 ? 40.649 32.713 -5.985 1.00 169.51 ? 207 LEU B CB 1 ATOM 4662 C CG . LEU B 1 208 ? 39.315 32.365 -6.651 1.00 167.12 ? 207 LEU B CG 1 ATOM 4663 C CD1 . LEU B 1 208 ? 39.150 33.119 -7.960 1.00 167.62 ? 207 LEU B CD1 1 ATOM 4664 C CD2 . LEU B 1 208 ? 39.182 30.864 -6.867 1.00 166.17 ? 207 LEU B CD2 1 ATOM 4665 N N . ALA B 1 209 ? 42.558 33.847 -3.738 1.00 171.29 ? 208 ALA B N 1 ATOM 4666 C CA . ALA B 1 209 ? 43.928 34.119 -3.326 1.00 173.39 ? 208 ALA B CA 1 ATOM 4667 C C . ALA B 1 209 ? 44.207 33.620 -1.909 1.00 173.31 ? 208 ALA B C 1 ATOM 4668 O O . ALA B 1 209 ? 45.094 32.792 -1.705 1.00 175.02 ? 208 ALA B O 1 ATOM 4669 C CB . ALA B 1 209 ? 44.223 35.607 -3.433 1.00 174.96 ? 208 ALA B CB 1 ATOM 4670 N N . SER B 1 210 ? 43.434 34.110 -0.941 1.00 171.14 ? 209 SER B N 1 ATOM 4671 C CA . SER B 1 210 ? 43.739 33.893 0.482 1.00 171.87 ? 209 SER B CA 1 ATOM 4672 C C . SER B 1 210 ? 42.613 33.286 1.326 1.00 170.99 ? 209 SER B C 1 ATOM 4673 O O . SER B 1 210 ? 42.761 33.168 2.545 1.00 172.81 ? 209 SER B O 1 ATOM 4674 C CB . SER B 1 210 ? 44.156 35.217 1.123 1.00 172.51 ? 209 SER B CB 1 ATOM 4675 O OG . SER B 1 210 ? 43.026 36.023 1.414 1.00 168.79 ? 209 SER B OG 1 ATOM 4676 N N . GLY B 1 211 ? 41.503 32.906 0.696 1.00 169.65 ? 210 GLY B N 1 ATOM 4677 C CA . GLY B 1 211 ? 40.357 32.352 1.420 1.00 169.26 ? 210 GLY B CA 1 ATOM 4678 C C . GLY B 1 211 ? 39.491 33.429 2.049 1.00 171.87 ? 210 GLY B C 1 ATOM 4679 O O . GLY B 1 211 ? 39.933 34.562 2.245 1.00 174.46 ? 210 GLY B O 1 ATOM 4680 N N . ASP B 1 212 ? 38.255 33.066 2.375 1.00 172.40 ? 211 ASP B N 1 ATOM 4681 C CA . ASP B 1 212 ? 37.275 34.015 2.904 1.00 173.97 ? 211 ASP B CA 1 ATOM 4682 C C . ASP B 1 212 ? 36.424 33.298 3.953 1.00 172.19 ? 211 ASP B C 1 ATOM 4683 O O . ASP B 1 212 ? 35.581 32.470 3.612 1.00 169.26 ? 211 ASP B O 1 ATOM 4684 C CB . ASP B 1 212 ? 36.404 34.538 1.750 1.00 173.10 ? 211 ASP B CB 1 ATOM 4685 C CG . ASP B 1 212 ? 35.571 35.751 2.133 1.00 174.50 ? 211 ASP B CG 1 ATOM 4686 O OD1 . ASP B 1 212 ? 34.831 35.686 3.139 1.00 175.59 ? 211 ASP B OD1 1 ATOM 4687 O OD2 . ASP B 1 212 ? 35.647 36.771 1.411 1.00 175.32 ? 211 ASP B OD2 1 ATOM 4688 N N . ASN B 1 213 ? 36.657 33.606 5.225 1.00 174.70 ? 212 ASN B N 1 ATOM 4689 C CA . ASN B 1 213 ? 35.970 32.918 6.316 1.00 175.12 ? 212 ASN B CA 1 ATOM 4690 C C . ASN B 1 213 ? 35.005 33.822 7.081 1.00 179.13 ? 212 ASN B C 1 ATOM 4691 O O . ASN B 1 213 ? 34.640 33.516 8.222 1.00 179.41 ? 212 ASN B O 1 ATOM 4692 C CB . ASN B 1 213 ? 36.989 32.283 7.268 1.00 176.92 ? 212 ASN B CB 1 ATOM 4693 C CG . ASN B 1 213 ? 37.806 33.310 8.027 1.00 181.72 ? 212 ASN B CG 1 ATOM 4694 O OD1 . ASN B 1 213 ? 37.928 34.462 7.605 1.00 184.71 ? 212 ASN B OD1 1 ATOM 4695 N ND2 . ASN B 1 213 ? 38.377 32.896 9.151 1.00 184.10 ? 212 ASN B ND2 1 ATOM 4696 N N . ASN B 1 214 ? 34.554 34.902 6.438 1.00 185.65 ? 213 ASN B N 1 ATOM 4697 C CA . ASN B 1 214 ? 33.651 35.893 7.062 1.00 190.68 ? 213 ASN B CA 1 ATOM 4698 C C . ASN B 1 214 ? 32.470 35.267 7.791 1.00 193.68 ? 213 ASN B C 1 ATOM 4699 O O . ASN B 1 214 ? 32.021 35.761 8.828 1.00 196.25 ? 213 ASN B O 1 ATOM 4700 C CB . ASN B 1 214 ? 33.088 36.849 6.000 1.00 190.01 ? 213 ASN B CB 1 ATOM 4701 C CG . ASN B 1 214 ? 34.090 37.897 5.558 1.00 192.51 ? 213 ASN B CG 1 ATOM 4702 O OD1 . ASN B 1 214 ? 35.184 38.009 6.114 1.00 195.07 ? 213 ASN B OD1 1 ATOM 4703 N ND2 . ASN B 1 214 ? 33.717 38.676 4.548 1.00 193.09 ? 213 ASN B ND2 1 ATOM 4704 N N . ARG B 1 215 ? 31.962 34.183 7.229 1.00 196.48 ? 214 ARG B N 1 ATOM 4705 C CA . ARG B 1 215 ? 30.792 33.520 7.787 1.00 199.42 ? 214 ARG B CA 1 ATOM 4706 C C . ARG B 1 215 ? 31.225 32.468 8.807 1.00 200.40 ? 214 ARG B C 1 ATOM 4707 O O . ARG B 1 215 ? 30.488 32.151 9.741 1.00 202.40 ? 214 ARG B O 1 ATOM 4708 C CB . ARG B 1 215 ? 29.978 32.864 6.664 1.00 199.76 ? 214 ARG B CB 1 ATOM 4709 C CG . ARG B 1 215 ? 29.935 33.667 5.371 1.00 202.46 ? 214 ARG B CG 1 ATOM 4710 C CD . ARG B 1 215 ? 28.532 33.894 4.850 1.00 205.96 ? 214 ARG B CD 1 ATOM 4711 N NE . ARG B 1 215 ? 28.548 34.835 3.730 1.00 213.80 ? 214 ARG B NE 1 ATOM 4712 C CZ . ARG B 1 215 ? 27.521 35.071 2.916 1.00 219.80 ? 214 ARG B CZ 1 ATOM 4713 N NH1 . ARG B 1 215 ? 26.366 34.434 3.079 1.00 221.46 ? 214 ARG B NH1 1 ATOM 4714 N NH2 . ARG B 1 215 ? 27.650 35.949 1.926 1.00 221.36 ? 214 ARG B NH2 1 ATOM 4715 N N . ILE B 1 216 ? 32.434 31.945 8.637 1.00 199.17 ? 215 ILE B N 1 ATOM 4716 C CA . ILE B 1 216 ? 32.889 30.786 9.388 1.00 195.42 ? 215 ILE B CA 1 ATOM 4717 C C . ILE B 1 216 ? 34.180 31.171 10.100 1.00 194.04 ? 215 ILE B C 1 ATOM 4718 O O . ILE B 1 216 ? 35.239 30.599 9.830 1.00 192.26 ? 215 ILE B O 1 ATOM 4719 C CB . ILE B 1 216 ? 33.118 29.571 8.456 1.00 194.04 ? 215 ILE B CB 1 ATOM 4720 C CG1 . ILE B 1 216 ? 32.217 29.656 7.216 1.00 189.88 ? 215 ILE B CG1 1 ATOM 4721 C CG2 . ILE B 1 216 ? 32.859 28.277 9.216 1.00 194.54 ? 215 ILE B CG2 1 ATOM 4722 C CD1 . ILE B 1 216 ? 32.479 28.571 6.197 1.00 188.59 ? 215 ILE B CD1 1 ATOM 4723 N N . PRO B 1 217 ? 34.090 32.153 11.019 1.00 192.35 ? 216 PRO B N 1 ATOM 4724 C CA . PRO B 1 217 ? 35.285 32.705 11.675 1.00 195.07 ? 216 PRO B CA 1 ATOM 4725 C C . PRO B 1 217 ? 36.053 31.716 12.560 1.00 197.71 ? 216 PRO B C 1 ATOM 4726 O O . PRO B 1 217 ? 37.227 31.938 12.853 1.00 201.89 ? 216 PRO B O 1 ATOM 4727 C CB . PRO B 1 217 ? 34.711 33.828 12.536 1.00 195.75 ? 216 PRO B CB 1 ATOM 4728 C CG . PRO B 1 217 ? 33.363 33.327 12.908 1.00 194.12 ? 216 PRO B CG 1 ATOM 4729 C CD . PRO B 1 217 ? 32.858 32.636 11.672 1.00 191.66 ? 216 PRO B CD 1 ATOM 4730 N N . VAL B 1 218 ? 35.390 30.643 12.988 1.00 196.58 ? 217 VAL B N 1 ATOM 4731 C CA . VAL B 1 218 ? 36.040 29.587 13.761 1.00 197.35 ? 217 VAL B CA 1 ATOM 4732 C C . VAL B 1 218 ? 37.075 28.806 12.939 1.00 198.56 ? 217 VAL B C 1 ATOM 4733 O O . VAL B 1 218 ? 37.959 28.154 13.509 1.00 200.07 ? 217 VAL B O 1 ATOM 4734 C CB . VAL B 1 218 ? 34.998 28.603 14.350 1.00 194.47 ? 217 VAL B CB 1 ATOM 4735 C CG1 . VAL B 1 218 ? 34.382 27.725 13.261 1.00 191.48 ? 217 VAL B CG1 1 ATOM 4736 C CG2 . VAL B 1 218 ? 35.613 27.753 15.455 1.00 195.39 ? 217 VAL B CG2 1 ATOM 4737 N N . ILE B 1 219 ? 36.967 28.867 11.612 1.00 197.02 ? 218 ILE B N 1 ATOM 4738 C CA . ILE B 1 219 ? 37.944 28.193 10.760 1.00 197.11 ? 218 ILE B CA 1 ATOM 4739 C C . ILE B 1 219 ? 38.888 29.145 10.021 1.00 198.05 ? 218 ILE B C 1 ATOM 4740 O O . ILE B 1 219 ? 38.488 30.201 9.526 1.00 195.96 ? 218 ILE B O 1 ATOM 4741 C CB . ILE B 1 219 ? 37.297 27.184 9.790 1.00 194.35 ? 218 ILE B CB 1 ATOM 4742 C CG1 . ILE B 1 219 ? 38.383 26.501 8.956 1.00 196.33 ? 218 ILE B CG1 1 ATOM 4743 C CG2 . ILE B 1 219 ? 36.268 27.855 8.892 1.00 192.27 ? 218 ILE B CG2 1 ATOM 4744 C CD1 . ILE B 1 219 ? 37.961 25.187 8.367 1.00 194.97 ? 218 ILE B CD1 1 ATOM 4745 N N . GLY B 1 220 ? 40.154 28.740 9.954 1.00 197.72 ? 219 GLY B N 1 ATOM 4746 C CA . GLY B 1 220 ? 41.189 29.496 9.258 1.00 195.47 ? 219 GLY B CA 1 ATOM 4747 C C . GLY B 1 220 ? 40.922 29.681 7.770 1.00 189.24 ? 219 GLY B C 1 ATOM 4748 O O . GLY B 1 220 ? 40.455 28.756 7.097 1.00 186.85 ? 219 GLY B O 1 ATOM 4749 N N . PRO B 1 221 ? 41.225 30.880 7.246 1.00 185.42 ? 220 PRO B N 1 ATOM 4750 C CA . PRO B 1 221 ? 40.891 31.160 5.853 1.00 181.83 ? 220 PRO B CA 1 ATOM 4751 C C . PRO B 1 221 ? 41.629 30.272 4.860 1.00 177.65 ? 220 PRO B C 1 ATOM 4752 O O . PRO B 1 221 ? 41.066 29.901 3.835 1.00 172.93 ? 220 PRO B O 1 ATOM 4753 C CB . PRO B 1 221 ? 41.320 32.626 5.659 1.00 186.28 ? 220 PRO B CB 1 ATOM 4754 C CG . PRO B 1 221 ? 41.674 33.144 7.011 1.00 188.76 ? 220 PRO B CG 1 ATOM 4755 C CD . PRO B 1 221 ? 42.045 31.954 7.834 1.00 188.18 ? 220 PRO B CD 1 ATOM 4756 N N . LEU B 1 222 ? 42.881 29.942 5.156 1.00 176.51 ? 221 LEU B N 1 ATOM 4757 C CA . LEU B 1 222 ? 43.699 29.158 4.233 1.00 174.60 ? 221 LEU B CA 1 ATOM 4758 C C . LEU B 1 222 ? 43.216 27.710 4.138 1.00 168.90 ? 221 LEU B C 1 ATOM 4759 O O . LEU B 1 222 ? 43.414 27.052 3.113 1.00 166.63 ? 221 LEU B O 1 ATOM 4760 C CB . LEU B 1 222 ? 45.174 29.211 4.645 1.00 180.31 ? 221 LEU B CB 1 ATOM 4761 C CG . LEU B 1 222 ? 45.817 30.607 4.705 1.00 184.77 ? 221 LEU B CG 1 ATOM 4762 C CD1 . LEU B 1 222 ? 47.254 30.525 5.199 1.00 188.08 ? 221 LEU B CD1 1 ATOM 4763 C CD2 . LEU B 1 222 ? 45.760 31.307 3.353 1.00 185.99 ? 221 LEU B CD2 1 ATOM 4764 N N . LYS B 1 223 ? 42.566 27.227 5.197 1.00 166.15 ? 222 LYS B N 1 ATOM 4765 C CA . LYS B 1 223 ? 42.005 25.878 5.203 1.00 164.18 ? 222 LYS B CA 1 ATOM 4766 C C . LYS B 1 223 ? 40.756 25.822 4.329 1.00 160.51 ? 222 LYS B C 1 ATOM 4767 O O . LYS B 1 223 ? 40.651 24.979 3.440 1.00 157.92 ? 222 LYS B O 1 ATOM 4768 C CB . LYS B 1 223 ? 41.670 25.425 6.630 1.00 163.84 ? 222 LYS B CB 1 ATOM 4769 C CG . LYS B 1 223 ? 41.789 23.924 6.836 1.00 164.10 ? 222 LYS B CG 1 ATOM 4770 C CD . LYS B 1 223 ? 43.247 23.510 6.966 1.00 168.77 ? 222 LYS B CD 1 ATOM 4771 C CE . LYS B 1 223 ? 43.433 22.008 6.817 1.00 169.85 ? 222 LYS B CE 1 ATOM 4772 N NZ . LYS B 1 223 ? 44.875 21.634 6.763 1.00 174.09 ? 222 LYS B NZ 1 ATOM 4773 N N . ILE B 1 224 ? 39.818 26.733 4.575 1.00 159.96 ? 223 ILE B N 1 ATOM 4774 C CA . ILE B 1 224 ? 38.570 26.790 3.802 1.00 156.85 ? 223 ILE B CA 1 ATOM 4775 C C . ILE B 1 224 ? 38.795 27.121 2.319 1.00 154.86 ? 223 ILE B C 1 ATOM 4776 O O . ILE B 1 224 ? 38.015 26.706 1.456 1.00 149.47 ? 223 ILE B O 1 ATOM 4777 C CB . ILE B 1 224 ? 37.563 27.794 4.427 1.00 157.27 ? 223 ILE B CB 1 ATOM 4778 C CG1 . ILE B 1 224 ? 36.157 27.621 3.844 1.00 155.04 ? 223 ILE B CG1 1 ATOM 4779 C CG2 . ILE B 1 224 ? 38.016 29.237 4.250 1.00 159.77 ? 223 ILE B CG2 1 ATOM 4780 C CD1 . ILE B 1 224 ? 35.532 26.274 4.132 1.00 155.28 ? 223 ILE B CD1 1 ATOM 4781 N N . ARG B 1 225 ? 39.863 27.864 2.037 1.00 158.10 ? 224 ARG B N 1 ATOM 4782 C CA . ARG B 1 225 ? 40.227 28.233 0.670 1.00 160.32 ? 224 ARG B CA 1 ATOM 4783 C C . ARG B 1 225 ? 40.283 27.015 -0.249 1.00 160.00 ? 224 ARG B C 1 ATOM 4784 O O . ARG B 1 225 ? 39.903 27.092 -1.420 1.00 158.70 ? 224 ARG B O 1 ATOM 4785 C CB . ARG B 1 225 ? 41.581 28.942 0.668 1.00 165.61 ? 224 ARG B CB 1 ATOM 4786 C CG . ARG B 1 225 ? 42.022 29.448 -0.696 1.00 168.37 ? 224 ARG B CG 1 ATOM 4787 C CD . ARG B 1 225 ? 43.374 30.133 -0.613 1.00 174.07 ? 224 ARG B CD 1 ATOM 4788 N NE . ARG B 1 225 ? 44.436 29.212 -0.209 1.00 177.15 ? 224 ARG B NE 1 ATOM 4789 C CZ . ARG B 1 225 ? 45.723 29.541 -0.099 1.00 181.42 ? 224 ARG B CZ 1 ATOM 4790 N NH1 . ARG B 1 225 ? 46.137 30.776 -0.370 1.00 183.87 ? 224 ARG B NH1 1 ATOM 4791 N NH2 . ARG B 1 225 ? 46.605 28.624 0.280 1.00 182.99 ? 224 ARG B NH2 1 ATOM 4792 N N . GLU B 1 226 ? 40.760 25.897 0.293 1.00 162.48 ? 225 GLU B N 1 ATOM 4793 C CA . GLU B 1 226 ? 40.882 24.646 -0.461 1.00 164.51 ? 225 GLU B CA 1 ATOM 4794 C C . GLU B 1 226 ? 39.548 24.232 -1.090 1.00 161.72 ? 225 GLU B C 1 ATOM 4795 O O . GLU B 1 226 ? 39.475 23.915 -2.281 1.00 161.15 ? 225 GLU B O 1 ATOM 4796 C CB . GLU B 1 226 ? 41.401 23.534 0.459 1.00 166.39 ? 225 GLU B CB 1 ATOM 4797 C CG . GLU B 1 226 ? 42.839 23.743 0.924 1.00 170.37 ? 225 GLU B CG 1 ATOM 4798 C CD . GLU B 1 226 ? 43.122 23.148 2.293 1.00 172.08 ? 225 GLU B CD 1 ATOM 4799 O OE1 . GLU B 1 226 ? 42.534 22.100 2.633 1.00 170.23 ? 225 GLU B OE1 1 ATOM 4800 O OE2 . GLU B 1 226 ? 43.944 23.731 3.032 1.00 175.57 ? 225 GLU B OE2 1 ATOM 4801 N N . GLN B 1 227 ? 38.492 24.252 -0.284 1.00 159.34 ? 226 GLN B N 1 ATOM 4802 C CA . GLN B 1 227 ? 37.154 23.919 -0.765 1.00 155.09 ? 226 GLN B CA 1 ATOM 4803 C C . GLN B 1 227 ? 36.642 24.961 -1.755 1.00 152.27 ? 226 GLN B C 1 ATOM 4804 O O . GLN B 1 227 ? 36.082 24.622 -2.801 1.00 147.74 ? 226 GLN B O 1 ATOM 4805 C CB . GLN B 1 227 ? 36.181 23.816 0.419 1.00 153.92 ? 226 GLN B CB 1 ATOM 4806 C CG . GLN B 1 227 ? 34.717 23.634 0.034 1.00 151.50 ? 226 GLN B CG 1 ATOM 4807 C CD . GLN B 1 227 ? 34.051 24.925 -0.413 1.00 150.67 ? 226 GLN B CD 1 ATOM 4808 O OE1 . GLN B 1 227 ? 33.517 25.009 -1.520 1.00 149.54 ? 226 GLN B OE1 1 ATOM 4809 N NE2 . GLN B 1 227 ? 34.085 25.943 0.444 1.00 151.31 ? 226 GLN B NE2 1 ATOM 4810 N N . GLN B 1 228 ? 36.830 26.230 -1.408 1.00 153.09 ? 227 GLN B N 1 ATOM 4811 C CA . GLN B 1 228 ? 36.304 27.333 -2.206 1.00 153.44 ? 227 GLN B CA 1 ATOM 4812 C C . GLN B 1 228 ? 36.869 27.320 -3.623 1.00 152.54 ? 227 GLN B C 1 ATOM 4813 O O . GLN B 1 228 ? 36.144 27.552 -4.589 1.00 150.49 ? 227 GLN B O 1 ATOM 4814 C CB . GLN B 1 228 ? 36.605 28.670 -1.526 1.00 157.94 ? 227 GLN B CB 1 ATOM 4815 C CG . GLN B 1 228 ? 35.871 28.863 -0.205 1.00 159.83 ? 227 GLN B CG 1 ATOM 4816 C CD . GLN B 1 228 ? 36.417 30.012 0.625 1.00 165.73 ? 227 GLN B CD 1 ATOM 4817 O OE1 . GLN B 1 228 ? 37.609 30.323 0.581 1.00 170.80 ? 227 GLN B OE1 1 ATOM 4818 N NE2 . GLN B 1 228 ? 35.542 30.646 1.397 1.00 167.12 ? 227 GLN B NE2 1 ATOM 4819 N N . ARG B 1 229 ? 38.162 27.038 -3.743 1.00 154.52 ? 228 ARG B N 1 ATOM 4820 C CA . ARG B 1 229 ? 38.803 26.930 -5.053 1.00 157.06 ? 228 ARG B CA 1 ATOM 4821 C C . ARG B 1 229 ? 38.198 25.820 -5.918 1.00 153.73 ? 228 ARG B C 1 ATOM 4822 O O . ARG B 1 229 ? 38.076 25.974 -7.137 1.00 153.97 ? 228 ARG B O 1 ATOM 4823 C CB . ARG B 1 229 ? 40.307 26.686 -4.890 1.00 162.00 ? 228 ARG B CB 1 ATOM 4824 C CG . ARG B 1 229 ? 41.081 27.910 -4.434 1.00 165.30 ? 228 ARG B CG 1 ATOM 4825 C CD . ARG B 1 229 ? 42.566 27.615 -4.307 1.00 169.16 ? 228 ARG B CD 1 ATOM 4826 N NE . ARG B 1 229 ? 43.333 28.815 -3.977 1.00 171.83 ? 228 ARG B NE 1 ATOM 4827 C CZ . ARG B 1 229 ? 44.660 28.859 -3.868 1.00 175.21 ? 228 ARG B CZ 1 ATOM 4828 N NH1 . ARG B 1 229 ? 45.393 27.768 -4.068 1.00 176.39 ? 228 ARG B NH1 1 ATOM 4829 N NH2 . ARG B 1 229 ? 45.261 30.005 -3.561 1.00 177.74 ? 228 ARG B NH2 1 ATOM 4830 N N . SER B 1 230 ? 37.819 24.716 -5.273 1.00 149.05 ? 229 SER B N 1 ATOM 4831 C CA . SER B 1 230 ? 37.307 23.528 -5.963 1.00 144.42 ? 229 SER B CA 1 ATOM 4832 C C . SER B 1 230 ? 35.962 23.751 -6.661 1.00 139.08 ? 229 SER B C 1 ATOM 4833 O O . SER B 1 230 ? 35.653 23.067 -7.640 1.00 135.03 ? 229 SER B O 1 ATOM 4834 C CB . SER B 1 230 ? 37.168 22.358 -4.985 1.00 143.69 ? 229 SER B CB 1 ATOM 4835 O OG . SER B 1 230 ? 35.973 22.457 -4.228 1.00 141.08 ? 229 SER B OG 1 ATOM 4836 N N . ALA B 1 231 ? 35.166 24.689 -6.146 1.00 136.80 ? 230 ALA B N 1 ATOM 4837 C CA . ALA B 1 231 ? 33.858 25.008 -6.727 1.00 134.56 ? 230 ALA B CA 1 ATOM 4838 C C . ALA B 1 231 ? 33.995 25.846 -7.999 1.00 136.60 ? 230 ALA B C 1 ATOM 4839 O O . ALA B 1 231 ? 34.495 26.972 -7.968 1.00 134.72 ? 230 ALA B O 1 ATOM 4840 C CB . ALA B 1 231 ? 32.989 25.735 -5.711 1.00 132.87 ? 230 ALA B CB 1 ATOM 4841 N N . VAL B 1 232 ? 33.528 25.288 -9.113 1.00 139.37 ? 231 VAL B N 1 ATOM 4842 C CA . VAL B 1 232 ? 33.588 25.961 -10.418 1.00 142.38 ? 231 VAL B CA 1 ATOM 4843 C C . VAL B 1 232 ? 32.878 27.314 -10.373 1.00 141.78 ? 231 VAL B C 1 ATOM 4844 O O . VAL B 1 232 ? 33.316 28.276 -10.999 1.00 141.51 ? 231 VAL B O 1 ATOM 4845 C CB . VAL B 1 232 ? 32.943 25.095 -11.530 1.00 142.62 ? 231 VAL B CB 1 ATOM 4846 C CG1 . VAL B 1 232 ? 32.888 25.855 -12.853 1.00 144.23 ? 231 VAL B CG1 1 ATOM 4847 C CG2 . VAL B 1 232 ? 33.705 23.787 -11.699 1.00 143.55 ? 231 VAL B CG2 1 ATOM 4848 N N . SER B 1 233 ? 31.777 27.371 -9.631 1.00 141.85 ? 232 SER B N 1 ATOM 4849 C CA . SER B 1 233 ? 30.997 28.594 -9.479 1.00 142.64 ? 232 SER B CA 1 ATOM 4850 C C . SER B 1 233 ? 31.829 29.782 -8.998 1.00 144.98 ? 232 SER B C 1 ATOM 4851 O O . SER B 1 233 ? 31.538 30.923 -9.343 1.00 147.37 ? 232 SER B O 1 ATOM 4852 C CB . SER B 1 233 ? 29.844 28.353 -8.502 1.00 141.82 ? 232 SER B CB 1 ATOM 4853 O OG . SER B 1 233 ? 30.315 27.817 -7.275 1.00 142.79 ? 232 SER B OG 1 ATOM 4854 N N . THR B 1 234 ? 32.857 29.517 -8.198 1.00 145.30 ? 233 THR B N 1 ATOM 4855 C CA . THR B 1 234 ? 33.741 30.574 -7.713 1.00 146.46 ? 233 THR B CA 1 ATOM 4856 C C . THR B 1 234 ? 34.469 31.278 -8.862 1.00 147.25 ? 233 THR B C 1 ATOM 4857 O O . THR B 1 234 ? 34.408 32.502 -8.997 1.00 146.43 ? 233 THR B O 1 ATOM 4858 C CB . THR B 1 234 ? 34.795 30.001 -6.744 1.00 148.98 ? 233 THR B CB 1 ATOM 4859 O OG1 . THR B 1 234 ? 34.173 29.071 -5.847 1.00 146.76 ? 233 THR B OG1 1 ATOM 4860 C CG2 . THR B 1 234 ? 35.455 31.115 -5.946 1.00 151.82 ? 233 THR B CG2 1 ATOM 4861 N N . SER B 1 235 ? 35.140 30.489 -9.694 1.00 148.21 ? 234 SER B N 1 ATOM 4862 C CA . SER B 1 235 ? 35.881 31.012 -10.841 1.00 151.05 ? 234 SER B CA 1 ATOM 4863 C C . SER B 1 235 ? 34.956 31.645 -11.889 1.00 151.54 ? 234 SER B C 1 ATOM 4864 O O . SER B 1 235 ? 35.329 32.606 -12.563 1.00 154.39 ? 234 SER B O 1 ATOM 4865 C CB . SER B 1 235 ? 36.711 29.890 -11.471 1.00 151.48 ? 234 SER B CB 1 ATOM 4866 O OG . SER B 1 235 ? 37.382 29.138 -10.471 1.00 150.86 ? 234 SER B OG 1 ATOM 4867 N N . TRP B 1 236 ? 33.748 31.102 -12.015 1.00 150.08 ? 235 TRP B N 1 ATOM 4868 C CA . TRP B 1 236 ? 32.741 31.632 -12.933 1.00 148.71 ? 235 TRP B CA 1 ATOM 4869 C C . TRP B 1 236 ? 32.330 33.072 -12.597 1.00 147.36 ? 235 TRP B C 1 ATOM 4870 O O . TRP B 1 236 ? 31.955 33.834 -13.487 1.00 144.42 ? 235 TRP B O 1 ATOM 4871 C CB . TRP B 1 236 ? 31.514 30.713 -12.922 1.00 147.33 ? 235 TRP B CB 1 ATOM 4872 C CG . TRP B 1 236 ? 30.444 31.103 -13.885 1.00 146.82 ? 235 TRP B CG 1 ATOM 4873 C CD1 . TRP B 1 236 ? 30.615 31.604 -15.139 1.00 147.97 ? 235 TRP B CD1 1 ATOM 4874 C CD2 . TRP B 1 236 ? 29.030 31.001 -13.679 1.00 145.64 ? 235 TRP B CD2 1 ATOM 4875 N NE1 . TRP B 1 236 ? 29.393 31.836 -15.726 1.00 147.10 ? 235 TRP B NE1 1 ATOM 4876 C CE2 . TRP B 1 236 ? 28.403 31.472 -14.851 1.00 145.43 ? 235 TRP B CE2 1 ATOM 4877 C CE3 . TRP B 1 236 ? 28.232 30.561 -12.613 1.00 144.34 ? 235 TRP B CE3 1 ATOM 4878 C CZ2 . TRP B 1 236 ? 27.009 31.517 -14.990 1.00 144.01 ? 235 TRP B CZ2 1 ATOM 4879 C CZ3 . TRP B 1 236 ? 26.846 30.606 -12.751 1.00 142.79 ? 235 TRP B CZ3 1 ATOM 4880 C CH2 . TRP B 1 236 ? 26.251 31.080 -13.932 1.00 142.63 ? 235 TRP B CH2 1 ATOM 4881 N N . LEU B 1 237 ? 32.408 33.439 -11.319 1.00 148.15 ? 236 LEU B N 1 ATOM 4882 C CA . LEU B 1 237 ? 32.002 34.772 -10.859 1.00 150.91 ? 236 LEU B CA 1 ATOM 4883 C C . LEU B 1 237 ? 33.120 35.822 -10.824 1.00 154.88 ? 236 LEU B C 1 ATOM 4884 O O . LEU B 1 237 ? 32.915 36.920 -10.298 1.00 155.80 ? 236 LEU B O 1 ATOM 4885 C CB . LEU B 1 237 ? 31.368 34.675 -9.466 1.00 151.44 ? 236 LEU B CB 1 ATOM 4886 C CG . LEU B 1 237 ? 30.025 33.951 -9.376 1.00 150.99 ? 236 LEU B CG 1 ATOM 4887 C CD1 . LEU B 1 237 ? 29.619 33.789 -7.917 1.00 150.16 ? 236 LEU B CD1 1 ATOM 4888 C CD2 . LEU B 1 237 ? 28.953 34.696 -10.160 1.00 151.20 ? 236 LEU B CD2 1 ATOM 4889 N N . LEU B 1 238 ? 34.290 35.507 -11.375 1.00 157.98 ? 237 LEU B N 1 ATOM 4890 C CA . LEU B 1 238 ? 35.333 36.519 -11.544 1.00 160.75 ? 237 LEU B CA 1 ATOM 4891 C C . LEU B 1 238 ? 34.821 37.642 -12.454 1.00 161.81 ? 237 LEU B C 1 ATOM 4892 O O . LEU B 1 238 ? 34.020 37.388 -13.356 1.00 162.90 ? 237 LEU B O 1 ATOM 4893 C CB . LEU B 1 238 ? 36.601 35.904 -12.141 1.00 162.21 ? 237 LEU B CB 1 ATOM 4894 C CG . LEU B 1 238 ? 37.435 35.048 -11.187 1.00 162.22 ? 237 LEU B CG 1 ATOM 4895 C CD1 . LEU B 1 238 ? 38.378 34.141 -11.960 1.00 162.80 ? 237 LEU B CD1 1 ATOM 4896 C CD2 . LEU B 1 238 ? 38.208 35.933 -10.222 1.00 164.67 ? 237 LEU B CD2 1 ATOM 4897 N N . PRO B 1 239 ? 35.273 38.887 -12.212 1.00 163.52 ? 238 PRO B N 1 ATOM 4898 C CA . PRO B 1 239 ? 34.877 40.048 -13.015 1.00 164.79 ? 238 PRO B CA 1 ATOM 4899 C C . PRO B 1 239 ? 34.996 39.850 -14.529 1.00 166.68 ? 238 PRO B C 1 ATOM 4900 O O . PRO B 1 239 ? 35.967 39.257 -15.002 1.00 164.69 ? 238 PRO B O 1 ATOM 4901 C CB . PRO B 1 239 ? 35.845 41.132 -12.546 1.00 167.81 ? 238 PRO B CB 1 ATOM 4902 C CG . PRO B 1 239 ? 36.124 40.783 -11.128 1.00 167.13 ? 238 PRO B CG 1 ATOM 4903 C CD . PRO B 1 239 ? 36.095 39.283 -11.052 1.00 164.89 ? 238 PRO B CD 1 ATOM 4904 N N . TYR B 1 240 ? 34.007 40.356 -15.265 1.00 170.79 ? 239 TYR B N 1 ATOM 4905 C CA . TYR B 1 240 ? 33.982 40.293 -16.731 1.00 177.66 ? 239 TYR B CA 1 ATOM 4906 C C . TYR B 1 240 ? 34.179 41.689 -17.339 1.00 184.95 ? 239 TYR B C 1 ATOM 4907 O O . TYR B 1 240 ? 33.752 42.696 -16.766 1.00 185.61 ? 239 TYR B O 1 ATOM 4908 C CB . TYR B 1 240 ? 32.649 39.710 -17.215 1.00 177.19 ? 239 TYR B CB 1 ATOM 4909 C CG . TYR B 1 240 ? 32.434 38.237 -16.908 1.00 176.83 ? 239 TYR B CG 1 ATOM 4910 C CD1 . TYR B 1 240 ? 31.885 37.824 -15.692 1.00 174.63 ? 239 TYR B CD1 1 ATOM 4911 C CD2 . TYR B 1 240 ? 32.751 37.258 -17.847 1.00 177.96 ? 239 TYR B CD2 1 ATOM 4912 C CE1 . TYR B 1 240 ? 31.675 36.481 -15.416 1.00 169.98 ? 239 TYR B CE1 1 ATOM 4913 C CE2 . TYR B 1 240 ? 32.544 35.914 -17.579 1.00 174.33 ? 239 TYR B CE2 1 ATOM 4914 C CZ . TYR B 1 240 ? 32.006 35.531 -16.365 1.00 170.25 ? 239 TYR B CZ 1 ATOM 4915 O OH . TYR B 1 240 ? 31.807 34.200 -16.103 1.00 165.53 ? 239 TYR B OH 1 ATOM 4916 N N . ASN B 1 241 ? 34.794 41.728 -18.518 1.00 192.94 ? 240 ASN B N 1 ATOM 4917 C CA . ASN B 1 241 ? 35.219 42.987 -19.150 1.00 202.62 ? 240 ASN B CA 1 ATOM 4918 C C . ASN B 1 241 ? 34.113 43.885 -19.705 1.00 206.59 ? 240 ASN B C 1 ATOM 4919 O O . ASN B 1 241 ? 34.348 45.052 -20.013 1.00 205.91 ? 240 ASN B O 1 ATOM 4920 C CB . ASN B 1 241 ? 36.228 42.701 -20.268 1.00 206.75 ? 240 ASN B CB 1 ATOM 4921 C CG . ASN B 1 241 ? 35.628 41.912 -21.424 1.00 205.92 ? 240 ASN B CG 1 ATOM 4922 O OD1 . ASN B 1 241 ? 34.406 41.844 -21.596 1.00 205.02 ? 240 ASN B OD1 1 ATOM 4923 N ND2 . ASN B 1 241 ? 36.505 41.304 -22.231 1.00 206.44 ? 240 ASN B ND2 1 ATOM 4924 N N . TYR B 1 242 ? 32.920 43.334 -19.871 1.00 210.87 ? 241 TYR B N 1 ATOM 4925 C CA . TYR B 1 242 ? 31.806 44.119 -20.382 1.00 215.34 ? 241 TYR B CA 1 ATOM 4926 C C . TYR B 1 242 ? 31.152 44.976 -19.293 1.00 210.50 ? 241 TYR B C 1 ATOM 4927 O O . TYR B 1 242 ? 30.437 45.935 -19.603 1.00 214.17 ? 241 TYR B O 1 ATOM 4928 C CB . TYR B 1 242 ? 30.765 43.219 -21.073 1.00 219.47 ? 241 TYR B CB 1 ATOM 4929 C CG . TYR B 1 242 ? 30.123 42.158 -20.193 1.00 225.18 ? 241 TYR B CG 1 ATOM 4930 C CD1 . TYR B 1 242 ? 29.035 42.463 -19.373 1.00 227.62 ? 241 TYR B CD1 1 ATOM 4931 C CD2 . TYR B 1 242 ? 30.588 40.842 -20.197 1.00 229.18 ? 241 TYR B CD2 1 ATOM 4932 C CE1 . TYR B 1 242 ? 28.440 41.494 -18.573 1.00 226.54 ? 241 TYR B CE1 1 ATOM 4933 C CE2 . TYR B 1 242 ? 29.999 39.868 -19.401 1.00 229.18 ? 241 TYR B CE2 1 ATOM 4934 C CZ . TYR B 1 242 ? 28.925 40.197 -18.590 1.00 226.76 ? 241 TYR B CZ 1 ATOM 4935 O OH . TYR B 1 242 ? 28.335 39.233 -17.797 1.00 220.25 ? 241 TYR B OH 1 ATOM 4936 N N . THR B 1 243 ? 31.399 44.627 -18.027 1.00 201.96 ? 242 THR B N 1 ATOM 4937 C CA . THR B 1 243 ? 30.872 45.385 -16.882 1.00 195.25 ? 242 THR B CA 1 ATOM 4938 C C . THR B 1 243 ? 31.957 46.218 -16.207 1.00 194.99 ? 242 THR B C 1 ATOM 4939 O O . THR B 1 243 ? 31.731 47.380 -15.867 1.00 196.06 ? 242 THR B O 1 ATOM 4940 C CB . THR B 1 243 ? 30.249 44.457 -15.818 1.00 190.78 ? 242 THR B CB 1 ATOM 4941 O OG1 . THR B 1 243 ? 29.191 43.693 -16.407 1.00 188.30 ? 242 THR B OG1 1 ATOM 4942 C CG2 . THR B 1 243 ? 29.688 45.264 -14.648 1.00 189.03 ? 242 THR B CG2 1 ATOM 4943 N N . TRP B 1 244 ? 33.121 45.609 -16.005 1.00 193.43 ? 243 TRP B N 1 ATOM 4944 C CA . TRP B 1 244 ? 34.266 46.284 -15.403 1.00 194.43 ? 243 TRP B CA 1 ATOM 4945 C C . TRP B 1 244 ? 35.192 46.806 -16.494 1.00 196.65 ? 243 TRP B C 1 ATOM 4946 O O . TRP B 1 244 ? 35.180 46.306 -17.620 1.00 197.20 ? 243 TRP B O 1 ATOM 4947 C CB . TRP B 1 244 ? 35.017 45.313 -14.491 1.00 192.49 ? 243 TRP B CB 1 ATOM 4948 C CG . TRP B 1 244 ? 34.155 44.771 -13.399 1.00 187.77 ? 243 TRP B CG 1 ATOM 4949 C CD1 . TRP B 1 244 ? 33.320 43.693 -13.467 1.00 184.48 ? 243 TRP B CD1 1 ATOM 4950 C CD2 . TRP B 1 244 ? 34.027 45.294 -12.075 1.00 186.28 ? 243 TRP B CD2 1 ATOM 4951 N NE1 . TRP B 1 244 ? 32.685 43.509 -12.263 1.00 182.05 ? 243 TRP B NE1 1 ATOM 4952 C CE2 . TRP B 1 244 ? 33.102 44.480 -11.391 1.00 182.29 ? 243 TRP B CE2 1 ATOM 4953 C CE3 . TRP B 1 244 ? 34.608 46.371 -11.399 1.00 190.07 ? 243 TRP B CE3 1 ATOM 4954 C CZ2 . TRP B 1 244 ? 32.745 44.710 -10.062 1.00 181.33 ? 243 TRP B CZ2 1 ATOM 4955 C CZ3 . TRP B 1 244 ? 34.254 46.598 -10.080 1.00 189.04 ? 243 TRP B CZ3 1 ATOM 4956 C CH2 . TRP B 1 244 ? 33.332 45.773 -9.427 1.00 184.15 ? 243 TRP B CH2 1 ATOM 4957 N N . SER B 1 245 ? 35.988 47.817 -16.160 1.00 196.88 ? 244 SER B N 1 ATOM 4958 C CA . SER B 1 245 ? 36.939 48.378 -17.111 1.00 199.13 ? 244 SER B CA 1 ATOM 4959 C C . SER B 1 245 ? 38.023 47.342 -17.411 1.00 198.26 ? 244 SER B C 1 ATOM 4960 O O . SER B 1 245 ? 38.548 46.716 -16.489 1.00 193.44 ? 244 SER B O 1 ATOM 4961 C CB . SER B 1 245 ? 37.573 49.651 -16.549 1.00 203.83 ? 244 SER B CB 1 ATOM 4962 O OG . SER B 1 245 ? 38.356 50.301 -17.532 1.00 209.68 ? 244 SER B OG 1 ATOM 4963 N N . PRO B 1 246 ? 38.362 47.148 -18.700 1.00 200.96 ? 245 PRO B N 1 ATOM 4964 C CA . PRO B 1 246 ? 39.440 46.208 -19.033 1.00 202.96 ? 245 PRO B CA 1 ATOM 4965 C C . PRO B 1 246 ? 40.792 46.513 -18.369 1.00 206.88 ? 245 PRO B C 1 ATOM 4966 O O . PRO B 1 246 ? 41.621 45.611 -18.206 1.00 203.88 ? 245 PRO B O 1 ATOM 4967 C CB . PRO B 1 246 ? 39.565 46.340 -20.556 1.00 204.30 ? 245 PRO B CB 1 ATOM 4968 C CG . PRO B 1 246 ? 38.236 46.827 -21.018 1.00 201.65 ? 245 PRO B CG 1 ATOM 4969 C CD . PRO B 1 246 ? 37.686 47.670 -19.904 1.00 200.77 ? 245 PRO B CD 1 ATOM 4970 N N . GLU B 1 247 ? 41.001 47.775 -17.995 1.00 212.40 ? 246 GLU B N 1 ATOM 4971 C CA . GLU B 1 247 ? 42.259 48.228 -17.402 1.00 217.19 ? 246 GLU B CA 1 ATOM 4972 C C . GLU B 1 247 ? 42.203 48.338 -15.868 1.00 213.05 ? 246 GLU B C 1 ATOM 4973 O O . GLU B 1 247 ? 43.182 48.735 -15.241 1.00 215.12 ? 246 GLU B O 1 ATOM 4974 C CB . GLU B 1 247 ? 42.646 49.598 -17.991 1.00 223.66 ? 246 GLU B CB 1 ATOM 4975 C CG . GLU B 1 247 ? 43.011 49.601 -19.476 1.00 228.03 ? 246 GLU B CG 1 ATOM 4976 C CD . GLU B 1 247 ? 41.849 49.273 -20.408 1.00 227.71 ? 246 GLU B CD 1 ATOM 4977 O OE1 . GLU B 1 247 ? 40.680 49.522 -20.045 1.00 228.69 ? 246 GLU B OE1 1 ATOM 4978 O OE2 . GLU B 1 247 ? 42.104 48.755 -21.516 1.00 229.66 ? 246 GLU B OE2 1 ATOM 4979 N N . LYS B 1 248 ? 41.073 47.990 -15.262 1.00 206.30 ? 247 LYS B N 1 ATOM 4980 C CA . LYS B 1 248 ? 40.914 48.166 -13.826 1.00 204.22 ? 247 LYS B CA 1 ATOM 4981 C C . LYS B 1 248 ? 41.808 47.202 -13.048 1.00 203.13 ? 247 LYS B C 1 ATOM 4982 O O . LYS B 1 248 ? 41.790 45.997 -13.291 1.00 200.69 ? 247 LYS B O 1 ATOM 4983 C CB . LYS B 1 248 ? 39.447 47.961 -13.427 1.00 200.11 ? 247 LYS B CB 1 ATOM 4984 C CG . LYS B 1 248 ? 39.163 48.086 -11.936 1.00 199.11 ? 247 LYS B CG 1 ATOM 4985 C CD . LYS B 1 248 ? 39.355 49.508 -11.426 1.00 202.67 ? 247 LYS B CD 1 ATOM 4986 C CE . LYS B 1 248 ? 39.347 49.556 -9.907 1.00 202.33 ? 247 LYS B CE 1 ATOM 4987 N NZ . LYS B 1 248 ? 38.120 48.944 -9.322 1.00 197.47 ? 247 LYS B NZ 1 ATOM 4988 N N . VAL B 1 249 ? 42.575 47.745 -12.105 1.00 204.24 ? 248 VAL B N 1 ATOM 4989 C CA . VAL B 1 249 ? 43.456 46.943 -11.253 1.00 203.98 ? 248 VAL B CA 1 ATOM 4990 C C . VAL B 1 249 ? 42.655 46.464 -10.044 1.00 201.77 ? 248 VAL B C 1 ATOM 4991 O O . VAL B 1 249 ? 42.148 47.280 -9.273 1.00 200.81 ? 248 VAL B O 1 ATOM 4992 C CB . VAL B 1 249 ? 44.664 47.772 -10.756 1.00 207.27 ? 248 VAL B CB 1 ATOM 4993 C CG1 . VAL B 1 249 ? 45.631 46.895 -9.969 1.00 207.77 ? 248 VAL B CG1 1 ATOM 4994 C CG2 . VAL B 1 249 ? 45.375 48.439 -11.927 1.00 210.03 ? 248 VAL B CG2 1 ATOM 4995 N N . PHE B 1 250 ? 42.532 45.149 -9.886 1.00 202.50 ? 249 PHE B N 1 ATOM 4996 C CA . PHE B 1 250 ? 41.774 44.576 -8.771 1.00 203.49 ? 249 PHE B CA 1 ATOM 4997 C C . PHE B 1 250 ? 42.677 44.186 -7.610 1.00 203.94 ? 249 PHE B C 1 ATOM 4998 O O . PHE B 1 250 ? 42.296 44.322 -6.445 1.00 202.37 ? 249 PHE B O 1 ATOM 4999 C CB . PHE B 1 250 ? 40.993 43.346 -9.232 1.00 204.16 ? 249 PHE B CB 1 ATOM 5000 C CG . PHE B 1 250 ? 39.851 43.663 -10.153 1.00 206.63 ? 249 PHE B CG 1 ATOM 5001 C CD1 . PHE B 1 250 ? 38.611 44.023 -9.640 1.00 206.98 ? 249 PHE B CD1 1 ATOM 5002 C CD2 . PHE B 1 250 ? 40.011 43.598 -11.530 1.00 208.47 ? 249 PHE B CD2 1 ATOM 5003 C CE1 . PHE B 1 250 ? 37.552 44.314 -10.485 1.00 205.92 ? 249 PHE B CE1 1 ATOM 5004 C CE2 . PHE B 1 250 ? 38.957 43.887 -12.380 1.00 207.15 ? 249 PHE B CE2 1 ATOM 5005 C CZ . PHE B 1 250 ? 37.725 44.246 -11.857 1.00 205.70 ? 249 PHE B CZ 1 ATOM 5006 N N . VAL B 1 251 ? 43.865 43.682 -7.932 1.00 205.74 ? 250 VAL B N 1 ATOM 5007 C CA . VAL B 1 251 ? 44.786 43.184 -6.914 1.00 207.81 ? 250 VAL B CA 1 ATOM 5008 C C . VAL B 1 251 ? 46.190 43.723 -7.138 1.00 213.58 ? 250 VAL B C 1 ATOM 5009 O O . VAL B 1 251 ? 46.746 43.607 -8.234 1.00 216.68 ? 250 VAL B O 1 ATOM 5010 C CB . VAL B 1 251 ? 44.833 41.642 -6.887 1.00 204.66 ? 250 VAL B CB 1 ATOM 5011 C CG1 . VAL B 1 251 ? 45.847 41.150 -5.858 1.00 206.54 ? 250 VAL B CG1 1 ATOM 5012 C CG2 . VAL B 1 251 ? 43.451 41.077 -6.592 1.00 200.41 ? 250 VAL B CG2 1 ATOM 5013 N N . GLN B 1 252 ? 46.747 44.316 -6.083 1.00 215.26 ? 251 GLN B N 1 ATOM 5014 C CA . GLN B 1 252 ? 48.127 44.784 -6.082 1.00 217.68 ? 251 GLN B CA 1 ATOM 5015 C C . GLN B 1 252 ? 48.932 43.956 -5.079 1.00 218.33 ? 251 GLN B C 1 ATOM 5016 O O . GLN B 1 252 ? 48.470 43.698 -3.965 1.00 216.09 ? 251 GLN B O 1 ATOM 5017 C CB . GLN B 1 252 ? 48.193 46.272 -5.712 1.00 219.09 ? 251 GLN B CB 1 ATOM 5018 C CG . GLN B 1 252 ? 47.668 47.224 -6.786 1.00 217.16 ? 251 GLN B CG 1 ATOM 5019 C CD . GLN B 1 252 ? 46.210 47.612 -6.605 1.00 211.70 ? 251 GLN B CD 1 ATOM 5020 O OE1 . GLN B 1 252 ? 45.401 46.833 -6.101 1.00 209.09 ? 251 GLN B OE1 1 ATOM 5021 N NE2 . GLN B 1 252 ? 45.866 48.825 -7.030 1.00 210.82 ? 251 GLN B NE2 1 ATOM 5022 N N . THR B 1 253 ? 50.128 43.538 -5.489 1.00 221.09 ? 252 THR B N 1 ATOM 5023 C CA . THR B 1 253 ? 51.052 42.805 -4.618 1.00 223.82 ? 252 THR B CA 1 ATOM 5024 C C . THR B 1 253 ? 52.384 43.558 -4.652 1.00 230.88 ? 252 THR B C 1 ATOM 5025 O O . THR B 1 253 ? 52.519 44.528 -5.403 1.00 232.46 ? 252 THR B O 1 ATOM 5026 C CB . THR B 1 253 ? 51.252 41.352 -5.111 1.00 221.77 ? 252 THR B CB 1 ATOM 5027 O OG1 . THR B 1 253 ? 52.160 41.330 -6.220 1.00 224.98 ? 252 THR B OG1 1 ATOM 5028 C CG2 . THR B 1 253 ? 49.927 40.731 -5.521 1.00 216.47 ? 252 THR B CG2 1 ATOM 5029 N N . PRO B 1 254 ? 53.375 43.121 -3.850 1.00 235.53 ? 253 PRO B N 1 ATOM 5030 C CA . PRO B 1 254 ? 54.651 43.842 -3.850 1.00 241.36 ? 253 PRO B CA 1 ATOM 5031 C C . PRO B 1 254 ? 55.381 43.825 -5.199 1.00 243.63 ? 253 PRO B C 1 ATOM 5032 O O . PRO B 1 254 ? 56.163 44.734 -5.480 1.00 248.68 ? 253 PRO B O 1 ATOM 5033 C CB . PRO B 1 254 ? 55.479 43.103 -2.785 1.00 243.57 ? 253 PRO B CB 1 ATOM 5034 C CG . PRO B 1 254 ? 54.495 42.325 -1.979 1.00 238.93 ? 253 PRO B CG 1 ATOM 5035 C CD . PRO B 1 254 ? 53.412 41.960 -2.945 1.00 234.18 ? 253 PRO B CD 1 ATOM 5036 N N . THR B 1 255 ? 55.120 42.806 -6.020 1.00 239.91 ? 254 THR B N 1 ATOM 5037 C CA . THR B 1 255 ? 55.831 42.614 -7.285 1.00 240.23 ? 254 THR B CA 1 ATOM 5038 C C . THR B 1 255 ? 55.015 42.929 -8.549 1.00 236.28 ? 254 THR B C 1 ATOM 5039 O O . THR B 1 255 ? 55.581 43.353 -9.557 1.00 239.24 ? 254 THR B O 1 ATOM 5040 C CB . THR B 1 255 ? 56.333 41.159 -7.401 1.00 239.51 ? 254 THR B CB 1 ATOM 5041 O OG1 . THR B 1 255 ? 55.226 40.254 -7.297 1.00 233.59 ? 254 THR B OG1 1 ATOM 5042 C CG2 . THR B 1 255 ? 57.343 40.848 -6.303 1.00 242.47 ? 254 THR B CG2 1 ATOM 5043 N N . ILE B 1 256 ? 53.699 42.731 -8.501 1.00 228.53 ? 255 ILE B N 1 ATOM 5044 C CA . ILE B 1 256 ? 52.894 42.791 -9.720 1.00 223.52 ? 255 ILE B CA 1 ATOM 5045 C C . ILE B 1 256 ? 51.448 43.225 -9.456 1.00 219.08 ? 255 ILE B C 1 ATOM 5046 O O . ILE B 1 256 ? 50.949 43.137 -8.326 1.00 215.98 ? 255 ILE B O 1 ATOM 5047 C CB . ILE B 1 256 ? 52.930 41.419 -10.444 1.00 220.21 ? 255 ILE B CB 1 ATOM 5048 C CG1 . ILE B 1 256 ? 52.567 41.551 -11.927 1.00 218.76 ? 255 ILE B CG1 1 ATOM 5049 C CG2 . ILE B 1 256 ? 52.040 40.402 -9.742 1.00 215.35 ? 255 ILE B CG2 1 ATOM 5050 C CD1 . ILE B 1 256 ? 52.757 40.271 -12.714 1.00 217.84 ? 255 ILE B CD1 1 ATOM 5051 N N . ASN B 1 257 ? 50.804 43.725 -10.510 1.00 218.76 ? 256 ASN B N 1 ATOM 5052 C CA . ASN B 1 257 ? 49.370 44.012 -10.513 1.00 216.40 ? 256 ASN B CA 1 ATOM 5053 C C . ASN B 1 257 ? 48.581 42.881 -11.147 1.00 213.08 ? 256 ASN B C 1 ATOM 5054 O O . ASN B 1 257 ? 49.139 42.032 -11.844 1.00 215.20 ? 256 ASN B O 1 ATOM 5055 C CB . ASN B 1 257 ? 49.085 45.273 -11.327 1.00 218.75 ? 256 ASN B CB 1 ATOM 5056 C CG . ASN B 1 257 ? 49.540 46.530 -10.633 1.00 224.44 ? 256 ASN B CG 1 ATOM 5057 O OD1 . ASN B 1 257 ? 49.552 46.611 -9.404 1.00 224.06 ? 256 ASN B OD1 1 ATOM 5058 N ND2 . ASN B 1 257 ? 49.899 47.541 -11.425 1.00 231.00 ? 256 ASN B ND2 1 ATOM 5059 N N . TYR B 1 258 ? 47.272 42.895 -10.916 1.00 207.73 ? 257 TYR B N 1 ATOM 5060 C CA . TYR B 1 258 ? 46.359 41.989 -11.596 1.00 201.25 ? 257 TYR B CA 1 ATOM 5061 C C . TYR B 1 258 ? 45.083 42.713 -12.015 1.00 200.43 ? 257 TYR B C 1 ATOM 5062 O O . TYR B 1 258 ? 44.348 43.249 -11.171 1.00 197.60 ? 257 TYR B O 1 ATOM 5063 C CB . TYR B 1 258 ? 46.028 40.792 -10.710 1.00 195.53 ? 257 TYR B CB 1 ATOM 5064 C CG . TYR B 1 258 ? 47.222 39.911 -10.419 1.00 196.27 ? 257 TYR B CG 1 ATOM 5065 C CD1 . TYR B 1 258 ? 47.710 39.029 -11.380 1.00 196.84 ? 257 TYR B CD1 1 ATOM 5066 C CD2 . TYR B 1 258 ? 47.869 39.963 -9.187 1.00 196.01 ? 257 TYR B CD2 1 ATOM 5067 C CE1 . TYR B 1 258 ? 48.804 38.219 -11.121 1.00 197.88 ? 257 TYR B CE1 1 ATOM 5068 C CE2 . TYR B 1 258 ? 48.963 39.157 -8.918 1.00 197.29 ? 257 TYR B CE2 1 ATOM 5069 C CZ . TYR B 1 258 ? 49.426 38.287 -9.887 1.00 197.97 ? 257 TYR B CZ 1 ATOM 5070 O OH . TYR B 1 258 ? 50.510 37.486 -9.621 1.00 198.72 ? 257 TYR B OH 1 ATOM 5071 N N . THR B 1 259 ? 44.864 42.750 -13.332 1.00 203.00 ? 258 THR B N 1 ATOM 5072 C CA . THR B 1 259 ? 43.601 43.179 -13.935 1.00 202.60 ? 258 THR B CA 1 ATOM 5073 C C . THR B 1 259 ? 42.847 41.933 -14.394 1.00 201.19 ? 258 THR B C 1 ATOM 5074 O O . THR B 1 259 ? 43.354 40.814 -14.302 1.00 201.77 ? 258 THR B O 1 ATOM 5075 C CB . THR B 1 259 ? 43.827 44.091 -15.164 1.00 204.96 ? 258 THR B CB 1 ATOM 5076 O OG1 . THR B 1 259 ? 44.471 43.352 -16.211 1.00 205.76 ? 258 THR B OG1 1 ATOM 5077 C CG2 . THR B 1 259 ? 44.675 45.299 -14.799 1.00 208.74 ? 258 THR B CG2 1 ATOM 5078 N N . LEU B 1 260 ? 41.638 42.132 -14.902 1.00 201.24 ? 259 LEU B N 1 ATOM 5079 C CA . LEU B 1 260 ? 40.841 41.030 -15.437 1.00 200.40 ? 259 LEU B CA 1 ATOM 5080 C C . LEU B 1 260 ? 41.474 40.321 -16.644 1.00 201.30 ? 259 LEU B C 1 ATOM 5081 O O . LEU B 1 260 ? 41.074 39.209 -16.997 1.00 201.03 ? 259 LEU B O 1 ATOM 5082 C CB . LEU B 1 260 ? 39.429 41.523 -15.788 1.00 200.01 ? 259 LEU B CB 1 ATOM 5083 C CG . LEU B 1 260 ? 39.287 42.672 -16.801 1.00 203.94 ? 259 LEU B CG 1 ATOM 5084 C CD1 . LEU B 1 260 ? 39.205 42.156 -18.232 1.00 205.28 ? 259 LEU B CD1 1 ATOM 5085 C CD2 . LEU B 1 260 ? 38.061 43.514 -16.473 1.00 202.80 ? 259 LEU B CD2 1 ATOM 5086 N N . ARG B 1 261 ? 42.455 40.966 -17.271 1.00 202.74 ? 260 ARG B N 1 ATOM 5087 C CA . ARG B 1 261 ? 43.191 40.359 -18.375 1.00 203.49 ? 260 ARG B CA 1 ATOM 5088 C C . ARG B 1 261 ? 44.404 39.542 -17.907 1.00 203.84 ? 260 ARG B C 1 ATOM 5089 O O . ARG B 1 261 ? 45.115 38.972 -18.736 1.00 206.60 ? 260 ARG B O 1 ATOM 5090 C CB . ARG B 1 261 ? 43.636 41.440 -19.363 1.00 207.50 ? 260 ARG B CB 1 ATOM 5091 C CG . ARG B 1 261 ? 42.490 42.255 -19.950 1.00 207.15 ? 260 ARG B CG 1 ATOM 5092 C CD . ARG B 1 261 ? 42.948 43.100 -21.152 1.00 212.10 ? 260 ARG B CD 1 ATOM 5093 N NE . ARG B 1 261 ? 43.005 44.512 -20.790 1.00 216.37 ? 260 ARG B NE 1 ATOM 5094 C CZ . ARG B 1 261 ? 44.022 45.113 -20.170 1.00 221.99 ? 260 ARG B CZ 1 ATOM 5095 N NH1 . ARG B 1 261 ? 45.121 44.448 -19.822 1.00 224.36 ? 260 ARG B NH1 1 ATOM 5096 N NH2 . ARG B 1 261 ? 43.939 46.408 -19.894 1.00 225.39 ? 260 ARG B NH2 1 ATOM 5097 N N . ASP B 1 262 ? 44.625 39.468 -16.591 1.00 202.01 ? 261 ASP B N 1 ATOM 5098 C CA . ASP B 1 262 ? 45.795 38.774 -16.024 1.00 202.50 ? 261 ASP B CA 1 ATOM 5099 C C . ASP B 1 262 ? 45.427 37.511 -15.220 1.00 199.45 ? 261 ASP B C 1 ATOM 5100 O O . ASP B 1 262 ? 46.186 37.075 -14.343 1.00 202.50 ? 261 ASP B O 1 ATOM 5101 C CB . ASP B 1 262 ? 46.591 39.740 -15.130 1.00 203.52 ? 261 ASP B CB 1 ATOM 5102 C CG . ASP B 1 262 ? 47.212 40.889 -15.907 1.00 205.44 ? 261 ASP B CG 1 ATOM 5103 O OD1 . ASP B 1 262 ? 47.855 40.634 -16.947 1.00 206.84 ? 261 ASP B OD1 1 ATOM 5104 O OD2 . ASP B 1 262 ? 47.071 42.049 -15.468 1.00 205.01 ? 261 ASP B OD2 1 ATOM 5105 N N . TYR B 1 263 ? 44.280 36.908 -15.530 1.00 193.64 ? 262 TYR B N 1 ATOM 5106 C CA . TYR B 1 263 ? 43.813 35.739 -14.790 1.00 188.68 ? 262 TYR B CA 1 ATOM 5107 C C . TYR B 1 263 ? 44.758 34.537 -14.924 1.00 188.19 ? 262 TYR B C 1 ATOM 5108 O O . TYR B 1 263 ? 44.950 33.790 -13.963 1.00 187.34 ? 262 TYR B O 1 ATOM 5109 C CB . TYR B 1 263 ? 42.385 35.346 -15.208 1.00 184.82 ? 262 TYR B CB 1 ATOM 5110 C CG . TYR B 1 263 ? 41.277 36.300 -14.767 1.00 181.90 ? 262 TYR B CG 1 ATOM 5111 C CD1 . TYR B 1 263 ? 41.258 36.851 -13.482 1.00 180.80 ? 262 TYR B CD1 1 ATOM 5112 C CD2 . TYR B 1 263 ? 40.222 36.616 -15.626 1.00 178.82 ? 262 TYR B CD2 1 ATOM 5113 C CE1 . TYR B 1 263 ? 40.242 37.708 -13.083 1.00 177.86 ? 262 TYR B CE1 1 ATOM 5114 C CE2 . TYR B 1 263 ? 39.201 37.470 -15.231 1.00 176.12 ? 262 TYR B CE2 1 ATOM 5115 C CZ . TYR B 1 263 ? 39.216 38.012 -13.961 1.00 175.96 ? 262 TYR B CZ 1 ATOM 5116 O OH . TYR B 1 263 ? 38.208 38.862 -13.563 1.00 173.71 ? 262 TYR B OH 1 ATOM 5117 N N . ARG B 1 264 ? 45.350 34.342 -16.100 1.00 188.02 ? 263 ARG B N 1 ATOM 5118 C CA . ARG B 1 264 ? 46.265 33.218 -16.279 1.00 188.31 ? 263 ARG B CA 1 ATOM 5119 C C . ARG B 1 264 ? 47.456 33.331 -15.328 1.00 188.75 ? 263 ARG B C 1 ATOM 5120 O O . ARG B 1 264 ? 47.801 32.358 -14.657 1.00 187.02 ? 263 ARG B O 1 ATOM 5121 C CB . ARG B 1 264 ? 46.739 33.098 -17.728 1.00 191.53 ? 263 ARG B CB 1 ATOM 5122 C CG . ARG B 1 264 ? 47.374 31.749 -18.037 1.00 193.56 ? 263 ARG B CG 1 ATOM 5123 C CD . ARG B 1 264 ? 47.512 31.517 -19.532 1.00 196.99 ? 263 ARG B CD 1 ATOM 5124 N NE . ARG B 1 264 ? 48.462 32.440 -20.153 1.00 202.88 ? 263 ARG B NE 1 ATOM 5125 C CZ . ARG B 1 264 ? 49.787 32.286 -20.164 1.00 208.44 ? 263 ARG B CZ 1 ATOM 5126 N NH1 . ARG B 1 264 ? 50.365 31.238 -19.579 1.00 209.96 ? 263 ARG B NH1 1 ATOM 5127 N NH2 . ARG B 1 264 ? 50.548 33.194 -20.765 1.00 212.16 ? 263 ARG B NH2 1 ATOM 5128 N N . LYS B 1 265 ? 48.056 34.523 -15.261 1.00 189.68 ? 264 LYS B N 1 ATOM 5129 C CA . LYS B 1 265 ? 49.135 34.822 -14.303 1.00 191.86 ? 264 LYS B CA 1 ATOM 5130 C C . LYS B 1 265 ? 48.701 34.566 -12.866 1.00 190.37 ? 264 LYS B C 1 ATOM 5131 O O . LYS B 1 265 ? 49.435 33.954 -12.087 1.00 190.58 ? 264 LYS B O 1 ATOM 5132 C CB . LYS B 1 265 ? 49.559 36.294 -14.386 1.00 193.39 ? 264 LYS B CB 1 ATOM 5133 C CG . LYS B 1 265 ? 50.462 36.657 -15.544 1.00 196.10 ? 264 LYS B CG 1 ATOM 5134 C CD . LYS B 1 265 ? 50.960 38.082 -15.376 1.00 199.22 ? 264 LYS B CD 1 ATOM 5135 C CE . LYS B 1 265 ? 51.825 38.512 -16.546 1.00 204.66 ? 264 LYS B CE 1 ATOM 5136 N NZ . LYS B 1 265 ? 52.325 39.907 -16.397 1.00 209.50 ? 264 LYS B NZ 1 ATOM 5137 N N . PHE B 1 266 ? 47.523 35.084 -12.521 1.00 189.67 ? 265 PHE B N 1 ATOM 5138 C CA . PHE B 1 266 ? 46.965 34.954 -11.175 1.00 190.78 ? 265 PHE B CA 1 ATOM 5139 C C . PHE B 1 266 ? 46.901 33.490 -10.750 1.00 192.81 ? 265 PHE B C 1 ATOM 5140 O O . PHE B 1 266 ? 47.419 33.120 -9.693 1.00 194.18 ? 265 PHE B O 1 ATOM 5141 C CB . PHE B 1 266 ? 45.565 35.585 -11.117 1.00 187.94 ? 265 PHE B CB 1 ATOM 5142 C CG . PHE B 1 266 ? 44.826 35.331 -9.827 1.00 186.82 ? 265 PHE B CG 1 ATOM 5143 C CD1 . PHE B 1 266 ? 45.064 36.113 -8.704 1.00 187.71 ? 265 PHE B CD1 1 ATOM 5144 C CD2 . PHE B 1 266 ? 43.879 34.315 -9.739 1.00 185.69 ? 265 PHE B CD2 1 ATOM 5145 C CE1 . PHE B 1 266 ? 44.382 35.882 -7.518 1.00 185.79 ? 265 PHE B CE1 1 ATOM 5146 C CE2 . PHE B 1 266 ? 43.195 34.078 -8.554 1.00 183.57 ? 265 PHE B CE2 1 ATOM 5147 C CZ . PHE B 1 266 ? 43.446 34.864 -7.442 1.00 183.33 ? 265 PHE B CZ 1 ATOM 5148 N N . PHE B 1 267 ? 46.285 32.662 -11.590 1.00 195.83 ? 266 PHE B N 1 ATOM 5149 C CA . PHE B 1 267 ? 46.114 31.244 -11.265 1.00 198.68 ? 266 PHE B CA 1 ATOM 5150 C C . PHE B 1 267 ? 47.443 30.506 -11.160 1.00 200.95 ? 266 PHE B C 1 ATOM 5151 O O . PHE B 1 267 ? 47.616 29.658 -10.281 1.00 202.52 ? 266 PHE B O 1 ATOM 5152 C CB . PHE B 1 267 ? 45.201 30.540 -12.274 1.00 199.74 ? 266 PHE B CB 1 ATOM 5153 C CG . PHE B 1 267 ? 43.734 30.751 -12.014 1.00 198.85 ? 266 PHE B CG 1 ATOM 5154 C CD1 . PHE B 1 267 ? 43.158 30.328 -10.821 1.00 197.13 ? 266 PHE B CD1 1 ATOM 5155 C CD2 . PHE B 1 267 ? 42.927 31.365 -12.964 1.00 199.78 ? 266 PHE B CD2 1 ATOM 5156 C CE1 . PHE B 1 267 ? 41.809 30.524 -10.576 1.00 195.07 ? 266 PHE B CE1 1 ATOM 5157 C CE2 . PHE B 1 267 ? 41.575 31.557 -12.727 1.00 197.19 ? 266 PHE B CE2 1 ATOM 5158 C CZ . PHE B 1 267 ? 41.015 31.136 -11.532 1.00 195.12 ? 266 PHE B CZ 1 ATOM 5159 N N . GLN B 1 268 ? 48.379 30.834 -12.046 1.00 201.27 ? 267 GLN B N 1 ATOM 5160 C CA . GLN B 1 268 ? 49.711 30.246 -11.978 1.00 202.72 ? 267 GLN B CA 1 ATOM 5161 C C . GLN B 1 268 ? 50.431 30.681 -10.703 1.00 203.43 ? 267 GLN B C 1 ATOM 5162 O O . GLN B 1 268 ? 51.025 29.851 -10.016 1.00 202.22 ? 267 GLN B O 1 ATOM 5163 C CB . GLN B 1 268 ? 50.528 30.581 -13.230 1.00 205.63 ? 267 GLN B CB 1 ATOM 5164 C CG . GLN B 1 268 ? 50.042 29.838 -14.469 1.00 204.12 ? 267 GLN B CG 1 ATOM 5165 C CD . GLN B 1 268 ? 50.878 30.105 -15.707 1.00 206.85 ? 267 GLN B CD 1 ATOM 5166 O OE1 . GLN B 1 268 ? 51.900 30.788 -15.652 1.00 211.07 ? 267 GLN B OE1 1 ATOM 5167 N NE2 . GLN B 1 268 ? 50.446 29.556 -16.837 1.00 205.10 ? 267 GLN B NE2 1 ATOM 5168 N N . ASP B 1 269 ? 50.329 31.966 -10.369 1.00 204.18 ? 268 ASP B N 1 ATOM 5169 C CA . ASP B 1 269 ? 51.059 32.544 -9.234 1.00 207.51 ? 268 ASP B CA 1 ATOM 5170 C C . ASP B 1 269 ? 50.549 32.089 -7.866 1.00 203.13 ? 268 ASP B C 1 ATOM 5171 O O . ASP B 1 269 ? 51.328 31.995 -6.914 1.00 204.83 ? 268 ASP B O 1 ATOM 5172 C CB . ASP B 1 269 ? 51.041 34.079 -9.308 1.00 211.77 ? 268 ASP B CB 1 ATOM 5173 C CG . ASP B 1 269 ? 51.896 34.626 -10.446 1.00 218.51 ? 268 ASP B CG 1 ATOM 5174 O OD1 . ASP B 1 269 ? 52.244 33.856 -11.367 1.00 222.44 ? 268 ASP B OD1 1 ATOM 5175 O OD2 . ASP B 1 269 ? 52.217 35.834 -10.423 1.00 222.86 ? 268 ASP B OD2 1 ATOM 5176 N N . ILE B 1 270 ? 49.251 31.817 -7.762 1.00 197.63 ? 269 ILE B N 1 ATOM 5177 C CA . ILE B 1 270 ? 48.672 31.330 -6.506 1.00 194.79 ? 269 ILE B CA 1 ATOM 5178 C C . ILE B 1 270 ? 48.699 29.805 -6.386 1.00 192.80 ? 269 ILE B C 1 ATOM 5179 O O . ILE B 1 270 ? 48.305 29.260 -5.354 1.00 190.43 ? 269 ILE B O 1 ATOM 5180 C CB . ILE B 1 270 ? 47.240 31.872 -6.262 1.00 191.54 ? 269 ILE B CB 1 ATOM 5181 C CG1 . ILE B 1 270 ? 46.247 31.386 -7.330 1.00 188.87 ? 269 ILE B CG1 1 ATOM 5182 C CG2 . ILE B 1 270 ? 47.253 33.391 -6.186 1.00 193.31 ? 269 ILE B CG2 1 ATOM 5183 C CD1 . ILE B 1 270 ? 45.198 30.434 -6.802 1.00 185.07 ? 269 ILE B CD1 1 ATOM 5184 N N . GLY B 1 271 ? 49.164 29.127 -7.435 1.00 193.69 ? 270 GLY B N 1 ATOM 5185 C CA . GLY B 1 271 ? 49.334 27.676 -7.417 1.00 194.37 ? 270 GLY B CA 1 ATOM 5186 C C . GLY B 1 271 ? 48.040 26.903 -7.606 1.00 191.47 ? 270 GLY B C 1 ATOM 5187 O O . GLY B 1 271 ? 47.814 25.885 -6.947 1.00 190.02 ? 270 GLY B O 1 ATOM 5188 N N . PHE B 1 272 ? 47.188 27.381 -8.511 1.00 190.55 ? 271 PHE B N 1 ATOM 5189 C CA . PHE B 1 272 ? 45.930 26.703 -8.813 1.00 186.85 ? 271 PHE B CA 1 ATOM 5190 C C . PHE B 1 272 ? 45.627 26.800 -10.305 1.00 185.88 ? 271 PHE B C 1 ATOM 5191 O O . PHE B 1 272 ? 44.723 27.518 -10.728 1.00 180.72 ? 271 PHE B O 1 ATOM 5192 C CB . PHE B 1 272 ? 44.791 27.297 -7.978 1.00 184.40 ? 271 PHE B CB 1 ATOM 5193 C CG . PHE B 1 272 ? 43.521 26.493 -8.020 1.00 182.38 ? 271 PHE B CG 1 ATOM 5194 C CD1 . PHE B 1 272 ? 43.501 25.176 -7.577 1.00 182.45 ? 271 PHE B CD1 1 ATOM 5195 C CD2 . PHE B 1 272 ? 42.340 27.058 -8.486 1.00 180.73 ? 271 PHE B CD2 1 ATOM 5196 C CE1 . PHE B 1 272 ? 42.332 24.433 -7.609 1.00 180.36 ? 271 PHE B CE1 1 ATOM 5197 C CE2 . PHE B 1 272 ? 41.168 26.321 -8.521 1.00 179.41 ? 271 PHE B CE2 1 ATOM 5198 C CZ . PHE B 1 272 ? 41.164 25.006 -8.081 1.00 179.32 ? 271 PHE B CZ 1 ATOM 5199 N N . GLU B 1 273 ? 46.393 26.055 -11.097 1.00 190.14 ? 272 GLU B N 1 ATOM 5200 C CA . GLU B 1 273 ? 46.243 26.065 -12.553 1.00 192.84 ? 272 GLU B CA 1 ATOM 5201 C C . GLU B 1 273 ? 44.870 25.568 -13.007 1.00 187.58 ? 272 GLU B C 1 ATOM 5202 O O . GLU B 1 273 ? 44.361 26.007 -14.036 1.00 184.72 ? 272 GLU B O 1 ATOM 5203 C CB . GLU B 1 273 ? 47.350 25.240 -13.226 1.00 200.59 ? 272 GLU B CB 1 ATOM 5204 C CG . GLU B 1 273 ? 48.754 25.805 -13.024 1.00 208.65 ? 272 GLU B CG 1 ATOM 5205 C CD . GLU B 1 273 ? 49.788 25.225 -13.980 1.00 215.30 ? 272 GLU B CD 1 ATOM 5206 O OE1 . GLU B 1 273 ? 49.548 25.233 -15.206 1.00 217.92 ? 272 GLU B OE1 1 ATOM 5207 O OE2 . GLU B 1 273 ? 50.857 24.778 -13.509 1.00 220.37 ? 272 GLU B OE2 1 ATOM 5208 N N . ASP B 1 274 ? 44.268 24.667 -12.232 1.00 184.72 ? 273 ASP B N 1 ATOM 5209 C CA . ASP B 1 274 ? 42.922 24.160 -12.524 1.00 181.15 ? 273 ASP B CA 1 ATOM 5210 C C . ASP B 1 274 ? 41.900 25.289 -12.657 1.00 178.10 ? 273 ASP B C 1 ATOM 5211 O O . ASP B 1 274 ? 40.979 25.216 -13.471 1.00 176.00 ? 273 ASP B O 1 ATOM 5212 C CB . ASP B 1 274 ? 42.452 23.211 -11.416 1.00 179.81 ? 273 ASP B CB 1 ATOM 5213 C CG . ASP B 1 274 ? 43.317 21.972 -11.292 1.00 182.52 ? 273 ASP B CG 1 ATOM 5214 O OD1 . ASP B 1 274 ? 44.553 22.087 -11.437 1.00 185.84 ? 273 ASP B OD1 1 ATOM 5215 O OD2 . ASP B 1 274 ? 42.757 20.885 -11.036 1.00 181.94 ? 273 ASP B OD2 1 ATOM 5216 N N . GLY B 1 275 ? 42.061 26.326 -11.845 1.00 177.30 ? 274 GLY B N 1 ATOM 5217 C CA . GLY B 1 275 ? 41.140 27.449 -11.861 1.00 175.41 ? 274 GLY B CA 1 ATOM 5218 C C . GLY B 1 275 ? 41.108 28.188 -13.187 1.00 175.79 ? 274 GLY B C 1 ATOM 5219 O O . GLY B 1 275 ? 40.053 28.671 -13.602 1.00 172.64 ? 274 GLY B O 1 ATOM 5220 N N . TRP B 1 276 ? 42.263 28.287 -13.844 1.00 178.09 ? 275 TRP B N 1 ATOM 5221 C CA . TRP B 1 276 ? 42.360 28.913 -15.169 1.00 178.75 ? 275 TRP B CA 1 ATOM 5222 C C . TRP B 1 276 ? 41.551 28.100 -16.178 1.00 175.57 ? 275 TRP B C 1 ATOM 5223 O O . TRP B 1 276 ? 40.811 28.657 -16.996 1.00 175.50 ? 275 TRP B O 1 ATOM 5224 C CB . TRP B 1 276 ? 43.838 29.021 -15.592 1.00 183.19 ? 275 TRP B CB 1 ATOM 5225 C CG . TRP B 1 276 ? 44.103 29.536 -16.995 1.00 185.41 ? 275 TRP B CG 1 ATOM 5226 C CD1 . TRP B 1 276 ? 44.878 28.937 -17.949 1.00 187.28 ? 275 TRP B CD1 1 ATOM 5227 C CD2 . TRP B 1 276 ? 43.613 30.749 -17.585 1.00 185.16 ? 275 TRP B CD2 1 ATOM 5228 N NE1 . TRP B 1 276 ? 44.896 29.695 -19.094 1.00 187.48 ? 275 TRP B NE1 1 ATOM 5229 C CE2 . TRP B 1 276 ? 44.127 30.812 -18.900 1.00 186.71 ? 275 TRP B CE2 1 ATOM 5230 C CE3 . TRP B 1 276 ? 42.786 31.786 -17.135 1.00 183.55 ? 275 TRP B CE3 1 ATOM 5231 C CZ2 . TRP B 1 276 ? 43.841 31.869 -19.767 1.00 187.96 ? 275 TRP B CZ2 1 ATOM 5232 C CZ3 . TRP B 1 276 ? 42.502 32.838 -18.000 1.00 184.00 ? 275 TRP B CZ3 1 ATOM 5233 C CH2 . TRP B 1 276 ? 43.030 32.870 -19.300 1.00 186.61 ? 275 TRP B CH2 1 ATOM 5234 N N . LEU B 1 277 ? 41.676 26.780 -16.086 1.00 172.37 ? 276 LEU B N 1 ATOM 5235 C CA . LEU B 1 277 ? 40.938 25.872 -16.954 1.00 169.28 ? 276 LEU B CA 1 ATOM 5236 C C . LEU B 1 277 ? 39.432 26.014 -16.698 1.00 165.41 ? 276 LEU B C 1 ATOM 5237 O O . LEU B 1 277 ? 38.642 26.078 -17.644 1.00 165.69 ? 276 LEU B O 1 ATOM 5238 C CB . LEU B 1 277 ? 41.407 24.426 -16.741 1.00 168.46 ? 276 LEU B CB 1 ATOM 5239 C CG . LEU B 1 277 ? 42.916 24.159 -16.875 1.00 170.47 ? 276 LEU B CG 1 ATOM 5240 C CD1 . LEU B 1 277 ? 43.250 22.737 -16.459 1.00 171.07 ? 276 LEU B CD1 1 ATOM 5241 C CD2 . LEU B 1 277 ? 43.417 24.428 -18.285 1.00 171.96 ? 276 LEU B CD2 1 ATOM 5242 N N . MET B 1 278 ? 39.048 26.096 -15.423 1.00 161.91 ? 277 MET B N 1 ATOM 5243 C CA . MET B 1 278 ? 37.651 26.344 -15.027 1.00 157.73 ? 277 MET B CA 1 ATOM 5244 C C . MET B 1 278 ? 37.104 27.640 -15.630 1.00 155.61 ? 277 MET B C 1 ATOM 5245 O O . MET B 1 278 ? 35.992 27.672 -16.160 1.00 150.63 ? 277 MET B O 1 ATOM 5246 C CB . MET B 1 278 ? 37.535 26.437 -13.500 1.00 158.81 ? 277 MET B CB 1 ATOM 5247 C CG . MET B 1 278 ? 37.669 25.119 -12.749 1.00 160.94 ? 277 MET B CG 1 ATOM 5248 S SD . MET B 1 278 ? 37.490 25.346 -10.964 1.00 162.14 ? 277 MET B SD 1 ATOM 5249 C CE . MET B 1 278 ? 37.538 23.652 -10.381 1.00 161.06 ? 277 MET B CE 1 ATOM 5250 N N . ARG B 1 279 ? 37.889 28.709 -15.534 1.00 158.72 ? 278 ARG B N 1 ATOM 5251 C CA . ARG B 1 279 ? 37.479 30.005 -16.072 1.00 160.50 ? 278 ARG B CA 1 ATOM 5252 C C . ARG B 1 279 ? 37.299 29.939 -17.586 1.00 160.56 ? 278 ARG B C 1 ATOM 5253 O O . ARG B 1 279 ? 36.306 30.442 -18.124 1.00 158.66 ? 278 ARG B O 1 ATOM 5254 C CB . ARG B 1 279 ? 38.498 31.091 -15.710 1.00 163.98 ? 278 ARG B CB 1 ATOM 5255 C CG . ARG B 1 279 ? 38.184 32.483 -16.253 1.00 164.87 ? 278 ARG B CG 1 ATOM 5256 C CD . ARG B 1 279 ? 36.893 33.057 -15.688 1.00 161.15 ? 278 ARG B CD 1 ATOM 5257 N NE . ARG B 1 279 ? 36.716 34.460 -16.063 1.00 160.29 ? 278 ARG B NE 1 ATOM 5258 C CZ . ARG B 1 279 ? 35.715 35.236 -15.655 1.00 156.90 ? 278 ARG B CZ 1 ATOM 5259 N NH1 . ARG B 1 279 ? 34.771 34.761 -14.844 1.00 153.22 ? 278 ARG B NH1 1 ATOM 5260 N NH2 . ARG B 1 279 ? 35.658 36.499 -16.060 1.00 157.46 ? 278 ARG B NH2 1 ATOM 5261 N N . GLN B 1 280 ? 38.257 29.320 -18.269 1.00 162.84 ? 279 GLN B N 1 ATOM 5262 C CA . GLN B 1 280 ? 38.149 29.137 -19.712 1.00 165.50 ? 279 GLN B CA 1 ATOM 5263 C C . GLN B 1 280 ? 36.894 28.351 -20.086 1.00 162.25 ? 279 GLN B C 1 ATOM 5264 O O . GLN B 1 280 ? 36.248 28.670 -21.081 1.00 161.10 ? 279 GLN B O 1 ATOM 5265 C CB . GLN B 1 280 ? 39.395 28.453 -20.275 1.00 171.28 ? 279 GLN B CB 1 ATOM 5266 C CG . GLN B 1 280 ? 40.621 29.353 -20.312 1.00 176.62 ? 279 GLN B CG 1 ATOM 5267 C CD . GLN B 1 280 ? 41.879 28.622 -20.747 1.00 181.83 ? 279 GLN B CD 1 ATOM 5268 O OE1 . GLN B 1 280 ? 42.201 27.549 -20.233 1.00 183.75 ? 279 GLN B OE1 1 ATOM 5269 N NE2 . GLN B 1 280 ? 42.605 29.208 -21.692 1.00 185.28 ? 279 GLN B NE2 1 ATOM 5270 N N . ASP B 1 281 ? 36.553 27.338 -19.289 1.00 161.28 ? 280 ASP B N 1 ATOM 5271 C CA . ASP B 1 281 ? 35.342 26.538 -19.519 1.00 160.40 ? 280 ASP B CA 1 ATOM 5272 C C . ASP B 1 281 ? 34.062 27.370 -19.427 1.00 158.10 ? 280 ASP B C 1 ATOM 5273 O O . ASP B 1 281 ? 33.113 27.149 -20.184 1.00 157.39 ? 280 ASP B O 1 ATOM 5274 C CB . ASP B 1 281 ? 35.225 25.403 -18.488 1.00 160.14 ? 280 ASP B CB 1 ATOM 5275 C CG . ASP B 1 281 ? 36.323 24.363 -18.615 1.00 163.06 ? 280 ASP B CG 1 ATOM 5276 O OD1 . ASP B 1 281 ? 36.752 24.064 -19.749 1.00 165.54 ? 280 ASP B OD1 1 ATOM 5277 O OD2 . ASP B 1 281 ? 36.747 23.829 -17.569 1.00 162.69 ? 280 ASP B OD2 1 ATOM 5278 N N . THR B 1 282 ? 34.039 28.323 -18.498 1.00 157.71 ? 281 THR B N 1 ATOM 5279 C CA . THR B 1 282 ? 32.781 28.955 -18.089 1.00 155.72 ? 281 THR B CA 1 ATOM 5280 C C . THR B 1 282 ? 32.540 30.379 -18.566 1.00 156.26 ? 281 THR B C 1 ATOM 5281 O O . THR B 1 282 ? 31.382 30.806 -18.616 1.00 154.03 ? 281 THR B O 1 ATOM 5282 C CB . THR B 1 282 ? 32.617 29.015 -16.548 1.00 154.32 ? 281 THR B CB 1 ATOM 5283 O OG1 . THR B 1 282 ? 33.619 29.855 -15.959 1.00 156.18 ? 281 THR B OG1 1 ATOM 5284 C CG2 . THR B 1 282 ? 32.647 27.631 -15.914 1.00 153.86 ? 281 THR B CG2 1 ATOM 5285 N N . GLU B 1 283 ? 33.603 31.116 -18.892 1.00 158.47 ? 282 GLU B N 1 ATOM 5286 C CA . GLU B 1 283 ? 33.464 32.548 -19.156 1.00 159.59 ? 282 GLU B CA 1 ATOM 5287 C C . GLU B 1 283 ? 32.589 32.867 -20.370 1.00 160.10 ? 282 GLU B C 1 ATOM 5288 O O . GLU B 1 283 ? 32.015 33.952 -20.448 1.00 161.45 ? 282 GLU B O 1 ATOM 5289 C CB . GLU B 1 283 ? 34.825 33.248 -19.252 1.00 163.30 ? 282 GLU B CB 1 ATOM 5290 C CG . GLU B 1 283 ? 35.617 33.000 -20.528 1.00 166.00 ? 282 GLU B CG 1 ATOM 5291 C CD . GLU B 1 283 ? 36.819 33.923 -20.648 1.00 169.60 ? 282 GLU B CD 1 ATOM 5292 O OE1 . GLU B 1 283 ? 37.495 34.164 -19.622 1.00 170.53 ? 282 GLU B OE1 1 ATOM 5293 O OE2 . GLU B 1 283 ? 37.088 34.412 -21.768 1.00 171.45 ? 282 GLU B OE2 1 ATOM 5294 N N . GLY B 1 284 ? 32.468 31.920 -21.297 1.00 160.56 ? 283 GLY B N 1 ATOM 5295 C CA . GLY B 1 284 ? 31.658 32.119 -22.495 1.00 162.53 ? 283 GLY B CA 1 ATOM 5296 C C . GLY B 1 284 ? 30.229 31.596 -22.437 1.00 162.06 ? 283 GLY B C 1 ATOM 5297 O O . GLY B 1 284 ? 29.496 31.716 -23.416 1.00 162.44 ? 283 GLY B O 1 ATOM 5298 N N . LEU B 1 285 ? 29.815 31.037 -21.300 1.00 162.47 ? 284 LEU B N 1 ATOM 5299 C CA . LEU B 1 285 ? 28.506 30.377 -21.202 1.00 163.28 ? 284 LEU B CA 1 ATOM 5300 C C . LEU B 1 285 ? 27.329 31.308 -21.455 1.00 161.21 ? 284 LEU B C 1 ATOM 5301 O O . LEU B 1 285 ? 26.435 30.996 -22.245 1.00 158.42 ? 284 LEU B O 1 ATOM 5302 C CB . LEU B 1 285 ? 28.327 29.712 -19.831 1.00 164.98 ? 284 LEU B CB 1 ATOM 5303 C CG . LEU B 1 285 ? 28.943 28.320 -19.665 1.00 168.49 ? 284 LEU B CG 1 ATOM 5304 C CD1 . LEU B 1 285 ? 28.779 27.838 -18.231 1.00 169.56 ? 284 LEU B CD1 1 ATOM 5305 C CD2 . LEU B 1 285 ? 28.317 27.323 -20.634 1.00 168.48 ? 284 LEU B CD2 1 ATOM 5306 N N . VAL B 1 286 ? 27.326 32.441 -20.766 1.00 162.53 ? 285 VAL B N 1 ATOM 5307 C CA . VAL B 1 286 ? 26.243 33.409 -20.888 1.00 164.92 ? 285 VAL B CA 1 ATOM 5308 C C . VAL B 1 286 ? 26.654 34.490 -21.886 1.00 169.46 ? 285 VAL B C 1 ATOM 5309 O O . VAL B 1 286 ? 27.689 35.128 -21.720 1.00 171.59 ? 285 VAL B O 1 ATOM 5310 C CB . VAL B 1 286 ? 25.917 34.053 -19.521 1.00 163.36 ? 285 VAL B CB 1 ATOM 5311 C CG1 . VAL B 1 286 ? 24.712 34.980 -19.632 1.00 163.11 ? 285 VAL B CG1 1 ATOM 5312 C CG2 . VAL B 1 286 ? 25.666 32.973 -18.477 1.00 160.44 ? 285 VAL B CG2 1 ATOM 5313 N N . GLU B 1 287 ? 25.847 34.690 -22.923 1.00 171.21 ? 286 GLU B N 1 ATOM 5314 C CA . GLU B 1 287 ? 26.099 35.761 -23.886 1.00 174.56 ? 286 GLU B CA 1 ATOM 5315 C C . GLU B 1 287 ? 25.905 37.112 -23.206 1.00 171.62 ? 286 GLU B C 1 ATOM 5316 O O . GLU B 1 287 ? 24.800 37.441 -22.777 1.00 166.59 ? 286 GLU B O 1 ATOM 5317 C CB . GLU B 1 287 ? 25.163 35.639 -25.089 1.00 179.52 ? 286 GLU B CB 1 ATOM 5318 C CG . GLU B 1 287 ? 25.476 34.448 -25.982 1.00 185.12 ? 286 GLU B CG 1 ATOM 5319 C CD . GLU B 1 287 ? 24.429 34.221 -27.056 1.00 190.67 ? 286 GLU B CD 1 ATOM 5320 O OE1 . GLU B 1 287 ? 23.232 34.110 -26.713 1.00 191.94 ? 286 GLU B OE1 1 ATOM 5321 O OE2 . GLU B 1 287 ? 24.804 34.141 -28.246 1.00 198.57 ? 286 GLU B OE2 1 ATOM 5322 N N . ALA B 1 288 ? 26.984 37.887 -23.122 1.00 174.05 ? 287 ALA B N 1 ATOM 5323 C CA . ALA B 1 288 ? 27.021 39.115 -22.324 1.00 177.71 ? 287 ALA B CA 1 ATOM 5324 C C . ALA B 1 288 ? 25.910 40.111 -22.655 1.00 176.89 ? 287 ALA B C 1 ATOM 5325 O O . ALA B 1 288 ? 25.330 40.722 -21.754 1.00 175.21 ? 287 ALA B O 1 ATOM 5326 C CB . ALA B 1 288 ? 28.379 39.787 -22.466 1.00 183.76 ? 287 ALA B CB 1 ATOM 5327 N N . THR B 1 289 ? 25.608 40.257 -23.944 1.00 175.86 ? 288 THR B N 1 ATOM 5328 C CA . THR B 1 289 ? 24.719 41.315 -24.426 1.00 174.82 ? 288 THR B CA 1 ATOM 5329 C C . THR B 1 289 ? 23.253 40.904 -24.631 1.00 172.48 ? 288 THR B C 1 ATOM 5330 O O . THR B 1 289 ? 22.375 41.766 -24.633 1.00 173.65 ? 288 THR B O 1 ATOM 5331 C CB . THR B 1 289 ? 25.251 41.919 -25.746 1.00 176.51 ? 288 THR B CB 1 ATOM 5332 O OG1 . THR B 1 289 ? 25.553 40.867 -26.672 1.00 176.92 ? 288 THR B OG1 1 ATOM 5333 C CG2 . THR B 1 289 ? 26.508 42.749 -25.498 1.00 176.47 ? 288 THR B CG2 1 ATOM 5334 N N . MET B 1 290 ? 22.991 39.607 -24.790 1.00 170.42 ? 289 MET B N 1 ATOM 5335 C CA . MET B 1 290 ? 21.633 39.114 -25.045 1.00 168.46 ? 289 MET B CA 1 ATOM 5336 C C . MET B 1 290 ? 20.752 39.250 -23.798 1.00 159.61 ? 289 MET B C 1 ATOM 5337 O O . MET B 1 290 ? 21.057 38.655 -22.770 1.00 156.53 ? 289 MET B O 1 ATOM 5338 C CB . MET B 1 290 ? 21.671 37.646 -25.484 1.00 171.85 ? 289 MET B CB 1 ATOM 5339 C CG . MET B 1 290 ? 22.424 37.396 -26.783 1.00 178.11 ? 289 MET B CG 1 ATOM 5340 S SD . MET B 1 290 ? 21.760 38.292 -28.202 1.00 186.76 ? 289 MET B SD 1 ATOM 5341 C CE . MET B 1 290 ? 20.151 37.519 -28.378 1.00 185.27 ? 289 MET B CE 1 ATOM 5342 N N . PRO B 1 291 ? 19.657 40.033 -23.884 1.00 154.11 ? 290 PRO B N 1 ATOM 5343 C CA . PRO B 1 291 ? 18.753 40.144 -22.737 1.00 148.67 ? 290 PRO B CA 1 ATOM 5344 C C . PRO B 1 291 ? 17.909 38.887 -22.543 1.00 143.30 ? 290 PRO B C 1 ATOM 5345 O O . PRO B 1 291 ? 17.817 38.065 -23.453 1.00 139.32 ? 290 PRO B O 1 ATOM 5346 C CB . PRO B 1 291 ? 17.849 41.336 -23.092 1.00 151.37 ? 290 PRO B CB 1 ATOM 5347 C CG . PRO B 1 291 ? 18.369 41.904 -24.369 1.00 155.31 ? 290 PRO B CG 1 ATOM 5348 C CD . PRO B 1 291 ? 19.200 40.850 -25.021 1.00 156.15 ? 290 PRO B CD 1 ATOM 5349 N N . PRO B 1 292 ? 17.288 38.736 -21.362 1.00 139.18 ? 291 PRO B N 1 ATOM 5350 C CA . PRO B 1 292 ? 16.450 37.561 -21.135 1.00 135.95 ? 291 PRO B CA 1 ATOM 5351 C C . PRO B 1 292 ? 15.178 37.522 -21.991 1.00 135.18 ? 291 PRO B C 1 ATOM 5352 O O . PRO B 1 292 ? 14.643 36.445 -22.236 1.00 133.68 ? 291 PRO B O 1 ATOM 5353 C CB . PRO B 1 292 ? 16.106 37.652 -19.641 1.00 133.72 ? 291 PRO B CB 1 ATOM 5354 C CG . PRO B 1 292 ? 16.282 39.085 -19.284 1.00 134.87 ? 291 PRO B CG 1 ATOM 5355 C CD . PRO B 1 292 ? 17.384 39.592 -20.164 1.00 137.95 ? 291 PRO B CD 1 ATOM 5356 N N . GLY B 1 293 ? 14.700 38.681 -22.433 1.00 135.72 ? 292 GLY B N 1 ATOM 5357 C CA . GLY B 1 293 ? 13.541 38.747 -23.318 1.00 134.90 ? 292 GLY B CA 1 ATOM 5358 C C . GLY B 1 293 ? 12.203 38.607 -22.611 1.00 133.37 ? 292 GLY B C 1 ATOM 5359 O O . GLY B 1 293 ? 11.218 38.189 -23.222 1.00 129.97 ? 292 GLY B O 1 ATOM 5360 N N . VAL B 1 294 ? 12.170 38.963 -21.327 1.00 134.00 ? 293 VAL B N 1 ATOM 5361 C CA . VAL B 1 294 ? 10.939 38.937 -20.523 1.00 134.37 ? 293 VAL B CA 1 ATOM 5362 C C . VAL B 1 294 ? 10.869 40.163 -19.620 1.00 135.92 ? 293 VAL B C 1 ATOM 5363 O O . VAL B 1 294 ? 11.872 40.850 -19.431 1.00 135.75 ? 293 VAL B O 1 ATOM 5364 C CB . VAL B 1 294 ? 10.854 37.674 -19.640 1.00 132.41 ? 293 VAL B CB 1 ATOM 5365 C CG1 . VAL B 1 294 ? 10.721 36.432 -20.503 1.00 132.94 ? 293 VAL B CG1 1 ATOM 5366 C CG2 . VAL B 1 294 ? 12.060 37.563 -18.712 1.00 131.70 ? 293 VAL B CG2 1 ATOM 5367 N N . GLN B 1 295 ? 9.686 40.428 -19.066 1.00 137.18 ? 294 GLN B N 1 ATOM 5368 C CA . GLN B 1 295 ? 9.509 41.560 -18.158 1.00 139.85 ? 294 GLN B CA 1 ATOM 5369 C C . GLN B 1 295 ? 10.442 41.375 -16.974 1.00 137.04 ? 294 GLN B C 1 ATOM 5370 O O . GLN B 1 295 ? 10.385 40.353 -16.292 1.00 136.49 ? 294 GLN B O 1 ATOM 5371 C CB . GLN B 1 295 ? 8.061 41.671 -17.669 1.00 144.31 ? 294 GLN B CB 1 ATOM 5372 C CG . GLN B 1 295 ? 7.781 42.952 -16.887 1.00 150.53 ? 294 GLN B CG 1 ATOM 5373 C CD . GLN B 1 295 ? 6.441 42.945 -16.169 1.00 154.14 ? 294 GLN B CD 1 ATOM 5374 O OE1 . GLN B 1 295 ? 6.258 43.650 -15.174 1.00 158.90 ? 294 GLN B OE1 1 ATOM 5375 N NE2 . GLN B 1 295 ? 5.497 42.153 -16.668 1.00 154.64 ? 294 GLN B NE2 1 ATOM 5376 N N . LEU B 1 296 ? 11.288 42.371 -16.736 1.00 137.64 ? 295 LEU B N 1 ATOM 5377 C CA . LEU B 1 296 ? 12.377 42.259 -15.777 1.00 138.15 ? 295 LEU B CA 1 ATOM 5378 C C . LEU B 1 296 ? 12.308 43.367 -14.736 1.00 138.53 ? 295 LEU B C 1 ATOM 5379 O O . LEU B 1 296 ? 12.133 44.540 -15.071 1.00 139.58 ? 295 LEU B O 1 ATOM 5380 C CB . LEU B 1 296 ? 13.715 42.326 -16.514 1.00 141.01 ? 295 LEU B CB 1 ATOM 5381 C CG . LEU B 1 296 ? 14.996 42.353 -15.673 1.00 143.67 ? 295 LEU B CG 1 ATOM 5382 C CD1 . LEU B 1 296 ? 15.059 41.156 -14.733 1.00 142.59 ? 295 LEU B CD1 1 ATOM 5383 C CD2 . LEU B 1 296 ? 16.211 42.399 -16.590 1.00 145.23 ? 295 LEU B CD2 1 ATOM 5384 N N . HIS B 1 297 ? 12.445 42.980 -13.474 1.00 139.69 ? 296 HIS B N 1 ATOM 5385 C CA . HIS B 1 297 ? 12.540 43.927 -12.381 1.00 143.40 ? 296 HIS B CA 1 ATOM 5386 C C . HIS B 1 297 ? 13.877 43.708 -11.692 1.00 144.20 ? 296 HIS B C 1 ATOM 5387 O O . HIS B 1 297 ? 14.088 42.678 -11.058 1.00 143.13 ? 296 HIS B O 1 ATOM 5388 C CB . HIS B 1 297 ? 11.372 43.736 -11.420 1.00 145.05 ? 296 HIS B CB 1 ATOM 5389 C CG . HIS B 1 297 ? 10.035 43.961 -12.055 1.00 147.19 ? 296 HIS B CG 1 ATOM 5390 N ND1 . HIS B 1 297 ? 9.334 45.140 -11.919 1.00 150.25 ? 296 HIS B ND1 1 ATOM 5391 C CD2 . HIS B 1 297 ? 9.278 43.162 -12.845 1.00 147.33 ? 296 HIS B CD2 1 ATOM 5392 C CE1 . HIS B 1 297 ? 8.198 45.055 -12.589 1.00 151.52 ? 296 HIS B CE1 1 ATOM 5393 N NE2 . HIS B 1 297 ? 8.140 43.865 -13.160 1.00 149.67 ? 296 HIS B NE2 1 ATOM 5394 N N . CYS B 1 298 ? 14.786 44.668 -11.844 1.00 146.57 ? 297 CYS B N 1 ATOM 5395 C CA . CYS B 1 298 ? 16.130 44.557 -11.280 1.00 147.77 ? 297 CYS B CA 1 ATOM 5396 C C . CYS B 1 298 ? 16.264 45.339 -9.981 1.00 148.51 ? 297 CYS B C 1 ATOM 5397 O O . CYS B 1 298 ? 16.306 46.569 -9.977 1.00 152.29 ? 297 CYS B O 1 ATOM 5398 C CB . CYS B 1 298 ? 17.178 45.019 -12.290 1.00 150.18 ? 297 CYS B CB 1 ATOM 5399 S SG . CYS B 1 298 ? 17.413 43.849 -13.644 1.00 149.35 ? 297 CYS B SG 1 ATOM 5400 N N . LEU B 1 299 ? 16.328 44.603 -8.878 1.00 146.72 ? 298 LEU B N 1 ATOM 5401 C CA . LEU B 1 299 ? 16.492 45.189 -7.556 1.00 148.75 ? 298 LEU B CA 1 ATOM 5402 C C . LEU B 1 299 ? 17.940 45.052 -7.112 1.00 149.69 ? 298 LEU B C 1 ATOM 5403 O O . LEU B 1 299 ? 18.514 43.961 -7.163 1.00 149.69 ? 298 LEU B O 1 ATOM 5404 C CB . LEU B 1 299 ? 15.576 44.499 -6.542 1.00 148.50 ? 298 LEU B CB 1 ATOM 5405 C CG . LEU B 1 299 ? 14.118 44.966 -6.525 1.00 149.18 ? 298 LEU B CG 1 ATOM 5406 C CD1 . LEU B 1 299 ? 13.478 44.840 -7.901 1.00 150.07 ? 298 LEU B CD1 1 ATOM 5407 C CD2 . LEU B 1 299 ? 13.321 44.189 -5.486 1.00 147.79 ? 298 LEU B CD2 1 ATOM 5408 N N . TYR B 1 300 ? 18.524 46.159 -6.669 1.00 150.31 ? 299 TYR B N 1 ATOM 5409 C CA . TYR B 1 300 ? 19.913 46.165 -6.224 1.00 152.54 ? 299 TYR B CA 1 ATOM 5410 C C . TYR B 1 300 ? 20.079 46.968 -4.937 1.00 153.97 ? 299 TYR B C 1 ATOM 5411 O O . TYR B 1 300 ? 19.486 48.031 -4.781 1.00 153.64 ? 299 TYR B O 1 ATOM 5412 C CB . TYR B 1 300 ? 20.822 46.723 -7.327 1.00 154.99 ? 299 TYR B CB 1 ATOM 5413 C CG . TYR B 1 300 ? 20.470 48.123 -7.790 1.00 157.58 ? 299 TYR B CG 1 ATOM 5414 C CD1 . TYR B 1 300 ? 19.547 48.330 -8.814 1.00 157.25 ? 299 TYR B CD1 1 ATOM 5415 C CD2 . TYR B 1 300 ? 21.070 49.239 -7.212 1.00 158.79 ? 299 TYR B CD2 1 ATOM 5416 C CE1 . TYR B 1 300 ? 19.227 49.609 -9.241 1.00 157.42 ? 299 TYR B CE1 1 ATOM 5417 C CE2 . TYR B 1 300 ? 20.757 50.520 -7.633 1.00 159.32 ? 299 TYR B CE2 1 ATOM 5418 C CZ . TYR B 1 300 ? 19.835 50.700 -8.646 1.00 159.01 ? 299 TYR B CZ 1 ATOM 5419 O OH . TYR B 1 300 ? 19.524 51.974 -9.063 1.00 160.84 ? 299 TYR B OH 1 ATOM 5420 N N . GLY B 1 301 ? 20.887 46.450 -4.016 1.00 154.42 ? 300 GLY B N 1 ATOM 5421 C CA . GLY B 1 301 ? 21.193 47.152 -2.770 1.00 156.52 ? 300 GLY B CA 1 ATOM 5422 C C . GLY B 1 301 ? 22.344 48.132 -2.935 1.00 160.16 ? 300 GLY B C 1 ATOM 5423 O O . GLY B 1 301 ? 23.287 47.877 -3.697 1.00 159.63 ? 300 GLY B O 1 ATOM 5424 N N . THR B 1 302 ? 22.264 49.258 -2.224 1.00 164.08 ? 301 THR B N 1 ATOM 5425 C CA . THR B 1 302 ? 23.309 50.282 -2.258 1.00 167.56 ? 301 THR B CA 1 ATOM 5426 C C . THR B 1 302 ? 23.583 50.800 -0.851 1.00 168.89 ? 301 THR B C 1 ATOM 5427 O O . THR B 1 302 ? 22.846 50.491 0.091 1.00 164.85 ? 301 THR B O 1 ATOM 5428 C CB . THR B 1 302 ? 22.925 51.470 -3.171 1.00 169.84 ? 301 THR B CB 1 ATOM 5429 O OG1 . THR B 1 302 ? 21.795 52.165 -2.628 1.00 170.33 ? 301 THR B OG1 1 ATOM 5430 C CG2 . THR B 1 302 ? 22.597 50.990 -4.579 1.00 168.48 ? 301 THR B CG2 1 ATOM 5431 N N . GLY B 1 303 ? 24.648 51.587 -0.725 1.00 173.21 ? 302 GLY B N 1 ATOM 5432 C CA . GLY B 1 303 ? 25.008 52.228 0.536 1.00 176.95 ? 302 GLY B CA 1 ATOM 5433 C C . GLY B 1 303 ? 25.699 51.314 1.533 1.00 176.52 ? 302 GLY B C 1 ATOM 5434 O O . GLY B 1 303 ? 25.809 51.657 2.710 1.00 179.66 ? 302 GLY B O 1 ATOM 5435 N N . VAL B 1 304 ? 26.175 50.161 1.068 1.00 173.70 ? 303 VAL B N 1 ATOM 5436 C CA . VAL B 1 304 ? 26.842 49.191 1.939 1.00 173.08 ? 303 VAL B CA 1 ATOM 5437 C C . VAL B 1 304 ? 28.278 49.002 1.449 1.00 172.95 ? 303 VAL B C 1 ATOM 5438 O O . VAL B 1 304 ? 28.487 48.706 0.273 1.00 171.39 ? 303 VAL B O 1 ATOM 5439 C CB . VAL B 1 304 ? 26.115 47.826 1.909 1.00 171.33 ? 303 VAL B CB 1 ATOM 5440 C CG1 . VAL B 1 304 ? 26.734 46.857 2.910 1.00 172.19 ? 303 VAL B CG1 1 ATOM 5441 C CG2 . VAL B 1 304 ? 24.628 48.004 2.190 1.00 169.90 ? 303 VAL B CG2 1 ATOM 5442 N N . PRO B 1 305 ? 29.271 49.156 2.347 1.00 173.42 ? 304 PRO B N 1 ATOM 5443 C CA . PRO B 1 305 ? 30.653 49.017 1.888 1.00 174.06 ? 304 PRO B CA 1 ATOM 5444 C C . PRO B 1 305 ? 30.890 47.644 1.274 1.00 169.78 ? 304 PRO B C 1 ATOM 5445 O O . PRO B 1 305 ? 30.615 46.635 1.916 1.00 167.61 ? 304 PRO B O 1 ATOM 5446 C CB . PRO B 1 305 ? 31.473 49.181 3.174 1.00 176.75 ? 304 PRO B CB 1 ATOM 5447 C CG . PRO B 1 305 ? 30.539 48.819 4.276 1.00 174.84 ? 304 PRO B CG 1 ATOM 5448 C CD . PRO B 1 305 ? 29.190 49.284 3.814 1.00 173.76 ? 304 PRO B CD 1 ATOM 5449 N N . THR B 1 306 ? 31.370 47.617 0.035 1.00 169.86 ? 305 THR B N 1 ATOM 5450 C CA . THR B 1 306 ? 31.568 46.368 -0.705 1.00 170.33 ? 305 THR B CA 1 ATOM 5451 C C . THR B 1 306 ? 33.025 46.292 -1.178 1.00 173.72 ? 305 THR B C 1 ATOM 5452 O O . THR B 1 306 ? 33.531 47.259 -1.739 1.00 177.76 ? 305 THR B O 1 ATOM 5453 C CB . THR B 1 306 ? 30.654 46.326 -1.949 1.00 169.10 ? 305 THR B CB 1 ATOM 5454 O OG1 . THR B 1 306 ? 29.323 46.719 -1.587 1.00 166.85 ? 305 THR B OG1 1 ATOM 5455 C CG2 . THR B 1 306 ? 30.623 44.927 -2.563 1.00 167.82 ? 305 THR B CG2 1 ATOM 5456 N N . PRO B 1 307 ? 33.701 45.143 -0.972 1.00 173.90 ? 306 PRO B N 1 ATOM 5457 C CA . PRO B 1 307 ? 35.100 45.053 -1.408 1.00 177.65 ? 306 PRO B CA 1 ATOM 5458 C C . PRO B 1 307 ? 35.265 45.386 -2.893 1.00 181.11 ? 306 PRO B C 1 ATOM 5459 O O . PRO B 1 307 ? 34.526 44.853 -3.724 1.00 177.04 ? 306 PRO B O 1 ATOM 5460 C CB . PRO B 1 307 ? 35.472 43.589 -1.131 1.00 175.83 ? 306 PRO B CB 1 ATOM 5461 C CG . PRO B 1 307 ? 34.177 42.867 -0.978 1.00 172.32 ? 306 PRO B CG 1 ATOM 5462 C CD . PRO B 1 307 ? 33.226 43.870 -0.404 1.00 171.68 ? 306 PRO B CD 1 ATOM 5463 N N . ASP B 1 308 ? 36.212 46.278 -3.194 1.00 188.52 ? 307 ASP B N 1 ATOM 5464 C CA . ASP B 1 308 ? 36.442 46.797 -4.551 1.00 192.22 ? 307 ASP B CA 1 ATOM 5465 C C . ASP B 1 308 ? 37.802 46.360 -5.104 1.00 194.11 ? 307 ASP B C 1 ATOM 5466 O O . ASP B 1 308 ? 37.899 45.923 -6.254 1.00 194.47 ? 307 ASP B O 1 ATOM 5467 C CB . ASP B 1 308 ? 36.358 48.330 -4.538 1.00 195.76 ? 307 ASP B CB 1 ATOM 5468 C CG . ASP B 1 308 ? 36.686 48.952 -5.888 1.00 198.48 ? 307 ASP B CG 1 ATOM 5469 O OD1 . ASP B 1 308 ? 36.233 48.421 -6.926 1.00 194.53 ? 307 ASP B OD1 1 ATOM 5470 O OD2 . ASP B 1 308 ? 37.395 49.982 -5.906 1.00 205.29 ? 307 ASP B OD2 1 ATOM 5471 N N . SER B 1 309 ? 38.847 46.500 -4.291 1.00 196.17 ? 308 SER B N 1 ATOM 5472 C CA . SER B 1 309 ? 40.193 46.076 -4.683 1.00 198.57 ? 308 SER B CA 1 ATOM 5473 C C . SER B 1 309 ? 40.996 45.689 -3.447 1.00 198.40 ? 308 SER B C 1 ATOM 5474 O O . SER B 1 309 ? 40.597 46.002 -2.322 1.00 196.74 ? 308 SER B O 1 ATOM 5475 C CB . SER B 1 309 ? 40.903 47.185 -5.465 1.00 204.42 ? 308 SER B CB 1 ATOM 5476 O OG . SER B 1 309 ? 40.861 48.420 -4.768 1.00 209.48 ? 308 SER B OG 1 ATOM 5477 N N . PHE B 1 310 ? 42.119 45.005 -3.668 1.00 199.78 ? 309 PHE B N 1 ATOM 5478 C CA . PHE B 1 310 ? 42.895 44.404 -2.584 1.00 201.99 ? 309 PHE B CA 1 ATOM 5479 C C . PHE B 1 310 ? 44.382 44.675 -2.712 1.00 206.05 ? 309 PHE B C 1 ATOM 5480 O O . PHE B 1 310 ? 44.937 44.636 -3.813 1.00 207.53 ? 309 PHE B O 1 ATOM 5481 C CB . PHE B 1 310 ? 42.681 42.893 -2.567 1.00 200.65 ? 309 PHE B CB 1 ATOM 5482 C CG . PHE B 1 310 ? 41.241 42.493 -2.515 1.00 199.55 ? 309 PHE B CG 1 ATOM 5483 C CD1 . PHE B 1 310 ? 40.551 42.500 -1.312 1.00 199.09 ? 309 PHE B CD1 1 ATOM 5484 C CD2 . PHE B 1 310 ? 40.569 42.127 -3.671 1.00 200.26 ? 309 PHE B CD2 1 ATOM 5485 C CE1 . PHE B 1 310 ? 39.215 42.141 -1.258 1.00 197.23 ? 309 PHE B CE1 1 ATOM 5486 C CE2 . PHE B 1 310 ? 39.233 41.765 -3.626 1.00 198.78 ? 309 PHE B CE2 1 ATOM 5487 C CZ . PHE B 1 310 ? 38.553 41.773 -2.418 1.00 197.08 ? 309 PHE B CZ 1 ATOM 5488 N N . TYR B 1 311 ? 45.022 44.944 -1.578 1.00 208.99 ? 310 TYR B N 1 ATOM 5489 C CA . TYR B 1 311 ? 46.475 45.004 -1.521 1.00 214.21 ? 310 TYR B CA 1 ATOM 5490 C C . TYR B 1 311 ? 46.995 43.848 -0.681 1.00 215.61 ? 310 TYR B C 1 ATOM 5491 O O . TYR B 1 311 ? 46.617 43.695 0.479 1.00 212.73 ? 310 TYR B O 1 ATOM 5492 C CB . TYR B 1 311 ? 46.964 46.329 -0.933 1.00 217.67 ? 310 TYR B CB 1 ATOM 5493 C CG . TYR B 1 311 ? 48.468 46.368 -0.758 1.00 221.70 ? 310 TYR B CG 1 ATOM 5494 C CD1 . TYR B 1 311 ? 49.313 46.511 -1.857 1.00 224.11 ? 310 TYR B CD1 1 ATOM 5495 C CD2 . TYR B 1 311 ? 49.048 46.237 0.503 1.00 222.93 ? 310 TYR B CD2 1 ATOM 5496 C CE1 . TYR B 1 311 ? 50.690 46.535 -1.705 1.00 227.68 ? 310 TYR B CE1 1 ATOM 5497 C CE2 . TYR B 1 311 ? 50.425 46.260 0.665 1.00 226.53 ? 310 TYR B CE2 1 ATOM 5498 C CZ . TYR B 1 311 ? 51.242 46.409 -0.442 1.00 228.81 ? 310 TYR B CZ 1 ATOM 5499 O OH . TYR B 1 311 ? 52.610 46.432 -0.288 1.00 231.57 ? 310 TYR B OH 1 ATOM 5500 N N . TYR B 1 312 ? 47.870 43.044 -1.275 1.00 220.81 ? 311 TYR B N 1 ATOM 5501 C CA . TYR B 1 312 ? 48.520 41.946 -0.570 1.00 225.78 ? 311 TYR B CA 1 ATOM 5502 C C . TYR B 1 312 ? 49.933 42.333 -0.172 1.00 231.58 ? 311 TYR B C 1 ATOM 5503 O O . TYR B 1 312 ? 50.762 42.643 -1.027 1.00 235.07 ? 311 TYR B O 1 ATOM 5504 C CB . TYR B 1 312 ? 48.550 40.695 -1.445 1.00 227.13 ? 311 TYR B CB 1 ATOM 5505 C CG . TYR B 1 312 ? 47.274 39.904 -1.365 1.00 225.88 ? 311 TYR B CG 1 ATOM 5506 C CD1 . TYR B 1 312 ? 47.101 38.938 -0.382 1.00 226.07 ? 311 TYR B CD1 1 ATOM 5507 C CD2 . TYR B 1 312 ? 46.231 40.129 -2.257 1.00 226.06 ? 311 TYR B CD2 1 ATOM 5508 C CE1 . TYR B 1 312 ? 45.932 38.208 -0.293 1.00 224.98 ? 311 TYR B CE1 1 ATOM 5509 C CE2 . TYR B 1 312 ? 45.054 39.403 -2.177 1.00 224.36 ? 311 TYR B CE2 1 ATOM 5510 C CZ . TYR B 1 312 ? 44.911 38.441 -1.192 1.00 224.10 ? 311 TYR B CZ 1 ATOM 5511 O OH . TYR B 1 312 ? 43.749 37.709 -1.091 1.00 223.89 ? 311 TYR B OH 1 ATOM 5512 N N . GLU B 1 313 ? 50.190 42.326 1.132 1.00 233.84 ? 312 GLU B N 1 ATOM 5513 C CA . GLU B 1 313 ? 51.525 42.554 1.669 1.00 240.18 ? 312 GLU B CA 1 ATOM 5514 C C . GLU B 1 313 ? 52.390 41.327 1.391 1.00 239.92 ? 312 GLU B C 1 ATOM 5515 O O . GLU B 1 313 ? 53.587 41.440 1.113 1.00 246.44 ? 312 GLU B O 1 ATOM 5516 C CB . GLU B 1 313 ? 51.437 42.787 3.181 1.00 242.07 ? 312 GLU B CB 1 ATOM 5517 C CG . GLU B 1 313 ? 52.767 43.104 3.855 1.00 248.46 ? 312 GLU B CG 1 ATOM 5518 C CD . GLU B 1 313 ? 52.731 42.932 5.363 1.00 249.15 ? 312 GLU B CD 1 ATOM 5519 O OE1 . GLU B 1 313 ? 51.752 42.360 5.886 1.00 246.04 ? 312 GLU B OE1 1 ATOM 5520 O OE2 . GLU B 1 313 ? 53.695 43.365 6.029 1.00 253.33 ? 312 GLU B OE2 1 ATOM 5521 N N . SER B 1 314 ? 51.767 40.156 1.491 1.00 232.92 ? 313 SER B N 1 ATOM 5522 C CA . SER B 1 314 ? 52.403 38.894 1.141 1.00 230.61 ? 313 SER B CA 1 ATOM 5523 C C . SER B 1 314 ? 51.408 38.028 0.381 1.00 223.52 ? 313 SER B C 1 ATOM 5524 O O . SER B 1 314 ? 50.267 37.846 0.809 1.00 217.95 ? 313 SER B O 1 ATOM 5525 C CB . SER B 1 314 ? 52.887 38.168 2.394 1.00 231.65 ? 313 SER B CB 1 ATOM 5526 O OG . SER B 1 314 ? 53.492 36.932 2.058 1.00 232.11 ? 313 SER B OG 1 ATOM 5527 N N . PHE B 1 315 ? 51.862 37.483 -0.741 1.00 222.62 ? 314 PHE B N 1 ATOM 5528 C CA . PHE B 1 315 ? 50.993 36.797 -1.690 1.00 218.67 ? 314 PHE B CA 1 ATOM 5529 C C . PHE B 1 315 ? 51.323 35.298 -1.702 1.00 219.42 ? 314 PHE B C 1 ATOM 5530 O O . PHE B 1 315 ? 52.499 34.949 -1.795 1.00 222.23 ? 314 PHE B O 1 ATOM 5531 C CB . PHE B 1 315 ? 51.240 37.399 -3.080 1.00 218.13 ? 314 PHE B CB 1 ATOM 5532 C CG . PHE B 1 315 ? 50.107 37.205 -4.045 1.00 212.83 ? 314 PHE B CG 1 ATOM 5533 C CD1 . PHE B 1 315 ? 48.869 37.777 -3.799 1.00 209.21 ? 314 PHE B CD1 1 ATOM 5534 C CD2 . PHE B 1 315 ? 50.285 36.474 -5.212 1.00 212.03 ? 314 PHE B CD2 1 ATOM 5535 C CE1 . PHE B 1 315 ? 47.820 37.609 -4.687 1.00 206.34 ? 314 PHE B CE1 1 ATOM 5536 C CE2 . PHE B 1 315 ? 49.242 36.303 -6.106 1.00 209.23 ? 314 PHE B CE2 1 ATOM 5537 C CZ . PHE B 1 315 ? 48.007 36.871 -5.842 1.00 206.72 ? 314 PHE B CZ 1 ATOM 5538 N N . PRO B 1 316 ? 50.331 34.406 -1.587 1.00 217.77 ? 315 PRO B N 1 ATOM 5539 C CA . PRO B 1 316 ? 48.927 34.731 -1.309 1.00 215.54 ? 315 PRO B CA 1 ATOM 5540 C C . PRO B 1 316 ? 48.449 34.215 0.061 1.00 215.23 ? 315 PRO B C 1 ATOM 5541 O O . PRO B 1 316 ? 47.240 34.105 0.291 1.00 212.45 ? 315 PRO B O 1 ATOM 5542 C CB . PRO B 1 316 ? 48.197 34.004 -2.439 1.00 211.88 ? 315 PRO B CB 1 ATOM 5543 C CG . PRO B 1 316 ? 49.020 32.781 -2.667 1.00 212.14 ? 315 PRO B CG 1 ATOM 5544 C CD . PRO B 1 316 ? 50.449 33.146 -2.346 1.00 216.90 ? 315 PRO B CD 1 ATOM 5545 N N . ASP B 1 317 ? 49.384 33.932 0.969 1.00 218.77 ? 316 ASP B N 1 ATOM 5546 C CA . ASP B 1 317 ? 49.071 33.266 2.242 1.00 217.60 ? 316 ASP B CA 1 ATOM 5547 C C . ASP B 1 317 ? 48.775 34.214 3.413 1.00 217.94 ? 316 ASP B C 1 ATOM 5548 O O . ASP B 1 317 ? 48.555 33.754 4.537 1.00 215.97 ? 316 ASP B O 1 ATOM 5549 C CB . ASP B 1 317 ? 50.226 32.339 2.637 1.00 220.25 ? 316 ASP B CB 1 ATOM 5550 C CG . ASP B 1 317 ? 50.549 31.315 1.565 1.00 219.88 ? 316 ASP B CG 1 ATOM 5551 O OD1 . ASP B 1 317 ? 49.611 30.688 1.031 1.00 215.31 ? 316 ASP B OD1 1 ATOM 5552 O OD2 . ASP B 1 317 ? 51.746 31.133 1.259 1.00 223.94 ? 316 ASP B OD2 1 ATOM 5553 N N . ARG B 1 318 ? 48.771 35.522 3.149 1.00 219.72 ? 317 ARG B N 1 ATOM 5554 C CA . ARG B 1 318 ? 48.505 36.540 4.166 1.00 220.29 ? 317 ARG B CA 1 ATOM 5555 C C . ARG B 1 318 ? 47.260 37.315 3.763 1.00 215.24 ? 317 ARG B C 1 ATOM 5556 O O . ARG B 1 318 ? 47.087 37.628 2.588 1.00 215.09 ? 317 ARG B O 1 ATOM 5557 C CB . ARG B 1 318 ? 49.695 37.500 4.252 1.00 227.07 ? 317 ARG B CB 1 ATOM 5558 C CG . ARG B 1 318 ? 49.561 38.628 5.276 1.00 230.43 ? 317 ARG B CG 1 ATOM 5559 C CD . ARG B 1 318 ? 50.906 39.293 5.509 1.00 237.40 ? 317 ARG B CD 1 ATOM 5560 N NE . ARG B 1 318 ? 51.936 38.339 5.915 1.00 242.71 ? 317 ARG B NE 1 ATOM 5561 C CZ . ARG B 1 318 ? 52.034 37.780 7.122 1.00 246.17 ? 317 ARG B CZ 1 ATOM 5562 N NH1 . ARG B 1 318 ? 51.161 38.063 8.086 1.00 245.37 ? 317 ARG B NH1 1 ATOM 5563 N NH2 . ARG B 1 318 ? 53.019 36.922 7.367 1.00 250.61 ? 317 ARG B NH2 1 ATOM 5564 N N . ASP B 1 319 ? 46.398 37.619 4.729 1.00 210.49 ? 318 ASP B N 1 ATOM 5565 C CA . ASP B 1 319 ? 45.152 38.317 4.428 1.00 206.08 ? 318 ASP B CA 1 ATOM 5566 C C . ASP B 1 319 ? 45.428 39.737 3.931 1.00 207.82 ? 318 ASP B C 1 ATOM 5567 O O . ASP B 1 319 ? 46.323 40.411 4.440 1.00 211.20 ? 318 ASP B O 1 ATOM 5568 C CB . ASP B 1 319 ? 44.225 38.338 5.644 1.00 202.97 ? 318 ASP B CB 1 ATOM 5569 C CG . ASP B 1 319 ? 43.610 36.979 5.931 1.00 198.78 ? 318 ASP B CG 1 ATOM 5570 O OD1 . ASP B 1 319 ? 43.223 36.274 4.972 1.00 194.11 ? 318 ASP B OD1 1 ATOM 5571 O OD2 . ASP B 1 319 ? 43.504 36.621 7.121 1.00 197.71 ? 318 ASP B OD2 1 ATOM 5572 N N . PRO B 1 320 ? 44.669 40.190 2.919 1.00 204.55 ? 319 PRO B N 1 ATOM 5573 C CA . PRO B 1 320 ? 44.962 41.468 2.296 1.00 204.91 ? 319 PRO B CA 1 ATOM 5574 C C . PRO B 1 320 ? 44.265 42.642 2.957 1.00 202.60 ? 319 PRO B C 1 ATOM 5575 O O . PRO B 1 320 ? 43.330 42.459 3.741 1.00 199.07 ? 319 PRO B O 1 ATOM 5576 C CB . PRO B 1 320 ? 44.402 41.284 0.891 1.00 203.31 ? 319 PRO B CB 1 ATOM 5577 C CG . PRO B 1 320 ? 43.194 40.435 1.111 1.00 200.03 ? 319 PRO B CG 1 ATOM 5578 C CD . PRO B 1 320 ? 43.503 39.542 2.287 1.00 200.53 ? 319 PRO B CD 1 ATOM 5579 N N . LYS B 1 321 ? 44.722 43.840 2.619 1.00 203.99 ? 320 LYS B N 1 ATOM 5580 C CA . LYS B 1 321 ? 44.039 45.059 3.025 1.00 204.07 ? 320 LYS B CA 1 ATOM 5581 C C . LYS B 1 321 ? 42.987 45.296 1.944 1.00 200.20 ? 320 LYS B C 1 ATOM 5582 O O . LYS B 1 321 ? 43.225 45.009 0.770 1.00 198.06 ? 320 LYS B O 1 ATOM 5583 C CB . LYS B 1 321 ? 45.004 46.255 3.152 1.00 210.02 ? 320 LYS B CB 1 ATOM 5584 C CG . LYS B 1 321 ? 46.486 45.907 3.336 1.00 214.79 ? 320 LYS B CG 1 ATOM 5585 C CD . LYS B 1 321 ? 46.774 44.990 4.521 1.00 215.76 ? 320 LYS B CD 1 ATOM 5586 C CE . LYS B 1 321 ? 48.151 44.347 4.406 1.00 219.38 ? 320 LYS B CE 1 ATOM 5587 N NZ . LYS B 1 321 ? 48.344 43.241 5.384 1.00 219.33 ? 320 LYS B NZ 1 ATOM 5588 N N . ILE B 1 322 ? 41.820 45.795 2.342 1.00 198.85 ? 321 ILE B N 1 ATOM 5589 C CA . ILE B 1 322 ? 40.677 45.887 1.436 1.00 197.23 ? 321 ILE B CA 1 ATOM 5590 C C . ILE B 1 322 ? 40.245 47.337 1.230 1.00 198.93 ? 321 ILE B C 1 ATOM 5591 O O . ILE B 1 322 ? 40.070 48.082 2.195 1.00 200.50 ? 321 ILE B O 1 ATOM 5592 C CB . ILE B 1 322 ? 39.467 45.097 1.986 1.00 194.80 ? 321 ILE B CB 1 ATOM 5593 C CG1 . ILE B 1 322 ? 39.865 43.643 2.283 1.00 194.25 ? 321 ILE B CG1 1 ATOM 5594 C CG2 . ILE B 1 322 ? 38.300 45.151 1.000 1.00 192.05 ? 321 ILE B CG2 1 ATOM 5595 C CD1 . ILE B 1 322 ? 38.813 42.848 3.027 1.00 191.16 ? 321 ILE B CD1 1 ATOM 5596 N N . CYS B 1 323 ? 40.077 47.723 -0.035 1.00 199.21 ? 322 CYS B N 1 ATOM 5597 C CA . CYS B 1 323 ? 39.476 49.012 -0.396 1.00 199.14 ? 322 CYS B CA 1 ATOM 5598 C C . CYS B 1 323 ? 38.014 48.774 -0.777 1.00 194.12 ? 322 CYS B C 1 ATOM 5599 O O . CYS B 1 323 ? 37.704 47.817 -1.491 1.00 190.15 ? 322 CYS B O 1 ATOM 5600 C CB . CYS B 1 323 ? 40.229 49.645 -1.571 1.00 201.20 ? 322 CYS B CB 1 ATOM 5601 S SG . CYS B 1 323 ? 39.674 51.310 -2.009 1.00 199.76 ? 322 CYS B SG 1 ATOM 5602 N N . PHE B 1 324 ? 37.123 49.641 -0.303 1.00 192.85 ? 323 PHE B N 1 ATOM 5603 C CA . PHE B 1 324 ? 35.685 49.427 -0.459 1.00 188.09 ? 323 PHE B CA 1 ATOM 5604 C C . PHE B 1 324 ? 35.029 50.405 -1.427 1.00 188.76 ? 323 PHE B C 1 ATOM 5605 O O . PHE B 1 324 ? 35.403 51.575 -1.500 1.00 192.19 ? 323 PHE B O 1 ATOM 5606 C CB . PHE B 1 324 ? 34.994 49.507 0.901 1.00 186.14 ? 323 PHE B CB 1 ATOM 5607 C CG . PHE B 1 324 ? 35.345 48.375 1.820 1.00 184.32 ? 323 PHE B CG 1 ATOM 5608 C CD1 . PHE B 1 324 ? 36.499 48.422 2.590 1.00 186.75 ? 323 PHE B CD1 1 ATOM 5609 C CD2 . PHE B 1 324 ? 34.528 47.257 1.909 1.00 179.63 ? 323 PHE B CD2 1 ATOM 5610 C CE1 . PHE B 1 324 ? 36.829 47.377 3.437 1.00 185.26 ? 323 PHE B CE1 1 ATOM 5611 C CE2 . PHE B 1 324 ? 34.853 46.210 2.754 1.00 178.59 ? 323 PHE B CE2 1 ATOM 5612 C CZ . PHE B 1 324 ? 36.005 46.269 3.519 1.00 181.25 ? 323 PHE B CZ 1 ATOM 5613 N N . GLY B 1 325 ? 34.053 49.896 -2.172 1.00 185.55 ? 324 GLY B N 1 ATOM 5614 C CA . GLY B 1 325 ? 33.206 50.703 -3.044 1.00 184.48 ? 324 GLY B CA 1 ATOM 5615 C C . GLY B 1 325 ? 31.745 50.500 -2.683 1.00 181.53 ? 324 GLY B C 1 ATOM 5616 O O . GLY B 1 325 ? 31.426 49.978 -1.610 1.00 179.93 ? 324 GLY B O 1 ATOM 5617 N N . ASP B 1 326 ? 30.855 50.897 -3.586 1.00 180.28 ? 325 ASP B N 1 ATOM 5618 C CA . ASP B 1 326 ? 29.423 50.833 -3.318 1.00 179.47 ? 325 ASP B CA 1 ATOM 5619 C C . ASP B 1 326 ? 28.838 49.493 -3.759 1.00 175.48 ? 325 ASP B C 1 ATOM 5620 O O . ASP B 1 326 ? 29.408 48.795 -4.603 1.00 175.59 ? 325 ASP B O 1 ATOM 5621 C CB . ASP B 1 326 ? 28.694 51.990 -4.015 1.00 182.71 ? 325 ASP B CB 1 ATOM 5622 C CG . ASP B 1 326 ? 27.413 52.403 -3.294 1.00 183.88 ? 325 ASP B CG 1 ATOM 5623 O OD1 . ASP B 1 326 ? 26.964 51.676 -2.378 1.00 184.49 ? 325 ASP B OD1 1 ATOM 5624 O OD2 . ASP B 1 326 ? 26.850 53.462 -3.646 1.00 186.06 ? 325 ASP B OD2 1 ATOM 5625 N N . GLY B 1 327 ? 27.690 49.153 -3.178 1.00 172.20 ? 326 GLY B N 1 ATOM 5626 C CA . GLY B 1 327 ? 26.993 47.898 -3.455 1.00 168.16 ? 326 GLY B CA 1 ATOM 5627 C C . GLY B 1 327 ? 26.172 47.477 -2.250 1.00 166.71 ? 326 GLY B C 1 ATOM 5628 O O . GLY B 1 327 ? 25.747 48.322 -1.450 1.00 171.66 ? 326 GLY B O 1 ATOM 5629 N N . ASP B 1 328 ? 25.975 46.167 -2.110 1.00 162.30 ? 327 ASP B N 1 ATOM 5630 C CA . ASP B 1 328 ? 25.157 45.601 -1.031 1.00 159.79 ? 327 ASP B CA 1 ATOM 5631 C C . ASP B 1 328 ? 25.977 44.840 0.021 1.00 158.70 ? 327 ASP B C 1 ATOM 5632 O O . ASP B 1 328 ? 25.409 44.147 0.870 1.00 157.15 ? 327 ASP B O 1 ATOM 5633 C CB . ASP B 1 328 ? 24.062 44.694 -1.618 1.00 158.69 ? 327 ASP B CB 1 ATOM 5634 C CG . ASP B 1 328 ? 24.618 43.555 -2.470 1.00 157.87 ? 327 ASP B CG 1 ATOM 5635 O OD1 . ASP B 1 328 ? 25.837 43.285 -2.412 1.00 158.51 ? 327 ASP B OD1 1 ATOM 5636 O OD2 . ASP B 1 328 ? 23.824 42.924 -3.201 1.00 156.47 ? 327 ASP B OD2 1 ATOM 5637 N N . GLY B 1 329 ? 27.301 44.979 -0.029 1.00 159.38 ? 328 GLY B N 1 ATOM 5638 C CA . GLY B 1 329 ? 28.193 44.253 0.875 1.00 158.74 ? 328 GLY B CA 1 ATOM 5639 C C . GLY B 1 329 ? 28.907 43.094 0.204 1.00 156.07 ? 328 GLY B C 1 ATOM 5640 O O . GLY B 1 329 ? 29.984 42.691 0.640 1.00 155.54 ? 328 GLY B O 1 ATOM 5641 N N . THR B 1 330 ? 28.308 42.563 -0.858 1.00 154.18 ? 329 THR B N 1 ATOM 5642 C CA . THR B 1 330 ? 28.888 41.454 -1.610 1.00 156.29 ? 329 THR B CA 1 ATOM 5643 C C . THR B 1 330 ? 28.955 41.806 -3.099 1.00 157.93 ? 329 THR B C 1 ATOM 5644 O O . THR B 1 330 ? 30.036 41.817 -3.695 1.00 156.13 ? 329 THR B O 1 ATOM 5645 C CB . THR B 1 330 ? 28.067 40.165 -1.388 1.00 155.19 ? 329 THR B CB 1 ATOM 5646 O OG1 . THR B 1 330 ? 27.998 39.880 0.016 1.00 155.27 ? 329 THR B OG1 1 ATOM 5647 C CG2 . THR B 1 330 ? 28.684 38.982 -2.125 1.00 155.13 ? 329 THR B CG2 1 ATOM 5648 N N . VAL B 1 331 ? 27.796 42.102 -3.686 1.00 160.83 ? 330 VAL B N 1 ATOM 5649 C CA . VAL B 1 331 ? 27.697 42.458 -5.104 1.00 163.51 ? 330 VAL B CA 1 ATOM 5650 C C . VAL B 1 331 ? 27.974 43.941 -5.337 1.00 165.44 ? 330 VAL B C 1 ATOM 5651 O O . VAL B 1 331 ? 27.332 44.815 -4.743 1.00 167.20 ? 330 VAL B O 1 ATOM 5652 C CB . VAL B 1 331 ? 26.310 42.112 -5.684 1.00 163.35 ? 330 VAL B CB 1 ATOM 5653 C CG1 . VAL B 1 331 ? 26.189 42.595 -7.127 1.00 163.63 ? 330 VAL B CG1 1 ATOM 5654 C CG2 . VAL B 1 331 ? 26.063 40.611 -5.602 1.00 162.47 ? 330 VAL B CG2 1 ATOM 5655 N N . ASN B 1 332 ? 28.928 44.208 -6.218 1.00 165.88 ? 331 ASN B N 1 ATOM 5656 C CA . ASN B 1 332 ? 29.345 45.570 -6.494 1.00 167.91 ? 331 ASN B CA 1 ATOM 5657 C C . ASN B 1 332 ? 28.249 46.294 -7.251 1.00 163.40 ? 331 ASN B C 1 ATOM 5658 O O . ASN B 1 332 ? 27.570 45.703 -8.092 1.00 161.83 ? 331 ASN B O 1 ATOM 5659 C CB . ASN B 1 332 ? 30.641 45.573 -7.302 1.00 171.51 ? 331 ASN B CB 1 ATOM 5660 C CG . ASN B 1 332 ? 31.774 44.872 -6.577 1.00 172.96 ? 331 ASN B CG 1 ATOM 5661 O OD1 . ASN B 1 332 ? 32.234 43.813 -7.000 1.00 174.70 ? 331 ASN B OD1 1 ATOM 5662 N ND2 . ASN B 1 332 ? 32.216 45.452 -5.468 1.00 174.25 ? 331 ASN B ND2 1 ATOM 5663 N N . LEU B 1 333 ? 28.078 47.574 -6.941 1.00 159.40 ? 332 LEU B N 1 ATOM 5664 C CA . LEU B 1 333 ? 27.111 48.425 -7.635 1.00 156.59 ? 332 LEU B CA 1 ATOM 5665 C C . LEU B 1 333 ? 27.271 48.367 -9.156 1.00 155.60 ? 332 LEU B C 1 ATOM 5666 O O . LEU B 1 333 ? 26.289 48.367 -9.895 1.00 153.99 ? 332 LEU B O 1 ATOM 5667 C CB . LEU B 1 333 ? 27.264 49.873 -7.166 1.00 158.89 ? 332 LEU B CB 1 ATOM 5668 C CG . LEU B 1 333 ? 26.437 50.931 -7.903 1.00 159.06 ? 332 LEU B CG 1 ATOM 5669 C CD1 . LEU B 1 333 ? 24.950 50.630 -7.782 1.00 156.24 ? 332 LEU B CD1 1 ATOM 5670 C CD2 . LEU B 1 333 ? 26.760 52.316 -7.364 1.00 162.12 ? 332 LEU B CD2 1 ATOM 5671 N N . LYS B 1 334 ? 28.512 48.311 -9.620 1.00 156.34 ? 333 LYS B N 1 ATOM 5672 C CA . LYS B 1 334 ? 28.791 48.307 -11.048 1.00 157.91 ? 333 LYS B CA 1 ATOM 5673 C C . LYS B 1 334 ? 28.101 47.174 -11.814 1.00 155.85 ? 333 LYS B C 1 ATOM 5674 O O . LYS B 1 334 ? 27.920 47.272 -13.025 1.00 154.51 ? 333 LYS B O 1 ATOM 5675 C CB . LYS B 1 334 ? 30.300 48.280 -11.275 1.00 162.00 ? 333 LYS B CB 1 ATOM 5676 C CG . LYS B 1 334 ? 30.982 49.555 -10.799 1.00 168.51 ? 333 LYS B CG 1 ATOM 5677 C CD . LYS B 1 334 ? 32.361 49.300 -10.215 1.00 173.55 ? 333 LYS B CD 1 ATOM 5678 C CE . LYS B 1 334 ? 32.931 50.564 -9.588 1.00 178.94 ? 333 LYS B CE 1 ATOM 5679 N NZ . LYS B 1 334 ? 34.407 50.490 -9.388 1.00 182.93 ? 333 LYS B NZ 1 ATOM 5680 N N . SER B 1 335 ? 27.710 46.113 -11.109 1.00 155.08 ? 334 SER B N 1 ATOM 5681 C CA . SER B 1 335 ? 26.913 45.028 -11.691 1.00 151.51 ? 334 SER B CA 1 ATOM 5682 C C . SER B 1 335 ? 25.573 45.499 -12.279 1.00 150.78 ? 334 SER B C 1 ATOM 5683 O O . SER B 1 335 ? 25.141 44.992 -13.311 1.00 148.20 ? 334 SER B O 1 ATOM 5684 C CB . SER B 1 335 ? 26.653 43.946 -10.638 1.00 148.78 ? 334 SER B CB 1 ATOM 5685 O OG . SER B 1 335 ? 27.863 43.504 -10.042 1.00 149.18 ? 334 SER B OG 1 ATOM 5686 N N . ALA B 1 336 ? 24.934 46.478 -11.636 1.00 152.30 ? 335 ALA B N 1 ATOM 5687 C CA . ALA B 1 336 ? 23.616 46.975 -12.068 1.00 150.56 ? 335 ALA B CA 1 ATOM 5688 C C . ALA B 1 336 ? 23.610 47.705 -13.420 1.00 152.32 ? 335 ALA B C 1 ATOM 5689 O O . ALA B 1 336 ? 22.545 48.062 -13.925 1.00 148.26 ? 335 ALA B O 1 ATOM 5690 C CB . ALA B 1 336 ? 23.011 47.865 -10.991 1.00 149.77 ? 335 ALA B CB 1 ATOM 5691 N N . LEU B 1 337 ? 24.790 47.934 -13.994 1.00 157.90 ? 336 LEU B N 1 ATOM 5692 C CA . LEU B 1 337 ? 24.906 48.541 -15.321 1.00 164.12 ? 336 LEU B CA 1 ATOM 5693 C C . LEU B 1 337 ? 24.277 47.694 -16.421 1.00 163.89 ? 336 LEU B C 1 ATOM 5694 O O . LEU B 1 337 ? 23.759 48.235 -17.396 1.00 166.20 ? 336 LEU B O 1 ATOM 5695 C CB . LEU B 1 337 ? 26.376 48.769 -15.675 1.00 169.30 ? 336 LEU B CB 1 ATOM 5696 C CG . LEU B 1 337 ? 27.132 49.796 -14.832 1.00 173.81 ? 336 LEU B CG 1 ATOM 5697 C CD1 . LEU B 1 337 ? 28.616 49.749 -15.166 1.00 177.59 ? 336 LEU B CD1 1 ATOM 5698 C CD2 . LEU B 1 337 ? 26.561 51.192 -15.040 1.00 175.53 ? 336 LEU B CD2 1 ATOM 5699 N N . GLN B 1 338 ? 24.343 46.373 -16.273 1.00 162.32 ? 337 GLN B N 1 ATOM 5700 C CA . GLN B 1 338 ? 23.827 45.459 -17.290 1.00 163.77 ? 337 GLN B CA 1 ATOM 5701 C C . GLN B 1 338 ? 22.323 45.633 -17.479 1.00 162.92 ? 337 GLN B C 1 ATOM 5702 O O . GLN B 1 338 ? 21.832 45.632 -18.608 1.00 164.32 ? 337 GLN B O 1 ATOM 5703 C CB . GLN B 1 338 ? 24.146 44.005 -16.920 1.00 164.23 ? 337 GLN B CB 1 ATOM 5704 C CG . GLN B 1 338 ? 23.767 42.972 -17.978 1.00 164.33 ? 337 GLN B CG 1 ATOM 5705 C CD . GLN B 1 338 ? 24.517 43.146 -19.288 1.00 167.48 ? 337 GLN B CD 1 ATOM 5706 O OE1 . GLN B 1 338 ? 25.589 43.751 -19.332 1.00 170.37 ? 337 GLN B OE1 1 ATOM 5707 N NE2 . GLN B 1 338 ? 23.955 42.609 -20.365 1.00 167.81 ? 337 GLN B NE2 1 ATOM 5708 N N . CYS B 1 339 ? 21.601 45.777 -16.371 1.00 161.57 ? 338 CYS B N 1 ATOM 5709 C CA . CYS B 1 339 ? 20.166 46.054 -16.410 1.00 162.17 ? 338 CYS B CA 1 ATOM 5710 C C . CYS B 1 339 ? 19.926 47.385 -17.109 1.00 166.89 ? 338 CYS B C 1 ATOM 5711 O O . CYS B 1 339 ? 19.022 47.515 -17.937 1.00 166.69 ? 338 CYS B O 1 ATOM 5712 C CB . CYS B 1 339 ? 19.602 46.115 -14.992 1.00 160.87 ? 338 CYS B CB 1 ATOM 5713 S SG . CYS B 1 339 ? 20.238 44.817 -13.912 1.00 161.45 ? 338 CYS B SG 1 ATOM 5714 N N . GLN B 1 340 ? 20.755 48.365 -16.762 1.00 172.00 ? 339 GLN B N 1 ATOM 5715 C CA . GLN B 1 340 ? 20.723 49.684 -17.385 1.00 177.43 ? 339 GLN B CA 1 ATOM 5716 C C . GLN B 1 340 ? 20.907 49.542 -18.898 1.00 176.83 ? 339 GLN B C 1 ATOM 5717 O O . GLN B 1 340 ? 20.158 50.124 -19.683 1.00 178.65 ? 339 GLN B O 1 ATOM 5718 C CB . GLN B 1 340 ? 21.833 50.564 -16.791 1.00 184.41 ? 339 GLN B CB 1 ATOM 5719 C CG . GLN B 1 340 ? 21.496 52.041 -16.688 1.00 192.07 ? 339 GLN B CG 1 ATOM 5720 C CD . GLN B 1 340 ? 22.532 52.815 -15.887 1.00 199.14 ? 339 GLN B CD 1 ATOM 5721 O OE1 . GLN B 1 340 ? 23.666 52.360 -15.705 1.00 202.87 ? 339 GLN B OE1 1 ATOM 5722 N NE2 . GLN B 1 340 ? 22.148 53.992 -15.405 1.00 203.20 ? 339 GLN B NE2 1 ATOM 5723 N N . ALA B 1 341 ? 21.892 48.743 -19.297 1.00 174.98 ? 340 ALA B N 1 ATOM 5724 C CA . ALA B 1 341 ? 22.171 48.512 -20.712 1.00 174.05 ? 340 ALA B CA 1 ATOM 5725 C C . ALA B 1 341 ? 21.022 47.796 -21.416 1.00 170.68 ? 340 ALA B C 1 ATOM 5726 O O . ALA B 1 341 ? 20.736 48.083 -22.570 1.00 171.18 ? 340 ALA B O 1 ATOM 5727 C CB . ALA B 1 341 ? 23.460 47.724 -20.878 1.00 174.47 ? 340 ALA B CB 1 ATOM 5728 N N . TRP B 1 342 ? 20.365 46.866 -20.725 1.00 167.40 ? 341 TRP B N 1 ATOM 5729 C CA . TRP B 1 342 ? 19.229 46.137 -21.310 1.00 163.52 ? 341 TRP B CA 1 ATOM 5730 C C . TRP B 1 342 ? 18.004 47.012 -21.522 1.00 163.83 ? 341 TRP B C 1 ATOM 5731 O O . TRP B 1 342 ? 17.211 46.773 -22.434 1.00 162.44 ? 341 TRP B O 1 ATOM 5732 C CB . TRP B 1 342 ? 18.811 44.944 -20.446 1.00 160.06 ? 341 TRP B CB 1 ATOM 5733 C CG . TRP B 1 342 ? 19.717 43.763 -20.544 1.00 159.81 ? 341 TRP B CG 1 ATOM 5734 C CD1 . TRP B 1 342 ? 20.394 43.328 -21.652 1.00 161.20 ? 341 TRP B CD1 1 ATOM 5735 C CD2 . TRP B 1 342 ? 20.016 42.832 -19.501 1.00 156.23 ? 341 TRP B CD2 1 ATOM 5736 N NE1 . TRP B 1 342 ? 21.111 42.196 -21.353 1.00 158.59 ? 341 TRP B NE1 1 ATOM 5737 C CE2 . TRP B 1 342 ? 20.895 41.869 -20.040 1.00 155.18 ? 341 TRP B CE2 1 ATOM 5738 C CE3 . TRP B 1 342 ? 19.632 42.723 -18.157 1.00 153.16 ? 341 TRP B CE3 1 ATOM 5739 C CZ2 . TRP B 1 342 ? 21.397 40.816 -19.285 1.00 152.58 ? 341 TRP B CZ2 1 ATOM 5740 C CZ3 . TRP B 1 342 ? 20.132 41.675 -17.408 1.00 150.48 ? 341 TRP B CZ3 1 ATOM 5741 C CH2 . TRP B 1 342 ? 21.005 40.735 -17.974 1.00 150.83 ? 341 TRP B CH2 1 ATOM 5742 N N . GLN B 1 343 ? 17.848 48.019 -20.671 1.00 165.16 ? 342 GLN B N 1 ATOM 5743 C CA . GLN B 1 343 ? 16.738 48.957 -20.771 1.00 167.70 ? 342 GLN B CA 1 ATOM 5744 C C . GLN B 1 343 ? 16.597 49.526 -22.191 1.00 172.03 ? 342 GLN B C 1 ATOM 5745 O O . GLN B 1 343 ? 15.489 49.654 -22.697 1.00 172.56 ? 342 GLN B O 1 ATOM 5746 C CB . GLN B 1 343 ? 16.926 50.071 -19.733 1.00 170.38 ? 342 GLN B CB 1 ATOM 5747 C CG . GLN B 1 343 ? 15.665 50.831 -19.365 1.00 172.51 ? 342 GLN B CG 1 ATOM 5748 C CD . GLN B 1 343 ? 15.865 51.732 -18.155 1.00 176.09 ? 342 GLN B CD 1 ATOM 5749 O OE1 . GLN B 1 343 ? 16.993 52.091 -17.807 1.00 178.75 ? 342 GLN B OE1 1 ATOM 5750 N NE2 . GLN B 1 343 ? 14.768 52.100 -17.503 1.00 177.68 ? 342 GLN B NE2 1 ATOM 5751 N N . SER B 1 344 ? 17.724 49.834 -22.831 1.00 176.72 ? 343 SER B N 1 ATOM 5752 C CA . SER B 1 344 ? 17.739 50.403 -24.180 1.00 179.10 ? 343 SER B CA 1 ATOM 5753 C C . SER B 1 344 ? 17.729 49.357 -25.313 1.00 177.54 ? 343 SER B C 1 ATOM 5754 O O . SER B 1 344 ? 17.637 49.718 -26.482 1.00 180.74 ? 343 SER B O 1 ATOM 5755 C CB . SER B 1 344 ? 18.968 51.315 -24.330 1.00 181.85 ? 343 SER B CB 1 ATOM 5756 O OG . SER B 1 344 ? 20.172 50.626 -24.033 1.00 181.45 ? 343 SER B OG 1 ATOM 5757 N N . ARG B 1 345 ? 17.812 48.079 -24.971 1.00 176.09 ? 344 ARG B N 1 ATOM 5758 C CA . ARG B 1 345 ? 18.151 47.030 -25.941 1.00 179.60 ? 344 ARG B CA 1 ATOM 5759 C C . ARG B 1 345 ? 17.087 45.941 -26.126 1.00 174.89 ? 344 ARG B C 1 ATOM 5760 O O . ARG B 1 345 ? 17.286 45.019 -26.921 1.00 172.39 ? 344 ARG B O 1 ATOM 5761 C CB . ARG B 1 345 ? 19.473 46.377 -25.508 1.00 184.53 ? 344 ARG B CB 1 ATOM 5762 C CG . ARG B 1 345 ? 20.651 47.341 -25.416 1.00 192.33 ? 344 ARG B CG 1 ATOM 5763 C CD . ARG B 1 345 ? 21.387 47.587 -26.720 1.00 198.76 ? 344 ARG B CD 1 ATOM 5764 N NE . ARG B 1 345 ? 22.250 46.452 -27.057 1.00 203.00 ? 344 ARG B NE 1 ATOM 5765 C CZ . ARG B 1 345 ? 23.419 46.536 -27.696 1.00 208.67 ? 344 ARG B CZ 1 ATOM 5766 N NH1 . ARG B 1 345 ? 23.903 47.709 -28.099 1.00 212.80 ? 344 ARG B NH1 1 ATOM 5767 N NH2 . ARG B 1 345 ? 24.116 45.428 -27.933 1.00 208.71 ? 344 ARG B NH2 1 ATOM 5768 N N . GLN B 1 346 ? 15.960 46.033 -25.426 1.00 172.63 ? 345 GLN B N 1 ATOM 5769 C CA . GLN B 1 346 ? 14.999 44.914 -25.410 1.00 168.56 ? 345 GLN B CA 1 ATOM 5770 C C . GLN B 1 346 ? 13.581 45.435 -25.495 1.00 170.62 ? 345 GLN B C 1 ATOM 5771 O O . GLN B 1 346 ? 13.326 46.580 -25.147 1.00 176.55 ? 345 GLN B O 1 ATOM 5772 C CB . GLN B 1 346 ? 15.208 44.056 -24.163 1.00 165.08 ? 345 GLN B CB 1 ATOM 5773 C CG . GLN B 1 346 ? 13.995 43.306 -23.630 1.00 162.33 ? 345 GLN B CG 1 ATOM 5774 C CD . GLN B 1 346 ? 14.294 42.551 -22.350 1.00 159.24 ? 345 GLN B CD 1 ATOM 5775 O OE1 . GLN B 1 346 ? 15.361 42.707 -21.760 1.00 159.49 ? 345 GLN B OE1 1 ATOM 5776 N NE2 . GLN B 1 346 ? 13.342 41.744 -21.901 1.00 156.58 ? 345 GLN B NE2 1 ATOM 5777 N N . GLU B 1 347 ? 12.677 44.586 -25.970 1.00 170.73 ? 346 GLU B N 1 ATOM 5778 C CA . GLU B 1 347 ? 11.284 44.962 -26.217 1.00 177.25 ? 346 GLU B CA 1 ATOM 5779 C C . GLU B 1 347 ? 10.448 44.941 -24.944 1.00 174.78 ? 346 GLU B C 1 ATOM 5780 O O . GLU B 1 347 ? 9.633 45.836 -24.690 1.00 176.80 ? 346 GLU B O 1 ATOM 5781 C CB . GLU B 1 347 ? 10.668 43.964 -27.202 1.00 185.11 ? 346 GLU B CB 1 ATOM 5782 C CG . GLU B 1 347 ? 9.271 44.324 -27.700 1.00 193.22 ? 346 GLU B CG 1 ATOM 5783 C CD . GLU B 1 347 ? 8.627 43.225 -28.532 1.00 198.46 ? 346 GLU B CD 1 ATOM 5784 O OE1 . GLU B 1 347 ? 9.357 42.380 -29.099 1.00 202.63 ? 346 GLU B OE1 1 ATOM 5785 O OE2 . GLU B 1 347 ? 7.381 43.211 -28.626 1.00 200.97 ? 346 GLU B OE2 1 ATOM 5786 N N . HIS B 1 348 ? 10.612 43.888 -24.160 1.00 172.86 ? 347 HIS B N 1 ATOM 5787 C CA . HIS B 1 348 ? 9.839 43.783 -22.934 1.00 171.82 ? 347 HIS B CA 1 ATOM 5788 C C . HIS B 1 348 ? 10.330 44.825 -21.924 1.00 170.78 ? 347 HIS B C 1 ATOM 5789 O O . HIS B 1 348 ? 11.446 45.348 -22.025 1.00 171.58 ? 347 HIS B O 1 ATOM 5790 C CB . HIS B 1 348 ? 9.834 42.352 -22.366 1.00 171.44 ? 347 HIS B CB 1 ATOM 5791 C CG . HIS B 1 348 ? 8.623 41.548 -22.748 1.00 171.26 ? 347 HIS B CG 1 ATOM 5792 N ND1 . HIS B 1 348 ? 8.523 40.861 -23.940 1.00 171.70 ? 347 HIS B ND1 1 ATOM 5793 C CD2 . HIS B 1 348 ? 7.461 41.323 -22.089 1.00 170.45 ? 347 HIS B CD2 1 ATOM 5794 C CE1 . HIS B 1 348 ? 7.353 40.250 -23.998 1.00 171.26 ? 347 HIS B CE1 1 ATOM 5795 N NE2 . HIS B 1 348 ? 6.690 40.513 -22.888 1.00 170.52 ? 347 HIS B NE2 1 ATOM 5796 N N . GLN B 1 349 ? 9.465 45.146 -20.971 1.00 170.00 ? 348 GLN B N 1 ATOM 5797 C CA . GLN B 1 349 ? 9.756 46.169 -19.963 1.00 171.61 ? 348 GLN B CA 1 ATOM 5798 C C . GLN B 1 349 ? 10.915 45.788 -19.050 1.00 165.52 ? 348 GLN B C 1 ATOM 5799 O O . GLN B 1 349 ? 11.066 44.624 -18.693 1.00 164.38 ? 348 GLN B O 1 ATOM 5800 C CB . GLN B 1 349 ? 8.532 46.419 -19.080 1.00 176.35 ? 348 GLN B CB 1 ATOM 5801 C CG . GLN B 1 349 ? 7.351 47.061 -19.785 1.00 183.79 ? 348 GLN B CG 1 ATOM 5802 C CD . GLN B 1 349 ? 6.231 47.423 -18.825 1.00 188.41 ? 348 GLN B CD 1 ATOM 5803 O OE1 . GLN B 1 349 ? 6.305 47.140 -17.627 1.00 188.19 ? 348 GLN B OE1 1 ATOM 5804 N NE2 . GLN B 1 349 ? 5.183 48.051 -19.349 1.00 192.91 ? 348 GLN B NE2 1 ATOM 5805 N N . VAL B 1 350 ? 11.707 46.782 -18.663 1.00 162.70 ? 349 VAL B N 1 ATOM 5806 C CA . VAL B 1 350 ? 12.821 46.598 -17.729 1.00 161.18 ? 349 VAL B CA 1 ATOM 5807 C C . VAL B 1 350 ? 12.710 47.686 -16.664 1.00 161.95 ? 349 VAL B C 1 ATOM 5808 O O . VAL B 1 350 ? 12.851 48.864 -16.982 1.00 166.01 ? 349 VAL B O 1 ATOM 5809 C CB . VAL B 1 350 ? 14.186 46.724 -18.448 1.00 161.55 ? 349 VAL B CB 1 ATOM 5810 C CG1 . VAL B 1 350 ? 15.336 46.430 -17.491 1.00 161.34 ? 349 VAL B CG1 1 ATOM 5811 C CG2 . VAL B 1 350 ? 14.246 45.800 -19.655 1.00 160.66 ? 349 VAL B CG2 1 ATOM 5812 N N . LEU B 1 351 ? 12.442 47.299 -15.417 1.00 160.84 ? 350 LEU B N 1 ATOM 5813 C CA . LEU B 1 351 ? 12.288 48.263 -14.327 1.00 161.86 ? 350 LEU B CA 1 ATOM 5814 C C . LEU B 1 351 ? 13.462 48.126 -13.366 1.00 160.13 ? 350 LEU B C 1 ATOM 5815 O O . LEU B 1 351 ? 13.774 47.027 -12.923 1.00 156.99 ? 350 LEU B O 1 ATOM 5816 C CB . LEU B 1 351 ? 10.958 48.046 -13.590 1.00 162.57 ? 350 LEU B CB 1 ATOM 5817 C CG . LEU B 1 351 ? 9.681 48.402 -14.370 1.00 163.32 ? 350 LEU B CG 1 ATOM 5818 C CD1 . LEU B 1 351 ? 9.278 47.292 -15.337 1.00 161.32 ? 350 LEU B CD1 1 ATOM 5819 C CD2 . LEU B 1 351 ? 8.533 48.720 -13.419 1.00 163.14 ? 350 LEU B CD2 1 ATOM 5820 N N . LEU B 1 352 ? 14.123 49.237 -13.067 1.00 160.51 ? 351 LEU B N 1 ATOM 5821 C CA . LEU B 1 352 ? 15.233 49.234 -12.116 1.00 159.61 ? 351 LEU B CA 1 ATOM 5822 C C . LEU B 1 352 ? 14.761 49.771 -10.773 1.00 157.71 ? 351 LEU B C 1 ATOM 5823 O O . LEU B 1 352 ? 13.976 50.715 -10.720 1.00 158.78 ? 351 LEU B O 1 ATOM 5824 C CB . LEU B 1 352 ? 16.407 50.060 -12.650 1.00 163.55 ? 351 LEU B CB 1 ATOM 5825 C CG . LEU B 1 352 ? 17.415 49.293 -13.513 1.00 165.30 ? 351 LEU B CG 1 ATOM 5826 C CD1 . LEU B 1 352 ? 16.732 48.447 -14.580 1.00 164.68 ? 351 LEU B CD1 1 ATOM 5827 C CD2 . LEU B 1 352 ? 18.404 50.260 -14.149 1.00 169.79 ? 351 LEU B CD2 1 ATOM 5828 N N . GLN B 1 353 ? 15.236 49.168 -9.690 1.00 155.31 ? 352 GLN B N 1 ATOM 5829 C CA . GLN B 1 353 ? 14.826 49.581 -8.349 1.00 155.42 ? 352 GLN B CA 1 ATOM 5830 C C . GLN B 1 353 ? 15.983 49.550 -7.349 1.00 156.26 ? 352 GLN B C 1 ATOM 5831 O O . GLN B 1 353 ? 16.469 48.485 -6.972 1.00 149.63 ? 352 GLN B O 1 ATOM 5832 C CB . GLN B 1 353 ? 13.681 48.691 -7.854 1.00 152.98 ? 352 GLN B CB 1 ATOM 5833 C CG . GLN B 1 353 ? 13.040 49.127 -6.542 1.00 152.32 ? 352 GLN B CG 1 ATOM 5834 C CD . GLN B 1 353 ? 12.265 50.425 -6.664 1.00 154.49 ? 352 GLN B CD 1 ATOM 5835 O OE1 . GLN B 1 353 ? 11.041 50.421 -6.786 1.00 150.98 ? 352 GLN B OE1 1 ATOM 5836 N NE2 . GLN B 1 353 ? 12.978 51.545 -6.636 1.00 159.74 ? 352 GLN B NE2 1 ATOM 5837 N N . GLU B 1 354 ? 16.408 50.731 -6.912 1.00 161.47 ? 353 GLU B N 1 ATOM 5838 C CA . GLU B 1 354 ? 17.436 50.855 -5.874 1.00 163.37 ? 353 GLU B CA 1 ATOM 5839 C C . GLU B 1 354 ? 16.864 50.492 -4.499 1.00 163.11 ? 353 GLU B C 1 ATOM 5840 O O . GLU B 1 354 ? 15.708 50.790 -4.194 1.00 160.95 ? 353 GLU B O 1 ATOM 5841 C CB . GLU B 1 354 ? 17.998 52.286 -5.845 1.00 167.58 ? 353 GLU B CB 1 ATOM 5842 C CG . GLU B 1 354 ? 19.208 52.480 -4.932 1.00 170.38 ? 353 GLU B CG 1 ATOM 5843 C CD . GLU B 1 354 ? 19.747 53.907 -4.929 1.00 175.21 ? 353 GLU B CD 1 ATOM 5844 O OE1 . GLU B 1 354 ? 19.613 54.613 -5.952 1.00 177.63 ? 353 GLU B OE1 1 ATOM 5845 O OE2 . GLU B 1 354 ? 20.323 54.322 -3.899 1.00 175.88 ? 353 GLU B OE2 1 ATOM 5846 N N . LEU B 1 355 ? 17.692 49.850 -3.678 1.00 165.88 ? 354 LEU B N 1 ATOM 5847 C CA . LEU B 1 355 ? 17.340 49.509 -2.296 1.00 168.74 ? 354 LEU B CA 1 ATOM 5848 C C . LEU B 1 355 ? 18.393 50.074 -1.338 1.00 170.54 ? 354 LEU B C 1 ATOM 5849 O O . LEU B 1 355 ? 19.309 49.362 -0.917 1.00 165.63 ? 354 LEU B O 1 ATOM 5850 C CB . LEU B 1 355 ? 17.251 47.995 -2.143 1.00 170.01 ? 354 LEU B CB 1 ATOM 5851 C CG . LEU B 1 355 ? 16.035 47.354 -2.808 1.00 171.89 ? 354 LEU B CG 1 ATOM 5852 C CD1 . LEU B 1 355 ? 16.297 45.887 -3.109 1.00 170.79 ? 354 LEU B CD1 1 ATOM 5853 C CD2 . LEU B 1 355 ? 14.810 47.516 -1.917 1.00 175.10 ? 354 LEU B CD2 1 ATOM 5854 N N . PRO B 1 356 ? 18.267 51.365 -0.995 1.00 176.54 ? 355 PRO B N 1 ATOM 5855 C CA . PRO B 1 356 ? 19.322 52.013 -0.226 1.00 179.90 ? 355 PRO B CA 1 ATOM 5856 C C . PRO B 1 356 ? 19.429 51.469 1.189 1.00 179.02 ? 355 PRO B C 1 ATOM 5857 O O . PRO B 1 356 ? 18.425 51.395 1.898 1.00 177.66 ? 355 PRO B O 1 ATOM 5858 C CB . PRO B 1 356 ? 18.890 53.483 -0.209 1.00 184.47 ? 355 PRO B CB 1 ATOM 5859 C CG . PRO B 1 356 ? 17.407 53.440 -0.335 1.00 183.63 ? 355 PRO B CG 1 ATOM 5860 C CD . PRO B 1 356 ? 17.103 52.248 -1.197 1.00 179.85 ? 355 PRO B CD 1 ATOM 5861 N N . GLY B 1 357 ? 20.640 51.084 1.583 1.00 180.18 ? 356 GLY B N 1 ATOM 5862 C CA . GLY B 1 357 ? 20.896 50.577 2.926 1.00 182.59 ? 356 GLY B CA 1 ATOM 5863 C C . GLY B 1 357 ? 20.513 49.121 3.138 1.00 182.17 ? 356 GLY B C 1 ATOM 5864 O O . GLY B 1 357 ? 20.549 48.631 4.267 1.00 182.08 ? 356 GLY B O 1 ATOM 5865 N N . SER B 1 358 ? 20.156 48.415 2.066 1.00 181.10 ? 357 SER B N 1 ATOM 5866 C CA . SER B 1 358 ? 19.783 47.008 2.184 1.00 178.39 ? 357 SER B CA 1 ATOM 5867 C C . SER B 1 358 ? 20.981 46.107 1.882 1.00 178.32 ? 357 SER B C 1 ATOM 5868 O O . SER B 1 358 ? 21.584 46.178 0.801 1.00 179.67 ? 357 SER B O 1 ATOM 5869 C CB . SER B 1 358 ? 18.615 46.670 1.256 1.00 176.22 ? 357 SER B CB 1 ATOM 5870 O OG . SER B 1 358 ? 19.046 46.551 -0.085 1.00 177.37 ? 357 SER B OG 1 ATOM 5871 N N . GLU B 1 359 ? 21.322 45.258 2.847 1.00 177.57 ? 358 GLU B N 1 ATOM 5872 C CA . GLU B 1 359 ? 22.420 44.300 2.683 1.00 175.95 ? 358 GLU B CA 1 ATOM 5873 C C . GLU B 1 359 ? 22.021 43.152 1.749 1.00 171.70 ? 358 GLU B C 1 ATOM 5874 O O . GLU B 1 359 ? 20.842 42.810 1.611 1.00 168.42 ? 358 GLU B O 1 ATOM 5875 C CB . GLU B 1 359 ? 22.855 43.746 4.051 1.00 177.29 ? 358 GLU B CB 1 ATOM 5876 C CG . GLU B 1 359 ? 24.255 43.129 4.093 1.00 177.43 ? 358 GLU B CG 1 ATOM 5877 C CD . GLU B 1 359 ? 24.288 41.629 3.826 1.00 174.36 ? 358 GLU B CD 1 ATOM 5878 O OE1 . GLU B 1 359 ? 23.347 40.913 4.235 1.00 171.02 ? 358 GLU B OE1 1 ATOM 5879 O OE2 . GLU B 1 359 ? 25.269 41.157 3.210 1.00 172.09 ? 358 GLU B OE2 1 ATOM 5880 N N . HIS B 1 360 ? 23.034 42.561 1.126 1.00 170.31 ? 359 HIS B N 1 ATOM 5881 C CA . HIS B 1 360 ? 22.879 41.506 0.124 1.00 167.07 ? 359 HIS B CA 1 ATOM 5882 C C . HIS B 1 360 ? 21.888 40.397 0.508 1.00 166.99 ? 359 HIS B C 1 ATOM 5883 O O . HIS B 1 360 ? 21.030 40.030 -0.288 1.00 165.96 ? 359 HIS B O 1 ATOM 5884 C CB . HIS B 1 360 ? 24.265 40.925 -0.183 1.00 165.33 ? 359 HIS B CB 1 ATOM 5885 C CG . HIS B 1 360 ? 24.268 39.846 -1.216 1.00 162.38 ? 359 HIS B CG 1 ATOM 5886 N ND1 . HIS B 1 360 ? 24.004 38.534 -0.900 1.00 162.01 ? 359 HIS B ND1 1 ATOM 5887 C CD2 . HIS B 1 360 ? 24.537 39.868 -2.543 1.00 161.48 ? 359 HIS B CD2 1 ATOM 5888 C CE1 . HIS B 1 360 ? 24.091 37.795 -1.989 1.00 161.75 ? 359 HIS B CE1 1 ATOM 5889 N NE2 . HIS B 1 360 ? 24.415 38.578 -3.001 1.00 161.14 ? 359 HIS B NE2 1 ATOM 5890 N N . ILE B 1 361 ? 22.003 39.870 1.723 1.00 169.34 ? 360 ILE B N 1 ATOM 5891 C CA . ILE B 1 361 ? 21.112 38.806 2.186 1.00 168.27 ? 360 ILE B CA 1 ATOM 5892 C C . ILE B 1 361 ? 19.846 39.381 2.822 1.00 167.08 ? 360 ILE B C 1 ATOM 5893 O O . ILE B 1 361 ? 18.752 38.865 2.610 1.00 163.57 ? 360 ILE B O 1 ATOM 5894 C CB . ILE B 1 361 ? 21.824 37.870 3.193 1.00 168.92 ? 360 ILE B CB 1 ATOM 5895 C CG1 . ILE B 1 361 ? 22.983 37.125 2.513 1.00 168.69 ? 360 ILE B CG1 1 ATOM 5896 C CG2 . ILE B 1 361 ? 20.840 36.866 3.790 1.00 166.73 ? 360 ILE B CG2 1 ATOM 5897 C CD1 . ILE B 1 361 ? 24.302 37.870 2.516 1.00 171.67 ? 360 ILE B CD1 1 ATOM 5898 N N . GLU B 1 362 ? 20.000 40.449 3.597 1.00 168.57 ? 361 GLU B N 1 ATOM 5899 C CA . GLU B 1 362 ? 18.876 41.059 4.302 1.00 170.71 ? 361 GLU B CA 1 ATOM 5900 C C . GLU B 1 362 ? 17.765 41.520 3.362 1.00 165.96 ? 361 GLU B C 1 ATOM 5901 O O . GLU B 1 362 ? 16.607 41.585 3.759 1.00 163.79 ? 361 GLU B O 1 ATOM 5902 C CB . GLU B 1 362 ? 19.351 42.244 5.146 1.00 181.74 ? 361 GLU B CB 1 ATOM 5903 C CG . GLU B 1 362 ? 20.246 41.858 6.316 1.00 191.56 ? 361 GLU B CG 1 ATOM 5904 C CD . GLU B 1 362 ? 20.879 43.059 7.002 1.00 205.56 ? 361 GLU B CD 1 ATOM 5905 O OE1 . GLU B 1 362 ? 20.277 44.156 6.988 1.00 215.06 ? 361 GLU B OE1 1 ATOM 5906 O OE2 . GLU B 1 362 ? 21.986 42.906 7.564 1.00 214.91 ? 361 GLU B OE2 1 ATOM 5907 N N . MET B 1 363 ? 18.113 41.829 2.115 1.00 163.26 ? 362 MET B N 1 ATOM 5908 C CA . MET B 1 363 ? 17.122 42.281 1.139 1.00 161.35 ? 362 MET B CA 1 ATOM 5909 C C . MET B 1 363 ? 15.997 41.262 0.926 1.00 157.59 ? 362 MET B C 1 ATOM 5910 O O . MET B 1 363 ? 14.878 41.644 0.589 1.00 156.19 ? 362 MET B O 1 ATOM 5911 C CB . MET B 1 363 ? 17.788 42.609 -0.202 1.00 161.82 ? 362 MET B CB 1 ATOM 5912 C CG . MET B 1 363 ? 18.059 41.399 -1.087 1.00 161.93 ? 362 MET B CG 1 ATOM 5913 S SD . MET B 1 363 ? 18.863 41.795 -2.651 1.00 167.50 ? 362 MET B SD 1 ATOM 5914 C CE . MET B 1 363 ? 17.539 42.588 -3.555 1.00 168.59 ? 362 MET B CE 1 ATOM 5915 N N . LEU B 1 364 ? 16.295 39.976 1.122 1.00 154.95 ? 363 LEU B N 1 ATOM 5916 C CA . LEU B 1 364 ? 15.306 38.904 0.947 1.00 152.25 ? 363 LEU B CA 1 ATOM 5917 C C . LEU B 1 364 ? 14.206 38.880 2.003 1.00 154.32 ? 363 LEU B C 1 ATOM 5918 O O . LEU B 1 364 ? 13.153 38.287 1.777 1.00 151.57 ? 363 LEU B O 1 ATOM 5919 C CB . LEU B 1 364 ? 15.986 37.529 0.926 1.00 148.24 ? 363 LEU B CB 1 ATOM 5920 C CG . LEU B 1 364 ? 16.830 37.185 -0.300 1.00 145.81 ? 363 LEU B CG 1 ATOM 5921 C CD1 . LEU B 1 364 ? 17.475 35.821 -0.108 1.00 144.63 ? 363 LEU B CD1 1 ATOM 5922 C CD2 . LEU B 1 364 ? 15.990 37.205 -1.568 1.00 144.34 ? 363 LEU B CD2 1 ATOM 5923 N N . ALA B 1 365 ? 14.459 39.497 3.154 1.00 158.17 ? 364 ALA B N 1 ATOM 5924 C CA . ALA B 1 365 ? 13.484 39.556 4.235 1.00 161.88 ? 364 ALA B CA 1 ATOM 5925 C C . ALA B 1 365 ? 13.059 40.997 4.517 1.00 164.55 ? 364 ALA B C 1 ATOM 5926 O O . ALA B 1 365 ? 12.419 41.273 5.531 1.00 168.14 ? 364 ALA B O 1 ATOM 5927 C CB . ALA B 1 365 ? 14.073 38.923 5.485 1.00 162.92 ? 364 ALA B CB 1 ATOM 5928 N N . ASN B 1 366 ? 13.404 41.913 3.616 1.00 163.91 ? 365 ASN B N 1 ATOM 5929 C CA . ASN B 1 366 ? 13.138 43.329 3.828 1.00 165.15 ? 365 ASN B CA 1 ATOM 5930 C C . ASN B 1 366 ? 11.723 43.695 3.386 1.00 159.55 ? 365 ASN B C 1 ATOM 5931 O O . ASN B 1 366 ? 11.274 43.286 2.316 1.00 156.93 ? 365 ASN B O 1 ATOM 5932 C CB . ASN B 1 366 ? 14.167 44.183 3.083 1.00 170.41 ? 365 ASN B CB 1 ATOM 5933 C CG . ASN B 1 366 ? 14.085 45.647 3.468 1.00 179.69 ? 365 ASN B CG 1 ATOM 5934 O OD1 . ASN B 1 366 ? 13.005 46.236 3.450 1.00 183.77 ? 365 ASN B OD1 1 ATOM 5935 N ND2 . ASN B 1 366 ? 15.217 46.240 3.837 1.00 187.21 ? 365 ASN B ND2 1 ATOM 5936 N N . ALA B 1 367 ? 11.038 44.478 4.216 1.00 155.58 ? 366 ALA B N 1 ATOM 5937 C CA . ALA B 1 367 ? 9.643 44.856 3.976 1.00 152.21 ? 366 ALA B CA 1 ATOM 5938 C C . ALA B 1 367 ? 9.438 45.610 2.663 1.00 149.90 ? 366 ALA B C 1 ATOM 5939 O O . ALA B 1 367 ? 8.400 45.465 2.020 1.00 146.76 ? 366 ALA B O 1 ATOM 5940 C CB . ALA B 1 367 ? 9.117 45.681 5.139 1.00 154.19 ? 366 ALA B CB 1 ATOM 5941 N N . THR B 1 368 ? 10.420 46.418 2.273 1.00 151.33 ? 367 THR B N 1 ATOM 5942 C CA . THR B 1 368 ? 10.351 47.147 1.007 1.00 152.85 ? 367 THR B CA 1 ATOM 5943 C C . THR B 1 368 ? 10.445 46.190 -0.179 1.00 149.41 ? 367 THR B C 1 ATOM 5944 O O . THR B 1 368 ? 9.743 46.356 -1.174 1.00 148.50 ? 367 THR B O 1 ATOM 5945 C CB . THR B 1 368 ? 11.470 48.202 0.889 1.00 154.80 ? 367 THR B CB 1 ATOM 5946 O OG1 . THR B 1 368 ? 12.748 47.577 1.063 1.00 157.30 ? 367 THR B OG1 1 ATOM 5947 C CG2 . THR B 1 368 ? 11.290 49.295 1.932 1.00 155.55 ? 367 THR B CG2 1 ATOM 5948 N N . THR B 1 369 ? 11.312 45.187 -0.070 1.00 147.61 ? 368 THR B N 1 ATOM 5949 C CA . THR B 1 369 ? 11.429 44.161 -1.105 1.00 146.74 ? 368 THR B CA 1 ATOM 5950 C C . THR B 1 369 ? 10.107 43.416 -1.263 1.00 144.12 ? 368 THR B C 1 ATOM 5951 O O . THR B 1 369 ? 9.642 43.184 -2.380 1.00 142.90 ? 368 THR B O 1 ATOM 5952 C CB . THR B 1 369 ? 12.523 43.128 -0.755 1.00 146.22 ? 368 THR B CB 1 ATOM 5953 O OG1 . THR B 1 369 ? 13.740 43.807 -0.418 1.00 149.52 ? 368 THR B OG1 1 ATOM 5954 C CG2 . THR B 1 369 ? 12.774 42.178 -1.926 1.00 144.56 ? 368 THR B CG2 1 ATOM 5955 N N . LEU B 1 370 ? 9.512 43.050 -0.133 1.00 141.80 ? 369 LEU B N 1 ATOM 5956 C CA . LEU B 1 370 ? 8.257 42.306 -0.122 1.00 140.03 ? 369 LEU B CA 1 ATOM 5957 C C . LEU B 1 370 ? 7.101 43.144 -0.678 1.00 138.65 ? 369 LEU B C 1 ATOM 5958 O O . LEU B 1 370 ? 6.237 42.629 -1.389 1.00 136.36 ? 369 LEU B O 1 ATOM 5959 C CB . LEU B 1 370 ? 7.926 41.847 1.303 1.00 141.90 ? 369 LEU B CB 1 ATOM 5960 C CG . LEU B 1 370 ? 8.932 40.926 2.009 1.00 140.98 ? 369 LEU B CG 1 ATOM 5961 C CD1 . LEU B 1 370 ? 8.639 40.852 3.502 1.00 140.23 ? 369 LEU B CD1 1 ATOM 5962 C CD2 . LEU B 1 370 ? 8.942 39.537 1.390 1.00 139.33 ? 369 LEU B CD2 1 ATOM 5963 N N . ALA B 1 371 ? 7.094 44.434 -0.354 1.00 138.11 ? 370 ALA B N 1 ATOM 5964 C CA . ALA B 1 371 ? 6.088 45.352 -0.881 1.00 139.20 ? 370 ALA B CA 1 ATOM 5965 C C . ALA B 1 371 ? 6.178 45.462 -2.408 1.00 140.06 ? 370 ALA B C 1 ATOM 5966 O O . ALA B 1 371 ? 5.155 45.548 -3.092 1.00 143.61 ? 370 ALA B O 1 ATOM 5967 C CB . ALA B 1 371 ? 6.242 46.724 -0.243 1.00 141.06 ? 370 ALA B CB 1 ATOM 5968 N N . TYR B 1 372 ? 7.398 45.467 -2.941 1.00 137.39 ? 371 TYR B N 1 ATOM 5969 C CA . TYR B 1 372 ? 7.585 45.505 -4.392 1.00 135.29 ? 371 TYR B CA 1 ATOM 5970 C C . TYR B 1 372 ? 7.088 44.217 -5.034 1.00 132.23 ? 371 TYR B C 1 ATOM 5971 O O . TYR B 1 372 ? 6.419 44.244 -6.059 1.00 129.23 ? 371 TYR B O 1 ATOM 5972 C CB . TYR B 1 372 ? 9.048 45.737 -4.763 1.00 134.71 ? 371 TYR B CB 1 ATOM 5973 C CG . TYR B 1 372 ? 9.227 46.188 -6.197 1.00 135.43 ? 371 TYR B CG 1 ATOM 5974 C CD1 . TYR B 1 372 ? 9.146 47.537 -6.539 1.00 136.97 ? 371 TYR B CD1 1 ATOM 5975 C CD2 . TYR B 1 372 ? 9.465 45.269 -7.214 1.00 133.54 ? 371 TYR B CD2 1 ATOM 5976 C CE1 . TYR B 1 372 ? 9.307 47.955 -7.851 1.00 137.35 ? 371 TYR B CE1 1 ATOM 5977 C CE2 . TYR B 1 372 ? 9.626 45.680 -8.530 1.00 133.14 ? 371 TYR B CE2 1 ATOM 5978 C CZ . TYR B 1 372 ? 9.547 47.023 -8.845 1.00 134.45 ? 371 TYR B CZ 1 ATOM 5979 O OH . TYR B 1 372 ? 9.711 47.435 -10.151 1.00 133.41 ? 371 TYR B OH 1 ATOM 5980 N N . LEU B 1 373 ? 7.412 43.089 -4.421 1.00 132.96 ? 372 LEU B N 1 ATOM 5981 C CA . LEU B 1 373 ? 6.931 41.797 -4.892 1.00 134.44 ? 372 LEU B CA 1 ATOM 5982 C C . LEU B 1 373 ? 5.398 41.752 -4.929 1.00 135.47 ? 372 LEU B C 1 ATOM 5983 O O . LEU B 1 373 ? 4.806 41.270 -5.889 1.00 133.95 ? 372 LEU B O 1 ATOM 5984 C CB . LEU B 1 373 ? 7.463 40.691 -3.976 1.00 134.66 ? 372 LEU B CB 1 ATOM 5985 C CG . LEU B 1 373 ? 7.447 39.263 -4.519 1.00 134.46 ? 372 LEU B CG 1 ATOM 5986 C CD1 . LEU B 1 373 ? 8.333 39.139 -5.751 1.00 134.00 ? 372 LEU B CD1 1 ATOM 5987 C CD2 . LEU B 1 373 ? 7.899 38.298 -3.433 1.00 133.45 ? 372 LEU B CD2 1 ATOM 5988 N N . LYS B 1 374 ? 4.767 42.252 -3.873 1.00 137.24 ? 373 LYS B N 1 ATOM 5989 C CA . LYS B 1 374 ? 3.307 42.379 -3.818 1.00 141.59 ? 373 LYS B CA 1 ATOM 5990 C C . LYS B 1 374 ? 2.732 43.077 -5.054 1.00 147.25 ? 373 LYS B C 1 ATOM 5991 O O . LYS B 1 374 ? 1.743 42.620 -5.640 1.00 144.93 ? 373 LYS B O 1 ATOM 5992 C CB . LYS B 1 374 ? 2.909 43.183 -2.571 1.00 145.09 ? 373 LYS B CB 1 ATOM 5993 C CG . LYS B 1 374 ? 2.326 42.372 -1.425 1.00 146.32 ? 373 LYS B CG 1 ATOM 5994 C CD . LYS B 1 374 ? 0.823 42.583 -1.318 1.00 149.79 ? 373 LYS B CD 1 ATOM 5995 C CE . LYS B 1 374 ? 0.243 41.956 -0.062 1.00 151.72 ? 373 LYS B CE 1 ATOM 5996 N NZ . LYS B 1 374 ? -1.135 42.444 0.227 1.00 154.71 ? 373 LYS B NZ 1 ATOM 5997 N N . ARG B 1 375 ? 3.347 44.204 -5.413 1.00 155.49 ? 374 ARG B N 1 ATOM 5998 C CA . ARG B 1 375 ? 2.978 44.973 -6.610 1.00 163.43 ? 374 ARG B CA 1 ATOM 5999 C C . ARG B 1 375 ? 3.056 44.140 -7.881 1.00 160.74 ? 374 ARG B C 1 ATOM 6000 O O . ARG B 1 375 ? 2.175 44.211 -8.733 1.00 164.98 ? 374 ARG B O 1 ATOM 6001 C CB . ARG B 1 375 ? 3.903 46.165 -6.806 1.00 171.89 ? 374 ARG B CB 1 ATOM 6002 C CG . ARG B 1 375 ? 3.291 47.297 -7.631 1.00 180.23 ? 374 ARG B CG 1 ATOM 6003 C CD . ARG B 1 375 ? 4.153 47.678 -8.830 1.00 185.14 ? 374 ARG B CD 1 ATOM 6004 N NE . ARG B 1 375 ? 5.268 48.554 -8.498 1.00 188.47 ? 374 ARG B NE 1 ATOM 6005 C CZ . ARG B 1 375 ? 6.044 49.144 -9.405 1.00 190.00 ? 374 ARG B CZ 1 ATOM 6006 N NH1 . ARG B 1 375 ? 7.035 49.930 -9.005 1.00 191.43 ? 374 ARG B NH1 1 ATOM 6007 N NH2 . ARG B 1 375 ? 5.843 48.952 -10.709 1.00 188.73 ? 374 ARG B NH2 1 ATOM 6008 N N . VAL B 1 376 ? 4.140 43.383 -8.020 1.00 155.53 ? 375 VAL B N 1 ATOM 6009 C CA . VAL B 1 376 ? 4.338 42.556 -9.202 1.00 154.02 ? 375 VAL B CA 1 ATOM 6010 C C . VAL B 1 376 ? 3.262 41.470 -9.284 1.00 150.26 ? 375 VAL B C 1 ATOM 6011 O O . VAL B 1 376 ? 2.689 41.238 -10.349 1.00 147.53 ? 375 VAL B O 1 ATOM 6012 C CB . VAL B 1 376 ? 5.746 41.921 -9.218 1.00 154.11 ? 375 VAL B CB 1 ATOM 6013 C CG1 . VAL B 1 376 ? 5.878 40.916 -10.359 1.00 155.21 ? 375 VAL B CG1 1 ATOM 6014 C CG2 . VAL B 1 376 ? 6.812 43.003 -9.344 1.00 155.14 ? 375 VAL B CG2 1 ATOM 6015 N N . LEU B 1 377 ? 2.980 40.830 -8.152 1.00 149.08 ? 376 LEU B N 1 ATOM 6016 C CA . LEU B 1 377 ? 2.068 39.686 -8.102 1.00 150.48 ? 376 LEU B CA 1 ATOM 6017 C C . LEU B 1 377 ? 0.588 40.056 -8.179 1.00 155.43 ? 376 LEU B C 1 ATOM 6018 O O . LEU B 1 377 ? -0.180 39.409 -8.899 1.00 157.80 ? 376 LEU B O 1 ATOM 6019 C CB . LEU B 1 377 ? 2.303 38.889 -6.818 1.00 147.52 ? 376 LEU B CB 1 ATOM 6020 C CG . LEU B 1 377 ? 3.697 38.292 -6.632 1.00 144.84 ? 376 LEU B CG 1 ATOM 6021 C CD1 . LEU B 1 377 ? 3.830 37.733 -5.224 1.00 144.36 ? 376 LEU B CD1 1 ATOM 6022 C CD2 . LEU B 1 377 ? 3.980 37.221 -7.675 1.00 142.27 ? 376 LEU B CD2 1 ATOM 6023 N N . LEU B 1 378 ? 0.191 41.077 -7.422 1.00 160.83 ? 377 LEU B N 1 ATOM 6024 C CA . LEU B 1 378 ? -1.218 41.444 -7.291 1.00 165.72 ? 377 LEU B CA 1 ATOM 6025 C C . LEU B 1 378 ? -1.636 42.618 -8.181 1.00 167.02 ? 377 LEU B C 1 ATOM 6026 O O . LEU B 1 378 ? -2.825 42.810 -8.443 1.00 168.29 ? 377 LEU B O 1 ATOM 6027 C CB . LEU B 1 378 ? -1.550 41.733 -5.825 1.00 168.56 ? 377 LEU B CB 1 ATOM 6028 C CG . LEU B 1 378 ? -1.099 40.670 -4.811 1.00 168.71 ? 377 LEU B CG 1 ATOM 6029 C CD1 . LEU B 1 378 ? -1.695 40.957 -3.441 1.00 170.07 ? 377 LEU B CD1 1 ATOM 6030 C CD2 . LEU B 1 378 ? -1.463 39.260 -5.258 1.00 168.26 ? 377 LEU B CD2 1 ATOM 6031 N N . GLY B 1 379 ? -0.666 43.388 -8.665 1.00 166.72 ? 378 GLY B N 1 ATOM 6032 C CA . GLY B 1 379 ? -0.942 44.501 -9.577 1.00 168.41 ? 378 GLY B CA 1 ATOM 6033 C C . GLY B 1 379 ? -1.186 44.008 -10.993 1.00 169.67 ? 378 GLY B C 1 ATOM 6034 O O . GLY B 1 379 ? -0.863 42.860 -11.299 1.00 162.64 ? 378 GLY B O 1 ATOM 6035 N N . PRO B 1 380 ? -1.739 44.880 -11.867 1.00 174.47 ? 379 PRO B N 1 ATOM 6036 C CA . PRO B 1 380 ? -2.368 44.500 -13.144 1.00 175.31 ? 379 PRO B CA 1 ATOM 6037 C C . PRO B 1 380 ? -1.450 43.769 -14.110 1.00 173.50 ? 379 PRO B C 1 ATOM 6038 O O . PRO B 1 380 ? -0.267 44.079 -14.155 1.00 176.39 ? 379 PRO B O 1 ATOM 6039 C CB . PRO B 1 380 ? -2.794 45.848 -13.754 1.00 176.41 ? 379 PRO B CB 1 ATOM 6040 C CG . PRO B 1 380 ? -2.734 46.840 -12.643 1.00 176.73 ? 379 PRO B CG 1 ATOM 6041 C CD . PRO B 1 380 ? -1.682 46.346 -11.702 1.00 175.00 ? 379 PRO B CD 1 HETATM 6042 C C1 . NAG C 2 . ? 22.821 -2.403 34.936 1.00 163.71 ? 401 NAG A C1 1 HETATM 6043 C C2 . NAG C 2 . ? 24.195 -2.746 34.381 1.00 164.09 ? 401 NAG A C2 1 HETATM 6044 C C3 . NAG C 2 . ? 25.057 -3.272 35.521 1.00 170.52 ? 401 NAG A C3 1 HETATM 6045 C C4 . NAG C 2 . ? 25.011 -2.333 36.735 1.00 176.60 ? 401 NAG A C4 1 HETATM 6046 C C5 . NAG C 2 . ? 23.609 -1.807 37.065 1.00 171.13 ? 401 NAG A C5 1 HETATM 6047 C C6 . NAG C 2 . ? 23.608 -0.712 38.141 1.00 167.54 ? 401 NAG A C6 1 HETATM 6048 C C7 . NAG C 2 . ? 24.275 -3.462 32.040 1.00 156.56 ? 401 NAG A C7 1 HETATM 6049 C C8 . NAG C 2 . ? 24.156 -4.615 31.089 1.00 153.69 ? 401 NAG A C8 1 HETATM 6050 N N2 . NAG C 2 . ? 24.113 -3.748 33.333 1.00 160.52 ? 401 NAG A N2 1 HETATM 6051 O O3 . NAG C 2 . ? 26.373 -3.434 35.041 1.00 169.62 ? 401 NAG A O3 1 HETATM 6052 O O4 . NAG C 2 . ? 25.620 -2.884 37.899 1.00 186.00 ? 401 NAG A O4 1 HETATM 6053 O O5 . NAG C 2 . ? 22.973 -1.361 35.880 1.00 168.51 ? 401 NAG A O5 1 HETATM 6054 O O6 . NAG C 2 . ? 23.971 0.551 37.623 1.00 160.60 ? 401 NAG A O6 1 HETATM 6055 O O7 . NAG C 2 . ? 24.507 -2.332 31.608 1.00 154.94 ? 401 NAG A O7 1 HETATM 6056 C C1 . NAG D 2 . ? 27.029 -3.154 37.841 1.00 197.69 ? 402 NAG A C1 1 HETATM 6057 C C2 . NAG D 2 . ? 27.866 -1.875 37.651 1.00 201.87 ? 402 NAG A C2 1 HETATM 6058 C C3 . NAG D 2 . ? 29.287 -1.932 38.216 1.00 209.04 ? 402 NAG A C3 1 HETATM 6059 C C4 . NAG D 2 . ? 29.397 -2.820 39.446 1.00 216.09 ? 402 NAG A C4 1 HETATM 6060 C C5 . NAG D 2 . ? 28.797 -4.185 39.120 1.00 214.93 ? 402 NAG A C5 1 HETATM 6061 C C6 . NAG D 2 . ? 28.968 -5.181 40.267 1.00 219.27 ? 402 NAG A C6 1 HETATM 6062 C C7 . NAG D 2 . ? 27.738 -0.385 35.650 1.00 195.92 ? 402 NAG A C7 1 HETATM 6063 C C8 . NAG D 2 . ? 27.412 0.816 36.495 1.00 193.17 ? 402 NAG A C8 1 HETATM 6064 N N2 . NAG D 2 . ? 27.938 -1.582 36.222 1.00 199.47 ? 402 NAG A N2 1 HETATM 6065 O O3 . NAG D 2 . ? 29.743 -0.634 38.533 1.00 208.25 ? 402 NAG A O3 1 HETATM 6066 O O4 . NAG D 2 . ? 30.760 -2.919 39.821 1.00 222.54 ? 402 NAG A O4 1 HETATM 6067 O O5 . NAG D 2 . ? 27.416 -4.005 38.906 1.00 205.21 ? 402 NAG A O5 1 HETATM 6068 O O6 . NAG D 2 . ? 28.244 -6.365 40.015 1.00 220.57 ? 402 NAG A O6 1 HETATM 6069 O O7 . NAG D 2 . ? 27.814 -0.244 34.430 1.00 193.72 ? 402 NAG A O7 1 HETATM 6070 C C1 . BMA E 3 . ? 30.993 -2.779 41.226 1.00 222.69 ? 403 BMA A C1 1 HETATM 6071 C C2 . BMA E 3 . ? 32.404 -3.251 41.559 1.00 224.82 ? 403 BMA A C2 1 HETATM 6072 C C3 . BMA E 3 . ? 32.639 -3.106 43.058 1.00 225.29 ? 403 BMA A C3 1 HETATM 6073 C C4 . BMA E 3 . ? 32.259 -1.709 43.554 1.00 222.53 ? 403 BMA A C4 1 HETATM 6074 C C5 . BMA E 3 . ? 30.886 -1.282 43.033 1.00 216.13 ? 403 BMA A C5 1 HETATM 6075 C C6 . BMA E 3 . ? 30.556 0.166 43.389 1.00 210.66 ? 403 BMA A C6 1 HETATM 6076 O O2 . BMA E 3 . ? 33.345 -2.477 40.843 1.00 226.36 ? 403 BMA A O2 1 HETATM 6077 O O3 . BMA E 3 . ? 33.989 -3.375 43.361 1.00 229.10 ? 403 BMA A O3 1 HETATM 6078 O O4 . BMA E 3 . ? 32.239 -1.726 44.963 1.00 223.53 ? 403 BMA A O4 1 HETATM 6079 O O5 . BMA E 3 . ? 30.847 -1.429 41.626 1.00 219.82 ? 403 BMA A O5 1 HETATM 6080 O O6 . BMA E 3 . ? 29.175 0.275 43.657 1.00 201.40 ? 403 BMA A O6 1 HETATM 6081 C C1 . NAG F 2 . ? -6.360 -1.690 39.281 1.00 201.81 ? 404 NAG A C1 1 HETATM 6082 C C2 . NAG F 2 . ? -7.189 -2.178 40.465 1.00 207.30 ? 404 NAG A C2 1 HETATM 6083 C C3 . NAG F 2 . ? -6.696 -1.516 41.744 1.00 207.64 ? 404 NAG A C3 1 HETATM 6084 C C4 . NAG F 2 . ? -5.209 -1.814 41.911 1.00 206.82 ? 404 NAG A C4 1 HETATM 6085 C C5 . NAG F 2 . ? -4.417 -1.469 40.645 1.00 202.96 ? 404 NAG A C5 1 HETATM 6086 C C6 . NAG F 2 . ? -2.971 -1.950 40.744 1.00 200.81 ? 404 NAG A C6 1 HETATM 6087 C C7 . NAG F 2 . ? -9.564 -2.904 40.358 1.00 204.59 ? 404 NAG A C7 1 HETATM 6088 C C8 . NAG F 2 . ? -9.187 -4.303 40.760 1.00 202.28 ? 404 NAG A C8 1 HETATM 6089 N N2 . NAG F 2 . ? -8.615 -1.964 40.240 1.00 206.66 ? 404 NAG A N2 1 HETATM 6090 O O3 . NAG F 2 . ? -7.408 -2.021 42.852 1.00 209.32 ? 404 NAG A O3 1 HETATM 6091 O O4 . NAG F 2 . ? -4.713 -1.077 43.006 1.00 207.50 ? 404 NAG A O4 1 HETATM 6092 O O5 . NAG F 2 . ? -5.003 -2.034 39.484 1.00 203.50 ? 404 NAG A O5 1 HETATM 6093 O O6 . NAG F 2 . ? -2.916 -3.361 40.692 1.00 196.58 ? 404 NAG A O6 1 HETATM 6094 O O7 . NAG F 2 . ? -10.749 -2.651 40.146 1.00 204.09 ? 404 NAG A O7 1 HETATM 6095 C C1 . NAG G 2 . ? -12.631 -16.837 26.929 1.00 190.87 ? 405 NAG A C1 1 HETATM 6096 C C2 . NAG G 2 . ? -12.729 -18.213 26.267 1.00 194.62 ? 405 NAG A C2 1 HETATM 6097 C C3 . NAG G 2 . ? -14.167 -18.547 25.865 1.00 197.59 ? 405 NAG A C3 1 HETATM 6098 C C4 . NAG G 2 . ? -15.213 -18.118 26.891 1.00 201.05 ? 405 NAG A C4 1 HETATM 6099 C C5 . NAG G 2 . ? -14.938 -16.715 27.430 1.00 198.00 ? 405 NAG A C5 1 HETATM 6100 C C6 . NAG G 2 . ? -15.900 -16.329 28.553 1.00 198.02 ? 405 NAG A C6 1 HETATM 6101 C C7 . NAG G 2 . ? -10.844 -19.068 24.924 1.00 193.74 ? 405 NAG A C7 1 HETATM 6102 C C8 . NAG G 2 . ? -10.111 -18.974 23.619 1.00 190.28 ? 405 NAG A C8 1 HETATM 6103 N N2 . NAG G 2 . ? -11.899 -18.258 25.070 1.00 193.57 ? 405 NAG A N2 1 HETATM 6104 O O3 . NAG G 2 . ? -14.289 -19.933 25.632 1.00 198.37 ? 405 NAG A O3 1 HETATM 6105 O O4 . NAG G 2 . ? -16.481 -18.159 26.275 1.00 204.44 ? 405 NAG A O4 1 HETATM 6106 O O5 . NAG G 2 . ? -13.619 -16.663 27.924 1.00 196.09 ? 405 NAG A O5 1 HETATM 6107 O O6 . NAG G 2 . ? -15.600 -17.048 29.731 1.00 195.48 ? 405 NAG A O6 1 HETATM 6108 O O7 . NAG G 2 . ? -10.453 -19.859 25.782 1.00 196.27 ? 405 NAG A O7 1 HETATM 6109 C C1 . NAG H 2 . ? -12.982 17.353 9.961 1.00 189.49 ? 406 NAG A C1 1 HETATM 6110 C C2 . NAG H 2 . ? -12.874 16.265 8.884 1.00 191.15 ? 406 NAG A C2 1 HETATM 6111 C C3 . NAG H 2 . ? -14.243 15.927 8.284 1.00 195.66 ? 406 NAG A C3 1 HETATM 6112 C C4 . NAG H 2 . ? -15.376 15.884 9.316 1.00 196.98 ? 406 NAG A C4 1 HETATM 6113 C C5 . NAG H 2 . ? -15.296 17.078 10.269 1.00 193.88 ? 406 NAG A C5 1 HETATM 6114 C C6 . NAG H 2 . ? -16.408 17.081 11.321 1.00 190.60 ? 406 NAG A C6 1 HETATM 6115 C C7 . NAG H 2 . ? -10.636 16.582 7.893 1.00 183.09 ? 406 NAG A C7 1 HETATM 6116 C C8 . NAG H 2 . ? -9.867 17.052 6.692 1.00 182.00 ? 406 NAG A C8 1 HETATM 6117 N N2 . NAG H 2 . ? -11.966 16.674 7.815 1.00 188.33 ? 406 NAG A N2 1 HETATM 6118 O O3 . NAG H 2 . ? -14.172 14.715 7.561 1.00 193.68 ? 406 NAG A O3 1 HETATM 6119 O O4 . NAG H 2 . ? -16.622 15.880 8.651 1.00 199.27 ? 406 NAG A O4 1 HETATM 6120 O O5 . NAG H 2 . ? -14.020 17.071 10.881 1.00 193.55 ? 406 NAG A O5 1 HETATM 6121 O O6 . NAG H 2 . ? -15.872 17.136 12.626 1.00 182.39 ? 406 NAG A O6 1 HETATM 6122 O O7 . NAG H 2 . ? -10.034 16.148 8.876 1.00 178.24 ? 406 NAG A O7 1 HETATM 6123 C C1 . MAY I 4 . ? -0.397 8.996 18.216 1.00 160.58 ? 407 MAY A C1 1 HETATM 6124 O O1 . MAY I 4 . ? 1.021 8.739 20.547 1.00 166.45 ? 407 MAY A O1 1 HETATM 6125 P P1 . MAY I 4 . ? -0.328 8.517 19.978 1.00 169.95 ? 407 MAY A P1 1 HETATM 6126 C C2 . MAY I 4 . ? 0.969 9.215 17.596 1.00 152.43 ? 407 MAY A C2 1 HETATM 6127 O O2 . MAY I 4 . ? -0.725 6.955 20.143 1.00 174.53 ? 407 MAY A O2 1 HETATM 6128 C C3 . MAY I 4 . ? 0.841 9.733 16.169 1.00 142.87 ? 407 MAY A C3 1 HETATM 6129 C CM . MAY I 4 . ? -0.148 5.954 19.297 1.00 168.15 ? 407 MAY A CM 1 HETATM 6130 C C1 . NAG J 2 . ? 38.921 11.896 -17.220 1.00 182.55 ? 401 NAG B C1 1 HETATM 6131 C C2 . NAG J 2 . ? 39.170 10.592 -16.463 1.00 181.91 ? 401 NAG B C2 1 HETATM 6132 C C3 . NAG J 2 . ? 39.494 9.406 -17.386 1.00 186.59 ? 401 NAG B C3 1 HETATM 6133 C C4 . NAG J 2 . ? 39.084 9.498 -18.871 1.00 187.89 ? 401 NAG B C4 1 HETATM 6134 C C5 . NAG J 2 . ? 38.607 10.883 -19.322 1.00 183.76 ? 401 NAG B C5 1 HETATM 6135 C C6 . NAG J 2 . ? 37.644 10.816 -20.509 1.00 180.15 ? 401 NAG B C6 1 HETATM 6136 C C7 . NAG J 2 . ? 40.164 10.243 -14.226 1.00 172.63 ? 401 NAG B C7 1 HETATM 6137 C C8 . NAG J 2 . ? 41.354 10.491 -13.345 1.00 172.74 ? 401 NAG B C8 1 HETATM 6138 N N2 . NAG J 2 . ? 40.230 10.739 -15.469 1.00 178.15 ? 401 NAG B N2 1 HETATM 6139 O O3 . NAG J 2 . ? 38.921 8.250 -16.819 1.00 187.10 ? 401 NAG B O3 1 HETATM 6140 O O4 . NAG J 2 . ? 40.184 9.109 -19.684 1.00 193.93 ? 401 NAG B O4 1 HETATM 6141 O O5 . NAG J 2 . ? 38.015 11.616 -18.269 1.00 182.22 ? 401 NAG B O5 1 HETATM 6142 O O6 . NAG J 2 . ? 36.393 10.294 -20.116 1.00 172.98 ? 401 NAG B O6 1 HETATM 6143 O O7 . NAG J 2 . ? 39.205 9.614 -13.777 1.00 167.26 ? 401 NAG B O7 1 HETATM 6144 C C1 . NAG K 2 . ? 40.106 7.870 -20.409 1.00 200.75 ? 402 NAG B C1 1 HETATM 6145 C C2 . NAG K 2 . ? 39.867 6.609 -19.574 1.00 203.47 ? 402 NAG B C2 1 HETATM 6146 C C3 . NAG K 2 . ? 39.892 5.346 -20.447 1.00 209.03 ? 402 NAG B C3 1 HETATM 6147 C C4 . NAG K 2 . ? 39.296 5.507 -21.853 1.00 211.28 ? 402 NAG B C4 1 HETATM 6148 C C5 . NAG K 2 . ? 39.574 6.889 -22.460 1.00 209.50 ? 402 NAG B C5 1 HETATM 6149 C C6 . NAG K 2 . ? 38.798 7.115 -23.758 1.00 209.41 ? 402 NAG B C6 1 HETATM 6150 C C7 . NAG K 2 . ? 40.790 5.863 -17.358 1.00 203.40 ? 402 NAG B C7 1 HETATM 6151 C C8 . NAG K 2 . ? 39.531 5.145 -16.950 1.00 200.12 ? 402 NAG B C8 1 HETATM 6152 N N2 . NAG K 2 . ? 40.891 6.505 -18.536 1.00 205.34 ? 402 NAG B N2 1 HETATM 6153 O O3 . NAG K 2 . ? 39.165 4.334 -19.789 1.00 208.59 ? 402 NAG B O3 1 HETATM 6154 O O4 . NAG K 2 . ? 39.746 4.493 -22.762 1.00 218.55 ? 402 NAG B O4 1 HETATM 6155 O O5 . NAG K 2 . ? 39.260 7.916 -21.536 1.00 201.85 ? 402 NAG B O5 1 HETATM 6156 O O6 . NAG K 2 . ? 39.665 7.005 -24.868 1.00 213.70 ? 402 NAG B O6 1 HETATM 6157 O O7 . NAG K 2 . ? 41.734 5.847 -16.567 1.00 203.98 ? 402 NAG B O7 1 HETATM 6158 C C1 . BMA L 3 . ? 39.838 3.134 -22.281 1.00 219.99 ? 403 BMA B C1 1 HETATM 6159 C C2 . BMA L 3 . ? 38.571 2.297 -22.482 1.00 219.04 ? 403 BMA B C2 1 HETATM 6160 C C3 . BMA L 3 . ? 38.725 0.906 -21.865 1.00 218.18 ? 403 BMA B C3 1 HETATM 6161 C C4 . BMA L 3 . ? 40.020 0.251 -22.337 1.00 221.48 ? 403 BMA B C4 1 HETATM 6162 C C5 . BMA L 3 . ? 41.191 1.200 -22.083 1.00 221.19 ? 403 BMA B C5 1 HETATM 6163 C C6 . BMA L 3 . ? 42.539 0.599 -22.482 1.00 224.02 ? 403 BMA B C6 1 HETATM 6164 O O2 . BMA L 3 . ? 38.299 2.168 -23.861 1.00 223.37 ? 403 BMA B O2 1 HETATM 6165 O O3 . BMA L 3 . ? 37.619 0.091 -22.194 1.00 216.59 ? 403 BMA B O3 1 HETATM 6166 O O4 . BMA L 3 . ? 40.229 -0.959 -21.639 1.00 223.14 ? 403 BMA B O4 1 HETATM 6167 O O5 . BMA L 3 . ? 40.977 2.429 -22.752 1.00 222.52 ? 403 BMA B O5 1 HETATM 6168 O O6 . BMA L 3 . ? 42.463 -0.014 -23.749 1.00 224.50 ? 403 BMA B O6 1 HETATM 6169 C C1 . NAG M 2 . ? 36.086 40.519 -23.386 1.00 201.46 ? 404 NAG B C1 1 HETATM 6170 C C2 . NAG M 2 . ? 36.776 40.998 -24.661 1.00 201.66 ? 404 NAG B C2 1 HETATM 6171 C C3 . NAG M 2 . ? 36.253 40.178 -25.837 1.00 200.89 ? 404 NAG B C3 1 HETATM 6172 C C4 . NAG M 2 . ? 36.409 38.686 -25.540 1.00 199.22 ? 404 NAG B C4 1 HETATM 6173 C C5 . NAG M 2 . ? 35.784 38.315 -24.193 1.00 193.46 ? 404 NAG B C5 1 HETATM 6174 C C6 . NAG M 2 . ? 36.030 36.852 -23.832 1.00 188.07 ? 404 NAG B C6 1 HETATM 6175 C C7 . NAG M 2 . ? 37.401 43.426 -24.474 1.00 198.03 ? 404 NAG B C7 1 HETATM 6176 C C8 . NAG M 2 . ? 38.683 43.162 -23.732 1.00 198.08 ? 404 NAG B C8 1 HETATM 6177 N N2 . NAG M 2 . ? 36.584 42.432 -24.870 1.00 199.05 ? 404 NAG B N2 1 HETATM 6178 O O3 . NAG M 2 . ? 36.941 40.519 -27.021 1.00 202.34 ? 404 NAG B O3 1 HETATM 6179 O O4 . NAG M 2 . ? 35.807 37.927 -26.565 1.00 199.96 ? 404 NAG B O4 1 HETATM 6180 O O5 . NAG M 2 . ? 36.308 39.138 -23.170 1.00 197.66 ? 404 NAG B O5 1 HETATM 6181 O O6 . NAG M 2 . ? 34.839 36.115 -23.982 1.00 180.32 ? 404 NAG B O6 1 HETATM 6182 O O7 . NAG M 2 . ? 37.122 44.599 -24.710 1.00 198.30 ? 404 NAG B O7 1 HETATM 6183 C C1 . NAG N 2 . ? 50.310 48.819 -10.860 1.00 237.28 ? 405 NAG B C1 1 HETATM 6184 C C2 . NAG N 2 . ? 51.743 49.247 -11.183 1.00 243.08 ? 405 NAG B C2 1 HETATM 6185 C C3 . NAG N 2 . ? 52.017 50.653 -10.639 1.00 250.01 ? 405 NAG B C3 1 HETATM 6186 C C4 . NAG N 2 . ? 50.860 51.623 -10.894 1.00 249.88 ? 405 NAG B C4 1 HETATM 6187 C C5 . NAG N 2 . ? 49.528 50.991 -10.484 1.00 243.68 ? 405 NAG B C5 1 HETATM 6188 C C6 . NAG N 2 . ? 48.322 51.888 -10.750 1.00 241.74 ? 405 NAG B C6 1 HETATM 6189 C C7 . NAG N 2 . ? 52.981 47.119 -11.190 1.00 236.06 ? 405 NAG B C7 1 HETATM 6190 C C8 . NAG N 2 . ? 54.006 46.277 -10.489 1.00 236.31 ? 405 NAG B C8 1 HETATM 6191 N N2 . NAG N 2 . ? 52.710 48.303 -10.634 1.00 240.33 ? 405 NAG B N2 1 HETATM 6192 O O3 . NAG N 2 . ? 53.217 51.168 -11.176 1.00 256.14 ? 405 NAG B O3 1 HETATM 6193 O O4 . NAG N 2 . ? 51.082 52.821 -10.180 1.00 253.34 ? 405 NAG B O4 1 HETATM 6194 O O5 . NAG N 2 . ? 49.370 49.803 -11.223 1.00 238.87 ? 405 NAG B O5 1 HETATM 6195 O O6 . NAG N 2 . ? 47.127 51.172 -10.501 1.00 234.77 ? 405 NAG B O6 1 HETATM 6196 O O7 . NAG N 2 . ? 52.442 46.700 -12.214 1.00 232.84 ? 405 NAG B O7 1 HETATM 6197 C C1 . NAG O 2 . ? 15.209 47.629 4.278 1.00 194.73 ? 406 NAG B C1 1 HETATM 6198 C C2 . NAG O 2 . ? 16.176 47.882 5.430 1.00 197.60 ? 406 NAG B C2 1 HETATM 6199 C C3 . NAG O 2 . ? 16.120 49.363 5.820 1.00 203.08 ? 406 NAG B C3 1 HETATM 6200 C C4 . NAG O 2 . ? 16.206 50.306 4.615 1.00 205.10 ? 406 NAG B C4 1 HETATM 6201 C C5 . NAG O 2 . ? 15.253 49.857 3.504 1.00 201.13 ? 406 NAG B C5 1 HETATM 6202 C C6 . NAG O 2 . ? 15.360 50.717 2.243 1.00 199.93 ? 406 NAG B C6 1 HETATM 6203 C C7 . NAG O 2 . ? 16.261 45.838 6.881 1.00 191.87 ? 406 NAG B C7 1 HETATM 6204 C C8 . NAG O 2 . ? 17.275 45.128 6.031 1.00 188.87 ? 406 NAG B C8 1 HETATM 6205 N N2 . NAG O 2 . ? 15.804 47.062 6.578 1.00 194.72 ? 406 NAG B N2 1 HETATM 6206 O O3 . NAG O 2 . ? 17.134 49.655 6.755 1.00 206.04 ? 406 NAG B O3 1 HETATM 6207 O O4 . NAG O 2 . ? 15.909 51.632 5.012 1.00 204.13 ? 406 NAG B O4 1 HETATM 6208 O O5 . NAG O 2 . ? 15.494 48.494 3.196 1.00 197.59 ? 406 NAG B O5 1 HETATM 6209 O O6 . NAG O 2 . ? 16.061 50.035 1.225 1.00 193.45 ? 406 NAG B O6 1 HETATM 6210 O O7 . NAG O 2 . ? 15.860 45.251 7.883 1.00 193.18 ? 406 NAG B O7 1 HETATM 6211 C C1 . MAY P 4 . ? 25.777 35.159 -2.792 1.00 179.10 ? 407 MAY B C1 1 HETATM 6212 O O1 . MAY P 4 . ? 25.400 33.628 -5.015 1.00 181.60 ? 407 MAY B O1 1 HETATM 6213 P P1 . MAY P 4 . ? 25.698 35.019 -4.607 1.00 184.45 ? 407 MAY B P1 1 HETATM 6214 C C2 . MAY P 4 . ? 26.656 34.095 -2.133 1.00 175.55 ? 407 MAY B C2 1 HETATM 6215 O O2 . MAY P 4 . ? 27.060 35.549 -5.307 1.00 189.07 ? 407 MAY B O2 1 HETATM 6216 C C3 . MAY P 4 . ? 27.398 34.627 -0.911 1.00 171.09 ? 407 MAY B C3 1 HETATM 6217 C CM . MAY P 4 . ? 28.365 35.302 -4.777 1.00 190.94 ? 407 MAY B CM 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 . HIS A 5 ? 1.9548 1.6256 2.0134 0.1243 0.0702 -0.0408 4 HIS A N 2 C CA . HIS A 5 ? 1.9157 1.6395 2.0062 0.1181 0.0547 -0.0393 4 HIS A CA 3 C C . HIS A 5 ? 1.8935 1.6322 1.9907 0.0894 0.0532 -0.0467 4 HIS A C 4 O O . HIS A 5 ? 1.9127 1.6276 1.9946 0.0716 0.0584 -0.0494 4 HIS A O 5 C CB . HIS A 5 ? 1.9437 1.6738 2.0355 0.1256 0.0448 -0.0292 4 HIS A CB 6 C CG . HIS A 5 ? 2.0032 1.6979 2.0704 0.1126 0.0519 -0.0263 4 HIS A CG 7 N ND1 . HIS A 5 ? 2.0809 1.7299 2.1177 0.1262 0.0605 -0.0198 4 HIS A ND1 8 C CD2 . HIS A 5 ? 1.9887 1.6871 2.0585 0.0878 0.0526 -0.0289 4 HIS A CD2 9 C CE1 . HIS A 5 ? 2.0833 1.7080 2.1046 0.1087 0.0681 -0.0187 4 HIS A CE1 10 N NE2 . HIS A 5 ? 2.0492 1.7053 2.0924 0.0852 0.0632 -0.0245 4 HIS A NE2 11 N N . PRO A 6 ? 1.8634 1.6413 1.9839 0.0850 0.0461 -0.0503 5 PRO A N 12 C CA . PRO A 6 ? 1.8378 1.6275 1.9613 0.0604 0.0435 -0.0572 5 PRO A CA 13 C C . PRO A 6 ? 1.7640 1.5754 1.9008 0.0465 0.0331 -0.0533 5 PRO A C 14 O O . PRO A 6 ? 1.7634 1.5906 1.9117 0.0565 0.0261 -0.0454 5 PRO A O 15 C CB . PRO A 6 ? 1.8386 1.6583 1.9785 0.0638 0.0413 -0.0608 5 PRO A CB 16 C CG . PRO A 6 ? 1.8231 1.6658 1.9837 0.0854 0.0366 -0.0539 5 PRO A CG 17 C CD . PRO A 6 ? 1.8502 1.6611 1.9946 0.1019 0.0413 -0.0489 5 PRO A CD 18 N N . PRO A 7 ? 1.7196 1.5321 1.8551 0.0241 0.0315 -0.0593 6 PRO A N 19 C CA . PRO A 7 ? 1.6850 1.5205 1.8364 0.0110 0.0225 -0.0563 6 PRO A CA 20 C C . PRO A 7 ? 1.6448 1.5230 1.8207 0.0157 0.0109 -0.0520 6 PRO A C 21 O O . PRO A 7 ? 1.6279 1.5216 1.8100 0.0212 0.0095 -0.0543 6 PRO A O 22 C CB . PRO A 7 ? 1.6922 1.5231 1.8396 -0.0119 0.0221 -0.0657 6 PRO A CB 23 C CG . PRO A 7 ? 1.7252 1.5388 1.8556 -0.0108 0.0278 -0.0738 6 PRO A CG 24 C CD . PRO A 7 ? 1.7508 1.5414 1.8690 0.0103 0.0378 -0.0699 6 PRO A CD 25 N N . VAL A 8 ? 1.6104 1.5049 1.7990 0.0128 0.0044 -0.0462 7 VAL A N 26 C CA . VAL A 8 ? 1.5886 1.5192 1.7987 0.0177 -0.0056 -0.0419 7 VAL A CA 27 C C . VAL A 8 ? 1.5398 1.4910 1.7635 0.0023 -0.0125 -0.0415 7 VAL A C 28 O O . VAL A 8 ? 1.5480 1.4887 1.7694 -0.0061 -0.0100 -0.0404 7 VAL A O 29 C CB . VAL A 8 ? 1.5968 1.5286 1.8091 0.0351 -0.0082 -0.0343 7 VAL A CB 30 C CG1 . VAL A 8 ? 1.5662 1.5341 1.8010 0.0376 -0.0188 -0.0312 7 VAL A CG1 31 C CG2 . VAL A 8 ? 1.6112 1.5275 1.8145 0.0534 -0.0033 -0.0342 7 VAL A CG2 32 N N . VAL A 9 ? 1.4580 1.4374 1.6963 -0.0003 -0.0199 -0.0422 8 VAL A N 33 C CA . VAL A 9 ? 1.4162 1.4177 1.6691 -0.0112 -0.0274 -0.0408 8 VAL A CA 34 C C . VAL A 9 ? 1.4117 1.4373 1.6801 -0.0024 -0.0335 -0.0351 8 VAL A C 35 O O . VAL A 9 ? 1.4325 1.4695 1.7059 0.0050 -0.0345 -0.0354 8 VAL A O 36 C CB . VAL A 9 ? 1.3953 1.4057 1.6480 -0.0227 -0.0317 -0.0467 8 VAL A CB 37 C CG1 . VAL A 9 ? 1.3382 1.3694 1.6061 -0.0330 -0.0399 -0.0452 8 VAL A CG1 38 C CG2 . VAL A 9 ? 1.4573 1.4421 1.6921 -0.0309 -0.0263 -0.0544 8 VAL A CG2 39 N N . LEU A 10 ? 1.3738 1.4058 1.6497 -0.0042 -0.0363 -0.0306 9 LEU A N 40 C CA . LEU A 10 ? 1.3772 1.4288 1.6656 0.0026 -0.0422 -0.0260 9 LEU A CA 41 C C . LEU A 10 ? 1.3960 1.4693 1.6983 -0.0065 -0.0478 -0.0255 9 LEU A C 42 O O . LEU A 10 ? 1.4105 1.4841 1.7158 -0.0163 -0.0479 -0.0258 9 LEU A O 43 C CB . LEU A 10 ? 1.4155 1.4558 1.6981 0.0084 -0.0409 -0.0212 9 LEU A CB 44 C CG . LEU A 10 ? 1.4274 1.4415 1.6918 0.0194 -0.0357 -0.0201 9 LEU A CG 45 C CD1 . LEU A 10 ? 1.4198 1.4214 1.6740 0.0257 -0.0353 -0.0146 9 LEU A CD1 46 C CD2 . LEU A 10 ? 1.4338 1.4542 1.7011 0.0327 -0.0386 -0.0215 9 LEU A CD2 47 N N . VAL A 11 ? 1.3935 1.4847 1.7054 -0.0030 -0.0519 -0.0247 10 VAL A N 48 C CA . VAL A 11 ? 1.3781 1.4868 1.7002 -0.0095 -0.0566 -0.0234 10 VAL A CA 49 C C . VAL A 11 ? 1.3940 1.5151 1.7268 -0.0044 -0.0598 -0.0196 10 VAL A C 50 O O . VAL A 11 ? 1.3800 1.5070 1.7174 0.0024 -0.0603 -0.0201 10 VAL A O 51 C CB . VAL A 11 ? 1.3771 1.4911 1.6966 -0.0116 -0.0566 -0.0260 10 VAL A CB 52 C CG1 . VAL A 11 ? 1.3532 1.4800 1.6781 -0.0176 -0.0619 -0.0238 10 VAL A CG1 53 C CG2 . VAL A 11 ? 1.4208 1.5188 1.7255 -0.0152 -0.0532 -0.0311 10 VAL A CG2 54 N N . PRO A 12 ? 1.4454 1.5707 1.7835 -0.0080 -0.0618 -0.0166 11 PRO A N 55 C CA . PRO A 12 ? 1.4392 1.5724 1.7842 -0.0039 -0.0644 -0.0138 11 PRO A CA 56 C C . PRO A 12 ? 1.4111 1.5590 1.7654 -0.0057 -0.0670 -0.0132 11 PRO A C 57 O O . PRO A 12 ? 1.4165 1.5680 1.7703 -0.0102 -0.0670 -0.0137 11 PRO A O 58 C CB . PRO A 12 ? 1.4617 1.5915 1.8077 -0.0077 -0.0627 -0.0112 11 PRO A CB 59 C CG . PRO A 12 ? 1.4628 1.5949 1.8120 -0.0162 -0.0623 -0.0127 11 PRO A CG 60 C CD . PRO A 12 ? 1.4675 1.5903 1.8069 -0.0163 -0.0609 -0.0165 11 PRO A CD 61 N N . GLY A 13 ? 1.3586 1.5121 1.7186 -0.0024 -0.0690 -0.0122 12 GLY A N 62 C CA . GLY A 13 ? 1.3444 1.5079 1.7124 -0.0049 -0.0697 -0.0113 12 GLY A CA 63 C C . GLY A 13 ? 1.3520 1.5163 1.7221 -0.0075 -0.0703 -0.0077 12 GLY A C 64 O O . GLY A 13 ? 1.2875 1.4475 1.6557 -0.0086 -0.0696 -0.0062 12 GLY A O 65 N N . ASP A 14 ? 1.3817 1.5508 1.7567 -0.0085 -0.0703 -0.0065 13 ASP A N 66 C CA . ASP A 14 ? 1.3741 1.5428 1.7513 -0.0091 -0.0700 -0.0030 13 ASP A CA 67 C C . ASP A 14 ? 1.3849 1.5473 1.7596 -0.0062 -0.0696 -0.0034 13 ASP A C 68 O O . ASP A 14 ? 1.4015 1.5606 1.7726 -0.0033 -0.0714 -0.0064 13 ASP A O 69 C CB . ASP A 14 ? 1.4035 1.5735 1.7835 -0.0103 -0.0686 -0.0020 13 ASP A CB 70 C CG . ASP A 14 ? 1.4608 1.6286 1.8416 -0.0096 -0.0676 0.0024 13 ASP A CG 71 O OD1 . ASP A 14 ? 1.5276 1.6958 1.9104 -0.0081 -0.0680 0.0043 13 ASP A OD1 72 O OD2 . ASP A 14 ? 1.4337 1.5988 1.8140 -0.0105 -0.0653 0.0042 13 ASP A OD2 73 N N . LEU A 15 ? 1.3924 1.5527 1.7685 -0.0064 -0.0671 -0.0005 14 LEU A N 74 C CA . LEU A 15 ? 1.3969 1.5476 1.7672 -0.0038 -0.0637 -0.0003 14 LEU A CA 75 C C . LEU A 15 ? 1.3839 1.5260 1.7450 -0.0024 -0.0627 -0.0019 14 LEU A C 76 O O . LEU A 15 ? 1.3763 1.5059 1.7265 0.0008 -0.0596 -0.0017 14 LEU A O 77 C CB . LEU A 15 ? 1.3991 1.5437 1.7634 -0.0010 -0.0647 -0.0020 14 LEU A CB 78 C CG . LEU A 15 ? 1.3477 1.4966 1.7181 -0.0027 -0.0652 -0.0017 14 LEU A CG 79 C CD1 . LEU A 15 ? 1.3503 1.4986 1.7189 -0.0031 -0.0694 -0.0067 14 LEU A CD1 80 N N . GLY A 16 ? 1.3988 1.5443 1.7613 -0.0045 -0.0644 -0.0032 15 GLY A N 81 C CA . GLY A 16 ? 1.3991 1.5340 1.7511 -0.0018 -0.0637 -0.0049 15 GLY A CA 82 C C . GLY A 16 ? 1.4125 1.5375 1.7608 -0.0050 -0.0573 -0.0040 15 GLY A C 83 O O . GLY A 16 ? 1.4745 1.5855 1.8106 -0.0023 -0.0550 -0.0047 15 GLY A O 84 N N . ASN A 17 ? 1.4015 1.5332 1.7613 -0.0107 -0.0540 -0.0027 16 ASN A N 85 C CA . ASN A 17 ? 1.4175 1.5421 1.7790 -0.0160 -0.0466 -0.0029 16 ASN A CA 86 C C . ASN A 17 ? 1.3996 1.5301 1.7745 -0.0187 -0.0405 -0.0009 16 ASN A C 87 O O . ASN A 17 ? 1.3645 1.5081 1.7502 -0.0173 -0.0440 0.0005 16 ASN A O 88 C CB . ASN A 17 ? 1.4309 1.5611 1.7984 -0.0228 -0.0494 -0.0063 16 ASN A CB 89 C CG . ASN A 17 ? 1.4140 1.5642 1.7965 -0.0262 -0.0569 -0.0067 16 ASN A CG 90 O OD1 . ASN A 17 ? 1.3969 1.5581 1.7953 -0.0308 -0.0567 -0.0067 16 ASN A OD1 91 N ND2 . ASN A 17 ? 1.4151 1.5696 1.7924 -0.0234 -0.0633 -0.0071 16 ASN A ND2 92 N N . GLN A 18 ? 1.4314 1.5506 1.8052 -0.0221 -0.0300 -0.0008 17 GLN A N 93 C CA . GLN A 18 ? 1.4726 1.5970 1.8613 -0.0246 -0.0210 0.0007 17 GLN A CA 94 C C . GLN A 18 ? 1.5070 1.6578 1.9247 -0.0300 -0.0266 -0.0008 17 GLN A C 95 O O . GLN A 18 ? 1.5472 1.7073 1.9704 -0.0348 -0.0351 -0.0039 17 GLN A O 96 C CB . GLN A 18 ? 1.5100 1.6160 1.8930 -0.0291 -0.0061 0.0006 17 GLN A CB 97 C CG . GLN A 18 ? 1.5311 1.6073 1.8811 -0.0215 -0.0002 0.0032 17 GLN A CG 98 C CD . GLN A 18 ? 1.5733 1.6268 1.9139 -0.0249 0.0181 0.0047 17 GLN A CD 99 O OE1 . GLN A 18 ? 1.5695 1.6324 1.9334 -0.0338 0.0282 0.0034 17 GLN A OE1 100 N NE2 . GLN A 18 ? 1.6219 1.6451 1.9285 -0.0174 0.0227 0.0075 17 GLN A NE2 101 N N . LEU A 19 ? 1.5229 1.6844 1.9571 -0.0281 -0.0223 0.0012 18 LEU A N 102 C CA . LEU A 19 ? 1.5229 1.7107 1.9873 -0.0311 -0.0278 0.0002 18 LEU A CA 103 C C . LEU A 19 ? 1.5083 1.7020 1.9947 -0.0331 -0.0141 0.0005 18 LEU A C 104 O O . LEU A 19 ? 1.4637 1.6415 1.9387 -0.0285 -0.0017 0.0033 18 LEU A O 105 C CB . LEU A 19 ? 1.5144 1.7126 1.9795 -0.0234 -0.0381 0.0033 18 LEU A CB 106 C CG . LEU A 19 ? 1.5362 1.7314 1.9839 -0.0220 -0.0500 0.0029 18 LEU A CG 107 C CD1 . LEU A 19 ? 1.5331 1.7325 1.9788 -0.0147 -0.0555 0.0067 18 LEU A CD1 108 C CD2 . LEU A 19 ? 1.5566 1.7629 2.0113 -0.0287 -0.0593 -0.0008 18 LEU A CD2 109 N N . GLU A 20 ? 1.4795 1.6960 1.9973 -0.0399 -0.0165 -0.0028 19 GLU A N 110 C CA . GLU A 20 ? 1.4515 1.6789 1.9985 -0.0432 -0.0026 -0.0037 19 GLU A CA 111 C C . GLU A 20 ? 1.3861 1.6462 1.9682 -0.0394 -0.0120 -0.0038 19 GLU A C 112 O O . GLU A 20 ? 1.3118 1.5877 1.8986 -0.0389 -0.0304 -0.0052 19 GLU A O 113 C CB . GLU A 20 ? 1.5008 1.7268 2.0596 -0.0570 0.0055 -0.0094 19 GLU A CB 114 C CG . GLU A 20 ? 1.5973 1.7875 2.1237 -0.0594 0.0205 -0.0082 19 GLU A CG 115 C CD . GLU A 20 ? 1.6832 1.8677 2.2194 -0.0738 0.0302 -0.0138 19 GLU A CD 116 O OE1 . GLU A 20 ? 1.6988 1.9099 2.2699 -0.0835 0.0244 -0.0199 19 GLU A OE1 117 O OE2 . GLU A 20 ? 1.7531 1.9054 2.2612 -0.0754 0.0434 -0.0123 19 GLU A OE2 118 N N . ALA A 21 ? 1.3825 1.6514 1.9877 -0.0359 0.0009 -0.0023 20 ALA A N 119 C CA . ALA A 21 ? 1.4030 1.7036 2.0443 -0.0297 -0.0070 -0.0018 20 ALA A CA 120 C C . ALA A 21 ? 1.4444 1.7648 2.1285 -0.0346 0.0080 -0.0052 20 ALA A C 121 O O . ALA A 21 ? 1.4655 1.7682 2.1450 -0.0399 0.0297 -0.0056 20 ALA A O 122 C CB . ALA A 21 ? 1.3930 1.6856 2.0195 -0.0149 -0.0080 0.0048 20 ALA A CB 123 N N . LYS A 22 ? 1.4791 1.8361 2.2048 -0.0325 -0.0034 -0.0076 21 LYS A N 124 C CA . LYS A 22 ? 1.4964 1.8804 2.2726 -0.0354 0.0091 -0.0112 21 LYS A CA 125 C C . LYS A 22 ? 1.4262 1.8343 2.2272 -0.0189 0.0011 -0.0070 21 LYS A C 126 O O . LYS A 22 ? 1.4045 1.8233 2.2000 -0.0109 -0.0221 -0.0049 21 LYS A O 127 C CB . LYS A 22 ? 1.5419 1.9530 2.3531 -0.0512 0.0001 -0.0209 21 LYS A CB 128 C CG . LYS A 22 ? 1.5924 2.0208 2.4498 -0.0619 0.0215 -0.0267 21 LYS A CG 129 C CD . LYS A 22 ? 1.6387 2.1095 2.5520 -0.0530 0.0189 -0.0277 21 LYS A CD 130 C CE . LYS A 22 ? 1.6706 2.1647 2.6377 -0.0666 0.0389 -0.0356 21 LYS A CE 131 N NZ . LYS A 22 ? 1.6823 2.2124 2.7022 -0.0549 0.0445 -0.0349 21 LYS A NZ 132 N N . LEU A 23 ? 1.3791 1.7926 2.2046 -0.0129 0.0215 -0.0053 22 LEU A N 133 C CA . LEU A 23 ? 1.3741 1.8037 2.2188 0.0051 0.0182 -0.0003 22 LEU A CA 134 C C . LEU A 23 ? 1.3879 1.8623 2.2989 0.0064 0.0206 -0.0048 22 LEU A C 135 O O . LEU A 23 ? 1.3823 1.8649 2.3229 -0.0045 0.0413 -0.0100 22 LEU A O 136 C CB . LEU A 23 ? 1.3976 1.7941 2.2140 0.0146 0.0411 0.0057 22 LEU A CB 137 C CG . LEU A 23 ? 1.4360 1.7878 2.1899 0.0136 0.0424 0.0093 22 LEU A CG 138 C CD1 . LEU A 23 ? 1.4665 1.7897 2.1978 0.0238 0.0633 0.0138 22 LEU A CD1 139 C CD2 . LEU A 23 ? 1.4346 1.7845 2.1640 0.0187 0.0161 0.0123 22 LEU A CD2 140 N N . ASP A 24 ? 1.4266 1.9292 2.3605 0.0205 -0.0003 -0.0027 23 ASP A N 141 C CA . ASP A 24 ? 1.4652 2.0102 2.4617 0.0294 0.0013 -0.0047 23 ASP A CA 142 C C . ASP A 24 ? 1.4586 2.0074 2.4490 0.0531 -0.0144 0.0035 23 ASP A C 143 O O . ASP A 24 ? 1.4223 2.0018 2.4353 0.0609 -0.0410 0.0028 23 ASP A O 144 C CB . ASP A 24 ? 1.5072 2.0970 2.5542 0.0168 -0.0156 -0.0150 23 ASP A CB 145 C CG . ASP A 24 ? 1.5600 2.1992 2.6797 0.0251 -0.0137 -0.0186 23 ASP A CG 146 O OD1 . ASP A 24 ? 1.5825 2.2186 2.7188 0.0341 0.0121 -0.0151 23 ASP A OD1 147 O OD2 . ASP A 24 ? 1.6305 2.3122 2.7914 0.0230 -0.0384 -0.0255 23 ASP A OD2 148 N N . LYS A 25 ? 1.4882 2.0026 2.4448 0.0646 0.0021 0.0111 24 LYS A N 149 C CA . LYS A 25 ? 1.5423 2.0455 2.4770 0.0853 -0.0099 0.0199 24 LYS A CA 150 C C . LYS A 25 ? 1.5630 2.0953 2.5461 0.1045 -0.0056 0.0223 24 LYS A C 151 O O . LYS A 25 ? 1.5411 2.0839 2.5584 0.1037 0.0187 0.0193 24 LYS A O 152 C CB . LYS A 25 ? 1.5858 2.0374 2.4624 0.0878 0.0061 0.0257 24 LYS A CB 153 C CG . LYS A 25 ? 1.6166 2.0385 2.4458 0.0711 0.0035 0.0236 24 LYS A CG 154 C CD . LYS A 25 ? 1.6471 2.0223 2.4227 0.0747 0.0157 0.0285 24 LYS A CD 155 C CE . LYS A 25 ? 1.6627 2.0247 2.4117 0.0881 -0.0002 0.0353 24 LYS A CE 156 N NZ . LYS A 25 ? 1.6870 2.0049 2.3836 0.0871 0.0080 0.0379 24 LYS A NZ 157 N N . PRO A 26 ? 1.6077 2.1512 2.5925 0.1229 -0.0283 0.0281 25 PRO A N 158 C CA . PRO A 26 ? 1.6481 2.2164 2.6758 0.1449 -0.0253 0.0316 25 PRO A CA 159 C C . PRO A 26 ? 1.7135 2.2452 2.7174 0.1574 0.0022 0.0380 25 PRO A C 160 O O . PRO A 26 ? 1.7804 2.3285 2.8248 0.1679 0.0209 0.0376 25 PRO A O 161 C CB . PRO A 26 ? 1.6387 2.2179 2.6586 0.1612 -0.0588 0.0374 25 PRO A CB 162 C CG . PRO A 26 ? 1.6283 2.1688 2.5830 0.1513 -0.0696 0.0401 25 PRO A CG 163 C CD . PRO A 26 ? 1.6159 2.1467 2.5605 0.1253 -0.0564 0.0321 25 PRO A CD 164 N N . THR A 27 ? 1.7429 2.2257 2.6827 0.1559 0.0049 0.0431 26 THR A N 165 C CA . THR A 27 ? 1.7558 2.1977 2.6646 0.1646 0.0300 0.0476 26 THR A CA 166 C C . THR A 27 ? 1.7374 2.1317 2.5811 0.1511 0.0336 0.0479 26 THR A C 167 O O . THR A 27 ? 1.7023 2.0945 2.5237 0.1393 0.0150 0.0467 26 THR A O 168 C CB . THR A 27 ? 1.7857 2.2200 2.6913 0.1908 0.0246 0.0564 26 THR A CB 169 O OG1 . THR A 27 ? 1.8116 2.2498 2.7003 0.1960 -0.0059 0.0611 26 THR A OG1 170 C CG2 . THR A 27 ? 1.7872 2.2602 2.7563 0.2082 0.0322 0.0563 26 THR A CG2 171 N N . VAL A 28 ? 1.7575 2.1142 2.5717 0.1535 0.0573 0.0490 27 VAL A N 172 C CA . VAL A 28 ? 1.7800 2.0922 2.5352 0.1417 0.0618 0.0483 27 VAL A CA 173 C C . VAL A 28 ? 1.8361 2.1086 2.5555 0.1547 0.0717 0.0530 27 VAL A C 174 O O . VAL A 28 ? 1.8996 2.1757 2.6385 0.1728 0.0791 0.0570 27 VAL A O 175 C CB . VAL A 28 ? 1.7834 2.0838 2.5311 0.1258 0.0827 0.0420 27 VAL A CB 176 C CG1 . VAL A 28 ? 1.8025 2.1285 2.5672 0.1086 0.0709 0.0371 27 VAL A CG1 177 C CG2 . VAL A 28 ? 1.7956 2.1019 2.5741 0.1335 0.1101 0.0406 27 VAL A CG2 178 N N . VAL A 29 ? 1.8446 2.0793 2.5126 0.1451 0.0716 0.0521 28 VAL A N 179 C CA . VAL A 29 ? 1.8600 2.0535 2.4899 0.1537 0.0798 0.0549 28 VAL A CA 180 C C . VAL A 29 ? 1.8550 2.0232 2.4758 0.1577 0.1080 0.0519 28 VAL A C 181 O O . VAL A 29 ? 1.9314 2.0733 2.5364 0.1704 0.1178 0.0544 28 VAL A O 182 C CB . VAL A 29 ? 1.8756 2.0398 2.4572 0.1412 0.0689 0.0536 28 VAL A CB 183 C CG1 . VAL A 29 ? 1.8615 2.0449 2.4472 0.1395 0.0437 0.0573 28 VAL A CG1 184 C CG2 . VAL A 29 ? 1.8898 2.0423 2.4505 0.1236 0.0753 0.0466 28 VAL A CG2 185 N N . HIS A 30 ? 1.8096 1.9820 2.4368 0.1471 0.1220 0.0465 29 HIS A N 186 C CA . HIS A 30 ? 1.8097 1.9564 2.4253 0.1504 0.1506 0.0434 29 HIS A CA 187 C C . HIS A 30 ? 1.7404 1.9158 2.3978 0.1473 0.1662 0.0407 29 HIS A C 188 O O . HIS A 30 ? 1.6892 1.8934 2.3689 0.1356 0.1554 0.0390 29 HIS A O 189 C CB . HIS A 30 ? 1.8717 1.9750 2.4299 0.1380 0.1554 0.0385 29 HIS A CB 190 C CG . HIS A 30 ? 1.9378 2.0086 2.4557 0.1402 0.1459 0.0392 29 HIS A CG 191 N ND1 . HIS A 30 ? 2.0380 2.0862 2.5473 0.1546 0.1560 0.0414 29 HIS A ND1 192 C CD2 . HIS A 30 ? 1.9384 1.9949 2.4237 0.1291 0.1286 0.0375 29 HIS A CD2 193 C CE1 . HIS A 30 ? 2.0646 2.0850 2.5371 0.1510 0.1455 0.0408 29 HIS A CE1 194 N NE2 . HIS A 30 ? 2.0044 2.0309 2.4636 0.1354 0.1288 0.0383 29 HIS A NE2 195 N N . TYR A 31 ? 1.7281 1.8933 2.3952 0.1571 0.1933 0.0400 30 TYR A N 196 C CA . TYR A 31 ? 1.7526 1.9432 2.4624 0.1548 0.2137 0.0373 30 TYR A CA 197 C C . TYR A 31 ? 1.7958 1.9767 2.4861 0.1351 0.2203 0.0327 30 TYR A C 198 O O . TYR A 31 ? 1.8260 2.0378 2.5565 0.1271 0.2262 0.0305 30 TYR A O 199 C CB . TYR A 31 ? 1.7801 1.9519 2.4936 0.1691 0.2454 0.0371 30 TYR A CB 200 C CG . TYR A 31 ? 1.7837 1.9801 2.5400 0.1907 0.2439 0.0417 30 TYR A CG 201 C CD1 . TYR A 31 ? 1.8103 1.9813 2.5387 0.2043 0.2352 0.0459 30 TYR A CD1 202 C CD2 . TYR A 31 ? 1.7731 2.0182 2.5992 0.1978 0.2510 0.0416 30 TYR A CD2 203 C CE1 . TYR A 31 ? 1.8263 2.0167 2.5912 0.2262 0.2338 0.0511 30 TYR A CE1 204 C CE2 . TYR A 31 ? 1.7677 2.0371 2.6346 0.2199 0.2481 0.0461 30 TYR A CE2 205 C CZ . TYR A 31 ? 1.8040 2.0444 2.6382 0.2350 0.2394 0.0514 30 TYR A CZ 206 O OH . TYR A 31 ? 1.8328 2.0940 2.7045 0.2590 0.2364 0.0567 30 TYR A OH 207 N N . LEU A 32 ? 1.8435 1.9811 2.4726 0.1273 0.2190 0.0309 31 LEU A N 208 C CA . LEU A 32 ? 1.8698 1.9922 2.4732 0.1110 0.2247 0.0274 31 LEU A CA 209 C C . LEU A 32 ? 1.8332 1.9802 2.4455 0.0975 0.1988 0.0271 31 LEU A C 210 O O . LEU A 32 ? 1.8611 1.9978 2.4556 0.0846 0.2024 0.0247 31 LEU A O 211 C CB . LEU A 32 ? 1.9243 1.9916 2.4585 0.1090 0.2320 0.0250 31 LEU A CB 212 C CG . LEU A 32 ? 1.9537 2.0002 2.4502 0.1109 0.2100 0.0252 31 LEU A CG 213 C CD1 . LEU A 32 ? 1.9639 1.9791 2.4067 0.0991 0.2013 0.0215 31 LEU A CD1 214 C CD2 . LEU A 32 ? 1.9944 2.0143 2.4748 0.1251 0.2221 0.0253 31 LEU A CD2 215 N N . CYS A 33 ? 1.7998 1.9759 2.4362 0.1011 0.1737 0.0297 32 CYS A N 216 C CA . CYS A 33 ? 1.8015 2.0025 2.4493 0.0892 0.1502 0.0290 32 CYS A CA 217 C C . CYS A 33 ? 1.7594 2.0028 2.4646 0.0837 0.1544 0.0268 32 CYS A C 218 O O . CYS A 33 ? 1.7491 2.0197 2.5003 0.0937 0.1622 0.0276 32 CYS A O 219 C CB . CYS A 33 ? 1.8099 2.0231 2.4579 0.0951 0.1226 0.0325 32 CYS A CB 220 S SG . CYS A 33 ? 1.8069 1.9759 2.3976 0.1010 0.1168 0.0345 32 CYS A SG 221 N N . SER A 34 ? 1.7110 1.9604 2.4150 0.0679 0.1489 0.0237 33 SER A N 222 C CA . SER A 34 ? 1.6809 1.9687 2.4378 0.0591 0.1520 0.0200 33 SER A CA 223 C C . SER A 34 ? 1.6143 1.9463 2.4129 0.0629 0.1250 0.0202 33 SER A C 224 O O . SER A 34 ? 1.5445 1.8741 2.3207 0.0627 0.1001 0.0220 33 SER A O 225 C CB . SER A 34 ? 1.7134 1.9891 2.4513 0.0408 0.1537 0.0165 33 SER A CB 226 O OG . SER A 34 ? 1.8094 2.0431 2.5069 0.0386 0.1785 0.0167 33 SER A OG 227 N N . LYS A 35 ? 1.6099 1.9818 2.4690 0.0666 0.1304 0.0180 34 LYS A N 228 C CA . LYS A 35 ? 1.6075 2.0258 2.5114 0.0701 0.1039 0.0170 34 LYS A CA 229 C C . LYS A 35 ? 1.5576 1.9962 2.4771 0.0508 0.0913 0.0105 34 LYS A C 230 O O . LYS A 35 ? 1.4892 1.9464 2.4120 0.0495 0.0627 0.0098 34 LYS A O 231 C CB . LYS A 35 ? 1.6394 2.0968 2.6078 0.0819 0.1138 0.0160 34 LYS A CB 232 C CG . LYS A 35 ? 1.6507 2.1078 2.6200 0.1059 0.1083 0.0228 34 LYS A CG 233 C CD . LYS A 35 ? 1.6586 2.1671 2.7011 0.1179 0.1075 0.0211 34 LYS A CD 234 C CE . LYS A 35 ? 1.6862 2.1949 2.7294 0.1439 0.0984 0.0287 34 LYS A CE 235 N NZ . LYS A 35 ? 1.7314 2.2049 2.7536 0.1559 0.1288 0.0324 34 LYS A NZ 236 N N . LYS A 36 ? 1.5670 1.9993 2.4943 0.0360 0.1141 0.0057 35 LYS A N 237 C CA . LYS A 36 ? 1.5985 2.0513 2.5490 0.0168 0.1075 -0.0015 35 LYS A CA 238 C C . LYS A 36 ? 1.6122 2.0243 2.5199 0.0015 0.1258 -0.0026 35 LYS A C 239 O O . LYS A 36 ? 1.6415 2.0214 2.5246 0.0038 0.1528 0.0000 35 LYS A O 240 C CB . LYS A 36 ? 1.6538 2.1528 2.6790 0.0132 0.1184 -0.0079 35 LYS A CB 241 C CG . LYS A 36 ? 1.7217 2.2503 2.7811 -0.0065 0.1066 -0.0172 35 LYS A CG 242 C CD . LYS A 36 ? 1.7813 2.3615 2.9217 -0.0096 0.1150 -0.0246 35 LYS A CD 243 C CE . LYS A 36 ? 1.8253 2.4379 3.0020 -0.0299 0.0986 -0.0355 35 LYS A CE 244 N NZ . LYS A 36 ? 1.8345 2.4686 3.0079 -0.0248 0.0566 -0.0365 35 LYS A NZ 245 N N . THR A 37 ? 1.5989 2.0107 2.4953 -0.0129 0.1106 -0.0066 36 THR A N 246 C CA . THR A 37 ? 1.5962 1.9753 2.4621 -0.0285 0.1273 -0.0087 36 THR A CA 247 C C . THR A 37 ? 1.5721 1.9807 2.4846 -0.0470 0.1282 -0.0177 36 THR A C 248 O O . THR A 37 ? 1.5310 1.9794 2.4814 -0.0492 0.1043 -0.0227 36 THR A O 249 C CB . THR A 37 ? 1.6033 1.9489 2.4084 -0.0298 0.1106 -0.0057 36 THR A CB 250 O OG1 . THR A 37 ? 1.5763 1.9472 2.3921 -0.0312 0.0793 -0.0082 36 THR A OG1 251 C CG2 . THR A 37 ? 1.6183 1.9318 2.3767 -0.0146 0.1123 0.0016 36 THR A CG2 252 N N . GLU A 38 ? 1.5723 1.9590 2.4797 -0.0605 0.1557 -0.0201 37 GLU A N 253 C CA . GLU A 38 ? 1.5868 1.9957 2.5369 -0.0809 0.1615 -0.0294 37 GLU A CA 254 C C . GLU A 38 ? 1.5830 1.9846 2.5098 -0.0930 0.1389 -0.0335 37 GLU A C 255 O O . GLU A 38 ? 1.5762 2.0066 2.5426 -0.1081 0.1301 -0.0428 37 GLU A O 256 C CB . GLU A 38 ? 1.6500 2.0297 2.5948 -0.0914 0.2016 -0.0297 37 GLU A CB 257 C CG . GLU A 38 ? 1.6870 2.0762 2.6622 -0.0820 0.2288 -0.0276 37 GLU A CG 258 C CD . GLU A 38 ? 1.7685 2.1198 2.7267 -0.0908 0.2711 -0.0264 37 GLU A CD 259 O OE1 . GLU A 38 ? 1.7989 2.1187 2.7267 -0.1054 0.2797 -0.0277 37 GLU A OE1 260 O OE2 . GLU A 38 ? 1.7895 2.1398 2.7626 -0.0824 0.2971 -0.0241 37 GLU A OE2 261 N N . SER A 39 ? 1.5931 1.9561 2.4565 -0.0866 0.1299 -0.0272 38 SER A N 262 C CA . SER A 39 ? 1.6179 1.9684 2.4532 -0.0958 0.1110 -0.0301 38 SER A CA 263 C C . SER A 39 ? 1.6033 1.9350 2.3892 -0.0812 0.0901 -0.0231 38 SER A C 264 O O . SER A 39 ? 1.5654 1.8950 2.3415 -0.0655 0.0897 -0.0168 38 SER A O 265 C CB . SER A 39 ? 1.6821 1.9915 2.4871 -0.1090 0.1347 -0.0307 38 SER A CB 266 O OG . SER A 39 ? 1.7289 1.9979 2.4904 -0.0989 0.1557 -0.0223 38 SER A OG 267 N N . TYR A 40 ? 1.6233 1.9413 2.3797 -0.0868 0.0738 -0.0249 39 TYR A N 268 C CA . TYR A 40 ? 1.6417 1.9378 2.3496 -0.0752 0.0580 -0.0188 39 TYR A CA 269 C C . TYR A 40 ? 1.6605 1.9128 2.3218 -0.0692 0.0770 -0.0123 39 TYR A C 270 O O . TYR A 40 ? 1.6455 1.8746 2.2973 -0.0774 0.0985 -0.0130 39 TYR A O 271 C CB . TYR A 40 ? 1.6453 1.9368 2.3349 -0.0831 0.0391 -0.0230 39 TYR A CB 272 C CG . TYR A 40 ? 1.6360 1.9621 2.3488 -0.0816 0.0118 -0.0266 39 TYR A CG 273 C CD1 . TYR A 40 ? 1.6251 1.9849 2.3839 -0.0929 0.0046 -0.0354 39 TYR A CD1 274 C CD2 . TYR A 40 ? 1.6398 1.9636 2.3273 -0.0690 -0.0069 -0.0216 39 TYR A CD2 275 C CE1 . TYR A 40 ? 1.6162 2.0056 2.3915 -0.0901 -0.0223 -0.0388 39 TYR A CE1 276 C CE2 . TYR A 40 ? 1.6230 1.9736 2.3253 -0.0665 -0.0312 -0.0241 39 TYR A CE2 277 C CZ . TYR A 40 ? 1.6146 1.9973 2.3590 -0.0763 -0.0398 -0.0325 39 TYR A CZ 278 O OH . TYR A 40 ? 1.6308 2.0383 2.3857 -0.0725 -0.0658 -0.0350 39 TYR A OH 279 N N . PHE A 41 ? 1.6729 1.9129 2.3043 -0.0550 0.0689 -0.0062 40 PHE A N 280 C CA . PHE A 41 ? 1.6842 1.8842 2.2693 -0.0480 0.0822 -0.0009 40 PHE A CA 281 C C . PHE A 41 ? 1.6970 1.8845 2.2455 -0.0399 0.0624 0.0018 40 PHE A C 282 O O . PHE A 41 ? 1.6490 1.8586 2.2093 -0.0374 0.0423 0.0011 40 PHE A O 283 C CB . PHE A 41 ? 1.6410 1.8382 2.2325 -0.0387 0.0992 0.0024 40 PHE A CB 284 C CG . PHE A 41 ? 1.5833 1.7941 2.1774 -0.0257 0.0849 0.0055 40 PHE A CG 285 C CD1 . PHE A 41 ? 1.5329 1.7824 2.1700 -0.0233 0.0725 0.0040 40 PHE A CD1 286 C CD2 . PHE A 41 ? 1.5950 1.7785 2.1477 -0.0156 0.0836 0.0095 40 PHE A CD2 287 C CE1 . PHE A 41 ? 1.5306 1.7880 2.1667 -0.0105 0.0608 0.0077 40 PHE A CE1 288 C CE2 . PHE A 41 ? 1.6031 1.7955 2.1573 -0.0048 0.0723 0.0120 40 PHE A CE2 289 C CZ . PHE A 41 ? 1.5594 1.7871 2.1540 -0.0018 0.0618 0.0117 40 PHE A CZ 290 N N . THR A 42 ? 1.7224 1.8743 2.2268 -0.0357 0.0685 0.0048 41 THR A N 291 C CA . THR A 42 ? 1.6811 1.8210 2.1527 -0.0291 0.0514 0.0065 41 THR A CA 292 C C . THR A 42 ? 1.6296 1.7761 2.0997 -0.0184 0.0442 0.0091 41 THR A C 293 O O . THR A 42 ? 1.5905 1.7213 2.0482 -0.0121 0.0567 0.0113 41 THR A O 294 C CB . THR A 42 ? 1.7045 1.8054 2.1307 -0.0263 0.0592 0.0085 41 THR A CB 295 O OG1 . THR A 42 ? 1.7697 1.8580 2.1936 -0.0355 0.0697 0.0069 41 THR A OG1 296 C CG2 . THR A 42 ? 1.6851 1.7790 2.0848 -0.0202 0.0406 0.0089 41 THR A CG2 297 N N . ILE A 43 ? 1.6023 1.7687 2.0825 -0.0165 0.0254 0.0088 42 ILE A N 298 C CA . ILE A 43 ? 1.5886 1.7574 2.0641 -0.0070 0.0182 0.0114 42 ILE A CA 299 C C . ILE A 43 ? 1.5266 1.6755 1.9667 -0.0035 0.0093 0.0118 42 ILE A C 300 O O . ILE A 43 ? 1.4291 1.5662 1.8538 0.0030 0.0101 0.0130 42 ILE A O 301 C CB . ILE A 43 ? 1.6188 1.8178 2.1237 -0.0055 0.0045 0.0118 42 ILE A CB 302 C CG1 . ILE A 43 ? 1.5996 1.7990 2.1054 0.0050 0.0044 0.0154 42 ILE A CG1 303 C CG2 . ILE A 43 ? 1.6497 1.8544 2.1462 -0.0089 -0.0132 0.0105 42 ILE A CG2 304 C CD1 . ILE A 43 ? 1.5945 1.8203 2.1268 0.0092 -0.0078 0.0171 42 ILE A CD1 305 N N . TRP A 44 ? 1.4997 1.6453 1.9285 -0.0083 0.0011 0.0099 43 TRP A N 306 C CA . TRP A 44 ? 1.4911 1.6211 1.8912 -0.0052 -0.0070 0.0093 43 TRP A CA 307 C C . TRP A 44 ? 1.5132 1.6268 1.8955 -0.0083 -0.0041 0.0080 43 TRP A C 308 O O . TRP A 44 ? 1.5476 1.6692 1.9416 -0.0148 -0.0051 0.0065 43 TRP A O 309 C CB . TRP A 44 ? 1.4864 1.6318 1.8926 -0.0054 -0.0224 0.0088 43 TRP A CB 310 C CG . TRP A 44 ? 1.4960 1.6300 1.8799 -0.0028 -0.0300 0.0074 43 TRP A CG 311 C CD1 . TRP A 44 ? 1.5114 1.6437 1.8871 -0.0048 -0.0365 0.0053 43 TRP A CD1 312 C CD2 . TRP A 44 ? 1.5199 1.6437 1.8893 0.0020 -0.0318 0.0069 43 TRP A CD2 313 N NE1 . TRP A 44 ? 1.5279 1.6529 1.8884 -0.0009 -0.0427 0.0038 43 TRP A NE1 314 C CE2 . TRP A 44 ? 1.5297 1.6496 1.8862 0.0024 -0.0405 0.0043 43 TRP A CE2 315 C CE3 . TRP A 44 ? 1.5420 1.6592 1.9088 0.0059 -0.0266 0.0078 43 TRP A CE3 316 C CZ2 . TRP A 44 ? 1.5651 1.6776 1.9091 0.0054 -0.0455 0.0018 43 TRP A CZ2 317 C CZ3 . TRP A 44 ? 1.5699 1.6760 1.9201 0.0084 -0.0311 0.0053 43 TRP A CZ3 318 C CH2 . TRP A 44 ? 1.5913 1.6965 1.9316 0.0076 -0.0411 0.0020 43 TRP A CH2 319 N N . LEU A 45 ? 1.5049 1.5939 1.8573 -0.0032 -0.0009 0.0084 44 LEU A N 320 C CA . LEU A 45 ? 1.5025 1.5787 1.8376 0.0035 0.0001 0.0088 44 LEU A CA 321 C C . LEU A 45 ? 1.5040 1.5610 1.8286 0.0051 0.0182 0.0105 44 LEU A C 322 O O . LEU A 45 ? 1.4832 1.5219 1.7925 0.0039 0.0276 0.0115 44 LEU A O 323 C CB . LEU A 45 ? 1.5078 1.5693 1.8151 0.0085 -0.0103 0.0069 44 LEU A CB 324 C CG . LEU A 45 ? 1.5426 1.5862 1.8256 0.0149 -0.0108 0.0056 44 LEU A CG 325 C CD1 . LEU A 45 ? 1.5329 1.5878 1.8305 0.0147 -0.0115 0.0049 44 LEU A CD1 326 C CD2 . LEU A 45 ? 1.5518 1.5892 1.8156 0.0192 -0.0253 0.0025 44 LEU A CD2 327 N N . ASN A 46 ? 1.4926 1.5515 1.8241 0.0081 0.0248 0.0111 45 ASN A N 328 C CA . ASN A 46 ? 1.5266 1.5642 1.8443 0.0109 0.0436 0.0124 45 ASN A CA 329 C C . ASN A 46 ? 1.5192 1.5418 1.8158 0.0179 0.0425 0.0112 45 ASN A C 330 O O . ASN A 46 ? 1.5189 1.5549 1.8335 0.0195 0.0412 0.0111 45 ASN A O 331 C CB . ASN A 46 ? 1.5462 1.6016 1.8997 0.0070 0.0581 0.0138 45 ASN A CB 332 C CG . ASN A 46 ? 1.6201 1.6522 1.9609 0.0079 0.0821 0.0151 45 ASN A CG 333 O OD1 . ASN A 46 ? 1.6380 1.6396 1.9413 0.0139 0.0882 0.0154 45 ASN A OD1 334 N ND2 . ASN A 46 ? 1.6509 1.6969 2.0227 0.0014 0.0962 0.0155 45 ASN A ND2 335 N N . LEU A 47 ? 1.5548 1.5476 1.8112 0.0223 0.0428 0.0100 46 LEU A N 336 C CA . LEU A 47 ? 1.6022 1.5777 1.8332 0.0279 0.0388 0.0069 46 LEU A CA 337 C C . LEU A 47 ? 1.6146 1.5796 1.8461 0.0310 0.0573 0.0076 46 LEU A C 338 O O . LEU A 47 ? 1.6328 1.5929 1.8583 0.0340 0.0544 0.0049 46 LEU A O 339 C CB . LEU A 47 ? 1.6929 1.6380 1.8785 0.0328 0.0336 0.0050 46 LEU A CB 340 C CG . LEU A 47 ? 1.7325 1.6862 1.9154 0.0324 0.0145 0.0037 46 LEU A CG 341 C CD1 . LEU A 47 ? 1.8331 1.7550 1.9702 0.0397 0.0104 0.0029 46 LEU A CD1 342 C CD2 . LEU A 47 ? 1.6505 1.6271 1.8516 0.0304 -0.0036 -0.0004 46 LEU A CD2 343 N N . GLU A 48 ? 1.6602 1.6211 1.9001 0.0299 0.0775 0.0108 47 GLU A N 344 C CA . GLU A 48 ? 1.7273 1.6791 1.9709 0.0335 0.0982 0.0115 47 GLU A CA 345 C C . GLU A 48 ? 1.7016 1.6828 1.9858 0.0344 0.0957 0.0119 47 GLU A C 346 O O . GLU A 48 ? 1.7162 1.6884 1.9993 0.0399 0.1074 0.0115 47 GLU A O 347 C CB . GLU A 48 ? 1.8130 1.7577 2.0633 0.0307 0.1220 0.0146 47 GLU A CB 348 C CG . GLU A 48 ? 1.9340 1.8396 2.1356 0.0322 0.1297 0.0154 47 GLU A CG 349 C CD . GLU A 48 ? 2.0282 1.9229 2.2353 0.0283 0.1570 0.0186 47 GLU A CD 350 O OE1 . GLU A 48 ? 2.0432 1.9680 2.2963 0.0206 0.1618 0.0195 47 GLU A OE1 351 O OE2 . GLU A 48 ? 2.0679 1.9226 2.2322 0.0325 0.1741 0.0199 47 GLU A OE2 352 N N . LEU A 49 ? 1.6572 1.6707 1.9740 0.0299 0.0808 0.0129 48 LEU A N 353 C CA . LEU A 49 ? 1.6256 1.6660 1.9782 0.0320 0.0763 0.0142 48 LEU A CA 354 C C . LEU A 49 ? 1.5621 1.5977 1.9014 0.0351 0.0620 0.0124 48 LEU A C 355 O O . LEU A 49 ? 1.5573 1.6067 1.9178 0.0388 0.0600 0.0141 48 LEU A O 356 C CB . LEU A 49 ? 1.6458 1.7204 2.0354 0.0262 0.0663 0.0158 48 LEU A CB 357 C CG . LEU A 49 ? 1.6990 1.7842 2.1119 0.0209 0.0803 0.0165 48 LEU A CG 358 C CD1 . LEU A 49 ? 1.7122 1.8275 2.1546 0.0137 0.0664 0.0162 48 LEU A CD1 359 C CD2 . LEU A 49 ? 1.7156 1.8085 2.1547 0.0257 0.0991 0.0177 48 LEU A CD2 360 N N . LEU A 50 ? 1.5071 1.5228 1.8121 0.0337 0.0522 0.0088 49 LEU A N 361 C CA . LEU A 50 ? 1.5170 1.5296 1.8117 0.0337 0.0379 0.0056 49 LEU A CA 362 C C . LEU A 50 ? 1.5879 1.5699 1.8514 0.0379 0.0442 0.0013 49 LEU A C 363 O O . LEU A 50 ? 1.6551 1.6307 1.9077 0.0364 0.0336 -0.0028 49 LEU A O 364 C CB . LEU A 50 ? 1.4856 1.5026 1.7702 0.0287 0.0202 0.0029 49 LEU A CB 365 C CG . LEU A 50 ? 1.4731 1.5157 1.7828 0.0242 0.0140 0.0060 49 LEU A CG 366 C CD1 . LEU A 50 ? 1.4832 1.5288 1.7830 0.0209 -0.0023 0.0031 49 LEU A CD1 367 C CD2 . LEU A 50 ? 1.4126 1.4807 1.7564 0.0239 0.0124 0.0096 49 LEU A CD2 368 N N . LEU A 51 ? 1.6132 1.5755 1.8629 0.0424 0.0626 0.0018 50 LEU A N 369 C CA . LEU A 51 ? 1.6768 1.6070 1.8944 0.0468 0.0707 -0.0025 50 LEU A CA 370 C C . LEU A 51 ? 1.6942 1.6292 1.9314 0.0509 0.0766 -0.0014 50 LEU A C 371 O O . LEU A 51 ? 1.6523 1.6143 1.9277 0.0527 0.0787 0.0040 50 LEU A O 372 C CB . LEU A 51 ? 1.7468 1.6520 1.9416 0.0509 0.0916 -0.0017 50 LEU A CB 373 C CG . LEU A 51 ? 1.8128 1.7118 1.9907 0.0482 0.0904 -0.0003 50 LEU A CG 374 C CD1 . LEU A 51 ? 1.9017 1.7728 2.0568 0.0522 0.1155 0.0013 50 LEU A CD1 375 C CD2 . LEU A 51 ? 1.8399 1.7261 1.9847 0.0466 0.0690 -0.0056 50 LEU A CD2 376 N N . PRO A 52 ? 1.7458 1.6533 1.9556 0.0530 0.0784 -0.0068 51 PRO A N 377 C CA . PRO A 52 ? 1.7494 1.6541 1.9726 0.0586 0.0873 -0.0055 51 PRO A CA 378 C C . PRO A 52 ? 1.7665 1.6819 2.0172 0.0670 0.1076 0.0007 51 PRO A C 379 O O . PRO A 52 ? 1.7434 1.6533 1.9893 0.0684 0.1217 0.0017 51 PRO A O 380 C CB . PRO A 52 ? 1.7823 1.6467 1.9624 0.0595 0.0915 -0.0136 51 PRO A CB 381 C CG . PRO A 52 ? 1.7928 1.6509 1.9466 0.0516 0.0728 -0.0201 51 PRO A CG 382 C CD . PRO A 52 ? 1.7787 1.6574 1.9447 0.0500 0.0694 -0.0151 51 PRO A CD 383 N N . VAL A 53 ? 1.7981 1.7282 2.0777 0.0728 0.1092 0.0050 52 VAL A N 384 C CA . VAL A 53 ? 1.8100 1.7580 2.1253 0.0822 0.1252 0.0110 52 VAL A CA 385 C C . VAL A 53 ? 1.7623 1.7500 2.1164 0.0787 0.1188 0.0158 52 VAL A C 386 O O . VAL A 53 ? 1.7139 1.7304 2.1040 0.0827 0.1120 0.0206 52 VAL A O 387 C CB . VAL A 53 ? 1.8599 1.7832 2.1598 0.0885 0.1513 0.0092 52 VAL A CB 388 C CG1 . VAL A 53 ? 1.8815 1.8226 2.2215 0.1003 0.1679 0.0144 52 VAL A CG1 389 C CG2 . VAL A 53 ? 1.9181 1.7957 2.1681 0.0895 0.1568 0.0022 52 VAL A CG2 390 N N . ILE A 54 ? 1.7127 1.6993 2.0571 0.0717 0.1210 0.0141 53 ILE A N 391 C CA . ILE A 54 ? 1.6317 1.6513 2.0092 0.0664 0.1163 0.0172 53 ILE A CA 392 C C . ILE A 54 ? 1.5481 1.5912 1.9392 0.0615 0.0919 0.0186 53 ILE A C 393 O O . ILE A 54 ? 1.4711 1.5464 1.8979 0.0603 0.0854 0.0217 53 ILE A O 394 C CB . ILE A 54 ? 1.6699 1.6761 2.0258 0.0591 0.1227 0.0151 53 ILE A CB 395 C CG1 . ILE A 54 ? 1.7477 1.7285 2.0886 0.0640 0.1502 0.0144 53 ILE A CG1 396 C CG2 . ILE A 54 ? 1.6469 1.6849 2.0362 0.0520 0.1174 0.0174 53 ILE A CG2 397 C CD1 . ILE A 54 ? 1.8233 1.7589 2.1071 0.0655 0.1542 0.0098 53 ILE A CD1 398 N N . ILE A 55 ? 1.5122 1.5388 1.8749 0.0585 0.0789 0.0157 54 ILE A N 399 C CA . ILE A 55 ? 1.4700 1.5139 1.8416 0.0541 0.0587 0.0168 54 ILE A CA 400 C C . ILE A 55 ? 1.4004 1.4679 1.8049 0.0606 0.0548 0.0224 54 ILE A C 401 O O . ILE A 55 ? 1.3767 1.4667 1.7974 0.0571 0.0406 0.0247 54 ILE A O 402 C CB . ILE A 55 ? 1.4860 1.5074 1.8266 0.0508 0.0495 0.0122 54 ILE A CB 403 C CG1 . ILE A 55 ? 1.5022 1.5414 1.8519 0.0449 0.0312 0.0132 54 ILE A CG1 404 C CG2 . ILE A 55 ? 1.4898 1.4902 1.8209 0.0579 0.0587 0.0118 54 ILE A CG2 405 C CD1 . ILE A 55 ? 1.5044 1.5525 1.8492 0.0369 0.0209 0.0108 54 ILE A CD1 406 N N . ASP A 56 ? 1.3702 1.4309 1.7823 0.0709 0.0669 0.0247 55 ASP A N 407 C CA . ASP A 56 ? 1.3965 1.4775 1.8376 0.0799 0.0621 0.0306 55 ASP A CA 408 C C . ASP A 56 ? 1.3979 1.5163 1.8787 0.0800 0.0581 0.0333 55 ASP A C 409 O O . ASP A 56 ? 1.3458 1.4862 1.8451 0.0821 0.0435 0.0370 55 ASP A O 410 C CB . ASP A 56 ? 1.4483 1.5127 1.8896 0.0929 0.0772 0.0325 55 ASP A CB 411 C CG . ASP A 56 ? 1.4682 1.4978 1.8743 0.0928 0.0772 0.0301 55 ASP A CG 412 O OD1 . ASP A 56 ? 1.4256 1.4525 1.8183 0.0852 0.0627 0.0293 55 ASP A OD1 413 O OD2 . ASP A 56 ? 1.4694 1.4736 1.8617 0.0999 0.0928 0.0285 55 ASP A OD2 414 N N . CYS A 57 ? 1.4569 1.5806 1.9486 0.0770 0.0712 0.0310 56 CYS A N 415 C CA . CYS A 57 ? 1.5041 1.6630 2.0352 0.0740 0.0687 0.0316 56 CYS A CA 416 C C . CYS A 57 ? 1.4585 1.6294 1.9855 0.0625 0.0504 0.0302 56 CYS A C 417 O O . CYS A 57 ? 1.4195 1.6193 1.9736 0.0617 0.0374 0.0315 56 CYS A O 418 C CB . CYS A 57 ? 1.5896 1.7456 2.1291 0.0711 0.0902 0.0289 56 CYS A CB 419 S SG . CYS A 57 ? 1.7421 1.8728 2.2735 0.0834 0.1168 0.0292 56 CYS A SG 420 N N . TRP A 58 ? 1.4770 1.6249 1.9690 0.0543 0.0489 0.0270 57 TRP A N 421 C CA . TRP A 58 ? 1.4597 1.6145 1.9439 0.0443 0.0336 0.0253 57 TRP A CA 422 C C . TRP A 58 ? 1.4233 1.5888 1.9097 0.0460 0.0154 0.0280 57 TRP A C 423 O O . TRP A 58 ? 1.4070 1.5939 1.9089 0.0419 0.0032 0.0282 57 TRP A O 424 C CB . TRP A 58 ? 1.4688 1.5951 1.9142 0.0386 0.0353 0.0217 57 TRP A CB 425 C CG . TRP A 58 ? 1.4174 1.5482 1.8536 0.0300 0.0215 0.0198 57 TRP A CG 426 C CD1 . TRP A 58 ? 1.4392 1.5784 1.8822 0.0229 0.0214 0.0184 57 TRP A CD1 427 C CD2 . TRP A 58 ? 1.3477 1.4733 1.7664 0.0277 0.0074 0.0188 57 TRP A CD2 428 N NE1 . TRP A 58 ? 1.4263 1.5654 1.8561 0.0176 0.0078 0.0168 57 TRP A NE1 429 C CE2 . TRP A 58 ? 1.3614 1.4937 1.7778 0.0204 -0.0007 0.0170 57 TRP A CE2 430 C CE3 . TRP A 58 ? 1.2962 1.4112 1.7020 0.0305 0.0024 0.0189 57 TRP A CE3 431 C CZ2 . TRP A 58 ? 1.3200 1.4511 1.7236 0.0169 -0.0133 0.0153 57 TRP A CZ2 432 C CZ3 . TRP A 58 ? 1.2893 1.4034 1.6835 0.0255 -0.0097 0.0170 57 TRP A CZ3 433 C CH2 . TRP A 58 ? 1.2965 1.4199 1.6907 0.0192 -0.0174 0.0153 57 TRP A CH2 434 N N . ILE A 59 ? 1.4136 1.5614 1.8823 0.0518 0.0148 0.0296 58 ILE A N 435 C CA . ILE A 59 ? 1.4291 1.5810 1.8957 0.0542 0.0012 0.0330 58 ILE A CA 436 C C . ILE A 59 ? 1.4000 1.5788 1.8977 0.0618 -0.0055 0.0376 58 ILE A C 437 O O . ILE A 59 ? 1.3240 1.5160 1.8250 0.0600 -0.0201 0.0393 58 ILE A O 438 C CB . ILE A 59 ? 1.4710 1.5964 1.9158 0.0596 0.0058 0.0341 58 ILE A CB 439 C CG1 . ILE A 59 ? 1.4712 1.5735 1.8857 0.0507 0.0066 0.0281 58 ILE A CG1 440 C CG2 . ILE A 59 ? 1.4983 1.6259 1.9427 0.0641 -0.0046 0.0392 58 ILE A CG2 441 C CD1 . ILE A 59 ? 1.5011 1.5749 1.8942 0.0536 0.0136 0.0266 58 ILE A CD1 442 N N . ASP A 60 ? 1.4481 1.6350 1.9684 0.0707 0.0047 0.0392 59 ASP A N 443 C CA . ASP A 60 ? 1.4927 1.7083 2.0471 0.0798 -0.0025 0.0431 59 ASP A CA 444 C C . ASP A 60 ? 1.4530 1.6983 2.0299 0.0711 -0.0144 0.0401 59 ASP A C 445 O O . ASP A 60 ? 1.5283 1.7957 2.1232 0.0760 -0.0293 0.0424 59 ASP A O 446 C CB . ASP A 60 ? 1.5562 1.7772 2.1354 0.0904 0.0136 0.0440 59 ASP A CB 447 C CG . ASP A 60 ? 1.5969 1.8436 2.2092 0.1049 0.0053 0.0490 59 ASP A CG 448 O OD1 . ASP A 60 ? 1.6044 1.8544 2.2096 0.1097 -0.0117 0.0533 59 ASP A OD1 449 O OD2 . ASP A 60 ? 1.6388 1.9023 2.2842 0.1124 0.0164 0.0488 59 ASP A OD2 450 N N . ASN A 61 ? 1.3754 1.6182 1.9482 0.0586 -0.0081 0.0348 60 ASN A N 451 C CA . ASN A 61 ? 1.3615 1.6273 1.9530 0.0483 -0.0165 0.0308 60 ASN A CA 452 C C . ASN A 61 ? 1.3902 1.6499 1.9573 0.0400 -0.0313 0.0294 60 ASN A C 453 O O . ASN A 61 ? 1.4537 1.7331 2.0335 0.0361 -0.0453 0.0278 60 ASN A O 454 C CB . ASN A 61 ? 1.3416 1.6041 1.9394 0.0393 0.0002 0.0262 60 ASN A CB 455 C CG . ASN A 61 ? 1.3550 1.6235 1.9785 0.0465 0.0184 0.0268 60 ASN A CG 456 O OD1 . ASN A 61 ? 1.3659 1.6573 2.0209 0.0562 0.0150 0.0290 60 ASN A OD1 457 N ND2 . ASN A 61 ? 1.3532 1.6003 1.9622 0.0427 0.0381 0.0249 60 ASN A ND2 458 N N . ILE A 62 ? 1.3693 1.6021 1.9022 0.0372 -0.0282 0.0294 61 ILE A N 459 C CA . ILE A 62 ? 1.3416 1.5678 1.8529 0.0290 -0.0386 0.0274 61 ILE A CA 460 C C . ILE A 62 ? 1.3239 1.5470 1.8218 0.0335 -0.0509 0.0312 61 ILE A C 461 O O . ILE A 62 ? 1.2556 1.4792 1.7420 0.0277 -0.0605 0.0297 61 ILE A O 462 C CB . ILE A 62 ? 1.3372 1.5390 1.8212 0.0236 -0.0305 0.0245 61 ILE A CB 463 C CG1 . ILE A 62 ? 1.3476 1.5483 1.8183 0.0149 -0.0392 0.0213 61 ILE A CG1 464 C CG2 . ILE A 62 ? 1.3385 1.5192 1.8017 0.0290 -0.0271 0.0264 61 ILE A CG2 465 C CD1 . ILE A 62 ? 1.4006 1.5820 1.8497 0.0105 -0.0328 0.0181 61 ILE A CD1 466 N N . ARG A 63 ? 1.3447 1.5613 1.8417 0.0440 -0.0488 0.0361 62 ARG A N 467 C CA . ARG A 63 ? 1.4256 1.6353 1.9078 0.0493 -0.0581 0.0409 62 ARG A CA 468 C C . ARG A 63 ? 1.4132 1.6438 1.9064 0.0506 -0.0739 0.0421 62 ARG A C 469 O O . ARG A 63 ? 1.4051 1.6594 1.9261 0.0517 -0.0779 0.0403 62 ARG A O 470 C CB . ARG A 63 ? 1.4988 1.6969 1.9802 0.0620 -0.0519 0.0466 62 ARG A CB 471 C CG . ARG A 63 ? 1.5537 1.7731 2.0659 0.0733 -0.0532 0.0495 62 ARG A CG 472 C CD . ARG A 63 ? 1.6291 1.8329 2.1395 0.0863 -0.0429 0.0544 62 ARG A CD 473 N NE . ARG A 63 ? 1.7038 1.9299 2.2449 0.1001 -0.0467 0.0583 62 ARG A NE 474 C CZ . ARG A 63 ? 1.7841 2.0204 2.3291 0.1107 -0.0616 0.0640 62 ARG A CZ 475 N NH1 . ARG A 63 ? 1.8162 2.0392 2.3330 0.1086 -0.0723 0.0669 62 ARG A NH1 476 N NH2 . ARG A 63 ? 1.8380 2.0977 2.4151 0.1244 -0.0658 0.0668 62 ARG A NH2 477 N N . LEU A 64 ? 1.3884 1.6096 1.8595 0.0499 -0.0825 0.0443 63 LEU A N 478 C CA . LEU A 64 ? 1.3800 1.6147 1.8525 0.0533 -0.0986 0.0461 63 LEU A CA 479 C C . LEU A 64 ? 1.3785 1.6059 1.8443 0.0684 -0.1029 0.0546 63 LEU A C 480 O O . LEU A 64 ? 1.3558 1.5588 1.8022 0.0721 -0.0938 0.0589 63 LEU A O 481 C CB . LEU A 64 ? 1.3646 1.5892 1.8117 0.0445 -0.1038 0.0438 63 LEU A CB 482 C CG . LEU A 64 ? 1.3471 1.5782 1.7984 0.0312 -0.1020 0.0359 63 LEU A CG 483 C CD1 . LEU A 64 ? 1.3551 1.5722 1.7798 0.0247 -0.1038 0.0343 63 LEU A CD1 484 C CD2 . LEU A 64 ? 1.3382 1.5947 1.8144 0.0284 -0.1115 0.0315 63 LEU A CD2 485 N N . VAL A 65 ? 1.3844 1.6322 1.8662 0.0771 -0.1173 0.0566 64 VAL A N 486 C CA . VAL A 65 ? 1.4139 1.6555 1.8887 0.0942 -0.1240 0.0655 64 VAL A CA 487 C C . VAL A 65 ? 1.4082 1.6387 1.8518 0.0956 -0.1376 0.0686 64 VAL A C 488 O O . VAL A 65 ? 1.3643 1.6121 1.8120 0.0908 -0.1520 0.0640 64 VAL A O 489 C CB . VAL A 65 ? 1.4489 1.7218 1.9623 0.1058 -0.1333 0.0659 64 VAL A CB 490 C CG1 . VAL A 65 ? 1.4880 1.7507 1.9942 0.1266 -0.1373 0.0761 64 VAL A CG1 491 C CG2 . VAL A 65 ? 1.4420 1.7290 1.9885 0.1010 -0.1184 0.0607 64 VAL A CG2 492 N N . TYR A 66 ? 1.4062 1.6055 1.8169 0.1016 -0.1318 0.0761 65 TYR A N 493 C CA . TYR A 66 ? 1.4545 1.6367 1.8295 0.1031 -0.1407 0.0800 65 TYR A CA 494 C C . TYR A 66 ? 1.5124 1.6965 1.8815 0.1225 -0.1569 0.0883 65 TYR A C 495 O O . TYR A 66 ? 1.5133 1.6865 1.8828 0.1369 -0.1525 0.0960 65 TYR A O 496 C CB . TYR A 66 ? 1.4834 1.6289 1.8252 0.0984 -0.1243 0.0837 65 TYR A CB 497 C CG . TYR A 66 ? 1.5435 1.6698 1.8479 0.0959 -0.1286 0.0860 65 TYR A CG 498 C CD1 . TYR A 66 ? 1.5207 1.6519 1.8198 0.0812 -0.1285 0.0783 65 TYR A CD1 499 C CD2 . TYR A 66 ? 1.6046 1.7052 1.8764 0.1092 -0.1314 0.0963 65 TYR A CD2 500 C CE1 . TYR A 66 ? 1.5353 1.6473 1.7990 0.0792 -0.1301 0.0801 65 TYR A CE1 501 C CE2 . TYR A 66 ? 1.6412 1.7206 1.8748 0.1070 -0.1331 0.0987 65 TYR A CE2 502 C CZ . TYR A 66 ? 1.6146 1.7005 1.8451 0.0917 -0.1320 0.0903 65 TYR A CZ 503 O OH . TYR A 66 ? 1.6672 1.7306 1.8587 0.0898 -0.1314 0.0923 65 TYR A OH 504 N N . ASN A 67 ? 1.5597 1.7567 1.9220 0.1234 -0.1765 0.0862 66 ASN A N 505 C CA . ASN A 67 ? 1.6477 1.8458 1.9988 0.1424 -0.1959 0.0936 66 ASN A CA 506 C C . ASN A 67 ? 1.7019 1.8596 1.9966 0.1458 -0.1945 0.1013 66 ASN A C 507 O O . ASN A 67 ? 1.6562 1.8077 1.9277 0.1353 -0.1986 0.0968 66 ASN A O 508 C CB . ASN A 67 ? 1.6981 1.9339 2.0739 0.1406 -0.2197 0.0855 66 ASN A CB 509 C CG . ASN A 67 ? 1.7955 2.0404 2.1677 0.1618 -0.2441 0.0917 66 ASN A CG 510 O OD1 . ASN A 67 ? 1.8986 2.1202 2.2489 0.1798 -0.2427 0.1034 66 ASN A OD1 511 N ND2 . ASN A 67 ? 1.8146 2.0928 2.2076 0.1598 -0.2675 0.0835 66 ASN A ND2 512 N N . LYS A 68 ? 1.7773 1.9050 2.0489 0.1601 -0.1865 0.1127 67 LYS A N 513 C CA . LYS A 68 ? 1.8400 1.9232 2.0566 0.1631 -0.1795 0.1212 67 LYS A CA 514 C C . LYS A 68 ? 1.8588 1.9367 2.0418 0.1732 -0.2019 0.1246 67 LYS A C 515 O O . LYS A 68 ? 1.8788 1.9259 2.0169 0.1684 -0.1965 0.1270 67 LYS A O 516 C CB . LYS A 68 ? 1.9069 1.9568 2.1066 0.1771 -0.1654 0.1330 67 LYS A CB 517 C CG . LYS A 68 ? 1.9239 1.9585 2.1324 0.1638 -0.1385 0.1304 67 LYS A CG 518 C CD . LYS A 68 ? 1.9712 1.9594 2.1458 0.1738 -0.1226 0.1419 67 LYS A CD 519 C CE . LYS A 68 ? 1.9404 1.9122 2.1223 0.1589 -0.0971 0.1376 67 LYS A CE 520 N NZ . LYS A 68 ? 1.9087 1.8978 2.1281 0.1634 -0.0932 0.1349 67 LYS A NZ 521 N N . THR A 69 ? 1.8494 1.9572 2.0543 0.1873 -0.2267 0.1244 68 THR A N 522 C CA . THR A 69 ? 1.8756 1.9808 2.0493 0.1985 -0.2523 0.1267 68 THR A CA 523 C C . THR A 69 ? 1.8565 1.9763 2.0270 0.1800 -0.2609 0.1142 68 THR A C 524 O O . THR A 69 ? 1.9088 2.0013 2.0301 0.1792 -0.2649 0.1158 68 THR A O 525 C CB . THR A 69 ? 1.8903 2.0276 2.0933 0.2196 -0.2789 0.1290 68 THR A CB 526 O OG1 . THR A 69 ? 1.8511 2.0387 2.1182 0.2097 -0.2833 0.1172 68 THR A OG1 527 C CG2 . THR A 69 ? 1.9208 2.0364 2.1174 0.2417 -0.2712 0.1430 68 THR A CG2 528 N N . SER A 70 ? 1.8017 1.9607 2.0219 0.1650 -0.2618 0.1018 69 SER A N 529 C CA . SER A 70 ? 1.7911 1.9626 2.0107 0.1468 -0.2680 0.0893 69 SER A CA 530 C C . SER A 70 ? 1.7747 1.9223 1.9759 0.1281 -0.2423 0.0860 69 SER A C 531 O O . SER A 70 ? 1.7620 1.9105 1.9522 0.1147 -0.2448 0.0772 69 SER A O 532 C CB . SER A 70 ? 1.7444 1.9655 2.0236 0.1382 -0.2790 0.0772 69 SER A CB 533 O OG . SER A 70 ? 1.6807 1.9129 1.9978 0.1293 -0.2575 0.0752 69 SER A OG 534 N N . ARG A 71 ? 1.7664 1.8933 1.9655 0.1274 -0.2184 0.0924 70 ARG A N 535 C CA . ARG A 71 ? 1.7558 1.8651 1.9454 0.1103 -0.1945 0.0887 70 ARG A CA 536 C C . ARG A 71 ? 1.7066 1.8464 1.9330 0.0930 -0.1937 0.0755 70 ARG A C 537 O O . ARG A 71 ? 1.6965 1.8294 1.9088 0.0801 -0.1881 0.0690 70 ARG A O 538 C CB . ARG A 71 ? 1.8035 1.8768 1.9384 0.1082 -0.1895 0.0916 70 ARG A CB 539 C CG . ARG A 71 ? 1.8794 1.9115 1.9700 0.1219 -0.1817 0.1053 70 ARG A CG 540 C CD . ARG A 71 ? 1.9116 1.9252 2.0087 0.1180 -0.1556 0.1100 70 ARG A CD 541 N NE . ARG A 71 ? 1.9843 1.9512 2.0327 0.1210 -0.1389 0.1195 70 ARG A NE 542 C CZ . ARG A 71 ? 2.0232 1.9694 2.0550 0.1067 -0.1172 0.1169 70 ARG A CZ 543 N NH1 . ARG A 71 ? 2.0336 2.0010 2.0918 0.0896 -0.1105 0.1054 70 ARG A NH1 544 N NH2 . ARG A 71 ? 2.0679 1.9707 2.0565 0.1101 -0.1010 0.1261 70 ARG A NH2 545 N N . ALA A 72 ? 1.6580 1.8294 1.9305 0.0935 -0.1981 0.0719 71 ALA A N 546 C CA . ALA A 72 ? 1.5806 1.7788 1.8878 0.0782 -0.1966 0.0603 71 ALA A CA 547 C C . ALA A 72 ? 1.5152 1.7329 1.8650 0.0790 -0.1879 0.0600 71 ALA A C 548 O O . ALA A 72 ? 1.5339 1.7533 1.8930 0.0931 -0.1896 0.0672 71 ALA A O 549 C CB . ALA A 72 ? 1.6037 1.8257 1.9201 0.0763 -0.2195 0.0525 71 ALA A CB 550 N N . THR A 73 ? 1.4259 1.6554 1.7988 0.0650 -0.1777 0.0519 72 THR A N 551 C CA . THR A 73 ? 1.4030 1.6473 1.8118 0.0646 -0.1672 0.0509 72 THR A CA 552 C C . THR A 73 ? 1.4224 1.7021 1.8714 0.0634 -0.1787 0.0446 72 THR A C 553 O O . THR A 73 ? 1.4109 1.7040 1.8623 0.0568 -0.1924 0.0378 72 THR A O 554 C CB . THR A 73 ? 1.3636 1.5990 1.7736 0.0511 -0.1489 0.0461 72 THR A CB 555 O OG1 . THR A 73 ? 1.3375 1.5801 1.7474 0.0383 -0.1526 0.0375 72 THR A OG1 556 C CG2 . THR A 73 ? 1.3832 1.5879 1.7620 0.0512 -0.1362 0.0511 72 THR A CG2 557 N N . GLN A 74 ? 1.4455 1.7392 1.9264 0.0691 -0.1717 0.0462 73 GLN A N 558 C CA . GLN A 74 ? 1.4756 1.8039 2.0017 0.0667 -0.1770 0.0398 73 GLN A CA 559 C C . GLN A 74 ? 1.4714 1.7997 2.0185 0.0616 -0.1556 0.0384 73 GLN A C 560 O O . GLN A 74 ? 1.4256 1.7302 1.9549 0.0647 -0.1410 0.0434 73 GLN A O 561 C CB . GLN A 74 ? 1.5405 1.8895 2.0881 0.0841 -0.1918 0.0445 73 GLN A CB 562 C CG . GLN A 74 ? 1.6227 1.9663 2.1423 0.0940 -0.2141 0.0484 73 GLN A CG 563 C CD . GLN A 74 ? 1.6538 2.0167 2.1937 0.1143 -0.2297 0.0540 73 GLN A CD 564 O OE1 . GLN A 74 ? 1.6762 2.0617 2.2578 0.1202 -0.2241 0.0539 73 GLN A OE1 565 N NE2 . GLN A 74 ? 1.6629 2.0158 2.1721 0.1263 -0.2490 0.0593 73 GLN A NE2 566 N N . PHE A 75 ? 1.5112 1.8644 2.0948 0.0534 -0.1533 0.0310 74 PHE A N 567 C CA . PHE A 75 ? 1.5365 1.8894 2.1399 0.0506 -0.1326 0.0301 74 PHE A CA 568 C C . PHE A 75 ? 1.5255 1.8903 2.1538 0.0668 -0.1300 0.0357 74 PHE A C 569 O O . PHE A 75 ? 1.4919 1.8758 2.1349 0.0781 -0.1466 0.0380 74 PHE A O 570 C CB . PHE A 75 ? 1.5702 1.9423 2.2027 0.0359 -0.1280 0.0207 74 PHE A CB 571 C CG . PHE A 75 ? 1.6304 1.9925 2.2415 0.0210 -0.1318 0.0145 74 PHE A CG 572 C CD1 . PHE A 75 ? 1.6604 1.9924 2.2317 0.0181 -0.1258 0.0168 74 PHE A CD1 573 C CD2 . PHE A 75 ? 1.6821 2.0652 2.3148 0.0097 -0.1407 0.0056 74 PHE A CD2 574 C CE1 . PHE A 75 ? 1.7042 2.0268 2.2571 0.0061 -0.1283 0.0112 74 PHE A CE1 575 C CE2 . PHE A 75 ? 1.7120 2.0826 2.3233 -0.0033 -0.1430 -0.0002 74 PHE A CE2 576 C CZ . PHE A 75 ? 1.7252 2.0654 2.2963 -0.0041 -0.1364 0.0029 74 PHE A CZ 577 N N . PRO A 76 ? 1.5396 1.8918 2.1710 0.0691 -0.1095 0.0379 75 PRO A N 578 C CA . PRO A 76 ? 1.5761 1.9397 2.2344 0.0844 -0.1040 0.0423 75 PRO A CA 579 C C . PRO A 76 ? 1.6232 2.0288 2.3340 0.0849 -0.1105 0.0371 75 PRO A C 580 O O . PRO A 76 ? 1.6280 2.0496 2.3555 0.0698 -0.1120 0.0289 75 PRO A O 581 C CB . PRO A 76 ? 1.5541 1.8955 2.2046 0.0817 -0.0790 0.0424 75 PRO A CB 582 C CG . PRO A 76 ? 1.5447 1.8568 2.1536 0.0704 -0.0760 0.0413 75 PRO A CG 583 C CD . PRO A 76 ? 1.5393 1.8639 2.1460 0.0596 -0.0917 0.0365 75 PRO A CD 584 N N . ASP A 77 ? 1.7034 2.1268 2.4414 0.1022 -0.1142 0.0414 76 ASP A N 585 C CA . ASP A 77 ? 1.7585 2.2268 2.5526 0.1039 -0.1220 0.0360 76 ASP A CA 586 C C . ASP A 77 ? 1.6313 2.1098 2.4557 0.0895 -0.0996 0.0285 76 ASP A C 587 O O . ASP A 77 ? 1.5533 2.0094 2.3677 0.0902 -0.0758 0.0308 76 ASP A O 588 C CB . ASP A 77 ? 1.9201 2.4039 2.7393 0.1278 -0.1266 0.0428 76 ASP A CB 589 C CG . ASP A 77 ? 2.0648 2.5997 2.9392 0.1325 -0.1461 0.0375 76 ASP A CG 590 O OD1 . ASP A 77 ? 2.1841 2.7394 3.0703 0.1173 -0.1602 0.0287 76 ASP A OD1 591 O OD2 . ASP A 77 ? 2.1735 2.7284 3.0803 0.1520 -0.1478 0.0415 76 ASP A OD2 592 N N . GLY A 78 ? 1.5541 2.0632 2.4121 0.0760 -0.1072 0.0192 77 GLY A N 593 C CA . GLY A 78 ? 1.5025 2.0211 2.3903 0.0607 -0.0857 0.0117 77 GLY A CA 594 C C . GLY A 78 ? 1.4758 1.9595 2.3246 0.0437 -0.0703 0.0095 77 GLY A C 595 O O . GLY A 78 ? 1.4499 1.9318 2.3136 0.0327 -0.0487 0.0052 77 GLY A O 596 N N . VAL A 79 ? 1.4670 1.9226 2.2662 0.0420 -0.0804 0.0126 78 VAL A N 597 C CA . VAL A 79 ? 1.4567 1.8795 2.2179 0.0286 -0.0681 0.0110 78 VAL A CA 598 C C . VAL A 79 ? 1.4387 1.8635 2.1863 0.0157 -0.0851 0.0054 78 VAL A C 599 O O . VAL A 79 ? 1.3988 1.8281 2.1338 0.0211 -0.1065 0.0069 78 VAL A O 600 C CB . VAL A 79 ? 1.4819 1.8674 2.1955 0.0370 -0.0626 0.0187 78 VAL A CB 601 C CG1 . VAL A 79 ? 1.4660 1.8214 2.1439 0.0244 -0.0522 0.0166 78 VAL A CG1 602 C CG2 . VAL A 79 ? 1.5008 1.8801 2.2231 0.0504 -0.0463 0.0239 78 VAL A CG2 603 N N . ASP A 80 ? 1.4567 1.8747 2.2037 -0.0005 -0.0745 -0.0009 79 ASP A N 604 C CA . ASP A 80 ? 1.4797 1.8930 2.2091 -0.0133 -0.0872 -0.0067 79 ASP A CA 605 C C . ASP A 80 ? 1.4486 1.8257 2.1386 -0.0209 -0.0729 -0.0060 79 ASP A C 606 O O . ASP A 80 ? 1.4312 1.7941 2.1202 -0.0228 -0.0519 -0.0048 79 ASP A O 607 C CB . ASP A 80 ? 1.5192 1.9620 2.2904 -0.0269 -0.0910 -0.0169 79 ASP A CB 608 C CG . ASP A 80 ? 1.5648 2.0154 2.3270 -0.0340 -0.1149 -0.0232 79 ASP A CG 609 O OD1 . ASP A 80 ? 1.5619 1.9854 2.2802 -0.0359 -0.1192 -0.0216 79 ASP A OD1 610 O OD2 . ASP A 80 ? 1.6313 2.1156 2.4310 -0.0376 -0.1297 -0.0302 79 ASP A OD2 611 N N . VAL A 81 ? 1.4319 1.7934 2.0885 -0.0243 -0.0843 -0.0067 80 VAL A N 612 C CA . VAL A 81 ? 1.4226 1.7514 2.0418 -0.0288 -0.0737 -0.0056 80 VAL A CA 613 C C . VAL A 81 ? 1.4285 1.7517 2.0356 -0.0413 -0.0808 -0.0124 80 VAL A C 614 O O . VAL A 81 ? 1.3959 1.7303 2.0021 -0.0424 -0.0988 -0.0154 80 VAL A O 615 C CB . VAL A 81 ? 1.4086 1.7180 1.9937 -0.0178 -0.0772 0.0014 80 VAL A CB 616 C CG1 . VAL A 81 ? 1.4097 1.6894 1.9637 -0.0206 -0.0648 0.0024 80 VAL A CG1 617 C CG2 . VAL A 81 ? 1.3976 1.7131 1.9942 -0.0047 -0.0741 0.0077 80 VAL A CG2 618 N N . ARG A 82 ? 1.4367 1.7397 2.0313 -0.0498 -0.0664 -0.0148 81 ARG A N 619 C CA . ARG A 82 ? 1.4643 1.7557 2.0427 -0.0606 -0.0703 -0.0208 81 ARG A CA 620 C C . ARG A 82 ? 1.4201 1.6787 1.9615 -0.0590 -0.0601 -0.0178 81 ARG A C 621 O O . ARG A 82 ? 1.3619 1.6068 1.8943 -0.0532 -0.0474 -0.0128 81 ARG A O 622 C CB . ARG A 82 ? 1.5323 1.8346 2.1393 -0.0753 -0.0645 -0.0292 81 ARG A CB 623 C CG . ARG A 82 ? 1.5876 1.8735 2.1975 -0.0804 -0.0404 -0.0284 81 ARG A CG 624 C CD . ARG A 82 ? 1.6261 1.9217 2.2653 -0.0970 -0.0333 -0.0374 81 ARG A CD 625 N NE . ARG A 82 ? 1.6983 1.9716 2.3338 -0.1019 -0.0076 -0.0358 81 ARG A NE 626 C CZ . ARG A 82 ? 1.7716 2.0480 2.4329 -0.1165 0.0063 -0.0422 81 ARG A CZ 627 N NH1 . ARG A 82 ? 1.8083 2.1130 2.5055 -0.1289 -0.0043 -0.0520 81 ARG A NH1 628 N NH2 . ARG A 82 ? 1.7887 2.0387 2.4389 -0.1192 0.0315 -0.0391 81 ARG A NH2 629 N N . VAL A 83 ? 1.3977 1.6441 1.9178 -0.0636 -0.0666 -0.0214 82 VAL A N 630 C CA . VAL A 83 ? 1.3728 1.5908 1.8606 -0.0615 -0.0592 -0.0195 82 VAL A CA 631 C C . VAL A 83 ? 1.3417 1.5443 1.8280 -0.0722 -0.0478 -0.0245 82 VAL A C 632 O O . VAL A 83 ? 1.3283 1.5320 1.8167 -0.0817 -0.0533 -0.0314 82 VAL A O 633 C CB . VAL A 83 ? 1.3945 1.6066 1.8590 -0.0584 -0.0712 -0.0202 82 VAL A CB 634 C CG1 . VAL A 83 ? 1.4075 1.5948 1.8442 -0.0537 -0.0639 -0.0179 82 VAL A CG1 635 C CG2 . VAL A 83 ? 1.4003 1.6264 1.8663 -0.0497 -0.0823 -0.0158 82 VAL A CG2 636 N N . PRO A 84 ? 1.2856 1.4707 1.7654 -0.0707 -0.0314 -0.0212 83 PRO A N 637 C CA . PRO A 84 ? 1.3274 1.4925 1.8019 -0.0802 -0.0181 -0.0247 83 PRO A CA 638 C C . PRO A 84 ? 1.3837 1.5211 1.8235 -0.0767 -0.0181 -0.0243 83 PRO A C 639 O O . PRO A 84 ? 1.3923 1.5260 1.8137 -0.0661 -0.0255 -0.0205 83 PRO A O 640 C CB . PRO A 84 ? 1.3211 1.4753 1.7964 -0.0770 -0.0004 -0.0197 83 PRO A CB 641 C CG . PRO A 84 ? 1.2901 1.4433 1.7500 -0.0628 -0.0056 -0.0131 83 PRO A CG 642 C CD . PRO A 84 ? 1.2674 1.4453 1.7383 -0.0600 -0.0241 -0.0141 83 PRO A CD 643 N N . GLY A 85 ? 1.4430 1.5609 1.8757 -0.0859 -0.0091 -0.0286 84 GLY A N 644 C CA . GLY A 85 ? 1.4722 1.5592 1.8716 -0.0810 -0.0054 -0.0275 84 GLY A CA 645 C C . GLY A 85 ? 1.4773 1.5645 1.8649 -0.0801 -0.0180 -0.0316 84 GLY A C 646 O O . GLY A 85 ? 1.4798 1.5463 1.8417 -0.0717 -0.0169 -0.0295 84 GLY A O 647 N N . PHE A 86 ? 1.4646 1.5741 1.8695 -0.0878 -0.0300 -0.0376 85 PHE A N 648 C CA . PHE A 86 ? 1.4655 1.5709 1.8553 -0.0881 -0.0400 -0.0423 85 PHE A CA 649 C C . PHE A 86 ? 1.4842 1.5609 1.8582 -0.0957 -0.0306 -0.0479 85 PHE A C 650 O O . PHE A 86 ? 1.4830 1.5559 1.8699 -0.1090 -0.0232 -0.0531 85 PHE A O 651 C CB . PHE A 86 ? 1.4572 1.5891 1.8642 -0.0946 -0.0556 -0.0479 85 PHE A CB 652 C CG . PHE A 86 ? 1.4790 1.6051 1.8650 -0.0925 -0.0655 -0.0516 85 PHE A CG 653 C CD1 . PHE A 86 ? 1.5085 1.6194 1.8835 -0.1025 -0.0657 -0.0606 85 PHE A CD1 654 C CD2 . PHE A 86 ? 1.4995 1.6328 1.8754 -0.0811 -0.0728 -0.0464 85 PHE A CD2 655 C CE1 . PHE A 86 ? 1.5369 1.6395 1.8895 -0.1001 -0.0730 -0.0643 85 PHE A CE1 656 C CE2 . PHE A 86 ? 1.5333 1.6592 1.8886 -0.0792 -0.0790 -0.0496 85 PHE A CE2 657 C CZ . PHE A 86 ? 1.5464 1.6568 1.8892 -0.0881 -0.0791 -0.0584 85 PHE A CZ 658 N N . GLY A 87 ? 1.4952 1.5511 1.8425 -0.0873 -0.0296 -0.0470 86 GLY A N 659 C CA . GLY A 87 ? 1.5461 1.5696 1.8738 -0.0915 -0.0194 -0.0511 86 GLY A CA 660 C C . GLY A 87 ? 1.5956 1.5922 1.9091 -0.0848 -0.0041 -0.0446 86 GLY A C 661 O O . GLY A 87 ? 1.6399 1.6045 1.9327 -0.0849 0.0057 -0.0461 86 GLY A O 662 N N . LYS A 88 ? 1.6277 1.6340 1.9491 -0.0785 -0.0018 -0.0373 87 LYS A N 663 C CA . LYS A 88 ? 1.7287 1.7088 2.0313 -0.0695 0.0107 -0.0300 87 LYS A CA 664 C C . LYS A 88 ? 1.7302 1.7181 2.0233 -0.0519 0.0022 -0.0232 87 LYS A C 665 O O . LYS A 88 ? 1.7084 1.7183 2.0093 -0.0482 -0.0104 -0.0245 87 LYS A O 666 C CB . LYS A 88 ? 1.7647 1.7467 2.0827 -0.0782 0.0224 -0.0283 87 LYS A CB 667 C CG . LYS A 88 ? 1.8056 1.7819 2.1383 -0.0976 0.0322 -0.0360 87 LYS A CG 668 C CD . LYS A 88 ? 1.8762 1.8089 2.1806 -0.0991 0.0464 -0.0367 87 LYS A CD 669 C CE . LYS A 88 ? 1.9487 1.8738 2.2694 -0.1207 0.0586 -0.0451 87 LYS A CE 670 N NZ . LYS A 88 ? 2.0089 1.8861 2.2992 -0.1225 0.0748 -0.0454 87 LYS A NZ 671 N N . THR A 89 ? 1.7451 1.7137 2.0202 -0.0413 0.0091 -0.0164 88 THR A N 672 C CA . THR A 89 ? 1.7142 1.6895 1.9805 -0.0252 -0.0001 -0.0114 88 THR A CA 673 C C . THR A 89 ? 1.7086 1.6858 1.9737 -0.0205 0.0023 -0.0059 88 THR A C 674 O O . THR A 89 ? 1.6894 1.6765 1.9513 -0.0096 -0.0069 -0.0033 88 THR A O 675 C CB . THR A 89 ? 1.7451 1.6940 1.9842 -0.0113 0.0004 -0.0092 88 THR A CB 676 O OG1 . THR A 89 ? 1.7650 1.6774 1.9813 -0.0107 0.0148 -0.0058 88 THR A OG1 677 C CG2 . THR A 89 ? 1.7389 1.6881 1.9790 -0.0134 -0.0028 -0.0149 88 THR A CG2 678 N N . PHE A 90 ? 1.7155 1.6832 1.9837 -0.0291 0.0155 -0.0049 89 PHE A N 679 C CA . PHE A 90 ? 1.7211 1.6845 1.9829 -0.0239 0.0209 0.0003 89 PHE A CA 680 C C . PHE A 90 ? 1.6496 1.6448 1.9303 -0.0212 0.0092 0.0003 89 PHE A C 681 O O . PHE A 90 ? 1.6180 1.6085 1.8855 -0.0114 0.0071 0.0040 89 PHE A O 682 C CB . PHE A 90 ? 1.7748 1.7249 2.0414 -0.0352 0.0401 0.0007 89 PHE A CB 683 C CG . PHE A 90 ? 1.7849 1.7650 2.0906 -0.0509 0.0405 -0.0049 89 PHE A CG 684 C CD1 . PHE A 90 ? 1.7757 1.7837 2.1054 -0.0517 0.0372 -0.0044 89 PHE A CD1 685 C CD2 . PHE A 90 ? 1.8124 1.7923 2.1307 -0.0644 0.0437 -0.0112 89 PHE A CD2 686 C CE1 . PHE A 90 ? 1.7770 1.8144 2.1439 -0.0641 0.0356 -0.0095 89 PHE A CE1 687 C CE2 . PHE A 90 ? 1.8091 1.8190 2.1645 -0.0784 0.0413 -0.0173 89 PHE A CE2 688 C CZ . PHE A 90 ? 1.7849 1.8246 2.1653 -0.0775 0.0366 -0.0162 89 PHE A CZ 689 N N . SER A 91 ? 1.5746 1.5993 1.8835 -0.0295 0.0015 -0.0038 90 SER A N 690 C CA . SER A 91 ? 1.5034 1.5557 1.8303 -0.0277 -0.0079 -0.0034 90 SER A CA 691 C C . SER A 91 ? 1.4663 1.5252 1.7845 -0.0171 -0.0210 -0.0027 90 SER A C 692 O O . SER A 91 ? 1.4143 1.4876 1.7397 -0.0137 -0.0267 -0.0014 90 SER A O 693 C CB . SER A 91 ? 1.4923 1.5713 1.8486 -0.0385 -0.0129 -0.0076 90 SER A CB 694 O OG . SER A 91 ? 1.5161 1.5946 1.8703 -0.0427 -0.0187 -0.0121 90 SER A OG 695 N N . LEU A 92 ? 1.4829 1.5311 1.7873 -0.0124 -0.0246 -0.0039 91 LEU A N 696 C CA . LEU A 92 ? 1.4754 1.5297 1.7741 -0.0023 -0.0355 -0.0041 91 LEU A CA 697 C C . LEU A 92 ? 1.4806 1.5148 1.7557 0.0100 -0.0357 -0.0010 91 LEU A C 698 O O . LEU A 92 ? 1.4571 1.5001 1.7314 0.0179 -0.0451 -0.0012 91 LEU A O 699 C CB . LEU A 92 ? 1.5003 1.5541 1.7983 -0.0026 -0.0384 -0.0076 91 LEU A CB 700 C CG . LEU A 92 ? 1.4433 1.5151 1.7577 -0.0122 -0.0420 -0.0117 91 LEU A CG 701 C CD1 . LEU A 92 ? 1.4631 1.5327 1.7854 -0.0246 -0.0357 -0.0138 91 LEU A CD1 702 C CD2 . LEU A 92 ? 1.3786 1.4481 1.6876 -0.0094 -0.0447 -0.0152 91 LEU A CD2 703 N N . GLU A 93 ? 1.5025 1.5087 1.7573 0.0117 -0.0257 0.0015 92 GLU A N 704 C CA . GLU A 93 ? 1.5381 1.5207 1.7645 0.0253 -0.0269 0.0049 92 GLU A CA 705 C C . GLU A 93 ? 1.5255 1.5071 1.7441 0.0288 -0.0280 0.0071 92 GLU A C 706 O O . GLU A 93 ? 1.4846 1.4635 1.6897 0.0401 -0.0382 0.0073 92 GLU A O 707 C CB . GLU A 93 ? 1.5961 1.5430 1.7977 0.0265 -0.0138 0.0080 92 GLU A CB 708 C CG . GLU A 93 ? 1.6177 1.5571 1.8180 0.0270 -0.0134 0.0059 92 GLU A CG 709 C CD . GLU A 93 ? 1.6615 1.5614 1.8356 0.0274 0.0014 0.0091 92 GLU A CD 710 O OE1 . GLU A 93 ? 1.7233 1.5954 1.8666 0.0402 0.0031 0.0144 92 GLU A OE1 711 O OE2 . GLU A 93 ? 1.6740 1.5686 1.8565 0.0147 0.0111 0.0061 92 GLU A OE2 712 N N . PHE A 94 ? 1.5662 1.5498 1.7939 0.0193 -0.0174 0.0080 93 PHE A N 713 C CA . PHE A 94 ? 1.6050 1.5844 1.8243 0.0218 -0.0150 0.0097 93 PHE A CA 714 C C . PHE A 94 ? 1.6573 1.6637 1.9074 0.0121 -0.0135 0.0079 93 PHE A C 715 O O . PHE A 94 ? 1.7373 1.7536 2.0081 0.0018 -0.0060 0.0072 93 PHE A O 716 C CB . PHE A 94 ? 1.6112 1.5565 1.8038 0.0228 0.0018 0.0140 93 PHE A CB 717 C CG . PHE A 94 ? 1.6381 1.5511 1.7908 0.0366 -0.0008 0.0173 93 PHE A CG 718 C CD1 . PHE A 94 ? 1.6723 1.5741 1.8161 0.0412 -0.0034 0.0179 93 PHE A CD1 719 C CD2 . PHE A 94 ? 1.6503 1.5419 1.7720 0.0460 -0.0008 0.0197 93 PHE A CD2 720 C CE1 . PHE A 94 ? 1.6871 1.5583 1.7933 0.0563 -0.0069 0.0215 93 PHE A CE1 721 C CE2 . PHE A 94 ? 1.6896 1.5502 1.7714 0.0605 -0.0055 0.0229 93 PHE A CE2 722 C CZ . PHE A 94 ? 1.7011 1.5522 1.7760 0.0663 -0.0089 0.0242 93 PHE A CZ 723 N N . LEU A 95 ? 1.6838 1.7017 1.9370 0.0156 -0.0213 0.0069 94 LEU A N 724 C CA . LEU A 95 ? 1.6698 1.7112 1.9500 0.0087 -0.0208 0.0059 94 LEU A CA 725 C C . LEU A 95 ? 1.6930 1.7257 1.9739 0.0058 -0.0055 0.0082 94 LEU A C 726 O O . LEU A 95 ? 1.6864 1.7370 1.9941 -0.0012 -0.0005 0.0080 94 LEU A O 727 C CB . LEU A 95 ? 1.6567 1.7117 1.9409 0.0125 -0.0331 0.0037 94 LEU A CB 728 C CG . LEU A 95 ? 1.6055 1.6797 1.9029 0.0123 -0.0460 0.0008 94 LEU A CG 729 C CD1 . LEU A 95 ? 1.5573 1.6457 1.8742 0.0048 -0.0447 0.0006 94 LEU A CD1 730 C CD2 . LEU A 95 ? 1.6352 1.6995 1.9154 0.0204 -0.0541 -0.0006 94 LEU A CD2 731 N N . ASP A 96 ? 1.7105 1.7158 1.9618 0.0120 0.0017 0.0102 95 ASP A N 732 C CA . ASP A 96 ? 1.6925 1.6858 1.9415 0.0099 0.0196 0.0124 95 ASP A CA 733 C C . ASP A 96 ? 1.6565 1.6198 1.8824 0.0097 0.0343 0.0153 95 ASP A C 734 O O . ASP A 96 ? 1.5080 1.4419 1.6958 0.0186 0.0342 0.0173 95 ASP A O 735 C CB . ASP A 96 ? 1.7231 1.7047 1.9521 0.0172 0.0187 0.0121 95 ASP A CB 736 C CG . ASP A 96 ? 1.7557 1.7274 1.9859 0.0155 0.0388 0.0139 95 ASP A CG 737 O OD1 . ASP A 96 ? 1.7859 1.7533 2.0258 0.0096 0.0553 0.0159 95 ASP A OD1 738 O OD2 . ASP A 96 ? 1.7116 1.6795 1.9343 0.0197 0.0391 0.0129 95 ASP A OD2 739 N N . PRO A 97 ? 1.6985 1.6678 1.9466 -0.0005 0.0471 0.0154 96 PRO A N 740 C CA . PRO A 97 ? 1.8117 1.7519 2.0399 -0.0027 0.0611 0.0177 96 PRO A CA 741 C C . PRO A 97 ? 1.8638 1.7649 2.0538 0.0032 0.0785 0.0220 96 PRO A C 742 O O . PRO A 97 ? 1.9203 1.7872 2.0748 0.0082 0.0839 0.0253 96 PRO A O 743 C CB . PRO A 97 ? 1.8065 1.7665 2.0738 -0.0174 0.0719 0.0151 96 PRO A CB 744 C CG . PRO A 97 ? 1.7250 1.7162 2.0255 -0.0198 0.0701 0.0135 96 PRO A CG 745 C CD . PRO A 97 ? 1.6774 1.6784 1.9691 -0.0101 0.0507 0.0132 96 PRO A CD 746 N N . SER A 98 ? 1.8695 1.7729 2.0642 0.0035 0.0880 0.0223 97 SER A N 747 C CA . SER A 98 ? 1.9340 1.7983 2.0888 0.0099 0.1055 0.0261 97 SER A CA 748 C C . SER A 98 ? 1.9595 1.8020 2.0694 0.0243 0.0891 0.0268 97 SER A C 749 O O . SER A 98 ? 1.9915 1.7929 2.0539 0.0325 0.0973 0.0306 97 SER A O 750 C CB . SER A 98 ? 1.9433 1.8176 2.1179 0.0067 0.1209 0.0253 97 SER A CB 751 O OG . SER A 98 ? 1.9527 1.8505 2.1399 0.0113 0.1043 0.0225 97 SER A OG 752 N N . LYS A 99 ? 2.0217 1.8915 2.1464 0.0274 0.0659 0.0230 98 LYS A N 753 C CA . LYS A 99 ? 2.1476 2.0043 2.2388 0.0392 0.0493 0.0216 98 LYS A CA 754 C C . LYS A 99 ? 2.1858 2.0461 2.2714 0.0444 0.0307 0.0211 98 LYS A C 755 O O . LYS A 99 ? 2.2604 2.1520 2.3730 0.0428 0.0132 0.0173 98 LYS A O 756 C CB . LYS A 99 ? 2.1994 2.0818 2.3114 0.0383 0.0386 0.0170 98 LYS A CB 757 C CG . LYS A 99 ? 2.2031 2.0825 2.3225 0.0350 0.0576 0.0174 98 LYS A CG 758 C CD . LYS A 99 ? 2.2621 2.0978 2.3320 0.0426 0.0714 0.0193 98 LYS A CD 759 C CE . LYS A 99 ? 2.3158 2.1270 2.3758 0.0391 0.0986 0.0245 98 LYS A CE 760 N NZ . LYS A 99 ? 2.3942 2.1608 2.4048 0.0463 0.1159 0.0267 98 LYS A NZ 761 N N . SER A 100 ? 2.2434 2.0694 2.2932 0.0509 0.0366 0.0255 99 SER A N 762 C CA . SER A 100 ? 2.2934 2.1169 2.3343 0.0581 0.0220 0.0261 99 SER A CA 763 C C . SER A 100 ? 2.3335 2.1769 2.3765 0.0670 -0.0056 0.0213 99 SER A C 764 O O . SER A 100 ? 2.5659 2.4456 2.6472 0.0612 -0.0164 0.0172 99 SER A O 765 C CB . SER A 100 ? 2.3278 2.1029 2.3198 0.0672 0.0331 0.0324 99 SER A CB 766 O OG . SER A 100 ? 2.2905 2.0619 2.2758 0.0748 0.0213 0.0336 99 SER A OG 767 N N . SER A 101 ? 2.2853 2.1052 2.2880 0.0806 -0.0165 0.0214 100 SER A N 768 C CA . SER A 101 ? 2.2359 2.0714 2.2384 0.0907 -0.0434 0.0167 100 SER A CA 769 C C . SER A 101 ? 2.2427 2.1221 2.2889 0.0824 -0.0562 0.0094 100 SER A C 770 O O . SER A 101 ? 2.4433 2.3505 2.5166 0.0828 -0.0705 0.0060 100 SER A O 771 C CB . SER A 101 ? 2.2097 2.0148 2.1630 0.1041 -0.0529 0.0162 100 SER A CB 772 O OG . SER A 101 ? 2.0931 1.8926 2.0397 0.0983 -0.0445 0.0138 100 SER A OG 773 N N . VAL A 102 ? 2.0734 1.9561 2.1251 0.0751 -0.0489 0.0074 101 VAL A N 774 C CA . VAL A 102 ? 1.8851 1.8007 1.9691 0.0684 -0.0598 0.0008 101 VAL A CA 775 C C . VAL A 102 ? 1.7593 1.7097 1.8898 0.0585 -0.0590 0.0004 101 VAL A C 776 O O . VAL A 102 ? 1.7066 1.6840 1.8622 0.0554 -0.0715 -0.0045 101 VAL A O 777 C CB . VAL A 102 ? 1.8806 1.7885 1.9593 0.0634 -0.0492 -0.0005 101 VAL A CB 778 C CG1 . VAL A 102 ? 1.8628 1.7929 1.9588 0.0603 -0.0645 -0.0082 101 VAL A CG1 779 C CG2 . VAL A 102 ? 1.9417 1.8069 1.9691 0.0718 -0.0412 0.0018 101 VAL A CG2 780 N N . GLY A 103 ? 1.7196 1.6678 1.8599 0.0530 -0.0443 0.0052 102 GLY A N 781 C CA . GLY A 103 ? 1.6469 1.6248 1.8267 0.0435 -0.0435 0.0045 102 GLY A CA 782 C C . GLY A 103 ? 1.6691 1.6532 1.8556 0.0459 -0.0498 0.0046 102 GLY A C 783 O O . GLY A 103 ? 1.5877 1.5892 1.8000 0.0378 -0.0462 0.0045 102 GLY A O 784 N N . SER A 104 ? 1.7917 1.7611 1.9546 0.0578 -0.0595 0.0047 103 SER A N 785 C CA . SER A 104 ? 1.7965 1.7687 1.9641 0.0623 -0.0641 0.0051 103 SER A CA 786 C C . SER A 104 ? 1.6374 1.6450 1.8401 0.0585 -0.0748 0.0000 103 SER A C 787 O O . SER A 104 ? 1.5240 1.5485 1.7362 0.0608 -0.0876 -0.0045 103 SER A O 788 C CB . SER A 104 ? 1.8767 1.8247 2.0105 0.0787 -0.0729 0.0068 103 SER A CB 789 O OG . SER A 104 ? 1.9872 1.9462 2.1187 0.0862 -0.0910 0.0020 103 SER A OG 790 N N . TYR A 105 ? 1.5367 1.5533 1.7571 0.0520 -0.0687 0.0004 104 TYR A N 791 C CA . TYR A 105 ? 1.4492 1.4951 1.6993 0.0476 -0.0751 -0.0036 104 TYR A CA 792 C C . TYR A 105 ? 1.4305 1.4735 1.6810 0.0530 -0.0755 -0.0039 104 TYR A C 793 O O . TYR A 105 ? 1.4444 1.4920 1.6945 0.0638 -0.0857 -0.0060 104 TYR A O 794 C CB . TYR A 105 ? 1.3937 1.4545 1.6647 0.0340 -0.0677 -0.0037 104 TYR A CB 795 C CG . TYR A 105 ? 1.3512 1.4379 1.6479 0.0285 -0.0720 -0.0070 104 TYR A CG 796 C CD1 . TYR A 105 ? 1.3345 1.4384 1.6432 0.0308 -0.0813 -0.0107 104 TYR A CD1 797 C CD2 . TYR A 105 ? 1.3348 1.4274 1.6426 0.0203 -0.0661 -0.0068 104 TYR A CD2 798 C CE1 . TYR A 105 ? 1.2871 1.4110 1.6167 0.0253 -0.0822 -0.0131 104 TYR A CE1 799 C CE2 . TYR A 105 ? 1.3074 1.4191 1.6325 0.0160 -0.0690 -0.0093 104 TYR A CE2 800 C CZ . TYR A 105 ? 1.2744 1.4005 1.6097 0.0186 -0.0758 -0.0119 104 TYR A CZ 801 O OH . TYR A 105 ? 1.2141 1.3557 1.5642 0.0140 -0.0758 -0.0139 104 TYR A OH 802 N N . PHE A 106 ? 1.3998 1.4349 1.6513 0.0458 -0.0648 -0.0025 105 PHE A N 803 C CA . PHE A 106 ? 1.4077 1.4347 1.6559 0.0505 -0.0629 -0.0031 105 PHE A CA 804 C C . PHE A 106 ? 1.4262 1.4188 1.6436 0.0609 -0.0583 0.0010 105 PHE A C 805 O O . PHE A 106 ? 1.3926 1.3737 1.6034 0.0673 -0.0564 0.0010 105 PHE A O 806 C CB . PHE A 106 ? 1.3857 1.4169 1.6462 0.0373 -0.0542 -0.0047 105 PHE A CB 807 C CG . PHE A 106 ? 1.3800 1.4368 1.6628 0.0334 -0.0589 -0.0090 105 PHE A CG 808 C CD1 . PHE A 106 ? 1.3964 1.4547 1.6811 0.0410 -0.0610 -0.0115 105 PHE A CD1 809 C CD2 . PHE A 106 ? 1.3455 1.4222 1.6456 0.0230 -0.0599 -0.0101 105 PHE A CD2 810 C CE1 . PHE A 106 ? 1.3741 1.4529 1.6768 0.0372 -0.0625 -0.0152 105 PHE A CE1 811 C CE2 . PHE A 106 ? 1.3421 1.4374 1.6575 0.0197 -0.0626 -0.0132 105 PHE A CE2 812 C CZ . PHE A 106 ? 1.3668 1.4628 1.6831 0.0262 -0.0631 -0.0159 105 PHE A CZ 813 N N . HIS A 107 ? 1.4493 1.4224 1.6452 0.0632 -0.0549 0.0049 106 HIS A N 814 C CA . HIS A 107 ? 1.5260 1.4601 1.6870 0.0721 -0.0474 0.0101 106 HIS A CA 815 C C . HIS A 107 ? 1.5296 1.4524 1.6759 0.0902 -0.0562 0.0111 106 HIS A C 816 O O . HIS A 107 ? 1.5374 1.4336 1.6665 0.0944 -0.0476 0.0138 106 HIS A O 817 C CB . HIS A 107 ? 1.5845 1.4999 1.7208 0.0754 -0.0451 0.0139 106 HIS A CB 818 C CG . HIS A 107 ? 1.6603 1.5323 1.7542 0.0878 -0.0390 0.0200 106 HIS A CG 819 N ND1 . HIS A 107 ? 1.6966 1.5378 1.7746 0.0820 -0.0200 0.0239 106 HIS A ND1 820 C CD2 . HIS A 107 ? 1.7543 1.6069 1.8169 0.1060 -0.0495 0.0229 106 HIS A CD2 821 C CE1 . HIS A 107 ? 1.7636 1.5652 1.7998 0.0963 -0.0172 0.0299 106 HIS A CE1 822 N NE2 . HIS A 107 ? 1.8061 1.6140 1.8311 0.1119 -0.0360 0.0296 106 HIS A NE2 823 N N . THR A 108 ? 1.5261 1.4684 1.6797 0.1011 -0.0733 0.0085 107 THR A N 824 C CA . THR A 108 ? 1.5571 1.4924 1.6997 0.1206 -0.0841 0.0091 107 THR A CA 825 C C . THR A 108 ? 1.5373 1.4792 1.6966 0.1216 -0.0799 0.0070 107 THR A C 826 O O . THR A 108 ? 1.5416 1.4586 1.6810 0.1349 -0.0777 0.0103 107 THR A O 827 C CB . THR A 108 ? 1.5756 1.5386 1.7321 0.1298 -0.1047 0.0045 107 THR A CB 828 O OG1 . THR A 108 ? 1.6144 1.5714 1.7555 0.1265 -0.1078 0.0051 107 THR A OG1 829 C CG2 . THR A 108 ? 1.6036 1.5577 1.7459 0.1529 -0.1179 0.0057 107 THR A CG2 830 N N . MET A 109 ? 1.4889 1.4609 1.6813 0.1082 -0.0780 0.0018 108 MET A N 831 C CA . MET A 109 ? 1.4814 1.4585 1.6876 0.1080 -0.0727 -0.0010 108 MET A CA 832 C C . MET A 109 ? 1.5164 1.4588 1.7008 0.1028 -0.0567 0.0018 108 MET A C 833 O O . MET A 109 ? 1.5195 1.4444 1.6942 0.1122 -0.0525 0.0022 108 MET A O 834 C CB . MET A 109 ? 1.4399 1.4510 1.6795 0.0934 -0.0723 -0.0067 108 MET A CB 835 C CG . MET A 109 ? 1.4165 1.4328 1.6683 0.0942 -0.0668 -0.0104 108 MET A CG 836 S SD . MET A 109 ? 1.3717 1.4203 1.6537 0.0776 -0.0643 -0.0161 108 MET A SD 837 C CE . MET A 109 ? 1.3730 1.4563 1.6807 0.0828 -0.0780 -0.0187 108 MET A CE 838 N N . VAL A 110 ? 1.5367 1.4691 1.7150 0.0875 -0.0471 0.0034 109 VAL A N 839 C CA . VAL A 110 ? 1.5806 1.4826 1.7429 0.0786 -0.0311 0.0047 109 VAL A CA 840 C C . VAL A 110 ? 1.6289 1.4881 1.7539 0.0934 -0.0256 0.0110 109 VAL A C 841 O O . VAL A 110 ? 1.6419 1.4741 1.7527 0.0953 -0.0157 0.0114 109 VAL A O 842 C CB . VAL A 110 ? 1.5817 1.4863 1.7506 0.0594 -0.0223 0.0044 109 VAL A CB 843 C CG1 . VAL A 110 ? 1.6079 1.4822 1.7638 0.0487 -0.0056 0.0045 109 VAL A CG1 844 C CG2 . VAL A 110 ? 1.5462 1.4895 1.7484 0.0465 -0.0280 -0.0009 109 VAL A CG2 845 N N . GLU A 111 ? 1.6773 1.5273 1.7835 0.1045 -0.0320 0.0159 110 GLU A N 846 C CA . GLU A 111 ? 1.7906 1.5977 1.8562 0.1214 -0.0286 0.0229 110 GLU A CA 847 C C . GLU A 111 ? 1.8416 1.6430 1.9032 0.1406 -0.0355 0.0230 110 GLU A C 848 O O . GLU A 111 ? 1.9056 1.6666 1.9377 0.1496 -0.0257 0.0276 110 GLU A O 849 C CB . GLU A 111 ? 1.8772 1.6773 1.9210 0.1320 -0.0378 0.0273 110 GLU A CB 850 C CG . GLU A 111 ? 1.9376 1.7120 1.9605 0.1201 -0.0219 0.0314 110 GLU A CG 851 C CD . GLU A 111 ? 2.0070 1.7314 1.9970 0.1195 -0.0013 0.0370 110 GLU A CD 852 O OE1 . GLU A 111 ? 1.9943 1.6946 1.9647 0.1346 -0.0021 0.0400 110 GLU A OE1 853 O OE2 . GLU A 111 ? 2.0747 1.7835 2.0598 0.1037 0.0166 0.0383 110 GLU A OE2 854 N N . SER A 112 ? 1.8437 1.6845 1.9356 0.1470 -0.0510 0.0179 111 SER A N 855 C CA . SER A 112 ? 1.8797 1.7222 1.9761 0.1652 -0.0570 0.0168 111 SER A CA 856 C C . SER A 112 ? 1.8496 1.6773 1.9483 0.1572 -0.0411 0.0143 111 SER A C 857 O O . SER A 112 ? 1.9085 1.7061 1.9868 0.1718 -0.0358 0.0172 111 SER A O 858 C CB . SER A 112 ? 1.8730 1.7648 2.0076 0.1705 -0.0744 0.0107 111 SER A CB 859 O OG . SER A 112 ? 1.8997 1.8009 2.0286 0.1813 -0.0913 0.0121 111 SER A OG 860 N N . LEU A 113 ? 1.7586 1.6053 1.8797 0.1348 -0.0339 0.0086 112 LEU A N 861 C CA . LEU A 113 ? 1.7242 1.5560 1.8452 0.1244 -0.0197 0.0047 112 LEU A CA 862 C C . LEU A 113 ? 1.7279 1.5080 1.8129 0.1228 -0.0038 0.0092 112 LEU A C 863 O O . LEU A 113 ? 1.7407 1.4934 1.8115 0.1286 0.0053 0.0086 112 LEU A O 864 C CB . LEU A 113 ? 1.7063 1.5652 1.8528 0.1001 -0.0170 -0.0016 112 LEU A CB 865 C CG . LEU A 113 ? 1.6988 1.6026 1.8788 0.0998 -0.0280 -0.0067 112 LEU A CG 866 C CD1 . LEU A 113 ? 1.6789 1.6070 1.8782 0.0782 -0.0279 -0.0104 112 LEU A CD1 867 C CD2 . LEU A 113 ? 1.7142 1.6186 1.9006 0.1071 -0.0243 -0.0112 112 LEU A CD2 868 N N . VAL A 114 ? 1.7284 1.4935 1.7981 0.1149 0.0010 0.0137 113 VAL A N 869 C CA . VAL A 114 ? 1.7862 1.5000 1.8207 0.1126 0.0183 0.0187 113 VAL A CA 870 C C . VAL A 114 ? 1.8578 1.5342 1.8577 0.1391 0.0177 0.0260 113 VAL A C 871 O O . VAL A 114 ? 1.8774 1.5113 1.8524 0.1410 0.0324 0.0277 113 VAL A O 872 C CB . VAL A 114 ? 1.8066 1.5128 1.8314 0.1017 0.0242 0.0228 113 VAL A CB 873 C CG1 . VAL A 114 ? 1.8634 1.5119 1.8464 0.1038 0.0429 0.0298 113 VAL A CG1 874 C CG2 . VAL A 114 ? 1.7843 1.5199 1.8414 0.0752 0.0285 0.0159 113 VAL A CG2 875 N N . GLY A 115 ? 1.8903 1.5818 1.8882 0.1598 0.0000 0.0297 114 GLY A N 876 C CA . GLY A 115 ? 1.9841 1.6472 1.9532 0.1887 -0.0055 0.0363 114 GLY A CA 877 C C . GLY A 115 ? 2.0153 1.6742 1.9922 0.1986 -0.0025 0.0330 114 GLY A C 878 O O . GLY A 115 ? 2.0360 1.6542 1.9816 0.2181 0.0023 0.0388 114 GLY A O 879 N N . TRP A 116 ? 2.0081 1.7062 2.0240 0.1862 -0.0044 0.0238 115 TRP A N 880 C CA . TRP A 116 ? 2.0323 1.7274 2.0569 0.1933 0.0008 0.0193 115 TRP A CA 881 C C . TRP A 116 ? 2.0117 1.6727 2.0224 0.1745 0.0222 0.0156 115 TRP A C 882 O O . TRP A 116 ? 2.0443 1.6990 2.0591 0.1773 0.0289 0.0106 115 TRP A O 883 C CB . TRP A 116 ? 2.0235 1.7740 2.0933 0.1908 -0.0102 0.0112 115 TRP A CB 884 C CG . TRP A 116 ? 2.0588 1.8485 2.1495 0.2044 -0.0313 0.0124 115 TRP A CG 885 C CD1 . TRP A 116 ? 2.1107 1.8910 2.1842 0.2279 -0.0442 0.0190 115 TRP A CD1 886 C CD2 . TRP A 116 ? 2.0315 1.8746 2.1631 0.1949 -0.0423 0.0060 115 TRP A CD2 887 N NE1 . TRP A 116 ? 2.0845 1.9111 2.1880 0.2323 -0.0635 0.0159 115 TRP A NE1 888 C CE2 . TRP A 116 ? 2.0494 1.9142 2.1892 0.2119 -0.0615 0.0081 115 TRP A CE2 889 C CE3 . TRP A 116 ? 1.9888 1.8610 2.1485 0.1738 -0.0378 -0.0012 115 TRP A CE3 890 C CZ2 . TRP A 116 ? 2.0145 1.9293 2.1922 0.2066 -0.0747 0.0025 115 TRP A CZ2 891 C CZ3 . TRP A 116 ? 1.9572 1.8764 2.1515 0.1701 -0.0500 -0.0054 115 TRP A CZ3 892 C CH2 . TRP A 116 ? 1.9669 1.9069 2.1711 0.1856 -0.0675 -0.0037 115 TRP A CH2 893 N N . GLY A 117 ? 1.9775 1.6171 1.9731 0.1549 0.0333 0.0170 116 GLY A N 894 C CA . GLY A 117 ? 1.9930 1.5959 1.9734 0.1366 0.0537 0.0132 116 GLY A CA 895 C C . GLY A 117 ? 1.9409 1.5684 1.9470 0.1053 0.0576 0.0042 116 GLY A C 896 O O . GLY A 117 ? 1.9377 1.5397 1.9360 0.0882 0.0723 -0.0012 116 GLY A O 897 N N . TYR A 118 ? 1.9156 1.5915 1.9520 0.0978 0.0441 0.0022 117 TYR A N 898 C CA . TYR A 118 ? 1.8952 1.5971 1.9566 0.0705 0.0454 -0.0053 117 TYR A CA 899 C C . TYR A 118 ? 1.8948 1.5804 1.9480 0.0548 0.0555 -0.0024 117 TYR A C 900 O O . TYR A 118 ? 1.9128 1.5718 1.9413 0.0658 0.0600 0.0062 117 TYR A O 901 C CB . TYR A 118 ? 1.8504 1.6070 1.9455 0.0696 0.0285 -0.0079 117 TYR A CB 902 C CG . TYR A 118 ? 1.8371 1.6136 1.9473 0.0755 0.0231 -0.0139 117 TYR A CG 903 C CD1 . TYR A 118 ? 1.8818 1.6525 1.9858 0.0993 0.0199 -0.0113 117 TYR A CD1 904 C CD2 . TYR A 118 ? 1.8150 1.6156 1.9452 0.0580 0.0218 -0.0223 117 TYR A CD2 905 C CE1 . TYR A 118 ? 1.8842 1.6729 2.0035 0.1046 0.0179 -0.0171 117 TYR A CE1 906 C CE2 . TYR A 118 ? 1.8185 1.6334 1.9585 0.0632 0.0194 -0.0276 117 TYR A CE2 907 C CZ . TYR A 118 ? 1.8386 1.6479 1.9744 0.0861 0.0188 -0.0251 117 TYR A CZ 908 O OH . TYR A 118 ? 1.8042 1.6278 1.9515 0.0913 0.0192 -0.0306 117 TYR A OH 909 N N . THR A 119 ? 1.8479 1.5500 1.9221 0.0299 0.0591 -0.0099 118 THR A N 910 C CA . THR A 119 ? 1.8670 1.5589 1.9420 0.0120 0.0706 -0.0092 118 THR A CA 911 C C . THR A 119 ? 1.8305 1.5701 1.9421 -0.0045 0.0613 -0.0140 118 THR A C 912 O O . THR A 119 ? 1.7995 1.5656 1.9325 -0.0143 0.0534 -0.0221 118 THR A O 913 C CB . THR A 119 ? 1.9194 1.5736 1.9822 -0.0046 0.0887 -0.0150 118 THR A CB 914 O OG1 . THR A 119 ? 1.9867 1.5931 2.0132 0.0121 0.0981 -0.0102 118 THR A OG1 915 C CG2 . THR A 119 ? 1.9514 1.5944 2.0176 -0.0231 0.1033 -0.0142 118 THR A CG2 916 N N . ARG A 120 ? 1.8608 1.6086 1.9770 -0.0064 0.0627 -0.0087 119 ARG A N 917 C CA . ARG A 120 ? 1.8795 1.6713 2.0296 -0.0188 0.0541 -0.0118 119 ARG A CA 918 C C . ARG A 120 ? 1.8637 1.6670 2.0373 -0.0430 0.0584 -0.0216 119 ARG A C 919 O O . ARG A 120 ? 1.8299 1.6057 1.9969 -0.0559 0.0743 -0.0240 119 ARG A O 920 C CB . ARG A 120 ? 1.9565 1.7462 2.1032 -0.0173 0.0597 -0.0048 119 ARG A CB 921 C CG . ARG A 120 ? 1.9923 1.7812 2.1209 0.0051 0.0499 0.0032 119 ARG A CG 922 C CD . ARG A 120 ? 2.0112 1.7981 2.1350 0.0051 0.0554 0.0088 119 ARG A CD 923 N NE . ARG A 120 ? 2.0110 1.8080 2.1246 0.0237 0.0410 0.0138 119 ARG A NE 924 C CZ . ARG A 120 ? 2.0854 1.8543 2.1648 0.0435 0.0382 0.0201 119 ARG A CZ 925 N NH1 . ARG A 120 ? 2.1626 1.8876 2.2113 0.0491 0.0504 0.0237 119 ARG A NH1 926 N NH2 . ARG A 120 ? 2.0392 1.8230 2.1146 0.0583 0.0225 0.0226 119 ARG A NH2 927 N N . GLY A 121 ? 1.8335 1.6764 2.0337 -0.0491 0.0440 -0.0274 120 GLY A N 928 C CA . GLY A 121 ? 1.8163 1.6758 2.0402 -0.0707 0.0431 -0.0373 120 GLY A CA 929 C C . GLY A 121 ? 1.8162 1.6553 2.0285 -0.0776 0.0455 -0.0460 120 GLY A C 930 O O . GLY A 121 ? 1.8506 1.7016 2.0795 -0.0956 0.0426 -0.0558 120 GLY A O 931 N N . GLU A 122 ? 1.8110 1.6193 1.9945 -0.0627 0.0500 -0.0428 121 GLU A N 932 C CA . GLU A 122 ? 1.8592 1.6410 2.0265 -0.0670 0.0550 -0.0505 121 GLU A CA 933 C C . GLU A 122 ? 1.8452 1.6363 2.0053 -0.0508 0.0446 -0.0506 121 GLU A C 934 O O . GLU A 122 ? 1.8403 1.6573 2.0139 -0.0572 0.0338 -0.0572 121 GLU A O 935 C CB . GLU A 122 ? 1.9584 1.6881 2.0963 -0.0642 0.0741 -0.0472 121 GLU A CB 936 C CG . GLU A 122 ? 1.9917 1.7075 2.1371 -0.0848 0.0886 -0.0497 121 GLU A CG 937 C CD . GLU A 122 ? 2.0450 1.7030 2.1579 -0.0843 0.1098 -0.0475 121 GLU A CD 938 O OE1 . GLU A 122 ? 2.0385 1.6674 2.1279 -0.0770 0.1129 -0.0501 121 GLU A OE1 939 O OE2 . GLU A 122 ? 2.1131 1.7525 2.2227 -0.0911 0.1250 -0.0431 121 GLU A OE2 940 N N . ASP A 123 ? 1.8693 1.6402 2.0088 -0.0293 0.0478 -0.0432 122 ASP A N 941 C CA . ASP A 123 ? 1.8850 1.6657 2.0215 -0.0125 0.0401 -0.0431 122 ASP A CA 942 C C . ASP A 123 ? 1.8452 1.6714 2.0053 -0.0067 0.0251 -0.0400 122 ASP A C 943 O O . ASP A 123 ? 1.7905 1.6361 1.9582 -0.0027 0.0181 -0.0434 122 ASP A O 944 C CB . ASP A 123 ? 1.9333 1.6839 2.0459 0.0107 0.0461 -0.0356 122 ASP A CB 945 C CG . ASP A 123 ? 2.0389 1.7377 2.1231 0.0083 0.0628 -0.0368 122 ASP A CG 946 O OD1 . ASP A 123 ? 2.1302 1.8149 2.2103 -0.0059 0.0688 -0.0464 122 ASP A OD1 947 O OD2 . ASP A 123 ? 2.0894 1.7591 2.1529 0.0211 0.0700 -0.0281 122 ASP A OD2 948 N N . VAL A 124 ? 1.8190 1.6585 1.9884 -0.0064 0.0222 -0.0335 123 VAL A N 949 C CA . VAL A 124 ? 1.7861 1.6651 1.9768 -0.0025 0.0093 -0.0305 123 VAL A CA 950 C C . VAL A 124 ? 1.7591 1.6586 1.9692 -0.0199 0.0071 -0.0319 123 VAL A C 951 O O . VAL A 124 ? 1.7498 1.6347 1.9570 -0.0273 0.0158 -0.0299 123 VAL A O 952 C CB . VAL A 124 ? 1.7866 1.6650 1.9707 0.0169 0.0056 -0.0217 123 VAL A CB 953 C CG1 . VAL A 124 ? 1.7859 1.6424 1.9566 0.0158 0.0135 -0.0157 123 VAL A CG1 954 C CG2 . VAL A 124 ? 1.7721 1.6903 1.9783 0.0209 -0.0076 -0.0205 123 VAL A CG2 955 N N . ARG A 125 ? 1.7022 1.6344 1.9318 -0.0257 -0.0033 -0.0353 124 ARG A N 956 C CA . ARG A 125 ? 1.6705 1.6269 1.9215 -0.0397 -0.0078 -0.0367 124 ARG A CA 957 C C . ARG A 125 ? 1.6328 1.6227 1.8999 -0.0342 -0.0196 -0.0337 124 ARG A C 958 O O . ARG A 125 ? 1.6148 1.6129 1.8799 -0.0260 -0.0249 -0.0343 124 ARG A O 959 C CB . ARG A 125 ? 1.6809 1.6388 1.9375 -0.0567 -0.0090 -0.0461 124 ARG A CB 960 C CG . ARG A 125 ? 1.7368 1.6603 1.9785 -0.0654 0.0033 -0.0510 124 ARG A CG 961 C CD . ARG A 125 ? 1.7678 1.6973 2.0191 -0.0847 -0.0003 -0.0619 124 ARG A CD 962 N NE . ARG A 125 ? 1.8447 1.7384 2.0780 -0.0929 0.0106 -0.0687 124 ARG A NE 963 C CZ . ARG A 125 ? 1.9128 1.8039 2.1502 -0.1111 0.0088 -0.0802 124 ARG A CZ 964 N NH1 . ARG A 125 ? 1.9280 1.8522 2.1872 -0.1218 -0.0052 -0.0856 124 ARG A NH1 965 N NH2 . ARG A 125 ? 1.9598 1.8140 2.1785 -0.1184 0.0205 -0.0865 124 ARG A NH2 966 N N . GLY A 126 ? 1.6062 1.6138 1.8895 -0.0389 -0.0220 -0.0308 125 GLY A N 967 C CA . GLY A 126 ? 1.5567 1.5931 1.8547 -0.0351 -0.0319 -0.0281 125 GLY A CA 968 C C . GLY A 126 ? 1.5064 1.5642 1.8191 -0.0456 -0.0399 -0.0325 125 GLY A C 969 O O . GLY A 126 ? 1.5255 1.5824 1.8445 -0.0581 -0.0391 -0.0377 125 GLY A O 970 N N . ALA A 127 ? 1.4501 1.5267 1.7680 -0.0405 -0.0481 -0.0308 126 ALA A N 971 C CA . ALA A 127 ? 1.4170 1.5129 1.7450 -0.0473 -0.0571 -0.0332 126 ALA A CA 972 C C . ALA A 127 ? 1.4126 1.5288 1.7549 -0.0431 -0.0618 -0.0274 126 ALA A C 973 O O . ALA A 127 ? 1.3944 1.5200 1.7353 -0.0383 -0.0666 -0.0255 126 ALA A O 974 C CB . ALA A 127 ? 1.3939 1.4867 1.7083 -0.0452 -0.0603 -0.0366 126 ALA A CB 975 N N . PRO A 128 ? 1.4010 1.5216 1.7559 -0.0452 -0.0586 -0.0247 127 PRO A N 976 C CA . PRO A 128 ? 1.3754 1.5130 1.7434 -0.0415 -0.0621 -0.0198 127 PRO A CA 977 C C . PRO A 128 ? 1.3534 1.5101 1.7337 -0.0458 -0.0716 -0.0209 127 PRO A C 978 O O . PRO A 128 ? 1.3373 1.4966 1.7204 -0.0538 -0.0760 -0.0262 127 PRO A O 979 C CB . PRO A 128 ? 1.3977 1.5308 1.7736 -0.0432 -0.0535 -0.0177 127 PRO A CB 980 C CG . PRO A 128 ? 1.4166 1.5392 1.7929 -0.0529 -0.0483 -0.0228 127 PRO A CG 981 C CD . PRO A 128 ? 1.4180 1.5264 1.7756 -0.0518 -0.0499 -0.0263 127 PRO A CD 982 N N . TYR A 129 ? 1.3202 1.4887 1.7063 -0.0401 -0.0754 -0.0161 128 TYR A N 983 C CA . TYR A 129 ? 1.3114 1.4957 1.7055 -0.0408 -0.0852 -0.0155 128 TYR A CA 984 C C . TYR A 129 ? 1.2859 1.4804 1.6920 -0.0348 -0.0849 -0.0095 128 TYR A C 985 O O . TYR A 129 ? 1.1915 1.3798 1.5969 -0.0307 -0.0774 -0.0066 128 TYR A O 986 C CB . TYR A 129 ? 1.3144 1.4943 1.6905 -0.0384 -0.0904 -0.0160 128 TYR A CB 987 C CG . TYR A 129 ? 1.3159 1.4882 1.6819 -0.0316 -0.0847 -0.0127 128 TYR A CG 988 C CD1 . TYR A 129 ? 1.3087 1.4689 1.6663 -0.0301 -0.0781 -0.0149 128 TYR A CD1 989 C CD2 . TYR A 129 ? 1.3103 1.4874 1.6765 -0.0265 -0.0860 -0.0078 128 TYR A CD2 990 C CE1 . TYR A 129 ? 1.2820 1.4396 1.6357 -0.0241 -0.0744 -0.0131 128 TYR A CE1 991 C CE2 . TYR A 129 ? 1.2866 1.4588 1.6477 -0.0223 -0.0807 -0.0063 128 TYR A CE2 992 C CZ . TYR A 129 ? 1.2796 1.4441 1.6363 -0.0212 -0.0757 -0.0094 128 TYR A CZ 993 O OH . TYR A 129 ? 1.2583 1.4221 1.6149 -0.0172 -0.0719 -0.0091 128 TYR A OH 994 N N . ASP A 130 ? 1.3072 1.5156 1.7222 -0.0334 -0.0935 -0.0079 129 ASP A N 995 C CA . ASP A 130 ? 1.2960 1.5118 1.7201 -0.0263 -0.0932 -0.0019 129 ASP A CA 996 C C . ASP A 130 ? 1.2779 1.4837 1.6841 -0.0206 -0.0923 0.0018 129 ASP A C 997 O O . ASP A 130 ? 1.2556 1.4618 1.6523 -0.0180 -0.0988 0.0038 129 ASP A O 998 C CB . ASP A 130 ? 1.3075 1.5413 1.7477 -0.0249 -0.1035 -0.0011 129 ASP A CB 999 C CG . ASP A 130 ? 1.2930 1.5344 1.7479 -0.0172 -0.1006 0.0045 129 ASP A CG 1000 O OD1 . ASP A 130 ? 1.2452 1.4752 1.6918 -0.0128 -0.0922 0.0081 129 ASP A OD1 1001 O OD2 . ASP A 130 ? 1.3053 1.5645 1.7812 -0.0152 -0.1071 0.0047 129 ASP A OD2 1002 N N . TRP A 131 ? 1.2676 1.4639 1.6690 -0.0189 -0.0841 0.0024 130 TRP A N 1003 C CA . TRP A 131 ? 1.2712 1.4594 1.6602 -0.0155 -0.0819 0.0042 130 TRP A CA 1004 C C . TRP A 131 ? 1.2800 1.4690 1.6705 -0.0106 -0.0820 0.0094 130 TRP A C 1005 O O . TRP A 131 ? 1.2797 1.4617 1.6614 -0.0093 -0.0793 0.0106 130 TRP A O 1006 C CB . TRP A 131 ? 1.2747 1.4548 1.6604 -0.0149 -0.0756 0.0022 130 TRP A CB 1007 C CG . TRP A 131 ? 1.2738 1.4520 1.6663 -0.0140 -0.0711 0.0026 130 TRP A CG 1008 C CD1 . TRP A 131 ? 1.2749 1.4478 1.6668 -0.0161 -0.0674 0.0004 130 TRP A CD1 1009 C CD2 . TRP A 131 ? 1.3341 1.5122 1.7319 -0.0104 -0.0679 0.0057 130 TRP A CD2 1010 N NE1 . TRP A 131 ? 1.3241 1.4933 1.7198 -0.0142 -0.0614 0.0021 130 TRP A NE1 1011 C CE2 . TRP A 131 ? 1.3434 1.5161 1.7429 -0.0106 -0.0618 0.0050 130 TRP A CE2 1012 C CE3 . TRP A 131 ? 1.3836 1.5622 1.7825 -0.0069 -0.0682 0.0089 130 TRP A CE3 1013 C CZ2 . TRP A 131 ? 1.3579 1.5267 1.7601 -0.0071 -0.0558 0.0070 130 TRP A CZ2 1014 C CZ3 . TRP A 131 ? 1.3778 1.5527 1.7805 -0.0035 -0.0630 0.0108 130 TRP A CZ3 1015 C CH2 . TRP A 131 ? 1.3546 1.5250 1.7588 -0.0035 -0.0568 0.0096 130 TRP A CH2 1016 N N . ARG A 132 ? 1.2832 1.4803 1.6861 -0.0077 -0.0842 0.0122 131 ARG A N 1017 C CA . ARG A 132 ? 1.3127 1.5087 1.7158 -0.0014 -0.0846 0.0177 131 ARG A CA 1018 C C . ARG A 132 ? 1.3398 1.5337 1.7300 0.0007 -0.0915 0.0206 131 ARG A C 1019 O O . ARG A 132 ? 1.3914 1.5763 1.7725 0.0055 -0.0897 0.0255 131 ARG A O 1020 C CB . ARG A 132 ? 1.3200 1.5271 1.7423 0.0026 -0.0852 0.0199 131 ARG A CB 1021 C CG . ARG A 132 ? 1.3250 1.5306 1.7570 0.0014 -0.0759 0.0179 131 ARG A CG 1022 C CD . ARG A 132 ? 1.3563 1.5736 1.8095 0.0061 -0.0741 0.0201 131 ARG A CD 1023 N NE . ARG A 132 ? 1.3660 1.6020 1.8371 0.0031 -0.0817 0.0179 131 ARG A NE 1024 C CZ . ARG A 132 ? 1.3803 1.6336 1.8765 0.0070 -0.0833 0.0189 131 ARG A CZ 1025 N NH1 . ARG A 132 ? 1.3507 1.6032 1.8555 0.0154 -0.0764 0.0230 131 ARG A NH1 1026 N NH2 . ARG A 132 ? 1.3783 1.6505 1.8924 0.0024 -0.0919 0.0151 131 ARG A NH2 1027 N N . ARG A 133 ? 1.3586 1.5577 1.7451 -0.0027 -0.0989 0.0174 132 ARG A N 1028 C CA . ARG A 133 ? 1.4309 1.6262 1.8005 -0.0003 -0.1068 0.0196 132 ARG A CA 1029 C C . ARG A 133 ? 1.4294 1.6119 1.7783 -0.0047 -0.1026 0.0169 132 ARG A C 1030 O O . ARG A 133 ? 1.3746 1.5548 1.7260 -0.0094 -0.0956 0.0126 132 ARG A O 1031 C CB . ARG A 133 ? 1.4800 1.6900 1.8587 -0.0011 -0.1197 0.0169 132 ARG A CB 1032 C CG . ARG A 133 ? 1.5106 1.7364 1.9128 0.0049 -0.1244 0.0199 132 ARG A CG 1033 C CD . ARG A 133 ? 1.5367 1.7818 1.9543 0.0026 -0.1380 0.0154 132 ARG A CD 1034 N NE . ARG A 133 ? 1.5852 1.8460 2.0222 0.0120 -0.1458 0.0196 132 ARG A NE 1035 C CZ . ARG A 133 ? 1.6438 1.9271 2.1021 0.0120 -0.1593 0.0160 132 ARG A CZ 1036 N NH1 . ARG A 133 ? 1.6567 1.9475 2.1181 0.0015 -0.1664 0.0073 132 ARG A NH1 1037 N NH2 . ARG A 133 ? 1.6871 1.9858 2.1653 0.0228 -0.1659 0.0204 132 ARG A NH2 1038 N N . ALA A 134 ? 1.4642 1.6375 1.7917 -0.0020 -0.1068 0.0196 133 ALA A N 1039 C CA . ALA A 134 ? 1.4840 1.6437 1.7895 -0.0054 -0.1016 0.0171 133 ALA A CA 1040 C C . ALA A 134 ? 1.5037 1.6664 1.8020 -0.0094 -0.1108 0.0110 133 ALA A C 1041 O O . ALA A 134 ? 1.5239 1.6996 1.8338 -0.0095 -0.1224 0.0093 133 ALA A O 1042 C CB . ALA A 134 ? 1.5106 1.6533 1.7916 -0.0004 -0.0987 0.0236 133 ALA A CB 1043 N N . PRO A 135 ? 1.5081 1.6589 1.7885 -0.0131 -0.1051 0.0069 134 PRO A N 1044 C CA . PRO A 135 ? 1.5391 1.6883 1.8087 -0.0176 -0.1126 0.0000 134 PRO A CA 1045 C C . PRO A 135 ? 1.5610 1.7113 1.8167 -0.0152 -0.1290 0.0004 134 PRO A C 1046 O O . PRO A 135 ? 1.5919 1.7488 1.8504 -0.0202 -0.1393 -0.0064 134 PRO A O 1047 C CB . PRO A 135 ? 1.5625 1.6940 1.8097 -0.0190 -0.1010 -0.0022 134 PRO A CB 1048 C CG . PRO A 135 ? 1.5420 1.6750 1.8041 -0.0181 -0.0874 0.0001 134 PRO A CG 1049 C CD . PRO A 135 ? 1.5101 1.6502 1.7845 -0.0141 -0.0901 0.0070 134 PRO A CD 1050 N N . ASN A 136 ? 1.5640 1.7068 1.8041 -0.0074 -0.1317 0.0081 135 ASN A N 1051 C CA . ASN A 136 ? 1.6069 1.7503 1.8316 -0.0021 -0.1494 0.0096 135 ASN A CA 1052 C C . ASN A 136 ? 1.5895 1.7594 1.8456 -0.0025 -0.1650 0.0067 135 ASN A C 1053 O O . ASN A 136 ? 1.6553 1.8315 1.9050 -0.0018 -0.1827 0.0031 135 ASN A O 1054 C CB . ASN A 136 ? 1.6136 1.7426 1.8181 0.0083 -0.1476 0.0203 135 ASN A CB 1055 C CG . ASN A 136 ? 1.5831 1.7220 1.8146 0.0127 -0.1415 0.0268 135 ASN A CG 1056 O OD1 . ASN A 136 ? 1.5230 1.6760 1.7842 0.0075 -0.1350 0.0235 135 ASN A OD1 1057 N ND2 . ASN A 136 ? 1.5920 1.7202 1.8095 0.0229 -0.1429 0.0361 135 ASN A ND2 1058 N N . GLU A 137 ? 1.5261 1.7114 1.8161 -0.0038 -0.1582 0.0077 136 GLU A N 1059 C CA . GLU A 137 ? 1.5145 1.7255 1.8387 -0.0046 -0.1685 0.0051 136 GLU A CA 1060 C C . GLU A 137 ? 1.4732 1.6937 1.8206 -0.0160 -0.1623 -0.0031 136 GLU A C 1061 O O . GLU A 137 ? 1.4928 1.7318 1.8722 -0.0176 -0.1624 -0.0042 136 GLU A O 1062 C CB . GLU A 137 ? 1.5414 1.7602 1.8846 0.0043 -0.1645 0.0134 136 GLU A CB 1063 C CG . GLU A 137 ? 1.5960 1.8054 1.9187 0.0170 -0.1718 0.0223 136 GLU A CG 1064 C CD . GLU A 137 ? 1.6475 1.8594 1.9863 0.0258 -0.1646 0.0303 136 GLU A CD 1065 O OE1 . GLU A 137 ? 1.6980 1.9202 2.0457 0.0364 -0.1759 0.0349 136 GLU A OE1 1066 O OE2 . GLU A 137 ? 1.6450 1.8484 1.9877 0.0225 -0.1481 0.0316 136 GLU A OE2 1067 N N . ASN A 138 ? 1.4406 1.6462 1.7707 -0.0231 -0.1554 -0.0085 137 ASN A N 1068 C CA . ASN A 138 ? 1.4125 1.6215 1.7580 -0.0333 -0.1498 -0.0163 137 ASN A CA 1069 C C . ASN A 138 ? 1.4228 1.6211 1.7475 -0.0408 -0.1557 -0.0252 137 ASN A C 1070 O O . ASN A 138 ? 1.4116 1.5979 1.7307 -0.0469 -0.1460 -0.0303 137 ASN A O 1071 C CB . ASN A 138 ? 1.4027 1.6020 1.7506 -0.0332 -0.1322 -0.0139 137 ASN A CB 1072 C CG . ASN A 138 ? 1.3889 1.6002 1.7632 -0.0302 -0.1266 -0.0093 137 ASN A CG 1073 O OD1 . ASN A 138 ? 1.3896 1.6130 1.7868 -0.0349 -0.1270 -0.0125 137 ASN A OD1 1074 N ND2 . ASN A 138 ? 1.3614 1.5677 1.7318 -0.0231 -0.1200 -0.0024 137 ASN A ND2 1075 N N . GLY A 139 ? 1.4319 1.6330 1.7435 -0.0393 -0.1723 -0.0272 138 GLY A N 1076 C CA . GLY A 139 ? 1.4649 1.6554 1.7545 -0.0467 -0.1808 -0.0370 138 GLY A CA 1077 C C . GLY A 139 ? 1.4494 1.6451 1.7589 -0.0598 -0.1789 -0.0473 138 GLY A C 1078 O O . GLY A 139 ? 1.4513 1.6278 1.7418 -0.0661 -0.1719 -0.0537 138 GLY A O 1079 N N . PRO A 140 ? 1.4178 1.6379 1.7656 -0.0639 -0.1832 -0.0489 139 PRO A N 1080 C CA . PRO A 140 ? 1.4156 1.6393 1.7841 -0.0776 -0.1790 -0.0584 139 PRO A CA 1081 C C . PRO A 140 ? 1.4040 1.6070 1.7653 -0.0801 -0.1580 -0.0576 139 PRO A C 1082 O O . PRO A 140 ? 1.3894 1.5788 1.7443 -0.0901 -0.1535 -0.0661 139 PRO A O 1083 C CB . PRO A 140 ? 1.3942 1.6474 1.8069 -0.0782 -0.1816 -0.0567 139 PRO A CB 1084 C CG . PRO A 140 ? 1.4040 1.6721 1.8169 -0.0661 -0.1965 -0.0501 139 PRO A CG 1085 C CD . PRO A 140 ? 1.4045 1.6487 1.7786 -0.0559 -0.1908 -0.0421 139 PRO A CD 1086 N N . TYR A 141 ? 1.3925 1.5923 1.7543 -0.0707 -0.1461 -0.0478 140 TYR A N 1087 C CA . TYR A 141 ? 1.4062 1.5876 1.7599 -0.0699 -0.1287 -0.0461 140 TYR A CA 1088 C C . TYR A 141 ? 1.4075 1.5651 1.7293 -0.0713 -0.1254 -0.0511 140 TYR A C 1089 O O . TYR A 141 ? 1.3894 1.5316 1.7065 -0.0764 -0.1161 -0.0559 140 TYR A O 1090 C CB . TYR A 141 ? 1.4079 1.5909 1.7639 -0.0589 -0.1206 -0.0358 140 TYR A CB 1091 C CG . TYR A 141 ? 1.4099 1.5752 1.7533 -0.0552 -0.1066 -0.0340 140 TYR A CG 1092 C CD1 . TYR A 141 ? 1.3868 1.5462 1.7397 -0.0573 -0.0964 -0.0345 140 TYR A CD1 1093 C CD2 . TYR A 141 ? 1.4148 1.5693 1.7371 -0.0489 -0.1033 -0.0316 140 TYR A CD2 1094 C CE1 . TYR A 141 ? 1.3728 1.5174 1.7145 -0.0518 -0.0861 -0.0327 140 TYR A CE1 1095 C CE2 . TYR A 141 ? 1.4080 1.5508 1.7241 -0.0447 -0.0918 -0.0307 140 TYR A CE2 1096 C CZ . TYR A 141 ? 1.3860 1.5246 1.7119 -0.0454 -0.0846 -0.0312 140 TYR A CZ 1097 O OH . TYR A 141 ? 1.3412 1.4693 1.6610 -0.0393 -0.0756 -0.0302 140 TYR A OH 1098 N N . PHE A 142 ? 1.4041 1.5562 1.7022 -0.0660 -0.1317 -0.0497 141 PHE A N 1099 C CA . PHE A 142 ? 1.4464 1.5748 1.7124 -0.0660 -0.1265 -0.0540 141 PHE A CA 1100 C C . PHE A 142 ? 1.5010 1.6188 1.7559 -0.0771 -0.1327 -0.0660 141 PHE A C 1101 O O . PHE A 142 ? 1.5214 1.6172 1.7576 -0.0792 -0.1232 -0.0711 141 PHE A O 1102 C CB . PHE A 142 ? 1.4572 1.5795 1.6980 -0.0580 -0.1296 -0.0492 141 PHE A CB 1103 C CG . PHE A 142 ? 1.4464 1.5732 1.6944 -0.0486 -0.1201 -0.0389 141 PHE A CG 1104 C CD1 . PHE A 142 ? 1.4450 1.5656 1.6982 -0.0456 -0.1048 -0.0371 141 PHE A CD1 1105 C CD2 . PHE A 142 ? 1.4458 1.5823 1.6952 -0.0425 -0.1271 -0.0315 141 PHE A CD2 1106 C CE1 . PHE A 142 ? 1.4463 1.5721 1.7079 -0.0386 -0.0974 -0.0294 141 PHE A CE1 1107 C CE2 . PHE A 142 ? 1.4353 1.5737 1.6910 -0.0355 -0.1176 -0.0232 141 PHE A CE2 1108 C CZ . PHE A 142 ? 1.4341 1.5681 1.6968 -0.0345 -0.1031 -0.0228 141 PHE A CZ 1109 N N . LEU A 143 ? 1.5572 1.6911 1.8249 -0.0841 -0.1489 -0.0710 142 LEU A N 1110 C CA . LEU A 143 ? 1.6386 1.7653 1.9012 -0.0973 -0.1562 -0.0841 142 LEU A CA 1111 C C . LEU A 143 ? 1.6092 1.7279 1.8882 -0.1057 -0.1420 -0.0880 142 LEU A C 1112 O O . LEU A 143 ? 1.5929 1.6880 1.8534 -0.1124 -0.1358 -0.0963 142 LEU A O 1113 C CB . LEU A 143 ? 1.7052 1.8574 1.9876 -0.1033 -0.1776 -0.0891 142 LEU A CB 1114 C CG . LEU A 143 ? 1.7967 1.9536 2.0576 -0.0948 -0.1954 -0.0863 142 LEU A CG 1115 C CD1 . LEU A 143 ? 1.8360 2.0250 2.1268 -0.0973 -0.2166 -0.0891 142 LEU A CD1 1116 C CD2 . LEU A 143 ? 1.8262 1.9555 2.0413 -0.0972 -0.2000 -0.0944 142 LEU A CD2 1117 N N . ALA A 144 ? 1.5666 1.7018 1.8774 -0.1046 -0.1359 -0.0818 143 ALA A N 1118 C CA . ALA A 144 ? 1.5716 1.6970 1.8958 -0.1109 -0.1209 -0.0834 143 ALA A CA 1119 C C . ALA A 144 ? 1.5491 1.6469 1.8494 -0.1033 -0.1048 -0.0801 143 ALA A C 1120 O O . ALA A 144 ? 1.5448 1.6212 1.8379 -0.1092 -0.0945 -0.0853 143 ALA A O 1121 C CB . ALA A 144 ? 1.5703 1.7166 1.9278 -0.1086 -0.1165 -0.0760 143 ALA A CB 1122 N N . LEU A 145 ? 1.4965 1.5950 1.7859 -0.0901 -0.1024 -0.0717 144 LEU A N 1123 C CA . LEU A 145 ? 1.4992 1.5771 1.7706 -0.0812 -0.0888 -0.0687 144 LEU A CA 1124 C C . LEU A 145 ? 1.5349 1.5875 1.7774 -0.0847 -0.0862 -0.0776 144 LEU A C 1125 O O . LEU A 145 ? 1.5692 1.6000 1.8025 -0.0840 -0.0743 -0.0800 144 LEU A O 1126 C CB . LEU A 145 ? 1.5090 1.5962 1.7778 -0.0687 -0.0880 -0.0598 144 LEU A CB 1127 C CG . LEU A 145 ? 1.5236 1.5964 1.7804 -0.0584 -0.0752 -0.0568 144 LEU A CG 1128 C CD1 . LEU A 145 ? 1.5139 1.5772 1.7790 -0.0564 -0.0654 -0.0557 144 LEU A CD1 1129 C CD2 . LEU A 145 ? 1.5123 1.5988 1.7744 -0.0489 -0.0746 -0.0487 144 LEU A CD2 1130 N N . ARG A 146 ? 1.5328 1.5859 1.7585 -0.0876 -0.0973 -0.0823 145 ARG A N 1131 C CA . ARG A 146 ? 1.5807 1.6076 1.7747 -0.0915 -0.0954 -0.0918 145 ARG A CA 1132 C C . ARG A 146 ? 1.6543 1.6662 1.8501 -0.1048 -0.0933 -0.1021 145 ARG A C 1133 O O . ARG A 146 ? 1.6870 1.6709 1.8638 -0.1046 -0.0813 -0.1068 145 ARG A O 1134 C CB . ARG A 146 ? 1.5997 1.6291 1.7731 -0.0938 -0.1106 -0.0959 145 ARG A CB 1135 C CG . ARG A 146 ? 1.6536 1.6526 1.7865 -0.0934 -0.1056 -0.1034 145 ARG A CG 1136 C CD . ARG A 146 ? 1.6951 1.6869 1.8088 -0.1055 -0.1221 -0.1159 145 ARG A CD 1137 N NE . ARG A 146 ? 1.7921 1.7524 1.8614 -0.1038 -0.1171 -0.1227 145 ARG A NE 1138 C CZ . ARG A 146 ? 1.8440 1.7976 1.8834 -0.0965 -0.1207 -0.1200 145 ARG A CZ 1139 N NH1 . ARG A 146 ? 1.8476 1.8234 1.8964 -0.0899 -0.1302 -0.1103 145 ARG A NH1 1140 N NH2 . ARG A 146 ? 1.8797 1.8011 1.8770 -0.0955 -0.1132 -0.1269 145 ARG A NH2 1141 N N . GLU A 147 ? 1.6857 1.7159 1.9057 -0.1163 -0.1038 -0.1058 146 GLU A N 1142 C CA . GLU A 147 ? 1.7166 1.7340 1.9424 -0.1315 -0.1011 -0.1163 146 GLU A CA 1143 C C . GLU A 147 ? 1.6053 1.6049 1.8368 -0.1289 -0.0815 -0.1120 146 GLU A C 1144 O O . GLU A 147 ? 1.6059 1.5770 1.8231 -0.1360 -0.0721 -0.1195 146 GLU A O 1145 C CB . GLU A 147 ? 1.8269 1.8729 2.0848 -0.1444 -0.1157 -0.1211 146 GLU A CB 1146 C CG . GLU A 147 ? 1.9455 2.0031 2.1936 -0.1498 -0.1378 -0.1295 146 GLU A CG 1147 C CD . GLU A 147 ? 2.0319 2.1162 2.3141 -0.1649 -0.1526 -0.1381 146 GLU A CD 1148 O OE1 . GLU A 147 ? 2.1019 2.2108 2.4216 -0.1648 -0.1498 -0.1319 146 GLU A OE1 1149 O OE2 . GLU A 147 ? 2.0731 2.1541 2.3453 -0.1769 -0.1670 -0.1518 146 GLU A OE2 1150 N N . MET A 148 ? 1.4973 1.5110 1.7465 -0.1183 -0.0757 -0.1000 147 MET A N 1151 C CA . MET A 148 ? 1.4813 1.4775 1.7323 -0.1132 -0.0588 -0.0945 147 MET A CA 1152 C C . MET A 148 ? 1.4765 1.4433 1.6986 -0.1023 -0.0476 -0.0941 147 MET A C 1153 O O . MET A 148 ? 1.4185 1.3573 1.6300 -0.1030 -0.0350 -0.0961 147 MET A O 1154 C CB . MET A 148 ? 1.4617 1.4788 1.7333 -0.1029 -0.0571 -0.0823 147 MET A CB 1155 C CG . MET A 148 ? 1.4781 1.4767 1.7493 -0.0976 -0.0417 -0.0765 147 MET A CG 1156 S SD . MET A 148 ? 1.4666 1.4875 1.7606 -0.0890 -0.0406 -0.0645 147 MET A SD 1157 C CE . MET A 148 ? 1.4523 1.4838 1.7376 -0.0711 -0.0454 -0.0573 147 MET A CE 1158 N N . ILE A 149 ? 1.5143 1.4866 1.7240 -0.0917 -0.0511 -0.0914 148 ILE A N 1159 C CA . ILE A 149 ? 1.5995 1.5478 1.7855 -0.0804 -0.0400 -0.0916 148 ILE A CA 1160 C C . ILE A 149 ? 1.6772 1.5938 1.8382 -0.0898 -0.0357 -0.1036 148 ILE A C 1161 O O . ILE A 149 ? 1.7060 1.5942 1.8528 -0.0842 -0.0222 -0.1046 148 ILE A O 1162 C CB . ILE A 149 ? 1.6167 1.5780 1.7960 -0.0698 -0.0431 -0.0876 148 ILE A CB 1163 C CG1 . ILE A 149 ? 1.5955 1.5822 1.7978 -0.0593 -0.0440 -0.0761 148 ILE A CG1 1164 C CG2 . ILE A 149 ? 1.6545 1.5912 1.8102 -0.0601 -0.0307 -0.0902 148 ILE A CG2 1165 C CD1 . ILE A 149 ? 1.6108 1.6154 1.8126 -0.0540 -0.0493 -0.0722 148 ILE A CD1 1166 N N . GLU A 150 ? 1.7022 1.6224 1.8567 -0.1034 -0.0477 -0.1130 149 GLU A N 1167 C CA . GLU A 150 ? 1.7735 1.6632 1.9032 -0.1148 -0.0456 -0.1265 149 GLU A CA 1168 C C . GLU A 150 ? 1.8491 1.7186 1.9856 -0.1250 -0.0359 -0.1305 149 GLU A C 1169 O O . GLU A 150 ? 1.9259 1.7591 2.0392 -0.1259 -0.0238 -0.1367 149 GLU A O 1170 C CB . GLU A 150 ? 1.7729 1.6741 1.8966 -0.1281 -0.0642 -0.1363 149 GLU A CB 1171 C CG . GLU A 150 ? 1.7682 1.6749 1.8707 -0.1184 -0.0707 -0.1341 149 GLU A CG 1172 C CD . GLU A 150 ? 1.7907 1.7095 1.8853 -0.1292 -0.0919 -0.1422 149 GLU A CD 1173 O OE1 . GLU A 150 ? 1.8096 1.7335 1.9167 -0.1453 -0.1025 -0.1518 149 GLU A OE1 1174 O OE2 . GLU A 150 ? 1.7960 1.7188 1.8716 -0.1213 -0.0981 -0.1392 149 GLU A OE2 1175 N N . GLU A 151 ? 1.8753 1.7656 2.0422 -0.1322 -0.0392 -0.1268 150 GLU A N 1176 C CA . GLU A 151 ? 1.9336 1.8045 2.1082 -0.1425 -0.0274 -0.1293 150 GLU A CA 1177 C C . GLU A 151 ? 1.8983 1.7403 2.0582 -0.1267 -0.0088 -0.1208 150 GLU A C 1178 O O . GLU A 151 ? 1.9940 1.7992 2.1372 -0.1312 0.0042 -0.1257 150 GLU A O 1179 C CB . GLU A 151 ? 1.9987 1.8999 2.2102 -0.1507 -0.0321 -0.1252 150 GLU A CB 1180 C CG . GLU A 151 ? 2.1210 2.0034 2.3424 -0.1667 -0.0202 -0.1306 150 GLU A CG 1181 C CD . GLU A 151 ? 2.1947 2.1026 2.4508 -0.1703 -0.0184 -0.1236 150 GLU A CD 1182 O OE1 . GLU A 151 ? 2.3036 2.1907 2.5634 -0.1769 -0.0021 -0.1227 150 GLU A OE1 1183 O OE2 . GLU A 151 ? 2.2037 2.1496 2.4816 -0.1662 -0.0316 -0.1188 150 GLU A OE2 1184 N N . MET A 152 ? 1.7918 1.6500 1.9581 -0.1082 -0.0083 -0.1083 151 MET A N 1185 C CA . MET A 152 ? 1.7502 1.5861 1.9052 -0.0909 0.0056 -0.0997 151 MET A CA 1186 C C . MET A 152 ? 1.7348 1.5388 1.8601 -0.0825 0.0144 -0.1047 151 MET A C 1187 O O . MET A 152 ? 1.6848 1.4552 1.7944 -0.0752 0.0282 -0.1032 151 MET A O 1188 C CB . MET A 152 ? 1.7332 1.5974 1.9037 -0.0740 0.0012 -0.0872 151 MET A CB 1189 C CG . MET A 152 ? 1.7365 1.6246 1.9325 -0.0793 -0.0031 -0.0810 151 MET A CG 1190 S SD . MET A 152 ? 1.6928 1.6158 1.9065 -0.0629 -0.0110 -0.0689 151 MET A SD 1191 C CE . MET A 152 ? 1.7209 1.6194 1.9220 -0.0441 0.0007 -0.0601 151 MET A CE 1192 N N . TYR A 153 ? 1.7419 1.5538 1.8576 -0.0827 0.0074 -0.1105 152 TYR A N 1193 C CA . TYR A 153 ? 1.8087 1.5897 1.8950 -0.0760 0.0169 -0.1168 152 TYR A CA 1194 C C . TYR A 153 ? 1.8469 1.5875 1.9127 -0.0899 0.0254 -0.1279 152 TYR A C 1195 O O . TYR A 153 ? 1.8392 1.5439 1.8841 -0.0806 0.0401 -0.1287 152 TYR A O 1196 C CB . TYR A 153 ? 1.8461 1.6403 1.9220 -0.0772 0.0082 -0.1220 152 TYR A CB 1197 C CG . TYR A 153 ? 1.8839 1.6441 1.9266 -0.0723 0.0190 -0.1303 152 TYR A CG 1198 C CD1 . TYR A 153 ? 1.9336 1.6643 1.9512 -0.0881 0.0191 -0.1444 152 TYR A CD1 1199 C CD2 . TYR A 153 ? 1.8816 1.6396 1.9189 -0.0521 0.0295 -0.1248 152 TYR A CD2 1200 C CE1 . TYR A 153 ? 1.9952 1.6916 1.9792 -0.0833 0.0302 -0.1524 152 TYR A CE1 1201 C CE2 . TYR A 153 ? 1.9269 1.6533 1.9344 -0.0467 0.0416 -0.1323 152 TYR A CE2 1202 C CZ . TYR A 153 ? 1.9828 1.6767 1.9616 -0.0620 0.0423 -0.1460 152 TYR A CZ 1203 O OH . TYR A 153 ? 2.0145 1.6736 1.9605 -0.0564 0.0555 -0.1540 152 TYR A OH 1204 N N . GLN A 154 ? 1.8905 1.6374 1.9639 -0.1121 0.0161 -0.1369 153 GLN A N 1205 C CA . GLN A 154 ? 1.9914 1.7024 2.0488 -0.1297 0.0229 -0.1497 153 GLN A CA 1206 C C . GLN A 154 ? 1.9513 1.6363 2.0113 -0.1290 0.0389 -0.1443 153 GLN A C 1207 O O . GLN A 154 ? 2.0063 1.6465 2.0414 -0.1297 0.0537 -0.1495 153 GLN A O 1208 C CB . GLN A 154 ? 2.0970 1.8285 2.1690 -0.1542 0.0065 -0.1613 153 GLN A CB 1209 C CG . GLN A 154 ? 2.2089 1.9558 2.2685 -0.1571 -0.0099 -0.1691 153 GLN A CG 1210 C CD . GLN A 154 ? 2.3585 2.0659 2.3761 -0.1543 -0.0022 -0.1789 153 GLN A CD 1211 O OE1 . GLN A 154 ? 2.4762 2.1425 2.4748 -0.1590 0.0119 -0.1858 153 GLN A OE1 1212 N NE2 . GLN A 154 ? 2.4190 2.1359 2.4199 -0.1463 -0.0102 -0.1795 153 GLN A NE2 1213 N N . LEU A 155 ? 1.8659 1.5758 1.9530 -0.1271 0.0370 -0.1338 154 LEU A N 1214 C CA . LEU A 155 ? 1.8691 1.5540 1.9564 -0.1261 0.0525 -0.1272 154 LEU A CA 1215 C C . LEU A 155 ? 1.8813 1.5350 1.9448 -0.1013 0.0663 -0.1177 154 LEU A C 1216 O O . LEU A 155 ? 1.9694 1.5780 2.0116 -0.1013 0.0825 -0.1188 154 LEU A O 1217 C CB . LEU A 155 ? 1.8114 1.5302 1.9303 -0.1278 0.0476 -0.1177 154 LEU A CB 1218 C CG . LEU A 155 ? 1.8100 1.5342 1.9506 -0.1532 0.0487 -0.1248 154 LEU A CG 1219 C CD1 . LEU A 155 ? 1.7311 1.5000 1.9063 -0.1541 0.0394 -0.1172 154 LEU A CD1 1220 C CD2 . LEU A 155 ? 1.8558 1.5332 1.9812 -0.1582 0.0706 -0.1240 154 LEU A CD2 1221 N N . TYR A 156 ? 1.8015 1.4789 1.8696 -0.0803 0.0600 -0.1089 155 TYR A N 1222 C CA . TYR A 156 ? 1.8048 1.4629 1.8591 -0.0546 0.0697 -0.0986 155 TYR A CA 1223 C C . TYR A 156 ? 1.8435 1.4847 1.8776 -0.0409 0.0746 -0.1029 155 TYR A C 1224 O O . TYR A 156 ? 1.8761 1.5036 1.9014 -0.0180 0.0820 -0.0955 155 TYR A O 1225 C CB . TYR A 156 ? 1.7427 1.4374 1.8192 -0.0397 0.0608 -0.0856 155 TYR A CB 1226 C CG . TYR A 156 ? 1.7212 1.4321 1.8168 -0.0541 0.0573 -0.0826 155 TYR A CG 1227 C CD1 . TYR A 156 ? 1.7292 1.4071 1.8148 -0.0617 0.0704 -0.0813 155 TYR A CD1 1228 C CD2 . TYR A 156 ? 1.7115 1.4681 1.8343 -0.0607 0.0428 -0.0813 155 TYR A CD2 1229 C CE1 . TYR A 156 ? 1.7185 1.4105 1.8228 -0.0754 0.0701 -0.0790 155 TYR A CE1 1230 C CE2 . TYR A 156 ? 1.6945 1.4658 1.8364 -0.0732 0.0412 -0.0790 155 TYR A CE2 1231 C CZ . TYR A 156 ? 1.7030 1.4429 1.8365 -0.0807 0.0553 -0.0780 155 TYR A CZ 1232 O OH . TYR A 156 ? 1.7248 1.4788 1.8784 -0.0931 0.0565 -0.0759 155 TYR A OH 1233 N N . GLY A 157 ? 1.8770 1.5186 1.9032 -0.0544 0.0705 -0.1152 156 GLY A N 1234 C CA . GLY A 157 ? 1.9661 1.5806 1.9664 -0.0456 0.0794 -0.1221 156 GLY A CA 1235 C C . GLY A 157 ? 1.9660 1.6046 1.9724 -0.0253 0.0771 -0.1171 156 GLY A C 1236 O O . GLY A 157 ? 2.0701 1.6850 2.0577 -0.0121 0.0884 -0.1200 156 GLY A O 1237 N N . GLY A 158 ? 1.9102 1.5949 1.9435 -0.0230 0.0641 -0.1100 157 GLY A N 1238 C CA . GLY A 158 ? 1.8745 1.5842 1.9182 -0.0051 0.0632 -0.1050 157 GLY A CA 1239 C C . GLY A 158 ? 1.8016 1.5587 1.8711 -0.0094 0.0483 -0.1003 157 GLY A C 1240 O O . GLY A 158 ? 1.7282 1.5023 1.8122 -0.0218 0.0383 -0.0980 157 GLY A O 1241 N N . PRO A 159 ? 1.7898 1.5672 1.8655 0.0007 0.0485 -0.0989 158 PRO A N 1242 C CA . PRO A 159 ? 1.7683 1.5868 1.8656 -0.0023 0.0365 -0.0944 158 PRO A CA 1243 C C . PRO A 159 ? 1.7475 1.5932 1.8733 0.0058 0.0299 -0.0834 158 PRO A C 1244 O O . PRO A 159 ? 1.7816 1.6176 1.9108 0.0200 0.0353 -0.0783 158 PRO A O 1245 C CB . PRO A 159 ? 1.7936 1.6175 1.8871 0.0085 0.0443 -0.0958 158 PRO A CB 1246 C CG . PRO A 159 ? 1.8118 1.6085 1.8951 0.0246 0.0596 -0.0970 158 PRO A CG 1247 C CD . PRO A 159 ? 1.8238 1.5840 1.8865 0.0163 0.0625 -0.1016 158 PRO A CD 1248 N N . VAL A 160 ? 1.7283 1.6057 1.8718 -0.0021 0.0178 -0.0799 159 VAL A N 1249 C CA . VAL A 160 ? 1.7168 1.6182 1.8844 0.0021 0.0104 -0.0708 159 VAL A CA 1250 C C . VAL A 160 ? 1.6867 1.6163 1.8748 0.0158 0.0089 -0.0649 159 VAL A C 1251 O O . VAL A 160 ? 1.7159 1.6555 1.9044 0.0171 0.0116 -0.0673 159 VAL A O 1252 C CB . VAL A 160 ? 1.7244 1.6439 1.9022 -0.0142 -0.0013 -0.0702 159 VAL A CB 1253 C CG1 . VAL A 160 ? 1.7462 1.6431 1.9097 -0.0305 -0.0010 -0.0778 159 VAL A CG1 1254 C CG2 . VAL A 160 ? 1.7386 1.6834 1.9229 -0.0186 -0.0090 -0.0705 159 VAL A CG2 1255 N N . VAL A 161 ? 1.6551 1.5961 1.8590 0.0253 0.0052 -0.0578 160 VAL A N 1256 C CA . VAL A 161 ? 1.6186 1.5899 1.8462 0.0355 0.0010 -0.0530 160 VAL A CA 1257 C C . VAL A 161 ? 1.5699 1.5639 1.8112 0.0259 -0.0099 -0.0489 160 VAL A C 1258 O O . VAL A 161 ? 1.5280 1.5163 1.7679 0.0222 -0.0138 -0.0458 160 VAL A O 1259 C CB . VAL A 161 ? 1.6563 1.6257 1.8916 0.0542 0.0017 -0.0485 160 VAL A CB 1260 C CG1 . VAL A 161 ? 1.6345 1.6380 1.8976 0.0633 -0.0036 -0.0458 160 VAL A CG1 1261 C CG2 . VAL A 161 ? 1.7333 1.6756 1.9533 0.0655 0.0132 -0.0520 160 VAL A CG2 1262 N N . LEU A 162 ? 1.5647 1.5819 1.8178 0.0220 -0.0130 -0.0487 161 LEU A N 1263 C CA . LEU A 162 ? 1.5610 1.6003 1.8284 0.0152 -0.0225 -0.0444 161 LEU A CA 1264 C C . LEU A 162 ? 1.4778 1.5365 1.7658 0.0262 -0.0259 -0.0401 161 LEU A C 1265 O O . LEU A 162 ? 1.4475 1.5159 1.7463 0.0352 -0.0218 -0.0414 161 LEU A O 1266 C CB . LEU A 162 ? 1.6363 1.6870 1.9028 0.0063 -0.0240 -0.0460 161 LEU A CB 1267 C CG . LEU A 162 ? 1.7132 1.7465 1.9574 -0.0043 -0.0233 -0.0516 161 LEU A CG 1268 C CD1 . LEU A 162 ? 1.7268 1.7708 1.9671 -0.0103 -0.0263 -0.0515 161 LEU A CD1 1269 C CD2 . LEU A 162 ? 1.7460 1.7716 1.9870 -0.0140 -0.0295 -0.0523 161 LEU A CD2 1270 N N . VAL A 163 ? 1.4173 1.4818 1.7113 0.0253 -0.0332 -0.0357 162 VAL A N 1271 C CA . VAL A 163 ? 1.3814 1.4641 1.6928 0.0340 -0.0390 -0.0326 162 VAL A CA 1272 C C . VAL A 163 ? 1.3925 1.4906 1.7123 0.0244 -0.0453 -0.0299 162 VAL A C 1273 O O . VAL A 163 ? 1.3879 1.4787 1.7009 0.0180 -0.0476 -0.0277 162 VAL A O 1274 C CB . VAL A 163 ? 1.3638 1.4327 1.6679 0.0445 -0.0416 -0.0296 162 VAL A CB 1275 C CG1 . VAL A 163 ? 1.3572 1.4452 1.6778 0.0547 -0.0499 -0.0279 162 VAL A CG1 1276 C CG2 . VAL A 163 ? 1.3746 1.4210 1.6650 0.0537 -0.0341 -0.0316 162 VAL A CG2 1277 N N . ALA A 164 ? 1.4401 1.5584 1.7754 0.0234 -0.0465 -0.0302 163 ALA A N 1278 C CA . ALA A 164 ? 1.4535 1.5841 1.7954 0.0150 -0.0511 -0.0275 163 ALA A CA 1279 C C . ALA A 164 ? 1.4204 1.5683 1.7800 0.0194 -0.0559 -0.0268 163 ALA A C 1280 O O . ALA A 164 ? 1.3895 1.5473 1.7620 0.0264 -0.0549 -0.0295 163 ALA A O 1281 C CB . ALA A 164 ? 1.4542 1.5876 1.7926 0.0071 -0.0473 -0.0286 163 ALA A CB 1282 N N . HIS A 165 ? 1.4031 1.5551 1.7646 0.0149 -0.0610 -0.0238 164 HIS A N 1283 C CA . HIS A 165 ? 1.3878 1.5531 1.7629 0.0173 -0.0663 -0.0240 164 HIS A CA 1284 C C . HIS A 165 ? 1.3546 1.5284 1.7358 0.0086 -0.0655 -0.0225 164 HIS A C 1285 O O . HIS A 165 ? 1.3047 1.4727 1.6774 0.0028 -0.0650 -0.0194 164 HIS A O 1286 C CB . HIS A 165 ? 1.3714 1.5283 1.7384 0.0219 -0.0724 -0.0219 164 HIS A CB 1287 C CG . HIS A 165 ? 1.3978 1.5655 1.7745 0.0239 -0.0793 -0.0231 164 HIS A CG 1288 N ND1 . HIS A 165 ? 1.3866 1.5529 1.7605 0.0186 -0.0811 -0.0209 164 HIS A ND1 1289 C CD2 . HIS A 165 ? 1.4089 1.5893 1.7992 0.0301 -0.0853 -0.0272 164 HIS A CD2 1290 C CE1 . HIS A 165 ? 1.3902 1.5650 1.7722 0.0210 -0.0876 -0.0239 164 HIS A CE1 1291 N NE2 . HIS A 165 ? 1.3944 1.5793 1.7876 0.0275 -0.0911 -0.0280 164 HIS A NE2 1292 N N . SER A 166 ? 1.3370 1.5244 1.7340 0.0081 -0.0653 -0.0249 165 SER A N 1293 C CA . SER A 166 ? 1.3980 1.5902 1.7999 0.0006 -0.0634 -0.0234 165 SER A CA 1294 C C . SER A 166 ? 1.3303 1.5149 1.7202 -0.0049 -0.0578 -0.0200 165 SER A C 1295 O O . SER A 166 ? 1.2901 1.4719 1.6754 -0.0048 -0.0520 -0.0213 165 SER A O 1296 C CB . SER A 166 ? 1.5209 1.7106 1.9204 0.0000 -0.0698 -0.0215 165 SER A CB 1297 O OG . SER A 166 ? 1.6936 1.8863 2.0986 -0.0059 -0.0677 -0.0206 165 SER A OG 1298 N N . MET A 167 ? 1.2885 1.4690 1.6719 -0.0087 -0.0600 -0.0157 166 MET A N 1299 C CA . MET A 167 ? 1.2792 1.4534 1.6505 -0.0125 -0.0579 -0.0123 166 MET A CA 1300 C C . MET A 167 ? 1.2514 1.4185 1.6104 -0.0123 -0.0586 -0.0133 166 MET A C 1301 O O . MET A 167 ? 1.1990 1.3605 1.5459 -0.0148 -0.0568 -0.0126 166 MET A O 1302 C CB . MET A 167 ? 1.3211 1.4939 1.6907 -0.0140 -0.0620 -0.0077 166 MET A CB 1303 C CG . MET A 167 ? 1.3573 1.5253 1.7156 -0.0160 -0.0620 -0.0035 166 MET A CG 1304 S SD . MET A 167 ? 1.4242 1.5926 1.7850 -0.0150 -0.0664 0.0019 166 MET A SD 1305 C CE . MET A 167 ? 1.4140 1.5863 1.7800 -0.0145 -0.0720 0.0007 166 MET A CE 1306 N N . GLY A 168 ? 1.2295 1.3941 1.5889 -0.0095 -0.0611 -0.0153 167 GLY A N 1307 C CA . GLY A 168 ? 1.2362 1.3913 1.5840 -0.0102 -0.0605 -0.0176 167 GLY A CA 1308 C C . GLY A 168 ? 1.2625 1.4134 1.6030 -0.0097 -0.0541 -0.0206 167 GLY A C 1309 O O . GLY A 168 ? 1.2970 1.4383 1.6228 -0.0126 -0.0535 -0.0224 167 GLY A O 1310 N N . ASN A 169 ? 1.2534 1.4115 1.6046 -0.0063 -0.0488 -0.0219 168 ASN A N 1311 C CA . ASN A 169 ? 1.2751 1.4298 1.6220 -0.0052 -0.0395 -0.0249 168 ASN A CA 1312 C C . ASN A 169 ? 1.2912 1.4390 1.6227 -0.0105 -0.0357 -0.0228 168 ASN A C 1313 O O . ASN A 169 ? 1.2608 1.3971 1.5754 -0.0110 -0.0301 -0.0250 168 ASN A O 1314 C CB . ASN A 169 ? 1.2634 1.4315 1.6319 -0.0010 -0.0343 -0.0274 168 ASN A CB 1315 C CG . ASN A 169 ? 1.2444 1.4172 1.6239 0.0070 -0.0391 -0.0298 168 ASN A CG 1316 O OD1 . ASN A 169 ? 1.1799 1.3457 1.5547 0.0126 -0.0355 -0.0325 168 ASN A OD1 1317 N ND2 . ASN A 169 ? 1.2153 1.3974 1.6068 0.0084 -0.0470 -0.0289 168 ASN A ND2 1318 N N . MET A 170 ? 1.3322 1.4843 1.6666 -0.0136 -0.0385 -0.0184 169 MET A N 1319 C CA . MET A 170 ? 1.4444 1.5874 1.7608 -0.0169 -0.0361 -0.0149 169 MET A CA 1320 C C . MET A 170 ? 1.4335 1.5674 1.7300 -0.0185 -0.0451 -0.0144 169 MET A C 1321 O O . MET A 170 ? 1.4222 1.5434 1.6958 -0.0195 -0.0431 -0.0146 169 MET A O 1322 C CB . MET A 170 ? 1.5774 1.7249 1.9015 -0.0185 -0.0373 -0.0099 169 MET A CB 1323 C CG . MET A 170 ? 1.7520 1.9064 2.0935 -0.0197 -0.0273 -0.0113 169 MET A CG 1324 S SD . MET A 170 ? 2.0562 2.1971 2.3828 -0.0232 -0.0119 -0.0086 169 MET A SD 1325 C CE . MET A 170 ? 1.9868 2.1223 2.3098 -0.0252 -0.0153 -0.0015 169 MET A CE 1326 N N . TYR A 171 ? 1.4084 1.5485 1.7135 -0.0190 -0.0548 -0.0142 170 TYR A N 1327 C CA . TYR A 171 ? 1.3712 1.5070 1.6651 -0.0220 -0.0640 -0.0157 170 TYR A CA 1328 C C . TYR A 171 ? 1.3166 1.4399 1.5946 -0.0232 -0.0607 -0.0217 170 TYR A C 1329 O O . TYR A 171 ? 1.3060 1.4196 1.5634 -0.0259 -0.0648 -0.0237 170 TYR A O 1330 C CB . TYR A 171 ? 1.3545 1.4991 1.6649 -0.0230 -0.0707 -0.0155 170 TYR A CB 1331 C CG . TYR A 171 ? 1.3639 1.5168 1.6804 -0.0238 -0.0790 -0.0110 170 TYR A CG 1332 C CD1 . TYR A 171 ? 1.3667 1.5254 1.6926 -0.0208 -0.0774 -0.0058 170 TYR A CD1 1333 C CD2 . TYR A 171 ? 1.3648 1.5202 1.6790 -0.0274 -0.0884 -0.0126 170 TYR A CD2 1334 C CE1 . TYR A 171 ? 1.3752 1.5402 1.7068 -0.0197 -0.0839 -0.0015 170 TYR A CE1 1335 C CE2 . TYR A 171 ? 1.3696 1.5354 1.6932 -0.0263 -0.0962 -0.0087 170 TYR A CE2 1336 C CZ . TYR A 171 ? 1.3739 1.5437 1.7055 -0.0217 -0.0934 -0.0026 170 TYR A CZ 1337 O OH . TYR A 171 ? 1.3885 1.5673 1.7294 -0.0190 -0.1002 0.0015 170 TYR A OH 1338 N N . THR A 172 ? 1.2760 1.3981 1.5620 -0.0204 -0.0539 -0.0250 171 THR A N 1339 C CA . THR A 172 ? 1.3001 1.4078 1.5712 -0.0205 -0.0493 -0.0309 171 THR A CA 1340 C C . THR A 172 ? 1.3182 1.4152 1.5712 -0.0191 -0.0395 -0.0325 171 THR A C 1341 O O . THR A 172 ? 1.3284 1.4094 1.5585 -0.0212 -0.0384 -0.0370 171 THR A O 1342 C CB . THR A 172 ? 1.2862 1.3927 1.5688 -0.0162 -0.0457 -0.0334 171 THR A CB 1343 O OG1 . THR A 172 ? 1.1878 1.2913 1.4713 -0.0207 -0.0528 -0.0344 171 THR A OG1 1344 C CG2 . THR A 172 ? 1.3386 1.4304 1.6088 -0.0125 -0.0359 -0.0387 171 THR A CG2 1345 N N . LEU A 173 ? 1.3134 1.4172 1.5751 -0.0164 -0.0315 -0.0291 172 LEU A N 1346 C CA . LEU A 173 ? 1.3839 1.4758 1.6272 -0.0159 -0.0196 -0.0297 172 LEU A CA 1347 C C . LEU A 173 ? 1.4416 1.5194 1.6540 -0.0196 -0.0260 -0.0279 172 LEU A C 1348 O O . LEU A 173 ? 1.4915 1.5505 1.6757 -0.0199 -0.0209 -0.0313 172 LEU A O 1349 C CB . LEU A 173 ? 1.3904 1.4931 1.6518 -0.0145 -0.0095 -0.0264 172 LEU A CB 1350 C CG . LEU A 173 ? 1.4292 1.5178 1.6711 -0.0152 0.0054 -0.0256 172 LEU A CG 1351 C CD1 . LEU A 173 ? 1.4636 1.5397 1.6936 -0.0122 0.0179 -0.0317 172 LEU A CD1 1352 C CD2 . LEU A 173 ? 1.4402 1.5404 1.7045 -0.0162 0.0159 -0.0229 172 LEU A CD2 1353 N N . TYR A 174 ? 1.4423 1.5283 1.6589 -0.0212 -0.0375 -0.0227 173 TYR A N 1354 C CA . TYR A 174 ? 1.4944 1.5702 1.6845 -0.0228 -0.0480 -0.0207 173 TYR A CA 1355 C C . TYR A 174 ? 1.5214 1.5876 1.6941 -0.0262 -0.0566 -0.0280 173 TYR A C 1356 O O . TYR A 174 ? 1.5454 1.5933 1.6852 -0.0268 -0.0577 -0.0305 173 TYR A O 1357 C CB . TYR A 174 ? 1.5155 1.6061 1.7214 -0.0226 -0.0606 -0.0149 173 TYR A CB 1358 C CG . TYR A 174 ? 1.5788 1.6653 1.7652 -0.0227 -0.0761 -0.0132 173 TYR A CG 1359 C CD1 . TYR A 174 ? 1.6254 1.6997 1.7875 -0.0188 -0.0762 -0.0070 173 TYR A CD1 1360 C CD2 . TYR A 174 ? 1.5816 1.6772 1.7755 -0.0263 -0.0910 -0.0177 173 TYR A CD2 1361 C CE1 . TYR A 174 ? 1.6359 1.7076 1.7803 -0.0167 -0.0930 -0.0052 173 TYR A CE1 1362 C CE2 . TYR A 174 ? 1.5963 1.6929 1.7776 -0.0259 -0.1074 -0.0171 173 TYR A CE2 1363 C CZ . TYR A 174 ? 1.6248 1.7100 1.7810 -0.0201 -0.1096 -0.0107 173 TYR A CZ 1364 O OH . TYR A 174 ? 1.6428 1.7296 1.7858 -0.0177 -0.1283 -0.0100 173 TYR A OH 1365 N N . PHE A 175 ? 1.5026 1.5786 1.6956 -0.0288 -0.0619 -0.0318 174 PHE A N 1366 C CA . PHE A 175 ? 1.5222 1.5887 1.7031 -0.0339 -0.0686 -0.0399 174 PHE A CA 1367 C C . PHE A 175 ? 1.5304 1.5740 1.6844 -0.0331 -0.0570 -0.0459 174 PHE A C 1368 O O . PHE A 175 ? 1.5318 1.5591 1.6562 -0.0365 -0.0626 -0.0511 174 PHE A O 1369 C CB . PHE A 175 ? 1.5234 1.6002 1.7310 -0.0362 -0.0700 -0.0419 174 PHE A CB 1370 C CG . PHE A 175 ? 1.5447 1.6080 1.7417 -0.0421 -0.0719 -0.0508 174 PHE A CG 1371 C CD1 . PHE A 175 ? 1.5489 1.6107 1.7360 -0.0500 -0.0857 -0.0559 174 PHE A CD1 1372 C CD2 . PHE A 175 ? 1.5547 1.6066 1.7526 -0.0396 -0.0603 -0.0543 174 PHE A CD2 1373 C CE1 . PHE A 175 ? 1.5862 1.6341 1.7642 -0.0575 -0.0869 -0.0653 174 PHE A CE1 1374 C CE2 . PHE A 175 ? 1.5912 1.6264 1.7774 -0.0454 -0.0605 -0.0625 174 PHE A CE2 1375 C CZ . PHE A 175 ? 1.6113 1.6439 1.7874 -0.0555 -0.0733 -0.0684 174 PHE A CZ 1376 N N . LEU A 176 ? 1.4993 1.5422 1.6642 -0.0280 -0.0414 -0.0457 175 LEU A N 1377 C CA . LEU A 176 ? 1.5167 1.5392 1.6613 -0.0254 -0.0272 -0.0514 175 LEU A CA 1378 C C . LEU A 176 ? 1.5183 1.5232 1.6293 -0.0246 -0.0205 -0.0509 175 LEU A C 1379 O O . LEU A 176 ? 1.4757 1.4573 1.5555 -0.0256 -0.0158 -0.0573 175 LEU A O 1380 C CB . LEU A 176 ? 1.5037 1.5349 1.6735 -0.0181 -0.0124 -0.0504 175 LEU A CB 1381 C CG . LEU A 176 ? 1.4889 1.5276 1.6818 -0.0160 -0.0152 -0.0520 175 LEU A CG 1382 C CD1 . LEU A 176 ? 1.4699 1.5235 1.6910 -0.0073 -0.0053 -0.0494 175 LEU A CD1 1383 C CD2 . LEU A 176 ? 1.5164 1.5324 1.6894 -0.0173 -0.0126 -0.0598 175 LEU A CD2 1384 N N . GLN A 177 ? 1.5525 1.5654 1.6673 -0.0228 -0.0187 -0.0433 176 GLN A N 1385 C CA . GLN A 177 ? 1.6702 1.6631 1.7496 -0.0217 -0.0114 -0.0410 176 GLN A CA 1386 C C . GLN A 177 ? 1.7313 1.7065 1.7718 -0.0251 -0.0271 -0.0443 176 GLN A C 1387 O O . GLN A 177 ? 1.7331 1.6825 1.7329 -0.0239 -0.0206 -0.0459 176 GLN A O 1388 C CB . GLN A 177 ? 1.6923 1.6953 1.7828 -0.0200 -0.0084 -0.0316 176 GLN A CB 1389 C CG . GLN A 177 ? 1.7153 1.7294 1.8347 -0.0175 0.0108 -0.0298 176 GLN A CG 1390 C CD . GLN A 177 ? 1.7668 1.7850 1.8919 -0.0176 0.0160 -0.0216 176 GLN A CD 1391 O OE1 . GLN A 177 ? 1.8063 1.8228 1.9198 -0.0181 0.0031 -0.0160 176 GLN A OE1 1392 N NE2 . GLN A 177 ? 1.8131 1.8370 1.9580 -0.0172 0.0353 -0.0211 176 GLN A NE2 1393 N N . ARG A 178 ? 1.7623 1.7515 1.8155 -0.0292 -0.0478 -0.0458 177 ARG A N 1394 C CA . ARG A 178 ? 1.8113 1.7906 1.8355 -0.0329 -0.0670 -0.0498 177 ARG A CA 1395 C C . ARG A 178 ? 1.7890 1.7546 1.7986 -0.0393 -0.0714 -0.0620 177 ARG A C 1396 O O . ARG A 178 ? 1.7802 1.7367 1.7645 -0.0436 -0.0880 -0.0677 177 ARG A O 1397 C CB . ARG A 178 ? 1.8352 1.8397 1.8848 -0.0343 -0.0869 -0.0453 177 ARG A CB 1398 C CG . ARG A 178 ? 1.8485 1.8622 1.9076 -0.0281 -0.0838 -0.0337 177 ARG A CG 1399 C CD . ARG A 178 ? 1.8432 1.8834 1.9346 -0.0284 -0.0998 -0.0295 177 ARG A CD 1400 N NE . ARG A 178 ? 1.8663 1.9063 1.9394 -0.0273 -0.1210 -0.0294 177 ARG A NE 1401 C CZ . ARG A 178 ? 1.8734 1.9040 1.9225 -0.0201 -0.1254 -0.0216 177 ARG A CZ 1402 N NH1 . ARG A 178 ? 1.8657 1.8845 1.9058 -0.0150 -0.1081 -0.0133 177 ARG A NH1 1403 N NH2 . ARG A 178 ? 1.9013 1.9338 1.9353 -0.0179 -0.1476 -0.0222 177 ARG A NH2 1404 N N . GLN A 179 ? 1.7391 1.7022 1.7636 -0.0395 -0.0574 -0.0664 178 GLN A N 1405 C CA . GLN A 179 ? 1.7436 1.6885 1.7520 -0.0453 -0.0582 -0.0779 178 GLN A CA 1406 C C . GLN A 179 ? 1.7907 1.7040 1.7601 -0.0415 -0.0408 -0.0824 178 GLN A C 1407 O O . GLN A 179 ? 1.7893 1.7012 1.7630 -0.0341 -0.0215 -0.0772 178 GLN A O 1408 C CB . GLN A 179 ? 1.7033 1.6588 1.7466 -0.0463 -0.0523 -0.0798 178 GLN A CB 1409 C CG . GLN A 179 ? 1.6602 1.6445 1.7417 -0.0496 -0.0654 -0.0751 178 GLN A CG 1410 C CD . GLN A 179 ? 1.6530 1.6443 1.7297 -0.0581 -0.0874 -0.0788 178 GLN A CD 1411 O OE1 . GLN A 179 ? 1.6634 1.6400 1.7210 -0.0661 -0.0948 -0.0891 178 GLN A OE1 1412 N NE2 . GLN A 179 ? 1.6198 1.6340 1.7151 -0.0563 -0.0984 -0.0710 178 GLN A NE2 1413 N N . PRO A 180 ? 1.8206 1.7082 1.7527 -0.0471 -0.0467 -0.0931 179 PRO A N 1414 C CA . PRO A 180 ? 1.8568 1.7107 1.7489 -0.0431 -0.0281 -0.0981 179 PRO A CA 1415 C C . PRO A 180 ? 1.8406 1.6912 1.7529 -0.0376 -0.0053 -0.0997 179 PRO A C 1416 O O . PRO A 180 ? 1.7715 1.6360 1.7167 -0.0394 -0.0079 -0.1009 179 PRO A O 1417 C CB . PRO A 180 ? 1.8992 1.7282 1.7514 -0.0519 -0.0426 -0.1109 179 PRO A CB 1418 C CG . PRO A 180 ? 1.8699 1.7217 1.7547 -0.0614 -0.0631 -0.1144 179 PRO A CG 1419 C CD . PRO A 180 ? 1.8273 1.7155 1.7540 -0.0578 -0.0694 -0.1019 179 PRO A CD 1420 N N . GLN A 181 ? 1.8900 1.7216 1.7823 -0.0302 0.0173 -0.0994 180 GLN A N 1421 C CA . GLN A 181 ? 1.8600 1.6909 1.7738 -0.0222 0.0400 -0.1003 180 GLN A CA 1422 C C . GLN A 181 ? 1.8196 1.6344 1.7301 -0.0249 0.0393 -0.1102 180 GLN A C 1423 O O . GLN A 181 ? 1.7251 1.5517 1.6693 -0.0197 0.0459 -0.1088 180 GLN A O 1424 C CB . GLN A 181 ? 1.9249 1.7338 1.8121 -0.0148 0.0655 -0.1005 180 GLN A CB 1425 C CG . GLN A 181 ? 1.9086 1.7278 1.8300 -0.0043 0.0894 -0.0989 180 GLN A CG 1426 C CD . GLN A 181 ? 1.8482 1.7073 1.8218 -0.0009 0.0885 -0.0889 180 GLN A CD 1427 O OE1 . GLN A 181 ? 1.8558 1.7254 1.8303 -0.0031 0.0863 -0.0818 180 GLN A OE1 1428 N NE2 . GLN A 181 ? 1.8089 1.6879 1.8238 0.0046 0.0898 -0.0884 180 GLN A NE2 1429 N N . ALA A 182 ? 1.8532 1.6392 1.7214 -0.0329 0.0308 -0.1204 181 ALA A N 1430 C CA . ALA A 182 ? 1.8749 1.6398 1.7347 -0.0377 0.0307 -0.1312 181 ALA A CA 1431 C C . ALA A 182 ? 1.8480 1.6367 1.7486 -0.0432 0.0167 -0.1293 181 ALA A C 1432 O O . ALA A 182 ? 1.8415 1.6210 1.7540 -0.0410 0.0252 -0.1326 181 ALA A O 1433 C CB . ALA A 182 ? 1.8985 1.6311 1.7063 -0.0480 0.0197 -0.1433 181 ALA A CB 1434 N N . TRP A 183 ? 1.8278 1.6445 1.7478 -0.0495 -0.0033 -0.1238 182 TRP A N 1435 C CA . TRP A 183 ? 1.7731 1.6130 1.7316 -0.0550 -0.0152 -0.1214 182 TRP A CA 1436 C C . TRP A 183 ? 1.7284 1.5867 1.7252 -0.0436 -0.0023 -0.1121 182 TRP A C 1437 O O . TRP A 183 ? 1.6937 1.5501 1.7079 -0.0434 0.0004 -0.1131 182 TRP A O 1438 C CB . TRP A 183 ? 1.7582 1.6254 1.7303 -0.0622 -0.0377 -0.1171 182 TRP A CB 1439 C CG . TRP A 183 ? 1.7441 1.6325 1.7530 -0.0693 -0.0486 -0.1160 182 TRP A CG 1440 C CD1 . TRP A 183 ? 1.7606 1.6444 1.7695 -0.0830 -0.0610 -0.1253 182 TRP A CD1 1441 C CD2 . TRP A 183 ? 1.7338 1.6499 1.7838 -0.0638 -0.0468 -0.1054 182 TRP A CD2 1442 N NE1 . TRP A 183 ? 1.7548 1.6611 1.8027 -0.0861 -0.0650 -0.1206 182 TRP A NE1 1443 C CE2 . TRP A 183 ? 1.7327 1.6579 1.8039 -0.0739 -0.0569 -0.1083 182 TRP A CE2 1444 C CE3 . TRP A 183 ? 1.7206 1.6542 1.7914 -0.0521 -0.0375 -0.0946 182 TRP A CE3 1445 C CZ2 . TRP A 183 ? 1.7036 1.6516 1.8115 -0.0714 -0.0569 -0.1000 182 TRP A CZ2 1446 C CZ3 . TRP A 183 ? 1.7029 1.6602 1.8104 -0.0500 -0.0400 -0.0873 182 TRP A CZ3 1447 C CH2 . TRP A 183 ? 1.6836 1.6466 1.8072 -0.0590 -0.0492 -0.0896 182 TRP A CH2 1448 N N . LYS A 184 ? 1.7541 1.6290 1.7627 -0.0343 0.0052 -0.1034 183 LYS A N 1449 C CA . LYS A 184 ? 1.7399 1.6360 1.7865 -0.0235 0.0149 -0.0953 183 LYS A CA 1450 C C . LYS A 184 ? 1.7015 1.5791 1.7471 -0.0140 0.0327 -0.0993 183 LYS A C 1451 O O . LYS A 184 ? 1.5973 1.4835 1.6690 -0.0078 0.0343 -0.0962 183 LYS A O 1452 C CB . LYS A 184 ? 1.7892 1.7034 1.8462 -0.0172 0.0216 -0.0874 183 LYS A CB 1453 C CG . LYS A 184 ? 1.8034 1.7389 1.8686 -0.0232 0.0053 -0.0808 183 LYS A CG 1454 C CD . LYS A 184 ? 1.8204 1.7701 1.8962 -0.0173 0.0148 -0.0731 183 LYS A CD 1455 C CE . LYS A 184 ? 1.8984 1.8240 1.9354 -0.0164 0.0268 -0.0754 183 LYS A CE 1456 N NZ . LYS A 184 ? 1.9418 1.8787 1.9869 -0.0131 0.0363 -0.0675 183 LYS A NZ 1457 N N . ASP A 185 ? 1.7351 1.5850 1.7479 -0.0116 0.0461 -0.1060 184 ASP A N 1458 C CA . ASP A 185 ? 1.7762 1.6051 1.7847 -0.0010 0.0650 -0.1104 184 ASP A CA 1459 C C . ASP A 185 ? 1.7963 1.6067 1.8015 -0.0046 0.0606 -0.1156 184 ASP A C 1460 O O . ASP A 185 ? 1.8421 1.6474 1.8616 0.0066 0.0710 -0.1144 184 ASP A O 1461 C CB . ASP A 185 ? 1.8529 1.6504 1.8199 0.0003 0.0805 -0.1178 184 ASP A CB 1462 C CG . ASP A 185 ? 1.8636 1.6744 1.8344 0.0064 0.0927 -0.1123 184 ASP A CG 1463 O OD1 . ASP A 185 ? 1.8449 1.6888 1.8475 0.0069 0.0861 -0.1034 184 ASP A OD1 1464 O OD2 . ASP A 185 ? 1.8472 1.6327 1.7876 0.0101 0.1103 -0.1172 184 ASP A OD2 1465 N N . LYS A 186 ? 1.8079 1.6081 1.7952 -0.0202 0.0453 -0.1214 185 LYS A N 1466 C CA . LYS A 186 ? 1.8365 1.6168 1.8199 -0.0269 0.0423 -0.1273 185 LYS A CA 1467 C C . LYS A 186 ? 1.7716 1.5756 1.7920 -0.0265 0.0340 -0.1192 185 LYS A C 1468 O O . LYS A 186 ? 1.7684 1.5591 1.7956 -0.0202 0.0418 -0.1184 185 LYS A O 1469 C CB . LYS A 186 ? 1.9045 1.6671 1.8584 -0.0456 0.0287 -0.1383 185 LYS A CB 1470 C CG . LYS A 186 ? 1.9665 1.7132 1.9225 -0.0568 0.0241 -0.1446 185 LYS A CG 1471 C CD . LYS A 186 ? 2.0617 1.7842 1.9848 -0.0747 0.0142 -0.1591 185 LYS A CD 1472 C CE . LYS A 186 ? 2.1210 1.8263 2.0492 -0.0874 0.0128 -0.1661 185 LYS A CE 1473 N NZ . LYS A 186 ? 2.2019 1.8780 2.0965 -0.1050 0.0059 -0.1829 185 LYS A NZ 1474 N N . TYR A 187 ? 1.7134 1.5493 1.7545 -0.0325 0.0190 -0.1130 186 TYR A N 1475 C CA . TYR A 187 ? 1.6979 1.5523 1.7676 -0.0364 0.0095 -0.1074 186 TYR A CA 1476 C C . TYR A 187 ? 1.7326 1.6131 1.8345 -0.0227 0.0121 -0.0959 186 TYR A C 1477 O O . TYR A 187 ? 1.7278 1.6148 1.8477 -0.0226 0.0086 -0.0913 186 TYR A O 1478 C CB . TYR A 187 ? 1.6927 1.5657 1.7675 -0.0516 -0.0090 -0.1085 186 TYR A CB 1479 C CG . TYR A 187 ? 1.7304 1.5814 1.7827 -0.0678 -0.0159 -0.1208 186 TYR A CG 1480 C CD1 . TYR A 187 ? 1.7454 1.5868 1.8062 -0.0777 -0.0170 -0.1247 186 TYR A CD1 1481 C CD2 . TYR A 187 ? 1.7846 1.6230 1.8058 -0.0737 -0.0211 -0.1290 186 TYR A CD2 1482 C CE1 . TYR A 187 ? 1.8203 1.6428 1.8639 -0.0946 -0.0234 -0.1375 186 TYR A CE1 1483 C CE2 . TYR A 187 ? 1.8327 1.6518 1.8334 -0.0894 -0.0297 -0.1419 186 TYR A CE2 1484 C CZ . TYR A 187 ? 1.8546 1.6672 1.8689 -0.1005 -0.0309 -0.1466 186 TYR A CZ 1485 O OH . TYR A 187 ? 1.9131 1.7078 1.9104 -0.1180 -0.0395 -0.1609 186 TYR A OH 1486 N N . ILE A 188 ? 1.7545 1.6488 1.8629 -0.0121 0.0185 -0.0918 187 ILE A N 1487 C CA . ILE A 188 ? 1.7531 1.6744 1.8935 -0.0002 0.0193 -0.0825 187 ILE A CA 1488 C C . ILE A 188 ? 1.7509 1.6640 1.8959 0.0165 0.0343 -0.0824 187 ILE A C 1489 O O . ILE A 188 ? 1.6948 1.5990 1.8281 0.0215 0.0464 -0.0862 187 ILE A O 1490 C CB . ILE A 188 ? 1.8071 1.7556 1.9596 -0.0012 0.0150 -0.0776 187 ILE A CB 1491 C CG1 . ILE A 188 ? 1.8231 1.7799 1.9704 -0.0155 -0.0004 -0.0775 187 ILE A CG1 1492 C CG2 . ILE A 188 ? 1.7966 1.7729 1.9833 0.0089 0.0146 -0.0697 187 ILE A CG2 1493 C CD1 . ILE A 188 ? 1.7874 1.7555 1.9534 -0.0208 -0.0115 -0.0741 187 ILE A CD1 1494 N N . ARG A 189 ? 1.8011 1.7166 1.9626 0.0260 0.0337 -0.0779 188 ARG A N 1495 C CA . ARG A 189 ? 1.8735 1.7859 2.0449 0.0449 0.0448 -0.0767 188 ARG A CA 1496 C C . ARG A 189 ? 1.8362 1.7848 2.0397 0.0537 0.0441 -0.0717 188 ARG A C 1497 O O . ARG A 189 ? 1.8566 1.8097 2.0679 0.0638 0.0560 -0.0737 188 ARG A O 1498 C CB . ARG A 189 ? 1.9267 1.8248 2.0990 0.0525 0.0426 -0.0733 188 ARG A CB 1499 C CG . ARG A 189 ? 1.9564 1.8650 2.1496 0.0742 0.0457 -0.0685 188 ARG A CG 1500 C CD . ARG A 189 ? 2.0177 1.9127 2.2064 0.0884 0.0614 -0.0730 188 ARG A CD 1501 N NE . ARG A 189 ? 2.0909 2.0002 2.3040 0.1105 0.0616 -0.0684 188 ARG A NE 1502 C CZ . ARG A 189 ? 2.1940 2.1006 2.4147 0.1277 0.0741 -0.0709 188 ARG A CZ 1503 N NH1 . ARG A 189 ? 2.2434 2.1302 2.4459 0.1253 0.0898 -0.0779 188 ARG A NH1 1504 N NH2 . ARG A 189 ? 2.2203 2.1441 2.4667 0.1483 0.0705 -0.0667 188 ARG A NH2 1505 N N . ALA A 190 ? 1.7846 1.7583 2.0077 0.0495 0.0311 -0.0658 189 ALA A N 1506 C CA . ALA A 190 ? 1.7446 1.7522 1.9989 0.0555 0.0289 -0.0620 189 ALA A CA 1507 C C . ALA A 190 ? 1.6628 1.6904 1.9275 0.0448 0.0152 -0.0572 189 ALA A C 1508 O O . ALA A 190 ? 1.6355 1.6534 1.8885 0.0360 0.0069 -0.0559 189 ALA A O 1509 C CB . ALA A 190 ? 1.7657 1.7826 2.0418 0.0737 0.0291 -0.0597 189 ALA A CB 1510 N N . PHE A 191 ? 1.5725 1.6275 1.8605 0.0454 0.0143 -0.0550 190 PHE A N 1511 C CA . PHE A 191 ? 1.5061 1.5803 1.8057 0.0371 0.0030 -0.0505 190 PHE A CA 1512 C C . PHE A 191 ? 1.4485 1.5485 1.7799 0.0467 -0.0008 -0.0483 190 PHE A C 1513 O O . PHE A 191 ? 1.4384 1.5542 1.7892 0.0516 0.0067 -0.0504 190 PHE A O 1514 C CB . PHE A 191 ? 1.5121 1.5899 1.8039 0.0265 0.0066 -0.0509 190 PHE A CB 1515 C CG . PHE A 191 ? 1.4844 1.5819 1.7897 0.0197 -0.0022 -0.0461 190 PHE A CG 1516 C CD1 . PHE A 191 ? 1.4761 1.5815 1.7906 0.0186 -0.0145 -0.0424 190 PHE A CD1 1517 C CD2 . PHE A 191 ? 1.4686 1.5728 1.7739 0.0143 0.0031 -0.0452 190 PHE A CD2 1518 C CE1 . PHE A 191 ? 1.4879 1.6089 1.8133 0.0129 -0.0212 -0.0385 190 PHE A CE1 1519 C CE2 . PHE A 191 ? 1.4558 1.5743 1.7712 0.0085 -0.0037 -0.0408 190 PHE A CE2 1520 C CZ . PHE A 191 ? 1.4806 1.6080 1.8068 0.0079 -0.0162 -0.0377 190 PHE A CZ 1521 N N . VAL A 192 ? 1.3945 1.4974 1.7304 0.0493 -0.0122 -0.0448 191 VAL A N 1522 C CA . VAL A 192 ? 1.3531 1.4783 1.7147 0.0580 -0.0198 -0.0432 191 VAL A CA 1523 C C . VAL A 192 ? 1.3580 1.4994 1.7286 0.0474 -0.0274 -0.0406 191 VAL A C 1524 O O . VAL A 192 ? 1.3329 1.4659 1.6905 0.0404 -0.0339 -0.0373 191 VAL A O 1525 C CB . VAL A 192 ? 1.3414 1.4544 1.6953 0.0684 -0.0276 -0.0406 191 VAL A CB 1526 C CG1 . VAL A 192 ? 1.3346 1.4702 1.7122 0.0784 -0.0381 -0.0398 191 VAL A CG1 1527 C CG2 . VAL A 192 ? 1.3684 1.4588 1.7084 0.0788 -0.0190 -0.0426 191 VAL A CG2 1528 N N . SER A 193 ? 1.3803 1.5444 1.7745 0.0463 -0.0252 -0.0423 192 SER A N 1529 C CA . SER A 193 ? 1.3688 1.5459 1.7712 0.0362 -0.0297 -0.0403 192 SER A CA 1530 C C . SER A 193 ? 1.3789 1.5753 1.8038 0.0413 -0.0405 -0.0408 192 SER A C 1531 O O . SER A 193 ? 1.4040 1.6184 1.8536 0.0484 -0.0398 -0.0449 192 SER A O 1532 C CB . SER A 193 ? 1.3441 1.5286 1.7539 0.0295 -0.0177 -0.0421 192 SER A CB 1533 O OG . SER A 193 ? 1.3149 1.5081 1.7304 0.0201 -0.0206 -0.0398 192 SER A OG 1534 N N . LEU A 194 ? 1.3709 1.5638 1.7875 0.0376 -0.0504 -0.0374 193 LEU A N 1535 C CA . LEU A 194 ? 1.4012 1.6072 1.8317 0.0423 -0.0621 -0.0383 193 LEU A CA 1536 C C . LEU A 194 ? 1.3855 1.6016 1.8243 0.0315 -0.0644 -0.0380 193 LEU A C 1537 O O . LEU A 194 ? 1.3778 1.5828 1.8007 0.0246 -0.0655 -0.0338 193 LEU A O 1538 C CB . LEU A 194 ? 1.4588 1.6471 1.8684 0.0486 -0.0703 -0.0347 193 LEU A CB 1539 C CG . LEU A 194 ? 1.5415 1.7115 1.9360 0.0583 -0.0666 -0.0339 193 LEU A CG 1540 C CD1 . LEU A 194 ? 1.5924 1.7411 1.9637 0.0626 -0.0723 -0.0295 193 LEU A CD1 1541 C CD2 . LEU A 194 ? 1.5601 1.7432 1.9735 0.0718 -0.0674 -0.0379 193 LEU A CD2 1542 N N . GLY A 195 ? 1.3936 1.6308 1.8589 0.0299 -0.0642 -0.0428 194 GLY A N 1543 C CA . GLY A 195 ? 1.3719 1.6169 1.8459 0.0197 -0.0656 -0.0434 194 GLY A CA 1544 C C . GLY A 195 ? 1.3529 1.5869 1.8138 0.0089 -0.0553 -0.0391 194 GLY A C 1545 O O . GLY A 195 ? 1.3705 1.5977 1.8217 0.0029 -0.0583 -0.0358 194 GLY A O 1546 N N . ALA A 196 ? 1.2919 1.5230 1.7509 0.0074 -0.0432 -0.0391 195 ALA A N 1547 C CA . ALA A 196 ? 1.2693 1.4869 1.7101 -0.0006 -0.0346 -0.0347 195 ALA A CA 1548 C C . ALA A 196 ? 1.2610 1.4844 1.7133 -0.0095 -0.0277 -0.0351 195 ALA A C 1549 O O . ALA A 196 ? 1.2583 1.4951 1.7332 -0.0111 -0.0196 -0.0400 195 ALA A O 1550 C CB . ALA A 196 ? 1.2827 1.4910 1.7120 0.0013 -0.0240 -0.0351 195 ALA A CB 1551 N N . PRO A 197 ? 1.2433 1.4562 1.6813 -0.0152 -0.0296 -0.0300 196 PRO A N 1552 C CA . PRO A 197 ? 1.2406 1.4532 1.6849 -0.0234 -0.0223 -0.0294 196 PRO A CA 1553 C C . PRO A 197 ? 1.2654 1.4648 1.6946 -0.0275 -0.0076 -0.0260 196 PRO A C 1554 O O . PRO A 197 ? 1.2418 1.4260 1.6515 -0.0307 -0.0058 -0.0200 196 PRO A O 1555 C CB . PRO A 197 ? 1.2390 1.4427 1.6705 -0.0247 -0.0313 -0.0247 196 PRO A CB 1556 C CG . PRO A 197 ? 1.2428 1.4370 1.6539 -0.0196 -0.0372 -0.0205 196 PRO A CG 1557 C CD . PRO A 197 ? 1.2407 1.4413 1.6576 -0.0137 -0.0384 -0.0247 196 PRO A CD 1558 N N . TRP A 198 ? 1.3264 1.5300 1.7630 -0.0262 0.0031 -0.0297 197 TRP A N 1559 C CA . TRP A 198 ? 1.4034 1.5911 1.8211 -0.0293 0.0189 -0.0269 197 TRP A CA 1560 C C . TRP A 198 ? 1.4597 1.6421 1.8813 -0.0381 0.0300 -0.0251 197 TRP A C 1561 O O . TRP A 198 ? 1.4554 1.6537 1.9077 -0.0431 0.0356 -0.0307 197 TRP A O 1562 C CB . TRP A 198 ? 1.3851 1.5791 1.8137 -0.0261 0.0313 -0.0322 197 TRP A CB 1563 C CG . TRP A 198 ? 1.3727 1.5713 1.8013 -0.0169 0.0225 -0.0350 197 TRP A CG 1564 C CD1 . TRP A 198 ? 1.4018 1.6199 1.8587 -0.0105 0.0204 -0.0412 197 TRP A CD1 1565 C CD2 . TRP A 198 ? 1.3708 1.5529 1.7695 -0.0128 0.0149 -0.0319 197 TRP A CD2 1566 N NE1 . TRP A 198 ? 1.4355 1.6467 1.8789 -0.0021 0.0133 -0.0412 197 TRP A NE1 1567 C CE2 . TRP A 198 ? 1.3997 1.5890 1.8083 -0.0046 0.0104 -0.0362 197 TRP A CE2 1568 C CE3 . TRP A 198 ? 1.3566 1.5190 1.7223 -0.0153 0.0108 -0.0265 197 TRP A CE3 1569 C CZ2 . TRP A 198 ? 1.3697 1.5447 1.7556 -0.0005 0.0040 -0.0354 197 TRP A CZ2 1570 C CZ3 . TRP A 198 ? 1.3379 1.4902 1.6845 -0.0117 0.0027 -0.0268 197 TRP A CZ3 1571 C CH2 . TRP A 198 ? 1.3529 1.5104 1.7093 -0.0053 0.0004 -0.0313 197 TRP A CH2 1572 N N . GLY A 199 ? 1.5073 1.6671 1.8982 -0.0399 0.0325 -0.0174 198 GLY A N 1573 C CA . GLY A 199 ? 1.5327 1.6803 1.9202 -0.0473 0.0441 -0.0141 198 GLY A CA 1574 C C . GLY A 199 ? 1.5180 1.6711 1.9188 -0.0505 0.0345 -0.0140 198 GLY A C 1575 O O . GLY A 199 ? 1.5382 1.6874 1.9490 -0.0585 0.0448 -0.0150 198 GLY A O 1576 N N . GLY A 200 ? 1.4998 1.6597 1.8997 -0.0448 0.0164 -0.0134 199 GLY A N 1577 C CA . GLY A 200 ? 1.4917 1.6510 1.8957 -0.0463 0.0076 -0.0122 199 GLY A CA 1578 C C . GLY A 200 ? 1.4608 1.6384 1.8965 -0.0511 0.0047 -0.0209 199 GLY A C 1579 O O . GLY A 200 ? 1.4197 1.6142 1.8792 -0.0532 0.0089 -0.0281 199 GLY A O 1580 N N . VAL A 201 ? 1.4599 1.6342 1.8960 -0.0524 -0.0029 -0.0206 200 VAL A N 1581 C CA . VAL A 201 ? 1.4771 1.6664 1.9385 -0.0567 -0.0092 -0.0295 200 VAL A CA 1582 C C . VAL A 201 ? 1.5060 1.6814 1.9648 -0.0639 -0.0056 -0.0295 200 VAL A C 1583 O O . VAL A 201 ? 1.4988 1.6542 1.9346 -0.0613 -0.0041 -0.0213 200 VAL A O 1584 C CB . VAL A 201 ? 1.4646 1.6648 1.9275 -0.0484 -0.0266 -0.0318 200 VAL A CB 1585 C CG1 . VAL A 201 ? 1.4701 1.6840 1.9397 -0.0419 -0.0293 -0.0339 200 VAL A CG1 1586 C CG2 . VAL A 201 ? 1.4577 1.6428 1.8960 -0.0426 -0.0329 -0.0239 200 VAL A CG2 1587 N N . ALA A 202 ? 1.5041 1.6908 1.9880 -0.0726 -0.0049 -0.0392 201 ALA A N 1588 C CA . ALA A 202 ? 1.4917 1.6637 1.9750 -0.0817 0.0004 -0.0412 201 ALA A CA 1589 C C . ALA A 202 ? 1.4665 1.6258 1.9316 -0.0763 -0.0106 -0.0384 201 ALA A C 1590 O O . ALA A 202 ? 1.4216 1.5585 1.8719 -0.0790 -0.0037 -0.0342 201 ALA A O 1591 C CB . ALA A 202 ? 1.5060 1.6964 2.0234 -0.0932 0.0008 -0.0547 201 ALA A CB 1592 N N . LYS A 203 ? 1.4775 1.6486 1.9422 -0.0679 -0.0261 -0.0402 202 LYS A N 1593 C CA . LYS A 203 ? 1.4901 1.6496 1.9390 -0.0630 -0.0351 -0.0388 202 LYS A CA 1594 C C . LYS A 203 ? 1.4368 1.5747 1.8611 -0.0572 -0.0296 -0.0272 202 LYS A C 1595 O O . LYS A 203 ? 1.4179 1.5414 1.8308 -0.0553 -0.0310 -0.0260 202 LYS A O 1596 C CB . LYS A 203 ? 1.5507 1.7235 1.9996 -0.0542 -0.0503 -0.0414 202 LYS A CB 1597 C CG . LYS A 203 ? 1.6257 1.8020 2.0649 -0.0447 -0.0520 -0.0336 202 LYS A CG 1598 C CD . LYS A 203 ? 1.7165 1.8891 2.1418 -0.0360 -0.0619 -0.0314 202 LYS A CD 1599 C CE . LYS A 203 ? 1.7926 1.9647 2.2076 -0.0290 -0.0614 -0.0234 202 LYS A CE 1600 N NZ . LYS A 203 ? 1.8095 1.9757 2.2119 -0.0221 -0.0673 -0.0208 202 LYS A NZ 1601 N N . THR A 204 ? 1.3727 1.5087 1.7888 -0.0535 -0.0239 -0.0192 203 THR A N 1602 C CA . THR A 204 ? 1.3457 1.4645 1.7404 -0.0469 -0.0204 -0.0082 203 THR A CA 1603 C C . THR A 204 ? 1.3345 1.4299 1.7193 -0.0501 -0.0114 -0.0055 203 THR A C 1604 O O . THR A 204 ? 1.2965 1.3792 1.6679 -0.0429 -0.0129 0.0006 203 THR A O 1605 C CB . THR A 204 ? 1.3818 1.4991 1.7679 -0.0453 -0.0142 -0.0021 203 THR A CB 1606 O OG1 . THR A 204 ? 1.3717 1.5084 1.7684 -0.0442 -0.0194 -0.0063 203 THR A OG1 1607 C CG2 . THR A 204 ? 1.4233 1.5291 1.7886 -0.0360 -0.0168 0.0082 203 THR A CG2 1608 N N . LEU A 205 ? 1.3255 1.4152 1.7187 -0.0610 -0.0010 -0.0105 204 LEU A N 1609 C CA . LEU A 205 ? 1.3709 1.4342 1.7533 -0.0655 0.0102 -0.0081 204 LEU A CA 1610 C C . LEU A 205 ? 1.3549 1.4105 1.7357 -0.0647 0.0043 -0.0124 204 LEU A C 1611 O O . LEU A 205 ? 1.3452 1.3780 1.7089 -0.0596 0.0090 -0.0060 204 LEU A O 1612 C CB . LEU A 205 ? 1.4306 1.4905 1.8263 -0.0801 0.0240 -0.0146 204 LEU A CB 1613 C CG . LEU A 205 ? 1.4740 1.5277 1.8627 -0.0817 0.0376 -0.0084 204 LEU A CG 1614 C CD1 . LEU A 205 ? 1.5169 1.5402 1.8725 -0.0729 0.0446 0.0054 204 LEU A CD1 1615 C CD2 . LEU A 205 ? 1.4565 1.5349 1.8536 -0.0770 0.0307 -0.0089 204 LEU A CD2 1616 N N . ARG A 206 ? 1.3442 1.4172 1.7409 -0.0689 -0.0056 -0.0234 205 ARG A N 1617 C CA . ARG A 206 ? 1.3848 1.4487 1.7764 -0.0686 -0.0113 -0.0289 205 ARG A CA 1618 C C . ARG A 206 ? 1.4031 1.4619 1.7787 -0.0545 -0.0165 -0.0205 205 ARG A C 1619 O O . ARG A 206 ? 1.3925 1.4313 1.7549 -0.0509 -0.0130 -0.0186 205 ARG A O 1620 C CB . ARG A 206 ? 1.3940 1.4783 1.8025 -0.0739 -0.0238 -0.0420 205 ARG A CB 1621 C CG . ARG A 206 ? 1.4349 1.5060 1.8348 -0.0759 -0.0292 -0.0500 205 ARG A CG 1622 C CD . ARG A 206 ? 1.4235 1.5096 1.8232 -0.0700 -0.0453 -0.0558 205 ARG A CD 1623 N NE . ARG A 206 ? 1.4504 1.5164 1.8301 -0.0669 -0.0480 -0.0588 205 ARG A NE 1624 C CZ . ARG A 206 ? 1.4760 1.5442 1.8446 -0.0595 -0.0590 -0.0615 205 ARG A CZ 1625 N NH1 . ARG A 206 ? 1.4292 1.5188 1.8049 -0.0541 -0.0693 -0.0613 205 ARG A NH1 1626 N NH2 . ARG A 206 ? 1.5294 1.5752 1.8768 -0.0570 -0.0585 -0.0641 205 ARG A NH2 1627 N N . VAL A 207 ? 1.4342 1.5111 1.8123 -0.0470 -0.0238 -0.0162 206 VAL A N 1628 C CA . VAL A 207 ? 1.4538 1.5303 1.8222 -0.0350 -0.0282 -0.0091 206 VAL A CA 1629 C C . VAL A 207 ? 1.4584 1.5163 1.8141 -0.0284 -0.0202 0.0010 206 VAL A C 1630 O O . VAL A 207 ? 1.4457 1.4922 1.7939 -0.0217 -0.0189 0.0034 206 VAL A O 1631 C CB . VAL A 207 ? 1.4600 1.5571 1.8338 -0.0302 -0.0353 -0.0060 206 VAL A CB 1632 C CG1 . VAL A 207 ? 1.4577 1.5552 1.8251 -0.0196 -0.0379 0.0014 206 VAL A CG1 1633 C CG2 . VAL A 207 ? 1.4708 1.5839 1.8545 -0.0331 -0.0440 -0.0150 206 VAL A CG2 1634 N N . LEU A 208 ? 1.4459 1.4993 1.7980 -0.0294 -0.0143 0.0069 207 LEU A N 1635 C CA . LEU A 208 ? 1.5057 1.5408 1.8432 -0.0210 -0.0083 0.0177 207 LEU A CA 1636 C C . LEU A 208 ? 1.5072 1.5147 1.8351 -0.0229 0.0016 0.0172 207 LEU A C 1637 O O . LEU A 208 ? 1.5183 1.5115 1.8363 -0.0123 0.0038 0.0242 207 LEU A O 1638 C CB . LEU A 208 ? 1.5737 1.6060 1.9037 -0.0219 -0.0039 0.0237 207 LEU A CB 1639 C CG . LEU A 208 ? 1.6226 1.6771 1.9567 -0.0184 -0.0131 0.0253 207 LEU A CG 1640 C CD1 . LEU A 208 ? 1.6455 1.6964 1.9729 -0.0237 -0.0064 0.0269 207 LEU A CD1 1641 C CD2 . LEU A 208 ? 1.6575 1.7155 1.9855 -0.0053 -0.0211 0.0337 207 LEU A CD2 1642 N N . ALA A 209 ? 1.4773 1.4776 1.8100 -0.0362 0.0076 0.0084 208 ALA A N 1643 C CA . ALA A 209 ? 1.5144 1.4854 1.8373 -0.0407 0.0184 0.0064 208 ALA A CA 1644 C C . ALA A 209 ? 1.5273 1.4919 1.8472 -0.0365 0.0148 0.0017 208 ALA A C 1645 O O . ALA A 209 ? 1.5422 1.4851 1.8486 -0.0274 0.0209 0.0078 208 ALA A O 1646 C CB . ALA A 209 ? 1.5342 1.5022 1.8671 -0.0583 0.0255 -0.0036 208 ALA A CB 1647 N N . SER A 210 ? 1.5022 1.4841 1.8326 -0.0420 0.0053 -0.0088 209 SER A N 1648 C CA . SER A 210 ? 1.5535 1.5246 1.8766 -0.0407 0.0032 -0.0157 209 SER A CA 1649 C C . SER A 210 ? 1.5149 1.5045 1.8400 -0.0330 -0.0076 -0.0168 209 SER A C 1650 O O . SER A 210 ? 1.5404 1.5200 1.8563 -0.0320 -0.0091 -0.0231 209 SER A O 1651 C CB . SER A 210 ? 1.6150 1.5794 1.9420 -0.0565 0.0029 -0.0301 209 SER A CB 1652 O OG . SER A 210 ? 1.6370 1.6290 1.9795 -0.0624 -0.0097 -0.0388 209 SER A OG 1653 N N . GLY A 211 ? 1.4536 1.4668 1.7881 -0.0279 -0.0140 -0.0112 210 GLY A N 1654 C CA . GLY A 211 ? 1.4365 1.4654 1.7727 -0.0217 -0.0225 -0.0119 210 GLY A CA 1655 C C . GLY A 211 ? 1.4707 1.5126 1.8121 -0.0291 -0.0324 -0.0226 210 GLY A C 1656 O O . GLY A 211 ? 1.5050 1.5432 1.8496 -0.0393 -0.0336 -0.0317 210 GLY A O 1657 N N . ASP A 212 ? 1.4636 1.5205 1.8065 -0.0237 -0.0399 -0.0217 211 ASP A N 1658 C CA . ASP A 212 ? 1.4789 1.5490 1.8257 -0.0275 -0.0508 -0.0302 211 ASP A CA 1659 C C . ASP A 212 ? 1.4651 1.5331 1.7993 -0.0192 -0.0546 -0.0295 211 ASP A C 1660 O O . ASP A 212 ? 1.4714 1.5486 1.8085 -0.0132 -0.0539 -0.0225 211 ASP A O 1661 C CB . ASP A 212 ? 1.5249 1.6170 1.8884 -0.0298 -0.0543 -0.0284 211 ASP A CB 1662 C CG . ASP A 212 ? 1.5868 1.6939 1.9592 -0.0336 -0.0652 -0.0378 211 ASP A CG 1663 O OD1 . ASP A 212 ? 1.6453 1.7523 2.0081 -0.0285 -0.0733 -0.0408 211 ASP A OD1 1664 O OD2 . ASP A 212 ? 1.6057 1.7246 1.9947 -0.0411 -0.0652 -0.0419 211 ASP A OD2 1665 N N . ASN A 213 ? 1.5099 1.5637 1.8284 -0.0196 -0.0581 -0.0370 212 ASN A N 1666 C CA . ASN A 213 ? 1.6062 1.6511 1.9067 -0.0116 -0.0589 -0.0361 212 ASN A CA 1667 C C . ASN A 213 ? 1.7049 1.7540 1.9967 -0.0111 -0.0724 -0.0436 212 ASN A C 1668 O O . ASN A 213 ? 1.6739 1.7078 1.9426 -0.0054 -0.0735 -0.0451 212 ASN A O 1669 C CB . ASN A 213 ? 1.6235 1.6421 1.9047 -0.0088 -0.0497 -0.0370 212 ASN A CB 1670 C CG . ASN A 213 ? 1.6400 1.6431 1.9086 -0.0158 -0.0549 -0.0488 212 ASN A CG 1671 O OD1 . ASN A 213 ? 1.6437 1.6581 1.9254 -0.0245 -0.0633 -0.0557 212 ASN A OD1 1672 N ND2 . ASN A 213 ? 1.6678 1.6449 1.9118 -0.0125 -0.0494 -0.0520 212 ASN A ND2 1673 N N . ASN A 214 ? 1.8218 1.8909 2.1314 -0.0160 -0.0819 -0.0478 213 ASN A N 1674 C CA . ASN A 214 ? 1.9108 1.9878 2.2167 -0.0142 -0.0971 -0.0552 213 ASN A CA 1675 C C . ASN A 214 ? 1.9371 2.0061 2.2225 -0.0036 -0.0989 -0.0506 213 ASN A C 1676 O O . ASN A 214 ? 1.9866 2.0469 2.2526 0.0008 -0.1096 -0.0562 213 ASN A O 1677 C CB . ASN A 214 ? 1.9423 2.0463 2.2761 -0.0180 -0.1032 -0.0570 213 ASN A CB 1678 C CG . ASN A 214 ? 1.9811 2.0933 2.3347 -0.0297 -0.1042 -0.0653 213 ASN A CG 1679 O OD1 . ASN A 214 ? 1.9647 2.0615 2.3099 -0.0354 -0.1024 -0.0709 213 ASN A OD1 1680 N ND2 . ASN A 214 ? 2.0179 2.1529 2.3977 -0.0337 -0.1054 -0.0664 213 ASN A ND2 1681 N N . ARG A 215 ? 1.9255 1.9966 2.2144 0.0001 -0.0888 -0.0406 214 ARG A N 1682 C CA . ARG A 215 ? 1.9014 1.9641 2.1734 0.0084 -0.0873 -0.0357 214 ARG A CA 1683 C C . ARG A 215 ? 1.8287 1.8666 2.0773 0.0122 -0.0761 -0.0331 214 ARG A C 1684 O O . ARG A 215 ? 1.8194 1.8408 2.0437 0.0187 -0.0749 -0.0318 214 ARG A O 1685 C CB . ARG A 215 ? 1.9263 2.0040 2.2157 0.0090 -0.0817 -0.0278 214 ARG A CB 1686 C CG . ARG A 215 ? 1.9774 2.0783 2.2909 0.0048 -0.0884 -0.0297 214 ARG A CG 1687 C CD . ARG A 215 ? 2.0458 2.1533 2.3573 0.0101 -0.0983 -0.0317 214 ARG A CD 1688 N NE . ARG A 215 ? 2.1224 2.2511 2.4570 0.0063 -0.1055 -0.0367 214 ARG A NE 1689 C CZ . ARG A 215 ? 2.1128 2.2530 2.4541 0.0110 -0.1135 -0.0387 214 ARG A CZ 1690 N NH1 . ARG A 215 ? 2.0832 2.2133 2.4070 0.0201 -0.1159 -0.0356 214 ARG A NH1 1691 N NH2 . ARG A 215 ? 2.1274 2.2882 2.4934 0.0069 -0.1175 -0.0438 214 ARG A NH2 1692 N N . ILE A 216 ? 1.7559 1.7888 2.0103 0.0088 -0.0667 -0.0321 215 ILE A N 1693 C CA . ILE A 216 ? 1.7858 1.7987 2.0250 0.0130 -0.0526 -0.0284 215 ILE A CA 1694 C C . ILE A 216 ? 1.7982 1.7920 2.0223 0.0106 -0.0519 -0.0354 215 ILE A C 1695 O O . ILE A 216 ? 1.8935 1.8825 2.1251 0.0096 -0.0416 -0.0331 215 ILE A O 1696 C CB . ILE A 216 ? 1.8144 1.8392 2.0766 0.0133 -0.0405 -0.0196 215 ILE A CB 1697 C CG1 . ILE A 216 ? 1.8601 1.9098 2.1450 0.0110 -0.0462 -0.0157 215 ILE A CG1 1698 C CG2 . ILE A 216 ? 1.8498 1.8615 2.1021 0.0192 -0.0261 -0.0147 215 ILE A CG2 1699 C CD1 . ILE A 216 ? 1.8711 1.9344 2.1783 0.0110 -0.0384 -0.0084 215 ILE A CD1 1700 N N . PRO A 217 ? 1.7544 1.7361 1.9561 0.0103 -0.0636 -0.0444 216 PRO A N 1701 C CA . PRO A 217 ? 1.7679 1.7315 1.9549 0.0059 -0.0658 -0.0538 216 PRO A CA 1702 C C . PRO A 217 ? 1.7846 1.7184 1.9477 0.0104 -0.0497 -0.0524 216 PRO A C 1703 O O . PRO A 217 ? 1.7800 1.6980 1.9353 0.0064 -0.0469 -0.0585 216 PRO A O 1704 C CB . PRO A 217 ? 1.8061 1.7648 1.9722 0.0067 -0.0842 -0.0633 216 PRO A CB 1705 C CG . PRO A 217 ? 1.8150 1.7704 1.9662 0.0162 -0.0833 -0.0565 216 PRO A CG 1706 C CD . PRO A 217 ? 1.7756 1.7544 1.9586 0.0157 -0.0746 -0.0463 216 PRO A CD 1707 N N . VAL A 218 ? 1.8008 1.7262 1.9530 0.0183 -0.0378 -0.0448 217 VAL A N 1708 C CA . VAL A 218 ? 1.8662 1.7661 2.0006 0.0236 -0.0190 -0.0425 217 VAL A CA 1709 C C . VAL A 218 ? 1.8489 1.7569 2.0103 0.0230 -0.0062 -0.0371 217 VAL A C 1710 O O . VAL A 218 ? 1.8216 1.7081 1.9712 0.0269 0.0082 -0.0372 217 VAL A O 1711 C CB . VAL A 218 ? 1.9374 1.8288 2.0585 0.0312 -0.0071 -0.0355 217 VAL A CB 1712 C CG1 . VAL A 218 ? 1.9227 1.8425 2.0807 0.0314 -0.0005 -0.0255 217 VAL A CG1 1713 C CG2 . VAL A 218 ? 1.9903 1.8494 2.0844 0.0370 0.0121 -0.0357 217 VAL A CG2 1714 N N . ILE A 219 ? 1.8583 1.7952 2.0537 0.0194 -0.0111 -0.0322 218 ILE A N 1715 C CA . ILE A 219 ? 1.9068 1.8505 2.1252 0.0204 -0.0015 -0.0265 218 ILE A CA 1716 C C . ILE A 219 ? 1.8820 1.8283 2.1096 0.0126 -0.0088 -0.0307 218 ILE A C 1717 O O . ILE A 219 ? 1.8323 1.7930 2.0677 0.0054 -0.0223 -0.0349 218 ILE A O 1718 C CB . ILE A 219 ? 1.9205 1.8904 2.1682 0.0240 0.0026 -0.0162 218 ILE A CB 1719 C CG1 . ILE A 219 ? 2.0038 1.9789 2.2718 0.0272 0.0103 -0.0103 218 ILE A CG1 1720 C CG2 . ILE A 219 ? 1.8955 1.8900 2.1579 0.0187 -0.0115 -0.0156 218 ILE A CG2 1721 C CD1 . ILE A 219 ? 2.0202 2.0156 2.3134 0.0334 0.0169 -0.0013 218 ILE A CD1 1722 N N . GLY A 220 ? 1.8629 1.7939 2.0902 0.0146 0.0020 -0.0295 219 GLY A N 1723 C CA . GLY A 220 ? 1.8738 1.8011 2.1078 0.0075 -0.0003 -0.0324 219 GLY A CA 1724 C C . GLY A 220 ? 1.8213 1.7753 2.0825 0.0043 -0.0059 -0.0260 219 GLY A C 1725 O O . GLY A 220 ? 1.7993 1.7707 2.0768 0.0110 -0.0032 -0.0165 219 GLY A O 1726 N N . PRO A 221 ? 1.7528 1.7098 2.0192 -0.0062 -0.0133 -0.0317 220 PRO A N 1727 C CA . PRO A 221 ? 1.6835 1.6635 1.9718 -0.0096 -0.0176 -0.0264 220 PRO A CA 1728 C C . PRO A 221 ? 1.6670 1.6451 1.9640 -0.0031 -0.0081 -0.0154 220 PRO A C 1729 O O . PRO A 221 ? 1.6268 1.6248 1.9382 -0.0002 -0.0109 -0.0079 220 PRO A O 1730 C CB . PRO A 221 ? 1.6860 1.6642 1.9771 -0.0230 -0.0234 -0.0362 220 PRO A CB 1731 C CG . PRO A 221 ? 1.7385 1.6970 2.0099 -0.0269 -0.0264 -0.0479 220 PRO A CG 1732 C CD . PRO A 221 ? 1.7784 1.7159 2.0315 -0.0161 -0.0158 -0.0437 220 PRO A CD 1733 N N . LEU A 222 ? 1.6721 1.6248 1.9582 0.0000 0.0024 -0.0147 221 LEU A N 1734 C CA . LEU A 222 ? 1.6899 1.6373 1.9815 0.0082 0.0107 -0.0040 221 LEU A CA 1735 C C . LEU A 222 ? 1.6647 1.6272 1.9671 0.0219 0.0125 0.0053 221 LEU A C 1736 O O . LEU A 222 ? 1.6575 1.6288 1.9705 0.0293 0.0129 0.0149 221 LEU A O 1737 C CB . LEU A 222 ? 1.7465 1.6593 2.0221 0.0090 0.0225 -0.0060 221 LEU A CB 1738 C CG . LEU A 222 ? 1.7492 1.6449 2.0163 -0.0063 0.0224 -0.0163 221 LEU A CG 1739 C CD1 . LEU A 222 ? 1.7854 1.6427 2.0342 -0.0051 0.0355 -0.0186 221 LEU A CD1 1740 C CD2 . LEU A 222 ? 1.6978 1.6053 1.9773 -0.0140 0.0198 -0.0129 221 LEU A CD2 1741 N N . LYS A 223 ? 1.6496 1.6149 1.9490 0.0252 0.0135 0.0022 222 LYS A N 1742 C CA . LYS A 223 ? 1.6143 1.5962 1.9281 0.0359 0.0165 0.0095 222 LYS A CA 1743 C C . LYS A 223 ? 1.5195 1.5318 1.8502 0.0330 0.0056 0.0126 222 LYS A C 1744 O O . LYS A 223 ? 1.4704 1.4995 1.8180 0.0394 0.0039 0.0204 222 LYS A O 1745 C CB . LYS A 223 ? 1.6558 1.6275 1.9587 0.0391 0.0240 0.0050 222 LYS A CB 1746 C CG . LYS A 223 ? 1.7131 1.6906 2.0302 0.0519 0.0352 0.0119 222 LYS A CG 1747 C CD . LYS A 223 ? 1.8555 1.8103 2.1674 0.0610 0.0469 0.0145 222 LYS A CD 1748 C CE . LYS A 223 ? 1.9081 1.8765 2.2435 0.0755 0.0556 0.0228 222 LYS A CE 1749 N NZ . LYS A 223 ? 1.9506 1.8975 2.2822 0.0867 0.0658 0.0267 222 LYS A NZ 1750 N N . ILE A 224 ? 1.4813 1.4999 1.8069 0.0239 -0.0025 0.0061 223 ILE A N 1751 C CA . ILE A 224 ? 1.4610 1.5048 1.7996 0.0207 -0.0120 0.0080 223 ILE A CA 1752 C C . ILE A 224 ? 1.4540 1.5078 1.8017 0.0184 -0.0173 0.0125 223 ILE A C 1753 O O . ILE A 224 ? 1.4231 1.4964 1.7827 0.0193 -0.0229 0.0166 223 ILE A O 1754 C CB . ILE A 224 ? 1.4777 1.5233 1.8070 0.0132 -0.0195 0.0001 223 ILE A CB 1755 C CG1 . ILE A 224 ? 1.4755 1.5433 1.8163 0.0121 -0.0264 0.0024 223 ILE A CG1 1756 C CG2 . ILE A 224 ? 1.4810 1.5202 1.8043 0.0043 -0.0251 -0.0066 223 ILE A CG2 1757 C CD1 . ILE A 224 ? 1.4815 1.5568 1.8305 0.0181 -0.0209 0.0070 223 ILE A CD1 1758 N N . ARG A 225 ? 1.4824 1.5200 1.8219 0.0149 -0.0144 0.0112 224 ARG A N 1759 C CA . ARG A 225 ? 1.4983 1.5385 1.8408 0.0127 -0.0162 0.0158 224 ARG A CA 1760 C C . ARG A 225 ? 1.4858 1.5362 1.8368 0.0232 -0.0173 0.0260 224 ARG A C 1761 O O . ARG A 225 ? 1.4449 1.5063 1.7991 0.0223 -0.0229 0.0298 224 ARG A O 1762 C CB . ARG A 225 ? 1.5503 1.5649 1.8810 0.0088 -0.0085 0.0140 224 ARG A CB 1763 C CG . ARG A 225 ? 1.5822 1.5933 1.9115 0.0056 -0.0072 0.0187 224 ARG A CG 1764 C CD . ARG A 225 ? 1.6251 1.6071 1.9422 0.0004 0.0028 0.0165 224 ARG A CD 1765 N NE . ARG A 225 ? 1.6513 1.6121 1.9592 0.0116 0.0109 0.0218 224 ARG A NE 1766 C CZ . ARG A 225 ? 1.7247 1.6547 2.0191 0.0100 0.0215 0.0215 224 ARG A CZ 1767 N NH1 . ARG A 225 ? 1.7292 1.6466 2.0191 -0.0039 0.0258 0.0154 224 ARG A NH1 1768 N NH2 . ARG A 225 ? 1.8094 1.7207 2.0960 0.0225 0.0291 0.0268 224 ARG A NH2 1769 N N . GLU A 226 ? 1.5226 1.5693 1.8773 0.0337 -0.0121 0.0298 225 GLU A N 1770 C CA . GLU A 226 ? 1.5616 1.6208 1.9285 0.0453 -0.0146 0.0387 225 GLU A CA 1771 C C . GLU A 226 ? 1.4835 1.5707 1.8644 0.0431 -0.0250 0.0392 225 GLU A C 1772 O O . GLU A 226 ? 1.5152 1.6122 1.8991 0.0464 -0.0324 0.0445 225 GLU A O 1773 C CB . GLU A 226 ? 1.6332 1.6888 2.0077 0.0562 -0.0064 0.0406 225 GLU A CB 1774 C CG . GLU A 226 ? 1.7137 1.7387 2.0731 0.0610 0.0045 0.0414 225 GLU A CG 1775 C CD . GLU A 226 ? 1.7873 1.8023 2.1471 0.0666 0.0156 0.0383 225 GLU A CD 1776 O OE1 . GLU A 226 ? 1.8089 1.8430 2.1870 0.0727 0.0167 0.0398 225 GLU A OE1 1777 O OE2 . GLU A 226 ? 1.8441 1.8309 2.1854 0.0642 0.0244 0.0338 225 GLU A OE2 1778 N N . GLN A 227 ? 1.3953 1.4924 1.7817 0.0376 -0.0254 0.0334 226 GLN A N 1779 C CA . GLN A 227 ? 1.3584 1.4783 1.7565 0.0341 -0.0336 0.0326 226 GLN A CA 1780 C C . GLN A 227 ? 1.2978 1.4201 1.6877 0.0261 -0.0408 0.0311 226 GLN A C 1781 O O . GLN A 227 ? 1.2712 1.4072 1.6663 0.0262 -0.0484 0.0335 226 GLN A O 1782 C CB . GLN A 227 ? 1.3480 1.4709 1.7486 0.0302 -0.0299 0.0272 226 GLN A CB 1783 C CG . GLN A 227 ? 1.3347 1.4756 1.7439 0.0248 -0.0365 0.0253 226 GLN A CG 1784 C CD . GLN A 227 ? 1.3184 1.4576 1.7161 0.0168 -0.0426 0.0214 226 GLN A CD 1785 O OE1 . GLN A 227 ? 1.3005 1.4504 1.7012 0.0143 -0.0497 0.0224 226 GLN A OE1 1786 N NE2 . GLN A 227 ? 1.2934 1.4194 1.6780 0.0132 -0.0402 0.0164 226 GLN A NE2 1787 N N . GLN A 228 ? 1.2707 1.3800 1.6486 0.0192 -0.0382 0.0261 227 GLN A N 1788 C CA . GLN A 228 ? 1.2527 1.3653 1.6261 0.0113 -0.0426 0.0234 227 GLN A CA 1789 C C . GLN A 228 ? 1.3075 1.4173 1.6758 0.0134 -0.0439 0.0295 227 GLN A C 1790 O O . GLN A 228 ? 1.3548 1.4735 1.7222 0.0104 -0.0488 0.0298 227 GLN A O 1791 C CB . GLN A 228 ? 1.2440 1.3448 1.6101 0.0038 -0.0395 0.0163 227 GLN A CB 1792 C CG . GLN A 228 ? 1.2459 1.3479 1.6112 0.0021 -0.0409 0.0098 227 GLN A CG 1793 C CD . GLN A 228 ? 1.2775 1.3664 1.6348 -0.0036 -0.0396 0.0021 227 GLN A CD 1794 O OE1 . GLN A 228 ? 1.3352 1.4094 1.6876 -0.0053 -0.0343 0.0019 227 GLN A OE1 1795 N NE2 . GLN A 228 ? 1.2830 1.3761 1.6381 -0.0064 -0.0451 -0.0044 227 GLN A NE2 1796 N N . ARG A 229 ? 1.3387 1.4329 1.7004 0.0192 -0.0387 0.0347 228 ARG A N 1797 C CA . ARG A 229 ? 1.3988 1.4850 1.7501 0.0235 -0.0393 0.0420 228 ARG A CA 1798 C C . ARG A 229 ? 1.4126 1.5161 1.7693 0.0305 -0.0496 0.0469 228 ARG A C 1799 O O . ARG A 229 ? 1.3857 1.4877 1.7313 0.0307 -0.0537 0.0502 228 ARG A O 1800 C CB . ARG A 229 ? 1.4485 1.5121 1.7906 0.0309 -0.0315 0.0475 228 ARG A CB 1801 C CG . ARG A 229 ? 1.5016 1.5434 1.8340 0.0220 -0.0212 0.0427 228 ARG A CG 1802 C CD . ARG A 229 ? 1.5560 1.5712 1.8769 0.0295 -0.0122 0.0481 228 ARG A CD 1803 N NE . ARG A 229 ? 1.5958 1.5882 1.9072 0.0187 -0.0018 0.0426 228 ARG A NE 1804 C CZ . ARG A 229 ? 1.6638 1.6266 1.9618 0.0217 0.0086 0.0457 228 ARG A CZ 1805 N NH1 . ARG A 229 ? 1.7111 1.6634 2.0029 0.0373 0.0099 0.0552 228 ARG A NH1 1806 N NH2 . ARG A 229 ? 1.6928 1.6365 1.9847 0.0090 0.0177 0.0387 228 ARG A NH2 1807 N N . SER A 230 ? 1.4117 1.5308 1.7852 0.0358 -0.0533 0.0466 229 SER A N 1808 C CA . SER A 230 ? 1.4322 1.5707 1.8166 0.0421 -0.0641 0.0498 229 SER A CA 1809 C C . SER A 230 ? 1.4220 1.5742 1.8063 0.0341 -0.0720 0.0456 229 SER A C 1810 O O . SER A 230 ? 1.4242 1.5866 1.8087 0.0376 -0.0823 0.0479 229 SER A O 1811 C CB . SER A 230 ? 1.4060 1.5594 1.8134 0.0474 -0.0633 0.0490 229 SER A CB 1812 O OG . SER A 230 ? 1.3770 1.5413 1.7942 0.0386 -0.0618 0.0420 229 SER A OG 1813 N N . ALA A 231 ? 1.3943 1.5458 1.7775 0.0242 -0.0678 0.0390 230 ALA A N 1814 C CA . ALA A 231 ? 1.3830 1.5442 1.7651 0.0170 -0.0731 0.0346 230 ALA A CA 1815 C C . ALA A 231 ? 1.3755 1.5264 1.7385 0.0148 -0.0736 0.0363 230 ALA A C 1816 O O . ALA A 231 ? 1.3832 1.5206 1.7372 0.0110 -0.0656 0.0356 230 ALA A O 1817 C CB . ALA A 231 ? 1.3848 1.5473 1.7713 0.0098 -0.0685 0.0278 230 ALA A CB 1818 N N . VAL A 232 ? 1.3717 1.5285 1.7286 0.0165 -0.0825 0.0378 231 VAL A N 1819 C CA . VAL A 232 ? 1.3903 1.5347 1.7246 0.0153 -0.0821 0.0397 231 VAL A CA 1820 C C . VAL A 232 ? 1.3512 1.4921 1.6827 0.0060 -0.0741 0.0337 231 VAL A C 1821 O O . VAL A 232 ? 1.3505 1.4773 1.6678 0.0036 -0.0662 0.0350 231 VAL A O 1822 C CB . VAL A 232 ? 1.4163 1.5683 1.7430 0.0177 -0.0949 0.0400 231 VAL A CB 1823 C CG1 . VAL A 232 ? 1.4262 1.5617 1.7246 0.0161 -0.0926 0.0413 231 VAL A CG1 1824 C CG2 . VAL A 232 ? 1.4573 1.6154 1.7887 0.0285 -0.1051 0.0458 231 VAL A CG2 1825 N N . SER A 233 ? 1.3206 1.4741 1.6664 0.0013 -0.0754 0.0274 232 SER A N 1826 C CA . SER A 233 ? 1.3410 1.4941 1.6876 -0.0052 -0.0695 0.0215 232 SER A CA 1827 C C . SER A 233 ? 1.3667 1.5113 1.7149 -0.0080 -0.0600 0.0207 232 SER A C 1828 O O . SER A 233 ? 1.3920 1.5349 1.7391 -0.0128 -0.0542 0.0171 232 SER A O 1829 C CB . SER A 233 ? 1.3156 1.4800 1.6760 -0.0073 -0.0724 0.0163 232 SER A CB 1830 O OG . SER A 233 ? 1.2842 1.4510 1.6556 -0.0049 -0.0718 0.0172 232 SER A OG 1831 N N . THR A 234 ? 1.3690 1.5089 1.7214 -0.0055 -0.0581 0.0231 233 THR A N 1832 C CA . THR A 234 ? 1.4290 1.5591 1.7827 -0.0094 -0.0497 0.0212 233 THR A CA 1833 C C . THR A 234 ? 1.4808 1.5969 1.8213 -0.0119 -0.0414 0.0244 233 THR A C 1834 O O . THR A 234 ? 1.5496 1.6648 1.8941 -0.0190 -0.0341 0.0197 233 THR A O 1835 C CB . THR A 234 ? 1.4418 1.5647 1.7980 -0.0055 -0.0483 0.0237 233 THR A CB 1836 O OG1 . THR A 234 ? 1.4516 1.5853 1.8172 -0.0018 -0.0541 0.0226 233 THR A OG1 1837 C CG2 . THR A 234 ? 1.4292 1.5439 1.7889 -0.0116 -0.0415 0.0184 233 THR A CG2 1838 N N . SER A 235 ? 1.4811 1.5860 1.8059 -0.0056 -0.0424 0.0323 234 SER A N 1839 C CA . SER A 235 ? 1.5413 1.6270 1.8468 -0.0065 -0.0335 0.0370 234 SER A CA 1840 C C . SER A 235 ? 1.5251 1.6128 1.8227 -0.0107 -0.0307 0.0344 234 SER A C 1841 O O . SER A 235 ? 1.5020 1.5767 1.7907 -0.0158 -0.0183 0.0346 234 SER A O 1842 C CB . SER A 235 ? 1.6124 1.6850 1.8995 0.0041 -0.0380 0.0468 234 SER A CB 1843 O OG . SER A 235 ? 1.6394 1.7135 1.9369 0.0099 -0.0412 0.0488 234 SER A OG 1844 N N . TRP A 236 ? 1.5299 1.6326 1.8309 -0.0091 -0.0407 0.0316 235 TRP A N 1845 C CA . TRP A 236 ? 1.5809 1.6849 1.8740 -0.0124 -0.0383 0.0281 235 TRP A CA 1846 C C . TRP A 236 ? 1.5629 1.6733 1.8721 -0.0202 -0.0279 0.0208 235 TRP A C 1847 O O . TRP A 236 ? 1.5776 1.6830 1.8793 -0.0233 -0.0190 0.0190 235 TRP A O 1848 C CB . TRP A 236 ? 1.5953 1.7134 1.8915 -0.0100 -0.0511 0.0253 235 TRP A CB 1849 C CG . TRP A 236 ? 1.6200 1.7364 1.9047 -0.0124 -0.0492 0.0214 235 TRP A CG 1850 C CD1 . TRP A 236 ? 1.6459 1.7457 1.9071 -0.0129 -0.0408 0.0235 235 TRP A CD1 1851 C CD2 . TRP A 236 ? 1.6257 1.7538 1.9187 -0.0143 -0.0544 0.0150 235 TRP A CD2 1852 N NE1 . TRP A 236 ? 1.6600 1.7615 1.9151 -0.0148 -0.0404 0.0181 235 TRP A NE1 1853 C CE2 . TRP A 236 ? 1.6711 1.7896 1.9457 -0.0156 -0.0490 0.0129 235 TRP A CE2 1854 C CE3 . TRP A 236 ? 1.5832 1.7259 1.8949 -0.0147 -0.0615 0.0111 235 TRP A CE3 1855 C CZ2 . TRP A 236 ? 1.6953 1.8185 1.9708 -0.0172 -0.0511 0.0066 235 TRP A CZ2 1856 C CZ3 . TRP A 236 ? 1.5755 1.7218 1.8873 -0.0165 -0.0633 0.0054 235 TRP A CZ3 1857 C CH2 . TRP A 236 ? 1.6283 1.7651 1.9227 -0.0176 -0.0584 0.0031 235 TRP A CH2 1858 N N . LEU A 237 ? 1.5255 1.6469 1.8568 -0.0228 -0.0293 0.0163 236 LEU A N 1859 C CA . LEU A 237 ? 1.5439 1.6758 1.8947 -0.0290 -0.0233 0.0084 236 LEU A CA 1860 C C . LEU A 237 ? 1.5720 1.6962 1.9296 -0.0361 -0.0109 0.0069 236 LEU A C 1861 O O . LEU A 237 ? 1.6123 1.7487 1.9915 -0.0417 -0.0078 -0.0007 236 LEU A O 1862 C CB . LEU A 237 ? 1.5402 1.6874 1.9086 -0.0277 -0.0331 0.0032 236 LEU A CB 1863 C CG . LEU A 237 ? 1.5574 1.7131 1.9241 -0.0232 -0.0422 0.0024 236 LEU A CG 1864 C CD1 . LEU A 237 ? 1.5783 1.7426 1.9569 -0.0213 -0.0497 -0.0010 236 LEU A CD1 1865 C CD2 . LEU A 237 ? 1.5574 1.7173 1.9245 -0.0241 -0.0381 -0.0015 236 LEU A CD2 1866 N N . LEU A 238 ? 1.5650 1.6688 1.9051 -0.0358 -0.0040 0.0138 237 LEU A N 1867 C CA . LEU A 238 ? 1.5317 1.6235 1.8755 -0.0441 0.0109 0.0126 237 LEU A CA 1868 C C . LEU A 238 ? 1.5225 1.6174 1.8716 -0.0502 0.0238 0.0085 237 LEU A C 1869 O O . LEU A 238 ? 1.5020 1.5959 1.8370 -0.0459 0.0237 0.0108 237 LEU A O 1870 C CB . LEU A 238 ? 1.5436 1.6072 1.8610 -0.0408 0.0174 0.0224 237 LEU A CB 1871 C CG . LEU A 238 ? 1.5172 1.5748 1.8334 -0.0358 0.0098 0.0257 237 LEU A CG 1872 C CD1 . LEU A 238 ? 1.5361 1.5681 1.8229 -0.0272 0.0119 0.0373 237 LEU A CD1 1873 C CD2 . LEU A 238 ? 1.5096 1.5654 1.8436 -0.0453 0.0166 0.0188 237 LEU A CD2 1874 N N . PRO A 239 ? 1.5056 1.6049 1.8765 -0.0605 0.0353 0.0017 238 PRO A N 1875 C CA . PRO A 239 ? 1.5214 1.6260 1.9039 -0.0670 0.0505 -0.0029 238 PRO A CA 1876 C C . PRO A 239 ? 1.5867 1.6670 1.9370 -0.0649 0.0645 0.0050 238 PRO A C 1877 O O . PRO A 239 ? 1.5700 1.6230 1.8916 -0.0628 0.0693 0.0139 238 PRO A O 1878 C CB . PRO A 239 ? 1.5263 1.6320 1.9327 -0.0796 0.0619 -0.0095 238 PRO A CB 1879 C CG . PRO A 239 ? 1.5183 1.6329 1.9362 -0.0788 0.0459 -0.0131 238 PRO A CG 1880 C CD . PRO A 239 ? 1.4996 1.6020 1.8891 -0.0669 0.0336 -0.0036 238 PRO A CD 1881 N N . TYR A 240 ? 1.6698 1.7579 2.0225 -0.0644 0.0710 0.0018 239 TYR A N 1882 C CA . TYR A 240 ? 1.7544 1.8182 2.0740 -0.0624 0.0856 0.0080 239 TYR A CA 1883 C C . TYR A 240 ? 1.8067 1.8691 2.1421 -0.0726 0.1112 0.0031 239 TYR A C 1884 O O . TYR A 240 ? 1.7451 1.8350 2.1219 -0.0785 0.1136 -0.0069 239 TYR A O 1885 C CB . TYR A 240 ? 1.7713 1.8407 2.0764 -0.0537 0.0754 0.0079 239 TYR A CB 1886 C CG . TYR A 240 ? 1.7903 1.8579 2.0762 -0.0445 0.0532 0.0131 239 TYR A CG 1887 C CD1 . TYR A 240 ? 1.7690 1.8599 2.0781 -0.0420 0.0353 0.0090 239 TYR A CD1 1888 C CD2 . TYR A 240 ? 1.8246 1.8672 2.0691 -0.0380 0.0502 0.0219 239 TYR A CD2 1889 C CE1 . TYR A 240 ? 1.7717 1.8624 2.0673 -0.0347 0.0174 0.0131 239 TYR A CE1 1890 C CE2 . TYR A 240 ? 1.8221 1.8674 2.0551 -0.0302 0.0295 0.0256 239 TYR A CE2 1891 C CZ . TYR A 240 ? 1.8043 1.8743 2.0648 -0.0292 0.0144 0.0210 239 TYR A CZ 1892 O OH . TYR A 240 ? 1.8067 1.8807 2.0596 -0.0226 -0.0036 0.0240 239 TYR A OH 1893 N N . ASN A 241 ? 1.9463 1.9763 2.2481 -0.0739 0.1302 0.0103 240 ASN A N 1894 C CA . ASN A 241 ? 2.0503 2.0724 2.3637 -0.0851 0.1592 0.0071 240 ASN A CA 1895 C C . ASN A 241 ? 2.0398 2.0789 2.3722 -0.0862 0.1717 -0.0004 240 ASN A C 1896 O O . ASN A 241 ? 1.9966 2.0396 2.3531 -0.0965 0.1952 -0.0058 240 ASN A O 1897 C CB . ASN A 241 ? 2.1803 2.1561 2.4448 -0.0850 0.1775 0.0185 240 ASN A CB 1898 C CG . ASN A 241 ? 2.2974 2.2500 2.5119 -0.0735 0.1753 0.0260 240 ASN A CG 1899 O OD1 . ASN A 241 ? 2.2879 2.2575 2.5068 -0.0684 0.1674 0.0212 240 ASN A OD1 1900 N ND2 . ASN A 241 ? 2.4495 2.3603 2.6134 -0.0691 0.1826 0.0377 240 ASN A ND2 1901 N N . TYR A 242 ? 2.0879 2.1357 2.4095 -0.0759 0.1575 -0.0010 241 TYR A N 1902 C CA . TYR A 242 ? 2.1845 2.2466 2.5220 -0.0748 0.1689 -0.0080 241 TYR A CA 1903 C C . TYR A 242 ? 2.0484 2.1543 2.4448 -0.0770 0.1608 -0.0197 241 TYR A C 1904 O O . TYR A 242 ? 2.1028 2.2251 2.5253 -0.0777 0.1742 -0.0269 241 TYR A O 1905 C CB . TYR A 242 ? 2.3248 2.3740 2.6237 -0.0633 0.1588 -0.0046 241 TYR A CB 1906 C CG . TYR A 242 ? 2.4442 2.5087 2.7438 -0.0553 0.1279 -0.0047 241 TYR A CG 1907 C CD1 . TYR A 242 ? 2.4675 2.5634 2.8022 -0.0521 0.1162 -0.0129 241 TYR A CD1 1908 C CD2 . TYR A 242 ? 2.5213 2.5680 2.7865 -0.0503 0.1114 0.0036 241 TYR A CD2 1909 C CE1 . TYR A 242 ? 2.4646 2.5709 2.7979 -0.0455 0.0911 -0.0126 241 TYR A CE1 1910 C CE2 . TYR A 242 ? 2.5375 2.5987 2.8063 -0.0442 0.0859 0.0031 241 TYR A CE2 1911 C CZ . TYR A 242 ? 2.4963 2.5858 2.7980 -0.0425 0.0769 -0.0048 241 TYR A CZ 1912 O OH . TYR A 242 ? 2.4416 2.5422 2.7451 -0.0372 0.0544 -0.0051 241 TYR A OH 1913 N N . THR A 243 ? 1.8819 2.0055 2.2978 -0.0771 0.1390 -0.0215 242 THR A N 1914 C CA . THR A 243 ? 1.7849 1.9477 2.2521 -0.0781 0.1276 -0.0321 242 THR A CA 1915 C C . THR A 243 ? 1.7390 1.9135 2.2407 -0.0910 0.1334 -0.0379 242 THR A C 1916 O O . THR A 243 ? 1.7029 1.9065 2.2509 -0.0963 0.1386 -0.0483 242 THR A O 1917 C CB . THR A 243 ? 1.7222 1.8966 2.1863 -0.0688 0.0984 -0.0315 242 THR A CB 1918 O OG1 . THR A 243 ? 1.7843 1.9487 2.2194 -0.0585 0.0928 -0.0277 242 THR A OG1 1919 C CG2 . THR A 243 ? 1.6602 1.8713 2.1712 -0.0680 0.0860 -0.0419 242 THR A CG2 1920 N N . TRP A 244 ? 1.7212 1.8731 2.2011 -0.0956 0.1318 -0.0317 243 TRP A N 1921 C CA . TRP A 244 ? 1.7013 1.8569 2.2071 -0.1091 0.1383 -0.0369 243 TRP A CA 1922 C C . TRP A 244 ? 1.7390 1.8673 2.2326 -0.1198 0.1692 -0.0334 243 TRP A C 1923 O O . TRP A 244 ? 1.8157 1.9139 2.2672 -0.1147 0.1814 -0.0237 243 TRP A O 1924 C CB . TRP A 244 ? 1.6666 1.8100 2.1544 -0.1072 0.1201 -0.0322 243 TRP A CB 1925 C CG . TRP A 244 ? 1.6172 1.7831 2.1136 -0.0972 0.0924 -0.0351 243 TRP A CG 1926 C CD1 . TRP A 244 ? 1.6064 1.7681 2.0764 -0.0842 0.0780 -0.0287 243 TRP A CD1 1927 C CD2 . TRP A 244 ? 1.5901 1.7843 2.1224 -0.0998 0.0766 -0.0455 243 TRP A CD2 1928 N NE1 . TRP A 244 ? 1.5805 1.7641 2.0671 -0.0787 0.0564 -0.0336 243 TRP A NE1 1929 C CE2 . TRP A 244 ? 1.5614 1.7643 2.0839 -0.0872 0.0545 -0.0436 243 TRP A CE2 1930 C CE3 . TRP A 244 ? 1.5862 1.7983 2.1570 -0.1120 0.0786 -0.0568 243 TRP A CE3 1931 C CZ2 . TRP A 244 ? 1.5399 1.7655 2.0851 -0.0850 0.0351 -0.0514 243 TRP A CZ2 1932 C CZ3 . TRP A 244 ? 1.5552 1.7924 2.1499 -0.1098 0.0567 -0.0655 243 TRP A CZ3 1933 C CH2 . TRP A 244 ? 1.5250 1.7673 2.1046 -0.0957 0.0356 -0.0623 243 TRP A CH2 1934 N N . SER A 245 ? 1.7209 1.8582 2.2499 -0.1351 0.1821 -0.0416 244 SER A N 1935 C CA . SER A 245 ? 1.7872 1.8965 2.3066 -0.1475 0.2143 -0.0387 244 SER A CA 1936 C C . SER A 245 ? 1.8076 1.8700 2.2729 -0.1452 0.2166 -0.0252 244 SER A C 1937 O O . SER A 245 ? 1.7303 1.7904 2.1909 -0.1435 0.1980 -0.0240 244 SER A O 1938 C CB . SER A 245 ? 1.8009 1.9324 2.3749 -0.1662 0.2257 -0.0522 244 SER A CB 1939 O OG . SER A 245 ? 1.8682 1.9736 2.4370 -0.1794 0.2610 -0.0503 244 SER A OG 1940 N N . PRO A 246 ? 1.8700 1.8933 2.2923 -0.1438 0.2394 -0.0147 245 PRO A N 1941 C CA . PRO A 246 ? 1.8354 1.8123 2.2048 -0.1398 0.2417 -0.0011 245 PRO A CA 1942 C C . PRO A 246 ? 1.7421 1.7054 2.1235 -0.1531 0.2491 -0.0033 245 PRO A C 1943 O O . PRO A 246 ? 1.6860 1.6197 2.0325 -0.1471 0.2417 0.0061 245 PRO A O 1944 C CB . PRO A 246 ? 1.8981 1.8371 2.2259 -0.1388 0.2700 0.0078 245 PRO A CB 1945 C CG . PRO A 246 ? 1.9142 1.8797 2.2600 -0.1352 0.2728 0.0014 245 PRO A CG 1946 C CD . PRO A 246 ? 1.8926 1.9108 2.3069 -0.1426 0.2616 -0.0140 245 PRO A CD 1947 N N . GLU A 247 ? 1.6966 1.6820 2.1286 -0.1708 0.2631 -0.0164 246 GLU A N 1948 C CA . GLU A 247 ? 1.7072 1.6799 2.1547 -0.1868 0.2727 -0.0212 246 GLU A CA 1949 C C . GLU A 247 ? 1.6432 1.6528 2.1327 -0.1906 0.2458 -0.0339 246 GLU A C 1950 O O . GLU A 247 ? 1.6351 1.6377 2.1411 -0.2048 0.2507 -0.0405 246 GLU A O 1951 C CB . GLU A 247 ? 1.7650 1.7360 2.2427 -0.2070 0.3078 -0.0290 246 GLU A CB 1952 C CG . GLU A 247 ? 1.8612 1.7849 2.2921 -0.2064 0.3409 -0.0163 246 GLU A CG 1953 C CD . GLU A 247 ? 1.9025 1.8295 2.3089 -0.1907 0.3398 -0.0100 246 GLU A CD 1954 O OE1 . GLU A 247 ? 1.8662 1.8388 2.3091 -0.1860 0.3238 -0.0191 246 GLU A OE1 1955 O OE2 . GLU A 247 ? 1.9537 1.8352 2.3018 -0.1828 0.3551 0.0038 246 GLU A OE2 1956 N N . LYS A 248 ? 1.5892 1.6346 2.0932 -0.1783 0.2182 -0.0375 247 LYS A N 1957 C CA . LYS A 248 ? 1.5761 1.6555 2.1168 -0.1809 0.1931 -0.0496 247 LYS A CA 1958 C C . LYS A 248 ? 1.5827 1.6369 2.0947 -0.1771 0.1795 -0.0441 247 LYS A C 1959 O O . LYS A 248 ? 1.5709 1.6025 2.0396 -0.1618 0.1711 -0.0309 247 LYS A O 1960 C CB . LYS A 248 ? 1.5455 1.6629 2.1014 -0.1667 0.1687 -0.0528 247 LYS A CB 1961 C CG . LYS A 248 ? 1.5412 1.6911 2.1282 -0.1664 0.1411 -0.0643 247 LYS A CG 1962 C CD . LYS A 248 ? 1.5559 1.7371 2.1997 -0.1835 0.1452 -0.0817 247 LYS A CD 1963 C CE . LYS A 248 ? 1.5507 1.7541 2.2149 -0.1840 0.1173 -0.0925 247 LYS A CE 1964 N NZ . LYS A 248 ? 1.5060 1.7298 2.1635 -0.1653 0.0908 -0.0903 247 LYS A NZ 1965 N N . VAL A 249 ? 1.5973 1.6564 2.1351 -0.1910 0.1771 -0.0553 248 VAL A N 1966 C CA . VAL A 249 ? 1.6268 1.6623 2.1410 -0.1884 0.1657 -0.0523 248 VAL A CA 1967 C C . VAL A 249 ? 1.5901 1.6557 2.1148 -0.1774 0.1334 -0.0575 248 VAL A C 1968 O O . VAL A 249 ? 1.5482 1.6501 2.1136 -0.1840 0.1212 -0.0720 248 VAL A O 1969 C CB . VAL A 249 ? 1.6687 1.6918 2.2034 -0.2098 0.1787 -0.0635 248 VAL A CB 1970 C CG1 . VAL A 249 ? 1.6822 1.6738 2.1863 -0.2059 0.1703 -0.0593 248 VAL A CG1 1971 C CG2 . VAL A 249 ? 1.7174 1.7130 2.2482 -0.2237 0.2140 -0.0602 248 VAL A CG2 1972 N N . PHE A 250 ? 1.5798 1.6302 2.0678 -0.1603 0.1200 -0.0458 249 PHE A N 1973 C CA . PHE A 250 ? 1.5299 1.6032 2.0221 -0.1491 0.0924 -0.0490 249 PHE A CA 1974 C C . PHE A 250 ? 1.5169 1.5745 2.0006 -0.1513 0.0837 -0.0525 249 PHE A C 1975 O O . PHE A 250 ? 1.5121 1.5908 2.0120 -0.1509 0.0648 -0.0622 249 PHE A O 1976 C CB . PHE A 250 ? 1.5373 1.6071 1.9992 -0.1299 0.0829 -0.0355 249 PHE A CB 1977 C CG . PHE A 250 ? 1.5567 1.6454 2.0264 -0.1258 0.0861 -0.0341 249 PHE A CG 1978 C CD1 . PHE A 250 ? 1.5141 1.6391 2.0102 -0.1217 0.0706 -0.0421 249 PHE A CD1 1979 C CD2 . PHE A 250 ? 1.6352 1.7023 2.0826 -0.1250 0.1053 -0.0247 249 PHE A CD2 1980 C CE1 . PHE A 250 ? 1.5428 1.6828 2.0451 -0.1172 0.0748 -0.0410 249 PHE A CE1 1981 C CE2 . PHE A 250 ? 1.6609 1.7425 2.1127 -0.1210 0.1095 -0.0241 249 PHE A CE2 1982 C CZ . PHE A 250 ? 1.6242 1.7427 2.1046 -0.1172 0.0946 -0.0324 249 PHE A CZ 1983 N N . VAL A 251 ? 1.5073 1.5248 1.9619 -0.1524 0.0978 -0.0441 250 VAL A N 1984 C CA . VAL A 251 ? 1.5231 1.5194 1.9639 -0.1524 0.0922 -0.0458 250 VAL A CA 1985 C C . VAL A 251 ? 1.5979 1.5598 2.0337 -0.1679 0.1141 -0.0481 250 VAL A C 1986 O O . VAL A 251 ? 1.6511 1.5841 2.0656 -0.1679 0.1343 -0.0373 250 VAL A O 1987 C CB . VAL A 251 ? 1.5056 1.4831 1.9096 -0.1323 0.0841 -0.0310 250 VAL A CB 1988 C CG1 . VAL A 251 ? 1.4986 1.4515 1.8881 -0.1317 0.0816 -0.0328 250 VAL A CG1 1989 C CG2 . VAL A 251 ? 1.4857 1.4952 1.8951 -0.1187 0.0636 -0.0296 250 VAL A CG2 1990 N N . GLN A 252 ? 1.6221 1.5851 2.0754 -0.1812 0.1099 -0.0625 251 GLN A N 1991 C CA . GLN A 252 ? 1.6750 1.6026 2.1233 -0.1974 0.1294 -0.0668 251 GLN A CA 1992 C C . GLN A 252 ? 1.6993 1.5986 2.1213 -0.1910 0.1223 -0.0660 251 GLN A C 1993 O O . GLN A 252 ? 1.6547 1.5727 2.0818 -0.1854 0.1010 -0.0730 251 GLN A O 1994 C CB . GLN A 252 ? 1.6924 1.6438 2.1861 -0.2214 0.1321 -0.0871 251 GLN A CB 1995 C CG . GLN A 252 ? 1.7024 1.6759 2.2252 -0.2309 0.1469 -0.0889 251 GLN A CG 1996 C CD . GLN A 252 ? 1.6779 1.7045 2.2333 -0.2246 0.1271 -0.0953 251 GLN A CD 1997 O OE1 . GLN A 252 ? 1.6869 1.7278 2.2300 -0.2070 0.1054 -0.0906 251 GLN A OE1 1998 N NE2 . GLN A 252 ? 1.6605 1.7157 2.2586 -0.2388 0.1361 -0.1060 251 GLN A NE2 1999 N N . THR A 253 ? 1.7723 1.6238 2.1637 -0.1908 0.1413 -0.0568 252 THR A N 2000 C CA . THR A 253 ? 1.7981 1.6164 2.1633 -0.1850 0.1394 -0.0558 252 THR A CA 2001 C C . THR A 253 ? 1.8309 1.6107 2.1937 -0.2054 0.1618 -0.0631 252 THR A C 2002 O O . THR A 253 ? 1.8277 1.6085 2.2087 -0.2222 0.1787 -0.0671 252 THR A O 2003 C CB . THR A 253 ? 1.8503 1.6432 2.1757 -0.1601 0.1406 -0.0348 252 THR A CB 2004 O OG1 . THR A 253 ? 1.8877 1.6393 2.1884 -0.1609 0.1648 -0.0229 252 THR A OG1 2005 C CG2 . THR A 253 ? 1.8594 1.6881 2.1885 -0.1435 0.1244 -0.0263 252 THR A CG2 2006 N N . PRO A 254 ? 1.8584 1.6026 2.1990 -0.2045 0.1641 -0.0652 253 PRO A N 2007 C CA . PRO A 254 ? 1.9079 1.6119 2.2450 -0.2251 0.1862 -0.0732 253 PRO A CA 2008 C C . PRO A 254 ? 1.9840 1.6478 2.2980 -0.2255 0.2150 -0.0580 253 PRO A C 2009 O O . PRO A 254 ? 2.0118 1.6520 2.3336 -0.2475 0.2366 -0.0657 253 PRO A O 2010 C CB . PRO A 254 ? 1.9112 1.5813 2.2206 -0.2176 0.1823 -0.0748 253 PRO A CB 2011 C CG . PRO A 254 ? 1.8639 1.5680 2.1747 -0.1991 0.1553 -0.0740 253 PRO A CG 2012 C CD . PRO A 254 ? 1.8395 1.5754 2.1565 -0.1851 0.1493 -0.0604 253 PRO A CD 2013 N N . THR A 255 ? 2.0519 1.7071 2.3370 -0.2016 0.2150 -0.0372 254 THR A N 2014 C CA . THR A 255 ? 2.1679 1.7789 2.4205 -0.1969 0.2400 -0.0203 254 THR A CA 2015 C C . THR A 255 ? 2.1642 1.7958 2.4232 -0.1959 0.2460 -0.0124 254 THR A C 2016 O O . THR A 255 ? 2.1889 1.7874 2.4320 -0.2034 0.2718 -0.0054 254 THR A O 2017 C CB . THR A 255 ? 2.2301 1.8070 2.4376 -0.1684 0.2373 -0.0010 254 THR A CB 2018 O OG1 . THR A 255 ? 2.2281 1.8450 2.4395 -0.1474 0.2120 0.0055 254 THR A OG1 2019 C CG2 . THR A 255 ? 2.2499 1.7942 2.4443 -0.1689 0.2386 -0.0070 254 THR A CG2 2020 N N . ILE A 256 ? 2.1557 1.8380 2.4351 -0.1868 0.2239 -0.0134 255 ILE A N 2021 C CA . ILE A 256 ? 2.1907 1.8883 2.4679 -0.1808 0.2280 -0.0037 255 ILE A CA 2022 C C . ILE A 256 ? 2.0555 1.8146 2.3732 -0.1832 0.2081 -0.0143 255 ILE A C 2023 O O . ILE A 256 ? 1.9482 1.7383 2.2876 -0.1823 0.1860 -0.0249 255 ILE A O 2024 C CB . ILE A 256 ? 2.2826 1.9569 2.5139 -0.1527 0.2235 0.0182 255 ILE A CB 2025 C CG1 . ILE A 256 ? 2.3446 2.0107 2.5576 -0.1489 0.2371 0.0300 255 ILE A CG1 2026 C CG2 . ILE A 256 ? 2.2362 1.9460 2.4732 -0.1338 0.1933 0.0196 255 ILE A CG2 2027 C CD1 . ILE A 256 ? 2.3721 2.0098 2.5365 -0.1225 0.2332 0.0511 255 ILE A CD1 2028 N N . ASN A 257 ? 2.0165 1.7892 2.3417 -0.1862 0.2178 -0.0113 256 ASN A N 2029 C CA . ASN A 257 ? 1.9386 1.7642 2.2949 -0.1839 0.2013 -0.0175 256 ASN A CA 2030 C C . ASN A 257 ? 1.8612 1.6914 2.1891 -0.1600 0.1885 -0.0020 256 ASN A C 2031 O O . ASN A 257 ? 1.9408 1.7341 2.2263 -0.1465 0.1955 0.0139 256 ASN A O 2032 C CB . ASN A 257 ? 1.9852 1.8234 2.3684 -0.2014 0.2215 -0.0242 256 ASN A CB 2033 C CG . ASN A 257 ? 2.0644 1.9156 2.4913 -0.2272 0.2292 -0.0439 256 ASN A CG 2034 O OD1 . ASN A 257 ? 2.0287 1.8987 2.4761 -0.2313 0.2104 -0.0563 256 ASN A OD1 2035 N ND2 . ASN A 257 ? 2.2011 2.0439 2.6436 -0.2453 0.2570 -0.0477 256 ASN A ND2 2036 N N . TYR A 258 ? 1.7193 1.5947 2.0710 -0.1548 0.1693 -0.0072 257 TYR A N 2037 C CA . TYR A 258 ? 1.6573 1.5415 1.9879 -0.1356 0.1581 0.0046 257 TYR A CA 2038 C C . TYR A 258 ? 1.6482 1.5704 2.0067 -0.1396 0.1558 -0.0020 257 TYR A C 2039 O O . TYR A 258 ? 1.5732 1.5340 1.9691 -0.1450 0.1419 -0.0151 257 TYR A O 2040 C CB . TYR A 258 ? 1.6094 1.5053 1.9324 -0.1190 0.1327 0.0078 257 TYR A CB 2041 C CG . TYR A 258 ? 1.6457 1.5037 1.9385 -0.1105 0.1351 0.0167 257 TYR A CG 2042 C CD1 . TYR A 258 ? 1.6745 1.4999 1.9269 -0.0958 0.1412 0.0335 257 TYR A CD1 2043 C CD2 . TYR A 258 ? 1.6738 1.5272 1.9768 -0.1161 0.1309 0.0082 257 TYR A CD2 2044 C CE1 . TYR A 258 ? 1.7426 1.5334 1.9685 -0.0857 0.1433 0.0420 257 TYR A CE1 2045 C CE2 . TYR A 258 ? 1.7186 1.5357 1.9940 -0.1072 0.1346 0.0162 257 TYR A CE2 2046 C CZ . TYR A 258 ? 1.7558 1.5425 1.9942 -0.0914 0.1409 0.0334 257 TYR A CZ 2047 O OH . TYR A 258 ? 1.7950 1.5459 2.0073 -0.0806 0.1446 0.0417 257 TYR A OH 2048 N N . THR A 259 ? 1.7087 1.6167 2.0461 -0.1363 0.1705 0.0068 258 THR A N 2049 C CA . THR A 259 ? 1.7077 1.6450 2.0606 -0.1351 0.1692 0.0038 258 THR A CA 2050 C C . THR A 259 ? 1.7253 1.6625 2.0466 -0.1147 0.1526 0.0152 258 THR A C 2051 O O . THR A 259 ? 1.7534 1.6697 2.0444 -0.1024 0.1434 0.0253 258 THR A O 2052 C CB . THR A 259 ? 1.7286 1.6477 2.0769 -0.1458 0.1994 0.0052 258 THR A CB 2053 O OG1 . THR A 259 ? 1.7272 1.5997 2.0213 -0.1360 0.2115 0.0216 258 THR A OG1 2054 C CG2 . THR A 259 ? 1.7542 1.6708 2.1346 -0.1680 0.2187 -0.0061 258 THR A CG2 2055 N N . LEU A 260 ? 1.7110 1.6718 2.0409 -0.1114 0.1490 0.0130 259 LEU A N 2056 C CA . LEU A 260 ? 1.7195 1.6805 2.0208 -0.0944 0.1342 0.0220 259 LEU A CA 2057 C C . LEU A 260 ? 1.7366 1.6551 1.9856 -0.0853 0.1443 0.0370 259 LEU A C 2058 O O . LEU A 260 ? 1.6780 1.5927 1.8999 -0.0705 0.1289 0.0451 259 LEU A O 2059 C CB . LEU A 260 ? 1.7505 1.7414 2.0708 -0.0943 0.1316 0.0154 259 LEU A CB 2060 C CG . LEU A 260 ? 1.8130 1.7989 2.1392 -0.1041 0.1576 0.0124 259 LEU A CG 2061 C CD1 . LEU A 260 ? 1.8662 1.8200 2.1432 -0.0953 0.1680 0.0241 259 LEU A CD1 2062 C CD2 . LEU A 260 ? 1.7882 1.8157 2.1573 -0.1076 0.1533 0.0000 259 LEU A CD2 2063 N N . ARG A 261 ? 1.7926 1.6784 2.0271 -0.0942 0.1698 0.0404 260 ARG A N 2064 C CA . ARG A 261 ? 1.8946 1.7340 2.0748 -0.0848 0.1806 0.0554 260 ARG A CA 2065 C C . ARG A 261 ? 1.8901 1.7019 2.0488 -0.0773 0.1751 0.0641 260 ARG A C 2066 O O . ARG A 261 ? 1.9460 1.7172 2.0579 -0.0671 0.1818 0.0775 260 ARG A O 2067 C CB . ARG A 261 ? 2.0026 1.8142 2.1721 -0.0973 0.2142 0.0562 260 ARG A CB 2068 C CG . ARG A 261 ? 2.0425 1.8787 2.2319 -0.1035 0.2230 0.0482 260 ARG A CG 2069 C CD . ARG A 261 ? 2.1022 1.9057 2.2720 -0.1128 0.2580 0.0513 260 ARG A CD 2070 N NE . ARG A 261 ? 2.1184 1.9403 2.2984 -0.1146 0.2670 0.0457 260 ARG A NE 2071 C CZ . ARG A 261 ? 2.1499 1.9571 2.3308 -0.1260 0.2997 0.0437 260 ARG A CZ 2072 N NH1 . ARG A 261 ? 2.1923 1.9660 2.3657 -0.1382 0.3274 0.0465 260 ARG A NH1 2073 N NH2 . ARG A 261 ? 2.1464 1.9713 2.3365 -0.1254 0.3065 0.0385 260 ARG A NH2 2074 N N . ASP A 262 ? 1.8540 1.6858 2.0442 -0.0810 0.1631 0.0565 261 ASP A N 2075 C CA . ASP A 262 ? 1.8681 1.6740 2.0423 -0.0747 0.1603 0.0630 261 ASP A CA 2076 C C . ASP A 262 ? 1.8455 1.6727 2.0235 -0.0590 0.1318 0.0649 261 ASP A C 2077 O O . ASP A 262 ? 1.8727 1.6919 2.0537 -0.0561 0.1270 0.0653 261 ASP A O 2078 C CB . ASP A 262 ? 1.8574 1.6604 2.0608 -0.0931 0.1737 0.0522 261 ASP A CB 2079 C CG . ASP A 262 ? 1.8974 1.6729 2.0961 -0.1095 0.2053 0.0513 261 ASP A CG 2080 O OD1 . ASP A 262 ? 1.9187 1.6508 2.0732 -0.1031 0.2211 0.0645 261 ASP A OD1 2081 O OD2 . ASP A 262 ? 1.8891 1.6859 2.1287 -0.1286 0.2145 0.0371 261 ASP A OD2 2082 N N . TYR A 263 ? 1.8006 1.6528 1.9779 -0.0493 0.1145 0.0660 262 TYR A N 2083 C CA . TYR A 263 ? 1.7399 1.6154 1.9254 -0.0364 0.0893 0.0667 262 TYR A CA 2084 C C . TYR A 263 ? 1.7373 1.5861 1.8924 -0.0195 0.0832 0.0796 262 TYR A C 2085 O O . TYR A 263 ? 1.6835 1.5430 1.8512 -0.0125 0.0705 0.0790 262 TYR A O 2086 C CB . TYR A 263 ? 1.7271 1.6316 1.9166 -0.0309 0.0739 0.0648 262 TYR A CB 2087 C CG . TYR A 263 ? 1.6715 1.6101 1.8973 -0.0433 0.0736 0.0515 262 TYR A CG 2088 C CD1 . TYR A 263 ? 1.6156 1.5750 1.8770 -0.0525 0.0708 0.0407 262 TYR A CD1 2089 C CD2 . TYR A 263 ? 1.6533 1.6024 1.8758 -0.0442 0.0750 0.0496 262 TYR A CD2 2090 C CE1 . TYR A 263 ? 1.5526 1.5432 1.8460 -0.0613 0.0684 0.0291 262 TYR A CE1 2091 C CE2 . TYR A 263 ? 1.5851 1.5648 1.8408 -0.0530 0.0745 0.0380 262 TYR A CE2 2092 C CZ . TYR A 263 ? 1.5401 1.5411 1.8317 -0.0610 0.0705 0.0282 262 TYR A CZ 2093 O OH . TYR A 263 ? 1.4923 1.5237 1.8161 -0.0675 0.0682 0.0172 262 TYR A OH 2094 N N . ARG A 264 ? 1.7873 1.6002 1.9014 -0.0117 0.0925 0.0915 263 ARG A N 2095 C CA . ARG A 264 ? 1.8509 1.6377 1.9354 0.0066 0.0859 0.1045 263 ARG A CA 2096 C C . ARG A 264 ? 1.8889 1.6567 1.9810 0.0039 0.0953 0.1040 263 ARG A C 2097 O O . ARG A 264 ? 1.8557 1.6277 1.9518 0.0168 0.0825 0.1072 263 ARG A O 2098 C CB . ARG A 264 ? 1.9222 1.6684 1.9558 0.0159 0.0952 0.1178 263 ARG A CB 2099 C CG . ARG A 264 ? 1.9951 1.7231 1.9985 0.0396 0.0804 0.1314 263 ARG A CG 2100 C CD . ARG A 264 ? 2.1515 1.8457 2.1019 0.0512 0.0827 0.1437 263 ARG A CD 2101 N NE . ARG A 264 ? 2.3482 1.9923 2.2662 0.0439 0.1123 0.1499 263 ARG A NE 2102 C CZ . ARG A 264 ? 2.4588 2.0593 2.3500 0.0519 0.1241 0.1603 263 ARG A CZ 2103 N NH1 . ARG A 264 ? 2.4994 2.1009 2.3929 0.0691 0.1085 0.1662 263 ARG A NH1 2104 N NH2 . ARG A 264 ? 2.5060 2.0600 2.3679 0.0427 0.1535 0.1650 263 ARG A NH2 2105 N N . LYS A 265 ? 1.9763 1.7236 2.0719 -0.0132 0.1184 0.0990 264 LYS A N 2106 C CA . LYS A 265 ? 2.0164 1.7448 2.1213 -0.0202 0.1293 0.0952 264 LYS A CA 2107 C C . LYS A 265 ? 1.9128 1.6776 2.0557 -0.0224 0.1131 0.0840 264 LYS A C 2108 O O . LYS A 265 ? 1.8530 1.6064 1.9943 -0.0145 0.1100 0.0859 264 LYS A O 2109 C CB . LYS A 265 ? 2.0848 1.7968 2.1987 -0.0434 0.1549 0.0870 264 LYS A CB 2110 C CG . LYS A 265 ? 2.2137 1.8743 2.2869 -0.0442 0.1796 0.0980 264 LYS A CG 2111 C CD . LYS A 265 ? 2.2948 1.9426 2.3863 -0.0698 0.2056 0.0874 264 LYS A CD 2112 C CE . LYS A 265 ? 2.4519 2.0456 2.5023 -0.0726 0.2343 0.0983 264 LYS A CE 2113 N NZ . LYS A 265 ? 2.4975 2.0798 2.5702 -0.0996 0.2617 0.0869 264 LYS A NZ 2114 N N . PHE A 266 ? 1.8278 1.6334 2.0024 -0.0327 0.1045 0.0724 265 PHE A N 2115 C CA . PHE A 266 ? 1.7927 1.6322 2.0005 -0.0355 0.0896 0.0614 265 PHE A CA 2116 C C . PHE A 266 ? 1.7978 1.6454 2.0005 -0.0160 0.0720 0.0684 265 PHE A C 2117 O O . PHE A 266 ? 1.7751 1.6197 1.9853 -0.0132 0.0695 0.0657 265 PHE A O 2118 C CB . PHE A 266 ? 1.7644 1.6444 2.0001 -0.0448 0.0814 0.0511 265 PHE A CB 2119 C CG . PHE A 266 ? 1.7508 1.6643 2.0144 -0.0446 0.0643 0.0417 265 PHE A CG 2120 C CD1 . PHE A 266 ? 1.7802 1.6996 2.0658 -0.0574 0.0663 0.0292 265 PHE A CD1 2121 C CD2 . PHE A 266 ? 1.7181 1.6555 1.9843 -0.0321 0.0464 0.0448 265 PHE A CD2 2122 C CE1 . PHE A 266 ? 1.7492 1.6951 2.0544 -0.0561 0.0509 0.0212 265 PHE A CE1 2123 C CE2 . PHE A 266 ? 1.6904 1.6543 1.9788 -0.0319 0.0332 0.0368 265 PHE A CE2 2124 C CZ . PHE A 266 ? 1.6989 1.6657 2.0045 -0.0432 0.0355 0.0256 265 PHE A CZ 2125 N N . PHE A 267 ? 1.8452 1.7024 2.0351 -0.0027 0.0605 0.0768 266 PHE A N 2126 C CA . PHE A 267 ? 1.8978 1.7688 2.0889 0.0151 0.0428 0.0825 266 PHE A CA 2127 C C . PHE A 267 ? 1.9397 1.7786 2.1109 0.0291 0.0474 0.0925 266 PHE A C 2128 O O . PHE A 267 ? 1.9427 1.7911 2.1262 0.0388 0.0392 0.0925 266 PHE A O 2129 C CB . PHE A 267 ? 1.9433 1.8307 2.1248 0.0250 0.0287 0.0883 266 PHE A CB 2130 C CG . PHE A 267 ? 1.9220 1.8480 2.1289 0.0168 0.0182 0.0784 266 PHE A CG 2131 C CD1 . PHE A 267 ? 1.9200 1.8741 2.1550 0.0166 0.0075 0.0712 266 PHE A CD1 2132 C CD2 . PHE A 267 ? 1.9107 1.8419 2.1108 0.0101 0.0203 0.0766 266 PHE A CD2 2133 C CE1 . PHE A 267 ? 1.8950 1.8803 2.1501 0.0100 -0.0012 0.0629 266 PHE A CE1 2134 C CE2 . PHE A 267 ? 1.8670 1.8309 2.0890 0.0039 0.0113 0.0678 266 PHE A CE2 2135 C CZ . PHE A 267 ? 1.8648 1.8552 2.1139 0.0040 0.0002 0.0612 266 PHE A CZ 2136 N N . GLN A 268 ? 1.9893 1.7885 2.1290 0.0310 0.0619 0.1013 267 GLN A N 2137 C CA . GLN A 268 ? 2.0372 1.7998 2.1546 0.0449 0.0685 0.1114 267 GLN A CA 2138 C C . GLN A 268 ? 2.0128 1.7646 2.1453 0.0353 0.0793 0.1028 267 GLN A C 2139 O O . GLN A 268 ? 2.0280 1.7730 2.1614 0.0483 0.0760 0.1060 267 GLN A O 2140 C CB . GLN A 268 ? 2.1235 1.8406 2.1991 0.0484 0.0836 0.1231 267 GLN A CB 2141 C CG . GLN A 268 ? 2.1796 1.9000 2.2309 0.0642 0.0700 0.1340 267 GLN A CG 2142 C CD . GLN A 268 ? 2.3145 1.9844 2.3170 0.0702 0.0850 0.1470 267 GLN A CD 2143 O OE1 . GLN A 268 ? 2.4124 2.0421 2.3991 0.0629 0.1073 0.1490 267 GLN A OE1 2144 N NE2 . GLN A 268 ? 2.3613 2.0305 2.3371 0.0831 0.0731 0.1557 267 GLN A NE2 2145 N N . ASP A 269 ? 1.9772 1.7291 2.1229 0.0128 0.0913 0.0910 268 ASP A N 2146 C CA . ASP A 269 ? 1.9860 1.7236 2.1426 0.0008 0.1019 0.0811 268 ASP A CA 2147 C C . ASP A 269 ? 1.9289 1.6972 2.1124 0.0023 0.0880 0.0716 268 ASP A C 2148 O O . ASP A 269 ? 1.9601 1.7104 2.1430 0.0023 0.0936 0.0677 268 ASP A O 2149 C CB . ASP A 269 ? 2.0099 1.7437 2.1771 -0.0245 0.1167 0.0697 268 ASP A CB 2150 C CG . ASP A 269 ? 2.0931 1.7838 2.2308 -0.0286 0.1382 0.0782 268 ASP A CG 2151 O OD1 . ASP A 269 ? 2.1644 1.8324 2.2703 -0.0108 0.1385 0.0938 268 ASP A OD1 2152 O OD2 . ASP A 269 ? 2.1209 1.8000 2.2670 -0.0497 0.1550 0.0692 268 ASP A OD2 2153 N N . ILE A 270 ? 1.8700 1.6807 2.0741 0.0033 0.0714 0.0679 269 ILE A N 2154 C CA . ILE A 270 ? 1.8231 1.6614 2.0495 0.0055 0.0592 0.0600 269 ILE A CA 2155 C C . ILE A 270 ? 1.8279 1.6732 2.0525 0.0276 0.0490 0.0696 269 ILE A C 2156 O O . ILE A 270 ? 1.7417 1.6059 1.9826 0.0311 0.0417 0.0645 269 ILE A O 2157 C CB . ILE A 270 ? 1.7406 1.6191 1.9916 -0.0055 0.0479 0.0498 269 ILE A CB 2158 C CG1 . ILE A 270 ? 1.7114 1.6119 1.9617 0.0019 0.0375 0.0568 269 ILE A CG1 2159 C CG2 . ILE A 270 ? 1.7324 1.6084 1.9923 -0.0267 0.0571 0.0384 269 ILE A CG2 2160 C CD1 . ILE A 270 ? 1.6802 1.6141 1.9474 0.0105 0.0210 0.0557 269 ILE A CD1 2161 N N . GLY A 271 ? 1.8752 1.7050 2.0799 0.0426 0.0488 0.0831 270 GLY A N 2162 C CA . GLY A 271 ? 1.8962 1.7327 2.1014 0.0649 0.0389 0.0925 270 GLY A CA 2163 C C . GLY A 271 ? 1.8627 1.7424 2.0878 0.0702 0.0202 0.0922 270 GLY A C 2164 O O . GLY A 271 ? 1.8582 1.7579 2.1012 0.0808 0.0121 0.0922 270 GLY A O 2165 N N . PHE A 272 ? 1.8240 1.7170 2.0463 0.0624 0.0148 0.0914 271 PHE A N 2166 C CA . PHE A 272 ? 1.7396 1.6700 1.9776 0.0659 -0.0022 0.0905 271 PHE A CA 2167 C C . PHE A 272 ? 1.7046 1.6304 1.9213 0.0681 -0.0070 0.0972 271 PHE A C 2168 O O . PHE A 272 ? 1.6067 1.5444 1.8252 0.0559 -0.0077 0.0916 271 PHE A O 2169 C CB . PHE A 272 ? 1.7062 1.6640 1.9682 0.0503 -0.0048 0.0776 271 PHE A CB 2170 C CG . PHE A 272 ? 1.7243 1.7183 2.0048 0.0536 -0.0204 0.0757 271 PHE A CG 2171 C CD1 . PHE A 272 ? 1.7610 1.7709 2.0565 0.0668 -0.0288 0.0787 271 PHE A CD1 2172 C CD2 . PHE A 272 ? 1.7074 1.7192 1.9921 0.0431 -0.0255 0.0703 271 PHE A CD2 2173 C CE1 . PHE A 272 ? 1.7298 1.7723 2.0443 0.0677 -0.0418 0.0760 271 PHE A CE1 2174 C CE2 . PHE A 272 ? 1.6773 1.7189 1.9776 0.0450 -0.0387 0.0680 271 PHE A CE2 2175 C CZ . PHE A 272 ? 1.6739 1.7308 1.9894 0.0564 -0.0469 0.0706 271 PHE A CZ 2176 N N . GLU A 273 ? 1.7649 1.6719 1.9597 0.0852 -0.0102 0.1092 272 GLU A N 2177 C CA . GLU A 273 ? 1.8395 1.7355 2.0058 0.0900 -0.0151 0.1168 272 GLU A CA 2178 C C . GLU A 273 ? 1.7548 1.6870 1.9336 0.0892 -0.0334 0.1127 272 GLU A C 2179 O O . GLU A 273 ? 1.7376 1.6648 1.8968 0.0846 -0.0343 0.1133 272 GLU A O 2180 C CB . GLU A 273 ? 1.9743 1.8427 2.1129 0.1118 -0.0180 0.1310 272 GLU A CB 2181 C CG . GLU A 273 ? 2.1203 1.9433 2.2374 0.1127 0.0024 0.1365 272 GLU A CG 2182 C CD . GLU A 273 ? 2.2634 2.0504 2.3423 0.1340 0.0016 0.1523 272 GLU A CD 2183 O OE1 . GLU A 273 ? 2.3563 2.1332 2.4059 0.1385 -0.0040 0.1587 272 GLU A OE1 2184 O OE2 . GLU A 273 ? 2.3061 2.0721 2.3812 0.1472 0.0071 0.1584 272 GLU A OE2 2185 N N . ASP A 274 ? 1.6934 1.6599 1.9041 0.0929 -0.0460 0.1080 273 ASP A N 2186 C CA . ASP A 274 ? 1.6437 1.6446 1.8700 0.0902 -0.0624 0.1026 273 ASP A CA 2187 C C . ASP A 274 ? 1.5939 1.6008 1.8208 0.0716 -0.0565 0.0936 273 ASP A C 2188 O O . ASP A 274 ? 1.5626 1.5808 1.7830 0.0691 -0.0657 0.0917 273 ASP A O 2189 C CB . ASP A 274 ? 1.6432 1.6773 1.9076 0.0928 -0.0706 0.0972 273 ASP A CB 2190 C CG . ASP A 274 ? 1.7062 1.7419 1.9775 0.1126 -0.0778 0.1051 273 ASP A CG 2191 O OD1 . ASP A 274 ? 1.8112 1.8162 2.0620 0.1224 -0.0694 0.1134 273 ASP A OD1 2192 O OD2 . ASP A 274 ? 1.7108 1.7783 2.0096 0.1183 -0.0910 0.1027 273 ASP A OD2 2193 N N . GLY A 275 ? 1.5897 1.5894 1.8249 0.0590 -0.0416 0.0876 274 GLY A N 2194 C CA . GLY A 275 ? 1.5919 1.5998 1.8328 0.0427 -0.0359 0.0787 274 GLY A CA 2195 C C . GLY A 275 ? 1.6385 1.6271 1.8511 0.0390 -0.0293 0.0819 274 GLY A C 2196 O O . GLY A 275 ? 1.6770 1.6781 1.8918 0.0308 -0.0308 0.0762 274 GLY A O 2197 N N . TRP A 276 ? 1.6761 1.6314 1.8602 0.0454 -0.0204 0.0912 275 TRP A N 2198 C CA . TRP A 276 ? 1.7174 1.6477 1.8681 0.0435 -0.0117 0.0959 275 TRP A CA 2199 C C . TRP A 276 ? 1.6887 1.6292 1.8236 0.0522 -0.0288 0.0987 275 TRP A C 2200 O O . TRP A 276 ? 1.6788 1.6176 1.8002 0.0456 -0.0258 0.0958 275 TRP A O 2201 C CB . TRP A 276 ? 1.7963 1.6845 1.9162 0.0508 0.0012 0.1068 275 TRP A CB 2202 C CG . TRP A 276 ? 1.8587 1.7136 1.9367 0.0514 0.0121 0.1141 275 TRP A CG 2203 C CD1 . TRP A 276 ? 1.9323 1.7553 1.9693 0.0673 0.0099 0.1271 275 TRP A CD1 2204 C CD2 . TRP A 276 ? 1.8687 1.7167 1.9402 0.0364 0.0280 0.1090 275 TRP A CD2 2205 N NE1 . TRP A 276 ? 1.9709 1.7648 1.9723 0.0626 0.0242 0.1307 275 TRP A NE1 2206 C CE2 . TRP A 276 ? 1.9202 1.7297 1.9438 0.0433 0.0365 0.1195 275 TRP A CE2 2207 C CE3 . TRP A 276 ? 1.8538 1.7243 1.9551 0.0189 0.0360 0.0966 275 TRP A CE3 2208 C CZ2 . TRP A 276 ? 1.9319 1.7243 1.9373 0.0323 0.0551 0.1178 275 TRP A CZ2 2209 C CZ3 . TRP A 276 ? 1.8818 1.7388 1.9692 0.0086 0.0531 0.0947 275 TRP A CZ3 2210 C CH2 . TRP A 276 ? 1.9078 1.7259 1.9480 0.0148 0.0637 0.1051 275 TRP A CH2 2211 N N . LEU A 277 ? 1.6850 1.6375 1.8239 0.0668 -0.0468 0.1032 276 LEU A N 2212 C CA . LEU A 277 ? 1.6956 1.6614 1.8236 0.0751 -0.0667 0.1043 276 LEU A CA 2213 C C . LEU A 277 ? 1.6264 1.6241 1.7789 0.0628 -0.0730 0.0924 276 LEU A C 2214 O O . LEU A 277 ? 1.5962 1.5935 1.7305 0.0605 -0.0785 0.0903 276 LEU A O 2215 C CB . LEU A 277 ? 1.7304 1.7087 1.8678 0.0927 -0.0851 0.1100 276 LEU A CB 2216 C CG . LEU A 277 ? 1.7962 1.7432 1.9115 0.1081 -0.0800 0.1225 276 LEU A CG 2217 C CD1 . LEU A 277 ? 1.8082 1.7761 1.9445 0.1254 -0.0980 0.1261 276 LEU A CD1 2218 C CD2 . LEU A 277 ? 1.8370 1.7456 1.8997 0.1158 -0.0773 0.1323 276 LEU A CD2 2219 N N . MET A 278 ? 1.5459 1.5673 1.7360 0.0552 -0.0711 0.0849 277 MET A N 2220 C CA . MET A 278 ? 1.5441 1.5916 1.7568 0.0437 -0.0743 0.0741 277 MET A CA 2221 C C . MET A 278 ? 1.5665 1.6026 1.7651 0.0322 -0.0614 0.0699 277 MET A C 2222 O O . MET A 278 ? 1.6052 1.6510 1.8006 0.0280 -0.0669 0.0646 277 MET A O 2223 C CB . MET A 278 ? 1.5561 1.6217 1.8041 0.0380 -0.0703 0.0681 277 MET A CB 2224 C CG . MET A 278 ? 1.6062 1.6909 1.8766 0.0469 -0.0819 0.0693 277 MET A CG 2225 S SD . MET A 278 ? 1.7178 1.8168 2.0211 0.0398 -0.0742 0.0620 277 MET A SD 2226 C CE . MET A 278 ? 1.7110 1.8324 2.0387 0.0511 -0.0864 0.0639 277 MET A CE 2227 N N . ARG A 279 ? 1.5900 1.6059 1.7822 0.0268 -0.0433 0.0715 278 ARG A N 2228 C CA . ARG A 279 ? 1.6315 1.6382 1.8158 0.0158 -0.0283 0.0672 278 ARG A CA 2229 C C . ARG A 279 ? 1.6379 1.6247 1.7837 0.0200 -0.0282 0.0719 278 ARG A C 2230 O O . ARG A 279 ? 1.7053 1.6966 1.8471 0.0139 -0.0254 0.0662 278 ARG A O 2231 C CB . ARG A 279 ? 1.6992 1.6876 1.8860 0.0086 -0.0086 0.0678 278 ARG A CB 2232 C CG . ARG A 279 ? 1.7319 1.7129 1.9163 -0.0033 0.0092 0.0629 278 ARG A CG 2233 C CD . ARG A 279 ? 1.6746 1.6856 1.8895 -0.0118 0.0065 0.0515 278 ARG A CD 2234 N NE . ARG A 279 ? 1.6796 1.6868 1.8999 -0.0227 0.0248 0.0463 278 ARG A NE 2235 C CZ . ARG A 279 ? 1.6652 1.6956 1.9124 -0.0299 0.0260 0.0365 278 ARG A CZ 2236 N NH1 . ARG A 279 ? 1.6601 1.7156 1.9271 -0.0276 0.0105 0.0313 278 ARG A NH1 2237 N NH2 . ARG A 279 ? 1.6731 1.7009 1.9279 -0.0389 0.0437 0.0319 278 ARG A NH2 2238 N N . GLN A 280 ? 1.6266 1.5893 1.7415 0.0316 -0.0312 0.0824 279 GLN A N 2239 C CA . GLN A 280 ? 1.6816 1.6215 1.7530 0.0377 -0.0334 0.0876 279 GLN A CA 2240 C C . GLN A 280 ? 1.6607 1.6222 1.7329 0.0396 -0.0533 0.0818 279 GLN A C 2241 O O . GLN A 280 ? 1.7107 1.6608 1.7568 0.0371 -0.0506 0.0796 279 GLN A O 2242 C CB . GLN A 280 ? 1.7879 1.6990 1.8255 0.0529 -0.0374 0.1006 279 GLN A CB 2243 C CG . GLN A 280 ? 1.8755 1.7522 1.8973 0.0503 -0.0134 0.1073 279 GLN A CG 2244 C CD . GLN A 280 ? 1.9760 1.8221 1.9646 0.0672 -0.0174 0.1209 279 GLN A CD 2245 O OE1 . GLN A 280 ? 1.9822 1.8427 1.9843 0.0793 -0.0349 0.1241 279 GLN A OE1 2246 N NE2 . GLN A 280 ? 2.0742 1.8765 2.0188 0.0690 0.0000 0.1295 279 GLN A NE2 2247 N N . ASP A 281 ? 1.6257 1.6170 1.7277 0.0432 -0.0717 0.0787 280 ASP A N 2248 C CA . ASP A 281 ? 1.6406 1.6546 1.7491 0.0428 -0.0905 0.0717 280 ASP A CA 2249 C C . ASP A 281 ? 1.6109 1.6349 1.7307 0.0296 -0.0822 0.0612 280 ASP A C 2250 O O . ASP A 281 ? 1.5703 1.5946 1.6743 0.0280 -0.0899 0.0564 280 ASP A O 2251 C CB . ASP A 281 ? 1.6397 1.6856 1.7864 0.0464 -0.1068 0.0692 280 ASP A CB 2252 C CG . ASP A 281 ? 1.6662 1.7081 1.8062 0.0619 -0.1190 0.0785 280 ASP A CG 2253 O OD1 . ASP A 281 ? 1.7085 1.7294 1.8107 0.0718 -0.1263 0.0852 280 ASP A OD1 2254 O OD2 . ASP A 281 ? 1.6367 1.6955 1.8080 0.0653 -0.1213 0.0793 280 ASP A OD2 2255 N N . THR A 282 ? 1.6342 1.6659 1.7809 0.0209 -0.0673 0.0574 281 THR A N 2256 C CA . THR A 282 ? 1.6565 1.7054 1.8244 0.0108 -0.0634 0.0473 281 THR A CA 2257 C C . THR A 282 ? 1.6907 1.7270 1.8516 0.0030 -0.0429 0.0442 281 THR A C 2258 O O . THR A 282 ? 1.6341 1.6800 1.8032 -0.0025 -0.0407 0.0364 281 THR A O 2259 C CB . THR A 282 ? 1.6421 1.7166 1.8511 0.0076 -0.0669 0.0430 281 THR A CB 2260 O OG1 . THR A 282 ? 1.7291 1.8191 1.9542 0.0006 -0.0672 0.0339 281 THR A OG1 2261 C CG2 . THR A 282 ? 1.6330 1.7023 1.8556 0.0048 -0.0529 0.0450 281 THR A CG2 2262 N N . GLU A 283 ? 1.7989 1.8132 1.9455 0.0026 -0.0270 0.0499 282 GLU A N 2263 C CA . GLU A 283 ? 1.8705 1.8772 2.0196 -0.0061 -0.0053 0.0462 282 GLU A CA 2264 C C . GLU A 283 ? 1.8414 1.8358 1.9638 -0.0070 0.0004 0.0433 282 GLU A C 2265 O O . GLU A 283 ? 1.8294 1.8276 1.9638 -0.0140 0.0155 0.0372 282 GLU A O 2266 C CB . GLU A 283 ? 1.9976 1.9817 2.1383 -0.0082 0.0125 0.0524 282 GLU A CB 2267 C CG . GLU A 283 ? 2.1319 2.0792 2.2241 -0.0014 0.0187 0.0625 282 GLU A CG 2268 C CD . GLU A 283 ? 2.2402 2.1623 2.3255 -0.0065 0.0420 0.0674 282 GLU A CD 2269 O OE1 . GLU A 283 ? 2.2328 2.1632 2.3457 -0.0106 0.0448 0.0664 282 GLU A OE1 2270 O OE2 . GLU A 283 ? 2.3852 2.2770 2.4357 -0.0069 0.0587 0.0718 282 GLU A OE2 2271 N N . GLY A 284 ? 1.8256 1.8058 1.9123 0.0004 -0.0118 0.0471 283 GLY A N 2272 C CA . GLY A 284 ? 1.8784 1.8424 1.9328 0.0001 -0.0073 0.0440 283 GLY A CA 2273 C C . GLY A 284 ? 1.8857 1.8682 1.9488 -0.0012 -0.0219 0.0349 283 GLY A C 2274 O O . GLY A 284 ? 1.9606 1.9282 1.9950 -0.0014 -0.0189 0.0313 283 GLY A O 2275 N N . LEU A 285 ? 1.8350 1.8466 1.9350 -0.0025 -0.0358 0.0309 284 LEU A N 2276 C CA . LEU A 285 ? 1.7995 1.8262 1.9071 -0.0043 -0.0501 0.0228 284 LEU A CA 2277 C C . LEU A 285 ? 1.7705 1.7957 1.8798 -0.0097 -0.0371 0.0145 284 LEU A C 2278 O O . LEU A 285 ? 1.7867 1.8022 1.8727 -0.0100 -0.0416 0.0095 284 LEU A O 2279 C CB . LEU A 285 ? 1.7303 1.7859 1.8781 -0.0054 -0.0628 0.0206 284 LEU A CB 2280 C CG . LEU A 285 ? 1.7500 1.8131 1.8983 0.0006 -0.0823 0.0253 284 LEU A CG 2281 C CD1 . LEU A 285 ? 1.7149 1.8046 1.9044 -0.0011 -0.0889 0.0231 284 LEU A CD1 2282 C CD2 . LEU A 285 ? 1.7989 1.8578 1.9225 0.0026 -0.0992 0.0220 284 LEU A CD2 2283 N N . VAL A 286 ? 1.7348 1.7697 1.8722 -0.0136 -0.0216 0.0127 285 VAL A N 2284 C CA . VAL A 286 ? 1.7691 1.8060 1.9147 -0.0169 -0.0087 0.0051 285 VAL A CA 2285 C C . VAL A 286 ? 1.8916 1.9072 2.0166 -0.0177 0.0139 0.0069 285 VAL A C 2286 O O . VAL A 286 ? 1.9766 1.9897 2.1100 -0.0195 0.0259 0.0116 285 VAL A O 2287 C CB . VAL A 286 ? 1.6978 1.7606 1.8890 -0.0194 -0.0066 0.0012 285 VAL A CB 2288 C CG1 . VAL A 286 ? 1.6884 1.7547 1.8893 -0.0202 0.0043 -0.0065 285 VAL A CG1 2289 C CG2 . VAL A 286 ? 1.6802 1.7605 1.8894 -0.0187 -0.0259 0.0007 285 VAL A CG2 2290 N N . GLU A 287 ? 1.9873 1.9856 2.0845 -0.0171 0.0214 0.0027 286 GLU A N 2291 C CA . GLU A 287 ? 2.0847 2.0616 2.1625 -0.0181 0.0466 0.0035 286 GLU A CA 2292 C C . GLU A 287 ? 2.0799 2.0773 2.2021 -0.0220 0.0640 -0.0009 286 GLU A C 2293 O O . GLU A 287 ? 1.9800 1.9934 2.1250 -0.0214 0.0632 -0.0082 286 GLU A O 2294 C CB . GLU A 287 ? 2.1574 2.1104 2.1947 -0.0161 0.0509 -0.0010 286 GLU A CB 2295 C CG . GLU A 287 ? 2.2438 2.1724 2.2308 -0.0122 0.0350 0.0030 286 GLU A CG 2296 C CD . GLU A 287 ? 2.3363 2.2422 2.2831 -0.0110 0.0352 -0.0037 286 GLU A CD 2297 O OE1 . GLU A 287 ? 2.3081 2.2266 2.2714 -0.0129 0.0294 -0.0125 286 GLU A OE1 2298 O OE2 . GLU A 287 ? 2.4461 2.3185 2.3415 -0.0080 0.0414 -0.0004 286 GLU A OE2 2299 N N . ALA A 288 ? 2.1469 2.1428 2.2808 -0.0256 0.0795 0.0032 287 ALA A N 2300 C CA . ALA A 288 ? 2.1272 2.1478 2.3099 -0.0302 0.0922 -0.0015 287 ALA A CA 2301 C C . ALA A 288 ? 2.0688 2.0962 2.2661 -0.0295 0.1079 -0.0097 287 ALA A C 2302 O O . ALA A 288 ? 1.9740 2.0298 2.2141 -0.0293 0.1055 -0.0158 287 ALA A O 2303 C CB . ALA A 288 ? 2.1880 2.1990 2.3739 -0.0360 0.1097 0.0035 287 ALA A CB 2304 N N . THR A 289 ? 2.0666 2.0667 2.2266 -0.0280 0.1235 -0.0097 288 THR A N 2305 C CA . THR A 289 ? 2.0533 2.0554 2.2248 -0.0269 0.1445 -0.0168 288 THR A CA 2306 C C . THR A 289 ? 2.0701 2.0695 2.2287 -0.0206 0.1359 -0.0230 288 THR A C 2307 O O . THR A 289 ? 2.1302 2.1403 2.3116 -0.0178 0.1485 -0.0299 288 THR A O 2308 C CB . THR A 289 ? 2.0656 2.0362 2.2041 -0.0292 0.1734 -0.0139 288 THR A CB 2309 O OG1 . THR A 289 ? 2.0701 2.0044 2.1468 -0.0265 0.1659 -0.0076 288 THR A OG1 2310 C CG2 . THR A 289 ? 2.0389 2.0155 2.2030 -0.0371 0.1902 -0.0105 288 THR A CG2 2311 N N . MET A 290 ? 2.0397 2.0253 2.1642 -0.0185 0.1147 -0.0212 289 MET A N 2312 C CA . MET A 290 ? 2.0026 1.9810 2.1105 -0.0145 0.1065 -0.0277 289 MET A CA 2313 C C . MET A 290 ? 1.8432 1.8519 1.9957 -0.0122 0.0951 -0.0328 289 MET A C 2314 O O . MET A 290 ? 1.7627 1.7897 1.9351 -0.0136 0.0761 -0.0302 289 MET A O 2315 C CB . MET A 290 ? 2.1118 2.0709 2.1764 -0.0146 0.0848 -0.0253 289 MET A CB 2316 C CG . MET A 290 ? 2.2849 2.2092 2.2960 -0.0145 0.0926 -0.0202 289 MET A CG 2317 S SD . MET A 290 ? 2.5948 2.4860 2.5689 -0.0123 0.1225 -0.0253 289 MET A SD 2318 C CE . MET A 290 ? 2.6107 2.4943 2.5661 -0.0102 0.1070 -0.0356 289 MET A CE 2319 N N . PRO A 291 ? 1.7884 1.8004 1.9547 -0.0076 0.1075 -0.0397 290 PRO A N 2320 C CA . PRO A 291 ? 1.7245 1.7604 1.9271 -0.0033 0.0964 -0.0438 290 PRO A CA 2321 C C . PRO A 291 ? 1.6920 1.7174 1.8725 -0.0032 0.0762 -0.0457 290 PRO A C 2322 O O . PRO A 291 ? 1.7217 1.7217 1.8597 -0.0058 0.0726 -0.0462 290 PRO A O 2323 C CB . PRO A 291 ? 1.7471 1.7847 1.9653 0.0032 0.1174 -0.0502 290 PRO A CB 2324 C CG . PRO A 291 ? 1.7985 1.8155 1.9928 0.0010 0.1418 -0.0496 290 PRO A CG 2325 C CD . PRO A 291 ? 1.8240 1.8162 1.9720 -0.0048 0.1331 -0.0437 290 PRO A CD 2326 N N . PRO A 292 ? 1.6268 1.6706 1.8351 -0.0005 0.0632 -0.0472 291 PRO A N 2327 C CA . PRO A 292 ? 1.6327 1.6663 1.8233 -0.0018 0.0466 -0.0495 291 PRO A CA 2328 C C . PRO A 292 ? 1.6765 1.6845 1.8388 0.0007 0.0547 -0.0567 291 PRO A C 2329 O O . PRO A 292 ? 1.6885 1.6801 1.8246 -0.0035 0.0431 -0.0597 291 PRO A O 2330 C CB . PRO A 292 ? 1.5864 1.6431 1.8137 0.0015 0.0361 -0.0489 291 PRO A CB 2331 C CG . PRO A 292 ? 1.5674 1.6433 1.8289 0.0076 0.0488 -0.0493 291 PRO A CG 2332 C CD . PRO A 292 ? 1.5767 1.6503 1.8321 0.0034 0.0624 -0.0468 291 PRO A CD 2333 N N . GLY A 293 ? 1.7184 1.7228 1.8871 0.0074 0.0749 -0.0601 292 GLY A N 2334 C CA . GLY A 293 ? 1.7630 1.7395 1.9022 0.0108 0.0862 -0.0672 292 GLY A CA 2335 C C . GLY A 293 ? 1.7238 1.6981 1.8726 0.0162 0.0809 -0.0717 292 GLY A C 2336 O O . GLY A 293 ? 1.7057 1.6525 1.8237 0.0159 0.0835 -0.0779 292 GLY A O 2337 N N . VAL A 294 ? 1.6914 1.6919 1.8800 0.0211 0.0736 -0.0686 293 VAL A N 2338 C CA . VAL A 294 ? 1.7089 1.7064 1.9071 0.0283 0.0695 -0.0713 293 VAL A CA 2339 C C . VAL A 294 ? 1.7002 1.7244 1.9419 0.0402 0.0740 -0.0694 293 VAL A C 2340 O O . VAL A 294 ? 1.6703 1.7194 1.9386 0.0398 0.0761 -0.0663 293 VAL A O 2341 C CB . VAL A 294 ? 1.6762 1.6739 1.8711 0.0211 0.0488 -0.0692 293 VAL A CB 2342 C CG1 . VAL A 294 ? 1.7251 1.6983 1.8809 0.0098 0.0423 -0.0730 293 VAL A CG1 2343 C CG2 . VAL A 294 ? 1.6321 1.6588 1.8540 0.0177 0.0366 -0.0622 293 VAL A CG2 2344 N N . GLN A 295 ? 1.7709 1.7888 2.0190 0.0509 0.0749 -0.0717 294 GLN A N 2345 C CA . GLN A 295 ? 1.8026 1.8458 2.0910 0.0646 0.0757 -0.0703 294 GLN A CA 2346 C C . GLN A 295 ? 1.7572 1.8274 2.0700 0.0607 0.0582 -0.0647 294 GLN A C 2347 O O . GLN A 295 ? 1.7201 1.7831 2.0207 0.0550 0.0439 -0.0619 294 GLN A O 2348 C CB . GLN A 295 ? 1.8579 1.8847 2.1422 0.0777 0.0762 -0.0722 294 GLN A CB 2349 C CG . GLN A 295 ? 1.8651 1.9169 2.1892 0.0952 0.0772 -0.0714 294 GLN A CG 2350 C CD . GLN A 295 ? 1.9086 1.9427 2.2263 0.1096 0.0738 -0.0711 294 GLN A CD 2351 O OE1 . GLN A 295 ? 1.8939 1.9472 2.2390 0.1234 0.0659 -0.0686 294 GLN A OE1 2352 N NE2 . GLN A 295 ? 1.9607 1.9565 2.2406 0.1065 0.0792 -0.0738 294 GLN A NE2 2353 N N . LEU A 296 ? 1.7449 1.8452 2.0926 0.0631 0.0606 -0.0638 295 LEU A N 2354 C CA . LEU A 296 ? 1.7094 1.8338 2.0778 0.0573 0.0462 -0.0596 295 LEU A CA 2355 C C . LEU A 296 ? 1.6514 1.8045 2.0603 0.0692 0.0406 -0.0602 295 LEU A C 2356 O O . LEU A 296 ? 1.6272 1.7955 2.0620 0.0775 0.0520 -0.0641 295 LEU A O 2357 C CB . LEU A 296 ? 1.7336 1.8658 2.1032 0.0455 0.0531 -0.0585 295 LEU A CB 2358 C CG . LEU A 296 ? 1.7446 1.9005 2.1365 0.0388 0.0418 -0.0549 295 LEU A CG 2359 C CD1 . LEU A 296 ? 1.7283 1.8779 2.1061 0.0348 0.0231 -0.0507 295 LEU A CD1 2360 C CD2 . LEU A 296 ? 1.8013 1.9564 2.1873 0.0278 0.0524 -0.0535 295 LEU A CD2 2361 N N . HIS A 297 ? 1.6093 1.7695 2.0232 0.0701 0.0228 -0.0568 296 HIS A N 2362 C CA . HIS A 297 ? 1.5823 1.7697 2.0308 0.0803 0.0128 -0.0575 296 HIS A CA 2363 C C . HIS A 297 ? 1.5069 1.7116 1.9667 0.0694 0.0014 -0.0552 296 HIS A C 2364 O O . HIS A 297 ? 1.4710 1.6642 1.9113 0.0638 -0.0094 -0.0510 296 HIS A O 2365 C CB . HIS A 297 ? 1.6277 1.8020 2.0659 0.0939 0.0025 -0.0555 296 HIS A CB 2366 C CG . HIS A 297 ? 1.7261 1.8798 2.1517 0.1056 0.0144 -0.0577 296 HIS A CG 2367 N ND1 . HIS A 297 ? 1.7859 1.9527 2.2363 0.1236 0.0174 -0.0606 296 HIS A ND1 2368 C CD2 . HIS A 297 ? 1.7728 1.8935 2.1640 0.1019 0.0240 -0.0582 296 HIS A CD2 2369 C CE1 . HIS A 297 ? 1.8227 1.9631 2.2529 0.1313 0.0299 -0.0621 296 HIS A CE1 2370 N NE2 . HIS A 297 ? 1.8182 1.9294 2.2113 0.1175 0.0340 -0.0611 296 HIS A NE2 2371 N N . CYS A 298 ? 1.4852 1.7166 1.9773 0.0660 0.0056 -0.0584 297 CYS A N 2372 C CA . CYS A 298 ? 1.4964 1.7424 1.9997 0.0548 -0.0027 -0.0572 297 CYS A CA 2373 C C . CYS A 298 ? 1.4749 1.7462 2.0081 0.0622 -0.0184 -0.0600 297 CYS A C 2374 O O . CYS A 298 ? 1.4509 1.7486 2.0209 0.0675 -0.0162 -0.0657 297 CYS A O 2375 C CB . CYS A 298 ? 1.5382 1.7927 2.0538 0.0433 0.0128 -0.0591 297 CYS A CB 2376 S SG . CYS A 298 ? 1.6419 1.8636 2.1130 0.0324 0.0254 -0.0546 297 CYS A SG 2377 N N . LEU A 299 ? 1.4855 1.7484 2.0024 0.0627 -0.0344 -0.0562 298 LEU A N 2378 C CA . LEU A 299 ? 1.4731 1.7544 2.0089 0.0696 -0.0519 -0.0585 298 LEU A CA 2379 C C . LEU A 299 ? 1.4033 1.6946 1.9465 0.0558 -0.0574 -0.0592 298 LEU A C 2380 O O . LEU A 299 ? 1.3576 1.6312 1.8760 0.0459 -0.0562 -0.0542 298 LEU A O 2381 C CB . LEU A 299 ? 1.5256 1.7862 2.0338 0.0803 -0.0644 -0.0539 298 LEU A CB 2382 C CG . LEU A 299 ? 1.5722 1.8261 2.0786 0.0986 -0.0641 -0.0541 298 LEU A CG 2383 C CD1 . LEU A 299 ? 1.5911 1.8319 2.0897 0.0977 -0.0452 -0.0544 298 LEU A CD1 2384 C CD2 . LEU A 299 ? 1.5885 1.8162 2.0624 0.1073 -0.0746 -0.0485 298 LEU A CD2 2385 N N . TYR A 300 ? 1.3794 1.6992 1.9580 0.0556 -0.0636 -0.0659 299 TYR A N 2386 C CA . TYR A 300 ? 1.3971 1.7257 1.9846 0.0422 -0.0682 -0.0680 299 TYR A CA 2387 C C . TYR A 300 ? 1.3663 1.7161 1.9756 0.0480 -0.0878 -0.0743 299 TYR A C 2388 O O . TYR A 300 ? 1.4042 1.7767 2.0422 0.0588 -0.0936 -0.0802 299 TYR A O 2389 C CB . TYR A 300 ? 1.4370 1.7773 2.0470 0.0290 -0.0504 -0.0714 299 TYR A CB 2390 C CG . TYR A 300 ? 1.4618 1.8309 2.1144 0.0339 -0.0433 -0.0793 299 TYR A CG 2391 C CD1 . TYR A 300 ? 1.4885 1.8535 2.1411 0.0412 -0.0283 -0.0785 299 TYR A CD1 2392 C CD2 . TYR A 300 ? 1.4787 1.8796 2.1732 0.0307 -0.0512 -0.0885 299 TYR A CD2 2393 C CE1 . TYR A 300 ? 1.5027 1.8952 2.1971 0.0465 -0.0199 -0.0859 299 TYR A CE1 2394 C CE2 . TYR A 300 ? 1.4706 1.9019 2.2102 0.0350 -0.0444 -0.0965 299 TYR A CE2 2395 C CZ . TYR A 300 ? 1.4758 1.9032 2.2160 0.0434 -0.0279 -0.0949 299 TYR A CZ 2396 O OH . TYR A 300 ? 1.4796 1.9385 2.2675 0.0485 -0.0193 -0.1030 299 TYR A OH 2397 N N . GLY A 301 ? 1.3045 1.6465 1.8992 0.0415 -0.0986 -0.0735 300 GLY A N 2398 C CA . GLY A 301 ? 1.2585 1.6173 1.8684 0.0452 -0.1185 -0.0804 300 GLY A CA 2399 C C . GLY A 301 ? 1.2306 1.6163 1.8796 0.0319 -0.1165 -0.0901 300 GLY A C 2400 O O . GLY A 301 ? 1.2061 1.5864 1.8564 0.0167 -0.1009 -0.0889 300 GLY A O 2401 N N . THR A 302 ? 1.2293 1.6432 1.9099 0.0376 -0.1327 -0.0998 301 THR A N 2402 C CA . THR A 302 ? 1.2270 1.6696 1.9501 0.0240 -0.1328 -0.1113 301 THR A CA 2403 C C . THR A 302 ? 1.2316 1.6873 1.9616 0.0272 -0.1595 -0.1201 301 THR A C 2404 O O . THR A 302 ? 1.2124 1.6563 1.9155 0.0426 -0.1772 -0.1169 301 THR A O 2405 C CB . THR A 302 ? 1.2235 1.6991 1.9961 0.0258 -0.1220 -0.1181 301 THR A CB 2406 O OG1 . THR A 302 ? 1.2435 1.7389 2.0325 0.0460 -0.1392 -0.1217 301 THR A OG1 2407 C CG2 . THR A 302 ? 1.2198 1.6792 1.9806 0.0237 -0.0954 -0.1099 301 THR A CG2 2408 N N . GLY A 303 ? 1.2400 1.7177 2.0040 0.0121 -0.1615 -0.1315 302 GLY A N 2409 C CA . GLY A 303 ? 1.2650 1.7588 2.0407 0.0127 -0.1876 -0.1428 302 GLY A CA 2410 C C . GLY A 303 ? 1.2956 1.7574 2.0259 0.0077 -0.1969 -0.1400 302 GLY A C 2411 O O . GLY A 303 ? 1.3534 1.8195 2.0786 0.0120 -0.2207 -0.1477 302 GLY A O 2412 N N . VAL A 304 ? 1.2706 1.7001 1.9674 -0.0004 -0.1785 -0.1294 303 VAL A N 2413 C CA . VAL A 304 ? 1.2571 1.6546 1.9109 -0.0043 -0.1835 -0.1256 303 VAL A CA 2414 C C . VAL A 304 ? 1.2268 1.6159 1.8861 -0.0254 -0.1669 -0.1274 303 VAL A C 2415 O O . VAL A 304 ? 1.2064 1.5907 1.8706 -0.0324 -0.1450 -0.1211 303 VAL A O 2416 C CB . VAL A 304 ? 1.2472 1.6115 1.8541 0.0064 -0.1767 -0.1104 303 VAL A CB 2417 C CG1 . VAL A 304 ? 1.2439 1.5773 1.8093 0.0041 -0.1816 -0.1072 303 VAL A CG1 2418 C CG2 . VAL A 304 ? 1.2531 1.6214 1.8536 0.0271 -0.1881 -0.1072 303 VAL A CG2 2419 N N . PRO A 305 ? 1.2456 1.6293 1.9005 -0.0351 -0.1771 -0.1360 304 PRO A N 2420 C CA . PRO A 305 ? 1.2482 1.6208 1.9076 -0.0548 -0.1604 -0.1378 304 PRO A CA 2421 C C . PRO A 305 ? 1.2214 1.5608 1.8444 -0.0549 -0.1412 -0.1225 304 PRO A C 2422 O O . PRO A 305 ? 1.1789 1.4946 1.7635 -0.0457 -0.1466 -0.1148 304 PRO A O 2423 C CB . PRO A 305 ? 1.2956 1.6598 1.9435 -0.0611 -0.1773 -0.1483 304 PRO A CB 2424 C CG . PRO A 305 ? 1.3023 1.6576 1.9184 -0.0426 -0.1982 -0.1457 304 PRO A CG 2425 C CD . PRO A 305 ? 1.2821 1.6613 1.9179 -0.0278 -0.2026 -0.1428 304 PRO A CD 2426 N N . THR A 306 ? 1.2222 1.5603 1.8579 -0.0649 -0.1192 -0.1183 305 THR A N 2427 C CA . THR A 306 ? 1.2447 1.5547 1.8491 -0.0642 -0.1022 -0.1041 305 THR A CA 2428 C C . THR A 306 ? 1.3196 1.6140 1.9244 -0.0805 -0.0858 -0.1044 305 THR A C 2429 O O . THR A 306 ? 1.3538 1.6626 1.9903 -0.0928 -0.0763 -0.1119 305 THR A O 2430 C CB . THR A 306 ? 1.2346 1.5524 1.8460 -0.0580 -0.0898 -0.0967 305 THR A CB 2431 O OG1 . THR A 306 ? 1.2295 1.5653 1.8493 -0.0438 -0.1037 -0.0987 305 THR A OG1 2432 C CG2 . THR A 306 ? 1.2487 1.5389 1.8241 -0.0541 -0.0786 -0.0825 305 THR A CG2 2433 N N . PRO A 307 ? 1.3987 1.6626 1.9690 -0.0805 -0.0810 -0.0962 306 PRO A N 2434 C CA . PRO A 307 ? 1.4220 1.6668 1.9893 -0.0943 -0.0651 -0.0957 306 PRO A CA 2435 C C . PRO A 307 ? 1.4128 1.6600 1.9944 -0.1009 -0.0442 -0.0914 306 PRO A C 2436 O O . PRO A 307 ? 1.3731 1.6187 1.9437 -0.0922 -0.0383 -0.0816 306 PRO A O 2437 C CB . PRO A 307 ? 1.4418 1.6558 1.9691 -0.0873 -0.0630 -0.0843 306 PRO A CB 2438 C CG . PRO A 307 ? 1.4386 1.6570 1.9513 -0.0718 -0.0722 -0.0771 306 PRO A CG 2439 C CD . PRO A 307 ? 1.4153 1.6603 1.9496 -0.0678 -0.0878 -0.0867 306 PRO A CD 2440 N N . ASP A 308 ? 1.4518 1.7011 2.0561 -0.1168 -0.0328 -0.0993 307 ASP A N 2441 C CA . ASP A 308 ? 1.4937 1.7441 2.1133 -0.1252 -0.0104 -0.0970 307 ASP A CA 2442 C C . ASP A 308 ? 1.5064 1.7222 2.1047 -0.1350 0.0090 -0.0905 307 ASP A C 2443 O O . ASP A 308 ? 1.5015 1.7003 2.0824 -0.1330 0.0259 -0.0795 307 ASP A O 2444 C CB . ASP A 308 ? 1.5366 1.8200 2.2061 -0.1366 -0.0098 -0.1122 307 ASP A CB 2445 C CG . ASP A 308 ? 1.5895 1.8726 2.2768 -0.1473 0.0169 -0.1109 307 ASP A CG 2446 O OD1 . ASP A 308 ? 1.6008 1.8723 2.2682 -0.1395 0.0295 -0.0991 307 ASP A OD1 2447 O OD2 . ASP A 308 ? 1.6513 1.9448 2.3720 -0.1641 0.0261 -0.1224 307 ASP A OD2 2448 N N . SER A 309 ? 1.5093 1.7125 2.1070 -0.1451 0.0065 -0.0977 308 SER A N 2449 C CA . SER A 309 ? 1.5223 1.6885 2.0974 -0.1533 0.0244 -0.0918 308 SER A CA 2450 C C . SER A 309 ? 1.4854 1.6337 2.0448 -0.1555 0.0139 -0.0966 308 SER A C 2451 O O . SER A 309 ? 1.4069 1.5733 1.9776 -0.1544 -0.0059 -0.1072 308 SER A O 2452 C CB . SER A 309 ? 1.5776 1.7437 2.1791 -0.1719 0.0463 -0.0983 308 SER A CB 2453 O OG . SER A 309 ? 1.6037 1.8000 2.2483 -0.1847 0.0375 -0.1165 308 SER A OG 2454 N N . PHE A 310 ? 1.5070 1.6176 2.0380 -0.1574 0.0274 -0.0887 309 PHE A N 2455 C CA . PHE A 310 ? 1.5611 1.6482 2.0698 -0.1563 0.0203 -0.0907 309 PHE A CA 2456 C C . PHE A 310 ? 1.6498 1.7041 2.1521 -0.1711 0.0383 -0.0935 309 PHE A C 2457 O O . PHE A 310 ? 1.6853 1.7194 2.1792 -0.1746 0.0592 -0.0847 309 PHE A O 2458 C CB . PHE A 310 ? 1.5541 1.6240 2.0269 -0.1372 0.0165 -0.0752 309 PHE A CB 2459 C CG . PHE A 310 ? 1.5493 1.6457 2.0245 -0.1231 0.0017 -0.0712 309 PHE A CG 2460 C CD1 . PHE A 310 ? 1.5633 1.6757 2.0415 -0.1177 -0.0181 -0.0786 309 PHE A CD1 2461 C CD2 . PHE A 310 ? 1.5455 1.6478 2.0170 -0.1154 0.0079 -0.0602 309 PHE A CD2 2462 C CE1 . PHE A 310 ? 1.5394 1.6721 2.0177 -0.1049 -0.0301 -0.0745 309 PHE A CE1 2463 C CE2 . PHE A 310 ? 1.5369 1.6608 2.0098 -0.1035 -0.0047 -0.0572 309 PHE A CE2 2464 C CZ . PHE A 310 ? 1.5350 1.6737 2.0119 -0.0983 -0.0231 -0.0641 309 PHE A CZ 2465 N N . TYR A 311 ? 1.7031 1.7488 2.2058 -0.1795 0.0305 -0.1058 310 TYR A N 2466 C CA . TYR A 311 ? 1.7919 1.7992 2.2811 -0.1918 0.0467 -0.1082 310 TYR A CA 2467 C C . TYR A 311 ? 1.7205 1.6973 2.1723 -0.1797 0.0416 -0.1025 310 TYR A C 2468 O O . TYR A 311 ? 1.6834 1.6697 2.1316 -0.1749 0.0228 -0.1102 310 TYR A O 2469 C CB . TYR A 311 ? 1.9341 1.9514 2.4548 -0.2147 0.0449 -0.1293 310 TYR A CB 2470 C CG . TYR A 311 ? 2.1369 2.1102 2.6410 -0.2285 0.0617 -0.1331 310 TYR A CG 2471 C CD1 . TYR A 311 ? 2.2126 2.1579 2.7119 -0.2375 0.0896 -0.1256 310 TYR A CD1 2472 C CD2 . TYR A 311 ? 2.2288 2.1845 2.7181 -0.2317 0.0510 -0.1438 310 TYR A CD2 2473 C CE1 . TYR A 311 ? 2.2829 2.1838 2.7645 -0.2496 0.1064 -0.1285 310 TYR A CE1 2474 C CE2 . TYR A 311 ? 2.2965 2.2086 2.7687 -0.2440 0.0673 -0.1477 310 TYR A CE2 2475 C CZ . TYR A 311 ? 2.3350 2.2197 2.8041 -0.2529 0.0951 -0.1398 310 TYR A CZ 2476 O OH . TYR A 311 ? 2.4267 2.2643 2.8768 -0.2649 0.1127 -0.1432 310 TYR A OH 2477 N N . TYR A 312 ? 1.6808 1.6198 2.1038 -0.1739 0.0591 -0.0889 311 TYR A N 2478 C CA . TYR A 312 ? 1.6724 1.5796 2.0618 -0.1621 0.0584 -0.0830 311 TYR A CA 2479 C C . TYR A 312 ? 1.7267 1.5955 2.1062 -0.1767 0.0719 -0.0914 311 TYR A C 2480 O O . TYR A 312 ? 1.7727 1.6167 2.1490 -0.1857 0.0926 -0.0874 311 TYR A O 2481 C CB . TYR A 312 ? 1.6621 1.5531 2.0259 -0.1428 0.0666 -0.0620 311 TYR A CB 2482 C CG . TYR A 312 ? 1.6239 1.5444 1.9881 -0.1254 0.0501 -0.0546 311 TYR A CG 2483 C CD1 . TYR A 312 ? 1.6393 1.5567 1.9879 -0.1120 0.0393 -0.0527 311 TYR A CD1 2484 C CD2 . TYR A 312 ? 1.5608 1.5103 1.9404 -0.1231 0.0470 -0.0501 311 TYR A CD2 2485 C CE1 . TYR A 312 ? 1.5918 1.5344 1.9416 -0.0977 0.0261 -0.0465 311 TYR A CE1 2486 C CE2 . TYR A 312 ? 1.5492 1.5228 1.9284 -0.1084 0.0328 -0.0442 311 TYR A CE2 2487 C CZ . TYR A 312 ? 1.5619 1.5322 1.9269 -0.0963 0.0225 -0.0424 311 TYR A CZ 2488 O OH . TYR A 312 ? 1.5740 1.5665 1.9393 -0.0833 0.0102 -0.0369 311 TYR A OH 2489 N N . GLU A 313 ? 1.7367 1.5980 2.1087 -0.1791 0.0608 -0.1034 312 GLU A N 2490 C CA . GLU A 313 ? 1.7897 1.6101 2.1469 -0.1915 0.0724 -0.1123 312 GLU A CA 2491 C C . GLU A 313 ? 1.8226 1.5996 2.1428 -0.1754 0.0880 -0.0954 312 GLU A C 2492 O O . GLU A 313 ? 1.8913 1.6274 2.1972 -0.1833 0.1074 -0.0946 312 GLU A O 2493 C CB . GLU A 313 ? 1.8197 1.6437 2.1739 -0.1959 0.0540 -0.1295 312 GLU A CB 2494 C CG . GLU A 313 ? 1.8876 1.6692 2.2261 -0.2106 0.0640 -0.1421 312 GLU A CG 2495 C CD . GLU A 313 ? 1.9040 1.6787 2.2243 -0.2080 0.0471 -0.1549 312 GLU A CD 2496 O OE1 . GLU A 313 ? 1.8583 1.6546 2.1719 -0.1914 0.0307 -0.1505 312 GLU A OE1 2497 O OE2 . GLU A 313 ? 1.9557 1.7000 2.2655 -0.2228 0.0514 -0.1695 312 GLU A OE2 2498 N N . SER A 314 ? 1.7965 1.5827 2.1026 -0.1526 0.0793 -0.0824 313 SER A N 2499 C CA . SER A 314 ? 1.8183 1.5728 2.0952 -0.1335 0.0910 -0.0649 313 SER A CA 2500 C C . SER A 314 ? 1.7491 1.5308 2.0286 -0.1145 0.0837 -0.0488 313 SER A C 2501 O O . SER A 314 ? 1.7385 1.5549 2.0299 -0.1086 0.0667 -0.0510 313 SER A O 2502 C CB . SER A 314 ? 1.8774 1.6080 2.1315 -0.1245 0.0884 -0.0686 313 SER A CB 2503 O OG . SER A 314 ? 1.9192 1.6221 2.1495 -0.1046 0.0997 -0.0518 313 SER A OG 2504 N N . PHE A 315 ? 1.7478 1.5110 2.0137 -0.1049 0.0966 -0.0328 314 PHE A N 2505 C CA . PHE A 315 ? 1.7027 1.4897 1.9710 -0.0900 0.0907 -0.0185 314 PHE A CA 2506 C C . PHE A 315 ? 1.7262 1.4976 1.9730 -0.0662 0.0910 -0.0036 314 PHE A C 2507 O O . PHE A 315 ? 1.8103 1.5418 2.0358 -0.0611 0.1048 0.0022 314 PHE A O 2508 C CB . PHE A 315 ? 1.7109 1.4887 1.9788 -0.0975 0.1047 -0.0120 314 PHE A CB 2509 C CG . PHE A 315 ? 1.6766 1.4860 1.9533 -0.0901 0.0968 -0.0036 314 PHE A CG 2510 C CD1 . PHE A 315 ? 1.6440 1.4957 1.9474 -0.0967 0.0828 -0.0130 314 PHE A CD1 2511 C CD2 . PHE A 315 ? 1.7184 1.5131 1.9744 -0.0760 0.1031 0.0131 314 PHE A CD2 2512 C CE1 . PHE A 315 ? 1.6305 1.5082 1.9403 -0.0902 0.0768 -0.0060 314 PHE A CE1 2513 C CE2 . PHE A 315 ? 1.6996 1.5210 1.9608 -0.0700 0.0956 0.0196 314 PHE A CE2 2514 C CZ . PHE A 315 ? 1.6515 1.5138 1.9398 -0.0776 0.0832 0.0098 314 PHE A CZ 2515 N N . PRO A 316 ? 1.6624 1.4636 1.9158 -0.0515 0.0767 0.0020 315 PRO A N 2516 C CA . PRO A 316 ? 1.6317 1.4756 1.9071 -0.0558 0.0606 -0.0050 315 PRO A CA 2517 C C . PRO A 316 ? 1.6290 1.4846 1.9063 -0.0499 0.0494 -0.0115 315 PRO A C 2518 O O . PRO A 316 ? 1.6195 1.5072 1.9097 -0.0475 0.0362 -0.0134 315 PRO A O 2519 C CB . PRO A 316 ? 1.6137 1.4764 1.8901 -0.0430 0.0557 0.0086 315 PRO A CB 2520 C CG . PRO A 316 ? 1.6331 1.4716 1.8901 -0.0248 0.0615 0.0218 315 PRO A CG 2521 C CD . PRO A 316 ? 1.6639 1.4598 1.9044 -0.0303 0.0772 0.0193 315 PRO A CD 2522 N N . ASP A 317 ? 1.6902 1.5168 1.9523 -0.0479 0.0561 -0.0152 316 ASP A N 2523 C CA . ASP A 317 ? 1.7487 1.5789 2.0061 -0.0396 0.0495 -0.0193 316 ASP A CA 2524 C C . ASP A 317 ? 1.7837 1.6183 2.0432 -0.0537 0.0410 -0.0369 316 ASP A C 2525 O O . ASP A 317 ? 1.7920 1.6243 2.0420 -0.0477 0.0366 -0.0413 316 ASP A O 2526 C CB . ASP A 317 ? 1.8262 1.6207 2.0635 -0.0271 0.0621 -0.0135 316 ASP A CB 2527 C CG . ASP A 317 ? 1.8534 1.6438 2.0879 -0.0099 0.0679 0.0039 316 ASP A CG 2528 O OD1 . ASP A 317 ? 1.7730 1.5941 2.0202 -0.0007 0.0584 0.0119 316 ASP A OD1 2529 O OD2 . ASP A 317 ? 1.9129 1.6679 2.1312 -0.0054 0.0813 0.0095 316 ASP A OD2 2530 N N . ARG A 318 ? 1.8129 1.6535 2.0844 -0.0719 0.0390 -0.0471 317 ARG A N 2531 C CA . ARG A 318 ? 1.8671 1.7142 2.1431 -0.0859 0.0284 -0.0650 317 ARG A CA 2532 C C . ARG A 318 ? 1.7751 1.6634 2.0767 -0.0922 0.0146 -0.0688 317 ARG A C 2533 O O . ARG A 318 ? 1.7344 1.6355 2.0510 -0.0954 0.0192 -0.0627 317 ARG A O 2534 C CB . ARG A 318 ? 1.9812 1.7988 2.2532 -0.1032 0.0387 -0.0758 317 ARG A CB 2535 C CG . ARG A 318 ? 2.0777 1.8921 2.3476 -0.1168 0.0282 -0.0957 317 ARG A CG 2536 C CD . ARG A 318 ? 2.1723 1.9608 2.4127 -0.1065 0.0279 -0.0983 317 ARG A CD 2537 N NE . ARG A 318 ? 2.3269 2.1059 2.5595 -0.1205 0.0180 -0.1184 317 ARG A NE 2538 C CZ . ARG A 318 ? 2.4553 2.2614 2.6957 -0.1245 -0.0023 -0.1295 317 ARG A CZ 2539 N NH1 . ARG A 318 ? 2.4970 2.3405 2.7535 -0.1159 -0.0136 -0.1223 317 ARG A NH1 2540 N NH2 . ARG A 318 ? 2.5415 2.3356 2.7716 -0.1369 -0.0123 -0.1484 317 ARG A NH2 2541 N N . ASP A 319 ? 1.7396 1.6466 2.0437 -0.0924 -0.0015 -0.0782 318 ASP A N 2542 C CA . ASP A 319 ? 1.7280 1.6735 2.0555 -0.0955 -0.0152 -0.0815 318 ASP A CA 2543 C C . ASP A 319 ? 1.7016 1.6579 2.0537 -0.1144 -0.0148 -0.0925 318 ASP A C 2544 O O . ASP A 319 ? 1.7102 1.6489 2.0606 -0.1278 -0.0126 -0.1049 318 ASP A O 2545 C CB . ASP A 319 ? 1.7736 1.7315 2.0939 -0.0902 -0.0326 -0.0890 318 ASP A CB 2546 C CG . ASP A 319 ? 1.8122 1.7688 2.1163 -0.0722 -0.0321 -0.0769 318 ASP A CG 2547 O OD1 . ASP A 319 ? 1.7629 1.7305 2.0747 -0.0640 -0.0265 -0.0637 318 ASP A OD1 2548 O OD2 . ASP A 319 ? 1.8992 1.8432 2.1825 -0.0667 -0.0369 -0.0813 318 ASP A OD2 2549 N N . PRO A 320 ? 1.6537 1.6385 2.0297 -0.1161 -0.0159 -0.0888 319 PRO A N 2550 C CA . PRO A 320 ? 1.6511 1.6468 2.0539 -0.1337 -0.0111 -0.0979 319 PRO A CA 2551 C C . PRO A 320 ? 1.6297 1.6562 2.0574 -0.1425 -0.0293 -0.1144 319 PRO A C 2552 O O . PRO A 320 ? 1.5468 1.5886 1.9694 -0.1325 -0.0466 -0.1163 319 PRO A O 2553 C CB . PRO A 320 ? 1.6254 1.6356 2.0387 -0.1286 -0.0026 -0.0849 319 PRO A CB 2554 C CG . PRO A 320 ? 1.6072 1.6348 2.0129 -0.1113 -0.0151 -0.0769 319 PRO A CG 2555 C CD . PRO A 320 ? 1.6192 1.6262 1.9987 -0.1024 -0.0199 -0.0765 319 PRO A CD 2556 N N . LYS A 321 ? 1.6704 1.7056 2.1255 -0.1609 -0.0250 -0.1260 320 LYS A N 2557 C CA . LYS A 321 ? 1.7001 1.7718 2.1879 -0.1691 -0.0422 -0.1415 320 LYS A CA 2558 C C . LYS A 321 ? 1.6356 1.7387 2.1477 -0.1638 -0.0399 -0.1338 320 LYS A C 2559 O O . LYS A 321 ? 1.6112 1.7051 2.1225 -0.1640 -0.0208 -0.1224 320 LYS A O 2560 C CB . LYS A 321 ? 1.8145 1.8842 2.3262 -0.1926 -0.0377 -0.1588 320 LYS A CB 2561 C CG . LYS A 321 ? 1.8847 1.9938 2.4330 -0.2014 -0.0587 -0.1775 320 LYS A CG 2562 C CD . LYS A 321 ? 1.9771 2.0734 2.5246 -0.2172 -0.0682 -0.1971 320 LYS A CD 2563 C CE . LYS A 321 ? 2.0057 2.1446 2.5985 -0.2293 -0.0875 -0.2172 320 LYS A CE 2564 N NZ . LYS A 321 ? 2.0462 2.1729 2.6436 -0.2494 -0.0944 -0.2383 320 LYS A NZ 2565 N N . ILE A 322 ? 1.6118 1.7491 2.1419 -0.1577 -0.0591 -0.1397 321 ILE A N 2566 C CA . ILE A 322 ? 1.5965 1.7612 2.1442 -0.1490 -0.0582 -0.1317 321 ILE A CA 2567 C C . ILE A 322 ? 1.6025 1.8052 2.1971 -0.1594 -0.0643 -0.1455 321 ILE A C 2568 O O . ILE A 322 ? 1.6485 1.8692 2.2584 -0.1628 -0.0839 -0.1603 321 ILE A O 2569 C CB . ILE A 322 ? 1.5848 1.7563 2.1121 -0.1289 -0.0741 -0.1241 321 ILE A CB 2570 C CG1 . ILE A 322 ? 1.6086 1.7461 2.0944 -0.1187 -0.0682 -0.1117 321 ILE A CG1 2571 C CG2 . ILE A 322 ? 1.5558 1.7513 2.0986 -0.1202 -0.0716 -0.1159 321 ILE A CG2 2572 C CD1 . ILE A 322 ? 1.6029 1.7424 2.0671 -0.1015 -0.0821 -0.1060 321 ILE A CD1 2573 N N . CYS A 323 ? 1.6129 1.8278 2.2301 -0.1636 -0.0475 -0.1407 322 CYS A N 2574 C CA . CYS A 323 ? 1.6259 1.8810 2.2912 -0.1701 -0.0505 -0.1515 322 CYS A CA 2575 C C . CYS A 323 ? 1.5576 1.8341 2.2241 -0.1518 -0.0577 -0.1428 322 CYS A C 2576 O O . CYS A 323 ? 1.5134 1.7732 2.1535 -0.1415 -0.0472 -0.1273 322 CYS A O 2577 C CB . CYS A 323 ? 1.6823 1.9346 2.3714 -0.1872 -0.0236 -0.1523 322 CYS A CB 2578 S SG . CYS A 323 ? 1.7578 2.0610 2.5139 -0.1980 -0.0230 -0.1676 322 CYS A SG 2579 N N . PHE A 324 ? 1.5148 1.8276 2.2117 -0.1475 -0.0763 -0.1532 323 PHE A N 2580 C CA . PHE A 324 ? 1.4634 1.7936 2.1584 -0.1286 -0.0856 -0.1460 323 PHE A CA 2581 C C . PHE A 324 ? 1.4606 1.8239 2.1989 -0.1299 -0.0768 -0.1494 323 PHE A C 2582 O O . PHE A 324 ? 1.4705 1.8589 2.2527 -0.1434 -0.0750 -0.1631 323 PHE A O 2583 C CB . PHE A 324 ? 1.4550 1.7962 2.1424 -0.1167 -0.1149 -0.1527 323 PHE A CB 2584 C CG . PHE A 324 ? 1.4727 1.7795 2.1117 -0.1108 -0.1219 -0.1467 323 PHE A CG 2585 C CD1 . PHE A 324 ? 1.4856 1.7746 2.1147 -0.1228 -0.1248 -0.1555 323 PHE A CD1 2586 C CD2 . PHE A 324 ? 1.4677 1.7590 2.0716 -0.0938 -0.1238 -0.1329 323 PHE A CD2 2587 C CE1 . PHE A 324 ? 1.4923 1.7486 2.0768 -0.1166 -0.1291 -0.1502 323 PHE A CE1 2588 C CE2 . PHE A 324 ? 1.4855 1.7464 2.0480 -0.0885 -0.1278 -0.1277 323 PHE A CE2 2589 C CZ . PHE A 324 ? 1.4909 1.7342 2.0433 -0.0992 -0.1301 -0.1361 323 PHE A CZ 2590 N N . GLY A 325 ? 1.4719 1.8345 2.1979 -0.1161 -0.0704 -0.1373 324 GLY A N 2591 C CA . GLY A 325 ? 1.4656 1.8572 2.2267 -0.1127 -0.0626 -0.1391 324 GLY A CA 2592 C C . GLY A 325 ? 1.4288 1.8330 2.1823 -0.0916 -0.0798 -0.1352 324 GLY A C 2593 O O . GLY A 325 ? 1.3969 1.7927 2.1252 -0.0816 -0.1001 -0.1342 324 GLY A O 2594 N N . ASP A 326 ? 1.4216 1.8427 2.1942 -0.0847 -0.0701 -0.1328 325 ASP A N 2595 C CA . ASP A 326 ? 1.4228 1.8557 2.1916 -0.0645 -0.0845 -0.1299 325 ASP A CA 2596 C C . ASP A 326 ? 1.3596 1.7613 2.0809 -0.0539 -0.0779 -0.1142 325 ASP A C 2597 O O . ASP A 326 ? 1.2980 1.6759 1.9978 -0.0611 -0.0594 -0.1058 325 ASP A O 2598 C CB . ASP A 326 ? 1.4671 1.9351 2.2833 -0.0610 -0.0779 -0.1365 325 ASP A CB 2599 C CG . ASP A 326 ? 1.4867 1.9771 2.3139 -0.0411 -0.1007 -0.1399 325 ASP A CG 2600 O OD1 . ASP A 326 ? 1.4646 1.9380 2.2559 -0.0293 -0.1191 -0.1348 325 ASP A OD1 2601 O OD2 . ASP A 326 ? 1.5305 2.0546 2.4025 -0.0366 -0.0994 -0.1473 325 ASP A OD2 2602 N N . GLY A 327 ? 1.3013 1.7028 2.0064 -0.0366 -0.0937 -0.1107 326 GLY A N 2603 C CA . GLY A 327 ? 1.2684 1.6426 1.9315 -0.0265 -0.0900 -0.0975 326 GLY A CA 2604 C C . GLY A 327 ? 1.2502 1.6181 1.8907 -0.0118 -0.1113 -0.0958 326 GLY A C 2605 O O . GLY A 327 ? 1.2321 1.6206 1.8918 -0.0042 -0.1287 -0.1040 326 GLY A O 2606 N N . ASP A 328 ? 1.2649 1.6038 1.8645 -0.0078 -0.1099 -0.0854 327 ASP A N 2607 C CA . ASP A 328 ? 1.3011 1.6271 1.8730 0.0057 -0.1256 -0.0819 327 ASP A CA 2608 C C . ASP A 328 ? 1.3263 1.6319 1.8710 0.0015 -0.1328 -0.0806 327 ASP A C 2609 O O . ASP A 328 ? 1.3477 1.6359 1.8629 0.0112 -0.1414 -0.0761 327 ASP A O 2610 C CB . ASP A 328 ? 1.2863 1.5951 1.8340 0.0148 -0.1176 -0.0717 327 ASP A CB 2611 C CG . ASP A 328 ? 1.2695 1.5582 1.7974 0.0056 -0.1017 -0.0635 327 ASP A CG 2612 O OD1 . ASP A 328 ? 1.2596 1.5424 1.7852 -0.0054 -0.0979 -0.0637 327 ASP A OD1 2613 O OD2 . ASP A 328 ? 1.2499 1.5279 1.7637 0.0098 -0.0937 -0.0571 327 ASP A OD2 2614 N N . GLY A 329 ? 1.3552 1.6608 1.9086 -0.0126 -0.1278 -0.0848 328 GLY A N 2615 C CA . GLY A 329 ? 1.3922 1.6764 1.9201 -0.0172 -0.1317 -0.0840 328 GLY A CA 2616 C C . GLY A 329 ? 1.4050 1.6676 1.9141 -0.0241 -0.1151 -0.0746 328 GLY A C 2617 O O . GLY A 329 ? 1.4408 1.6887 1.9383 -0.0313 -0.1131 -0.0750 328 GLY A O 2618 N N . THR A 330 ? 1.3869 1.6468 1.8921 -0.0212 -0.1038 -0.0664 329 THR A N 2619 C CA . THR A 330 ? 1.3887 1.6303 1.8766 -0.0258 -0.0902 -0.0573 329 THR A CA 2620 C C . THR A 330 ? 1.3307 1.5792 1.8330 -0.0313 -0.0757 -0.0556 329 THR A C 2621 O O . THR A 330 ? 1.3073 1.5492 1.8117 -0.0409 -0.0646 -0.0546 329 THR A O 2622 C CB . THR A 330 ? 1.4443 1.6703 1.9051 -0.0167 -0.0918 -0.0486 329 THR A CB 2623 O OG1 . THR A 330 ? 1.5007 1.7174 1.9457 -0.0114 -0.1028 -0.0501 329 THR A OG1 2624 C CG2 . THR A 330 ? 1.4470 1.6577 1.8931 -0.0206 -0.0806 -0.0400 329 THR A CG2 2625 N N . VAL A 331 ? 1.2965 1.5550 1.8055 -0.0245 -0.0746 -0.0550 330 VAL A N 2626 C CA . VAL A 331 ? 1.3216 1.5844 1.8405 -0.0282 -0.0598 -0.0536 330 VAL A CA 2627 C C . VAL A 331 ? 1.3310 1.6163 1.8858 -0.0342 -0.0556 -0.0631 330 VAL A C 2628 O O . VAL A 331 ? 1.3148 1.6204 1.8912 -0.0286 -0.0660 -0.0704 330 VAL A O 2629 C CB . VAL A 331 ? 1.3278 1.5888 1.8368 -0.0184 -0.0585 -0.0496 330 VAL A CB 2630 C CG1 . VAL A 331 ? 1.3235 1.5876 1.8410 -0.0217 -0.0424 -0.0494 330 VAL A CG1 2631 C CG2 . VAL A 331 ? 1.3316 1.5719 1.8091 -0.0150 -0.0607 -0.0411 330 VAL A CG2 2632 N N . ASN A 332 ? 1.3794 1.6607 1.9408 -0.0454 -0.0398 -0.0629 331 ASN A N 2633 C CA . ASN A 332 ? 1.3953 1.6970 1.9934 -0.0541 -0.0321 -0.0722 331 ASN A CA 2634 C C . ASN A 332 ? 1.3691 1.6882 1.9866 -0.0476 -0.0256 -0.0746 331 ASN A C 2635 O O . ASN A 332 ? 1.3076 1.6141 1.9044 -0.0416 -0.0179 -0.0674 331 ASN A O 2636 C CB . ASN A 332 ? 1.4134 1.6997 2.0080 -0.0678 -0.0133 -0.0698 331 ASN A CB 2637 C CG . ASN A 332 ? 1.4498 1.7166 2.0251 -0.0733 -0.0182 -0.0675 331 ASN A CG 2638 O OD1 . ASN A 332 ? 1.4847 1.7265 2.0290 -0.0723 -0.0124 -0.0576 331 ASN A OD1 2639 N ND2 . ASN A 332 ? 1.4747 1.7528 2.0677 -0.0781 -0.0298 -0.0770 331 ASN A ND2 2640 N N . LEU A 333 ? 1.3786 1.7272 2.0369 -0.0487 -0.0293 -0.0853 332 LEU A N 2641 C CA . LEU A 333 ? 1.3869 1.7557 2.0711 -0.0422 -0.0215 -0.0890 332 LEU A CA 2642 C C . LEU A 333 ? 1.3839 1.7388 2.0598 -0.0479 0.0047 -0.0839 332 LEU A C 2643 O O . LEU A 333 ? 1.4120 1.7657 2.0828 -0.0390 0.0124 -0.0812 332 LEU A O 2644 C CB . LEU A 333 ? 1.4097 1.8152 2.1465 -0.0463 -0.0266 -0.1026 332 LEU A CB 2645 C CG . LEU A 333 ? 1.4330 1.8648 2.2072 -0.0407 -0.0158 -0.1080 332 LEU A CG 2646 C CD1 . LEU A 333 ? 1.4304 1.8616 2.1906 -0.0205 -0.0258 -0.1038 332 LEU A CD1 2647 C CD2 . LEU A 333 ? 1.4431 1.9145 2.2743 -0.0465 -0.0226 -0.1227 332 LEU A CD2 2648 N N . LYS A 334 ? 1.3620 1.7030 2.0330 -0.0623 0.0190 -0.0824 333 LYS A N 2649 C CA . LYS A 334 ? 1.3716 1.6955 2.0306 -0.0681 0.0450 -0.0773 333 LYS A CA 2650 C C . LYS A 334 ? 1.3805 1.6778 1.9943 -0.0585 0.0477 -0.0665 333 LYS A C 2651 O O . LYS A 334 ? 1.3617 1.6471 1.9644 -0.0591 0.0671 -0.0634 333 LYS A O 2652 C CB . LYS A 334 ? 1.3731 1.6795 2.0260 -0.0838 0.0580 -0.0759 333 LYS A CB 2653 C CG . LYS A 334 ? 1.3971 1.7295 2.0988 -0.0967 0.0611 -0.0885 333 LYS A CG 2654 C CD . LYS A 334 ? 1.4366 1.7533 2.1301 -0.1094 0.0591 -0.0890 333 LYS A CD 2655 C CE . LYS A 334 ? 1.4604 1.8056 2.2048 -0.1228 0.0580 -0.1039 333 LYS A CE 2656 N NZ . LYS A 334 ? 1.5010 1.8247 2.2378 -0.1390 0.0662 -0.1049 333 LYS A NZ 2657 N N . SER A 335 ? 1.3849 1.6726 1.9729 -0.0502 0.0287 -0.0614 334 SER A N 2658 C CA . SER A 335 ? 1.3486 1.6155 1.8988 -0.0415 0.0276 -0.0532 334 SER A CA 2659 C C . SER A 335 ? 1.2953 1.5704 1.8528 -0.0321 0.0332 -0.0559 334 SER A C 2660 O O . SER A 335 ? 1.3335 1.5892 1.8634 -0.0296 0.0433 -0.0511 334 SER A O 2661 C CB . SER A 335 ? 1.3539 1.6144 1.8847 -0.0351 0.0065 -0.0493 334 SER A CB 2662 O OG . SER A 335 ? 1.4038 1.6559 1.9278 -0.0423 0.0018 -0.0472 334 SER A OG 2663 N N . ALA A 336 ? 1.2229 1.5257 1.8165 -0.0263 0.0264 -0.0639 335 ALA A N 2664 C CA . ALA A 336 ? 1.2087 1.5201 1.8118 -0.0150 0.0310 -0.0667 335 ALA A CA 2665 C C . ALA A 336 ? 1.2264 1.5370 1.8390 -0.0186 0.0573 -0.0687 335 ALA A C 2666 O O . ALA A 336 ? 1.1597 1.4731 1.7762 -0.0090 0.0644 -0.0707 335 ALA A O 2667 C CB . ALA A 336 ? 1.1735 1.5156 1.8139 -0.0060 0.0156 -0.0745 335 ALA A CB 2668 N N . LEU A 337 ? 1.2838 1.5879 1.8980 -0.0320 0.0731 -0.0681 336 LEU A N 2669 C CA . LEU A 337 ? 1.3713 1.6681 1.9874 -0.0367 0.1013 -0.0688 336 LEU A CA 2670 C C . LEU A 337 ? 1.4323 1.6966 2.0001 -0.0310 0.1104 -0.0618 336 LEU A C 2671 O O . LEU A 337 ? 1.4207 1.6810 1.9893 -0.0283 0.1305 -0.0638 336 LEU A O 2672 C CB . LEU A 337 ? 1.4184 1.7059 2.0358 -0.0527 0.1165 -0.0676 336 LEU A CB 2673 C CG . LEU A 337 ? 1.4482 1.7664 2.1165 -0.0625 0.1137 -0.0767 336 LEU A CG 2674 C CD1 . LEU A 337 ? 1.4752 1.7740 2.1333 -0.0786 0.1283 -0.0738 336 LEU A CD1 2675 C CD2 . LEU A 337 ? 1.4659 1.8178 2.1870 -0.0609 0.1259 -0.0872 336 LEU A CD2 2676 N N . GLN A 338 ? 1.4951 1.7362 2.0214 -0.0295 0.0961 -0.0542 337 GLN A N 2677 C CA . GLN A 338 ? 1.5349 1.7448 2.0133 -0.0255 0.1012 -0.0484 337 GLN A CA 2678 C C . GLN A 338 ? 1.5124 1.7252 1.9917 -0.0137 0.1012 -0.0523 337 GLN A C 2679 O O . GLN A 338 ? 1.5104 1.7039 1.9661 -0.0114 0.1172 -0.0521 337 GLN A O 2680 C CB . GLN A 338 ? 1.5692 1.7610 2.0122 -0.0260 0.0822 -0.0411 337 GLN A CB 2681 C CG . GLN A 338 ? 1.5965 1.7569 1.9900 -0.0236 0.0843 -0.0358 337 GLN A CG 2682 C CD . GLN A 338 ? 1.6510 1.7877 2.0188 -0.0293 0.1057 -0.0322 337 GLN A CD 2683 O OE1 . GLN A 338 ? 1.7053 1.8442 2.0869 -0.0370 0.1176 -0.0313 337 GLN A OE1 2684 N NE2 . GLN A 338 ? 1.6735 1.7844 2.0009 -0.0259 0.1112 -0.0304 337 GLN A NE2 2685 N N . CYS A 339 ? 1.4762 1.7099 1.9793 -0.0057 0.0838 -0.0558 338 CYS A N 2686 C CA . CYS A 339 ? 1.5038 1.7409 2.0116 0.0070 0.0836 -0.0595 338 CYS A CA 2687 C C . CYS A 339 ? 1.5022 1.7541 2.0411 0.0094 0.1059 -0.0658 338 CYS A C 2688 O O . CYS A 339 ? 1.5053 1.7442 2.0310 0.0166 0.1192 -0.0674 338 CYS A O 2689 C CB . CYS A 339 ? 1.4942 1.7513 2.0239 0.0156 0.0612 -0.0615 338 CYS A CB 2690 S SG . CYS A 339 ? 1.5457 1.7938 2.0532 0.0103 0.0377 -0.0553 338 CYS A SG 2691 N N . GLN A 340 ? 1.4934 1.7723 2.0747 0.0029 0.1104 -0.0701 339 GLN A N 2692 C CA . GLN A 340 ? 1.5263 1.8243 2.1458 0.0027 0.1334 -0.0769 339 GLN A CA 2693 C C . GLN A 340 ? 1.5221 1.7889 2.1073 -0.0025 0.1612 -0.0738 339 GLN A C 2694 O O . GLN A 340 ? 1.4868 1.7520 2.0774 0.0042 0.1803 -0.0774 339 GLN A O 2695 C CB . GLN A 340 ? 1.5826 1.9108 2.2490 -0.0083 0.1335 -0.0820 339 GLN A CB 2696 C CG . GLN A 340 ? 1.6399 2.0077 2.3684 -0.0042 0.1428 -0.0923 339 GLN A CG 2697 C CD . GLN A 340 ? 1.6777 2.0775 2.4540 -0.0161 0.1368 -0.0990 339 GLN A CD 2698 O OE1 . GLN A 340 ? 1.6534 2.0399 2.4136 -0.0299 0.1348 -0.0956 339 GLN A OE1 2699 N NE2 . GLN A 340 ? 1.7019 2.1439 2.5376 -0.0105 0.1335 -0.1092 339 GLN A NE2 2700 N N . ALA A 341 ? 1.5328 1.7729 2.0801 -0.0133 0.1631 -0.0669 340 ALA A N 2701 C CA . ALA A 341 ? 1.5550 1.7605 2.0612 -0.0180 0.1873 -0.0628 340 ALA A CA 2702 C C . ALA A 341 ? 1.5447 1.7228 2.0071 -0.0080 0.1876 -0.0613 340 ALA A C 2703 O O . ALA A 341 ? 1.5345 1.6922 1.9765 -0.0068 0.2114 -0.0622 340 ALA A O 2704 C CB . ALA A 341 ? 1.5808 1.7628 2.0533 -0.0291 0.1848 -0.0548 340 ALA A CB 2705 N N . TRP A 342 ? 1.5402 1.7154 1.9867 -0.0015 0.1623 -0.0595 341 TRP A N 2706 C CA . TRP A 342 ? 1.6004 1.7492 2.0066 0.0064 0.1608 -0.0594 341 TRP A CA 2707 C C . TRP A 342 ? 1.5914 1.7503 2.0208 0.0183 0.1735 -0.0665 341 TRP A C 2708 O O . TRP A 342 ? 1.6297 1.7625 2.0269 0.0233 0.1855 -0.0680 341 TRP A O 2709 C CB . TRP A 342 ? 1.6223 1.7669 2.0107 0.0089 0.1318 -0.0563 341 TRP A CB 2710 C CG . TRP A 342 ? 1.6655 1.7917 2.0185 0.0001 0.1197 -0.0493 341 TRP A CG 2711 C CD1 . TRP A 342 ? 1.7346 1.8331 2.0479 -0.0059 0.1301 -0.0451 341 TRP A CD1 2712 C CD2 . TRP A 342 ? 1.6540 1.7872 2.0072 -0.0018 0.0949 -0.0455 341 TRP A CD2 2713 N NE1 . TRP A 342 ? 1.7459 1.8363 2.0378 -0.0107 0.1120 -0.0389 341 TRP A NE1 2714 C CE2 . TRP A 342 ? 1.6885 1.8006 2.0058 -0.0087 0.0913 -0.0393 341 TRP A CE2 2715 C CE3 . TRP A 342 ? 1.6163 1.7702 1.9950 0.0024 0.0761 -0.0466 341 TRP A CE3 2716 C CZ2 . TRP A 342 ? 1.6782 1.7923 1.9893 -0.0115 0.0704 -0.0346 341 TRP A CZ2 2717 C CZ3 . TRP A 342 ? 1.6047 1.7577 1.9738 -0.0013 0.0569 -0.0419 341 TRP A CZ3 2718 C CH2 . TRP A 342 ? 1.6305 1.7652 1.9685 -0.0082 0.0546 -0.0362 341 TRP A CH2 2719 N N . GLN A 343 ? 1.5755 1.7719 2.0605 0.0234 0.1701 -0.0712 342 GLN A N 2720 C CA . GLN A 343 ? 1.6051 1.8164 2.1198 0.0369 0.1809 -0.0778 342 GLN A CA 2721 C C . GLN A 343 ? 1.6908 1.8873 2.1981 0.0367 0.2149 -0.0808 342 GLN A C 2722 O O . GLN A 343 ? 1.7228 1.9083 2.2226 0.0482 0.2263 -0.0844 342 GLN A O 2723 C CB . GLN A 343 ? 1.6023 1.8604 2.1825 0.0404 0.1727 -0.0827 342 GLN A CB 2724 C CG . GLN A 343 ? 1.6262 1.9038 2.2382 0.0587 0.1709 -0.0882 342 GLN A CG 2725 C CD . GLN A 343 ? 1.6299 1.9540 2.3023 0.0632 0.1547 -0.0928 342 GLN A CD 2726 O OE1 . GLN A 343 ? 1.6179 1.9633 2.3174 0.0508 0.1526 -0.0943 342 GLN A OE1 2727 N NE2 . GLN A 343 ? 1.6605 1.9987 2.3522 0.0813 0.1426 -0.0954 342 GLN A NE2 2728 N N . SER A 344 ? 1.7754 1.9681 2.2820 0.0240 0.2327 -0.0792 343 SER A N 2729 C CA . SER A 344 ? 1.9036 2.0804 2.4021 0.0226 0.2681 -0.0817 343 SER A CA 2730 C C . SER A 344 ? 2.0189 2.1435 2.4433 0.0217 0.2773 -0.0776 343 SER A C 2731 O O . SER A 344 ? 2.0860 2.1895 2.4925 0.0227 0.3069 -0.0797 343 SER A O 2732 C CB . SER A 344 ? 1.9259 2.1152 2.4503 0.0083 0.2859 -0.0813 343 SER A CB 2733 O OG . SER A 344 ? 1.9280 2.0982 2.4176 -0.0033 0.2727 -0.0736 343 SER A OG 2734 N N . ARG A 345 ? 2.0991 2.2031 2.4808 0.0198 0.2521 -0.0725 344 ARG A N 2735 C CA . ARG A 345 ? 2.2347 2.2918 2.5462 0.0179 0.2548 -0.0693 344 ARG A CA 2736 C C . ARG A 345 ? 2.2223 2.2676 2.5128 0.0273 0.2373 -0.0721 344 ARG A C 2737 O O . ARG A 345 ? 2.2846 2.3078 2.5329 0.0238 0.2181 -0.0690 344 ARG A O 2738 C CB . ARG A 345 ? 2.3283 2.3725 2.6098 0.0069 0.2389 -0.0613 344 ARG A CB 2739 C CG . ARG A 345 ? 2.4096 2.4698 2.7200 -0.0029 0.2508 -0.0582 344 ARG A CG 2740 C CD . ARG A 345 ? 2.5566 2.5932 2.8482 -0.0070 0.2869 -0.0580 344 ARG A CD 2741 N NE . ARG A 345 ? 2.7192 2.7068 2.9364 -0.0090 0.2906 -0.0524 344 ARG A NE 2742 C CZ . ARG A 345 ? 2.8808 2.8396 3.0660 -0.0156 0.3138 -0.0475 344 ARG A CZ 2743 N NH1 . ARG A 345 ? 2.9449 2.9189 3.1680 -0.0229 0.3378 -0.0477 344 ARG A NH1 2744 N NH2 . ARG A 345 ? 2.9575 2.8708 3.0709 -0.0151 0.3126 -0.0426 344 ARG A NH2 2745 N N . GLN A 346 ? 2.1943 2.2544 2.5159 0.0392 0.2445 -0.0782 345 GLN A N 2746 C CA . GLN A 346 ? 2.1763 2.2346 2.4941 0.0486 0.2251 -0.0804 345 GLN A CA 2747 C C . GLN A 346 ? 2.1180 2.1385 2.3922 0.0552 0.2379 -0.0850 345 GLN A C 2748 O O . GLN A 346 ? 2.0653 2.0844 2.3517 0.0635 0.2628 -0.0899 345 GLN A O 2749 C CB . GLN A 346 ? 2.2090 2.3073 2.5893 0.0604 0.2217 -0.0839 345 GLN A CB 2750 C CG . GLN A 346 ? 2.2060 2.3364 2.6201 0.0580 0.1945 -0.0805 345 GLN A CG 2751 C CD . GLN A 346 ? 2.2152 2.3786 2.6806 0.0728 0.1880 -0.0844 345 GLN A CD 2752 O OE1 . GLN A 346 ? 2.1793 2.3424 2.6420 0.0805 0.1675 -0.0833 345 GLN A OE1 2753 N NE2 . GLN A 346 ? 2.2382 2.4293 2.7504 0.0774 0.2063 -0.0891 345 GLN A NE2 2754 N N . GLU A 347 ? 2.0495 2.0400 2.2745 0.0510 0.2214 -0.0841 346 GLU A N 2755 C CA . GLU A 347 ? 2.0152 1.9753 2.2079 0.0583 0.2238 -0.0898 346 GLU A CA 2756 C C . GLU A 347 ? 1.9653 1.9451 2.1887 0.0664 0.2035 -0.0899 346 GLU A C 2757 O O . GLU A 347 ? 1.9452 1.9326 2.1937 0.0802 0.2120 -0.0935 346 GLU A O 2758 C CB . GLU A 347 ? 2.0301 1.9502 2.1574 0.0483 0.2147 -0.0900 346 GLU A CB 2759 C CG . GLU A 347 ? 2.0573 1.9567 2.1506 0.0413 0.2329 -0.0882 346 GLU A CG 2760 C CD . GLU A 347 ? 2.0935 1.9516 2.1186 0.0335 0.2232 -0.0894 346 GLU A CD 2761 O OE1 . GLU A 347 ? 2.0832 1.9378 2.0954 0.0294 0.1971 -0.0901 346 GLU A OE1 2762 O OE2 . GLU A 347 ? 2.1086 1.9374 2.0925 0.0314 0.2418 -0.0899 346 GLU A OE2 2763 N N . HIS A 348 ? 1.9617 1.9497 2.1835 0.0586 0.1773 -0.0853 347 HIS A N 2764 C CA . HIS A 348 ? 1.9995 2.0029 2.2458 0.0653 0.1583 -0.0843 347 HIS A CA 2765 C C . HIS A 348 ? 1.9590 2.0057 2.2645 0.0727 0.1561 -0.0821 347 HIS A C 2766 O O . HIS A 348 ? 1.9237 1.9919 2.2520 0.0670 0.1621 -0.0802 347 HIS A O 2767 C CB . HIS A 348 ? 2.0233 2.0205 2.2485 0.0541 0.1333 -0.0805 347 HIS A CB 2768 C CG . HIS A 348 ? 2.1039 2.0617 2.2765 0.0479 0.1310 -0.0846 347 HIS A CG 2769 N ND1 . HIS A 348 ? 2.1342 2.0680 2.2664 0.0397 0.1392 -0.0863 347 HIS A ND1 2770 C CD2 . HIS A 348 ? 2.1539 2.0904 2.3066 0.0484 0.1221 -0.0880 347 HIS A CD2 2771 C CE1 . HIS A 348 ? 2.1882 2.0899 2.2790 0.0352 0.1330 -0.0915 347 HIS A CE1 2772 N NE2 . HIS A 348 ? 2.1912 2.0942 2.2951 0.0395 0.1234 -0.0928 347 HIS A NE2 2773 N N . GLN A 349 ? 1.9659 2.0236 2.2946 0.0852 0.1467 -0.0826 348 GLN A N 2774 C CA . GLN A 349 ? 1.9627 2.0619 2.3468 0.0940 0.1406 -0.0816 348 GLN A CA 2775 C C . GLN A 349 ? 1.9244 2.0469 2.3243 0.0833 0.1207 -0.0765 348 GLN A C 2776 O O . GLN A 349 ? 1.9175 2.0255 2.2900 0.0746 0.1050 -0.0728 348 GLN A O 2777 C CB . GLN A 349 ? 2.0239 2.1238 2.4202 0.1113 0.1319 -0.0822 348 GLN A CB 2778 C CG . GLN A 349 ? 2.1192 2.2012 2.5104 0.1261 0.1520 -0.0873 348 GLN A CG 2779 C CD . GLN A 349 ? 2.1961 2.2804 2.6026 0.1457 0.1427 -0.0868 348 GLN A CD 2780 O OE1 . GLN A 349 ? 2.2164 2.3138 2.6340 0.1478 0.1210 -0.0825 348 GLN A OE1 2781 N NE2 . GLN A 349 ? 2.2633 2.3323 2.6680 0.1613 0.1600 -0.0910 348 GLN A NE2 2782 N N . VAL A 350 ? 1.9358 2.0947 2.3815 0.0839 0.1221 -0.0771 349 VAL A N 2783 C CA . VAL A 350 ? 1.9161 2.0983 2.3808 0.0748 0.1045 -0.0734 349 VAL A CA 2784 C C . VAL A 350 ? 1.8917 2.1116 2.4083 0.0862 0.0954 -0.0760 349 VAL A C 2785 O O . VAL A 350 ? 1.9246 2.1688 2.4795 0.0905 0.1091 -0.0808 349 VAL A O 2786 C CB . VAL A 350 ? 1.9107 2.0978 2.3771 0.0598 0.1165 -0.0725 349 VAL A CB 2787 C CG1 . VAL A 350 ? 1.8376 2.0432 2.3182 0.0501 0.0985 -0.0688 349 VAL A CG1 2788 C CG2 . VAL A 350 ? 1.9854 2.1345 2.3989 0.0512 0.1268 -0.0706 349 VAL A CG2 2789 N N . LEU A 351 ? 1.8679 2.0924 2.3856 0.0915 0.0726 -0.0732 350 LEU A N 2790 C CA . LEU A 351 ? 1.8676 2.1254 2.4288 0.1039 0.0598 -0.0756 350 LEU A CA 2791 C C . LEU A 351 ? 1.8029 2.0810 2.3788 0.0934 0.0422 -0.0740 350 LEU A C 2792 O O . LEU A 351 ? 1.7657 2.0262 2.3115 0.0853 0.0305 -0.0689 350 LEU A O 2793 C CB . LEU A 351 ? 1.9216 2.1648 2.4691 0.1215 0.0482 -0.0737 350 LEU A CB 2794 C CG . LEU A 351 ? 1.9777 2.2029 2.5170 0.1359 0.0649 -0.0763 350 LEU A CG 2795 C CD1 . LEU A 351 ? 1.9976 2.1796 2.4850 0.1268 0.0765 -0.0748 350 LEU A CD1 2796 C CD2 . LEU A 351 ? 1.9921 2.2163 2.5371 0.1576 0.0522 -0.0752 350 LEU A CD2 2797 N N . LEU A 352 ? 1.7531 2.0681 2.3764 0.0930 0.0414 -0.0790 351 LEU A N 2798 C CA . LEU A 352 ? 1.7117 2.0462 2.3511 0.0833 0.0248 -0.0791 351 LEU A CA 2799 C C . LEU A 352 ? 1.6792 2.0351 2.3419 0.0980 0.0022 -0.0814 351 LEU A C 2800 O O . LEU A 352 ? 1.7227 2.0969 2.4143 0.1139 0.0026 -0.0857 351 LEU A O 2801 C CB . LEU A 352 ? 1.7240 2.0830 2.3986 0.0699 0.0383 -0.0843 351 LEU A CB 2802 C CG . LEU A 352 ? 1.7607 2.0969 2.4056 0.0515 0.0520 -0.0800 351 LEU A CG 2803 C CD1 . LEU A 352 ? 1.8059 2.1052 2.4047 0.0528 0.0654 -0.0754 351 LEU A CD1 2804 C CD2 . LEU A 352 ? 1.7760 2.1328 2.4559 0.0399 0.0705 -0.0852 351 LEU A CD2 2805 N N . GLN A 353 ? 1.6142 1.9666 2.2628 0.0939 -0.0176 -0.0783 352 GLN A N 2806 C CA . GLN A 353 ? 1.5663 1.9333 2.2278 0.1081 -0.0409 -0.0797 352 GLN A CA 2807 C C . GLN A 353 ? 1.5157 1.8970 2.1858 0.0975 -0.0577 -0.0816 352 GLN A C 2808 O O . GLN A 353 ? 1.5015 1.8604 2.1381 0.0880 -0.0627 -0.0761 352 GLN A O 2809 C CB . GLN A 353 ? 1.5843 1.9178 2.2030 0.1206 -0.0487 -0.0726 352 GLN A CB 2810 C CG . GLN A 353 ? 1.5786 1.9197 2.2023 0.1393 -0.0710 -0.0727 352 GLN A CG 2811 C CD . GLN A 353 ? 1.5779 1.9449 2.2400 0.1585 -0.0714 -0.0783 352 GLN A CD 2812 O OE1 . GLN A 353 ? 1.6076 1.9570 2.2554 0.1756 -0.0680 -0.0753 352 GLN A OE1 2813 N NE2 . GLN A 353 ? 1.5477 1.9569 2.2605 0.1557 -0.0749 -0.0868 352 GLN A NE2 2814 N N . GLU A 354 ? 1.4834 1.9023 2.1999 0.0993 -0.0665 -0.0901 353 GLU A N 2815 C CA . GLU A 354 ? 1.4610 1.8944 2.1877 0.0905 -0.0845 -0.0939 353 GLU A CA 2816 C C . GLU A 354 ? 1.4711 1.8926 2.1721 0.1047 -0.1094 -0.0907 353 GLU A C 2817 O O . GLU A 354 ? 1.4801 1.9002 2.1788 0.1248 -0.1170 -0.0893 353 GLU A O 2818 C CB . GLU A 354 ? 1.4316 1.9106 2.2188 0.0874 -0.0869 -0.1058 353 GLU A CB 2819 C CG . GLU A 354 ? 1.4028 1.8965 2.2028 0.0742 -0.1028 -0.1119 353 GLU A CG 2820 C CD . GLU A 354 ? 1.3844 1.9248 2.2481 0.0691 -0.1051 -0.1254 353 GLU A CD 2821 O OE1 . GLU A 354 ? 1.3903 1.9492 2.2890 0.0674 -0.0850 -0.1292 353 GLU A OE1 2822 O OE2 . GLU A 354 ? 1.3604 1.9188 2.2399 0.0661 -0.1266 -0.1329 353 GLU A OE2 2823 N N . LEU A 355 ? 1.4553 1.8653 2.1346 0.0947 -0.1205 -0.0890 354 LEU A N 2824 C CA . LEU A 355 ? 1.4680 1.8644 2.1198 0.1060 -0.1429 -0.0863 354 LEU A CA 2825 C C . LEU A 355 ? 1.4686 1.8866 2.1399 0.0987 -0.1609 -0.0948 354 LEU A C 2826 O O . LEU A 355 ? 1.4764 1.8790 2.1258 0.0854 -0.1623 -0.0931 354 LEU A O 2827 C CB . LEU A 355 ? 1.4779 1.8326 2.0769 0.1013 -0.1376 -0.0759 354 LEU A CB 2828 C CG . LEU A 355 ? 1.4940 1.8225 2.0672 0.1101 -0.1248 -0.0683 354 LEU A CG 2829 C CD1 . LEU A 355 ? 1.4909 1.7875 2.0262 0.0974 -0.1138 -0.0606 354 LEU A CD1 2830 C CD2 . LEU A 355 ? 1.5225 1.8391 2.0786 0.1323 -0.1388 -0.0654 354 LEU A CD2 2831 N N . PRO A 356 ? 1.4739 1.9281 2.1874 0.1074 -0.1751 -0.1046 355 PRO A N 2832 C CA . PRO A 356 ? 1.4746 1.9529 2.2124 0.0978 -0.1917 -0.1152 355 PRO A CA 2833 C C . PRO A 356 ? 1.5015 1.9575 2.1983 0.1031 -0.2138 -0.1130 355 PRO A C 2834 O O . PRO A 356 ? 1.5316 1.9744 2.2038 0.1234 -0.2281 -0.1086 355 PRO A O 2835 C CB . PRO A 356 ? 1.4739 1.9969 2.2667 0.1097 -0.2034 -0.1260 355 PRO A CB 2836 C CG . PRO A 356 ? 1.4966 2.0086 2.2750 0.1340 -0.2037 -0.1186 355 PRO A CG 2837 C CD . PRO A 356 ? 1.4864 1.9598 2.2251 0.1284 -0.1790 -0.1067 355 PRO A CD 2838 N N . GLY A 357 ? 1.5087 1.9570 2.1954 0.0854 -0.2149 -0.1158 356 GLY A N 2839 C CA . GLY A 357 ? 1.5174 1.9432 2.1646 0.0883 -0.2335 -0.1149 356 GLY A CA 2840 C C . GLY A 357 ? 1.5170 1.8970 2.1068 0.0913 -0.2243 -0.1012 356 GLY A C 2841 O O . GLY A 357 ? 1.4935 1.8502 2.0456 0.0964 -0.2372 -0.0990 356 GLY A O 2842 N N . SER A 358 ? 1.5050 1.8716 2.0878 0.0877 -0.2018 -0.0926 357 SER A N 2843 C CA . SER A 358 ? 1.5058 1.8325 2.0402 0.0888 -0.1922 -0.0806 357 SER A CA 2844 C C . SER A 358 ? 1.4413 1.7553 1.9654 0.0690 -0.1787 -0.0783 357 SER A C 2845 O O . SER A 358 ? 1.3317 1.6571 1.8783 0.0560 -0.1635 -0.0795 357 SER A O 2846 C CB . SER A 358 ? 1.5302 1.8467 2.0589 0.0973 -0.1778 -0.0731 357 SER A CB 2847 O OG . SER A 358 ? 1.5610 1.8857 2.1091 0.0836 -0.1577 -0.0730 357 SER A OG 2848 N N . GLU A 359 ? 1.4578 1.7462 1.9460 0.0678 -0.1836 -0.0746 358 GLU A N 2849 C CA . GLU A 359 ? 1.4481 1.7217 1.9235 0.0520 -0.1716 -0.0715 358 GLU A CA 2850 C C . GLU A 359 ? 1.4274 1.6834 1.8876 0.0490 -0.1529 -0.0614 358 GLU A C 2851 O O . GLU A 359 ? 1.4726 1.7169 1.9183 0.0594 -0.1504 -0.0558 358 GLU A O 2852 C CB . GLU A 359 ? 1.4948 1.7459 1.9365 0.0533 -0.1816 -0.0711 358 GLU A CB 2853 C CG . GLU A 359 ? 1.5154 1.7575 1.9520 0.0375 -0.1733 -0.0716 358 GLU A CG 2854 C CD . GLU A 359 ? 1.5331 1.7499 1.9439 0.0341 -0.1574 -0.0609 358 GLU A CD 2855 O OE1 . GLU A 359 ? 1.5338 1.7310 1.9180 0.0436 -0.1564 -0.0540 358 GLU A OE1 2856 O OE2 . GLU A 359 ? 1.5755 1.7918 1.9933 0.0218 -0.1457 -0.0596 358 GLU A OE2 2857 N N . HIS A 360 ? 1.4082 1.6612 1.8708 0.0347 -0.1405 -0.0596 359 HIS A N 2858 C CA . HIS A 360 ? 1.4271 1.6674 1.8793 0.0299 -0.1245 -0.0516 359 HIS A CA 2859 C C . HIS A 360 ? 1.4594 1.6751 1.8801 0.0376 -0.1228 -0.0437 359 HIS A C 2860 O O . HIS A 360 ? 1.5457 1.7564 1.9630 0.0400 -0.1147 -0.0398 359 HIS A O 2861 C CB . HIS A 360 ? 1.4036 1.6396 1.8556 0.0160 -0.1159 -0.0504 359 HIS A CB 2862 C CG . HIS A 360 ? 1.3851 1.6117 1.8293 0.0110 -0.1019 -0.0432 359 HIS A CG 2863 N ND1 . HIS A 360 ? 1.3851 1.6179 1.8381 0.0118 -0.0939 -0.0422 359 HIS A ND1 2864 C CD2 . HIS A 360 ? 1.3884 1.6003 1.8167 0.0055 -0.0954 -0.0372 359 HIS A CD2 2865 C CE1 . HIS A 360 ? 1.3845 1.6058 1.8249 0.0067 -0.0845 -0.0363 359 HIS A CE1 2866 N NE2 . HIS A 360 ? 1.3862 1.5965 1.8135 0.0032 -0.0858 -0.0330 359 HIS A NE2 2867 N N . ILE A 361 ? 1.4311 1.6299 1.8281 0.0408 -0.1291 -0.0420 360 ILE A N 2868 C CA . ILE A 361 ? 1.4663 1.6399 1.8338 0.0467 -0.1252 -0.0348 360 ILE A CA 2869 C C . ILE A 361 ? 1.5044 1.6707 1.8598 0.0622 -0.1343 -0.0348 360 ILE A C 2870 O O . ILE A 361 ? 1.4834 1.6343 1.8245 0.0676 -0.1281 -0.0296 360 ILE A O 2871 C CB . ILE A 361 ? 1.5023 1.6573 1.8475 0.0432 -0.1240 -0.0322 360 ILE A CB 2872 C CG1 . ILE A 361 ? 1.5227 1.6818 1.8778 0.0303 -0.1139 -0.0305 360 ILE A CG1 2873 C CG2 . ILE A 361 ? 1.5297 1.6583 1.8457 0.0494 -0.1187 -0.0254 360 ILE A CG2 2874 C CD1 . ILE A 361 ? 1.5801 1.7532 1.9522 0.0230 -0.1179 -0.0367 360 ILE A CD1 2875 N N . GLU A 362 ? 1.5369 1.7134 1.8975 0.0694 -0.1497 -0.0408 361 GLU A N 2876 C CA . GLU A 362 ? 1.5544 1.7237 1.9016 0.0868 -0.1614 -0.0406 361 GLU A CA 2877 C C . GLU A 362 ? 1.4448 1.6223 1.8066 0.0947 -0.1572 -0.0395 361 GLU A C 2878 O O . GLU A 362 ? 1.4153 1.5762 1.7578 0.1092 -0.1604 -0.0357 361 GLU A O 2879 C CB . GLU A 362 ? 1.6936 1.8796 2.0508 0.0925 -0.1814 -0.0492 361 GLU A CB 2880 C CG . GLU A 362 ? 1.8394 2.0098 2.1722 0.0884 -0.1877 -0.0508 361 GLU A CG 2881 C CD . GLU A 362 ? 1.9545 2.1445 2.3013 0.0904 -0.2083 -0.0618 361 GLU A CD 2882 O OE1 . GLU A 362 ? 2.0575 2.2672 2.4227 0.1016 -0.2224 -0.0666 361 GLU A OE1 2883 O OE2 . GLU A 362 ? 1.9937 2.1794 2.3337 0.0808 -0.2108 -0.0662 361 GLU A OE2 2884 N N . MET A 363 ? 1.3734 1.5730 1.7664 0.0856 -0.1486 -0.0425 362 MET A N 2885 C CA . MET A 363 ? 1.3969 1.6035 1.8038 0.0924 -0.1423 -0.0422 362 MET A CA 2886 C C . MET A 363 ? 1.4336 1.6098 1.8113 0.0963 -0.1314 -0.0344 362 MET A C 2887 O O . MET A 363 ? 1.4532 1.6249 1.8304 0.1078 -0.1296 -0.0335 362 MET A O 2888 C CB . MET A 363 ? 1.3670 1.5964 1.8056 0.0800 -0.1313 -0.0460 362 MET A CB 2889 C CG . MET A 363 ? 1.3518 1.5670 1.7781 0.0669 -0.1154 -0.0409 362 MET A CG 2890 S SD . MET A 363 ? 1.3111 1.5468 1.7660 0.0540 -0.1021 -0.0444 362 MET A SD 2891 C CE . MET A 363 ? 1.3188 1.5828 1.8054 0.0490 -0.1114 -0.0527 362 MET A CE 2892 N N . LEU A 364 ? 1.4308 1.5868 1.7864 0.0865 -0.1236 -0.0294 363 LEU A N 2893 C CA . LEU A 364 ? 1.4201 1.5478 1.7506 0.0867 -0.1124 -0.0232 363 LEU A CA 2894 C C . LEU A 364 ? 1.4185 1.5190 1.7191 0.1019 -0.1168 -0.0189 363 LEU A C 2895 O O . LEU A 364 ? 1.3698 1.4467 1.6525 0.1044 -0.1072 -0.0148 363 LEU A O 2896 C CB . LEU A 364 ? 1.4159 1.5333 1.7363 0.0720 -0.1034 -0.0198 363 LEU A CB 2897 C CG . LEU A 364 ? 1.4027 1.5371 1.7434 0.0576 -0.0960 -0.0216 363 LEU A CG 2898 C CD1 . LEU A 364 ? 1.4167 1.5416 1.7476 0.0464 -0.0899 -0.0180 363 LEU A CD1 2899 C CD2 . LEU A 364 ? 1.3742 1.5079 1.7197 0.0570 -0.0875 -0.0223 363 LEU A CD2 2900 N N . ALA A 365 ? 1.4724 1.5734 1.7648 0.1116 -0.1310 -0.0201 364 ALA A N 2901 C CA . ALA A 365 ? 1.5450 1.6175 1.8040 0.1281 -0.1368 -0.0154 364 ALA A CA 2902 C C . ALA A 365 ? 1.5955 1.6835 1.8657 0.1466 -0.1541 -0.0193 364 ALA A C 2903 O O . ALA A 365 ? 1.6787 1.7463 1.9211 0.1632 -0.1640 -0.0162 364 ALA A O 2904 C CB . ALA A 365 ? 1.5782 1.6314 1.8089 0.1257 -0.1394 -0.0129 364 ALA A CB 2905 N N . ASN A 366 ? 1.6045 1.7283 1.9155 0.1444 -0.1572 -0.0261 365 ASN A N 2906 C CA . ASN A 366 ? 1.6793 1.8263 2.0114 0.1606 -0.1741 -0.0314 365 ASN A CA 2907 C C . ASN A 366 ? 1.6534 1.7899 1.9823 0.1777 -0.1701 -0.0282 365 ASN A C 2908 O O . ASN A 366 ? 1.6302 1.7615 1.9646 0.1716 -0.1532 -0.0266 365 ASN A O 2909 C CB . ASN A 366 ? 1.7455 1.9364 2.1263 0.1499 -0.1768 -0.0408 365 ASN A CB 2910 C CG . ASN A 366 ? 1.8956 2.1162 2.3040 0.1645 -0.1968 -0.0483 365 ASN A CG 2911 O OD1 . ASN A 366 ? 1.9514 2.1710 2.3611 0.1835 -0.2016 -0.0470 365 ASN A OD1 2912 N ND2 . ASN A 366 ? 2.0229 2.2689 2.4528 0.1564 -0.2094 -0.0565 365 ASN A ND2 2913 N N . ALA A 367 ? 1.6632 1.7951 1.9816 0.1998 -0.1865 -0.0275 366 ALA A N 2914 C CA . ALA A 367 ? 1.6707 1.7877 1.9811 0.2200 -0.1841 -0.0235 366 ALA A CA 2915 C C . ALA A 367 ? 1.6237 1.7715 1.9785 0.2203 -0.1762 -0.0291 366 ALA A C 2916 O O . ALA A 367 ? 1.7069 1.8363 2.0536 0.2278 -0.1632 -0.0254 366 ALA A O 2917 C CB . ALA A 367 ? 1.7089 1.8204 2.0032 0.2455 -0.2068 -0.0224 366 ALA A CB 2918 N N . THR A 368 ? 1.5249 1.7170 1.9251 0.2119 -0.1825 -0.0381 367 THR A N 2919 C CA . THR A 368 ? 1.4580 1.6800 1.9017 0.2103 -0.1722 -0.0439 367 THR A CA 2920 C C . THR A 368 ? 1.3865 1.5944 1.8238 0.1913 -0.1477 -0.0416 367 THR A C 2921 O O . THR A 368 ? 1.3971 1.6029 1.8431 0.1952 -0.1338 -0.0418 367 THR A O 2922 C CB . THR A 368 ? 1.4667 1.7383 1.9611 0.2029 -0.1826 -0.0546 367 THR A CB 2923 O OG1 . THR A 368 ? 1.4878 1.7612 1.9780 0.1806 -0.1815 -0.0561 367 THR A OG1 2924 C CG2 . THR A 368 ? 1.5013 1.7931 2.0092 0.2231 -0.2092 -0.0590 367 THR A CG2 2925 N N . THR A 369 ? 1.3441 1.5418 1.7653 0.1717 -0.1430 -0.0397 368 THR A N 2926 C CA . THR A 369 ? 1.3416 1.5248 1.7532 0.1542 -0.1230 -0.0373 368 THR A CA 2927 C C . THR A 369 ? 1.4020 1.5462 1.7794 0.1614 -0.1123 -0.0310 368 THR A C 2928 O O . THR A 369 ? 1.3610 1.4982 1.7397 0.1569 -0.0970 -0.0316 368 THR A O 2929 C CB . THR A 369 ? 1.3272 1.5038 1.7248 0.1353 -0.1223 -0.0354 368 THR A CB 2930 O OG1 . THR A 369 ? 1.3311 1.5382 1.7553 0.1293 -0.1332 -0.0413 368 THR A OG1 2931 C CG2 . THR A 369 ? 1.3010 1.4698 1.6951 0.1178 -0.1046 -0.0342 368 THR A CG2 2932 N N . LEU A 370 ? 1.4864 1.6026 1.8307 0.1722 -0.1197 -0.0252 369 LEU A N 2933 C CA . LEU A 370 ? 1.5802 1.6543 1.8888 0.1784 -0.1088 -0.0188 369 LEU A CA 2934 C C . LEU A 370 ? 1.6175 1.6886 1.9334 0.1970 -0.1050 -0.0197 369 LEU A C 2935 O O . LEU A 370 ? 1.6130 1.6582 1.9129 0.1955 -0.0896 -0.0181 369 LEU A O 2936 C CB . LEU A 370 ? 1.6283 1.6714 1.8984 0.1873 -0.1167 -0.0120 369 LEU A CB 2937 C CG . LEU A 370 ? 1.5998 1.6386 1.8565 0.1712 -0.1182 -0.0104 369 LEU A CG 2938 C CD1 . LEU A 370 ? 1.6446 1.6564 1.8651 0.1846 -0.1284 -0.0047 369 LEU A CD1 2939 C CD2 . LEU A 370 ? 1.5774 1.5978 1.8224 0.1513 -0.1000 -0.0083 369 LEU A CD2 2940 N N . ALA A 371 ? 1.6459 1.7438 1.9870 0.2146 -0.1194 -0.0230 370 ALA A N 2941 C CA . ALA A 371 ? 1.6659 1.7670 2.0210 0.2345 -0.1166 -0.0244 370 ALA A CA 2942 C C . ALA A 371 ? 1.6386 1.7548 2.0195 0.2232 -0.0985 -0.0300 370 ALA A C 2943 O O . ALA A 371 ? 1.6596 1.7572 2.0332 0.2323 -0.0856 -0.0295 370 ALA A O 2944 C CB . ALA A 371 ? 1.6726 1.8080 2.0579 0.2541 -0.1377 -0.0283 370 ALA A CB 2945 N N . TYR A 372 ? 1.5796 1.7259 1.9872 0.2038 -0.0966 -0.0352 371 TYR A N 2946 C CA . TYR A 372 ? 1.5954 1.7522 2.0213 0.1918 -0.0785 -0.0399 371 TYR A CA 2947 C C . TYR A 372 ? 1.5918 1.7099 1.9811 0.1792 -0.0626 -0.0366 371 TYR A C 2948 O O . TYR A 372 ? 1.5957 1.7019 1.9820 0.1802 -0.0474 -0.0387 371 TYR A O 2949 C CB . TYR A 372 ? 1.6025 1.7948 2.0595 0.1737 -0.0796 -0.0452 371 TYR A CB 2950 C CG . TYR A 372 ? 1.6682 1.8762 2.1496 0.1667 -0.0621 -0.0506 371 TYR A CG 2951 C CD1 . TYR A 372 ? 1.7152 1.9551 2.2380 0.1784 -0.0608 -0.0566 371 TYR A CD1 2952 C CD2 . TYR A 372 ? 1.7008 1.8913 2.1634 0.1490 -0.0465 -0.0500 371 TYR A CD2 2953 C CE1 . TYR A 372 ? 1.7366 1.9880 2.2796 0.1720 -0.0417 -0.0614 371 TYR A CE1 2954 C CE2 . TYR A 372 ? 1.7026 1.9026 2.1809 0.1433 -0.0296 -0.0546 371 TYR A CE2 2955 C CZ . TYR A 372 ? 1.7141 1.9433 2.2317 0.1546 -0.0258 -0.0601 371 TYR A CZ 2956 O OH . TYR A 372 ? 1.6918 1.9279 2.2232 0.1489 -0.0062 -0.0645 371 TYR A OH 2957 N N . LEU A 373 ? 1.6036 1.7025 1.9661 0.1670 -0.0659 -0.0322 372 LEU A N 2958 C CA . LEU A 373 ? 1.6505 1.7147 1.9809 0.1542 -0.0530 -0.0298 372 LEU A CA 2959 C C . LEU A 373 ? 1.6715 1.6992 1.9766 0.1687 -0.0448 -0.0274 372 LEU A C 2960 O O . LEU A 373 ? 1.6860 1.6932 1.9780 0.1620 -0.0303 -0.0296 372 LEU A O 2961 C CB . LEU A 373 ? 1.7186 1.7703 2.0285 0.1422 -0.0589 -0.0252 372 LEU A CB 2962 C CG . LEU A 373 ? 1.7812 1.8110 2.0706 0.1226 -0.0478 -0.0246 372 LEU A CG 2963 C CD1 . LEU A 373 ? 1.7728 1.8244 2.0804 0.1067 -0.0424 -0.0296 372 LEU A CD1 2964 C CD2 . LEU A 373 ? 1.8257 1.8450 2.0990 0.1146 -0.0531 -0.0199 372 LEU A CD2 2965 N N . LYS A 374 ? 1.6864 1.7037 1.9821 0.1890 -0.0544 -0.0230 373 LYS A N 2966 C CA . LYS A 374 ? 1.7465 1.7280 2.0184 0.2070 -0.0472 -0.0199 373 LYS A CA 2967 C C . LYS A 374 ? 1.7145 1.7015 2.0031 0.2140 -0.0346 -0.0254 373 LYS A C 2968 O O . LYS A 374 ? 1.7099 1.6617 1.9745 0.2142 -0.0198 -0.0256 373 LYS A O 2969 C CB . LYS A 374 ? 1.8160 1.7961 2.0835 0.2323 -0.0631 -0.0149 373 LYS A CB 2970 C CG . LYS A 374 ? 1.8889 1.8253 2.1113 0.2363 -0.0647 -0.0064 373 LYS A CG 2971 C CD . LYS A 374 ? 1.9816 1.8766 2.1760 0.2580 -0.0573 -0.0017 373 LYS A CD 2972 C CE . LYS A 374 ? 2.0394 1.8893 2.1874 0.2653 -0.0591 0.0075 373 LYS A CE 2973 N NZ . LYS A 374 ? 2.1124 1.9246 2.2341 0.2927 -0.0561 0.0133 373 LYS A NZ 2974 N N . ARG A 375 ? 1.7286 1.7587 2.0585 0.2197 -0.0398 -0.0303 374 ARG A N 2975 C CA . ARG A 375 ? 1.8246 1.8678 2.1777 0.2253 -0.0265 -0.0365 374 ARG A CA 2976 C C . ARG A 375 ? 1.8177 1.8430 2.1550 0.2046 -0.0081 -0.0402 374 ARG A C 2977 O O . ARG A 375 ? 1.8565 1.8587 2.1817 0.2100 0.0073 -0.0429 374 ARG A O 2978 C CB . ARG A 375 ? 1.9085 2.0060 2.3124 0.2258 -0.0340 -0.0419 374 ARG A CB 2979 C CG . ARG A 375 ? 2.0333 2.1549 2.4688 0.2526 -0.0423 -0.0435 374 ARG A CG 2980 C CD . ARG A 375 ? 2.1169 2.2866 2.6048 0.2493 -0.0377 -0.0516 374 ARG A CD 2981 N NE . ARG A 375 ? 2.2101 2.4209 2.7386 0.2649 -0.0572 -0.0542 374 ARG A NE 2982 C CZ . ARG A 375 ? 2.3316 2.5510 2.8774 0.2927 -0.0639 -0.0544 374 ARG A CZ 2983 N NH1 . ARG A 375 ? 2.3565 2.6174 2.9416 0.3046 -0.0845 -0.0580 374 ARG A NH1 2984 N NH2 . ARG A 375 ? 2.3935 2.5799 2.9178 0.3092 -0.0511 -0.0515 374 ARG A NH2 2985 N N . VAL A 376 ? 1.7816 1.8171 2.1181 0.1817 -0.0105 -0.0409 375 VAL A N 2986 C CA . VAL A 376 ? 1.7976 1.8200 2.1194 0.1616 0.0029 -0.0446 375 VAL A CA 2987 C C . VAL A 376 ? 1.8263 1.8011 2.1069 0.1573 0.0110 -0.0433 375 VAL A C 2988 O O . VAL A 376 ? 1.8346 1.7885 2.1001 0.1529 0.0252 -0.0480 375 VAL A O 2989 C CB . VAL A 376 ? 1.7941 1.8377 2.1236 0.1402 -0.0037 -0.0446 375 VAL A CB 2990 C CG1 . VAL A 376 ? 1.7906 1.8172 2.0995 0.1207 0.0069 -0.0478 375 VAL A CG1 2991 C CG2 . VAL A 376 ? 1.7809 1.8682 2.1506 0.1417 -0.0079 -0.0473 375 VAL A CG2 2992 N N . LEU A 377 ? 1.8545 1.8107 2.1161 0.1583 0.0029 -0.0375 376 LEU A N 2993 C CA . LEU A 377 ? 1.9361 1.8474 2.1605 0.1506 0.0109 -0.0363 376 LEU A CA 2994 C C . LEU A 377 ? 2.0183 1.8930 2.2223 0.1686 0.0214 -0.0359 376 LEU A C 2995 O O . LEU A 377 ? 2.0499 1.8910 2.2295 0.1602 0.0346 -0.0398 376 LEU A O 2996 C CB . LEU A 377 ? 1.9449 1.8471 2.1560 0.1456 0.0015 -0.0298 376 LEU A CB 2997 C CG . LEU A 377 ? 1.9391 1.8701 2.1650 0.1272 -0.0074 -0.0297 376 LEU A CG 2998 C CD1 . LEU A 377 ? 1.9798 1.9005 2.1926 0.1276 -0.0152 -0.0228 376 LEU A CD1 2999 C CD2 . LEU A 377 ? 1.9260 1.8523 2.1455 0.1041 0.0000 -0.0349 376 LEU A CD2 3000 N N . LEU A 378 ? 2.0670 1.9468 2.2798 0.1935 0.0148 -0.0314 377 LEU A N 3001 C CA . LEU A 378 ? 2.1012 1.9435 2.2925 0.2144 0.0233 -0.0291 377 LEU A CA 3002 C C . LEU A 378 ? 2.0823 1.9368 2.2942 0.2312 0.0318 -0.0341 377 LEU A C 3003 O O . LEU A 378 ? 2.1350 1.9547 2.3274 0.2452 0.0438 -0.0343 377 LEU A O 3004 C CB . LEU A 378 ? 2.1310 1.9629 2.3114 0.2343 0.0107 -0.0200 377 LEU A CB 3005 C CG . LEU A 378 ? 2.1532 1.9736 2.3137 0.2197 0.0037 -0.0146 377 LEU A CG 3006 C CD1 . LEU A 378 ? 2.2149 2.0118 2.3529 0.2419 -0.0050 -0.0053 377 LEU A CD1 3007 C CD2 . LEU A 378 ? 2.1479 1.9327 2.2806 0.1957 0.0182 -0.0169 377 LEU A CD2 3008 N N . GLY A 379 ? 2.0131 1.9150 2.2642 0.2294 0.0277 -0.0384 378 GLY A N 3009 C CA . GLY A 379 ? 1.9841 1.9008 2.2587 0.2424 0.0389 -0.0441 378 GLY A CA 3010 C C . GLY A 379 ? 1.9549 1.8574 2.2163 0.2236 0.0569 -0.0515 378 GLY A C 3011 O O . GLY A 379 ? 1.8720 1.7634 2.1138 0.1997 0.0567 -0.0527 378 GLY A O 3012 N N . ARG B 4 ? 1.8402 2.3309 2.5065 0.1307 -0.0195 0.1333 3 ARG B N 3013 C CA . ARG B 4 ? 1.8213 2.3007 2.4807 0.1109 -0.0313 0.1305 3 ARG B CA 3014 C C . ARG B 4 ? 1.7828 2.2096 2.4097 0.0977 -0.0276 0.1247 3 ARG B C 3015 O O . ARG B 4 ? 1.8205 2.2062 2.4151 0.1082 -0.0268 0.1258 3 ARG B O 3016 C CB . ARG B 4 ? 1.8719 2.3529 2.5221 0.1254 -0.0429 0.1360 3 ARG B CB 3017 C CG . ARG B 4 ? 1.8915 2.3636 2.5322 0.1076 -0.0545 0.1337 3 ARG B CG 3018 C CD . ARG B 4 ? 1.8887 2.4066 2.5642 0.0902 -0.0630 0.1311 3 ARG B CD 3019 N NE . ARG B 4 ? 1.8755 2.3761 2.5414 0.0660 -0.0665 0.1244 3 ARG B NE 3020 C CZ . ARG B 4 ? 1.8239 2.3191 2.4974 0.0464 -0.0599 0.1182 3 ARG B CZ 3021 N NH1 . ARG B 4 ? 1.7846 2.2892 2.4740 0.0463 -0.0496 0.1180 3 ARG B NH1 3022 N NH2 . ARG B 4 ? 1.8177 2.2978 2.4817 0.0280 -0.0633 0.1125 3 ARG B NH2 3023 N N . HIS B 5 ? 1.6858 2.1145 2.3226 0.0746 -0.0259 0.1192 4 HIS B N 3024 C CA . HIS B 5 ? 1.6450 2.0316 2.2580 0.0601 -0.0233 0.1138 4 HIS B CA 3025 C C . HIS B 5 ? 1.5281 1.9224 2.1514 0.0365 -0.0292 0.1098 4 HIS B C 3026 O O . HIS B 5 ? 1.4849 1.9115 2.1354 0.0259 -0.0309 0.1083 4 HIS B O 3027 C CB . HIS B 5 ? 1.6843 2.0575 2.2931 0.0590 -0.0133 0.1104 4 HIS B CB 3028 C CG . HIS B 5 ? 1.7082 2.1184 2.3473 0.0510 -0.0092 0.1100 4 HIS B CG 3029 N ND1 . HIS B 5 ? 1.7350 2.1718 2.3887 0.0659 -0.0018 0.1141 4 HIS B ND1 3030 C CD2 . HIS B 5 ? 1.7023 2.1257 2.3591 0.0301 -0.0104 0.1069 4 HIS B CD2 3031 C CE1 . HIS B 5 ? 1.7138 2.1786 2.3930 0.0528 0.0013 0.1142 4 HIS B CE1 3032 N NE2 . HIS B 5 ? 1.6888 2.1444 2.3695 0.0312 -0.0043 0.1097 4 HIS B NE2 3033 N N . PRO B 6 ? 1.4513 1.8146 2.0524 0.0285 -0.0317 0.1084 5 PRO B N 3034 C CA . PRO B 6 ? 1.4037 1.7746 2.0127 0.0093 -0.0362 0.1044 5 PRO B CA 3035 C C . PRO B 6 ? 1.3471 1.7140 1.9657 -0.0083 -0.0313 0.0985 5 PRO B C 3036 O O . PRO B 6 ? 1.3075 1.6555 1.9184 -0.0075 -0.0251 0.0974 5 PRO B O 3037 C CB . PRO B 6 ? 1.4181 1.7572 1.9984 0.0091 -0.0380 0.1064 5 PRO B CB 3038 C CG . PRO B 6 ? 1.4416 1.7458 1.9996 0.0192 -0.0322 0.1089 5 PRO B CG 3039 C CD . PRO B 6 ? 1.4540 1.7747 2.0220 0.0366 -0.0301 0.1108 5 PRO B CD 3040 N N . PRO B 7 ? 1.2872 1.6703 1.9209 -0.0233 -0.0348 0.0944 6 PRO B N 3041 C CA . PRO B 7 ? 1.2443 1.6229 1.8869 -0.0388 -0.0309 0.0894 6 PRO B CA 3042 C C . PRO B 7 ? 1.2155 1.5608 1.8392 -0.0451 -0.0268 0.0876 6 PRO B C 3043 O O . PRO B 7 ? 1.1963 1.5232 1.8010 -0.0430 -0.0274 0.0896 6 PRO B O 3044 C CB . PRO B 7 ? 1.2540 1.6518 1.9113 -0.0508 -0.0365 0.0853 6 PRO B CB 3045 C CG . PRO B 7 ? 1.2779 1.6821 1.9260 -0.0436 -0.0439 0.0874 6 PRO B CG 3046 C CD . PRO B 7 ? 1.2908 1.6968 1.9333 -0.0255 -0.0436 0.0940 6 PRO B CD 3047 N N . VAL B 8 ? 1.2002 1.5391 1.8298 -0.0532 -0.0230 0.0846 7 VAL B N 3048 C CA . VAL B 8 ? 1.2094 1.5207 1.8258 -0.0599 -0.0203 0.0831 7 VAL B CA 3049 C C . VAL B 8 ? 1.1599 1.4757 1.7903 -0.0745 -0.0195 0.0787 7 VAL B C 3050 O O . VAL B 8 ? 1.0999 1.4307 1.7464 -0.0777 -0.0196 0.0769 7 VAL B O 3051 C CB . VAL B 8 ? 1.2503 1.5432 1.8550 -0.0528 -0.0178 0.0838 7 VAL B CB 3052 C CG1 . VAL B 8 ? 1.2751 1.5412 1.8691 -0.0625 -0.0173 0.0817 7 VAL B CG1 3053 C CG2 . VAL B 8 ? 1.2914 1.5755 1.8798 -0.0358 -0.0177 0.0881 7 VAL B CG2 3054 N N . VAL B 9 ? 1.1479 1.4503 1.7722 -0.0826 -0.0181 0.0777 8 VAL B N 3055 C CA . VAL B 9 ? 1.1230 1.4282 1.7604 -0.0945 -0.0167 0.0738 8 VAL B CA 3056 C C . VAL B 9 ? 1.1284 1.4135 1.7596 -0.1000 -0.0154 0.0743 8 VAL B C 3057 O O . VAL B 9 ? 1.1465 1.4138 1.7628 -0.1004 -0.0138 0.0771 8 VAL B O 3058 C CB . VAL B 9 ? 1.1217 1.4337 1.7612 -0.0999 -0.0151 0.0719 8 VAL B CB 3059 C CG1 . VAL B 9 ? 1.1200 1.4382 1.7758 -0.1092 -0.0131 0.0676 8 VAL B CG1 3060 C CG2 . VAL B 9 ? 1.1133 1.4417 1.7544 -0.0948 -0.0190 0.0711 8 VAL B CG2 3061 N N . LEU B 10 ? 1.1215 1.4087 1.7634 -0.1046 -0.0169 0.0719 9 LEU B N 3062 C CA . LEU B 10 ? 1.1747 1.4456 1.8134 -0.1110 -0.0184 0.0714 9 LEU B CA 3063 C C . LEU B 10 ? 1.1899 1.4694 1.8458 -0.1220 -0.0171 0.0697 9 LEU B C 3064 O O . LEU B 10 ? 1.1812 1.4769 1.8531 -0.1234 -0.0171 0.0674 9 LEU B O 3065 C CB . LEU B 10 ? 1.2020 1.4693 1.8388 -0.1076 -0.0223 0.0700 9 LEU B CB 3066 C CG . LEU B 10 ? 1.2291 1.4912 1.8507 -0.0946 -0.0217 0.0715 9 LEU B CG 3067 C CD1 . LEU B 10 ? 1.2325 1.4893 1.8492 -0.0917 -0.0241 0.0701 9 LEU B CD1 3068 C CD2 . LEU B 10 ? 1.2564 1.4958 1.8566 -0.0892 -0.0211 0.0735 9 LEU B CD2 3069 N N . VAL B 11 ? 1.2568 1.5250 1.9100 -0.1297 -0.0155 0.0713 10 VAL B N 3070 C CA . VAL B 11 ? 1.2920 1.5713 1.9638 -0.1395 -0.0126 0.0708 10 VAL B CA 3071 C C . VAL B 11 ? 1.3282 1.5993 2.0060 -0.1484 -0.0180 0.0707 10 VAL B C 3072 O O . VAL B 11 ? 1.3955 1.6465 2.0599 -0.1527 -0.0193 0.0729 10 VAL B O 3073 C CB . VAL B 11 ? 1.3106 1.5890 1.9776 -0.1427 -0.0044 0.0740 10 VAL B CB 3074 C CG1 . VAL B 11 ? 1.3125 1.6078 2.0011 -0.1503 0.0010 0.0732 10 VAL B CG1 3075 C CG2 . VAL B 11 ? 1.3015 1.5838 1.9565 -0.1335 -0.0021 0.0739 10 VAL B CG2 3076 N N . PRO B 12 ? 1.3185 1.6036 2.0155 -0.1514 -0.0221 0.0682 11 PRO B N 3077 C CA . PRO B 12 ? 1.3302 1.6108 2.0347 -0.1599 -0.0300 0.0675 11 PRO B CA 3078 C C . PRO B 12 ? 1.3505 1.6385 2.0723 -0.1724 -0.0266 0.0701 11 PRO B C 3079 O O . PRO B 12 ? 1.3077 1.6076 2.0377 -0.1731 -0.0165 0.0722 11 PRO B O 3080 C CB . PRO B 12 ? 1.3249 1.6212 2.0446 -0.1565 -0.0353 0.0651 11 PRO B CB 3081 C CG . PRO B 12 ? 1.3221 1.6355 2.0530 -0.1516 -0.0271 0.0648 11 PRO B CG 3082 C CD . PRO B 12 ? 1.3195 1.6238 2.0313 -0.1465 -0.0211 0.0658 11 PRO B CD 3083 N N . GLY B 13 ? 1.3813 1.6632 2.1087 -0.1824 -0.0352 0.0698 12 GLY B N 3084 C CA . GLY B 13 ? 1.3919 1.6860 2.1426 -0.1962 -0.0333 0.0728 12 GLY B CA 3085 C C . GLY B 13 ? 1.3765 1.6991 2.1586 -0.1976 -0.0378 0.0714 12 GLY B C 3086 O O . GLY B 13 ? 1.3408 1.6723 2.1254 -0.1871 -0.0404 0.0687 12 GLY B O 3087 N N . ASP B 14 ? 1.3864 1.7235 2.1937 -0.2107 -0.0388 0.0741 13 ASP B N 3088 C CA . ASP B 14 ? 1.3804 1.7472 2.2213 -0.2120 -0.0444 0.0736 13 ASP B CA 3089 C C . ASP B 14 ? 1.3540 1.7125 2.1870 -0.2087 -0.0622 0.0694 13 ASP B C 3090 O O . ASP B 14 ? 1.3813 1.7142 2.1919 -0.2136 -0.0720 0.0672 13 ASP B O 3091 C CB . ASP B 14 ? 1.4244 1.8090 2.2949 -0.2287 -0.0434 0.0781 13 ASP B CB 3092 C CG . ASP B 14 ? 1.4318 1.8551 2.3433 -0.2275 -0.0450 0.0790 13 ASP B CG 3093 O OD1 . ASP B 14 ? 1.4078 1.8394 2.3219 -0.2141 -0.0495 0.0758 13 ASP B OD1 3094 O OD2 . ASP B 14 ? 1.4659 1.9117 2.4078 -0.2399 -0.0413 0.0835 13 ASP B OD2 3095 N N . LEU B 15 ? 1.3037 1.6813 2.1522 -0.1993 -0.0658 0.0683 14 LEU B N 3096 C CA . LEU B 15 ? 1.2896 1.6598 2.1278 -0.1934 -0.0811 0.0654 14 LEU B CA 3097 C C . LEU B 15 ? 1.2679 1.6099 2.0680 -0.1839 -0.0805 0.0630 14 LEU B C 3098 O O . LEU B 15 ? 1.2207 1.5504 2.0041 -0.1797 -0.0918 0.0610 14 LEU B O 3099 C CB . LEU B 15 ? 1.3293 1.6965 2.1725 -0.2062 -0.0983 0.0642 14 LEU B CB 3100 C CG . LEU B 15 ? 1.3473 1.7409 2.2287 -0.2209 -0.0993 0.0673 14 LEU B CG 3101 C CD1 . LEU B 15 ? 1.3851 1.7594 2.2577 -0.2388 -0.1091 0.0661 14 LEU B CD1 3102 C CD2 . LEU B 15 ? 1.3451 1.7701 2.2589 -0.2175 -0.1098 0.0683 14 LEU B CD2 3103 N N . GLY B 16 ? 1.2531 1.5869 2.0401 -0.1798 -0.0671 0.0637 15 GLY B N 3104 C CA . GLY B 16 ? 1.2619 1.5709 2.0155 -0.1725 -0.0656 0.0623 15 GLY B CA 3105 C C . GLY B 16 ? 1.2390 1.5508 1.9853 -0.1596 -0.0622 0.0621 15 GLY B C 3106 O O . GLY B 16 ? 1.2455 1.5413 1.9676 -0.1529 -0.0608 0.0616 15 GLY B O 3107 N N . ASN B 17 ? 1.2210 1.5525 1.9885 -0.1558 -0.0604 0.0630 16 ASN B N 3108 C CA . ASN B 17 ? 1.2327 1.5650 1.9946 -0.1456 -0.0575 0.0634 16 ASN B CA 3109 C C . ASN B 17 ? 1.2222 1.5674 2.0019 -0.1418 -0.0630 0.0645 16 ASN B C 3110 O O . ASN B 17 ? 1.2080 1.5689 2.0111 -0.1453 -0.0655 0.0648 16 ASN B O 3111 C CB . ASN B 17 ? 1.2192 1.5550 1.9808 -0.1424 -0.0451 0.0630 16 ASN B CB 3112 C CG . ASN B 17 ? 1.1989 1.5514 1.9829 -0.1448 -0.0381 0.0624 16 ASN B CG 3113 O OD1 . ASN B 17 ? 1.1686 1.5319 1.9673 -0.1401 -0.0367 0.0618 16 ASN B OD1 3114 N ND2 . ASN B 17 ? 1.1891 1.5420 1.9739 -0.1513 -0.0327 0.0629 16 ASN B ND2 3115 N N . GLN B 18 ? 1.2166 1.5556 1.9856 -0.1343 -0.0645 0.0661 17 GLN B N 3116 C CA . GLN B 18 ? 1.2430 1.5892 2.0240 -0.1292 -0.0702 0.0685 17 GLN B CA 3117 C C . GLN B 18 ? 1.2570 1.6184 2.0625 -0.1267 -0.0632 0.0677 17 GLN B C 3118 O O . GLN B 18 ? 1.2597 1.6225 2.0662 -0.1274 -0.0527 0.0654 17 GLN B O 3119 C CB . GLN B 18 ? 1.2592 1.5932 2.0218 -0.1224 -0.0704 0.0717 17 GLN B CB 3120 C CG . GLN B 18 ? 1.2783 1.5971 2.0143 -0.1219 -0.0765 0.0725 17 GLN B CG 3121 C CD . GLN B 18 ? 1.2862 1.5959 2.0059 -0.1149 -0.0766 0.0775 17 GLN B CD 3122 O OE1 . GLN B 18 ? 1.2825 1.5958 2.0121 -0.1114 -0.0741 0.0811 17 GLN B OE1 3123 N NE2 . GLN B 18 ? 1.2997 1.5956 1.9928 -0.1126 -0.0789 0.0781 17 GLN B NE2 3124 N N . LEU B 19 ? 1.2910 1.6628 2.1144 -0.1225 -0.0696 0.0695 18 LEU B N 3125 C CA . LEU B 19 ? 1.3355 1.7193 2.1806 -0.1166 -0.0631 0.0687 18 LEU B CA 3126 C C . LEU B 19 ? 1.3759 1.7558 2.2233 -0.1072 -0.0698 0.0725 18 LEU B C 3127 O O . LEU B 19 ? 1.3681 1.7454 2.2101 -0.1061 -0.0819 0.0762 18 LEU B O 3128 C CB . LEU B 19 ? 1.3502 1.7565 2.2225 -0.1200 -0.0627 0.0678 18 LEU B CB 3129 C CG . LEU B 19 ? 1.3957 1.8059 2.2677 -0.1295 -0.0542 0.0655 18 LEU B CG 3130 C CD1 . LEU B 19 ? 1.4158 1.8503 2.3173 -0.1346 -0.0549 0.0666 18 LEU B CD1 3131 C CD2 . LEU B 19 ? 1.3940 1.7993 2.2586 -0.1267 -0.0397 0.0623 18 LEU B CD2 3132 N N . GLU B 20 ? 1.3958 1.7724 2.2487 -0.1003 -0.0624 0.0716 19 GLU B N 3133 C CA . GLU B 20 ? 1.3930 1.7605 2.2458 -0.0909 -0.0672 0.0758 19 GLU B CA 3134 C C . GLU B 20 ? 1.3370 1.7153 2.2138 -0.0814 -0.0637 0.0741 19 GLU B C 3135 O O . GLU B 20 ? 1.2680 1.6546 2.1548 -0.0818 -0.0532 0.0686 19 GLU B O 3136 C CB . GLU B 20 ? 1.4749 1.8210 2.3077 -0.0913 -0.0615 0.0768 19 GLU B CB 3137 C CG . GLU B 20 ? 1.5449 1.8802 2.3544 -0.0965 -0.0649 0.0808 19 GLU B CG 3138 C CD . GLU B 20 ? 1.6194 1.9390 2.4146 -0.0982 -0.0582 0.0828 19 GLU B CD 3139 O OE1 . GLU B 20 ? 1.6631 1.9770 2.4650 -0.0967 -0.0525 0.0803 19 GLU B OE1 3140 O OE2 . GLU B 20 ? 1.6637 1.9765 2.4411 -0.1013 -0.0586 0.0867 19 GLU B OE2 3141 N N . ALA B 21 ? 1.3270 1.7040 2.2108 -0.0715 -0.0722 0.0791 20 ALA B N 3142 C CA . ALA B 21 ? 1.3351 1.7217 2.2419 -0.0592 -0.0695 0.0781 20 ALA B CA 3143 C C . ALA B 21 ? 1.3685 1.7337 2.2675 -0.0477 -0.0731 0.0829 20 ALA B C 3144 O O . ALA B 21 ? 1.4118 1.7608 2.2919 -0.0489 -0.0810 0.0894 20 ALA B O 3145 C CB . ALA B 21 ? 1.3294 1.7462 2.2639 -0.0570 -0.0776 0.0800 20 ALA B CB 3146 N N . LYS B 22 ? 1.3746 1.7376 2.2863 -0.0360 -0.0663 0.0799 21 LYS B N 3147 C CA . LYS B 22 ? 1.4052 1.7457 2.3118 -0.0229 -0.0696 0.0844 21 LYS B CA 3148 C C . LYS B 22 ? 1.4307 1.7906 2.3661 -0.0061 -0.0707 0.0844 21 LYS B C 3149 O O . LYS B 22 ? 1.4412 1.8212 2.3954 -0.0037 -0.0609 0.0776 21 LYS B O 3150 C CB . LYS B 22 ? 1.4122 1.7229 2.3013 -0.0247 -0.0590 0.0793 21 LYS B CB 3151 C CG . LYS B 22 ? 1.4324 1.7096 2.3049 -0.0192 -0.0632 0.0862 21 LYS B CG 3152 C CD . LYS B 22 ? 1.4614 1.7301 2.3460 0.0002 -0.0641 0.0871 21 LYS B CD 3153 C CE . LYS B 22 ? 1.4886 1.7169 2.3532 0.0039 -0.0664 0.0936 21 LYS B CE 3154 N NZ . LYS B 22 ? 1.4914 1.7105 2.3657 0.0253 -0.0711 0.0980 21 LYS B NZ 3155 N N . LEU B 23 ? 1.4605 1.8155 2.3991 0.0063 -0.0823 0.0927 22 LEU B N 3156 C CA . LEU B 23 ? 1.4887 1.8672 2.4578 0.0239 -0.0862 0.0944 22 LEU B CA 3157 C C . LEU B 23 ? 1.5308 1.8835 2.4970 0.0434 -0.0840 0.0963 22 LEU B C 3158 O O . LEU B 23 ? 1.6011 1.9194 2.5427 0.0447 -0.0891 0.1025 22 LEU B O 3159 C CB . LEU B 23 ? 1.5015 1.9005 2.4804 0.0250 -0.1051 0.1033 22 LEU B CB 3160 C CG . LEU B 23 ? 1.4892 1.9081 2.4670 0.0063 -0.1116 0.1025 22 LEU B CG 3161 C CD1 . LEU B 23 ? 1.5058 1.9427 2.4931 0.0099 -0.1325 0.1102 22 LEU B CD1 3162 C CD2 . LEU B 23 ? 1.4694 1.9177 2.4709 -0.0019 -0.1000 0.0944 22 LEU B CD2 3163 N N . ASP B 24 ? 1.5209 1.8896 2.5119 0.0586 -0.0756 0.0912 23 ASP B N 3164 C CA . ASP B 24 ? 1.5505 1.9026 2.5467 0.0825 -0.0760 0.0937 23 ASP B CA 3165 C C . ASP B 24 ? 1.5184 1.9137 2.5559 0.0988 -0.0725 0.0917 23 ASP B C 3166 O O . ASP B 24 ? 1.4881 1.8836 2.5344 0.1105 -0.0574 0.0835 23 ASP B O 3167 C CB . ASP B 24 ? 1.5838 1.8925 2.5558 0.0851 -0.0629 0.0859 23 ASP B CB 3168 C CG . ASP B 24 ? 1.6372 1.9199 2.6092 0.1102 -0.0636 0.0885 23 ASP B CG 3169 O OD1 . ASP B 24 ? 1.6428 1.9284 2.6222 0.1228 -0.0773 0.0997 23 ASP B OD1 3170 O OD2 . ASP B 24 ? 1.6742 1.9314 2.6369 0.1179 -0.0511 0.0790 23 ASP B OD2 3171 N N . LYS B 25 ? 1.4991 1.9316 2.5615 0.0989 -0.0868 0.0992 24 LYS B N 3172 C CA . LYS B 25 ? 1.4890 1.9730 2.5964 0.1080 -0.0843 0.0984 24 LYS B CA 3173 C C . LYS B 25 ? 1.4934 1.9837 2.6228 0.1378 -0.0880 0.1032 24 LYS B C 3174 O O . LYS B 25 ? 1.4915 1.9579 2.6069 0.1485 -0.1021 0.1116 24 LYS B O 3175 C CB . LYS B 25 ? 1.5029 2.0250 2.6291 0.0929 -0.1003 0.1040 24 LYS B CB 3176 C CG . LYS B 25 ? 1.5108 2.0260 2.6148 0.0649 -0.0985 0.1001 24 LYS B CG 3177 C CD . LYS B 25 ? 1.5214 2.0717 2.6439 0.0506 -0.1145 0.1043 24 LYS B CD 3178 C CE . LYS B 25 ? 1.5190 2.1205 2.6875 0.0490 -0.1073 0.1020 24 LYS B CE 3179 N NZ . LYS B 25 ? 1.5208 2.1513 2.7038 0.0291 -0.1214 0.1043 24 LYS B NZ 3180 N N . PRO B 26 ? 1.5040 2.0270 2.6678 0.1523 -0.0745 0.0985 25 PRO B N 3181 C CA . PRO B 26 ? 1.5710 2.1064 2.7610 0.1832 -0.0775 0.1033 25 PRO B CA 3182 C C . PRO B 26 ? 1.6136 2.1909 2.8366 0.1878 -0.1004 0.1149 25 PRO B C 3183 O O . PRO B 26 ? 1.6548 2.2238 2.8812 0.2098 -0.1131 0.1230 25 PRO B O 3184 C CB . PRO B 26 ? 1.5574 2.1224 2.7757 0.1944 -0.0545 0.0946 25 PRO B CB 3185 C CG . PRO B 26 ? 1.5031 2.0930 2.7257 0.1666 -0.0462 0.0897 25 PRO B CG 3186 C CD . PRO B 26 ? 1.4795 2.0300 2.6588 0.1420 -0.0552 0.0896 25 PRO B CD 3187 N N . THR B 27 ? 1.6237 2.2439 2.8696 0.1669 -0.1063 0.1157 26 THR B N 3188 C CA . THR B 27 ? 1.6434 2.3038 2.9189 0.1660 -0.1306 0.1253 26 THR B CA 3189 C C . THR B 27 ? 1.5953 2.2738 2.8693 0.1337 -0.1383 0.1240 26 THR B C 3190 O O . THR B 27 ? 1.5514 2.2215 2.8116 0.1148 -0.1223 0.1162 26 THR B O 3191 C CB . THR B 27 ? 1.6700 2.3904 3.0060 0.1861 -0.1291 0.1284 26 THR B CB 3192 O OG1 . THR B 27 ? 1.6906 2.4345 3.0474 0.1829 -0.1028 0.1200 26 THR B OG1 3193 C CG2 . THR B 27 ? 1.7001 2.4069 3.0407 0.2220 -0.1324 0.1337 26 THR B CG2 3194 N N . VAL B 28 ? 1.5988 2.3002 2.8855 0.1283 -0.1638 0.1315 27 VAL B N 3195 C CA . VAL B 28 ? 1.6037 2.3190 2.8871 0.0989 -0.1750 0.1303 27 VAL B CA 3196 C C . VAL B 28 ? 1.5862 2.3615 2.9209 0.0969 -0.1936 0.1355 27 VAL B C 3197 O O . VAL B 28 ? 1.5736 2.3795 2.9444 0.1196 -0.2002 0.1413 27 VAL B O 3198 C CB . VAL B 28 ? 1.6476 2.3166 2.8783 0.0885 -0.1911 0.1331 27 VAL B CB 3199 C CG1 . VAL B 28 ? 1.6647 2.2833 2.8497 0.0796 -0.1720 0.1268 27 VAL B CG1 3200 C CG2 . VAL B 28 ? 1.6773 2.3315 2.8982 0.1109 -0.2102 0.1429 27 VAL B CG2 3201 N N . VAL B 29 ? 1.5869 2.3784 2.9248 0.0695 -0.2026 0.1333 28 VAL B N 3202 C CA . VAL B 29 ? 1.6287 2.4771 3.0155 0.0615 -0.2216 0.1372 28 VAL B CA 3203 C C . VAL B 29 ? 1.6796 2.5300 3.0614 0.0688 -0.2556 0.1447 28 VAL B C 3204 O O . VAL B 29 ? 1.6888 2.5904 3.1187 0.0738 -0.2729 0.1498 28 VAL B O 3205 C CB . VAL B 29 ? 1.6280 2.4901 3.0198 0.0280 -0.2198 0.1319 28 VAL B CB 3206 C CG1 . VAL B 29 ? 1.6066 2.4735 3.0081 0.0223 -0.1869 0.1262 28 VAL B CG1 3207 C CG2 . VAL B 29 ? 1.6381 2.4522 2.9730 0.0092 -0.2319 0.1287 28 VAL B CG2 3208 N N . HIS B 30 ? 1.7292 2.5262 3.0538 0.0692 -0.2653 0.1457 29 HIS B N 3209 C CA . HIS B 30 ? 1.7729 2.5640 3.0823 0.0775 -0.2966 0.1533 29 HIS B CA 3210 C C . HIS B 30 ? 1.7809 2.5154 3.0395 0.0962 -0.2941 0.1581 29 HIS B C 3211 O O . HIS B 30 ? 1.7544 2.4468 2.9777 0.0921 -0.2727 0.1537 29 HIS B O 3212 C CB . HIS B 30 ? 1.7887 2.5736 3.0745 0.0503 -0.3169 0.1500 29 HIS B CB 3213 C CG . HIS B 30 ? 1.7757 2.6152 3.1114 0.0307 -0.3265 0.1469 29 HIS B CG 3214 N ND1 . HIS B 30 ? 1.7838 2.6795 3.1748 0.0396 -0.3453 0.1526 29 HIS B ND1 3215 C CD2 . HIS B 30 ? 1.7532 2.5990 3.0922 0.0019 -0.3206 0.1395 29 HIS B CD2 3216 C CE1 . HIS B 30 ? 1.7602 2.6960 3.1884 0.0154 -0.3501 0.1488 29 HIS B CE1 3217 N NE2 . HIS B 30 ? 1.7504 2.6545 3.1464 -0.0077 -0.3352 0.1409 29 HIS B NE2 3218 N N . TYR B 31 ? 1.7961 2.5303 3.0516 0.1160 -0.3167 0.1677 30 TYR B N 3219 C CA . TYR B 31 ? 1.8195 2.5005 3.0286 0.1350 -0.3162 0.1749 30 TYR B CA 3220 C C . TYR B 31 ? 1.7894 2.4160 2.9347 0.1177 -0.3135 0.1730 30 TYR B C 3221 O O . TYR B 31 ? 1.7814 2.3605 2.8896 0.1252 -0.2995 0.1755 30 TYR B O 3222 C CB . TYR B 31 ? 1.8815 2.5739 3.0967 0.1574 -0.3451 0.1869 30 TYR B CB 3223 C CG . TYR B 31 ? 1.9138 2.6445 3.1821 0.1853 -0.3435 0.1916 30 TYR B CG 3224 C CD1 . TYR B 31 ? 1.9170 2.7165 3.2493 0.1840 -0.3529 0.1904 30 TYR B CD1 3225 C CD2 . TYR B 31 ? 1.9387 2.6367 3.1940 0.2133 -0.3324 0.1976 30 TYR B CD2 3226 C CE1 . TYR B 31 ? 1.9286 2.7667 3.3119 0.2115 -0.3501 0.1952 30 TYR B CE1 3227 C CE2 . TYR B 31 ? 1.9584 2.6895 3.2608 0.2416 -0.3302 0.2016 30 TYR B CE2 3228 C CZ . TYR B 31 ? 1.9554 2.7583 3.3225 0.2415 -0.3385 0.2004 30 TYR B CZ 3229 O OH . TYR B 31 ? 1.9906 2.8299 3.4068 0.2715 -0.3350 0.2048 30 TYR B OH 3230 N N . LEU B 32 ? 1.7628 2.3963 2.8959 0.0944 -0.3266 0.1686 31 LEU B N 3231 C CA . LEU B 32 ? 1.7533 2.3389 2.8269 0.0793 -0.3243 0.1668 31 LEU B CA 3232 C C . LEU B 32 ? 1.6972 2.2626 2.7582 0.0629 -0.2952 0.1575 31 LEU B C 3233 O O . LEU B 32 ? 1.6397 2.1669 2.6542 0.0515 -0.2899 0.1560 31 LEU B O 3234 C CB . LEU B 32 ? 1.7842 2.3785 2.8425 0.0628 -0.3501 0.1649 31 LEU B CB 3235 C CG . LEU B 32 ? 1.7940 2.4351 2.8949 0.0427 -0.3572 0.1563 31 LEU B CG 3236 C CD1 . LEU B 32 ? 1.7997 2.4199 2.8635 0.0174 -0.3624 0.1485 31 LEU B CD1 3237 C CD2 . LEU B 32 ? 1.8210 2.5112 2.9661 0.0512 -0.3853 0.1611 31 LEU B CD2 3238 N N . CYS B 33 ? 1.6808 2.2724 2.7820 0.0624 -0.2765 0.1516 32 CYS B N 3239 C CA . CYS B 33 ? 1.6813 2.2532 2.7699 0.0498 -0.2492 0.1433 32 CYS B CA 3240 C C . CYS B 33 ? 1.6776 2.2085 2.7413 0.0648 -0.2325 0.1461 32 CYS B C 3241 O O . CYS B 33 ? 1.7092 2.2414 2.7878 0.0873 -0.2331 0.1517 32 CYS B O 3242 C CB . CYS B 33 ? 1.7042 2.3176 2.8413 0.0440 -0.2346 0.1363 32 CYS B CB 3243 S SG . CYS B 33 ? 1.7652 2.4331 2.9441 0.0252 -0.2523 0.1337 32 CYS B SG 3244 N N . SER B 34 ? 1.6480 2.1424 2.6746 0.0522 -0.2178 0.1422 33 SER B N 3245 C CA . SER B 34 ? 1.6371 2.0906 2.6389 0.0617 -0.2021 0.1441 33 SER B CA 3246 C C . SER B 34 ? 1.6021 2.0654 2.6319 0.0693 -0.1817 0.1372 33 SER B C 3247 O O . SER B 34 ? 1.5472 2.0334 2.5962 0.0571 -0.1702 0.1285 33 SER B O 3248 C CB . SER B 34 ? 1.6178 2.0360 2.5767 0.0441 -0.1930 0.1418 33 SER B CB 3249 O OG . SER B 34 ? 1.6176 1.9961 2.5528 0.0507 -0.1800 0.1446 33 SER B OG 3250 N N . LYS B 35 ? 1.6124 2.0558 2.6416 0.0901 -0.1772 0.1412 34 LYS B N 3251 C CA . LYS B 35 ? 1.5876 2.0304 2.6345 0.1002 -0.1570 0.1340 34 LYS B CA 3252 C C . LYS B 35 ? 1.5846 1.9880 2.5991 0.0878 -0.1391 0.1274 34 LYS B C 3253 O O . LYS B 35 ? 1.5681 1.9777 2.5923 0.0834 -0.1218 0.1174 34 LYS B O 3254 C CB . LYS B 35 ? 1.6009 2.0307 2.6554 0.1288 -0.1598 0.1404 34 LYS B CB 3255 C CG . LYS B 35 ? 1.5896 2.0678 2.6931 0.1474 -0.1658 0.1419 34 LYS B CG 3256 C CD . LYS B 35 ? 1.6133 2.0731 2.7228 0.1772 -0.1605 0.1446 34 LYS B CD 3257 C CE . LYS B 35 ? 1.6066 2.1189 2.7692 0.1977 -0.1627 0.1454 34 LYS B CE 3258 N NZ . LYS B 35 ? 1.6185 2.1592 2.7990 0.2066 -0.1895 0.1570 34 LYS B NZ 3259 N N . LYS B 36 ? 1.6008 1.9649 2.5768 0.0822 -0.1436 0.1336 35 LYS B N 3260 C CA . LYS B 36 ? 1.6023 1.9275 2.5490 0.0720 -0.1288 0.1294 35 LYS B CA 3261 C C . LYS B 36 ? 1.5839 1.8932 2.4985 0.0527 -0.1327 0.1332 35 LYS B C 3262 O O . LYS B 36 ? 1.5893 1.8972 2.4908 0.0537 -0.1478 0.1426 35 LYS B O 3263 C CB . LYS B 36 ? 1.6420 1.9269 2.5747 0.0889 -0.1262 0.1345 35 LYS B CB 3264 C CG . LYS B 36 ? 1.6747 1.9211 2.5838 0.0792 -0.1106 0.1284 35 LYS B CG 3265 C CD . LYS B 36 ? 1.7555 1.9599 2.6525 0.0960 -0.1087 0.1327 35 LYS B CD 3266 C CE . LYS B 36 ? 1.8119 1.9793 2.6889 0.0851 -0.0942 0.1246 35 LYS B CE 3267 N NZ . LYS B 36 ? 1.8301 2.0136 2.7237 0.0851 -0.0806 0.1089 35 LYS B NZ 3268 N N . THR B 37 ? 1.5514 1.8495 2.4527 0.0363 -0.1192 0.1258 36 THR B N 3269 C CA . THR B 37 ? 1.5413 1.8192 2.4108 0.0202 -0.1189 0.1295 36 THR B CA 3270 C C . THR B 37 ? 1.5852 1.8255 2.4355 0.0166 -0.1065 0.1289 36 THR B C 3271 O O . THR B 37 ? 1.5458 1.7805 2.4064 0.0200 -0.0960 0.1204 36 THR B O 3272 C CB . THR B 37 ? 1.4952 1.7954 2.3663 0.0022 -0.1151 0.1218 36 THR B CB 3273 O OG1 . THR B 37 ? 1.4543 1.7639 2.3409 -0.0014 -0.1011 0.1106 36 THR B OG1 3274 C CG2 . THR B 37 ? 1.4894 1.8221 2.3759 0.0022 -0.1292 0.1228 36 THR B CG2 3275 N N . GLU B 38 ? 1.6608 1.8751 2.4826 0.0094 -0.1079 0.1379 37 GLU B N 3276 C CA . GLU B 38 ? 1.6971 1.8756 2.5013 0.0029 -0.0975 0.1391 37 GLU B CA 3277 C C . GLU B 38 ? 1.6233 1.8075 2.4271 -0.0146 -0.0856 0.1286 37 GLU B C 3278 O O . GLU B 38 ? 1.6296 1.7920 2.4290 -0.0197 -0.0768 0.1243 37 GLU B O 3279 C CB . GLU B 38 ? 1.7660 1.9188 2.5415 -0.0004 -0.1015 0.1539 37 GLU B CB 3280 C CG . GLU B 38 ? 1.8255 1.9642 2.5952 0.0175 -0.1133 0.1662 37 GLU B CG 3281 C CD . GLU B 38 ? 1.8900 2.0051 2.6277 0.0143 -0.1169 0.1821 37 GLU B CD 3282 O OE1 . GLU B 38 ? 1.9035 2.0121 2.6249 -0.0020 -0.1082 0.1837 37 GLU B OE1 3283 O OE2 . GLU B 38 ? 1.9300 2.0336 2.6585 0.0291 -0.1280 0.1935 37 GLU B OE2 3284 N N . SER B 39 ? 1.5365 1.7486 2.3439 -0.0237 -0.0865 0.1246 38 SER B N 3285 C CA . SER B 39 ? 1.4918 1.7116 2.2979 -0.0389 -0.0767 0.1158 38 SER B CA 3286 C C . SER B 39 ? 1.4449 1.6987 2.2661 -0.0415 -0.0783 0.1084 38 SER B C 3287 O O . SER B 39 ? 1.4569 1.7290 2.2920 -0.0328 -0.0870 0.1097 38 SER B O 3288 C CB . SER B 39 ? 1.4891 1.6970 2.2723 -0.0513 -0.0746 0.1232 38 SER B CB 3289 O OG . SER B 39 ? 1.4650 1.6801 2.2370 -0.0487 -0.0838 0.1316 38 SER B OG 3290 N N . TYR B 40 ? 1.3681 1.6302 2.1874 -0.0538 -0.0705 0.1011 39 TYR B N 3291 C CA . TYR B 40 ? 1.3249 1.6143 2.1536 -0.0588 -0.0715 0.0956 39 TYR B CA 3292 C C . TYR B 40 ? 1.3484 1.6424 2.1637 -0.0623 -0.0808 0.1023 39 TYR B C 3293 O O . TYR B 40 ? 1.3606 1.6378 2.1548 -0.0652 -0.0811 0.1092 39 TYR B O 3294 C CB . TYR B 40 ? 1.2866 1.5794 2.1123 -0.0700 -0.0611 0.0875 39 TYR B CB 3295 C CG . TYR B 40 ? 1.2659 1.5645 2.1063 -0.0665 -0.0531 0.0780 39 TYR B CG 3296 C CD1 . TYR B 40 ? 1.2664 1.5897 2.1234 -0.0657 -0.0513 0.0730 39 TYR B CD1 3297 C CD2 . TYR B 40 ? 1.2598 1.5381 2.0961 -0.0645 -0.0470 0.0740 39 TYR B CD2 3298 C CE1 . TYR B 40 ? 1.2693 1.5983 2.1374 -0.0615 -0.0420 0.0648 39 TYR B CE1 3299 C CE2 . TYR B 40 ? 1.2531 1.5344 2.0983 -0.0600 -0.0393 0.0644 39 TYR B CE2 3300 C CZ . TYR B 40 ? 1.2601 1.5676 2.1206 -0.0577 -0.0360 0.0601 39 TYR B CZ 3301 O OH . TYR B 40 ? 1.2874 1.5982 2.1544 -0.0522 -0.0264 0.0511 39 TYR B OH 3302 N N . PHE B 41 ? 1.3646 1.6804 2.1915 -0.0621 -0.0881 0.1001 40 PHE B N 3303 C CA . PHE B 41 ? 1.3803 1.6988 2.1925 -0.0653 -0.0987 0.1043 40 PHE B CA 3304 C C . PHE B 41 ? 1.3460 1.6839 2.1667 -0.0742 -0.0991 0.0971 40 PHE B C 3305 O O . PHE B 41 ? 1.3266 1.6799 2.1688 -0.0756 -0.0930 0.0911 40 PHE B O 3306 C CB . PHE B 41 ? 1.4040 1.7250 2.2200 -0.0546 -0.1136 0.1111 40 PHE B CB 3307 C CG . PHE B 41 ? 1.3828 1.7315 2.2297 -0.0508 -0.1208 0.1074 40 PHE B CG 3308 C CD1 . PHE B 41 ? 1.3904 1.7488 2.2633 -0.0423 -0.1148 0.1048 40 PHE B CD1 3309 C CD2 . PHE B 41 ? 1.3635 1.7288 2.2137 -0.0559 -0.1335 0.1064 40 PHE B CD2 3310 C CE1 . PHE B 41 ? 1.3808 1.7691 2.2856 -0.0384 -0.1197 0.1023 40 PHE B CE1 3311 C CE2 . PHE B 41 ? 1.3548 1.7493 2.2378 -0.0543 -0.1402 0.1038 40 PHE B CE2 3312 C CZ . PHE B 41 ? 1.3549 1.7631 2.2668 -0.0453 -0.1325 0.1024 40 PHE B CZ 3313 N N . THR B 42 ? 1.3543 1.6890 2.1559 -0.0798 -0.1056 0.0981 41 THR B N 3314 C CA . THR B 42 ? 1.3589 1.7051 2.1631 -0.0892 -0.1065 0.0919 41 THR B CA 3315 C C . THR B 42 ? 1.3755 1.7436 2.2047 -0.0893 -0.1178 0.0903 41 THR B C 3316 O O . THR B 42 ? 1.3806 1.7503 2.2067 -0.0856 -0.1328 0.0941 41 THR B O 3317 C CB . THR B 42 ? 1.3656 1.6976 2.1386 -0.0935 -0.1111 0.0929 41 THR B CB 3318 O OG1 . THR B 42 ? 1.3731 1.6889 2.1258 -0.0927 -0.1005 0.0960 41 THR B OG1 3319 C CG2 . THR B 42 ? 1.3555 1.6932 2.1282 -0.1033 -0.1110 0.0862 41 THR B CG2 3320 N N . ILE B 43 ? 1.3900 1.7764 2.2440 -0.0937 -0.1106 0.0854 42 ILE B N 3321 C CA . ILE B 43 ? 1.4280 1.8403 2.3110 -0.0963 -0.1193 0.0843 42 ILE B CA 3322 C C . ILE B 43 ? 1.4108 1.8250 2.2878 -0.1103 -0.1243 0.0806 42 ILE B C 3323 O O . ILE B 43 ? 1.3716 1.7995 2.2611 -0.1151 -0.1386 0.0808 42 ILE B O 3324 C CB . ILE B 43 ? 1.4669 1.9002 2.3825 -0.0922 -0.1077 0.0822 42 ILE B CB 3325 C CG1 . ILE B 43 ? 1.5104 1.9746 2.4612 -0.0901 -0.1180 0.0840 42 ILE B CG1 3326 C CG2 . ILE B 43 ? 1.4527 1.8878 2.3683 -0.1016 -0.0927 0.0769 42 ILE B CG2 3327 C CD1 . ILE B 43 ? 1.5085 1.9951 2.4918 -0.0825 -0.1055 0.0828 42 ILE B CD1 3328 N N . TRP B 44 ? 1.4073 1.8068 2.2648 -0.1168 -0.1134 0.0774 43 TRP B N 3329 C CA . TRP B 44 ? 1.4114 1.8046 2.2567 -0.1288 -0.1170 0.0740 43 TRP B CA 3330 C C . TRP B 44 ? 1.4114 1.7779 2.2198 -0.1281 -0.1117 0.0731 43 TRP B C 3331 O O . TRP B 44 ? 1.4352 1.7964 2.2385 -0.1248 -0.0984 0.0732 43 TRP B O 3332 C CB . TRP B 44 ? 1.4144 1.8218 2.2800 -0.1375 -0.1062 0.0712 43 TRP B CB 3333 C CG . TRP B 44 ? 1.4290 1.8262 2.2819 -0.1502 -0.1095 0.0685 43 TRP B CG 3334 C CD1 . TRP B 44 ? 1.4425 1.8218 2.2734 -0.1540 -0.0999 0.0664 43 TRP B CD1 3335 C CD2 . TRP B 44 ? 1.4381 1.8403 2.2983 -0.1606 -0.1247 0.0675 43 TRP B CD2 3336 N NE1 . TRP B 44 ? 1.4637 1.8334 2.2863 -0.1654 -0.1071 0.0642 43 TRP B NE1 3337 C CE2 . TRP B 44 ? 1.4396 1.8224 2.2796 -0.1709 -0.1226 0.0645 43 TRP B CE2 3338 C CE3 . TRP B 44 ? 1.4356 1.8565 2.3177 -0.1624 -0.1410 0.0688 43 TRP B CE3 3339 C CZ2 . TRP B 44 ? 1.4177 1.7959 2.2574 -0.1841 -0.1360 0.0621 43 TRP B CZ2 3340 C CZ3 . TRP B 44 ? 1.4206 1.8410 2.3048 -0.1764 -0.1553 0.0665 43 TRP B CZ3 3341 C CH2 . TRP B 44 ? 1.4129 1.8103 2.2751 -0.1877 -0.1526 0.0629 43 TRP B CH2 3342 N N . LEU B 45 ? 1.4108 1.7610 2.1935 -0.1306 -0.1221 0.0722 44 LEU B N 3343 C CA . LEU B 45 ? 1.4399 1.7933 2.2242 -0.1349 -0.1409 0.0713 44 LEU B CA 3344 C C . LEU B 45 ? 1.4544 1.8006 2.2232 -0.1248 -0.1518 0.0757 44 LEU B C 3345 O O . LEU B 45 ? 1.4693 1.7956 2.2078 -0.1184 -0.1473 0.0777 44 LEU B O 3346 C CB . LEU B 45 ? 1.4861 1.8198 2.2451 -0.1438 -0.1459 0.0662 44 LEU B CB 3347 C CG . LEU B 45 ? 1.5436 1.8722 2.2937 -0.1493 -0.1674 0.0635 44 LEU B CG 3348 C CD1 . LEU B 45 ? 1.5447 1.9032 2.3356 -0.1562 -0.1783 0.0645 44 LEU B CD1 3349 C CD2 . LEU B 45 ? 1.5720 1.8764 2.2963 -0.1585 -0.1698 0.0573 44 LEU B CD2 3350 N N . ASN B 46 ? 1.4601 1.8238 2.2504 -0.1227 -0.1657 0.0780 45 ASN B N 3351 C CA . ASN B 46 ? 1.5076 1.8636 2.2809 -0.1132 -0.1794 0.0828 45 ASN B CA 3352 C C . ASN B 46 ? 1.5119 1.8784 2.2928 -0.1187 -0.2024 0.0807 45 ASN B C 3353 O O . ASN B 46 ? 1.4681 1.8628 2.2871 -0.1203 -0.2092 0.0817 45 ASN B O 3354 C CB . ASN B 46 ? 1.5363 1.9017 2.3270 -0.1008 -0.1744 0.0897 45 ASN B CB 3355 C CG . ASN B 46 ? 1.5951 1.9440 2.3588 -0.0897 -0.1836 0.0967 45 ASN B CG 3356 O OD1 . ASN B 46 ? 1.6153 1.9549 2.3559 -0.0901 -0.1996 0.0964 45 ASN B OD1 3357 N ND2 . ASN B 46 ? 1.6238 1.9664 2.3877 -0.0799 -0.1735 0.1031 45 ASN B ND2 3358 N N . LEU B 47 ? 1.5497 1.8940 2.2940 -0.1212 -0.2143 0.0776 46 LEU B N 3359 C CA . LEU B 47 ? 1.5991 1.9485 2.3447 -0.1290 -0.2384 0.0737 46 LEU B CA 3360 C C . LEU B 47 ? 1.5880 1.9549 2.3481 -0.1200 -0.2563 0.0796 46 LEU B C 3361 O O . LEU B 47 ? 1.5794 1.9672 2.3637 -0.1271 -0.2752 0.0778 46 LEU B O 3362 C CB . LEU B 47 ? 1.6749 1.9904 2.3701 -0.1313 -0.2465 0.0681 46 LEU B CB 3363 C CG . LEU B 47 ? 1.7029 1.9988 2.3811 -0.1392 -0.2319 0.0616 46 LEU B CG 3364 C CD1 . LEU B 47 ? 1.7612 2.0210 2.3852 -0.1364 -0.2382 0.0565 46 LEU B CD1 3365 C CD2 . LEU B 47 ? 1.6915 2.0021 2.4015 -0.1563 -0.2352 0.0564 46 LEU B CD2 3366 N N . GLU B 48 ? 1.5890 1.9476 2.3354 -0.1047 -0.2507 0.0875 47 GLU B N 3367 C CA . GLU B 48 ? 1.6182 1.9897 2.3748 -0.0934 -0.2673 0.0946 47 GLU B CA 3368 C C . GLU B 48 ? 1.5652 1.9756 2.3788 -0.0923 -0.2683 0.0968 47 GLU B C 3369 O O . GLU B 48 ? 1.5474 1.9776 2.3797 -0.0864 -0.2874 0.1007 47 GLU B O 3370 C CB . GLU B 48 ? 1.6818 2.0321 2.4104 -0.0776 -0.2583 0.1039 47 GLU B CB 3371 C CG . GLU B 48 ? 1.7539 2.0694 2.4256 -0.0755 -0.2588 0.1040 47 GLU B CG 3372 C CD . GLU B 48 ? 1.8113 2.1076 2.4578 -0.0614 -0.2491 0.1151 47 GLU B CD 3373 O OE1 . GLU B 48 ? 1.7929 2.0929 2.4587 -0.0576 -0.2315 0.1198 47 GLU B OE1 3374 O OE2 . GLU B 48 ? 1.8953 2.1710 2.5005 -0.0546 -0.2591 0.1194 47 GLU B OE2 3375 N N . LEU B 49 ? 1.5304 1.9524 2.3707 -0.0970 -0.2477 0.0946 48 LEU B N 3376 C CA . LEU B 49 ? 1.5284 1.9868 2.4211 -0.0947 -0.2441 0.0964 48 LEU B CA 3377 C C . LEU B 49 ? 1.5394 2.0273 2.4663 -0.1103 -0.2549 0.0915 48 LEU B C 3378 O O . LEU B 49 ? 1.5150 2.0390 2.4889 -0.1086 -0.2544 0.0936 48 LEU B O 3379 C CB . LEU B 49 ? 1.5236 1.9805 2.4270 -0.0922 -0.2170 0.0959 48 LEU B CB 3380 C CG . LEU B 49 ? 1.5528 1.9845 2.4317 -0.0782 -0.2052 0.1011 48 LEU B CG 3381 C CD1 . LEU B 49 ? 1.5508 1.9789 2.4367 -0.0795 -0.1806 0.0983 48 LEU B CD1 3382 C CD2 . LEU B 49 ? 1.5726 2.0132 2.4656 -0.0612 -0.2146 0.1090 48 LEU B CD2 3383 N N . LEU B 50 ? 1.6012 2.0735 2.5052 -0.1254 -0.2640 0.0851 49 LEU B N 3384 C CA . LEU B 50 ? 1.6441 2.1383 2.5772 -0.1443 -0.2728 0.0802 49 LEU B CA 3385 C C . LEU B 50 ? 1.6820 2.1873 2.6187 -0.1501 -0.3045 0.0790 49 LEU B C 3386 O O . LEU B 50 ? 1.6732 2.1943 2.6319 -0.1683 -0.3157 0.0747 49 LEU B O 3387 C CB . LEU B 50 ? 1.6604 2.1278 2.5677 -0.1591 -0.2615 0.0733 49 LEU B CB 3388 C CG . LEU B 50 ? 1.6500 2.1054 2.5503 -0.1542 -0.2324 0.0740 49 LEU B CG 3389 C CD1 . LEU B 50 ? 1.6595 2.0919 2.5385 -0.1685 -0.2239 0.0679 49 LEU B CD1 3390 C CD2 . LEU B 50 ? 1.6315 2.1208 2.5786 -0.1501 -0.2173 0.0779 49 LEU B CD2 3391 N N . LEU B 51 ? 1.7203 2.2172 2.6357 -0.1353 -0.3196 0.0832 50 LEU B N 3392 C CA . LEU B 51 ? 1.7746 2.2823 2.6910 -0.1384 -0.3518 0.0825 50 LEU B CA 3393 C C . LEU B 51 ? 1.7413 2.3025 2.7224 -0.1373 -0.3610 0.0874 50 LEU B C 3394 O O . LEU B 51 ? 1.6914 2.2749 2.7065 -0.1269 -0.3422 0.0928 50 LEU B O 3395 C CB . LEU B 51 ? 1.8421 2.3229 2.7122 -0.1209 -0.3636 0.0870 50 LEU B CB 3396 C CG . LEU B 51 ? 1.8819 2.3140 2.6912 -0.1170 -0.3486 0.0849 50 LEU B CG 3397 C CD1 . LEU B 51 ? 1.9055 2.3151 2.6728 -0.0990 -0.3584 0.0918 50 LEU B CD1 3398 C CD2 . LEU B 51 ? 1.9125 2.3206 2.6931 -0.1349 -0.3538 0.0738 50 LEU B CD2 3399 N N . PRO B 52 ? 1.7519 2.3351 2.7511 -0.1477 -0.3903 0.0853 51 PRO B N 3400 C CA . PRO B 52 ? 1.7462 2.3845 2.8086 -0.1444 -0.4016 0.0911 51 PRO B CA 3401 C C . PRO B 52 ? 1.7369 2.3868 2.8097 -0.1162 -0.3965 0.1012 51 PRO B C 3402 O O . PRO B 52 ? 1.7389 2.3540 2.7649 -0.1006 -0.3979 0.1044 51 PRO B O 3403 C CB . PRO B 52 ? 1.7726 2.4198 2.8330 -0.1558 -0.4395 0.0874 51 PRO B CB 3404 C CG . PRO B 52 ? 1.7850 2.3904 2.8003 -0.1759 -0.4413 0.0767 51 PRO B CG 3405 C CD . PRO B 52 ? 1.7729 2.3327 2.7387 -0.1649 -0.4135 0.0764 51 PRO B CD 3406 N N . VAL B 53 ? 1.7045 2.4022 2.8382 -0.1098 -0.3902 0.1065 52 VAL B N 3407 C CA . VAL B 53 ? 1.6717 2.3835 2.8235 -0.0823 -0.3829 0.1158 52 VAL B CA 3408 C C . VAL B 53 ? 1.6745 2.3558 2.8041 -0.0713 -0.3493 0.1165 52 VAL B C 3409 O O . VAL B 53 ? 1.6141 2.3184 2.7808 -0.0636 -0.3284 0.1186 52 VAL B O 3410 C CB . VAL B 53 ? 1.6651 2.3747 2.8005 -0.0640 -0.4117 0.1226 52 VAL B CB 3411 C CG1 . VAL B 53 ? 1.6929 2.4138 2.8259 -0.0800 -0.4470 0.1185 52 VAL B CG1 3412 C CG2 . VAL B 53 ? 1.6544 2.3105 2.7268 -0.0480 -0.4052 0.1263 52 VAL B CG2 3413 N N . ILE B 54 ? 1.7490 2.3793 2.8186 -0.0716 -0.3438 0.1143 53 ILE B N 3414 C CA . ILE B 54 ? 1.7884 2.3882 2.8345 -0.0637 -0.3144 0.1147 53 ILE B CA 3415 C C . ILE B 54 ? 1.7432 2.3553 2.8138 -0.0777 -0.2903 0.1087 53 ILE B C 3416 O O . ILE B 54 ? 1.7274 2.3354 2.8042 -0.0691 -0.2663 0.1095 53 ILE B O 3417 C CB . ILE B 54 ? 1.8555 2.4028 2.8355 -0.0647 -0.3131 0.1134 53 ILE B CB 3418 C CG1 . ILE B 54 ? 1.9259 2.4578 2.8765 -0.0490 -0.3344 0.1209 53 ILE B CG1 3419 C CG2 . ILE B 54 ? 1.8338 2.3544 2.7954 -0.0593 -0.2834 0.1136 53 ILE B CG2 3420 C CD1 . ILE B 54 ? 1.9554 2.4806 2.8799 -0.0590 -0.3626 0.1173 53 ILE B CD1 3421 N N . ILE B 55 ? 1.7199 2.3450 2.8026 -0.0996 -0.2976 0.1030 54 ILE B N 3422 C CA . ILE B 55 ? 1.6909 2.3291 2.7974 -0.1143 -0.2766 0.0987 54 ILE B CA 3423 C C . ILE B 55 ? 1.6250 2.3016 2.7824 -0.1038 -0.2593 0.1026 54 ILE B C 3424 O O . ILE B 55 ? 1.5715 2.2454 2.7332 -0.1067 -0.2341 0.1004 54 ILE B O 3425 C CB . ILE B 55 ? 1.7117 2.3657 2.8344 -0.1395 -0.2912 0.0940 54 ILE B CB 3426 C CG1 . ILE B 55 ? 1.7151 2.3737 2.8529 -0.1552 -0.2674 0.0908 54 ILE B CG1 3427 C CG2 . ILE B 55 ? 1.7060 2.4092 2.8795 -0.1405 -0.3139 0.0979 54 ILE B CG2 3428 C CD1 . ILE B 55 ? 1.7364 2.3467 2.8224 -0.1622 -0.2544 0.0853 54 ILE B CD1 3429 N N . ASP B 56 ? 1.5850 2.2972 2.7797 -0.0906 -0.2728 0.1084 55 ASP B N 3430 C CA . ASP B 56 ? 1.5400 2.2904 2.7840 -0.0780 -0.2560 0.1120 55 ASP B CA 3431 C C . ASP B 56 ? 1.5450 2.2675 2.7671 -0.0589 -0.2320 0.1122 55 ASP B C 3432 O O . ASP B 56 ? 1.4842 2.2198 2.7274 -0.0558 -0.2081 0.1108 55 ASP B O 3433 C CB . ASP B 56 ? 1.5357 2.3305 2.8242 -0.0649 -0.2767 0.1185 55 ASP B CB 3434 C CG . ASP B 56 ? 1.5227 2.3595 2.8513 -0.0860 -0.2960 0.1181 55 ASP B CG 3435 O OD1 . ASP B 56 ? 1.4717 2.3156 2.8114 -0.1085 -0.2848 0.1141 55 ASP B OD1 3436 O OD2 . ASP B 56 ? 1.5632 2.4262 2.9129 -0.0804 -0.3231 0.1223 55 ASP B OD2 3437 N N . CYS B 57 ? 1.6070 2.2898 2.7852 -0.0471 -0.2385 0.1141 56 CYS B N 3438 C CA . CYS B 57 ? 1.6421 2.2925 2.7952 -0.0320 -0.2180 0.1142 56 CYS B CA 3439 C C . CYS B 57 ? 1.6091 2.2354 2.7383 -0.0465 -0.1959 0.1074 56 CYS B C 3440 O O . CYS B 57 ? 1.6369 2.2591 2.7703 -0.0397 -0.1737 0.1051 56 CYS B O 3441 C CB . CYS B 57 ? 1.6953 2.3072 2.8051 -0.0200 -0.2301 0.1190 56 CYS B CB 3442 S SG . CYS B 57 ? 1.7774 2.4103 2.9021 -0.0052 -0.2621 0.1278 56 CYS B SG 3443 N N . TRP B 58 ? 1.5591 2.1685 2.6617 -0.0653 -0.2031 0.1038 57 TRP B N 3444 C CA . TRP B 58 ? 1.5064 2.0928 2.5848 -0.0791 -0.1852 0.0980 57 TRP B CA 3445 C C . TRP B 58 ? 1.4593 2.0746 2.5731 -0.0871 -0.1675 0.0952 57 TRP B C 3446 O O . TRP B 58 ? 1.4137 2.0170 2.5189 -0.0851 -0.1458 0.0923 57 TRP B O 3447 C CB . TRP B 58 ? 1.5117 2.0780 2.5589 -0.0962 -0.1989 0.0949 57 TRP B CB 3448 C CG . TRP B 58 ? 1.4851 2.0272 2.5062 -0.1091 -0.1830 0.0895 57 TRP B CG 3449 C CD1 . TRP B 58 ? 1.4834 1.9909 2.4666 -0.1052 -0.1707 0.0882 57 TRP B CD1 3450 C CD2 . TRP B 58 ? 1.4645 2.0155 2.4961 -0.1280 -0.1784 0.0856 57 TRP B CD2 3451 N NE1 . TRP B 58 ? 1.4478 1.9435 2.4175 -0.1188 -0.1594 0.0834 57 TRP B NE1 3452 C CE2 . TRP B 58 ? 1.4549 1.9746 2.4520 -0.1327 -0.1635 0.0819 57 TRP B CE2 3453 C CE3 . TRP B 58 ? 1.4700 2.0529 2.5380 -0.1419 -0.1854 0.0855 57 TRP B CE3 3454 C CZ2 . TRP B 58 ? 1.4596 1.9757 2.4544 -0.1491 -0.1557 0.0784 57 TRP B CZ2 3455 C CZ3 . TRP B 58 ? 1.4641 2.0423 2.5299 -0.1603 -0.1768 0.0822 57 TRP B CZ3 3456 C CH2 . TRP B 58 ? 1.4560 1.9995 2.4840 -0.1629 -0.1621 0.0788 57 TRP B CH2 3457 N N . ILE B 59 ? 1.4499 2.1036 2.6032 -0.0965 -0.1772 0.0967 58 ILE B N 3458 C CA . ILE B 59 ? 1.4499 2.1360 2.6410 -0.1046 -0.1603 0.0961 58 ILE B CA 3459 C C . ILE B 59 ? 1.4071 2.1060 2.6174 -0.0842 -0.1403 0.0972 58 ILE B C 3460 O O . ILE B 59 ? 1.3587 2.0574 2.5701 -0.0862 -0.1174 0.0945 58 ILE B O 3461 C CB . ILE B 59 ? 1.4965 2.2282 2.7347 -0.1167 -0.1759 0.0992 58 ILE B CB 3462 C CG1 . ILE B 59 ? 1.5222 2.2377 2.7401 -0.1407 -0.1927 0.0962 58 ILE B CG1 3463 C CG2 . ILE B 59 ? 1.4923 2.2635 2.7755 -0.1210 -0.1553 0.1010 58 ILE B CG2 3464 C CD1 . ILE B 59 ? 1.5372 2.2915 2.7956 -0.1538 -0.2152 0.0986 58 ILE B CD1 3465 N N . ASP B 60 ? 1.3975 2.1047 2.6196 -0.0637 -0.1493 0.1010 59 ASP B N 3466 C CA . ASP B 60 ? 1.3946 2.1107 2.6336 -0.0416 -0.1322 0.1015 59 ASP B CA 3467 C C . ASP B 60 ? 1.3916 2.0652 2.5903 -0.0367 -0.1124 0.0962 59 ASP B C 3468 O O . ASP B 60 ? 1.3693 2.0481 2.5780 -0.0258 -0.0920 0.0936 59 ASP B O 3469 C CB . ASP B 60 ? 1.4229 2.1462 2.6737 -0.0196 -0.1486 0.1072 59 ASP B CB 3470 C CG . ASP B 60 ? 1.4246 2.1698 2.7069 0.0042 -0.1337 0.1084 59 ASP B CG 3471 O OD1 . ASP B 60 ? 1.4069 2.1768 2.7145 0.0025 -0.1132 0.1058 59 ASP B OD1 3472 O OD2 . ASP B 60 ? 1.4401 2.1763 2.7202 0.0260 -0.1422 0.1123 59 ASP B OD2 3473 N N . ASN B 61 ? 1.4029 2.0356 2.5564 -0.0446 -0.1186 0.0945 60 ASN B N 3474 C CA . ASN B 61 ? 1.4062 1.9991 2.5216 -0.0422 -0.1031 0.0899 60 ASN B CA 3475 C C . ASN B 61 ? 1.3558 1.9419 2.4578 -0.0596 -0.0884 0.0847 60 ASN B C 3476 O O . ASN B 61 ? 1.3409 1.9131 2.4305 -0.0558 -0.0702 0.0802 60 ASN B O 3477 C CB . ASN B 61 ? 1.4388 1.9936 2.5141 -0.0411 -0.1159 0.0920 60 ASN B CB 3478 C CG . ASN B 61 ? 1.4821 2.0369 2.5633 -0.0231 -0.1306 0.0985 60 ASN B CG 3479 O OD1 . ASN B 61 ? 1.4937 2.0626 2.5993 -0.0058 -0.1255 0.0998 60 ASN B OD1 3480 N ND2 . ASN B 61 ? 1.5025 2.0397 2.5591 -0.0258 -0.1485 0.1027 60 ASN B ND2 3481 N N . ILE B 62 ? 1.3072 1.9004 2.4092 -0.0782 -0.0973 0.0852 61 ILE B N 3482 C CA . ILE B 62 ? 1.2835 1.8639 2.3668 -0.0946 -0.0860 0.0815 61 ILE B CA 3483 C C . ILE B 62 ? 1.2566 1.8671 2.3700 -0.1020 -0.0707 0.0814 61 ILE B C 3484 O O . ILE B 62 ? 1.2066 1.8052 2.3037 -0.1108 -0.0566 0.0787 61 ILE B O 3485 C CB . ILE B 62 ? 1.2877 1.8529 2.3494 -0.1109 -0.1019 0.0816 61 ILE B CB 3486 C CG1 . ILE B 62 ? 1.2741 1.8138 2.3049 -0.1225 -0.0902 0.0778 61 ILE B CG1 3487 C CG2 . ILE B 62 ? 1.2795 1.8761 2.3737 -0.1231 -0.1152 0.0842 61 ILE B CG2 3488 C CD1 . ILE B 62 ? 1.2729 1.7881 2.2731 -0.1335 -0.1038 0.0769 61 ILE B CD1 3489 N N . ARG B 63 ? 1.2505 1.9010 2.4079 -0.0982 -0.0736 0.0851 62 ARG B N 3490 C CA . ARG B 63 ? 1.2276 1.9114 2.4179 -0.1040 -0.0570 0.0866 62 ARG B CA 3491 C C . ARG B 63 ? 1.1972 1.8719 2.3763 -0.0918 -0.0321 0.0827 62 ARG B C 3492 O O . ARG B 63 ? 1.1808 1.8366 2.3443 -0.0741 -0.0296 0.0796 62 ARG B O 3493 C CB . ARG B 63 ? 1.2429 1.9754 2.4865 -0.0981 -0.0640 0.0919 62 ARG B CB 3494 C CG . ARG B 63 ? 1.2558 1.9964 2.5126 -0.0711 -0.0614 0.0922 62 ARG B CG 3495 C CD . ARG B 63 ? 1.2555 2.0436 2.5636 -0.0644 -0.0744 0.0982 62 ARG B CD 3496 N NE . ARG B 63 ? 1.2591 2.0582 2.5839 -0.0364 -0.0672 0.0988 62 ARG B NE 3497 C CZ . ARG B 63 ? 1.2622 2.0819 2.6080 -0.0237 -0.0433 0.0977 62 ARG B CZ 3498 N NH1 . ARG B 63 ? 1.2640 2.0971 2.6168 -0.0370 -0.0235 0.0969 62 ARG B NH1 3499 N NH2 . ARG B 63 ? 1.2629 2.0876 2.6204 0.0035 -0.0387 0.0976 62 ARG B NH2 3500 N N . LEU B 64 ? 1.1876 1.8730 2.3721 -0.1019 -0.0143 0.0830 63 LEU B N 3501 C CA . LEU B 64 ? 1.2132 1.8960 2.3902 -0.0904 0.0100 0.0794 63 LEU B CA 3502 C C . LEU B 64 ? 1.2140 1.9435 2.4385 -0.0808 0.0226 0.0831 63 LEU B C 3503 O O . LEU B 64 ? 1.2048 1.9706 2.4668 -0.0929 0.0187 0.0895 63 LEU B O 3504 C CB . LEU B 64 ? 1.2272 1.8927 2.3776 -0.1055 0.0234 0.0783 63 LEU B CB 3505 C CG . LEU B 64 ? 1.2327 1.8531 2.3351 -0.1120 0.0155 0.0742 63 LEU B CG 3506 C CD1 . LEU B 64 ? 1.2268 1.8360 2.3093 -0.1274 0.0266 0.0752 63 LEU B CD1 3507 C CD2 . LEU B 64 ? 1.2446 1.8375 2.3198 -0.0949 0.0194 0.0675 63 LEU B CD2 3508 N N . VAL B 65 ? 1.2347 1.9630 2.4577 -0.0592 0.0377 0.0789 64 VAL B N 3509 C CA . VAL B 65 ? 1.2610 2.0327 2.5267 -0.0456 0.0530 0.0817 64 VAL B CA 3510 C C . VAL B 65 ? 1.2854 2.0605 2.5417 -0.0485 0.0806 0.0804 64 VAL B C 3511 O O . VAL B 65 ? 1.2754 2.0150 2.4905 -0.0418 0.0914 0.0730 64 VAL B O 3512 C CB . VAL B 65 ? 1.2691 2.0353 2.5374 -0.0166 0.0538 0.0775 64 VAL B CB 3513 C CG1 . VAL B 65 ? 1.2675 2.0851 2.5874 -0.0010 0.0662 0.0818 64 VAL B CG1 3514 C CG2 . VAL B 65 ? 1.2693 2.0167 2.5300 -0.0133 0.0270 0.0785 64 VAL B CG2 3515 N N . TYR B 66 ? 1.3064 2.1238 2.6001 -0.0593 0.0916 0.0879 65 TYR B N 3516 C CA . TYR B 66 ? 1.3226 2.1451 2.6072 -0.0634 0.1188 0.0888 65 TYR B CA 3517 C C . TYR B 66 ? 1.3629 2.2115 2.6679 -0.0385 0.1420 0.0870 65 TYR B C 3518 O O . TYR B 66 ? 1.3729 2.2675 2.7287 -0.0297 0.1426 0.0924 65 TYR B O 3519 C CB . TYR B 66 ? 1.3050 2.1573 2.6176 -0.0896 0.1210 0.0991 65 TYR B CB 3520 C CG . TYR B 66 ? 1.3095 2.1563 2.6015 -0.0977 0.1469 0.1014 65 TYR B CG 3521 C CD1 . TYR B 66 ? 1.3019 2.1031 2.5425 -0.1097 0.1457 0.0985 65 TYR B CD1 3522 C CD2 . TYR B 66 ? 1.3147 2.2025 2.6380 -0.0922 0.1733 0.1072 65 TYR B CD2 3523 C CE1 . TYR B 66 ? 1.3012 2.0956 2.5198 -0.1162 0.1683 0.1015 65 TYR B CE1 3524 C CE2 . TYR B 66 ? 1.3143 2.1953 2.6149 -0.0992 0.1978 0.1104 65 TYR B CE2 3525 C CZ . TYR B 66 ? 1.3059 2.1390 2.5530 -0.1112 0.1944 0.1076 65 TYR B CZ 3526 O OH . TYR B 66 ? 1.3029 2.1277 2.5247 -0.1172 0.2177 0.1115 65 TYR B OH 3527 N N . ASN B 67 ? 1.4088 2.2279 2.6733 -0.0263 0.1604 0.0791 66 ASN B N 3528 C CA . ASN B 67 ? 1.4696 2.3066 2.7436 -0.0018 0.1857 0.0758 66 ASN B CA 3529 C C . ASN B 67 ? 1.4878 2.3494 2.7679 -0.0122 0.2124 0.0824 66 ASN B C 3530 O O . ASN B 67 ? 1.4969 2.3270 2.7325 -0.0214 0.2214 0.0798 66 ASN B O 3531 C CB . ASN B 67 ? 1.5230 2.3088 2.7445 0.0172 0.1890 0.0621 66 ASN B CB 3532 C CG . ASN B 67 ? 1.5981 2.3951 2.8248 0.0465 0.2126 0.0562 66 ASN B CG 3533 O OD1 . ASN B 67 ? 1.6558 2.5023 2.9279 0.0549 0.2278 0.0629 66 ASN B OD1 3534 N ND2 . ASN B 67 ? 1.6386 2.3886 2.8180 0.0626 0.2157 0.0431 66 ASN B ND2 3535 N N . LYS B 68 ? 1.5099 2.4289 2.8460 -0.0112 0.2246 0.0919 67 LYS B N 3536 C CA . LYS B 68 ? 1.5358 2.4850 2.8860 -0.0238 0.2505 0.1014 67 LYS B CA 3537 C C . LYS B 68 ? 1.5505 2.4840 2.8632 -0.0056 0.2816 0.0951 67 LYS B C 3538 O O . LYS B 68 ? 1.5489 2.4808 2.8433 -0.0186 0.3004 0.1005 67 LYS B O 3539 C CB . LYS B 68 ? 1.5422 2.5622 2.9673 -0.0256 0.2569 0.1134 67 LYS B CB 3540 C CG . LYS B 68 ? 1.5080 2.5506 2.9711 -0.0545 0.2319 0.1231 67 LYS B CG 3541 C CD . LYS B 68 ? 1.4876 2.6012 3.0205 -0.0638 0.2454 0.1369 67 LYS B CD 3542 C CE . LYS B 68 ? 1.4551 2.5892 3.0243 -0.0952 0.2196 0.1458 67 LYS B CE 3543 N NZ . LYS B 68 ? 1.4407 2.5910 3.0420 -0.0867 0.1894 0.1434 67 LYS B NZ 3544 N N . THR B 69 ? 1.5406 2.4603 2.8398 0.0245 0.2867 0.0838 68 THR B N 3545 C CA . THR B 69 ? 1.5576 2.4592 2.8179 0.0447 0.3149 0.0756 68 THR B CA 3546 C C . THR B 69 ? 1.5706 2.4101 2.7594 0.0363 0.3097 0.0665 68 THR B C 3547 O O . THR B 69 ? 1.5844 2.4145 2.7413 0.0328 0.3305 0.0673 68 THR B O 3548 C CB . THR B 69 ? 1.5565 2.4575 2.8219 0.0805 0.3209 0.0650 68 THR B CB 3549 O OG1 . THR B 69 ? 1.5383 2.3997 2.7855 0.0854 0.2921 0.0561 68 THR B OG1 3550 C CG2 . THR B 69 ? 1.5389 2.5073 2.8765 0.0924 0.3307 0.0748 68 THR B CG2 3551 N N . SER B 70 ? 1.5676 2.3665 2.7320 0.0330 0.2820 0.0588 69 SER B N 3552 C CA . SER B 70 ? 1.5804 2.3243 2.6823 0.0245 0.2742 0.0506 69 SER B CA 3553 C C . SER B 70 ? 1.5705 2.3090 2.6643 -0.0060 0.2641 0.0601 69 SER B C 3554 O O . SER B 70 ? 1.5601 2.2592 2.6043 -0.0136 0.2609 0.0555 69 SER B O 3555 C CB . SER B 70 ? 1.5719 2.2746 2.6509 0.0336 0.2503 0.0389 69 SER B CB 3556 O OG . SER B 70 ? 1.5171 2.2282 2.6254 0.0207 0.2245 0.0450 69 SER B OG 3557 N N . ARG B 71 ? 1.5681 2.3447 2.7098 -0.0232 0.2582 0.0730 70 ARG B N 3558 C CA . ARG B 71 ? 1.5625 2.3313 2.6982 -0.0522 0.2467 0.0818 70 ARG B CA 3559 C C . ARG B 71 ? 1.5324 2.2539 2.6306 -0.0589 0.2202 0.0744 70 ARG B C 3560 O O . ARG B 71 ? 1.5207 2.2120 2.5802 -0.0717 0.2177 0.0747 70 ARG B O 3561 C CB . ARG B 71 ? 1.6028 2.3677 2.7121 -0.0616 0.2702 0.0879 70 ARG B CB 3562 C CG . ARG B 71 ? 1.6369 2.4523 2.7864 -0.0593 0.2980 0.0982 70 ARG B CG 3563 C CD . ARG B 71 ? 1.6750 2.4870 2.8039 -0.0777 0.3159 0.1091 70 ARG B CD 3564 N NE . ARG B 71 ? 1.6620 2.4900 2.8225 -0.1069 0.3037 0.1222 70 ARG B NE 3565 C CZ . ARG B 71 ? 1.6587 2.5370 2.8755 -0.1189 0.3136 0.1352 70 ARG B CZ 3566 N NH1 . ARG B 71 ? 1.6837 2.6064 2.9352 -0.1031 0.3376 0.1379 70 ARG B NH1 3567 N NH2 . ARG B 71 ? 1.6297 2.5144 2.8691 -0.1470 0.2994 0.1453 70 ARG B NH2 3568 N N . ALA B 72 ? 1.4989 2.2152 2.6092 -0.0491 0.2010 0.0686 71 ALA B N 3569 C CA . ALA B 72 ? 1.4842 2.1589 2.5624 -0.0535 0.1773 0.0620 71 ALA B CA 3570 C C . ALA B 72 ? 1.4695 2.1550 2.5793 -0.0515 0.1551 0.0631 71 ALA B C 3571 O O . ALA B 72 ? 1.4904 2.2092 2.6402 -0.0394 0.1584 0.0654 71 ALA B O 3572 C CB . ALA B 72 ? 1.4945 2.1311 2.5276 -0.0367 0.1817 0.0490 71 ALA B CB 3573 N N . THR B 73 ? 1.4348 2.0928 2.5259 -0.0623 0.1328 0.0619 72 THR B N 3574 C CA . THR B 73 ? 1.3965 2.0598 2.5100 -0.0610 0.1105 0.0633 72 THR B CA 3575 C C . THR B 73 ? 1.3877 2.0218 2.4805 -0.0426 0.1033 0.0543 72 THR B C 3576 O O . THR B 73 ? 1.3902 1.9917 2.4444 -0.0373 0.1094 0.0463 72 THR B O 3577 C CB . THR B 73 ? 1.3830 2.0315 2.4864 -0.0821 0.0903 0.0673 72 THR B CB 3578 O OG1 . THR B 73 ? 1.3886 1.9955 2.4442 -0.0859 0.0882 0.0617 72 THR B OG1 3579 C CG2 . THR B 73 ? 1.3889 2.0631 2.5148 -0.1020 0.0944 0.0765 72 THR B CG2 3580 N N . GLN B 74 ? 1.3744 2.0200 2.4930 -0.0337 0.0894 0.0562 73 GLN B N 3581 C CA . GLN B 74 ? 1.3800 1.9962 2.4812 -0.0182 0.0796 0.0500 73 GLN B CA 3582 C C . GLN B 74 ? 1.3467 1.9620 2.4583 -0.0248 0.0549 0.0555 73 GLN B C 3583 O O . GLN B 74 ? 1.3174 1.9619 2.4579 -0.0362 0.0464 0.0629 73 GLN B O 3584 C CB . GLN B 74 ? 1.3998 2.0310 2.5224 0.0070 0.0908 0.0471 73 GLN B CB 3585 C CG . GLN B 74 ? 1.4154 2.0551 2.5331 0.0166 0.1175 0.0423 73 GLN B CG 3586 C CD . GLN B 74 ? 1.4224 2.0795 2.5638 0.0438 0.1292 0.0396 73 GLN B CD 3587 O OE1 . GLN B 74 ? 1.4066 2.0649 2.5654 0.0569 0.1164 0.0410 73 GLN B OE1 3588 N NE2 . GLN B 74 ? 1.4356 2.1052 2.5758 0.0539 0.1542 0.0361 73 GLN B NE2 3589 N N . PHE B 75 ? 1.3447 1.9258 2.4320 -0.0181 0.0433 0.0519 74 PHE B N 3590 C CA . PHE B 75 ? 1.3619 1.9402 2.4559 -0.0204 0.0212 0.0574 74 PHE B CA 3591 C C . PHE B 75 ? 1.3726 1.9764 2.5024 -0.0014 0.0177 0.0609 74 PHE B C 3592 O O . PHE B 75 ? 1.3447 1.9546 2.4839 0.0165 0.0323 0.0571 74 PHE B O 3593 C CB . PHE B 75 ? 1.3933 1.9268 2.4490 -0.0201 0.0118 0.0540 74 PHE B CB 3594 C CG . PHE B 75 ? 1.4068 1.9158 2.4278 -0.0352 0.0158 0.0499 74 PHE B CG 3595 C CD1 . PHE B 75 ? 1.3766 1.8971 2.3974 -0.0532 0.0151 0.0531 74 PHE B CD1 3596 C CD2 . PHE B 75 ? 1.4516 1.9251 2.4404 -0.0315 0.0192 0.0432 74 PHE B CD2 3597 C CE1 . PHE B 75 ? 1.3831 1.8813 2.3723 -0.0647 0.0182 0.0500 74 PHE B CE1 3598 C CE2 . PHE B 75 ? 1.4534 1.9080 2.4131 -0.0445 0.0214 0.0399 74 PHE B CE2 3599 C CZ . PHE B 75 ? 1.4168 1.8842 2.3766 -0.0599 0.0211 0.0435 74 PHE B CZ 3600 N N . PRO B 76 ? 1.3846 2.0030 2.5335 -0.0041 -0.0019 0.0681 75 PRO B N 3601 C CA . PRO B 76 ? 1.4088 2.0492 2.5898 0.0158 -0.0084 0.0721 75 PRO B CA 3602 C C . PRO B 76 ? 1.4398 2.0451 2.5994 0.0371 -0.0061 0.0680 75 PRO B C 3603 O O . PRO B 76 ? 1.4440 2.0065 2.5638 0.0325 -0.0068 0.0637 75 PRO B O 3604 C CB . PRO B 76 ? 1.3977 2.0467 2.5874 0.0064 -0.0337 0.0796 75 PRO B CB 3605 C CG . PRO B 76 ? 1.3738 2.0230 2.5523 -0.0196 -0.0360 0.0796 75 PRO B CG 3606 C CD . PRO B 76 ? 1.3691 1.9868 2.5117 -0.0246 -0.0191 0.0725 75 PRO B CD 3607 N N . ASP B 77 ? 1.4708 2.0940 2.6577 0.0603 -0.0035 0.0696 76 ASP B N 3608 C CA . ASP B 77 ? 1.5300 2.1171 2.6970 0.0819 -0.0006 0.0655 76 ASP B CA 3609 C C . ASP B 77 ? 1.5494 2.0981 2.6873 0.0781 -0.0202 0.0696 76 ASP B C 3610 O O . ASP B 77 ? 1.5752 2.1379 2.7248 0.0733 -0.0391 0.0780 76 ASP B O 3611 C CB . ASP B 77 ? 1.5800 2.1954 2.7843 0.1094 0.0031 0.0681 76 ASP B CB 3612 C CG . ASP B 77 ? 1.6481 2.2258 2.8310 0.1332 0.0146 0.0607 76 ASP B CG 3613 O OD1 . ASP B 77 ? 1.6858 2.2204 2.8280 0.1266 0.0223 0.0522 76 ASP B OD1 3614 O OD2 . ASP B 77 ? 1.6866 2.2774 2.8937 0.1590 0.0152 0.0631 76 ASP B OD2 3615 N N . GLY B 78 ? 1.5665 2.0667 2.6656 0.0793 -0.0156 0.0637 77 GLY B N 3616 C CA . GLY B 78 ? 1.5727 2.0336 2.6420 0.0752 -0.0305 0.0680 77 GLY B CA 3617 C C . GLY B 78 ? 1.5346 1.9885 2.5834 0.0500 -0.0397 0.0706 77 GLY B C 3618 O O . GLY B 78 ? 1.5166 1.9441 2.5436 0.0461 -0.0521 0.0760 77 GLY B O 3619 N N . VAL B 79 ? 1.4811 1.9565 2.5350 0.0337 -0.0326 0.0672 78 VAL B N 3620 C CA . VAL B 79 ? 1.4363 1.9061 2.4717 0.0115 -0.0405 0.0692 78 VAL B CA 3621 C C . VAL B 79 ? 1.3847 1.8350 2.3943 -0.0001 -0.0269 0.0611 78 VAL B C 3622 O O . VAL B 79 ? 1.3933 1.8561 2.4105 0.0015 -0.0119 0.0550 78 VAL B O 3623 C CB . VAL B 79 ? 1.4305 1.9407 2.4928 0.0002 -0.0468 0.0732 78 VAL B CB 3624 C CG1 . VAL B 79 ? 1.4182 1.9172 2.4573 -0.0209 -0.0545 0.0743 78 VAL B CG1 3625 C CG2 . VAL B 79 ? 1.4389 1.9738 2.5304 0.0115 -0.0621 0.0809 78 VAL B CG2 3626 N N . ASP B 80 ? 1.3398 1.7610 2.3190 -0.0113 -0.0322 0.0615 79 ASP B N 3627 C CA . ASP B 80 ? 1.3355 1.7410 2.2911 -0.0234 -0.0225 0.0547 79 ASP B CA 3628 C C . ASP B 80 ? 1.2570 1.6630 2.1994 -0.0411 -0.0302 0.0584 79 ASP B C 3629 O O . ASP B 80 ? 1.2274 1.6281 2.1649 -0.0433 -0.0431 0.0651 79 ASP B O 3630 C CB . ASP B 80 ? 1.4011 1.7686 2.3321 -0.0190 -0.0197 0.0504 79 ASP B CB 3631 C CG . ASP B 80 ? 1.4473 1.8045 2.3629 -0.0230 -0.0065 0.0403 79 ASP B CG 3632 O OD1 . ASP B 80 ? 1.4289 1.7982 2.3397 -0.0355 -0.0025 0.0386 79 ASP B OD1 3633 O OD2 . ASP B 80 ? 1.4627 1.7975 2.3688 -0.0133 -0.0008 0.0338 79 ASP B OD2 3634 N N . VAL B 81 ? 1.2392 1.6498 2.1736 -0.0524 -0.0220 0.0542 80 VAL B N 3635 C CA . VAL B 81 ? 1.2615 1.6728 2.1839 -0.0675 -0.0279 0.0571 80 VAL B CA 3636 C C . VAL B 81 ? 1.2466 1.6398 2.1435 -0.0757 -0.0209 0.0522 80 VAL B C 3637 O O . VAL B 81 ? 1.2190 1.6116 2.1130 -0.0739 -0.0095 0.0460 80 VAL B O 3638 C CB . VAL B 81 ? 1.2918 1.7320 2.2343 -0.0746 -0.0273 0.0588 80 VAL B CB 3639 C CG1 . VAL B 81 ? 1.2995 1.7362 2.2291 -0.0881 -0.0368 0.0622 80 VAL B CG1 3640 C CG2 . VAL B 81 ? 1.3117 1.7771 2.2866 -0.0654 -0.0324 0.0625 80 VAL B CG2 3641 N N . ARG B 82 ? 1.2419 1.6215 2.1202 -0.0837 -0.0277 0.0552 81 ARG B N 3642 C CA . ARG B 82 ? 1.2530 1.6200 2.1102 -0.0916 -0.0229 0.0518 81 ARG B CA 3643 C C . ARG B 82 ? 1.2015 1.5707 2.0482 -0.1014 -0.0277 0.0554 81 ARG B C 3644 O O . ARG B 82 ? 1.1348 1.5075 1.9842 -0.1025 -0.0368 0.0604 81 ARG B O 3645 C CB . ARG B 82 ? 1.3366 1.6808 2.1797 -0.0900 -0.0238 0.0508 81 ARG B CB 3646 C CG . ARG B 82 ? 1.3854 1.7192 2.2202 -0.0920 -0.0328 0.0584 81 ARG B CG 3647 C CD . ARG B 82 ? 1.4314 1.7433 2.2546 -0.0928 -0.0322 0.0584 81 ARG B CD 3648 N NE . ARG B 82 ? 1.4722 1.7753 2.2860 -0.0954 -0.0384 0.0671 81 ARG B NE 3649 C CZ . ARG B 82 ? 1.5002 1.7848 2.3058 -0.0972 -0.0387 0.0706 81 ARG B CZ 3650 N NH1 . ARG B 82 ? 1.5348 1.8052 2.3402 -0.0975 -0.0348 0.0652 81 ARG B NH1 3651 N NH2 . ARG B 82 ? 1.4801 1.7588 2.2762 -0.0992 -0.0426 0.0798 81 ARG B NH2 3652 N N . VAL B 83 ? 1.2274 1.5930 2.0603 -0.1075 -0.0222 0.0524 82 VAL B N 3653 C CA . VAL B 83 ? 1.2434 1.6076 2.0634 -0.1149 -0.0253 0.0551 82 VAL B CA 3654 C C . VAL B 83 ? 1.2258 1.5765 2.0292 -0.1161 -0.0273 0.0564 82 VAL B C 3655 O O . VAL B 83 ? 1.2116 1.5575 2.0078 -0.1172 -0.0227 0.0529 82 VAL B O 3656 C CB . VAL B 83 ? 1.2606 1.6299 2.0757 -0.1197 -0.0177 0.0524 82 VAL B CB 3657 C CG1 . VAL B 83 ? 1.2648 1.6299 2.0667 -0.1258 -0.0215 0.0555 82 VAL B CG1 3658 C CG2 . VAL B 83 ? 1.2755 1.6604 2.1092 -0.1188 -0.0122 0.0515 82 VAL B CG2 3659 N N . PRO B 84 ? 1.2073 1.5529 2.0047 -0.1161 -0.0343 0.0618 83 PRO B N 3660 C CA . PRO B 84 ? 1.2052 1.5413 1.9894 -0.1173 -0.0344 0.0645 83 PRO B CA 3661 C C . PRO B 84 ? 1.2150 1.5521 1.9859 -0.1209 -0.0325 0.0646 83 PRO B C 3662 O O . PRO B 84 ? 1.1647 1.5050 1.9332 -0.1225 -0.0331 0.0636 83 PRO B O 3663 C CB . PRO B 84 ? 1.1991 1.5298 1.9801 -0.1143 -0.0414 0.0709 83 PRO B CB 3664 C CG . PRO B 84 ? 1.1939 1.5317 1.9791 -0.1144 -0.0471 0.0707 83 PRO B CG 3665 C CD . PRO B 84 ? 1.1959 1.5450 1.9971 -0.1154 -0.0425 0.0655 83 PRO B CD 3666 N N . GLY B 85 ? 1.2494 1.5837 2.0127 -0.1221 -0.0304 0.0661 84 GLY B N 3667 C CA . GLY B 85 ? 1.2716 1.6075 2.0226 -0.1227 -0.0289 0.0676 84 GLY B CA 3668 C C . GLY B 85 ? 1.2783 1.6189 2.0265 -0.1241 -0.0255 0.0634 84 GLY B C 3669 O O . GLY B 85 ? 1.3318 1.6722 2.0692 -0.1228 -0.0249 0.0647 84 GLY B O 3670 N N . PHE B 86 ? 1.2612 1.6039 2.0162 -0.1256 -0.0231 0.0585 85 PHE B N 3671 C CA . PHE B 86 ? 1.2584 1.6044 2.0070 -0.1264 -0.0201 0.0550 85 PHE B CA 3672 C C . PHE B 86 ? 1.2623 1.6123 2.0060 -0.1269 -0.0211 0.0564 85 PHE B C 3673 O O . PHE B 86 ? 1.2824 1.6335 2.0325 -0.1294 -0.0224 0.0568 85 PHE B O 3674 C CB . PHE B 86 ? 1.2673 1.6132 2.0205 -0.1269 -0.0170 0.0488 85 PHE B CB 3675 C CG . PHE B 86 ? 1.2819 1.6296 2.0245 -0.1270 -0.0137 0.0458 85 PHE B CG 3676 C CD1 . PHE B 86 ? 1.2951 1.6441 2.0302 -0.1278 -0.0155 0.0431 85 PHE B CD1 3677 C CD2 . PHE B 86 ? 1.2800 1.6283 2.0200 -0.1268 -0.0093 0.0464 85 PHE B CD2 3678 C CE1 . PHE B 86 ? 1.3020 1.6516 2.0241 -0.1267 -0.0136 0.0410 85 PHE B CE1 3679 C CE2 . PHE B 86 ? 1.3032 1.6509 2.0303 -0.1265 -0.0056 0.0451 85 PHE B CE2 3680 C CZ . PHE B 86 ? 1.3111 1.6588 2.0277 -0.1256 -0.0081 0.0424 85 PHE B CZ 3681 N N . GLY B 87 ? 1.2531 1.6057 1.9867 -0.1246 -0.0207 0.0579 86 GLY B N 3682 C CA . GLY B 87 ? 1.2642 1.6252 1.9959 -0.1233 -0.0218 0.0603 86 GLY B CA 3683 C C . GLY B 87 ? 1.2803 1.6431 2.0108 -0.1199 -0.0213 0.0664 86 GLY B C 3684 O O . GLY B 87 ? 1.2840 1.6570 2.0148 -0.1172 -0.0208 0.0695 86 GLY B O 3685 N N . LYS B 88 ? 1.2942 1.6485 2.0233 -0.1194 -0.0213 0.0683 87 LYS B N 3686 C CA . LYS B 88 ? 1.2878 1.6399 2.0097 -0.1150 -0.0204 0.0735 87 LYS B CA 3687 C C . LYS B 88 ? 1.2265 1.5661 1.9345 -0.1116 -0.0220 0.0726 87 LYS B C 3688 O O . LYS B 88 ? 1.1713 1.5068 1.8781 -0.1137 -0.0228 0.0692 87 LYS B O 3689 C CB . LYS B 88 ? 1.3382 1.6878 2.0664 -0.1175 -0.0209 0.0768 87 LYS B CB 3690 C CG . LYS B 88 ? 1.3865 1.7443 2.1280 -0.1229 -0.0195 0.0782 87 LYS B CG 3691 C CD . LYS B 88 ? 1.4348 1.8064 2.1781 -0.1215 -0.0158 0.0831 87 LYS B CD 3692 C CE . LYS B 88 ? 1.4919 1.8718 2.2509 -0.1297 -0.0153 0.0854 87 LYS B CE 3693 N NZ . LYS B 88 ? 1.5240 1.9227 2.2897 -0.1292 -0.0112 0.0913 87 LYS B NZ 3694 N N . THR B 89 ? 1.1994 1.5318 1.8956 -0.1070 -0.0222 0.0755 88 THR B N 3695 C CA . THR B 89 ? 1.1952 1.5124 1.8758 -0.1047 -0.0252 0.0737 88 THR B CA 3696 C C . THR B 89 ? 1.2088 1.5161 1.8831 -0.1054 -0.0304 0.0741 88 THR B C 3697 O O . THR B 89 ? 1.2485 1.5426 1.9121 -0.1063 -0.0353 0.0715 88 THR B O 3698 C CB . THR B 89 ? 1.1920 1.5040 1.8555 -0.0958 -0.0220 0.0749 88 THR B CB 3699 O OG1 . THR B 89 ? 1.2064 1.5252 1.8668 -0.0897 -0.0177 0.0793 88 THR B OG1 3700 C CG2 . THR B 89 ? 1.1855 1.5057 1.8532 -0.0944 -0.0194 0.0744 88 THR B CG2 3701 N N . PHE B 90 ? 1.1933 1.5053 1.8733 -0.1055 -0.0302 0.0777 89 PHE B N 3702 C CA . PHE B 90 ? 1.2442 1.5463 1.9147 -0.1045 -0.0361 0.0790 89 PHE B CA 3703 C C . PHE B 90 ? 1.1959 1.4940 1.8735 -0.1099 -0.0448 0.0752 89 PHE B C 3704 O O . PHE B 90 ? 1.2051 1.4922 1.8699 -0.1094 -0.0524 0.0741 89 PHE B O 3705 C CB . PHE B 90 ? 1.3398 1.6465 2.0155 -0.1039 -0.0342 0.0850 89 PHE B CB 3706 C CG . PHE B 90 ? 1.4032 1.7178 2.1013 -0.1095 -0.0346 0.0847 89 PHE B CG 3707 C CD1 . PHE B 90 ? 1.4400 1.7520 2.1466 -0.1113 -0.0416 0.0835 89 PHE B CD1 3708 C CD2 . PHE B 90 ? 1.4389 1.7633 2.1493 -0.1124 -0.0285 0.0854 89 PHE B CD2 3709 C CE1 . PHE B 90 ? 1.4610 1.7780 2.1862 -0.1140 -0.0410 0.0827 89 PHE B CE1 3710 C CE2 . PHE B 90 ? 1.4575 1.7845 2.1846 -0.1168 -0.0292 0.0837 89 PHE B CE2 3711 C CZ . PHE B 90 ? 1.4716 1.7939 2.2052 -0.1167 -0.0346 0.0823 89 PHE B CZ 3712 N N . SER B 91 ? 1.1325 1.4404 1.8302 -0.1151 -0.0438 0.0730 90 SER B N 3713 C CA . SER B 91 ? 1.1253 1.4357 1.8360 -0.1201 -0.0500 0.0704 90 SER B CA 3714 C C . SER B 91 ? 1.1594 1.4625 1.8635 -0.1245 -0.0529 0.0671 90 SER B C 3715 O O . SER B 91 ? 1.1625 1.4672 1.8756 -0.1298 -0.0597 0.0657 90 SER B O 3716 C CB . SER B 91 ? 1.0915 1.4144 1.8241 -0.1225 -0.0454 0.0690 90 SER B CB 3717 O OG . SER B 91 ? 1.0440 1.3698 1.7753 -0.1231 -0.0379 0.0672 90 SER B OG 3718 N N . LEU B 92 ? 1.1789 1.4745 1.8687 -0.1224 -0.0478 0.0665 91 LEU B N 3719 C CA . LEU B 92 ? 1.1849 1.4671 1.8630 -0.1258 -0.0497 0.0642 91 LEU B CA 3720 C C . LEU B 92 ? 1.2114 1.4736 1.8634 -0.1215 -0.0553 0.0630 91 LEU B C 3721 O O . LEU B 92 ? 1.1726 1.4196 1.8149 -0.1265 -0.0618 0.0601 91 LEU B O 3722 C CB . LEU B 92 ? 1.1619 1.4437 1.8351 -0.1233 -0.0413 0.0646 91 LEU B CB 3723 C CG . LEU B 92 ? 1.1266 1.4232 1.8170 -0.1264 -0.0351 0.0647 91 LEU B CG 3724 C CD1 . LEU B 92 ? 1.0968 1.3880 1.7765 -0.1244 -0.0298 0.0653 91 LEU B CD1 3725 C CD2 . LEU B 92 ? 1.1251 1.4286 1.8334 -0.1347 -0.0372 0.0637 91 LEU B CD2 3726 N N . GLU B 93 ? 1.2665 1.5277 1.9060 -0.1125 -0.0523 0.0651 92 GLU B N 3727 C CA . GLU B 93 ? 1.3330 1.5744 1.9435 -0.1056 -0.0551 0.0637 92 GLU B CA 3728 C C . GLU B 93 ? 1.3817 1.6137 1.9845 -0.1091 -0.0671 0.0616 92 GLU B C 3729 O O . GLU B 93 ? 1.3994 1.6099 1.9800 -0.1093 -0.0740 0.0573 92 GLU B O 3730 C CB . GLU B 93 ? 1.3479 1.5947 1.9491 -0.0947 -0.0464 0.0678 92 GLU B CB 3731 C CG . GLU B 93 ? 1.3420 1.5965 1.9462 -0.0893 -0.0366 0.0694 92 GLU B CG 3732 C CD . GLU B 93 ? 1.3306 1.5958 1.9312 -0.0798 -0.0278 0.0743 92 GLU B CD 3733 O OE1 . GLU B 93 ? 1.3661 1.6192 1.9434 -0.0709 -0.0262 0.0745 92 GLU B OE1 3734 O OE2 . GLU B 93 ? 1.2454 1.5312 1.8661 -0.0813 -0.0223 0.0779 92 GLU B OE2 3735 N N . PHE B 94 ? 1.4234 1.6700 2.0430 -0.1113 -0.0705 0.0646 93 PHE B N 3736 C CA . PHE B 94 ? 1.4874 1.7289 2.1019 -0.1135 -0.0835 0.0637 93 PHE B CA 3737 C C . PHE B 94 ? 1.4809 1.7414 2.1276 -0.1210 -0.0889 0.0649 93 PHE B C 3738 O O . PHE B 94 ? 1.4838 1.7601 2.1504 -0.1197 -0.0816 0.0684 93 PHE B O 3739 C CB . PHE B 94 ? 1.5483 1.7862 2.1448 -0.1041 -0.0822 0.0682 93 PHE B CB 3740 C CG . PHE B 94 ? 1.6047 1.8218 2.1648 -0.0954 -0.0797 0.0663 93 PHE B CG 3741 C CD1 . PHE B 94 ? 1.5912 1.8069 2.1440 -0.0891 -0.0670 0.0666 93 PHE B CD1 3742 C CD2 . PHE B 94 ? 1.6680 1.8673 2.2001 -0.0922 -0.0902 0.0641 93 PHE B CD2 3743 C CE1 . PHE B 94 ? 1.6173 1.8144 2.1368 -0.0786 -0.0633 0.0648 93 PHE B CE1 3744 C CE2 . PHE B 94 ? 1.7017 1.8798 2.1968 -0.0824 -0.0866 0.0615 93 PHE B CE2 3745 C CZ . PHE B 94 ? 1.6600 1.8371 2.1494 -0.0750 -0.0723 0.0619 93 PHE B CZ 3746 N N . LEU B 95 ? 1.4827 1.7419 2.1352 -0.1286 -0.1017 0.0617 94 LEU B N 3747 C CA . LEU B 95 ? 1.4576 1.7388 2.1443 -0.1347 -0.1060 0.0630 94 LEU B CA 3748 C C . LEU B 95 ? 1.4166 1.7057 2.1085 -0.1286 -0.1129 0.0671 94 LEU B C 3749 O O . LEU B 95 ? 1.3750 1.6821 2.0932 -0.1274 -0.1101 0.0701 94 LEU B O 3750 C CB . LEU B 95 ? 1.4897 1.7720 2.1874 -0.1467 -0.1168 0.0591 94 LEU B CB 3751 C CG . LEU B 95 ? 1.4928 1.7730 2.1975 -0.1555 -0.1091 0.0571 94 LEU B CG 3752 C CD1 . LEU B 95 ? 1.4572 1.7523 2.1789 -0.1527 -0.0931 0.0599 94 LEU B CD1 3753 C CD2 . LEU B 95 ? 1.5252 1.7760 2.1957 -0.1548 -0.1087 0.0535 94 LEU B CD2 3754 N N . ASP B 96 ? 1.4256 1.6996 2.0906 -0.1239 -0.1221 0.0674 95 ASP B N 3755 C CA . ASP B 96 ? 1.4750 1.7530 2.1398 -0.1172 -0.1294 0.0727 95 ASP B CA 3756 C C . ASP B 96 ? 1.5146 1.7784 2.1507 -0.1077 -0.1205 0.0773 95 ASP B C 3757 O O . ASP B 96 ? 1.5771 1.8223 2.1802 -0.1042 -0.1241 0.0756 95 ASP B O 3758 C CB . ASP B 96 ? 1.5223 1.7966 2.1797 -0.1200 -0.1500 0.0703 95 ASP B CB 3759 C CG . ASP B 96 ? 1.5416 1.8224 2.2020 -0.1122 -0.1596 0.0768 95 ASP B CG 3760 O OD1 . ASP B 96 ? 1.5146 1.7941 2.1715 -0.1038 -0.1497 0.0835 95 ASP B OD1 3761 O OD2 . ASP B 96 ? 1.5523 1.8392 2.2189 -0.1147 -0.1779 0.0756 95 ASP B OD2 3762 N N . PRO B 97 ? 1.5148 1.7866 2.1628 -0.1036 -0.1089 0.0831 96 PRO B N 3763 C CA . PRO B 97 ? 1.5498 1.8122 2.1766 -0.0972 -0.0970 0.0881 96 PRO B CA 3764 C C . PRO B 97 ? 1.6137 1.8610 2.2085 -0.0897 -0.1027 0.0929 96 PRO B C 3765 O O . PRO B 97 ? 1.6857 1.9221 2.2542 -0.0846 -0.0942 0.0946 96 PRO B O 3766 C CB . PRO B 97 ? 1.5294 1.8034 2.1799 -0.0971 -0.0876 0.0933 96 PRO B CB 3767 C CG . PRO B 97 ? 1.5183 1.8026 2.1931 -0.0983 -0.0975 0.0930 96 PRO B CG 3768 C CD . PRO B 97 ? 1.5045 1.7932 2.1851 -0.1042 -0.1075 0.0858 96 PRO B CD 3769 N N . SER B 98 ? 1.6372 1.8848 2.2339 -0.0881 -0.1165 0.0955 97 SER B N 3770 C CA . SER B 98 ? 1.7270 1.9588 2.2898 -0.0806 -0.1241 0.1002 97 SER B CA 3771 C C . SER B 98 ? 1.8458 2.0621 2.3788 -0.0811 -0.1340 0.0920 97 SER B C 3772 O O . SER B 98 ? 1.8702 2.0683 2.3643 -0.0737 -0.1341 0.0936 97 SER B O 3773 C CB . SER B 98 ? 1.7410 1.9780 2.3148 -0.0778 -0.1386 0.1053 97 SER B CB 3774 O OG . SER B 98 ? 1.8188 2.0392 2.3568 -0.0697 -0.1462 0.1112 97 SER B OG 3775 N N . LYS B 99 ? 1.9609 2.1828 2.5109 -0.0899 -0.1422 0.0832 98 LYS B N 3776 C CA . LYS B 99 ? 2.0407 2.2461 2.5659 -0.0929 -0.1565 0.0746 98 LYS B CA 3777 C C . LYS B 99 ? 2.0810 2.2762 2.5963 -0.0946 -0.1443 0.0686 98 LYS B C 3778 O O . LYS B 99 ? 2.1251 2.3265 2.6620 -0.1038 -0.1445 0.0633 98 LYS B O 3779 C CB . LYS B 99 ? 2.0516 2.2698 2.6033 -0.1030 -0.1756 0.0700 98 LYS B CB 3780 C CG . LYS B 99 ? 2.0685 2.2997 2.6331 -0.0993 -0.1894 0.0764 98 LYS B CG 3781 C CD . LYS B 99 ? 2.1249 2.3361 2.6467 -0.0908 -0.2024 0.0783 98 LYS B CD 3782 C CE . LYS B 99 ? 2.1312 2.3352 2.6338 -0.0784 -0.1891 0.0893 98 LYS B CE 3783 N NZ . LYS B 99 ? 2.1550 2.3407 2.6158 -0.0694 -0.2020 0.0930 98 LYS B NZ 3784 N N . SER B 100 ? 2.1222 2.3023 2.6050 -0.0846 -0.1327 0.0705 99 SER B N 3785 C CA . SER B 100 ? 2.1614 2.3317 2.6319 -0.0821 -0.1193 0.0662 99 SER B CA 3786 C C . SER B 100 ? 2.2387 2.3919 2.7001 -0.0891 -0.1290 0.0551 99 SER B C 3787 O O . SER B 100 ? 2.4064 2.5703 2.8969 -0.0987 -0.1282 0.0528 99 SER B O 3788 C CB . SER B 100 ? 2.1742 2.3310 2.6076 -0.0683 -0.1071 0.0700 99 SER B CB 3789 O OG . SER B 100 ? 2.1482 2.3000 2.5742 -0.0635 -0.0928 0.0671 99 SER B OG 3790 N N . SER B 101 ? 2.1924 2.3176 2.6124 -0.0847 -0.1379 0.0484 100 SER B N 3791 C CA . SER B 101 ? 2.1575 2.2577 2.5593 -0.0890 -0.1438 0.0377 100 SER B CA 3792 C C . SER B 101 ? 2.1450 2.2535 2.5797 -0.1066 -0.1559 0.0336 100 SER B C 3793 O O . SER B 101 ? 2.1901 2.2932 2.6341 -0.1125 -0.1506 0.0303 100 SER B O 3794 C CB . SER B 101 ? 2.1627 2.2308 2.5151 -0.0836 -0.1576 0.0302 100 SER B CB 3795 O OG . SER B 101 ? 2.0783 2.1532 2.4356 -0.0901 -0.1777 0.0307 100 SER B OG 3796 N N . VAL B 102 ? 2.0739 2.1967 2.5264 -0.1143 -0.1721 0.0348 101 VAL B N 3797 C CA . VAL B 102 ? 1.9968 2.1292 2.4796 -0.1315 -0.1861 0.0310 101 VAL B CA 3798 C C . VAL B 102 ? 1.9332 2.0904 2.4594 -0.1385 -0.1724 0.0355 101 VAL B C 3799 O O . VAL B 102 ? 1.9604 2.1184 2.5048 -0.1521 -0.1769 0.0321 101 VAL B O 3800 C CB . VAL B 102 ? 1.9629 2.1102 2.4586 -0.1365 -0.2070 0.0322 101 VAL B CB 3801 C CG1 . VAL B 102 ? 1.9589 2.0797 2.4060 -0.1284 -0.2210 0.0279 101 VAL B CG1 3802 C CG2 . VAL B 102 ? 1.9506 2.1308 2.4799 -0.1313 -0.1995 0.0427 101 VAL B CG2 3803 N N . GLY B 103 ? 1.8500 2.0254 2.3905 -0.1297 -0.1555 0.0431 102 GLY B N 3804 C CA . GLY B 103 ? 1.7660 1.9642 2.3439 -0.1350 -0.1432 0.0468 102 GLY B CA 3805 C C . GLY B 103 ? 1.7140 1.9035 2.2837 -0.1308 -0.1262 0.0467 102 GLY B C 3806 O O . GLY B 103 ? 1.6900 1.8985 2.2859 -0.1323 -0.1147 0.0506 102 GLY B O 3807 N N . SER B 104 ? 1.6714 1.8323 2.2044 -0.1247 -0.1250 0.0421 103 SER B N 3808 C CA . SER B 104 ? 1.5851 1.7386 2.1099 -0.1180 -0.1095 0.0427 103 SER B CA 3809 C C . SER B 104 ? 1.4717 1.6251 2.0149 -0.1292 -0.1076 0.0415 103 SER B C 3810 O O . SER B 104 ? 1.4338 1.5706 1.9722 -0.1400 -0.1182 0.0366 103 SER B O 3811 C CB . SER B 104 ? 1.6412 1.7633 2.1216 -0.1062 -0.1080 0.0380 103 SER B CB 3812 O OG . SER B 104 ? 1.7031 1.7959 2.1617 -0.1135 -0.1225 0.0296 103 SER B OG 3813 N N . TYR B 105 ? 1.4069 1.5782 1.9699 -0.1271 -0.0941 0.0464 104 TYR B N 3814 C CA . TYR B 105 ? 1.3767 1.5500 1.9561 -0.1364 -0.0900 0.0471 104 TYR B CA 3815 C C . TYR B 105 ? 1.3752 1.5407 1.9419 -0.1264 -0.0770 0.0489 104 TYR B C 3816 O O . TYR B 105 ? 1.3586 1.4960 1.9004 -0.1238 -0.0776 0.0459 104 TYR B O 3817 C CB . TYR B 105 ? 1.3429 1.5481 1.9609 -0.1444 -0.0879 0.0511 104 TYR B CB 3818 C CG . TYR B 105 ? 1.3390 1.5506 1.9760 -0.1543 -0.0822 0.0529 104 TYR B CG 3819 C CD1 . TYR B 105 ? 1.3734 1.5692 2.0083 -0.1669 -0.0885 0.0509 104 TYR B CD1 3820 C CD2 . TYR B 105 ? 1.3209 1.5540 1.9774 -0.1521 -0.0707 0.0568 104 TYR B CD2 3821 C CE1 . TYR B 105 ? 1.3738 1.5756 2.0252 -0.1765 -0.0816 0.0543 104 TYR B CE1 3822 C CE2 . TYR B 105 ? 1.3192 1.5577 1.9895 -0.1602 -0.0644 0.0590 104 TYR B CE2 3823 C CZ . TYR B 105 ? 1.3428 1.5664 2.0108 -0.1723 -0.0690 0.0585 104 TYR B CZ 3824 O OH . TYR B 105 ? 1.3197 1.5487 2.0005 -0.1807 -0.0610 0.0622 104 TYR B OH 3825 N N . PHE B 106 ? 1.3736 1.5623 1.9563 -0.1204 -0.0664 0.0536 105 PHE B N 3826 C CA . PHE B 106 ? 1.4020 1.5886 1.9757 -0.1102 -0.0556 0.0559 105 PHE B CA 3827 C C . PHE B 106 ? 1.4021 1.5837 1.9547 -0.0946 -0.0509 0.0563 105 PHE B C 3828 O O . PHE B 106 ? 1.4030 1.5842 1.9482 -0.0841 -0.0427 0.0582 105 PHE B O 3829 C CB . PHE B 106 ? 1.4034 1.6177 2.0034 -0.1115 -0.0477 0.0602 105 PHE B CB 3830 C CG . PHE B 106 ? 1.4411 1.6545 2.0498 -0.1195 -0.0452 0.0613 105 PHE B CG 3831 C CD1 . PHE B 106 ? 1.4677 1.6664 2.0605 -0.1138 -0.0405 0.0627 105 PHE B CD1 3832 C CD2 . PHE B 106 ? 1.4679 1.6957 2.1003 -0.1313 -0.0465 0.0618 105 PHE B CD2 3833 C CE1 . PHE B 106 ? 1.4831 1.6793 2.0809 -0.1208 -0.0374 0.0651 105 PHE B CE1 3834 C CE2 . PHE B 106 ? 1.4886 1.7163 2.1276 -0.1383 -0.0420 0.0638 105 PHE B CE2 3835 C CZ . PHE B 106 ? 1.4815 1.6923 2.1019 -0.1336 -0.0375 0.0658 105 PHE B CZ 3836 N N . HIS B 107 ? 1.4011 1.5807 1.9444 -0.0922 -0.0556 0.0550 106 HIS B N 3837 C CA . HIS B 107 ? 1.3822 1.5611 1.9072 -0.0776 -0.0488 0.0567 106 HIS B CA 3838 C C . HIS B 107 ? 1.3881 1.5464 1.8862 -0.0642 -0.0430 0.0547 106 HIS B C 3839 O O . HIS B 107 ? 1.3439 1.5152 1.8429 -0.0522 -0.0322 0.0587 106 HIS B O 3840 C CB . HIS B 107 ? 1.4058 1.5753 1.9141 -0.0770 -0.0564 0.0548 106 HIS B CB 3841 C CG . HIS B 107 ? 1.4353 1.5988 1.9178 -0.0614 -0.0484 0.0563 106 HIS B CG 3842 N ND1 . HIS B 107 ? 1.4376 1.6252 1.9321 -0.0547 -0.0369 0.0637 106 HIS B ND1 3843 C CD2 . HIS B 107 ? 1.4614 1.5973 1.9062 -0.0511 -0.0496 0.0514 106 HIS B CD2 3844 C CE1 . HIS B 107 ? 1.4251 1.6033 1.8925 -0.0409 -0.0299 0.0643 106 HIS B CE1 3845 N NE2 . HIS B 107 ? 1.4552 1.6012 1.8904 -0.0374 -0.0372 0.0565 106 HIS B NE2 3846 N N . THR B 108 ? 1.4241 1.5500 1.8990 -0.0661 -0.0504 0.0485 107 THR B N 3847 C CA . THR B 108 ? 1.4524 1.5521 1.8970 -0.0516 -0.0457 0.0456 107 THR B CA 3848 C C . THR B 108 ? 1.3951 1.5050 1.8515 -0.0452 -0.0366 0.0502 107 THR B C 3849 O O . THR B 108 ? 1.3842 1.4950 1.8294 -0.0280 -0.0274 0.0521 107 THR B O 3850 C CB . THR B 108 ? 1.5145 1.5726 1.9318 -0.0575 -0.0570 0.0375 107 THR B CB 3851 O OG1 . THR B 108 ? 1.5631 1.6149 1.9727 -0.0658 -0.0686 0.0330 107 THR B OG1 3852 C CG2 . THR B 108 ? 1.5726 1.5979 1.9519 -0.0392 -0.0520 0.0333 107 THR B CG2 3853 N N . MET B 109 ? 1.3545 1.4734 1.8333 -0.0582 -0.0390 0.0525 108 MET B N 3854 C CA . MET B 109 ? 1.3440 1.4721 1.8321 -0.0529 -0.0321 0.0572 108 MET B CA 3855 C C . MET B 109 ? 1.3056 1.4702 1.8134 -0.0440 -0.0234 0.0627 108 MET B C 3856 O O . MET B 109 ? 1.2791 1.4492 1.7835 -0.0299 -0.0167 0.0658 108 MET B O 3857 C CB . MET B 109 ? 1.3372 1.4698 1.8444 -0.0692 -0.0354 0.0590 108 MET B CB 3858 C CG . MET B 109 ? 1.3545 1.4912 1.8648 -0.0635 -0.0297 0.0639 108 MET B CG 3859 S SD . MET B 109 ? 1.3489 1.4923 1.8784 -0.0812 -0.0307 0.0671 108 MET B SD 3860 C CE . MET B 109 ? 1.3852 1.4882 1.8965 -0.0939 -0.0382 0.0635 108 MET B CE 3861 N N . VAL B 110 ? 1.2692 1.4583 1.7982 -0.0524 -0.0240 0.0642 109 VAL B N 3862 C CA . VAL B 110 ? 1.2308 1.4534 1.7806 -0.0479 -0.0168 0.0694 109 VAL B CA 3863 C C . VAL B 110 ? 1.2467 1.4716 1.7822 -0.0312 -0.0090 0.0713 109 VAL B C 3864 O O . VAL B 110 ? 1.2369 1.4831 1.7831 -0.0216 -0.0017 0.0759 109 VAL B O 3865 C CB . VAL B 110 ? 1.1957 1.4379 1.7680 -0.0604 -0.0194 0.0706 109 VAL B CB 3866 C CG1 . VAL B 110 ? 1.1799 1.4530 1.7727 -0.0575 -0.0124 0.0761 109 VAL B CG1 3867 C CG2 . VAL B 110 ? 1.1773 1.4212 1.7657 -0.0746 -0.0248 0.0690 109 VAL B CG2 3868 N N . GLU B 111 ? 1.2766 1.4805 1.7879 -0.0273 -0.0106 0.0678 110 GLU B N 3869 C CA . GLU B 111 ? 1.3133 1.5163 1.8061 -0.0099 -0.0015 0.0692 110 GLU B CA 3870 C C . GLU B 111 ? 1.3217 1.5161 1.8020 0.0069 0.0043 0.0691 110 GLU B C 3871 O O . GLU B 111 ? 1.3003 1.5144 1.7847 0.0215 0.0149 0.0738 110 GLU B O 3872 C CB . GLU B 111 ? 1.3736 1.5488 1.8348 -0.0079 -0.0056 0.0639 110 GLU B CB 3873 C CG . GLU B 111 ? 1.4153 1.6067 1.8840 -0.0135 -0.0048 0.0678 110 GLU B CG 3874 C CD . GLU B 111 ? 1.4409 1.6624 1.9219 -0.0037 0.0095 0.0762 110 GLU B CD 3875 O OE1 . GLU B 111 ? 1.5072 1.7337 1.9830 0.0116 0.0194 0.0778 110 GLU B OE1 3876 O OE2 . GLU B 111 ? 1.3918 1.6323 1.8888 -0.0114 0.0111 0.0819 110 GLU B OE2 3877 N N . SER B 112 ? 1.3563 1.5220 1.8225 0.0050 -0.0023 0.0647 111 SER B N 3878 C CA . SER B 112 ? 1.3915 1.5447 1.8445 0.0214 0.0019 0.0652 111 SER B CA 3879 C C . SER B 112 ? 1.3647 1.5544 1.8478 0.0246 0.0065 0.0726 111 SER B C 3880 O O . SER B 112 ? 1.4030 1.6051 1.8860 0.0431 0.0143 0.0762 111 SER B O 3881 C CB . SER B 112 ? 1.4162 1.5275 1.8476 0.0157 -0.0067 0.0600 111 SER B CB 3882 O OG . SER B 112 ? 1.4317 1.5062 1.8312 0.0155 -0.0118 0.0522 111 SER B OG 3883 N N . LEU B 113 ? 1.3044 1.5120 1.8129 0.0074 0.0012 0.0745 112 LEU B N 3884 C CA . LEU B 113 ? 1.2698 1.5116 1.8057 0.0082 0.0032 0.0804 112 LEU B CA 3885 C C . LEU B 113 ? 1.2690 1.5476 1.8241 0.0160 0.0114 0.0853 112 LEU B C 3886 O O . LEU B 113 ? 1.2468 1.5481 1.8137 0.0279 0.0154 0.0900 112 LEU B O 3887 C CB . LEU B 113 ? 1.2257 1.4784 1.7823 -0.0119 -0.0030 0.0802 112 LEU B CB 3888 C CG . LEU B 113 ? 1.2327 1.4574 1.7768 -0.0199 -0.0091 0.0778 112 LEU B CG 3889 C CD1 . LEU B 113 ? 1.2061 1.4399 1.7685 -0.0397 -0.0134 0.0765 112 LEU B CD1 3890 C CD2 . LEU B 113 ? 1.2543 1.4782 1.7942 -0.0097 -0.0086 0.0817 112 LEU B CD2 3891 N N . VAL B 114 ? 1.3093 1.5944 1.8679 0.0091 0.0138 0.0851 113 VAL B N 3892 C CA . VAL B 114 ? 1.3546 1.6721 1.9300 0.0146 0.0231 0.0911 113 VAL B CA 3893 C C . VAL B 114 ? 1.3971 1.7142 1.9570 0.0380 0.0333 0.0930 113 VAL B C 3894 O O . VAL B 114 ? 1.3844 1.7358 1.9653 0.0469 0.0409 0.0994 113 VAL B O 3895 C CB . VAL B 114 ? 1.3636 1.6798 1.9378 0.0042 0.0241 0.0912 113 VAL B CB 3896 C CG1 . VAL B 114 ? 1.3748 1.7177 1.9583 0.0121 0.0364 0.0983 113 VAL B CG1 3897 C CG2 . VAL B 114 ? 1.3336 1.6591 1.9303 -0.0162 0.0162 0.0909 113 VAL B CG2 3898 N N . GLY B 115 ? 1.4525 1.7309 1.9761 0.0480 0.0331 0.0871 114 GLY B N 3899 C CA . GLY B 115 ? 1.5041 1.7742 2.0069 0.0729 0.0427 0.0873 114 GLY B CA 3900 C C . GLY B 115 ? 1.5148 1.7992 2.0296 0.0866 0.0438 0.0910 114 GLY B C 3901 O O . GLY B 115 ? 1.5045 1.8052 2.0204 0.1077 0.0543 0.0948 114 GLY B O 3902 N N . TRP B 116 ? 1.5366 1.8161 2.0601 0.0758 0.0333 0.0904 115 TRP B N 3903 C CA . TRP B 116 ? 1.5949 1.8875 2.1287 0.0876 0.0319 0.0947 115 TRP B CA 3904 C C . TRP B 116 ? 1.5623 1.9078 2.1385 0.0814 0.0316 0.1016 115 TRP B C 3905 O O . TRP B 116 ? 1.5952 1.9564 2.1829 0.0893 0.0280 0.1055 115 TRP B O 3906 C CB . TRP B 116 ? 1.6519 1.9102 2.1695 0.0805 0.0214 0.0915 115 TRP B CB 3907 C CG . TRP B 116 ? 1.7191 1.9238 2.1979 0.0812 0.0191 0.0844 115 TRP B CG 3908 C CD1 . TRP B 116 ? 1.7863 1.9651 2.2359 0.0974 0.0252 0.0801 115 TRP B CD1 3909 C CD2 . TRP B 116 ? 1.7359 1.9061 2.2007 0.0646 0.0097 0.0803 115 TRP B CD2 3910 N NE1 . TRP B 116 ? 1.8370 1.9653 2.2546 0.0905 0.0183 0.0729 115 TRP B NE1 3911 C CE2 . TRP B 116 ? 1.8065 1.9305 2.2351 0.0697 0.0090 0.0735 115 TRP B CE2 3912 C CE3 . TRP B 116 ? 1.6968 1.8711 2.1760 0.0457 0.0023 0.0818 115 TRP B CE3 3913 C CZ2 . TRP B 116 ? 1.8258 1.9097 2.2360 0.0546 0.0003 0.0688 115 TRP B CZ2 3914 C CZ3 . TRP B 116 ? 1.7086 1.8450 2.1698 0.0322 -0.0040 0.0779 115 TRP B CZ3 3915 C CH2 . TRP B 116 ? 1.7717 1.8645 2.2006 0.0357 -0.0054 0.0718 115 TRP B CH2 3916 N N . GLY B 117 ? 1.5356 1.9064 2.1334 0.0667 0.0341 0.1033 116 GLY B N 3917 C CA . GLY B 117 ? 1.4929 1.9128 2.1307 0.0597 0.0343 0.1097 116 GLY B CA 3918 C C . GLY B 117 ? 1.4374 1.8660 2.0944 0.0349 0.0248 0.1081 116 GLY B C 3919 O O . GLY B 117 ? 1.4399 1.9051 2.1282 0.0275 0.0227 0.1121 116 GLY B O 3920 N N . TYR B 118 ? 1.3783 1.7740 2.0176 0.0222 0.0189 0.1022 117 TYR B N 3921 C CA . TYR B 118 ? 1.3016 1.7027 1.9567 0.0006 0.0114 0.1000 117 TYR B CA 3922 C C . TYR B 118 ? 1.2741 1.6885 1.9434 -0.0109 0.0156 0.1017 117 TYR B C 3923 O O . TYR B 118 ? 1.2788 1.6917 1.9396 -0.0034 0.0242 0.1041 117 TYR B O 3924 C CB . TYR B 118 ? 1.2727 1.6376 1.9069 -0.0077 0.0046 0.0940 117 TYR B CB 3925 C CG . TYR B 118 ? 1.2498 1.6047 1.8754 -0.0028 -0.0007 0.0938 117 TYR B CG 3926 C CD1 . TYR B 118 ? 1.2532 1.5938 1.8600 0.0158 0.0014 0.0954 117 TYR B CD1 3927 C CD2 . TYR B 118 ? 1.2222 1.5800 1.8560 -0.0157 -0.0075 0.0922 117 TYR B CD2 3928 C CE1 . TYR B 118 ? 1.2666 1.5955 1.8632 0.0209 -0.0036 0.0966 117 TYR B CE1 3929 C CE2 . TYR B 118 ? 1.2271 1.5747 1.8498 -0.0109 -0.0119 0.0931 117 TYR B CE2 3930 C CZ . TYR B 118 ? 1.2487 1.5816 1.8529 0.0070 -0.0103 0.0959 117 TYR B CZ 3931 O OH . TYR B 118 ? 1.2401 1.5603 1.8310 0.0124 -0.0147 0.0982 117 TYR B OH 3932 N N . THR B 119 ? 1.2204 1.6452 1.9085 -0.0283 0.0099 0.1006 118 THR B N 3933 C CA . THR B 119 ? 1.2115 1.6469 1.9141 -0.0406 0.0127 0.1030 118 THR B CA 3934 C C . THR B 119 ? 1.1956 1.6133 1.8970 -0.0562 0.0055 0.0978 118 THR B C 3935 O O . THR B 119 ? 1.2110 1.6284 1.9180 -0.0630 -0.0014 0.0940 118 THR B O 3936 C CB . THR B 119 ? 1.2031 1.6768 1.9380 -0.0459 0.0139 0.1084 118 THR B CB 3937 O OG1 . THR B 119 ? 1.1885 1.6841 1.9289 -0.0301 0.0208 0.1139 118 THR B OG1 3938 C CG2 . THR B 119 ? 1.2109 1.6919 1.9590 -0.0586 0.0181 0.1124 118 THR B CG2 3939 N N . ARG B 120 ? 1.1812 1.5847 1.8744 -0.0607 0.0075 0.0979 119 ARG B N 3940 C CA . ARG B 120 ? 1.1617 1.5493 1.8544 -0.0730 0.0011 0.0934 119 ARG B CA 3941 C C . ARG B 120 ? 1.1349 1.5378 1.8511 -0.0856 -0.0024 0.0929 119 ARG B C 3942 O O . ARG B 120 ? 1.1239 1.5457 1.8571 -0.0898 0.0006 0.0977 119 ARG B O 3943 C CB . ARG B 120 ? 1.1860 1.5607 1.8683 -0.0743 0.0032 0.0953 119 ARG B CB 3944 C CG . ARG B 120 ? 1.2079 1.5597 1.8619 -0.0642 0.0037 0.0932 119 ARG B CG 3945 C CD . ARG B 120 ? 1.2271 1.5669 1.8688 -0.0653 0.0040 0.0951 119 ARG B CD 3946 N NE . ARG B 120 ? 1.2624 1.5866 1.8758 -0.0526 0.0079 0.0948 119 ARG B NE 3947 C CZ . ARG B 120 ? 1.2795 1.5779 1.8696 -0.0488 0.0019 0.0884 119 ARG B CZ 3948 N NH1 . ARG B 120 ? 1.2704 1.5585 1.8647 -0.0575 -0.0071 0.0830 119 ARG B NH1 3949 N NH2 . ARG B 120 ? 1.2843 1.5662 1.8459 -0.0366 0.0055 0.0872 119 ARG B NH2 3950 N N . GLY B 121 ? 1.1174 1.5111 1.8336 -0.0918 -0.0087 0.0870 120 GLY B N 3951 C CA . GLY B 121 ? 1.1003 1.5024 1.8332 -0.1028 -0.0126 0.0843 120 GLY B CA 3952 C C . GLY B 121 ? 1.0979 1.5197 1.8417 -0.1028 -0.0154 0.0840 120 GLY B C 3953 O O . GLY B 121 ? 1.0843 1.5117 1.8392 -0.1119 -0.0200 0.0805 120 GLY B O 3954 N N . GLU B 122 ? 1.1082 1.5397 1.8479 -0.0919 -0.0134 0.0873 121 GLU B N 3955 C CA . GLU B 122 ? 1.1208 1.5747 1.8720 -0.0898 -0.0172 0.0882 121 GLU B CA 3956 C C . GLU B 122 ? 1.1325 1.5768 1.8663 -0.0797 -0.0201 0.0863 121 GLU B C 3957 O O . GLU B 122 ? 1.1044 1.5402 1.8320 -0.0844 -0.0254 0.0815 121 GLU B O 3958 C CB . GLU B 122 ? 1.1286 1.6084 1.8952 -0.0844 -0.0118 0.0957 121 GLU B CB 3959 C CG . GLU B 122 ? 1.1418 1.6338 1.9284 -0.0969 -0.0092 0.0992 121 GLU B CG 3960 C CD . GLU B 122 ? 1.1587 1.6825 1.9656 -0.0935 -0.0030 0.1077 121 GLU B CD 3961 O OE1 . GLU B 122 ? 1.1833 1.7291 1.9991 -0.0856 -0.0056 0.1092 121 GLU B OE1 3962 O OE2 . GLU B 122 ? 1.1456 1.6737 1.9602 -0.0984 0.0045 0.1137 121 GLU B OE2 3963 N N . ASP B 123 ? 1.1677 1.6105 1.8910 -0.0654 -0.0159 0.0902 122 ASP B N 3964 C CA . ASP B 123 ? 1.2151 1.6443 1.9193 -0.0546 -0.0181 0.0897 122 ASP B CA 3965 C C . ASP B 123 ? 1.2273 1.6236 1.9104 -0.0582 -0.0179 0.0857 122 ASP B C 3966 O O . ASP B 123 ? 1.2322 1.6154 1.9019 -0.0567 -0.0209 0.0845 122 ASP B O 3967 C CB . ASP B 123 ? 1.2545 1.6861 1.9511 -0.0367 -0.0127 0.0946 122 ASP B CB 3968 C CG . ASP B 123 ? 1.2746 1.7432 1.9953 -0.0314 -0.0111 0.1000 122 ASP B CG 3969 O OD1 . ASP B 123 ? 1.2966 1.7881 2.0346 -0.0367 -0.0183 0.1001 122 ASP B OD1 3970 O OD2 . ASP B 123 ? 1.2752 1.7507 1.9971 -0.0219 -0.0025 0.1041 122 ASP B OD2 3971 N N . VAL B 124 ? 1.2228 1.6070 1.9034 -0.0629 -0.0143 0.0846 123 VAL B N 3972 C CA . VAL B 124 ? 1.2211 1.5787 1.8873 -0.0683 -0.0150 0.0811 123 VAL B CA 3973 C C . VAL B 124 ? 1.1847 1.5447 1.8639 -0.0816 -0.0162 0.0781 123 VAL B C 3974 O O . VAL B 124 ? 1.1416 1.5112 1.8317 -0.0843 -0.0144 0.0798 123 VAL B O 3975 C CB . VAL B 124 ? 1.2409 1.5775 1.8880 -0.0604 -0.0120 0.0816 123 VAL B CB 3976 C CG1 . VAL B 124 ? 1.2438 1.5872 1.8958 -0.0601 -0.0084 0.0832 123 VAL B CG1 3977 C CG2 . VAL B 124 ? 1.2488 1.5588 1.8822 -0.0670 -0.0148 0.0781 123 VAL B CG2 3978 N N . ARG B 125 ? 1.1830 1.5340 1.8608 -0.0890 -0.0184 0.0746 124 ARG B N 3979 C CA . ARG B 125 ? 1.1722 1.5239 1.8617 -0.0994 -0.0192 0.0714 124 ARG B CA 3980 C C . ARG B 125 ? 1.1986 1.5340 1.8814 -0.1039 -0.0193 0.0690 124 ARG B C 3981 O O . ARG B 125 ? 1.2250 1.5505 1.8959 -0.1023 -0.0187 0.0694 124 ARG B O 3982 C CB . ARG B 125 ? 1.1581 1.5231 1.8588 -0.1045 -0.0211 0.0686 124 ARG B CB 3983 C CG . ARG B 125 ? 1.1485 1.5330 1.8604 -0.1030 -0.0225 0.0709 124 ARG B CG 3984 C CD . ARG B 125 ? 1.1503 1.5438 1.8723 -0.1106 -0.0265 0.0665 124 ARG B CD 3985 N NE . ARG B 125 ? 1.1602 1.5745 1.8931 -0.1101 -0.0301 0.0685 124 ARG B NE 3986 C CZ . ARG B 125 ? 1.2068 1.6304 1.9486 -0.1175 -0.0358 0.0644 124 ARG B CZ 3987 N NH1 . ARG B 125 ? 1.2256 1.6371 1.9639 -0.1241 -0.0373 0.0576 124 ARG B NH1 3988 N NH2 . ARG B 125 ? 1.2270 1.6726 1.9818 -0.1180 -0.0402 0.0669 124 ARG B NH2 3989 N N . GLY B 126 ? 1.2207 1.5543 1.9122 -0.1096 -0.0200 0.0675 125 GLY B N 3990 C CA . GLY B 126 ? 1.2342 1.5583 1.9260 -0.1151 -0.0205 0.0657 125 GLY B CA 3991 C C . GLY B 126 ? 1.2323 1.5635 1.9349 -0.1202 -0.0182 0.0626 125 GLY B C 3992 O O . GLY B 126 ? 1.2201 1.5604 1.9313 -0.1208 -0.0181 0.0605 125 GLY B O 3993 N N . ALA B 127 ? 1.2452 1.5710 1.9466 -0.1241 -0.0160 0.0622 126 ALA B N 3994 C CA . ALA B 127 ? 1.2457 1.5780 1.9562 -0.1277 -0.0117 0.0593 126 ALA B CA 3995 C C . ALA B 127 ? 1.2437 1.5776 1.9679 -0.1327 -0.0115 0.0595 126 ALA B C 3996 O O . ALA B 127 ? 1.2415 1.5743 1.9664 -0.1371 -0.0074 0.0607 126 ALA B O 3997 C CB . ALA B 127 ? 1.2579 1.5864 1.9551 -0.1273 -0.0071 0.0602 126 ALA B CB 3998 N N . PRO B 128 ? 1.2339 1.5715 1.9696 -0.1323 -0.0161 0.0590 127 PRO B N 3999 C CA . PRO B 128 ? 1.2307 1.5739 1.9826 -0.1360 -0.0177 0.0591 127 PRO B CA 4000 C C . PRO B 128 ? 1.2376 1.5923 2.0044 -0.1358 -0.0109 0.0565 127 PRO B C 4001 O O . PRO B 128 ? 1.2568 1.6123 2.0203 -0.1323 -0.0068 0.0533 127 PRO B O 4002 C CB . PRO B 128 ? 1.2348 1.5773 1.9907 -0.1331 -0.0249 0.0599 127 PRO B CB 4003 C CG . PRO B 128 ? 1.2310 1.5726 1.9810 -0.1289 -0.0232 0.0592 127 PRO B CG 4004 C CD . PRO B 128 ? 1.2287 1.5670 1.9643 -0.1285 -0.0197 0.0591 127 PRO B CD 4005 N N . TYR B 129 ? 1.2315 1.5952 2.0147 -0.1396 -0.0100 0.0576 128 TYR B N 4006 C CA . TYR B 129 ? 1.2322 1.6093 2.0312 -0.1379 -0.0016 0.0557 128 TYR B CA 4007 C C . TYR B 129 ? 1.2327 1.6245 2.0573 -0.1394 -0.0049 0.0574 128 TYR B C 4008 O O . TYR B 129 ? 1.2248 1.6151 2.0526 -0.1434 -0.0148 0.0600 128 TYR B O 4009 C CB . TYR B 129 ? 1.2173 1.5948 2.0084 -0.1416 0.0085 0.0568 128 TYR B CB 4010 C CG . TYR B 129 ? 1.2102 1.5834 1.9992 -0.1508 0.0067 0.0620 128 TYR B CG 4011 C CD1 . TYR B 129 ? 1.2092 1.5646 1.9768 -0.1524 0.0013 0.0637 128 TYR B CD1 4012 C CD2 . TYR B 129 ? 1.2134 1.6000 2.0225 -0.1580 0.0106 0.0652 128 TYR B CD2 4013 C CE1 . TYR B 129 ? 1.2203 1.5662 1.9831 -0.1607 -0.0007 0.0677 128 TYR B CE1 4014 C CE2 . TYR B 129 ? 1.2062 1.5860 2.0134 -0.1687 0.0082 0.0698 128 TYR B CE2 4015 C CZ . TYR B 129 ? 1.2130 1.5698 1.9951 -0.1700 0.0022 0.0707 128 TYR B CZ 4016 O OH . TYR B 129 ? 1.2074 1.5519 1.9847 -0.1804 -0.0006 0.0746 128 TYR B OH 4017 N N . ASP B 130 ? 1.2283 1.6348 2.0706 -0.1352 0.0028 0.0558 129 ASP B N 4018 C CA . ASP B 130 ? 1.2268 1.6531 2.0981 -0.1355 0.0006 0.0580 129 ASP B CA 4019 C C . ASP B 130 ? 1.2536 1.6903 2.1347 -0.1467 0.0044 0.0624 129 ASP B C 4020 O O . ASP B 130 ? 1.2342 1.6831 2.1238 -0.1476 0.0174 0.0633 129 ASP B O 4021 C CB . ASP B 130 ? 1.2250 1.6639 2.1123 -0.1249 0.0091 0.0548 129 ASP B CB 4022 C CG . ASP B 130 ? 1.2180 1.6778 2.1369 -0.1213 0.0036 0.0574 129 ASP B CG 4023 O OD1 . ASP B 130 ? 1.2051 1.6749 2.1372 -0.1298 -0.0051 0.0617 129 ASP B OD1 4024 O OD2 . ASP B 130 ? 1.1892 1.6548 2.1194 -0.1095 0.0072 0.0548 129 ASP B OD2 4025 N N . TRP B 131 ? 1.2962 1.7261 2.1742 -0.1556 -0.0068 0.0651 130 TRP B N 4026 C CA . TRP B 131 ? 1.3349 1.7681 2.2190 -0.1690 -0.0057 0.0694 130 TRP B CA 4027 C C . TRP B 131 ? 1.2964 1.7594 2.2181 -0.1744 -0.0042 0.0727 130 TRP B C 4028 O O . TRP B 131 ? 1.2876 1.7563 2.2190 -0.1875 -0.0021 0.0770 130 TRP B O 4029 C CB . TRP B 131 ? 1.3931 1.8056 2.2595 -0.1764 -0.0195 0.0699 130 TRP B CB 4030 C CG . TRP B 131 ? 1.4107 1.8211 2.2780 -0.1715 -0.0344 0.0679 130 TRP B CG 4031 C CD1 . TRP B 131 ? 1.4175 1.8095 2.2610 -0.1640 -0.0398 0.0657 130 TRP B CD1 4032 C CD2 . TRP B 131 ? 1.4211 1.8495 2.3139 -0.1733 -0.0456 0.0688 130 TRP B CD2 4033 N NE1 . TRP B 131 ? 1.4284 1.8230 2.2776 -0.1609 -0.0527 0.0655 130 TRP B NE1 4034 C CE2 . TRP B 131 ? 1.4280 1.8443 2.3066 -0.1661 -0.0576 0.0672 130 TRP B CE2 4035 C CE3 . TRP B 131 ? 1.4206 1.8760 2.3479 -0.1803 -0.0467 0.0716 130 TRP B CE3 4036 C CZ2 . TRP B 131 ? 1.4326 1.8601 2.3266 -0.1649 -0.0718 0.0680 130 TRP B CZ2 4037 C CZ3 . TRP B 131 ? 1.4355 1.9052 2.3821 -0.1792 -0.0617 0.0720 130 TRP B CZ3 4038 C CH2 . TRP B 131 ? 1.4463 1.9006 2.3744 -0.1712 -0.0746 0.0701 130 TRP B CH2 4039 N N . ARG B 132 ? 1.2728 1.7548 2.2167 -0.1644 -0.0057 0.0712 131 ARG B N 4040 C CA . ARG B 132 ? 1.2812 1.7972 2.2651 -0.1662 -0.0026 0.0745 131 ARG B CA 4041 C C . ARG B 132 ? 1.2437 1.7741 2.2359 -0.1657 0.0187 0.0764 131 ARG B C 4042 O O . ARG B 132 ? 1.2328 1.7915 2.2566 -0.1725 0.0249 0.0813 131 ARG B O 4043 C CB . ARG B 132 ? 1.3350 1.8651 2.3374 -0.1516 -0.0087 0.0725 131 ARG B CB 4044 C CG . ARG B 132 ? 1.3694 1.8877 2.3644 -0.1503 -0.0292 0.0719 131 ARG B CG 4045 C CD . ARG B 132 ? 1.3922 1.9244 2.4063 -0.1351 -0.0342 0.0717 131 ARG B CD 4046 N NE . ARG B 132 ? 1.4197 1.9383 2.4187 -0.1208 -0.0234 0.0677 131 ARG B NE 4047 C CZ . ARG B 132 ? 1.4524 1.9774 2.4640 -0.1054 -0.0230 0.0668 131 ARG B CZ 4048 N NH1 . ARG B 132 ? 1.4720 2.0200 2.5133 -0.1003 -0.0330 0.0704 131 ARG B NH1 4049 N NH2 . ARG B 132 ? 1.4546 1.9617 2.4486 -0.0949 -0.0136 0.0622 131 ARG B NH2 4050 N N . ARG B 133 ? 1.2136 1.7258 2.1775 -0.1577 0.0296 0.0727 132 ARG B N 4051 C CA . ARG B 133 ? 1.2142 1.7355 2.1775 -0.1543 0.0503 0.0733 132 ARG B CA 4052 C C . ARG B 133 ? 1.2096 1.7124 2.1458 -0.1645 0.0577 0.0766 132 ARG B C 4053 O O . ARG B 133 ? 1.1998 1.6798 2.1152 -0.1721 0.0469 0.0773 132 ARG B O 4054 C CB . ARG B 133 ? 1.2276 1.7401 2.1761 -0.1369 0.0566 0.0658 132 ARG B CB 4055 C CG . ARG B 133 ? 1.2345 1.7645 2.2098 -0.1243 0.0529 0.0633 132 ARG B CG 4056 C CD . ARG B 133 ? 1.2656 1.7797 2.2224 -0.1082 0.0580 0.0552 132 ARG B CD 4057 N NE . ARG B 133 ? 1.3076 1.8408 2.2913 -0.0937 0.0618 0.0536 132 ARG B NE 4058 C CZ . ARG B 133 ? 1.3374 1.8577 2.3104 -0.0781 0.0659 0.0463 132 ARG B CZ 4059 N NH1 . ARG B 133 ? 1.3605 1.8503 2.2979 -0.0768 0.0659 0.0398 132 ARG B NH1 4060 N NH2 . ARG B 133 ? 1.3417 1.8793 2.3404 -0.0636 0.0693 0.0455 132 ARG B NH2 4061 N N . ALA B 134 ? 1.2138 1.7258 2.1488 -0.1633 0.0768 0.0790 133 ALA B N 4062 C CA . ALA B 134 ? 1.2134 1.7072 2.1197 -0.1706 0.0862 0.0831 133 ALA B CA 4063 C C . ALA B 134 ? 1.2044 1.6758 2.0735 -0.1581 0.0893 0.0762 133 ALA B C 4064 O O . ALA B 134 ? 1.2318 1.7044 2.1014 -0.1453 0.0876 0.0685 133 ALA B O 4065 C CB . ALA B 134 ? 1.2456 1.7619 2.1689 -0.1763 0.1061 0.0907 133 ALA B CB 4066 N N . PRO B 135 ? 1.1903 1.6401 2.0269 -0.1620 0.0931 0.0790 134 PRO B N 4067 C CA . PRO B 135 ? 1.2196 1.6500 2.0213 -0.1513 0.0941 0.0726 134 PRO B CA 4068 C C . PRO B 135 ? 1.2818 1.7208 2.0800 -0.1383 0.1073 0.0661 134 PRO B C 4069 O O . PRO B 135 ? 1.3093 1.7344 2.0869 -0.1287 0.1026 0.0576 134 PRO B O 4070 C CB . PRO B 135 ? 1.2166 1.6291 1.9896 -0.1581 0.0992 0.0797 134 PRO B CB 4071 C CG . PRO B 135 ? 1.2167 1.6273 2.0039 -0.1724 0.0920 0.0873 134 PRO B CG 4072 C CD . PRO B 135 ? 1.2060 1.6451 2.0354 -0.1767 0.0930 0.0881 134 PRO B CD 4073 N N . ASN B 136 ? 1.3190 1.7804 2.1370 -0.1381 0.1238 0.0700 135 ASN B N 4074 C CA . ASN B 136 ? 1.3619 1.8320 2.1769 -0.1240 0.1386 0.0637 135 ASN B CA 4075 C C . ASN B 136 ? 1.4039 1.8738 2.2289 -0.1114 0.1297 0.0531 135 ASN B C 4076 O O . ASN B 136 ? 1.4857 1.9476 2.2933 -0.0985 0.1364 0.0442 135 ASN B O 4077 C CB . ASN B 136 ? 1.3570 1.8577 2.2008 -0.1259 0.1580 0.0710 135 ASN B CB 4078 C CG . ASN B 136 ? 1.3477 1.8756 2.2398 -0.1318 0.1508 0.0751 135 ASN B CG 4079 O OD1 . ASN B 136 ? 1.3210 1.8419 2.2212 -0.1373 0.1312 0.0742 135 ASN B OD1 4080 N ND2 . ASN B 136 ? 1.3593 1.9201 2.2839 -0.1300 0.1668 0.0798 135 ASN B ND2 4081 N N . GLU B 137 ? 1.4049 1.8810 2.2552 -0.1152 0.1146 0.0540 136 GLU B N 4082 C CA . GLU B 137 ? 1.4269 1.9011 2.2874 -0.1041 0.1054 0.0461 136 GLU B CA 4083 C C . GLU B 137 ? 1.4306 1.8815 2.2747 -0.1070 0.0862 0.0429 136 GLU B C 4084 O O . GLU B 137 ? 1.4517 1.9015 2.3086 -0.1024 0.0755 0.0401 136 GLU B O 4085 C CB . GLU B 137 ? 1.4243 1.9270 2.3285 -0.1032 0.1037 0.0504 136 GLU B CB 4086 C CG . GLU B 137 ? 1.4404 1.9720 2.3679 -0.0974 0.1236 0.0532 136 GLU B CG 4087 C CD . GLU B 137 ? 1.4319 1.9964 2.4070 -0.0981 0.1196 0.0587 136 GLU B CD 4088 O OE1 . GLU B 137 ? 1.4212 2.0040 2.4176 -0.0832 0.1276 0.0559 136 GLU B OE1 4089 O OE2 . GLU B 137 ? 1.4234 1.9948 2.4140 -0.1130 0.1074 0.0655 136 GLU B OE2 4090 N N . ASN B 138 ? 1.4155 1.8484 2.2314 -0.1139 0.0825 0.0440 137 ASN B N 4091 C CA . ASN B 138 ? 1.3916 1.8047 2.1910 -0.1154 0.0670 0.0410 137 ASN B CA 4092 C C . ASN B 138 ? 1.3634 1.7581 2.1278 -0.1129 0.0685 0.0361 137 ASN B C 4093 O O . ASN B 138 ? 1.3846 1.7668 2.1321 -0.1175 0.0593 0.0375 137 ASN B O 4094 C CB . ASN B 138 ? 1.3826 1.7944 2.1872 -0.1264 0.0562 0.0484 137 ASN B CB 4095 C CG . ASN B 138 ? 1.3709 1.7934 2.2031 -0.1274 0.0464 0.0502 137 ASN B CG 4096 O OD1 . ASN B 138 ? 1.3494 1.7654 2.1826 -0.1219 0.0376 0.0464 137 ASN B OD1 4097 N ND2 . ASN B 138 ? 1.3721 1.8105 2.2261 -0.1350 0.0473 0.0564 137 ASN B ND2 4098 N N . GLY B 139 ? 1.3124 1.7060 2.0657 -0.1044 0.0798 0.0298 138 GLY B N 4099 C CA . GLY B 139 ? 1.3043 1.6803 2.0229 -0.1011 0.0799 0.0234 138 GLY B CA 4100 C C . GLY B 139 ? 1.2880 1.6488 1.9967 -0.1022 0.0635 0.0181 138 GLY B C 4101 O O . GLY B 139 ? 1.2890 1.6404 1.9764 -0.1057 0.0570 0.0187 138 GLY B O 4102 N N . PRO B 140 ? 1.2897 1.6489 2.0149 -0.0991 0.0570 0.0138 139 PRO B N 4103 C CA . PRO B 140 ? 1.2847 1.6309 2.0038 -0.1017 0.0427 0.0101 139 PRO B CA 4104 C C . PRO B 140 ? 1.2283 1.5763 1.9478 -0.1100 0.0328 0.0178 139 PRO B C 4105 O O . PRO B 140 ? 1.2292 1.5694 1.9350 -0.1126 0.0242 0.0159 139 PRO B O 4106 C CB . PRO B 140 ? 1.3053 1.6514 2.0463 -0.0975 0.0397 0.0082 139 PRO B CB 4107 C CG . PRO B 140 ? 1.3238 1.6789 2.0746 -0.0887 0.0532 0.0060 139 PRO B CG 4108 C CD . PRO B 140 ? 1.3116 1.6814 2.0622 -0.0925 0.0628 0.0130 139 PRO B CD 4109 N N . TYR B 141 ? 1.1762 1.5348 1.9118 -0.1136 0.0339 0.0261 140 TYR B N 4110 C CA . TYR B 141 ? 1.1746 1.5323 1.9078 -0.1199 0.0261 0.0330 140 TYR B CA 4111 C C . TYR B 141 ? 1.1939 1.5450 1.9022 -0.1210 0.0264 0.0341 140 TYR B C 4112 O O . TYR B 141 ? 1.1912 1.5376 1.8908 -0.1222 0.0176 0.0352 140 TYR B O 4113 C CB . TYR B 141 ? 1.1559 1.5231 1.9064 -0.1242 0.0281 0.0403 140 TYR B CB 4114 C CG . TYR B 141 ? 1.1334 1.4953 1.8755 -0.1299 0.0228 0.0468 140 TYR B CG 4115 C CD1 . TYR B 141 ? 1.1274 1.4844 1.8701 -0.1308 0.0123 0.0483 140 TYR B CD1 4116 C CD2 . TYR B 141 ? 1.1359 1.4955 1.8677 -0.1338 0.0291 0.0518 140 TYR B CD2 4117 C CE1 . TYR B 141 ? 1.1147 1.4644 1.8474 -0.1338 0.0082 0.0533 140 TYR B CE1 4118 C CE2 . TYR B 141 ? 1.1386 1.4887 1.8604 -0.1379 0.0241 0.0574 140 TYR B CE2 4119 C CZ . TYR B 141 ? 1.1170 1.4620 1.8391 -0.1371 0.0136 0.0575 140 TYR B CZ 4120 O OH . TYR B 141 ? 1.0655 1.3988 1.7755 -0.1391 0.0093 0.0621 140 TYR B OH 4121 N N . PHE B 142 ? 1.2274 1.5790 1.9241 -0.1197 0.0370 0.0346 141 PHE B N 4122 C CA . PHE B 142 ? 1.2763 1.6204 1.9466 -0.1197 0.0376 0.0371 141 PHE B CA 4123 C C . PHE B 142 ? 1.2961 1.6330 1.9474 -0.1160 0.0302 0.0295 141 PHE B C 4124 O O . PHE B 142 ? 1.2788 1.6115 1.9139 -0.1159 0.0234 0.0320 141 PHE B O 4125 C CB . PHE B 142 ? 1.2998 1.6455 1.9608 -0.1194 0.0522 0.0407 141 PHE B CB 4126 C CG . PHE B 142 ? 1.2779 1.6309 1.9571 -0.1261 0.0581 0.0496 141 PHE B CG 4127 C CD1 . PHE B 142 ? 1.2657 1.6122 1.9441 -0.1318 0.0512 0.0568 141 PHE B CD1 4128 C CD2 . PHE B 142 ? 1.2713 1.6378 1.9691 -0.1267 0.0703 0.0506 141 PHE B CD2 4129 C CE1 . PHE B 142 ? 1.2551 1.6055 1.9492 -0.1398 0.0549 0.0641 141 PHE B CE1 4130 C CE2 . PHE B 142 ? 1.2593 1.6348 1.9770 -0.1350 0.0742 0.0588 141 PHE B CE2 4131 C CZ . PHE B 142 ? 1.2519 1.6179 1.9669 -0.1425 0.0657 0.0652 141 PHE B CZ 4132 N N . LEU B 143 ? 1.3380 1.6730 1.9915 -0.1128 0.0306 0.0203 142 LEU B N 4133 C CA . LEU B 143 ? 1.3850 1.7121 2.0232 -0.1117 0.0212 0.0118 142 LEU B CA 4134 C C . LEU B 143 ? 1.3283 1.6583 1.9780 -0.1163 0.0078 0.0141 142 LEU B C 4135 O O . LEU B 143 ? 1.3174 1.6472 1.9551 -0.1173 -0.0011 0.0137 142 LEU B O 4136 C CB . LEU B 143 ? 1.4535 1.7735 2.0930 -0.1079 0.0240 0.0010 142 LEU B CB 4137 C CG . LEU B 143 ? 1.5444 1.8613 2.1693 -0.1009 0.0386 -0.0032 142 LEU B CG 4138 C CD1 . LEU B 143 ? 1.5665 1.8759 2.1977 -0.0951 0.0421 -0.0133 142 LEU B CD1 4139 C CD2 . LEU B 143 ? 1.5901 1.8985 2.1796 -0.0988 0.0381 -0.0066 142 LEU B CD2 4140 N N . ALA B 144 ? 1.2876 1.6217 1.9608 -0.1184 0.0069 0.0172 143 ALA B N 4141 C CA . ALA B 144 ? 1.2697 1.6075 1.9545 -0.1222 -0.0029 0.0207 143 ALA B CA 4142 C C . ALA B 144 ? 1.2524 1.5948 1.9309 -0.1223 -0.0058 0.0287 143 ALA B C 4143 O O . ALA B 144 ? 1.2652 1.6119 1.9437 -0.1233 -0.0139 0.0301 143 ALA B O 4144 C CB . ALA B 144 ? 1.2602 1.5997 1.9668 -0.1231 -0.0021 0.0235 143 ALA B CB 4145 N N . LEU B 145 ? 1.2148 1.5563 1.8891 -0.1213 0.0012 0.0342 144 LEU B N 4146 C CA . LEU B 145 ? 1.1710 1.5114 1.8361 -0.1203 -0.0006 0.0417 144 LEU B CA 4147 C C . LEU B 145 ? 1.1630 1.5022 1.8074 -0.1169 -0.0052 0.0410 144 LEU B C 4148 O O . LEU B 145 ? 1.1117 1.4545 1.7540 -0.1146 -0.0124 0.0445 144 LEU B O 4149 C CB . LEU B 145 ? 1.1860 1.5219 1.8489 -0.1218 0.0081 0.0473 144 LEU B CB 4150 C CG . LEU B 145 ? 1.2317 1.5599 1.8823 -0.1210 0.0071 0.0553 144 LEU B CG 4151 C CD1 . LEU B 145 ? 1.2358 1.5649 1.8931 -0.1193 -0.0010 0.0574 144 LEU B CD1 4152 C CD2 . LEU B 145 ? 1.2570 1.5799 1.9102 -0.1260 0.0153 0.0606 144 LEU B CD2 4153 N N . ARG B 146 ? 1.2087 1.5439 1.8372 -0.1155 -0.0010 0.0364 145 ARG B N 4154 C CA . ARG B 146 ? 1.2764 1.6098 1.8819 -0.1118 -0.0069 0.0350 145 ARG B CA 4155 C C . ARG B 146 ? 1.2682 1.6101 1.8814 -0.1131 -0.0201 0.0303 145 ARG B C 4156 O O . ARG B 146 ? 1.2472 1.5951 1.8545 -0.1102 -0.0286 0.0337 145 ARG B O 4157 C CB . ARG B 146 ? 1.3659 1.6921 1.9509 -0.1098 -0.0003 0.0290 145 ARG B CB 4158 C CG . ARG B 146 ? 1.4734 1.7947 2.0278 -0.1050 -0.0046 0.0305 145 ARG B CG 4159 C CD . ARG B 146 ? 1.5730 1.8910 2.1095 -0.1037 -0.0110 0.0192 145 ARG B CD 4160 N NE . ARG B 146 ? 1.6793 1.9890 2.2074 -0.1027 0.0004 0.0116 145 ARG B NE 4161 C CZ . ARG B 146 ? 1.7983 2.1065 2.3404 -0.1050 0.0008 0.0020 145 ARG B CZ 4162 N NH1 . ARG B 146 ? 1.8063 2.1201 2.3718 -0.1102 -0.0094 -0.0006 145 ARG B NH1 4163 N NH2 . ARG B 146 ? 1.8774 2.1778 2.4094 -0.1012 0.0128 -0.0043 145 ARG B NH2 4164 N N . GLU B 147 ? 1.2982 1.6410 1.9255 -0.1176 -0.0217 0.0230 146 GLU B N 4165 C CA . GLU B 147 ? 1.3294 1.6797 1.9667 -0.1217 -0.0335 0.0188 146 GLU B CA 4166 C C . GLU B 147 ? 1.2598 1.6227 1.9154 -0.1223 -0.0379 0.0268 146 GLU B C 4167 O O . GLU B 147 ? 1.2438 1.6187 1.9034 -0.1231 -0.0476 0.0275 146 GLU B O 4168 C CB . GLU B 147 ? 1.3998 1.7431 2.0472 -0.1267 -0.0333 0.0101 146 GLU B CB 4169 C CG . GLU B 147 ? 1.4980 1.8283 2.1242 -0.1251 -0.0317 -0.0004 146 GLU B CG 4170 C CD . GLU B 147 ? 1.5874 1.9073 2.2210 -0.1298 -0.0346 -0.0102 146 GLU B CD 4171 O OE1 . GLU B 147 ? 1.6277 1.9464 2.2815 -0.1314 -0.0307 -0.0078 146 GLU B OE1 4172 O OE2 . GLU B 147 ? 1.6312 1.9418 2.2482 -0.1315 -0.0417 -0.0204 146 GLU B OE2 4173 N N . MET B 148 ? 1.2195 1.5808 1.8862 -0.1216 -0.0308 0.0327 147 MET B N 4174 C CA . MET B 148 ? 1.2126 1.5833 1.8927 -0.1205 -0.0330 0.0400 147 MET B CA 4175 C C . MET B 148 ? 1.2063 1.5818 1.8748 -0.1133 -0.0360 0.0459 147 MET B C 4176 O O . MET B 148 ? 1.1667 1.5558 1.8440 -0.1110 -0.0415 0.0494 147 MET B O 4177 C CB . MET B 148 ? 1.2007 1.5650 1.8892 -0.1205 -0.0259 0.0440 147 MET B CB 4178 C CG . MET B 148 ? 1.1875 1.5586 1.8863 -0.1187 -0.0274 0.0503 147 MET B CG 4179 S SD . MET B 148 ? 1.1778 1.5406 1.8851 -0.1200 -0.0223 0.0532 147 MET B SD 4180 C CE . MET B 148 ? 1.1918 1.5426 1.8840 -0.1169 -0.0177 0.0561 147 MET B CE 4181 N N . ILE B 149 ? 1.2413 1.6057 1.8903 -0.1092 -0.0316 0.0478 148 ILE B N 4182 C CA . ILE B 149 ? 1.2792 1.6434 1.9132 -0.1010 -0.0344 0.0541 148 ILE B CA 4183 C C . ILE B 149 ? 1.2624 1.6401 1.8928 -0.0986 -0.0455 0.0518 148 ILE B C 4184 O O . ILE B 149 ? 1.2204 1.6097 1.8542 -0.0920 -0.0513 0.0569 148 ILE B O 4185 C CB . ILE B 149 ? 1.3327 1.6794 1.9443 -0.0986 -0.0269 0.0573 148 ILE B CB 4186 C CG1 . ILE B 149 ? 1.3425 1.6783 1.9604 -0.1015 -0.0184 0.0611 148 ILE B CG1 4187 C CG2 . ILE B 149 ? 1.3446 1.6878 1.9362 -0.0893 -0.0310 0.0638 148 ILE B CG2 4188 C CD1 . ILE B 149 ? 1.3676 1.6897 1.9722 -0.1043 -0.0090 0.0630 148 ILE B CD1 4189 N N . GLU B 150 ? 1.2720 1.6486 1.8955 -0.1034 -0.0488 0.0438 149 GLU B N 4190 C CA . GLU B 150 ? 1.2914 1.6806 1.9113 -0.1033 -0.0619 0.0400 149 GLU B CA 4191 C C . GLU B 150 ? 1.2920 1.7028 1.9402 -0.1076 -0.0698 0.0404 149 GLU B C 4192 O O . GLU B 150 ? 1.2994 1.7281 1.9522 -0.1038 -0.0799 0.0433 149 GLU B O 4193 C CB . GLU B 150 ? 1.3083 1.6878 1.9133 -0.1085 -0.0639 0.0293 149 GLU B CB 4194 C CG . GLU B 150 ? 1.3425 1.7048 1.9160 -0.1028 -0.0567 0.0299 149 GLU B CG 4195 C CD . GLU B 150 ? 1.3963 1.7473 1.9528 -0.1062 -0.0559 0.0186 149 GLU B CD 4196 O OE1 . GLU B 150 ? 1.4638 1.8179 2.0307 -0.1131 -0.0636 0.0094 149 GLU B OE1 4197 O OE2 . GLU B 150 ? 1.4091 1.7465 1.9402 -0.1019 -0.0469 0.0190 149 GLU B OE2 4198 N N . GLU B 151 ? 1.2907 1.7010 1.9585 -0.1152 -0.0650 0.0385 150 GLU B N 4199 C CA . GLU B 151 ? 1.3033 1.7329 1.9984 -0.1206 -0.0697 0.0405 150 GLU B CA 4200 C C . GLU B 151 ? 1.2681 1.7124 1.9721 -0.1114 -0.0679 0.0506 150 GLU B C 4201 O O . GLU B 151 ? 1.2412 1.7093 1.9615 -0.1108 -0.0750 0.0538 150 GLU B O 4202 C CB . GLU B 151 ? 1.3588 1.7800 2.0684 -0.1289 -0.0630 0.0384 150 GLU B CB 4203 C CG . GLU B 151 ? 1.3988 1.8367 2.1343 -0.1377 -0.0676 0.0399 150 GLU B CG 4204 C CD . GLU B 151 ? 1.4257 1.8540 2.1733 -0.1430 -0.0597 0.0415 150 GLU B CD 4205 O OE1 . GLU B 151 ? 1.4210 1.8631 2.1885 -0.1474 -0.0593 0.0471 150 GLU B OE1 4206 O OE2 . GLU B 151 ? 1.4632 1.8717 2.2009 -0.1422 -0.0536 0.0380 150 GLU B OE2 4207 N N . MET B 152 ? 1.2566 1.6869 1.9505 -0.1041 -0.0584 0.0555 151 MET B N 4208 C CA . MET B 152 ? 1.2577 1.6958 1.9553 -0.0936 -0.0555 0.0640 151 MET B CA 4209 C C . MET B 152 ? 1.2530 1.7017 1.9414 -0.0828 -0.0630 0.0677 151 MET B C 4210 O O . MET B 152 ? 1.2270 1.6954 1.9282 -0.0749 -0.0651 0.0734 151 MET B O 4211 C CB . MET B 152 ? 1.2701 1.6855 1.9550 -0.0895 -0.0454 0.0669 151 MET B CB 4212 C CG . MET B 152 ? 1.2433 1.6521 1.9396 -0.0975 -0.0393 0.0650 151 MET B CG 4213 S SD . MET B 152 ? 1.2123 1.5953 1.8946 -0.0959 -0.0308 0.0665 151 MET B SD 4214 C CE . MET B 152 ? 1.1991 1.5832 1.8797 -0.0848 -0.0283 0.0734 151 MET B CE 4215 N N . TYR B 153 ? 1.2640 1.7005 1.9300 -0.0813 -0.0666 0.0651 152 TYR B N 4216 C CA . TYR B 153 ? 1.3046 1.7496 1.9585 -0.0707 -0.0757 0.0688 152 TYR B CA 4217 C C . TYR B 153 ? 1.3053 1.7825 1.9813 -0.0734 -0.0886 0.0673 152 TYR B C 4218 O O . TYR B 153 ? 1.3242 1.8213 2.0079 -0.0626 -0.0944 0.0735 152 TYR B O 4219 C CB . TYR B 153 ? 1.3431 1.7683 1.9664 -0.0705 -0.0772 0.0657 152 TYR B CB 4220 C CG . TYR B 153 ? 1.3859 1.8187 1.9931 -0.0598 -0.0886 0.0693 152 TYR B CG 4221 C CD1 . TYR B 153 ? 1.3963 1.8484 2.0079 -0.0638 -0.1034 0.0639 152 TYR B CD1 4222 C CD2 . TYR B 153 ? 1.4287 1.8471 2.0147 -0.0459 -0.0858 0.0782 152 TYR B CD2 4223 C CE1 . TYR B 153 ? 1.4263 1.8865 2.0226 -0.0533 -0.1158 0.0674 152 TYR B CE1 4224 C CE2 . TYR B 153 ? 1.4633 1.8873 2.0329 -0.0346 -0.0969 0.0826 152 TYR B CE2 4225 C CZ . TYR B 153 ? 1.4688 1.9152 2.0438 -0.0379 -0.1123 0.0772 152 TYR B CZ 4226 O OH . TYR B 153 ? 1.5365 1.9898 2.0946 -0.0259 -0.1253 0.0817 152 TYR B OH 4227 N N . GLN B 154 ? 1.2900 1.7721 1.9768 -0.0879 -0.0933 0.0591 153 GLN B N 4228 C CA . GLN B 154 ? 1.2642 1.7756 1.9734 -0.0947 -0.1069 0.0567 153 GLN B CA 4229 C C . GLN B 154 ? 1.2076 1.7457 1.9511 -0.0953 -0.1036 0.0633 153 GLN B C 4230 O O . GLN B 154 ? 1.1576 1.7269 1.9202 -0.0915 -0.1125 0.0675 153 GLN B O 4231 C CB . GLN B 154 ? 1.2889 1.7916 1.9976 -0.1110 -0.1123 0.0453 153 GLN B CB 4232 C CG . GLN B 154 ? 1.3262 1.8092 2.0008 -0.1095 -0.1180 0.0380 153 GLN B CG 4233 C CD . GLN B 154 ? 1.3448 1.8185 2.0169 -0.1239 -0.1248 0.0254 153 GLN B CD 4234 O OE1 . GLN B 154 ? 1.3277 1.7982 2.0181 -0.1348 -0.1202 0.0222 153 GLN B OE1 4235 N NE2 . GLN B 154 ? 1.3948 1.8615 2.0414 -0.1234 -0.1359 0.0182 153 GLN B NE2 4236 N N . LEU B 155 ? 1.1923 1.7194 1.9433 -0.0994 -0.0908 0.0646 154 LEU B N 4237 C CA . LEU B 155 ? 1.1728 1.7219 1.9525 -0.1000 -0.0848 0.0714 154 LEU B CA 4238 C C . LEU B 155 ? 1.1776 1.7407 1.9588 -0.0815 -0.0808 0.0807 154 LEU B C 4239 O O . LEU B 155 ? 1.1825 1.7791 1.9895 -0.0785 -0.0832 0.0863 154 LEU B O 4240 C CB . LEU B 155 ? 1.1325 1.6622 1.9134 -0.1069 -0.0722 0.0710 154 LEU B CB 4241 C CG . LEU B 155 ? 1.0952 1.6297 1.8966 -0.1246 -0.0736 0.0677 154 LEU B CG 4242 C CD1 . LEU B 155 ? 1.0670 1.5736 1.8597 -0.1295 -0.0638 0.0655 154 LEU B CD1 4243 C CD2 . LEU B 155 ? 1.0643 1.6316 1.8971 -0.1272 -0.0721 0.0757 154 LEU B CD2 4244 N N . TYR B 156 ? 1.1816 1.7190 1.9359 -0.0692 -0.0745 0.0824 155 TYR B N 4245 C CA . TYR B 156 ? 1.1702 1.7112 1.9210 -0.0506 -0.0685 0.0904 155 TYR B CA 4246 C C . TYR B 156 ? 1.1951 1.7388 1.9311 -0.0354 -0.0770 0.0937 155 TYR B C 4247 O O . TYR B 156 ? 1.1666 1.7105 1.8973 -0.0178 -0.0729 0.1002 155 TYR B O 4248 C CB . TYR B 156 ? 1.1482 1.6569 1.8804 -0.0473 -0.0557 0.0908 155 TYR B CB 4249 C CG . TYR B 156 ? 1.1247 1.6303 1.8695 -0.0617 -0.0495 0.0878 155 TYR B CG 4250 C CD1 . TYR B 156 ? 1.1265 1.6585 1.8984 -0.0655 -0.0464 0.0915 155 TYR B CD1 4251 C CD2 . TYR B 156 ? 1.1122 1.5902 1.8431 -0.0715 -0.0465 0.0823 155 TYR B CD2 4252 C CE1 . TYR B 156 ? 1.1206 1.6475 1.9019 -0.0784 -0.0410 0.0901 155 TYR B CE1 4253 C CE2 . TYR B 156 ? 1.1159 1.5909 1.8581 -0.0831 -0.0420 0.0802 155 TYR B CE2 4254 C CZ . TYR B 156 ? 1.1135 1.6111 1.8792 -0.0865 -0.0395 0.0843 155 TYR B CZ 4255 O OH . TYR B 156 ? 1.0775 1.5696 1.8520 -0.0974 -0.0350 0.0837 155 TYR B OH 4256 N N . GLY B 157 ? 1.2415 1.7852 1.9684 -0.0414 -0.0889 0.0891 156 GLY B N 4257 C CA . GLY B 157 ? 1.2670 1.8201 1.9831 -0.0281 -0.1004 0.0927 156 GLY B CA 4258 C C . GLY B 157 ? 1.2871 1.8064 1.9663 -0.0144 -0.0967 0.0964 156 GLY B C 4259 O O . GLY B 157 ? 1.3284 1.8536 1.9980 0.0013 -0.1040 0.1023 156 GLY B O 4260 N N . GLY B 158 ? 1.2893 1.7736 1.9484 -0.0204 -0.0858 0.0938 157 GLY B N 4261 C CA . GLY B 158 ? 1.3286 1.7788 1.9542 -0.0101 -0.0809 0.0983 157 GLY B CA 4262 C C . GLY B 158 ? 1.3241 1.7417 1.9324 -0.0222 -0.0710 0.0942 157 GLY B C 4263 O O . GLY B 158 ? 1.2986 1.7184 1.9221 -0.0356 -0.0660 0.0884 157 GLY B O 4264 N N . PRO B 159 ? 1.3267 1.7144 1.9040 -0.0172 -0.0679 0.0980 158 PRO B N 4265 C CA . PRO B 159 ? 1.3093 1.6684 1.8716 -0.0284 -0.0579 0.0957 158 PRO B CA 4266 C C . PRO B 159 ? 1.2896 1.6351 1.8600 -0.0316 -0.0478 0.0956 158 PRO B C 4267 O O . PRO B 159 ? 1.2715 1.6189 1.8473 -0.0210 -0.0469 0.0992 158 PRO B O 4268 C CB . PRO B 159 ? 1.3382 1.6714 1.8666 -0.0202 -0.0573 0.1027 158 PRO B CB 4269 C CG . PRO B 159 ? 1.3687 1.7084 1.8937 -0.0014 -0.0643 0.1100 158 PRO B CG 4270 C CD . PRO B 159 ? 1.3463 1.7263 1.9020 -0.0001 -0.0734 0.1062 158 PRO B CD 4271 N N . VAL B 160 ? 1.2790 1.6114 1.8495 -0.0452 -0.0406 0.0914 159 VAL B N 4272 C CA . VAL B 160 ? 1.2742 1.5970 1.8546 -0.0508 -0.0334 0.0899 159 VAL B CA 4273 C C . VAL B 160 ? 1.2841 1.5740 1.8441 -0.0501 -0.0271 0.0944 159 VAL B C 4274 O O . VAL B 160 ? 1.2638 1.5367 1.8038 -0.0511 -0.0250 0.0981 159 VAL B O 4275 C CB . VAL B 160 ? 1.2814 1.6116 1.8785 -0.0659 -0.0304 0.0827 159 VAL B CB 4276 C CG1 . VAL B 160 ? 1.2851 1.6425 1.9005 -0.0692 -0.0370 0.0777 159 VAL B CG1 4277 C CG2 . VAL B 160 ? 1.3095 1.6239 1.8936 -0.0743 -0.0249 0.0818 159 VAL B CG2 4278 N N . VAL B 161 ? 1.2902 1.5701 1.8541 -0.0492 -0.0241 0.0941 160 VAL B N 4279 C CA . VAL B 161 ? 1.3122 1.5600 1.8601 -0.0525 -0.0194 0.0966 160 VAL B CA 4280 C C . VAL B 161 ? 1.2938 1.5424 1.8563 -0.0682 -0.0158 0.0915 160 VAL B C 4281 O O . VAL B 161 ? 1.2534 1.5164 1.8332 -0.0702 -0.0169 0.0871 160 VAL B O 4282 C CB . VAL B 161 ? 1.3446 1.5765 1.8831 -0.0402 -0.0197 0.0984 160 VAL B CB 4283 C CG1 . VAL B 161 ? 1.3777 1.5715 1.8967 -0.0453 -0.0165 0.1004 160 VAL B CG1 4284 C CG2 . VAL B 161 ? 1.3658 1.6035 1.8953 -0.0216 -0.0235 0.1035 160 VAL B CG2 4285 N N . LEU B 162 ? 1.2922 1.5270 1.8485 -0.0788 -0.0114 0.0929 161 LEU B N 4286 C CA . LEU B 162 ? 1.2723 1.5080 1.8436 -0.0929 -0.0083 0.0891 161 LEU B CA 4287 C C . LEU B 162 ? 1.2724 1.4823 1.8354 -0.0960 -0.0086 0.0904 161 LEU B C 4288 O O . LEU B 162 ? 1.2744 1.4586 1.8169 -0.0938 -0.0074 0.0956 161 LEU B O 4289 C CB . LEU B 162 ? 1.2757 1.5126 1.8470 -0.1028 -0.0021 0.0905 161 LEU B CB 4290 C CG . LEU B 162 ? 1.2827 1.5390 1.8554 -0.1000 -0.0019 0.0882 161 LEU B CG 4291 C CD1 . LEU B 162 ? 1.3017 1.5567 1.8716 -0.1087 0.0065 0.0895 161 LEU B CD1 4292 C CD2 . LEU B 162 ? 1.2716 1.5514 1.8662 -0.1004 -0.0060 0.0810 161 LEU B CD2 4293 N N . VAL B 163 ? 1.2640 1.4785 1.8408 -0.1010 -0.0109 0.0856 162 VAL B N 4294 C CA . VAL B 163 ? 1.3053 1.4956 1.8744 -0.1060 -0.0133 0.0850 162 VAL B CA 4295 C C . VAL B 163 ? 1.3442 1.5449 1.9341 -0.1213 -0.0133 0.0821 162 VAL B C 4296 O O . VAL B 163 ? 1.3422 1.5637 1.9498 -0.1218 -0.0151 0.0780 162 VAL B O 4297 C CB . VAL B 163 ? 1.2882 1.4737 1.8508 -0.0952 -0.0176 0.0817 162 VAL B CB 4298 C CG1 . VAL B 163 ? 1.2957 1.4499 1.8433 -0.0995 -0.0213 0.0799 162 VAL B CG1 4299 C CG2 . VAL B 163 ? 1.2931 1.4797 1.8431 -0.0779 -0.0168 0.0847 162 VAL B CG2 4300 N N . ALA B 164 ? 1.3879 1.5751 1.9770 -0.1334 -0.0110 0.0850 163 ALA B N 4301 C CA . ALA B 164 ? 1.3920 1.5937 2.0049 -0.1477 -0.0105 0.0834 163 ALA B CA 4302 C C . ALA B 164 ? 1.3987 1.5798 2.0099 -0.1593 -0.0160 0.0831 163 ALA B C 4303 O O . ALA B 164 ? 1.3849 1.5359 1.9748 -0.1602 -0.0170 0.0859 163 ALA B O 4304 C CB . ALA B 164 ? 1.3968 1.6106 2.0175 -0.1539 -0.0010 0.0876 163 ALA B CB 4305 N N . HIS B 165 ? 1.4111 1.6075 2.0445 -0.1681 -0.0208 0.0795 164 HIS B N 4306 C CA . HIS B 165 ? 1.4560 1.6369 2.0911 -0.1806 -0.0290 0.0780 164 HIS B CA 4307 C C . HIS B 165 ? 1.4594 1.6616 2.1248 -0.1966 -0.0266 0.0804 164 HIS B C 4308 O O . HIS B 165 ? 1.4163 1.6490 2.1049 -0.1949 -0.0229 0.0796 164 HIS B O 4309 C CB . HIS B 165 ? 1.4764 1.6559 2.1086 -0.1753 -0.0398 0.0713 164 HIS B CB 4310 C CG . HIS B 165 ? 1.5142 1.6783 2.1468 -0.1881 -0.0511 0.0683 164 HIS B CG 4311 N ND1 . HIS B 165 ? 1.5174 1.7026 2.1750 -0.1968 -0.0587 0.0658 164 HIS B ND1 4312 C CD2 . HIS B 165 ? 1.5537 1.6822 2.1642 -0.1940 -0.0572 0.0670 164 HIS B CD2 4313 C CE1 . HIS B 165 ? 1.5586 1.7240 2.2103 -0.2083 -0.0701 0.0629 164 HIS B CE1 4314 N NE2 . HIS B 165 ? 1.5829 1.7121 2.2053 -0.2075 -0.0693 0.0632 164 HIS B NE2 4315 N N . SER B 166 ? 1.5133 1.6989 2.1788 -0.2119 -0.0285 0.0835 165 SER B N 4316 C CA . SER B 166 ? 1.5560 1.7635 2.2537 -0.2289 -0.0267 0.0866 165 SER B CA 4317 C C . SER B 166 ? 1.4753 1.7132 2.1916 -0.2263 -0.0118 0.0911 165 SER B C 4318 O O . SER B 166 ? 1.4366 1.6655 2.1355 -0.2209 -0.0011 0.0957 165 SER B O 4319 C CB . SER B 166 ? 1.6435 1.8668 2.3622 -0.2337 -0.0404 0.0806 165 SER B CB 4320 O OG . SER B 166 ? 1.8144 2.0586 2.5662 -0.2513 -0.0409 0.0839 165 SER B OG 4321 N N . MET B 167 ? 1.4316 1.7037 2.1806 -0.2285 -0.0114 0.0895 166 MET B N 4322 C CA . MET B 167 ? 1.4377 1.7379 2.2041 -0.2251 0.0030 0.0924 166 MET B CA 4323 C C . MET B 167 ? 1.4198 1.7176 2.1654 -0.2080 0.0095 0.0902 166 MET B C 4324 O O . MET B 167 ? 1.3885 1.6970 2.1344 -0.2051 0.0226 0.0931 166 MET B O 4325 C CB . MET B 167 ? 1.4390 1.7741 2.2423 -0.2260 0.0001 0.0895 166 MET B CB 4326 C CG . MET B 167 ? 1.4459 1.8104 2.2704 -0.2235 0.0160 0.0924 166 MET B CG 4327 S SD . MET B 167 ? 1.4522 1.8571 2.3222 -0.2231 0.0120 0.0899 166 MET B SD 4328 C CE . MET B 167 ? 1.4436 1.8424 2.3001 -0.2053 0.0010 0.0814 166 MET B CE 4329 N N . GLY B 168 ? 1.3997 1.6842 2.1272 -0.1972 0.0004 0.0852 167 GLY B N 4330 C CA . GLY B 168 ? 1.3752 1.6576 2.0842 -0.1828 0.0044 0.0834 167 GLY B CA 4331 C C . GLY B 168 ? 1.3905 1.6583 2.0775 -0.1818 0.0139 0.0892 167 GLY B C 4332 O O . GLY B 168 ? 1.4046 1.6793 2.0833 -0.1731 0.0203 0.0888 167 GLY B O 4333 N N . ASN B 169 ? 1.3798 1.6251 2.0554 -0.1909 0.0139 0.0947 168 ASN B N 4334 C CA . ASN B 169 ? 1.3909 1.6183 2.0431 -0.1903 0.0227 0.1020 168 ASN B CA 4335 C C . ASN B 169 ? 1.4142 1.6598 2.0764 -0.1951 0.0373 0.1069 168 ASN B C 4336 O O . ASN B 169 ? 1.4079 1.6491 2.0499 -0.1877 0.0450 0.1102 168 ASN B O 4337 C CB . ASN B 169 ? 1.3932 1.5882 2.0309 -0.2003 0.0192 0.1072 168 ASN B CB 4338 C CG . ASN B 169 ? 1.3821 1.5530 2.0004 -0.1917 0.0069 0.1023 168 ASN B CG 4339 O OD1 . ASN B 169 ? 1.3672 1.5239 1.9611 -0.1778 0.0066 0.1031 168 ASN B OD1 4340 N ND2 . ASN B 169 ? 1.3709 1.5384 1.9998 -0.1989 -0.0033 0.0974 168 ASN B ND2 4341 N N . MET B 170 ? 1.4462 1.7130 2.1390 -0.2067 0.0409 0.1075 169 MET B N 4342 C CA . MET B 170 ? 1.5042 1.7925 2.2102 -0.2105 0.0568 0.1120 169 MET B CA 4343 C C . MET B 170 ? 1.4117 1.7196 2.1183 -0.1960 0.0611 0.1053 169 MET B C 4344 O O . MET B 170 ? 1.3770 1.6881 2.0707 -0.1914 0.0736 0.1080 169 MET B O 4345 C CB . MET B 170 ? 1.6506 1.9622 2.3952 -0.2252 0.0586 0.1139 169 MET B CB 4346 C CG . MET B 170 ? 1.8471 2.1415 2.5940 -0.2440 0.0573 0.1219 169 MET B CG 4347 S SD . MET B 170 ? 2.1593 2.4594 2.9101 -0.2572 0.0793 0.1357 169 MET B SD 4348 C CE . MET B 170 ? 2.1490 2.4955 2.9563 -0.2701 0.0834 0.1363 169 MET B CE 4349 N N . TYR B 171 ? 1.3616 1.6801 2.0809 -0.1892 0.0506 0.0967 170 TYR B N 4350 C CA . TYR B 171 ? 1.3464 1.6775 2.0641 -0.1761 0.0518 0.0895 170 TYR B CA 4351 C C . TYR B 171 ? 1.3353 1.6499 2.0195 -0.1664 0.0519 0.0892 170 TYR B C 4352 O O . TYR B 171 ? 1.3381 1.6586 2.0121 -0.1598 0.0599 0.0873 170 TYR B O 4353 C CB . TYR B 171 ? 1.3338 1.6724 2.0666 -0.1715 0.0390 0.0820 170 TYR B CB 4354 C CG . TYR B 171 ? 1.3108 1.6752 2.0745 -0.1711 0.0418 0.0786 170 TYR B CG 4355 C CD1 . TYR B 171 ? 1.3008 1.6792 2.0924 -0.1810 0.0408 0.0817 170 TYR B CD1 4356 C CD2 . TYR B 171 ? 1.2969 1.6709 2.0621 -0.1604 0.0445 0.0721 170 TYR B CD2 4357 C CE1 . TYR B 171 ? 1.2667 1.6707 2.0882 -0.1785 0.0429 0.0792 170 TYR B CE1 4358 C CE2 . TYR B 171 ? 1.2785 1.6734 2.0706 -0.1576 0.0472 0.0691 170 TYR B CE2 4359 C CZ . TYR B 171 ? 1.2550 1.6662 2.0758 -0.1657 0.0467 0.0730 170 TYR B CZ 4360 O OH . TYR B 171 ? 1.2315 1.6654 2.0806 -0.1609 0.0489 0.0706 170 TYR B OH 4361 N N . THR B 172 ? 1.2967 1.5906 1.9629 -0.1646 0.0426 0.0909 171 THR B N 4362 C CA . THR B 172 ? 1.2604 1.5418 1.8980 -0.1542 0.0404 0.0910 171 THR B CA 4363 C C . THR B 172 ? 1.2780 1.5471 1.8923 -0.1552 0.0509 0.0991 171 THR B C 4364 O O . THR B 172 ? 1.2759 1.5443 1.8702 -0.1464 0.0525 0.0982 171 THR B O 4365 C CB . THR B 172 ? 1.2290 1.4964 1.8569 -0.1484 0.0278 0.0897 171 THR B CB 4366 O OG1 . THR B 172 ? 1.1266 1.4089 1.7669 -0.1422 0.0207 0.0820 171 THR B OG1 4367 C CG2 . THR B 172 ? 1.2614 1.5117 1.8593 -0.1396 0.0264 0.0941 171 THR B CG2 4368 N N . LEU B 173 ? 1.2755 1.5351 1.8917 -0.1666 0.0578 0.1074 172 LEU B N 4369 C CA . LEU B 173 ? 1.2989 1.5473 1.8936 -0.1689 0.0703 0.1168 172 LEU B CA 4370 C C . LEU B 173 ? 1.2835 1.5524 1.8807 -0.1658 0.0831 0.1146 172 LEU B C 4371 O O . LEU B 173 ? 1.2879 1.5498 1.8572 -0.1585 0.0888 0.1172 172 LEU B O 4372 C CB . LEU B 173 ? 1.3413 1.5783 1.9438 -0.1850 0.0764 0.1264 172 LEU B CB 4373 C CG . LEU B 173 ? 1.4047 1.6329 1.9892 -0.1901 0.0928 0.1382 172 LEU B CG 4374 C CD1 . LEU B 173 ? 1.4369 1.6384 1.9791 -0.1788 0.0908 0.1434 172 LEU B CD1 4375 C CD2 . LEU B 173 ? 1.4332 1.6519 2.0312 -0.2092 0.0982 0.1478 172 LEU B CD2 4376 N N . TYR B 174 ? 1.2502 1.5437 1.8792 -0.1702 0.0874 0.1099 173 TYR B N 4377 C CA . TYR B 174 ? 1.2402 1.5531 1.8729 -0.1646 0.0994 0.1056 173 TYR B CA 4378 C C . TYR B 174 ? 1.2045 1.5136 1.8140 -0.1505 0.0927 0.0969 173 TYR B C 4379 O O . TYR B 174 ? 1.1799 1.4865 1.7656 -0.1442 0.1012 0.0969 173 TYR B O 4380 C CB . TYR B 174 ? 1.2252 1.5645 1.8980 -0.1680 0.1003 0.1000 173 TYR B CB 4381 C CG . TYR B 174 ? 1.2117 1.5699 1.8906 -0.1589 0.1105 0.0929 173 TYR B CG 4382 C CD1 . TYR B 174 ? 1.2225 1.5951 1.9078 -0.1610 0.1299 0.0979 173 TYR B CD1 4383 C CD2 . TYR B 174 ? 1.2038 1.5650 1.8829 -0.1484 0.1013 0.0813 173 TYR B CD2 4384 C CE1 . TYR B 174 ? 1.2386 1.6267 1.9277 -0.1506 0.1401 0.0905 173 TYR B CE1 4385 C CE2 . TYR B 174 ? 1.2231 1.5968 1.9056 -0.1396 0.1101 0.0738 173 TYR B CE2 4386 C CZ . TYR B 174 ? 1.2441 1.6308 1.9307 -0.1396 0.1295 0.0779 173 TYR B CZ 4387 O OH . TYR B 174 ? 1.2613 1.6582 1.9487 -0.1286 0.1391 0.0695 173 TYR B OH 4388 N N . PHE B 175 ? 1.1734 1.4819 1.7896 -0.1463 0.0771 0.0898 174 PHE B N 4389 C CA . PHE B 175 ? 1.1912 1.4977 1.7905 -0.1355 0.0682 0.0817 174 PHE B CA 4390 C C . PHE B 175 ? 1.2027 1.4922 1.7652 -0.1298 0.0672 0.0867 174 PHE B C 4391 O O . PHE B 175 ? 1.1934 1.4832 1.7354 -0.1229 0.0695 0.0826 174 PHE B O 4392 C CB . PHE B 175 ? 1.1967 1.5046 1.8104 -0.1341 0.0527 0.0768 174 PHE B CB 4393 C CG . PHE B 175 ? 1.2273 1.5334 1.8261 -0.1253 0.0420 0.0708 174 PHE B CG 4394 C CD1 . PHE B 175 ? 1.2278 1.5423 1.8258 -0.1209 0.0417 0.0615 174 PHE B CD1 4395 C CD2 . PHE B 175 ? 1.2409 1.5373 1.8278 -0.1215 0.0319 0.0743 174 PHE B CD2 4396 C CE1 . PHE B 175 ? 1.2295 1.5436 1.8165 -0.1153 0.0304 0.0560 174 PHE B CE1 4397 C CE2 . PHE B 175 ? 1.2430 1.5430 1.8212 -0.1143 0.0216 0.0694 174 PHE B CE2 4398 C CZ . PHE B 175 ? 1.2268 1.5361 1.8059 -0.1125 0.0203 0.0604 174 PHE B CZ 4399 N N . LEU B 176 ? 1.2317 1.5049 1.7842 -0.1320 0.0632 0.0953 175 LEU B N 4400 C CA . LEU B 176 ? 1.2997 1.5548 1.8173 -0.1250 0.0605 0.1017 175 LEU B CA 4401 C C . LEU B 176 ? 1.3808 1.6293 1.8735 -0.1251 0.0750 0.1084 175 LEU B C 4402 O O . LEU B 176 ? 1.4182 1.6596 1.8803 -0.1162 0.0726 0.1087 175 LEU B O 4403 C CB . LEU B 176 ? 1.2925 1.5274 1.8048 -0.1271 0.0553 0.1104 175 LEU B CB 4404 C CG . LEU B 176 ? 1.2581 1.4940 1.7826 -0.1225 0.0407 0.1055 175 LEU B CG 4405 C CD1 . LEU B 176 ? 1.2587 1.4721 1.7794 -0.1262 0.0387 0.1130 175 LEU B CD1 4406 C CD2 . LEU B 176 ? 1.2500 1.4891 1.7586 -0.1094 0.0299 0.1022 175 LEU B CD2 4407 N N . GLN B 177 ? 1.4342 1.6860 1.9399 -0.1354 0.0898 0.1142 176 GLN B N 4408 C CA . GLN B 177 ? 1.5102 1.7584 1.9946 -0.1364 0.1071 0.1216 176 GLN B CA 4409 C C . GLN B 177 ? 1.5418 1.8016 2.0126 -0.1267 0.1110 0.1118 176 GLN B C 4410 O O . GLN B 177 ? 1.5834 1.8345 2.0213 -0.1218 0.1205 0.1162 176 GLN B O 4411 C CB . GLN B 177 ? 1.5291 1.7870 2.0396 -0.1502 0.1229 0.1285 176 GLN B CB 4412 C CG . GLN B 177 ? 1.5613 1.7996 2.0728 -0.1618 0.1228 0.1410 176 GLN B CG 4413 C CD . GLN B 177 ? 1.6029 1.8528 2.1407 -0.1777 0.1387 0.1490 176 GLN B CD 4414 O OE1 . GLN B 177 ? 1.6230 1.9004 2.1865 -0.1791 0.1480 0.1440 176 GLN B OE1 4415 N NE2 . GLN B 177 ? 1.6507 1.8795 2.1829 -0.1897 0.1418 0.1617 176 GLN B NE2 4416 N N . ARG B 178 ? 1.5437 1.8201 2.0371 -0.1237 0.1037 0.0986 177 ARG B N 4417 C CA . ARG B 178 ? 1.6077 1.8921 2.0901 -0.1152 0.1063 0.0872 177 ARG B CA 4418 C C . ARG B 178 ? 1.6059 1.8829 2.0643 -0.1058 0.0890 0.0789 177 ARG B C 4419 O O . ARG B 178 ? 1.6592 1.9380 2.1028 -0.0992 0.0890 0.0686 177 ARG B O 4420 C CB . ARG B 178 ? 1.6213 1.9255 2.1409 -0.1171 0.1085 0.0777 177 ARG B CB 4421 C CG . ARG B 178 ? 1.6631 1.9807 2.2102 -0.1258 0.1250 0.0851 177 ARG B CG 4422 C CD . ARG B 178 ? 1.6924 2.0297 2.2795 -0.1268 0.1229 0.0770 177 ARG B CD 4423 N NE . ARG B 178 ? 1.7494 2.0961 2.3347 -0.1176 0.1327 0.0673 177 ARG B NE 4424 C CZ . ARG B 178 ? 1.8126 2.1718 2.4026 -0.1162 0.1533 0.0703 177 ARG B CZ 4425 N NH1 . ARG B 178 ? 1.8563 2.2221 2.4555 -0.1257 0.1665 0.0838 177 ARG B NH1 4426 N NH2 . ARG B 178 ? 1.8377 2.2023 2.4230 -0.1052 0.1613 0.0598 177 ARG B NH2 4427 N N . GLN B 179 ? 1.5455 1.8144 2.0004 -0.1050 0.0742 0.0829 178 GLN B N 4428 C CA . GLN B 179 ? 1.5146 1.7808 1.9506 -0.0967 0.0571 0.0766 178 GLN B CA 4429 C C . GLN B 179 ? 1.5075 1.7574 1.9015 -0.0900 0.0571 0.0853 178 GLN B C 4430 O O . GLN B 179 ? 1.5144 1.7513 1.8990 -0.0924 0.0645 0.0986 178 GLN B O 4431 C CB . GLN B 179 ? 1.4863 1.7569 1.9443 -0.0973 0.0412 0.0763 178 GLN B CB 4432 C CG . GLN B 179 ? 1.4664 1.7508 1.9633 -0.1035 0.0402 0.0695 178 GLN B CG 4433 C CD . GLN B 179 ? 1.4843 1.7783 1.9878 -0.1027 0.0414 0.0568 178 GLN B CD 4434 O OE1 . GLN B 179 ? 1.5093 1.8033 1.9978 -0.0980 0.0319 0.0488 178 GLN B OE1 4435 N NE2 . GLN B 179 ? 1.4849 1.7865 2.0109 -0.1071 0.0525 0.0546 178 GLN B NE2 4436 N N . PRO B 180 ? 1.4993 1.7479 1.8662 -0.0821 0.0477 0.0781 179 PRO B N 4437 C CA . PRO B 180 ? 1.5407 1.7737 1.8651 -0.0743 0.0454 0.0867 179 PRO B CA 4438 C C . PRO B 180 ? 1.5200 1.7462 1.8447 -0.0707 0.0330 0.0968 179 PRO B C 4439 O O . PRO B 180 ? 1.4259 1.6631 1.7791 -0.0715 0.0209 0.0930 179 PRO B O 4440 C CB . PRO B 180 ? 1.5760 1.8122 1.8774 -0.0673 0.0329 0.0739 179 PRO B CB 4441 C CG . PRO B 180 ? 1.5451 1.7980 1.8823 -0.0719 0.0227 0.0602 179 PRO B CG 4442 C CD . PRO B 180 ? 1.5052 1.7645 1.8781 -0.0803 0.0372 0.0619 179 PRO B CD 4443 N N . GLN B 181 ? 1.5732 1.7801 1.8645 -0.0657 0.0372 0.1102 180 GLN B N 4444 C CA . GLN B 181 ? 1.5893 1.7846 1.8763 -0.0602 0.0277 0.1214 180 GLN B CA 4445 C C . GLN B 181 ? 1.5413 1.7504 1.8344 -0.0509 0.0047 0.1147 180 GLN B C 4446 O O . GLN B 181 ? 1.5136 1.7257 1.8272 -0.0486 -0.0033 0.1176 180 GLN B O 4447 C CB . GLN B 181 ? 1.6676 1.8371 1.9104 -0.0544 0.0349 0.1368 180 GLN B CB 4448 C CG . GLN B 181 ? 1.7022 1.8519 1.9405 -0.0500 0.0307 0.1506 180 GLN B CG 4449 C CD . GLN B 181 ? 1.7015 1.8439 1.9686 -0.0627 0.0424 0.1552 180 GLN B CD 4450 O OE1 . GLN B 181 ? 1.7290 1.8678 1.9999 -0.0744 0.0604 0.1586 180 GLN B OE1 4451 N NE2 . GLN B 181 ? 1.6769 1.8175 1.9638 -0.0601 0.0322 0.1554 180 GLN B NE2 4452 N N . ALA B 182 ? 1.4922 1.7105 1.7679 -0.0459 -0.0055 0.1057 181 ALA B N 4453 C CA . ALA B 182 ? 1.4315 1.6671 1.7153 -0.0389 -0.0282 0.0992 181 ALA B CA 4454 C C . ALA B 182 ? 1.3874 1.6442 1.7188 -0.0457 -0.0338 0.0905 181 ALA B C 4455 O O . ALA B 182 ? 1.3717 1.6413 1.7202 -0.0403 -0.0475 0.0918 181 ALA B O 4456 C CB . ALA B 182 ? 1.4211 1.6617 1.6790 -0.0360 -0.0381 0.0888 181 ALA B CB 4457 N N . TRP B 183 ? 1.3763 1.6376 1.7288 -0.0565 -0.0225 0.0824 182 TRP B N 4458 C CA . TRP B 183 ? 1.3608 1.6394 1.7557 -0.0633 -0.0261 0.0750 182 TRP B CA 4459 C C . TRP B 183 ? 1.3633 1.6381 1.7773 -0.0629 -0.0229 0.0845 182 TRP B C 4460 O O . TRP B 183 ? 1.3164 1.6049 1.7536 -0.0609 -0.0328 0.0833 182 TRP B O 4461 C CB . TRP B 183 ? 1.3396 1.6206 1.7497 -0.0731 -0.0141 0.0657 182 TRP B CB 4462 C CG . TRP B 183 ? 1.2817 1.5786 1.7311 -0.0795 -0.0189 0.0581 182 TRP B CG 4463 C CD1 . TRP B 183 ? 1.2670 1.5773 1.7294 -0.0822 -0.0305 0.0468 182 TRP B CD1 4464 C CD2 . TRP B 183 ? 1.2528 1.5520 1.7315 -0.0846 -0.0125 0.0619 182 TRP B CD2 4465 N NE1 . TRP B 183 ? 1.2314 1.5519 1.7289 -0.0882 -0.0305 0.0445 182 TRP B NE1 4466 C CE2 . TRP B 183 ? 1.2274 1.5417 1.7344 -0.0891 -0.0199 0.0533 182 TRP B CE2 4467 C CE3 . TRP B 183 ? 1.2592 1.5476 1.7414 -0.0865 -0.0020 0.0716 182 TRP B CE3 4468 C CZ2 . TRP B 183 ? 1.2075 1.5268 1.7437 -0.0938 -0.0168 0.0546 182 TRP B CZ2 4469 C CZ3 . TRP B 183 ? 1.2318 1.5253 1.7438 -0.0919 -0.0005 0.0714 182 TRP B CZ3 4470 C CH2 . TRP B 183 ? 1.1965 1.5056 1.7340 -0.0947 -0.0076 0.0631 182 TRP B CH2 4471 N N . LYS B 184 ? 1.3994 1.6552 1.8029 -0.0653 -0.0086 0.0939 183 LYS B N 4472 C CA . LYS B 184 ? 1.3940 1.6403 1.8111 -0.0661 -0.0054 0.1020 183 LYS B CA 4473 C C . LYS B 184 ? 1.3981 1.6404 1.8048 -0.0531 -0.0175 0.1091 183 LYS B C 4474 O O . LYS B 184 ? 1.3497 1.5963 1.7762 -0.0503 -0.0220 0.1097 183 LYS B O 4475 C CB . LYS B 184 ? 1.4399 1.6640 1.8440 -0.0725 0.0109 0.1115 183 LYS B CB 4476 C CG . LYS B 184 ? 1.4360 1.6674 1.8590 -0.0851 0.0243 0.1061 183 LYS B CG 4477 C CD . LYS B 184 ? 1.4626 1.6758 1.8779 -0.0931 0.0402 0.1169 183 LYS B CD 4478 C CE . LYS B 184 ? 1.5101 1.7098 1.8878 -0.0896 0.0490 0.1247 183 LYS B CE 4479 N NZ . LYS B 184 ? 1.5337 1.7195 1.9082 -0.1002 0.0671 0.1355 183 LYS B NZ 4480 N N . ASP B 185 ? 1.4410 1.6749 1.8149 -0.0437 -0.0223 0.1148 184 ASP B N 4481 C CA . ASP B 185 ? 1.4705 1.7009 1.8318 -0.0286 -0.0344 0.1227 184 ASP B CA 4482 C C . ASP B 185 ? 1.4475 1.7081 1.8365 -0.0234 -0.0499 0.1152 184 ASP B C 4483 O O . ASP B 185 ? 1.4756 1.7387 1.8728 -0.0129 -0.0561 0.1203 184 ASP B O 4484 C CB . ASP B 185 ? 1.5111 1.7296 1.8307 -0.0194 -0.0386 0.1294 184 ASP B CB 4485 C CG . ASP B 185 ? 1.5191 1.7046 1.8080 -0.0225 -0.0224 0.1412 184 ASP B CG 4486 O OD1 . ASP B 185 ? 1.4865 1.6618 1.7893 -0.0344 -0.0080 0.1424 184 ASP B OD1 4487 O OD2 . ASP B 185 ? 1.5237 1.6942 1.7746 -0.0135 -0.0246 0.1497 184 ASP B OD2 4488 N N . LYS B 186 ? 1.4182 1.7009 1.8216 -0.0308 -0.0553 0.1033 185 LYS B N 4489 C CA . LYS B 186 ? 1.4039 1.7171 1.8361 -0.0291 -0.0695 0.0965 185 LYS B CA 4490 C C . LYS B 186 ? 1.3151 1.6381 1.7837 -0.0355 -0.0643 0.0934 185 LYS B C 4491 O O . LYS B 186 ? 1.2747 1.6129 1.7623 -0.0282 -0.0707 0.0958 185 LYS B O 4492 C CB . LYS B 186 ? 1.4554 1.7844 1.8877 -0.0362 -0.0783 0.0847 185 LYS B CB 4493 C CG . LYS B 186 ? 1.4764 1.8367 1.9437 -0.0398 -0.0912 0.0771 185 LYS B CG 4494 C CD . LYS B 186 ? 1.5261 1.8989 1.9871 -0.0450 -0.1048 0.0664 185 LYS B CD 4495 C CE . LYS B 186 ? 1.5262 1.9304 2.0247 -0.0507 -0.1177 0.0603 185 LYS B CE 4496 N NZ . LYS B 186 ? 1.5625 1.9791 2.0541 -0.0554 -0.1354 0.0506 185 LYS B NZ 4497 N N . TYR B 187 ? 1.2561 1.5716 1.7338 -0.0480 -0.0524 0.0883 186 TYR B N 4498 C CA . TYR B 187 ? 1.2019 1.5293 1.7131 -0.0555 -0.0494 0.0833 186 TYR B CA 4499 C C . TYR B 187 ? 1.2267 1.5387 1.7437 -0.0553 -0.0400 0.0892 186 TYR B C 4500 O O . TYR B 187 ? 1.1817 1.5038 1.7229 -0.0577 -0.0397 0.0867 186 TYR B O 4501 C CB . TYR B 187 ? 1.1645 1.4954 1.6853 -0.0683 -0.0445 0.0732 186 TYR B CB 4502 C CG . TYR B 187 ? 1.1669 1.5151 1.6909 -0.0708 -0.0562 0.0643 186 TYR B CG 4503 C CD1 . TYR B 187 ? 1.1451 1.5151 1.6979 -0.0747 -0.0646 0.0595 186 TYR B CD1 4504 C CD2 . TYR B 187 ? 1.2030 1.5443 1.6995 -0.0700 -0.0589 0.0605 186 TYR B CD2 4505 C CE1 . TYR B 187 ? 1.1600 1.5441 1.7166 -0.0793 -0.0766 0.0510 186 TYR B CE1 4506 C CE2 . TYR B 187 ? 1.2162 1.5702 1.7131 -0.0732 -0.0715 0.0508 186 TYR B CE2 4507 C CZ . TYR B 187 ? 1.2046 1.5797 1.7328 -0.0787 -0.0809 0.0460 186 TYR B CZ 4508 O OH . TYR B 187 ? 1.2387 1.6248 1.7683 -0.0842 -0.0945 0.0361 186 TYR B OH 4509 N N . ILE B 188 ? 1.2941 1.5803 1.7878 -0.0532 -0.0324 0.0969 187 ILE B N 4510 C CA . ILE B 188 ? 1.3183 1.5854 1.8146 -0.0548 -0.0247 0.1017 187 ILE B CA 4511 C C . ILE B 188 ? 1.3460 1.5976 1.8252 -0.0403 -0.0285 0.1107 187 ILE B C 4512 O O . ILE B 188 ? 1.3344 1.5708 1.7865 -0.0335 -0.0292 0.1180 187 ILE B O 4513 C CB . ILE B 188 ? 1.3535 1.6005 1.8397 -0.0659 -0.0123 0.1042 187 ILE B CB 4514 C CG1 . ILE B 188 ? 1.3424 1.6049 1.8446 -0.0774 -0.0077 0.0954 187 ILE B CG1 4515 C CG2 . ILE B 188 ? 1.3733 1.6009 1.8642 -0.0699 -0.0070 0.1079 187 ILE B CG2 4516 C CD1 . ILE B 188 ? 1.3115 1.5902 1.8449 -0.0828 -0.0098 0.0879 187 ILE B CD1 4517 N N . ARG B 189 ? 1.3625 1.6163 1.8555 -0.0346 -0.0303 0.1105 188 ARG B N 4518 C CA . ARG B 189 ? 1.3958 1.6322 1.8736 -0.0189 -0.0325 0.1181 188 ARG B CA 4519 C C . ARG B 189 ? 1.4069 1.6045 1.8661 -0.0238 -0.0241 0.1232 188 ARG B C 4520 O O . ARG B 189 ? 1.4517 1.6230 1.8841 -0.0158 -0.0236 0.1319 188 ARG B O 4521 C CB . ARG B 189 ? 1.3981 1.6526 1.8973 -0.0101 -0.0360 0.1151 188 ARG B CB 4522 C CG . ARG B 189 ? 1.4327 1.6626 1.9188 0.0035 -0.0341 0.1201 188 ARG B CG 4523 C CD . ARG B 189 ? 1.5064 1.7244 1.9694 0.0221 -0.0390 0.1290 188 ARG B CD 4524 N NE . ARG B 189 ? 1.6212 1.8127 2.0709 0.0367 -0.0366 0.1327 188 ARG B NE 4525 C CZ . ARG B 189 ? 1.7680 1.9394 2.1945 0.0556 -0.0396 0.1411 188 ARG B CZ 4526 N NH1 . ARG B 189 ? 1.8343 2.0104 2.2476 0.0621 -0.0459 0.1476 188 ARG B NH1 4527 N NH2 . ARG B 189 ? 1.7935 1.9376 2.2073 0.0690 -0.0366 0.1428 188 ARG B NH2 4528 N N . ALA B 190 ? 1.3883 1.5816 1.8617 -0.0374 -0.0183 0.1182 189 ALA B N 4529 C CA . ALA B 190 ? 1.4157 1.5746 1.8762 -0.0456 -0.0117 0.1219 189 ALA B CA 4530 C C . ALA B 190 ? 1.4030 1.5688 1.8846 -0.0638 -0.0068 0.1155 189 ALA B C 4531 O O . ALA B 190 ? 1.3622 1.5556 1.8672 -0.0672 -0.0087 0.1081 189 ALA B O 4532 C CB . ALA B 190 ? 1.4340 1.5695 1.8835 -0.0334 -0.0140 0.1239 189 ALA B CB 4533 N N . PHE B 191 ? 1.4412 1.5816 1.9148 -0.0757 -0.0009 0.1191 190 PHE B N 4534 C CA . PHE B 191 ? 1.4373 1.5831 1.9312 -0.0931 0.0030 0.1145 190 PHE B CA 4535 C C . PHE B 191 ? 1.4349 1.5491 1.9207 -0.0975 0.0017 0.1156 190 PHE B C 4536 O O . PHE B 191 ? 1.4741 1.5570 1.9392 -0.1001 0.0046 0.1230 190 PHE B O 4537 C CB . PHE B 191 ? 1.4694 1.6191 1.9638 -0.1054 0.0119 0.1184 190 PHE B CB 4538 C CG . PHE B 191 ? 1.4996 1.6544 2.0158 -0.1233 0.0169 0.1159 190 PHE B CG 4539 C CD1 . PHE B 191 ? 1.4991 1.6659 2.0379 -0.1274 0.0118 0.1080 190 PHE B CD1 4540 C CD2 . PHE B 191 ? 1.5332 1.6833 2.0478 -0.1355 0.0271 0.1222 190 PHE B CD2 4541 C CE1 . PHE B 191 ? 1.5071 1.6811 2.0671 -0.1429 0.0147 0.1063 190 PHE B CE1 4542 C CE2 . PHE B 191 ? 1.5317 1.6916 2.0706 -0.1516 0.0316 0.1206 190 PHE B CE2 4543 C CZ . PHE B 191 ? 1.5179 1.6902 2.0801 -0.1550 0.0244 0.1125 190 PHE B CZ 4544 N N . VAL B 192 ? 1.3903 1.5106 1.8899 -0.0977 -0.0030 0.1082 191 VAL B N 4545 C CA . VAL B 192 ? 1.4207 1.5117 1.9120 -0.1020 -0.0062 0.1065 191 VAL B CA 4546 C C . VAL B 192 ? 1.4269 1.5250 1.9391 -0.1224 -0.0052 0.1035 191 VAL B C 4547 O O . VAL B 192 ? 1.4139 1.5402 1.9495 -0.1257 -0.0069 0.0975 191 VAL B O 4548 C CB . VAL B 192 ? 1.4273 1.5214 1.9183 -0.0887 -0.0119 0.1001 191 VAL B CB 4549 C CG1 . VAL B 192 ? 1.4508 1.5103 1.9275 -0.0921 -0.0160 0.0969 191 VAL B CG1 4550 C CG2 . VAL B 192 ? 1.4395 1.5365 1.9172 -0.0675 -0.0126 0.1033 191 VAL B CG2 4551 N N . SER B 193 ? 1.4690 1.5417 1.9736 -0.1359 -0.0029 0.1084 192 SER B N 4552 C CA . SER B 193 ? 1.4937 1.5754 2.0210 -0.1565 -0.0017 0.1074 192 SER B CA 4553 C C . SER B 193 ? 1.5228 1.5795 2.0464 -0.1647 -0.0106 0.1026 192 SER B C 4554 O O . SER B 193 ? 1.5520 1.5694 2.0513 -0.1656 -0.0127 0.1055 192 SER B O 4555 C CB . SER B 193 ? 1.5316 1.6055 2.0559 -0.1688 0.0079 0.1172 192 SER B CB 4556 O OG . SER B 193 ? 1.5507 1.6381 2.1013 -0.1888 0.0101 0.1173 192 SER B OG 4557 N N . LEU B 194 ? 1.5102 1.5874 2.0556 -0.1702 -0.0167 0.0952 193 LEU B N 4558 C CA . LEU B 194 ? 1.5576 1.6134 2.0980 -0.1770 -0.0274 0.0890 193 LEU B CA 4559 C C . LEU B 194 ? 1.5693 1.6375 2.1367 -0.1996 -0.0304 0.0889 193 LEU B C 4560 O O . LEU B 194 ? 1.5818 1.6858 2.1775 -0.2027 -0.0309 0.0862 193 LEU B O 4561 C CB . LEU B 194 ? 1.5607 1.6288 2.1008 -0.1632 -0.0338 0.0808 193 LEU B CB 4562 C CG . LEU B 194 ? 1.5754 1.6434 2.0979 -0.1407 -0.0301 0.0812 193 LEU B CG 4563 C CD1 . LEU B 194 ? 1.5703 1.6540 2.0964 -0.1300 -0.0346 0.0744 193 LEU B CD1 4564 C CD2 . LEU B 194 ? 1.6201 1.6456 2.1086 -0.1318 -0.0303 0.0836 193 LEU B CD2 4565 N N . GLY B 195 ? 1.5856 1.6244 2.1455 -0.2153 -0.0327 0.0921 194 GLY B N 4566 C CA . GLY B 195 ? 1.5772 1.6279 2.1650 -0.2386 -0.0372 0.0923 194 GLY B CA 4567 C C . GLY B 195 ? 1.5353 1.6275 2.1571 -0.2469 -0.0257 0.0987 194 GLY B C 4568 O O . GLY B 195 ? 1.4806 1.6051 2.1350 -0.2555 -0.0293 0.0961 194 GLY B O 4569 N N . ALA B 196 ? 1.5334 1.6241 2.1461 -0.2430 -0.0120 0.1073 195 ALA B N 4570 C CA . ALA B 196 ? 1.5138 1.6415 2.1523 -0.2473 0.0012 0.1131 195 ALA B CA 4571 C C . ALA B 196 ? 1.5412 1.6753 2.2040 -0.2716 0.0057 0.1202 195 ALA B C 4572 O O . ALA B 196 ? 1.5678 1.6695 2.2145 -0.2832 0.0079 0.1273 195 ALA B O 4573 C CB . ALA B 196 ? 1.5256 1.6472 2.1412 -0.2342 0.0134 0.1195 195 ALA B CB 4574 N N . PRO B 197 ? 1.5342 1.7105 2.2366 -0.2793 0.0077 0.1190 196 PRO B N 4575 C CA . PRO B 197 ? 1.5676 1.7596 2.3012 -0.3025 0.0124 0.1260 196 PRO B CA 4576 C C . PRO B 197 ? 1.5798 1.7862 2.3181 -0.3053 0.0340 0.1375 196 PRO B C 4577 O O . PRO B 197 ? 1.5625 1.8100 2.3348 -0.3092 0.0437 0.1398 196 PRO B O 4578 C CB . PRO B 197 ? 1.5245 1.7585 2.2976 -0.3037 0.0045 0.1192 196 PRO B CB 4579 C CG . PRO B 197 ? 1.4902 1.7403 2.2560 -0.2803 0.0078 0.1134 196 PRO B CG 4580 C CD . PRO B 197 ? 1.5031 1.7149 2.2247 -0.2662 0.0050 0.1112 196 PRO B CD 4581 N N . TRP B 198 ? 1.6106 1.7824 2.3131 -0.3022 0.0419 0.1449 197 TRP B N 4582 C CA . TRP B 198 ? 1.6388 1.8187 2.3370 -0.3032 0.0626 0.1565 197 TRP B CA 4583 C C . TRP B 198 ? 1.6850 1.8819 2.4166 -0.3287 0.0716 0.1662 197 TRP B C 4584 O O . TRP B 198 ? 1.7163 1.8868 2.4474 -0.3480 0.0650 0.1705 197 TRP B O 4585 C CB . TRP B 198 ? 1.6791 1.8137 2.3302 -0.2961 0.0669 0.1639 197 TRP B CB 4586 C CG . TRP B 198 ? 1.6542 1.7691 2.2731 -0.2727 0.0566 0.1557 197 TRP B CG 4587 C CD1 . TRP B 198 ? 1.6795 1.7516 2.2682 -0.2675 0.0450 0.1538 197 TRP B CD1 4588 C CD2 . TRP B 198 ? 1.6121 1.7501 2.2273 -0.2515 0.0574 0.1487 197 TRP B CD2 4589 N NE1 . TRP B 198 ? 1.6441 1.7154 2.2133 -0.2440 0.0395 0.1468 197 TRP B NE1 4590 C CE2 . TRP B 198 ? 1.6167 1.7280 2.2023 -0.2351 0.0463 0.1437 197 TRP B CE2 4591 C CE3 . TRP B 198 ? 1.6031 1.7807 2.2371 -0.2448 0.0664 0.1460 197 TRP B CE3 4592 C CZ2 . TRP B 198 ? 1.6123 1.7384 2.1899 -0.2147 0.0434 0.1368 197 TRP B CZ2 4593 C CZ3 . TRP B 198 ? 1.5998 1.7869 2.2222 -0.2246 0.0627 0.1381 197 TRP B CZ3 4594 C CH2 . TRP B 198 ? 1.5973 1.7602 2.1933 -0.2108 0.0511 0.1340 197 TRP B CH2 4595 N N . GLY B 199 ? 1.6892 1.9303 2.4507 -0.3289 0.0865 0.1693 198 GLY B N 4596 C CA . GLY B 199 ? 1.7204 1.9875 2.5202 -0.3519 0.0974 0.1792 198 GLY B CA 4597 C C . GLY B 199 ? 1.7100 2.0031 2.5544 -0.3662 0.0819 0.1729 198 GLY B C 4598 O O . GLY B 199 ? 1.7344 2.0376 2.6082 -0.3906 0.0838 0.1809 198 GLY B O 4599 N N . GLY B 200 ? 1.6733 1.9776 2.5229 -0.3518 0.0660 0.1594 199 GLY B N 4600 C CA . GLY B 200 ? 1.6358 1.9717 2.5283 -0.3609 0.0514 0.1531 199 GLY B CA 4601 C C . GLY B 200 ? 1.6277 1.9350 2.5183 -0.3794 0.0300 0.1500 199 GLY B C 4602 O O . GLY B 200 ? 1.5928 1.8523 2.4484 -0.3857 0.0272 0.1527 199 GLY B O 4603 N N . VAL B 201 ? 1.6200 1.9552 2.5469 -0.3872 0.0142 0.1439 200 VAL B N 4604 C CA . VAL B 201 ? 1.6622 1.9719 2.5868 -0.4038 -0.0094 0.1383 200 VAL B CA 4605 C C . VAL B 201 ? 1.6710 2.0220 2.6510 -0.4261 -0.0181 0.1405 200 VAL B C 4606 O O . VAL B 201 ? 1.6419 2.0458 2.6631 -0.4207 -0.0120 0.1418 200 VAL B O 4607 C CB . VAL B 201 ? 1.6693 1.9590 2.5664 -0.3853 -0.0291 0.1241 200 VAL B CB 4608 C CG1 . VAL B 201 ? 1.6887 1.9334 2.5317 -0.3670 -0.0236 0.1222 200 VAL B CG1 4609 C CG2 . VAL B 201 ? 1.6294 1.9645 2.5529 -0.3680 -0.0310 0.1183 200 VAL B CG2 4610 N N . ALA B 202 ? 1.7155 2.0411 2.6963 -0.4510 -0.0335 0.1406 201 ALA B N 4611 C CA . ALA B 202 ? 1.7066 2.0694 2.7410 -0.4767 -0.0434 0.1438 201 ALA B CA 4612 C C . ALA B 202 ? 1.6623 2.0639 2.7261 -0.4675 -0.0626 0.1337 201 ALA B C 4613 O O . ALA B 202 ? 1.6399 2.0955 2.7589 -0.4775 -0.0628 0.1382 201 ALA B O 4614 C CB . ALA B 202 ? 1.7521 2.0713 2.7744 -0.5054 -0.0593 0.1439 201 ALA B CB 4615 N N . LYS B 203 ? 1.6465 2.0220 2.6742 -0.4478 -0.0782 0.1212 202 LYS B N 4616 C CA . LYS B 203 ? 1.6310 2.0351 2.6793 -0.4396 -0.0992 0.1119 202 LYS B CA 4617 C C . LYS B 203 ? 1.5591 2.0258 2.6522 -0.4250 -0.0877 0.1156 202 LYS B C 4618 O O . LYS B 203 ? 1.5206 2.0235 2.6482 -0.4251 -0.1037 0.1123 202 LYS B O 4619 C CB . LYS B 203 ? 1.6545 2.0179 2.6513 -0.4186 -0.1133 0.0994 202 LYS B CB 4620 C CG . LYS B 203 ? 1.6691 2.0272 2.6377 -0.3891 -0.0956 0.0987 202 LYS B CG 4621 C CD . LYS B 203 ? 1.6880 2.0454 2.6397 -0.3672 -0.1095 0.0885 202 LYS B CD 4622 C CE . LYS B 203 ? 1.6767 2.0416 2.6144 -0.3408 -0.0917 0.0889 202 LYS B CE 4623 N NZ . LYS B 203 ? 1.6729 2.0418 2.5999 -0.3210 -0.1034 0.0811 202 LYS B NZ 4624 N N . THR B 204 ? 1.5242 2.0010 2.6139 -0.4117 -0.0606 0.1223 203 THR B N 4625 C CA . THR B 204 ? 1.4721 2.0028 2.5994 -0.3966 -0.0454 0.1260 203 THR B CA 4626 C C . THR B 204 ? 1.4582 2.0455 2.6512 -0.4137 -0.0483 0.1324 203 THR B C 4627 O O . THR B 204 ? 1.4259 2.0571 2.6533 -0.4009 -0.0518 0.1307 203 THR B O 4628 C CB . THR B 204 ? 1.4560 1.9847 2.5695 -0.3881 -0.0143 0.1340 203 THR B CB 4629 O OG1 . THR B 204 ? 1.4539 1.9288 2.5085 -0.3774 -0.0124 0.1301 203 THR B OG1 4630 C CG2 . THR B 204 ? 1.4210 1.9918 2.5567 -0.3654 0.0006 0.1340 203 THR B CG2 4631 N N . LEU B 205 ? 1.4634 2.0497 2.6745 -0.4426 -0.0467 0.1405 204 LEU B N 4632 C CA . LEU B 205 ? 1.4554 2.0988 2.7332 -0.4619 -0.0472 0.1485 204 LEU B CA 4633 C C . LEU B 205 ? 1.4533 2.1188 2.7584 -0.4654 -0.0792 0.1404 204 LEU B C 4634 O O . LEU B 205 ? 1.4105 2.1347 2.7688 -0.4612 -0.0805 0.1433 204 LEU B O 4635 C CB . LEU B 205 ? 1.4928 2.1241 2.7811 -0.4957 -0.0410 0.1591 204 LEU B CB 4636 C CG . LEU B 205 ? 1.5166 2.1456 2.7976 -0.4973 -0.0060 0.1723 204 LEU B CG 4637 C CD1 . LEU B 205 ? 1.4935 2.1885 2.8226 -0.4849 0.0176 0.1800 204 LEU B CD1 4638 C CD2 . LEU B 205 ? 1.5222 2.0943 2.7343 -0.4773 0.0045 0.1685 204 LEU B CD2 4639 N N . ARG B 206 ? 1.5010 2.1191 2.7679 -0.4715 -0.1050 0.1304 205 ARG B N 4640 C CA . ARG B 206 ? 1.5502 2.1821 2.8339 -0.4749 -0.1378 0.1219 205 ARG B CA 4641 C C . ARG B 206 ? 1.5275 2.1837 2.8130 -0.4429 -0.1410 0.1164 205 ARG B C 4642 O O . ARG B 206 ? 1.5101 2.2126 2.8391 -0.4411 -0.1559 0.1162 205 ARG B O 4643 C CB . ARG B 206 ? 1.6058 2.1738 2.8369 -0.4843 -0.1622 0.1111 205 ARG B CB 4644 C CG . ARG B 206 ? 1.6322 2.2109 2.8785 -0.4936 -0.1982 0.1025 205 ARG B CG 4645 C CD . ARG B 206 ? 1.6566 2.1814 2.8406 -0.4785 -0.2181 0.0887 205 ARG B CD 4646 N NE . ARG B 206 ? 1.6897 2.2373 2.8895 -0.4757 -0.2483 0.0816 205 ARG B NE 4647 C CZ . ARG B 206 ? 1.7269 2.2423 2.8811 -0.4588 -0.2665 0.0706 205 ARG B CZ 4648 N NH1 . ARG B 206 ? 1.7532 2.2141 2.8458 -0.4431 -0.2573 0.0651 205 ARG B NH1 4649 N NH2 . ARG B 206 ? 1.7268 2.2662 2.8976 -0.4570 -0.2941 0.0657 205 ARG B NH2 4650 N N . VAL B 207 ? 1.5301 2.1544 2.7686 -0.4180 -0.1277 0.1125 206 VAL B N 4651 C CA . VAL B 207 ? 1.5134 2.1527 2.7474 -0.3877 -0.1285 0.1077 206 VAL B CA 4652 C C . VAL B 207 ? 1.4716 2.1764 2.7647 -0.3793 -0.1152 0.1152 206 VAL B C 4653 O O . VAL B 207 ? 1.4382 2.1755 2.7584 -0.3683 -0.1302 0.1131 206 VAL B O 4654 C CB . VAL B 207 ? 1.5357 2.1347 2.7160 -0.3657 -0.1110 0.1045 206 VAL B CB 4655 C CG1 . VAL B 207 ? 1.5314 2.1492 2.7129 -0.3362 -0.1077 0.1014 206 VAL B CG1 4656 C CG2 . VAL B 207 ? 1.5618 2.0994 2.6844 -0.3686 -0.1252 0.0964 206 VAL B CG2 4657 N N . LEU B 208 ? 1.4513 2.1743 2.7627 -0.3834 -0.0869 0.1243 207 LEU B N 4658 C CA . LEU B 208 ? 1.4237 2.2070 2.7877 -0.3731 -0.0691 0.1315 207 LEU B CA 4659 C C . LEU B 208 ? 1.4086 2.2472 2.8387 -0.3907 -0.0840 0.1368 207 LEU B C 4660 O O . LEU B 208 ? 1.3860 2.2737 2.8580 -0.3756 -0.0851 0.1383 207 LEU B O 4661 C CB . LEU B 208 ? 1.4307 2.2165 2.7933 -0.3752 -0.0346 0.1403 207 LEU B CB 4662 C CG . LEU B 208 ? 1.4344 2.1763 2.7388 -0.3544 -0.0178 0.1359 207 LEU B CG 4663 C CD1 . LEU B 208 ? 1.4500 2.1783 2.7403 -0.3650 0.0090 0.1446 207 LEU B CD1 4664 C CD2 . LEU B 208 ? 1.4139 2.1771 2.7227 -0.3231 -0.0083 0.1321 207 LEU B CD2 4665 N N . ALA B 209 ? 1.4126 2.2428 2.8525 -0.4227 -0.0960 0.1395 208 ALA B N 4666 C CA . ALA B 209 ? 1.3996 2.2834 2.9051 -0.4442 -0.1109 0.1451 208 ALA B CA 4667 C C . ALA B 209 ? 1.3913 2.2870 2.9067 -0.4374 -0.1465 0.1366 208 ALA B C 4668 O O . ALA B 209 ? 1.3766 2.3299 2.9435 -0.4270 -0.1513 0.1398 208 ALA B O 4669 C CB . ALA B 209 ? 1.4247 2.2893 2.9336 -0.4823 -0.1154 0.1498 208 ALA B CB 4670 N N . SER B 210 ? 1.3994 2.2399 2.8631 -0.4415 -0.1707 0.1262 209 SER B N 4671 C CA . SER B 210 ? 1.4056 2.2512 2.8732 -0.4409 -0.2078 0.1183 209 SER B CA 4672 C C . SER B 210 ? 1.4304 2.2297 2.8368 -0.4153 -0.2200 0.1074 209 SER B C 4673 O O . SER B 210 ? 1.4570 2.2526 2.8565 -0.4143 -0.2508 0.1007 209 SER B O 4674 C CB . SER B 210 ? 1.4190 2.2466 2.8889 -0.4768 -0.2333 0.1154 209 SER B CB 4675 O OG . SER B 210 ? 1.4204 2.1729 2.8199 -0.4813 -0.2380 0.1068 209 SER B OG 4676 N N . GLY B 211 ? 1.4394 2.2047 2.8018 -0.3952 -0.1966 0.1061 210 GLY B N 4677 C CA . GLY B 211 ? 1.4681 2.1897 2.7732 -0.3721 -0.2049 0.0971 210 GLY B CA 4678 C C . GLY B 211 ? 1.5416 2.1996 2.7890 -0.3846 -0.2188 0.0887 210 GLY B C 4679 O O . GLY B 211 ? 1.5757 2.2237 2.8293 -0.4120 -0.2314 0.0880 210 GLY B O 4680 N N . ASP B 212 ? 1.5811 2.1962 2.7730 -0.3642 -0.2165 0.0824 211 ASP B N 4681 C CA . ASP B 212 ? 1.6416 2.1943 2.7741 -0.3704 -0.2253 0.0743 211 ASP B CA 4682 C C . ASP B 212 ? 1.6417 2.1691 2.7313 -0.3473 -0.2377 0.0669 211 ASP B C 4683 O O . ASP B 212 ? 1.6136 2.1339 2.6834 -0.3248 -0.2209 0.0677 211 ASP B O 4684 C CB . ASP B 212 ? 1.6496 2.1718 2.7553 -0.3704 -0.1976 0.0773 211 ASP B CB 4685 C CG . ASP B 212 ? 1.7059 2.1662 2.7580 -0.3805 -0.2051 0.0705 211 ASP B CG 4686 O OD1 . ASP B 212 ? 1.7451 2.1721 2.7544 -0.3690 -0.2197 0.0618 211 ASP B OD1 4687 O OD2 . ASP B 212 ? 1.7219 2.1658 2.7734 -0.3990 -0.1952 0.0743 211 ASP B OD2 4688 N N . ASN B 213 ? 1.6829 2.1969 2.7577 -0.3536 -0.2672 0.0598 212 ASN B N 4689 C CA . ASN B 213 ? 1.7087 2.2014 2.7437 -0.3324 -0.2801 0.0540 212 ASN B CA 4690 C C . ASN B 213 ? 1.8012 2.2324 2.7722 -0.3347 -0.2901 0.0443 212 ASN B C 4691 O O . ASN B 213 ? 1.8227 2.2345 2.7596 -0.3229 -0.3069 0.0385 212 ASN B O 4692 C CB . ASN B 213 ? 1.7091 2.2384 2.7743 -0.3306 -0.3064 0.0543 212 ASN B CB 4693 C CG . ASN B 213 ? 1.7686 2.2947 2.8411 -0.3564 -0.3359 0.0487 212 ASN B CG 4694 O OD1 . ASN B 213 ? 1.8121 2.3210 2.8850 -0.3796 -0.3340 0.0470 212 ASN B OD1 4695 N ND2 . ASN B 213 ? 1.7922 2.3333 2.8694 -0.3527 -0.3645 0.0459 212 ASN B ND2 4696 N N . ASN B 214 ? 1.9009 2.2998 2.8532 -0.3477 -0.2781 0.0430 213 ASN B N 4697 C CA . ASN B 214 ? 2.0051 2.3427 2.8968 -0.3497 -0.2856 0.0335 213 ASN B CA 4698 C C . ASN B 214 ? 2.0688 2.3792 2.9108 -0.3233 -0.2838 0.0291 213 ASN B C 4699 O O . ASN B 214 ? 2.1300 2.4009 2.9257 -0.3212 -0.2995 0.0201 213 ASN B O 4700 C CB . ASN B 214 ? 2.0109 2.3196 2.8888 -0.3585 -0.2646 0.0357 213 ASN B CB 4701 C CG . ASN B 214 ? 2.0306 2.3447 2.9392 -0.3894 -0.2706 0.0380 213 ASN B CG 4702 O OD1 . ASN B 214 ? 2.0447 2.3825 2.9843 -0.4063 -0.2926 0.0366 213 ASN B OD1 4703 N ND2 . ASN B 214 ? 2.0479 2.3400 2.9484 -0.3976 -0.2513 0.0423 213 ASN B ND2 4704 N N . ARG B 215 ? 2.0945 2.4253 2.9454 -0.3035 -0.2637 0.0355 214 ARG B N 4705 C CA . ARG B 215 ? 2.1530 2.4618 2.9618 -0.2796 -0.2581 0.0334 214 ARG B CA 4706 C C . ARG B 215 ? 2.1562 2.4864 2.9713 -0.2680 -0.2751 0.0340 214 ARG B C 4707 O O . ARG B 215 ? 2.2035 2.5096 2.9772 -0.2532 -0.2805 0.0307 214 ARG B O 4708 C CB . ARG B 215 ? 2.1529 2.4703 2.9668 -0.2654 -0.2291 0.0399 214 ARG B CB 4709 C CG . ARG B 215 ? 2.1843 2.4979 3.0101 -0.2777 -0.2114 0.0430 214 ARG B CG 4710 C CD . ARG B 215 ? 2.2516 2.5336 3.0400 -0.2654 -0.1921 0.0427 214 ARG B CD 4711 N NE . ARG B 215 ? 2.3523 2.6248 3.1462 -0.2783 -0.1789 0.0457 214 ARG B NE 4712 C CZ . ARG B 215 ? 2.4417 2.6953 3.2143 -0.2698 -0.1602 0.0477 214 ARG B CZ 4713 N NH1 . ARG B 215 ? 2.4741 2.7187 3.2214 -0.2495 -0.1520 0.0467 214 ARG B NH1 4714 N NH2 . ARG B 215 ? 2.4630 2.7072 3.2401 -0.2823 -0.1497 0.0515 214 ARG B NH2 4715 N N . ILE B 216 ? 2.1083 2.4842 2.9749 -0.2744 -0.2832 0.0389 215 ILE B N 4716 C CA . ILE B 216 ? 2.0477 2.4498 2.9274 -0.2605 -0.2962 0.0420 215 ILE B CA 4717 C C . ILE B 216 ? 2.0147 2.4376 2.9200 -0.2767 -0.3260 0.0395 215 ILE B C 4718 O O . ILE B 216 ? 1.9587 2.4294 2.9168 -0.2788 -0.3306 0.0456 215 ILE B O 4719 C CB . ILE B 216 ? 2.0028 2.4453 2.9243 -0.2478 -0.2770 0.0512 215 ILE B CB 4720 C CG1 . ILE B 216 ? 1.9564 2.3870 2.8709 -0.2444 -0.2468 0.0533 215 ILE B CG1 4721 C CG2 . ILE B 216 ? 2.0118 2.4583 2.9212 -0.2251 -0.2818 0.0544 215 ILE B CG2 4722 C CD1 . ILE B 216 ? 1.9152 2.3819 2.8684 -0.2337 -0.2275 0.0607 215 ILE B CD1 4723 N N . PRO B 217 ? 2.0180 2.4049 2.8855 -0.2877 -0.3468 0.0302 216 PRO B N 4724 C CA . PRO B 217 ? 2.0402 2.4423 2.9293 -0.3074 -0.3776 0.0261 216 PRO B CA 4725 C C . PRO B 217 ? 2.0562 2.4917 2.9641 -0.2968 -0.4002 0.0292 216 PRO B C 4726 O O . PRO B 217 ? 2.0864 2.5527 3.0316 -0.3122 -0.4237 0.0289 216 PRO B O 4727 C CB . PRO B 217 ? 2.0882 2.4325 2.9168 -0.3153 -0.3925 0.0139 216 PRO B CB 4728 C CG . PRO B 217 ? 2.0970 2.4072 2.8713 -0.2900 -0.3779 0.0131 216 PRO B CG 4729 C CD . PRO B 217 ? 2.0507 2.3814 2.8501 -0.2789 -0.3452 0.0225 216 PRO B CD 4730 N N . VAL B 218 ? 2.0523 2.4817 2.9350 -0.2710 -0.3938 0.0329 217 VAL B N 4731 C CA . VAL B 218 ? 2.0470 2.5059 2.9452 -0.2571 -0.4124 0.0378 217 VAL B CA 4732 C C . VAL B 218 ? 2.0178 2.5379 2.9886 -0.2558 -0.4063 0.0477 217 VAL B C 4733 O O . VAL B 218 ? 2.0168 2.5703 3.0145 -0.2496 -0.4268 0.0518 217 VAL B O 4734 C CB . VAL B 218 ? 2.0347 2.4681 2.8862 -0.2299 -0.4034 0.0410 217 VAL B CB 4735 C CG1 . VAL B 218 ? 1.9873 2.4320 2.8560 -0.2155 -0.3699 0.0492 217 VAL B CG1 4736 C CG2 . VAL B 218 ? 2.0412 2.4907 2.8916 -0.2169 -0.4291 0.0447 217 VAL B CG2 4737 N N . ILE B 219 ? 1.9835 2.5181 2.9844 -0.2601 -0.3783 0.0517 218 ILE B N 4738 C CA . ILE B 219 ? 1.9429 2.5347 3.0114 -0.2584 -0.3694 0.0605 218 ILE B CA 4739 C C . ILE B 219 ? 1.9285 2.5502 3.0462 -0.2854 -0.3697 0.0608 218 ILE B C 4740 O O . ILE B 219 ? 1.9161 2.5111 3.0181 -0.3029 -0.3599 0.0567 218 ILE B O 4741 C CB . ILE B 219 ? 1.9050 2.5012 2.9780 -0.2381 -0.3369 0.0669 218 ILE B CB 4742 C CG1 . ILE B 219 ? 1.8878 2.5427 3.0290 -0.2346 -0.3283 0.0750 218 ILE B CG1 4743 C CG2 . ILE B 219 ? 1.8988 2.4615 2.9448 -0.2446 -0.3108 0.0639 218 ILE B CG2 4744 C CD1 . ILE B 219 ? 1.8673 2.5284 3.0120 -0.2092 -0.3056 0.0808 218 ILE B CD1 4745 N N . GLY B 220 ? 1.8851 2.5635 3.0639 -0.2881 -0.3808 0.0667 219 GLY B N 4746 C CA . GLY B 220 ? 1.8245 2.5419 3.0603 -0.3135 -0.3805 0.0695 219 GLY B CA 4747 C C . GLY B 220 ? 1.7381 2.4606 2.9915 -0.3176 -0.3440 0.0742 219 GLY B C 4748 O O . GLY B 220 ? 1.7067 2.4335 2.9592 -0.2959 -0.3193 0.0787 219 GLY B O 4749 N N . PRO B 221 ? 1.6857 2.4059 2.9533 -0.3460 -0.3409 0.0734 220 PRO B N 4750 C CA . PRO B 221 ? 1.6384 2.3566 2.9138 -0.3504 -0.3065 0.0782 220 PRO B CA 4751 C C . PRO B 221 ? 1.5461 2.3229 2.8806 -0.3394 -0.2849 0.0883 220 PRO B C 4752 O O . PRO B 221 ? 1.4911 2.2618 2.8177 -0.3274 -0.2547 0.0915 220 PRO B O 4753 C CB . PRO B 221 ? 1.6944 2.4034 2.9800 -0.3854 -0.3131 0.0768 220 PRO B CB 4754 C CG . PRO B 221 ? 1.7348 2.4304 3.0068 -0.3986 -0.3517 0.0686 220 PRO B CG 4755 C CD . PRO B 221 ? 1.7129 2.4390 2.9980 -0.3759 -0.3690 0.0696 220 PRO B CD 4756 N N . LEU B 222 ? 1.4933 2.3269 2.8863 -0.3427 -0.3006 0.0930 221 LEU B N 4757 C CA . LEU B 222 ? 1.4288 2.3224 2.8826 -0.3321 -0.2802 0.1028 221 LEU B CA 4758 C C . LEU B 222 ? 1.3614 2.2547 2.8013 -0.2957 -0.2673 0.1039 221 LEU B C 4759 O O . LEU B 222 ? 1.3143 2.2352 2.7814 -0.2822 -0.2403 0.1097 221 LEU B O 4760 C CB . LEU B 222 ? 1.4568 2.4143 2.9797 -0.3447 -0.3023 0.1078 221 LEU B CB 4761 C CG . LEU B 222 ? 1.5029 2.4676 3.0497 -0.3840 -0.3163 0.1077 221 LEU B CG 4762 C CD1 . LEU B 222 ? 1.4984 2.5311 3.1165 -0.3946 -0.3410 0.1126 221 LEU B CD1 4763 C CD2 . LEU B 222 ? 1.5143 2.4788 3.0735 -0.4008 -0.2831 0.1136 221 LEU B CD2 4764 N N . LYS B 223 ? 1.3529 2.2122 2.7477 -0.2803 -0.2858 0.0983 222 LYS B N 4765 C CA . LYS B 223 ? 1.3375 2.1879 2.7127 -0.2477 -0.2752 0.0994 222 LYS B CA 4766 C C . LYS B 223 ? 1.3201 2.1273 2.6511 -0.2405 -0.2454 0.0970 222 LYS B C 4767 O O . LYS B 223 ? 1.2795 2.0989 2.6218 -0.2230 -0.2211 0.1003 222 LYS B O 4768 C CB . LYS B 223 ? 1.3539 2.1790 2.6920 -0.2351 -0.3036 0.0957 222 LYS B CB 4769 C CG . LYS B 223 ? 1.3489 2.1902 2.6958 -0.2035 -0.3023 0.1005 222 LYS B CG 4770 C CD . LYS B 223 ? 1.3635 2.2704 2.7785 -0.1997 -0.3162 0.1072 222 LYS B CD 4771 C CE . LYS B 223 ? 1.3656 2.2914 2.7964 -0.1665 -0.3071 0.1131 222 LYS B CE 4772 N NZ . LYS B 223 ? 1.3722 2.3670 2.8753 -0.1611 -0.3163 0.1203 222 LYS B NZ 4773 N N . ILE B 224 ? 1.3468 2.1036 2.6273 -0.2537 -0.2480 0.0907 223 ILE B N 4774 C CA . ILE B 224 ? 1.3355 2.0511 2.5729 -0.2480 -0.2226 0.0883 223 ILE B CA 4775 C C . ILE B 224 ? 1.2952 2.0294 2.5591 -0.2563 -0.1938 0.0927 223 ILE B C 4776 O O . ILE B 224 ? 1.2396 1.9568 2.4827 -0.2442 -0.1697 0.0927 223 ILE B O 4777 C CB . ILE B 224 ? 1.3787 2.0383 2.5583 -0.2598 -0.2326 0.0809 223 ILE B CB 4778 C CG1 . ILE B 224 ? 1.3798 1.9982 2.5128 -0.2481 -0.2100 0.0787 223 ILE B CG1 4779 C CG2 . ILE B 224 ? 1.4078 2.0648 2.5979 -0.2896 -0.2384 0.0797 223 ILE B CG2 4780 C CD1 . ILE B 224 ? 1.3915 2.0022 2.5059 -0.2215 -0.2059 0.0792 223 ILE B CD1 4781 N N . ARG B 225 ? 1.3094 2.0788 2.6186 -0.2775 -0.1969 0.0968 224 ARG B N 4782 C CA . ARG B 225 ? 1.3207 2.1120 2.6584 -0.2871 -0.1697 0.1028 224 ARG B CA 4783 C C . ARG B 225 ? 1.3028 2.1187 2.6578 -0.2622 -0.1446 0.1065 224 ARG B C 4784 O O . ARG B 225 ? 1.2916 2.1002 2.6378 -0.2609 -0.1174 0.1084 224 ARG B O 4785 C CB . ARG B 225 ? 1.3527 2.1908 2.7486 -0.3112 -0.1792 0.1085 224 ARG B CB 4786 C CG . ARG B 225 ? 1.3700 2.2314 2.7959 -0.3245 -0.1508 0.1164 224 ARG B CG 4787 C CD . ARG B 225 ? 1.4053 2.3158 2.8927 -0.3503 -0.1611 0.1230 224 ARG B CD 4788 N NE . ARG B 225 ? 1.4058 2.3762 2.9489 -0.3373 -0.1718 0.1266 224 ARG B NE 4789 C CZ . ARG B 225 ? 1.4195 2.4463 3.0273 -0.3549 -0.1818 0.1332 224 ARG B CZ 4790 N NH1 . ARG B 225 ? 1.4434 2.4735 3.0691 -0.3886 -0.1820 0.1371 224 ARG B NH1 4791 N NH2 . ARG B 225 ? 1.4052 2.4860 3.0616 -0.3388 -0.1917 0.1365 224 ARG B NH2 4792 N N . GLU B 226 ? 1.3178 2.1606 2.6949 -0.2420 -0.1545 0.1073 225 GLU B N 4793 C CA . GLU B 226 ? 1.3311 2.1951 2.7244 -0.2160 -0.1333 0.1098 225 GLU B CA 4794 C C . GLU B 226 ? 1.3291 2.1461 2.6692 -0.2024 -0.1135 0.1051 225 GLU B C 4795 O O . GLU B 226 ? 1.3184 2.1420 2.6626 -0.1947 -0.0867 0.1065 225 GLU B O 4796 C CB . GLU B 226 ? 1.3409 2.2273 2.7537 -0.1950 -0.1520 0.1107 225 GLU B CB 4797 C CG . GLU B 226 ? 1.3512 2.2955 2.8265 -0.2041 -0.1699 0.1163 225 GLU B CG 4798 C CD . GLU B 226 ? 1.3708 2.3200 2.8474 -0.1923 -0.2015 0.1157 225 GLU B CD 4799 O OE1 . GLU B 226 ? 1.3653 2.2903 2.8123 -0.1677 -0.2020 0.1139 225 GLU B OE1 4800 O OE2 . GLU B 226 ? 1.3958 2.3725 2.9023 -0.2084 -0.2267 0.1173 225 GLU B OE2 4801 N N . GLN B 227 ? 1.3313 2.1016 2.6211 -0.1999 -0.1270 0.0995 226 GLN B N 4802 C CA . GLN B 227 ? 1.3087 2.0350 2.5489 -0.1892 -0.1115 0.0951 226 GLN B CA 4803 C C . GLN B 227 ? 1.2853 1.9928 2.5073 -0.2054 -0.0937 0.0949 226 GLN B C 4804 O O . GLN B 227 ? 1.2366 1.9333 2.4432 -0.1967 -0.0712 0.0941 226 GLN B O 4805 C CB . GLN B 227 ? 1.3231 2.0078 2.5171 -0.1848 -0.1305 0.0904 226 GLN B CB 4806 C CG . GLN B 227 ? 1.3241 1.9641 2.4678 -0.1774 -0.1169 0.0862 226 GLN B CG 4807 C CD . GLN B 227 ? 1.3314 1.9447 2.4486 -0.1954 -0.1103 0.0842 226 GLN B CD 4808 O OE1 . GLN B 227 ? 1.3242 1.9278 2.4296 -0.1944 -0.0894 0.0840 226 GLN B OE1 4809 N NE2 . GLN B 227 ? 1.3479 1.9473 2.4537 -0.2112 -0.1287 0.0826 226 GLN B NE2 4810 N N . GLN B 228 ? 1.2981 1.9991 2.5195 -0.2288 -0.1051 0.0954 227 GLN B N 4811 C CA . GLN B 228 ? 1.3181 1.9945 2.5173 -0.2449 -0.0913 0.0959 227 GLN B CA 4812 C C . GLN B 228 ? 1.2876 1.9929 2.5153 -0.2465 -0.0644 0.1019 227 GLN B C 4813 O O . GLN B 228 ? 1.2783 1.9611 2.4786 -0.2454 -0.0451 0.1019 227 GLN B O 4814 C CB . GLN B 228 ? 1.3788 2.0447 2.5775 -0.2704 -0.1100 0.0956 227 GLN B CB 4815 C CG . GLN B 228 ? 1.4288 2.0567 2.5872 -0.2691 -0.1339 0.0886 227 GLN B CG 4816 C CD . GLN B 228 ? 1.5037 2.1261 2.6670 -0.2928 -0.1570 0.0870 227 GLN B CD 4817 O OE1 . GLN B 228 ? 1.5397 2.1999 2.7498 -0.3080 -0.1632 0.0913 227 GLN B OE1 4818 N NE2 . GLN B 228 ? 1.5531 2.1284 2.6681 -0.2960 -0.1700 0.0804 227 GLN B NE2 4819 N N . ARG B 229 ? 1.2773 2.0337 2.5597 -0.2480 -0.0631 0.1074 228 ARG B N 4820 C CA . ARG B 229 ? 1.2885 2.0777 2.6012 -0.2472 -0.0358 0.1138 228 ARG B CA 4821 C C . ARG B 229 ? 1.2563 2.0364 2.5482 -0.2216 -0.0143 0.1106 228 ARG B C 4822 O O . ARG B 229 ? 1.2620 2.0413 2.5468 -0.2215 0.0104 0.1132 228 ARG B O 4823 C CB . ARG B 229 ? 1.3083 2.1592 2.6876 -0.2499 -0.0395 0.1201 228 ARG B CB 4824 C CG . ARG B 229 ? 1.3347 2.2024 2.7434 -0.2804 -0.0546 0.1249 228 ARG B CG 4825 C CD . ARG B 229 ? 1.3375 2.2724 2.8173 -0.2826 -0.0583 0.1319 228 ARG B CD 4826 N NE . ARG B 229 ? 1.3548 2.3078 2.8661 -0.3150 -0.0718 0.1369 228 ARG B NE 4827 C CZ . ARG B 229 ? 1.3550 2.3690 2.9331 -0.3250 -0.0768 0.1442 228 ARG B CZ 4828 N NH1 . ARG B 229 ? 1.3389 2.4032 2.9597 -0.3026 -0.0684 0.1475 228 ARG B NH1 4829 N NH2 . ARG B 229 ? 1.3751 2.3999 2.9782 -0.3576 -0.0905 0.1482 228 ARG B NH2 4830 N N . SER B 230 ? 1.2040 1.9749 2.4840 -0.2007 -0.0246 0.1052 229 SER B N 4831 C CA . SER B 230 ? 1.1546 1.9158 2.4168 -0.1762 -0.0078 0.1012 229 SER B CA 4832 C C . SER B 230 ? 1.1202 1.8353 2.3289 -0.1758 0.0042 0.0967 229 SER B C 4833 O O . SER B 230 ? 1.0747 1.7850 2.2708 -0.1614 0.0235 0.0942 229 SER B O 4834 C CB . SER B 230 ? 1.1479 1.9043 2.4073 -0.1564 -0.0242 0.0973 229 SER B CB 4835 O OG . SER B 230 ? 1.1456 1.8564 2.3585 -0.1576 -0.0384 0.0923 229 SER B OG 4836 N N . ALA B 231 ? 1.1132 1.7945 2.2901 -0.1904 -0.0080 0.0952 230 ALA B N 4837 C CA . ALA B 231 ? 1.1150 1.7545 2.2429 -0.1905 0.0008 0.0917 230 ALA B CA 4838 C C . ALA B 231 ? 1.1407 1.7828 2.2668 -0.2017 0.0217 0.0965 230 ALA B C 4839 O O . ALA B 231 ? 1.1103 1.7588 2.2495 -0.2217 0.0196 0.1021 230 ALA B O 4840 C CB . ALA B 231 ? 1.1163 1.7202 2.2118 -0.1999 -0.0186 0.0889 230 ALA B CB 4841 N N . VAL B 232 ? 1.1845 1.8190 2.2917 -0.1890 0.0413 0.0944 231 VAL B N 4842 C CA . VAL B 232 ? 1.2254 1.8598 2.3244 -0.1963 0.0630 0.0993 231 VAL B CA 4843 C C . VAL B 232 ? 1.2387 1.8404 2.3076 -0.2140 0.0577 0.1021 231 VAL B C 4844 O O . VAL B 232 ? 1.2317 1.8382 2.3066 -0.2292 0.0684 0.1097 231 VAL B O 4845 C CB . VAL B 232 ? 1.2418 1.8637 2.3131 -0.1780 0.0809 0.0943 231 VAL B CB 4846 C CG1 . VAL B 232 ? 1.2695 1.8862 2.3240 -0.1852 0.1021 0.0997 231 VAL B CG1 4847 C CG2 . VAL B 232 ? 1.2345 1.8857 2.3338 -0.1592 0.0889 0.0914 231 VAL B CG2 4848 N N . SER B 233 ? 1.2620 1.8296 2.2980 -0.2114 0.0419 0.0963 232 SER B N 4849 C CA . SER B 233 ? 1.2940 1.8269 2.2984 -0.2244 0.0354 0.0978 232 SER B CA 4850 C C . SER B 233 ? 1.3145 1.8540 2.3401 -0.2468 0.0273 0.1039 232 SER B C 4851 O O . SER B 233 ? 1.3591 1.8751 2.3649 -0.2599 0.0303 0.1081 232 SER B O 4852 C CB . SER B 233 ? 1.3037 1.8068 2.2779 -0.2164 0.0183 0.0906 232 SER B CB 4853 O OG . SER B 233 ? 1.3043 1.8212 2.2999 -0.2141 0.0011 0.0878 232 SER B OG 4854 N N . THR B 234 ? 1.2951 1.8650 2.3603 -0.2514 0.0159 0.1044 233 THR B N 4855 C CA . THR B 234 ? 1.2983 1.8780 2.3885 -0.2745 0.0060 0.1096 233 THR B CA 4856 C C . THR B 234 ? 1.2965 1.8930 2.4053 -0.2890 0.0266 0.1196 233 THR B C 4857 O O . THR B 234 ? 1.2975 1.8719 2.3940 -0.3079 0.0262 0.1244 233 THR B O 4858 C CB . THR B 234 ? 1.3028 1.9201 2.4375 -0.2748 -0.0098 0.1087 233 THR B CB 4859 O OG1 . THR B 234 ? 1.2840 1.8899 2.4020 -0.2570 -0.0241 0.1008 233 THR B OG1 4860 C CG2 . THR B 234 ? 1.3328 1.9509 2.4845 -0.2995 -0.0281 0.1110 233 THR B CG2 4861 N N . SER B 235 ? 1.2870 1.9205 2.4236 -0.2793 0.0455 0.1231 234 SER B N 4862 C CA . SER B 235 ? 1.3096 1.9641 2.4653 -0.2907 0.0688 0.1336 234 SER B CA 4863 C C . SER B 235 ? 1.3446 1.9606 2.4526 -0.2912 0.0847 0.1367 234 SER B C 4864 O O . SER B 235 ? 1.3805 1.9947 2.4907 -0.3083 0.0973 0.1467 234 SER B O 4865 C CB . SER B 235 ? 1.2877 1.9889 2.4789 -0.2749 0.0867 0.1351 234 SER B CB 4866 O OG . SER B 235 ? 1.2567 1.9893 2.4860 -0.2684 0.0702 0.1314 234 SER B OG 4867 N N . TRP B 236 ? 1.3503 1.9360 2.4158 -0.2728 0.0833 0.1286 235 TRP B N 4868 C CA . TRP B 236 ? 1.3613 1.9099 2.3791 -0.2705 0.0946 0.1305 235 TRP B CA 4869 C C . TRP B 236 ? 1.3640 1.8757 2.3590 -0.2892 0.0845 0.1348 235 TRP B C 4870 O O . TRP B 236 ? 1.3437 1.8323 2.3111 -0.2942 0.0971 0.1416 235 TRP B O 4871 C CB . TRP B 236 ? 1.3628 1.8897 2.3453 -0.2482 0.0901 0.1200 235 TRP B CB 4872 C CG . TRP B 236 ? 1.3833 1.8767 2.3185 -0.2429 0.0999 0.1211 235 TRP B CG 4873 C CD1 . TRP B 236 ? 1.4027 1.8941 2.3253 -0.2468 0.1204 0.1296 235 TRP B CD1 4874 C CD2 . TRP B 236 ? 1.3932 1.8525 2.2879 -0.2320 0.0894 0.1141 235 TRP B CD2 4875 N NE1 . TRP B 236 ? 1.4190 1.8756 2.2942 -0.2385 0.1215 0.1280 235 TRP B NE1 4876 C CE2 . TRP B 236 ? 1.4092 1.8475 2.2687 -0.2295 0.1027 0.1185 235 TRP B CE2 4877 C CE3 . TRP B 236 ? 1.3844 1.8302 2.2696 -0.2240 0.0705 0.1053 235 TRP B CE3 4878 C CZ2 . TRP B 236 ? 1.4153 1.8223 2.2338 -0.2192 0.0962 0.1140 235 TRP B CZ2 4879 C CZ3 . TRP B 236 ? 1.3881 1.8036 2.2336 -0.2145 0.0661 0.1013 235 TRP B CZ3 4880 C CH2 . TRP B 236 ? 1.4024 1.8001 2.2167 -0.2121 0.0782 0.1054 235 TRP B CH2 4881 N N . LEU B 237 ? 1.3736 1.8776 2.3776 -0.2987 0.0617 0.1308 236 LEU B N 4882 C CA . LEU B 237 ? 1.4298 1.8942 2.4097 -0.3149 0.0498 0.1327 236 LEU B CA 4883 C C . LEU B 237 ? 1.4670 1.9411 2.4765 -0.3426 0.0499 0.1421 236 LEU B C 4884 O O . LEU B 237 ? 1.4957 1.9357 2.4882 -0.3579 0.0372 0.1426 236 LEU B O 4885 C CB . LEU B 237 ? 1.4483 1.8919 2.4136 -0.3097 0.0245 0.1221 236 LEU B CB 4886 C CG . LEU B 237 ? 1.4618 1.8845 2.3906 -0.2865 0.0221 0.1139 236 LEU B CG 4887 C CD1 . LEU B 237 ? 1.4580 1.8678 2.3793 -0.2826 -0.0010 0.1049 236 LEU B CD1 4888 C CD2 . LEU B 237 ? 1.4921 1.8763 2.3763 -0.2833 0.0308 0.1168 236 LEU B CD2 4889 N N . LEU B 238 ? 1.4763 1.9959 2.5300 -0.3494 0.0643 0.1496 237 LEU B N 4890 C CA . LEU B 238 ? 1.4975 2.0290 2.5812 -0.3775 0.0684 0.1608 237 LEU B CA 4891 C C . LEU B 238 ? 1.5374 2.0276 2.5828 -0.3875 0.0823 0.1701 237 LEU B C 4892 O O . LEU B 238 ? 1.5688 2.0422 2.5784 -0.3707 0.0974 0.1710 237 LEU B O 4893 C CB . LEU B 238 ? 1.4778 2.0697 2.6156 -0.3797 0.0864 0.1684 237 LEU B CB 4894 C CG . LEU B 238 ? 1.4462 2.0839 2.6332 -0.3761 0.0710 0.1626 237 LEU B CG 4895 C CD1 . LEU B 238 ? 1.4202 2.1149 2.6505 -0.3663 0.0932 0.1682 237 LEU B CD1 4896 C CD2 . LEU B 238 ? 1.4652 2.1085 2.6829 -0.4041 0.0496 0.1645 237 LEU B CD2 4897 N N . PRO B 239 ? 1.5632 2.0350 2.6145 -0.4149 0.0759 0.1772 238 PRO B N 4898 C CA . PRO B 239 ? 1.6054 2.0344 2.6212 -0.4264 0.0880 0.1878 238 PRO B CA 4899 C C . PRO B 239 ? 1.6265 2.0700 2.6365 -0.4200 0.1197 0.1998 238 PRO B C 4900 O O . PRO B 239 ? 1.5703 2.0647 2.6224 -0.4216 0.1357 0.2054 238 PRO B O 4901 C CB . PRO B 239 ? 1.6342 2.0619 2.6796 -0.4606 0.0789 0.1950 238 PRO B CB 4902 C CG . PRO B 239 ? 1.6129 2.0546 2.6825 -0.4626 0.0506 0.1822 238 PRO B CG 4903 C CD . PRO B 239 ? 1.5645 2.0487 2.6518 -0.4362 0.0532 0.1743 238 PRO B CD 4904 N N . TYR B 240 ? 1.7112 2.1099 2.6681 -0.4117 0.1284 0.2036 239 TYR B N 4905 C CA . TYR B 240 ? 1.8026 2.2053 2.7422 -0.4050 0.1572 0.2152 239 TYR B CA 4906 C C . TYR B 240 ? 1.9119 2.2809 2.8343 -0.4280 0.1679 0.2318 239 TYR B C 4907 O O . TYR B 240 ? 1.9434 2.2660 2.8430 -0.4396 0.1518 0.2315 239 TYR B O 4908 C CB . TYR B 240 ? 1.8216 2.2000 2.7107 -0.3755 0.1587 0.2074 239 TYR B CB 4909 C CG . TYR B 240 ? 1.8021 2.2125 2.7041 -0.3519 0.1539 0.1932 239 TYR B CG 4910 C CD1 . TYR B 240 ? 1.7766 2.1797 2.6786 -0.3434 0.1291 0.1790 239 TYR B CD1 4911 C CD2 . TYR B 240 ? 1.8023 2.2465 2.7127 -0.3374 0.1747 0.1941 239 TYR B CD2 4912 C CE1 . TYR B 240 ? 1.7059 2.1345 2.6179 -0.3228 0.1251 0.1673 239 TYR B CE1 4913 C CE2 . TYR B 240 ? 1.7453 2.2133 2.6649 -0.3160 0.1701 0.1811 239 TYR B CE2 4914 C CZ . TYR B 240 ? 1.6959 2.1557 2.6170 -0.3095 0.1452 0.1682 239 TYR B CZ 4915 O OH . TYR B 240 ? 1.6265 2.1070 2.5560 -0.2893 0.1410 0.1566 239 TYR B OH 4916 N N . ASN B 241 ? 2.0037 2.3934 2.9338 -0.4330 0.1960 0.2464 240 ASN B N 4917 C CA . ASN B 241 ? 2.1370 2.5024 3.0593 -0.4581 0.2100 0.2653 240 ASN B CA 4918 C C . ASN B 241 ? 2.2311 2.5309 3.0873 -0.4524 0.2110 0.2714 240 ASN B C 4919 O O . ASN B 241 ? 2.2371 2.5047 3.0816 -0.4741 0.2172 0.2861 240 ASN B O 4920 C CB . ASN B 241 ? 2.1647 2.5755 3.1151 -0.4639 0.2426 0.2803 240 ASN B CB 4921 C CG . ASN B 241 ? 2.1656 2.5795 3.0787 -0.4348 0.2631 0.2800 240 ASN B CG 4922 O OD1 . ASN B 241 ? 2.1851 2.5594 3.0453 -0.4145 0.2550 0.2728 240 ASN B OD1 4923 N ND2 . ASN B 241 ? 2.1465 2.6091 3.0878 -0.4325 0.2899 0.2876 240 ASN B ND2 4924 N N . TYR B 242 ? 2.3059 2.5864 3.1197 -0.4233 0.2054 0.2610 241 TYR B N 4925 C CA . TYR B 242 ? 2.4027 2.6244 3.1547 -0.4143 0.2046 0.2661 241 TYR B CA 4926 C C . TYR B 242 ? 2.3640 2.5367 3.0970 -0.4197 0.1779 0.2589 241 TYR B C 4927 O O . TYR B 242 ? 2.4436 2.5628 3.1311 -0.4187 0.1765 0.2661 241 TYR B O 4928 C CB . TYR B 242 ? 2.4674 2.6895 3.1819 -0.3814 0.2090 0.2586 241 TYR B CB 4929 C CG . TYR B 242 ? 2.5318 2.7701 3.2539 -0.3611 0.1892 0.2378 241 TYR B CG 4930 C CD1 . TYR B 242 ? 2.5840 2.7853 3.2792 -0.3515 0.1660 0.2277 241 TYR B CD1 4931 C CD2 . TYR B 242 ? 2.5543 2.8439 3.3093 -0.3505 0.1947 0.2290 241 TYR B CD2 4932 C CE1 . TYR B 242 ? 2.5631 2.7793 3.2649 -0.3338 0.1496 0.2103 241 TYR B CE1 4933 C CE2 . TYR B 242 ? 2.5486 2.8499 3.3091 -0.3328 0.1771 0.2114 241 TYR B CE2 4934 C CZ . TYR B 242 ? 2.5388 2.8041 3.2730 -0.3253 0.1549 0.2026 241 TYR B CZ 4935 O OH . TYR B 242 ? 2.4505 2.7277 3.1902 -0.3088 0.1390 0.1866 241 TYR B OH 4936 N N . THR B 243 ? 2.2393 2.4293 3.0050 -0.4241 0.1571 0.2449 242 THR B N 4937 C CA . THR B 243 ? 2.1744 2.3204 2.9237 -0.4293 0.1315 0.2362 242 THR B CA 4938 C C . THR B 243 ? 2.1605 2.3039 2.9440 -0.4633 0.1234 0.2407 242 THR B C 4939 O O . THR B 243 ? 2.1999 2.2906 2.9588 -0.4766 0.1132 0.2437 242 THR B O 4940 C CB . THR B 243 ? 2.1117 2.2716 2.8655 -0.4092 0.1108 0.2160 242 THR B CB 4941 O OG1 . THR B 243 ? 2.0902 2.2512 2.8132 -0.3794 0.1164 0.2113 242 THR B OG1 4942 C CG2 . THR B 243 ? 2.1124 2.2251 2.8446 -0.4127 0.0862 0.2070 242 THR B CG2 4943 N N . TRP B 244 ? 2.1029 2.3031 2.9435 -0.4767 0.1270 0.2408 243 TRP B N 4944 C CA . TRP B 244 ? 2.0988 2.3076 2.9810 -0.5109 0.1190 0.2453 243 TRP B CA 4945 C C . TRP B 244 ? 2.1156 2.3388 3.0172 -0.5335 0.1453 0.2667 243 TRP B C 4946 O O . TRP B 244 ? 2.1172 2.3625 3.0128 -0.5205 0.1705 0.2757 243 TRP B O 4947 C CB . TRP B 244 ? 2.0368 2.3032 2.9737 -0.5119 0.1058 0.2335 243 TRP B CB 4948 C CG . TRP B 244 ? 1.9876 2.2410 2.9056 -0.4905 0.0812 0.2139 243 TRP B CG 4949 C CD1 . TRP B 244 ? 1.9477 2.2132 2.8482 -0.4587 0.0824 0.2040 243 TRP B CD1 4950 C CD2 . TRP B 244 ? 1.9805 2.2042 2.8929 -0.5000 0.0525 0.2022 243 TRP B CD2 4951 N NE1 . TRP B 244 ? 1.9277 2.1752 2.8142 -0.4481 0.0575 0.1882 243 TRP B NE1 4952 C CE2 . TRP B 244 ? 1.9377 2.1590 2.8293 -0.4719 0.0390 0.1864 243 TRP B CE2 4953 C CE3 . TRP B 244 ? 2.0343 2.2316 2.9557 -0.5301 0.0366 0.2033 243 TRP B CE3 4954 C CZ2 . TRP B 244 ? 1.9390 2.1336 2.8171 -0.4715 0.0119 0.1723 243 TRP B CZ2 4955 C CZ3 . TRP B 244 ? 2.0358 2.2046 2.9423 -0.5294 0.0079 0.1877 243 TRP B CZ3 4956 C CH2 . TRP B 244 ? 1.9815 2.1496 2.8657 -0.4996 -0.0032 0.1727 243 TRP B CH2 4957 N N . SER B 245 ? 2.1158 2.3253 3.0392 -0.5680 0.1396 0.2749 244 SER B N 4958 C CA . SER B 245 ? 2.1317 2.3559 3.0783 -0.5938 0.1647 0.2968 244 SER B CA 4959 C C . SER B 245 ? 2.0718 2.3795 3.0816 -0.5949 0.1809 0.3000 244 SER B C 4960 O O . SER B 245 ? 1.9818 2.3312 3.0366 -0.5968 0.1638 0.2879 244 SER B O 4961 C CB . SER B 245 ? 2.1972 2.3892 3.1580 -0.6330 0.1515 0.3033 244 SER B CB 4962 O OG . SER B 245 ? 2.2643 2.4618 3.2405 -0.6586 0.1773 0.3266 244 SER B OG 4963 N N . PRO B 246 ? 2.0971 2.4292 3.1090 -0.5921 0.2140 0.3163 245 PRO B N 4964 C CA . PRO B 246 ? 2.0757 2.4874 3.1481 -0.5923 0.2322 0.3203 245 PRO B CA 4965 C C . PRO B 246 ? 2.0868 2.5420 3.2317 -0.6273 0.2245 0.3251 245 PRO B C 4966 O O . PRO B 246 ? 2.0067 2.5311 3.2084 -0.6238 0.2286 0.3222 245 PRO B O 4967 C CB . PRO B 246 ? 2.0984 2.5130 3.1510 -0.5896 0.2701 0.3403 245 PRO B CB 4968 C CG . PRO B 246 ? 2.1146 2.4583 3.0886 -0.5721 0.2686 0.3402 245 PRO B CG 4969 C CD . PRO B 246 ? 2.1285 2.4167 3.0829 -0.5833 0.2360 0.3305 245 PRO B CD 4970 N N . GLU B 247 ? 2.1712 2.5851 3.3137 -0.6603 0.2126 0.3324 246 GLU B N 4971 C CA . GLU B 247 ? 2.1980 2.6471 3.4071 -0.6984 0.2035 0.3381 246 GLU B CA 4972 C C . GLU B 247 ? 2.1460 2.5819 3.3671 -0.7066 0.1619 0.3185 246 GLU B C 4973 O O . GLU B 247 ? 2.1462 2.6073 3.4200 -0.7387 0.1481 0.3206 246 GLU B O 4974 C CB . GLU B 247 ? 2.2947 2.7063 3.4967 -0.7349 0.2172 0.3600 246 GLU B CB 4975 C CG . GLU B 247 ? 2.3429 2.7762 3.5447 -0.7353 0.2602 0.3834 246 GLU B CG 4976 C CD . GLU B 247 ? 2.3752 2.7718 3.5049 -0.6984 0.2774 0.3835 246 GLU B CD 4977 O OE1 . GLU B 247 ? 2.4281 2.7622 3.4988 -0.6812 0.2580 0.3714 246 GLU B OE1 4978 O OE2 . GLU B 247 ? 2.3874 2.8190 3.5195 -0.6859 0.3104 0.3955 246 GLU B OE2 4979 N N . LYS B 248 ? 2.0893 2.4869 3.2621 -0.6782 0.1420 0.2998 247 LYS B N 4980 C CA . LYS B 248 ? 2.0700 2.4463 3.2431 -0.6840 0.1038 0.2814 247 LYS B CA 4981 C C . LYS B 248 ? 2.0094 2.4596 3.2489 -0.6841 0.0899 0.2722 247 LYS B C 4982 O O . LYS B 248 ? 1.9575 2.4554 3.2123 -0.6563 0.1006 0.2680 247 LYS B O 4983 C CB . LYS B 248 ? 2.0587 2.3803 3.1640 -0.6508 0.0897 0.2650 247 LYS B CB 4984 C CG . LYS B 248 ? 2.0573 2.3535 3.1543 -0.6520 0.0519 0.2451 247 LYS B CG 4985 C CD . LYS B 248 ? 2.1257 2.3651 3.2095 -0.6859 0.0344 0.2470 247 LYS B CD 4986 C CE . LYS B 248 ? 2.1253 2.3513 3.2109 -0.6905 -0.0033 0.2271 247 LYS B CE 4987 N NZ . LYS B 248 ? 2.0883 2.2889 3.1257 -0.6527 -0.0153 0.2095 247 LYS B NZ 4988 N N . VAL B 249 ? 2.0088 2.4655 3.2855 -0.7150 0.0649 0.2689 248 VAL B N 4989 C CA . VAL B 249 ? 1.9620 2.4861 3.3020 -0.7173 0.0467 0.2602 248 VAL B CA 4990 C C . VAL B 249 ? 1.9537 2.4518 3.2607 -0.6939 0.0150 0.2372 248 VAL B C 4991 O O . VAL B 249 ? 1.9749 2.4116 3.2431 -0.7040 -0.0091 0.2277 248 VAL B O 4992 C CB . VAL B 249 ? 1.9782 2.5224 3.3744 -0.7632 0.0311 0.2669 248 VAL B CB 4993 C CG1 . VAL B 249 ? 1.9354 2.5573 3.4016 -0.7639 0.0135 0.2599 248 VAL B CG1 4994 C CG2 . VAL B 249 ? 1.9993 2.5587 3.4222 -0.7906 0.0629 0.2914 248 VAL B CG2 4995 N N . PHE B 250 ? 1.9439 2.4861 3.2639 -0.6623 0.0161 0.2287 249 PHE B N 4996 C CA . PHE B 250 ? 1.9732 2.4953 3.2631 -0.6384 -0.0111 0.2085 249 PHE B CA 4997 C C . PHE B 250 ? 1.9463 2.5139 3.2884 -0.6490 -0.0400 0.1999 249 PHE B C 4998 O O . PHE B 250 ? 1.9452 2.4811 3.2628 -0.6474 -0.0708 0.1848 249 PHE B O 4999 C CB . PHE B 250 ? 1.9848 2.5206 3.2518 -0.5967 0.0051 0.2037 249 PHE B CB 5000 C CG . PHE B 250 ? 2.0544 2.5375 3.2588 -0.5809 0.0256 0.2076 249 PHE B CG 5001 C CD1 . PHE B 250 ? 2.1019 2.5195 3.2429 -0.5673 0.0108 0.1962 249 PHE B CD1 5002 C CD2 . PHE B 250 ? 2.0709 2.5709 3.2791 -0.5785 0.0597 0.2229 249 PHE B CD2 5003 C CE1 . PHE B 250 ? 2.1220 2.4942 3.2078 -0.5517 0.0281 0.2002 249 PHE B CE1 5004 C CE2 . PHE B 250 ? 2.0899 2.5418 3.2390 -0.5633 0.0765 0.2267 249 PHE B CE2 5005 C CZ . PHE B 250 ? 2.1124 2.5014 3.2018 -0.5500 0.0600 0.2154 249 PHE B CZ 5006 N N . VAL B 251 ? 1.9203 2.5633 3.3334 -0.6581 -0.0297 0.2097 250 VAL B N 5007 C CA . VAL B 251 ? 1.9101 2.6065 3.3791 -0.6650 -0.0561 0.2031 250 VAL B CA 5008 C C . VAL B 251 ? 1.9415 2.6901 3.4835 -0.7027 -0.0536 0.2172 250 VAL B C 5009 O O . VAL B 251 ? 1.9553 2.7452 3.5322 -0.7068 -0.0215 0.2335 250 VAL B O 5010 C CB . VAL B 251 ? 1.8448 2.5956 3.3356 -0.6285 -0.0500 0.1983 250 VAL B CB 5011 C CG1 . VAL B 251 ? 1.8294 2.6378 3.3804 -0.6352 -0.0777 0.1933 250 VAL B CG1 5012 C CG2 . VAL B 251 ? 1.8304 2.5317 3.2526 -0.5935 -0.0542 0.1845 250 VAL B CG2 5013 N N . GLN B 252 ? 1.9563 2.7024 3.5200 -0.7305 -0.0879 0.2107 251 GLN B N 5014 C CA . GLN B 252 ? 1.9432 2.7444 3.5833 -0.7687 -0.0928 0.2222 251 GLN B CA 5015 C C . GLN B 252 ? 1.9110 2.7772 3.6071 -0.7636 -0.1209 0.2140 251 GLN B C 5016 O O . GLN B 252 ? 1.9020 2.7415 3.5668 -0.7504 -0.1524 0.1968 251 GLN B O 5017 C CB . GLN B 252 ? 1.9865 2.7294 3.6083 -0.8107 -0.1120 0.2222 251 GLN B CB 5018 C CG . GLN B 252 ? 1.9949 2.6813 3.5747 -0.8228 -0.0832 0.2350 251 GLN B CG 5019 C CD . GLN B 252 ? 1.9882 2.5811 3.4742 -0.8028 -0.0882 0.2229 251 GLN B CD 5020 O OE1 . GLN B 252 ? 1.9717 2.5519 3.4209 -0.7675 -0.0975 0.2083 251 GLN B OE1 5021 N NE2 . GLN B 252 ? 2.0117 2.5390 3.4594 -0.8249 -0.0814 0.2299 251 GLN B NE2 5022 N N . THR B 253 ? 1.8901 2.8420 3.6680 -0.7727 -0.1085 0.2271 252 THR B N 5023 C CA . THR B 253 ? 1.8799 2.9026 3.7216 -0.7703 -0.1345 0.2223 252 THR B CA 5024 C C . THR B 253 ? 1.9256 3.0005 3.8460 -0.8162 -0.1412 0.2352 252 THR B C 5025 O O . THR B 253 ? 1.9520 3.0067 3.8735 -0.8460 -0.1220 0.2481 252 THR B O 5026 C CB . THR B 253 ? 1.8216 2.9098 3.6946 -0.7301 -0.1112 0.2260 252 THR B CB 5027 O OG1 . THR B 253 ? 1.8198 2.9724 3.7559 -0.7411 -0.0765 0.2457 252 THR B OG1 5028 C CG2 . THR B 253 ? 1.7973 2.8330 3.5944 -0.6899 -0.0924 0.2184 252 THR B CG2 5029 N N . PRO B 254 ? 1.9395 3.0824 3.9270 -0.8227 -0.1685 0.2327 253 PRO B N 5030 C CA . PRO B 254 ? 1.9689 3.1657 4.0361 -0.8684 -0.1770 0.2450 253 PRO B CA 5031 C C . PRO B 254 ? 1.9573 3.2157 4.0838 -0.8776 -0.1314 0.2685 253 PRO B C 5032 O O . PRO B 254 ? 1.9988 3.2774 4.1723 -0.9211 -0.1286 0.2818 253 PRO B O 5033 C CB . PRO B 254 ? 1.9543 3.2197 4.0805 -0.8624 -0.2130 0.2374 253 PRO B CB 5034 C CG . PRO B 254 ? 1.9328 3.1535 3.9917 -0.8218 -0.2322 0.2182 253 PRO B CG 5035 C CD . PRO B 254 ? 1.9083 3.0845 3.9050 -0.7896 -0.1925 0.2201 253 PRO B CD 5036 N N . THR B 255 ? 1.9025 3.1882 4.0245 -0.8374 -0.0959 0.2735 254 THR B N 5037 C CA . THR B 255 ? 1.8668 3.2169 4.0440 -0.8390 -0.0508 0.2949 254 THR B CA 5038 C C . THR B 255 ? 1.8546 3.1513 3.9716 -0.8305 -0.0076 0.3040 254 THR B C 5039 O O . THR B 255 ? 1.8705 3.1973 4.0223 -0.8501 0.0260 0.3238 254 THR B O 5040 C CB . THR B 255 ? 1.8137 3.2461 4.0402 -0.7987 -0.0387 0.2956 254 THR B CB 5041 O OG1 . THR B 255 ? 1.7776 3.1644 3.9331 -0.7521 -0.0369 0.2808 254 THR B OG1 5042 C CG2 . THR B 255 ? 1.8038 3.3046 4.1041 -0.8083 -0.0775 0.2912 254 THR B CG2 5043 N N . ILE B 256 ? 1.8120 3.0314 3.8398 -0.8019 -0.0084 0.2906 255 ILE B N 5044 C CA . ILE B 256 ? 1.7816 2.9583 3.7528 -0.7854 0.0320 0.2982 255 ILE B CA 5045 C C . ILE B 256 ? 1.7932 2.8660 3.6647 -0.7747 0.0197 0.2842 255 ILE B C 5046 O O . ILE B 256 ? 1.7757 2.8136 3.6167 -0.7674 -0.0166 0.2661 255 ILE B O 5047 C CB . ILE B 256 ? 1.7178 2.9466 3.7023 -0.7409 0.0631 0.3003 255 ILE B CB 5048 C CG1 . ILE B 256 ? 1.7158 2.9275 3.6684 -0.7327 0.1110 0.3145 255 ILE B CG1 5049 C CG2 . ILE B 256 ? 1.6812 2.8827 3.6180 -0.6991 0.0434 0.2797 255 ILE B CG2 5050 C CD1 . ILE B 256 ? 1.6798 2.9462 3.6506 -0.6927 0.1435 0.3175 255 ILE B CD1 5051 N N . ASN B 257 ? 1.8216 2.8468 3.6435 -0.7741 0.0507 0.2937 256 ASN B N 5052 C CA . ASN B 257 ? 1.8537 2.7869 3.5813 -0.7568 0.0473 0.2829 256 ASN B CA 5053 C C . ASN B 257 ? 1.8245 2.7576 3.5140 -0.7095 0.0706 0.2781 256 ASN B C 5054 O O . ASN B 257 ? 1.8171 2.8131 3.5463 -0.6925 0.0969 0.2860 256 ASN B O 5055 C CB . ASN B 257 ? 1.9142 2.7909 3.6061 -0.7836 0.0664 0.2969 256 ASN B CB 5056 C CG . ASN B 257 ? 1.9907 2.8395 3.6975 -0.8301 0.0393 0.2983 256 ASN B CG 5057 O OD1 . ASN B 257 ? 1.9893 2.8261 3.6978 -0.8370 0.0000 0.2825 256 ASN B OD1 5058 N ND2 . ASN B 257 ? 2.0763 2.9104 3.7901 -0.8629 0.0603 0.3173 256 ASN B ND2 5059 N N . TYR B 258 ? 1.8067 2.6676 3.4183 -0.6886 0.0610 0.2649 257 TYR B N 5060 C CA . TYR B 258 ? 1.7445 2.5920 3.3099 -0.6475 0.0826 0.2605 257 TYR B CA 5061 C C . TYR B 258 ? 1.7902 2.5522 3.2729 -0.6432 0.0883 0.2591 257 TYR B C 5062 O O . TYR B 258 ? 1.7883 2.4917 3.2279 -0.6468 0.0610 0.2472 257 TYR B O 5063 C CB . TYR B 258 ? 1.6677 2.5308 3.2307 -0.6151 0.0613 0.2427 257 TYR B CB 5064 C CG . TYR B 258 ? 1.6222 2.5715 3.2637 -0.6113 0.0588 0.2446 257 TYR B CG 5065 C CD1 . TYR B 258 ? 1.5999 2.6053 3.2735 -0.5912 0.0916 0.2534 257 TYR B CD1 5066 C CD2 . TYR B 258 ? 1.5969 2.5712 3.2794 -0.6264 0.0234 0.2376 257 TYR B CD2 5067 C CE1 . TYR B 258 ? 1.5621 2.6474 3.3087 -0.5851 0.0900 0.2555 257 TYR B CE1 5068 C CE2 . TYR B 258 ? 1.5616 2.6169 3.3175 -0.6213 0.0199 0.2401 257 TYR B CE2 5069 C CZ . TYR B 258 ? 1.5406 2.6516 3.3294 -0.6001 0.0537 0.2493 257 TYR B CZ 5070 O OH . TYR B 258 ? 1.4986 2.6906 3.3612 -0.5925 0.0508 0.2521 257 TYR B OH 5071 N N . THR B 259 ? 1.8315 2.5883 3.2932 -0.6354 0.1242 0.2720 258 THR B N 5072 C CA . THR B 259 ? 1.8767 2.5614 3.2596 -0.6222 0.1343 0.2715 258 THR B CA 5073 C C . THR B 259 ? 1.8662 2.5584 3.2194 -0.5791 0.1475 0.2628 258 THR B C 5074 O O . THR B 259 ? 1.8413 2.5909 3.2340 -0.5614 0.1510 0.2584 258 THR B O 5075 C CB . THR B 259 ? 1.9149 2.5843 3.2883 -0.6424 0.1654 0.2929 258 THR B CB 5076 O OG1 . THR B 259 ? 1.8941 2.6235 3.3004 -0.6309 0.2000 0.3045 258 THR B OG1 5077 C CG2 . THR B 259 ? 1.9523 2.6177 3.3609 -0.6882 0.1550 0.3035 258 THR B CG2 5078 N N . LEU B 260 ? 1.9096 2.5432 3.1934 -0.5623 0.1543 0.2605 259 LEU B N 5079 C CA . LEU B 260 ? 1.9097 2.5443 3.1602 -0.5239 0.1669 0.2526 259 LEU B CA 5080 C C . LEU B 260 ? 1.8957 2.5816 3.1710 -0.5125 0.2026 0.2635 259 LEU B C 5081 O O . LEU B 260 ? 1.8922 2.5922 3.1538 -0.4811 0.2117 0.2554 259 LEU B O 5082 C CB . LEU B 260 ? 1.9548 2.5168 3.1277 -0.5114 0.1664 0.2496 259 LEU B CB 5083 C CG . LEU B 260 ? 2.0283 2.5512 3.1691 -0.5281 0.1866 0.2668 259 LEU B CG 5084 C CD1 . LEU B 260 ? 2.0456 2.5845 3.1694 -0.5099 0.2213 0.2765 259 LEU B CD1 5085 C CD2 . LEU B 260 ? 2.0608 2.5068 3.1377 -0.5260 0.1694 0.2613 259 LEU B CD2 5086 N N . ARG B 261 ? 1.8933 2.6058 3.2041 -0.5381 0.2231 0.2817 260 ARG B N 5087 C CA . ARG B 261 ? 1.8755 2.6414 3.2148 -0.5291 0.2588 0.2932 260 ARG B CA 5088 C C . ARG B 261 ? 1.8272 2.6726 3.2451 -0.5288 0.2575 0.2918 260 ARG B C 5089 O O . ARG B 261 ? 1.8348 2.7315 3.2835 -0.5197 0.2871 0.3006 260 ARG B O 5090 C CB . ARG B 261 ? 1.9300 2.6868 3.2672 -0.5556 0.2856 0.3157 260 ARG B CB 5091 C CG . ARG B 261 ? 1.9773 2.6568 3.2363 -0.5539 0.2895 0.3196 260 ARG B CG 5092 C CD . ARG B 261 ? 2.0434 2.7186 3.2965 -0.5737 0.3230 0.3438 260 ARG B CD 5093 N NE . ARG B 261 ? 2.1142 2.7451 3.3616 -0.6096 0.3103 0.3537 260 ARG B NE 5094 C CZ . ARG B 261 ? 2.1569 2.8142 3.4632 -0.6451 0.3006 0.3606 260 ARG B CZ 5095 N NH1 . ARG B 261 ? 2.1367 2.8704 3.5174 -0.6499 0.3018 0.3600 260 ARG B NH1 5096 N NH2 . ARG B 261 ? 2.2225 2.8282 3.5130 -0.6762 0.2885 0.3683 260 ARG B NH2 5097 N N . ASP B 262 ? 1.7904 2.6459 3.2389 -0.5368 0.2236 0.2807 261 ASP B N 5098 C CA . ASP B 262 ? 1.7458 2.6766 3.2714 -0.5380 0.2173 0.2798 261 ASP B CA 5099 C C . ASP B 262 ? 1.7039 2.6461 3.2281 -0.5055 0.1968 0.2607 261 ASP B C 5100 O O . ASP B 262 ? 1.7090 2.6974 3.2876 -0.5078 0.1779 0.2563 261 ASP B O 5101 C CB . ASP B 262 ? 1.7389 2.6818 3.3119 -0.5779 0.1933 0.2847 261 ASP B CB 5102 C CG . ASP B 262 ? 1.7567 2.7016 3.3471 -0.6130 0.2153 0.3059 261 ASP B CG 5103 O OD1 . ASP B 262 ? 1.7505 2.7402 3.3683 -0.6102 0.2507 0.3203 261 ASP B OD1 5104 O OD2 . ASP B 262 ? 1.7708 2.6714 3.3469 -0.6437 0.1975 0.3084 261 ASP B OD2 5105 N N . TYR B 263 ? 1.6645 2.5655 3.1274 -0.4756 0.2004 0.2502 262 TYR B N 5106 C CA . TYR B 263 ? 1.6036 2.5068 3.0583 -0.4458 0.1816 0.2328 262 TYR B CA 5107 C C . TYR B 263 ? 1.5553 2.5292 3.0657 -0.4260 0.1939 0.2328 262 TYR B C 5108 O O . TYR B 263 ? 1.5292 2.5247 3.0642 -0.4140 0.1715 0.2227 262 TYR B O 5109 C CB . TYR B 263 ? 1.5987 2.4451 2.9783 -0.4196 0.1854 0.2228 262 TYR B CB 5110 C CG . TYR B 263 ? 1.6042 2.3798 2.9271 -0.4306 0.1658 0.2182 262 TYR B CG 5111 C CD1 . TYR B 263 ? 1.5935 2.3520 2.9237 -0.4476 0.1328 0.2118 262 TYR B CD1 5112 C CD2 . TYR B 263 ? 1.6030 2.3283 2.8630 -0.4217 0.1796 0.2195 262 TYR B CD2 5113 C CE1 . TYR B 263 ? 1.5958 2.2890 2.8728 -0.4549 0.1165 0.2070 262 TYR B CE1 5114 C CE2 . TYR B 263 ? 1.6064 2.2690 2.8161 -0.4288 0.1624 0.2155 262 TYR B CE2 5115 C CZ . TYR B 263 ? 1.6070 2.2533 2.8253 -0.4449 0.1318 0.2092 262 TYR B CZ 5116 O OH . TYR B 263 ? 1.6165 2.1997 2.7838 -0.4498 0.1160 0.2047 262 TYR B OH 5117 N N . ARG B 264 ? 1.5353 2.5444 3.0641 -0.4212 0.2296 0.2444 263 ARG B N 5118 C CA . ARG B 264 ? 1.4991 2.5753 3.0805 -0.4001 0.2438 0.2447 263 ARG B CA 5119 C C . ARG B 264 ? 1.4588 2.5939 3.1187 -0.4185 0.2245 0.2487 263 ARG B C 5120 O O . ARG B 264 ? 1.4153 2.5841 3.1064 -0.3989 0.2104 0.2403 263 ARG B O 5121 C CB . ARG B 264 ? 1.5287 2.6328 3.1155 -0.3930 0.2877 0.2573 263 ARG B CB 5122 C CG . ARG B 264 ? 1.5246 2.6836 3.1459 -0.3606 0.3049 0.2536 263 ARG B CG 5123 C CD . ARG B 264 ? 1.5707 2.7399 3.1740 -0.3462 0.3488 0.2619 263 ARG B CD 5124 N NE . ARG B 264 ? 1.6191 2.8260 3.2632 -0.3741 0.3734 0.2828 263 ARG B NE 5125 C CZ . ARG B 264 ? 1.6379 2.9215 3.3602 -0.3798 0.3870 0.2936 263 ARG B CZ 5126 N NH1 . ARG B 264 ? 1.6252 2.9575 3.3947 -0.3576 0.3776 0.2855 263 ARG B NH1 5127 N NH2 . ARG B 264 ? 1.6644 2.9773 3.4193 -0.4079 0.4104 0.3136 263 ARG B NH2 5128 N N . LYS B 265 ? 1.4573 2.6022 3.1473 -0.4565 0.2225 0.2616 264 LYS B N 5129 C CA . LYS B 265 ? 1.4437 2.6394 3.2064 -0.4804 0.1993 0.2654 264 LYS B CA 5130 C C . LYS B 265 ? 1.4362 2.6086 3.1881 -0.4758 0.1556 0.2491 264 LYS B C 5131 O O . LYS B 265 ? 1.4047 2.6271 3.2092 -0.4697 0.1376 0.2457 264 LYS B O 5132 C CB . LYS B 265 ? 1.4599 2.6481 3.2398 -0.5258 0.1988 0.2796 264 LYS B CB 5133 C CG . LYS B 265 ? 1.4650 2.7000 3.2856 -0.5404 0.2381 0.3001 264 LYS B CG 5134 C CD . LYS B 265 ? 1.4982 2.7274 3.3437 -0.5888 0.2305 0.3134 264 LYS B CD 5135 C CE . LYS B 265 ? 1.5397 2.8128 3.4237 -0.6060 0.2714 0.3361 264 LYS B CE 5136 N NZ . LYS B 265 ? 1.5950 2.8606 3.5045 -0.6559 0.2644 0.3501 264 LYS B NZ 5137 N N . PHE B 266 ? 1.4755 2.5722 3.1589 -0.4792 0.1390 0.2400 265 PHE B N 5138 C CA . PHE B 266 ? 1.5075 2.5721 3.1690 -0.4755 0.0992 0.2247 265 PHE B CA 5139 C C . PHE B 266 ? 1.5228 2.6117 3.1914 -0.4385 0.0923 0.2137 265 PHE B C 5140 O O . PHE B 266 ? 1.5181 2.6364 3.2231 -0.4377 0.0651 0.2086 265 PHE B O 5141 C CB . PHE B 266 ? 1.5272 2.5065 3.1071 -0.4766 0.0912 0.2170 265 PHE B CB 5142 C CG . PHE B 266 ? 1.5359 2.4784 3.0838 -0.4668 0.0554 0.2007 265 PHE B CG 5143 C CD1 . PHE B 266 ? 1.5479 2.4781 3.1061 -0.4922 0.0226 0.1970 265 PHE B CD1 5144 C CD2 . PHE B 266 ? 1.5438 2.4622 3.0492 -0.4327 0.0548 0.1891 265 PHE B CD2 5145 C CE1 . PHE B 266 ? 1.5462 2.4417 3.0712 -0.4820 -0.0086 0.1824 265 PHE B CE1 5146 C CE2 . PHE B 266 ? 1.5378 2.4233 3.0134 -0.4238 0.0241 0.1756 265 PHE B CE2 5147 C CZ . PHE B 266 ? 1.5358 2.4099 3.0200 -0.4476 -0.0069 0.1724 265 PHE B CZ 5148 N N . PHE B 267 ? 1.5772 2.6528 3.2104 -0.4081 0.1165 0.2105 266 PHE B N 5149 C CA . PHE B 267 ? 1.6092 2.6983 3.2413 -0.3719 0.1118 0.1999 266 PHE B CA 5150 C C . PHE B 267 ? 1.5859 2.7544 3.2946 -0.3631 0.1159 0.2054 266 PHE B C 5151 O O . PHE B 267 ? 1.5941 2.7802 3.3205 -0.3454 0.0947 0.1977 266 PHE B O 5152 C CB . PHE B 267 ? 1.6514 2.7081 3.2294 -0.3434 0.1375 0.1950 266 PHE B CB 5153 C CG . PHE B 267 ? 1.6898 2.6721 3.1932 -0.3392 0.1241 0.1845 266 PHE B CG 5154 C CD1 . PHE B 267 ? 1.6824 2.6403 3.1671 -0.3298 0.0932 0.1724 266 PHE B CD1 5155 C CD2 . PHE B 267 ? 1.7335 2.6716 3.1855 -0.3436 0.1428 0.1874 266 PHE B CD2 5156 C CE1 . PHE B 267 ? 1.6996 2.5931 3.1190 -0.3255 0.0825 0.1635 266 PHE B CE1 5157 C CE2 . PHE B 267 ? 1.7436 2.6176 3.1308 -0.3385 0.1303 0.1782 266 PHE B CE2 5158 C CZ . PHE B 267 ? 1.7293 2.5824 3.1017 -0.3296 0.1008 0.1662 266 PHE B CZ 5159 N N . GLN B 268 ? 1.5587 2.7756 3.3130 -0.3747 0.1434 0.2194 267 GLN B N 5160 C CA . GLN B 268 ? 1.5231 2.8220 3.3572 -0.3681 0.1488 0.2264 267 GLN B CA 5161 C C . GLN B 268 ? 1.5049 2.8342 3.3901 -0.3913 0.1117 0.2271 267 GLN B C 5162 O O . GLN B 268 ? 1.4612 2.8338 3.3882 -0.3744 0.0957 0.2238 267 GLN B O 5163 C CB . GLN B 268 ? 1.5324 2.8769 3.4035 -0.3772 0.1888 0.2426 267 GLN B CB 5164 C CG . GLN B 268 ? 1.5324 2.8613 3.3619 -0.3461 0.2258 0.2409 267 GLN B CG 5165 C CD . GLN B 268 ? 1.5398 2.9157 3.4039 -0.3522 0.2676 0.2572 267 GLN B CD 5166 O OE1 . GLN B 268 ? 1.5549 2.9824 3.4821 -0.3795 0.2705 0.2712 267 GLN B OE1 5167 N NE2 . GLN B 268 ? 1.5376 2.8958 3.3596 -0.3269 0.3003 0.2557 267 GLN B NE2 5168 N N . ASP B 269 ? 1.5262 2.8282 3.4035 -0.4289 0.0963 0.2305 268 ASP B N 5169 C CA . ASP B 269 ? 1.5435 2.8724 3.4685 -0.4566 0.0609 0.2314 268 ASP B CA 5170 C C . ASP B 269 ? 1.5063 2.8062 3.4055 -0.4441 0.0202 0.2160 268 ASP B C 5171 O O . ASP B 269 ? 1.4975 2.8387 3.4461 -0.4515 -0.0081 0.2154 268 ASP B O 5172 C CB . ASP B 269 ? 1.6100 2.9090 3.5270 -0.5010 0.0567 0.2385 268 ASP B CB 5173 C CG . ASP B 269 ? 1.6648 3.0091 3.6282 -0.5213 0.0919 0.2573 268 ASP B CG 5174 O OD1 . ASP B 269 ? 1.6943 3.0794 3.6780 -0.4975 0.1255 0.2636 268 ASP B OD1 5175 O OD2 . ASP B 269 ? 1.7175 3.0545 3.6954 -0.5612 0.0867 0.2659 268 ASP B OD2 5176 N N . ILE B 270 ? 1.4852 2.7159 3.3078 -0.4256 0.0171 0.2043 269 ILE B N 5177 C CA . ILE B 270 ? 1.4699 2.6695 3.2617 -0.4114 -0.0178 0.1905 269 ILE B CA 5178 C C . ILE B 270 ? 1.4342 2.6579 3.2333 -0.3705 -0.0149 0.1854 269 ILE B C 5179 O O . ILE B 270 ? 1.4180 2.6217 3.1958 -0.3560 -0.0422 0.1756 269 ILE B O 5180 C CB . ILE B 270 ? 1.4859 2.5984 3.1934 -0.4145 -0.0268 0.1805 269 ILE B CB 5181 C CG1 . ILE B 270 ? 1.4819 2.5578 3.1365 -0.3905 0.0044 0.1785 269 ILE B CG1 5182 C CG2 . ILE B 270 ? 1.5202 2.6046 3.2199 -0.4545 -0.0353 0.1844 269 ILE B CG2 5183 C CD1 . ILE B 270 ? 1.4642 2.4999 3.0673 -0.3600 -0.0066 0.1656 269 ILE B CD1 5184 N N . GLY B 271 ? 1.4227 2.6869 3.2496 -0.3516 0.0183 0.1921 270 GLY B N 5185 C CA . GLY B 271 ? 1.4183 2.7088 3.2579 -0.3124 0.0236 0.1882 270 GLY B CA 5186 C C . GLY B 271 ? 1.4267 2.6551 3.1931 -0.2842 0.0304 0.1770 270 GLY B C 5187 O O . GLY B 271 ? 1.4138 2.6359 3.1702 -0.2583 0.0156 0.1694 270 GLY B O 5188 N N . PHE B 272 ? 1.4471 2.6299 3.1629 -0.2896 0.0524 0.1764 271 PHE B N 5189 C CA . PHE B 272 ? 1.4419 2.5675 3.0897 -0.2653 0.0603 0.1662 271 PHE B CA 5190 C C . PHE B 272 ? 1.4414 2.5559 3.0650 -0.2609 0.0985 0.1700 271 PHE B C 5191 O O . PHE B 272 ? 1.4096 2.4743 2.9824 -0.2729 0.1043 0.1689 271 PHE B O 5192 C CB . PHE B 272 ? 1.4518 2.5123 3.0421 -0.2775 0.0345 0.1578 271 PHE B CB 5193 C CG . PHE B 272 ? 1.4645 2.4723 2.9925 -0.2525 0.0362 0.1471 271 PHE B CG 5194 C CD1 . PHE B 272 ? 1.4621 2.4772 2.9927 -0.2232 0.0293 0.1411 271 PHE B CD1 5195 C CD2 . PHE B 272 ? 1.4828 2.4336 2.9505 -0.2587 0.0437 0.1436 271 PHE B CD2 5196 C CE1 . PHE B 272 ? 1.4703 2.4369 2.9456 -0.2027 0.0305 0.1319 271 PHE B CE1 5197 C CE2 . PHE B 272 ? 1.4986 2.4047 2.9131 -0.2373 0.0443 0.1341 271 PHE B CE2 5198 C CZ . PHE B 272 ? 1.4935 2.4074 2.9123 -0.2105 0.0379 0.1282 271 PHE B CZ 5199 N N . GLU B 273 ? 1.4680 2.6292 3.1271 -0.2419 0.1244 0.1746 272 GLU B N 5200 C CA . GLU B 273 ? 1.5107 2.6671 3.1490 -0.2352 0.1625 0.1785 272 GLU B CA 5201 C C . GLU B 273 ? 1.4911 2.5826 3.0533 -0.2163 0.1685 0.1672 272 GLU B C 5202 O O . GLU B 273 ? 1.4762 2.5413 3.0009 -0.2206 0.1907 0.1695 272 GLU B O 5203 C CB . GLU B 273 ? 1.5703 2.7902 3.2608 -0.2140 0.1886 0.1842 272 GLU B CB 5204 C CG . GLU B 273 ? 1.6215 2.9136 3.3927 -0.2344 0.1889 0.1978 272 GLU B CG 5205 C CD . GLU B 273 ? 1.6690 3.0235 3.4880 -0.2162 0.2239 0.2060 272 GLU B CD 5206 O OE1 . GLU B 273 ? 1.7163 3.0580 3.5055 -0.2090 0.2578 0.2083 272 GLU B OE1 5207 O OE2 . GLU B 273 ? 1.6896 3.1074 3.5760 -0.2085 0.2177 0.2104 272 GLU B OE2 5208 N N . ASP B 274 ? 1.4708 2.5371 3.0104 -0.1963 0.1482 0.1558 273 ASP B N 5209 C CA . ASP B 274 ? 1.4688 2.4744 2.9394 -0.1803 0.1498 0.1447 273 ASP B CA 5210 C C . ASP B 274 ? 1.4639 2.4183 2.8847 -0.2027 0.1452 0.1447 273 ASP B C 5211 O O . ASP B 274 ? 1.4673 2.3827 2.8370 -0.1951 0.1592 0.1405 273 ASP B O 5212 C CB . ASP B 274 ? 1.4625 2.4486 2.9209 -0.1625 0.1234 0.1346 273 ASP B CB 5213 C CG . ASP B 274 ? 1.4694 2.4969 2.9686 -0.1354 0.1272 0.1336 273 ASP B CG 5214 O OD1 . ASP B 274 ? 1.4721 2.5583 3.0305 -0.1380 0.1360 0.1424 273 ASP B OD1 5215 O OD2 . ASP B 274 ? 1.4795 2.4809 2.9525 -0.1115 0.1211 0.1244 273 ASP B OD2 5216 N N . GLY B 275 ? 1.4493 2.4029 2.8842 -0.2295 0.1246 0.1492 274 GLY B N 5217 C CA . GLY B 275 ? 1.4571 2.3611 2.8466 -0.2501 0.1183 0.1494 274 GLY B CA 5218 C C . GLY B 275 ? 1.4692 2.3670 2.8429 -0.2606 0.1471 0.1580 274 GLY B C 5219 O O . GLY B 275 ? 1.4636 2.3124 2.7834 -0.2636 0.1500 0.1558 274 GLY B O 5220 N N . TRP B 276 ? 1.4657 2.4141 2.8865 -0.2658 0.1686 0.1686 275 TRP B N 5221 C CA . TRP B 276 ? 1.4788 2.4261 2.8868 -0.2743 0.1997 0.1787 275 TRP B CA 5222 C C . TRP B 276 ? 1.4645 2.3843 2.8218 -0.2473 0.2198 0.1714 275 TRP B C 5223 O O . TRP B 276 ? 1.4922 2.3742 2.8016 -0.2517 0.2322 0.1736 275 TRP B O 5224 C CB . TRP B 276 ? 1.4901 2.5049 2.9652 -0.2828 0.2197 0.1918 275 TRP B CB 5225 C CG . TRP B 276 ? 1.5184 2.5405 2.9856 -0.2892 0.2561 0.2040 275 TRP B CG 5226 C CD1 . TRP B 276 ? 1.5190 2.5849 3.0116 -0.2735 0.2882 0.2096 275 TRP B CD1 5227 C CD2 . TRP B 276 ? 1.5404 2.5242 2.9706 -0.3119 0.2646 0.2127 275 TRP B CD2 5228 N NE1 . TRP B 276 ? 1.5311 2.5888 3.0033 -0.2855 0.3166 0.2215 275 TRP B NE1 5229 C CE2 . TRP B 276 ? 1.5511 2.5579 2.9850 -0.3093 0.3024 0.2240 275 TRP B CE2 5230 C CE3 . TRP B 276 ? 1.5503 2.4809 2.9426 -0.3327 0.2446 0.2121 275 TRP B CE3 5231 C CZ2 . TRP B 276 ? 1.5877 2.5656 2.9881 -0.3276 0.3199 0.2358 275 TRP B CZ2 5232 C CZ3 . TRP B 276 ? 1.5764 2.4778 2.9368 -0.3499 0.2617 0.2234 275 TRP B CZ3 5233 C CH2 . TRP B 276 ? 1.6004 2.5251 2.9648 -0.3477 0.2986 0.2355 275 TRP B CH2 5234 N N . LEU B 277 ? 1.4155 2.3517 2.7819 -0.2192 0.2210 0.1624 276 LEU B N 5235 C CA . LEU B 277 ? 1.4010 2.3101 2.7205 -0.1926 0.2368 0.1532 276 LEU B CA 5236 C C . LEU B 277 ? 1.3942 2.2398 2.6508 -0.1926 0.2189 0.1438 276 LEU B C 5237 O O . LEU B 277 ? 1.4253 2.2377 2.6325 -0.1868 0.2325 0.1415 276 LEU B O 5238 C CB . LEU B 277 ? 1.3734 2.3096 2.7175 -0.1634 0.2380 0.1450 276 LEU B CB 5239 C CG . LEU B 277 ? 1.3534 2.3581 2.7656 -0.1591 0.2539 0.1538 276 LEU B CG 5240 C CD1 . LEU B 277 ? 1.3480 2.3713 2.7805 -0.1287 0.2490 0.1447 276 LEU B CD1 5241 C CD2 . LEU B 277 ? 1.3655 2.3905 2.7777 -0.1581 0.2918 0.1626 276 LEU B CD2 5242 N N . MET B 278 ? 1.3541 2.1847 2.6131 -0.1991 0.1884 0.1388 277 MET B N 5243 C CA . MET B 278 ? 1.3374 2.1123 2.5429 -0.2011 0.1702 0.1312 277 MET B CA 5244 C C . MET B 278 ? 1.3321 2.0764 2.5040 -0.2205 0.1768 0.1383 277 MET B C 5245 O O . MET B 278 ? 1.2997 2.0034 2.4199 -0.2140 0.1794 0.1337 277 MET B O 5246 C CB . MET B 278 ? 1.3483 2.1179 2.5675 -0.2087 0.1382 0.1274 277 MET B CB 5247 C CG . MET B 278 ? 1.3656 2.1480 2.6010 -0.1873 0.1259 0.1191 277 MET B CG 5248 S SD . MET B 278 ? 1.3815 2.1538 2.6253 -0.1972 0.0885 0.1159 277 MET B SD 5249 C CE . MET B 278 ? 1.3617 2.1430 2.6148 -0.1677 0.0803 0.1076 277 MET B CE 5250 N N . ARG B 279 ? 1.3549 2.1185 2.5571 -0.2447 0.1786 0.1498 278 ARG B N 5251 C CA . ARG B 279 ? 1.3974 2.1307 2.5701 -0.2645 0.1850 0.1584 278 ARG B CA 5252 C C . ARG B 279 ? 1.4103 2.1371 2.5529 -0.2552 0.2151 0.1629 278 ARG B C 5253 O O . ARG B 279 ? 1.4177 2.1016 2.5090 -0.2558 0.2171 0.1629 278 ARG B O 5254 C CB . ARG B 279 ? 1.4188 2.1767 2.6349 -0.2937 0.1824 0.1706 278 ARG B CB 5255 C CG . ARG B 279 ? 1.4505 2.1754 2.6384 -0.3159 0.1895 0.1811 278 ARG B CG 5256 C CD . ARG B 279 ? 1.4398 2.1062 2.5769 -0.3183 0.1679 0.1742 278 ARG B CD 5257 N NE . ARG B 279 ? 1.4467 2.0814 2.5619 -0.3407 0.1720 0.1850 278 ARG B NE 5258 C CZ . ARG B 279 ? 1.4350 2.0181 2.5081 -0.3461 0.1559 0.1820 278 ARG B CZ 5259 N NH1 . ARG B 279 ? 1.4042 1.9639 2.4533 -0.3315 0.1351 0.1687 278 ARG B NH1 5260 N NH2 . ARG B 279 ? 1.4578 2.0122 2.5126 -0.3658 0.1614 0.1929 278 ARG B NH2 5261 N N . GLN B 280 ? 1.4146 2.1842 2.5881 -0.2455 0.2383 0.1667 279 GLN B N 5262 C CA . GLN B 280 ? 1.4601 2.2251 2.6029 -0.2337 0.2681 0.1699 279 GLN B CA 5263 C C . GLN B 280 ? 1.4517 2.1758 2.5373 -0.2108 0.2642 0.1562 279 GLN B C 5264 O O . GLN B 280 ? 1.4626 2.1576 2.5009 -0.2082 0.2771 0.1582 279 GLN B O 5265 C CB . GLN B 280 ? 1.5003 2.3202 2.6872 -0.2228 0.2935 0.1744 279 GLN B CB 5266 C CG . GLN B 280 ? 1.5362 2.3986 2.7757 -0.2473 0.3056 0.1914 279 GLN B CG 5267 C CD . GLN B 280 ? 1.5648 2.4884 2.8553 -0.2348 0.3298 0.1957 279 GLN B CD 5268 O OE1 . GLN B 280 ? 1.5720 2.5202 2.8893 -0.2152 0.3223 0.1863 279 GLN B OE1 5269 N NE2 . GLN B 280 ? 1.5956 2.5442 2.9000 -0.2456 0.3596 0.2108 279 GLN B NE2 5270 N N . ASP B 281 ? 1.4387 2.1605 2.5286 -0.1952 0.2458 0.1429 280 ASP B N 5271 C CA . ASP B 281 ? 1.4567 2.1406 2.4969 -0.1758 0.2390 0.1294 280 ASP B CA 5272 C C . ASP B 281 ? 1.4593 2.0951 2.4524 -0.1858 0.2243 0.1289 280 ASP B C 5273 O O . ASP B 281 ? 1.4765 2.0818 2.4216 -0.1750 0.2283 0.1235 280 ASP B O 5274 C CB . ASP B 281 ? 1.4462 2.1347 2.5035 -0.1613 0.2194 0.1174 280 ASP B CB 5275 C CG . ASP B 281 ? 1.4559 2.1864 2.5531 -0.1445 0.2328 0.1155 280 ASP B CG 5276 O OD1 . ASP B 281 ? 1.4850 2.2284 2.5763 -0.1335 0.2592 0.1170 280 ASP B OD1 5277 O OD2 . ASP B 281 ? 1.4330 2.1827 2.5658 -0.1407 0.2169 0.1125 280 ASP B OD2 5278 N N . THR B 282 ? 1.4521 2.0814 2.4588 -0.2056 0.2067 0.1342 281 THR B N 5279 C CA . THR B 282 ? 1.4551 2.0396 2.4219 -0.2113 0.1879 0.1313 281 THR B CA 5280 C C . THR B 282 ? 1.4777 2.0382 2.4211 -0.2292 0.1931 0.1428 281 THR B C 5281 O O . THR B 282 ? 1.4766 1.9981 2.3776 -0.2278 0.1835 0.1404 281 THR B O 5282 C CB . THR B 282 ? 1.4323 2.0131 2.4180 -0.2179 0.1600 0.1264 281 THR B CB 5283 O OG1 . THR B 282 ? 1.4355 2.0378 2.4608 -0.2388 0.1560 0.1354 281 THR B OG1 5284 C CG2 . THR B 282 ? 1.4161 2.0117 2.4181 -0.1999 0.1507 0.1153 281 THR B CG2 5285 N N . GLU B 283 ? 1.4889 2.0720 2.4603 -0.2459 0.2076 0.1558 282 GLU B N 5286 C CA . GLU B 283 ? 1.5176 2.0751 2.4709 -0.2662 0.2099 0.1679 282 GLU B CA 5287 C C . GLU B 283 ? 1.5541 2.0777 2.4511 -0.2583 0.2233 0.1714 282 GLU B C 5288 O O . GLU B 283 ? 1.5928 2.0810 2.4606 -0.2692 0.2183 0.1782 282 GLU B O 5289 C CB . GLU B 283 ? 1.5387 2.1289 2.5369 -0.2881 0.2232 0.1821 282 GLU B CB 5290 C CG . GLU B 283 ? 1.5603 2.1799 2.5670 -0.2838 0.2559 0.1914 282 GLU B CG 5291 C CD . GLU B 283 ? 1.5831 2.2299 2.6309 -0.3098 0.2692 0.2082 282 GLU B CD 5292 O OE1 . GLU B 283 ? 1.5719 2.2410 2.6663 -0.3258 0.2537 0.2088 282 GLU B OE1 5293 O OE2 . GLU B 283 ? 1.6115 2.2577 2.6448 -0.3150 0.2949 0.2212 282 GLU B OE2 5294 N N . GLY B 284 ? 1.5629 2.0950 2.4426 -0.2385 0.2389 0.1664 283 GLY B N 5295 C CA . GLY B 284 ? 1.6163 2.1182 2.4406 -0.2293 0.2505 0.1687 283 GLY B CA 5296 C C . GLY B 284 ? 1.6351 2.1050 2.4171 -0.2125 0.2333 0.1556 283 GLY B C 5297 O O . GLY B 284 ? 1.6636 2.1092 2.3991 -0.2039 0.2399 0.1566 283 GLY B O 5298 N N . LEU B 285 ? 1.6352 2.1052 2.4326 -0.2082 0.2110 0.1440 284 LEU B N 5299 C CA . LEU B 285 ? 1.6644 2.1105 2.4287 -0.1925 0.1956 0.1313 284 LEU B CA 5300 C C . LEU B 285 ? 1.6661 2.0730 2.3862 -0.1946 0.1867 0.1351 284 LEU B C 5301 O O . LEU B 285 ? 1.6497 2.0389 2.3305 -0.1818 0.1873 0.1307 284 LEU B O 5302 C CB . LEU B 285 ? 1.6746 2.1281 2.4656 -0.1900 0.1742 0.1207 284 LEU B CB 5303 C CG . LEU B 285 ? 1.7000 2.1825 2.5190 -0.1773 0.1779 0.1114 284 LEU B CG 5304 C CD1 . LEU B 285 ? 1.7042 2.1906 2.5474 -0.1769 0.1559 0.1040 284 LEU B CD1 5305 C CD2 . LEU B 285 ? 1.7144 2.1868 2.5001 -0.1584 0.1852 0.1019 284 LEU B CD2 5306 N N . VAL B 286 ? 1.6854 2.0782 2.4117 -0.2101 0.1773 0.1428 285 VAL B N 5307 C CA . VAL B 286 ? 1.7415 2.0959 2.4284 -0.2111 0.1680 0.1470 285 VAL B CA 5308 C C . VAL B 286 ? 1.8098 2.1512 2.4777 -0.2212 0.1857 0.1630 285 VAL B C 5309 O O . VAL B 286 ? 1.8242 2.1765 2.5189 -0.2385 0.1943 0.1730 285 VAL B O 5310 C CB . VAL B 286 ? 1.7227 2.0625 2.4216 -0.2203 0.1469 0.1454 285 VAL B CB 5311 C CG1 . VAL B 286 ? 1.7466 2.0466 2.4040 -0.2172 0.1373 0.1487 285 VAL B CG1 5312 C CG2 . VAL B 286 ? 1.6734 2.0286 2.3938 -0.2117 0.1314 0.1315 285 VAL B CG2 5313 N N . GLU B 287 ? 1.8551 2.1733 2.4767 -0.2110 0.1906 0.1661 286 GLU B N 5314 C CA . GLU B 287 ? 1.9123 2.2119 2.5082 -0.2193 0.2066 0.1826 286 GLU B CA 5315 C C . GLU B 287 ? 1.8859 2.1557 2.4790 -0.2341 0.1955 0.1916 286 GLU B C 5316 O O . GLU B 287 ? 1.8388 2.0817 2.4091 -0.2268 0.1776 0.1873 286 GLU B O 5317 C CB . GLU B 287 ? 1.9997 2.2787 2.5423 -0.2028 0.2106 0.1830 286 GLU B CB 5318 C CG . GLU B 287 ? 2.0646 2.3670 2.6020 -0.1895 0.2253 0.1757 286 GLU B CG 5319 C CD . GLU B 287 ? 2.1600 2.4412 2.6431 -0.1725 0.2237 0.1728 286 GLU B CD 5320 O OE1 . GLU B 287 ? 2.1872 2.4520 2.6533 -0.1636 0.2025 0.1646 286 GLU B OE1 5321 O OE2 . GLU B 287 ? 2.2684 2.5504 2.7257 -0.1677 0.2436 0.1787 286 GLU B OE2 5322 N N . ALA B 288 ? 1.9071 2.1818 2.5238 -0.2546 0.2065 0.2039 287 ALA B N 5323 C CA . ALA B 288 ? 1.9610 2.2085 2.5823 -0.2720 0.1952 0.2108 287 ALA B CA 5324 C C . ALA B 288 ? 1.9840 2.1821 2.5548 -0.2662 0.1880 0.2173 287 ALA B C 5325 O O . ALA B 288 ? 1.9733 2.1450 2.5388 -0.2681 0.1696 0.2138 287 ALA B O 5326 C CB . ALA B 288 ? 2.0234 2.2839 2.6747 -0.2965 0.2114 0.2250 287 ALA B CB 5327 N N . THR B 289 ? 1.9882 2.1734 2.5203 -0.2576 0.2023 0.2265 288 THR B N 5328 C CA . THR B 289 ? 2.0069 2.1451 2.4902 -0.2528 0.1985 0.2367 288 THR B CA 5329 C C . THR B 289 ? 1.9939 2.1184 2.4410 -0.2279 0.1836 0.2272 288 THR B C 5330 O O . THR B 289 ? 2.0321 2.1190 2.4465 -0.2219 0.1734 0.2324 288 THR B O 5331 C CB . THR B 289 ? 2.0408 2.1675 2.4981 -0.2594 0.2227 0.2559 288 THR B CB 5332 O OG1 . THR B 289 ? 2.0362 2.1948 2.4910 -0.2485 0.2390 0.2527 288 THR B OG1 5333 C CG2 . THR B 289 ? 2.0298 2.1575 2.5175 -0.2876 0.2350 0.2695 288 THR B CG2 5334 N N . MET B 290 ? 1.9556 2.1100 2.4094 -0.2136 0.1818 0.2136 289 MET B N 5335 C CA . MET B 290 ? 1.9435 2.0901 2.3670 -0.1918 0.1675 0.2043 289 MET B CA 5336 C C . MET B 290 ? 1.8313 1.9680 2.2648 -0.1873 0.1442 0.1947 289 MET B C 5337 O O . MET B 290 ? 1.7729 1.9311 2.2434 -0.1919 0.1369 0.1839 289 MET B O 5338 C CB . MET B 290 ? 1.9729 2.1528 2.4037 -0.1805 0.1715 0.1913 289 MET B CB 5339 C CG . MET B 290 ? 2.0542 2.2439 2.4690 -0.1803 0.1953 0.1988 289 MET B CG 5340 S SD . MET B 290 ? 2.1977 2.3506 2.5475 -0.1714 0.2020 0.2142 289 MET B SD 5341 C CE . MET B 290 ? 2.1897 2.3389 2.5108 -0.1479 0.1788 0.1990 289 MET B CE 5342 N N . PRO B 291 ? 1.7838 1.8882 2.1834 -0.1770 0.1329 0.1991 290 PRO B N 5343 C CA . PRO B 291 ? 1.7150 1.8115 2.1223 -0.1700 0.1126 0.1900 290 PRO B CA 5344 C C . PRO B 291 ? 1.6355 1.7585 2.0508 -0.1550 0.1010 0.1746 290 PRO B C 5345 O O . PRO B 291 ? 1.5831 1.7225 1.9880 -0.1475 0.1064 0.1714 290 PRO B O 5346 C CB . PRO B 291 ? 1.7764 1.8319 2.1429 -0.1607 0.1066 0.2008 290 PRO B CB 5347 C CG . PRO B 291 ? 1.8413 1.8806 2.1791 -0.1654 0.1237 0.2167 290 PRO B CG 5348 C CD . PRO B 291 ? 1.8353 1.9095 2.1880 -0.1699 0.1386 0.2131 290 PRO B CD 5349 N N . PRO B 292 ? 1.5767 1.7024 2.0088 -0.1509 0.0855 0.1651 291 PRO B N 5350 C CA . PRO B 292 ? 1.5247 1.6747 1.9659 -0.1384 0.0747 0.1518 291 PRO B CA 5351 C C . PRO B 292 ? 1.5279 1.6719 1.9365 -0.1209 0.0671 0.1525 291 PRO B C 5352 O O . PRO B 292 ? 1.5004 1.6661 1.9125 -0.1130 0.0615 0.1427 291 PRO B O 5353 C CB . PRO B 292 ? 1.4893 1.6389 1.9525 -0.1390 0.0618 0.1448 291 PRO B CB 5354 C CG . PRO B 292 ? 1.5195 1.6348 1.9700 -0.1451 0.0618 0.1545 291 PRO B CG 5355 C CD . PRO B 292 ? 1.5638 1.6703 2.0073 -0.1584 0.0778 0.1660 291 PRO B CD 5356 N N . GLY B 293 ? 1.5552 1.6691 1.9324 -0.1151 0.0659 0.1640 292 GLY B N 5357 C CA . GLY B 293 ? 1.5574 1.6656 1.9023 -0.0979 0.0579 0.1666 292 GLY B CA 5358 C C . GLY B 293 ? 1.5337 1.6489 1.8848 -0.0839 0.0399 0.1595 292 GLY B C 5359 O O . GLY B 293 ? 1.4917 1.6175 1.8290 -0.0707 0.0305 0.1568 292 GLY B O 5360 N N . VAL B 294 ? 1.5365 1.6467 1.9083 -0.0869 0.0352 0.1565 293 VAL B N 5361 C CA . VAL B 294 ? 1.5365 1.6531 1.9157 -0.0733 0.0207 0.1510 293 VAL B CA 5362 C C . VAL B 294 ? 1.5680 1.6541 1.9421 -0.0718 0.0188 0.1562 293 VAL B C 5363 O O . VAL B 294 ? 1.5740 1.6375 1.9462 -0.0851 0.0272 0.1616 293 VAL B O 5364 C CB . VAL B 294 ? 1.4887 1.6386 1.9035 -0.0769 0.0159 0.1371 293 VAL B CB 5365 C CG1 . VAL B 294 ? 1.4858 1.6622 1.9030 -0.0762 0.0152 0.1304 293 VAL B CG1 5366 C CG2 . VAL B 294 ? 1.4714 1.6215 1.9110 -0.0934 0.0230 0.1337 293 VAL B CG2 5367 N N . GLN B 295 ? 1.5846 1.6703 1.9570 -0.0557 0.0079 0.1544 294 GLN B N 5368 C CA . GLN B 295 ? 1.6313 1.6860 1.9960 -0.0510 0.0057 0.1576 294 GLN B CA 5369 C C . GLN B 295 ? 1.5875 1.6425 1.9766 -0.0673 0.0089 0.1502 294 GLN B C 5370 O O . GLN B 295 ? 1.5614 1.6466 1.9777 -0.0699 0.0060 0.1400 294 GLN B O 5371 C CB . GLN B 295 ? 1.6853 1.7480 2.0497 -0.0294 -0.0051 0.1551 294 GLN B CB 5372 C CG . GLN B 295 ? 1.7820 1.8069 2.1303 -0.0199 -0.0067 0.1589 294 GLN B CG 5373 C CD . GLN B 295 ? 1.8209 1.8597 2.1759 0.0013 -0.0152 0.1548 294 GLN B CD 5374 O OE1 . GLN B 295 ? 1.8902 1.9067 2.2405 0.0080 -0.0157 0.1530 294 GLN B OE1 5375 N NE2 . GLN B 295 ? 1.8111 1.8871 2.1772 0.0118 -0.0216 0.1532 294 GLN B NE2 5376 N N . LEU B 296 ? 1.6102 1.6306 1.9888 -0.0784 0.0140 0.1558 295 LEU B N 5377 C CA . LEU B 296 ? 1.6094 1.6294 2.0100 -0.0970 0.0164 0.1500 295 LEU B CA 5378 C C . LEU B 296 ? 1.6308 1.6131 2.0195 -0.0956 0.0116 0.1495 295 LEU B C 5379 O O . LEU B 296 ? 1.6668 1.6096 2.0268 -0.0909 0.0124 0.1583 295 LEU B O 5380 C CB . LEU B 296 ? 1.6455 1.6626 2.0496 -0.1172 0.0277 0.1566 295 LEU B CB 5381 C CG . LEU B 296 ? 1.6713 1.6879 2.0993 -0.1388 0.0301 0.1530 295 LEU B CG 5382 C CD1 . LEU B 296 ? 1.6350 1.6875 2.0952 -0.1398 0.0246 0.1400 295 LEU B CD1 5383 C CD2 . LEU B 296 ? 1.6884 1.7081 2.1214 -0.1568 0.0432 0.1615 295 LEU B CD2 5384 N N . HIS B 297 ? 1.6356 1.6279 2.0439 -0.0992 0.0065 0.1391 296 HIS B N 5385 C CA . HIS B 297 ? 1.6984 1.6549 2.0952 -0.1002 0.0015 0.1361 296 HIS B CA 5386 C C . HIS B 297 ? 1.6998 1.6602 2.1187 -0.1238 0.0015 0.1311 296 HIS B C 5387 O O . HIS B 297 ? 1.6667 1.6599 2.1117 -0.1275 -0.0009 0.1227 296 HIS B O 5388 C CB . HIS B 297 ? 1.7172 1.6809 2.1128 -0.0800 -0.0054 0.1282 296 HIS B CB 5389 C CG . HIS B 297 ? 1.7496 1.7144 2.1283 -0.0560 -0.0064 0.1334 296 HIS B CG 5390 N ND1 . HIS B 297 ? 1.8110 1.7373 2.1603 -0.0394 -0.0087 0.1374 296 HIS B ND1 5391 C CD2 . HIS B 297 ? 1.7369 1.7366 2.1241 -0.0457 -0.0066 0.1351 296 HIS B CD2 5392 C CE1 . HIS B 297 ? 1.8244 1.7653 2.1672 -0.0189 -0.0102 0.1421 296 HIS B CE1 5393 N NE2 . HIS B 297 ? 1.7785 1.7641 2.1441 -0.0233 -0.0096 0.1406 296 HIS B NE2 5394 N N . CYS B 298 ? 1.7441 1.6713 2.1533 -0.1403 0.0040 0.1371 297 CYS B N 5395 C CA . CYS B 298 ? 1.7499 1.6822 2.1825 -0.1648 0.0031 0.1337 297 CYS B CA 5396 C C . CYS B 298 ? 1.7743 1.6720 2.1962 -0.1688 -0.0072 0.1263 297 CYS B C 5397 O O . CYS B 298 ? 1.8468 1.6968 2.2425 -0.1718 -0.0087 0.1306 297 CYS B O 5398 C CB . CYS B 298 ? 1.7825 1.7064 2.2173 -0.1845 0.0130 0.1452 297 CYS B CB 5399 S SG . CYS B 298 ? 1.7499 1.7215 2.2032 -0.1844 0.0258 0.1507 297 CYS B SG 5400 N N . LEU B 299 ? 1.7383 1.6580 2.1782 -0.1684 -0.0146 0.1151 298 LEU B N 5401 C CA . LEU B 299 ? 1.7774 1.6679 2.2066 -0.1719 -0.0256 0.1062 298 LEU B CA 5402 C C . LEU B 299 ? 1.7774 1.6773 2.2326 -0.1988 -0.0303 0.1036 298 LEU B C 5403 O O . LEU B 299 ? 1.7515 1.6960 2.2400 -0.2060 -0.0286 0.1022 298 LEU B O 5404 C CB . LEU B 299 ? 1.7688 1.6760 2.1972 -0.1527 -0.0310 0.0961 298 LEU B CB 5405 C CG . LEU B 299 ? 1.7936 1.6816 2.1927 -0.1254 -0.0297 0.0964 298 LEU B CG 5406 C CD1 . LEU B 299 ? 1.8009 1.7026 2.1982 -0.1148 -0.0209 0.1066 298 LEU B CD1 5407 C CD2 . LEU B 299 ? 1.7669 1.6777 2.1707 -0.1093 -0.0330 0.0874 298 LEU B CD2 5408 N N . TYR B 300 ? 1.8043 1.6617 2.2448 -0.2134 -0.0371 0.1028 299 TYR B N 5409 C CA . TYR B 300 ? 1.8215 1.6865 2.2877 -0.2409 -0.0438 0.1006 299 TYR B CA 5410 C C . TYR B 300 ? 1.8602 1.6838 2.3060 -0.2468 -0.0595 0.0901 299 TYR B C 5411 O O . TYR B 300 ? 1.8858 1.6578 2.2938 -0.2387 -0.0619 0.0892 299 TYR B O 5412 C CB . TYR B 300 ? 1.8509 1.7103 2.3276 -0.2625 -0.0346 0.1135 299 TYR B CB 5413 C CG . TYR B 300 ? 1.9158 1.7165 2.3547 -0.2626 -0.0321 0.1209 299 TYR B CG 5414 C CD1 . TYR B 300 ? 1.9229 1.7131 2.3386 -0.2440 -0.0211 0.1301 299 TYR B CD1 5415 C CD2 . TYR B 300 ? 1.9512 1.7052 2.3766 -0.2813 -0.0418 0.1188 299 TYR B CD2 5416 C CE1 . TYR B 300 ? 1.9558 1.6901 2.3353 -0.2424 -0.0190 0.1380 299 TYR B CE1 5417 C CE2 . TYR B 300 ? 1.9897 1.6851 2.3786 -0.2812 -0.0396 0.1260 299 TYR B CE2 5418 C CZ . TYR B 300 ? 1.9967 1.6822 2.3625 -0.2609 -0.0277 0.1360 299 TYR B CZ 5419 O OH . TYR B 300 ? 2.0526 1.6778 2.3806 -0.2593 -0.0258 0.1441 299 TYR B OH 5420 N N . GLY B 301 ? 1.8509 1.6960 2.3200 -0.2599 -0.0707 0.0820 300 GLY B N 5421 C CA . GLY B 301 ? 1.8963 1.7040 2.3466 -0.2682 -0.0878 0.0709 300 GLY B CA 5422 C C . GLY B 301 ? 1.9494 1.7299 2.4059 -0.2990 -0.0938 0.0746 300 GLY B C 5423 O O . GLY B 301 ? 1.9203 1.7319 2.4129 -0.3188 -0.0873 0.0839 300 GLY B O 5424 N N . THR B 302 ? 2.0303 1.7523 2.4515 -0.3032 -0.1057 0.0673 301 THR B N 5425 C CA . THR B 302 ? 2.0848 1.7733 2.5083 -0.3344 -0.1139 0.0696 301 THR B CA 5426 C C . THR B 302 ? 2.1210 1.7729 2.5230 -0.3422 -0.1362 0.0537 301 THR B C 5427 O O . THR B 302 ? 2.0800 1.7256 2.4579 -0.3203 -0.1428 0.0419 301 THR B O 5428 C CB . THR B 302 ? 2.1417 1.7772 2.5343 -0.3347 -0.1038 0.0800 301 THR B CB 5429 O OG1 . THR B 302 ? 2.1834 1.7643 2.5239 -0.3102 -0.1076 0.0719 301 THR B OG1 5430 C CG2 . THR B 302 ? 2.1085 1.7770 2.5160 -0.3253 -0.0826 0.0956 301 THR B CG2 5431 N N . GLY B 303 ? 2.1809 1.8089 2.5913 -0.3742 -0.1475 0.0538 302 GLY B N 5432 C CA . GLY B 303 ? 2.2500 1.8361 2.6372 -0.3859 -0.1710 0.0384 302 GLY B CA 5433 C C . GLY B 303 ? 2.2198 1.8511 2.6359 -0.3933 -0.1874 0.0285 302 GLY B C 5434 O O . GLY B 303 ? 2.2784 1.8785 2.6692 -0.3961 -0.2078 0.0136 302 GLY B O 5435 N N . VAL B 304 ? 2.1437 1.8459 2.6103 -0.3956 -0.1793 0.0365 303 VAL B N 5436 C CA . VAL B 304 ? 2.1098 1.8594 2.6070 -0.4003 -0.1940 0.0291 303 VAL B CA 5437 C C . VAL B 304 ? 2.0738 1.8678 2.6296 -0.4327 -0.1965 0.0380 303 VAL B C 5438 O O . VAL B 304 ? 2.0329 1.8596 2.6195 -0.4363 -0.1770 0.0523 303 VAL B O 5439 C CB . VAL B 304 ? 2.0681 1.8664 2.5753 -0.3710 -0.1821 0.0302 303 VAL B CB 5440 C CG1 . VAL B 304 ? 2.0570 1.8966 2.5887 -0.3731 -0.1984 0.0226 303 VAL B CG1 5441 C CG2 . VAL B 304 ? 2.0794 1.8409 2.5350 -0.3387 -0.1750 0.0246 303 VAL B CG2 5442 N N . PRO B 305 ? 2.0732 1.8707 2.6451 -0.4556 -0.2204 0.0297 304 PRO B N 5443 C CA . PRO B 305 ? 2.0458 1.8894 2.6780 -0.4869 -0.2228 0.0390 304 PRO B CA 5444 C C . PRO B 305 ? 1.9502 1.8697 2.6308 -0.4757 -0.2071 0.0485 304 PRO B C 5445 O O . PRO B 305 ? 1.9126 1.8607 2.5950 -0.4558 -0.2123 0.0420 304 PRO B O 5446 C CB . PRO B 305 ? 2.0794 1.9194 2.7168 -0.5057 -0.2546 0.0257 304 PRO B CB 5447 C CG . PRO B 305 ? 2.0785 1.8957 2.6688 -0.4767 -0.2648 0.0109 304 PRO B CG 5448 C CD . PRO B 305 ? 2.0974 1.8670 2.6375 -0.4518 -0.2459 0.0121 304 PRO B CD 5449 N N . THR B 306 ? 1.9297 1.8782 2.6460 -0.4876 -0.1873 0.0639 305 THR B N 5450 C CA . THR B 306 ? 1.8992 1.9147 2.6578 -0.4758 -0.1693 0.0732 305 THR B CA 5451 C C . THR B 306 ? 1.9047 1.9697 2.7262 -0.5053 -0.1682 0.0833 305 THR B C 5452 O O . THR B 306 ? 1.9598 2.0055 2.7885 -0.5307 -0.1637 0.0917 305 THR B O 5453 C CB . THR B 306 ? 1.8930 1.8997 2.6321 -0.4574 -0.1414 0.0835 305 THR B CB 5454 O OG1 . THR B 306 ? 1.9018 1.8555 2.5823 -0.4343 -0.1425 0.0757 305 THR B OG1 5455 C CG2 . THR B 306 ? 1.8457 1.9138 2.6166 -0.4391 -0.1249 0.0891 305 THR B CG2 5456 N N . PRO B 307 ? 1.8699 1.9994 2.7380 -0.5017 -0.1711 0.0836 306 PRO B N 5457 C CA . PRO B 307 ? 1.8785 2.0604 2.8106 -0.5280 -0.1691 0.0936 306 PRO B CA 5458 C C . PRO B 307 ? 1.9148 2.1046 2.8617 -0.5369 -0.1399 0.1104 306 PRO B C 5459 O O . PRO B 307 ? 1.8668 2.0614 2.7985 -0.5137 -0.1175 0.1154 306 PRO B O 5460 C CB . PRO B 307 ? 1.8209 2.0680 2.7916 -0.5109 -0.1706 0.0920 306 PRO B CB 5461 C CG . PRO B 307 ? 1.7964 2.0265 2.7243 -0.4756 -0.1639 0.0854 306 PRO B CG 5462 C CD . PRO B 307 ? 1.8328 1.9909 2.6990 -0.4730 -0.1743 0.0763 306 PRO B CD 5463 N N . ASP B 308 ? 1.9998 2.1888 2.9740 -0.5709 -0.1411 0.1188 307 ASP B N 5464 C CA . ASP B 308 ? 2.0432 2.2324 3.0279 -0.5841 -0.1140 0.1362 307 ASP B CA 5465 C C . ASP B 308 ? 2.0188 2.2802 3.0763 -0.6037 -0.1035 0.1486 307 ASP B C 5466 O O . ASP B 308 ? 2.0071 2.3000 3.0817 -0.5962 -0.0752 0.1613 307 ASP B O 5467 C CB . ASP B 308 ? 2.1216 2.2424 3.0737 -0.6091 -0.1206 0.1382 307 ASP B CB 5468 C CG . ASP B 308 ? 2.1535 2.2715 3.1161 -0.6263 -0.0937 0.1579 307 ASP B CG 5469 O OD1 . ASP B 308 ? 2.1000 2.2348 3.0564 -0.6059 -0.0672 0.1671 307 ASP B OD1 5470 O OD2 . ASP B 308 ? 2.2425 2.3396 3.2178 -0.6609 -0.0994 0.1643 307 ASP B OD2 5471 N N . SER B 309 ? 2.0221 2.3097 3.1217 -0.6283 -0.1264 0.1449 308 SER B N 5472 C CA . SER B 309 ? 2.0024 2.3647 3.1774 -0.6468 -0.1191 0.1561 308 SER B CA 5473 C C . SER B 309 ? 1.9752 2.3740 3.1888 -0.6561 -0.1510 0.1455 308 SER B C 5474 O O . SER B 309 ? 1.9796 2.3372 3.1583 -0.6553 -0.1793 0.1305 308 SER B O 5475 C CB . SER B 309 ? 2.0722 2.4261 3.2686 -0.6834 -0.1063 0.1720 308 SER B CB 5476 O OG . SER B 309 ? 2.1661 2.4584 3.3347 -0.7094 -0.1299 0.1656 308 SER B OG 5477 N N . PHE B 310 ? 1.9434 2.4196 3.2275 -0.6632 -0.1462 0.1536 309 PHE B N 5478 C CA . PHE B 310 ? 1.9420 2.4646 3.2679 -0.6658 -0.1748 0.1450 309 PHE B CA 5479 C C . PHE B 310 ? 1.9475 2.5300 3.3512 -0.7004 -0.1790 0.1559 309 PHE B C 5480 O O . PHE B 310 ? 1.9397 2.5618 3.3834 -0.7087 -0.1502 0.1722 309 PHE B O 5481 C CB . PHE B 310 ? 1.9061 2.4746 3.2430 -0.6279 -0.1669 0.1420 309 PHE B CB 5482 C CG . PHE B 310 ? 1.9314 2.4508 3.1997 -0.5938 -0.1604 0.1329 309 PHE B CG 5483 C CD1 . PHE B 310 ? 1.9546 2.4323 3.1774 -0.5825 -0.1873 0.1170 309 PHE B CD1 5484 C CD2 . PHE B 310 ? 1.9485 2.4636 3.1969 -0.5735 -0.1274 0.1405 309 PHE B CD2 5485 C CE1 . PHE B 310 ? 1.9648 2.4008 3.1279 -0.5519 -0.1802 0.1096 309 PHE B CE1 5486 C CE2 . PHE B 310 ? 1.9636 2.4366 3.1525 -0.5435 -0.1226 0.1325 309 PHE B CE2 5487 C CZ . PHE B 310 ? 1.9683 2.4031 3.1164 -0.5330 -0.1484 0.1175 309 PHE B CZ 5488 N N . TYR B 311 ? 1.9751 2.5652 3.4000 -0.7203 -0.2151 0.1468 310 TYR B N 5489 C CA . TYR B 311 ? 1.9910 2.6500 3.4979 -0.7503 -0.2244 0.1554 310 TYR B CA 5490 C C . TYR B 311 ? 1.9755 2.6957 3.5210 -0.7315 -0.2453 0.1483 310 TYR B C 5491 O O . TYR B 311 ? 1.9594 2.6520 3.4711 -0.7213 -0.2762 0.1324 310 TYR B O 5492 C CB . TYR B 311 ? 2.0459 2.6694 3.5549 -0.7945 -0.2520 0.1521 310 TYR B CB 5493 C CG . TYR B 311 ? 2.0423 2.7411 3.6399 -0.8269 -0.2661 0.1601 310 TYR B CG 5494 C CD1 . TYR B 311 ? 2.0343 2.7865 3.6943 -0.8470 -0.2373 0.1807 310 TYR B CD1 5495 C CD2 . TYR B 311 ? 2.0435 2.7631 3.6636 -0.8364 -0.3081 0.1478 310 TYR B CD2 5496 C CE1 . TYR B 311 ? 2.0258 2.8527 3.7721 -0.8765 -0.2492 0.1889 310 TYR B CE1 5497 C CE2 . TYR B 311 ? 2.0362 2.8294 3.7413 -0.8658 -0.3227 0.1554 310 TYR B CE2 5498 C CZ . TYR B 311 ? 2.0250 2.8733 3.7952 -0.8860 -0.2928 0.1761 310 TYR B CZ 5499 O OH . TYR B 311 ? 2.0042 2.9306 3.8635 -0.9154 -0.3064 0.1846 310 TYR B OH 5500 N N . TYR B 312 ? 1.9908 2.7931 3.6058 -0.7261 -0.2278 0.1606 311 TYR B N 5501 C CA . TYR B 312 ? 2.0166 2.8843 3.6776 -0.7091 -0.2462 0.1566 311 TYR B CA 5502 C C . TYR B 312 ? 2.0442 2.9714 3.7832 -0.7449 -0.2686 0.1620 311 TYR B C 5503 O O . TYR B 312 ? 2.0537 3.0270 3.8508 -0.7673 -0.2479 0.1780 311 TYR B O 5504 C CB . TYR B 312 ? 2.0073 2.9283 3.6941 -0.6749 -0.2128 0.1655 311 TYR B CB 5505 C CG . TYR B 312 ? 2.0284 2.9062 3.6479 -0.6338 -0.2050 0.1555 311 TYR B CG 5506 C CD1 . TYR B 312 ? 2.0303 2.9181 3.6409 -0.6072 -0.2275 0.1445 311 TYR B CD1 5507 C CD2 . TYR B 312 ? 2.0660 2.8926 3.6305 -0.6221 -0.1759 0.1577 311 TYR B CD2 5508 C CE1 . TYR B 312 ? 2.0493 2.8983 3.6005 -0.5717 -0.2200 0.1363 311 TYR B CE1 5509 C CE2 . TYR B 312 ? 2.0760 2.8661 3.5825 -0.5861 -0.1698 0.1488 311 TYR B CE2 5510 C CZ . TYR B 312 ? 2.0706 2.8723 3.5716 -0.5618 -0.1914 0.1383 311 TYR B CZ 5511 O OH . TYR B 312 ? 2.0981 2.8647 3.5440 -0.5282 -0.1851 0.1303 311 TYR B OH 5512 N N . GLU B 313 ? 2.0733 2.9991 3.8122 -0.7504 -0.3113 0.1490 312 GLU B N 5513 C CA . GLU B 313 ? 2.1081 3.0954 3.9223 -0.7813 -0.3391 0.1522 312 GLU B CA 5514 C C . GLU B 313 ? 2.0470 3.1320 3.9368 -0.7600 -0.3282 0.1622 312 GLU B C 5515 O O . GLU B 313 ? 2.0779 3.2353 4.0503 -0.7835 -0.3276 0.1744 312 GLU B O 5516 C CB . GLU B 313 ? 2.1539 3.1072 3.9362 -0.7873 -0.3892 0.1336 312 GLU B CB 5517 C CG . GLU B 313 ? 2.1916 3.2023 4.0462 -0.8216 -0.4249 0.1346 312 GLU B CG 5518 C CD . GLU B 313 ? 2.2157 3.2084 4.0422 -0.8159 -0.4739 0.1165 312 GLU B CD 5519 O OE1 . GLU B 313 ? 2.2138 3.1617 3.9727 -0.7807 -0.4774 0.1050 312 GLU B OE1 5520 O OE2 . GLU B 313 ? 2.2427 3.2674 4.1152 -0.8472 -0.5093 0.1141 312 GLU B OE2 5521 N N . SER B 314 ? 1.9677 3.0533 3.8286 -0.7150 -0.3199 0.1572 313 SER B N 5522 C CA . SER B 314 ? 1.8916 3.0585 3.8117 -0.6872 -0.3048 0.1659 313 SER B CA 5523 C C . SER B 314 ? 1.8255 2.9681 3.6989 -0.6460 -0.2691 0.1663 313 SER B C 5524 O O . SER B 314 ? 1.8018 2.8791 3.6002 -0.6251 -0.2748 0.1543 313 SER B O 5525 C CB . SER B 314 ? 1.8857 3.0879 3.8279 -0.6738 -0.3447 0.1573 313 SER B CB 5526 O OG . SER B 314 ? 1.8476 3.1258 3.8456 -0.6443 -0.3300 0.1659 313 SER B OG 5527 N N . PHE B 315 ? 1.7808 2.9777 3.7001 -0.6348 -0.2324 0.1801 314 PHE B N 5528 C CA . PHE B 315 ? 1.7519 2.9262 3.6301 -0.6014 -0.1945 0.1819 314 PHE B CA 5529 C C . PHE B 315 ? 1.7316 2.9628 3.6424 -0.5620 -0.1872 0.1830 314 PHE B C 5530 O O . PHE B 315 ? 1.7150 3.0249 3.7038 -0.5654 -0.1869 0.1922 314 PHE B O 5531 C CB . PHE B 315 ? 1.7343 2.9205 3.6332 -0.6194 -0.1548 0.1972 314 PHE B CB 5532 C CG . PHE B 315 ? 1.7054 2.8405 3.5404 -0.5966 -0.1205 0.1971 314 PHE B CG 5533 C CD1 . PHE B 315 ? 1.7155 2.7642 3.4690 -0.5964 -0.1277 0.1870 314 PHE B CD1 5534 C CD2 . PHE B 315 ? 1.6753 2.8491 3.5317 -0.5752 -0.0812 0.2072 314 PHE B CD2 5535 C CE1 . PHE B 315 ? 1.7128 2.7173 3.4097 -0.5758 -0.0981 0.1872 314 PHE B CE1 5536 C CE2 . PHE B 315 ? 1.6757 2.8021 3.4718 -0.5550 -0.0519 0.2065 314 PHE B CE2 5537 C CZ . PHE B 315 ? 1.6978 2.7408 3.4156 -0.5558 -0.0611 0.1968 314 PHE B CZ 5538 N N . PRO B 316 ? 1.7420 2.9356 3.5966 -0.5251 -0.1822 0.1741 315 PRO B N 5539 C CA . PRO B 316 ? 1.7728 2.8783 3.5382 -0.5186 -0.1867 0.1626 315 PRO B CA 5540 C C . PRO B 316 ? 1.7904 2.8682 3.5191 -0.5011 -0.2221 0.1488 315 PRO B C 5541 O O . PRO B 316 ? 1.8002 2.8144 3.4576 -0.4849 -0.2220 0.1396 315 PRO B O 5542 C CB . PRO B 316 ? 1.7406 2.8332 3.4767 -0.4890 -0.1472 0.1655 315 PRO B CB 5543 C CG . PRO B 316 ? 1.7007 2.8651 3.4943 -0.4639 -0.1371 0.1711 315 PRO B CG 5544 C CD . PRO B 316 ? 1.7106 2.9448 3.5858 -0.4891 -0.1529 0.1794 315 PRO B CD 5545 N N . ASP B 317 ? 1.8034 2.9289 3.5797 -0.5049 -0.2525 0.1482 316 ASP B N 5546 C CA . ASP B 317 ? 1.8038 2.9129 3.5510 -0.4843 -0.2848 0.1374 316 ASP B CA 5547 C C . ASP B 317 ? 1.8388 2.8972 3.5447 -0.5073 -0.3226 0.1259 316 ASP B C 5548 O O . ASP B 317 ? 1.8276 2.8711 3.5069 -0.4926 -0.3512 0.1171 316 ASP B O 5549 C CB . ASP B 317 ? 1.7876 2.9756 3.6051 -0.4710 -0.2990 0.1428 316 ASP B CB 5550 C CG . ASP B 317 ? 1.7533 2.9909 3.6099 -0.4441 -0.2628 0.1529 316 ASP B CG 5551 O OD1 . ASP B 317 ? 1.7232 2.9246 3.5328 -0.4176 -0.2382 0.1503 316 ASP B OD1 5552 O OD2 . ASP B 317 ? 1.7535 3.0667 3.6882 -0.4493 -0.2592 0.1630 316 ASP B OD2 5553 N N . ARG B 318 ? 1.8735 2.9031 3.5717 -0.5424 -0.3223 0.1260 317 ARG B N 5554 C CA . ARG B 318 ? 1.9124 2.8883 3.5692 -0.5664 -0.3564 0.1144 317 ARG B CA 5555 C C . ARG B 318 ? 1.9004 2.7947 3.4829 -0.5696 -0.3390 0.1092 317 ARG B C 5556 O O . ARG B 318 ? 1.8980 2.7892 3.4851 -0.5751 -0.3057 0.1180 317 ARG B O 5557 C CB . ARG B 318 ? 1.9659 2.9787 3.6830 -0.6091 -0.3747 0.1191 317 ARG B CB 5558 C CG . ARG B 318 ? 2.0395 2.9976 3.7179 -0.6382 -0.4119 0.1064 317 ARG B CG 5559 C CD . ARG B 318 ? 2.0868 3.0963 3.8370 -0.6777 -0.4361 0.1110 317 ARG B CD 5560 N NE . ARG B 318 ? 2.1033 3.1963 3.9223 -0.6660 -0.4527 0.1160 317 ARG B NE 5561 C CZ . ARG B 318 ? 2.1494 3.2473 3.9564 -0.6507 -0.4888 0.1065 317 ARG B CZ 5562 N NH1 . ARG B 318 ? 2.1906 3.2146 3.9176 -0.6452 -0.5122 0.0909 317 ARG B NH1 5563 N NH2 . ARG B 318 ? 2.1564 3.3342 4.0312 -0.6393 -0.5013 0.1132 317 ARG B NH2 5564 N N . ASP B 319 ? 1.8848 2.7142 3.3985 -0.5647 -0.3611 0.0953 318 ASP B N 5565 C CA . ASP B 319 ? 1.8790 2.6306 3.3204 -0.5637 -0.3460 0.0898 318 ASP B CA 5566 C C . ASP B 319 ? 1.9072 2.6346 3.3544 -0.6025 -0.3428 0.0931 318 ASP B C 5567 O O . ASP B 319 ? 1.9339 2.6765 3.4139 -0.6335 -0.3689 0.0918 318 ASP B O 5568 C CB . ASP B 319 ? 1.8841 2.5748 3.2529 -0.5493 -0.3706 0.0743 318 ASP B CB 5569 C CG . ASP B 319 ? 1.8356 2.5338 3.1833 -0.5087 -0.3645 0.0727 318 ASP B CG 5570 O OD1 . ASP B 319 ? 1.7697 2.4823 3.1232 -0.4883 -0.3321 0.0803 318 ASP B OD1 5571 O OD2 . ASP B 319 ? 1.8341 2.5211 3.1568 -0.4977 -0.3924 0.0639 318 ASP B OD2 5572 N N . PRO B 320 ? 1.8889 2.5782 3.3046 -0.6014 -0.3114 0.0980 319 PRO B N 5573 C CA . PRO B 320 ? 1.8977 2.5661 3.3217 -0.6370 -0.3037 0.1042 319 PRO B CA 5574 C C . PRO B 320 ? 1.9180 2.5032 3.2764 -0.6523 -0.3233 0.0919 319 PRO B C 5575 O O . PRO B 320 ? 1.9092 2.4475 3.2069 -0.6306 -0.3356 0.0790 319 PRO B O 5576 C CB . PRO B 320 ? 1.8814 2.5467 3.2966 -0.6229 -0.2602 0.1155 319 PRO B CB 5577 C CG . PRO B 320 ? 1.8687 2.5037 3.2278 -0.5832 -0.2538 0.1072 319 PRO B CG 5578 C CD . PRO B 320 ? 1.8614 2.5250 3.2325 -0.5678 -0.2821 0.0986 319 PRO B CD 5579 N N . LYS B 321 ? 1.9379 2.5043 3.3085 -0.6892 -0.3246 0.0966 320 LYS B N 5580 C CA . LYS B 321 ? 1.9886 2.4696 3.2952 -0.7043 -0.3374 0.0864 320 LYS B CA 5581 C C . LYS B 321 ? 1.9686 2.4065 3.2313 -0.6889 -0.3011 0.0932 320 LYS B C 5582 O O . LYS B 321 ? 1.9176 2.3928 3.2148 -0.6874 -0.2696 0.1085 320 LYS B O 5583 C CB . LYS B 321 ? 2.0554 2.5307 3.3934 -0.7524 -0.3564 0.0885 320 LYS B CB 5584 C CG . LYS B 321 ? 2.0581 2.6183 3.4846 -0.7749 -0.3723 0.0953 320 LYS B CG 5585 C CD . LYS B 321 ? 2.0552 2.6504 3.4922 -0.7571 -0.4040 0.0841 320 LYS B CD 5586 C CE . LYS B 321 ? 2.0365 2.7304 3.5682 -0.7680 -0.4092 0.0950 320 LYS B CE 5587 N NZ . LYS B 321 ? 2.0198 2.7523 3.5613 -0.7419 -0.4336 0.0870 320 LYS B NZ 5588 N N . ILE B 322 ? 2.0027 2.3636 3.1890 -0.6759 -0.3053 0.0818 321 ILE B N 5589 C CA . ILE B 322 ? 2.0110 2.3319 3.1509 -0.6547 -0.2739 0.0867 321 ILE B CA 5590 C C . ILE B 322 ? 2.0731 2.3175 3.1678 -0.6753 -0.2734 0.0858 321 ILE B C 5591 O O . ILE B 322 ? 2.1233 2.3148 3.1800 -0.6859 -0.3004 0.0722 321 ILE B O 5592 C CB . ILE B 322 ? 2.0061 2.3032 3.0919 -0.6138 -0.2742 0.0754 321 ILE B CB 5593 C CG1 . ILE B 322 ? 1.9630 2.3288 3.0887 -0.5926 -0.2768 0.0758 321 ILE B CG1 5594 C CG2 . ILE B 322 ? 1.9969 2.2594 3.0405 -0.5921 -0.2426 0.0811 321 ILE B CG2 5595 C CD1 . ILE B 322 ? 1.9471 2.2920 3.0240 -0.5567 -0.2821 0.0646 321 ILE B CD1 5596 N N . CYS B 323 ? 2.0786 2.3154 3.1749 -0.6799 -0.2427 0.1005 322 CYS B N 5597 C CA . CYS B 323 ? 2.1201 2.2797 3.1663 -0.6923 -0.2366 0.1019 322 CYS B CA 5598 C C . CYS B 323 ? 2.0906 2.2096 3.0754 -0.6545 -0.2171 0.0996 322 CYS B C 5599 O O . CYS B 323 ? 2.0231 2.1817 3.0201 -0.6301 -0.1938 0.1069 322 CYS B O 5600 C CB . CYS B 323 ? 2.1280 2.3031 3.2135 -0.7224 -0.2150 0.1215 322 CYS B CB 5601 S SG . CYS B 323 ? 2.1610 2.2395 3.1894 -0.7427 -0.2095 0.1255 322 CYS B SG 5602 N N . PHE B 324 ? 2.1224 2.1631 3.0418 -0.6496 -0.2270 0.0893 323 PHE B N 5603 C CA . PHE B 324 ? 2.0943 2.0971 2.9551 -0.6125 -0.2132 0.0851 323 PHE B CA 5604 C C . PHE B 324 ? 2.1340 2.0808 2.9569 -0.6138 -0.1927 0.0948 323 PHE B C 5605 O O . PHE B 324 ? 2.1950 2.0979 3.0093 -0.6421 -0.1989 0.0977 323 PHE B O 5606 C CB . PHE B 324 ? 2.1010 2.0600 2.9112 -0.5965 -0.2386 0.0650 323 PHE B CB 5607 C CG . PHE B 324 ? 2.0523 2.0628 2.8879 -0.5851 -0.2555 0.0561 323 PHE B CG 5608 C CD1 . PHE B 324 ? 2.0618 2.0988 2.9350 -0.6111 -0.2822 0.0511 323 PHE B CD1 5609 C CD2 . PHE B 324 ? 1.9899 2.0227 2.8124 -0.5489 -0.2455 0.0535 323 PHE B CD2 5610 C CE1 . PHE B 324 ? 2.0201 2.1036 2.9150 -0.5991 -0.2986 0.0440 323 PHE B CE1 5611 C CE2 . PHE B 324 ? 1.9550 2.0318 2.7987 -0.5380 -0.2607 0.0466 323 PHE B CE2 5612 C CZ . PHE B 324 ? 1.9686 2.0704 2.8475 -0.5621 -0.2873 0.0421 323 PHE B CZ 5613 N N . GLY B 325 ? 2.1004 2.0489 2.9006 -0.5829 -0.1691 0.1001 324 GLY B N 5614 C CA . GLY B 325 ? 2.1197 2.0140 2.8757 -0.5755 -0.1505 0.1084 324 GLY B CA 5615 C C . GLY B 325 ? 2.1134 1.9716 2.8122 -0.5375 -0.1499 0.0979 324 GLY B C 5616 O O . GLY B 325 ? 2.0958 1.9578 2.7828 -0.5221 -0.1667 0.0831 324 GLY B O 5617 N N . ASP B 326 ? 2.1201 1.9453 2.7842 -0.5220 -0.1302 0.1065 325 ASP B N 5618 C CA . ASP B 326 ? 2.1396 1.9291 2.7503 -0.4866 -0.1286 0.0981 325 ASP B CA 5619 C C . ASP B 326 ? 2.0666 1.9099 2.6909 -0.4575 -0.1134 0.1002 325 ASP B C 5620 O O . ASP B 326 ? 2.0365 1.9330 2.7019 -0.4625 -0.0983 0.1110 325 ASP B O 5621 C CB . ASP B 326 ? 2.2182 1.9416 2.7821 -0.4827 -0.1177 0.1058 325 ASP B CB 5622 C CG . ASP B 326 ? 2.2717 1.9390 2.7758 -0.4546 -0.1260 0.0929 325 ASP B CG 5623 O OD1 . ASP B 326 ? 2.2757 1.9601 2.7739 -0.4350 -0.1360 0.0795 325 ASP B OD1 5624 O OD2 . ASP B 326 ? 2.3339 1.9392 2.7962 -0.4512 -0.1217 0.0969 325 ASP B OD2 5625 N N . GLY B 327 ? 2.0422 1.8698 2.6307 -0.4272 -0.1171 0.0897 326 GLY B N 5626 C CA . GLY B 327 ? 1.9737 1.8455 2.5700 -0.3990 -0.1053 0.0898 326 GLY B CA 5627 C C . GLY B 327 ? 1.9674 1.8294 2.5371 -0.3761 -0.1187 0.0747 326 GLY B C 5628 O O . GLY B 327 ? 2.0611 1.8700 2.5910 -0.3735 -0.1314 0.0653 326 GLY B O 5629 N N . ASP B 328 ? 1.8880 1.7998 2.4786 -0.3597 -0.1154 0.0725 327 ASP B N 5630 C CA . ASP B 328 ? 1.8646 1.7740 2.4326 -0.3367 -0.1248 0.0603 327 ASP B CA 5631 C C . ASP B 328 ? 1.8306 1.7734 2.4256 -0.3446 -0.1420 0.0524 327 ASP B C 5632 O O . ASP B 328 ? 1.8128 1.7631 2.3950 -0.3259 -0.1480 0.0443 327 ASP B O 5633 C CB . ASP B 328 ? 1.8441 1.7776 2.4076 -0.3086 -0.1082 0.0640 327 ASP B CB 5634 C CG . ASP B 328 ? 1.7987 1.7920 2.4077 -0.3112 -0.0960 0.0723 327 ASP B CG 5635 O OD1 . ASP B 328 ? 1.7838 1.8074 2.4313 -0.3311 -0.1011 0.0741 327 ASP B OD1 5636 O OD2 . ASP B 328 ? 1.7761 1.7863 2.3825 -0.2927 -0.0815 0.0766 327 ASP B OD2 5637 N N . GLY B 329 ? 1.8199 1.7833 2.4525 -0.3721 -0.1499 0.0554 328 GLY B N 5638 C CA . GLY B 329 ? 1.7891 1.7894 2.4527 -0.3805 -0.1671 0.0495 328 GLY B CA 5639 C C . GLY B 329 ? 1.7150 1.7821 2.4328 -0.3820 -0.1564 0.0583 328 GLY B C 5640 O O . GLY B 329 ? 1.6838 1.7862 2.4397 -0.3963 -0.1689 0.0574 328 GLY B O 5641 N N . THR B 330 ? 1.6845 1.7684 2.4050 -0.3666 -0.1339 0.0663 329 THR B N 5642 C CA . THR B 330 ? 1.6764 1.8190 2.4428 -0.3649 -0.1209 0.0742 329 THR B CA 5643 C C . THR B 330 ? 1.6934 1.8392 2.4680 -0.3710 -0.0983 0.0867 329 THR B C 5644 O O . THR B 330 ? 1.6471 1.8236 2.4616 -0.3895 -0.0920 0.0950 329 THR B O 5645 C CB . THR B 330 ? 1.6572 1.8215 2.4176 -0.3370 -0.1164 0.0704 329 THR B CB 5646 O OG1 . THR B 330 ? 1.6642 1.8225 2.4128 -0.3314 -0.1366 0.0600 329 THR B OG1 5647 C CG2 . THR B 330 ? 1.6229 1.8435 2.4279 -0.3340 -0.1038 0.0770 329 THR B CG2 5648 N N . VAL B 331 ? 1.7529 1.8680 2.4897 -0.3548 -0.0859 0.0887 330 VAL B N 5649 C CA . VAL B 331 ? 1.7883 1.9006 2.5235 -0.3572 -0.0648 0.1007 330 VAL B CA 5650 C C . VAL B 331 ? 1.8334 1.9007 2.5516 -0.3781 -0.0661 0.1061 330 VAL B C 5651 O O . VAL B 331 ? 1.8860 1.9021 2.5647 -0.3752 -0.0765 0.1002 330 VAL B O 5652 C CB . VAL B 331 ? 1.8012 1.9016 2.5034 -0.3301 -0.0524 0.1012 330 VAL B CB 5653 C CG1 . VAL B 331 ? 1.8104 1.9022 2.5043 -0.3324 -0.0328 0.1137 330 VAL B CG1 5654 C CG2 . VAL B 331 ? 1.7694 1.9135 2.4900 -0.3119 -0.0493 0.0971 330 VAL B CG2 5655 N N . ASN B 332 ? 1.8230 1.9088 2.5706 -0.3985 -0.0545 0.1179 331 ASN B N 5656 C CA . ASN B 332 ? 1.8654 1.9115 2.6027 -0.4224 -0.0547 0.1251 331 ASN B CA 5657 C C . ASN B 332 ? 1.8405 1.8386 2.5294 -0.4088 -0.0428 0.1308 331 ASN B C 5658 O O . ASN B 332 ? 1.8188 1.8314 2.4986 -0.3885 -0.0271 0.1353 331 ASN B O 5659 C CB . ASN B 332 ? 1.8823 1.9670 2.6671 -0.4472 -0.0422 0.1381 331 ASN B CB 5660 C CG . ASN B 332 ? 1.8659 2.0025 2.7031 -0.4600 -0.0546 0.1334 331 ASN B CG 5661 O OD1 . ASN B 332 ? 1.8573 2.0492 2.7311 -0.4532 -0.0438 0.1367 331 ASN B OD1 5662 N ND2 . ASN B 332 ? 1.8880 2.0055 2.7272 -0.4773 -0.0784 0.1251 331 ASN B ND2 5663 N N . LEU B 333 ? 1.8200 1.7593 2.4770 -0.4195 -0.0514 0.1303 332 LEU B N 5664 C CA . LEU B 333 ? 1.8172 1.7052 2.4272 -0.4077 -0.0415 0.1369 332 LEU B CA 5665 C C . LEU B 333 ? 1.7964 1.7014 2.4143 -0.4097 -0.0173 0.1542 332 LEU B C 5666 O O . LEU B 333 ? 1.7912 1.6814 2.3781 -0.3881 -0.0061 0.1589 332 LEU B O 5667 C CB . LEU B 333 ? 1.8772 1.7002 2.4596 -0.4262 -0.0536 0.1360 332 LEU B CB 5668 C CG . LEU B 333 ? 1.9152 1.6785 2.4495 -0.4174 -0.0440 0.1450 332 LEU B CG 5669 C CD1 . LEU B 333 ? 1.8970 1.6463 2.3930 -0.3798 -0.0432 0.1381 332 LEU B CD1 5670 C CD2 . LEU B 333 ? 1.9837 1.6819 2.4943 -0.4390 -0.0572 0.1432 332 LEU B CD2 5671 N N . LYS B 334 ? 1.7810 1.7186 2.4404 -0.4352 -0.0094 0.1637 333 LYS B N 5672 C CA . LYS B 334 ? 1.7933 1.7467 2.4598 -0.4392 0.0149 0.1808 333 LYS B CA 5673 C C . LYS B 334 ? 1.7566 1.7454 2.4194 -0.4108 0.0293 0.1812 333 LYS B C 5674 O O . LYS B 334 ? 1.7449 1.7318 2.3939 -0.4061 0.0484 0.1939 333 LYS B O 5675 C CB . LYS B 334 ? 1.8143 1.8074 2.5336 -0.4705 0.0212 0.1897 333 LYS B CB 5676 C CG . LYS B 334 ? 1.9098 1.8625 2.6302 -0.5028 0.0097 0.1929 333 LYS B CG 5677 C CD . LYS B 334 ? 1.9386 1.9372 2.7182 -0.5307 0.0005 0.1912 333 LYS B CD 5678 C CE . LYS B 334 ? 2.0225 1.9762 2.7999 -0.5631 -0.0159 0.1912 333 LYS B CE 5679 N NZ . LYS B 334 ? 2.0363 2.0376 2.8765 -0.5963 -0.0198 0.1957 333 LYS B NZ 5680 N N . SER B 335 ? 1.7336 1.7520 2.4064 -0.3925 0.0197 0.1675 334 SER B N 5681 C CA . SER B 335 ? 1.6817 1.7275 2.3473 -0.3650 0.0296 0.1654 334 SER B CA 5682 C C . SER B 335 ? 1.7030 1.7079 2.3177 -0.3437 0.0342 0.1685 334 SER B C 5683 O O . SER B 335 ? 1.6683 1.6885 2.2738 -0.3294 0.0484 0.1741 334 SER B O 5684 C CB . SER B 335 ? 1.6325 1.7070 2.3135 -0.3509 0.0156 0.1500 334 SER B CB 5685 O OG . SER B 335 ? 1.6095 1.7218 2.3369 -0.3683 0.0091 0.1471 334 SER B OG 5686 N N . ALA B 336 ? 1.7510 1.7037 2.3319 -0.3411 0.0217 0.1647 335 ALA B N 5687 C CA . ALA B 336 ? 1.7578 1.6714 2.2913 -0.3185 0.0238 0.1671 335 ALA B CA 5688 C C . ALA B 336 ? 1.7954 1.6855 2.3066 -0.3221 0.0402 0.1844 335 ALA B C 5689 O O . ALA B 336 ? 1.7660 1.6281 2.2392 -0.3020 0.0426 0.1882 335 ALA B O 5690 C CB . ALA B 336 ? 1.7748 1.6375 2.2782 -0.3138 0.0070 0.1584 335 ALA B CB 5691 N N . LEU B 337 ? 1.8540 1.7565 2.3889 -0.3471 0.0516 0.1957 336 LEU B N 5692 C CA . LEU B 337 ? 1.9453 1.8298 2.4607 -0.3522 0.0698 0.2139 336 LEU B CA 5693 C C . LEU B 337 ? 1.9371 1.8490 2.4410 -0.3295 0.0834 0.2177 336 LEU B C 5694 O O . LEU B 337 ? 1.9875 1.8716 2.4558 -0.3210 0.0930 0.2297 336 LEU B O 5695 C CB . LEU B 337 ? 1.9925 1.8963 2.5437 -0.3843 0.0814 0.2252 336 LEU B CB 5696 C CG . LEU B 337 ? 2.0568 1.9287 2.6183 -0.4130 0.0695 0.2252 336 LEU B CG 5697 C CD1 . LEU B 337 ? 2.0768 1.9852 2.6856 -0.4442 0.0811 0.2354 336 LEU B CD1 5698 C CD2 . LEU B 337 ? 2.1194 1.9177 2.6319 -0.4141 0.0677 0.2338 336 LEU B CD2 5699 N N . GLN B 338 ? 1.8902 1.8545 2.4225 -0.3201 0.0835 0.2077 337 GLN B N 5700 C CA . GLN B 338 ? 1.9022 1.8944 2.4257 -0.3004 0.0951 0.2092 337 GLN B CA 5701 C C . GLN B 338 ? 1.9153 1.8792 2.3957 -0.2737 0.0879 0.2068 337 GLN B C 5702 O O . GLN B 338 ? 1.9436 1.9024 2.3972 -0.2617 0.0980 0.2154 337 GLN B O 5703 C CB . GLN B 338 ? 1.8767 1.9248 2.4384 -0.2952 0.0937 0.1968 337 GLN B CB 5704 C CG . GLN B 338 ? 1.8702 1.9480 2.4254 -0.2776 0.1058 0.1969 337 GLN B CG 5705 C CD . GLN B 338 ? 1.9085 1.9939 2.4610 -0.2870 0.1282 0.2120 337 GLN B CD 5706 O OE1 . GLN B 338 ? 1.9389 2.0238 2.5104 -0.3099 0.1368 0.2217 337 GLN B OE1 5707 N NE2 . GLN B 338 ? 1.9182 2.0112 2.4465 -0.2698 0.1379 0.2140 337 GLN B NE2 5708 N N . CYS B 339 ? 1.9060 1.8531 2.3799 -0.2640 0.0705 0.1952 338 CYS B N 5709 C CA . CYS B 339 ? 1.9348 1.8553 2.3713 -0.2386 0.0628 0.1931 338 CYS B CA 5710 C C . CYS B 339 ? 2.0252 1.8935 2.4224 -0.2392 0.0677 0.2079 338 CYS B C 5711 O O . CYS B 339 ? 2.0370 1.8933 2.4029 -0.2201 0.0705 0.2142 338 CYS B O 5712 C CB . CYS B 339 ? 1.9217 1.8309 2.3595 -0.2308 0.0453 0.1792 338 CYS B CB 5713 S SG . CYS B 339 ? 1.8963 1.8565 2.3815 -0.2380 0.0382 0.1640 338 CYS B SG 5714 N N . GLN B 340 ? 2.0998 1.9364 2.4988 -0.2618 0.0678 0.2136 339 GLN B N 5715 C CA . GLN B 340 ? 2.1987 1.9808 2.5620 -0.2671 0.0734 0.2292 339 GLN B CA 5716 C C . GLN B 340 ? 2.1912 1.9847 2.5426 -0.2665 0.0920 0.2451 339 GLN B C 5717 O O . GLN B 340 ? 2.2385 1.9999 2.5494 -0.2515 0.0950 0.2556 339 GLN B O 5718 C CB . GLN B 340 ? 2.2914 2.0466 2.6685 -0.2980 0.0715 0.2323 339 GLN B CB 5719 C CG . GLN B 340 ? 2.4260 2.1090 2.7627 -0.2998 0.0666 0.2400 339 GLN B CG 5720 C CD . GLN B 340 ? 2.5190 2.1757 2.8716 -0.3311 0.0602 0.2388 339 GLN B CD 5721 O OE1 . GLN B 340 ? 2.5394 2.2339 2.9347 -0.3554 0.0634 0.2378 339 GLN B OE1 5722 N NE2 . GLN B 340 ? 2.6036 2.1949 2.9220 -0.3305 0.0503 0.2388 339 GLN B NE2 5723 N N . ALA B 341 ? 2.1411 1.9807 2.5265 -0.2812 0.1043 0.2466 340 ALA B N 5724 C CA . ALA B 341 ? 2.1281 1.9822 2.5028 -0.2809 0.1239 0.2606 340 ALA B CA 5725 C C . ALA B 341 ? 2.0891 1.9574 2.4385 -0.2511 0.1227 0.2571 340 ALA B C 5726 O O . ALA B 341 ? 2.1116 1.9649 2.4276 -0.2430 0.1329 0.2702 340 ALA B O 5727 C CB . ALA B 341 ? 2.1015 2.0061 2.5212 -0.3003 0.1374 0.2607 340 ALA B CB 5728 N N . TRP B 342 ? 2.0330 1.9297 2.3977 -0.2354 0.1096 0.2399 341 TRP B N 5729 C CA . TRP B 342 ? 1.9852 1.8977 2.3300 -0.2087 0.1058 0.2352 341 TRP B CA 5730 C C . TRP B 342 ? 2.0179 1.8877 2.3189 -0.1887 0.0967 0.2409 341 TRP B C 5731 O O . TRP B 342 ? 2.0081 1.8810 2.2827 -0.1701 0.0973 0.2447 341 TRP B O 5732 C CB . TRP B 342 ? 1.9185 1.8704 2.2925 -0.1988 0.0939 0.2161 341 TRP B CB 5733 C CG . TRP B 342 ? 1.8871 1.8873 2.2976 -0.2085 0.1027 0.2098 341 TRP B CG 5734 C CD1 . TRP B 342 ? 1.8977 1.9181 2.3089 -0.2136 0.1200 0.2171 341 TRP B CD1 5735 C CD2 . TRP B 342 ? 1.8175 1.8513 2.2672 -0.2119 0.0949 0.1950 341 TRP B CD2 5736 N NE1 . TRP B 342 ? 1.8371 1.9015 2.2871 -0.2194 0.1236 0.2072 341 TRP B NE1 5737 C CE2 . TRP B 342 ? 1.7829 1.8559 2.2572 -0.2186 0.1078 0.1940 341 TRP B CE2 5738 C CE3 . TRP B 342 ? 1.7739 1.8072 2.2383 -0.2090 0.0788 0.1830 341 TRP B CE3 5739 C CZ2 . TRP B 342 ? 1.7244 1.8348 2.2380 -0.2221 0.1042 0.1819 341 TRP B CZ2 5740 C CZ3 . TRP B 342 ? 1.7149 1.7855 2.2169 -0.2135 0.0753 0.1714 341 TRP B CZ3 5741 C CH2 . TRP B 342 ? 1.6986 1.8067 2.2253 -0.2199 0.0874 0.1711 341 TRP B CH2 5742 N N . GLN B 343 ? 2.0508 1.8805 2.3437 -0.1917 0.0876 0.2411 342 GLN B N 5743 C CA . GLN B 343 ? 2.1114 1.8966 2.3636 -0.1718 0.0792 0.2468 342 GLN B CA 5744 C C . GLN B 343 ? 2.1876 1.9483 2.4003 -0.1662 0.0899 0.2657 342 GLN B C 5745 O O . GLN B 343 ? 2.2077 1.9582 2.3903 -0.1417 0.0835 0.2688 342 GLN B O 5746 C CB . GLN B 343 ? 2.1626 1.9010 2.4101 -0.1813 0.0716 0.2458 342 GLN B CB 5747 C CG . GLN B 343 ? 2.2135 1.9128 2.4281 -0.1561 0.0592 0.2447 342 GLN B CG 5748 C CD . GLN B 343 ? 2.2736 1.9306 2.4862 -0.1646 0.0504 0.2387 342 GLN B CD 5749 O OE1 . GLN B 343 ? 2.3065 1.9510 2.5341 -0.1922 0.0540 0.2401 342 GLN B OE1 5750 N NE2 . GLN B 343 ? 2.3071 1.9426 2.5013 -0.1406 0.0387 0.2317 342 GLN B NE2 5751 N N . SER B 344 ? 2.2488 2.0029 2.4627 -0.1887 0.1063 0.2786 343 SER B N 5752 C CA . SER B 344 ? 2.3004 2.0293 2.4751 -0.1862 0.1190 0.2985 343 SER B CA 5753 C C . SER B 344 ? 2.2678 2.0385 2.4390 -0.1780 0.1291 0.2996 343 SER B C 5754 O O . SER B 344 ? 2.3267 2.0794 2.4610 -0.1725 0.1389 0.3153 343 SER B O 5755 C CB . SER B 344 ? 2.3448 2.0436 2.5210 -0.2160 0.1336 0.3138 343 SER B CB 5756 O OG . SER B 344 ? 2.3101 2.0510 2.5330 -0.2400 0.1432 0.3083 343 SER B OG 5757 N N . ARG B 345 ? 2.2205 2.0435 2.4265 -0.1766 0.1264 0.2831 344 ARG B N 5758 C CA . ARG B 345 ? 2.2506 2.1136 2.4599 -0.1751 0.1387 0.2824 344 ARG B CA 5759 C C . ARG B 345 ? 2.1815 2.0760 2.3875 -0.1514 0.1263 0.2684 344 ARG B C 5760 O O . ARG B 345 ? 2.1399 2.0647 2.3452 -0.1484 0.1346 0.2656 344 ARG B O 5761 C CB . ARG B 345 ? 2.2849 2.1844 2.5419 -0.1983 0.1502 0.2764 344 ARG B CB 5762 C CG . ARG B 345 ? 2.3880 2.2648 2.6548 -0.2256 0.1636 0.2906 344 ARG B CG 5763 C CD . ARG B 345 ? 2.4773 2.3504 2.7241 -0.2349 0.1874 0.3093 344 ARG B CD 5764 N NE . ARG B 345 ? 2.5030 2.4286 2.7813 -0.2414 0.2022 0.3037 344 ARG B NE 5765 C CZ . ARG B 345 ? 2.5671 2.5053 2.8561 -0.2597 0.2257 0.3165 344 ARG B CZ 5766 N NH1 . ARG B 345 ? 2.6375 2.5392 2.9087 -0.2761 0.2380 0.3371 344 ARG B NH1 5767 N NH2 . ARG B 345 ? 2.5412 2.5290 2.8596 -0.2613 0.2380 0.3091 344 ARG B NH2 5768 N N . GLN B 346 ? 2.1559 2.0436 2.3597 -0.1345 0.1071 0.2597 345 GLN B N 5769 C CA . GLN B 346 ? 2.0900 2.0132 2.3011 -0.1160 0.0943 0.2450 345 GLN B CA 5770 C C . GLN B 346 ? 2.1325 2.0355 2.3145 -0.0918 0.0783 0.2473 345 GLN B C 5771 O O . GLN B 346 ? 2.2265 2.0897 2.3918 -0.0887 0.0746 0.2557 345 GLN B O 5772 C CB . GLN B 346 ? 2.0192 1.9752 2.2776 -0.1230 0.0876 0.2272 345 GLN B CB 5773 C CG . GLN B 346 ? 1.9733 1.9526 2.2418 -0.1046 0.0701 0.2130 345 GLN B CG 5774 C CD . GLN B 346 ? 1.9105 1.9169 2.2228 -0.1130 0.0651 0.1978 345 GLN B CD 5775 O OE1 . GLN B 346 ? 1.9067 1.9117 2.2412 -0.1315 0.0722 0.1976 345 GLN B OE1 5776 N NE2 . GLN B 346 ? 1.8644 1.8955 2.1893 -0.0997 0.0524 0.1858 345 GLN B NE2 5777 N N . GLU B 347 ? 2.1267 2.0570 2.3031 -0.0748 0.0686 0.2397 346 GLU B N 5778 C CA . GLU B 347 ? 2.2214 2.1411 2.3722 -0.0502 0.0527 0.2424 346 GLU B CA 5779 C C . GLU B 347 ? 2.1788 2.1070 2.3550 -0.0405 0.0378 0.2312 346 GLU B C 5780 O O . GLU B 347 ? 2.2187 2.1209 2.3779 -0.0249 0.0289 0.2369 346 GLU B O 5781 C CB . GLU B 347 ? 2.3145 2.2650 2.4536 -0.0381 0.0466 0.2371 346 GLU B CB 5782 C CG . GLU B 347 ? 2.4289 2.3726 2.5396 -0.0128 0.0297 0.2418 346 GLU B CG 5783 C CD . GLU B 347 ? 2.4860 2.4641 2.5905 -0.0030 0.0200 0.2334 346 GLU B CD 5784 O OE1 . GLU B 347 ? 2.5328 2.5279 2.6384 -0.0142 0.0299 0.2283 346 GLU B OE1 5785 O OE2 . GLU B 347 ? 2.5164 2.5045 2.6150 0.0162 0.0019 0.2317 346 GLU B OE2 5786 N N . HIS B 348 ? 2.1291 2.0940 2.3446 -0.0481 0.0355 0.2155 347 HIS B N 5787 C CA . HIS B 348 ? 2.1044 2.0801 2.3438 -0.0394 0.0232 0.2051 347 HIS B CA 5788 C C . HIS B 348 ? 2.1021 2.0424 2.3442 -0.0475 0.0264 0.2080 347 HIS B C 5789 O O . HIS B 348 ? 2.1213 2.0386 2.3593 -0.0656 0.0380 0.2150 347 HIS B O 5790 C CB . HIS B 348 ? 2.0712 2.0934 2.3493 -0.0449 0.0196 0.1885 347 HIS B CB 5791 C CG . HIS B 348 ? 2.0580 2.1111 2.3377 -0.0286 0.0067 0.1822 347 HIS B CG 5792 N ND1 . HIS B 348 ? 2.0629 2.1323 2.3284 -0.0264 0.0062 0.1820 347 HIS B ND1 5793 C CD2 . HIS B 348 ? 2.0367 2.1082 2.3314 -0.0143 -0.0064 0.1757 347 HIS B CD2 5794 C CE1 . HIS B 348 ? 2.0462 2.1420 2.3186 -0.0130 -0.0084 0.1753 347 HIS B CE1 5795 N NE2 . HIS B 348 ? 2.0291 2.1286 2.3213 -0.0056 -0.0156 0.1721 347 HIS B NE2 5796 N N . GLN B 349 ? 2.0919 2.0273 2.3399 -0.0337 0.0159 0.2029 348 GLN B N 5797 C CA . GLN B 349 ? 2.1258 2.0234 2.3710 -0.0377 0.0164 0.2038 348 GLN B CA 5798 C C . GLN B 349 ? 2.0358 1.9417 2.3112 -0.0617 0.0220 0.1951 348 GLN B C 5799 O O . GLN B 349 ? 1.9976 1.9444 2.3035 -0.0674 0.0210 0.1841 348 GLN B O 5800 C CB . GLN B 349 ? 2.1855 2.0825 2.4324 -0.0155 0.0049 0.1979 348 GLN B CB 5801 C CG . GLN B 349 ? 2.2942 2.1772 2.5117 0.0108 -0.0021 0.2075 348 GLN B CG 5802 C CD . GLN B 349 ? 2.3521 2.2332 2.5731 0.0332 -0.0111 0.2023 348 GLN B CD 5803 O OE1 . GLN B 349 ? 2.3386 2.2294 2.5824 0.0290 -0.0117 0.1911 348 GLN B OE1 5804 N NE2 . GLN B 349 ? 2.4208 2.2901 2.6185 0.0585 -0.0179 0.2110 348 GLN B NE2 5805 N N . VAL B 350 ? 2.0166 1.8822 2.2828 -0.0753 0.0266 0.2003 349 VAL B N 5806 C CA . VAL B 350 ? 1.9869 1.8565 2.2806 -0.0983 0.0294 0.1928 349 VAL B CA 5807 C C . VAL B 350 ? 2.0155 1.8411 2.2967 -0.0968 0.0231 0.1907 349 VAL B C 5808 O O . VAL B 350 ? 2.0924 1.8701 2.3448 -0.0985 0.0255 0.2014 349 VAL B O 5809 C CB . VAL B 350 ? 1.9919 1.8570 2.2892 -0.1231 0.0427 0.2019 349 VAL B CB 5810 C CG1 . VAL B 350 ? 1.9738 1.8511 2.3051 -0.1465 0.0438 0.1938 349 VAL B CG1 5811 C CG2 . VAL B 350 ? 1.9683 1.8683 2.2675 -0.1213 0.0505 0.2052 349 VAL B CG2 5812 N N . LEU B 351 ? 1.9908 1.8298 2.2906 -0.0931 0.0153 0.1772 350 LEU B N 5813 C CA . LEU B 351 ? 2.0225 1.8196 2.3077 -0.0897 0.0088 0.1728 350 LEU B CA 5814 C C . LEU B 351 ? 1.9927 1.7905 2.3007 -0.1146 0.0075 0.1645 350 LEU B C 5815 O O . LEU B 351 ? 1.9281 1.7688 2.2677 -0.1214 0.0065 0.1555 350 LEU B O 5816 C CB . LEU B 351 ? 2.0284 1.8368 2.3115 -0.0628 0.0008 0.1642 350 LEU B CB 5817 C CG . LEU B 351 ? 2.0475 1.8506 2.3071 -0.0351 -0.0008 0.1723 350 LEU B CG 5818 C CD1 . LEU B 351 ? 2.0001 1.8537 2.2756 -0.0303 0.0003 0.1743 350 LEU B CD1 5819 C CD2 . LEU B 351 ? 2.0504 1.8458 2.3021 -0.0097 -0.0075 0.1654 350 LEU B CD2 5820 N N . LEU B 352 ? 2.0192 1.7685 2.3109 -0.1287 0.0068 0.1678 351 LEU B N 5821 C CA . LEU B 352 ? 2.0019 1.7485 2.3139 -0.1531 0.0028 0.1598 351 LEU B CA 5822 C C . LEU B 352 ? 1.9935 1.7088 2.2898 -0.1431 -0.0082 0.1481 351 LEU B C 5823 O O . LEU B 352 ? 2.0331 1.7047 2.2950 -0.1256 -0.0104 0.1503 351 LEU B O 5824 C CB . LEU B 352 ? 2.0632 1.7794 2.3715 -0.1801 0.0087 0.1707 351 LEU B CB 5825 C CG . LEU B 352 ? 2.0609 1.8195 2.4000 -0.1999 0.0198 0.1776 351 LEU B CG 5826 C CD1 . LEU B 352 ? 2.0409 1.8360 2.3799 -0.1821 0.0274 0.1824 351 LEU B CD1 5827 C CD2 . LEU B 352 ? 2.1316 1.8566 2.4627 -0.2241 0.0278 0.1915 351 LEU B CD2 5828 N N . GLN B 353 ? 1.9484 1.6849 2.2677 -0.1529 -0.0149 0.1356 352 GLN B N 5829 C CA . GLN B 353 ? 1.9644 1.6735 2.2671 -0.1432 -0.0251 0.1233 352 GLN B CA 5830 C C . GLN B 353 ? 1.9708 1.6766 2.2897 -0.1683 -0.0339 0.1140 352 GLN B C 5831 O O . GLN B 353 ? 1.8606 1.6124 2.2123 -0.1770 -0.0357 0.1084 352 GLN B O 5832 C CB . GLN B 353 ? 1.9195 1.6644 2.2284 -0.1173 -0.0262 0.1156 352 GLN B CB 5833 C CG . GLN B 353 ? 1.9279 1.6451 2.2143 -0.1012 -0.0338 0.1039 352 GLN B CG 5834 C CD . GLN B 353 ? 1.9882 1.6489 2.2325 -0.0821 -0.0336 0.1075 352 GLN B CD 5835 O OE1 . GLN B 353 ? 1.9457 1.6124 2.1785 -0.0538 -0.0306 0.1089 352 GLN B OE1 5836 N NE2 . GLN B 353 ? 2.0804 1.6859 2.3027 -0.0977 -0.0371 0.1093 352 GLN B NE2 5837 N N . GLU B 354 ? 2.0636 1.7130 2.3582 -0.1796 -0.0404 0.1124 353 GLU B N 5838 C CA . GLU B 354 ? 2.0876 1.7271 2.3925 -0.2029 -0.0520 0.1024 353 GLU B CA 5839 C C . GLU B 354 ? 2.0865 1.7285 2.3821 -0.1865 -0.0618 0.0866 353 GLU B C 5840 O O . GLU B 354 ? 2.0759 1.6972 2.3421 -0.1590 -0.0607 0.0830 353 GLU B O 5841 C CB . GLU B 354 ? 2.1721 1.7449 2.4502 -0.2205 -0.0572 0.1050 353 GLU B CB 5842 C CG . GLU B 354 ? 2.2061 1.7692 2.4981 -0.2502 -0.0708 0.0960 353 GLU B CG 5843 C CD . GLU B 354 ? 2.2992 1.7933 2.5645 -0.2700 -0.0767 0.0986 353 GLU B CD 5844 O OE1 . GLU B 354 ? 2.3446 1.8101 2.5943 -0.2708 -0.0667 0.1125 353 GLU B OE1 5845 O OE2 . GLU B 354 ? 2.3189 1.7858 2.5778 -0.2856 -0.0920 0.0868 353 GLU B OE2 5846 N N . LEU B 355 ? 2.1045 1.7728 2.4251 -0.2030 -0.0707 0.0780 354 LEU B N 5847 C CA . LEU B 355 ? 2.1439 1.8128 2.4543 -0.1912 -0.0808 0.0633 354 LEU B CA 5848 C C . LEU B 355 ? 2.1787 1.8170 2.4838 -0.2152 -0.0970 0.0537 354 LEU B C 5849 O O . LEU B 355 ? 2.0942 1.7677 2.4311 -0.2332 -0.1045 0.0502 354 LEU B O 5850 C CB . LEU B 355 ? 2.1263 1.8614 2.4716 -0.1854 -0.0778 0.0618 354 LEU B CB 5851 C CG . LEU B 355 ? 2.1396 1.9043 2.4870 -0.1594 -0.0651 0.0677 354 LEU B CG 5852 C CD1 . LEU B 355 ? 2.0904 1.9194 2.4794 -0.1633 -0.0607 0.0700 354 LEU B CD1 5853 C CD2 . LEU B 355 ? 2.1962 1.9435 2.5133 -0.1312 -0.0662 0.0596 354 LEU B CD2 5854 N N . PRO B 356 ? 2.2905 1.8619 2.5551 -0.2153 -0.1034 0.0492 355 PRO B N 5855 C CA . PRO B 356 ? 2.3463 1.8837 2.6050 -0.2420 -0.1202 0.0406 355 PRO B CA 5856 C C . PRO B 356 ? 2.3327 1.8811 2.5879 -0.2386 -0.1343 0.0250 355 PRO B C 5857 O O . PRO B 356 ? 2.3295 1.8658 2.5547 -0.2111 -0.1333 0.0167 355 PRO B O 5858 C CB . PRO B 356 ? 2.4474 1.9054 2.6560 -0.2361 -0.1223 0.0388 355 PRO B CB 5859 C CG . PRO B 356 ? 2.4474 1.9005 2.6291 -0.1972 -0.1107 0.0397 355 PRO B CG 5860 C CD . PRO B 356 ? 2.3630 1.8865 2.5839 -0.1890 -0.0970 0.0506 355 PRO B CD 5861 N N . GLY B 357 ? 2.3288 1.9019 2.6150 -0.2659 -0.1468 0.0218 356 GLY B N 5862 C CA . GLY B 357 ? 2.3571 1.9403 2.6401 -0.2657 -0.1627 0.0077 356 GLY B CA 5863 C C . GLY B 357 ? 2.3221 1.9686 2.6306 -0.2488 -0.1563 0.0086 356 GLY B C 5864 O O . GLY B 357 ? 2.3208 1.9753 2.6218 -0.2435 -0.1673 -0.0018 356 GLY B O 5865 N N . SER B 358 ? 2.2850 1.9743 2.6217 -0.2407 -0.1390 0.0210 357 SER B N 5866 C CA . SER B 358 ? 2.2230 1.9700 2.5847 -0.2261 -0.1325 0.0225 357 SER B CA 5867 C C . SER B 358 ? 2.1873 1.9871 2.6008 -0.2483 -0.1356 0.0275 357 SER B C 5868 O O . SER B 358 ? 2.1899 2.0056 2.6311 -0.2640 -0.1280 0.0378 357 SER B O 5869 C CB . SER B 358 ? 2.1902 1.9540 2.5511 -0.2026 -0.1133 0.0314 357 SER B CB 5870 O OG . SER B 358 ? 2.1875 1.9740 2.5776 -0.2149 -0.1030 0.0440 357 SER B OG 5871 N N . GLU B 359 ? 2.1648 1.9916 2.5902 -0.2481 -0.1462 0.0206 358 GLU B N 5872 C CA . GLU B 359 ? 2.1103 1.9897 2.5851 -0.2649 -0.1500 0.0248 358 GLU B CA 5873 C C . GLU B 359 ? 2.0300 1.9590 2.5344 -0.2529 -0.1322 0.0344 358 GLU B C 5874 O O . GLU B 359 ? 1.9937 1.9239 2.4813 -0.2297 -0.1211 0.0354 358 GLU B O 5875 C CB . GLU B 359 ? 2.1241 2.0139 2.5982 -0.2659 -0.1681 0.0148 358 GLU B CB 5876 C CG . GLU B 359 ? 2.0958 2.0281 2.6175 -0.2880 -0.1788 0.0171 358 GLU B CG 5877 C CD . GLU B 359 ? 2.0255 2.0160 2.5833 -0.2780 -0.1701 0.0232 358 GLU B CD 5878 O OE1 . GLU B 359 ? 1.9865 1.9832 2.5279 -0.2554 -0.1645 0.0214 358 GLU B OE1 5879 O OE2 . GLU B 359 ? 1.9684 1.9983 2.5716 -0.2928 -0.1684 0.0300 358 GLU B OE2 5880 N N . HIS B 360 ? 1.9839 1.9541 2.5330 -0.2691 -0.1300 0.0411 359 HIS B N 5881 C CA . HIS B 360 ? 1.9179 1.9332 2.4968 -0.2614 -0.1138 0.0497 359 HIS B CA 5882 C C . HIS B 360 ? 1.9120 1.9480 2.4849 -0.2373 -0.1090 0.0473 359 HIS B C 5883 O O . HIS B 360 ? 1.8963 1.9422 2.4670 -0.2231 -0.0946 0.0523 359 HIS B O 5884 C CB . HIS B 360 ? 1.8655 1.9233 2.4930 -0.2811 -0.1162 0.0541 359 HIS B CB 5885 C CG . HIS B 360 ? 1.8032 1.9054 2.4610 -0.2743 -0.1000 0.0619 359 HIS B CG 5886 N ND1 . HIS B 360 ? 1.7833 1.9181 2.4541 -0.2598 -0.0990 0.0599 359 HIS B ND1 5887 C CD2 . HIS B 360 ? 1.7809 1.8981 2.4564 -0.2802 -0.0843 0.0714 359 HIS B CD2 5888 C CE1 . HIS B 360 ? 1.7615 1.9279 2.4561 -0.2568 -0.0841 0.0667 359 HIS B CE1 5889 N NE2 . HIS B 360 ? 1.7559 1.9133 2.4532 -0.2685 -0.0747 0.0735 359 HIS B NE2 5890 N N . ILE B 361 ? 1.9408 1.9828 2.5105 -0.2333 -0.1216 0.0401 360 ILE B N 5891 C CA . ILE B 361 ? 1.9229 1.9833 2.4872 -0.2125 -0.1172 0.0387 360 ILE B CA 5892 C C . ILE B 361 ? 1.9349 1.9591 2.4541 -0.1939 -0.1158 0.0336 360 ILE B C 5893 O O . ILE B 361 ? 1.8892 1.9235 2.4020 -0.1758 -0.1043 0.0362 360 ILE B O 5894 C CB . ILE B 361 ? 1.9172 2.0025 2.4984 -0.2153 -0.1302 0.0352 360 ILE B CB 5895 C CG1 . ILE B 361 ? 1.8839 2.0117 2.5136 -0.2288 -0.1291 0.0410 360 ILE B CG1 5896 C CG2 . ILE B 361 ? 1.8894 1.9863 2.4591 -0.1944 -0.1256 0.0344 360 ILE B CG2 5897 C CD1 . ILE B 361 ? 1.9162 2.0418 2.5645 -0.2528 -0.1409 0.0405 360 ILE B CD1 5898 N N . GLU B 362 ? 1.9778 1.9604 2.4666 -0.1986 -0.1275 0.0262 361 GLU B N 5899 C CA . GLU B 362 ? 2.0324 1.9778 2.4758 -0.1796 -0.1263 0.0201 361 GLU B CA 5900 C C . GLU B 362 ? 1.9804 1.9143 2.4110 -0.1649 -0.1102 0.0256 361 GLU B C 5901 O O . GLU B 362 ? 1.9654 1.8878 2.3699 -0.1435 -0.1038 0.0236 361 GLU B O 5902 C CB . GLU B 362 ? 2.1991 2.0958 2.6102 -0.1891 -0.1422 0.0104 361 GLU B CB 5903 C CG . GLU B 362 ? 2.3206 2.2234 2.7341 -0.1993 -0.1612 0.0030 361 GLU B CG 5904 C CD . GLU B 362 ? 2.5233 2.3783 2.9087 -0.2138 -0.1794 -0.0070 361 GLU B CD 5905 O OE1 . GLU B 362 ? 2.6721 2.4791 3.0201 -0.2071 -0.1767 -0.0112 361 GLU B OE1 5906 O OE2 . GLU B 362 ? 2.6334 2.4980 3.0341 -0.2317 -0.1974 -0.0109 361 GLU B OE2 5907 N N . MET B 363 ? 1.9384 1.8770 2.3876 -0.1758 -0.1034 0.0332 362 MET B N 5908 C CA . MET B 363 ? 1.9217 1.8499 2.3589 -0.1623 -0.0897 0.0394 362 MET B CA 5909 C C . MET B 363 ? 1.8601 1.8221 2.3053 -0.1417 -0.0783 0.0429 362 MET B C 5910 O O . MET B 363 ? 1.8523 1.8030 2.2791 -0.1239 -0.0698 0.0453 362 MET B O 5911 C CB . MET B 363 ? 1.9193 1.8522 2.3768 -0.1785 -0.0838 0.0484 362 MET B CB 5912 C CG . MET B 363 ? 1.8903 1.8749 2.3871 -0.1818 -0.0750 0.0554 362 MET B CG 5913 S SD . MET B 363 ? 1.9524 1.9423 2.4692 -0.1996 -0.0659 0.0663 362 MET B SD 5914 C CE . MET B 363 ? 1.9864 1.9482 2.4709 -0.1807 -0.0550 0.0723 362 MET B CE 5915 N N . LEU B 364 ? 1.8035 1.8066 2.2770 -0.1444 -0.0786 0.0436 363 LEU B N 5916 C CA . LEU B 364 ? 1.7548 1.7908 2.2392 -0.1285 -0.0689 0.0469 363 LEU B CA 5917 C C . LEU B 364 ? 1.7928 1.8191 2.2513 -0.1086 -0.0676 0.0427 363 LEU B C 5918 O O . LEU B 364 ? 1.7493 1.7969 2.2127 -0.0941 -0.0581 0.0464 363 LEU B O 5919 C CB . LEU B 364 ? 1.6785 1.7558 2.1980 -0.1372 -0.0701 0.0486 363 LEU B CB 5920 C CG . LEU B 364 ? 1.6297 1.7297 2.1804 -0.1514 -0.0660 0.0542 363 LEU B CG 5921 C CD1 . LEU B 364 ? 1.5922 1.7289 2.1739 -0.1565 -0.0679 0.0545 363 LEU B CD1 5922 C CD2 . LEU B 364 ? 1.6087 1.7157 2.1598 -0.1429 -0.0537 0.0603 363 LEU B CD2 5923 N N . ALA B 365 ? 1.8609 1.8563 2.2924 -0.1085 -0.0770 0.0350 364 ALA B N 5924 C CA . ALA B 365 ? 1.9217 1.9047 2.3241 -0.0889 -0.0747 0.0306 364 ALA B CA 5925 C C . ALA B 365 ? 1.9857 1.9189 2.3473 -0.0791 -0.0758 0.0251 364 ALA B C 5926 O O . ALA B 365 ? 2.0480 1.9618 2.3786 -0.0633 -0.0750 0.0194 364 ALA B O 5927 C CB . ALA B 365 ? 1.9343 1.9223 2.3334 -0.0935 -0.0847 0.0254 364 ALA B CB 5928 N N . ASN B 366 ? 1.9857 1.8965 2.3456 -0.0877 -0.0766 0.0272 365 ASN B N 5929 C CA . ASN B 366 ? 2.0324 1.8895 2.3528 -0.0805 -0.0789 0.0221 365 ASN B CA 5930 C C . ASN B 366 ? 1.9676 1.8208 2.2737 -0.0548 -0.0656 0.0265 365 ASN B C 5931 O O . ASN B 366 ? 1.9168 1.7993 2.2465 -0.0515 -0.0568 0.0355 365 ASN B O 5932 C CB . ASN B 366 ? 2.1065 1.9378 2.4303 -0.1025 -0.0857 0.0237 365 ASN B CB 5933 C CG . ASN B 366 ? 2.2597 2.0278 2.5399 -0.0988 -0.0913 0.0169 365 ASN B CG 5934 O OD1 . ASN B 366 ? 2.3278 2.0734 2.5810 -0.0758 -0.0833 0.0168 365 ASN B OD1 5935 N ND2 . ASN B 366 ? 2.3669 2.1057 2.6403 -0.1210 -0.1055 0.0110 365 ASN B ND2 5936 N N . ALA B 367 ? 1.9427 1.7592 2.2092 -0.0359 -0.0647 0.0196 366 ALA B N 5937 C CA . ALA B 367 ? 1.9057 1.7195 2.1578 -0.0078 -0.0521 0.0230 366 ALA B CA 5938 C C . ALA B 367 ? 1.8806 1.6805 2.1344 -0.0064 -0.0484 0.0309 366 ALA B C 5939 O O . ALA B 367 ? 1.8303 1.6525 2.0932 0.0114 -0.0383 0.0382 366 ALA B O 5940 C CB . ALA B 367 ? 1.9609 1.7313 2.1664 0.0118 -0.0521 0.0130 366 ALA B CB 5941 N N . THR B 368 ? 1.9138 1.6772 2.1588 -0.0255 -0.0568 0.0300 367 THR B N 5942 C CA . THR B 368 ? 1.9389 1.6855 2.1832 -0.0266 -0.0534 0.0389 367 THR B CA 5943 C C . THR B 368 ? 1.8640 1.6628 2.1499 -0.0358 -0.0479 0.0497 367 THR B C 5944 O O . THR B 368 ? 1.8491 1.6554 2.1377 -0.0240 -0.0408 0.0584 367 THR B O 5945 C CB . THR B 368 ? 1.9865 1.6816 2.2133 -0.0486 -0.0632 0.0364 367 THR B CB 5946 O OG1 . THR B 368 ? 2.0023 1.7184 2.2560 -0.0775 -0.0718 0.0344 367 THR B OG1 5947 C CG2 . THR B 368 ? 2.0322 1.6663 2.2114 -0.0378 -0.0692 0.0251 367 THR B CG2 5948 N N . THR B 369 ? 1.8195 1.6529 2.1359 -0.0559 -0.0517 0.0489 368 THR B N 5949 C CA . THR B 369 ? 1.7795 1.6621 2.1337 -0.0639 -0.0463 0.0573 368 THR B CA 5950 C C . THR B 369 ? 1.7307 1.6501 2.0951 -0.0418 -0.0377 0.0607 368 THR B C 5951 O O . THR B 369 ? 1.7037 1.6443 2.0815 -0.0374 -0.0321 0.0687 368 THR B O 5952 C CB . THR B 369 ? 1.7526 1.6662 2.1366 -0.0853 -0.0519 0.0545 368 THR B CB 5953 O OG1 . THR B 369 ? 1.8071 1.6899 2.1841 -0.1061 -0.0617 0.0504 368 THR B OG1 5954 C CG2 . THR B 369 ? 1.7054 1.6622 2.1247 -0.0942 -0.0460 0.0624 368 THR B CG2 5955 N N . LEU B 370 ? 1.7010 1.6281 2.0586 -0.0287 -0.0369 0.0548 369 LEU B N 5956 C CA . LEU B 370 ? 1.6617 1.6265 2.0320 -0.0094 -0.0285 0.0582 369 LEU B CA 5957 C C . LEU B 370 ? 1.6540 1.6059 2.0078 0.0137 -0.0225 0.0629 369 LEU B C 5958 O O . LEU B 370 ? 1.6069 1.5940 1.9801 0.0237 -0.0171 0.0696 369 LEU B O 5959 C CB . LEU B 370 ? 1.6860 1.6569 2.0484 -0.0007 -0.0276 0.0516 369 LEU B CB 5960 C CG . LEU B 370 ? 1.6645 1.6504 2.0416 -0.0196 -0.0342 0.0474 369 LEU B CG 5961 C CD1 . LEU B 370 ? 1.6658 1.6416 2.0206 -0.0088 -0.0342 0.0406 369 LEU B CD1 5962 C CD2 . LEU B 370 ? 1.6134 1.6501 2.0304 -0.0283 -0.0311 0.0534 369 LEU B CD2 5963 N N . ALA B 371 ? 1.6762 1.5770 1.9942 0.0225 -0.0244 0.0594 370 ALA B N 5964 C CA . ALA B 371 ? 1.7026 1.5846 2.0018 0.0460 -0.0195 0.0642 370 ALA B CA 5965 C C . ALA B 371 ? 1.7066 1.5963 2.0184 0.0397 -0.0196 0.0745 370 ALA B C 5966 O O . ALA B 371 ? 1.7450 1.6509 2.0604 0.0585 -0.0153 0.0814 370 ALA B O 5967 C CB . ALA B 371 ? 1.7622 1.5798 2.0174 0.0542 -0.0226 0.0576 370 ALA B CB 5968 N N . TYR B 372 ? 1.6742 1.5535 1.9924 0.0139 -0.0245 0.0758 371 TYR B N 5969 C CA . TYR B 372 ? 1.6417 1.5287 1.9699 0.0064 -0.0233 0.0858 371 TYR B CA 5970 C C . TYR B 372 ? 1.5717 1.5180 1.9341 0.0073 -0.0200 0.0900 371 TYR B C 5971 O O . TYR B 372 ? 1.5283 1.4881 1.8935 0.0175 -0.0180 0.0978 371 TYR B O 5972 C CB . TYR B 372 ? 1.6403 1.5072 1.9706 -0.0222 -0.0271 0.0867 371 TYR B CB 5973 C CG . TYR B 372 ? 1.6538 1.5113 1.9806 -0.0270 -0.0243 0.0979 371 TYR B CG 5974 C CD1 . TYR B 372 ? 1.7018 1.5069 1.9955 -0.0206 -0.0246 0.1028 371 TYR B CD1 5975 C CD2 . TYR B 372 ? 1.6075 1.5057 1.9607 -0.0369 -0.0211 0.1037 371 TYR B CD2 5976 C CE1 . TYR B 372 ? 1.7122 1.5069 1.9995 -0.0246 -0.0214 0.1145 371 TYR B CE1 5977 C CE2 . TYR B 372 ? 1.6080 1.4966 1.9539 -0.0404 -0.0178 0.1142 371 TYR B CE2 5978 C CZ . TYR B 372 ? 1.6525 1.4901 1.9656 -0.0344 -0.0178 0.1203 371 TYR B CZ 5979 O OH . TYR B 372 ? 1.6465 1.4729 1.9494 -0.0377 -0.0140 0.1322 371 TYR B OH 5980 N N . LEU B 373 ? 1.5618 1.5414 1.9485 -0.0032 -0.0206 0.0848 372 LEU B N 5981 C CA . LEU B 373 ? 1.5523 1.5849 1.9706 -0.0033 -0.0182 0.0874 372 LEU B CA 5982 C C . LEU B 373 ? 1.5578 1.6117 1.9777 0.0218 -0.0146 0.0905 372 LEU B C 5983 O O . LEU B 373 ? 1.5233 1.6072 1.9590 0.0257 -0.0143 0.0961 372 LEU B O 5984 C CB . LEU B 373 ? 1.5402 1.5971 1.9791 -0.0160 -0.0193 0.0811 372 LEU B CB 5985 C CG . LEU B 373 ? 1.5107 1.6149 1.9830 -0.0247 -0.0182 0.0828 372 LEU B CG 5986 C CD1 . LEU B 373 ? 1.5015 1.6074 1.9823 -0.0409 -0.0188 0.0866 372 LEU B CD1 5987 C CD2 . LEU B 373 ? 1.4875 1.6082 1.9745 -0.0337 -0.0194 0.0772 372 LEU B CD2 5988 N N . LYS B 374 ? 1.5904 1.6298 1.9940 0.0389 -0.0122 0.0867 373 LYS B N 5989 C CA . LYS B 374 ? 1.6388 1.6971 2.0436 0.0653 -0.0076 0.0902 373 LYS B CA 5990 C C . LYS B 374 ? 1.7152 1.7672 2.1123 0.0779 -0.0091 0.0985 373 LYS B C 5991 O O . LYS B 374 ? 1.6666 1.7569 2.0831 0.0892 -0.0086 0.1039 373 LYS B O 5992 C CB . LYS B 374 ? 1.7023 1.7304 2.0799 0.0835 -0.0038 0.0846 373 LYS B CB 5993 C CG . LYS B 374 ? 1.7032 1.7623 2.0939 0.0905 0.0021 0.0809 373 LYS B CG 5994 C CD . LYS B 374 ? 1.7385 1.8197 2.1328 0.1196 0.0097 0.0853 373 LYS B CD 5995 C CE . LYS B 374 ? 1.7524 1.8583 2.1540 0.1281 0.0183 0.0824 373 LYS B CE 5996 N NZ . LYS B 374 ? 1.7868 1.9056 2.1856 0.1594 0.0276 0.0858 373 LYS B NZ 5997 N N . ARG B 375 ? 1.8457 1.8482 2.2138 0.0757 -0.0115 0.0999 374 ARG B N 5998 C CA . ARG B 375 ? 1.9559 1.9432 2.3103 0.0863 -0.0133 0.1091 374 ARG B CA 5999 C C . ARG B 375 ? 1.9021 1.9258 2.2794 0.0747 -0.0159 0.1152 374 ARG B C 6000 O O . ARG B 375 ? 1.9491 1.9902 2.3290 0.0897 -0.0178 0.1223 374 ARG B O 6001 C CB . ARG B 375 ? 2.0944 2.0207 2.4158 0.0779 -0.0151 0.1102 374 ARG B CB 6002 C CG . ARG B 375 ? 2.2191 2.1144 2.5142 0.0979 -0.0158 0.1193 374 ARG B CG 6003 C CD . ARG B 375 ? 2.2926 2.1646 2.5770 0.0807 -0.0177 0.1276 374 ARG B CD 6004 N NE . ARG B 375 ? 2.3615 2.1778 2.6216 0.0640 -0.0181 0.1254 374 ARG B NE 6005 C CZ . ARG B 375 ? 2.3961 2.1814 2.6413 0.0495 -0.0181 0.1336 374 ARG B CZ 6006 N NH1 . ARG B 375 ? 2.4369 2.1731 2.6632 0.0326 -0.0190 0.1313 374 ARG B NH1 6007 N NH2 . ARG B 375 ? 2.3732 2.1761 2.6217 0.0509 -0.0173 0.1444 374 ARG B NH2 6008 N N . VAL B 376 ? 1.8279 1.8614 2.2200 0.0487 -0.0165 0.1122 375 VAL B N 6009 C CA . VAL B 376 ? 1.7924 1.8566 2.2028 0.0368 -0.0182 0.1164 375 VAL B CA 6010 C C . VAL B 376 ? 1.7176 1.8351 2.1564 0.0456 -0.0196 0.1159 375 VAL B C 6011 O O . VAL B 376 ? 1.6743 1.8126 2.1183 0.0511 -0.0231 0.1213 375 VAL B O 6012 C CB . VAL B 376 ? 1.7894 1.8546 2.2115 0.0090 -0.0173 0.1125 375 VAL B CB 6013 C CG1 . VAL B 376 ? 1.7856 1.8850 2.2265 -0.0009 -0.0178 0.1150 375 VAL B CG1 6014 C CG2 . VAL B 376 ? 1.8267 1.8431 2.2246 -0.0023 -0.0164 0.1148 375 VAL B CG2 6015 N N . LEU B 377 ? 1.6902 1.8283 2.1457 0.0464 -0.0172 0.1098 376 LEU B N 6016 C CA . LEU B 377 ? 1.6806 1.8698 2.1669 0.0499 -0.0178 0.1093 376 LEU B CA 6017 C C . LEU B 377 ? 1.7358 1.9443 2.2253 0.0754 -0.0182 0.1143 376 LEU B C 6018 O O . LEU B 377 ? 1.7461 1.9929 2.2565 0.0781 -0.0225 0.1176 376 LEU B O 6019 C CB . LEU B 377 ? 1.6335 1.8362 2.1351 0.0416 -0.0139 0.1027 376 LEU B CB 6020 C CG . LEU B 377 ? 1.6010 1.7950 2.1071 0.0173 -0.0145 0.0976 376 LEU B CG 6021 C CD1 . LEU B 377 ? 1.5902 1.7907 2.1040 0.0141 -0.0114 0.0921 376 LEU B CD1 6022 C CD2 . LEU B 377 ? 1.5522 1.7741 2.0792 0.0028 -0.0174 0.0984 376 LEU B CD2 6023 N N . LEU B 378 ? 1.8195 2.0021 2.2889 0.0943 -0.0142 0.1144 377 LEU B N 6024 C CA . LEU B 378 ? 1.8730 2.0759 2.3476 0.1214 -0.0126 0.1189 377 LEU B CA 6025 C C . LEU B 378 ? 1.9056 2.0836 2.3567 0.1405 -0.0166 0.1262 377 LEU B C 6026 O O . LEU B 378 ? 1.9101 2.1132 2.3707 0.1626 -0.0181 0.1317 377 LEU B O 6027 C CB . LEU B 378 ? 1.9139 2.1086 2.3820 0.1345 -0.0039 0.1143 377 LEU B CB 6028 C CG . LEU B 378 ? 1.9042 2.1167 2.3892 0.1173 0.0003 0.1079 377 LEU B CG 6029 C CD1 . LEU B 378 ? 1.9248 2.1350 2.4021 0.1351 0.0099 0.1049 377 LEU B CD1 6030 C CD2 . LEU B 378 ? 1.8672 2.1341 2.3916 0.1042 -0.0021 0.1099 377 LEU B CD2 6031 N N . GLY B 379 ? 1.9275 2.0575 2.3493 0.1319 -0.0185 0.1272 378 GLY B N 6032 C CA . GLY B 379 ? 1.9677 2.0679 2.3631 0.1480 -0.0223 0.1356 378 GLY B CA 6033 C C . GLY B 379 ? 1.9704 2.0990 2.3770 0.1438 -0.0301 0.1425 378 GLY B C 6034 O O . GLY B 379 ? 1.8625 2.0240 2.2928 0.1242 -0.0322 0.1393 378 GLY B O 6035 N N . PRO B 380 ? 2.0431 2.1561 2.4298 0.1630 -0.0349 0.1517 379 PRO B N 6036 C CA . PRO B 380 ? 2.0396 2.1852 2.4359 0.1679 -0.0444 0.1589 379 PRO B CA 6037 C C . PRO B 380 ? 2.0152 2.1651 2.4120 0.1416 -0.0474 0.1584 379 PRO B C 6038 O O . PRO B 380 ? 2.0710 2.1827 2.4483 0.1246 -0.0424 0.1576 379 PRO B O 6039 C CB . PRO B 380 ? 2.0773 2.1854 2.4399 0.1925 -0.0477 0.1693 379 PRO B CB 6040 C CG . PRO B 380 ? 2.1021 2.1677 2.4448 0.2058 -0.0396 0.1666 379 PRO B CG 6041 C CD . PRO B 380 ? 2.0816 2.1372 2.4304 0.1803 -0.0324 0.1560 379 PRO B CD 6042 C C1 . NAG C . ? 1.8465 2.1375 2.2362 0.1792 -0.2959 0.0874 401 NAG A C1 6043 C C2 . NAG C . ? 1.8189 2.1504 2.2654 0.1928 -0.3055 0.0870 401 NAG A C2 6044 C C3 . NAG C . ? 1.9018 2.2404 2.3366 0.2165 -0.3359 0.0930 401 NAG A C3 6045 C C4 . NAG C . ? 1.9872 2.3284 2.3945 0.2091 -0.3609 0.0855 401 NAG A C4 6046 C C5 . NAG C . ? 1.9483 2.2500 2.3037 0.1908 -0.3454 0.0838 401 NAG A C5 6047 C C6 . NAG C . ? 1.9090 2.2152 2.2416 0.1807 -0.3678 0.0736 401 NAG A C6 6048 C C7 . NAG C . ? 1.7022 2.0411 2.2051 0.1898 -0.2637 0.0887 401 NAG A C7 6049 C C8 . NAG C . ? 1.6713 1.9907 2.1775 0.2000 -0.2409 0.0971 401 NAG A C8 6050 N N2 . NAG C . ? 1.7731 2.0928 2.2328 0.2007 -0.2821 0.0947 401 NAG A N2 6051 O O3 . NAG C . ? 1.8551 2.2389 2.3506 0.2281 -0.3466 0.0906 401 NAG A O3 6052 O O4 . NAG C . ? 2.1160 2.4538 2.4973 0.2323 -0.3898 0.0923 401 NAG A O4 6053 O O5 . NAG C . ? 1.9067 2.2099 2.2857 0.1709 -0.3176 0.0784 401 NAG A O5 6054 O O6 . NAG C . ? 1.7933 2.1366 2.1719 0.1600 -0.3700 0.0579 401 NAG A O6 6055 O O7 . NAG C . ? 1.6612 2.0287 2.1970 0.1723 -0.2638 0.0768 401 NAG A O7 6056 C C1 . NAG D . ? 2.2319 2.6147 2.6645 0.2499 -0.4125 0.0912 402 NAG A C1 6057 C C2 . NAG D . ? 2.2465 2.6853 2.7383 0.2328 -0.4288 0.0729 402 NAG A C2 6058 C C3 . NAG D . ? 2.3087 2.7942 2.8396 0.2505 -0.4656 0.0690 402 NAG A C3 6059 C C4 . NAG D . ? 2.4250 2.8839 2.9014 0.2789 -0.4908 0.0815 402 NAG A C4 6060 C C5 . NAG D . ? 2.4377 2.8501 2.8786 0.2969 -0.4661 0.1004 402 NAG A C5 6061 C C6 . NAG D . ? 2.5211 2.9030 2.9072 0.3281 -0.4884 0.1150 402 NAG A C6 6062 C C7 . NAG D . ? 2.1314 2.6087 2.7039 0.1905 -0.3909 0.0538 402 NAG A C7 6063 C C8 . NAG D . ? 2.1054 2.5809 2.6533 0.1722 -0.4064 0.0421 402 NAG A C8 6064 N N2 . NAG D . ? 2.1904 2.6512 2.7371 0.2176 -0.4018 0.0673 402 NAG A N2 6065 O O3 . NAG D . ? 2.2773 2.7990 2.8359 0.2313 -0.4852 0.0513 402 NAG A O3 6066 O O4 . NAG D . ? 2.4756 2.9831 2.9968 0.2971 -0.5251 0.0777 402 NAG A O4 6067 O O5 . NAG D . ? 2.3449 2.7116 2.7404 0.2775 -0.4364 0.1023 402 NAG A O5 6068 O O6 . NAG D . ? 2.5684 2.8985 2.9134 0.3406 -0.4618 0.1319 402 NAG A O6 6069 O O7 . NAG D . ? 2.0852 2.5765 2.6987 0.1806 -0.3674 0.0508 402 NAG A O7 6070 C C1 . BMA E . ? 2.4940 2.9952 2.9717 0.3086 -0.5628 0.0767 403 BMA A C1 6071 C C2 . BMA E . ? 2.4903 3.0386 3.0132 0.3358 -0.5983 0.0770 403 BMA A C2 6072 C C3 . BMA E . ? 2.5163 3.0557 2.9878 0.3490 -0.6409 0.0757 403 BMA A C3 6073 C C4 . BMA E . ? 2.4863 3.0278 2.9409 0.3184 -0.6502 0.0578 403 BMA A C4 6074 C C5 . BMA E . ? 2.4316 2.9289 2.8513 0.2916 -0.6085 0.0584 403 BMA A C5 6075 C C6 . BMA E . ? 2.3634 2.8657 2.7747 0.2608 -0.6146 0.0398 403 BMA A C6 6076 O O2 . BMA E . ? 2.4575 3.0728 3.0704 0.3212 -0.6031 0.0604 403 BMA A O2 6077 O O3 . BMA E . ? 2.5307 3.1222 3.0519 0.3720 -0.6780 0.0728 403 BMA A O3 6078 O O4 . BMA E . ? 2.5298 3.0461 2.9172 0.3319 -0.6842 0.0594 403 BMA A O4 6079 O O5 . BMA E . ? 2.4537 2.9682 2.9300 0.2821 -0.5744 0.0593 403 BMA A O5 6080 O O6 . BMA E . ? 2.2906 2.7322 2.6293 0.2496 -0.5899 0.0455 403 BMA A O6 6081 C C1 . NAG F . ? 2.5585 2.4412 2.6682 -0.0588 0.1823 0.0448 404 NAG A C1 6082 C C2 . NAG F . ? 2.6507 2.4961 2.7295 -0.0639 0.2162 0.0490 404 NAG A C2 6083 C C3 . NAG F . ? 2.6844 2.5005 2.7045 -0.0529 0.2148 0.0547 404 NAG A C3 6084 C C4 . NAG F . ? 2.6933 2.4922 2.6724 -0.0394 0.1877 0.0648 404 NAG A C4 6085 C C5 . NAG F . ? 2.6175 2.4572 2.6368 -0.0365 0.1563 0.0602 404 NAG A C5 6086 C C6 . NAG F . ? 2.6060 2.4312 2.5927 -0.0236 0.1321 0.0702 404 NAG A C6 6087 C C7 . NAG F . ? 2.5935 2.4477 2.7322 -0.0897 0.2691 0.0377 404 NAG A C7 6088 C C8 . NAG F . ? 2.5918 2.4016 2.6922 -0.0911 0.2810 0.0493 404 NAG A C8 6089 N N2 . NAG F . ? 2.6201 2.4869 2.7448 -0.0769 0.2398 0.0384 404 NAG A N2 6090 O O3 . NAG F . ? 2.7309 2.5067 2.7155 -0.0568 0.2476 0.0597 404 NAG A O3 6091 O O4 . NAG F . ? 2.7263 2.5034 2.6544 -0.0295 0.1811 0.0678 404 NAG A O4 6092 O O5 . NAG F . ? 2.5989 2.4629 2.6702 -0.0469 0.1616 0.0548 404 NAG A O5 6093 O O6 . NAG F . ? 2.5648 2.3643 2.5399 -0.0241 0.1428 0.0790 404 NAG A O6 6094 O O7 . NAG F . ? 2.5642 2.4423 2.7477 -0.1004 0.2871 0.0275 404 NAG A O7 6095 C C1 . NAG G . ? 2.2973 2.1623 2.7922 -0.2722 0.2656 -0.0683 405 NAG A C1 6096 C C2 . NAG G . ? 2.3564 2.1887 2.8496 -0.2893 0.2746 -0.0770 405 NAG A C2 6097 C C3 . NAG G . ? 2.3659 2.2239 2.9175 -0.3193 0.2849 -0.0994 405 NAG A C3 6098 C C4 . NAG G . ? 2.3941 2.2700 2.9748 -0.3302 0.3089 -0.1008 405 NAG A C4 6099 C C5 . NAG G . ? 2.3466 2.2534 2.9228 -0.3083 0.2961 -0.0906 405 NAG A C5 6100 C C6 . NAG G . ? 2.3364 2.2534 2.9339 -0.3171 0.3239 -0.0902 405 NAG A C6 6101 C C7 . NAG G . ? 2.3777 2.1681 2.8154 -0.2679 0.2474 -0.0694 405 NAG A C7 6102 C C8 . NAG G . ? 2.3315 2.1328 2.7654 -0.2579 0.2189 -0.0750 405 NAG A C8 6103 N N2 . NAG G . ? 2.3452 2.1814 2.8282 -0.2786 0.2464 -0.0801 405 NAG A N2 6104 O O3 . NAG G . ? 2.3933 2.2082 2.9354 -0.3374 0.3030 -0.1048 405 NAG A O3 6105 O O4 . NAG G . ? 2.4014 2.3186 3.0477 -0.3545 0.3082 -0.1242 405 NAG A O4 6106 O O5 . NAG G . ? 2.3553 2.2256 2.8696 -0.2842 0.2916 -0.0694 405 NAG A O5 6107 O O6 . NAG G . ? 2.3401 2.1984 2.8887 -0.3167 0.3563 -0.0738 405 NAG A O6 6108 O O7 . NAG G . ? 2.4395 2.1793 2.8383 -0.2649 0.2706 -0.0553 405 NAG A O7 6109 C C1 . NAG H . ? 2.1574 2.4313 2.6109 0.1695 -0.2328 -0.0649 406 NAG A C1 6110 C C2 . NAG H . ? 2.1820 2.4567 2.6241 0.1628 -0.2496 -0.0704 406 NAG A C2 6111 C C3 . NAG H . ? 2.2157 2.5271 2.6913 0.1722 -0.2754 -0.0822 406 NAG A C3 6112 C C4 . NAG H . ? 2.1966 2.5532 2.7344 0.1703 -0.2712 -0.0902 406 NAG A C4 6113 C C5 . NAG H . ? 2.1605 2.5073 2.6985 0.1797 -0.2525 -0.0819 406 NAG A C5 6114 C C6 . NAG H . ? 2.0850 2.4739 2.6827 0.1787 -0.2449 -0.0895 406 NAG A C6 6115 C C7 . NAG H . ? 2.1351 2.3344 2.4869 0.1596 -0.2361 -0.0544 406 NAG A C7 6116 C C8 . NAG H . ? 2.1547 2.3107 2.4495 0.1699 -0.2400 -0.0468 406 NAG A C8 6117 N N2 . NAG H . ? 2.1800 2.4114 2.5643 0.1710 -0.2535 -0.0622 406 NAG A N2 6118 O O3 . NAG H . ? 2.1901 2.5062 2.6627 0.1600 -0.2877 -0.0899 406 NAG A O3 6119 O O4 . NAG H . ? 2.2049 2.5941 2.7721 0.1840 -0.2972 -0.1001 406 NAG A O4 6120 O O5 . NAG H . ? 2.1767 2.4920 2.6850 0.1655 -0.2297 -0.0731 406 NAG A O5 6121 O O6 . NAG H . ? 1.9830 2.3633 2.5836 0.1651 -0.2169 -0.0849 406 NAG A O6 6122 O O7 . NAG H . ? 2.0676 2.2711 2.4336 0.1423 -0.2174 -0.0531 406 NAG A O7 6123 C C1 . MAY I . ? 1.8423 2.0236 2.2352 -0.0007 -0.0791 -0.0197 407 MAY A C1 6124 O O1 . MAY I . ? 1.9196 2.0978 2.3068 -0.0085 -0.0691 -0.0120 407 MAY A O1 6125 P P1 . MAY I . ? 1.9580 2.1434 2.3558 -0.0073 -0.0709 -0.0173 407 MAY A P1 6126 C C2 . MAY I . ? 1.7477 1.9168 2.1269 0.0004 -0.0785 -0.0153 407 MAY A C2 6127 O O2 . MAY I . ? 2.0125 2.2002 2.4183 -0.0131 -0.0676 -0.0181 407 MAY A O2 6128 C C3 . MAY I . ? 1.6331 1.7935 2.0017 0.0068 -0.0834 -0.0168 407 MAY A C3 6129 C CM . MAY I . ? 1.9352 2.1162 2.3373 -0.0142 -0.0693 -0.0170 407 MAY A CM 6130 C C1 . NAG J . ? 1.6713 2.4198 2.8447 0.0927 0.2372 0.0344 401 NAG B C1 6131 C C2 . NAG J . ? 1.6622 2.4011 2.8482 0.1169 0.2253 0.0294 401 NAG B C2 6132 C C3 . NAG J . ? 1.7319 2.4566 2.9009 0.1492 0.2467 0.0180 401 NAG B C3 6133 C C4 . NAG J . ? 1.7717 2.4735 2.8938 0.1519 0.2710 0.0087 401 NAG B C4 6134 C C5 . NAG J . ? 1.7223 2.4298 2.8297 0.1223 0.2744 0.0153 401 NAG B C5 6135 C C6 . NAG J . ? 1.7136 2.3751 2.7561 0.1219 0.2851 0.0035 401 NAG B C6 6136 C C7 . NAG J . ? 1.5055 2.2871 2.7663 0.1216 0.1898 0.0431 401 NAG B C7 6137 C C8 . NAG J . ? 1.4662 2.3054 2.7914 0.1229 0.1805 0.0554 401 NAG B C8 6138 N N2 . NAG J . ? 1.5774 2.3665 2.8249 0.1182 0.2151 0.0411 401 NAG B N2 6139 O O3 . NAG J . ? 1.7610 2.4407 2.9072 0.1632 0.2301 0.0090 401 NAG B O3 6140 O O4 . NAG J . ? 1.8307 2.5647 2.9728 0.1765 0.2997 0.0079 401 NAG B O4 6141 O O5 . NAG J . ? 1.7017 2.4050 2.8167 0.0965 0.2479 0.0226 401 NAG B O5 6142 O O6 . NAG J . ? 1.6540 2.2616 2.6565 0.1171 0.2626 -0.0064 401 NAG B O6 6143 O O7 . NAG J . ? 1.4663 2.1982 2.6905 0.1232 0.1740 0.0361 401 NAG B O7 6144 C C1 . NAG K . ? 1.9409 2.6389 3.0478 0.2064 0.3128 -0.0075 402 NAG B C1 6145 C C2 . NAG K . ? 1.9885 2.6514 3.0910 0.2243 0.2932 -0.0152 402 NAG B C2 6146 C C3 . NAG K . ? 2.0843 2.7085 3.1492 0.2567 0.3098 -0.0321 402 NAG B C3 6147 C C4 . NAG K . ? 2.1425 2.7355 3.1493 0.2548 0.3287 -0.0440 402 NAG B C4 6148 C C5 . NAG K . ? 2.1016 2.7378 3.1206 0.2345 0.3452 -0.0326 402 NAG B C5 6149 C C6 . NAG K . ? 2.1341 2.7334 3.0888 0.2295 0.3586 -0.0434 402 NAG B C6 6150 C C7 . NAG K . ? 1.9507 2.6472 3.1302 0.2381 0.2600 -0.0014 402 NAG B C7 6151 C C8 . NAG K . ? 1.9489 2.5760 3.0786 0.2340 0.2388 -0.0115 402 NAG B C8 6152 N N2 . NAG K . ? 1.9752 2.6855 3.1412 0.2329 0.2847 -0.0032 402 NAG B N2 6153 O O3 . NAG K . ? 2.1049 2.6756 3.1449 0.2628 0.2876 -0.0408 402 NAG B O3 6154 O O4 . NAG K . ? 2.2485 2.8234 3.2320 0.2887 0.3515 -0.0577 402 NAG B O4 6155 O O5 . NAG K . ? 1.9893 2.6453 3.0346 0.2031 0.3238 -0.0189 402 NAG B O5 6156 O O6 . NAG K . ? 2.1821 2.8037 3.1338 0.2514 0.3930 -0.0457 402 NAG B O6 6157 O O7 . NAG K . ? 1.9249 2.6664 3.1588 0.2461 0.2537 0.0093 402 NAG B O7 6158 C C1 . BMA L . ? 2.2789 2.8204 3.2591 0.3148 0.3425 -0.0671 403 BMA B C1 6159 C C2 . BMA L . ? 2.3155 2.7767 3.2301 0.3129 0.3269 -0.0850 403 BMA B C2 6160 C C3 . BMA L . ? 2.3161 2.7421 3.2315 0.3388 0.3165 -0.0924 403 BMA B C3 6161 C C4 . BMA L . ? 2.3420 2.7933 3.2796 0.3786 0.3433 -0.0952 403 BMA B C4 6162 C C5 . BMA L . ? 2.2868 2.8241 3.2931 0.3770 0.3565 -0.0759 403 BMA B C5 6163 C C6 . BMA L . ? 2.3001 2.8732 3.3383 0.4171 0.3838 -0.0763 403 BMA B C6 6164 O O2 . BMA L . ? 2.3977 2.8305 3.2587 0.3212 0.3471 -0.0998 403 BMA B O2 6165 O O3 . BMA L . ? 2.3416 2.6923 3.1953 0.3373 0.3051 -0.1099 403 BMA B O3 6166 O O4 . BMA L . ? 2.3706 2.7927 3.3147 0.4028 0.3320 -0.0991 403 BMA B O4 6167 O O5 . BMA L . ? 2.2974 2.8606 3.2965 0.3516 0.3676 -0.0706 403 BMA B O5 6168 O O6 . BMA L . ? 2.3366 2.8716 3.3215 0.4399 0.4080 -0.0945 403 BMA B O6 6169 C C1 . NAG M . ? 2.0932 2.5613 3.0000 -0.4059 0.3112 0.2870 404 NAG B C1 6170 C C2 . NAG M . ? 2.0940 2.5717 2.9963 -0.4164 0.3460 0.3083 404 NAG B C2 6171 C C3 . NAG M . ? 2.0989 2.5766 2.9571 -0.3868 0.3656 0.3056 404 NAG B C3 6172 C C4 . NAG M . ? 2.0540 2.5757 2.9395 -0.3636 0.3626 0.2873 404 NAG B C4 6173 C C5 . NAG M . ? 1.9809 2.4928 2.8767 -0.3580 0.3270 0.2683 404 NAG B C5 6174 C C6 . NAG M . ? 1.8883 2.4429 2.8146 -0.3369 0.3237 0.2519 404 NAG B C6 6175 C C7 . NAG M . ? 2.0621 2.4914 2.9707 -0.4724 0.3461 0.3377 404 NAG B C7 6176 C C8 . NAG M . ? 2.0168 2.5053 3.0041 -0.4920 0.3440 0.3371 404 NAG B C8 6177 N N2 . NAG M . ? 2.0867 2.5154 2.9607 -0.4388 0.3465 0.3246 404 NAG B N2 6178 O O3 . NAG M . ? 2.1148 2.6051 2.9681 -0.3942 0.4000 0.3250 404 NAG B O3 6179 O O4 . NAG M . ? 2.0814 2.5955 2.9205 -0.3361 0.3766 0.2820 404 NAG B O4 6180 O O5 . NAG M . ? 2.0211 2.5338 2.9552 -0.3852 0.3107 0.2725 404 NAG B O5 6181 O O6 . NAG M . ? 1.8144 2.3424 2.6943 -0.3108 0.3131 0.2369 404 NAG B O6 6182 O O7 . NAG M . ? 2.0924 2.4726 2.9692 -0.4885 0.3465 0.3508 404 NAG B O7 6183 C C1 . NAG N . ? 2.1640 2.9635 3.8880 -0.9102 0.0363 0.3196 405 NAG B C1 6184 C C2 . NAG N . ? 2.1855 3.0528 3.9974 -0.9526 0.0466 0.3395 405 NAG B C2 6185 C C3 . NAG N . ? 2.2907 3.1068 4.1015 -1.0030 0.0211 0.3411 405 NAG B C3 6186 C C4 . NAG N . ? 2.3575 3.0618 4.0747 -1.0036 0.0235 0.3394 405 NAG B C4 6187 C C5 . NAG N . ? 2.3210 2.9755 3.9618 -0.9556 0.0123 0.3181 405 NAG B C5 6188 C C6 . NAG N . ? 2.3629 2.9105 3.9114 -0.9508 0.0153 0.3163 405 NAG B C6 6189 C C7 . NAG N . ? 2.0042 3.0362 3.9286 -0.9141 0.0598 0.3397 405 NAG B C7 6190 C C8 . NAG N . ? 1.9490 3.0732 3.9564 -0.9112 0.0414 0.3353 405 NAG B C8 6191 N N2 . NAG N . ? 2.0925 3.0545 3.9844 -0.9471 0.0342 0.3355 405 NAG B N2 6192 O O3 . NAG N . ? 2.3258 3.1957 4.2104 -1.0444 0.0380 0.3634 405 NAG B O3 6193 O O4 . NAG N . ? 2.4200 3.0727 4.1330 -1.0465 -0.0067 0.3360 405 NAG B O4 6194 O O5 . NAG N . ? 2.2407 2.9466 3.8885 -0.9160 0.0419 0.3218 405 NAG B O5 6195 O O6 . NAG N . ? 2.3057 2.8216 3.7926 -0.9042 0.0102 0.2991 405 NAG B O6 6196 O O7 . NAG N . ? 1.9783 3.0014 3.8671 -0.8861 0.0956 0.3465 405 NAG B O7 6197 C C1 . NAG O . ? 2.4989 2.1718 2.7281 -0.1196 -0.1127 0.0030 406 NAG B C1 6198 C C2 . NAG O . ? 2.5487 2.1964 2.7627 -0.1367 -0.1319 -0.0093 406 NAG B C2 6199 C C3 . NAG O . ? 2.6594 2.2326 2.8241 -0.1354 -0.1395 -0.0185 406 NAG B C3 6200 C C4 . NAG O . ? 2.6943 2.2390 2.8595 -0.1438 -0.1340 -0.0095 406 NAG B C4 6201 C C5 . NAG O . ? 2.6260 2.2058 2.8102 -0.1248 -0.1145 0.0039 406 NAG B C5 6202 C C6 . NAG O . ? 2.6194 2.1736 2.8035 -0.1327 -0.1086 0.0148 406 NAG B C6 6203 C C7 . NAG O . ? 2.4452 2.1626 2.6823 -0.1298 -0.1371 -0.0144 406 NAG B C7 6204 C C8 . NAG O . ? 2.3748 2.1367 2.6644 -0.1536 -0.1388 -0.0054 406 NAG B C8 6205 N N2 . NAG O . ? 2.5084 2.1762 2.7137 -0.1225 -0.1339 -0.0163 406 NAG B N2 6206 O O3 . NAG O . ? 2.7090 2.2576 2.8618 -0.1559 -0.1598 -0.0300 406 NAG B O3 6207 O O4 . NAG O . ? 2.7232 2.1953 2.8375 -0.1361 -0.1388 -0.0179 406 NAG B O4 6208 O O5 . NAG O . ? 2.5431 2.1909 2.7734 -0.1308 -0.1101 0.0104 406 NAG B O5 6209 O O6 . NAG O . ? 2.5062 2.1072 2.7365 -0.1525 -0.1042 0.0265 406 NAG B O6 6210 O O7 . NAG O . ? 2.4633 2.1904 2.6862 -0.1160 -0.1379 -0.0195 406 NAG B O7 6211 C C1 . MAY P . ? 1.9182 2.1863 2.7004 -0.2570 -0.0733 0.0729 407 MAY B C1 6212 O O1 . MAY P . ? 1.9294 2.2387 2.7316 -0.2399 -0.0405 0.0805 407 MAY B O1 6213 P P1 . MAY P . ? 1.9783 2.2605 2.7692 -0.2555 -0.0491 0.0813 407 MAY B P1 6214 C C2 . MAY P . ? 1.8502 2.1540 2.6657 -0.2566 -0.0823 0.0711 407 MAY B C2 6215 O O2 . MAY P . ? 2.0202 2.3205 2.8431 -0.2763 -0.0429 0.0887 407 MAY B O2 6216 C C3 . MAY P . ? 1.7946 2.0917 2.6141 -0.2693 -0.1035 0.0668 407 MAY B C3 6217 C CM . MAY P . ? 2.0206 2.3511 2.8829 -0.2890 -0.0520 0.0889 407 MAY B CM # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLY 1 0 ? ? ? A . n A 1 2 ALA 2 1 ? ? ? A . n A 1 3 GLY 3 2 ? ? ? A . n A 1 4 ARG 4 3 ? ? ? A . n A 1 5 HIS 5 4 4 HIS HIS A . n A 1 6 PRO 6 5 5 PRO PRO A . n A 1 7 PRO 7 6 6 PRO PRO A . n A 1 8 VAL 8 7 7 VAL VAL A . n A 1 9 VAL 9 8 8 VAL VAL A . n A 1 10 LEU 10 9 9 LEU LEU A . n A 1 11 VAL 11 10 10 VAL VAL A . n A 1 12 PRO 12 11 11 PRO PRO A . n A 1 13 GLY 13 12 12 GLY GLY A . n A 1 14 ASP 14 13 13 ASP ASP A . n A 1 15 LEU 15 14 14 LEU LEU A . n A 1 16 GLY 16 15 15 GLY GLY A . n A 1 17 ASN 17 16 16 ASN ASN A . n A 1 18 GLN 18 17 17 GLN GLN A . n A 1 19 LEU 19 18 18 LEU LEU A . n A 1 20 GLU 20 19 19 GLU GLU A . n A 1 21 ALA 21 20 20 ALA ALA A . n A 1 22 LYS 22 21 21 LYS LYS A . n A 1 23 LEU 23 22 22 LEU LEU A . n A 1 24 ASP 24 23 23 ASP ASP A . n A 1 25 LYS 25 24 24 LYS LYS A . n A 1 26 PRO 26 25 25 PRO PRO A . n A 1 27 THR 27 26 26 THR THR A . n A 1 28 VAL 28 27 27 VAL VAL A . n A 1 29 VAL 29 28 28 VAL VAL A . n A 1 30 HIS 30 29 29 HIS HIS A . n A 1 31 TYR 31 30 30 TYR TYR A . n A 1 32 LEU 32 31 31 LEU LEU A . n A 1 33 CYS 33 32 32 CYS CYS A . n A 1 34 SER 34 33 33 SER SER A . n A 1 35 LYS 35 34 34 LYS LYS A . n A 1 36 LYS 36 35 35 LYS LYS A . n A 1 37 THR 37 36 36 THR THR A . n A 1 38 GLU 38 37 37 GLU GLU A . n A 1 39 SER 39 38 38 SER SER A . n A 1 40 TYR 40 39 39 TYR TYR A . n A 1 41 PHE 41 40 40 PHE PHE A . n A 1 42 THR 42 41 41 THR THR A . n A 1 43 ILE 43 42 42 ILE ILE A . n A 1 44 TRP 44 43 43 TRP TRP A . n A 1 45 LEU 45 44 44 LEU LEU A . n A 1 46 ASN 46 45 45 ASN ASN A . n A 1 47 LEU 47 46 46 LEU LEU A . n A 1 48 GLU 48 47 47 GLU GLU A . n A 1 49 LEU 49 48 48 LEU LEU A . n A 1 50 LEU 50 49 49 LEU LEU A . n A 1 51 LEU 51 50 50 LEU LEU A . n A 1 52 PRO 52 51 51 PRO PRO A . n A 1 53 VAL 53 52 52 VAL VAL A . n A 1 54 ILE 54 53 53 ILE ILE A . n A 1 55 ILE 55 54 54 ILE ILE A . n A 1 56 ASP 56 55 55 ASP ASP A . n A 1 57 CYS 57 56 56 CYS CYS A . n A 1 58 TRP 58 57 57 TRP TRP A . n A 1 59 ILE 59 58 58 ILE ILE A . n A 1 60 ASP 60 59 59 ASP ASP A . n A 1 61 ASN 61 60 60 ASN ASN A . n A 1 62 ILE 62 61 61 ILE ILE A . n A 1 63 ARG 63 62 62 ARG ARG A . n A 1 64 LEU 64 63 63 LEU LEU A . n A 1 65 VAL 65 64 64 VAL VAL A . n A 1 66 TYR 66 65 65 TYR TYR A . n A 1 67 ASN 67 66 66 ASN ASN A . n A 1 68 LYS 68 67 67 LYS LYS A . n A 1 69 THR 69 68 68 THR THR A . n A 1 70 SER 70 69 69 SER SER A . n A 1 71 ARG 71 70 70 ARG ARG A . n A 1 72 ALA 72 71 71 ALA ALA A . n A 1 73 THR 73 72 72 THR THR A . n A 1 74 GLN 74 73 73 GLN GLN A . n A 1 75 PHE 75 74 74 PHE PHE A . n A 1 76 PRO 76 75 75 PRO PRO A . n A 1 77 ASP 77 76 76 ASP ASP A . n A 1 78 GLY 78 77 77 GLY GLY A . n A 1 79 VAL 79 78 78 VAL VAL A . n A 1 80 ASP 80 79 79 ASP ASP A . n A 1 81 VAL 81 80 80 VAL VAL A . n A 1 82 ARG 82 81 81 ARG ARG A . n A 1 83 VAL 83 82 82 VAL VAL A . n A 1 84 PRO 84 83 83 PRO PRO A . n A 1 85 GLY 85 84 84 GLY GLY A . n A 1 86 PHE 86 85 85 PHE PHE A . n A 1 87 GLY 87 86 86 GLY GLY A . n A 1 88 LYS 88 87 87 LYS LYS A . n A 1 89 THR 89 88 88 THR THR A . n A 1 90 PHE 90 89 89 PHE PHE A . n A 1 91 SER 91 90 90 SER SER A . n A 1 92 LEU 92 91 91 LEU LEU A . n A 1 93 GLU 93 92 92 GLU GLU A . n A 1 94 PHE 94 93 93 PHE PHE A . n A 1 95 LEU 95 94 94 LEU LEU A . n A 1 96 ASP 96 95 95 ASP ASP A . n A 1 97 PRO 97 96 96 PRO PRO A . n A 1 98 SER 98 97 97 SER SER A . n A 1 99 LYS 99 98 98 LYS LYS A . n A 1 100 SER 100 99 99 SER SER A . n A 1 101 SER 101 100 100 SER SER A . n A 1 102 VAL 102 101 101 VAL VAL A . n A 1 103 GLY 103 102 102 GLY GLY A . n A 1 104 SER 104 103 103 SER SER A . n A 1 105 TYR 105 104 104 TYR TYR A . n A 1 106 PHE 106 105 105 PHE PHE A . n A 1 107 HIS 107 106 106 HIS HIS A . n A 1 108 THR 108 107 107 THR THR A . n A 1 109 MET 109 108 108 MET MET A . n A 1 110 VAL 110 109 109 VAL VAL A . n A 1 111 GLU 111 110 110 GLU GLU A . n A 1 112 SER 112 111 111 SER SER A . n A 1 113 LEU 113 112 112 LEU LEU A . n A 1 114 VAL 114 113 113 VAL VAL A . n A 1 115 GLY 115 114 114 GLY GLY A . n A 1 116 TRP 116 115 115 TRP TRP A . n A 1 117 GLY 117 116 116 GLY GLY A . n A 1 118 TYR 118 117 117 TYR TYR A . n A 1 119 THR 119 118 118 THR THR A . n A 1 120 ARG 120 119 119 ARG ARG A . n A 1 121 GLY 121 120 120 GLY GLY A . n A 1 122 GLU 122 121 121 GLU GLU A . n A 1 123 ASP 123 122 122 ASP ASP A . n A 1 124 VAL 124 123 123 VAL VAL A . n A 1 125 ARG 125 124 124 ARG ARG A . n A 1 126 GLY 126 125 125 GLY GLY A . n A 1 127 ALA 127 126 126 ALA ALA A . n A 1 128 PRO 128 127 127 PRO PRO A . n A 1 129 TYR 129 128 128 TYR TYR A . n A 1 130 ASP 130 129 129 ASP ASP A . n A 1 131 TRP 131 130 130 TRP TRP A . n A 1 132 ARG 132 131 131 ARG ARG A . n A 1 133 ARG 133 132 132 ARG ARG A . n A 1 134 ALA 134 133 133 ALA ALA A . n A 1 135 PRO 135 134 134 PRO PRO A . n A 1 136 ASN 136 135 135 ASN ASN A . n A 1 137 GLU 137 136 136 GLU GLU A . n A 1 138 ASN 138 137 137 ASN ASN A . n A 1 139 GLY 139 138 138 GLY GLY A . n A 1 140 PRO 140 139 139 PRO PRO A . n A 1 141 TYR 141 140 140 TYR TYR A . n A 1 142 PHE 142 141 141 PHE PHE A . n A 1 143 LEU 143 142 142 LEU LEU A . n A 1 144 ALA 144 143 143 ALA ALA A . n A 1 145 LEU 145 144 144 LEU LEU A . n A 1 146 ARG 146 145 145 ARG ARG A . n A 1 147 GLU 147 146 146 GLU GLU A . n A 1 148 MET 148 147 147 MET MET A . n A 1 149 ILE 149 148 148 ILE ILE A . n A 1 150 GLU 150 149 149 GLU GLU A . n A 1 151 GLU 151 150 150 GLU GLU A . n A 1 152 MET 152 151 151 MET MET A . n A 1 153 TYR 153 152 152 TYR TYR A . n A 1 154 GLN 154 153 153 GLN GLN A . n A 1 155 LEU 155 154 154 LEU LEU A . n A 1 156 TYR 156 155 155 TYR TYR A . n A 1 157 GLY 157 156 156 GLY GLY A . n A 1 158 GLY 158 157 157 GLY GLY A . n A 1 159 PRO 159 158 158 PRO PRO A . n A 1 160 VAL 160 159 159 VAL VAL A . n A 1 161 VAL 161 160 160 VAL VAL A . n A 1 162 LEU 162 161 161 LEU LEU A . n A 1 163 VAL 163 162 162 VAL VAL A . n A 1 164 ALA 164 163 163 ALA ALA A . n A 1 165 HIS 165 164 164 HIS HIS A . n A 1 166 SER 166 165 165 SER SER A . n A 1 167 MET 167 166 166 MET MET A . n A 1 168 GLY 168 167 167 GLY GLY A . n A 1 169 ASN 169 168 168 ASN ASN A . n A 1 170 MET 170 169 169 MET MET A . n A 1 171 TYR 171 170 170 TYR TYR A . n A 1 172 THR 172 171 171 THR THR A . n A 1 173 LEU 173 172 172 LEU LEU A . n A 1 174 TYR 174 173 173 TYR TYR A . n A 1 175 PHE 175 174 174 PHE PHE A . n A 1 176 LEU 176 175 175 LEU LEU A . n A 1 177 GLN 177 176 176 GLN GLN A . n A 1 178 ARG 178 177 177 ARG ARG A . n A 1 179 GLN 179 178 178 GLN GLN A . n A 1 180 PRO 180 179 179 PRO PRO A . n A 1 181 GLN 181 180 180 GLN GLN A . n A 1 182 ALA 182 181 181 ALA ALA A . n A 1 183 TRP 183 182 182 TRP TRP A . n A 1 184 LYS 184 183 183 LYS LYS A . n A 1 185 ASP 185 184 184 ASP ASP A . n A 1 186 LYS 186 185 185 LYS LYS A . n A 1 187 TYR 187 186 186 TYR TYR A . n A 1 188 ILE 188 187 187 ILE ILE A . n A 1 189 ARG 189 188 188 ARG ARG A . n A 1 190 ALA 190 189 189 ALA ALA A . n A 1 191 PHE 191 190 190 PHE PHE A . n A 1 192 VAL 192 191 191 VAL VAL A . n A 1 193 SER 193 192 192 SER SER A . n A 1 194 LEU 194 193 193 LEU LEU A . n A 1 195 GLY 195 194 194 GLY GLY A . n A 1 196 ALA 196 195 195 ALA ALA A . n A 1 197 PRO 197 196 196 PRO PRO A . n A 1 198 TRP 198 197 197 TRP TRP A . n A 1 199 GLY 199 198 198 GLY GLY A . n A 1 200 GLY 200 199 199 GLY GLY A . n A 1 201 VAL 201 200 200 VAL VAL A . n A 1 202 ALA 202 201 201 ALA ALA A . n A 1 203 LYS 203 202 202 LYS LYS A . n A 1 204 THR 204 203 203 THR THR A . n A 1 205 LEU 205 204 204 LEU LEU A . n A 1 206 ARG 206 205 205 ARG ARG A . n A 1 207 VAL 207 206 206 VAL VAL A . n A 1 208 LEU 208 207 207 LEU LEU A . n A 1 209 ALA 209 208 208 ALA ALA A . n A 1 210 SER 210 209 209 SER SER A . n A 1 211 GLY 211 210 210 GLY GLY A . n A 1 212 ASP 212 211 211 ASP ASP A . n A 1 213 ASN 213 212 212 ASN ASN A . n A 1 214 ASN 214 213 213 ASN ASN A . n A 1 215 ARG 215 214 214 ARG ARG A . n A 1 216 ILE 216 215 215 ILE ILE A . n A 1 217 PRO 217 216 216 PRO PRO A . n A 1 218 VAL 218 217 217 VAL VAL A . n A 1 219 ILE 219 218 218 ILE ILE A . n A 1 220 GLY 220 219 219 GLY GLY A . n A 1 221 PRO 221 220 220 PRO PRO A . n A 1 222 LEU 222 221 221 LEU LEU A . n A 1 223 LYS 223 222 222 LYS LYS A . n A 1 224 ILE 224 223 223 ILE ILE A . n A 1 225 ARG 225 224 224 ARG ARG A . n A 1 226 GLU 226 225 225 GLU GLU A . n A 1 227 GLN 227 226 226 GLN GLN A . n A 1 228 GLN 228 227 227 GLN GLN A . n A 1 229 ARG 229 228 228 ARG ARG A . n A 1 230 SER 230 229 229 SER SER A . n A 1 231 ALA 231 230 230 ALA ALA A . n A 1 232 VAL 232 231 231 VAL VAL A . n A 1 233 SER 233 232 232 SER SER A . n A 1 234 THR 234 233 233 THR THR A . n A 1 235 SER 235 234 234 SER SER A . n A 1 236 TRP 236 235 235 TRP TRP A . n A 1 237 LEU 237 236 236 LEU LEU A . n A 1 238 LEU 238 237 237 LEU LEU A . n A 1 239 PRO 239 238 238 PRO PRO A . n A 1 240 TYR 240 239 239 TYR TYR A . n A 1 241 ASN 241 240 240 ASN ASN A . n A 1 242 TYR 242 241 241 TYR TYR A . n A 1 243 THR 243 242 242 THR THR A . n A 1 244 TRP 244 243 243 TRP TRP A . n A 1 245 SER 245 244 244 SER SER A . n A 1 246 PRO 246 245 245 PRO PRO A . n A 1 247 GLU 247 246 246 GLU GLU A . n A 1 248 LYS 248 247 247 LYS LYS A . n A 1 249 VAL 249 248 248 VAL VAL A . n A 1 250 PHE 250 249 249 PHE PHE A . n A 1 251 VAL 251 250 250 VAL VAL A . n A 1 252 GLN 252 251 251 GLN GLN A . n A 1 253 THR 253 252 252 THR THR A . n A 1 254 PRO 254 253 253 PRO PRO A . n A 1 255 THR 255 254 254 THR THR A . n A 1 256 ILE 256 255 255 ILE ILE A . n A 1 257 ASN 257 256 256 ASN ASN A . n A 1 258 TYR 258 257 257 TYR TYR A . n A 1 259 THR 259 258 258 THR THR A . n A 1 260 LEU 260 259 259 LEU LEU A . n A 1 261 ARG 261 260 260 ARG ARG A . n A 1 262 ASP 262 261 261 ASP ASP A . n A 1 263 TYR 263 262 262 TYR TYR A . n A 1 264 ARG 264 263 263 ARG ARG A . n A 1 265 LYS 265 264 264 LYS LYS A . n A 1 266 PHE 266 265 265 PHE PHE A . n A 1 267 PHE 267 266 266 PHE PHE A . n A 1 268 GLN 268 267 267 GLN GLN A . n A 1 269 ASP 269 268 268 ASP ASP A . n A 1 270 ILE 270 269 269 ILE ILE A . n A 1 271 GLY 271 270 270 GLY GLY A . n A 1 272 PHE 272 271 271 PHE PHE A . n A 1 273 GLU 273 272 272 GLU GLU A . n A 1 274 ASP 274 273 273 ASP ASP A . n A 1 275 GLY 275 274 274 GLY GLY A . n A 1 276 TRP 276 275 275 TRP TRP A . n A 1 277 LEU 277 276 276 LEU LEU A . n A 1 278 MET 278 277 277 MET MET A . n A 1 279 ARG 279 278 278 ARG ARG A . n A 1 280 GLN 280 279 279 GLN GLN A . n A 1 281 ASP 281 280 280 ASP ASP A . n A 1 282 THR 282 281 281 THR THR A . n A 1 283 GLU 283 282 282 GLU GLU A . n A 1 284 GLY 284 283 283 GLY GLY A . n A 1 285 LEU 285 284 284 LEU LEU A . n A 1 286 VAL 286 285 285 VAL VAL A . n A 1 287 GLU 287 286 286 GLU GLU A . n A 1 288 ALA 288 287 287 ALA ALA A . n A 1 289 THR 289 288 288 THR THR A . n A 1 290 MET 290 289 289 MET MET A . n A 1 291 PRO 291 290 290 PRO PRO A . n A 1 292 PRO 292 291 291 PRO PRO A . n A 1 293 GLY 293 292 292 GLY GLY A . n A 1 294 VAL 294 293 293 VAL VAL A . n A 1 295 GLN 295 294 294 GLN GLN A . n A 1 296 LEU 296 295 295 LEU LEU A . n A 1 297 HIS 297 296 296 HIS HIS A . n A 1 298 CYS 298 297 297 CYS CYS A . n A 1 299 LEU 299 298 298 LEU LEU A . n A 1 300 TYR 300 299 299 TYR TYR A . n A 1 301 GLY 301 300 300 GLY GLY A . n A 1 302 THR 302 301 301 THR THR A . n A 1 303 GLY 303 302 302 GLY GLY A . n A 1 304 VAL 304 303 303 VAL VAL A . n A 1 305 PRO 305 304 304 PRO PRO A . n A 1 306 THR 306 305 305 THR THR A . n A 1 307 PRO 307 306 306 PRO PRO A . n A 1 308 ASP 308 307 307 ASP ASP A . n A 1 309 SER 309 308 308 SER SER A . n A 1 310 PHE 310 309 309 PHE PHE A . n A 1 311 TYR 311 310 310 TYR TYR A . n A 1 312 TYR 312 311 311 TYR TYR A . n A 1 313 GLU 313 312 312 GLU GLU A . n A 1 314 SER 314 313 313 SER SER A . n A 1 315 PHE 315 314 314 PHE PHE A . n A 1 316 PRO 316 315 315 PRO PRO A . n A 1 317 ASP 317 316 316 ASP ASP A . n A 1 318 ARG 318 317 317 ARG ARG A . n A 1 319 ASP 319 318 318 ASP ASP A . n A 1 320 PRO 320 319 319 PRO PRO A . n A 1 321 LYS 321 320 320 LYS LYS A . n A 1 322 ILE 322 321 321 ILE ILE A . n A 1 323 CYS 323 322 322 CYS CYS A . n A 1 324 PHE 324 323 323 PHE PHE A . n A 1 325 GLY 325 324 324 GLY GLY A . n A 1 326 ASP 326 325 325 ASP ASP A . n A 1 327 GLY 327 326 326 GLY GLY A . n A 1 328 ASP 328 327 327 ASP ASP A . n A 1 329 GLY 329 328 328 GLY GLY A . n A 1 330 THR 330 329 329 THR THR A . n A 1 331 VAL 331 330 330 VAL VAL A . n A 1 332 ASN 332 331 331 ASN ASN A . n A 1 333 LEU 333 332 332 LEU LEU A . n A 1 334 LYS 334 333 333 LYS LYS A . n A 1 335 SER 335 334 334 SER SER A . n A 1 336 ALA 336 335 335 ALA ALA A . n A 1 337 LEU 337 336 336 LEU LEU A . n A 1 338 GLN 338 337 337 GLN GLN A . n A 1 339 CYS 339 338 338 CYS CYS A . n A 1 340 GLN 340 339 339 GLN GLN A . n A 1 341 ALA 341 340 340 ALA ALA A . n A 1 342 TRP 342 341 341 TRP TRP A . n A 1 343 GLN 343 342 342 GLN GLN A . n A 1 344 SER 344 343 343 SER SER A . n A 1 345 ARG 345 344 344 ARG ARG A . n A 1 346 GLN 346 345 345 GLN GLN A . n A 1 347 GLU 347 346 346 GLU GLU A . n A 1 348 HIS 348 347 347 HIS HIS A . n A 1 349 GLN 349 348 348 GLN GLN A . n A 1 350 VAL 350 349 349 VAL VAL A . n A 1 351 LEU 351 350 350 LEU LEU A . n A 1 352 LEU 352 351 351 LEU LEU A . n A 1 353 GLN 353 352 352 GLN GLN A . n A 1 354 GLU 354 353 353 GLU GLU A . n A 1 355 LEU 355 354 354 LEU LEU A . n A 1 356 PRO 356 355 355 PRO PRO A . n A 1 357 GLY 357 356 356 GLY GLY A . n A 1 358 SER 358 357 357 SER SER A . n A 1 359 GLU 359 358 358 GLU GLU A . n A 1 360 HIS 360 359 359 HIS HIS A . n A 1 361 ILE 361 360 360 ILE ILE A . n A 1 362 GLU 362 361 361 GLU GLU A . n A 1 363 MET 363 362 362 MET MET A . n A 1 364 LEU 364 363 363 LEU LEU A . n A 1 365 ALA 365 364 364 ALA ALA A . n A 1 366 ASN 366 365 365 ASN ASN A . n A 1 367 ALA 367 366 366 ALA ALA A . n A 1 368 THR 368 367 367 THR THR A . n A 1 369 THR 369 368 368 THR THR A . n A 1 370 LEU 370 369 369 LEU LEU A . n A 1 371 ALA 371 370 370 ALA ALA A . n A 1 372 TYR 372 371 371 TYR TYR A . n A 1 373 LEU 373 372 372 LEU LEU A . n A 1 374 LYS 374 373 373 LYS LYS A . n A 1 375 ARG 375 374 374 ARG ARG A . n A 1 376 VAL 376 375 375 VAL VAL A . n A 1 377 LEU 377 376 376 LEU LEU A . n A 1 378 LEU 378 377 377 LEU LEU A . n A 1 379 GLY 379 378 378 GLY GLY A . n A 1 380 PRO 380 379 ? ? ? A . n B 1 1 GLY 1 0 ? ? ? B . n B 1 2 ALA 2 1 ? ? ? B . n B 1 3 GLY 3 2 ? ? ? B . n B 1 4 ARG 4 3 3 ARG ARG B . n B 1 5 HIS 5 4 4 HIS HIS B . n B 1 6 PRO 6 5 5 PRO PRO B . n B 1 7 PRO 7 6 6 PRO PRO B . n B 1 8 VAL 8 7 7 VAL VAL B . n B 1 9 VAL 9 8 8 VAL VAL B . n B 1 10 LEU 10 9 9 LEU LEU B . n B 1 11 VAL 11 10 10 VAL VAL B . n B 1 12 PRO 12 11 11 PRO PRO B . n B 1 13 GLY 13 12 12 GLY GLY B . n B 1 14 ASP 14 13 13 ASP ASP B . n B 1 15 LEU 15 14 14 LEU LEU B . n B 1 16 GLY 16 15 15 GLY GLY B . n B 1 17 ASN 17 16 16 ASN ASN B . n B 1 18 GLN 18 17 17 GLN GLN B . n B 1 19 LEU 19 18 18 LEU LEU B . n B 1 20 GLU 20 19 19 GLU GLU B . n B 1 21 ALA 21 20 20 ALA ALA B . n B 1 22 LYS 22 21 21 LYS LYS B . n B 1 23 LEU 23 22 22 LEU LEU B . n B 1 24 ASP 24 23 23 ASP ASP B . n B 1 25 LYS 25 24 24 LYS LYS B . n B 1 26 PRO 26 25 25 PRO PRO B . n B 1 27 THR 27 26 26 THR THR B . n B 1 28 VAL 28 27 27 VAL VAL B . n B 1 29 VAL 29 28 28 VAL VAL B . n B 1 30 HIS 30 29 29 HIS HIS B . n B 1 31 TYR 31 30 30 TYR TYR B . n B 1 32 LEU 32 31 31 LEU LEU B . n B 1 33 CYS 33 32 32 CYS CYS B . n B 1 34 SER 34 33 33 SER SER B . n B 1 35 LYS 35 34 34 LYS LYS B . n B 1 36 LYS 36 35 35 LYS LYS B . n B 1 37 THR 37 36 36 THR THR B . n B 1 38 GLU 38 37 37 GLU GLU B . n B 1 39 SER 39 38 38 SER SER B . n B 1 40 TYR 40 39 39 TYR TYR B . n B 1 41 PHE 41 40 40 PHE PHE B . n B 1 42 THR 42 41 41 THR THR B . n B 1 43 ILE 43 42 42 ILE ILE B . n B 1 44 TRP 44 43 43 TRP TRP B . n B 1 45 LEU 45 44 44 LEU LEU B . n B 1 46 ASN 46 45 45 ASN ASN B . n B 1 47 LEU 47 46 46 LEU LEU B . n B 1 48 GLU 48 47 47 GLU GLU B . n B 1 49 LEU 49 48 48 LEU LEU B . n B 1 50 LEU 50 49 49 LEU LEU B . n B 1 51 LEU 51 50 50 LEU LEU B . n B 1 52 PRO 52 51 51 PRO PRO B . n B 1 53 VAL 53 52 52 VAL VAL B . n B 1 54 ILE 54 53 53 ILE ILE B . n B 1 55 ILE 55 54 54 ILE ILE B . n B 1 56 ASP 56 55 55 ASP ASP B . n B 1 57 CYS 57 56 56 CYS CYS B . n B 1 58 TRP 58 57 57 TRP TRP B . n B 1 59 ILE 59 58 58 ILE ILE B . n B 1 60 ASP 60 59 59 ASP ASP B . n B 1 61 ASN 61 60 60 ASN ASN B . n B 1 62 ILE 62 61 61 ILE ILE B . n B 1 63 ARG 63 62 62 ARG ARG B . n B 1 64 LEU 64 63 63 LEU LEU B . n B 1 65 VAL 65 64 64 VAL VAL B . n B 1 66 TYR 66 65 65 TYR TYR B . n B 1 67 ASN 67 66 66 ASN ASN B . n B 1 68 LYS 68 67 67 LYS LYS B . n B 1 69 THR 69 68 68 THR THR B . n B 1 70 SER 70 69 69 SER SER B . n B 1 71 ARG 71 70 70 ARG ARG B . n B 1 72 ALA 72 71 71 ALA ALA B . n B 1 73 THR 73 72 72 THR THR B . n B 1 74 GLN 74 73 73 GLN GLN B . n B 1 75 PHE 75 74 74 PHE PHE B . n B 1 76 PRO 76 75 75 PRO PRO B . n B 1 77 ASP 77 76 76 ASP ASP B . n B 1 78 GLY 78 77 77 GLY GLY B . n B 1 79 VAL 79 78 78 VAL VAL B . n B 1 80 ASP 80 79 79 ASP ASP B . n B 1 81 VAL 81 80 80 VAL VAL B . n B 1 82 ARG 82 81 81 ARG ARG B . n B 1 83 VAL 83 82 82 VAL VAL B . n B 1 84 PRO 84 83 83 PRO PRO B . n B 1 85 GLY 85 84 84 GLY GLY B . n B 1 86 PHE 86 85 85 PHE PHE B . n B 1 87 GLY 87 86 86 GLY GLY B . n B 1 88 LYS 88 87 87 LYS LYS B . n B 1 89 THR 89 88 88 THR THR B . n B 1 90 PHE 90 89 89 PHE PHE B . n B 1 91 SER 91 90 90 SER SER B . n B 1 92 LEU 92 91 91 LEU LEU B . n B 1 93 GLU 93 92 92 GLU GLU B . n B 1 94 PHE 94 93 93 PHE PHE B . n B 1 95 LEU 95 94 94 LEU LEU B . n B 1 96 ASP 96 95 95 ASP ASP B . n B 1 97 PRO 97 96 96 PRO PRO B . n B 1 98 SER 98 97 97 SER SER B . n B 1 99 LYS 99 98 98 LYS LYS B . n B 1 100 SER 100 99 99 SER SER B . n B 1 101 SER 101 100 100 SER SER B . n B 1 102 VAL 102 101 101 VAL VAL B . n B 1 103 GLY 103 102 102 GLY GLY B . n B 1 104 SER 104 103 103 SER SER B . n B 1 105 TYR 105 104 104 TYR TYR B . n B 1 106 PHE 106 105 105 PHE PHE B . n B 1 107 HIS 107 106 106 HIS HIS B . n B 1 108 THR 108 107 107 THR THR B . n B 1 109 MET 109 108 108 MET MET B . n B 1 110 VAL 110 109 109 VAL VAL B . n B 1 111 GLU 111 110 110 GLU GLU B . n B 1 112 SER 112 111 111 SER SER B . n B 1 113 LEU 113 112 112 LEU LEU B . n B 1 114 VAL 114 113 113 VAL VAL B . n B 1 115 GLY 115 114 114 GLY GLY B . n B 1 116 TRP 116 115 115 TRP TRP B . n B 1 117 GLY 117 116 116 GLY GLY B . n B 1 118 TYR 118 117 117 TYR TYR B . n B 1 119 THR 119 118 118 THR THR B . n B 1 120 ARG 120 119 119 ARG ARG B . n B 1 121 GLY 121 120 120 GLY GLY B . n B 1 122 GLU 122 121 121 GLU GLU B . n B 1 123 ASP 123 122 122 ASP ASP B . n B 1 124 VAL 124 123 123 VAL VAL B . n B 1 125 ARG 125 124 124 ARG ARG B . n B 1 126 GLY 126 125 125 GLY GLY B . n B 1 127 ALA 127 126 126 ALA ALA B . n B 1 128 PRO 128 127 127 PRO PRO B . n B 1 129 TYR 129 128 128 TYR TYR B . n B 1 130 ASP 130 129 129 ASP ASP B . n B 1 131 TRP 131 130 130 TRP TRP B . n B 1 132 ARG 132 131 131 ARG ARG B . n B 1 133 ARG 133 132 132 ARG ARG B . n B 1 134 ALA 134 133 133 ALA ALA B . n B 1 135 PRO 135 134 134 PRO PRO B . n B 1 136 ASN 136 135 135 ASN ASN B . n B 1 137 GLU 137 136 136 GLU GLU B . n B 1 138 ASN 138 137 137 ASN ASN B . n B 1 139 GLY 139 138 138 GLY GLY B . n B 1 140 PRO 140 139 139 PRO PRO B . n B 1 141 TYR 141 140 140 TYR TYR B . n B 1 142 PHE 142 141 141 PHE PHE B . n B 1 143 LEU 143 142 142 LEU LEU B . n B 1 144 ALA 144 143 143 ALA ALA B . n B 1 145 LEU 145 144 144 LEU LEU B . n B 1 146 ARG 146 145 145 ARG ARG B . n B 1 147 GLU 147 146 146 GLU GLU B . n B 1 148 MET 148 147 147 MET MET B . n B 1 149 ILE 149 148 148 ILE ILE B . n B 1 150 GLU 150 149 149 GLU GLU B . n B 1 151 GLU 151 150 150 GLU GLU B . n B 1 152 MET 152 151 151 MET MET B . n B 1 153 TYR 153 152 152 TYR TYR B . n B 1 154 GLN 154 153 153 GLN GLN B . n B 1 155 LEU 155 154 154 LEU LEU B . n B 1 156 TYR 156 155 155 TYR TYR B . n B 1 157 GLY 157 156 156 GLY GLY B . n B 1 158 GLY 158 157 157 GLY GLY B . n B 1 159 PRO 159 158 158 PRO PRO B . n B 1 160 VAL 160 159 159 VAL VAL B . n B 1 161 VAL 161 160 160 VAL VAL B . n B 1 162 LEU 162 161 161 LEU LEU B . n B 1 163 VAL 163 162 162 VAL VAL B . n B 1 164 ALA 164 163 163 ALA ALA B . n B 1 165 HIS 165 164 164 HIS HIS B . n B 1 166 SER 166 165 165 SER SER B . n B 1 167 MET 167 166 166 MET MET B . n B 1 168 GLY 168 167 167 GLY GLY B . n B 1 169 ASN 169 168 168 ASN ASN B . n B 1 170 MET 170 169 169 MET MET B . n B 1 171 TYR 171 170 170 TYR TYR B . n B 1 172 THR 172 171 171 THR THR B . n B 1 173 LEU 173 172 172 LEU LEU B . n B 1 174 TYR 174 173 173 TYR TYR B . n B 1 175 PHE 175 174 174 PHE PHE B . n B 1 176 LEU 176 175 175 LEU LEU B . n B 1 177 GLN 177 176 176 GLN GLN B . n B 1 178 ARG 178 177 177 ARG ARG B . n B 1 179 GLN 179 178 178 GLN GLN B . n B 1 180 PRO 180 179 179 PRO PRO B . n B 1 181 GLN 181 180 180 GLN GLN B . n B 1 182 ALA 182 181 181 ALA ALA B . n B 1 183 TRP 183 182 182 TRP TRP B . n B 1 184 LYS 184 183 183 LYS LYS B . n B 1 185 ASP 185 184 184 ASP ASP B . n B 1 186 LYS 186 185 185 LYS LYS B . n B 1 187 TYR 187 186 186 TYR TYR B . n B 1 188 ILE 188 187 187 ILE ILE B . n B 1 189 ARG 189 188 188 ARG ARG B . n B 1 190 ALA 190 189 189 ALA ALA B . n B 1 191 PHE 191 190 190 PHE PHE B . n B 1 192 VAL 192 191 191 VAL VAL B . n B 1 193 SER 193 192 192 SER SER B . n B 1 194 LEU 194 193 193 LEU LEU B . n B 1 195 GLY 195 194 194 GLY GLY B . n B 1 196 ALA 196 195 195 ALA ALA B . n B 1 197 PRO 197 196 196 PRO PRO B . n B 1 198 TRP 198 197 197 TRP TRP B . n B 1 199 GLY 199 198 198 GLY GLY B . n B 1 200 GLY 200 199 199 GLY GLY B . n B 1 201 VAL 201 200 200 VAL VAL B . n B 1 202 ALA 202 201 201 ALA ALA B . n B 1 203 LYS 203 202 202 LYS LYS B . n B 1 204 THR 204 203 203 THR THR B . n B 1 205 LEU 205 204 204 LEU LEU B . n B 1 206 ARG 206 205 205 ARG ARG B . n B 1 207 VAL 207 206 206 VAL VAL B . n B 1 208 LEU 208 207 207 LEU LEU B . n B 1 209 ALA 209 208 208 ALA ALA B . n B 1 210 SER 210 209 209 SER SER B . n B 1 211 GLY 211 210 210 GLY GLY B . n B 1 212 ASP 212 211 211 ASP ASP B . n B 1 213 ASN 213 212 212 ASN ASN B . n B 1 214 ASN 214 213 213 ASN ASN B . n B 1 215 ARG 215 214 214 ARG ARG B . n B 1 216 ILE 216 215 215 ILE ILE B . n B 1 217 PRO 217 216 216 PRO PRO B . n B 1 218 VAL 218 217 217 VAL VAL B . n B 1 219 ILE 219 218 218 ILE ILE B . n B 1 220 GLY 220 219 219 GLY GLY B . n B 1 221 PRO 221 220 220 PRO PRO B . n B 1 222 LEU 222 221 221 LEU LEU B . n B 1 223 LYS 223 222 222 LYS LYS B . n B 1 224 ILE 224 223 223 ILE ILE B . n B 1 225 ARG 225 224 224 ARG ARG B . n B 1 226 GLU 226 225 225 GLU GLU B . n B 1 227 GLN 227 226 226 GLN GLN B . n B 1 228 GLN 228 227 227 GLN GLN B . n B 1 229 ARG 229 228 228 ARG ARG B . n B 1 230 SER 230 229 229 SER SER B . n B 1 231 ALA 231 230 230 ALA ALA B . n B 1 232 VAL 232 231 231 VAL VAL B . n B 1 233 SER 233 232 232 SER SER B . n B 1 234 THR 234 233 233 THR THR B . n B 1 235 SER 235 234 234 SER SER B . n B 1 236 TRP 236 235 235 TRP TRP B . n B 1 237 LEU 237 236 236 LEU LEU B . n B 1 238 LEU 238 237 237 LEU LEU B . n B 1 239 PRO 239 238 238 PRO PRO B . n B 1 240 TYR 240 239 239 TYR TYR B . n B 1 241 ASN 241 240 240 ASN ASN B . n B 1 242 TYR 242 241 241 TYR TYR B . n B 1 243 THR 243 242 242 THR THR B . n B 1 244 TRP 244 243 243 TRP TRP B . n B 1 245 SER 245 244 244 SER SER B . n B 1 246 PRO 246 245 245 PRO PRO B . n B 1 247 GLU 247 246 246 GLU GLU B . n B 1 248 LYS 248 247 247 LYS LYS B . n B 1 249 VAL 249 248 248 VAL VAL B . n B 1 250 PHE 250 249 249 PHE PHE B . n B 1 251 VAL 251 250 250 VAL VAL B . n B 1 252 GLN 252 251 251 GLN GLN B . n B 1 253 THR 253 252 252 THR THR B . n B 1 254 PRO 254 253 253 PRO PRO B . n B 1 255 THR 255 254 254 THR THR B . n B 1 256 ILE 256 255 255 ILE ILE B . n B 1 257 ASN 257 256 256 ASN ASN B . n B 1 258 TYR 258 257 257 TYR TYR B . n B 1 259 THR 259 258 258 THR THR B . n B 1 260 LEU 260 259 259 LEU LEU B . n B 1 261 ARG 261 260 260 ARG ARG B . n B 1 262 ASP 262 261 261 ASP ASP B . n B 1 263 TYR 263 262 262 TYR TYR B . n B 1 264 ARG 264 263 263 ARG ARG B . n B 1 265 LYS 265 264 264 LYS LYS B . n B 1 266 PHE 266 265 265 PHE PHE B . n B 1 267 PHE 267 266 266 PHE PHE B . n B 1 268 GLN 268 267 267 GLN GLN B . n B 1 269 ASP 269 268 268 ASP ASP B . n B 1 270 ILE 270 269 269 ILE ILE B . n B 1 271 GLY 271 270 270 GLY GLY B . n B 1 272 PHE 272 271 271 PHE PHE B . n B 1 273 GLU 273 272 272 GLU GLU B . n B 1 274 ASP 274 273 273 ASP ASP B . n B 1 275 GLY 275 274 274 GLY GLY B . n B 1 276 TRP 276 275 275 TRP TRP B . n B 1 277 LEU 277 276 276 LEU LEU B . n B 1 278 MET 278 277 277 MET MET B . n B 1 279 ARG 279 278 278 ARG ARG B . n B 1 280 GLN 280 279 279 GLN GLN B . n B 1 281 ASP 281 280 280 ASP ASP B . n B 1 282 THR 282 281 281 THR THR B . n B 1 283 GLU 283 282 282 GLU GLU B . n B 1 284 GLY 284 283 283 GLY GLY B . n B 1 285 LEU 285 284 284 LEU LEU B . n B 1 286 VAL 286 285 285 VAL VAL B . n B 1 287 GLU 287 286 286 GLU GLU B . n B 1 288 ALA 288 287 287 ALA ALA B . n B 1 289 THR 289 288 288 THR THR B . n B 1 290 MET 290 289 289 MET MET B . n B 1 291 PRO 291 290 290 PRO PRO B . n B 1 292 PRO 292 291 291 PRO PRO B . n B 1 293 GLY 293 292 292 GLY GLY B . n B 1 294 VAL 294 293 293 VAL VAL B . n B 1 295 GLN 295 294 294 GLN GLN B . n B 1 296 LEU 296 295 295 LEU LEU B . n B 1 297 HIS 297 296 296 HIS HIS B . n B 1 298 CYS 298 297 297 CYS CYS B . n B 1 299 LEU 299 298 298 LEU LEU B . n B 1 300 TYR 300 299 299 TYR TYR B . n B 1 301 GLY 301 300 300 GLY GLY B . n B 1 302 THR 302 301 301 THR THR B . n B 1 303 GLY 303 302 302 GLY GLY B . n B 1 304 VAL 304 303 303 VAL VAL B . n B 1 305 PRO 305 304 304 PRO PRO B . n B 1 306 THR 306 305 305 THR THR B . n B 1 307 PRO 307 306 306 PRO PRO B . n B 1 308 ASP 308 307 307 ASP ASP B . n B 1 309 SER 309 308 308 SER SER B . n B 1 310 PHE 310 309 309 PHE PHE B . n B 1 311 TYR 311 310 310 TYR TYR B . n B 1 312 TYR 312 311 311 TYR TYR B . n B 1 313 GLU 313 312 312 GLU GLU B . n B 1 314 SER 314 313 313 SER SER B . n B 1 315 PHE 315 314 314 PHE PHE B . n B 1 316 PRO 316 315 315 PRO PRO B . n B 1 317 ASP 317 316 316 ASP ASP B . n B 1 318 ARG 318 317 317 ARG ARG B . n B 1 319 ASP 319 318 318 ASP ASP B . n B 1 320 PRO 320 319 319 PRO PRO B . n B 1 321 LYS 321 320 320 LYS LYS B . n B 1 322 ILE 322 321 321 ILE ILE B . n B 1 323 CYS 323 322 322 CYS CYS B . n B 1 324 PHE 324 323 323 PHE PHE B . n B 1 325 GLY 325 324 324 GLY GLY B . n B 1 326 ASP 326 325 325 ASP ASP B . n B 1 327 GLY 327 326 326 GLY GLY B . n B 1 328 ASP 328 327 327 ASP ASP B . n B 1 329 GLY 329 328 328 GLY GLY B . n B 1 330 THR 330 329 329 THR THR B . n B 1 331 VAL 331 330 330 VAL VAL B . n B 1 332 ASN 332 331 331 ASN ASN B . n B 1 333 LEU 333 332 332 LEU LEU B . n B 1 334 LYS 334 333 333 LYS LYS B . n B 1 335 SER 335 334 334 SER SER B . n B 1 336 ALA 336 335 335 ALA ALA B . n B 1 337 LEU 337 336 336 LEU LEU B . n B 1 338 GLN 338 337 337 GLN GLN B . n B 1 339 CYS 339 338 338 CYS CYS B . n B 1 340 GLN 340 339 339 GLN GLN B . n B 1 341 ALA 341 340 340 ALA ALA B . n B 1 342 TRP 342 341 341 TRP TRP B . n B 1 343 GLN 343 342 342 GLN GLN B . n B 1 344 SER 344 343 343 SER SER B . n B 1 345 ARG 345 344 344 ARG ARG B . n B 1 346 GLN 346 345 345 GLN GLN B . n B 1 347 GLU 347 346 346 GLU GLU B . n B 1 348 HIS 348 347 347 HIS HIS B . n B 1 349 GLN 349 348 348 GLN GLN B . n B 1 350 VAL 350 349 349 VAL VAL B . n B 1 351 LEU 351 350 350 LEU LEU B . n B 1 352 LEU 352 351 351 LEU LEU B . n B 1 353 GLN 353 352 352 GLN GLN B . n B 1 354 GLU 354 353 353 GLU GLU B . n B 1 355 LEU 355 354 354 LEU LEU B . n B 1 356 PRO 356 355 355 PRO PRO B . n B 1 357 GLY 357 356 356 GLY GLY B . n B 1 358 SER 358 357 357 SER SER B . n B 1 359 GLU 359 358 358 GLU GLU B . n B 1 360 HIS 360 359 359 HIS HIS B . n B 1 361 ILE 361 360 360 ILE ILE B . n B 1 362 GLU 362 361 361 GLU GLU B . n B 1 363 MET 363 362 362 MET MET B . n B 1 364 LEU 364 363 363 LEU LEU B . n B 1 365 ALA 365 364 364 ALA ALA B . n B 1 366 ASN 366 365 365 ASN ASN B . n B 1 367 ALA 367 366 366 ALA ALA B . n B 1 368 THR 368 367 367 THR THR B . n B 1 369 THR 369 368 368 THR THR B . n B 1 370 LEU 370 369 369 LEU LEU B . n B 1 371 ALA 371 370 370 ALA ALA B . n B 1 372 TYR 372 371 371 TYR TYR B . n B 1 373 LEU 373 372 372 LEU LEU B . n B 1 374 LYS 374 373 373 LYS LYS B . n B 1 375 ARG 375 374 374 ARG ARG B . n B 1 376 VAL 376 375 375 VAL VAL B . n B 1 377 LEU 377 376 376 LEU LEU B . n B 1 378 LEU 378 377 377 LEU LEU B . n B 1 379 GLY 379 378 378 GLY GLY B . n B 1 380 PRO 380 379 379 PRO PRO B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 401 380 NAG NAG A . D 2 NAG 2 402 384 NAG NAG A . E 3 BMA 3 403 385 BMA MAN A . F 2 NAG 1 404 381 NAG NAG A . G 2 NAG 1 405 382 NAG NAG A . H 2 NAG 1 406 383 NAG NAG A . I 4 MAY 1 407 386 MAY MAY A . J 2 NAG 1 401 380 NAG NAG B . K 2 NAG 2 402 384 NAG NAG B . L 3 BMA 3 403 385 BMA MAN B . M 2 NAG 1 404 381 NAG NAG B . N 2 NAG 1 405 382 NAG NAG B . O 2 NAG 1 406 383 NAG NAG B . P 4 MAY 1 407 386 MAY MAY 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_defined_assembly ? monomeric 1 2 author_defined_assembly ? 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 2 1 B,J,K,L,M,N,O,P # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2015-03-25 2 'Structure model' 1 1 2017-09-13 3 'Structure model' 1 2 2017-11-22 # _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' 'Author supporting evidence' 2 2 'Structure model' 'Derived calculations' 3 2 'Structure model' 'Source and taxonomy' 4 3 'Structure model' 'Refinement description' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 2 'Structure model' entity_src_gen 2 2 'Structure model' pdbx_audit_support 3 2 'Structure model' pdbx_struct_oper_list 4 3 'Structure model' software # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 2 'Structure model' '_entity_src_gen.pdbx_alt_source_flag' 2 2 'Structure model' '_pdbx_audit_support.funding_organization' 3 2 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' # 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[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 3.1670 8.8001 22.5619 0.0181 0.1909 0.3918 -0.0128 -0.0677 -0.0040 1.0226 3.0118 2.0959 -0.3623 -0.7027 0.4418 0.0103 -0.0758 0.0655 -0.1090 -0.0473 0.0598 0.1205 -0.0095 -0.0307 'X-RAY DIFFRACTION' 2 ? refined 25.4359 31.3639 -6.6904 0.1300 0.4903 0.9609 -0.2198 -0.0156 0.0823 1.5017 2.3590 2.5926 -0.4384 0.1183 -0.3610 -0.0205 -0.0516 0.0720 0.1319 0.1752 -0.7063 -0.0073 -0.4737 0.5098 # 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.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 4 A 386 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 3 B 386 ? ? ? ? ? ? # 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 ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0073 1 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 2 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? . 3 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 4 ? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 5 ? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.15 6 # 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 VAL A 52 ? ? 74.63 -62.41 2 1 SER A 99 ? ? -49.62 -86.95 3 1 TYR A 104 ? ? -125.78 -82.18 4 1 GLU A 121 ? ? -118.57 -85.40 5 1 SER A 165 ? ? 50.12 -127.78 6 1 THR A 329 ? ? -127.34 -58.94 7 1 VAL B 52 ? ? 73.69 -60.75 8 1 SER B 99 ? ? -49.32 -87.06 9 1 TYR B 104 ? ? -125.74 -82.34 10 1 GLU B 121 ? ? -118.37 -85.56 11 1 SER B 165 ? ? 49.91 -127.99 12 1 THR B 329 ? ? -127.33 -58.61 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LEU 14 ? CD2 ? A LEU 15 CD2 2 1 N 1 A MAY 407 ? C4 ? I MAY 1 C4 3 1 N 1 A MAY 407 ? C5 ? I MAY 1 C5 4 1 N 1 A MAY 407 ? C6 ? I MAY 1 C6 5 1 N 1 A MAY 407 ? C7 ? I MAY 1 C7 6 1 N 1 A MAY 407 ? C8 ? I MAY 1 C8 7 1 N 1 A MAY 407 ? C9 ? I MAY 1 C9 8 1 N 1 A MAY 407 ? C10 ? I MAY 1 C10 9 1 N 1 A MAY 407 ? C11 ? I MAY 1 C11 10 1 N 1 A MAY 407 ? C12 ? I MAY 1 C12 11 1 N 1 A MAY 407 ? C13 ? I MAY 1 C13 12 1 N 1 A MAY 407 ? C14 ? I MAY 1 C14 13 1 N 1 A MAY 407 ? C15 ? I MAY 1 C15 14 1 N 1 A MAY 407 ? C16 ? I MAY 1 C16 15 1 N 1 A MAY 407 ? C17 ? I MAY 1 C17 16 1 N 1 A MAY 407 ? C18 ? I MAY 1 C18 17 1 N 1 A MAY 407 ? C19 ? I MAY 1 C19 18 1 N 1 A MAY 407 ? C20 ? I MAY 1 C20 19 1 N 1 B MAY 407 ? C4 ? P MAY 1 C4 20 1 N 1 B MAY 407 ? C5 ? P MAY 1 C5 21 1 N 1 B MAY 407 ? C6 ? P MAY 1 C6 22 1 N 1 B MAY 407 ? C7 ? P MAY 1 C7 23 1 N 1 B MAY 407 ? C8 ? P MAY 1 C8 24 1 N 1 B MAY 407 ? C9 ? P MAY 1 C9 25 1 N 1 B MAY 407 ? C10 ? P MAY 1 C10 26 1 N 1 B MAY 407 ? C11 ? P MAY 1 C11 27 1 N 1 B MAY 407 ? C12 ? P MAY 1 C12 28 1 N 1 B MAY 407 ? C13 ? P MAY 1 C13 29 1 N 1 B MAY 407 ? C14 ? P MAY 1 C14 30 1 N 1 B MAY 407 ? C15 ? P MAY 1 C15 31 1 N 1 B MAY 407 ? C16 ? P MAY 1 C16 32 1 N 1 B MAY 407 ? C17 ? P MAY 1 C17 33 1 N 1 B MAY 407 ? C18 ? P MAY 1 C18 34 1 N 1 B MAY 407 ? C19 ? P MAY 1 C19 35 1 N 1 B MAY 407 ? C20 ? P MAY 1 C20 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLY 0 ? A GLY 1 2 1 Y 1 A ALA 1 ? A ALA 2 3 1 Y 1 A GLY 2 ? A GLY 3 4 1 Y 1 A ARG 3 ? A ARG 4 5 1 Y 1 A PRO 379 ? A PRO 380 6 1 Y 1 B GLY 0 ? B GLY 1 7 1 Y 1 B ALA 1 ? B ALA 2 8 1 Y 1 B GLY 2 ? B GLY 3 # _pdbx_audit_support.funding_organization 'National Institutes of Health/National Heart, Lung, and Blood Institute' _pdbx_audit_support.country 'United States' _pdbx_audit_support.grant_number HL086865 _pdbx_audit_support.ordinal 1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-MANNOSE BMA 4 'METHYL ARACHIDONYL FLUOROPHOSPHONATE' MAY #