data_4YYA # _entry.id 4YYA # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4YYA WWPDB D_1000208275 # loop_ _pdbx_database_related.db_name _pdbx_database_related.details _pdbx_database_related.db_id _pdbx_database_related.content_type PDB . 4yy1 unspecified PDB . 4yy0 unspecified PDB . 4yy7 unspecified PDB . 4yy9 unspecified PDB . 4yyb 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 4YYA _pdbx_database_status.recvd_initial_deposition_date 2015-03-23 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _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 'Wang, F.' 1 'Qi, J.' 2 'Bi, Y.' 3 'Zhang, W.' 4 'Wang, M.' 5 'Wang, M.' 6 'Liu, J.' 7 'Yan, J.' 8 'Shi, Y.' 9 'Gao, G.F.' 10 # _citation.abstract ? _citation.abstract_id_CAS ? _citation.book_id_ISBN ? _citation.book_publisher ? _citation.book_publisher_city ? _citation.book_title ? _citation.coordinate_linkage ? _citation.country ? _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev 'To Be Published' _citation.journal_id_ASTM ? _citation.journal_id_CSD 0353 _citation.journal_id_ISSN ? _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume ? _citation.language ? _citation.page_first ? _citation.page_last ? _citation.title 'Structure of hemagglutinin from a H6N1 influenza virus (A/chicken/Taiwan/A2837/2013)' _citation.year ? _citation.database_id_CSD ? _citation.pdbx_database_id_DOI ? _citation.pdbx_database_id_PubMed ? _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Wang, F.' 1 primary 'Qi, J.' 2 primary 'Bi, Y.' 3 primary 'Zhang, W.' 4 primary 'Wang, M.' 5 primary 'Wang, M.' 6 primary 'Liu, J.' 7 primary 'Yan, J.' 8 primary 'Shi, Y.' 9 primary 'Gao, G.F.' 10 # _cell.angle_alpha 90.00 _cell.angle_alpha_esd ? _cell.angle_beta 90.00 _cell.angle_beta_esd ? _cell.angle_gamma 120.00 _cell.angle_gamma_esd ? _cell.entry_id 4YYA _cell.details ? _cell.formula_units_Z ? _cell.length_a 114.194 _cell.length_a_esd ? _cell.length_b 114.194 _cell.length_b_esd ? _cell.length_c 164.962 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 6 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 4YYA _symmetry.cell_setting ? _symmetry.Int_Tables_number 173 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 63' _symmetry.pdbx_full_space_group_name_H-M ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man HA1 36548.293 1 ? ? ? ? 2 polymer man HA2 19651.691 1 ? ? ? ? 3 non-polymer syn N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 4 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 5 non-polymer man BETA-D-GALACTOSE 180.156 2 ? ? ? ? 6 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 7 water nat water 18.015 136 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;DKICIGYHANNSTTQVDTLLEKNVTVTHSVELLENQKEKRFCKIMNKAPLDLKDCTIEGWILGNPKCDLLLGDQSWSYIV ERPNAQNGICYPGVLNELEELKAFIGSGERVERFEMFPKSTWAGVDTSRGVTNACPSYTLDSSFYRNLVWLVKTDSATYP VIKGTYNNTGTQPILYFWGVHHPLDTTVQDNLYGSGDKYVRMGTESMNFAKSPEIAARPAVNGQRSRIDYYWSVLRPGET LNVESNGNLIAPWYAYKFVSTNKKGAVFKSDLPIENCDATCQTITGVLRTNKTFQNVSPLWIGECPKYVKSESLRLATGL RNVPQ ; ;DKICIGYHANNSTTQVDTLLEKNVTVTHSVELLENQKEKRFCKIMNKAPLDLKDCTIEGWILGNPKCDLLLGDQSWSYIV ERPNAQNGICYPGVLNELEELKAFIGSGERVERFEMFPKSTWAGVDTSRGVTNACPSYTLDSSFYRNLVWLVKTDSATYP VIKGTYNNTGTQPILYFWGVHHPLDTTVQDNLYGSGDKYVRMGTESMNFAKSPEIAARPAVNGQRSRIDYYWSVLRPGET LNVESNGNLIAPWYAYKFVSTNKKGAVFKSDLPIENCDATCQTITGVLRTNKTFQNVSPLWIGECPKYVKSESLRLATGL RNVPQ ; A ? 2 'polypeptide(L)' no no ;GIFGAIAGFIEGGWTGMIDGWYGYHHENSQGSGYAADRESTQKAIDGITNKVNSIINKMNTQFEAVDHEFSNLERRIGNL NKRMEDGFLDVWTYNAELLVLLENERTLDLHDANVKNLYEKVKSQLRDNANDLGNGCFEFWHKCDNECMESVKNGTYDYP KYQKESKLNRQ ; ;GIFGAIAGFIEGGWTGMIDGWYGYHHENSQGSGYAADRESTQKAIDGITNKVNSIINKMNTQFEAVDHEFSNLERRIGNL NKRMEDGFLDVWTYNAELLVLLENERTLDLHDANVKNLYEKVKSQLRDNANDLGNGCFEFWHKCDNECMESVKNGTYDYP KYQKESKLNRQ ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 LYS n 1 3 ILE n 1 4 CYS n 1 5 ILE n 1 6 GLY n 1 7 TYR n 1 8 HIS n 1 9 ALA n 1 10 ASN n 1 11 ASN n 1 12 SER n 1 13 THR n 1 14 THR n 1 15 GLN n 1 16 VAL n 1 17 ASP n 1 18 THR n 1 19 LEU n 1 20 LEU n 1 21 GLU n 1 22 LYS n 1 23 ASN n 1 24 VAL n 1 25 THR n 1 26 VAL n 1 27 THR n 1 28 HIS n 1 29 SER n 1 30 VAL n 1 31 GLU n 1 32 LEU n 1 33 LEU n 1 34 GLU n 1 35 ASN n 1 36 GLN n 1 37 LYS n 1 38 GLU n 1 39 LYS n 1 40 ARG n 1 41 PHE n 1 42 CYS n 1 43 LYS n 1 44 ILE n 1 45 MET n 1 46 ASN n 1 47 LYS n 1 48 ALA n 1 49 PRO n 1 50 LEU n 1 51 ASP n 1 52 LEU n 1 53 LYS n 1 54 ASP n 1 55 CYS n 1 56 THR n 1 57 ILE n 1 58 GLU n 1 59 GLY n 1 60 TRP n 1 61 ILE n 1 62 LEU n 1 63 GLY n 1 64 ASN n 1 65 PRO n 1 66 LYS n 1 67 CYS n 1 68 ASP n 1 69 LEU n 1 70 LEU n 1 71 LEU n 1 72 GLY n 1 73 ASP n 1 74 GLN n 1 75 SER n 1 76 TRP n 1 77 SER n 1 78 TYR n 1 79 ILE n 1 80 VAL n 1 81 GLU n 1 82 ARG n 1 83 PRO n 1 84 ASN n 1 85 ALA n 1 86 GLN n 1 87 ASN n 1 88 GLY n 1 89 ILE n 1 90 CYS n 1 91 TYR n 1 92 PRO n 1 93 GLY n 1 94 VAL n 1 95 LEU n 1 96 ASN n 1 97 GLU n 1 98 LEU n 1 99 GLU n 1 100 GLU n 1 101 LEU n 1 102 LYS n 1 103 ALA n 1 104 PHE n 1 105 ILE n 1 106 GLY n 1 107 SER n 1 108 GLY n 1 109 GLU n 1 110 ARG n 1 111 VAL n 1 112 GLU n 1 113 ARG n 1 114 PHE n 1 115 GLU n 1 116 MET n 1 117 PHE n 1 118 PRO n 1 119 LYS n 1 120 SER n 1 121 THR n 1 122 TRP n 1 123 ALA n 1 124 GLY n 1 125 VAL n 1 126 ASP n 1 127 THR n 1 128 SER n 1 129 ARG n 1 130 GLY n 1 131 VAL n 1 132 THR n 1 133 ASN n 1 134 ALA n 1 135 CYS n 1 136 PRO n 1 137 SER n 1 138 TYR n 1 139 THR n 1 140 LEU n 1 141 ASP n 1 142 SER n 1 143 SER n 1 144 PHE n 1 145 TYR n 1 146 ARG n 1 147 ASN n 1 148 LEU n 1 149 VAL n 1 150 TRP n 1 151 LEU n 1 152 VAL n 1 153 LYS n 1 154 THR n 1 155 ASP n 1 156 SER n 1 157 ALA n 1 158 THR n 1 159 TYR n 1 160 PRO n 1 161 VAL n 1 162 ILE n 1 163 LYS n 1 164 GLY n 1 165 THR n 1 166 TYR n 1 167 ASN n 1 168 ASN n 1 169 THR n 1 170 GLY n 1 171 THR n 1 172 GLN n 1 173 PRO n 1 174 ILE n 1 175 LEU n 1 176 TYR n 1 177 PHE n 1 178 TRP n 1 179 GLY n 1 180 VAL n 1 181 HIS n 1 182 HIS n 1 183 PRO n 1 184 LEU n 1 185 ASP n 1 186 THR n 1 187 THR n 1 188 VAL n 1 189 GLN n 1 190 ASP n 1 191 ASN n 1 192 LEU n 1 193 TYR n 1 194 GLY n 1 195 SER n 1 196 GLY n 1 197 ASP n 1 198 LYS n 1 199 TYR n 1 200 VAL n 1 201 ARG n 1 202 MET n 1 203 GLY n 1 204 THR n 1 205 GLU n 1 206 SER n 1 207 MET n 1 208 ASN n 1 209 PHE n 1 210 ALA n 1 211 LYS n 1 212 SER n 1 213 PRO n 1 214 GLU n 1 215 ILE n 1 216 ALA n 1 217 ALA n 1 218 ARG n 1 219 PRO n 1 220 ALA n 1 221 VAL n 1 222 ASN n 1 223 GLY n 1 224 GLN n 1 225 ARG n 1 226 SER n 1 227 ARG n 1 228 ILE n 1 229 ASP n 1 230 TYR n 1 231 TYR n 1 232 TRP n 1 233 SER n 1 234 VAL n 1 235 LEU n 1 236 ARG n 1 237 PRO n 1 238 GLY n 1 239 GLU n 1 240 THR n 1 241 LEU n 1 242 ASN n 1 243 VAL n 1 244 GLU n 1 245 SER n 1 246 ASN n 1 247 GLY n 1 248 ASN n 1 249 LEU n 1 250 ILE n 1 251 ALA n 1 252 PRO n 1 253 TRP n 1 254 TYR n 1 255 ALA n 1 256 TYR n 1 257 LYS n 1 258 PHE n 1 259 VAL n 1 260 SER n 1 261 THR n 1 262 ASN n 1 263 LYS n 1 264 LYS n 1 265 GLY n 1 266 ALA n 1 267 VAL n 1 268 PHE n 1 269 LYS n 1 270 SER n 1 271 ASP n 1 272 LEU n 1 273 PRO n 1 274 ILE n 1 275 GLU n 1 276 ASN n 1 277 CYS n 1 278 ASP n 1 279 ALA n 1 280 THR n 1 281 CYS n 1 282 GLN n 1 283 THR n 1 284 ILE n 1 285 THR n 1 286 GLY n 1 287 VAL n 1 288 LEU n 1 289 ARG n 1 290 THR n 1 291 ASN n 1 292 LYS n 1 293 THR n 1 294 PHE n 1 295 GLN n 1 296 ASN n 1 297 VAL n 1 298 SER n 1 299 PRO n 1 300 LEU n 1 301 TRP n 1 302 ILE n 1 303 GLY n 1 304 GLU n 1 305 CYS n 1 306 PRO n 1 307 LYS n 1 308 TYR n 1 309 VAL n 1 310 LYS n 1 311 SER n 1 312 GLU n 1 313 SER n 1 314 LEU n 1 315 ARG n 1 316 LEU n 1 317 ALA n 1 318 THR n 1 319 GLY n 1 320 LEU n 1 321 ARG n 1 322 ASN n 1 323 VAL n 1 324 PRO n 1 325 GLN n 2 1 GLY n 2 2 ILE n 2 3 PHE n 2 4 GLY n 2 5 ALA n 2 6 ILE n 2 7 ALA n 2 8 GLY n 2 9 PHE n 2 10 ILE n 2 11 GLU n 2 12 GLY n 2 13 GLY n 2 14 TRP n 2 15 THR n 2 16 GLY n 2 17 MET n 2 18 ILE n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 TYR n 2 25 HIS n 2 26 HIS n 2 27 GLU n 2 28 ASN n 2 29 SER n 2 30 GLN n 2 31 GLY n 2 32 SER n 2 33 GLY n 2 34 TYR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 ARG n 2 39 GLU n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 LYS n 2 44 ALA n 2 45 ILE n 2 46 ASP n 2 47 GLY n 2 48 ILE n 2 49 THR n 2 50 ASN n 2 51 LYS n 2 52 VAL n 2 53 ASN n 2 54 SER n 2 55 ILE n 2 56 ILE n 2 57 ASN n 2 58 LYS n 2 59 MET n 2 60 ASN n 2 61 THR n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 ALA n 2 66 VAL n 2 67 ASP n 2 68 HIS n 2 69 GLU n 2 70 PHE n 2 71 SER n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 ILE n 2 78 GLY n 2 79 ASN n 2 80 LEU n 2 81 ASN n 2 82 LYS n 2 83 ARG n 2 84 MET n 2 85 GLU n 2 86 ASP n 2 87 GLY n 2 88 PHE n 2 89 LEU n 2 90 ASP n 2 91 VAL n 2 92 TRP n 2 93 THR n 2 94 TYR n 2 95 ASN n 2 96 ALA n 2 97 GLU n 2 98 LEU n 2 99 LEU n 2 100 VAL n 2 101 LEU n 2 102 LEU n 2 103 GLU n 2 104 ASN n 2 105 GLU n 2 106 ARG n 2 107 THR n 2 108 LEU n 2 109 ASP n 2 110 LEU n 2 111 HIS n 2 112 ASP n 2 113 ALA n 2 114 ASN n 2 115 VAL n 2 116 LYS n 2 117 ASN n 2 118 LEU n 2 119 TYR n 2 120 GLU n 2 121 LYS n 2 122 VAL n 2 123 LYS n 2 124 SER n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 ALA n 2 131 ASN n 2 132 ASP n 2 133 LEU n 2 134 GLY n 2 135 ASN n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 PHE n 2 141 TRP n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASN n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 GLU n 2 151 SER n 2 152 VAL n 2 153 LYS n 2 154 ASN n 2 155 GLY n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 TYR n 2 160 PRO n 2 161 LYS n 2 162 TYR n 2 163 GLN n 2 164 LYS n 2 165 GLU n 2 166 SER n 2 167 LYS n 2 168 LEU n 2 169 ASN n 2 170 ARG n 2 171 GLN n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _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 _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _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 _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample 'Biological sequence' 1 325 ? ? ? ? ? ? ? ? ? 'unidentified influenza virus' 119212 ? ? ? ? ? ? ? ? 'Insect cell expression vector pTIE1' 266783 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample 'Biological sequence' 1 171 ? ? ? ? ? ? ? ? ? 'unidentified influenza virus' 119212 ? ? ? ? ? ? ? ? 'Insect cell expression vector pTIE1' 266783 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin 1 PDB 4YYA 4YYA ? 1 ? 1 2 PDB 4YYA 4YYA ? 2 ? 1 # 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 4YYA A 1 ? 325 ? 4YYA 1 ? 325 ? 1 325 2 2 4YYA B 1 ? 171 ? 4YYA 330 ? 500 ? 330 500 # 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 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 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 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 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 4YYA _exptl.crystals_number ? _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 5.52 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 77.74 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.id 1 _exptl_crystal.preparation ? _exptl_crystal.size_max ? _exptl_crystal.size_mid ? _exptl_crystal.size_min ? _exptl_crystal.size_rad ? _exptl_crystal.colour_lustre ? _exptl_crystal.colour_modifier ? _exptl_crystal.colour_primary ? _exptl_crystal.density_meas ? _exptl_crystal.density_meas_esd ? _exptl_crystal.density_meas_gt ? _exptl_crystal.density_meas_lt ? _exptl_crystal.density_meas_temp ? _exptl_crystal.density_meas_temp_esd ? _exptl_crystal.density_meas_temp_gt ? _exptl_crystal.density_meas_temp_lt ? _exptl_crystal.pdbx_crystal_image_url ? _exptl_crystal.pdbx_crystal_image_format ? _exptl_crystal.pdbx_mosaicity ? _exptl_crystal.pdbx_mosaicity_esd ? # _exptl_crystal_grow.apparatus ? _exptl_crystal_grow.atmosphere ? _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.details ? _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.method_ref ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pressure ? _exptl_crystal_grow.pressure_esd ? _exptl_crystal_grow.seeding ? _exptl_crystal_grow.seeding_ref ? _exptl_crystal_grow.temp 291.15 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details '0.2M ammonium acetate, 0.1M sodium acetate pH4.0, 15%(w/v) PEG4000' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.ambient_environment ? _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.ambient_temp_esd ? _diffrn.crystal_id 1 _diffrn.crystal_support ? _diffrn.crystal_treatment ? _diffrn.details ? _diffrn.id 1 _diffrn.ambient_pressure ? _diffrn.ambient_pressure_esd ? _diffrn.ambient_pressure_gt ? _diffrn.ambient_pressure_lt ? _diffrn.ambient_temp_gt ? _diffrn.ambient_temp_lt ? # _diffrn_detector.details ? _diffrn_detector.detector CCD _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'ADSC QUANTUM 315r' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2013-09-10 # _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 1.07138 _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 'SSRF BEAMLINE BL17U' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 1.07138 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL17U _diffrn_source.pdbx_synchrotron_site SSRF # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 4YYA _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 2.595 _reflns.d_resolution_low 50 _reflns.details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.number_all ? _reflns.number_obs 37568 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 99.9 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 13.1 _reflns.pdbx_Rmerge_I_obs 0.126 _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 22.0 _reflns.pdbx_res_netI_over_av_sigmaI_2 ? _reflns.pdbx_res_netI_over_sigmaI_2 ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_d_res_high_opt ? _reflns.pdbx_d_res_low_opt ? _reflns.pdbx_d_res_opt_method ? _reflns.phase_calculation_details ? _reflns.pdbx_Rrim_I_all ? _reflns.pdbx_Rpim_I_all ? _reflns.pdbx_d_opt ? _reflns.pdbx_number_measured_all ? _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.pdbx_CC_half ? _reflns.pdbx_R_split ? # _reflns_shell.d_res_high 2.6 _reflns_shell.d_res_low 2.69 _reflns_shell.meanI_over_sigI_all ? _reflns_shell.meanI_over_sigI_obs 6.8 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_possible ? _reflns_shell.number_unique_all ? _reflns_shell.number_unique_obs ? _reflns_shell.percent_possible_all 100 _reflns_shell.percent_possible_obs ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.Rmerge_I_obs 0.494 _reflns_shell.meanI_over_sigI_gt ? _reflns_shell.meanI_over_uI_all ? _reflns_shell.meanI_over_uI_gt ? _reflns_shell.number_measured_gt ? _reflns_shell.number_unique_gt ? _reflns_shell.percent_possible_gt ? _reflns_shell.Rmerge_F_gt ? _reflns_shell.Rmerge_I_gt ? _reflns_shell.pdbx_redundancy 13.2 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_netI_over_sigmaI_all ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_CC_half ? _reflns_shell.pdbx_R_split ? # _refine.aniso_B[1][1] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][2] ? _refine.aniso_B[2][3] ? _refine.aniso_B[3][3] ? _refine.B_iso_max ? _refine.B_iso_mean ? _refine.B_iso_min ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.details ? _refine.diff_density_max ? _refine.diff_density_max_esd ? _refine.diff_density_min ? _refine.diff_density_min_esd ? _refine.diff_density_rms ? _refine.diff_density_rms_esd ? _refine.entry_id 4YYA _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 2.595 _refine.ls_d_res_low 46.946 _refine.ls_extinction_coef ? _refine.ls_extinction_coef_esd ? _refine.ls_extinction_expression ? _refine.ls_extinction_method ? _refine.ls_goodness_of_fit_all ? _refine.ls_goodness_of_fit_all_esd ? _refine.ls_goodness_of_fit_obs ? _refine.ls_goodness_of_fit_obs_esd ? _refine.ls_hydrogen_treatment ? _refine.ls_matrix_type ? _refine.ls_number_constraints ? _refine.ls_number_parameters ? _refine.ls_number_reflns_all ? _refine.ls_number_reflns_obs 37568 _refine.ls_number_reflns_R_free 1879 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 99.69 _refine.ls_percent_reflns_R_free 5.00 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.1834 _refine.ls_R_factor_R_free 0.2082 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.1821 _refine.ls_R_Fsqd_factor_obs ? _refine.ls_R_I_factor_obs ? _refine.ls_redundancy_reflns_all ? _refine.ls_redundancy_reflns_obs ? _refine.ls_restrained_S_all ? _refine.ls_restrained_S_obs ? _refine.ls_shift_over_esd_max ? _refine.ls_shift_over_esd_mean ? _refine.ls_structure_factor_coef ? _refine.ls_weighting_details ? _refine.ls_weighting_scheme ? _refine.ls_wR_factor_all ? _refine.ls_wR_factor_obs ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.ls_R_factor_gt ? _refine.ls_goodness_of_fit_gt ? _refine.ls_goodness_of_fit_ref ? _refine.ls_shift_over_su_max ? _refine.ls_shift_over_su_max_lt ? _refine.ls_shift_over_su_mean ? _refine.ls_shift_over_su_mean_lt ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.37 _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method 'FREE R-VALUE' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_R_Free_selection_details ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error 21.07 _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_diffrn_id 1 _refine.overall_SU_B ? _refine.overall_SU_ML 0.23 _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_average_fsc_overall ? _refine.pdbx_average_fsc_work ? _refine.pdbx_average_fsc_free ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4073 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 0 _refine_hist.number_atoms_solvent 136 _refine_hist.number_atoms_total 4209 _refine_hist.d_res_high 2.595 _refine_hist.d_res_low 46.946 # loop_ _refine_ls_restr.pdbx_refine_id _refine_ls_restr.criterion _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.number _refine_ls_restr.rejects _refine_ls_restr.type _refine_ls_restr.weight _refine_ls_restr.pdbx_restraint_function 'X-RAY DIFFRACTION' ? 0.006 ? 4175 ? f_bond_d ? ? 'X-RAY DIFFRACTION' ? 1.037 ? 5664 ? f_angle_d ? ? 'X-RAY DIFFRACTION' ? 14.592 ? 1527 ? f_dihedral_angle_d ? ? 'X-RAY DIFFRACTION' ? 0.290 ? 632 ? f_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.018 ? 723 ? f_plane_restr ? ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_all _refine_ls_shell.number_reflns_obs _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.R_factor_all _refine_ls_shell.R_factor_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.R_factor_R_work _refine_ls_shell.redundancy_reflns_all _refine_ls_shell.redundancy_reflns_obs _refine_ls_shell.wR_factor_all _refine_ls_shell.wR_factor_obs _refine_ls_shell.wR_factor_R_free _refine_ls_shell.wR_factor_R_work _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.pdbx_phase_error _refine_ls_shell.pdbx_fsc_work _refine_ls_shell.pdbx_fsc_free 'X-RAY DIFFRACTION' 2.5946 2.6648 . . 128 2674 97.00 . . . 0.2633 . 0.2230 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.6648 2.7432 . . 153 2721 100.00 . . . 0.2209 . 0.2104 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.7432 2.8317 . . 123 2770 100.00 . . . 0.2200 . 0.2086 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.8317 2.9329 . . 144 2748 100.00 . . . 0.2594 . 0.2211 . . . . . . . . . . 'X-RAY DIFFRACTION' 2.9329 3.0503 . . 135 2753 100.00 . . . 0.2423 . 0.2120 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.0503 3.1891 . . 152 2754 100.00 . . . 0.2297 . 0.1979 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.1891 3.3572 . . 141 2755 100.00 . . . 0.1976 . 0.1981 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.3572 3.5675 . . 138 2743 100.00 . . . 0.2370 . 0.1981 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.5675 3.8428 . . 165 2726 100.00 . . . 0.1846 . 0.1689 . . . . . . . . . . 'X-RAY DIFFRACTION' 3.8428 4.2293 . . 143 2765 100.00 . . . 0.1899 . 0.1527 . . . . . . . . . . 'X-RAY DIFFRACTION' 4.2293 4.8408 . . 144 2748 100.00 . . . 0.1818 . 0.1389 . . . . . . . . . . 'X-RAY DIFFRACTION' 4.8408 6.0968 . . 154 2763 100.00 . . . 0.1820 . 0.1615 . . . . . . . . . . 'X-RAY DIFFRACTION' 6.0968 46.9538 . . 159 2769 99.00 . . . 0.2197 . 0.2004 . . . . . . . . . . # _struct.entry_id 4YYA _struct.title ;The structure of hemagglutinin from a H6N1 influenza virus (A/Taiwan/2/2013) in complex with avian receptor analog 3'SLNLN ; _struct.pdbx_descriptor 'HA1, HA2' _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 4YYA _struct_keywords.text 'Hemagglutinin, IMMUNE SYSTEM' _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 3 ? H N N 5 ? I N N 3 ? J N N 3 ? K N N 6 ? L N N 7 ? M N N 7 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 THR A 56 ? GLY A 63 ? THR A 56 GLY A 63 1 ? 8 HELX_P HELX_P2 AA2 GLU A 97 ? SER A 107 ? GLU A 97 SER A 107 1 ? 11 HELX_P HELX_P3 AA3 PRO A 118 ? TRP A 122 ? PRO A 118 TRP A 122 5 ? 5 HELX_P HELX_P4 AA4 ASP A 185 ? GLY A 194 ? ASP A 185 GLY A 194 1 ? 10 HELX_P HELX_P5 AA5 ASP B 37 ? MET B 59 ? ASP B 366 MET B 388 1 ? 23 HELX_P HELX_P6 AA6 GLU B 74 ? ARG B 127 ? GLU B 403 ARG B 456 1 ? 54 HELX_P HELX_P7 AA7 ASP B 145 ? ASN B 154 ? ASP B 474 ASN B 483 1 ? 10 HELX_P HELX_P8 AA8 ASP B 158 ? GLN B 171 ? ASP B 487 GLN B 500 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 4 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4 B CYS 466 1_555 ? ? ? ? ? ? ? 2.043 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 277 SG ? ? A CYS 42 A CYS 277 1_555 ? ? ? ? ? ? ? 2.035 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.038 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.043 ? disulf5 disulf ? ? A CYS 281 SG ? ? ? 1_555 A CYS 305 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.031 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 473 B CYS 477 1_555 ? ? ? ? ? ? ? 2.050 ? covale1 covale one ? A ASN 23 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 23 A NAG 601 1_555 ? ? ? ? ? ? ? 1.435 ? covale2 covale one ? A ASN 167 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 167 A NAG 602 1_555 ? ? ? ? ? ? ? 1.438 ? covale3 covale one ? B ASN 154 ND2 ? ? ? 1_555 I NAG . C1 ? ? B ASN 483 B NAG 601 1_555 ? ? ? ? ? ? ? 1.441 ? covale4 covale one ? E SIA . C2 ? ? ? 1_555 F GAL . O3 ? ? A SIA 603 A GAL 604 1_555 ? ? ? ? ? ? ? 1.430 ? covale5 covale both ? F GAL . C1 ? ? ? 1_555 G NAG . O4 ? ? A GAL 604 A NAG 605 1_555 ? ? ? ? ? ? ? 1.454 ? covale6 covale one ? G NAG . C1 ? ? ? 1_555 H GAL . O3 ? ? A NAG 605 A GAL 606 1_555 ? ? ? ? ? ? ? 1.427 ? covale7 covale both ? I NAG . O4 ? ? ? 1_555 J NAG . C1 ? ? B NAG 601 B NAG 602 1_555 ? ? ? ? ? ? ? 1.439 ? covale8 covale both ? J NAG . O4 ? ? ? 1_555 K BMA . C1 ? ? B NAG 602 B BMA 603 1_555 ? ? ? ? ? ? ? 1.442 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 5 ? AA2 ? 2 ? AA3 ? 2 ? AA4 ? 3 ? AA5 ? 2 ? AA6 ? 3 ? AA7 ? 6 ? AA8 ? 5 ? AA9 ? 4 ? AB1 ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA1 3 4 ? anti-parallel AA1 4 5 ? anti-parallel AA2 1 2 ? anti-parallel AA3 1 2 ? anti-parallel AA4 1 2 ? parallel AA4 2 3 ? parallel AA5 1 2 ? parallel AA6 1 2 ? parallel AA6 2 3 ? parallel AA7 1 2 ? anti-parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel AA7 4 5 ? anti-parallel AA7 5 6 ? anti-parallel AA8 1 2 ? anti-parallel AA8 2 3 ? anti-parallel AA8 3 4 ? anti-parallel AA8 4 5 ? anti-parallel AA9 1 2 ? anti-parallel AA9 2 3 ? anti-parallel AA9 3 4 ? anti-parallel AB1 1 2 ? anti-parallel AB1 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 GLY B 31 ? ALA B 36 ? GLY B 360 ALA B 365 AA1 2 TYR B 22 ? ASN B 28 ? TYR B 351 ASN B 357 AA1 3 LYS A 2 ? TYR A 7 ? LYS A 2 TYR A 7 AA1 4 CYS B 137 ? PHE B 140 ? CYS B 466 PHE B 469 AA1 5 ALA B 130 ? ASP B 132 ? ALA B 459 ASP B 461 AA2 1 GLN A 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA2 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AA3 1 SER A 29 ? GLU A 31 ? SER A 29 GLU A 31 AA3 2 ARG A 315 ? ALA A 317 ? ARG A 315 ALA A 317 AA4 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AA4 2 PHE A 294 ? GLN A 295 ? PHE A 294 GLN A 295 AA4 3 LYS A 307 ? TYR A 308 ? LYS A 307 TYR A 308 AA5 1 PHE A 41 ? ILE A 44 ? PHE A 41 ILE A 44 AA5 2 ILE A 274 ? ALA A 279 ? ILE A 274 ALA A 279 AA6 1 LEU A 50 ? ASP A 51 ? LEU A 50 ASP A 51 AA6 2 ILE A 79 ? GLU A 81 ? ILE A 79 GLU A 81 AA6 3 VAL A 267 ? LYS A 269 ? VAL A 267 LYS A 269 AA7 1 GLN A 74 ? SER A 75 ? GLN A 74 SER A 75 AA7 2 GLY A 108 ? GLU A 115 ? GLY A 108 GLU A 115 AA7 3 TYR A 254 ? SER A 260 ? TYR A 254 SER A 260 AA7 4 ILE A 174 ? HIS A 182 ? ILE A 174 HIS A 182 AA7 5 LEU A 249 ? PRO A 252 ? LEU A 249 PRO A 252 AA7 6 LEU A 148 ? TRP A 150 ? LEU A 148 TRP A 150 AA8 1 GLN A 74 ? SER A 75 ? GLN A 74 SER A 75 AA8 2 GLY A 108 ? GLU A 115 ? GLY A 108 GLU A 115 AA8 3 TYR A 254 ? SER A 260 ? TYR A 254 SER A 260 AA8 4 ILE A 174 ? HIS A 182 ? ILE A 174 HIS A 182 AA8 5 ARG A 227 ? LEU A 235 ? ARG A 227 LEU A 235 AA9 1 ILE A 162 ? ASN A 167 ? ILE A 162 ASN A 167 AA9 2 THR A 240 ? SER A 245 ? THR A 240 SER A 245 AA9 3 VAL A 200 ? GLY A 203 ? VAL A 200 GLY A 203 AA9 4 ASN A 208 ? LYS A 211 ? ASN A 208 LYS A 211 AB1 1 GLY A 286 ? VAL A 287 ? GLY A 286 VAL A 287 AB1 2 CYS A 281 ? THR A 283 ? CYS A 281 THR A 283 AB1 3 TRP A 301 ? GLY A 303 ? TRP A 301 GLY A 303 # 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 ALA B 35 ? O ALA B 364 N TYR B 24 ? N TYR B 353 AA1 2 3 O HIS B 25 ? O HIS B 354 N CYS A 4 ? N CYS A 4 AA1 3 4 N ILE A 3 ? N ILE A 3 O PHE B 138 ? O PHE B 467 AA1 4 5 O GLU B 139 ? O GLU B 468 N ASN B 131 ? N ASN B 460 AA2 1 2 N VAL A 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AA3 1 2 N VAL A 30 ? N VAL A 30 O LEU A 316 ? O LEU A 316 AA4 1 2 N GLU A 34 ? N GLU A 34 O PHE A 294 ? O PHE A 294 AA4 2 3 N GLN A 295 ? N GLN A 295 O LYS A 307 ? O LYS A 307 AA5 1 2 N LYS A 43 ? N LYS A 43 O CYS A 277 ? O CYS A 277 AA6 1 2 N LEU A 50 ? N LEU A 50 O VAL A 80 ? O VAL A 80 AA6 2 3 N ILE A 79 ? N ILE A 79 O PHE A 268 ? O PHE A 268 AA7 1 2 N GLN A 74 ? N GLN A 74 O VAL A 111 ? O VAL A 111 AA7 2 3 N GLU A 112 ? N GLU A 112 O LYS A 257 ? O LYS A 257 AA7 3 4 O TYR A 256 ? O TYR A 256 N LEU A 175 ? N LEU A 175 AA7 4 5 N GLY A 179 ? N GLY A 179 O ILE A 250 ? O ILE A 250 AA7 5 6 O ALA A 251 ? O ALA A 251 N VAL A 149 ? N VAL A 149 AA8 1 2 N GLN A 74 ? N GLN A 74 O VAL A 111 ? O VAL A 111 AA8 2 3 N GLU A 112 ? N GLU A 112 O LYS A 257 ? O LYS A 257 AA8 3 4 O TYR A 256 ? O TYR A 256 N LEU A 175 ? N LEU A 175 AA8 4 5 N HIS A 182 ? N HIS A 182 O ARG A 227 ? O ARG A 227 AA9 1 2 N GLY A 164 ? N GLY A 164 O VAL A 243 ? O VAL A 243 AA9 2 3 O GLU A 244 ? O GLU A 244 N ARG A 201 ? N ARG A 201 AA9 3 4 N MET A 202 ? N MET A 202 O PHE A 209 ? O PHE A 209 AB1 1 2 O GLY A 286 ? O GLY A 286 N THR A 283 ? N THR A 283 AB1 2 3 N GLN A 282 ? N GLN A 282 O ILE A 302 ? O ILE A 302 # _struct_site.id AC1 _struct_site.pdbx_evidence_code Software _struct_site.pdbx_auth_asym_id A _struct_site.pdbx_auth_comp_id SIA _struct_site.pdbx_auth_seq_id 603 _struct_site.pdbx_auth_ins_code ? _struct_site.pdbx_num_residues 9 _struct_site.details 'binding site for Poly-Saccharide residues SIA A 603 through GAL A 606' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 9 TYR A 91 ? TYR A 91 . ? 1_555 ? 2 AC1 9 ARG A 129 ? ARG A 129 . ? 1_555 ? 3 AC1 9 VAL A 131 ? VAL A 131 . ? 1_555 ? 4 AC1 9 THR A 132 ? THR A 132 . ? 1_555 ? 5 AC1 9 ASN A 133 ? ASN A 133 . ? 1_555 ? 6 AC1 9 HIS A 181 ? HIS A 181 . ? 1_555 ? 7 AC1 9 GLY A 223 ? GLY A 223 . ? 1_555 ? 8 AC1 9 GLN A 224 ? GLN A 224 . ? 1_555 ? 9 AC1 9 SER A 226 ? SER A 226 . ? 1_555 ? # _atom_sites.entry_id 4YYA _atom_sites.fract_transf_matrix[1][1] 0.008757 _atom_sites.fract_transf_matrix[1][2] 0.005056 _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] 0.010112 _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] 0.006062 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? -36.900 38.203 -71.885 1.00 30.43 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? -37.218 39.215 -70.869 1.00 46.23 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? -38.279 38.721 -69.887 1.00 44.94 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? -39.291 38.134 -70.295 1.00 36.89 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? -37.682 40.522 -71.519 1.00 41.77 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? -36.529 41.360 -72.043 1.00 53.13 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? -35.384 40.850 -72.082 1.00 48.44 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? -36.775 42.530 -72.422 1.00 49.74 ? 1 ASP A OD2 1 ATOM 9 N N . LYS A 1 2 ? -38.054 38.963 -68.596 1.00 40.12 ? 2 LYS A N 1 ATOM 10 C CA . LYS A 1 2 ? -38.927 38.398 -67.570 1.00 43.59 ? 2 LYS A CA 1 ATOM 11 C C . LYS A 1 2 ? -38.850 39.071 -66.200 1.00 42.55 ? 2 LYS A C 1 ATOM 12 O O . LYS A 1 2 ? -37.831 39.667 -65.831 1.00 39.69 ? 2 LYS A O 1 ATOM 13 C CB . LYS A 1 2 ? -38.661 36.894 -67.426 1.00 48.69 ? 2 LYS A CB 1 ATOM 14 C CG . LYS A 1 2 ? -37.215 36.545 -67.139 1.00 53.43 ? 2 LYS A CG 1 ATOM 15 C CD . LYS A 1 2 ? -37.009 35.031 -67.101 1.00 65.85 ? 2 LYS A CD 1 ATOM 16 C CE . LYS A 1 2 ? -37.814 34.385 -65.983 1.00 60.54 ? 2 LYS A CE 1 ATOM 17 N NZ . LYS A 1 2 ? -37.553 32.918 -65.880 1.00 68.90 ? 2 LYS A NZ 1 ATOM 18 N N . ILE A 1 3 ? -39.945 38.968 -65.451 1.00 35.49 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? -39.986 39.446 -64.078 1.00 29.63 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? -40.586 38.348 -63.205 1.00 32.22 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? -41.536 37.673 -63.615 1.00 32.87 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? -40.779 40.773 -63.951 1.00 29.57 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? -40.643 41.360 -62.545 1.00 30.65 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? -42.246 40.589 -64.319 1.00 30.20 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? -41.043 42.827 -62.459 1.00 30.81 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? -40.010 38.152 -62.022 1.00 35.87 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? -40.477 37.127 -61.096 1.00 33.57 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? -40.893 37.761 -59.782 1.00 34.09 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? -40.345 38.793 -59.383 1.00 33.61 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? -39.371 36.106 -60.818 1.00 35.55 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? -38.686 35.293 -62.278 1.00 49.32 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? -41.859 37.144 -59.107 1.00 29.09 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? -42.249 37.574 -57.768 1.00 26.28 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? -41.665 36.560 -56.787 1.00 32.34 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? -41.642 35.357 -57.082 1.00 32.85 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? -43.787 37.668 -57.625 1.00 29.26 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? -44.318 38.871 -58.403 1.00 30.64 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? -44.211 37.803 -56.171 1.00 26.46 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? -44.497 38.617 -59.876 1.00 32.29 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? -41.173 37.031 -55.641 1.00 24.44 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? -40.538 36.144 -54.683 1.00 23.87 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? -40.408 36.733 -53.291 1.00 28.09 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? -40.903 37.835 -53.006 1.00 27.13 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? -39.728 36.000 -52.417 1.00 26.94 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? -39.648 36.387 -51.017 1.00 26.84 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? -38.243 36.199 -50.439 1.00 29.35 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? -37.416 35.458 -50.984 1.00 26.31 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? -40.694 35.634 -50.183 1.00 23.99 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? -40.739 34.149 -50.453 1.00 25.38 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? -41.477 33.644 -51.509 1.00 25.36 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? -40.054 33.252 -49.645 1.00 28.73 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? -41.526 32.297 -51.763 1.00 29.06 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? -40.101 31.898 -49.886 1.00 26.89 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? -40.837 31.427 -50.948 1.00 29.31 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? -40.889 30.078 -51.202 1.00 29.15 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? -37.993 36.888 -49.330 1.00 30.13 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? -36.699 36.886 -48.657 1.00 30.20 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? -36.306 35.516 -48.096 1.00 31.69 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? -37.136 34.795 -47.531 1.00 31.37 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? -36.745 37.904 -47.520 1.00 31.10 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? -35.440 38.109 -46.823 1.00 36.60 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? -34.337 38.655 -47.445 1.00 40.04 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? -35.072 37.876 -45.539 1.00 31.53 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? -33.341 38.733 -46.580 1.00 36.31 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? -33.760 38.267 -45.419 1.00 37.08 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? -35.035 35.164 -48.264 1.00 30.65 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? -34.436 34.041 -47.548 1.00 30.28 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? -33.117 34.523 -46.945 1.00 30.16 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? -32.532 35.492 -47.434 1.00 34.35 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? -34.212 32.863 -48.479 1.00 27.90 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? -32.646 33.870 -45.886 1.00 29.63 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? -31.379 34.270 -45.262 1.00 30.22 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? -30.639 33.109 -44.598 1.00 29.87 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? -30.994 31.948 -44.809 1.00 32.02 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? -31.584 35.432 -44.273 1.00 23.59 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? -32.487 35.063 -43.092 1.00 32.03 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? -32.714 33.881 -42.791 1.00 27.41 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? -32.999 36.087 -42.409 1.00 27.74 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? -29.631 33.424 -43.786 1.00 30.45 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? -28.808 32.389 -43.154 1.00 34.15 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? -29.333 31.933 -41.791 1.00 36.45 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? -28.662 31.179 -41.079 1.00 36.82 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? -27.346 32.852 -43.030 1.00 30.57 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? -27.171 34.029 -42.060 1.00 45.51 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? -28.148 34.615 -41.582 1.00 43.24 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? -25.914 34.383 -41.778 1.00 47.99 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? -30.527 32.394 -41.430 1.00 40.96 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? -31.108 32.081 -40.127 1.00 39.91 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? -31.337 30.580 -39.918 1.00 38.77 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? -31.764 29.865 -40.830 1.00 36.52 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? -32.421 32.840 -39.935 1.00 37.47 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? -33.078 32.446 -38.746 1.00 39.28 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? -31.026 30.118 -38.709 1.00 31.56 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? -31.320 28.755 -38.278 1.00 33.83 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? -32.253 28.790 -37.072 1.00 33.39 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? -32.515 27.761 -36.444 1.00 33.77 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? -30.043 27.981 -37.901 1.00 36.53 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? -29.339 28.688 -36.872 1.00 34.77 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? -29.137 27.804 -39.115 1.00 33.79 ? 13 THR A CG2 1 ATOM 100 N N . THR A 1 14 ? -32.740 29.984 -36.747 1.00 33.70 ? 14 THR A N 1 ATOM 101 C CA . THR A 1 14 ? -33.660 30.153 -35.626 1.00 35.76 ? 14 THR A CA 1 ATOM 102 C C . THR A 1 14 ? -35.060 29.632 -35.979 1.00 36.49 ? 14 THR A C 1 ATOM 103 O O . THR A 1 14 ? -35.582 29.918 -37.066 1.00 34.88 ? 14 THR A O 1 ATOM 104 C CB . THR A 1 14 ? -33.752 31.618 -35.191 1.00 37.71 ? 14 THR A CB 1 ATOM 105 O OG1 . THR A 1 14 ? -32.458 32.077 -34.778 1.00 43.03 ? 14 THR A OG1 1 ATOM 106 C CG2 . THR A 1 14 ? -34.713 31.755 -34.033 1.00 35.31 ? 14 THR A CG2 1 ATOM 107 N N . GLN A 1 15 ? -35.662 28.873 -35.064 1.00 29.37 ? 15 GLN A N 1 ATOM 108 C CA . GLN A 1 15 ? -36.945 28.226 -35.324 1.00 30.29 ? 15 GLN A CA 1 ATOM 109 C C . GLN A 1 15 ? -38.030 28.655 -34.342 1.00 28.05 ? 15 GLN A C 1 ATOM 110 O O . GLN A 1 15 ? -37.737 29.084 -33.220 1.00 25.23 ? 15 GLN A O 1 ATOM 111 C CB . GLN A 1 15 ? -36.785 26.704 -35.275 1.00 27.98 ? 15 GLN A CB 1 ATOM 112 C CG . GLN A 1 15 ? -35.664 26.155 -36.150 1.00 32.42 ? 15 GLN A CG 1 ATOM 113 C CD . GLN A 1 15 ? -35.448 24.669 -35.935 1.00 41.07 ? 15 GLN A CD 1 ATOM 114 O OE1 . GLN A 1 15 ? -35.494 24.184 -34.802 1.00 45.47 ? 15 GLN A OE1 1 ATOM 115 N NE2 . GLN A 1 15 ? -35.226 23.934 -37.022 1.00 43.43 ? 15 GLN A NE2 1 ATOM 116 N N . VAL A 1 16 ? -39.283 28.539 -34.775 1.00 25.77 ? 16 VAL A N 1 ATOM 117 C CA . VAL A 1 16 ? -40.430 28.770 -33.897 1.00 25.16 ? 16 VAL A CA 1 ATOM 118 C C . VAL A 1 16 ? -41.355 27.572 -34.012 1.00 25.46 ? 16 VAL A C 1 ATOM 119 O O . VAL A 1 16 ? -41.205 26.758 -34.928 1.00 24.77 ? 16 VAL A O 1 ATOM 120 C CB . VAL A 1 16 ? -41.220 30.037 -34.287 1.00 23.80 ? 16 VAL A CB 1 ATOM 121 C CG1 . VAL A 1 16 ? -40.329 31.258 -34.240 1.00 23.33 ? 16 VAL A CG1 1 ATOM 122 C CG2 . VAL A 1 16 ? -41.836 29.874 -35.688 1.00 19.31 ? 16 VAL A CG2 1 ATOM 123 N N . ASP A 1 17 ? -42.309 27.460 -33.093 1.00 28.37 ? 17 ASP A N 1 ATOM 124 C CA . ASP A 1 17 ? -43.350 26.455 -33.231 1.00 26.58 ? 17 ASP A CA 1 ATOM 125 C C . ASP A 1 17 ? -44.677 27.142 -33.568 1.00 29.84 ? 17 ASP A C 1 ATOM 126 O O . ASP A 1 17 ? -44.889 28.306 -33.211 1.00 28.81 ? 17 ASP A O 1 ATOM 127 C CB . ASP A 1 17 ? -43.474 25.621 -31.952 1.00 24.92 ? 17 ASP A CB 1 ATOM 128 C CG . ASP A 1 17 ? -42.255 24.739 -31.696 1.00 39.56 ? 17 ASP A CG 1 ATOM 129 O OD1 . ASP A 1 17 ? -41.522 24.422 -32.663 1.00 41.91 ? 17 ASP A OD1 1 ATOM 130 O OD2 . ASP A 1 17 ? -42.040 24.348 -30.523 1.00 38.98 ? 17 ASP A OD2 1 ATOM 131 N N . THR A 1 18 ? -45.547 26.431 -34.286 1.00 30.86 ? 18 THR A N 1 ATOM 132 C CA . THR A 1 18 ? -46.915 26.887 -34.546 1.00 28.67 ? 18 THR A CA 1 ATOM 133 C C . THR A 1 18 ? -47.867 25.773 -34.128 1.00 32.75 ? 18 THR A C 1 ATOM 134 O O . THR A 1 18 ? -47.419 24.675 -33.786 1.00 30.52 ? 18 THR A O 1 ATOM 135 C CB . THR A 1 18 ? -47.153 27.208 -36.036 1.00 27.00 ? 18 THR A CB 1 ATOM 136 O OG1 . THR A 1 18 ? -47.381 25.993 -36.757 1.00 30.58 ? 18 THR A OG1 1 ATOM 137 C CG2 . THR A 1 18 ? -45.958 27.939 -36.631 1.00 27.60 ? 18 THR A CG2 1 ATOM 138 N N . LEU A 1 19 ? -49.172 26.036 -34.166 1.00 30.71 ? 19 LEU A N 1 ATOM 139 C CA . LEU A 1 19 ? -50.141 25.000 -33.823 1.00 30.95 ? 19 LEU A CA 1 ATOM 140 C C . LEU A 1 19 ? -50.080 23.814 -34.790 1.00 32.19 ? 19 LEU A C 1 ATOM 141 O O . LEU A 1 19 ? -50.276 22.673 -34.385 1.00 34.02 ? 19 LEU A O 1 ATOM 142 C CB . LEU A 1 19 ? -51.560 25.573 -33.745 1.00 32.51 ? 19 LEU A CB 1 ATOM 143 C CG . LEU A 1 19 ? -51.960 26.316 -32.465 1.00 31.24 ? 19 LEU A CG 1 ATOM 144 C CD1 . LEU A 1 19 ? -53.243 27.094 -32.674 1.00 37.00 ? 19 LEU A CD1 1 ATOM 145 C CD2 . LEU A 1 19 ? -52.136 25.350 -31.303 1.00 31.65 ? 19 LEU A CD2 1 ATOM 146 N N . LEU A 1 20 ? -49.780 24.081 -36.059 1.00 31.00 ? 20 LEU A N 1 ATOM 147 C CA . LEU A 1 20 ? -49.746 23.025 -37.072 1.00 33.09 ? 20 LEU A CA 1 ATOM 148 C C . LEU A 1 20 ? -48.369 22.381 -37.258 1.00 34.33 ? 20 LEU A C 1 ATOM 149 O O . LEU A 1 20 ? -48.254 21.323 -37.879 1.00 33.79 ? 20 LEU A O 1 ATOM 150 C CB . LEU A 1 20 ? -50.231 23.564 -38.418 1.00 33.09 ? 20 LEU A CB 1 ATOM 151 C CG . LEU A 1 20 ? -51.647 24.131 -38.487 1.00 33.37 ? 20 LEU A CG 1 ATOM 152 C CD1 . LEU A 1 20 ? -51.874 24.834 -39.824 1.00 35.18 ? 20 LEU A CD1 1 ATOM 153 C CD2 . LEU A 1 20 ? -52.663 23.028 -38.294 1.00 29.75 ? 20 LEU A CD2 1 ATOM 154 N N . GLU A 1 21 ? -47.327 23.005 -36.714 1.00 36.19 ? 21 GLU A N 1 ATOM 155 C CA . GLU A 1 21 ? -45.965 22.666 -37.125 1.00 35.83 ? 21 GLU A CA 1 ATOM 156 C C . GLU A 1 21 ? -44.920 23.020 -36.073 1.00 34.77 ? 21 GLU A C 1 ATOM 157 O O . GLU A 1 21 ? -44.906 24.145 -35.561 1.00 33.31 ? 21 GLU A O 1 ATOM 158 C CB . GLU A 1 21 ? -45.646 23.422 -38.414 1.00 38.76 ? 21 GLU A CB 1 ATOM 159 C CG . GLU A 1 21 ? -44.997 22.609 -39.509 1.00 47.52 ? 21 GLU A CG 1 ATOM 160 C CD . GLU A 1 21 ? -44.999 23.343 -40.845 1.00 56.05 ? 21 GLU A CD 1 ATOM 161 O OE1 . GLU A 1 21 ? -44.047 23.141 -41.629 1.00 52.01 ? 21 GLU A OE1 1 ATOM 162 O OE2 . GLU A 1 21 ? -45.953 24.118 -41.109 1.00 54.04 ? 21 GLU A OE2 1 ATOM 163 N N . LYS A 1 22 ? -44.039 22.069 -35.765 1.00 29.84 ? 22 LYS A N 1 ATOM 164 C CA . LYS A 1 22 ? -42.909 22.335 -34.878 1.00 32.65 ? 22 LYS A CA 1 ATOM 165 C C . LYS A 1 22 ? -41.628 22.606 -35.663 1.00 33.51 ? 22 LYS A C 1 ATOM 166 O O . LYS A 1 22 ? -41.501 22.196 -36.823 1.00 31.08 ? 22 LYS A O 1 ATOM 167 C CB . LYS A 1 22 ? -42.681 21.165 -33.918 1.00 34.47 ? 22 LYS A CB 1 ATOM 168 C CG . LYS A 1 22 ? -43.702 21.057 -32.799 1.00 38.24 ? 22 LYS A CG 1 ATOM 169 C CD . LYS A 1 22 ? -43.450 19.814 -31.953 1.00 47.01 ? 22 LYS A CD 1 ATOM 170 C CE . LYS A 1 22 ? -44.532 19.634 -30.898 1.00 55.92 ? 22 LYS A CE 1 ATOM 171 N NZ . LYS A 1 22 ? -44.397 18.329 -30.186 1.00 67.44 ? 22 LYS A NZ 1 ATOM 172 N N . ASN A 1 23 ? -40.688 23.293 -35.017 1.00 37.93 ? 23 ASN A N 1 ATOM 173 C CA . ASN A 1 23 ? -39.359 23.529 -35.580 1.00 36.68 ? 23 ASN A CA 1 ATOM 174 C C . ASN A 1 23 ? -39.358 24.083 -37.009 1.00 36.62 ? 23 ASN A C 1 ATOM 175 O O . ASN A 1 23 ? -38.775 23.500 -37.923 1.00 32.94 ? 23 ASN A O 1 ATOM 176 C CB . ASN A 1 23 ? -38.471 22.282 -35.410 1.00 37.20 ? 23 ASN A CB 1 ATOM 177 C CG . ASN A 1 23 ? -38.137 22.015 -33.939 1.00 51.53 ? 23 ASN A CG 1 ATOM 178 O OD1 . ASN A 1 23 ? -38.204 22.936 -33.115 1.00 53.03 ? 23 ASN A OD1 1 ATOM 179 N ND2 . ASN A 1 23 ? -37.793 20.763 -33.602 1.00 47.74 ? 23 ASN A ND2 1 ATOM 180 N N . VAL A 1 24 ? -40.034 25.218 -37.174 1.00 34.68 ? 24 VAL A N 1 ATOM 181 C CA . VAL A 1 24 ? -40.070 25.947 -38.436 1.00 30.93 ? 24 VAL A CA 1 ATOM 182 C C . VAL A 1 24 ? -39.019 27.058 -38.416 1.00 31.21 ? 24 VAL A C 1 ATOM 183 O O . VAL A 1 24 ? -39.095 27.977 -37.595 1.00 29.54 ? 24 VAL A O 1 ATOM 184 C CB . VAL A 1 24 ? -41.458 26.574 -38.667 1.00 30.45 ? 24 VAL A CB 1 ATOM 185 C CG1 . VAL A 1 24 ? -41.513 27.291 -40.006 1.00 29.17 ? 24 VAL A CG1 1 ATOM 186 C CG2 . VAL A 1 24 ? -42.538 25.506 -38.590 1.00 32.11 ? 24 VAL A CG2 1 ATOM 187 N N . THR A 1 25 ? -38.037 26.970 -39.311 1.00 28.71 ? 25 THR A N 1 ATOM 188 C CA . THR A 1 25 ? -37.003 27.998 -39.424 1.00 29.66 ? 25 THR A CA 1 ATOM 189 C C . THR A 1 25 ? -37.588 29.275 -40.042 1.00 29.52 ? 25 THR A C 1 ATOM 190 O O . THR A 1 25 ? -38.220 29.226 -41.106 1.00 26.93 ? 25 THR A O 1 ATOM 191 C CB . THR A 1 25 ? -35.826 27.507 -40.297 1.00 34.05 ? 25 THR A CB 1 ATOM 192 O OG1 . THR A 1 25 ? -35.321 26.269 -39.777 1.00 36.37 ? 25 THR A OG1 1 ATOM 193 C CG2 . THR A 1 25 ? -34.700 28.540 -40.329 1.00 28.59 ? 25 THR A CG2 1 ATOM 194 N N . VAL A 1 26 ? -37.374 30.415 -39.387 1.00 25.83 ? 26 VAL A N 1 ATOM 195 C CA . VAL A 1 26 ? -37.893 31.691 -39.890 1.00 27.47 ? 26 VAL A CA 1 ATOM 196 C C . VAL A 1 26 ? -36.791 32.736 -40.084 1.00 30.30 ? 26 VAL A C 1 ATOM 197 O O . VAL A 1 26 ? -35.783 32.720 -39.380 1.00 32.08 ? 26 VAL A O 1 ATOM 198 C CB . VAL A 1 26 ? -39.001 32.272 -38.976 1.00 27.13 ? 26 VAL A CB 1 ATOM 199 C CG1 . VAL A 1 26 ? -40.254 31.408 -39.026 1.00 21.26 ? 26 VAL A CG1 1 ATOM 200 C CG2 . VAL A 1 26 ? -38.495 32.429 -37.543 1.00 23.83 ? 26 VAL A CG2 1 ATOM 201 N N . THR A 1 27 ? -37.004 33.651 -41.029 1.00 28.16 ? 27 THR A N 1 ATOM 202 C CA . THR A 1 27 ? -36.008 34.666 -41.373 1.00 26.19 ? 27 THR A CA 1 ATOM 203 C C . THR A 1 27 ? -35.762 35.655 -40.242 1.00 31.51 ? 27 THR A C 1 ATOM 204 O O . THR A 1 27 ? -34.633 36.092 -40.030 1.00 36.77 ? 27 THR A O 1 ATOM 205 C CB . THR A 1 27 ? -36.397 35.443 -42.652 1.00 29.11 ? 27 THR A CB 1 ATOM 206 O OG1 . THR A 1 27 ? -37.608 36.178 -42.425 1.00 25.56 ? 27 THR A OG1 1 ATOM 207 C CG2 . THR A 1 27 ? -36.585 34.483 -43.822 1.00 24.97 ? 27 THR A CG2 1 ATOM 208 N N . HIS A 1 28 ? -36.826 36.023 -39.533 1.00 29.49 ? 28 HIS A N 1 ATOM 209 C CA . HIS A 1 28 ? -36.724 36.932 -38.392 1.00 26.24 ? 28 HIS A CA 1 ATOM 210 C C . HIS A 1 28 ? -37.693 36.507 -37.294 1.00 30.48 ? 28 HIS A C 1 ATOM 211 O O . HIS A 1 28 ? -38.807 36.051 -37.578 1.00 28.07 ? 28 HIS A O 1 ATOM 212 C CB . HIS A 1 28 ? -37.034 38.372 -38.807 1.00 25.44 ? 28 HIS A CB 1 ATOM 213 C CG . HIS A 1 28 ? -36.225 38.854 -39.969 1.00 33.00 ? 28 HIS A CG 1 ATOM 214 N ND1 . HIS A 1 28 ? -36.567 38.582 -41.278 1.00 29.75 ? 28 HIS A ND1 1 ATOM 215 C CD2 . HIS A 1 28 ? -35.083 39.583 -40.019 1.00 26.41 ? 28 HIS A CD2 1 ATOM 216 C CE1 . HIS A 1 28 ? -35.672 39.126 -42.083 1.00 34.57 ? 28 HIS A CE1 1 ATOM 217 N NE2 . HIS A 1 28 ? -34.763 39.737 -41.348 1.00 36.16 ? 28 HIS A NE2 1 ATOM 218 N N . SER A 1 29 ? -37.268 36.658 -36.044 1.00 26.29 ? 29 SER A N 1 ATOM 219 C CA . SER A 1 29 ? -38.108 36.321 -34.905 1.00 27.26 ? 29 SER A CA 1 ATOM 220 C C . SER A 1 29 ? -37.682 37.122 -33.682 1.00 29.83 ? 29 SER A C 1 ATOM 221 O O . SER A 1 29 ? -36.688 37.851 -33.725 1.00 30.88 ? 29 SER A O 1 ATOM 222 C CB . SER A 1 29 ? -38.049 34.825 -34.612 1.00 23.77 ? 29 SER A CB 1 ATOM 223 O OG . SER A 1 29 ? -36.731 34.415 -34.321 1.00 28.57 ? 29 SER A OG 1 ATOM 224 N N . VAL A 1 30 ? -38.436 36.996 -32.596 1.00 35.13 ? 30 VAL A N 1 ATOM 225 C CA . VAL A 1 30 ? -38.128 37.738 -31.382 1.00 35.97 ? 30 VAL A CA 1 ATOM 226 C C . VAL A 1 30 ? -38.464 36.901 -30.156 1.00 33.70 ? 30 VAL A C 1 ATOM 227 O O . VAL A 1 30 ? -39.568 36.360 -30.047 1.00 35.05 ? 30 VAL A O 1 ATOM 228 C CB . VAL A 1 30 ? -38.860 39.107 -31.352 1.00 33.52 ? 30 VAL A CB 1 ATOM 229 C CG1 . VAL A 1 30 ? -40.340 38.931 -31.633 1.00 30.31 ? 30 VAL A CG1 1 ATOM 230 C CG2 . VAL A 1 30 ? -38.648 39.804 -30.024 1.00 37.56 ? 30 VAL A CG2 1 ATOM 231 N N . GLU A 1 31 ? -37.493 36.769 -29.256 1.00 35.52 ? 31 GLU A N 1 ATOM 232 C CA . GLU A 1 31 ? -37.675 36.020 -28.015 1.00 31.44 ? 31 GLU A CA 1 ATOM 233 C C . GLU A 1 31 ? -38.253 36.939 -26.944 1.00 32.37 ? 31 GLU A C 1 ATOM 234 O O . GLU A 1 31 ? -37.722 38.025 -26.701 1.00 34.15 ? 31 GLU A O 1 ATOM 235 C CB . GLU A 1 31 ? -36.335 35.435 -27.556 1.00 34.60 ? 31 GLU A CB 1 ATOM 236 C CG . GLU A 1 31 ? -36.341 34.807 -26.169 1.00 36.95 ? 31 GLU A CG 1 ATOM 237 C CD . GLU A 1 31 ? -37.234 33.584 -26.077 1.00 37.98 ? 31 GLU A CD 1 ATOM 238 O OE1 . GLU A 1 31 ? -38.279 33.663 -25.397 1.00 38.53 ? 31 GLU A OE1 1 ATOM 239 O OE2 . GLU A 1 31 ? -36.893 32.540 -26.675 1.00 38.78 ? 31 GLU A OE2 1 ATOM 240 N N . LEU A 1 32 ? -39.340 36.506 -26.308 1.00 34.24 ? 32 LEU A N 1 ATOM 241 C CA . LEU A 1 32 ? -40.037 37.339 -25.332 1.00 32.43 ? 32 LEU A CA 1 ATOM 242 C C . LEU A 1 32 ? -39.693 36.955 -23.894 1.00 32.30 ? 32 LEU A C 1 ATOM 243 O O . LEU A 1 32 ? -40.053 37.668 -22.948 1.00 32.88 ? 32 LEU A O 1 ATOM 244 C CB . LEU A 1 32 ? -41.548 37.236 -25.529 1.00 30.73 ? 32 LEU A CB 1 ATOM 245 C CG . LEU A 1 32 ? -42.160 37.531 -26.897 1.00 32.15 ? 32 LEU A CG 1 ATOM 246 C CD1 . LEU A 1 32 ? -43.661 37.250 -26.864 1.00 29.72 ? 32 LEU A CD1 1 ATOM 247 C CD2 . LEU A 1 32 ? -41.906 38.963 -27.328 1.00 25.98 ? 32 LEU A CD2 1 ATOM 248 N N . LEU A 1 33 ? -39.006 35.829 -23.724 1.00 32.73 ? 33 LEU A N 1 ATOM 249 C CA . LEU A 1 33 ? -38.733 35.309 -22.385 1.00 34.62 ? 33 LEU A CA 1 ATOM 250 C C . LEU A 1 33 ? -37.272 35.439 -21.986 1.00 36.25 ? 33 LEU A C 1 ATOM 251 O O . LEU A 1 33 ? -36.374 35.055 -22.747 1.00 43.37 ? 33 LEU A O 1 ATOM 252 C CB . LEU A 1 33 ? -39.160 33.843 -22.284 1.00 36.88 ? 33 LEU A CB 1 ATOM 253 C CG . LEU A 1 33 ? -39.025 33.165 -20.919 1.00 35.52 ? 33 LEU A CG 1 ATOM 254 C CD1 . LEU A 1 33 ? -40.195 32.238 -20.695 1.00 34.12 ? 33 LEU A CD1 1 ATOM 255 C CD2 . LEU A 1 33 ? -37.716 32.391 -20.816 1.00 33.64 ? 33 LEU A CD2 1 ATOM 256 N N . GLU A 1 34 ? -37.039 35.963 -20.783 1.00 37.42 ? 34 GLU A N 1 ATOM 257 C CA . GLU A 1 34 ? -35.694 35.998 -20.208 1.00 38.19 ? 34 GLU A CA 1 ATOM 258 C C . GLU A 1 34 ? -35.440 34.818 -19.271 1.00 35.47 ? 34 GLU A C 1 ATOM 259 O O . GLU A 1 34 ? -36.208 34.584 -18.334 1.00 34.62 ? 34 GLU A O 1 ATOM 260 C CB . GLU A 1 34 ? -35.443 37.308 -19.449 1.00 38.56 ? 34 GLU A CB 1 ATOM 261 C CG . GLU A 1 34 ? -34.006 37.463 -18.965 1.00 38.11 ? 34 GLU A CG 1 ATOM 262 C CD . GLU A 1 34 ? -32.989 37.201 -20.068 1.00 49.55 ? 34 GLU A CD 1 ATOM 263 O OE1 . GLU A 1 34 ? -32.605 38.162 -20.767 1.00 52.16 ? 34 GLU A OE1 1 ATOM 264 O OE2 . GLU A 1 34 ? -32.574 36.032 -20.249 1.00 49.16 ? 34 GLU A OE2 1 ATOM 265 N N . ASN A 1 35 ? -34.355 34.087 -19.517 1.00 32.25 ? 35 ASN A N 1 ATOM 266 C CA . ASN A 1 35 ? -33.967 32.977 -18.645 1.00 35.37 ? 35 ASN A CA 1 ATOM 267 C C . ASN A 1 35 ? -32.643 33.225 -17.910 1.00 35.33 ? 35 ASN A C 1 ATOM 268 O O . ASN A 1 35 ? -32.138 32.345 -17.210 1.00 37.53 ? 35 ASN A O 1 ATOM 269 C CB . ASN A 1 35 ? -33.899 31.669 -19.439 1.00 32.64 ? 35 ASN A CB 1 ATOM 270 C CG . ASN A 1 35 ? -32.905 31.731 -20.594 1.00 40.56 ? 35 ASN A CG 1 ATOM 271 O OD1 . ASN A 1 35 ? -32.334 32.786 -20.896 1.00 38.50 ? 35 ASN A OD1 1 ATOM 272 N ND2 . ASN A 1 35 ? -32.708 30.595 -21.259 1.00 37.06 ? 35 ASN A ND2 1 ATOM 273 N N . GLN A 1 36 ? -32.100 34.431 -18.059 1.00 35.27 ? 36 GLN A N 1 ATOM 274 C CA . GLN A 1 36 ? -30.789 34.779 -17.510 1.00 39.59 ? 36 GLN A CA 1 ATOM 275 C C . GLN A 1 36 ? -30.898 35.691 -16.279 1.00 40.06 ? 36 GLN A C 1 ATOM 276 O O . GLN A 1 36 ? -31.726 36.605 -16.252 1.00 36.83 ? 36 GLN A O 1 ATOM 277 C CB . GLN A 1 36 ? -29.962 35.479 -18.594 1.00 41.75 ? 36 GLN A CB 1 ATOM 278 C CG . GLN A 1 36 ? -28.581 34.897 -18.827 1.00 53.54 ? 36 GLN A CG 1 ATOM 279 C CD . GLN A 1 36 ? -28.616 33.467 -19.330 1.00 52.15 ? 36 GLN A CD 1 ATOM 280 O OE1 . GLN A 1 36 ? -29.589 33.035 -19.949 1.00 52.55 ? 36 GLN A OE1 1 ATOM 281 N NE2 . GLN A 1 36 ? -27.547 32.722 -19.064 1.00 58.19 ? 36 GLN A NE2 1 ATOM 282 N N . LYS A 1 37 ? -30.061 35.444 -15.269 1.00 42.26 ? 37 LYS A N 1 ATOM 283 C CA . LYS A 1 37 ? -29.997 36.303 -14.080 1.00 42.99 ? 37 LYS A CA 1 ATOM 284 C C . LYS A 1 37 ? -28.563 36.508 -13.584 1.00 43.17 ? 37 LYS A C 1 ATOM 285 O O . LYS A 1 37 ? -27.691 35.671 -13.825 1.00 49.13 ? 37 LYS A O 1 ATOM 286 C CB . LYS A 1 37 ? -30.880 35.761 -12.939 1.00 40.51 ? 37 LYS A CB 1 ATOM 287 C CG . LYS A 1 37 ? -30.398 34.457 -12.296 1.00 36.42 ? 37 LYS A CG 1 ATOM 288 C CD . LYS A 1 37 ? -30.876 33.245 -13.083 1.00 47.99 ? 37 LYS A CD 1 ATOM 289 C CE . LYS A 1 37 ? -30.211 31.956 -12.610 1.00 45.92 ? 37 LYS A CE 1 ATOM 290 N NZ . LYS A 1 37 ? -30.552 31.628 -11.207 1.00 50.16 ? 37 LYS A NZ 1 ATOM 291 N N . GLU A 1 38 ? -28.320 37.630 -12.909 1.00 46.11 ? 38 GLU A N 1 ATOM 292 C CA . GLU A 1 38 ? -27.063 37.835 -12.192 1.00 44.64 ? 38 GLU A CA 1 ATOM 293 C C . GLU A 1 38 ? -27.241 37.307 -10.775 1.00 46.01 ? 38 GLU A C 1 ATOM 294 O O . GLU A 1 38 ? -28.028 37.856 -9.999 1.00 46.59 ? 38 GLU A O 1 ATOM 295 C CB . GLU A 1 38 ? -26.689 39.319 -12.152 1.00 48.83 ? 38 GLU A CB 1 ATOM 296 C CG . GLU A 1 38 ? -26.506 39.971 -13.515 1.00 47.14 ? 38 GLU A CG 1 ATOM 297 C CD . GLU A 1 38 ? -26.334 41.482 -13.422 1.00 55.92 ? 38 GLU A CD 1 ATOM 298 O OE1 . GLU A 1 38 ? -26.479 42.043 -12.310 1.00 52.37 ? 38 GLU A OE1 1 ATOM 299 O OE2 . GLU A 1 38 ? -26.057 42.112 -14.467 1.00 60.11 ? 38 GLU A OE2 1 ATOM 300 N N . LYS A 1 39 ? -26.516 36.244 -10.436 1.00 44.10 ? 39 LYS A N 1 ATOM 301 C CA . LYS A 1 39 ? -26.709 35.574 -9.150 1.00 43.83 ? 39 LYS A CA 1 ATOM 302 C C . LYS A 1 39 ? -26.145 36.394 -7.985 1.00 46.87 ? 39 LYS A C 1 ATOM 303 O O . LYS A 1 39 ? -25.091 36.065 -7.429 1.00 45.68 ? 39 LYS A O 1 ATOM 304 C CB . LYS A 1 39 ? -26.095 34.170 -9.179 1.00 41.28 ? 39 LYS A CB 1 ATOM 305 C CG . LYS A 1 39 ? -26.454 33.377 -10.436 1.00 50.17 ? 39 LYS A CG 1 ATOM 306 C CD . LYS A 1 39 ? -26.826 31.933 -10.118 1.00 53.72 ? 39 LYS A CD 1 ATOM 307 C CE . LYS A 1 39 ? -25.673 31.179 -9.483 1.00 64.22 ? 39 LYS A CE 1 ATOM 308 N NZ . LYS A 1 39 ? -26.084 29.836 -8.978 1.00 67.29 ? 39 LYS A NZ 1 ATOM 309 N N . ARG A 1 40 ? -26.869 37.451 -7.616 1.00 43.65 ? 40 ARG A N 1 ATOM 310 C CA . ARG A 1 40 ? -26.452 38.364 -6.554 1.00 41.85 ? 40 ARG A CA 1 ATOM 311 C C . ARG A 1 40 ? -27.579 39.324 -6.181 1.00 41.85 ? 40 ARG A C 1 ATOM 312 O O . ARG A 1 40 ? -28.548 39.480 -6.930 1.00 38.57 ? 40 ARG A O 1 ATOM 313 C CB . ARG A 1 40 ? -25.245 39.179 -7.010 1.00 43.65 ? 40 ARG A CB 1 ATOM 314 C CG . ARG A 1 40 ? -25.544 40.067 -8.202 1.00 46.26 ? 40 ARG A CG 1 ATOM 315 C CD . ARG A 1 40 ? -24.302 40.779 -8.694 1.00 51.78 ? 40 ARG A CD 1 ATOM 316 N NE . ARG A 1 40 ? -24.605 41.724 -9.766 1.00 54.64 ? 40 ARG A NE 1 ATOM 317 C CZ . ARG A 1 40 ? -23.743 42.610 -10.254 1.00 57.72 ? 40 ARG A CZ 1 ATOM 318 N NH1 . ARG A 1 40 ? -22.514 42.683 -9.765 1.00 55.01 ? 40 ARG A NH1 1 ATOM 319 N NH2 . ARG A 1 40 ? -24.117 43.430 -11.228 1.00 54.26 ? 40 ARG A NH2 1 ATOM 320 N N . PHE A 1 41 ? -27.447 39.974 -5.028 1.00 44.57 ? 41 PHE A N 1 ATOM 321 C CA . PHE A 1 41 ? -28.377 41.032 -4.650 1.00 40.70 ? 41 PHE A CA 1 ATOM 322 C C . PHE A 1 41 ? -27.771 42.407 -4.915 1.00 42.75 ? 41 PHE A C 1 ATOM 323 O O . PHE A 1 41 ? -26.586 42.628 -4.662 1.00 47.76 ? 41 PHE A O 1 ATOM 324 C CB . PHE A 1 41 ? -28.786 40.901 -3.185 1.00 35.94 ? 41 PHE A CB 1 ATOM 325 C CG . PHE A 1 41 ? -29.616 39.689 -2.904 1.00 35.35 ? 41 PHE A CG 1 ATOM 326 C CD1 . PHE A 1 41 ? -30.879 39.552 -3.469 1.00 34.59 ? 41 PHE A CD1 1 ATOM 327 C CD2 . PHE A 1 41 ? -29.139 38.681 -2.078 1.00 34.22 ? 41 PHE A CD2 1 ATOM 328 C CE1 . PHE A 1 41 ? -31.655 38.425 -3.216 1.00 33.33 ? 41 PHE A CE1 1 ATOM 329 C CE2 . PHE A 1 41 ? -29.906 37.554 -1.819 1.00 36.66 ? 41 PHE A CE2 1 ATOM 330 C CZ . PHE A 1 41 ? -31.166 37.426 -2.389 1.00 33.30 ? 41 PHE A CZ 1 ATOM 331 N N . CYS A 1 42 ? -28.586 43.322 -5.435 1.00 36.58 ? 42 CYS A N 1 ATOM 332 C CA . CYS A 1 42 ? -28.134 44.668 -5.757 1.00 37.59 ? 42 CYS A CA 1 ATOM 333 C C . CYS A 1 42 ? -29.047 45.692 -5.112 1.00 39.85 ? 42 CYS A C 1 ATOM 334 O O . CYS A 1 42 ? -29.985 45.334 -4.396 1.00 36.14 ? 42 CYS A O 1 ATOM 335 C CB . CYS A 1 42 ? -28.137 44.886 -7.269 1.00 39.57 ? 42 CYS A CB 1 ATOM 336 S SG . CYS A 1 42 ? -27.049 43.789 -8.187 1.00 55.09 ? 42 CYS A SG 1 ATOM 337 N N . LYS A 1 43 ? -28.779 46.966 -5.384 1.00 41.90 ? 43 LYS A N 1 ATOM 338 C CA . LYS A 1 43 ? -29.616 48.054 -4.894 1.00 42.88 ? 43 LYS A CA 1 ATOM 339 C C . LYS A 1 43 ? -30.844 48.274 -5.784 1.00 44.46 ? 43 LYS A C 1 ATOM 340 O O . LYS A 1 43 ? -30.799 48.057 -6.998 1.00 43.95 ? 43 LYS A O 1 ATOM 341 C CB . LYS A 1 43 ? -28.792 49.343 -4.771 1.00 47.30 ? 43 LYS A CB 1 ATOM 342 C CG . LYS A 1 43 ? -27.678 49.250 -3.727 1.00 53.21 ? 43 LYS A CG 1 ATOM 343 C CD . LYS A 1 43 ? -26.883 50.546 -3.594 1.00 55.81 ? 43 LYS A CD 1 ATOM 344 C CE . LYS A 1 43 ? -25.736 50.595 -4.593 1.00 68.89 ? 43 LYS A CE 1 ATOM 345 N NZ . LYS A 1 43 ? -24.901 51.824 -4.436 1.00 82.62 ? 43 LYS A NZ 1 ATOM 346 N N . ILE A 1 44 ? -31.940 48.693 -5.160 1.00 41.09 ? 44 ILE A N 1 ATOM 347 C CA . ILE A 1 44 ? -33.185 48.990 -5.851 1.00 38.91 ? 44 ILE A CA 1 ATOM 348 C C . ILE A 1 44 ? -33.521 50.449 -5.564 1.00 44.10 ? 44 ILE A C 1 ATOM 349 O O . ILE A 1 44 ? -33.609 50.835 -4.396 1.00 42.64 ? 44 ILE A O 1 ATOM 350 C CB . ILE A 1 44 ? -34.328 48.089 -5.329 1.00 39.17 ? 44 ILE A CB 1 ATOM 351 C CG1 . ILE A 1 44 ? -34.079 46.632 -5.722 1.00 38.46 ? 44 ILE A CG1 1 ATOM 352 C CG2 . ILE A 1 44 ? -35.683 48.562 -5.851 1.00 32.45 ? 44 ILE A CG2 1 ATOM 353 C CD1 . ILE A 1 44 ? -34.029 46.413 -7.229 1.00 35.22 ? 44 ILE A CD1 1 ATOM 354 N N . MET A 1 45 ? -33.701 51.252 -6.616 1.00 59.82 ? 45 MET A N 1 ATOM 355 C CA . MET A 1 45 ? -33.891 52.704 -6.477 1.00 62.22 ? 45 MET A CA 1 ATOM 356 C C . MET A 1 45 ? -32.694 53.314 -5.747 1.00 65.23 ? 45 MET A C 1 ATOM 357 O O . MET A 1 45 ? -32.855 54.150 -4.849 1.00 63.63 ? 45 MET A O 1 ATOM 358 C CB . MET A 1 45 ? -35.200 53.029 -5.738 1.00 65.88 ? 45 MET A CB 1 ATOM 359 C CG . MET A 1 45 ? -36.442 52.403 -6.367 1.00 71.32 ? 45 MET A CG 1 ATOM 360 S SD . MET A 1 45 ? -37.069 53.285 -7.819 1.00 94.70 ? 45 MET A SD 1 ATOM 361 C CE . MET A 1 45 ? -38.106 54.519 -7.028 1.00 85.66 ? 45 MET A CE 1 ATOM 362 N N . ASN A 1 46 ? -31.500 52.871 -6.141 1.00 62.84 ? 46 ASN A N 1 ATOM 363 C CA . ASN A 1 46 ? -30.238 53.230 -5.485 1.00 64.52 ? 46 ASN A CA 1 ATOM 364 C C . ASN A 1 46 ? -30.272 53.121 -3.954 1.00 61.34 ? 46 ASN A C 1 ATOM 365 O O . ASN A 1 46 ? -29.560 53.842 -3.252 1.00 60.26 ? 46 ASN A O 1 ATOM 366 C CB . ASN A 1 46 ? -29.747 54.615 -5.940 1.00 69.67 ? 46 ASN A CB 1 ATOM 367 C CG . ASN A 1 46 ? -28.233 54.770 -5.815 1.00 81.49 ? 46 ASN A CG 1 ATOM 368 O OD1 . ASN A 1 46 ? -27.738 55.573 -5.017 1.00 81.45 ? 46 ASN A OD1 1 ATOM 369 N ND2 . ASN A 1 46 ? -27.492 53.989 -6.599 1.00 73.30 ? 46 ASN A ND2 1 ATOM 370 N N . LYS A 1 47 ? -31.096 52.207 -3.448 1.00 59.86 ? 47 LYS A N 1 ATOM 371 C CA . LYS A 1 47 ? -31.206 51.970 -2.013 1.00 52.19 ? 47 LYS A CA 1 ATOM 372 C C . LYS A 1 47 ? -30.760 50.541 -1.690 1.00 49.93 ? 47 LYS A C 1 ATOM 373 O O . LYS A 1 47 ? -31.261 49.574 -2.265 1.00 51.31 ? 47 LYS A O 1 ATOM 374 C CB . LYS A 1 47 ? -32.641 52.219 -1.533 1.00 54.41 ? 47 LYS A CB 1 ATOM 375 C CG . LYS A 1 47 ? -32.831 52.123 -0.018 1.00 57.36 ? 47 LYS A CG 1 ATOM 376 C CD . LYS A 1 47 ? -34.167 52.737 0.426 1.00 56.05 ? 47 LYS A CD 1 ATOM 377 C CE . LYS A 1 47 ? -34.260 52.770 1.953 1.00 61.28 ? 47 LYS A CE 1 ATOM 378 N NZ . LYS A 1 47 ? -35.494 53.438 2.478 1.00 61.99 ? 47 LYS A NZ 1 ATOM 379 N N . ALA A 1 48 ? -29.804 50.416 -0.777 1.00 45.51 ? 48 ALA A N 1 ATOM 380 C CA . ALA A 1 48 ? -29.233 49.120 -0.418 1.00 43.97 ? 48 ALA A CA 1 ATOM 381 C C . ALA A 1 48 ? -30.202 48.270 0.392 1.00 38.53 ? 48 ALA A C 1 ATOM 382 O O . ALA A 1 48 ? -31.003 48.801 1.167 1.00 39.28 ? 48 ALA A O 1 ATOM 383 C CB . ALA A 1 48 ? -27.944 49.315 0.366 1.00 44.51 ? 48 ALA A CB 1 ATOM 384 N N . PRO A 1 49 ? -30.124 46.941 0.224 1.00 32.89 ? 49 PRO A N 1 ATOM 385 C CA . PRO A 1 49 ? -30.921 46.051 1.074 1.00 33.71 ? 49 PRO A CA 1 ATOM 386 C C . PRO A 1 49 ? -30.297 45.892 2.462 1.00 38.38 ? 49 PRO A C 1 ATOM 387 O O . PRO A 1 49 ? -29.134 46.256 2.656 1.00 35.73 ? 49 PRO A O 1 ATOM 388 C CB . PRO A 1 49 ? -30.864 44.717 0.328 1.00 27.92 ? 49 PRO A CB 1 ATOM 389 C CG . PRO A 1 49 ? -29.572 44.764 -0.427 1.00 28.42 ? 49 PRO A CG 1 ATOM 390 C CD . PRO A 1 49 ? -29.393 46.206 -0.827 1.00 28.61 ? 49 PRO A CD 1 ATOM 391 N N . LEU A 1 50 ? -31.059 45.349 3.407 1.00 35.61 ? 50 LEU A N 1 ATOM 392 C CA . LEU A 1 50 ? -30.548 45.077 4.742 1.00 32.29 ? 50 LEU A CA 1 ATOM 393 C C . LEU A 1 50 ? -30.153 43.608 4.888 1.00 36.61 ? 50 LEU A C 1 ATOM 394 O O . LEU A 1 50 ? -31.021 42.734 4.872 1.00 39.55 ? 50 LEU A O 1 ATOM 395 C CB . LEU A 1 50 ? -31.608 45.430 5.794 1.00 37.01 ? 50 LEU A CB 1 ATOM 396 C CG . LEU A 1 50 ? -31.253 45.153 7.257 1.00 38.36 ? 50 LEU A CG 1 ATOM 397 C CD1 . LEU A 1 50 ? -30.036 45.968 7.639 1.00 34.76 ? 50 LEU A CD1 1 ATOM 398 C CD2 . LEU A 1 50 ? -32.414 45.453 8.201 1.00 33.23 ? 50 LEU A CD2 1 ATOM 399 N N . ASP A 1 51 ? -28.856 43.334 5.037 1.00 42.94 ? 51 ASP A N 1 ATOM 400 C CA . ASP A 1 51 ? -28.382 41.970 5.284 1.00 38.46 ? 51 ASP A CA 1 ATOM 401 C C . ASP A 1 51 ? -28.443 41.657 6.776 1.00 41.82 ? 51 ASP A C 1 ATOM 402 O O . ASP A 1 51 ? -27.846 42.367 7.589 1.00 46.40 ? 51 ASP A O 1 ATOM 403 C CB . ASP A 1 51 ? -26.943 41.797 4.796 1.00 39.82 ? 51 ASP A CB 1 ATOM 404 C CG . ASP A 1 51 ? -26.510 40.331 4.732 1.00 44.98 ? 51 ASP A CG 1 ATOM 405 O OD1 . ASP A 1 51 ? -27.302 39.433 5.107 1.00 44.08 ? 51 ASP A OD1 1 ATOM 406 O OD2 . ASP A 1 51 ? -25.364 40.073 4.305 1.00 46.72 ? 51 ASP A OD2 1 ATOM 407 N N . LEU A 1 52 ? -29.161 40.598 7.137 1.00 40.96 ? 52 LEU A N 1 ATOM 408 C CA . LEU A 1 52 ? -29.286 40.214 8.538 1.00 43.63 ? 52 LEU A CA 1 ATOM 409 C C . LEU A 1 52 ? -28.013 39.484 8.980 1.00 43.93 ? 52 LEU A C 1 ATOM 410 O O . LEU A 1 52 ? -27.659 39.507 10.167 1.00 40.07 ? 52 LEU A O 1 ATOM 411 C CB . LEU A 1 52 ? -30.640 39.549 8.803 1.00 41.54 ? 52 LEU A CB 1 ATOM 412 C CG . LEU A 1 52 ? -31.874 40.439 8.687 1.00 37.86 ? 52 LEU A CG 1 ATOM 413 C CD1 . LEU A 1 52 ? -33.128 39.687 9.116 1.00 35.64 ? 52 LEU A CD1 1 ATOM 414 C CD2 . LEU A 1 52 ? -31.697 41.689 9.527 1.00 37.74 ? 52 LEU A CD2 1 ATOM 415 N N . LYS A 1 53 ? -27.334 38.847 8.023 1.00 39.09 ? 53 LYS A N 1 ATOM 416 C CA . LYS A 1 53 ? -26.182 37.985 8.307 1.00 46.01 ? 53 LYS A CA 1 ATOM 417 C C . LYS A 1 53 ? -26.606 36.864 9.261 1.00 48.02 ? 53 LYS A C 1 ATOM 418 O O . LYS A 1 53 ? -27.529 36.104 8.966 1.00 44.92 ? 53 LYS A O 1 ATOM 419 C CB . LYS A 1 53 ? -25.033 38.802 8.907 1.00 45.76 ? 53 LYS A CB 1 ATOM 420 C CG . LYS A 1 53 ? -24.155 39.483 7.869 1.00 50.27 ? 53 LYS A CG 1 ATOM 421 C CD . LYS A 1 53 ? -23.828 40.913 8.275 1.00 53.47 ? 53 LYS A CD 1 ATOM 422 C CE . LYS A 1 53 ? -22.991 41.608 7.203 1.00 63.20 ? 53 LYS A CE 1 ATOM 423 N NZ . LYS A 1 53 ? -22.813 43.072 7.469 1.00 64.15 ? 53 LYS A NZ 1 ATOM 424 N N . ASP A 1 54 ? -25.936 36.767 10.406 1.00 44.43 ? 54 ASP A N 1 ATOM 425 C CA . ASP A 1 54 ? -26.106 35.621 11.292 1.00 46.70 ? 54 ASP A CA 1 ATOM 426 C C . ASP A 1 54 ? -27.239 35.831 12.297 1.00 44.80 ? 54 ASP A C 1 ATOM 427 O O . ASP A 1 54 ? -27.396 35.058 13.245 1.00 46.68 ? 54 ASP A O 1 ATOM 428 C CB . ASP A 1 54 ? -24.795 35.293 12.008 1.00 46.89 ? 54 ASP A CB 1 ATOM 429 C CG . ASP A 1 54 ? -24.763 33.873 12.544 1.00 63.95 ? 54 ASP A CG 1 ATOM 430 O OD1 . ASP A 1 54 ? -25.424 32.988 11.947 1.00 59.12 ? 54 ASP A OD1 1 ATOM 431 O OD2 . ASP A 1 54 ? -24.078 33.645 13.567 1.00 72.45 ? 54 ASP A OD2 1 ATOM 432 N N . CYS A 1 55 ? -28.038 36.871 12.076 1.00 45.37 ? 55 CYS A N 1 ATOM 433 C CA . CYS A 1 55 ? -29.226 37.107 12.896 1.00 45.24 ? 55 CYS A CA 1 ATOM 434 C C . CYS A 1 55 ? -30.502 36.794 12.112 1.00 43.45 ? 55 CYS A C 1 ATOM 435 O O . CYS A 1 55 ? -30.564 37.000 10.898 1.00 42.51 ? 55 CYS A O 1 ATOM 436 C CB . CYS A 1 55 ? -29.265 38.556 13.389 1.00 43.00 ? 55 CYS A CB 1 ATOM 437 S SG . CYS A 1 55 ? -28.022 38.967 14.646 1.00 66.34 ? 55 CYS A SG 1 ATOM 438 N N . THR A 1 56 ? -31.511 36.275 12.805 1.00 40.83 ? 56 THR A N 1 ATOM 439 C CA . THR A 1 56 ? -32.835 36.102 12.216 1.00 38.93 ? 56 THR A CA 1 ATOM 440 C C . THR A 1 56 ? -33.610 37.392 12.434 1.00 42.12 ? 56 THR A C 1 ATOM 441 O O . THR A 1 56 ? -33.137 38.280 13.148 1.00 44.21 ? 56 THR A O 1 ATOM 442 C CB . THR A 1 56 ? -33.607 34.936 12.858 1.00 42.38 ? 56 THR A CB 1 ATOM 443 O OG1 . THR A 1 56 ? -33.989 35.287 14.194 1.00 41.08 ? 56 THR A OG1 1 ATOM 444 C CG2 . THR A 1 56 ? -32.750 33.682 12.888 1.00 41.66 ? 56 THR A CG2 1 ATOM 445 N N . ILE A 1 57 ? -34.789 37.498 11.827 1.00 42.58 ? 57 ILE A N 1 ATOM 446 C CA . ILE A 1 57 ? -35.629 38.678 12.006 1.00 42.02 ? 57 ILE A CA 1 ATOM 447 C C . ILE A 1 57 ? -35.941 38.912 13.489 1.00 40.99 ? 57 ILE A C 1 ATOM 448 O O . ILE A 1 57 ? -35.846 40.041 13.983 1.00 39.65 ? 57 ILE A O 1 ATOM 449 C CB . ILE A 1 57 ? -36.932 38.584 11.173 1.00 41.32 ? 57 ILE A CB 1 ATOM 450 C CG1 . ILE A 1 57 ? -36.604 38.686 9.683 1.00 43.08 ? 57 ILE A CG1 1 ATOM 451 C CG2 . ILE A 1 57 ? -37.904 39.684 11.558 1.00 35.98 ? 57 ILE A CG2 1 ATOM 452 C CD1 . ILE A 1 57 ? -37.813 38.610 8.773 1.00 47.39 ? 57 ILE A CD1 1 ATOM 453 N N . GLU A 1 58 ? -36.277 37.840 14.200 1.00 39.69 ? 58 GLU A N 1 ATOM 454 C CA . GLU A 1 58 ? -36.602 37.938 15.618 1.00 43.57 ? 58 GLU A CA 1 ATOM 455 C C . GLU A 1 58 ? -35.416 38.431 16.449 1.00 42.18 ? 58 GLU A C 1 ATOM 456 O O . GLU A 1 58 ? -35.576 39.298 17.305 1.00 41.20 ? 58 GLU A O 1 ATOM 457 C CB . GLU A 1 58 ? -37.095 36.591 16.154 1.00 44.00 ? 58 GLU A CB 1 ATOM 458 C CG . GLU A 1 58 ? -38.274 36.016 15.393 1.00 45.43 ? 58 GLU A CG 1 ATOM 459 C CD . GLU A 1 58 ? -37.866 34.950 14.391 1.00 52.15 ? 58 GLU A CD 1 ATOM 460 O OE1 . GLU A 1 58 ? -37.334 35.303 13.311 1.00 46.22 ? 58 GLU A OE1 1 ATOM 461 O OE2 . GLU A 1 58 ? -38.074 33.754 14.692 1.00 51.55 ? 58 GLU A OE2 1 ATOM 462 N N . GLY A 1 59 ? -34.231 37.878 16.196 1.00 40.77 ? 59 GLY A N 1 ATOM 463 C CA . GLY A 1 59 ? -33.034 38.280 16.915 1.00 41.72 ? 59 GLY A CA 1 ATOM 464 C C . GLY A 1 59 ? -32.662 39.734 16.672 1.00 42.41 ? 59 GLY A C 1 ATOM 465 O O . GLY A 1 59 ? -32.216 40.437 17.584 1.00 39.93 ? 59 GLY A O 1 ATOM 466 N N . TRP A 1 60 ? -32.837 40.183 15.433 1.00 37.92 ? 60 TRP A N 1 ATOM 467 C CA . TRP A 1 60 ? -32.570 41.569 15.074 1.00 34.84 ? 60 TRP A CA 1 ATOM 468 C C . TRP A 1 60 ? -33.514 42.522 15.797 1.00 37.49 ? 60 TRP A C 1 ATOM 469 O O . TRP A 1 60 ? -33.073 43.492 16.417 1.00 40.91 ? 60 TRP A O 1 ATOM 470 C CB . TRP A 1 60 ? -32.667 41.751 13.552 1.00 32.91 ? 60 TRP A CB 1 ATOM 471 C CG . TRP A 1 60 ? -32.923 43.169 13.104 1.00 35.79 ? 60 TRP A CG 1 ATOM 472 C CD1 . TRP A 1 60 ? -32.269 44.301 13.517 1.00 43.12 ? 60 TRP A CD1 1 ATOM 473 C CD2 . TRP A 1 60 ? -33.891 43.599 12.133 1.00 37.39 ? 60 TRP A CD2 1 ATOM 474 N NE1 . TRP A 1 60 ? -32.787 45.405 12.875 1.00 39.50 ? 60 TRP A NE1 1 ATOM 475 C CE2 . TRP A 1 60 ? -33.777 45.002 12.022 1.00 37.16 ? 60 TRP A CE2 1 ATOM 476 C CE3 . TRP A 1 60 ? -34.840 42.933 11.353 1.00 37.64 ? 60 TRP A CE3 1 ATOM 477 C CZ2 . TRP A 1 60 ? -34.587 45.749 11.156 1.00 33.35 ? 60 TRP A CZ2 1 ATOM 478 C CZ3 . TRP A 1 60 ? -35.640 43.673 10.497 1.00 33.56 ? 60 TRP A CZ3 1 ATOM 479 C CH2 . TRP A 1 60 ? -35.508 45.069 10.405 1.00 32.68 ? 60 TRP A CH2 1 ATOM 480 N N . ILE A 1 61 ? -34.810 42.244 15.723 1.00 36.51 ? 61 ILE A N 1 ATOM 481 C CA . ILE A 1 61 ? -35.805 43.201 16.182 1.00 35.04 ? 61 ILE A CA 1 ATOM 482 C C . ILE A 1 61 ? -36.028 43.136 17.698 1.00 36.59 ? 61 ILE A C 1 ATOM 483 O O . ILE A 1 61 ? -36.514 44.095 18.299 1.00 40.59 ? 61 ILE A O 1 ATOM 484 C CB . ILE A 1 61 ? -37.133 43.046 15.393 1.00 35.21 ? 61 ILE A CB 1 ATOM 485 C CG1 . ILE A 1 61 ? -37.834 44.393 15.243 1.00 36.19 ? 61 ILE A CG1 1 ATOM 486 C CG2 . ILE A 1 61 ? -38.039 42.014 16.037 1.00 34.45 ? 61 ILE A CG2 1 ATOM 487 C CD1 . ILE A 1 61 ? -37.129 45.329 14.297 1.00 40.58 ? 61 ILE A CD1 1 ATOM 488 N N . LEU A 1 62 ? -35.663 42.017 18.319 1.00 37.89 ? 62 LEU A N 1 ATOM 489 C CA . LEU A 1 62 ? -35.762 41.906 19.775 1.00 40.71 ? 62 LEU A CA 1 ATOM 490 C C . LEU A 1 62 ? -34.546 42.533 20.440 1.00 41.82 ? 62 LEU A C 1 ATOM 491 O O . LEU A 1 62 ? -34.616 42.984 21.585 1.00 42.98 ? 62 LEU A O 1 ATOM 492 C CB . LEU A 1 62 ? -35.896 40.449 20.224 1.00 38.98 ? 62 LEU A CB 1 ATOM 493 C CG . LEU A 1 62 ? -37.264 39.801 20.013 1.00 42.66 ? 62 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 62 ? -37.280 38.362 20.508 1.00 41.14 ? 62 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 62 ? -38.343 40.613 20.705 1.00 38.32 ? 62 LEU A CD2 1 ATOM 496 N N . GLY A 1 63 ? -33.431 42.560 19.716 1.00 39.63 ? 63 GLY A N 1 ATOM 497 C CA . GLY A 1 63 ? -32.189 43.068 20.268 1.00 43.01 ? 63 GLY A CA 1 ATOM 498 C C . GLY A 1 63 ? -31.350 41.988 20.929 1.00 44.20 ? 63 GLY A C 1 ATOM 499 O O . GLY A 1 63 ? -30.757 42.211 21.987 1.00 47.42 ? 63 GLY A O 1 ATOM 500 N N . ASN A 1 64 ? -31.319 40.811 20.311 1.00 38.30 ? 64 ASN A N 1 ATOM 501 C CA . ASN A 1 64 ? -30.412 39.740 20.710 1.00 40.38 ? 64 ASN A CA 1 ATOM 502 C C . ASN A 1 64 ? -28.997 40.306 20.781 1.00 42.40 ? 64 ASN A C 1 ATOM 503 O O . ASN A 1 64 ? -28.517 40.898 19.809 1.00 41.25 ? 64 ASN A O 1 ATOM 504 C CB . ASN A 1 64 ? -30.490 38.601 19.686 1.00 36.21 ? 64 ASN A CB 1 ATOM 505 C CG . ASN A 1 64 ? -29.621 37.400 20.047 1.00 40.52 ? 64 ASN A CG 1 ATOM 506 O OD1 . ASN A 1 64 ? -28.456 37.534 20.433 1.00 45.97 ? 64 ASN A OD1 1 ATOM 507 N ND2 . ASN A 1 64 ? -30.187 36.207 19.889 1.00 39.21 ? 64 ASN A ND2 1 ATOM 508 N N . PRO A 1 65 ? -28.328 40.130 21.934 1.00 46.21 ? 65 PRO A N 1 ATOM 509 C CA . PRO A 1 65 ? -27.024 40.747 22.215 1.00 48.13 ? 65 PRO A CA 1 ATOM 510 C C . PRO A 1 65 ? -25.951 40.413 21.174 1.00 48.27 ? 65 PRO A C 1 ATOM 511 O O . PRO A 1 65 ? -24.925 41.092 21.137 1.00 51.90 ? 65 PRO A O 1 ATOM 512 C CB . PRO A 1 65 ? -26.639 40.154 23.576 1.00 51.00 ? 65 PRO A CB 1 ATOM 513 C CG . PRO A 1 65 ? -27.926 39.719 24.188 1.00 50.14 ? 65 PRO A CG 1 ATOM 514 C CD . PRO A 1 65 ? -28.795 39.288 23.050 1.00 46.16 ? 65 PRO A CD 1 ATOM 515 N N . LYS A 1 66 ? -26.183 39.392 20.351 1.00 49.05 ? 66 LYS A N 1 ATOM 516 C CA . LYS A 1 66 ? -25.253 39.038 19.281 1.00 50.92 ? 66 LYS A CA 1 ATOM 517 C C . LYS A 1 66 ? -25.640 39.651 17.932 1.00 49.26 ? 66 LYS A C 1 ATOM 518 O O . LYS A 1 66 ? -25.011 39.374 16.906 1.00 49.20 ? 66 LYS A O 1 ATOM 519 C CB . LYS A 1 66 ? -25.118 37.517 19.168 1.00 51.21 ? 66 LYS A CB 1 ATOM 520 C CG . LYS A 1 66 ? -24.304 36.888 20.296 1.00 57.23 ? 66 LYS A CG 1 ATOM 521 C CD . LYS A 1 66 ? -24.098 35.394 20.072 1.00 62.15 ? 66 LYS A CD 1 ATOM 522 C CE . LYS A 1 66 ? -23.193 34.794 21.145 1.00 63.21 ? 66 LYS A CE 1 ATOM 523 N NZ . LYS A 1 66 ? -23.085 33.308 21.035 1.00 66.80 ? 66 LYS A NZ 1 ATOM 524 N N . CYS A 1 67 ? -26.672 40.488 17.941 1.00 46.06 ? 67 CYS A N 1 ATOM 525 C CA . CYS A 1 67 ? -27.101 41.183 16.734 1.00 47.55 ? 67 CYS A CA 1 ATOM 526 C C . CYS A 1 67 ? -26.810 42.680 16.850 1.00 50.30 ? 67 CYS A C 1 ATOM 527 O O . CYS A 1 67 ? -27.473 43.505 16.214 1.00 50.20 ? 67 CYS A O 1 ATOM 528 C CB . CYS A 1 67 ? -28.592 40.939 16.482 1.00 42.87 ? 67 CYS A CB 1 ATOM 529 S SG . CYS A 1 67 ? -29.024 39.188 16.407 1.00 51.38 ? 67 CYS A SG 1 ATOM 530 N N . ASP A 1 68 ? -25.810 43.021 17.659 1.00 48.87 ? 68 ASP A N 1 ATOM 531 C CA . ASP A 1 68 ? -25.463 44.415 17.919 1.00 47.24 ? 68 ASP A CA 1 ATOM 532 C C . ASP A 1 68 ? -24.978 45.169 16.676 1.00 45.78 ? 68 ASP A C 1 ATOM 533 O O . ASP A 1 68 ? -25.122 46.388 16.595 1.00 46.12 ? 68 ASP A O 1 ATOM 534 C CB . ASP A 1 68 ? -24.425 44.516 19.049 1.00 52.93 ? 68 ASP A CB 1 ATOM 535 C CG . ASP A 1 68 ? -25.050 44.437 20.441 1.00 59.35 ? 68 ASP A CG 1 ATOM 536 O OD1 . ASP A 1 68 ? -26.282 44.617 20.566 1.00 58.12 ? 68 ASP A OD1 1 ATOM 537 O OD2 . ASP A 1 68 ? -24.298 44.209 21.416 1.00 60.86 ? 68 ASP A OD2 1 ATOM 538 N N . LEU A 1 69 ? -24.408 44.453 15.712 1.00 36.83 ? 69 LEU A N 1 ATOM 539 C CA . LEU A 1 69 ? -24.029 45.070 14.439 1.00 38.44 ? 69 LEU A CA 1 ATOM 540 C C . LEU A 1 69 ? -25.229 45.725 13.749 1.00 38.59 ? 69 LEU A C 1 ATOM 541 O O . LEU A 1 69 ? -25.091 46.755 13.087 1.00 40.51 ? 69 LEU A O 1 ATOM 542 C CB . LEU A 1 69 ? -23.384 44.045 13.499 1.00 42.43 ? 69 LEU A CB 1 ATOM 543 C CG . LEU A 1 69 ? -23.063 44.527 12.074 1.00 52.15 ? 69 LEU A CG 1 ATOM 544 C CD1 . LEU A 1 69 ? -22.122 45.733 12.082 1.00 43.48 ? 69 LEU A CD1 1 ATOM 545 C CD2 . LEU A 1 69 ? -22.480 43.399 11.231 1.00 49.41 ? 69 LEU A CD2 1 ATOM 546 N N . LEU A 1 70 ? -26.408 45.133 13.923 1.00 47.24 ? 70 LEU A N 1 ATOM 547 C CA . LEU A 1 70 ? -27.629 45.639 13.298 1.00 49.72 ? 70 LEU A CA 1 ATOM 548 C C . LEU A 1 70 ? -28.321 46.694 14.160 1.00 46.30 ? 70 LEU A C 1 ATOM 549 O O . LEU A 1 70 ? -29.121 47.491 13.659 1.00 46.19 ? 70 LEU A O 1 ATOM 550 C CB . LEU A 1 70 ? -28.599 44.486 13.013 1.00 49.43 ? 70 LEU A CB 1 ATOM 551 C CG . LEU A 1 70 ? -28.079 43.399 12.070 1.00 52.61 ? 70 LEU A CG 1 ATOM 552 C CD1 . LEU A 1 70 ? -29.032 42.213 12.010 1.00 51.16 ? 70 LEU A CD1 1 ATOM 553 C CD2 . LEU A 1 70 ? -27.851 43.971 10.682 1.00 44.73 ? 70 LEU A CD2 1 ATOM 554 N N . LEU A 1 71 ? -27.994 46.698 15.451 1.00 40.60 ? 71 LEU A N 1 ATOM 555 C CA . LEU A 1 71 ? -28.688 47.518 16.450 1.00 40.28 ? 71 LEU A CA 1 ATOM 556 C C . LEU A 1 71 ? -28.785 49.009 16.111 1.00 38.38 ? 71 LEU A C 1 ATOM 557 O O . LEU A 1 71 ? -27.774 49.663 15.825 1.00 40.31 ? 71 LEU A O 1 ATOM 558 C CB . LEU A 1 71 ? -28.022 47.358 17.817 1.00 44.49 ? 71 LEU A CB 1 ATOM 559 C CG . LEU A 1 71 ? -28.842 47.917 18.979 1.00 42.41 ? 71 LEU A CG 1 ATOM 560 C CD1 . LEU A 1 71 ? -29.982 46.970 19.293 1.00 38.73 ? 71 LEU A CD1 1 ATOM 561 C CD2 . LEU A 1 71 ? -27.976 48.149 20.205 1.00 40.35 ? 71 LEU A CD2 1 ATOM 562 N N . GLY A 1 72 ? -30.003 49.545 16.156 1.00 34.20 ? 72 GLY A N 1 ATOM 563 C CA . GLY A 1 72 ? -30.218 50.963 15.916 1.00 36.73 ? 72 GLY A CA 1 ATOM 564 C C . GLY A 1 72 ? -31.113 51.259 14.726 1.00 38.57 ? 72 GLY A C 1 ATOM 565 O O . GLY A 1 72 ? -32.092 50.549 14.474 1.00 39.04 ? 72 GLY A O 1 ATOM 566 N N . ASP A 1 73 ? -30.786 52.319 13.995 1.00 48.39 ? 73 ASP A N 1 ATOM 567 C CA . ASP A 1 73 ? -31.577 52.709 12.836 1.00 46.66 ? 73 ASP A CA 1 ATOM 568 C C . ASP A 1 73 ? -31.197 51.892 11.605 1.00 48.18 ? 73 ASP A C 1 ATOM 569 O O . ASP A 1 73 ? -30.015 51.600 11.380 1.00 46.76 ? 73 ASP A O 1 ATOM 570 C CB . ASP A 1 73 ? -31.393 54.200 12.543 1.00 44.67 ? 73 ASP A CB 1 ATOM 571 C CG . ASP A 1 73 ? -31.680 55.069 13.752 1.00 51.33 ? 73 ASP A CG 1 ATOM 572 O OD1 . ASP A 1 73 ? -32.376 54.589 14.673 1.00 51.97 ? 73 ASP A OD1 1 ATOM 573 O OD2 . ASP A 1 73 ? -31.210 56.230 13.785 1.00 52.70 ? 73 ASP A OD2 1 ATOM 574 N N . GLN A 1 74 ? -32.202 51.522 10.815 1.00 38.48 ? 74 GLN A N 1 ATOM 575 C CA . GLN A 1 74 ? -31.968 50.853 9.539 1.00 35.61 ? 74 GLN A CA 1 ATOM 576 C C . GLN A 1 74 ? -32.916 51.363 8.462 1.00 35.39 ? 74 GLN A C 1 ATOM 577 O O . GLN A 1 74 ? -34.094 51.601 8.734 1.00 34.96 ? 74 GLN A O 1 ATOM 578 C CB . GLN A 1 74 ? -32.111 49.331 9.683 1.00 32.96 ? 74 GLN A CB 1 ATOM 579 C CG . GLN A 1 74 ? -31.047 48.658 10.558 1.00 34.35 ? 74 GLN A CG 1 ATOM 580 C CD . GLN A 1 74 ? -29.656 48.653 9.923 1.00 36.97 ? 74 GLN A CD 1 ATOM 581 O OE1 . GLN A 1 74 ? -29.470 49.088 8.780 1.00 41.06 ? 74 GLN A OE1 1 ATOM 582 N NE2 . GLN A 1 74 ? -28.674 48.148 10.665 1.00 39.92 ? 74 GLN A NE2 1 ATOM 583 N N . SER A 1 75 ? -32.383 51.552 7.256 1.00 37.39 ? 75 SER A N 1 ATOM 584 C CA . SER A 1 75 ? -33.188 51.781 6.061 1.00 37.66 ? 75 SER A CA 1 ATOM 585 C C . SER A 1 75 ? -32.892 50.646 5.091 1.00 39.26 ? 75 SER A C 1 ATOM 586 O O . SER A 1 75 ? -31.773 50.125 5.070 1.00 42.93 ? 75 SER A O 1 ATOM 587 C CB . SER A 1 75 ? -32.835 53.113 5.402 1.00 37.80 ? 75 SER A CB 1 ATOM 588 O OG . SER A 1 75 ? -33.452 54.197 6.062 1.00 45.29 ? 75 SER A OG 1 ATOM 589 N N . TRP A 1 76 ? -33.878 50.259 4.286 1.00 40.44 ? 76 TRP A N 1 ATOM 590 C CA . TRP A 1 76 ? -33.679 49.157 3.347 1.00 34.58 ? 76 TRP A CA 1 ATOM 591 C C . TRP A 1 76 ? -34.653 49.174 2.178 1.00 37.32 ? 76 TRP A C 1 ATOM 592 O O . TRP A 1 76 ? -35.799 49.599 2.317 1.00 39.54 ? 76 TRP A O 1 ATOM 593 C CB . TRP A 1 76 ? -33.759 47.807 4.073 1.00 34.30 ? 76 TRP A CB 1 ATOM 594 C CG . TRP A 1 76 ? -35.121 47.484 4.614 1.00 36.45 ? 76 TRP A CG 1 ATOM 595 C CD1 . TRP A 1 76 ? -36.120 46.806 3.976 1.00 34.97 ? 76 TRP A CD1 1 ATOM 596 C CD2 . TRP A 1 76 ? -35.627 47.818 5.913 1.00 36.55 ? 76 TRP A CD2 1 ATOM 597 N NE1 . TRP A 1 76 ? -37.215 46.700 4.798 1.00 33.30 ? 76 TRP A NE1 1 ATOM 598 C CE2 . TRP A 1 76 ? -36.941 47.316 5.990 1.00 32.80 ? 76 TRP A CE2 1 ATOM 599 C CE3 . TRP A 1 76 ? -35.096 48.496 7.013 1.00 31.90 ? 76 TRP A CE3 1 ATOM 600 C CZ2 . TRP A 1 76 ? -37.735 47.471 7.131 1.00 31.43 ? 76 TRP A CZ2 1 ATOM 601 C CZ3 . TRP A 1 76 ? -35.880 48.651 8.139 1.00 36.38 ? 76 TRP A CZ3 1 ATOM 602 C CH2 . TRP A 1 76 ? -37.189 48.137 8.192 1.00 34.95 ? 76 TRP A CH2 1 ATOM 603 N N . SER A 1 77 ? -34.181 48.705 1.027 1.00 42.90 ? 77 SER A N 1 ATOM 604 C CA . SER A 1 77 ? -35.029 48.514 -0.143 1.00 39.65 ? 77 SER A CA 1 ATOM 605 C C . SER A 1 77 ? -35.678 47.128 -0.087 1.00 38.68 ? 77 SER A C 1 ATOM 606 O O . SER A 1 77 ? -36.726 46.896 -0.698 1.00 40.13 ? 77 SER A O 1 ATOM 607 C CB . SER A 1 77 ? -34.206 48.655 -1.418 1.00 40.02 ? 77 SER A CB 1 ATOM 608 O OG . SER A 1 77 ? -33.057 47.830 -1.371 1.00 37.33 ? 77 SER A OG 1 ATOM 609 N N . TYR A 1 78 ? -35.031 46.217 0.644 1.00 34.73 ? 78 TYR A N 1 ATOM 610 C CA . TYR A 1 78 ? -35.569 44.890 0.970 1.00 35.50 ? 78 TYR A CA 1 ATOM 611 C C . TYR A 1 78 ? -34.676 44.196 1.995 1.00 36.92 ? 78 TYR A C 1 ATOM 612 O O . TYR A 1 78 ? -33.580 44.676 2.299 1.00 37.29 ? 78 TYR A O 1 ATOM 613 C CB . TYR A 1 78 ? -35.735 44.008 -0.275 1.00 32.97 ? 78 TYR A CB 1 ATOM 614 C CG . TYR A 1 78 ? -34.472 43.774 -1.073 1.00 32.01 ? 78 TYR A CG 1 ATOM 615 C CD1 . TYR A 1 78 ? -34.064 44.682 -2.034 1.00 30.33 ? 78 TYR A CD1 1 ATOM 616 C CD2 . TYR A 1 78 ? -33.707 42.634 -0.884 1.00 28.97 ? 78 TYR A CD2 1 ATOM 617 C CE1 . TYR A 1 78 ? -32.926 44.472 -2.772 1.00 33.09 ? 78 TYR A CE1 1 ATOM 618 C CE2 . TYR A 1 78 ? -32.564 42.413 -1.620 1.00 29.89 ? 78 TYR A CE2 1 ATOM 619 C CZ . TYR A 1 78 ? -32.179 43.339 -2.563 1.00 32.94 ? 78 TYR A CZ 1 ATOM 620 O OH . TYR A 1 78 ? -31.044 43.140 -3.314 1.00 35.67 ? 78 TYR A OH 1 ATOM 621 N N . ILE A 1 79 ? -35.138 43.064 2.518 1.00 32.78 ? 79 ILE A N 1 ATOM 622 C CA . ILE A 1 79 ? -34.411 42.358 3.569 1.00 32.44 ? 79 ILE A CA 1 ATOM 623 C C . ILE A 1 79 ? -33.872 41.002 3.103 1.00 34.30 ? 79 ILE A C 1 ATOM 624 O O . ILE A 1 79 ? -34.612 40.181 2.557 1.00 39.70 ? 79 ILE A O 1 ATOM 625 C CB . ILE A 1 79 ? -35.305 42.162 4.809 1.00 34.32 ? 79 ILE A CB 1 ATOM 626 C CG1 . ILE A 1 79 ? -35.656 43.523 5.414 1.00 32.40 ? 79 ILE A CG1 1 ATOM 627 C CG2 . ILE A 1 79 ? -34.625 41.272 5.846 1.00 32.29 ? 79 ILE A CG2 1 ATOM 628 C CD1 . ILE A 1 79 ? -36.669 43.452 6.547 1.00 34.07 ? 79 ILE A CD1 1 ATOM 629 N N . VAL A 1 80 ? -32.578 40.775 3.309 1.00 30.17 ? 80 VAL A N 1 ATOM 630 C CA . VAL A 1 80 ? -31.985 39.473 3.033 1.00 31.40 ? 80 VAL A CA 1 ATOM 631 C C . VAL A 1 80 ? -31.740 38.745 4.344 1.00 33.74 ? 80 VAL A C 1 ATOM 632 O O . VAL A 1 80 ? -30.942 39.195 5.168 1.00 38.09 ? 80 VAL A O 1 ATOM 633 C CB . VAL A 1 80 ? -30.664 39.601 2.259 1.00 36.34 ? 80 VAL A CB 1 ATOM 634 C CG1 . VAL A 1 80 ? -30.026 38.231 2.058 1.00 33.97 ? 80 VAL A CG1 1 ATOM 635 C CG2 . VAL A 1 80 ? -30.904 40.269 0.917 1.00 31.21 ? 80 VAL A CG2 1 ATOM 636 N N . GLU A 1 81 ? -32.445 37.635 4.548 1.00 39.58 ? 81 GLU A N 1 ATOM 637 C CA . GLU A 1 81 ? -32.244 36.808 5.733 1.00 40.52 ? 81 GLU A CA 1 ATOM 638 C C . GLU A 1 81 ? -31.479 35.552 5.326 1.00 43.60 ? 81 GLU A C 1 ATOM 639 O O . GLU A 1 81 ? -31.794 34.932 4.304 1.00 46.12 ? 81 GLU A O 1 ATOM 640 C CB . GLU A 1 81 ? -33.583 36.423 6.368 1.00 42.84 ? 81 GLU A CB 1 ATOM 641 C CG . GLU A 1 81 ? -33.441 35.745 7.733 1.00 54.27 ? 81 GLU A CG 1 ATOM 642 C CD . GLU A 1 81 ? -34.771 35.269 8.310 1.00 64.20 ? 81 GLU A CD 1 ATOM 643 O OE1 . GLU A 1 81 ? -34.773 34.806 9.471 1.00 61.67 ? 81 GLU A OE1 1 ATOM 644 O OE2 . GLU A 1 81 ? -35.808 35.349 7.609 1.00 65.51 ? 81 GLU A OE2 1 ATOM 645 N N . ARG A 1 82 ? -30.470 35.180 6.111 1.00 36.92 ? 82 ARG A N 1 ATOM 646 C CA . ARG A 1 82 ? -29.633 34.032 5.768 1.00 39.94 ? 82 ARG A CA 1 ATOM 647 C C . ARG A 1 82 ? -30.221 32.743 6.344 1.00 42.97 ? 82 ARG A C 1 ATOM 648 O O . ARG A 1 82 ? -30.703 32.727 7.480 1.00 44.53 ? 82 ARG A O 1 ATOM 649 C CB . ARG A 1 82 ? -28.184 34.244 6.228 1.00 38.04 ? 82 ARG A CB 1 ATOM 650 C CG . ARG A 1 82 ? -27.541 35.536 5.718 1.00 35.03 ? 82 ARG A CG 1 ATOM 651 C CD . ARG A 1 82 ? -27.704 35.698 4.230 1.00 39.15 ? 82 ARG A CD 1 ATOM 652 N NE . ARG A 1 82 ? -27.012 36.870 3.692 1.00 33.66 ? 82 ARG A NE 1 ATOM 653 C CZ . ARG A 1 82 ? -26.757 37.039 2.397 1.00 36.41 ? 82 ARG A CZ 1 ATOM 654 N NH1 . ARG A 1 82 ? -27.139 36.113 1.528 1.00 34.32 ? 82 ARG A NH1 1 ATOM 655 N NH2 . ARG A 1 82 ? -26.121 38.123 1.971 1.00 34.04 ? 82 ARG A NH2 1 ATOM 656 N N . PRO A 1 83 ? -30.182 31.658 5.552 1.00 55.10 ? 83 PRO A N 1 ATOM 657 C CA . PRO A 1 83 ? -30.877 30.395 5.839 1.00 60.13 ? 83 PRO A CA 1 ATOM 658 C C . PRO A 1 83 ? -30.477 29.748 7.165 1.00 63.17 ? 83 PRO A C 1 ATOM 659 O O . PRO A 1 83 ? -31.347 29.245 7.883 1.00 62.78 ? 83 PRO A O 1 ATOM 660 C CB . PRO A 1 83 ? -30.450 29.488 4.677 1.00 51.64 ? 83 PRO A CB 1 ATOM 661 C CG . PRO A 1 83 ? -30.039 30.417 3.593 1.00 53.64 ? 83 PRO A CG 1 ATOM 662 C CD . PRO A 1 83 ? -29.426 31.592 4.288 1.00 52.66 ? 83 PRO A CD 1 ATOM 663 N N . ASN A 1 84 ? -29.186 29.743 7.480 1.00 60.08 ? 84 ASN A N 1 ATOM 664 C CA . ASN A 1 84 ? -28.734 29.118 8.720 1.00 69.94 ? 84 ASN A CA 1 ATOM 665 C C . ASN A 1 84 ? -28.280 30.119 9.786 1.00 65.30 ? 84 ASN A C 1 ATOM 666 O O . ASN A 1 84 ? -27.336 29.856 10.533 1.00 66.60 ? 84 ASN A O 1 ATOM 667 C CB . ASN A 1 84 ? -27.648 28.073 8.440 1.00 76.24 ? 84 ASN A CB 1 ATOM 668 C CG . ASN A 1 84 ? -28.158 26.912 7.596 1.00 84.07 ? 84 ASN A CG 1 ATOM 669 O OD1 . ASN A 1 84 ? -29.283 26.437 7.779 1.00 76.60 ? 84 ASN A OD1 1 ATOM 670 N ND2 . ASN A 1 84 ? -27.332 26.456 6.657 1.00 88.31 ? 84 ASN A ND2 1 ATOM 671 N N . ALA A 1 85 ? -28.964 31.260 9.849 1.00 52.41 ? 85 ALA A N 1 ATOM 672 C CA . ALA A 1 85 ? -28.712 32.271 10.876 1.00 50.52 ? 85 ALA A CA 1 ATOM 673 C C . ALA A 1 85 ? -29.021 31.697 12.256 1.00 53.04 ? 85 ALA A C 1 ATOM 674 O O . ALA A 1 85 ? -30.048 31.040 12.442 1.00 49.40 ? 85 ALA A O 1 ATOM 675 C CB . ALA A 1 85 ? -29.552 33.506 10.620 1.00 41.10 ? 85 ALA A CB 1 ATOM 676 N N . GLN A 1 86 ? -28.144 31.957 13.223 1.00 49.80 ? 86 GLN A N 1 ATOM 677 C CA . GLN A 1 86 ? -28.238 31.315 14.534 1.00 52.35 ? 86 GLN A CA 1 ATOM 678 C C . GLN A 1 86 ? -28.815 32.220 15.613 1.00 42.38 ? 86 GLN A C 1 ATOM 679 O O . GLN A 1 86 ? -29.364 31.737 16.605 1.00 42.53 ? 86 GLN A O 1 ATOM 680 C CB . GLN A 1 86 ? -26.860 30.803 14.981 1.00 51.58 ? 86 GLN A CB 1 ATOM 681 C CG . GLN A 1 86 ? -26.265 29.683 14.123 1.00 56.50 ? 86 GLN A CG 1 ATOM 682 C CD . GLN A 1 86 ? -26.969 28.342 14.305 1.00 65.53 ? 86 GLN A CD 1 ATOM 683 O OE1 . GLN A 1 86 ? -28.145 28.190 13.970 1.00 63.99 ? 86 GLN A OE1 1 ATOM 684 N NE2 . GLN A 1 86 ? -26.245 27.360 14.834 1.00 73.10 ? 86 GLN A NE2 1 ATOM 685 N N . ASN A 1 87 ? -28.688 33.528 15.421 1.00 43.42 ? 87 ASN A N 1 ATOM 686 C CA . ASN A 1 87 ? -29.061 34.479 16.460 1.00 43.78 ? 87 ASN A CA 1 ATOM 687 C C . ASN A 1 87 ? -30.499 34.981 16.373 1.00 45.74 ? 87 ASN A C 1 ATOM 688 O O . ASN A 1 87 ? -30.778 35.999 15.729 1.00 44.34 ? 87 ASN A O 1 ATOM 689 C CB . ASN A 1 87 ? -28.075 35.643 16.477 1.00 42.41 ? 87 ASN A CB 1 ATOM 690 C CG . ASN A 1 87 ? -26.650 35.180 16.683 1.00 52.55 ? 87 ASN A CG 1 ATOM 691 O OD1 . ASN A 1 87 ? -26.384 34.320 17.533 1.00 49.99 ? 87 ASN A OD1 1 ATOM 692 N ND2 . ASN A 1 87 ? -25.724 35.725 15.894 1.00 49.94 ? 87 ASN A ND2 1 ATOM 693 N N . GLY A 1 88 ? -31.403 34.261 17.035 1.00 37.53 ? 88 GLY A N 1 ATOM 694 C CA . GLY A 1 88 ? -32.803 34.637 17.075 1.00 38.95 ? 88 GLY A CA 1 ATOM 695 C C . GLY A 1 88 ? -33.283 34.814 18.499 1.00 42.09 ? 88 GLY A C 1 ATOM 696 O O . GLY A 1 88 ? -32.797 35.681 19.230 1.00 43.26 ? 88 GLY A O 1 ATOM 697 N N . ILE A 1 89 ? -34.251 33.996 18.896 1.00 41.39 ? 89 ILE A N 1 ATOM 698 C CA . ILE A 1 89 ? -34.730 34.007 20.270 1.00 48.94 ? 89 ILE A CA 1 ATOM 699 C C . ILE A 1 89 ? -33.804 33.136 21.123 1.00 46.15 ? 89 ILE A C 1 ATOM 700 O O . ILE A 1 89 ? -33.794 31.910 20.995 1.00 51.67 ? 89 ILE A O 1 ATOM 701 C CB . ILE A 1 89 ? -36.192 33.525 20.347 1.00 45.19 ? 89 ILE A CB 1 ATOM 702 C CG1 . ILE A 1 89 ? -37.108 34.564 19.694 1.00 44.73 ? 89 ILE A CG1 1 ATOM 703 C CG2 . ILE A 1 89 ? -36.616 33.275 21.785 1.00 43.58 ? 89 ILE A CG2 1 ATOM 704 C CD1 . ILE A 1 89 ? -38.551 34.116 19.545 1.00 43.20 ? 89 ILE A CD1 1 ATOM 705 N N . CYS A 1 90 ? -33.010 33.775 21.977 1.00 50.28 ? 90 CYS A N 1 ATOM 706 C CA . CYS A 1 90 ? -32.042 33.050 22.793 1.00 60.69 ? 90 CYS A CA 1 ATOM 707 C C . CYS A 1 90 ? -32.671 32.439 24.055 1.00 57.46 ? 90 CYS A C 1 ATOM 708 O O . CYS A 1 90 ? -32.464 31.258 24.333 1.00 55.00 ? 90 CYS A O 1 ATOM 709 C CB . CYS A 1 90 ? -30.843 33.941 23.122 1.00 59.28 ? 90 CYS A CB 1 ATOM 710 S SG . CYS A 1 90 ? -31.286 35.559 23.781 1.00 77.38 ? 90 CYS A SG 1 ATOM 711 N N . TYR A 1 91 ? -33.438 33.226 24.809 1.00 44.73 ? 91 TYR A N 1 ATOM 712 C CA . TYR A 1 91 ? -34.191 32.676 25.937 1.00 48.94 ? 91 TYR A CA 1 ATOM 713 C C . TYR A 1 91 ? -35.478 32.054 25.404 1.00 47.71 ? 91 TYR A C 1 ATOM 714 O O . TYR A 1 91 ? -36.328 32.759 24.858 1.00 44.48 ? 91 TYR A O 1 ATOM 715 C CB . TYR A 1 91 ? -34.516 33.751 26.980 1.00 47.71 ? 91 TYR A CB 1 ATOM 716 C CG . TYR A 1 91 ? -34.858 33.205 28.359 1.00 48.90 ? 91 TYR A CG 1 ATOM 717 C CD1 . TYR A 1 91 ? -36.147 32.788 28.669 1.00 44.51 ? 91 TYR A CD1 1 ATOM 718 C CD2 . TYR A 1 91 ? -33.889 33.119 29.353 1.00 53.14 ? 91 TYR A CD2 1 ATOM 719 C CE1 . TYR A 1 91 ? -36.460 32.293 29.930 1.00 51.54 ? 91 TYR A CE1 1 ATOM 720 C CE2 . TYR A 1 91 ? -34.188 32.626 30.615 1.00 50.82 ? 91 TYR A CE2 1 ATOM 721 C CZ . TYR A 1 91 ? -35.474 32.215 30.900 1.00 57.26 ? 91 TYR A CZ 1 ATOM 722 O OH . TYR A 1 91 ? -35.776 31.726 32.154 1.00 51.99 ? 91 TYR A OH 1 ATOM 723 N N . PRO A 1 92 ? -35.627 30.732 25.578 1.00 51.73 ? 92 PRO A N 1 ATOM 724 C CA . PRO A 1 92 ? -36.716 29.945 24.980 1.00 49.74 ? 92 PRO A CA 1 ATOM 725 C C . PRO A 1 92 ? -38.104 30.534 25.230 1.00 53.06 ? 92 PRO A C 1 ATOM 726 O O . PRO A 1 92 ? -38.362 31.096 26.304 1.00 47.23 ? 92 PRO A O 1 ATOM 727 C CB . PRO A 1 92 ? -36.589 28.578 25.668 1.00 49.44 ? 92 PRO A CB 1 ATOM 728 C CG . PRO A 1 92 ? -35.756 28.831 26.902 1.00 54.70 ? 92 PRO A CG 1 ATOM 729 C CD . PRO A 1 92 ? -34.815 29.931 26.510 1.00 52.75 ? 92 PRO A CD 1 ATOM 730 N N . GLY A 1 93 ? -38.981 30.405 24.237 1.00 45.47 ? 93 GLY A N 1 ATOM 731 C CA . GLY A 1 93 ? -40.321 30.953 24.316 1.00 44.08 ? 93 GLY A CA 1 ATOM 732 C C . GLY A 1 93 ? -40.857 31.336 22.946 1.00 45.88 ? 93 GLY A C 1 ATOM 733 O O . GLY A 1 93 ? -40.104 31.433 21.976 1.00 47.60 ? 93 GLY A O 1 ATOM 734 N N . VAL A 1 94 ? -42.162 31.570 22.863 1.00 50.02 ? 94 VAL A N 1 ATOM 735 C CA . VAL A 1 94 ? -42.804 31.867 21.584 1.00 48.94 ? 94 VAL A CA 1 ATOM 736 C C . VAL A 1 94 ? -42.960 33.371 21.354 1.00 40.23 ? 94 VAL A C 1 ATOM 737 O O . VAL A 1 94 ? -43.377 34.095 22.261 1.00 41.79 ? 94 VAL A O 1 ATOM 738 C CB . VAL A 1 94 ? -44.192 31.198 21.515 1.00 48.26 ? 94 VAL A CB 1 ATOM 739 C CG1 . VAL A 1 94 ? -44.899 31.546 20.223 1.00 47.85 ? 94 VAL A CG1 1 ATOM 740 C CG2 . VAL A 1 94 ? -44.056 29.689 21.655 1.00 47.78 ? 94 VAL A CG2 1 ATOM 741 N N . LEU A 1 95 ? -42.616 33.841 20.153 1.00 46.71 ? 95 LEU A N 1 ATOM 742 C CA . LEU A 1 95 ? -42.974 35.201 19.744 1.00 44.29 ? 95 LEU A CA 1 ATOM 743 C C . LEU A 1 95 ? -44.391 35.147 19.170 1.00 44.15 ? 95 LEU A C 1 ATOM 744 O O . LEU A 1 95 ? -44.639 34.493 18.149 1.00 41.19 ? 95 LEU A O 1 ATOM 745 C CB . LEU A 1 95 ? -41.995 35.761 18.699 1.00 39.76 ? 95 LEU A CB 1 ATOM 746 C CG . LEU A 1 95 ? -41.590 37.235 18.852 1.00 43.35 ? 95 LEU A CG 1 ATOM 747 C CD1 . LEU A 1 95 ? -40.765 37.740 17.667 1.00 41.87 ? 95 LEU A CD1 1 ATOM 748 C CD2 . LEU A 1 95 ? -42.804 38.126 19.067 1.00 40.65 ? 95 LEU A CD2 1 ATOM 749 N N . ASN A 1 96 ? -45.323 35.820 19.835 1.00 40.90 ? 96 ASN A N 1 ATOM 750 C CA . ASN A 1 96 ? -46.722 35.765 19.438 1.00 37.80 ? 96 ASN A CA 1 ATOM 751 C C . ASN A 1 96 ? -46.981 36.465 18.116 1.00 37.57 ? 96 ASN A C 1 ATOM 752 O O . ASN A 1 96 ? -46.423 37.537 17.859 1.00 33.92 ? 96 ASN A O 1 ATOM 753 C CB . ASN A 1 96 ? -47.595 36.397 20.506 1.00 42.70 ? 96 ASN A CB 1 ATOM 754 C CG . ASN A 1 96 ? -48.845 35.597 20.769 1.00 56.51 ? 96 ASN A CG 1 ATOM 755 O OD1 . ASN A 1 96 ? -48.775 34.487 21.310 1.00 55.70 ? 96 ASN A OD1 1 ATOM 756 N ND2 . ASN A 1 96 ? -50.002 36.149 20.391 1.00 44.61 ? 96 ASN A ND2 1 ATOM 757 N N . GLU A 1 97 ? -47.835 35.857 17.293 1.00 38.79 ? 97 GLU A N 1 ATOM 758 C CA . GLU A 1 97 ? -48.191 36.405 15.988 1.00 32.78 ? 97 GLU A CA 1 ATOM 759 C C . GLU A 1 97 ? -46.938 36.682 15.176 1.00 33.00 ? 97 GLU A C 1 ATOM 760 O O . GLU A 1 97 ? -46.808 37.743 14.556 1.00 30.77 ? 97 GLU A O 1 ATOM 761 C CB . GLU A 1 97 ? -49.025 37.680 16.140 1.00 31.23 ? 97 GLU A CB 1 ATOM 762 C CG . GLU A 1 97 ? -50.314 37.488 16.930 1.00 35.44 ? 97 GLU A CG 1 ATOM 763 C CD . GLU A 1 97 ? -51.399 36.772 16.135 1.00 50.87 ? 97 GLU A CD 1 ATOM 764 O OE1 . GLU A 1 97 ? -52.488 36.534 16.705 1.00 56.29 ? 97 GLU A OE1 1 ATOM 765 O OE2 . GLU A 1 97 ? -51.173 36.453 14.942 1.00 49.64 ? 97 GLU A OE2 1 ATOM 766 N N . LEU A 1 98 ? -46.022 35.717 15.193 1.00 30.70 ? 98 LEU A N 1 ATOM 767 C CA . LEU A 1 98 ? -44.741 35.840 14.505 1.00 30.62 ? 98 LEU A CA 1 ATOM 768 C C . LEU A 1 98 ? -44.900 36.114 13.018 1.00 32.24 ? 98 LEU A C 1 ATOM 769 O O . LEU A 1 98 ? -44.255 37.018 12.478 1.00 34.08 ? 98 LEU A O 1 ATOM 770 C CB . LEU A 1 98 ? -43.906 34.577 14.707 1.00 31.56 ? 98 LEU A CB 1 ATOM 771 C CG . LEU A 1 98 ? -42.580 34.561 13.948 1.00 36.05 ? 98 LEU A CG 1 ATOM 772 C CD1 . LEU A 1 98 ? -41.715 35.734 14.388 1.00 30.22 ? 98 LEU A CD1 1 ATOM 773 C CD2 . LEU A 1 98 ? -41.848 33.237 14.151 1.00 26.83 ? 98 LEU A CD2 1 ATOM 774 N N . GLU A 1 99 ? -45.752 35.335 12.356 1.00 34.87 ? 99 GLU A N 1 ATOM 775 C CA . GLU A 1 99 ? -45.923 35.464 10.912 1.00 35.93 ? 99 GLU A CA 1 ATOM 776 C C . GLU A 1 99 ? -46.503 36.830 10.553 1.00 35.34 ? 99 GLU A C 1 ATOM 777 O O . GLU A 1 99 ? -46.095 37.445 9.563 1.00 33.21 ? 99 GLU A O 1 ATOM 778 C CB . GLU A 1 99 ? -46.794 34.331 10.359 1.00 33.55 ? 99 GLU A CB 1 ATOM 779 C CG . GLU A 1 99 ? -46.153 32.948 10.421 1.00 36.39 ? 99 GLU A CG 1 ATOM 780 C CD . GLU A 1 99 ? -46.082 32.374 11.841 1.00 48.16 ? 99 GLU A CD 1 ATOM 781 O OE1 . GLU A 1 99 ? -46.796 32.876 12.746 1.00 40.37 ? 99 GLU A OE1 1 ATOM 782 O OE2 . GLU A 1 99 ? -45.306 31.412 12.047 1.00 46.98 ? 99 GLU A OE2 1 ATOM 783 N N . GLU A 1 100 ? -47.435 37.311 11.371 1.00 30.56 ? 100 GLU A N 1 ATOM 784 C CA . GLU A 1 100 ? -47.996 38.644 11.174 1.00 33.16 ? 100 GLU A CA 1 ATOM 785 C C . GLU A 1 100 ? -46.950 39.736 11.401 1.00 34.10 ? 100 GLU A C 1 ATOM 786 O O . GLU A 1 100 ? -46.931 40.744 10.688 1.00 33.71 ? 100 GLU A O 1 ATOM 787 C CB . GLU A 1 100 ? -49.218 38.857 12.069 1.00 31.28 ? 100 GLU A CB 1 ATOM 788 C CG . GLU A 1 100 ? -50.493 38.264 11.501 1.00 35.88 ? 100 GLU A CG 1 ATOM 789 C CD . GLU A 1 100 ? -50.977 39.009 10.270 1.00 37.37 ? 100 GLU A CD 1 ATOM 790 O OE1 . GLU A 1 100 ? -50.976 40.261 10.298 1.00 39.73 ? 100 GLU A OE1 1 ATOM 791 O OE2 . GLU A 1 100 ? -51.368 38.349 9.279 1.00 36.02 ? 100 GLU A OE2 1 ATOM 792 N N . LEU A 1 101 ? -46.076 39.528 12.383 1.00 29.53 ? 101 LEU A N 1 ATOM 793 C CA . LEU A 1 101 ? -44.966 40.445 12.629 1.00 31.66 ? 101 LEU A CA 1 ATOM 794 C C . LEU A 1 101 ? -44.012 40.552 11.436 1.00 29.68 ? 101 LEU A C 1 ATOM 795 O O . LEU A 1 101 ? -43.621 41.659 11.053 1.00 30.25 ? 101 LEU A O 1 ATOM 796 C CB . LEU A 1 101 ? -44.188 40.035 13.883 1.00 33.65 ? 101 LEU A CB 1 ATOM 797 C CG . LEU A 1 101 ? -42.905 40.833 14.135 1.00 32.08 ? 101 LEU A CG 1 ATOM 798 C CD1 . LEU A 1 101 ? -43.239 42.279 14.456 1.00 30.92 ? 101 LEU A CD1 1 ATOM 799 C CD2 . LEU A 1 101 ? -42.072 40.217 15.247 1.00 35.10 ? 101 LEU A CD2 1 ATOM 800 N N . LYS A 1 102 ? -43.637 39.414 10.852 1.00 27.71 ? 102 LYS A N 1 ATOM 801 C CA . LYS A 1 102 ? -42.771 39.412 9.667 1.00 31.58 ? 102 LYS A CA 1 ATOM 802 C C . LYS A 1 102 ? -43.412 40.125 8.482 1.00 32.21 ? 102 LYS A C 1 ATOM 803 O O . LYS A 1 102 ? -42.749 40.888 7.779 1.00 34.43 ? 102 LYS A O 1 ATOM 804 C CB . LYS A 1 102 ? -42.381 37.986 9.266 1.00 30.29 ? 102 LYS A CB 1 ATOM 805 C CG . LYS A 1 102 ? -41.423 37.303 10.240 1.00 36.76 ? 102 LYS A CG 1 ATOM 806 C CD . LYS A 1 102 ? -41.061 35.904 9.758 1.00 36.04 ? 102 LYS A CD 1 ATOM 807 C CE . LYS A 1 102 ? -40.016 35.269 10.659 1.00 42.50 ? 102 LYS A CE 1 ATOM 808 N NZ . LYS A 1 102 ? -39.639 33.905 10.196 1.00 47.14 ? 102 LYS A NZ 1 ATOM 809 N N . ALA A 1 103 ? -44.699 39.874 8.258 1.00 26.19 ? 103 ALA A N 1 ATOM 810 C CA . ALA A 1 103 ? -45.408 40.552 7.178 1.00 29.00 ? 103 ALA A CA 1 ATOM 811 C C . ALA A 1 103 ? -45.423 42.061 7.420 1.00 28.86 ? 103 ALA A C 1 ATOM 812 O O . ALA A 1 103 ? -45.288 42.852 6.485 1.00 30.99 ? 103 ALA A O 1 ATOM 813 C CB . ALA A 1 103 ? -46.827 40.010 7.026 1.00 25.26 ? 103 ALA A CB 1 ATOM 814 N N . PHE A 1 104 ? -45.575 42.458 8.679 1.00 28.79 ? 104 PHE A N 1 ATOM 815 C CA . PHE A 1 104 ? -45.594 43.874 9.019 1.00 31.07 ? 104 PHE A CA 1 ATOM 816 C C . PHE A 1 104 ? -44.237 44.514 8.739 1.00 33.99 ? 104 PHE A C 1 ATOM 817 O O . PHE A 1 104 ? -44.149 45.535 8.048 1.00 34.62 ? 104 PHE A O 1 ATOM 818 C CB . PHE A 1 104 ? -45.990 44.078 10.481 1.00 25.95 ? 104 PHE A CB 1 ATOM 819 C CG . PHE A 1 104 ? -45.849 45.493 10.946 1.00 30.24 ? 104 PHE A CG 1 ATOM 820 C CD1 . PHE A 1 104 ? -46.747 46.473 10.526 1.00 32.93 ? 104 PHE A CD1 1 ATOM 821 C CD2 . PHE A 1 104 ? -44.816 45.853 11.801 1.00 29.32 ? 104 PHE A CD2 1 ATOM 822 C CE1 . PHE A 1 104 ? -46.614 47.793 10.955 1.00 35.12 ? 104 PHE A CE1 1 ATOM 823 C CE2 . PHE A 1 104 ? -44.673 47.169 12.234 1.00 31.21 ? 104 PHE A CE2 1 ATOM 824 C CZ . PHE A 1 104 ? -45.574 48.141 11.811 1.00 33.90 ? 104 PHE A CZ 1 ATOM 825 N N . ILE A 1 105 ? -43.183 43.900 9.271 1.00 29.32 ? 105 ILE A N 1 ATOM 826 C CA . ILE A 1 105 ? -41.828 44.396 9.080 1.00 30.93 ? 105 ILE A CA 1 ATOM 827 C C . ILE A 1 105 ? -41.487 44.472 7.591 1.00 32.95 ? 105 ILE A C 1 ATOM 828 O O . ILE A 1 105 ? -40.890 45.452 7.137 1.00 32.19 ? 105 ILE A O 1 ATOM 829 C CB . ILE A 1 105 ? -40.807 43.538 9.863 1.00 32.72 ? 105 ILE A CB 1 ATOM 830 C CG1 . ILE A 1 105 ? -40.949 43.814 11.363 1.00 29.39 ? 105 ILE A CG1 1 ATOM 831 C CG2 . ILE A 1 105 ? -39.390 43.827 9.415 1.00 27.63 ? 105 ILE A CG2 1 ATOM 832 C CD1 . ILE A 1 105 ? -40.066 42.955 12.241 1.00 29.97 ? 105 ILE A CD1 1 ATOM 833 N N . GLY A 1 106 ? -41.894 43.455 6.832 1.00 38.16 ? 106 GLY A N 1 ATOM 834 C CA . GLY A 1 106 ? -41.674 43.426 5.394 1.00 32.83 ? 106 GLY A CA 1 ATOM 835 C C . GLY A 1 106 ? -42.307 44.596 4.662 1.00 35.17 ? 106 GLY A C 1 ATOM 836 O O . GLY A 1 106 ? -41.806 45.018 3.623 1.00 36.93 ? 106 GLY A O 1 ATOM 837 N N . SER A 1 107 ? -43.400 45.126 5.206 1.00 31.06 ? 107 SER A N 1 ATOM 838 C CA . SER A 1 107 ? -44.090 46.255 4.589 1.00 33.86 ? 107 SER A CA 1 ATOM 839 C C . SER A 1 107 ? -43.399 47.578 4.914 1.00 38.22 ? 107 SER A C 1 ATOM 840 O O . SER A 1 107 ? -43.893 48.651 4.558 1.00 43.27 ? 107 SER A O 1 ATOM 841 C CB . SER A 1 107 ? -45.556 46.305 5.036 1.00 34.37 ? 107 SER A CB 1 ATOM 842 O OG . SER A 1 107 ? -45.691 46.765 6.371 1.00 33.05 ? 107 SER A OG 1 ATOM 843 N N . GLY A 1 108 ? -42.256 47.500 5.588 1.00 34.83 ? 108 GLY A N 1 ATOM 844 C CA . GLY A 1 108 ? -41.557 48.691 6.028 1.00 34.66 ? 108 GLY A CA 1 ATOM 845 C C . GLY A 1 108 ? -40.365 49.062 5.175 1.00 36.47 ? 108 GLY A C 1 ATOM 846 O O . GLY A 1 108 ? -40.062 48.400 4.180 1.00 34.26 ? 108 GLY A O 1 ATOM 847 N N . GLU A 1 109 ? -39.664 50.108 5.599 1.00 40.97 ? 109 GLU A N 1 ATOM 848 C CA . GLU A 1 109 ? -38.690 50.790 4.758 1.00 43.24 ? 109 GLU A CA 1 ATOM 849 C C . GLU A 1 109 ? -37.568 51.356 5.627 1.00 42.66 ? 109 GLU A C 1 ATOM 850 O O . GLU A 1 109 ? -36.418 51.484 5.192 1.00 40.91 ? 109 GLU A O 1 ATOM 851 C CB . GLU A 1 109 ? -39.422 51.911 4.018 1.00 44.67 ? 109 GLU A CB 1 ATOM 852 C CG . GLU A 1 109 ? -38.582 52.818 3.159 1.00 52.54 ? 109 GLU A CG 1 ATOM 853 C CD . GLU A 1 109 ? -39.418 53.921 2.527 1.00 58.07 ? 109 GLU A CD 1 ATOM 854 O OE1 . GLU A 1 109 ? -38.943 55.074 2.462 1.00 61.64 ? 109 GLU A OE1 1 ATOM 855 O OE2 . GLU A 1 109 ? -40.555 53.631 2.094 1.00 63.97 ? 109 GLU A OE2 1 ATOM 856 N N . ARG A 1 110 ? -37.916 51.686 6.866 1.00 36.35 ? 110 ARG A N 1 ATOM 857 C CA . ARG A 1 110 ? -36.977 52.290 7.794 1.00 37.38 ? 110 ARG A CA 1 ATOM 858 C C . ARG A 1 110 ? -37.455 52.133 9.235 1.00 37.15 ? 110 ARG A C 1 ATOM 859 O O . ARG A 1 110 ? -38.642 52.298 9.520 1.00 39.09 ? 110 ARG A O 1 ATOM 860 C CB . ARG A 1 110 ? -36.788 53.773 7.457 1.00 39.95 ? 110 ARG A CB 1 ATOM 861 C CG . ARG A 1 110 ? -36.101 54.572 8.545 1.00 45.38 ? 110 ARG A CG 1 ATOM 862 C CD . ARG A 1 110 ? -35.576 55.916 8.054 1.00 49.16 ? 110 ARG A CD 1 ATOM 863 N NE . ARG A 1 110 ? -34.788 56.562 9.105 1.00 64.73 ? 110 ARG A NE 1 ATOM 864 C CZ . ARG A 1 110 ? -33.530 56.241 9.406 1.00 59.90 ? 110 ARG A CZ 1 ATOM 865 N NH1 . ARG A 1 110 ? -32.899 56.881 10.383 1.00 61.41 ? 110 ARG A NH1 1 ATOM 866 N NH2 . ARG A 1 110 ? -32.898 55.283 8.733 1.00 45.44 ? 110 ARG A NH2 1 ATOM 867 N N . VAL A 1 111 ? -36.540 51.791 10.139 1.00 35.12 ? 111 VAL A N 1 ATOM 868 C CA . VAL A 1 111 ? -36.847 51.832 11.569 1.00 39.98 ? 111 VAL A CA 1 ATOM 869 C C . VAL A 1 111 ? -35.898 52.787 12.297 1.00 41.92 ? 111 VAL A C 1 ATOM 870 O O . VAL A 1 111 ? -34.703 52.840 11.994 1.00 43.74 ? 111 VAL A O 1 ATOM 871 C CB . VAL A 1 111 ? -36.808 50.432 12.235 1.00 36.85 ? 111 VAL A CB 1 ATOM 872 C CG1 . VAL A 1 111 ? -37.922 49.549 11.696 1.00 34.52 ? 111 VAL A CG1 1 ATOM 873 C CG2 . VAL A 1 111 ? -35.456 49.770 12.020 1.00 35.20 ? 111 VAL A CG2 1 ATOM 874 N N . GLU A 1 112 ? -36.442 53.558 13.234 1.00 39.85 ? 112 GLU A N 1 ATOM 875 C CA . GLU A 1 112 ? -35.632 54.396 14.108 1.00 40.54 ? 112 GLU A CA 1 ATOM 876 C C . GLU A 1 112 ? -35.763 53.890 15.533 1.00 40.32 ? 112 GLU A C 1 ATOM 877 O O . GLU A 1 112 ? -36.836 53.987 16.132 1.00 41.15 ? 112 GLU A O 1 ATOM 878 C CB . GLU A 1 112 ? -36.086 55.854 14.049 1.00 44.93 ? 112 GLU A CB 1 ATOM 879 C CG . GLU A 1 112 ? -35.763 56.586 12.759 1.00 55.23 ? 112 GLU A CG 1 ATOM 880 C CD . GLU A 1 112 ? -36.213 58.044 12.790 1.00 76.95 ? 112 GLU A CD 1 ATOM 881 O OE1 . GLU A 1 112 ? -36.454 58.573 13.903 1.00 72.16 ? 112 GLU A OE1 1 ATOM 882 O OE2 . GLU A 1 112 ? -36.327 58.656 11.702 1.00 72.10 ? 112 GLU A OE2 1 ATOM 883 N N . ARG A 1 113 ? -34.677 53.346 16.072 1.00 36.99 ? 113 ARG A N 1 ATOM 884 C CA . ARG A 1 113 ? -34.664 52.869 17.452 1.00 36.40 ? 113 ARG A CA 1 ATOM 885 C C . ARG A 1 113 ? -34.619 54.053 18.418 1.00 42.10 ? 113 ARG A C 1 ATOM 886 O O . ARG A 1 113 ? -33.977 55.072 18.136 1.00 42.02 ? 113 ARG A O 1 ATOM 887 C CB . ARG A 1 113 ? -33.463 51.952 17.672 1.00 34.41 ? 113 ARG A CB 1 ATOM 888 C CG . ARG A 1 113 ? -33.436 51.222 19.005 1.00 35.41 ? 113 ARG A CG 1 ATOM 889 C CD . ARG A 1 113 ? -32.443 50.068 18.954 1.00 36.13 ? 113 ARG A CD 1 ATOM 890 N NE . ARG A 1 113 ? -32.335 49.373 20.232 1.00 43.23 ? 113 ARG A NE 1 ATOM 891 C CZ . ARG A 1 113 ? -31.471 49.702 21.187 1.00 41.62 ? 113 ARG A CZ 1 ATOM 892 N NH1 . ARG A 1 113 ? -30.641 50.718 21.006 1.00 37.37 ? 113 ARG A NH1 1 ATOM 893 N NH2 . ARG A 1 113 ? -31.440 49.016 22.321 1.00 43.65 ? 113 ARG A NH2 1 ATOM 894 N N . PHE A 1 114 ? -35.322 53.925 19.542 1.00 40.84 ? 114 PHE A N 1 ATOM 895 C CA . PHE A 1 114 ? -35.357 54.968 20.567 1.00 41.79 ? 114 PHE A CA 1 ATOM 896 C C . PHE A 1 114 ? -35.771 54.373 21.912 1.00 48.44 ? 114 PHE A C 1 ATOM 897 O O . PHE A 1 114 ? -36.484 53.366 21.957 1.00 46.58 ? 114 PHE A O 1 ATOM 898 C CB . PHE A 1 114 ? -36.321 56.092 20.166 1.00 39.66 ? 114 PHE A CB 1 ATOM 899 C CG . PHE A 1 114 ? -37.769 55.709 20.258 1.00 46.80 ? 114 PHE A CG 1 ATOM 900 C CD1 . PHE A 1 114 ? -38.354 54.914 19.278 1.00 42.18 ? 114 PHE A CD1 1 ATOM 901 C CD2 . PHE A 1 114 ? -38.548 56.141 21.322 1.00 42.49 ? 114 PHE A CD2 1 ATOM 902 C CE1 . PHE A 1 114 ? -39.687 54.553 19.361 1.00 39.91 ? 114 PHE A CE1 1 ATOM 903 C CE2 . PHE A 1 114 ? -39.882 55.787 21.411 1.00 47.59 ? 114 PHE A CE2 1 ATOM 904 C CZ . PHE A 1 114 ? -40.453 54.989 20.429 1.00 43.48 ? 114 PHE A CZ 1 ATOM 905 N N . GLU A 1 115 ? -35.322 54.990 23.003 1.00 51.86 ? 115 GLU A N 1 ATOM 906 C CA . GLU A 1 115 ? -35.686 54.526 24.340 1.00 50.67 ? 115 GLU A CA 1 ATOM 907 C C . GLU A 1 115 ? -37.131 54.928 24.650 1.00 53.70 ? 115 GLU A C 1 ATOM 908 O O . GLU A 1 115 ? -37.451 56.118 24.716 1.00 55.27 ? 115 GLU A O 1 ATOM 909 C CB . GLU A 1 115 ? -34.723 55.096 25.389 1.00 53.74 ? 115 GLU A CB 1 ATOM 910 C CG . GLU A 1 115 ? -34.721 54.349 26.720 1.00 58.05 ? 115 GLU A CG 1 ATOM 911 C CD . GLU A 1 115 ? -33.692 54.893 27.701 1.00 59.62 ? 115 GLU A CD 1 ATOM 912 O OE1 . GLU A 1 115 ? -33.179 54.109 28.528 1.00 54.95 ? 115 GLU A OE1 1 ATOM 913 O OE2 . GLU A 1 115 ? -33.400 56.107 27.648 1.00 64.83 ? 115 GLU A OE2 1 ATOM 914 N N . MET A 1 116 ? -37.999 53.934 24.827 1.00 52.75 ? 116 MET A N 1 ATOM 915 C CA . MET A 1 116 ? -39.428 54.167 25.044 1.00 50.96 ? 116 MET A CA 1 ATOM 916 C C . MET A 1 116 ? -39.737 54.254 26.536 1.00 50.71 ? 116 MET A C 1 ATOM 917 O O . MET A 1 116 ? -40.461 55.145 26.986 1.00 53.87 ? 116 MET A O 1 ATOM 918 C CB . MET A 1 116 ? -40.240 53.039 24.398 1.00 49.66 ? 116 MET A CB 1 ATOM 919 C CG . MET A 1 116 ? -41.738 53.305 24.259 1.00 47.66 ? 116 MET A CG 1 ATOM 920 S SD . MET A 1 116 ? -42.595 51.896 23.498 1.00 47.15 ? 116 MET A SD 1 ATOM 921 C CE . MET A 1 116 ? -44.247 52.575 23.291 1.00 39.56 ? 116 MET A CE 1 ATOM 922 N N . PHE A 1 117 ? -39.192 53.313 27.299 1.00 47.55 ? 117 PHE A N 1 ATOM 923 C CA . PHE A 1 117 ? -39.288 53.360 28.751 1.00 47.11 ? 117 PHE A CA 1 ATOM 924 C C . PHE A 1 117 ? -37.897 53.233 29.354 1.00 47.54 ? 117 PHE A C 1 ATOM 925 O O . PHE A 1 117 ? -37.327 52.137 29.365 1.00 45.80 ? 117 PHE A O 1 ATOM 926 C CB . PHE A 1 117 ? -40.169 52.226 29.278 1.00 47.30 ? 117 PHE A CB 1 ATOM 927 C CG . PHE A 1 117 ? -41.609 52.319 28.856 1.00 47.67 ? 117 PHE A CG 1 ATOM 928 C CD1 . PHE A 1 117 ? -42.482 53.188 29.497 1.00 44.72 ? 117 PHE A CD1 1 ATOM 929 C CD2 . PHE A 1 117 ? -42.097 51.519 27.832 1.00 44.45 ? 117 PHE A CD2 1 ATOM 930 C CE1 . PHE A 1 117 ? -43.818 53.267 29.116 1.00 46.73 ? 117 PHE A CE1 1 ATOM 931 C CE2 . PHE A 1 117 ? -43.427 51.591 27.447 1.00 47.08 ? 117 PHE A CE2 1 ATOM 932 C CZ . PHE A 1 117 ? -44.290 52.466 28.090 1.00 46.39 ? 117 PHE A CZ 1 ATOM 933 N N . PRO A 1 118 ? -37.341 54.353 29.850 1.00 53.98 ? 118 PRO A N 1 ATOM 934 C CA . PRO A 1 118 ? -36.073 54.273 30.585 1.00 51.88 ? 118 PRO A CA 1 ATOM 935 C C . PRO A 1 118 ? -36.292 53.404 31.817 1.00 53.14 ? 118 PRO A C 1 ATOM 936 O O . PRO A 1 118 ? -37.426 53.354 32.307 1.00 52.20 ? 118 PRO A O 1 ATOM 937 C CB . PRO A 1 118 ? -35.823 55.722 31.019 1.00 52.51 ? 118 PRO A CB 1 ATOM 938 C CG . PRO A 1 118 ? -36.654 56.562 30.101 1.00 55.26 ? 118 PRO A CG 1 ATOM 939 C CD . PRO A 1 118 ? -37.866 55.730 29.792 1.00 53.96 ? 118 PRO A CD 1 ATOM 940 N N . LYS A 1 119 ? -35.251 52.738 32.311 1.00 54.17 ? 119 LYS A N 1 ATOM 941 C CA . LYS A 1 119 ? -35.407 51.848 33.460 1.00 57.79 ? 119 LYS A CA 1 ATOM 942 C C . LYS A 1 119 ? -35.877 52.609 34.698 1.00 58.83 ? 119 LYS A C 1 ATOM 943 O O . LYS A 1 119 ? -36.386 52.014 35.647 1.00 61.09 ? 119 LYS A O 1 ATOM 944 C CB . LYS A 1 119 ? -34.105 51.095 33.754 1.00 53.92 ? 119 LYS A CB 1 ATOM 945 C CG . LYS A 1 119 ? -33.402 50.546 32.516 1.00 54.61 ? 119 LYS A CG 1 ATOM 946 C CD . LYS A 1 119 ? -32.558 49.325 32.862 1.00 53.35 ? 119 LYS A CD 1 ATOM 947 C CE . LYS A 1 119 ? -31.311 49.250 31.998 1.00 53.70 ? 119 LYS A CE 1 ATOM 948 N NZ . LYS A 1 119 ? -30.620 47.935 32.134 1.00 58.21 ? 119 LYS A NZ 1 ATOM 949 N N . SER A 1 120 ? -35.711 53.929 34.676 1.00 54.37 ? 120 SER A N 1 ATOM 950 C CA . SER A 1 120 ? -36.175 54.785 35.761 1.00 56.34 ? 120 SER A CA 1 ATOM 951 C C . SER A 1 120 ? -37.706 54.789 35.853 1.00 59.84 ? 120 SER A C 1 ATOM 952 O O . SER A 1 120 ? -38.274 55.173 36.878 1.00 61.99 ? 120 SER A O 1 ATOM 953 C CB . SER A 1 120 ? -35.646 56.212 35.581 1.00 59.87 ? 120 SER A CB 1 ATOM 954 O OG . SER A 1 120 ? -36.519 56.988 34.779 1.00 64.01 ? 120 SER A OG 1 ATOM 955 N N . THR A 1 121 ? -38.369 54.351 34.786 1.00 60.48 ? 121 THR A N 1 ATOM 956 C CA . THR A 1 121 ? -39.828 54.263 34.772 1.00 63.91 ? 121 THR A CA 1 ATOM 957 C C . THR A 1 121 ? -40.335 53.331 35.872 1.00 61.52 ? 121 THR A C 1 ATOM 958 O O . THR A 1 121 ? -41.373 53.590 36.488 1.00 57.48 ? 121 THR A O 1 ATOM 959 C CB . THR A 1 121 ? -40.361 53.762 33.407 1.00 56.78 ? 121 THR A CB 1 ATOM 960 O OG1 . THR A 1 121 ? -40.537 54.875 32.520 1.00 60.97 ? 121 THR A OG1 1 ATOM 961 N N . TRP A 1 122 ? -39.592 52.255 36.122 1.00 52.03 ? 122 TRP A N 1 ATOM 962 C CA . TRP A 1 122 ? -40.055 51.188 37.009 1.00 58.70 ? 122 TRP A CA 1 ATOM 963 C C . TRP A 1 122 ? -39.569 51.355 38.459 1.00 59.44 ? 122 TRP A C 1 ATOM 964 O O . TRP A 1 122 ? -38.427 51.024 38.791 1.00 54.80 ? 122 TRP A O 1 ATOM 965 C CB . TRP A 1 122 ? -39.649 49.826 36.432 1.00 56.76 ? 122 TRP A CB 1 ATOM 966 C CG . TRP A 1 122 ? -39.814 49.759 34.928 1.00 58.78 ? 122 TRP A CG 1 ATOM 967 C CD1 . TRP A 1 122 ? -38.822 49.653 33.990 1.00 57.14 ? 122 TRP A CD1 1 ATOM 968 C CD2 . TRP A 1 122 ? -41.050 49.823 34.197 1.00 53.50 ? 122 TRP A CD2 1 ATOM 969 N NE1 . TRP A 1 122 ? -39.369 49.636 32.726 1.00 52.66 ? 122 TRP A NE1 1 ATOM 970 C CE2 . TRP A 1 122 ? -40.729 49.739 32.826 1.00 53.27 ? 122 TRP A CE2 1 ATOM 971 C CE3 . TRP A 1 122 ? -42.389 49.936 34.573 1.00 53.71 ? 122 TRP A CE3 1 ATOM 972 C CZ2 . TRP A 1 122 ? -41.713 49.766 31.830 1.00 53.41 ? 122 TRP A CZ2 1 ATOM 973 C CZ3 . TRP A 1 122 ? -43.358 49.962 33.587 1.00 55.10 ? 122 TRP A CZ3 1 ATOM 974 C CH2 . TRP A 1 122 ? -43.017 49.877 32.231 1.00 50.67 ? 122 TRP A CH2 1 ATOM 975 N N . ALA A 1 123 ? -40.458 51.847 39.319 1.00 57.44 ? 123 ALA A N 1 ATOM 976 C CA . ALA A 1 123 ? -40.093 52.237 40.685 1.00 64.12 ? 123 ALA A CA 1 ATOM 977 C C . ALA A 1 123 ? -40.261 51.127 41.723 1.00 64.95 ? 123 ALA A C 1 ATOM 978 O O . ALA A 1 123 ? -41.320 50.497 41.813 1.00 61.47 ? 123 ALA A O 1 ATOM 979 C CB . ALA A 1 123 ? -40.886 53.469 41.112 1.00 60.08 ? 123 ALA A CB 1 ATOM 980 N N . GLY A 1 124 ? -39.220 50.911 42.523 1.00 64.56 ? 124 GLY A N 1 ATOM 981 C CA . GLY A 1 124 ? -39.274 49.926 43.590 1.00 68.51 ? 124 GLY A CA 1 ATOM 982 C C . GLY A 1 124 ? -38.945 48.512 43.146 1.00 70.29 ? 124 GLY A C 1 ATOM 983 O O . GLY A 1 124 ? -39.357 47.543 43.792 1.00 69.43 ? 124 GLY A O 1 ATOM 984 N N . VAL A 1 125 ? -38.198 48.395 42.050 1.00 59.14 ? 125 VAL A N 1 ATOM 985 C CA . VAL A 1 125 ? -37.803 47.096 41.507 1.00 57.31 ? 125 VAL A CA 1 ATOM 986 C C . VAL A 1 125 ? -36.374 47.140 40.963 1.00 60.25 ? 125 VAL A C 1 ATOM 987 O O . VAL A 1 125 ? -35.820 48.223 40.743 1.00 57.93 ? 125 VAL A O 1 ATOM 988 C CB . VAL A 1 125 ? -38.751 46.649 40.377 1.00 58.67 ? 125 VAL A CB 1 ATOM 989 C CG1 . VAL A 1 125 ? -40.021 46.031 40.939 1.00 49.43 ? 125 VAL A CG1 1 ATOM 990 C CG2 . VAL A 1 125 ? -39.075 47.824 39.467 1.00 54.10 ? 125 VAL A CG2 1 ATOM 991 N N . ASP A 1 126 ? -35.779 45.971 40.734 1.00 58.65 ? 126 ASP A N 1 ATOM 992 C CA . ASP A 1 126 ? -34.418 45.921 40.202 1.00 62.91 ? 126 ASP A CA 1 ATOM 993 C C . ASP A 1 126 ? -34.370 45.739 38.673 1.00 66.45 ? 126 ASP A C 1 ATOM 994 O O . ASP A 1 126 ? -34.995 44.833 38.112 1.00 58.15 ? 126 ASP A O 1 ATOM 995 C CB . ASP A 1 126 ? -33.603 44.832 40.899 1.00 62.56 ? 126 ASP A CB 1 ATOM 996 C CG . ASP A 1 126 ? -32.129 44.894 40.548 1.00 72.03 ? 126 ASP A CG 1 ATOM 997 O OD1 . ASP A 1 126 ? -31.604 46.006 40.317 1.00 76.32 ? 126 ASP A OD1 1 ATOM 998 O OD2 . ASP A 1 126 ? -31.495 43.823 40.502 1.00 74.15 ? 126 ASP A OD2 1 ATOM 999 N N . THR A 1 127 ? -33.613 46.611 38.011 1.00 60.46 ? 127 THR A N 1 ATOM 1000 C CA . THR A 1 127 ? -33.525 46.628 36.557 1.00 56.01 ? 127 THR A CA 1 ATOM 1001 C C . THR A 1 127 ? -32.102 46.342 36.090 1.00 59.57 ? 127 THR A C 1 ATOM 1002 O O . THR A 1 127 ? -31.766 46.576 34.928 1.00 63.24 ? 127 THR A O 1 ATOM 1003 C CB . THR A 1 127 ? -33.963 47.999 35.989 1.00 58.00 ? 127 THR A CB 1 ATOM 1004 O OG1 . THR A 1 127 ? -33.028 49.010 36.392 1.00 56.20 ? 127 THR A OG1 1 ATOM 1005 C CG2 . THR A 1 127 ? -35.357 48.370 36.479 1.00 49.08 ? 127 THR A CG2 1 ATOM 1006 N N . SER A 1 128 ? -31.272 45.831 36.993 1.00 51.59 ? 128 SER A N 1 ATOM 1007 C CA . SER A 1 128 ? -29.852 45.652 36.705 1.00 54.55 ? 128 SER A CA 1 ATOM 1008 C C . SER A 1 128 ? -29.385 44.195 36.756 1.00 53.66 ? 128 SER A C 1 ATOM 1009 O O . SER A 1 128 ? -28.228 43.899 36.451 1.00 51.69 ? 128 SER A O 1 ATOM 1010 C CB . SER A 1 128 ? -29.013 46.511 37.658 1.00 56.43 ? 128 SER A CB 1 ATOM 1011 O OG . SER A 1 128 ? -29.467 46.386 38.997 1.00 60.89 ? 128 SER A OG 1 ATOM 1012 N N . ARG A 1 129 ? -30.286 43.292 37.132 1.00 76.90 ? 129 ARG A N 1 ATOM 1013 C CA . ARG A 1 129 ? -29.919 41.898 37.372 1.00 84.58 ? 129 ARG A CA 1 ATOM 1014 C C . ARG A 1 129 ? -30.658 40.951 36.422 1.00 82.98 ? 129 ARG A C 1 ATOM 1015 O O . ARG A 1 129 ? -30.651 39.731 36.612 1.00 78.82 ? 129 ARG A O 1 ATOM 1016 C CB . ARG A 1 129 ? -30.198 41.532 38.838 1.00 86.35 ? 129 ARG A CB 1 ATOM 1017 C CG . ARG A 1 129 ? -29.196 40.571 39.477 1.00 98.38 ? 129 ARG A CG 1 ATOM 1018 C CD . ARG A 1 129 ? -29.154 40.718 41.003 1.00 102.25 ? 129 ARG A CD 1 ATOM 1019 N NE . ARG A 1 129 ? -28.564 41.991 41.420 1.00 108.99 ? 129 ARG A NE 1 ATOM 1020 C CZ . ARG A 1 129 ? -29.216 42.940 42.086 1.00 109.18 ? 129 ARG A CZ 1 ATOM 1021 N NH1 . ARG A 1 129 ? -30.488 42.762 42.423 1.00 102.88 ? 129 ARG A NH1 1 ATOM 1022 N NH2 . ARG A 1 129 ? -28.600 44.069 42.417 1.00 101.94 ? 129 ARG A NH2 1 ATOM 1023 N N . GLY A 1 130 ? -31.280 41.520 35.391 1.00 77.62 ? 130 GLY A N 1 ATOM 1024 C CA . GLY A 1 130 ? -32.046 40.741 34.434 1.00 61.66 ? 130 GLY A CA 1 ATOM 1025 C C . GLY A 1 130 ? -31.229 40.187 33.280 1.00 64.20 ? 130 GLY A C 1 ATOM 1026 O O . GLY A 1 130 ? -31.435 40.574 32.123 1.00 61.09 ? 130 GLY A O 1 ATOM 1027 N N . VAL A 1 131 ? -30.310 39.273 33.591 1.00 53.46 ? 131 VAL A N 1 ATOM 1028 C CA . VAL A 1 131 ? -29.502 38.611 32.569 1.00 49.28 ? 131 VAL A CA 1 ATOM 1029 C C . VAL A 1 131 ? -29.638 37.090 32.647 1.00 53.10 ? 131 VAL A C 1 ATOM 1030 O O . VAL A 1 131 ? -30.259 36.558 33.569 1.00 51.42 ? 131 VAL A O 1 ATOM 1031 C CB . VAL A 1 131 ? -28.009 38.986 32.679 1.00 54.41 ? 131 VAL A CB 1 ATOM 1032 C CG1 . VAL A 1 131 ? -27.821 40.488 32.533 1.00 44.84 ? 131 VAL A CG1 1 ATOM 1033 C CG2 . VAL A 1 131 ? -27.434 38.501 34.006 1.00 53.32 ? 131 VAL A CG2 1 ATOM 1034 N N . THR A 1 132 ? -29.043 36.402 31.675 1.00 52.29 ? 132 THR A N 1 ATOM 1035 C CA . THR A 1 132 ? -29.114 34.948 31.588 1.00 49.69 ? 132 THR A CA 1 ATOM 1036 C C . THR A 1 132 ? -28.044 34.422 30.641 1.00 53.86 ? 132 THR A C 1 ATOM 1037 O O . THR A 1 132 ? -27.681 35.095 29.672 1.00 53.32 ? 132 THR A O 1 ATOM 1038 C CB . THR A 1 132 ? -30.501 34.475 31.089 1.00 49.22 ? 132 THR A CB 1 ATOM 1039 O OG1 . THR A 1 132 ? -30.451 33.074 30.787 1.00 51.60 ? 132 THR A OG1 1 ATOM 1040 C CG2 . THR A 1 132 ? -30.904 35.233 29.834 1.00 51.13 ? 132 THR A CG2 1 ATOM 1041 N N . ASN A 1 133 ? -27.532 33.226 30.919 1.00 52.10 ? 133 ASN A N 1 ATOM 1042 C CA . ASN A 1 133 ? -26.569 32.601 30.019 1.00 55.26 ? 133 ASN A CA 1 ATOM 1043 C C . ASN A 1 133 ? -27.249 31.942 28.822 1.00 56.86 ? 133 ASN A C 1 ATOM 1044 O O . ASN A 1 133 ? -26.594 31.334 27.971 1.00 51.49 ? 133 ASN A O 1 ATOM 1045 C CB . ASN A 1 133 ? -25.657 31.616 30.756 1.00 56.58 ? 133 ASN A CB 1 ATOM 1046 C CG . ASN A 1 133 ? -26.420 30.694 31.689 1.00 65.61 ? 133 ASN A CG 1 ATOM 1047 O OD1 . ASN A 1 133 ? -27.629 30.504 31.548 1.00 67.15 ? 133 ASN A OD1 1 ATOM 1048 N ND2 . ASN A 1 133 ? -25.710 30.112 32.652 1.00 65.86 ? 133 ASN A ND2 1 ATOM 1049 N N . ALA A 1 134 ? -28.570 32.070 28.764 1.00 63.84 ? 134 ALA A N 1 ATOM 1050 C CA . ALA A 1 134 ? -29.304 31.702 27.564 1.00 69.15 ? 134 ALA A CA 1 ATOM 1051 C C . ALA A 1 134 ? -29.033 32.747 26.484 1.00 64.02 ? 134 ALA A C 1 ATOM 1052 O O . ALA A 1 134 ? -29.018 32.432 25.294 1.00 59.89 ? 134 ALA A O 1 ATOM 1053 C CB . ALA A 1 134 ? -30.785 31.611 27.858 1.00 64.85 ? 134 ALA A CB 1 ATOM 1054 N N . CYS A 1 135 ? -28.812 33.991 26.911 1.00 55.19 ? 135 CYS A N 1 ATOM 1055 C CA . CYS A 1 135 ? -28.566 35.093 25.984 1.00 53.53 ? 135 CYS A CA 1 ATOM 1056 C C . CYS A 1 135 ? -27.201 35.735 26.197 1.00 53.06 ? 135 CYS A C 1 ATOM 1057 O O . CYS A 1 135 ? -27.108 36.825 26.758 1.00 52.84 ? 135 CYS A O 1 ATOM 1058 C CB . CYS A 1 135 ? -29.646 36.170 26.123 1.00 51.85 ? 135 CYS A CB 1 ATOM 1059 S SG . CYS A 1 135 ? -31.328 35.585 25.823 1.00 64.75 ? 135 CYS A SG 1 ATOM 1060 N N . PRO A 1 136 ? -26.134 35.073 25.730 1.00 44.80 ? 136 PRO A N 1 ATOM 1061 C CA . PRO A 1 136 ? -24.807 35.685 25.838 1.00 48.85 ? 136 PRO A CA 1 ATOM 1062 C C . PRO A 1 136 ? -24.582 36.740 24.761 1.00 52.66 ? 136 PRO A C 1 ATOM 1063 O O . PRO A 1 136 ? -25.163 36.637 23.677 1.00 51.42 ? 136 PRO A O 1 ATOM 1064 C CB . PRO A 1 136 ? -23.865 34.505 25.581 1.00 51.98 ? 136 PRO A CB 1 ATOM 1065 C CG . PRO A 1 136 ? -24.645 33.603 24.670 1.00 43.36 ? 136 PRO A CG 1 ATOM 1066 C CD . PRO A 1 136 ? -26.086 33.737 25.106 1.00 49.79 ? 136 PRO A CD 1 ATOM 1067 N N . SER A 1 137 ? -23.760 37.743 25.057 1.00 55.33 ? 137 SER A N 1 ATOM 1068 C CA . SER A 1 137 ? -23.233 38.614 24.014 1.00 50.46 ? 137 SER A CA 1 ATOM 1069 C C . SER A 1 137 ? -21.903 38.023 23.564 1.00 55.86 ? 137 SER A C 1 ATOM 1070 O O . SER A 1 137 ? -21.576 36.889 23.924 1.00 55.82 ? 137 SER A O 1 ATOM 1071 C CB . SER A 1 137 ? -23.054 40.048 24.516 1.00 52.55 ? 137 SER A CB 1 ATOM 1072 O OG . SER A 1 137 ? -22.037 40.144 25.495 1.00 61.03 ? 137 SER A OG 1 ATOM 1073 N N . TYR A 1 138 ? -21.137 38.773 22.780 1.00 55.98 ? 138 TYR A N 1 ATOM 1074 C CA . TYR A 1 138 ? -19.831 38.291 22.338 1.00 59.66 ? 138 TYR A CA 1 ATOM 1075 C C . TYR A 1 138 ? -18.744 38.560 23.387 1.00 62.30 ? 138 TYR A C 1 ATOM 1076 O O . TYR A 1 138 ? -17.585 38.187 23.202 1.00 60.23 ? 138 TYR A O 1 ATOM 1077 C CB . TYR A 1 138 ? -19.453 38.902 20.981 1.00 55.88 ? 138 TYR A CB 1 ATOM 1078 C CG . TYR A 1 138 ? -20.167 38.274 19.796 1.00 60.62 ? 138 TYR A CG 1 ATOM 1079 C CD1 . TYR A 1 138 ? -20.787 39.065 18.832 1.00 60.08 ? 138 TYR A CD1 1 ATOM 1080 C CD2 . TYR A 1 138 ? -20.209 36.894 19.634 1.00 60.25 ? 138 TYR A CD2 1 ATOM 1081 C CE1 . TYR A 1 138 ? -21.442 38.497 17.745 1.00 55.35 ? 138 TYR A CE1 1 ATOM 1082 C CE2 . TYR A 1 138 ? -20.860 36.316 18.551 1.00 61.53 ? 138 TYR A CE2 1 ATOM 1083 C CZ . TYR A 1 138 ? -21.474 37.121 17.610 1.00 64.60 ? 138 TYR A CZ 1 ATOM 1084 O OH . TYR A 1 138 ? -22.118 36.543 16.533 1.00 58.88 ? 138 TYR A OH 1 ATOM 1085 N N . THR A 1 139 ? -19.131 39.187 24.495 1.00 58.69 ? 139 THR A N 1 ATOM 1086 C CA . THR A 1 139 ? -18.177 39.562 25.539 1.00 63.75 ? 139 THR A CA 1 ATOM 1087 C C . THR A 1 139 ? -18.507 39.018 26.940 1.00 67.11 ? 139 THR A C 1 ATOM 1088 O O . THR A 1 139 ? -17.608 38.844 27.766 1.00 69.98 ? 139 THR A O 1 ATOM 1089 C CB . THR A 1 139 ? -17.975 41.092 25.595 1.00 63.49 ? 139 THR A CB 1 ATOM 1090 O OG1 . THR A 1 139 ? -19.245 41.743 25.720 1.00 66.38 ? 139 THR A OG1 1 ATOM 1091 C CG2 . THR A 1 139 ? -17.290 41.578 24.325 1.00 56.27 ? 139 THR A CG2 1 ATOM 1092 N N . LEU A 1 140 ? -19.785 38.759 27.209 1.00 67.29 ? 140 LEU A N 1 ATOM 1093 C CA . LEU A 1 140 ? -20.188 38.151 28.481 1.00 67.68 ? 140 LEU A CA 1 ATOM 1094 C C . LEU A 1 140 ? -21.102 36.944 28.293 1.00 69.21 ? 140 LEU A C 1 ATOM 1095 O O . LEU A 1 140 ? -21.888 36.885 27.342 1.00 64.92 ? 140 LEU A O 1 ATOM 1096 C CB . LEU A 1 140 ? -20.859 39.167 29.409 1.00 65.33 ? 140 LEU A CB 1 ATOM 1097 C CG . LEU A 1 140 ? -21.265 40.527 28.849 1.00 71.49 ? 140 LEU A CG 1 ATOM 1098 C CD1 . LEU A 1 140 ? -22.463 41.066 29.614 1.00 64.80 ? 140 LEU A CD1 1 ATOM 1099 C CD2 . LEU A 1 140 ? -20.104 41.513 28.928 1.00 76.08 ? 140 LEU A CD2 1 ATOM 1100 N N . ASP A 1 141 ? -21.001 35.992 29.216 1.00 78.79 ? 141 ASP A N 1 ATOM 1101 C CA . ASP A 1 141 ? -21.775 34.760 29.141 1.00 78.13 ? 141 ASP A CA 1 ATOM 1102 C C . ASP A 1 141 ? -23.241 34.998 29.485 1.00 70.45 ? 141 ASP A C 1 ATOM 1103 O O . ASP A 1 141 ? -24.110 34.237 29.067 1.00 69.46 ? 141 ASP A O 1 ATOM 1104 C CB . ASP A 1 141 ? -21.176 33.703 30.070 1.00 82.07 ? 141 ASP A CB 1 ATOM 1105 C CG . ASP A 1 141 ? -19.683 33.517 29.855 1.00 98.74 ? 141 ASP A CG 1 ATOM 1106 O OD1 . ASP A 1 141 ? -19.301 32.665 29.023 1.00 95.58 ? 141 ASP A OD1 1 ATOM 1107 O OD2 . ASP A 1 141 ? -18.891 34.228 30.515 1.00 100.93 ? 141 ASP A OD2 1 ATOM 1108 N N . SER A 1 142 ? -23.515 36.065 30.229 1.00 54.36 ? 142 SER A N 1 ATOM 1109 C CA . SER A 1 142 ? -24.883 36.361 30.641 1.00 54.29 ? 142 SER A CA 1 ATOM 1110 C C . SER A 1 142 ? -25.323 37.788 30.317 1.00 56.90 ? 142 SER A C 1 ATOM 1111 O O . SER A 1 142 ? -24.903 38.742 30.977 1.00 60.91 ? 142 SER A O 1 ATOM 1112 C CB . SER A 1 142 ? -25.060 36.080 32.134 1.00 54.15 ? 142 SER A CB 1 ATOM 1113 O OG . SER A 1 142 ? -24.789 34.720 32.420 1.00 54.61 ? 142 SER A OG 1 ATOM 1114 N N . SER A 1 143 ? -26.182 37.918 29.305 1.00 56.31 ? 143 SER A N 1 ATOM 1115 C CA . SER A 1 143 ? -26.742 39.211 28.907 1.00 56.34 ? 143 SER A CA 1 ATOM 1116 C C . SER A 1 143 ? -28.250 39.075 28.658 1.00 55.01 ? 143 SER A C 1 ATOM 1117 O O . SER A 1 143 ? -28.880 38.150 29.177 1.00 55.26 ? 143 SER A O 1 ATOM 1118 C CB . SER A 1 143 ? -26.031 39.738 27.658 1.00 51.75 ? 143 SER A CB 1 ATOM 1119 O OG . SER A 1 143 ? -26.200 41.136 27.536 1.00 54.57 ? 143 SER A OG 1 ATOM 1120 N N . PHE A 1 144 ? -28.822 39.988 27.873 1.00 48.13 ? 144 PHE A N 1 ATOM 1121 C CA . PHE A 1 144 ? -30.252 39.957 27.549 1.00 44.77 ? 144 PHE A CA 1 ATOM 1122 C C . PHE A 1 144 ? -30.555 40.864 26.362 1.00 46.40 ? 144 PHE A C 1 ATOM 1123 O O . PHE A 1 144 ? -29.698 41.641 25.934 1.00 45.70 ? 144 PHE A O 1 ATOM 1124 C CB . PHE A 1 144 ? -31.075 40.414 28.751 1.00 39.90 ? 144 PHE A CB 1 ATOM 1125 C CG . PHE A 1 144 ? -32.511 39.960 28.727 1.00 41.04 ? 144 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 144 ? -32.830 38.604 28.764 1.00 40.94 ? 144 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 144 ? -33.544 40.889 28.713 1.00 36.16 ? 144 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 144 ? -34.159 38.181 28.766 1.00 34.61 ? 144 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 144 ? -34.871 40.480 28.717 1.00 36.96 ? 144 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 144 ? -35.181 39.122 28.741 1.00 34.58 ? 144 PHE A CZ 1 ATOM 1131 N N . TYR A 1 145 ? -31.779 40.772 25.849 1.00 46.88 ? 145 TYR A N 1 ATOM 1132 C CA . TYR A 1 145 ? -32.222 41.589 24.726 1.00 47.23 ? 145 TYR A CA 1 ATOM 1133 C C . TYR A 1 145 ? -32.052 43.089 24.987 1.00 46.22 ? 145 TYR A C 1 ATOM 1134 O O . TYR A 1 145 ? -32.422 43.585 26.051 1.00 48.96 ? 145 TYR A O 1 ATOM 1135 C CB . TYR A 1 145 ? -33.680 41.261 24.398 1.00 45.97 ? 145 TYR A CB 1 ATOM 1136 C CG . TYR A 1 145 ? -33.920 39.787 24.150 1.00 44.35 ? 145 TYR A CG 1 ATOM 1137 C CD1 . TYR A 1 145 ? -33.631 39.217 22.920 1.00 43.29 ? 145 TYR A CD1 1 ATOM 1138 C CD2 . TYR A 1 145 ? -34.434 38.966 25.147 1.00 44.64 ? 145 TYR A CD2 1 ATOM 1139 C CE1 . TYR A 1 145 ? -33.846 37.869 22.686 1.00 44.38 ? 145 TYR A CE1 1 ATOM 1140 C CE2 . TYR A 1 145 ? -34.656 37.615 24.920 1.00 45.59 ? 145 TYR A CE2 1 ATOM 1141 C CZ . TYR A 1 145 ? -34.361 37.075 23.688 1.00 44.43 ? 145 TYR A CZ 1 ATOM 1142 O OH . TYR A 1 145 ? -34.578 35.736 23.454 1.00 45.84 ? 145 TYR A OH 1 ATOM 1143 N N . ARG A 1 146 ? -31.479 43.796 24.014 1.00 45.86 ? 146 ARG A N 1 ATOM 1144 C CA . ARG A 1 146 ? -31.208 45.229 24.133 1.00 48.69 ? 146 ARG A CA 1 ATOM 1145 C C . ARG A 1 146 ? -32.489 46.063 24.225 1.00 49.28 ? 146 ARG A C 1 ATOM 1146 O O . ARG A 1 146 ? -32.474 47.169 24.769 1.00 52.12 ? 146 ARG A O 1 ATOM 1147 C CB . ARG A 1 146 ? -30.371 45.723 22.940 1.00 48.59 ? 146 ARG A CB 1 ATOM 1148 C CG . ARG A 1 146 ? -29.092 44.930 22.657 1.00 50.13 ? 146 ARG A CG 1 ATOM 1149 C CD . ARG A 1 146 ? -28.059 45.085 23.757 1.00 53.48 ? 146 ARG A CD 1 ATOM 1150 N NE . ARG A 1 146 ? -26.863 44.275 23.517 1.00 58.56 ? 146 ARG A NE 1 ATOM 1151 C CZ . ARG A 1 146 ? -25.971 43.962 24.454 1.00 60.22 ? 146 ARG A CZ 1 ATOM 1152 N NH1 . ARG A 1 146 ? -26.143 44.384 25.699 1.00 55.59 ? 146 ARG A NH1 1 ATOM 1153 N NH2 . ARG A 1 146 ? -24.914 43.220 24.149 1.00 54.08 ? 146 ARG A NH2 1 ATOM 1154 N N . ASN A 1 147 ? -33.589 45.536 23.687 1.00 44.26 ? 147 ASN A N 1 ATOM 1155 C CA . ASN A 1 147 ? -34.848 46.278 23.629 1.00 43.41 ? 147 ASN A CA 1 ATOM 1156 C C . ASN A 1 147 ? -35.824 45.899 24.738 1.00 45.33 ? 147 ASN A C 1 ATOM 1157 O O . ASN A 1 147 ? -36.915 46.464 24.842 1.00 40.99 ? 147 ASN A O 1 ATOM 1158 C CB . ASN A 1 147 ? -35.517 46.098 22.263 1.00 39.41 ? 147 ASN A CB 1 ATOM 1159 C CG . ASN A 1 147 ? -34.646 46.580 21.125 1.00 45.46 ? 147 ASN A CG 1 ATOM 1160 O OD1 . ASN A 1 147 ? -33.854 47.513 21.288 1.00 41.50 ? 147 ASN A OD1 1 ATOM 1161 N ND2 . ASN A 1 147 ? -34.785 45.945 19.961 1.00 40.22 ? 147 ASN A ND2 1 ATOM 1162 N N . LEU A 1 148 ? -35.427 44.936 25.560 1.00 48.51 ? 148 LEU A N 1 ATOM 1163 C CA . LEU A 1 148 ? -36.255 44.504 26.675 1.00 49.87 ? 148 LEU A CA 1 ATOM 1164 C C . LEU A 1 148 ? -35.476 44.587 27.985 1.00 49.65 ? 148 LEU A C 1 ATOM 1165 O O . LEU A 1 148 ? -34.241 44.566 27.989 1.00 50.93 ? 148 LEU A O 1 ATOM 1166 C CB . LEU A 1 148 ? -36.750 43.076 26.445 1.00 48.68 ? 148 LEU A CB 1 ATOM 1167 C CG . LEU A 1 148 ? -37.639 42.883 25.219 1.00 48.90 ? 148 LEU A CG 1 ATOM 1168 C CD1 . LEU A 1 148 ? -38.101 41.438 25.106 1.00 45.32 ? 148 LEU A CD1 1 ATOM 1169 C CD2 . LEU A 1 148 ? -38.831 43.822 25.291 1.00 47.25 ? 148 LEU A CD2 1 ATOM 1170 N N . VAL A 1 149 ? -36.190 44.694 29.098 1.00 41.96 ? 149 VAL A N 1 ATOM 1171 C CA . VAL A 1 149 ? -35.533 44.636 30.397 1.00 46.78 ? 149 VAL A CA 1 ATOM 1172 C C . VAL A 1 149 ? -36.240 43.670 31.345 1.00 40.42 ? 149 VAL A C 1 ATOM 1173 O O . VAL A 1 149 ? -37.432 43.811 31.627 1.00 38.87 ? 149 VAL A O 1 ATOM 1174 C CB . VAL A 1 149 ? -35.356 46.036 31.035 1.00 47.44 ? 149 VAL A CB 1 ATOM 1175 C CG1 . VAL A 1 149 ? -36.655 46.824 30.996 1.00 47.95 ? 149 VAL A CG1 1 ATOM 1176 C CG2 . VAL A 1 149 ? -34.839 45.904 32.457 1.00 46.74 ? 149 VAL A CG2 1 ATOM 1177 N N . TRP A 1 150 ? -35.491 42.676 31.811 1.00 41.02 ? 150 TRP A N 1 ATOM 1178 C CA . TRP A 1 150 ? -36.014 41.669 32.723 1.00 47.58 ? 150 TRP A CA 1 ATOM 1179 C C . TRP A 1 150 ? -36.048 42.237 34.141 1.00 48.30 ? 150 TRP A C 1 ATOM 1180 O O . TRP A 1 150 ? -35.001 42.446 34.758 1.00 54.13 ? 150 TRP A O 1 ATOM 1181 C CB . TRP A 1 150 ? -35.127 40.425 32.659 1.00 47.87 ? 150 TRP A CB 1 ATOM 1182 C CG . TRP A 1 150 ? -35.680 39.211 33.331 1.00 46.27 ? 150 TRP A CG 1 ATOM 1183 C CD1 . TRP A 1 150 ? -36.705 39.156 34.232 1.00 45.28 ? 150 TRP A CD1 1 ATOM 1184 C CD2 . TRP A 1 150 ? -35.233 37.861 33.145 1.00 44.94 ? 150 TRP A CD2 1 ATOM 1185 N NE1 . TRP A 1 150 ? -36.919 37.855 34.619 1.00 44.20 ? 150 TRP A NE1 1 ATOM 1186 C CE2 . TRP A 1 150 ? -36.030 37.043 33.968 1.00 46.15 ? 150 TRP A CE2 1 ATOM 1187 C CE3 . TRP A 1 150 ? -34.235 37.271 32.363 1.00 46.97 ? 150 TRP A CE3 1 ATOM 1188 C CZ2 . TRP A 1 150 ? -35.860 35.656 34.029 1.00 50.17 ? 150 TRP A CZ2 1 ATOM 1189 C CZ3 . TRP A 1 150 ? -34.065 35.897 32.426 1.00 51.49 ? 150 TRP A CZ3 1 ATOM 1190 C CH2 . TRP A 1 150 ? -34.874 35.105 33.253 1.00 51.75 ? 150 TRP A CH2 1 ATOM 1191 N N . LEU A 1 151 ? -37.253 42.492 34.647 1.00 56.80 ? 151 LEU A N 1 ATOM 1192 C CA . LEU A 1 151 ? -37.423 43.106 35.962 1.00 60.53 ? 151 LEU A CA 1 ATOM 1193 C C . LEU A 1 151 ? -37.498 42.054 37.068 1.00 62.94 ? 151 LEU A C 1 ATOM 1194 O O . LEU A 1 151 ? -38.267 41.096 36.979 1.00 63.78 ? 151 LEU A O 1 ATOM 1195 C CB . LEU A 1 151 ? -38.667 43.998 35.985 1.00 60.42 ? 151 LEU A CB 1 ATOM 1196 C CG . LEU A 1 151 ? -38.689 45.031 34.857 1.00 61.37 ? 151 LEU A CG 1 ATOM 1197 C CD1 . LEU A 1 151 ? -39.910 45.939 34.904 1.00 56.18 ? 151 LEU A CD1 1 ATOM 1198 C CD2 . LEU A 1 151 ? -37.428 45.856 34.921 1.00 67.30 ? 151 LEU A CD2 1 ATOM 1199 N N . VAL A 1 152 ? -36.680 42.241 38.101 1.00 63.06 ? 152 VAL A N 1 ATOM 1200 C CA . VAL A 1 152 ? -36.670 41.365 39.271 1.00 64.21 ? 152 VAL A CA 1 ATOM 1201 C C . VAL A 1 152 ? -36.921 42.211 40.525 1.00 60.80 ? 152 VAL A C 1 ATOM 1202 O O . VAL A 1 152 ? -36.498 43.370 40.583 1.00 57.98 ? 152 VAL A O 1 ATOM 1203 C CB . VAL A 1 152 ? -35.326 40.604 39.373 1.00 62.80 ? 152 VAL A CB 1 ATOM 1204 C CG1 . VAL A 1 152 ? -35.230 39.826 40.672 1.00 74.47 ? 152 VAL A CG1 1 ATOM 1205 C CG2 . VAL A 1 152 ? -35.161 39.661 38.189 1.00 62.25 ? 152 VAL A CG2 1 ATOM 1206 N N . LYS A 1 153 ? -37.624 41.654 41.512 1.00 60.25 ? 153 LYS A N 1 ATOM 1207 C CA . LYS A 1 153 ? -37.853 42.368 42.772 1.00 65.99 ? 153 LYS A CA 1 ATOM 1208 C C . LYS A 1 153 ? -36.524 42.659 43.480 1.00 63.97 ? 153 LYS A C 1 ATOM 1209 O O . LYS A 1 153 ? -35.529 41.959 43.264 1.00 57.23 ? 153 LYS A O 1 ATOM 1210 C CB . LYS A 1 153 ? -38.810 41.594 43.688 1.00 63.81 ? 153 LYS A CB 1 ATOM 1211 C CG . LYS A 1 153 ? -38.159 40.485 44.508 1.00 65.74 ? 153 LYS A CG 1 ATOM 1212 C CD . LYS A 1 153 ? -39.201 39.690 45.294 1.00 67.18 ? 153 LYS A CD 1 ATOM 1213 C CE . LYS A 1 153 ? -38.571 38.932 46.464 1.00 75.99 ? 153 LYS A CE 1 ATOM 1214 N NZ . LYS A 1 153 ? -37.428 38.067 46.055 1.00 74.21 ? 153 LYS A NZ 1 ATOM 1215 N N . THR A 1 154 ? -36.508 43.700 44.309 1.00 73.54 ? 154 THR A N 1 ATOM 1216 C CA . THR A 1 154 ? -35.275 44.150 44.963 1.00 85.98 ? 154 THR A CA 1 ATOM 1217 C C . THR A 1 154 ? -34.882 43.349 46.211 1.00 90.58 ? 154 THR A C 1 ATOM 1218 O O . THR A 1 154 ? -35.708 42.643 46.793 1.00 89.26 ? 154 THR A O 1 ATOM 1219 C CB . THR A 1 154 ? -35.345 45.645 45.330 1.00 85.32 ? 154 THR A CB 1 ATOM 1220 O OG1 . THR A 1 154 ? -36.716 46.048 45.441 1.00 83.52 ? 154 THR A OG1 1 ATOM 1221 C CG2 . THR A 1 154 ? -34.658 46.489 44.264 1.00 75.68 ? 154 THR A CG2 1 ATOM 1222 N N . ASP A 1 155 ? -33.608 43.489 46.591 1.00 130.17 ? 155 ASP A N 1 ATOM 1223 C CA . ASP A 1 155 ? -32.977 42.876 47.778 1.00 140.83 ? 155 ASP A CA 1 ATOM 1224 C C . ASP A 1 155 ? -33.718 41.758 48.535 1.00 139.56 ? 155 ASP A C 1 ATOM 1225 O O . ASP A 1 155 ? -33.227 40.629 48.619 1.00 139.91 ? 155 ASP A O 1 ATOM 1226 C CB . ASP A 1 155 ? -32.508 43.964 48.765 1.00 141.38 ? 155 ASP A CB 1 ATOM 1227 C CG . ASP A 1 155 ? -33.647 44.854 49.260 1.00 144.67 ? 155 ASP A CG 1 ATOM 1228 O OD1 . ASP A 1 155 ? -34.781 44.354 49.442 1.00 135.75 ? 155 ASP A OD1 1 ATOM 1229 O OD2 . ASP A 1 155 ? -33.400 46.061 49.478 1.00 143.59 ? 155 ASP A OD2 1 ATOM 1230 N N . SER A 1 156 ? -34.882 42.089 49.092 1.00 114.41 ? 156 SER A N 1 ATOM 1231 C CA . SER A 1 156 ? -35.646 41.165 49.929 1.00 114.37 ? 156 SER A CA 1 ATOM 1232 C C . SER A 1 156 ? -37.106 41.604 50.039 1.00 109.40 ? 156 SER A C 1 ATOM 1233 O O . SER A 1 156 ? -37.931 40.905 50.629 1.00 106.45 ? 156 SER A O 1 ATOM 1234 C CB . SER A 1 156 ? -35.035 41.083 51.333 1.00 117.98 ? 156 SER A CB 1 ATOM 1235 O OG . SER A 1 156 ? -33.688 40.641 51.301 1.00 117.68 ? 156 SER A OG 1 ATOM 1236 N N . ALA A 1 157 ? -37.418 42.765 49.472 1.00 90.82 ? 157 ALA A N 1 ATOM 1237 C CA . ALA A 1 157 ? -38.762 43.332 49.560 1.00 88.44 ? 157 ALA A CA 1 ATOM 1238 C C . ALA A 1 157 ? -39.777 42.530 48.744 1.00 89.66 ? 157 ALA A C 1 ATOM 1239 O O . ALA A 1 157 ? -39.485 41.430 48.275 1.00 91.58 ? 157 ALA A O 1 ATOM 1240 C CB . ALA A 1 157 ? -38.747 44.778 49.104 1.00 85.00 ? 157 ALA A CB 1 ATOM 1241 N N . THR A 1 158 ? -40.975 43.084 48.578 1.00 84.46 ? 158 THR A N 1 ATOM 1242 C CA . THR A 1 158 ? -41.962 42.501 47.673 1.00 76.64 ? 158 THR A CA 1 ATOM 1243 C C . THR A 1 158 ? -41.850 43.177 46.311 1.00 74.78 ? 158 THR A C 1 ATOM 1244 O O . THR A 1 158 ? -41.265 44.254 46.198 1.00 73.64 ? 158 THR A O 1 ATOM 1245 C CB . THR A 1 158 ? -43.405 42.665 48.197 1.00 75.58 ? 158 THR A CB 1 ATOM 1246 O OG1 . THR A 1 158 ? -43.774 44.051 48.186 1.00 73.61 ? 158 THR A OG1 1 ATOM 1247 C CG2 . THR A 1 158 ? -43.526 42.116 49.606 1.00 73.15 ? 158 THR A CG2 1 ATOM 1248 N N . TYR A 1 159 ? -42.397 42.539 45.279 1.00 81.92 ? 159 TYR A N 1 ATOM 1249 C CA . TYR A 1 159 ? -42.497 43.159 43.961 1.00 72.98 ? 159 TYR A CA 1 ATOM 1250 C C . TYR A 1 159 ? -43.776 43.995 43.970 1.00 70.91 ? 159 TYR A C 1 ATOM 1251 O O . TYR A 1 159 ? -44.885 43.447 43.980 1.00 68.40 ? 159 TYR A O 1 ATOM 1252 C CB . TYR A 1 159 ? -42.551 42.077 42.879 1.00 69.92 ? 159 TYR A CB 1 ATOM 1253 C CG . TYR A 1 159 ? -42.276 42.522 41.452 1.00 68.77 ? 159 TYR A CG 1 ATOM 1254 C CD1 . TYR A 1 159 ? -41.353 41.842 40.667 1.00 67.57 ? 159 TYR A CD1 1 ATOM 1255 C CD2 . TYR A 1 159 ? -42.965 43.584 40.877 1.00 66.98 ? 159 TYR A CD2 1 ATOM 1256 C CE1 . TYR A 1 159 ? -41.104 42.222 39.362 1.00 63.43 ? 159 TYR A CE1 1 ATOM 1257 C CE2 . TYR A 1 159 ? -42.727 43.969 39.569 1.00 64.39 ? 159 TYR A CE2 1 ATOM 1258 C CZ . TYR A 1 159 ? -41.795 43.285 38.816 1.00 65.62 ? 159 TYR A CZ 1 ATOM 1259 O OH . TYR A 1 159 ? -41.552 43.668 37.515 1.00 64.74 ? 159 TYR A OH 1 ATOM 1260 N N . PRO A 1 160 ? -43.625 45.329 43.992 1.00 58.09 ? 160 PRO A N 1 ATOM 1261 C CA . PRO A 1 160 ? -44.782 46.226 44.092 1.00 59.64 ? 160 PRO A CA 1 ATOM 1262 C C . PRO A 1 160 ? -45.448 46.400 42.733 1.00 60.92 ? 160 PRO A C 1 ATOM 1263 O O . PRO A 1 160 ? -44.995 45.797 41.759 1.00 58.84 ? 160 PRO A O 1 ATOM 1264 C CB . PRO A 1 160 ? -44.147 47.545 44.530 1.00 56.84 ? 160 PRO A CB 1 ATOM 1265 C CG . PRO A 1 160 ? -42.790 47.525 43.876 1.00 58.58 ? 160 PRO A CG 1 ATOM 1266 C CD . PRO A 1 160 ? -42.355 46.072 43.873 1.00 57.87 ? 160 PRO A CD 1 ATOM 1267 N N . VAL A 1 161 ? -46.507 47.201 42.664 1.00 62.29 ? 161 VAL A N 1 ATOM 1268 C CA . VAL A 1 161 ? -47.125 47.512 41.379 1.00 59.64 ? 161 VAL A CA 1 ATOM 1269 C C . VAL A 1 161 ? -46.315 48.597 40.675 1.00 62.05 ? 161 VAL A C 1 ATOM 1270 O O . VAL A 1 161 ? -46.223 49.729 41.157 1.00 60.87 ? 161 VAL A O 1 ATOM 1271 C CB . VAL A 1 161 ? -48.591 47.973 41.527 1.00 57.94 ? 161 VAL A CB 1 ATOM 1272 C CG1 . VAL A 1 161 ? -49.171 48.340 40.174 1.00 55.44 ? 161 VAL A CG1 1 ATOM 1273 C CG2 . VAL A 1 161 ? -49.429 46.881 42.172 1.00 59.20 ? 161 VAL A CG2 1 ATOM 1274 N N . ILE A 1 162 ? -45.717 48.241 39.542 1.00 61.67 ? 162 ILE A N 1 ATOM 1275 C CA . ILE A 1 162 ? -44.965 49.198 38.739 1.00 59.05 ? 162 ILE A CA 1 ATOM 1276 C C . ILE A 1 162 ? -45.829 49.675 37.574 1.00 57.75 ? 162 ILE A C 1 ATOM 1277 O O . ILE A 1 162 ? -46.702 48.942 37.102 1.00 55.63 ? 162 ILE A O 1 ATOM 1278 C CB . ILE A 1 162 ? -43.665 48.585 38.206 1.00 58.25 ? 162 ILE A CB 1 ATOM 1279 C CG1 . ILE A 1 162 ? -43.966 47.340 37.373 1.00 54.30 ? 162 ILE A CG1 1 ATOM 1280 C CG2 . ILE A 1 162 ? -42.735 48.228 39.357 1.00 54.33 ? 162 ILE A CG2 1 ATOM 1281 C CD1 . ILE A 1 162 ? -42.728 46.596 36.932 1.00 50.86 ? 162 ILE A CD1 1 ATOM 1282 N N . LYS A 1 163 ? -45.592 50.902 37.118 1.00 55.36 ? 163 LYS A N 1 ATOM 1283 C CA . LYS A 1 163 ? -46.399 51.482 36.048 1.00 55.02 ? 163 LYS A CA 1 ATOM 1284 C C . LYS A 1 163 ? -45.555 52.262 35.049 1.00 56.05 ? 163 LYS A C 1 ATOM 1285 O O . LYS A 1 163 ? -44.474 52.754 35.385 1.00 55.63 ? 163 LYS A O 1 ATOM 1286 C CB . LYS A 1 163 ? -47.483 52.395 36.625 1.00 54.11 ? 163 LYS A CB 1 ATOM 1287 C CG . LYS A 1 163 ? -48.625 51.669 37.311 1.00 56.74 ? 163 LYS A CG 1 ATOM 1288 C CD . LYS A 1 163 ? -49.685 52.656 37.781 1.00 60.03 ? 163 LYS A CD 1 ATOM 1289 C CE . LYS A 1 163 ? -50.830 51.946 38.490 1.00 69.00 ? 163 LYS A CE 1 ATOM 1290 N NZ . LYS A 1 163 ? -51.812 52.909 39.070 1.00 68.56 ? 163 LYS A NZ 1 ATOM 1291 N N . GLY A 1 164 ? -46.064 52.381 33.827 1.00 46.73 ? 164 GLY A N 1 ATOM 1292 C CA . GLY A 1 164 ? -45.366 53.093 32.774 1.00 42.43 ? 164 GLY A CA 1 ATOM 1293 C C . GLY A 1 164 ? -46.348 53.658 31.770 1.00 44.21 ? 164 GLY A C 1 ATOM 1294 O O . GLY A 1 164 ? -47.431 53.100 31.561 1.00 44.29 ? 164 GLY A O 1 ATOM 1295 N N . THR A 1 165 ? -45.976 54.771 31.148 1.00 49.61 ? 165 THR A N 1 ATOM 1296 C CA . THR A 1 165 ? -46.831 55.401 30.152 1.00 52.06 ? 165 THR A CA 1 ATOM 1297 C C . THR A 1 165 ? -45.990 56.028 29.038 1.00 52.58 ? 165 THR A C 1 ATOM 1298 O O . THR A 1 165 ? -44.967 56.668 29.302 1.00 50.77 ? 165 THR A O 1 ATOM 1299 C CB . THR A 1 165 ? -47.739 56.466 30.802 1.00 55.73 ? 165 THR A CB 1 ATOM 1300 O OG1 . THR A 1 165 ? -48.569 55.847 31.795 1.00 62.12 ? 165 THR A OG1 1 ATOM 1301 C CG2 . THR A 1 165 ? -48.622 57.142 29.762 1.00 52.57 ? 165 THR A CG2 1 ATOM 1302 N N . TYR A 1 166 ? -46.405 55.821 27.794 1.00 42.44 ? 166 TYR A N 1 ATOM 1303 C CA . TYR A 1 166 ? -45.802 56.532 26.678 1.00 44.37 ? 166 TYR A CA 1 ATOM 1304 C C . TYR A 1 166 ? -46.894 57.086 25.772 1.00 47.66 ? 166 TYR A C 1 ATOM 1305 O O . TYR A 1 166 ? -47.800 56.359 25.365 1.00 48.01 ? 166 TYR A O 1 ATOM 1306 C CB . TYR A 1 166 ? -44.854 55.630 25.887 1.00 41.99 ? 166 TYR A CB 1 ATOM 1307 C CG . TYR A 1 166 ? -44.125 56.366 24.791 1.00 43.66 ? 166 TYR A CG 1 ATOM 1308 C CD1 . TYR A 1 166 ? -44.655 56.446 23.511 1.00 43.10 ? 166 TYR A CD1 1 ATOM 1309 C CD2 . TYR A 1 166 ? -42.909 56.990 25.039 1.00 39.82 ? 166 TYR A CD2 1 ATOM 1310 C CE1 . TYR A 1 166 ? -43.998 57.124 22.508 1.00 44.10 ? 166 TYR A CE1 1 ATOM 1311 C CE2 . TYR A 1 166 ? -42.239 57.671 24.039 1.00 41.23 ? 166 TYR A CE2 1 ATOM 1312 C CZ . TYR A 1 166 ? -42.790 57.733 22.774 1.00 45.51 ? 166 TYR A CZ 1 ATOM 1313 O OH . TYR A 1 166 ? -42.137 58.409 21.768 1.00 45.59 ? 166 TYR A OH 1 ATOM 1314 N N . ASN A 1 167 ? -46.804 58.375 25.466 1.00 52.32 ? 167 ASN A N 1 ATOM 1315 C CA . ASN A 1 167 ? -47.754 59.028 24.576 1.00 50.07 ? 167 ASN A CA 1 ATOM 1316 C C . ASN A 1 167 ? -47.092 59.293 23.225 1.00 53.06 ? 167 ASN A C 1 ATOM 1317 O O . ASN A 1 167 ? -46.177 60.115 23.130 1.00 53.45 ? 167 ASN A O 1 ATOM 1318 C CB . ASN A 1 167 ? -48.233 60.335 25.220 1.00 57.54 ? 167 ASN A CB 1 ATOM 1319 C CG . ASN A 1 167 ? -49.251 61.083 24.372 1.00 64.44 ? 167 ASN A CG 1 ATOM 1320 O OD1 . ASN A 1 167 ? -49.731 60.582 23.350 1.00 59.76 ? 167 ASN A OD1 1 ATOM 1321 N ND2 . ASN A 1 167 ? -49.582 62.305 24.803 1.00 64.02 ? 167 ASN A ND2 1 ATOM 1322 N N . ASN A 1 168 ? -47.540 58.583 22.189 1.00 47.30 ? 168 ASN A N 1 ATOM 1323 C CA . ASN A 1 168 ? -47.017 58.776 20.838 1.00 42.76 ? 168 ASN A CA 1 ATOM 1324 C C . ASN A 1 168 ? -47.498 60.107 20.268 1.00 47.18 ? 168 ASN A C 1 ATOM 1325 O O . ASN A 1 168 ? -48.607 60.213 19.735 1.00 48.08 ? 168 ASN A O 1 ATOM 1326 C CB . ASN A 1 168 ? -47.429 57.621 19.920 1.00 43.24 ? 168 ASN A CB 1 ATOM 1327 C CG . ASN A 1 168 ? -46.669 57.614 18.595 1.00 41.27 ? 168 ASN A CG 1 ATOM 1328 O OD1 . ASN A 1 168 ? -46.022 58.596 18.222 1.00 42.88 ? 168 ASN A OD1 1 ATOM 1329 N ND2 . ASN A 1 168 ? -46.758 56.499 17.872 1.00 36.79 ? 168 ASN A ND2 1 ATOM 1330 N N . THR A 1 169 ? -46.649 61.121 20.391 1.00 50.82 ? 169 THR A N 1 ATOM 1331 C CA . THR A 1 169 ? -46.957 62.458 19.905 1.00 56.07 ? 169 THR A CA 1 ATOM 1332 C C . THR A 1 169 ? -46.331 62.681 18.531 1.00 59.85 ? 169 THR A C 1 ATOM 1333 O O . THR A 1 169 ? -46.469 63.755 17.941 1.00 62.98 ? 169 THR A O 1 ATOM 1334 C CB . THR A 1 169 ? -46.474 63.540 20.898 1.00 60.92 ? 169 THR A CB 1 ATOM 1335 O OG1 . THR A 1 169 ? -45.076 63.363 21.166 1.00 58.60 ? 169 THR A OG1 1 ATOM 1336 C CG2 . THR A 1 169 ? -47.248 63.445 22.209 1.00 51.49 ? 169 THR A CG2 1 ATOM 1337 N N . GLY A 1 170 ? -45.647 61.656 18.027 1.00 50.14 ? 170 GLY A N 1 ATOM 1338 C CA . GLY A 1 170 ? -45.022 61.729 16.719 1.00 46.65 ? 170 GLY A CA 1 ATOM 1339 C C . GLY A 1 170 ? -45.976 61.429 15.575 1.00 49.18 ? 170 GLY A C 1 ATOM 1340 O O . GLY A 1 170 ? -47.173 61.207 15.790 1.00 51.51 ? 170 GLY A O 1 ATOM 1341 N N . THR A 1 171 ? -45.435 61.422 14.357 1.00 49.11 ? 171 THR A N 1 ATOM 1342 C CA . THR A 1 171 ? -46.212 61.160 13.147 1.00 51.78 ? 171 THR A CA 1 ATOM 1343 C C . THR A 1 171 ? -46.114 59.703 12.690 1.00 53.36 ? 171 THR A C 1 ATOM 1344 O O . THR A 1 171 ? -46.842 59.284 11.784 1.00 49.86 ? 171 THR A O 1 ATOM 1345 C CB . THR A 1 171 ? -45.749 62.055 11.980 1.00 58.60 ? 171 THR A CB 1 ATOM 1346 O OG1 . THR A 1 171 ? -44.340 61.878 11.765 1.00 54.30 ? 171 THR A OG1 1 ATOM 1347 C CG2 . THR A 1 171 ? -46.041 63.518 12.270 1.00 52.92 ? 171 THR A CG2 1 ATOM 1348 N N . GLN A 1 172 ? -45.206 58.945 13.303 1.00 46.04 ? 172 GLN A N 1 ATOM 1349 C CA . GLN A 1 172 ? -44.956 57.563 12.899 1.00 46.25 ? 172 GLN A CA 1 ATOM 1350 C C . GLN A 1 172 ? -45.520 56.552 13.902 1.00 42.20 ? 172 GLN A C 1 ATOM 1351 O O . GLN A 1 172 ? -45.510 56.793 15.113 1.00 44.66 ? 172 GLN A O 1 ATOM 1352 C CB . GLN A 1 172 ? -43.451 57.314 12.724 1.00 46.45 ? 172 GLN A CB 1 ATOM 1353 C CG . GLN A 1 172 ? -42.734 58.287 11.792 1.00 51.73 ? 172 GLN A CG 1 ATOM 1354 C CD . GLN A 1 172 ? -41.434 58.815 12.388 1.00 65.40 ? 172 GLN A CD 1 ATOM 1355 O OE1 . GLN A 1 172 ? -40.393 58.836 11.721 1.00 64.14 ? 172 GLN A OE1 1 ATOM 1356 N NE2 . GLN A 1 172 ? -41.491 59.254 13.650 1.00 56.35 ? 172 GLN A NE2 1 ATOM 1357 N N . PRO A 1 173 ? -46.019 55.413 13.396 1.00 37.02 ? 173 PRO A N 1 ATOM 1358 C CA . PRO A 1 173 ? -46.417 54.311 14.280 1.00 36.38 ? 173 PRO A CA 1 ATOM 1359 C C . PRO A 1 173 ? -45.186 53.723 14.968 1.00 35.82 ? 173 PRO A C 1 ATOM 1360 O O . PRO A 1 173 ? -44.090 53.774 14.401 1.00 33.52 ? 173 PRO A O 1 ATOM 1361 C CB . PRO A 1 173 ? -47.027 53.287 13.314 1.00 36.35 ? 173 PRO A CB 1 ATOM 1362 C CG . PRO A 1 173 ? -46.452 53.627 11.966 1.00 31.53 ? 173 PRO A CG 1 ATOM 1363 C CD . PRO A 1 173 ? -46.292 55.119 11.977 1.00 32.66 ? 173 PRO A CD 1 ATOM 1364 N N . ILE A 1 174 ? -45.362 53.183 16.171 1.00 36.77 ? 174 ILE A N 1 ATOM 1365 C CA . ILE A 1 174 ? -44.243 52.653 16.943 1.00 34.56 ? 174 ILE A CA 1 ATOM 1366 C C . ILE A 1 174 ? -44.350 51.143 17.149 1.00 34.27 ? 174 ILE A C 1 ATOM 1367 O O . ILE A 1 174 ? -45.321 50.658 17.738 1.00 33.91 ? 174 ILE A O 1 ATOM 1368 C CB . ILE A 1 174 ? -44.134 53.356 18.316 1.00 37.63 ? 174 ILE A CB 1 ATOM 1369 C CG1 . ILE A 1 174 ? -43.708 54.813 18.123 1.00 38.80 ? 174 ILE A CG1 1 ATOM 1370 C CG2 . ILE A 1 174 ? -43.143 52.627 19.229 1.00 32.11 ? 174 ILE A CG2 1 ATOM 1371 C CD1 . ILE A 1 174 ? -43.705 55.624 19.389 1.00 39.20 ? 174 ILE A CD1 1 ATOM 1372 N N . LEU A 1 175 ? -43.351 50.404 16.668 1.00 34.58 ? 175 LEU A N 1 ATOM 1373 C CA . LEU A 1 175 ? -43.300 48.957 16.877 1.00 38.00 ? 175 LEU A CA 1 ATOM 1374 C C . LEU A 1 175 ? -42.558 48.651 18.173 1.00 37.12 ? 175 LEU A C 1 ATOM 1375 O O . LEU A 1 175 ? -41.392 49.031 18.333 1.00 39.82 ? 175 LEU A O 1 ATOM 1376 C CB . LEU A 1 175 ? -42.612 48.265 15.692 1.00 36.21 ? 175 LEU A CB 1 ATOM 1377 C CG . LEU A 1 175 ? -42.372 46.752 15.758 1.00 36.79 ? 175 LEU A CG 1 ATOM 1378 C CD1 . LEU A 1 175 ? -43.688 45.998 15.830 1.00 31.52 ? 175 LEU A CD1 1 ATOM 1379 C CD2 . LEU A 1 175 ? -41.553 46.280 14.560 1.00 30.66 ? 175 LEU A CD2 1 ATOM 1380 N N . TYR A 1 176 ? -43.226 47.979 19.106 1.00 34.19 ? 176 TYR A N 1 ATOM 1381 C CA . TYR A 1 176 ? -42.602 47.684 20.398 1.00 34.45 ? 176 TYR A CA 1 ATOM 1382 C C . TYR A 1 176 ? -42.865 46.261 20.861 1.00 35.89 ? 176 TYR A C 1 ATOM 1383 O O . TYR A 1 176 ? -43.748 45.579 20.330 1.00 33.56 ? 176 TYR A O 1 ATOM 1384 C CB . TYR A 1 176 ? -43.055 48.675 21.467 1.00 32.51 ? 176 TYR A CB 1 ATOM 1385 C CG . TYR A 1 176 ? -44.521 48.591 21.811 1.00 35.49 ? 176 TYR A CG 1 ATOM 1386 C CD1 . TYR A 1 176 ? -45.468 49.256 21.050 1.00 33.95 ? 176 TYR A CD1 1 ATOM 1387 C CD2 . TYR A 1 176 ? -44.956 47.864 22.913 1.00 36.43 ? 176 TYR A CD2 1 ATOM 1388 C CE1 . TYR A 1 176 ? -46.810 49.192 21.368 1.00 36.58 ? 176 TYR A CE1 1 ATOM 1389 C CE2 . TYR A 1 176 ? -46.293 47.795 23.238 1.00 35.35 ? 176 TYR A CE2 1 ATOM 1390 C CZ . TYR A 1 176 ? -47.214 48.462 22.464 1.00 37.04 ? 176 TYR A CZ 1 ATOM 1391 O OH . TYR A 1 176 ? -48.549 48.400 22.784 1.00 38.73 ? 176 TYR A OH 1 ATOM 1392 N N . PHE A 1 177 ? -42.103 45.825 21.862 1.00 40.66 ? 177 PHE A N 1 ATOM 1393 C CA . PHE A 1 177 ? -42.156 44.439 22.315 1.00 41.82 ? 177 PHE A CA 1 ATOM 1394 C C . PHE A 1 177 ? -42.225 44.341 23.834 1.00 46.01 ? 177 PHE A C 1 ATOM 1395 O O . PHE A 1 177 ? -41.822 45.263 24.551 1.00 44.44 ? 177 PHE A O 1 ATOM 1396 C CB . PHE A 1 177 ? -40.928 43.674 21.810 1.00 39.30 ? 177 PHE A CB 1 ATOM 1397 C CG . PHE A 1 177 ? -40.702 43.806 20.335 1.00 40.65 ? 177 PHE A CG 1 ATOM 1398 C CD1 . PHE A 1 177 ? -40.000 44.888 19.821 1.00 39.62 ? 177 PHE A CD1 1 ATOM 1399 C CD2 . PHE A 1 177 ? -41.198 42.852 19.455 1.00 43.75 ? 177 PHE A CD2 1 ATOM 1400 C CE1 . PHE A 1 177 ? -39.798 45.019 18.456 1.00 41.05 ? 177 PHE A CE1 1 ATOM 1401 C CE2 . PHE A 1 177 ? -40.997 42.974 18.087 1.00 41.25 ? 177 PHE A CE2 1 ATOM 1402 C CZ . PHE A 1 177 ? -40.298 44.062 17.589 1.00 39.85 ? 177 PHE A CZ 1 ATOM 1403 N N . TRP A 1 178 ? -42.737 43.217 24.323 1.00 39.32 ? 178 TRP A N 1 ATOM 1404 C CA . TRP A 1 178 ? -42.724 42.938 25.755 1.00 41.72 ? 178 TRP A CA 1 ATOM 1405 C C . TRP A 1 178 ? -42.884 41.447 25.983 1.00 41.79 ? 178 TRP A C 1 ATOM 1406 O O . TRP A 1 178 ? -43.136 40.697 25.041 1.00 41.40 ? 178 TRP A O 1 ATOM 1407 C CB . TRP A 1 178 ? -43.803 43.732 26.500 1.00 39.11 ? 178 TRP A CB 1 ATOM 1408 C CG . TRP A 1 178 ? -45.202 43.233 26.319 1.00 42.72 ? 178 TRP A CG 1 ATOM 1409 C CD1 . TRP A 1 178 ? -45.902 42.416 27.163 1.00 45.31 ? 178 TRP A CD1 1 ATOM 1410 C CD2 . TRP A 1 178 ? -46.087 43.547 25.236 1.00 41.73 ? 178 TRP A CD2 1 ATOM 1411 N NE1 . TRP A 1 178 ? -47.166 42.198 26.665 1.00 43.44 ? 178 TRP A NE1 1 ATOM 1412 C CE2 . TRP A 1 178 ? -47.304 42.879 25.488 1.00 44.06 ? 178 TRP A CE2 1 ATOM 1413 C CE3 . TRP A 1 178 ? -45.964 44.323 24.082 1.00 42.55 ? 178 TRP A CE3 1 ATOM 1414 C CZ2 . TRP A 1 178 ? -48.393 42.969 24.616 1.00 40.95 ? 178 TRP A CZ2 1 ATOM 1415 C CZ3 . TRP A 1 178 ? -47.041 44.411 23.219 1.00 39.36 ? 178 TRP A CZ3 1 ATOM 1416 C CH2 . TRP A 1 178 ? -48.241 43.738 23.489 1.00 42.22 ? 178 TRP A CH2 1 ATOM 1417 N N . GLY A 1 179 ? -42.728 41.011 27.227 1.00 37.36 ? 179 GLY A N 1 ATOM 1418 C CA . GLY A 1 179 ? -42.815 39.597 27.522 1.00 36.89 ? 179 GLY A CA 1 ATOM 1419 C C . GLY A 1 179 ? -43.423 39.312 28.877 1.00 40.63 ? 179 GLY A C 1 ATOM 1420 O O . GLY A 1 179 ? -43.635 40.219 29.687 1.00 42.24 ? 179 GLY A O 1 ATOM 1421 N N . VAL A 1 180 ? -43.724 38.041 29.110 1.00 46.77 ? 180 VAL A N 1 ATOM 1422 C CA . VAL A 1 180 ? -44.166 37.573 30.412 1.00 48.44 ? 180 VAL A CA 1 ATOM 1423 C C . VAL A 1 180 ? -43.302 36.368 30.734 1.00 49.01 ? 180 VAL A C 1 ATOM 1424 O O . VAL A 1 180 ? -43.195 35.451 29.914 1.00 48.19 ? 180 VAL A O 1 ATOM 1425 C CB . VAL A 1 180 ? -45.644 37.152 30.390 1.00 52.23 ? 180 VAL A CB 1 ATOM 1426 C CG1 . VAL A 1 180 ? -46.063 36.593 31.744 1.00 49.87 ? 180 VAL A CG1 1 ATOM 1427 C CG2 . VAL A 1 180 ? -46.525 38.326 30.002 1.00 44.25 ? 180 VAL A CG2 1 ATOM 1428 N N . HIS A 1 181 ? -42.669 36.369 31.905 1.00 47.24 ? 181 HIS A N 1 ATOM 1429 C CA . HIS A 1 181 ? -41.821 35.241 32.291 1.00 49.48 ? 181 HIS A CA 1 ATOM 1430 C C . HIS A 1 181 ? -42.637 34.121 32.928 1.00 47.39 ? 181 HIS A C 1 ATOM 1431 O O . HIS A 1 181 ? -43.511 34.372 33.759 1.00 54.68 ? 181 HIS A O 1 ATOM 1432 C CB . HIS A 1 181 ? -40.702 35.685 33.237 1.00 51.59 ? 181 HIS A CB 1 ATOM 1433 C CG . HIS A 1 181 ? -39.674 34.628 33.493 1.00 51.86 ? 181 HIS A CG 1 ATOM 1434 N ND1 . HIS A 1 181 ? -39.410 34.130 34.753 1.00 53.07 ? 181 HIS A ND1 1 ATOM 1435 C CD2 . HIS A 1 181 ? -38.845 33.970 32.649 1.00 53.22 ? 181 HIS A CD2 1 ATOM 1436 C CE1 . HIS A 1 181 ? -38.465 33.214 34.670 1.00 55.02 ? 181 HIS A CE1 1 ATOM 1437 N NE2 . HIS A 1 181 ? -38.103 33.094 33.409 1.00 55.71 ? 181 HIS A NE2 1 ATOM 1438 N N . HIS A 1 182 ? -42.348 32.887 32.529 1.00 50.71 ? 182 HIS A N 1 ATOM 1439 C CA . HIS A 1 182 ? -43.001 31.713 33.100 1.00 55.00 ? 182 HIS A CA 1 ATOM 1440 C C . HIS A 1 182 ? -41.964 30.791 33.742 1.00 56.04 ? 182 HIS A C 1 ATOM 1441 O O . HIS A 1 182 ? -41.375 29.947 33.057 1.00 57.18 ? 182 HIS A O 1 ATOM 1442 C CB . HIS A 1 182 ? -43.759 30.950 32.012 1.00 55.36 ? 182 HIS A CB 1 ATOM 1443 C CG . HIS A 1 182 ? -44.762 31.776 31.275 1.00 54.35 ? 182 HIS A CG 1 ATOM 1444 N ND1 . HIS A 1 182 ? -46.046 31.973 31.732 1.00 55.15 ? 182 HIS A ND1 1 ATOM 1445 C CD2 . HIS A 1 182 ? -44.680 32.447 30.098 1.00 57.04 ? 182 HIS A CD2 1 ATOM 1446 C CE1 . HIS A 1 182 ? -46.709 32.731 30.879 1.00 57.66 ? 182 HIS A CE1 1 ATOM 1447 N NE2 . HIS A 1 182 ? -45.902 33.032 29.879 1.00 57.96 ? 182 HIS A NE2 1 ATOM 1448 N N . PRO A 1 183 ? -41.731 30.954 35.058 1.00 55.05 ? 183 PRO A N 1 ATOM 1449 C CA . PRO A 1 183 ? -40.744 30.153 35.803 1.00 54.60 ? 183 PRO A CA 1 ATOM 1450 C C . PRO A 1 183 ? -41.089 28.664 35.815 1.00 53.46 ? 183 PRO A C 1 ATOM 1451 O O . PRO A 1 183 ? -42.265 28.311 35.694 1.00 51.82 ? 183 PRO A O 1 ATOM 1452 C CB . PRO A 1 183 ? -40.841 30.712 37.226 1.00 54.42 ? 183 PRO A CB 1 ATOM 1453 C CG . PRO A 1 183 ? -41.394 32.089 37.062 1.00 57.05 ? 183 PRO A CG 1 ATOM 1454 C CD . PRO A 1 183 ? -42.346 31.997 35.900 1.00 53.80 ? 183 PRO A CD 1 ATOM 1455 N N . LEU A 1 184 ? -40.080 27.809 35.972 1.00 54.65 ? 184 LEU A N 1 ATOM 1456 C CA . LEU A 1 184 ? -40.296 26.363 35.975 1.00 59.38 ? 184 LEU A CA 1 ATOM 1457 C C . LEU A 1 184 ? -40.995 25.862 37.241 1.00 59.51 ? 184 LEU A C 1 ATOM 1458 O O . LEU A 1 184 ? -41.769 24.902 37.181 1.00 61.83 ? 184 LEU A O 1 ATOM 1459 C CB . LEU A 1 184 ? -38.982 25.605 35.764 1.00 63.26 ? 184 LEU A CB 1 ATOM 1460 C CG . LEU A 1 184 ? -37.920 25.688 36.863 1.00 70.69 ? 184 LEU A CG 1 ATOM 1461 C CD1 . LEU A 1 184 ? -37.198 24.356 37.018 1.00 72.96 ? 184 LEU A CD1 1 ATOM 1462 C CD2 . LEU A 1 184 ? -36.919 26.798 36.568 1.00 67.00 ? 184 LEU A CD2 1 ATOM 1463 N N . ASP A 1 185 ? -40.720 26.501 38.380 1.00 65.41 ? 185 ASP A N 1 ATOM 1464 C CA . ASP A 1 185 ? -41.348 26.120 39.651 1.00 67.30 ? 185 ASP A CA 1 ATOM 1465 C C . ASP A 1 185 ? -41.785 27.324 40.492 1.00 68.65 ? 185 ASP A C 1 ATOM 1466 O O . ASP A 1 185 ? -41.523 28.473 40.131 1.00 69.35 ? 185 ASP A O 1 ATOM 1467 C CB . ASP A 1 185 ? -40.440 25.181 40.466 1.00 67.84 ? 185 ASP A CB 1 ATOM 1468 C CG . ASP A 1 185 ? -39.097 25.812 40.825 1.00 75.78 ? 185 ASP A CG 1 ATOM 1469 O OD1 . ASP A 1 185 ? -39.077 26.936 41.375 1.00 75.35 ? 185 ASP A OD1 1 ATOM 1470 O OD2 . ASP A 1 185 ? -38.054 25.172 40.566 1.00 78.43 ? 185 ASP A OD2 1 ATOM 1471 N N . THR A 1 186 ? -42.444 27.048 41.615 1.00 59.06 ? 186 THR A N 1 ATOM 1472 C CA . THR A 1 186 ? -42.954 28.102 42.493 1.00 64.40 ? 186 THR A CA 1 ATOM 1473 C C . THR A 1 186 ? -41.876 28.754 43.362 1.00 60.68 ? 186 THR A C 1 ATOM 1474 O O . THR A 1 186 ? -42.097 29.823 43.933 1.00 60.99 ? 186 THR A O 1 ATOM 1475 C CB . THR A 1 186 ? -44.106 27.595 43.392 1.00 69.21 ? 186 THR A CB 1 ATOM 1476 O OG1 . THR A 1 186 ? -43.777 26.303 43.917 1.00 68.85 ? 186 THR A OG1 1 ATOM 1477 C CG2 . THR A 1 186 ? -45.407 27.501 42.600 1.00 61.08 ? 186 THR A CG2 1 ATOM 1478 N N . THR A 1 187 ? -40.717 28.109 43.468 1.00 63.24 ? 187 THR A N 1 ATOM 1479 C CA . THR A 1 187 ? -39.605 28.672 44.233 1.00 69.49 ? 187 THR A CA 1 ATOM 1480 C C . THR A 1 187 ? -38.933 29.791 43.442 1.00 71.38 ? 187 THR A C 1 ATOM 1481 O O . THR A 1 187 ? -38.733 30.894 43.959 1.00 70.43 ? 187 THR A O 1 ATOM 1482 C CB . THR A 1 187 ? -38.545 27.609 44.619 1.00 72.98 ? 187 THR A CB 1 ATOM 1483 O OG1 . THR A 1 187 ? -37.699 27.336 43.496 1.00 79.68 ? 187 THR A OG1 1 ATOM 1484 C CG2 . THR A 1 187 ? -39.211 26.321 45.084 1.00 72.43 ? 187 THR A CG2 1 ATOM 1485 N N . VAL A 1 188 ? -38.580 29.491 42.191 1.00 59.68 ? 188 VAL A N 1 ATOM 1486 C CA . VAL A 1 188 ? -38.010 30.480 41.278 1.00 56.14 ? 188 VAL A CA 1 ATOM 1487 C C . VAL A 1 188 ? -38.936 31.687 41.158 1.00 50.38 ? 188 VAL A C 1 ATOM 1488 O O . VAL A 1 188 ? -38.487 32.835 41.206 1.00 47.67 ? 188 VAL A O 1 ATOM 1489 C CB . VAL A 1 188 ? -37.745 29.873 39.879 1.00 59.43 ? 188 VAL A CB 1 ATOM 1490 C CG1 . VAL A 1 188 ? -37.270 30.942 38.903 1.00 52.27 ? 188 VAL A CG1 1 ATOM 1491 C CG2 . VAL A 1 188 ? -36.718 28.753 39.973 1.00 62.10 ? 188 VAL A CG2 1 ATOM 1492 N N . GLN A 1 189 ? -40.229 31.416 41.018 1.00 50.76 ? 189 GLN A N 1 ATOM 1493 C CA . GLN A 1 189 ? -41.247 32.460 41.014 1.00 53.85 ? 189 GLN A CA 1 ATOM 1494 C C . GLN A 1 189 ? -41.116 33.346 42.246 1.00 55.67 ? 189 GLN A C 1 ATOM 1495 O O . GLN A 1 189 ? -40.929 34.561 42.137 1.00 52.87 ? 189 GLN A O 1 ATOM 1496 C CB . GLN A 1 189 ? -42.643 31.836 40.978 1.00 54.49 ? 189 GLN A CB 1 ATOM 1497 C CG . GLN A 1 189 ? -43.779 32.826 41.205 1.00 53.73 ? 189 GLN A CG 1 ATOM 1498 C CD . GLN A 1 189 ? -44.010 33.745 40.015 1.00 53.67 ? 189 GLN A CD 1 ATOM 1499 O OE1 . GLN A 1 189 ? -43.436 33.549 38.943 1.00 52.27 ? 189 GLN A OE1 1 ATOM 1500 N NE2 . GLN A 1 189 ? -44.860 34.752 40.200 1.00 52.63 ? 189 GLN A NE2 1 ATOM 1501 N N . ASP A 1 190 ? -41.195 32.717 43.416 1.00 70.85 ? 190 ASP A N 1 ATOM 1502 C CA . ASP A 1 190 ? -41.098 33.415 44.695 1.00 70.24 ? 190 ASP A CA 1 ATOM 1503 C C . ASP A 1 190 ? -39.757 34.142 44.841 1.00 66.31 ? 190 ASP A C 1 ATOM 1504 O O . ASP A 1 190 ? -39.704 35.268 45.335 1.00 65.66 ? 190 ASP A O 1 ATOM 1505 C CB . ASP A 1 190 ? -41.290 32.420 45.843 1.00 72.87 ? 190 ASP A CB 1 ATOM 1506 C CG . ASP A 1 190 ? -41.852 33.067 47.094 1.00 87.19 ? 190 ASP A CG 1 ATOM 1507 O OD1 . ASP A 1 190 ? -41.133 33.876 47.723 1.00 84.71 ? 190 ASP A OD1 1 ATOM 1508 O OD2 . ASP A 1 190 ? -43.010 32.756 47.456 1.00 94.17 ? 190 ASP A OD2 1 ATOM 1509 N N . ASN A 1 191 ? -38.680 33.502 44.393 1.00 58.90 ? 191 ASN A N 1 ATOM 1510 C CA . ASN A 1 191 ? -37.344 34.088 44.500 1.00 64.89 ? 191 ASN A CA 1 ATOM 1511 C C . ASN A 1 191 ? -37.128 35.318 43.613 1.00 68.66 ? 191 ASN A C 1 ATOM 1512 O O . ASN A 1 191 ? -36.231 36.123 43.872 1.00 67.78 ? 191 ASN A O 1 ATOM 1513 C CB . ASN A 1 191 ? -36.264 33.036 44.209 1.00 65.13 ? 191 ASN A CB 1 ATOM 1514 C CG . ASN A 1 191 ? -36.079 32.049 45.352 1.00 83.15 ? 191 ASN A CG 1 ATOM 1515 O OD1 . ASN A 1 191 ? -36.978 31.850 46.174 1.00 85.17 ? 191 ASN A OD1 1 ATOM 1516 N ND2 . ASN A 1 191 ? -34.902 31.428 45.411 1.00 85.00 ? 191 ASN A ND2 1 ATOM 1517 N N . LEU A 1 192 ? -37.948 35.457 42.572 1.00 63.41 ? 192 LEU A N 1 ATOM 1518 C CA . LEU A 1 192 ? -37.784 36.531 41.589 1.00 57.59 ? 192 LEU A CA 1 ATOM 1519 C C . LEU A 1 192 ? -38.823 37.643 41.728 1.00 57.68 ? 192 LEU A C 1 ATOM 1520 O O . LEU A 1 192 ? -38.500 38.827 41.606 1.00 58.71 ? 192 LEU A O 1 ATOM 1521 C CB . LEU A 1 192 ? -37.823 35.965 40.164 1.00 54.86 ? 192 LEU A CB 1 ATOM 1522 C CG . LEU A 1 192 ? -36.498 35.644 39.466 1.00 60.98 ? 192 LEU A CG 1 ATOM 1523 C CD1 . LEU A 1 192 ? -35.544 34.933 40.401 1.00 59.24 ? 192 LEU A CD1 1 ATOM 1524 C CD2 . LEU A 1 192 ? -36.730 34.795 38.223 1.00 58.02 ? 192 LEU A CD2 1 ATOM 1525 N N . TYR A 1 193 ? -40.068 37.260 41.992 1.00 59.86 ? 193 TYR A N 1 ATOM 1526 C CA . TYR A 1 193 ? -41.175 38.211 41.978 1.00 61.16 ? 193 TYR A CA 1 ATOM 1527 C C . TYR A 1 193 ? -41.932 38.209 43.305 1.00 64.83 ? 193 TYR A C 1 ATOM 1528 O O . TYR A 1 193 ? -42.825 39.031 43.524 1.00 68.51 ? 193 TYR A O 1 ATOM 1529 C CB . TYR A 1 193 ? -42.112 37.900 40.800 1.00 59.91 ? 193 TYR A CB 1 ATOM 1530 C CG . TYR A 1 193 ? -41.367 37.523 39.533 1.00 54.71 ? 193 TYR A CG 1 ATOM 1531 C CD1 . TYR A 1 193 ? -40.711 38.487 38.775 1.00 54.85 ? 193 TYR A CD1 1 ATOM 1532 C CD2 . TYR A 1 193 ? -41.310 36.204 39.101 1.00 52.64 ? 193 TYR A CD2 1 ATOM 1533 C CE1 . TYR A 1 193 ? -40.022 38.148 37.622 1.00 55.03 ? 193 TYR A CE1 1 ATOM 1534 C CE2 . TYR A 1 193 ? -40.622 35.856 37.950 1.00 55.53 ? 193 TYR A CE2 1 ATOM 1535 C CZ . TYR A 1 193 ? -39.982 36.833 37.214 1.00 56.26 ? 193 TYR A CZ 1 ATOM 1536 O OH . TYR A 1 193 ? -39.298 36.499 36.066 1.00 49.37 ? 193 TYR A OH 1 ATOM 1537 N N . GLY A 1 194 ? -41.564 37.287 44.191 1.00 74.86 ? 194 GLY A N 1 ATOM 1538 C CA . GLY A 1 194 ? -42.197 37.183 45.496 1.00 73.83 ? 194 GLY A CA 1 ATOM 1539 C C . GLY A 1 194 ? -43.470 36.357 45.476 1.00 77.27 ? 194 GLY A C 1 ATOM 1540 O O . GLY A 1 194 ? -43.772 35.693 44.482 1.00 81.30 ? 194 GLY A O 1 ATOM 1541 N N . SER A 1 195 ? -44.219 36.398 46.576 1.00 75.42 ? 195 SER A N 1 ATOM 1542 C CA . SER A 1 195 ? -45.478 35.659 46.685 1.00 77.01 ? 195 SER A CA 1 ATOM 1543 C C . SER A 1 195 ? -46.646 36.476 46.134 1.00 71.89 ? 195 SER A C 1 ATOM 1544 O O . SER A 1 195 ? -46.517 37.683 45.916 1.00 71.26 ? 195 SER A O 1 ATOM 1545 C CB . SER A 1 195 ? -45.741 35.266 48.145 1.00 83.08 ? 195 SER A CB 1 ATOM 1546 O OG . SER A 1 195 ? -46.976 35.786 48.614 1.00 73.82 ? 195 SER A OG 1 ATOM 1547 N N . GLY A 1 196 ? -47.779 35.815 45.901 1.00 58.17 ? 196 GLY A N 1 ATOM 1548 C CA . GLY A 1 196 ? -48.977 36.491 45.426 1.00 56.04 ? 196 GLY A CA 1 ATOM 1549 C C . GLY A 1 196 ? -49.317 36.154 43.986 1.00 59.58 ? 196 GLY A C 1 ATOM 1550 O O . GLY A 1 196 ? -48.496 35.585 43.264 1.00 55.31 ? 196 GLY A O 1 ATOM 1551 N N . ASP A 1 197 ? -50.529 36.497 43.564 1.00 76.00 ? 197 ASP A N 1 ATOM 1552 C CA . ASP A 1 197 ? -50.927 36.279 42.179 1.00 76.21 ? 197 ASP A CA 1 ATOM 1553 C C . ASP A 1 197 ? -50.473 37.447 41.312 1.00 73.28 ? 197 ASP A C 1 ATOM 1554 O O . ASP A 1 197 ? -50.865 38.596 41.543 1.00 70.00 ? 197 ASP A O 1 ATOM 1555 C CB . ASP A 1 197 ? -52.438 36.060 42.071 1.00 76.19 ? 197 ASP A CB 1 ATOM 1556 C CG . ASP A 1 197 ? -52.890 34.791 42.768 1.00 90.84 ? 197 ASP A CG 1 ATOM 1557 O OD1 . ASP A 1 197 ? -52.100 33.821 42.797 1.00 91.41 ? 197 ASP A OD1 1 ATOM 1558 O OD2 . ASP A 1 197 ? -54.027 34.767 43.291 1.00 89.84 ? 197 ASP A OD2 1 ATOM 1559 N N . LYS A 1 198 ? -49.637 37.148 40.320 1.00 56.89 ? 198 LYS A N 1 ATOM 1560 C CA . LYS A 1 198 ? -49.030 38.190 39.501 1.00 55.34 ? 198 LYS A CA 1 ATOM 1561 C C . LYS A 1 198 ? -49.725 38.361 38.147 1.00 52.85 ? 198 LYS A C 1 ATOM 1562 O O . LYS A 1 198 ? -50.444 37.471 37.680 1.00 50.20 ? 198 LYS A O 1 ATOM 1563 C CB . LYS A 1 198 ? -47.530 37.932 39.322 1.00 52.70 ? 198 LYS A CB 1 ATOM 1564 C CG . LYS A 1 198 ? -46.750 37.803 40.638 1.00 61.40 ? 198 LYS A CG 1 ATOM 1565 C CD . LYS A 1 198 ? -46.998 38.987 41.575 1.00 56.43 ? 198 LYS A CD 1 ATOM 1566 C CE . LYS A 1 198 ? -46.094 38.925 42.805 1.00 60.07 ? 198 LYS A CE 1 ATOM 1567 N NZ . LYS A 1 198 ? -46.186 40.160 43.646 1.00 62.68 ? 198 LYS A NZ 1 ATOM 1568 N N . TYR A 1 199 ? -49.516 39.521 37.532 1.00 61.04 ? 199 TYR A N 1 ATOM 1569 C CA . TYR A 1 199 ? -50.167 39.845 36.270 1.00 58.70 ? 199 TYR A CA 1 ATOM 1570 C C . TYR A 1 199 ? -49.338 40.830 35.463 1.00 59.75 ? 199 TYR A C 1 ATOM 1571 O O . TYR A 1 199 ? -48.505 41.561 36.009 1.00 57.49 ? 199 TYR A O 1 ATOM 1572 C CB . TYR A 1 199 ? -51.555 40.442 36.519 1.00 58.40 ? 199 TYR A CB 1 ATOM 1573 C CG . TYR A 1 199 ? -51.534 41.739 37.302 1.00 64.68 ? 199 TYR A CG 1 ATOM 1574 C CD1 . TYR A 1 199 ? -51.567 41.734 38.691 1.00 64.47 ? 199 TYR A CD1 1 ATOM 1575 C CD2 . TYR A 1 199 ? -51.491 42.968 36.651 1.00 63.48 ? 199 TYR A CD2 1 ATOM 1576 C CE1 . TYR A 1 199 ? -51.552 42.914 39.410 1.00 63.34 ? 199 TYR A CE1 1 ATOM 1577 C CE2 . TYR A 1 199 ? -51.476 44.152 37.362 1.00 65.42 ? 199 TYR A CE2 1 ATOM 1578 C CZ . TYR A 1 199 ? -51.506 44.117 38.740 1.00 68.96 ? 199 TYR A CZ 1 ATOM 1579 O OH . TYR A 1 199 ? -51.490 45.291 39.454 1.00 71.16 ? 199 TYR A OH 1 ATOM 1580 N N . VAL A 1 200 ? -49.575 40.840 34.156 1.00 58.26 ? 200 VAL A N 1 ATOM 1581 C CA . VAL A 1 200 ? -49.035 41.866 33.280 1.00 47.49 ? 200 VAL A CA 1 ATOM 1582 C C . VAL A 1 200 ? -50.198 42.418 32.476 1.00 48.41 ? 200 VAL A C 1 ATOM 1583 O O . VAL A 1 200 ? -50.847 41.684 31.730 1.00 50.41 ? 200 VAL A O 1 ATOM 1584 C CB . VAL A 1 200 ? -47.970 41.302 32.335 1.00 47.94 ? 200 VAL A CB 1 ATOM 1585 C CG1 . VAL A 1 200 ? -47.571 42.347 31.304 1.00 45.82 ? 200 VAL A CG1 1 ATOM 1586 C CG2 . VAL A 1 200 ? -46.754 40.844 33.126 1.00 46.47 ? 200 VAL A CG2 1 ATOM 1587 N N . ARG A 1 201 ? -50.485 43.703 32.645 1.00 53.83 ? 201 ARG A N 1 ATOM 1588 C CA . ARG A 1 201 ? -51.592 44.310 31.923 1.00 54.08 ? 201 ARG A CA 1 ATOM 1589 C C . ARG A 1 201 ? -51.131 45.507 31.108 1.00 52.38 ? 201 ARG A C 1 ATOM 1590 O O . ARG A 1 201 ? -50.313 46.307 31.563 1.00 51.83 ? 201 ARG A O 1 ATOM 1591 C CB . ARG A 1 201 ? -52.734 44.682 32.873 1.00 51.94 ? 201 ARG A CB 1 ATOM 1592 C CG . ARG A 1 201 ? -53.517 43.472 33.347 1.00 52.96 ? 201 ARG A CG 1 ATOM 1593 C CD . ARG A 1 201 ? -54.399 43.784 34.533 1.00 56.99 ? 201 ARG A CD 1 ATOM 1594 N NE . ARG A 1 201 ? -54.979 42.567 35.099 1.00 62.02 ? 201 ARG A NE 1 ATOM 1595 C CZ . ARG A 1 201 ? -55.111 42.330 36.402 1.00 66.16 ? 201 ARG A CZ 1 ATOM 1596 N NH1 . ARG A 1 201 ? -54.710 43.230 37.291 1.00 60.73 ? 201 ARG A NH1 1 ATOM 1597 N NH2 . ARG A 1 201 ? -55.647 41.189 36.815 1.00 64.04 ? 201 ARG A NH2 1 ATOM 1598 N N . MET A 1 202 ? -51.652 45.603 29.891 1.00 56.39 ? 202 MET A N 1 ATOM 1599 C CA . MET A 1 202 ? -51.285 46.669 28.973 1.00 54.86 ? 202 MET A CA 1 ATOM 1600 C C . MET A 1 202 ? -52.516 47.113 28.199 1.00 54.93 ? 202 MET A C 1 ATOM 1601 O O . MET A 1 202 ? -53.417 46.313 27.943 1.00 54.05 ? 202 MET A O 1 ATOM 1602 C CB . MET A 1 202 ? -50.181 46.199 28.022 1.00 53.56 ? 202 MET A CB 1 ATOM 1603 C CG . MET A 1 202 ? -48.804 46.114 28.667 1.00 55.09 ? 202 MET A CG 1 ATOM 1604 S SD . MET A 1 202 ? -47.530 45.637 27.491 1.00 70.81 ? 202 MET A SD 1 ATOM 1605 C CE . MET A 1 202 ? -46.043 46.131 28.360 1.00 58.46 ? 202 MET A CE 1 ATOM 1606 N N . GLY A 1 203 ? -52.558 48.390 27.839 1.00 44.94 ? 203 GLY A N 1 ATOM 1607 C CA . GLY A 1 203 ? -53.718 48.932 27.163 1.00 43.16 ? 203 GLY A CA 1 ATOM 1608 C C . GLY A 1 203 ? -53.415 50.220 26.423 1.00 45.57 ? 203 GLY A C 1 ATOM 1609 O O . GLY A 1 203 ? -52.592 51.028 26.863 1.00 44.99 ? 203 GLY A O 1 ATOM 1610 N N . THR A 1 204 ? -54.070 50.391 25.278 1.00 43.71 ? 204 THR A N 1 ATOM 1611 C CA . THR A 1 204 ? -54.047 51.642 24.538 1.00 45.83 ? 204 THR A CA 1 ATOM 1612 C C . THR A 1 204 ? -55.493 52.014 24.274 1.00 46.88 ? 204 THR A C 1 ATOM 1613 O O . THR A 1 204 ? -56.396 51.434 24.872 1.00 49.42 ? 204 THR A O 1 ATOM 1614 C CB . THR A 1 204 ? -53.288 51.513 23.201 1.00 46.13 ? 204 THR A CB 1 ATOM 1615 O OG1 . THR A 1 204 ? -54.016 50.658 22.310 1.00 49.65 ? 204 THR A OG1 1 ATOM 1616 C CG2 . THR A 1 204 ? -51.902 50.946 23.428 1.00 40.94 ? 204 THR A CG2 1 ATOM 1617 N N . GLU A 1 205 ? -55.714 52.967 23.376 1.00 51.44 ? 205 GLU A N 1 ATOM 1618 C CA . GLU A 1 205 ? -57.065 53.366 23.004 1.00 50.53 ? 205 GLU A CA 1 ATOM 1619 C C . GLU A 1 205 ? -57.787 52.263 22.225 1.00 51.95 ? 205 GLU A C 1 ATOM 1620 O O . GLU A 1 205 ? -59.015 52.219 22.202 1.00 56.25 ? 205 GLU A O 1 ATOM 1621 C CB . GLU A 1 205 ? -57.042 54.661 22.176 1.00 49.08 ? 205 GLU A CB 1 ATOM 1622 C CG . GLU A 1 205 ? -56.789 55.952 22.966 1.00 48.61 ? 205 GLU A CG 1 ATOM 1623 C CD . GLU A 1 205 ? -55.311 56.225 23.220 1.00 59.68 ? 205 GLU A CD 1 ATOM 1624 O OE1 . GLU A 1 205 ? -54.980 57.328 23.714 1.00 57.47 ? 205 GLU A OE1 1 ATOM 1625 O OE2 . GLU A 1 205 ? -54.478 55.338 22.927 1.00 57.99 ? 205 GLU A OE2 1 ATOM 1626 N N . SER A 1 206 ? -57.023 51.370 21.598 1.00 55.08 ? 206 SER A N 1 ATOM 1627 C CA . SER A 1 206 ? -57.593 50.357 20.706 1.00 59.09 ? 206 SER A CA 1 ATOM 1628 C C . SER A 1 206 ? -57.153 48.933 21.048 1.00 57.85 ? 206 SER A C 1 ATOM 1629 O O . SER A 1 206 ? -57.604 47.966 20.426 1.00 58.62 ? 206 SER A O 1 ATOM 1630 C CB . SER A 1 206 ? -57.218 50.663 19.252 1.00 57.06 ? 206 SER A CB 1 ATOM 1631 O OG . SER A 1 206 ? -55.827 50.497 19.035 1.00 57.08 ? 206 SER A OG 1 ATOM 1632 N N . MET A 1 207 ? -56.268 48.808 22.030 1.00 55.14 ? 207 MET A N 1 ATOM 1633 C CA . MET A 1 207 ? -55.694 47.517 22.383 1.00 54.36 ? 207 MET A CA 1 ATOM 1634 C C . MET A 1 207 ? -55.672 47.383 23.895 1.00 53.60 ? 207 MET A C 1 ATOM 1635 O O . MET A 1 207 ? -55.382 48.347 24.600 1.00 53.84 ? 207 MET A O 1 ATOM 1636 C CB . MET A 1 207 ? -54.265 47.415 21.823 1.00 53.52 ? 207 MET A CB 1 ATOM 1637 C CG . MET A 1 207 ? -53.600 46.048 21.960 1.00 54.91 ? 207 MET A CG 1 ATOM 1638 S SD . MET A 1 207 ? -52.908 45.696 23.596 1.00 59.70 ? 207 MET A SD 1 ATOM 1639 C CE . MET A 1 207 ? -51.475 46.775 23.623 1.00 50.84 ? 207 MET A CE 1 ATOM 1640 N N . ASN A 1 208 ? -56.001 46.197 24.393 1.00 45.42 ? 208 ASN A N 1 ATOM 1641 C CA . ASN A 1 208 ? -55.745 45.867 25.791 1.00 50.76 ? 208 ASN A CA 1 ATOM 1642 C C . ASN A 1 208 ? -55.297 44.414 25.939 1.00 52.03 ? 208 ASN A C 1 ATOM 1643 O O . ASN A 1 208 ? -55.757 43.528 25.213 1.00 51.98 ? 208 ASN A O 1 ATOM 1644 C CB . ASN A 1 208 ? -56.926 46.216 26.716 1.00 50.09 ? 208 ASN A CB 1 ATOM 1645 C CG . ASN A 1 208 ? -58.238 45.623 26.250 1.00 60.37 ? 208 ASN A CG 1 ATOM 1646 O OD1 . ASN A 1 208 ? -58.468 44.417 26.381 1.00 63.71 ? 208 ASN A OD1 1 ATOM 1647 N ND2 . ASN A 1 208 ? -59.119 46.473 25.719 1.00 58.76 ? 208 ASN A ND2 1 ATOM 1648 N N . PHE A 1 209 ? -54.381 44.190 26.874 1.00 45.05 ? 209 PHE A N 1 ATOM 1649 C CA . PHE A 1 209 ? -53.704 42.915 27.010 1.00 44.37 ? 209 PHE A CA 1 ATOM 1650 C C . PHE A 1 209 ? -53.602 42.572 28.484 1.00 46.20 ? 209 PHE A C 1 ATOM 1651 O O . PHE A 1 209 ? -53.322 43.441 29.315 1.00 46.72 ? 209 PHE A O 1 ATOM 1652 C CB . PHE A 1 209 ? -52.309 43.027 26.396 1.00 43.64 ? 209 PHE A CB 1 ATOM 1653 C CG . PHE A 1 209 ? -51.385 41.892 26.740 1.00 42.02 ? 209 PHE A CG 1 ATOM 1654 C CD1 . PHE A 1 209 ? -50.564 41.958 27.863 1.00 43.57 ? 209 PHE A CD1 1 ATOM 1655 C CD2 . PHE A 1 209 ? -51.304 40.778 25.917 1.00 42.55 ? 209 PHE A CD2 1 ATOM 1656 C CE1 . PHE A 1 209 ? -49.698 40.917 28.175 1.00 42.24 ? 209 PHE A CE1 1 ATOM 1657 C CE2 . PHE A 1 209 ? -50.438 39.733 26.214 1.00 44.16 ? 209 PHE A CE2 1 ATOM 1658 C CZ . PHE A 1 209 ? -49.633 39.802 27.347 1.00 48.21 ? 209 PHE A CZ 1 ATOM 1659 N N . ALA A 1 210 ? -53.826 41.304 28.805 1.00 44.40 ? 210 ALA A N 1 ATOM 1660 C CA . ALA A 1 210 ? -53.707 40.837 30.177 1.00 45.86 ? 210 ALA A CA 1 ATOM 1661 C C . ALA A 1 210 ? -53.220 39.401 30.182 1.00 46.82 ? 210 ALA A C 1 ATOM 1662 O O . ALA A 1 210 ? -53.780 38.545 29.493 1.00 46.87 ? 210 ALA A O 1 ATOM 1663 C CB . ALA A 1 210 ? -55.036 40.943 30.888 1.00 39.66 ? 210 ALA A CB 1 ATOM 1664 N N . LYS A 1 211 ? -52.172 39.137 30.955 1.00 52.42 ? 211 LYS A N 1 ATOM 1665 C CA . LYS A 1 211 ? -51.669 37.777 31.095 1.00 54.77 ? 211 LYS A CA 1 ATOM 1666 C C . LYS A 1 211 ? -51.116 37.518 32.491 1.00 59.07 ? 211 LYS A C 1 ATOM 1667 O O . LYS A 1 211 ? -50.692 38.442 33.190 1.00 55.93 ? 211 LYS A O 1 ATOM 1668 C CB . LYS A 1 211 ? -50.608 37.469 30.032 1.00 55.52 ? 211 LYS A CB 1 ATOM 1669 C CG . LYS A 1 211 ? -50.915 36.212 29.227 1.00 59.92 ? 211 LYS A CG 1 ATOM 1670 C CD . LYS A 1 211 ? -49.697 35.305 29.085 1.00 63.61 ? 211 LYS A CD 1 ATOM 1671 C CE . LYS A 1 211 ? -50.114 33.846 28.881 1.00 65.05 ? 211 LYS A CE 1 ATOM 1672 N NZ . LYS A 1 211 ? -51.108 33.644 27.784 1.00 62.76 ? 211 LYS A NZ 1 ATOM 1673 N N . SER A 1 212 ? -51.135 36.251 32.890 1.00 63.35 ? 212 SER A N 1 ATOM 1674 C CA . SER A 1 212 ? -50.604 35.835 34.176 1.00 59.16 ? 212 SER A CA 1 ATOM 1675 C C . SER A 1 212 ? -49.638 34.683 33.947 1.00 59.89 ? 212 SER A C 1 ATOM 1676 O O . SER A 1 212 ? -49.833 33.887 33.025 1.00 64.29 ? 212 SER A O 1 ATOM 1677 C CB . SER A 1 212 ? -51.741 35.411 35.105 1.00 58.66 ? 212 SER A CB 1 ATOM 1678 O OG . SER A 1 212 ? -52.645 36.483 35.294 1.00 68.05 ? 212 SER A OG 1 ATOM 1679 N N . PRO A 1 213 ? -48.586 34.593 34.779 1.00 54.83 ? 213 PRO A N 1 ATOM 1680 C CA . PRO A 1 213 ? -47.576 33.542 34.594 1.00 53.51 ? 213 PRO A CA 1 ATOM 1681 C C . PRO A 1 213 ? -48.149 32.129 34.709 1.00 55.58 ? 213 PRO A C 1 ATOM 1682 O O . PRO A 1 213 ? -49.028 31.868 35.534 1.00 55.42 ? 213 PRO A O 1 ATOM 1683 C CB . PRO A 1 213 ? -46.576 33.805 35.727 1.00 54.30 ? 213 PRO A CB 1 ATOM 1684 C CG . PRO A 1 213 ? -47.317 34.650 36.726 1.00 54.61 ? 213 PRO A CG 1 ATOM 1685 C CD . PRO A 1 213 ? -48.271 35.476 35.918 1.00 53.78 ? 213 PRO A CD 1 ATOM 1686 N N . GLU A 1 214 ? -47.641 31.233 33.870 1.00 61.05 ? 214 GLU A N 1 ATOM 1687 C CA . GLU A 1 214 ? -48.066 29.842 33.835 1.00 63.17 ? 214 GLU A CA 1 ATOM 1688 C C . GLU A 1 214 ? -46.881 28.969 34.241 1.00 62.65 ? 214 GLU A C 1 ATOM 1689 O O . GLU A 1 214 ? -46.013 28.653 33.424 1.00 60.37 ? 214 GLU A O 1 ATOM 1690 C CB . GLU A 1 214 ? -48.571 29.484 32.430 1.00 59.20 ? 214 GLU A CB 1 ATOM 1691 C CG . GLU A 1 214 ? -49.750 30.349 31.968 1.00 64.71 ? 214 GLU A CG 1 ATOM 1692 C CD . GLU A 1 214 ? -49.965 30.351 30.451 1.00 76.52 ? 214 GLU A CD 1 ATOM 1693 O OE1 . GLU A 1 214 ? -49.144 29.759 29.705 1.00 68.48 ? 214 GLU A OE1 1 ATOM 1694 O OE2 . GLU A 1 214 ? -50.968 30.953 30.006 1.00 75.24 ? 214 GLU A OE2 1 ATOM 1695 N N . ILE A 1 215 ? -46.855 28.589 35.516 1.00 57.20 ? 215 ILE A N 1 ATOM 1696 C CA . ILE A 1 215 ? -45.693 27.934 36.112 1.00 54.02 ? 215 ILE A CA 1 ATOM 1697 C C . ILE A 1 215 ? -45.670 26.416 35.898 1.00 53.88 ? 215 ILE A C 1 ATOM 1698 O O . ILE A 1 215 ? -46.544 25.693 36.384 1.00 52.55 ? 215 ILE A O 1 ATOM 1699 C CB . ILE A 1 215 ? -45.605 28.244 37.619 1.00 55.07 ? 215 ILE A CB 1 ATOM 1700 C CG1 . ILE A 1 215 ? -45.563 29.756 37.839 1.00 57.37 ? 215 ILE A CG1 1 ATOM 1701 C CG2 . ILE A 1 215 ? -44.387 27.581 38.236 1.00 52.09 ? 215 ILE A CG2 1 ATOM 1702 C CD1 . ILE A 1 215 ? -45.437 30.158 39.291 1.00 60.82 ? 215 ILE A CD1 1 ATOM 1703 N N . ALA A 1 216 ? -44.650 25.951 35.179 1.00 51.58 ? 216 ALA A N 1 ATOM 1704 C CA . ALA A 1 216 ? -44.454 24.533 34.898 1.00 55.31 ? 216 ALA A CA 1 ATOM 1705 C C . ALA A 1 216 ? -43.073 24.312 34.300 1.00 55.68 ? 216 ALA A C 1 ATOM 1706 O O . ALA A 1 216 ? -42.501 25.218 33.690 1.00 54.64 ? 216 ALA A O 1 ATOM 1707 C CB . ALA A 1 216 ? -45.524 24.021 33.940 1.00 59.67 ? 216 ALA A CB 1 ATOM 1708 N N . ALA A 1 217 ? -42.545 23.104 34.459 1.00 56.13 ? 217 ALA A N 1 ATOM 1709 C CA . ALA A 1 217 ? -41.260 22.764 33.861 1.00 60.40 ? 217 ALA A CA 1 ATOM 1710 C C . ALA A 1 217 ? -41.442 22.269 32.427 1.00 57.26 ? 217 ALA A C 1 ATOM 1711 O O . ALA A 1 217 ? -42.102 21.254 32.191 1.00 58.58 ? 217 ALA A O 1 ATOM 1712 C CB . ALA A 1 217 ? -40.548 21.716 34.695 1.00 62.53 ? 217 ALA A CB 1 ATOM 1713 N N . ARG A 1 218 ? -40.865 22.990 31.472 1.00 60.72 ? 218 ARG A N 1 ATOM 1714 C CA . ARG A 1 218 ? -40.870 22.557 30.079 1.00 63.05 ? 218 ARG A CA 1 ATOM 1715 C C . ARG A 1 218 ? -39.519 21.915 29.810 1.00 63.79 ? 218 ARG A C 1 ATOM 1716 O O . ARG A 1 218 ? -38.593 22.097 30.601 1.00 64.10 ? 218 ARG A O 1 ATOM 1717 C CB . ARG A 1 218 ? -41.094 23.745 29.135 1.00 58.59 ? 218 ARG A CB 1 ATOM 1718 C CG . ARG A 1 218 ? -42.491 24.346 29.181 1.00 59.14 ? 218 ARG A CG 1 ATOM 1719 C CD . ARG A 1 218 ? -42.615 25.373 30.286 1.00 57.89 ? 218 ARG A CD 1 ATOM 1720 N NE . ARG A 1 218 ? -43.936 25.993 30.334 1.00 61.60 ? 218 ARG A NE 1 ATOM 1721 C CZ . ARG A 1 218 ? -44.245 27.014 31.125 1.00 64.50 ? 218 ARG A CZ 1 ATOM 1722 N NH1 . ARG A 1 218 ? -43.324 27.524 31.933 1.00 58.82 ? 218 ARG A NH1 1 ATOM 1723 N NH2 . ARG A 1 218 ? -45.470 27.523 31.109 1.00 67.92 ? 218 ARG A NH2 1 ATOM 1724 N N . PRO A 1 219 ? -39.404 21.145 28.711 1.00 61.74 ? 219 PRO A N 1 ATOM 1725 C CA . PRO A 1 219 ? -38.096 20.590 28.335 1.00 61.75 ? 219 PRO A CA 1 ATOM 1726 C C . PRO A 1 219 ? -37.035 21.684 28.232 1.00 64.18 ? 219 PRO A C 1 ATOM 1727 O O . PRO A 1 219 ? -37.360 22.820 27.886 1.00 63.47 ? 219 PRO A O 1 ATOM 1728 C CB . PRO A 1 219 ? -38.362 19.995 26.951 1.00 63.28 ? 219 PRO A CB 1 ATOM 1729 C CG . PRO A 1 219 ? -39.800 19.597 26.998 1.00 60.28 ? 219 PRO A CG 1 ATOM 1730 C CD . PRO A 1 219 ? -40.490 20.633 27.852 1.00 58.29 ? 219 PRO A CD 1 ATOM 1731 N N . ALA A 1 220 ? -35.784 21.355 28.530 1.00 60.90 ? 220 ALA A N 1 ATOM 1732 C CA . ALA A 1 220 ? -34.731 22.365 28.537 1.00 59.17 ? 220 ALA A CA 1 ATOM 1733 C C . ALA A 1 220 ? -34.324 22.801 27.128 1.00 59.08 ? 220 ALA A C 1 ATOM 1734 O O . ALA A 1 220 ? -34.048 21.964 26.264 1.00 56.66 ? 220 ALA A O 1 ATOM 1735 C CB . ALA A 1 220 ? -33.521 21.868 29.309 1.00 59.66 ? 220 ALA A CB 1 ATOM 1736 N N . VAL A 1 221 ? -34.292 24.116 26.910 1.00 55.82 ? 221 VAL A N 1 ATOM 1737 C CA . VAL A 1 221 ? -33.778 24.708 25.674 1.00 52.66 ? 221 VAL A CA 1 ATOM 1738 C C . VAL A 1 221 ? -32.802 25.822 26.054 1.00 50.61 ? 221 VAL A C 1 ATOM 1739 O O . VAL A 1 221 ? -33.169 26.743 26.790 1.00 50.47 ? 221 VAL A O 1 ATOM 1740 C CB . VAL A 1 221 ? -34.916 25.290 24.792 1.00 53.72 ? 221 VAL A CB 1 ATOM 1741 C CG1 . VAL A 1 221 ? -34.351 25.930 23.523 1.00 42.05 ? 221 VAL A CG1 1 ATOM 1742 C CG2 . VAL A 1 221 ? -35.917 24.215 24.426 1.00 46.27 ? 221 VAL A CG2 1 ATOM 1743 N N . ASN A 1 222 ? -31.568 25.735 25.558 1.00 56.17 ? 222 ASN A N 1 ATOM 1744 C CA . ASN A 1 222 ? -30.496 26.656 25.949 1.00 61.33 ? 222 ASN A CA 1 ATOM 1745 C C . ASN A 1 222 ? -30.282 26.743 27.468 1.00 64.88 ? 222 ASN A C 1 ATOM 1746 O O . ASN A 1 222 ? -29.967 27.811 28.001 1.00 66.37 ? 222 ASN A O 1 ATOM 1747 C CB . ASN A 1 222 ? -30.703 28.055 25.341 1.00 61.27 ? 222 ASN A CB 1 ATOM 1748 C CG . ASN A 1 222 ? -30.648 28.050 23.819 1.00 63.04 ? 222 ASN A CG 1 ATOM 1749 O OD1 . ASN A 1 222 ? -30.057 27.158 23.209 1.00 67.54 ? 222 ASN A OD1 1 ATOM 1750 N ND2 . ASN A 1 222 ? -31.266 29.054 23.200 1.00 57.53 ? 222 ASN A ND2 1 ATOM 1751 N N . GLY A 1 223 ? -30.464 25.614 28.152 1.00 55.89 ? 223 GLY A N 1 ATOM 1752 C CA . GLY A 1 223 ? -30.249 25.532 29.587 1.00 53.16 ? 223 GLY A CA 1 ATOM 1753 C C . GLY A 1 223 ? -31.427 25.978 30.436 1.00 57.02 ? 223 GLY A C 1 ATOM 1754 O O . GLY A 1 223 ? -31.299 26.092 31.657 1.00 59.42 ? 223 GLY A O 1 ATOM 1755 N N . GLN A 1 224 ? -32.576 26.222 29.807 1.00 59.53 ? 224 GLN A N 1 ATOM 1756 C CA . GLN A 1 224 ? -33.722 26.779 30.527 1.00 54.99 ? 224 GLN A CA 1 ATOM 1757 C C . GLN A 1 224 ? -34.984 25.920 30.441 1.00 57.36 ? 224 GLN A C 1 ATOM 1758 O O . GLN A 1 224 ? -35.389 25.495 29.354 1.00 57.75 ? 224 GLN A O 1 ATOM 1759 C CB . GLN A 1 224 ? -34.023 28.191 30.022 1.00 53.80 ? 224 GLN A CB 1 ATOM 1760 C CG . GLN A 1 224 ? -32.786 29.047 29.786 1.00 58.14 ? 224 GLN A CG 1 ATOM 1761 C CD . GLN A 1 224 ? -31.986 29.285 31.052 1.00 60.24 ? 224 GLN A CD 1 ATOM 1762 O OE1 . GLN A 1 224 ? -32.545 29.386 32.146 1.00 57.34 ? 224 GLN A OE1 1 ATOM 1763 N NE2 . GLN A 1 224 ? -30.668 29.379 30.907 1.00 57.41 ? 224 GLN A NE2 1 ATOM 1764 N N . ARG A 1 225 ? -35.598 25.674 31.597 1.00 59.58 ? 225 ARG A N 1 ATOM 1765 C CA . ARG A 1 225 ? -36.852 24.931 31.675 1.00 59.39 ? 225 ARG A CA 1 ATOM 1766 C C . ARG A 1 225 ? -37.989 25.932 31.829 1.00 56.37 ? 225 ARG A C 1 ATOM 1767 O O . ARG A 1 225 ? -39.167 25.581 31.744 1.00 56.13 ? 225 ARG A O 1 ATOM 1768 C CB . ARG A 1 225 ? -36.839 23.968 32.865 1.00 67.37 ? 225 ARG A CB 1 ATOM 1769 C CG . ARG A 1 225 ? -35.633 23.030 32.922 1.00 72.37 ? 225 ARG A CG 1 ATOM 1770 C CD . ARG A 1 225 ? -35.925 21.683 32.276 1.00 77.96 ? 225 ARG A CD 1 ATOM 1771 N NE . ARG A 1 225 ? -36.956 20.938 33.003 1.00 83.19 ? 225 ARG A NE 1 ATOM 1772 C CZ . ARG A 1 225 ? -37.383 19.720 32.673 1.00 87.06 ? 225 ARG A CZ 1 ATOM 1773 N NH1 . ARG A 1 225 ? -36.870 19.091 31.621 1.00 81.34 ? 225 ARG A NH1 1 ATOM 1774 N NH2 . ARG A 1 225 ? -38.325 19.129 33.398 1.00 80.90 ? 225 ARG A NH2 1 ATOM 1775 N N . SER A 1 226 ? -37.620 27.185 32.072 1.00 47.51 ? 226 SER A N 1 ATOM 1776 C CA . SER A 1 226 ? -38.581 28.278 32.108 1.00 50.50 ? 226 SER A CA 1 ATOM 1777 C C . SER A 1 226 ? -38.843 28.777 30.691 1.00 48.92 ? 226 SER A C 1 ATOM 1778 O O . SER A 1 226 ? -38.135 28.405 29.751 1.00 47.90 ? 226 SER A O 1 ATOM 1779 C CB . SER A 1 226 ? -38.048 29.427 32.960 1.00 47.48 ? 226 SER A CB 1 ATOM 1780 O OG . SER A 1 226 ? -37.811 29.004 34.283 1.00 59.36 ? 226 SER A OG 1 ATOM 1781 N N . ARG A 1 227 ? -39.854 29.627 30.542 1.00 41.97 ? 227 ARG A N 1 ATOM 1782 C CA . ARG A 1 227 ? -40.184 30.189 29.241 1.00 42.82 ? 227 ARG A CA 1 ATOM 1783 C C . ARG A 1 227 ? -40.476 31.683 29.331 1.00 44.25 ? 227 ARG A C 1 ATOM 1784 O O . ARG A 1 227 ? -40.691 32.223 30.417 1.00 45.09 ? 227 ARG A O 1 ATOM 1785 C CB . ARG A 1 227 ? -41.398 29.468 28.643 1.00 40.45 ? 227 ARG A CB 1 ATOM 1786 C CG . ARG A 1 227 ? -41.143 28.032 28.211 1.00 43.79 ? 227 ARG A CG 1 ATOM 1787 C CD . ARG A 1 227 ? -40.108 27.964 27.102 1.00 41.50 ? 227 ARG A CD 1 ATOM 1788 N NE . ARG A 1 227 ? -39.976 26.616 26.555 1.00 43.22 ? 227 ARG A NE 1 ATOM 1789 C CZ . ARG A 1 227 ? -39.101 25.717 26.990 1.00 47.90 ? 227 ARG A CZ 1 ATOM 1790 N NH1 . ARG A 1 227 ? -38.274 26.022 27.985 1.00 51.02 ? 227 ARG A NH1 1 ATOM 1791 N NH2 . ARG A 1 227 ? -39.052 24.517 26.430 1.00 45.53 ? 227 ARG A NH2 1 ATOM 1792 N N . ILE A 1 228 ? -40.482 32.344 28.179 1.00 46.80 ? 228 ILE A N 1 ATOM 1793 C CA . ILE A 1 228 ? -40.995 33.703 28.082 1.00 44.26 ? 228 ILE A CA 1 ATOM 1794 C C . ILE A 1 228 ? -41.975 33.779 26.918 1.00 45.80 ? 228 ILE A C 1 ATOM 1795 O O . ILE A 1 228 ? -41.674 33.316 25.817 1.00 48.27 ? 228 ILE A O 1 ATOM 1796 C CB . ILE A 1 228 ? -39.867 34.733 27.884 1.00 44.82 ? 228 ILE A CB 1 ATOM 1797 C CG1 . ILE A 1 228 ? -39.009 34.822 29.147 1.00 50.45 ? 228 ILE A CG1 1 ATOM 1798 C CG2 . ILE A 1 228 ? -40.438 36.108 27.561 1.00 42.97 ? 228 ILE A CG2 1 ATOM 1799 C CD1 . ILE A 1 228 ? -37.933 35.887 29.085 1.00 48.12 ? 228 ILE A CD1 1 ATOM 1800 N N . ASP A 1 229 ? -43.159 34.330 27.163 1.00 50.94 ? 229 ASP A N 1 ATOM 1801 C CA . ASP A 1 229 ? -44.057 34.641 26.064 1.00 48.57 ? 229 ASP A CA 1 ATOM 1802 C C . ASP A 1 229 ? -43.773 36.058 25.582 1.00 48.53 ? 229 ASP A C 1 ATOM 1803 O O . ASP A 1 229 ? -44.098 37.036 26.264 1.00 45.65 ? 229 ASP A O 1 ATOM 1804 C CB . ASP A 1 229 ? -45.526 34.479 26.469 1.00 52.17 ? 229 ASP A CB 1 ATOM 1805 C CG . ASP A 1 229 ? -46.012 33.038 26.354 1.00 63.97 ? 229 ASP A CG 1 ATOM 1806 O OD1 . ASP A 1 229 ? -45.475 32.290 25.505 1.00 65.29 ? 229 ASP A OD1 1 ATOM 1807 O OD2 . ASP A 1 229 ? -46.934 32.657 27.112 1.00 66.02 ? 229 ASP A OD2 1 ATOM 1808 N N . TYR A 1 230 ? -43.144 36.160 24.414 1.00 38.22 ? 230 TYR A N 1 ATOM 1809 C CA . TYR A 1 230 ? -42.846 37.458 23.821 1.00 34.36 ? 230 TYR A CA 1 ATOM 1810 C C . TYR A 1 230 ? -44.070 37.995 23.091 1.00 33.84 ? 230 TYR A C 1 ATOM 1811 O O . TYR A 1 230 ? -44.879 37.226 22.561 1.00 36.37 ? 230 TYR A O 1 ATOM 1812 C CB . TYR A 1 230 ? -41.676 37.343 22.850 1.00 32.71 ? 230 TYR A CB 1 ATOM 1813 C CG . TYR A 1 230 ? -40.433 36.741 23.457 1.00 37.26 ? 230 TYR A CG 1 ATOM 1814 C CD1 . TYR A 1 230 ? -40.253 35.362 23.494 1.00 39.25 ? 230 TYR A CD1 1 ATOM 1815 C CD2 . TYR A 1 230 ? -39.430 37.548 23.980 1.00 35.69 ? 230 TYR A CD2 1 ATOM 1816 C CE1 . TYR A 1 230 ? -39.117 34.805 24.042 1.00 40.27 ? 230 TYR A CE1 1 ATOM 1817 C CE2 . TYR A 1 230 ? -38.288 36.998 24.531 1.00 37.49 ? 230 TYR A CE2 1 ATOM 1818 C CZ . TYR A 1 230 ? -38.140 35.627 24.559 1.00 42.37 ? 230 TYR A CZ 1 ATOM 1819 O OH . TYR A 1 230 ? -37.008 35.071 25.104 1.00 42.87 ? 230 TYR A OH 1 ATOM 1820 N N . TYR A 1 231 ? -44.212 39.313 23.065 1.00 31.17 ? 231 TYR A N 1 ATOM 1821 C CA . TYR A 1 231 ? -45.345 39.928 22.392 1.00 33.80 ? 231 TYR A CA 1 ATOM 1822 C C . TYR A 1 231 ? -44.881 41.165 21.655 1.00 30.55 ? 231 TYR A C 1 ATOM 1823 O O . TYR A 1 231 ? -43.794 41.683 21.916 1.00 31.97 ? 231 TYR A O 1 ATOM 1824 C CB . TYR A 1 231 ? -46.447 40.286 23.395 1.00 33.62 ? 231 TYR A CB 1 ATOM 1825 C CG . TYR A 1 231 ? -47.075 39.088 24.063 1.00 37.01 ? 231 TYR A CG 1 ATOM 1826 C CD1 . TYR A 1 231 ? -48.114 38.394 23.455 1.00 39.11 ? 231 TYR A CD1 1 ATOM 1827 C CD2 . TYR A 1 231 ? -46.635 38.652 25.306 1.00 41.38 ? 231 TYR A CD2 1 ATOM 1828 C CE1 . TYR A 1 231 ? -48.693 37.299 24.065 1.00 42.04 ? 231 TYR A CE1 1 ATOM 1829 C CE2 . TYR A 1 231 ? -47.209 37.561 25.924 1.00 38.56 ? 231 TYR A CE2 1 ATOM 1830 C CZ . TYR A 1 231 ? -48.236 36.890 25.301 1.00 46.97 ? 231 TYR A CZ 1 ATOM 1831 O OH . TYR A 1 231 ? -48.810 35.800 25.912 1.00 50.65 ? 231 TYR A OH 1 ATOM 1832 N N . TRP A 1 232 ? -45.704 41.632 20.727 1.00 36.01 ? 232 TRP A N 1 ATOM 1833 C CA . TRP A 1 232 ? -45.386 42.824 19.965 1.00 33.88 ? 232 TRP A CA 1 ATOM 1834 C C . TRP A 1 232 ? -46.686 43.506 19.603 1.00 33.97 ? 232 TRP A C 1 ATOM 1835 O O . TRP A 1 232 ? -47.740 42.865 19.528 1.00 34.73 ? 232 TRP A O 1 ATOM 1836 C CB . TRP A 1 232 ? -44.623 42.470 18.689 1.00 34.38 ? 232 TRP A CB 1 ATOM 1837 C CG . TRP A 1 232 ? -45.465 41.743 17.675 1.00 38.24 ? 232 TRP A CG 1 ATOM 1838 C CD1 . TRP A 1 232 ? -45.678 40.396 17.599 1.00 34.30 ? 232 TRP A CD1 1 ATOM 1839 C CD2 . TRP A 1 232 ? -46.197 42.327 16.582 1.00 34.14 ? 232 TRP A CD2 1 ATOM 1840 N NE1 . TRP A 1 232 ? -46.499 40.107 16.534 1.00 33.94 ? 232 TRP A NE1 1 ATOM 1841 C CE2 . TRP A 1 232 ? -46.833 41.272 15.895 1.00 34.08 ? 232 TRP A CE2 1 ATOM 1842 C CE3 . TRP A 1 232 ? -46.379 43.638 16.125 1.00 34.05 ? 232 TRP A CE3 1 ATOM 1843 C CZ2 . TRP A 1 232 ? -47.638 41.488 14.767 1.00 31.89 ? 232 TRP A CZ2 1 ATOM 1844 C CZ3 . TRP A 1 232 ? -47.179 43.855 15.005 1.00 34.24 ? 232 TRP A CZ3 1 ATOM 1845 C CH2 . TRP A 1 232 ? -47.797 42.783 14.338 1.00 31.69 ? 232 TRP A CH2 1 ATOM 1846 N N . SER A 1 233 ? -46.610 44.809 19.380 1.00 36.57 ? 233 SER A N 1 ATOM 1847 C CA . SER A 1 233 ? -47.766 45.565 18.946 1.00 34.13 ? 233 SER A CA 1 ATOM 1848 C C . SER A 1 233 ? -47.290 46.816 18.238 1.00 35.86 ? 233 SER A C 1 ATOM 1849 O O . SER A 1 233 ? -46.087 47.082 18.161 1.00 36.96 ? 233 SER A O 1 ATOM 1850 C CB . SER A 1 233 ? -48.640 45.935 20.140 1.00 33.12 ? 233 SER A CB 1 ATOM 1851 O OG . SER A 1 233 ? -49.789 46.639 19.716 1.00 38.25 ? 233 SER A OG 1 ATOM 1852 N N . VAL A 1 234 ? -48.235 47.578 17.708 1.00 34.30 ? 234 VAL A N 1 ATOM 1853 C CA . VAL A 1 234 ? -47.913 48.834 17.055 1.00 34.76 ? 234 VAL A CA 1 ATOM 1854 C C . VAL A 1 234 ? -48.715 49.960 17.700 1.00 38.65 ? 234 VAL A C 1 ATOM 1855 O O . VAL A 1 234 ? -49.949 49.953 17.659 1.00 39.35 ? 234 VAL A O 1 ATOM 1856 C CB . VAL A 1 234 ? -48.194 48.765 15.546 1.00 31.56 ? 234 VAL A CB 1 ATOM 1857 C CG1 . VAL A 1 234 ? -48.072 50.143 14.915 1.00 32.73 ? 234 VAL A CG1 1 ATOM 1858 C CG2 . VAL A 1 234 ? -47.233 47.796 14.882 1.00 30.72 ? 234 VAL A CG2 1 ATOM 1859 N N . LEU A 1 235 ? -48.015 50.907 18.321 1.00 38.38 ? 235 LEU A N 1 ATOM 1860 C CA . LEU A 1 235 ? -48.671 52.056 18.940 1.00 37.36 ? 235 LEU A CA 1 ATOM 1861 C C . LEU A 1 235 ? -48.857 53.136 17.884 1.00 38.77 ? 235 LEU A C 1 ATOM 1862 O O . LEU A 1 235 ? -47.879 53.718 17.407 1.00 40.77 ? 235 LEU A O 1 ATOM 1863 C CB . LEU A 1 235 ? -47.835 52.599 20.103 1.00 40.21 ? 235 LEU A CB 1 ATOM 1864 C CG . LEU A 1 235 ? -48.477 53.715 20.934 1.00 45.62 ? 235 LEU A CG 1 ATOM 1865 C CD1 . LEU A 1 235 ? -49.649 53.168 21.730 1.00 42.24 ? 235 LEU A CD1 1 ATOM 1866 C CD2 . LEU A 1 235 ? -47.468 54.384 21.859 1.00 42.03 ? 235 LEU A CD2 1 ATOM 1867 N N . ARG A 1 236 ? -50.107 53.398 17.514 1.00 48.22 ? 236 ARG A N 1 ATOM 1868 C CA . ARG A 1 236 ? -50.408 54.330 16.428 1.00 50.22 ? 236 ARG A CA 1 ATOM 1869 C C . ARG A 1 236 ? -50.126 55.770 16.843 1.00 50.46 ? 236 ARG A C 1 ATOM 1870 O O . ARG A 1 236 ? -50.117 56.080 18.038 1.00 52.76 ? 236 ARG A O 1 ATOM 1871 C CB . ARG A 1 236 ? -51.870 54.183 15.985 1.00 54.38 ? 236 ARG A CB 1 ATOM 1872 C CG . ARG A 1 236 ? -52.265 52.774 15.544 1.00 61.01 ? 236 ARG A CG 1 ATOM 1873 C CD . ARG A 1 236 ? -53.779 52.665 15.377 1.00 72.34 ? 236 ARG A CD 1 ATOM 1874 N NE . ARG A 1 236 ? -54.264 51.285 15.439 1.00 77.15 ? 236 ARG A NE 1 ATOM 1875 C CZ . ARG A 1 236 ? -55.549 50.945 15.534 1.00 82.15 ? 236 ARG A CZ 1 ATOM 1876 N NH1 . ARG A 1 236 ? -56.486 51.884 15.582 1.00 75.51 ? 236 ARG A NH1 1 ATOM 1877 N NH2 . ARG A 1 236 ? -55.897 49.665 15.585 1.00 82.59 ? 236 ARG A NH2 1 ATOM 1878 N N . PRO A 1 237 ? -49.878 56.652 15.856 1.00 41.71 ? 237 PRO A N 1 ATOM 1879 C CA . PRO A 1 237 ? -49.671 58.078 16.145 1.00 40.86 ? 237 PRO A CA 1 ATOM 1880 C C . PRO A 1 237 ? -50.873 58.664 16.881 1.00 46.47 ? 237 PRO A C 1 ATOM 1881 O O . PRO A 1 237 ? -51.996 58.581 16.366 1.00 43.27 ? 237 PRO A O 1 ATOM 1882 C CB . PRO A 1 237 ? -49.586 58.707 14.752 1.00 40.14 ? 237 PRO A CB 1 ATOM 1883 C CG . PRO A 1 237 ? -49.135 57.603 13.859 1.00 37.57 ? 237 PRO A CG 1 ATOM 1884 C CD . PRO A 1 237 ? -49.739 56.350 14.418 1.00 36.88 ? 237 PRO A CD 1 ATOM 1885 N N . GLY A 1 238 ? -50.646 59.241 18.059 1.00 48.45 ? 238 GLY A N 1 ATOM 1886 C CA . GLY A 1 238 ? -51.728 59.827 18.832 1.00 46.72 ? 238 GLY A CA 1 ATOM 1887 C C . GLY A 1 238 ? -52.203 58.928 19.961 1.00 53.07 ? 238 GLY A C 1 ATOM 1888 O O . GLY A 1 238 ? -52.870 59.389 20.896 1.00 54.16 ? 238 GLY A O 1 ATOM 1889 N N . GLU A 1 239 ? -51.868 57.643 19.877 1.00 52.34 ? 239 GLU A N 1 ATOM 1890 C CA . GLU A 1 239 ? -52.216 56.693 20.928 1.00 50.35 ? 239 GLU A CA 1 ATOM 1891 C C . GLU A 1 239 ? -51.212 56.780 22.070 1.00 50.64 ? 239 GLU A C 1 ATOM 1892 O O . GLU A 1 239 ? -50.066 57.188 21.869 1.00 47.22 ? 239 GLU A O 1 ATOM 1893 C CB . GLU A 1 239 ? -52.241 55.265 20.380 1.00 46.45 ? 239 GLU A CB 1 ATOM 1894 C CG . GLU A 1 239 ? -53.503 54.903 19.615 1.00 51.86 ? 239 GLU A CG 1 ATOM 1895 C CD . GLU A 1 239 ? -53.550 53.430 19.222 1.00 58.19 ? 239 GLU A CD 1 ATOM 1896 O OE1 . GLU A 1 239 ? -52.485 52.767 19.224 1.00 49.50 ? 239 GLU A OE1 1 ATOM 1897 O OE2 . GLU A 1 239 ? -54.658 52.935 18.913 1.00 61.87 ? 239 GLU A OE2 1 ATOM 1898 N N . THR A 1 240 ? -51.647 56.399 23.269 1.00 48.17 ? 240 THR A N 1 ATOM 1899 C CA . THR A 1 240 ? -50.732 56.259 24.397 1.00 51.65 ? 240 THR A CA 1 ATOM 1900 C C . THR A 1 240 ? -50.819 54.843 24.968 1.00 50.68 ? 240 THR A C 1 ATOM 1901 O O . THR A 1 240 ? -51.877 54.210 24.920 1.00 49.82 ? 240 THR A O 1 ATOM 1902 C CB . THR A 1 240 ? -50.975 57.322 25.509 1.00 55.28 ? 240 THR A CB 1 ATOM 1903 O OG1 . THR A 1 240 ? -51.715 56.742 26.589 1.00 56.89 ? 240 THR A OG1 1 ATOM 1904 C CG2 . THR A 1 240 ? -51.726 58.532 24.955 1.00 51.88 ? 240 THR A CG2 1 ATOM 1905 N N . LEU A 1 241 ? -49.701 54.340 25.484 1.00 53.50 ? 241 LEU A N 1 ATOM 1906 C CA . LEU A 1 241 ? -49.660 53.000 26.060 1.00 52.59 ? 241 LEU A CA 1 ATOM 1907 C C . LEU A 1 241 ? -49.545 53.082 27.576 1.00 54.92 ? 241 LEU A C 1 ATOM 1908 O O . LEU A 1 241 ? -48.748 53.863 28.101 1.00 54.00 ? 241 LEU A O 1 ATOM 1909 C CB . LEU A 1 241 ? -48.472 52.209 25.498 1.00 48.96 ? 241 LEU A CB 1 ATOM 1910 C CG . LEU A 1 241 ? -48.096 50.912 26.226 1.00 50.65 ? 241 LEU A CG 1 ATOM 1911 C CD1 . LEU A 1 241 ? -49.189 49.870 26.064 1.00 51.46 ? 241 LEU A CD1 1 ATOM 1912 C CD2 . LEU A 1 241 ? -46.759 50.361 25.746 1.00 48.35 ? 241 LEU A CD2 1 ATOM 1913 N N . ASN A 1 242 ? -50.346 52.284 28.274 1.00 53.67 ? 242 ASN A N 1 ATOM 1914 C CA . ASN A 1 242 ? -50.209 52.144 29.717 1.00 52.37 ? 242 ASN A CA 1 ATOM 1915 C C . ASN A 1 242 ? -49.736 50.744 30.079 1.00 51.35 ? 242 ASN A C 1 ATOM 1916 O O . ASN A 1 242 ? -50.288 49.754 29.600 1.00 56.59 ? 242 ASN A O 1 ATOM 1917 C CB . ASN A 1 242 ? -51.528 52.460 30.431 1.00 54.36 ? 242 ASN A CB 1 ATOM 1918 C CG . ASN A 1 242 ? -51.824 53.948 30.482 1.00 58.22 ? 242 ASN A CG 1 ATOM 1919 O OD1 . ASN A 1 242 ? -50.915 54.777 30.412 1.00 62.58 ? 242 ASN A OD1 1 ATOM 1920 N ND2 . ASN A 1 242 ? -53.099 54.295 30.613 1.00 61.26 ? 242 ASN A ND2 1 ATOM 1921 N N . VAL A 1 243 ? -48.704 50.668 30.913 1.00 44.87 ? 243 VAL A N 1 ATOM 1922 C CA . VAL A 1 243 ? -48.197 49.391 31.395 1.00 46.40 ? 243 VAL A CA 1 ATOM 1923 C C . VAL A 1 243 ? -48.464 49.286 32.891 1.00 50.96 ? 243 VAL A C 1 ATOM 1924 O O . VAL A 1 243 ? -48.299 50.261 33.630 1.00 54.68 ? 243 VAL A O 1 ATOM 1925 C CB . VAL A 1 243 ? -46.687 49.247 31.136 1.00 47.17 ? 243 VAL A CB 1 ATOM 1926 C CG1 . VAL A 1 243 ? -46.202 47.867 31.538 1.00 43.15 ? 243 VAL A CG1 1 ATOM 1927 C CG2 . VAL A 1 243 ? -46.379 49.497 29.677 1.00 49.80 ? 243 VAL A CG2 1 ATOM 1928 N N . GLU A 1 244 ? -48.889 48.109 33.333 1.00 60.34 ? 244 GLU A N 1 ATOM 1929 C CA . GLU A 1 244 ? -49.141 47.878 34.747 1.00 62.34 ? 244 GLU A CA 1 ATOM 1930 C C . GLU A 1 244 ? -48.886 46.413 35.066 1.00 62.52 ? 244 GLU A C 1 ATOM 1931 O O . GLU A 1 244 ? -49.517 45.519 34.490 1.00 59.99 ? 244 GLU A O 1 ATOM 1932 C CB . GLU A 1 244 ? -50.577 48.270 35.119 1.00 60.50 ? 244 GLU A CB 1 ATOM 1933 C CG . GLU A 1 244 ? -50.883 48.192 36.610 1.00 68.59 ? 244 GLU A CG 1 ATOM 1934 C CD . GLU A 1 244 ? -52.359 48.410 36.923 1.00 79.42 ? 244 GLU A CD 1 ATOM 1935 O OE1 . GLU A 1 244 ? -52.852 47.811 37.908 1.00 70.91 ? 244 GLU A OE1 1 ATOM 1936 O OE2 . GLU A 1 244 ? -53.023 49.180 36.190 1.00 75.21 ? 244 GLU A OE2 1 ATOM 1937 N N . SER A 1 245 ? -47.951 46.173 35.979 1.00 52.77 ? 245 SER A N 1 ATOM 1938 C CA . SER A 1 245 ? -47.609 44.819 36.393 1.00 55.06 ? 245 SER A CA 1 ATOM 1939 C C . SER A 1 245 ? -47.196 44.804 37.859 1.00 57.00 ? 245 SER A C 1 ATOM 1940 O O . SER A 1 245 ? -46.830 45.841 38.424 1.00 54.65 ? 245 SER A O 1 ATOM 1941 C CB . SER A 1 245 ? -46.472 44.267 35.526 1.00 47.99 ? 245 SER A CB 1 ATOM 1942 O OG . SER A 1 245 ? -46.072 42.982 35.962 1.00 48.46 ? 245 SER A OG 1 ATOM 1943 N N . ASN A 1 246 ? -47.266 43.627 38.472 1.00 60.86 ? 246 ASN A N 1 ATOM 1944 C CA . ASN A 1 246 ? -46.751 43.432 39.822 1.00 63.01 ? 246 ASN A CA 1 ATOM 1945 C C . ASN A 1 246 ? -45.775 42.260 39.848 1.00 65.13 ? 246 ASN A C 1 ATOM 1946 O O . ASN A 1 246 ? -45.523 41.670 40.902 1.00 67.33 ? 246 ASN A O 1 ATOM 1947 C CB . ASN A 1 246 ? -47.890 43.191 40.817 1.00 60.10 ? 246 ASN A CB 1 ATOM 1948 C CG . ASN A 1 246 ? -48.635 41.895 40.551 1.00 64.87 ? 246 ASN A CG 1 ATOM 1949 O OD1 . ASN A 1 246 ? -48.584 41.348 39.448 1.00 66.19 ? 246 ASN A OD1 1 ATOM 1950 N ND2 . ASN A 1 246 ? -49.342 41.403 41.561 1.00 67.03 ? 246 ASN A ND2 1 ATOM 1951 N N . GLY A 1 247 ? -45.232 41.921 38.680 1.00 62.04 ? 247 GLY A N 1 ATOM 1952 C CA . GLY A 1 247 ? -44.278 40.829 38.572 1.00 61.74 ? 247 GLY A CA 1 ATOM 1953 C C . GLY A 1 247 ? -44.354 40.074 37.257 1.00 62.80 ? 247 GLY A C 1 ATOM 1954 O O . GLY A 1 247 ? -45.349 40.171 36.533 1.00 63.62 ? 247 GLY A O 1 ATOM 1955 N N . ASN A 1 248 ? -43.293 39.323 36.959 1.00 60.31 ? 248 ASN A N 1 ATOM 1956 C CA . ASN A 1 248 ? -43.185 38.524 35.734 1.00 59.60 ? 248 ASN A CA 1 ATOM 1957 C C . ASN A 1 248 ? -43.179 39.338 34.437 1.00 57.49 ? 248 ASN A C 1 ATOM 1958 O O . ASN A 1 248 ? -43.448 38.804 33.360 1.00 57.39 ? 248 ASN A O 1 ATOM 1959 C CB . ASN A 1 248 ? -44.269 37.439 35.680 1.00 55.56 ? 248 ASN A CB 1 ATOM 1960 C CG . ASN A 1 248 ? -44.261 36.552 36.903 1.00 58.48 ? 248 ASN A CG 1 ATOM 1961 O OD1 . ASN A 1 248 ? -44.828 36.900 37.937 1.00 63.04 ? 248 ASN A OD1 1 ATOM 1962 N ND2 . ASN A 1 248 ? -43.618 35.399 36.792 1.00 58.32 ? 248 ASN A ND2 1 ATOM 1963 N N . LEU A 1 249 ? -42.851 40.622 34.535 1.00 47.31 ? 249 LEU A N 1 ATOM 1964 C CA . LEU A 1 249 ? -42.824 41.475 33.355 1.00 45.86 ? 249 LEU A CA 1 ATOM 1965 C C . LEU A 1 249 ? -41.438 41.584 32.731 1.00 47.13 ? 249 LEU A C 1 ATOM 1966 O O . LEU A 1 249 ? -40.479 41.994 33.388 1.00 49.77 ? 249 LEU A O 1 ATOM 1967 C CB . LEU A 1 249 ? -43.339 42.880 33.682 1.00 48.03 ? 249 LEU A CB 1 ATOM 1968 C CG . LEU A 1 249 ? -43.191 43.911 32.556 1.00 44.08 ? 249 LEU A CG 1 ATOM 1969 C CD1 . LEU A 1 249 ? -44.053 43.513 31.380 1.00 45.09 ? 249 LEU A CD1 1 ATOM 1970 C CD2 . LEU A 1 249 ? -43.546 45.318 33.021 1.00 43.43 ? 249 LEU A CD2 1 ATOM 1971 N N . ILE A 1 250 ? -41.338 41.208 31.458 1.00 54.35 ? 250 ILE A N 1 ATOM 1972 C CA . ILE A 1 250 ? -40.200 41.603 30.639 1.00 50.02 ? 250 ILE A CA 1 ATOM 1973 C C . ILE A 1 250 ? -40.630 42.907 29.970 1.00 50.07 ? 250 ILE A C 1 ATOM 1974 O O . ILE A 1 250 ? -41.467 42.900 29.067 1.00 52.44 ? 250 ILE A O 1 ATOM 1975 C CB . ILE A 1 250 ? -39.844 40.543 29.575 1.00 48.21 ? 250 ILE A CB 1 ATOM 1976 C CG1 . ILE A 1 250 ? -39.746 39.147 30.205 1.00 49.50 ? 250 ILE A CG1 1 ATOM 1977 C CG2 . ILE A 1 250 ? -38.540 40.903 28.872 1.00 46.62 ? 250 ILE A CG2 1 ATOM 1978 C CD1 . ILE A 1 250 ? -38.738 39.038 31.341 1.00 46.78 ? 250 ILE A CD1 1 ATOM 1979 N N . ALA A 1 251 ? -40.079 44.029 30.426 1.00 45.99 ? 251 ALA A N 1 ATOM 1980 C CA . ALA A 1 251 ? -40.591 45.340 30.028 1.00 47.96 ? 251 ALA A CA 1 ATOM 1981 C C . ALA A 1 251 ? -40.075 45.824 28.675 1.00 44.43 ? 251 ALA A C 1 ATOM 1982 O O . ALA A 1 251 ? -38.942 45.527 28.289 1.00 45.42 ? 251 ALA A O 1 ATOM 1983 C CB . ALA A 1 251 ? -40.289 46.374 31.107 1.00 46.82 ? 251 ALA A CB 1 ATOM 1984 N N . PRO A 1 252 ? -40.908 46.588 27.953 1.00 38.87 ? 252 PRO A N 1 ATOM 1985 C CA . PRO A 1 252 ? -40.386 47.283 26.773 1.00 41.99 ? 252 PRO A CA 1 ATOM 1986 C C . PRO A 1 252 ? -39.389 48.342 27.234 1.00 44.21 ? 252 PRO A C 1 ATOM 1987 O O . PRO A 1 252 ? -39.657 49.030 28.223 1.00 45.91 ? 252 PRO A O 1 ATOM 1988 C CB . PRO A 1 252 ? -41.633 47.941 26.166 1.00 36.00 ? 252 PRO A CB 1 ATOM 1989 C CG . PRO A 1 252 ? -42.634 48.005 27.289 1.00 39.36 ? 252 PRO A CG 1 ATOM 1990 C CD . PRO A 1 252 ? -42.351 46.815 28.154 1.00 38.58 ? 252 PRO A CD 1 ATOM 1991 N N . TRP A 1 253 ? -38.257 48.454 26.545 1.00 43.94 ? 253 TRP A N 1 ATOM 1992 C CA . TRP A 1 253 ? -37.218 49.414 26.900 1.00 39.82 ? 253 TRP A CA 1 ATOM 1993 C C . TRP A 1 253 ? -36.955 50.325 25.706 1.00 41.92 ? 253 TRP A C 1 ATOM 1994 O O . TRP A 1 253 ? -37.249 51.522 25.747 1.00 39.94 ? 253 TRP A O 1 ATOM 1995 C CB . TRP A 1 253 ? -35.943 48.671 27.305 1.00 39.61 ? 253 TRP A CB 1 ATOM 1996 C CG . TRP A 1 253 ? -34.818 49.566 27.768 1.00 45.11 ? 253 TRP A CG 1 ATOM 1997 C CD1 . TRP A 1 253 ? -34.895 50.896 28.074 1.00 41.19 ? 253 TRP A CD1 1 ATOM 1998 C CD2 . TRP A 1 253 ? -33.448 49.185 27.979 1.00 44.78 ? 253 TRP A CD2 1 ATOM 1999 N NE1 . TRP A 1 253 ? -33.661 51.362 28.457 1.00 44.91 ? 253 TRP A NE1 1 ATOM 2000 C CE2 . TRP A 1 253 ? -32.757 50.333 28.409 1.00 45.06 ? 253 TRP A CE2 1 ATOM 2001 C CE3 . TRP A 1 253 ? -32.744 47.983 27.845 1.00 42.88 ? 253 TRP A CE3 1 ATOM 2002 C CZ2 . TRP A 1 253 ? -31.388 50.319 28.703 1.00 41.80 ? 253 TRP A CZ2 1 ATOM 2003 C CZ3 . TRP A 1 253 ? -31.387 47.968 28.137 1.00 45.15 ? 253 TRP A CZ3 1 ATOM 2004 C CH2 . TRP A 1 253 ? -30.723 49.129 28.561 1.00 42.52 ? 253 TRP A CH2 1 ATOM 2005 N N . TYR A 1 254 ? -36.398 49.746 24.646 1.00 42.82 ? 254 TYR A N 1 ATOM 2006 C CA . TYR A 1 254 ? -36.249 50.437 23.370 1.00 45.94 ? 254 TYR A CA 1 ATOM 2007 C C . TYR A 1 254 ? -37.302 49.953 22.363 1.00 41.97 ? 254 TYR A C 1 ATOM 2008 O O . TYR A 1 254 ? -37.679 48.779 22.360 1.00 40.02 ? 254 TYR A O 1 ATOM 2009 C CB . TYR A 1 254 ? -34.845 50.213 22.806 1.00 47.39 ? 254 TYR A CB 1 ATOM 2010 C CG . TYR A 1 254 ? -33.764 51.012 23.495 1.00 50.79 ? 254 TYR A CG 1 ATOM 2011 C CD1 . TYR A 1 254 ? -33.137 50.537 24.644 1.00 52.51 ? 254 TYR A CD1 1 ATOM 2012 C CD2 . TYR A 1 254 ? -33.357 52.238 22.987 1.00 51.98 ? 254 TYR A CD2 1 ATOM 2013 C CE1 . TYR A 1 254 ? -32.140 51.269 25.269 1.00 50.53 ? 254 TYR A CE1 1 ATOM 2014 C CE2 . TYR A 1 254 ? -32.365 52.975 23.605 1.00 52.81 ? 254 TYR A CE2 1 ATOM 2015 C CZ . TYR A 1 254 ? -31.761 52.487 24.744 1.00 54.91 ? 254 TYR A CZ 1 ATOM 2016 O OH . TYR A 1 254 ? -30.773 53.222 25.354 1.00 52.51 ? 254 TYR A OH 1 ATOM 2017 N N . ALA A 1 255 ? -37.771 50.858 21.510 1.00 41.15 ? 255 ALA A N 1 ATOM 2018 C CA . ALA A 1 255 ? -38.766 50.513 20.495 1.00 36.92 ? 255 ALA A CA 1 ATOM 2019 C C . ALA A 1 255 ? -38.373 51.110 19.145 1.00 34.15 ? 255 ALA A C 1 ATOM 2020 O O . ALA A 1 255 ? -37.292 51.685 19.009 1.00 37.54 ? 255 ALA A O 1 ATOM 2021 C CB . ALA A 1 255 ? -40.143 50.987 20.917 1.00 38.61 ? 255 ALA A CB 1 ATOM 2022 N N . TYR A 1 256 ? -39.244 50.988 18.149 1.00 36.42 ? 256 TYR A N 1 ATOM 2023 C CA . TYR A 1 256 ? -38.904 51.464 16.809 1.00 36.09 ? 256 TYR A CA 1 ATOM 2024 C C . TYR A 1 256 ? -39.949 52.386 16.196 1.00 34.22 ? 256 TYR A C 1 ATOM 2025 O O . TYR A 1 256 ? -41.126 52.036 16.112 1.00 38.30 ? 256 TYR A O 1 ATOM 2026 C CB . TYR A 1 256 ? -38.671 50.282 15.859 1.00 32.87 ? 256 TYR A CB 1 ATOM 2027 C CG . TYR A 1 256 ? -37.511 49.398 16.230 1.00 32.55 ? 256 TYR A CG 1 ATOM 2028 C CD1 . TYR A 1 256 ? -36.215 49.722 15.849 1.00 36.52 ? 256 TYR A CD1 1 ATOM 2029 C CD2 . TYR A 1 256 ? -37.709 48.233 16.953 1.00 33.52 ? 256 TYR A CD2 1 ATOM 2030 C CE1 . TYR A 1 256 ? -35.144 48.908 16.186 1.00 34.44 ? 256 TYR A CE1 1 ATOM 2031 C CE2 . TYR A 1 256 ? -36.645 47.414 17.296 1.00 37.82 ? 256 TYR A CE2 1 ATOM 2032 C CZ . TYR A 1 256 ? -35.368 47.757 16.909 1.00 38.10 ? 256 TYR A CZ 1 ATOM 2033 O OH . TYR A 1 256 ? -34.312 46.946 17.252 1.00 43.45 ? 256 TYR A OH 1 ATOM 2034 N N . LYS A 1 257 ? -39.520 53.562 15.758 1.00 36.48 ? 257 LYS A N 1 ATOM 2035 C CA . LYS A 1 257 ? -40.365 54.365 14.891 1.00 41.60 ? 257 LYS A CA 1 ATOM 2036 C C . LYS A 1 257 ? -40.318 53.742 13.499 1.00 37.00 ? 257 LYS A C 1 ATOM 2037 O O . LYS A 1 257 ? -39.245 53.542 12.927 1.00 38.55 ? 257 LYS A O 1 ATOM 2038 C CB . LYS A 1 257 ? -39.918 55.823 14.888 1.00 45.62 ? 257 LYS A CB 1 ATOM 2039 C CG . LYS A 1 257 ? -40.538 56.607 16.033 1.00 46.20 ? 257 LYS A CG 1 ATOM 2040 C CD . LYS A 1 257 ? -39.604 57.670 16.577 1.00 54.68 ? 257 LYS A CD 1 ATOM 2041 C CE . LYS A 1 257 ? -40.219 58.335 17.798 1.00 55.89 ? 257 LYS A CE 1 ATOM 2042 N NZ . LYS A 1 257 ? -39.324 59.385 18.358 1.00 67.77 ? 257 LYS A NZ 1 ATOM 2043 N N . PHE A 1 258 ? -41.490 53.414 12.972 1.00 40.98 ? 258 PHE A N 1 ATOM 2044 C CA . PHE A 1 258 ? -41.593 52.570 11.793 1.00 40.26 ? 258 PHE A CA 1 ATOM 2045 C C . PHE A 1 258 ? -42.125 53.352 10.592 1.00 38.97 ? 258 PHE A C 1 ATOM 2046 O O . PHE A 1 258 ? -43.210 53.933 10.659 1.00 43.09 ? 258 PHE A O 1 ATOM 2047 C CB . PHE A 1 258 ? -42.522 51.408 12.130 1.00 39.22 ? 258 PHE A CB 1 ATOM 2048 C CG . PHE A 1 258 ? -42.612 50.370 11.068 1.00 41.27 ? 258 PHE A CG 1 ATOM 2049 C CD1 . PHE A 1 258 ? -41.729 49.300 11.055 1.00 40.26 ? 258 PHE A CD1 1 ATOM 2050 C CD2 . PHE A 1 258 ? -43.596 50.444 10.094 1.00 40.46 ? 258 PHE A CD2 1 ATOM 2051 C CE1 . PHE A 1 258 ? -41.814 48.329 10.074 1.00 43.15 ? 258 PHE A CE1 1 ATOM 2052 C CE2 . PHE A 1 258 ? -43.689 49.480 9.112 1.00 43.87 ? 258 PHE A CE2 1 ATOM 2053 C CZ . PHE A 1 258 ? -42.799 48.417 9.104 1.00 41.76 ? 258 PHE A CZ 1 ATOM 2054 N N . VAL A 1 259 ? -41.357 53.376 9.503 1.00 32.35 ? 259 VAL A N 1 ATOM 2055 C CA . VAL A 1 259 ? -41.808 53.991 8.255 1.00 36.89 ? 259 VAL A CA 1 ATOM 2056 C C . VAL A 1 259 ? -42.300 52.907 7.301 1.00 38.42 ? 259 VAL A C 1 ATOM 2057 O O . VAL A 1 259 ? -41.513 52.064 6.847 1.00 39.12 ? 259 VAL A O 1 ATOM 2058 C CB . VAL A 1 259 ? -40.681 54.781 7.560 1.00 40.14 ? 259 VAL A CB 1 ATOM 2059 C CG1 . VAL A 1 259 ? -41.246 55.614 6.423 1.00 37.16 ? 259 VAL A CG1 1 ATOM 2060 C CG2 . VAL A 1 259 ? -39.963 55.675 8.551 1.00 42.57 ? 259 VAL A CG2 1 ATOM 2061 N N . SER A 1 260 ? -43.595 52.921 6.998 1.00 46.62 ? 260 SER A N 1 ATOM 2062 C CA . SER A 1 260 ? -44.176 51.928 6.092 1.00 49.66 ? 260 SER A CA 1 ATOM 2063 C C . SER A 1 260 ? -43.865 52.252 4.634 1.00 57.57 ? 260 SER A C 1 ATOM 2064 O O . SER A 1 260 ? -44.013 53.399 4.201 1.00 56.59 ? 260 SER A O 1 ATOM 2065 C CB . SER A 1 260 ? -45.689 51.849 6.281 1.00 50.20 ? 260 SER A CB 1 ATOM 2066 O OG . SER A 1 260 ? -46.287 51.099 5.240 1.00 61.78 ? 260 SER A OG 1 ATOM 2067 N N . THR A 1 261 ? -43.437 51.240 3.880 1.00 86.15 ? 261 THR A N 1 ATOM 2068 C CA . THR A 1 261 ? -43.180 51.417 2.450 1.00 90.73 ? 261 THR A CA 1 ATOM 2069 C C . THR A 1 261 ? -44.503 51.594 1.697 1.00 96.46 ? 261 THR A C 1 ATOM 2070 O O . THR A 1 261 ? -45.484 50.883 1.945 1.00 94.52 ? 261 THR A O 1 ATOM 2071 C CB . THR A 1 261 ? -42.310 50.261 1.837 1.00 90.63 ? 261 THR A CB 1 ATOM 2072 O OG1 . THR A 1 261 ? -41.706 50.692 0.608 1.00 100.99 ? 261 THR A OG1 1 ATOM 2073 C CG2 . THR A 1 261 ? -43.131 48.994 1.579 1.00 91.23 ? 261 THR A CG2 1 ATOM 2074 N N . ASN A 1 262 ? -44.536 52.581 0.811 1.00 120.63 ? 262 ASN A N 1 ATOM 2075 C CA . ASN A 1 262 ? -45.660 52.748 -0.095 1.00 130.36 ? 262 ASN A CA 1 ATOM 2076 C C . ASN A 1 262 ? -45.672 51.597 -1.095 1.00 131.12 ? 262 ASN A C 1 ATOM 2077 O O . ASN A 1 262 ? -46.731 51.181 -1.576 1.00 129.77 ? 262 ASN A O 1 ATOM 2078 C CB . ASN A 1 262 ? -45.567 54.093 -0.824 1.00 136.27 ? 262 ASN A CB 1 ATOM 2079 C CG . ASN A 1 262 ? -46.241 54.071 -2.188 1.00 140.98 ? 262 ASN A CG 1 ATOM 2080 O OD1 . ASN A 1 262 ? -45.574 53.982 -3.222 1.00 144.23 ? 262 ASN A OD1 1 ATOM 2081 N ND2 . ASN A 1 262 ? -47.569 54.144 -2.196 1.00 135.75 ? 262 ASN A ND2 1 ATOM 2082 N N . LYS A 1 263 ? -44.482 51.073 -1.380 1.00 102.09 ? 263 LYS A N 1 ATOM 2083 C CA . LYS A 1 263 ? -44.315 50.033 -2.387 1.00 99.81 ? 263 LYS A CA 1 ATOM 2084 C C . LYS A 1 263 ? -44.764 48.656 -1.905 1.00 98.62 ? 263 LYS A C 1 ATOM 2085 O O . LYS A 1 263 ? -45.810 48.506 -1.267 1.00 97.74 ? 263 LYS A O 1 ATOM 2086 C CB . LYS A 1 263 ? -42.854 49.954 -2.847 1.00 103.53 ? 263 LYS A CB 1 ATOM 2087 C CG . LYS A 1 263 ? -42.162 51.299 -3.033 1.00 106.46 ? 263 LYS A CG 1 ATOM 2088 C CD . LYS A 1 263 ? -42.900 52.194 -4.019 1.00 116.69 ? 263 LYS A CD 1 ATOM 2089 C CE . LYS A 1 263 ? -42.261 53.577 -4.080 1.00 120.85 ? 263 LYS A CE 1 ATOM 2090 N NZ . LYS A 1 263 ? -43.242 54.641 -4.442 1.00 116.31 ? 263 LYS A NZ 1 ATOM 2091 N N . LYS A 1 264 ? -43.949 47.655 -2.213 1.00 95.25 ? 264 LYS A N 1 ATOM 2092 C CA . LYS A 1 264 ? -44.320 46.262 -2.010 1.00 90.60 ? 264 LYS A CA 1 ATOM 2093 C C . LYS A 1 264 ? -43.687 45.679 -0.752 1.00 87.97 ? 264 LYS A C 1 ATOM 2094 O O . LYS A 1 264 ? -44.388 45.206 0.149 1.00 89.91 ? 264 LYS A O 1 ATOM 2095 C CB . LYS A 1 264 ? -43.902 45.449 -3.233 1.00 84.76 ? 264 LYS A CB 1 ATOM 2096 C CG . LYS A 1 264 ? -44.287 43.985 -3.200 1.00 81.01 ? 264 LYS A CG 1 ATOM 2097 C CD . LYS A 1 264 ? -43.789 43.328 -4.473 1.00 78.71 ? 264 LYS A CD 1 ATOM 2098 C CE . LYS A 1 264 ? -44.020 41.832 -4.479 1.00 74.81 ? 264 LYS A CE 1 ATOM 2099 N NZ . LYS A 1 264 ? -43.493 41.255 -5.751 1.00 63.27 ? 264 LYS A NZ 1 ATOM 2100 N N . GLY A 1 265 ? -42.359 45.714 -0.693 1.00 61.48 ? 265 GLY A N 1 ATOM 2101 C CA . GLY A 1 265 ? -41.643 45.149 0.435 1.00 52.57 ? 265 GLY A CA 1 ATOM 2102 C C . GLY A 1 265 ? -41.376 43.664 0.267 1.00 44.62 ? 265 GLY A C 1 ATOM 2103 O O . GLY A 1 265 ? -42.295 42.884 0.006 1.00 47.79 ? 265 GLY A O 1 ATOM 2104 N N . ALA A 1 266 ? -40.117 43.265 0.425 1.00 38.95 ? 266 ALA A N 1 ATOM 2105 C CA . ALA A 1 266 ? -39.753 41.859 0.286 1.00 38.35 ? 266 ALA A CA 1 ATOM 2106 C C . ALA A 1 266 ? -38.814 41.387 1.393 1.00 36.65 ? 266 ALA A C 1 ATOM 2107 O O . ALA A 1 266 ? -37.996 42.158 1.893 1.00 32.05 ? 266 ALA A O 1 ATOM 2108 C CB . ALA A 1 266 ? -39.127 41.607 -1.078 1.00 35.43 ? 266 ALA A CB 1 ATOM 2109 N N . VAL A 1 267 ? -38.941 40.116 1.767 1.00 44.11 ? 267 VAL A N 1 ATOM 2110 C CA . VAL A 1 267 ? -37.977 39.469 2.647 1.00 38.09 ? 267 VAL A CA 1 ATOM 2111 C C . VAL A 1 267 ? -37.426 38.248 1.925 1.00 40.70 ? 267 VAL A C 1 ATOM 2112 O O . VAL A 1 267 ? -38.122 37.242 1.768 1.00 44.87 ? 267 VAL A O 1 ATOM 2113 C CB . VAL A 1 267 ? -38.604 39.041 3.991 1.00 42.21 ? 267 VAL A CB 1 ATOM 2114 C CG1 . VAL A 1 267 ? -37.597 38.257 4.825 1.00 37.34 ? 267 VAL A CG1 1 ATOM 2115 C CG2 . VAL A 1 267 ? -39.092 40.255 4.768 1.00 40.62 ? 267 VAL A CG2 1 ATOM 2116 N N . PHE A 1 268 ? -36.182 38.342 1.467 1.00 38.75 ? 268 PHE A N 1 ATOM 2117 C CA . PHE A 1 268 ? -35.570 37.257 0.714 1.00 35.68 ? 268 PHE A CA 1 ATOM 2118 C C . PHE A 1 268 ? -34.777 36.321 1.620 1.00 39.60 ? 268 PHE A C 1 ATOM 2119 O O . PHE A 1 268 ? -33.883 36.762 2.344 1.00 42.82 ? 268 PHE A O 1 ATOM 2120 C CB . PHE A 1 268 ? -34.668 37.823 -0.382 1.00 36.75 ? 268 PHE A CB 1 ATOM 2121 C CG . PHE A 1 268 ? -35.417 38.529 -1.476 1.00 39.26 ? 268 PHE A CG 1 ATOM 2122 C CD1 . PHE A 1 268 ? -36.706 38.134 -1.813 1.00 38.93 ? 268 PHE A CD1 1 ATOM 2123 C CD2 . PHE A 1 268 ? -34.839 39.588 -2.165 1.00 37.80 ? 268 PHE A CD2 1 ATOM 2124 C CE1 . PHE A 1 268 ? -37.410 38.780 -2.825 1.00 34.20 ? 268 PHE A CE1 1 ATOM 2125 C CE2 . PHE A 1 268 ? -35.535 40.242 -3.178 1.00 36.46 ? 268 PHE A CE2 1 ATOM 2126 C CZ . PHE A 1 268 ? -36.822 39.837 -3.507 1.00 37.07 ? 268 PHE A CZ 1 ATOM 2127 N N . LYS A 1 269 ? -35.117 35.034 1.583 1.00 44.65 ? 269 LYS A N 1 ATOM 2128 C CA . LYS A 1 269 ? -34.353 34.005 2.285 1.00 44.60 ? 269 LYS A CA 1 ATOM 2129 C C . LYS A 1 269 ? -33.356 33.418 1.294 1.00 46.51 ? 269 LYS A C 1 ATOM 2130 O O . LYS A 1 269 ? -33.713 32.574 0.462 1.00 49.51 ? 269 LYS A O 1 ATOM 2131 C CB . LYS A 1 269 ? -35.278 32.900 2.795 1.00 46.42 ? 269 LYS A CB 1 ATOM 2132 C CG . LYS A 1 269 ? -35.129 32.568 4.270 1.00 60.32 ? 269 LYS A CG 1 ATOM 2133 C CD . LYS A 1 269 ? -36.502 32.510 4.928 1.00 68.07 ? 269 LYS A CD 1 ATOM 2134 C CE . LYS A 1 269 ? -37.287 33.788 4.631 1.00 67.84 ? 269 LYS A CE 1 ATOM 2135 N NZ . LYS A 1 269 ? -38.760 33.561 4.527 1.00 65.53 ? 269 LYS A NZ 1 ATOM 2136 N N . SER A 1 270 ? -32.109 33.866 1.371 1.00 38.12 ? 270 SER A N 1 ATOM 2137 C CA . SER A 1 270 ? -31.111 33.473 0.386 1.00 40.03 ? 270 SER A CA 1 ATOM 2138 C C . SER A 1 270 ? -29.705 33.539 0.958 1.00 44.03 ? 270 SER A C 1 ATOM 2139 O O . SER A 1 270 ? -29.449 34.262 1.924 1.00 44.39 ? 270 SER A O 1 ATOM 2140 C CB . SER A 1 270 ? -31.213 34.374 -0.848 1.00 37.36 ? 270 SER A CB 1 ATOM 2141 O OG . SER A 1 270 ? -30.243 34.029 -1.817 1.00 37.57 ? 270 SER A OG 1 ATOM 2142 N N . ASP A 1 271 ? -28.796 32.780 0.355 1.00 47.82 ? 271 ASP A N 1 ATOM 2143 C CA . ASP A 1 271 ? -27.387 32.825 0.730 1.00 52.29 ? 271 ASP A CA 1 ATOM 2144 C C . ASP A 1 271 ? -26.567 33.522 -0.358 1.00 51.04 ? 271 ASP A C 1 ATOM 2145 O O . ASP A 1 271 ? -25.340 33.398 -0.400 1.00 53.28 ? 271 ASP A O 1 ATOM 2146 C CB . ASP A 1 271 ? -26.850 31.413 0.997 1.00 54.69 ? 271 ASP A CB 1 ATOM 2147 C CG . ASP A 1 271 ? -27.082 30.464 -0.175 1.00 77.57 ? 271 ASP A CG 1 ATOM 2148 O OD1 . ASP A 1 271 ? -26.228 29.579 -0.402 1.00 79.10 ? 271 ASP A OD1 1 ATOM 2149 O OD2 . ASP A 1 271 ? -28.120 30.596 -0.870 1.00 78.36 ? 271 ASP A OD2 1 ATOM 2150 N N . LEU A 1 272 ? -27.259 34.260 -1.228 1.00 43.82 ? 272 LEU A N 1 ATOM 2151 C CA . LEU A 1 272 ? -26.625 34.994 -2.328 1.00 44.63 ? 272 LEU A CA 1 ATOM 2152 C C . LEU A 1 272 ? -25.901 36.250 -1.834 1.00 42.14 ? 272 LEU A C 1 ATOM 2153 O O . LEU A 1 272 ? -26.366 36.924 -0.909 1.00 39.90 ? 272 LEU A O 1 ATOM 2154 C CB . LEU A 1 272 ? -27.654 35.379 -3.402 1.00 36.48 ? 272 LEU A CB 1 ATOM 2155 C CG . LEU A 1 272 ? -28.195 34.281 -4.323 1.00 42.76 ? 272 LEU A CG 1 ATOM 2156 C CD1 . LEU A 1 272 ? -29.125 34.862 -5.394 1.00 35.10 ? 272 LEU A CD1 1 ATOM 2157 C CD2 . LEU A 1 272 ? -27.051 33.525 -4.972 1.00 39.68 ? 272 LEU A CD2 1 ATOM 2158 N N . PRO A 1 273 ? -24.758 36.571 -2.460 1.00 38.17 ? 273 PRO A N 1 ATOM 2159 C CA . PRO A 1 273 ? -23.952 37.733 -2.067 1.00 39.24 ? 273 PRO A CA 1 ATOM 2160 C C . PRO A 1 273 ? -24.639 39.054 -2.392 1.00 39.82 ? 273 PRO A C 1 ATOM 2161 O O . PRO A 1 273 ? -25.279 39.161 -3.438 1.00 39.25 ? 273 PRO A O 1 ATOM 2162 C CB . PRO A 1 273 ? -22.695 37.593 -2.933 1.00 42.79 ? 273 PRO A CB 1 ATOM 2163 C CG . PRO A 1 273 ? -23.151 36.804 -4.139 1.00 42.46 ? 273 PRO A CG 1 ATOM 2164 C CD . PRO A 1 273 ? -24.152 35.826 -3.581 1.00 40.18 ? 273 PRO A CD 1 ATOM 2165 N N . ILE A 1 274 ? -24.509 40.039 -1.507 1.00 44.77 ? 274 ILE A N 1 ATOM 2166 C CA . ILE A 1 274 ? -24.944 41.400 -1.800 1.00 42.99 ? 274 ILE A CA 1 ATOM 2167 C C . ILE A 1 274 ? -23.730 42.165 -2.318 1.00 47.82 ? 274 ILE A C 1 ATOM 2168 O O . ILE A 1 274 ? -22.741 42.322 -1.600 1.00 53.70 ? 274 ILE A O 1 ATOM 2169 C CB . ILE A 1 274 ? -25.480 42.113 -0.545 1.00 43.06 ? 274 ILE A CB 1 ATOM 2170 C CG1 . ILE A 1 274 ? -26.586 41.288 0.110 1.00 41.40 ? 274 ILE A CG1 1 ATOM 2171 C CG2 . ILE A 1 274 ? -25.982 43.514 -0.886 1.00 38.46 ? 274 ILE A CG2 1 ATOM 2172 C CD1 . ILE A 1 274 ? -27.212 41.959 1.308 1.00 39.78 ? 274 ILE A CD1 1 ATOM 2173 N N . GLU A 1 275 ? -23.798 42.633 -3.561 1.00 52.68 ? 275 GLU A N 1 ATOM 2174 C CA . GLU A 1 275 ? -22.658 43.300 -4.184 1.00 52.00 ? 275 GLU A CA 1 ATOM 2175 C C . GLU A 1 275 ? -22.928 44.786 -4.388 1.00 54.48 ? 275 GLU A C 1 ATOM 2176 O O . GLU A 1 275 ? -24.030 45.268 -4.112 1.00 53.02 ? 275 GLU A O 1 ATOM 2177 C CB . GLU A 1 275 ? -22.291 42.617 -5.508 1.00 53.73 ? 275 GLU A CB 1 ATOM 2178 C CG . GLU A 1 275 ? -21.887 41.150 -5.355 1.00 51.83 ? 275 GLU A CG 1 ATOM 2179 C CD . GLU A 1 275 ? -21.466 40.502 -6.670 1.00 64.37 ? 275 GLU A CD 1 ATOM 2180 O OE1 . GLU A 1 275 ? -21.330 41.224 -7.686 1.00 60.51 ? 275 GLU A OE1 1 ATOM 2181 O OE2 . GLU A 1 275 ? -21.267 39.266 -6.682 1.00 60.31 ? 275 GLU A OE2 1 ATOM 2182 N N . ASN A 1 276 ? -21.922 45.513 -4.862 1.00 56.17 ? 276 ASN A N 1 ATOM 2183 C CA . ASN A 1 276 ? -22.081 46.943 -5.089 1.00 60.01 ? 276 ASN A CA 1 ATOM 2184 C C . ASN A 1 276 ? -22.555 47.215 -6.513 1.00 65.32 ? 276 ASN A C 1 ATOM 2185 O O . ASN A 1 276 ? -21.751 47.492 -7.408 1.00 66.01 ? 276 ASN A O 1 ATOM 2186 C CB . ASN A 1 276 ? -20.774 47.688 -4.811 1.00 60.17 ? 276 ASN A CB 1 ATOM 2187 C CG . ASN A 1 276 ? -20.960 49.191 -4.768 1.00 67.07 ? 276 ASN A CG 1 ATOM 2188 O OD1 . ASN A 1 276 ? -22.068 49.684 -4.539 1.00 63.65 ? 276 ASN A OD1 1 ATOM 2189 N ND2 . ASN A 1 276 ? -19.876 49.931 -4.992 1.00 69.32 ? 276 ASN A ND2 1 ATOM 2190 N N . CYS A 1 277 ? -23.866 47.126 -6.717 1.00 74.99 ? 277 CYS A N 1 ATOM 2191 C CA . CYS A 1 277 ? -24.455 47.301 -8.041 1.00 69.65 ? 277 CYS A CA 1 ATOM 2192 C C . CYS A 1 277 ? -25.877 47.844 -7.947 1.00 64.10 ? 277 CYS A C 1 ATOM 2193 O O . CYS A 1 277 ? -26.520 47.763 -6.895 1.00 65.22 ? 277 CYS A O 1 ATOM 2194 C CB . CYS A 1 277 ? -24.441 45.972 -8.809 1.00 68.70 ? 277 CYS A CB 1 ATOM 2195 S SG . CYS A 1 277 ? -25.185 44.559 -7.913 1.00 86.74 ? 277 CYS A SG 1 ATOM 2196 N N . ASP A 1 278 ? -26.360 48.407 -9.047 1.00 51.64 ? 278 ASP A N 1 ATOM 2197 C CA . ASP A 1 278 ? -27.735 48.877 -9.110 1.00 48.68 ? 278 ASP A CA 1 ATOM 2198 C C . ASP A 1 278 ? -28.597 47.935 -9.946 1.00 51.07 ? 278 ASP A C 1 ATOM 2199 O O . ASP A 1 278 ? -28.093 47.230 -10.826 1.00 47.59 ? 278 ASP A O 1 ATOM 2200 C CB . ASP A 1 278 ? -27.791 50.286 -9.690 1.00 45.71 ? 278 ASP A CB 1 ATOM 2201 C CG . ASP A 1 278 ? -28.073 51.331 -8.639 1.00 62.51 ? 278 ASP A CG 1 ATOM 2202 O OD1 . ASP A 1 278 ? -28.904 51.064 -7.744 1.00 65.64 ? 278 ASP A OD1 1 ATOM 2203 O OD2 . ASP A 1 278 ? -27.463 52.418 -8.704 1.00 71.55 ? 278 ASP A OD2 1 ATOM 2204 N N . ALA A 1 279 ? -29.897 47.924 -9.665 1.00 41.43 ? 279 ALA A N 1 ATOM 2205 C CA . ALA A 1 279 ? -30.835 47.109 -10.429 1.00 36.09 ? 279 ALA A CA 1 ATOM 2206 C C . ALA A 1 279 ? -32.221 47.735 -10.429 1.00 33.98 ? 279 ALA A C 1 ATOM 2207 O O . ALA A 1 279 ? -32.536 48.568 -9.581 1.00 35.92 ? 279 ALA A O 1 ATOM 2208 C CB . ALA A 1 279 ? -30.892 45.692 -9.872 1.00 34.21 ? 279 ALA A CB 1 ATOM 2209 N N . THR A 1 280 ? -33.047 47.319 -11.384 1.00 40.42 ? 280 THR A N 1 ATOM 2210 C CA . THR A 1 280 ? -34.444 47.735 -11.435 1.00 38.34 ? 280 THR A CA 1 ATOM 2211 C C . THR A 1 280 ? -35.340 46.558 -11.069 1.00 36.11 ? 280 THR A C 1 ATOM 2212 O O . THR A 1 280 ? -36.467 46.731 -10.591 1.00 38.57 ? 280 THR A O 1 ATOM 2213 C CB . THR A 1 280 ? -34.818 48.266 -12.826 1.00 44.11 ? 280 THR A CB 1 ATOM 2214 O OG1 . THR A 1 280 ? -34.180 47.466 -13.832 1.00 48.04 ? 280 THR A OG1 1 ATOM 2215 C CG2 . THR A 1 280 ? -34.372 49.708 -12.975 1.00 36.06 ? 280 THR A CG2 1 ATOM 2216 N N . CYS A 1 281 ? -34.819 45.358 -11.302 1.00 38.43 ? 281 CYS A N 1 ATOM 2217 C CA . CYS A 1 281 ? -35.545 44.124 -11.029 1.00 37.10 ? 281 CYS A CA 1 ATOM 2218 C C . CYS A 1 281 ? -34.698 43.143 -10.222 1.00 35.45 ? 281 CYS A C 1 ATOM 2219 O O . CYS A 1 281 ? -33.672 42.651 -10.701 1.00 38.41 ? 281 CYS A O 1 ATOM 2220 C CB . CYS A 1 281 ? -35.973 43.466 -12.342 1.00 36.61 ? 281 CYS A CB 1 ATOM 2221 S SG . CYS A 1 281 ? -36.658 41.803 -12.154 1.00 42.85 ? 281 CYS A SG 1 ATOM 2222 N N . GLN A 1 282 ? -35.132 42.847 -9.003 1.00 30.82 ? 282 GLN A N 1 ATOM 2223 C CA . GLN A 1 282 ? -34.397 41.920 -8.148 1.00 30.42 ? 282 GLN A CA 1 ATOM 2224 C C . GLN A 1 282 ? -35.281 40.740 -7.735 1.00 31.26 ? 282 GLN A C 1 ATOM 2225 O O . GLN A 1 282 ? -36.224 40.914 -6.955 1.00 30.70 ? 282 GLN A O 1 ATOM 2226 C CB . GLN A 1 282 ? -33.890 42.651 -6.900 1.00 27.80 ? 282 GLN A CB 1 ATOM 2227 C CG . GLN A 1 282 ? -33.140 41.764 -5.913 1.00 30.27 ? 282 GLN A CG 1 ATOM 2228 C CD . GLN A 1 282 ? -31.759 41.378 -6.412 1.00 36.23 ? 282 GLN A CD 1 ATOM 2229 O OE1 . GLN A 1 282 ? -30.877 42.230 -6.554 1.00 38.67 ? 282 GLN A OE1 1 ATOM 2230 N NE2 . GLN A 1 282 ? -31.563 40.091 -6.682 1.00 34.18 ? 282 GLN A NE2 1 ATOM 2231 N N . THR A 1 283 ? -34.990 39.548 -8.256 1.00 26.00 ? 283 THR A N 1 ATOM 2232 C CA . THR A 1 283 ? -35.671 38.336 -7.791 1.00 29.45 ? 283 THR A CA 1 ATOM 2233 C C . THR A 1 283 ? -34.879 37.701 -6.659 1.00 31.88 ? 283 THR A C 1 ATOM 2234 O O . THR A 1 283 ? -33.722 38.055 -6.428 1.00 31.75 ? 283 THR A O 1 ATOM 2235 C CB . THR A 1 283 ? -35.879 37.290 -8.910 1.00 28.14 ? 283 THR A CB 1 ATOM 2236 O OG1 . THR A 1 283 ? -34.662 36.565 -9.123 1.00 29.30 ? 283 THR A OG1 1 ATOM 2237 C CG2 . THR A 1 283 ? -36.331 37.962 -10.210 1.00 28.35 ? 283 THR A CG2 1 ATOM 2238 N N . ILE A 1 284 ? -35.501 36.754 -5.967 1.00 32.22 ? 284 ILE A N 1 ATOM 2239 C CA . ILE A 1 284 ? -34.857 36.065 -4.858 1.00 34.54 ? 284 ILE A CA 1 ATOM 2240 C C . ILE A 1 284 ? -33.658 35.230 -5.324 1.00 35.53 ? 284 ILE A C 1 ATOM 2241 O O . ILE A 1 284 ? -32.762 34.924 -4.535 1.00 35.83 ? 284 ILE A O 1 ATOM 2242 C CB . ILE A 1 284 ? -35.869 35.178 -4.096 1.00 34.63 ? 284 ILE A CB 1 ATOM 2243 C CG1 . ILE A 1 284 ? -35.286 34.694 -2.764 1.00 35.33 ? 284 ILE A CG1 1 ATOM 2244 C CG2 . ILE A 1 284 ? -36.309 33.996 -4.951 1.00 32.79 ? 284 ILE A CG2 1 ATOM 2245 C CD1 . ILE A 1 284 ? -36.232 33.820 -1.966 1.00 33.69 ? 284 ILE A CD1 1 ATOM 2246 N N . THR A 1 285 ? -33.639 34.872 -6.608 1.00 35.69 ? 285 THR A N 1 ATOM 2247 C CA . THR A 1 285 ? -32.552 34.056 -7.154 1.00 37.87 ? 285 THR A CA 1 ATOM 2248 C C . THR A 1 285 ? -31.552 34.857 -7.990 1.00 37.34 ? 285 THR A C 1 ATOM 2249 O O . THR A 1 285 ? -30.636 34.280 -8.582 1.00 40.34 ? 285 THR A O 1 ATOM 2250 C CB . THR A 1 285 ? -33.076 32.866 -7.995 1.00 41.62 ? 285 THR A CB 1 ATOM 2251 O OG1 . THR A 1 285 ? -33.839 33.359 -9.098 1.00 46.00 ? 285 THR A OG1 1 ATOM 2252 C CG2 . THR A 1 285 ? -33.948 31.942 -7.152 1.00 40.98 ? 285 THR A CG2 1 ATOM 2253 N N . GLY A 1 286 ? -31.728 36.175 -8.043 1.00 30.77 ? 286 GLY A N 1 ATOM 2254 C CA . GLY A 1 286 ? -30.806 37.018 -8.784 1.00 36.80 ? 286 GLY A CA 1 ATOM 2255 C C . GLY A 1 286 ? -31.443 38.202 -9.496 1.00 38.06 ? 286 GLY A C 1 ATOM 2256 O O . GLY A 1 286 ? -32.667 38.360 -9.485 1.00 33.12 ? 286 GLY A O 1 ATOM 2257 N N . VAL A 1 287 ? -30.601 39.022 -10.125 1.00 36.94 ? 287 VAL A N 1 ATOM 2258 C CA . VAL A 1 287 ? -31.028 40.228 -10.839 1.00 35.18 ? 287 VAL A CA 1 ATOM 2259 C C . VAL A 1 287 ? -31.398 39.935 -12.288 1.00 38.05 ? 287 VAL A C 1 ATOM 2260 O O . VAL A 1 287 ? -30.729 39.141 -12.951 1.00 38.85 ? 287 VAL A O 1 ATOM 2261 C CB . VAL A 1 287 ? -29.892 41.261 -10.868 1.00 41.07 ? 287 VAL A CB 1 ATOM 2262 C CG1 . VAL A 1 287 ? -30.338 42.545 -11.555 1.00 36.46 ? 287 VAL A CG1 1 ATOM 2263 C CG2 . VAL A 1 287 ? -29.419 41.551 -9.464 1.00 41.85 ? 287 VAL A CG2 1 ATOM 2264 N N . LEU A 1 288 ? -32.452 40.582 -12.784 1.00 40.55 ? 288 LEU A N 1 ATOM 2265 C CA . LEU A 1 288 ? -32.778 40.533 -14.208 1.00 44.21 ? 288 LEU A CA 1 ATOM 2266 C C . LEU A 1 288 ? -32.467 41.874 -14.887 1.00 40.82 ? 288 LEU A C 1 ATOM 2267 O O . LEU A 1 288 ? -32.929 42.928 -14.440 1.00 45.86 ? 288 LEU A O 1 ATOM 2268 C CB . LEU A 1 288 ? -34.251 40.175 -14.422 1.00 43.62 ? 288 LEU A CB 1 ATOM 2269 C CG . LEU A 1 288 ? -34.779 38.914 -13.744 1.00 41.17 ? 288 LEU A CG 1 ATOM 2270 C CD1 . LEU A 1 288 ? -36.204 38.629 -14.193 1.00 35.74 ? 288 LEU A CD1 1 ATOM 2271 C CD2 . LEU A 1 288 ? -33.885 37.735 -14.053 1.00 39.05 ? 288 LEU A CD2 1 ATOM 2272 N N . ARG A 1 289 ? -31.668 41.836 -15.949 1.00 34.81 ? 289 ARG A N 1 ATOM 2273 C CA . ARG A 1 289 ? -31.491 43.004 -16.806 1.00 42.27 ? 289 ARG A CA 1 ATOM 2274 C C . ARG A 1 289 ? -32.065 42.712 -18.185 1.00 38.44 ? 289 ARG A C 1 ATOM 2275 O O . ARG A 1 289 ? -31.380 42.168 -19.054 1.00 36.36 ? 289 ARG A O 1 ATOM 2276 C CB . ARG A 1 289 ? -30.019 43.403 -16.906 1.00 42.42 ? 289 ARG A CB 1 ATOM 2277 C CG . ARG A 1 289 ? -29.466 43.905 -15.596 1.00 44.03 ? 289 ARG A CG 1 ATOM 2278 C CD . ARG A 1 289 ? -28.028 44.378 -15.694 1.00 41.75 ? 289 ARG A CD 1 ATOM 2279 N NE . ARG A 1 289 ? -27.392 44.275 -14.383 1.00 50.58 ? 289 ARG A NE 1 ATOM 2280 C CZ . ARG A 1 289 ? -27.577 45.140 -13.389 1.00 44.17 ? 289 ARG A CZ 1 ATOM 2281 N NH1 . ARG A 1 289 ? -28.366 46.195 -13.557 1.00 35.61 ? 289 ARG A NH1 1 ATOM 2282 N NH2 . ARG A 1 289 ? -26.969 44.949 -12.226 1.00 48.32 ? 289 ARG A NH2 1 ATOM 2283 N N . THR A 1 290 ? -33.333 43.066 -18.370 1.00 41.55 ? 290 THR A N 1 ATOM 2284 C CA . THR A 1 290 ? -34.015 42.791 -19.623 1.00 46.07 ? 290 THR A CA 1 ATOM 2285 C C . THR A 1 290 ? -35.006 43.860 -20.014 1.00 41.92 ? 290 THR A C 1 ATOM 2286 O O . THR A 1 290 ? -35.471 44.644 -19.181 1.00 41.56 ? 290 THR A O 1 ATOM 2287 C CB . THR A 1 290 ? -34.815 41.491 -19.569 1.00 42.63 ? 290 THR A CB 1 ATOM 2288 O OG1 . THR A 1 290 ? -34.612 40.845 -18.309 1.00 51.41 ? 290 THR A OG1 1 ATOM 2289 C CG2 . THR A 1 290 ? -34.397 40.584 -20.692 1.00 40.89 ? 290 THR A CG2 1 ATOM 2290 N N . ASN A 1 291 ? -35.337 43.856 -21.298 1.00 47.81 ? 291 ASN A N 1 ATOM 2291 C CA . ASN A 1 291 ? -36.447 44.624 -21.823 1.00 53.34 ? 291 ASN A CA 1 ATOM 2292 C C . ASN A 1 291 ? -37.543 43.629 -22.204 1.00 50.33 ? 291 ASN A C 1 ATOM 2293 O O . ASN A 1 291 ? -38.524 43.986 -22.865 1.00 53.20 ? 291 ASN A O 1 ATOM 2294 C CB . ASN A 1 291 ? -35.997 45.397 -23.061 1.00 45.94 ? 291 ASN A CB 1 ATOM 2295 C CG . ASN A 1 291 ? -35.473 44.476 -24.158 1.00 58.26 ? 291 ASN A CG 1 ATOM 2296 O OD1 . ASN A 1 291 ? -34.934 43.398 -23.878 1.00 58.06 ? 291 ASN A OD1 1 ATOM 2297 N ND2 . ASN A 1 291 ? -35.633 44.892 -25.412 1.00 68.05 ? 291 ASN A ND2 1 ATOM 2298 N N . LYS A 1 292 ? -37.362 42.374 -21.792 1.00 40.16 ? 292 LYS A N 1 ATOM 2299 C CA . LYS A 1 292 ? -38.285 41.300 -22.161 1.00 41.67 ? 292 LYS A CA 1 ATOM 2300 C C . LYS A 1 292 ? -39.576 41.265 -21.340 1.00 39.92 ? 292 LYS A C 1 ATOM 2301 O O . LYS A 1 292 ? -39.642 41.802 -20.227 1.00 42.53 ? 292 LYS A O 1 ATOM 2302 C CB . LYS A 1 292 ? -37.576 39.941 -22.138 1.00 40.67 ? 292 LYS A CB 1 ATOM 2303 C CG . LYS A 1 292 ? -36.770 39.676 -23.401 1.00 42.79 ? 292 LYS A CG 1 ATOM 2304 C CD . LYS A 1 292 ? -35.884 38.447 -23.269 1.00 45.22 ? 292 LYS A CD 1 ATOM 2305 C CE . LYS A 1 292 ? -34.815 38.446 -24.363 1.00 49.95 ? 292 LYS A CE 1 ATOM 2306 N NZ . LYS A 1 292 ? -33.808 37.358 -24.175 1.00 58.95 ? 292 LYS A NZ 1 ATOM 2307 N N . THR A 1 293 ? -40.591 40.621 -21.910 1.00 35.14 ? 293 THR A N 1 ATOM 2308 C CA . THR A 1 293 ? -41.945 40.623 -21.361 1.00 34.59 ? 293 THR A CA 1 ATOM 2309 C C . THR A 1 293 ? -42.144 39.504 -20.341 1.00 32.95 ? 293 THR A C 1 ATOM 2310 O O . THR A 1 293 ? -42.931 39.642 -19.402 1.00 29.50 ? 293 THR A O 1 ATOM 2311 C CB . THR A 1 293 ? -42.978 40.428 -22.485 1.00 38.21 ? 293 THR A CB 1 ATOM 2312 O OG1 . THR A 1 293 ? -42.583 41.176 -23.645 1.00 45.47 ? 293 THR A OG1 1 ATOM 2313 C CG2 . THR A 1 293 ? -44.366 40.862 -22.031 1.00 38.68 ? 293 THR A CG2 1 ATOM 2314 N N . PHE A 1 294 ? -41.435 38.394 -20.541 1.00 26.11 ? 294 PHE A N 1 ATOM 2315 C CA . PHE A 1 294 ? -41.571 37.225 -19.679 1.00 27.50 ? 294 PHE A CA 1 ATOM 2316 C C . PHE A 1 294 ? -40.234 36.798 -19.090 1.00 28.54 ? 294 PHE A C 1 ATOM 2317 O O . PHE A 1 294 ? -39.175 37.165 -19.607 1.00 26.77 ? 294 PHE A O 1 ATOM 2318 C CB . PHE A 1 294 ? -42.156 36.045 -20.461 1.00 25.70 ? 294 PHE A CB 1 ATOM 2319 C CG . PHE A 1 294 ? -43.487 36.329 -21.103 1.00 28.21 ? 294 PHE A CG 1 ATOM 2320 C CD1 . PHE A 1 294 ? -44.663 36.227 -20.369 1.00 24.80 ? 294 PHE A CD1 1 ATOM 2321 C CD2 . PHE A 1 294 ? -43.565 36.670 -22.449 1.00 30.15 ? 294 PHE A CD2 1 ATOM 2322 C CE1 . PHE A 1 294 ? -45.895 36.472 -20.964 1.00 23.35 ? 294 PHE A CE1 1 ATOM 2323 C CE2 . PHE A 1 294 ? -44.795 36.918 -23.053 1.00 29.88 ? 294 PHE A CE2 1 ATOM 2324 C CZ . PHE A 1 294 ? -45.961 36.819 -22.309 1.00 26.74 ? 294 PHE A CZ 1 ATOM 2325 N N . GLN A 1 295 ? -40.295 36.001 -18.022 1.00 24.95 ? 295 GLN A N 1 ATOM 2326 C CA . GLN A 1 295 ? -39.103 35.432 -17.399 1.00 24.10 ? 295 GLN A CA 1 ATOM 2327 C C . GLN A 1 295 ? -39.467 34.156 -16.644 1.00 27.79 ? 295 GLN A C 1 ATOM 2328 O O . GLN A 1 295 ? -40.557 34.058 -16.073 1.00 27.80 ? 295 GLN A O 1 ATOM 2329 C CB . GLN A 1 295 ? -38.445 36.450 -16.458 1.00 23.10 ? 295 GLN A CB 1 ATOM 2330 C CG . GLN A 1 295 ? -39.381 37.021 -15.392 1.00 22.95 ? 295 GLN A CG 1 ATOM 2331 C CD . GLN A 1 295 ? -39.287 36.281 -14.065 1.00 24.98 ? 295 GLN A CD 1 ATOM 2332 O OE1 . GLN A 1 295 ? -38.438 35.396 -13.884 1.00 26.31 ? 295 GLN A OE1 1 ATOM 2333 N NE2 . GLN A 1 295 ? -40.154 36.647 -13.127 1.00 21.25 ? 295 GLN A NE2 1 ATOM 2334 N N . ASN A 1 296 ? -38.562 33.179 -16.641 1.00 25.87 ? 296 ASN A N 1 ATOM 2335 C CA . ASN A 1 296 ? -38.813 31.923 -15.943 1.00 25.61 ? 296 ASN A CA 1 ATOM 2336 C C . ASN A 1 296 ? -37.823 31.704 -14.795 1.00 28.49 ? 296 ASN A C 1 ATOM 2337 O O . ASN A 1 296 ? -37.508 30.567 -14.430 1.00 25.87 ? 296 ASN A O 1 ATOM 2338 C CB . ASN A 1 296 ? -38.776 30.746 -16.918 1.00 24.17 ? 296 ASN A CB 1 ATOM 2339 C CG . ASN A 1 296 ? -37.415 30.562 -17.562 1.00 31.27 ? 296 ASN A CG 1 ATOM 2340 O OD1 . ASN A 1 296 ? -36.471 31.309 -17.286 1.00 32.11 ? 296 ASN A OD1 1 ATOM 2341 N ND2 . ASN A 1 296 ? -37.303 29.556 -18.419 1.00 32.09 ? 296 ASN A ND2 1 ATOM 2342 N N . VAL A 1 297 ? -37.334 32.807 -14.236 1.00 29.17 ? 297 VAL A N 1 ATOM 2343 C CA . VAL A 1 297 ? -36.327 32.763 -13.180 1.00 29.35 ? 297 VAL A CA 1 ATOM 2344 C C . VAL A 1 297 ? -36.952 32.603 -11.791 1.00 31.58 ? 297 VAL A C 1 ATOM 2345 O O . VAL A 1 297 ? -36.533 31.743 -11.015 1.00 32.44 ? 297 VAL A O 1 ATOM 2346 C CB . VAL A 1 297 ? -35.438 34.020 -13.224 1.00 34.39 ? 297 VAL A CB 1 ATOM 2347 C CG1 . VAL A 1 297 ? -34.483 34.040 -12.057 1.00 29.30 ? 297 VAL A CG1 1 ATOM 2348 C CG2 . VAL A 1 297 ? -34.667 34.077 -14.538 1.00 29.84 ? 297 VAL A CG2 1 ATOM 2349 N N . SER A 1 298 ? -37.956 33.427 -11.487 1.00 33.25 ? 298 SER A N 1 ATOM 2350 C CA . SER A 1 298 ? -38.623 33.382 -10.187 1.00 31.57 ? 298 SER A CA 1 ATOM 2351 C C . SER A 1 298 ? -39.922 34.191 -10.134 1.00 33.10 ? 298 SER A C 1 ATOM 2352 O O . SER A 1 298 ? -40.028 35.258 -10.750 1.00 31.65 ? 298 SER A O 1 ATOM 2353 C CB . SER A 1 298 ? -37.689 33.890 -9.085 1.00 33.98 ? 298 SER A CB 1 ATOM 2354 O OG . SER A 1 298 ? -38.388 34.015 -7.857 1.00 31.23 ? 298 SER A OG 1 ATOM 2355 N N . PRO A 1 299 ? -40.910 33.690 -9.368 1.00 31.32 ? 299 PRO A N 1 ATOM 2356 C CA . PRO A 1 299 ? -42.136 34.442 -9.082 1.00 29.12 ? 299 PRO A CA 1 ATOM 2357 C C . PRO A 1 299 ? -41.936 35.437 -7.933 1.00 32.20 ? 299 PRO A C 1 ATOM 2358 O O . PRO A 1 299 ? -42.797 36.299 -7.721 1.00 34.94 ? 299 PRO A O 1 ATOM 2359 C CB . PRO A 1 299 ? -43.113 33.345 -8.647 1.00 28.84 ? 299 PRO A CB 1 ATOM 2360 C CG . PRO A 1 299 ? -42.232 32.320 -7.985 1.00 28.86 ? 299 PRO A CG 1 ATOM 2361 C CD . PRO A 1 299 ? -40.934 32.340 -8.768 1.00 28.44 ? 299 PRO A CD 1 ATOM 2362 N N . LEU A 1 300 ? -40.829 35.309 -7.199 1.00 31.26 ? 300 LEU A N 1 ATOM 2363 C CA . LEU A 1 300 ? -40.545 36.184 -6.056 1.00 32.79 ? 300 LEU A CA 1 ATOM 2364 C C . LEU A 1 300 ? -39.571 37.302 -6.420 1.00 30.88 ? 300 LEU A C 1 ATOM 2365 O O . LEU A 1 300 ? -38.399 37.042 -6.727 1.00 30.78 ? 300 LEU A O 1 ATOM 2366 C CB . LEU A 1 300 ? -39.958 35.374 -4.898 1.00 31.57 ? 300 LEU A CB 1 ATOM 2367 C CG . LEU A 1 300 ? -40.854 35.087 -3.696 1.00 41.66 ? 300 LEU A CG 1 ATOM 2368 C CD1 . LEU A 1 300 ? -42.300 34.977 -4.131 1.00 41.36 ? 300 LEU A CD1 1 ATOM 2369 C CD2 . LEU A 1 300 ? -40.414 33.798 -3.003 1.00 41.87 ? 300 LEU A CD2 1 ATOM 2370 N N . TRP A 1 301 ? -40.036 38.547 -6.367 1.00 25.33 ? 301 TRP A N 1 ATOM 2371 C CA . TRP A 1 301 ? -39.169 39.670 -6.714 1.00 30.68 ? 301 TRP A CA 1 ATOM 2372 C C . TRP A 1 301 ? -39.560 40.985 -6.055 1.00 32.13 ? 301 TRP A C 1 ATOM 2373 O O . TRP A 1 301 ? -40.634 41.103 -5.460 1.00 33.98 ? 301 TRP A O 1 ATOM 2374 C CB . TRP A 1 301 ? -39.118 39.865 -8.232 1.00 28.66 ? 301 TRP A CB 1 ATOM 2375 C CG . TRP A 1 301 ? -40.403 40.367 -8.817 1.00 31.75 ? 301 TRP A CG 1 ATOM 2376 C CD1 . TRP A 1 301 ? -40.880 41.653 -8.797 1.00 30.15 ? 301 TRP A CD1 1 ATOM 2377 C CD2 . TRP A 1 301 ? -41.366 39.594 -9.529 1.00 27.19 ? 301 TRP A CD2 1 ATOM 2378 N NE1 . TRP A 1 301 ? -42.087 41.717 -9.445 1.00 31.34 ? 301 TRP A NE1 1 ATOM 2379 C CE2 . TRP A 1 301 ? -42.407 40.467 -9.908 1.00 33.09 ? 301 TRP A CE2 1 ATOM 2380 C CE3 . TRP A 1 301 ? -41.451 38.249 -9.888 1.00 27.07 ? 301 TRP A CE3 1 ATOM 2381 C CZ2 . TRP A 1 301 ? -43.518 40.031 -10.628 1.00 33.23 ? 301 TRP A CZ2 1 ATOM 2382 C CZ3 . TRP A 1 301 ? -42.550 37.817 -10.598 1.00 33.27 ? 301 TRP A CZ3 1 ATOM 2383 C CH2 . TRP A 1 301 ? -43.572 38.704 -10.962 1.00 32.69 ? 301 TRP A CH2 1 ATOM 2384 N N . ILE A 1 302 ? -38.669 41.966 -6.183 1.00 38.15 ? 302 ILE A N 1 ATOM 2385 C CA . ILE A 1 302 ? -38.930 43.343 -5.785 1.00 36.69 ? 302 ILE A CA 1 ATOM 2386 C C . ILE A 1 302 ? -38.517 44.196 -6.990 1.00 37.21 ? 302 ILE A C 1 ATOM 2387 O O . ILE A 1 302 ? -37.641 43.791 -7.764 1.00 40.75 ? 302 ILE A O 1 ATOM 2388 C CB . ILE A 1 302 ? -38.134 43.723 -4.496 1.00 41.73 ? 302 ILE A CB 1 ATOM 2389 C CG1 . ILE A 1 302 ? -38.635 45.033 -3.890 1.00 43.21 ? 302 ILE A CG1 1 ATOM 2390 C CG2 . ILE A 1 302 ? -36.645 43.813 -4.774 1.00 39.43 ? 302 ILE A CG2 1 ATOM 2391 C CD1 . ILE A 1 302 ? -40.055 44.962 -3.404 1.00 52.06 ? 302 ILE A CD1 1 ATOM 2392 N N . GLY A 1 303 ? -39.165 45.343 -7.185 1.00 34.83 ? 303 GLY A N 1 ATOM 2393 C CA . GLY A 1 303 ? -38.882 46.180 -8.341 1.00 35.07 ? 303 GLY A CA 1 ATOM 2394 C C . GLY A 1 303 ? -39.808 45.909 -9.517 1.00 36.52 ? 303 GLY A C 1 ATOM 2395 O O . GLY A 1 303 ? -40.836 45.248 -9.361 1.00 37.67 ? 303 GLY A O 1 ATOM 2396 N N . GLU A 1 304 ? -39.448 46.417 -10.694 1.00 48.76 ? 304 GLU A N 1 ATOM 2397 C CA . GLU A 1 304 ? -40.270 46.241 -11.892 1.00 50.56 ? 304 GLU A CA 1 ATOM 2398 C C . GLU A 1 304 ? -39.775 45.063 -12.734 1.00 48.20 ? 304 GLU A C 1 ATOM 2399 O O . GLU A 1 304 ? -38.821 45.195 -13.505 1.00 49.95 ? 304 GLU A O 1 ATOM 2400 C CB . GLU A 1 304 ? -40.283 47.526 -12.732 1.00 48.55 ? 304 GLU A CB 1 ATOM 2401 C CG . GLU A 1 304 ? -40.755 48.773 -11.977 1.00 61.20 ? 304 GLU A CG 1 ATOM 2402 C CD . GLU A 1 304 ? -42.183 48.651 -11.444 1.00 78.12 ? 304 GLU A CD 1 ATOM 2403 O OE1 . GLU A 1 304 ? -43.131 48.984 -12.191 1.00 81.58 ? 304 GLU A OE1 1 ATOM 2404 O OE2 . GLU A 1 304 ? -42.360 48.233 -10.275 1.00 70.84 ? 304 GLU A OE2 1 ATOM 2405 N N . CYS A 1 305 ? -40.434 43.916 -12.593 1.00 39.89 ? 305 CYS A N 1 ATOM 2406 C CA . CYS A 1 305 ? -39.984 42.684 -13.245 1.00 38.89 ? 305 CYS A CA 1 ATOM 2407 C C . CYS A 1 305 ? -40.912 42.206 -14.360 1.00 33.18 ? 305 CYS A C 1 ATOM 2408 O O . CYS A 1 305 ? -42.076 42.601 -14.419 1.00 35.25 ? 305 CYS A O 1 ATOM 2409 C CB . CYS A 1 305 ? -39.826 41.570 -12.204 1.00 34.61 ? 305 CYS A CB 1 ATOM 2410 S SG . CYS A 1 305 ? -38.410 41.809 -11.126 1.00 49.52 ? 305 CYS A SG 1 ATOM 2411 N N . PRO A 1 306 ? -40.391 41.355 -15.259 1.00 33.61 ? 306 PRO A N 1 ATOM 2412 C CA . PRO A 1 306 ? -41.268 40.750 -16.273 1.00 31.63 ? 306 PRO A CA 1 ATOM 2413 C C . PRO A 1 306 ? -42.152 39.657 -15.671 1.00 31.05 ? 306 PRO A C 1 ATOM 2414 O O . PRO A 1 306 ? -41.817 39.110 -14.612 1.00 31.06 ? 306 PRO A O 1 ATOM 2415 C CB . PRO A 1 306 ? -40.284 40.126 -17.269 1.00 30.13 ? 306 PRO A CB 1 ATOM 2416 C CG . PRO A 1 306 ? -38.968 40.834 -17.018 1.00 34.37 ? 306 PRO A CG 1 ATOM 2417 C CD . PRO A 1 306 ? -38.962 41.128 -15.549 1.00 28.14 ? 306 PRO A CD 1 ATOM 2418 N N . LYS A 1 307 ? -43.259 39.345 -16.339 1.00 28.95 ? 307 LYS A N 1 ATOM 2419 C CA . LYS A 1 307 ? -44.204 38.332 -15.867 1.00 31.79 ? 307 LYS A CA 1 ATOM 2420 C C . LYS A 1 307 ? -43.547 36.951 -15.729 1.00 29.69 ? 307 LYS A C 1 ATOM 2421 O O . LYS A 1 307 ? -42.896 36.471 -16.662 1.00 28.69 ? 307 LYS A O 1 ATOM 2422 C CB . LYS A 1 307 ? -45.404 38.263 -16.824 1.00 32.27 ? 307 LYS A CB 1 ATOM 2423 C CG . LYS A 1 307 ? -46.299 37.047 -16.656 1.00 33.99 ? 307 LYS A CG 1 ATOM 2424 C CD . LYS A 1 307 ? -47.546 37.168 -17.531 1.00 37.50 ? 307 LYS A CD 1 ATOM 2425 C CE . LYS A 1 307 ? -48.529 38.147 -16.913 1.00 41.70 ? 307 LYS A CE 1 ATOM 2426 N NZ . LYS A 1 307 ? -49.231 38.955 -17.943 1.00 40.26 ? 307 LYS A NZ 1 ATOM 2427 N N . TYR A 1 308 ? -43.706 36.318 -14.568 1.00 25.66 ? 308 TYR A N 1 ATOM 2428 C CA . TYR A 1 308 ? -43.164 34.971 -14.367 1.00 27.82 ? 308 TYR A CA 1 ATOM 2429 C C . TYR A 1 308 ? -44.015 33.912 -15.056 1.00 27.43 ? 308 TYR A C 1 ATOM 2430 O O . TYR A 1 308 ? -45.252 33.939 -14.998 1.00 24.94 ? 308 TYR A O 1 ATOM 2431 C CB . TYR A 1 308 ? -43.019 34.628 -12.882 1.00 25.90 ? 308 TYR A CB 1 ATOM 2432 C CG . TYR A 1 308 ? -42.453 33.245 -12.628 1.00 27.33 ? 308 TYR A CG 1 ATOM 2433 C CD1 . TYR A 1 308 ? -41.164 32.907 -13.036 1.00 28.61 ? 308 TYR A CD1 1 ATOM 2434 C CD2 . TYR A 1 308 ? -43.199 32.283 -11.964 1.00 27.39 ? 308 TYR A CD2 1 ATOM 2435 C CE1 . TYR A 1 308 ? -40.645 31.643 -12.796 1.00 28.12 ? 308 TYR A CE1 1 ATOM 2436 C CE2 . TYR A 1 308 ? -42.689 31.021 -11.717 1.00 27.38 ? 308 TYR A CE2 1 ATOM 2437 C CZ . TYR A 1 308 ? -41.413 30.706 -12.135 1.00 31.49 ? 308 TYR A CZ 1 ATOM 2438 O OH . TYR A 1 308 ? -40.901 29.451 -11.889 1.00 33.37 ? 308 TYR A OH 1 ATOM 2439 N N . VAL A 1 309 ? -43.330 32.962 -15.680 1.00 27.05 ? 309 VAL A N 1 ATOM 2440 C CA . VAL A 1 309 ? -43.966 31.969 -16.524 1.00 26.53 ? 309 VAL A CA 1 ATOM 2441 C C . VAL A 1 309 ? -43.098 30.715 -16.496 1.00 30.41 ? 309 VAL A C 1 ATOM 2442 O O . VAL A 1 309 ? -41.892 30.812 -16.254 1.00 32.09 ? 309 VAL A O 1 ATOM 2443 C CB . VAL A 1 309 ? -44.140 32.550 -17.938 1.00 26.96 ? 309 VAL A CB 1 ATOM 2444 C CG1 . VAL A 1 309 ? -43.282 31.817 -18.952 1.00 27.55 ? 309 VAL A CG1 1 ATOM 2445 C CG2 . VAL A 1 309 ? -45.606 32.552 -18.325 1.00 25.99 ? 309 VAL A CG2 1 ATOM 2446 N N . LYS A 1 310 ? -43.693 29.542 -16.701 1.00 27.61 ? 310 LYS A N 1 ATOM 2447 C CA . LYS A 1 310 ? -42.924 28.295 -16.592 1.00 28.88 ? 310 LYS A CA 1 ATOM 2448 C C . LYS A 1 310 ? -42.193 27.889 -17.877 1.00 31.19 ? 310 LYS A C 1 ATOM 2449 O O . LYS A 1 310 ? -41.368 26.976 -17.866 1.00 38.92 ? 310 LYS A O 1 ATOM 2450 C CB . LYS A 1 310 ? -43.813 27.147 -16.111 1.00 24.68 ? 310 LYS A CB 1 ATOM 2451 C CG . LYS A 1 310 ? -44.658 27.508 -14.910 1.00 39.51 ? 310 LYS A CG 1 ATOM 2452 C CD . LYS A 1 310 ? -44.686 26.398 -13.868 1.00 44.99 ? 310 LYS A CD 1 ATOM 2453 C CE . LYS A 1 310 ? -45.479 25.203 -14.349 1.00 48.46 ? 310 LYS A CE 1 ATOM 2454 N NZ . LYS A 1 310 ? -45.633 24.186 -13.267 1.00 55.66 ? 310 LYS A NZ 1 ATOM 2455 N N . SER A 1 311 ? -42.486 28.577 -18.975 1.00 27.04 ? 311 SER A N 1 ATOM 2456 C CA . SER A 1 311 ? -41.936 28.230 -20.288 1.00 34.10 ? 311 SER A CA 1 ATOM 2457 C C . SER A 1 311 ? -40.413 28.353 -20.380 1.00 33.59 ? 311 SER A C 1 ATOM 2458 O O . SER A 1 311 ? -39.800 29.150 -19.668 1.00 39.35 ? 311 SER A O 1 ATOM 2459 C CB . SER A 1 311 ? -42.570 29.121 -21.357 1.00 33.91 ? 311 SER A CB 1 ATOM 2460 O OG . SER A 1 311 ? -43.909 29.413 -21.015 1.00 36.55 ? 311 SER A OG 1 ATOM 2461 N N . GLU A 1 312 ? -39.807 27.572 -21.270 1.00 39.09 ? 312 GLU A N 1 ATOM 2462 C CA . GLU A 1 312 ? -38.380 27.703 -21.541 1.00 45.12 ? 312 GLU A CA 1 ATOM 2463 C C . GLU A 1 312 ? -38.115 28.736 -22.629 1.00 45.14 ? 312 GLU A C 1 ATOM 2464 O O . GLU A 1 312 ? -37.034 29.328 -22.685 1.00 43.63 ? 312 GLU A O 1 ATOM 2465 C CB . GLU A 1 312 ? -37.772 26.357 -21.946 1.00 46.44 ? 312 GLU A CB 1 ATOM 2466 C CG . GLU A 1 312 ? -37.697 25.322 -20.820 1.00 57.25 ? 312 GLU A CG 1 ATOM 2467 C CD . GLU A 1 312 ? -36.733 25.711 -19.699 1.00 64.47 ? 312 GLU A CD 1 ATOM 2468 O OE1 . GLU A 1 312 ? -35.959 26.681 -19.860 1.00 65.23 ? 312 GLU A OE1 1 ATOM 2469 O OE2 . GLU A 1 312 ? -36.748 25.034 -18.648 1.00 77.38 ? 312 GLU A OE2 1 ATOM 2470 N N . SER A 1 313 ? -39.107 28.943 -23.493 1.00 40.47 ? 313 SER A N 1 ATOM 2471 C CA . SER A 1 313 ? -38.972 29.866 -24.615 1.00 40.74 ? 313 SER A CA 1 ATOM 2472 C C . SER A 1 313 ? -40.335 30.327 -25.118 1.00 36.25 ? 313 SER A C 1 ATOM 2473 O O . SER A 1 313 ? -41.286 29.544 -25.192 1.00 41.22 ? 313 SER A O 1 ATOM 2474 C CB . SER A 1 313 ? -38.183 29.217 -25.759 1.00 38.52 ? 313 SER A CB 1 ATOM 2475 O OG . SER A 1 313 ? -38.037 30.108 -26.854 1.00 43.24 ? 313 SER A OG 1 ATOM 2476 N N . LEU A 1 314 ? -40.420 31.609 -25.447 1.00 28.62 ? 314 LEU A N 1 ATOM 2477 C CA . LEU A 1 314 ? -41.619 32.192 -26.024 1.00 30.52 ? 314 LEU A CA 1 ATOM 2478 C C . LEU A 1 314 ? -41.169 33.000 -27.238 1.00 31.32 ? 314 LEU A C 1 ATOM 2479 O O . LEU A 1 314 ? -41.125 34.237 -27.212 1.00 31.52 ? 314 LEU A O 1 ATOM 2480 C CB . LEU A 1 314 ? -42.361 33.049 -24.992 1.00 29.59 ? 314 LEU A CB 1 ATOM 2481 C CG . LEU A 1 314 ? -43.001 32.230 -23.857 1.00 32.87 ? 314 LEU A CG 1 ATOM 2482 C CD1 . LEU A 1 314 ? -43.444 33.091 -22.673 1.00 24.78 ? 314 LEU A CD1 1 ATOM 2483 C CD2 . LEU A 1 314 ? -44.179 31.423 -24.395 1.00 25.37 ? 314 LEU A CD2 1 ATOM 2484 N N . ARG A 1 315 ? -40.809 32.276 -28.296 1.00 29.43 ? 315 ARG A N 1 ATOM 2485 C CA . ARG A 1 315 ? -40.250 32.878 -29.498 1.00 28.46 ? 315 ARG A CA 1 ATOM 2486 C C . ARG A 1 315 ? -41.335 33.170 -30.532 1.00 28.60 ? 315 ARG A C 1 ATOM 2487 O O . ARG A 1 315 ? -42.000 32.257 -31.045 1.00 23.39 ? 315 ARG A O 1 ATOM 2488 C CB . ARG A 1 315 ? -39.167 31.973 -30.090 1.00 32.76 ? 315 ARG A CB 1 ATOM 2489 C CG . ARG A 1 315 ? -38.533 32.500 -31.367 1.00 28.18 ? 315 ARG A CG 1 ATOM 2490 C CD . ARG A 1 315 ? -37.058 32.189 -31.406 1.00 29.30 ? 315 ARG A CD 1 ATOM 2491 N NE . ARG A 1 315 ? -36.287 33.384 -31.740 1.00 39.35 ? 315 ARG A NE 1 ATOM 2492 C CZ . ARG A 1 315 ? -35.214 33.791 -31.074 1.00 40.96 ? 315 ARG A CZ 1 ATOM 2493 N NH1 . ARG A 1 315 ? -34.777 33.091 -30.038 1.00 32.54 ? 315 ARG A NH1 1 ATOM 2494 N NH2 . ARG A 1 315 ? -34.579 34.893 -31.448 1.00 51.05 ? 315 ARG A NH2 1 ATOM 2495 N N . LEU A 1 316 ? -41.499 34.456 -30.827 1.00 28.91 ? 316 LEU A N 1 ATOM 2496 C CA . LEU A 1 316 ? -42.534 34.939 -31.732 1.00 27.29 ? 316 LEU A CA 1 ATOM 2497 C C . LEU A 1 316 ? -41.940 35.156 -33.123 1.00 30.90 ? 316 LEU A C 1 ATOM 2498 O O . LEU A 1 316 ? -40.945 35.873 -33.283 1.00 30.60 ? 316 LEU A O 1 ATOM 2499 C CB . LEU A 1 316 ? -43.091 36.258 -31.194 1.00 31.44 ? 316 LEU A CB 1 ATOM 2500 C CG . LEU A 1 316 ? -44.561 36.656 -31.319 1.00 33.40 ? 316 LEU A CG 1 ATOM 2501 C CD1 . LEU A 1 316 ? -45.477 35.494 -30.985 1.00 29.72 ? 316 LEU A CD1 1 ATOM 2502 C CD2 . LEU A 1 316 ? -44.846 37.815 -30.368 1.00 28.43 ? 316 LEU A CD2 1 ATOM 2503 N N . ALA A 1 317 ? -42.547 34.536 -34.131 1.00 26.71 ? 317 ALA A N 1 ATOM 2504 C CA . ALA A 1 317 ? -42.138 34.770 -35.512 1.00 26.41 ? 317 ALA A CA 1 ATOM 2505 C C . ALA A 1 317 ? -42.495 36.195 -35.930 1.00 25.80 ? 317 ALA A C 1 ATOM 2506 O O . ALA A 1 317 ? -43.557 36.714 -35.570 1.00 21.63 ? 317 ALA A O 1 ATOM 2507 C CB . ALA A 1 317 ? -42.801 33.775 -36.440 1.00 27.50 ? 317 ALA A CB 1 ATOM 2508 N N . THR A 1 318 ? -41.603 36.826 -36.688 1.00 27.61 ? 318 THR A N 1 ATOM 2509 C CA . THR A 1 318 ? -41.875 38.140 -37.260 1.00 28.90 ? 318 THR A CA 1 ATOM 2510 C C . THR A 1 318 ? -41.672 38.073 -38.764 1.00 30.30 ? 318 THR A C 1 ATOM 2511 O O . THR A 1 318 ? -42.525 38.520 -39.537 1.00 31.77 ? 318 THR A O 1 ATOM 2512 C CB . THR A 1 318 ? -41.000 39.241 -36.636 1.00 30.04 ? 318 THR A CB 1 ATOM 2513 O OG1 . THR A 1 318 ? -39.617 38.906 -36.797 1.00 34.62 ? 318 THR A OG1 1 ATOM 2514 C CG2 . THR A 1 318 ? -41.315 39.393 -35.155 1.00 25.04 ? 318 THR A CG2 1 ATOM 2515 N N . GLY A 1 319 ? -40.541 37.505 -39.173 1.00 27.95 ? 319 GLY A N 1 ATOM 2516 C CA . GLY A 1 319 ? -40.280 37.274 -40.581 1.00 26.62 ? 319 GLY A CA 1 ATOM 2517 C C . GLY A 1 319 ? -41.044 36.066 -41.107 1.00 28.79 ? 319 GLY A C 1 ATOM 2518 O O . GLY A 1 319 ? -41.920 35.523 -40.426 1.00 25.59 ? 319 GLY A O 1 ATOM 2519 N N . LEU A 1 320 ? -40.710 35.635 -42.320 1.00 34.63 ? 320 LEU A N 1 ATOM 2520 C CA . LEU A 1 320 ? -41.416 34.530 -42.958 1.00 34.48 ? 320 LEU A CA 1 ATOM 2521 C C . LEU A 1 320 ? -40.642 33.218 -42.869 1.00 33.75 ? 320 LEU A C 1 ATOM 2522 O O . LEU A 1 320 ? -39.509 33.186 -42.391 1.00 36.23 ? 320 LEU A O 1 ATOM 2523 C CB . LEU A 1 320 ? -41.724 34.864 -44.417 1.00 35.48 ? 320 LEU A CB 1 ATOM 2524 C CG . LEU A 1 320 ? -40.657 35.604 -45.219 1.00 36.36 ? 320 LEU A CG 1 ATOM 2525 C CD1 . LEU A 1 320 ? -40.692 35.164 -46.664 1.00 39.14 ? 320 LEU A CD1 1 ATOM 2526 C CD2 . LEU A 1 320 ? -40.900 37.092 -45.157 1.00 36.96 ? 320 LEU A CD2 1 ATOM 2527 N N . ARG A 1 321 ? -41.270 32.138 -43.320 1.00 25.70 ? 321 ARG A N 1 ATOM 2528 C CA . ARG A 1 321 ? -40.625 30.829 -43.396 1.00 26.45 ? 321 ARG A CA 1 ATOM 2529 C C . ARG A 1 321 ? -39.343 30.901 -44.243 1.00 30.35 ? 321 ARG A C 1 ATOM 2530 O O . ARG A 1 321 ? -39.362 31.366 -45.384 1.00 30.25 ? 321 ARG A O 1 ATOM 2531 C CB . ARG A 1 321 ? -41.603 29.817 -43.997 1.00 25.32 ? 321 ARG A CB 1 ATOM 2532 C CG . ARG A 1 321 ? -41.110 28.382 -44.035 1.00 31.34 ? 321 ARG A CG 1 ATOM 2533 C CD . ARG A 1 321 ? -42.095 27.506 -44.804 1.00 34.47 ? 321 ARG A CD 1 ATOM 2534 N NE . ARG A 1 321 ? -43.397 27.411 -44.144 1.00 35.52 ? 321 ARG A NE 1 ATOM 2535 C CZ . ARG A 1 321 ? -43.727 26.452 -43.281 1.00 34.13 ? 321 ARG A CZ 1 ATOM 2536 N NH1 . ARG A 1 321 ? -42.847 25.506 -42.967 1.00 29.34 ? 321 ARG A NH1 1 ATOM 2537 N NH2 . ARG A 1 321 ? -44.936 26.440 -42.733 1.00 32.69 ? 321 ARG A NH2 1 ATOM 2538 N N . ASN A 1 322 ? -38.227 30.459 -43.674 1.00 32.23 ? 322 ASN A N 1 ATOM 2539 C CA . ASN A 1 322 ? -36.941 30.559 -44.344 1.00 35.83 ? 322 ASN A CA 1 ATOM 2540 C C . ASN A 1 322 ? -36.714 29.363 -45.264 1.00 39.59 ? 322 ASN A C 1 ATOM 2541 O O . ASN A 1 322 ? -36.559 28.233 -44.795 1.00 42.97 ? 322 ASN A O 1 ATOM 2542 C CB . ASN A 1 322 ? -35.816 30.648 -43.311 1.00 34.01 ? 322 ASN A CB 1 ATOM 2543 C CG . ASN A 1 322 ? -34.507 31.128 -43.907 1.00 39.84 ? 322 ASN A CG 1 ATOM 2544 O OD1 . ASN A 1 322 ? -34.489 31.929 -44.852 1.00 38.21 ? 322 ASN A OD1 1 ATOM 2545 N ND2 . ASN A 1 322 ? -33.397 30.643 -43.355 1.00 40.10 ? 322 ASN A ND2 1 ATOM 2546 N N . VAL A 1 323 ? -36.707 29.617 -46.572 1.00 31.54 ? 323 VAL A N 1 ATOM 2547 C CA . VAL A 1 323 ? -36.527 28.568 -47.575 1.00 37.83 ? 323 VAL A CA 1 ATOM 2548 C C . VAL A 1 323 ? -35.415 28.951 -48.557 1.00 39.02 ? 323 VAL A C 1 ATOM 2549 O O . VAL A 1 323 ? -35.701 29.319 -49.697 1.00 36.94 ? 323 VAL A O 1 ATOM 2550 C CB . VAL A 1 323 ? -37.829 28.332 -48.374 1.00 39.03 ? 323 VAL A CB 1 ATOM 2551 C CG1 . VAL A 1 323 ? -37.775 27.007 -49.109 1.00 35.35 ? 323 VAL A CG1 1 ATOM 2552 C CG2 . VAL A 1 323 ? -39.046 28.363 -47.455 1.00 31.91 ? 323 VAL A CG2 1 ATOM 2553 N N . PRO A 1 324 ? -34.140 28.885 -48.114 1.00 48.55 ? 324 PRO A N 1 ATOM 2554 C CA . PRO A 1 324 ? -33.038 29.267 -49.013 1.00 54.75 ? 324 PRO A CA 1 ATOM 2555 C C . PRO A 1 324 ? -32.781 28.196 -50.072 1.00 52.91 ? 324 PRO A C 1 ATOM 2556 O O . PRO A 1 324 ? -33.062 27.020 -49.819 1.00 50.10 ? 324 PRO A O 1 ATOM 2557 C CB . PRO A 1 324 ? -31.820 29.363 -48.075 1.00 53.78 ? 324 PRO A CB 1 ATOM 2558 C CG . PRO A 1 324 ? -32.372 29.305 -46.666 1.00 43.34 ? 324 PRO A CG 1 ATOM 2559 C CD . PRO A 1 324 ? -33.649 28.526 -46.770 1.00 45.16 ? 324 PRO A CD 1 ATOM 2560 N N . GLN A 1 325 ? -32.262 28.594 -51.232 1.00 59.87 ? 325 GLN A N 1 ATOM 2561 C CA . GLN A 1 325 ? -31.954 27.648 -52.307 1.00 69.17 ? 325 GLN A CA 1 ATOM 2562 C C . GLN A 1 325 ? -30.677 28.025 -53.055 1.00 67.66 ? 325 GLN A C 1 ATOM 2563 O O . GLN A 1 325 ? -29.573 27.731 -52.596 1.00 71.56 ? 325 GLN A O 1 ATOM 2564 C CB . GLN A 1 325 ? -33.132 27.530 -53.282 1.00 64.29 ? 325 GLN A CB 1 ATOM 2565 C CG . GLN A 1 325 ? -33.839 28.853 -53.551 1.00 65.52 ? 325 GLN A CG 1 ATOM 2566 C CD . GLN A 1 325 ? -34.972 28.735 -54.561 1.00 65.87 ? 325 GLN A CD 1 ATOM 2567 O OE1 . GLN A 1 325 ? -35.344 27.630 -54.983 1.00 64.10 ? 325 GLN A OE1 1 ATOM 2568 N NE2 . GLN A 1 325 ? -35.531 29.881 -54.955 1.00 53.12 ? 325 GLN A NE2 1 ATOM 2569 N N . GLY B 2 1 ? -48.517 26.139 -46.783 1.00 63.12 ? 330 GLY B N 1 ATOM 2570 C CA . GLY B 2 1 ? -49.242 27.367 -46.513 1.00 58.08 ? 330 GLY B CA 1 ATOM 2571 C C . GLY B 2 1 ? -50.621 27.388 -47.149 1.00 55.17 ? 330 GLY B C 1 ATOM 2572 O O . GLY B 2 1 ? -50.822 26.872 -48.258 1.00 51.96 ? 330 GLY B O 1 ATOM 2573 N N . ILE B 2 2 ? -51.570 28.004 -46.451 1.00 42.86 ? 331 ILE B N 1 ATOM 2574 C CA . ILE B 2 2 ? -52.952 28.043 -46.910 1.00 39.02 ? 331 ILE B CA 1 ATOM 2575 C C . ILE B 2 2 ? -53.184 28.959 -48.115 1.00 32.95 ? 331 ILE B C 1 ATOM 2576 O O . ILE B 2 2 ? -54.237 28.898 -48.741 1.00 35.19 ? 331 ILE B O 1 ATOM 2577 C CB . ILE B 2 2 ? -53.920 28.410 -45.766 1.00 33.23 ? 331 ILE B CB 1 ATOM 2578 C CG1 . ILE B 2 2 ? -53.720 29.856 -45.312 1.00 33.40 ? 331 ILE B CG1 1 ATOM 2579 C CG2 . ILE B 2 2 ? -53.756 27.453 -44.601 1.00 32.07 ? 331 ILE B CG2 1 ATOM 2580 C CD1 . ILE B 2 2 ? -54.640 30.253 -44.156 1.00 38.61 ? 331 ILE B CD1 1 ATOM 2581 N N . PHE B 2 3 ? -52.224 29.816 -48.440 1.00 32.11 ? 332 PHE B N 1 ATOM 2582 C CA . PHE B 2 3 ? -52.368 30.625 -49.650 1.00 34.80 ? 332 PHE B CA 1 ATOM 2583 C C . PHE B 2 3 ? -51.556 30.052 -50.804 1.00 31.20 ? 332 PHE B C 1 ATOM 2584 O O . PHE B 2 3 ? -51.712 30.476 -51.946 1.00 44.48 ? 332 PHE B O 1 ATOM 2585 C CB . PHE B 2 3 ? -52.051 32.099 -49.387 1.00 33.34 ? 332 PHE B CB 1 ATOM 2586 C CG . PHE B 2 3 ? -53.009 32.753 -48.424 1.00 31.93 ? 332 PHE B CG 1 ATOM 2587 C CD1 . PHE B 2 3 ? -52.747 32.754 -47.055 1.00 29.53 ? 332 PHE B CD1 1 ATOM 2588 C CD2 . PHE B 2 3 ? -54.184 33.340 -48.882 1.00 27.94 ? 332 PHE B CD2 1 ATOM 2589 C CE1 . PHE B 2 3 ? -53.634 33.345 -46.157 1.00 29.36 ? 332 PHE B CE1 1 ATOM 2590 C CE2 . PHE B 2 3 ? -55.077 33.934 -47.992 1.00 30.12 ? 332 PHE B CE2 1 ATOM 2591 C CZ . PHE B 2 3 ? -54.801 33.936 -46.628 1.00 30.30 ? 332 PHE B CZ 1 ATOM 2592 N N . GLY B 2 4 ? -50.701 29.078 -50.501 1.00 29.76 ? 333 GLY B N 1 ATOM 2593 C CA . GLY B 2 4 ? -50.085 28.252 -51.526 1.00 26.76 ? 333 GLY B CA 1 ATOM 2594 C C . GLY B 2 4 ? -48.902 28.865 -52.250 1.00 29.07 ? 333 GLY B C 1 ATOM 2595 O O . GLY B 2 4 ? -48.368 28.264 -53.187 1.00 31.62 ? 333 GLY B O 1 ATOM 2596 N N . ALA B 2 5 ? -48.486 30.054 -51.820 1.00 25.63 ? 334 ALA B N 1 ATOM 2597 C CA . ALA B 2 5 ? -47.363 30.744 -52.449 1.00 25.55 ? 334 ALA B CA 1 ATOM 2598 C C . ALA B 2 5 ? -46.010 30.352 -51.834 1.00 29.81 ? 334 ALA B C 1 ATOM 2599 O O . ALA B 2 5 ? -45.186 29.703 -52.488 1.00 27.53 ? 334 ALA B O 1 ATOM 2600 C CB . ALA B 2 5 ? -47.567 32.253 -52.400 1.00 25.12 ? 334 ALA B CB 1 ATOM 2601 N N . ILE B 2 6 ? -45.774 30.761 -50.588 1.00 27.13 ? 335 ILE B N 1 ATOM 2602 C CA . ILE B 2 6 ? -44.490 30.502 -49.936 1.00 27.67 ? 335 ILE B CA 1 ATOM 2603 C C . ILE B 2 6 ? -44.254 29.001 -49.760 1.00 31.41 ? 335 ILE B C 1 ATOM 2604 O O . ILE B 2 6 ? -45.114 28.288 -49.235 1.00 28.11 ? 335 ILE B O 1 ATOM 2605 C CB . ILE B 2 6 ? -44.381 31.237 -48.588 1.00 31.22 ? 335 ILE B CB 1 ATOM 2606 C CG1 . ILE B 2 6 ? -44.368 32.753 -48.835 1.00 32.57 ? 335 ILE B CG1 1 ATOM 2607 C CG2 . ILE B 2 6 ? -43.137 30.786 -47.823 1.00 25.70 ? 335 ILE B CG2 1 ATOM 2608 C CD1 . ILE B 2 6 ? -44.114 33.594 -47.600 1.00 28.29 ? 335 ILE B CD1 1 ATOM 2609 N N . ALA B 2 7 ? -43.091 28.528 -50.209 1.00 35.23 ? 336 ALA B N 1 ATOM 2610 C CA . ALA B 2 7 ? -42.791 27.092 -50.254 1.00 38.50 ? 336 ALA B CA 1 ATOM 2611 C C . ALA B 2 7 ? -43.944 26.326 -50.911 1.00 37.47 ? 336 ALA B C 1 ATOM 2612 O O . ALA B 2 7 ? -44.318 25.230 -50.477 1.00 34.00 ? 336 ALA B O 1 ATOM 2613 C CB . ALA B 2 7 ? -42.494 26.550 -48.859 1.00 26.32 ? 336 ALA B CB 1 ATOM 2614 N N . GLY B 2 8 ? -44.499 26.936 -51.956 1.00 34.42 ? 337 GLY B N 1 ATOM 2615 C CA . GLY B 2 8 ? -45.604 26.383 -52.717 1.00 28.03 ? 337 GLY B CA 1 ATOM 2616 C C . GLY B 2 8 ? -45.290 26.504 -54.195 1.00 33.27 ? 337 GLY B C 1 ATOM 2617 O O . GLY B 2 8 ? -44.298 25.936 -54.661 1.00 32.04 ? 337 GLY B O 1 ATOM 2618 N N . PHE B 2 9 ? -46.104 27.251 -54.940 1.00 27.65 ? 338 PHE B N 1 ATOM 2619 C CA . PHE B 2 9 ? -45.827 27.412 -56.365 1.00 29.85 ? 338 PHE B CA 1 ATOM 2620 C C . PHE B 2 9 ? -44.610 28.318 -56.592 1.00 33.74 ? 338 PHE B C 1 ATOM 2621 O O . PHE B 2 9 ? -44.004 28.294 -57.665 1.00 36.26 ? 338 PHE B O 1 ATOM 2622 C CB . PHE B 2 9 ? -47.065 27.855 -57.169 1.00 29.80 ? 338 PHE B CB 1 ATOM 2623 C CG . PHE B 2 9 ? -47.453 29.284 -56.959 1.00 34.63 ? 338 PHE B CG 1 ATOM 2624 C CD1 . PHE B 2 9 ? -46.904 30.294 -57.745 1.00 31.12 ? 338 PHE B CD1 1 ATOM 2625 C CD2 . PHE B 2 9 ? -48.377 29.623 -55.983 1.00 31.92 ? 338 PHE B CD2 1 ATOM 2626 C CE1 . PHE B 2 9 ? -47.263 31.619 -57.548 1.00 29.97 ? 338 PHE B CE1 1 ATOM 2627 C CE2 . PHE B 2 9 ? -48.739 30.942 -55.780 1.00 31.02 ? 338 PHE B CE2 1 ATOM 2628 C CZ . PHE B 2 9 ? -48.181 31.941 -56.562 1.00 30.77 ? 338 PHE B CZ 1 ATOM 2629 N N . ILE B 2 10 ? -44.251 29.105 -55.581 1.00 30.44 ? 339 ILE B N 1 ATOM 2630 C CA . ILE B 2 10 ? -42.933 29.737 -55.558 1.00 31.60 ? 339 ILE B CA 1 ATOM 2631 C C . ILE B 2 10 ? -42.083 28.957 -54.554 1.00 32.52 ? 339 ILE B C 1 ATOM 2632 O O . ILE B 2 10 ? -42.151 29.203 -53.347 1.00 33.32 ? 339 ILE B O 1 ATOM 2633 C CB . ILE B 2 10 ? -42.999 31.236 -55.199 1.00 30.75 ? 339 ILE B CB 1 ATOM 2634 C CG1 . ILE B 2 10 ? -43.987 31.960 -56.117 1.00 30.59 ? 339 ILE B CG1 1 ATOM 2635 C CG2 . ILE B 2 10 ? -41.630 31.868 -55.337 1.00 27.42 ? 339 ILE B CG2 1 ATOM 2636 C CD1 . ILE B 2 10 ? -44.244 33.410 -55.735 1.00 30.50 ? 339 ILE B CD1 1 ATOM 2637 N N . GLU B 2 11 ? -41.284 28.024 -55.074 1.00 43.14 ? 340 GLU B N 1 ATOM 2638 C CA . GLU B 2 11 ? -40.662 26.952 -54.286 1.00 40.67 ? 340 GLU B CA 1 ATOM 2639 C C . GLU B 2 11 ? -39.696 27.387 -53.191 1.00 38.27 ? 340 GLU B C 1 ATOM 2640 O O . GLU B 2 11 ? -39.617 26.743 -52.142 1.00 43.28 ? 340 GLU B O 1 ATOM 2641 C CB . GLU B 2 11 ? -39.960 25.950 -55.213 1.00 51.27 ? 340 GLU B CB 1 ATOM 2642 C CG . GLU B 2 11 ? -40.902 25.171 -56.129 1.00 65.07 ? 340 GLU B CG 1 ATOM 2643 C CD . GLU B 2 11 ? -40.180 24.495 -57.291 1.00 83.61 ? 340 GLU B CD 1 ATOM 2644 O OE1 . GLU B 2 11 ? -40.517 24.804 -58.458 1.00 78.48 ? 340 GLU B OE1 1 ATOM 2645 O OE2 . GLU B 2 11 ? -39.287 23.653 -57.040 1.00 79.04 ? 340 GLU B OE2 1 ATOM 2646 N N . GLY B 2 12 ? -38.943 28.453 -53.432 1.00 30.49 ? 341 GLY B N 1 ATOM 2647 C CA . GLY B 2 12 ? -37.979 28.898 -52.444 1.00 26.12 ? 341 GLY B CA 1 ATOM 2648 C C . GLY B 2 12 ? -37.883 30.403 -52.331 1.00 29.43 ? 341 GLY B C 1 ATOM 2649 O O . GLY B 2 12 ? -38.470 31.148 -53.129 1.00 22.51 ? 341 GLY B O 1 ATOM 2650 N N . GLY B 2 13 ? -37.135 30.854 -51.330 1.00 27.14 ? 342 GLY B N 1 ATOM 2651 C CA . GLY B 2 13 ? -36.870 32.267 -51.175 1.00 26.14 ? 342 GLY B CA 1 ATOM 2652 C C . GLY B 2 13 ? -35.638 32.689 -51.954 1.00 30.90 ? 342 GLY B C 1 ATOM 2653 O O . GLY B 2 13 ? -35.022 31.873 -52.652 1.00 30.01 ? 342 GLY B O 1 ATOM 2654 N N . TRP B 2 14 ? -35.288 33.968 -51.825 1.00 31.74 ? 343 TRP B N 1 ATOM 2655 C CA . TRP B 2 14 ? -34.145 34.559 -52.507 1.00 31.18 ? 343 TRP B CA 1 ATOM 2656 C C . TRP B 2 14 ? -33.157 35.137 -51.494 1.00 35.37 ? 343 TRP B C 1 ATOM 2657 O O . TRP B 2 14 ? -33.425 36.176 -50.882 1.00 35.24 ? 343 TRP B O 1 ATOM 2658 C CB . TRP B 2 14 ? -34.620 35.698 -53.408 1.00 29.71 ? 343 TRP B CB 1 ATOM 2659 C CG . TRP B 2 14 ? -35.430 35.276 -54.585 1.00 31.46 ? 343 TRP B CG 1 ATOM 2660 C CD1 . TRP B 2 14 ? -35.421 34.054 -55.196 1.00 29.10 ? 343 TRP B CD1 1 ATOM 2661 C CD2 . TRP B 2 14 ? -36.371 36.084 -55.311 1.00 31.74 ? 343 TRP B CD2 1 ATOM 2662 N NE1 . TRP B 2 14 ? -36.294 34.056 -56.260 1.00 31.67 ? 343 TRP B NE1 1 ATOM 2663 C CE2 . TRP B 2 14 ? -36.890 35.286 -56.352 1.00 27.98 ? 343 TRP B CE2 1 ATOM 2664 C CE3 . TRP B 2 14 ? -36.824 37.402 -55.180 1.00 29.64 ? 343 TRP B CE3 1 ATOM 2665 C CZ2 . TRP B 2 14 ? -37.848 35.763 -57.255 1.00 28.86 ? 343 TRP B CZ2 1 ATOM 2666 C CZ3 . TRP B 2 14 ? -37.768 37.878 -56.082 1.00 28.61 ? 343 TRP B CZ3 1 ATOM 2667 C CH2 . TRP B 2 14 ? -38.270 37.060 -57.105 1.00 29.60 ? 343 TRP B CH2 1 ATOM 2668 N N . THR B 2 15 ? -32.010 34.484 -51.320 1.00 35.04 ? 344 THR B N 1 ATOM 2669 C CA . THR B 2 15 ? -30.948 35.046 -50.482 1.00 40.73 ? 344 THR B CA 1 ATOM 2670 C C . THR B 2 15 ? -30.415 36.343 -51.093 1.00 41.64 ? 344 THR B C 1 ATOM 2671 O O . THR B 2 15 ? -29.872 37.198 -50.385 1.00 38.11 ? 344 THR B O 1 ATOM 2672 C CB . THR B 2 15 ? -29.793 34.052 -50.262 1.00 40.89 ? 344 THR B CB 1 ATOM 2673 O OG1 . THR B 2 15 ? -29.335 33.551 -51.526 1.00 41.84 ? 344 THR B OG1 1 ATOM 2674 C CG2 . THR B 2 15 ? -30.262 32.892 -49.399 1.00 34.86 ? 344 THR B CG2 1 ATOM 2675 N N . GLY B 2 16 ? -30.590 36.479 -52.408 1.00 39.43 ? 345 GLY B N 1 ATOM 2676 C CA . GLY B 2 16 ? -30.146 37.652 -53.140 1.00 36.56 ? 345 GLY B CA 1 ATOM 2677 C C . GLY B 2 16 ? -30.991 38.898 -52.945 1.00 38.74 ? 345 GLY B C 1 ATOM 2678 O O . GLY B 2 16 ? -30.553 40.001 -53.292 1.00 43.02 ? 345 GLY B O 1 ATOM 2679 N N . MET B 2 17 ? -32.201 38.742 -52.410 1.00 36.29 ? 346 MET B N 1 ATOM 2680 C CA . MET B 2 17 ? -33.028 39.910 -52.107 1.00 38.34 ? 346 MET B CA 1 ATOM 2681 C C . MET B 2 17 ? -32.916 40.228 -50.624 1.00 38.99 ? 346 MET B C 1 ATOM 2682 O O . MET B 2 17 ? -33.607 39.632 -49.798 1.00 38.43 ? 346 MET B O 1 ATOM 2683 C CB . MET B 2 17 ? -34.487 39.682 -52.496 1.00 31.47 ? 346 MET B CB 1 ATOM 2684 C CG . MET B 2 17 ? -35.322 40.942 -52.429 1.00 35.76 ? 346 MET B CG 1 ATOM 2685 S SD . MET B 2 17 ? -37.011 40.657 -52.990 1.00 45.43 ? 346 MET B SD 1 ATOM 2686 C CE . MET B 2 17 ? -37.608 39.555 -51.699 1.00 29.31 ? 346 MET B CE 1 ATOM 2687 N N . ILE B 2 18 ? -32.044 41.177 -50.294 1.00 43.31 ? 347 ILE B N 1 ATOM 2688 C CA . ILE B 2 18 ? -31.669 41.432 -48.904 1.00 48.27 ? 347 ILE B CA 1 ATOM 2689 C C . ILE B 2 18 ? -32.364 42.638 -48.265 1.00 47.26 ? 347 ILE B C 1 ATOM 2690 O O . ILE B 2 18 ? -32.322 42.808 -47.042 1.00 53.20 ? 347 ILE B O 1 ATOM 2691 C CB . ILE B 2 18 ? -30.142 41.604 -48.771 1.00 49.18 ? 347 ILE B CB 1 ATOM 2692 C CG1 . ILE B 2 18 ? -29.683 42.880 -49.477 1.00 51.26 ? 347 ILE B CG1 1 ATOM 2693 C CG2 . ILE B 2 18 ? -29.408 40.388 -49.336 1.00 46.64 ? 347 ILE B CG2 1 ATOM 2694 C CD1 . ILE B 2 18 ? -28.172 43.041 -49.525 1.00 51.59 ? 347 ILE B CD1 1 ATOM 2695 N N . ASP B 2 19 ? -33.004 43.466 -49.087 1.00 54.35 ? 348 ASP B N 1 ATOM 2696 C CA . ASP B 2 19 ? -33.562 44.736 -48.613 1.00 61.27 ? 348 ASP B CA 1 ATOM 2697 C C . ASP B 2 19 ? -35.069 44.711 -48.304 1.00 60.61 ? 348 ASP B C 1 ATOM 2698 O O . ASP B 2 19 ? -35.686 45.767 -48.119 1.00 58.40 ? 348 ASP B O 1 ATOM 2699 C CB . ASP B 2 19 ? -33.238 45.873 -49.596 1.00 60.14 ? 348 ASP B CB 1 ATOM 2700 C CG . ASP B 2 19 ? -33.678 45.562 -51.025 1.00 72.88 ? 348 ASP B CG 1 ATOM 2701 O OD1 . ASP B 2 19 ? -33.628 44.376 -51.425 1.00 68.38 ? 348 ASP B OD1 1 ATOM 2702 O OD2 . ASP B 2 19 ? -34.067 46.506 -51.753 1.00 71.32 ? 348 ASP B OD2 1 ATOM 2703 N N . GLY B 2 20 ? -35.659 43.519 -48.230 1.00 42.06 ? 349 GLY B N 1 ATOM 2704 C CA . GLY B 2 20 ? -37.064 43.403 -47.865 1.00 36.18 ? 349 GLY B CA 1 ATOM 2705 C C . GLY B 2 20 ? -37.597 41.981 -47.840 1.00 35.61 ? 349 GLY B C 1 ATOM 2706 O O . GLY B 2 20 ? -36.880 41.032 -48.169 1.00 39.87 ? 349 GLY B O 1 ATOM 2707 N N . TRP B 2 21 ? -38.865 41.838 -47.461 1.00 33.51 ? 350 TRP B N 1 ATOM 2708 C CA . TRP B 2 21 ? -39.500 40.527 -47.339 1.00 31.30 ? 350 TRP B CA 1 ATOM 2709 C C . TRP B 2 21 ? -40.060 40.023 -48.665 1.00 30.06 ? 350 TRP B C 1 ATOM 2710 O O . TRP B 2 21 ? -39.892 38.852 -49.011 1.00 30.79 ? 350 TRP B O 1 ATOM 2711 C CB . TRP B 2 21 ? -40.620 40.580 -46.299 1.00 26.70 ? 350 TRP B CB 1 ATOM 2712 C CG . TRP B 2 21 ? -40.130 40.477 -44.891 1.00 28.28 ? 350 TRP B CG 1 ATOM 2713 C CD1 . TRP B 2 21 ? -38.948 39.932 -44.470 1.00 30.90 ? 350 TRP B CD1 1 ATOM 2714 C CD2 . TRP B 2 21 ? -40.810 40.926 -43.710 1.00 26.76 ? 350 TRP B CD2 1 ATOM 2715 N NE1 . TRP B 2 21 ? -38.855 40.012 -43.098 1.00 27.82 ? 350 TRP B NE1 1 ATOM 2716 C CE2 . TRP B 2 21 ? -39.983 40.620 -42.610 1.00 27.70 ? 350 TRP B CE2 1 ATOM 2717 C CE3 . TRP B 2 21 ? -42.036 41.556 -43.479 1.00 26.75 ? 350 TRP B CE3 1 ATOM 2718 C CZ2 . TRP B 2 21 ? -40.347 40.925 -41.294 1.00 22.64 ? 350 TRP B CZ2 1 ATOM 2719 C CZ3 . TRP B 2 21 ? -42.396 41.859 -42.179 1.00 25.55 ? 350 TRP B CZ3 1 ATOM 2720 C CH2 . TRP B 2 21 ? -41.554 41.542 -41.101 1.00 27.52 ? 350 TRP B CH2 1 ATOM 2721 N N . TYR B 2 22 ? -40.736 40.904 -49.398 1.00 28.16 ? 351 TYR B N 1 ATOM 2722 C CA . TYR B 2 22 ? -41.330 40.543 -50.682 1.00 30.31 ? 351 TYR B CA 1 ATOM 2723 C C . TYR B 2 22 ? -40.756 41.432 -51.774 1.00 32.87 ? 351 TYR B C 1 ATOM 2724 O O . TYR B 2 22 ? -40.485 42.617 -51.544 1.00 34.89 ? 351 TYR B O 1 ATOM 2725 C CB . TYR B 2 22 ? -42.853 40.720 -50.645 1.00 29.09 ? 351 TYR B CB 1 ATOM 2726 C CG . TYR B 2 22 ? -43.481 40.500 -49.287 1.00 27.87 ? 351 TYR B CG 1 ATOM 2727 C CD1 . TYR B 2 22 ? -43.479 39.247 -48.694 1.00 26.84 ? 351 TYR B CD1 1 ATOM 2728 C CD2 . TYR B 2 22 ? -44.093 41.544 -48.608 1.00 27.72 ? 351 TYR B CD2 1 ATOM 2729 C CE1 . TYR B 2 22 ? -44.056 39.041 -47.459 1.00 24.46 ? 351 TYR B CE1 1 ATOM 2730 C CE2 . TYR B 2 22 ? -44.674 41.348 -47.371 1.00 28.32 ? 351 TYR B CE2 1 ATOM 2731 C CZ . TYR B 2 22 ? -44.654 40.093 -46.803 1.00 29.84 ? 351 TYR B CZ 1 ATOM 2732 O OH . TYR B 2 22 ? -45.236 39.884 -45.571 1.00 27.78 ? 351 TYR B OH 1 ATOM 2733 N N . GLY B 2 23 ? -40.576 40.881 -52.968 1.00 30.36 ? 352 GLY B N 1 ATOM 2734 C CA . GLY B 2 23 ? -40.099 41.703 -54.063 1.00 31.24 ? 352 GLY B CA 1 ATOM 2735 C C . GLY B 2 23 ? -39.999 40.994 -55.393 1.00 28.80 ? 352 GLY B C 1 ATOM 2736 O O . GLY B 2 23 ? -40.710 40.015 -55.653 1.00 28.37 ? 352 GLY B O 1 ATOM 2737 N N . TYR B 2 24 ? -39.100 41.484 -56.238 1.00 30.95 ? 353 TYR B N 1 ATOM 2738 C CA . TYR B 2 24 ? -39.040 41.024 -57.612 1.00 31.22 ? 353 TYR B CA 1 ATOM 2739 C C . TYR B 2 24 ? -37.634 40.660 -58.043 1.00 32.82 ? 353 TYR B C 1 ATOM 2740 O O . TYR B 2 24 ? -36.650 41.188 -57.516 1.00 37.98 ? 353 TYR B O 1 ATOM 2741 C CB . TYR B 2 24 ? -39.537 42.120 -58.550 1.00 30.56 ? 353 TYR B CB 1 ATOM 2742 C CG . TYR B 2 24 ? -40.809 42.807 -58.132 1.00 31.49 ? 353 TYR B CG 1 ATOM 2743 C CD1 . TYR B 2 24 ? -40.780 43.902 -57.281 1.00 30.67 ? 353 TYR B CD1 1 ATOM 2744 C CD2 . TYR B 2 24 ? -42.040 42.388 -58.621 1.00 32.94 ? 353 TYR B CD2 1 ATOM 2745 C CE1 . TYR B 2 24 ? -41.938 44.550 -56.915 1.00 31.84 ? 353 TYR B CE1 1 ATOM 2746 C CE2 . TYR B 2 24 ? -43.209 43.032 -58.258 1.00 29.21 ? 353 TYR B CE2 1 ATOM 2747 C CZ . TYR B 2 24 ? -43.149 44.114 -57.408 1.00 32.45 ? 353 TYR B CZ 1 ATOM 2748 O OH . TYR B 2 24 ? -44.303 44.764 -57.036 1.00 35.20 ? 353 TYR B OH 1 ATOM 2749 N N . HIS B 2 25 ? -37.551 39.761 -59.018 1.00 30.99 ? 354 HIS B N 1 ATOM 2750 C CA . HIS B 2 25 ? -36.329 39.572 -59.783 1.00 32.50 ? 354 HIS B CA 1 ATOM 2751 C C . HIS B 2 25 ? -36.682 39.811 -61.240 1.00 34.92 ? 354 HIS B C 1 ATOM 2752 O O . HIS B 2 25 ? -37.587 39.161 -61.777 1.00 34.73 ? 354 HIS B O 1 ATOM 2753 C CB . HIS B 2 25 ? -35.773 38.158 -59.618 1.00 31.07 ? 354 HIS B CB 1 ATOM 2754 C CG . HIS B 2 25 ? -34.532 37.902 -60.421 1.00 40.15 ? 354 HIS B CG 1 ATOM 2755 N ND1 . HIS B 2 25 ? -33.269 38.213 -59.960 1.00 39.50 ? 354 HIS B ND1 1 ATOM 2756 C CD2 . HIS B 2 25 ? -34.364 37.377 -61.658 1.00 37.37 ? 354 HIS B CD2 1 ATOM 2757 C CE1 . HIS B 2 25 ? -32.377 37.881 -60.875 1.00 38.90 ? 354 HIS B CE1 1 ATOM 2758 N NE2 . HIS B 2 25 ? -33.010 37.372 -61.914 1.00 41.59 ? 354 HIS B NE2 1 ATOM 2759 N N . HIS B 2 26 ? -35.991 40.750 -61.879 1.00 31.51 ? 355 HIS B N 1 ATOM 2760 C CA . HIS B 2 26 ? -36.255 41.042 -63.281 1.00 30.66 ? 355 HIS B CA 1 ATOM 2761 C C . HIS B 2 26 ? -35.055 40.673 -64.140 1.00 35.99 ? 355 HIS B C 1 ATOM 2762 O O . HIS B 2 26 ? -33.939 40.500 -63.639 1.00 33.31 ? 355 HIS B O 1 ATOM 2763 C CB . HIS B 2 26 ? -36.591 42.516 -63.479 1.00 31.22 ? 355 HIS B CB 1 ATOM 2764 C CG . HIS B 2 26 ? -35.387 43.401 -63.544 1.00 40.46 ? 355 HIS B CG 1 ATOM 2765 N ND1 . HIS B 2 26 ? -34.836 43.995 -62.428 1.00 42.32 ? 355 HIS B ND1 1 ATOM 2766 C CD2 . HIS B 2 26 ? -34.624 43.787 -64.594 1.00 40.37 ? 355 HIS B CD2 1 ATOM 2767 C CE1 . HIS B 2 26 ? -33.787 44.710 -62.790 1.00 44.77 ? 355 HIS B CE1 1 ATOM 2768 N NE2 . HIS B 2 26 ? -33.633 44.603 -64.094 1.00 45.94 ? 355 HIS B NE2 1 ATOM 2769 N N . GLU B 2 27 ? -35.285 40.572 -65.442 1.00 38.13 ? 356 GLU B N 1 ATOM 2770 C CA . GLU B 2 27 ? -34.245 40.135 -66.354 1.00 41.42 ? 356 GLU B CA 1 ATOM 2771 C C . GLU B 2 27 ? -34.530 40.677 -67.754 1.00 40.93 ? 356 GLU B C 1 ATOM 2772 O O . GLU B 2 27 ? -35.532 40.312 -68.376 1.00 41.95 ? 356 GLU B O 1 ATOM 2773 C CB . GLU B 2 27 ? -34.202 38.608 -66.360 1.00 42.23 ? 356 GLU B CB 1 ATOM 2774 C CG . GLU B 2 27 ? -32.906 38.000 -66.837 1.00 52.99 ? 356 GLU B CG 1 ATOM 2775 C CD . GLU B 2 27 ? -32.954 36.481 -66.824 1.00 74.43 ? 356 GLU B CD 1 ATOM 2776 O OE1 . GLU B 2 27 ? -33.411 35.906 -65.805 1.00 63.79 ? 356 GLU B OE1 1 ATOM 2777 O OE2 . GLU B 2 27 ? -32.543 35.867 -67.835 1.00 75.74 ? 356 GLU B OE2 1 ATOM 2778 N N . ASN B 2 28 ? -33.661 41.562 -68.239 1.00 38.18 ? 357 ASN B N 1 ATOM 2779 C CA . ASN B 2 28 ? -33.792 42.115 -69.590 1.00 35.84 ? 357 ASN B CA 1 ATOM 2780 C C . ASN B 2 28 ? -32.433 42.384 -70.252 1.00 37.69 ? 357 ASN B C 1 ATOM 2781 O O . ASN B 2 28 ? -31.397 41.918 -69.765 1.00 38.57 ? 357 ASN B O 1 ATOM 2782 C CB . ASN B 2 28 ? -34.635 43.391 -69.567 1.00 29.73 ? 357 ASN B CB 1 ATOM 2783 C CG . ASN B 2 28 ? -34.004 44.491 -68.736 1.00 31.56 ? 357 ASN B CG 1 ATOM 2784 O OD1 . ASN B 2 28 ? -32.864 44.365 -68.271 1.00 35.25 ? 357 ASN B OD1 1 ATOM 2785 N ND2 . ASN B 2 28 ? -34.740 45.585 -68.548 1.00 30.59 ? 357 ASN B ND2 1 ATOM 2786 N N . SER B 2 29 ? -32.440 43.156 -71.337 1.00 40.12 ? 358 SER B N 1 ATOM 2787 C CA . SER B 2 29 ? -31.215 43.469 -72.079 1.00 45.83 ? 358 SER B CA 1 ATOM 2788 C C . SER B 2 29 ? -30.147 44.176 -71.238 1.00 43.73 ? 358 SER B C 1 ATOM 2789 O O . SER B 2 29 ? -28.952 44.017 -71.482 1.00 45.91 ? 358 SER B O 1 ATOM 2790 C CB . SER B 2 29 ? -31.541 44.298 -73.321 1.00 41.69 ? 358 SER B CB 1 ATOM 2791 O OG . SER B 2 29 ? -32.436 43.598 -74.162 1.00 49.54 ? 358 SER B OG 1 ATOM 2792 N N . GLN B 2 30 ? -30.580 44.951 -70.249 1.00 35.72 ? 359 GLN B N 1 ATOM 2793 C CA . GLN B 2 30 ? -29.652 45.627 -69.350 1.00 36.46 ? 359 GLN B CA 1 ATOM 2794 C C . GLN B 2 30 ? -29.208 44.724 -68.204 1.00 37.81 ? 359 GLN B C 1 ATOM 2795 O O . GLN B 2 30 ? -28.365 45.120 -67.389 1.00 35.57 ? 359 GLN B O 1 ATOM 2796 C CB . GLN B 2 30 ? -30.271 46.914 -68.790 1.00 36.16 ? 359 GLN B CB 1 ATOM 2797 C CG . GLN B 2 30 ? -30.126 48.144 -69.687 1.00 37.81 ? 359 GLN B CG 1 ATOM 2798 C CD . GLN B 2 30 ? -30.636 47.921 -71.102 1.00 39.34 ? 359 GLN B CD 1 ATOM 2799 O OE1 . GLN B 2 30 ? -29.860 47.617 -72.014 1.00 35.55 ? 359 GLN B OE1 1 ATOM 2800 N NE2 . GLN B 2 30 ? -31.945 48.075 -71.293 1.00 39.86 ? 359 GLN B NE2 1 ATOM 2801 N N . GLY B 2 31 ? -29.780 43.523 -68.127 1.00 39.76 ? 360 GLY B N 1 ATOM 2802 C CA . GLY B 2 31 ? -29.343 42.549 -67.136 1.00 43.99 ? 360 GLY B CA 1 ATOM 2803 C C . GLY B 2 31 ? -30.354 42.123 -66.078 1.00 41.45 ? 360 GLY B C 1 ATOM 2804 O O . GLY B 2 31 ? -31.562 42.310 -66.241 1.00 44.06 ? 360 GLY B O 1 ATOM 2805 N N . SER B 2 32 ? -29.841 41.547 -64.991 1.00 38.91 ? 361 SER B N 1 ATOM 2806 C CA . SER B 2 32 ? -30.655 40.972 -63.926 1.00 36.88 ? 361 SER B CA 1 ATOM 2807 C C . SER B 2 32 ? -30.519 41.762 -62.629 1.00 40.61 ? 361 SER B C 1 ATOM 2808 O O . SER B 2 32 ? -29.609 42.578 -62.491 1.00 40.02 ? 361 SER B O 1 ATOM 2809 C CB . SER B 2 32 ? -30.223 39.532 -63.666 1.00 34.25 ? 361 SER B CB 1 ATOM 2810 O OG . SER B 2 32 ? -30.238 38.784 -64.862 1.00 56.63 ? 361 SER B OG 1 ATOM 2811 N N . GLY B 2 33 ? -31.413 41.508 -61.675 1.00 40.55 ? 362 GLY B N 1 ATOM 2812 C CA . GLY B 2 33 ? -31.375 42.209 -60.405 1.00 38.93 ? 362 GLY B CA 1 ATOM 2813 C C . GLY B 2 33 ? -32.556 41.918 -59.500 1.00 41.27 ? 362 GLY B C 1 ATOM 2814 O O . GLY B 2 33 ? -33.651 41.596 -59.972 1.00 40.95 ? 362 GLY B O 1 ATOM 2815 N N . TYR B 2 34 ? -32.330 42.025 -58.193 1.00 40.87 ? 363 TYR B N 1 ATOM 2816 C CA . TYR B 2 34 ? -33.403 41.916 -57.211 1.00 36.17 ? 363 TYR B CA 1 ATOM 2817 C C . TYR B 2 34 ? -33.824 43.305 -56.745 1.00 37.91 ? 363 TYR B C 1 ATOM 2818 O O . TYR B 2 34 ? -33.031 44.248 -56.785 1.00 41.91 ? 363 TYR B O 1 ATOM 2819 C CB . TYR B 2 34 ? -32.949 41.092 -56.003 1.00 34.01 ? 363 TYR B CB 1 ATOM 2820 C CG . TYR B 2 34 ? -32.653 39.647 -56.317 1.00 36.25 ? 363 TYR B CG 1 ATOM 2821 C CD1 . TYR B 2 34 ? -33.670 38.704 -56.351 1.00 36.72 ? 363 TYR B CD1 1 ATOM 2822 C CD2 . TYR B 2 34 ? -31.356 39.221 -56.571 1.00 33.91 ? 363 TYR B CD2 1 ATOM 2823 C CE1 . TYR B 2 34 ? -33.404 37.374 -56.636 1.00 37.47 ? 363 TYR B CE1 1 ATOM 2824 C CE2 . TYR B 2 34 ? -31.081 37.897 -56.857 1.00 34.78 ? 363 TYR B CE2 1 ATOM 2825 C CZ . TYR B 2 34 ? -32.107 36.978 -56.887 1.00 40.60 ? 363 TYR B CZ 1 ATOM 2826 O OH . TYR B 2 34 ? -31.838 35.657 -57.171 1.00 40.28 ? 363 TYR B OH 1 ATOM 2827 N N . ALA B 2 35 ? -35.074 43.428 -56.310 1.00 41.09 ? 364 ALA B N 1 ATOM 2828 C CA . ALA B 2 35 ? -35.565 44.663 -55.701 1.00 40.80 ? 364 ALA B CA 1 ATOM 2829 C C . ALA B 2 35 ? -36.769 44.358 -54.824 1.00 35.86 ? 364 ALA B C 1 ATOM 2830 O O . ALA B 2 35 ? -37.704 43.685 -55.257 1.00 35.16 ? 364 ALA B O 1 ATOM 2831 C CB . ALA B 2 35 ? -35.933 45.687 -56.765 1.00 36.73 ? 364 ALA B CB 1 ATOM 2832 N N . ALA B 2 36 ? -36.752 44.853 -53.593 1.00 39.13 ? 365 ALA B N 1 ATOM 2833 C CA . ALA B 2 36 ? -37.891 44.668 -52.706 1.00 37.86 ? 365 ALA B CA 1 ATOM 2834 C C . ALA B 2 36 ? -39.046 45.556 -53.152 1.00 36.83 ? 365 ALA B C 1 ATOM 2835 O O . ALA B 2 36 ? -38.817 46.658 -53.663 1.00 39.29 ? 365 ALA B O 1 ATOM 2836 C CB . ALA B 2 36 ? -37.506 44.992 -51.282 1.00 39.02 ? 365 ALA B CB 1 ATOM 2837 N N . ASP B 2 37 ? -40.277 45.075 -52.974 1.00 34.59 ? 366 ASP B N 1 ATOM 2838 C CA . ASP B 2 37 ? -41.449 45.939 -53.084 1.00 36.33 ? 366 ASP B CA 1 ATOM 2839 C C . ASP B 2 37 ? -41.585 46.614 -51.727 1.00 38.57 ? 366 ASP B C 1 ATOM 2840 O O . ASP B 2 37 ? -42.057 45.991 -50.771 1.00 42.58 ? 366 ASP B O 1 ATOM 2841 C CB . ASP B 2 37 ? -42.702 45.116 -53.404 1.00 37.31 ? 366 ASP B CB 1 ATOM 2842 C CG . ASP B 2 37 ? -43.918 45.980 -53.707 1.00 42.18 ? 366 ASP B CG 1 ATOM 2843 O OD1 . ASP B 2 37 ? -43.984 46.557 -54.819 1.00 48.78 ? 366 ASP B OD1 1 ATOM 2844 O OD2 . ASP B 2 37 ? -44.818 46.071 -52.842 1.00 41.49 ? 366 ASP B OD2 1 ATOM 2845 N N . ARG B 2 38 ? -41.139 47.866 -51.628 1.00 42.69 ? 367 ARG B N 1 ATOM 2846 C CA . ARG B 2 38 ? -41.080 48.545 -50.334 1.00 53.72 ? 367 ARG B CA 1 ATOM 2847 C C . ARG B 2 38 ? -42.460 48.699 -49.704 1.00 46.55 ? 367 ARG B C 1 ATOM 2848 O O . ARG B 2 38 ? -42.610 48.563 -48.493 1.00 45.87 ? 367 ARG B O 1 ATOM 2849 C CB . ARG B 2 38 ? -40.402 49.917 -50.447 1.00 61.99 ? 367 ARG B CB 1 ATOM 2850 C CG . ARG B 2 38 ? -38.921 49.893 -50.835 1.00 75.25 ? 367 ARG B CG 1 ATOM 2851 C CD . ARG B 2 38 ? -38.311 51.298 -50.755 1.00 93.76 ? 367 ARG B CD 1 ATOM 2852 N NE . ARG B 2 38 ? -39.297 52.338 -51.052 1.00 105.47 ? 367 ARG B NE 1 ATOM 2853 C CZ . ARG B 2 38 ? -39.623 52.743 -52.278 1.00 101.00 ? 367 ARG B CZ 1 ATOM 2854 N NH1 . ARG B 2 38 ? -39.042 52.196 -53.340 1.00 88.40 ? 367 ARG B NH1 1 ATOM 2855 N NH2 . ARG B 2 38 ? -40.535 53.694 -52.441 1.00 91.80 ? 367 ARG B NH2 1 ATOM 2856 N N . GLU B 2 39 ? -43.463 48.964 -50.535 1.00 43.59 ? 368 GLU B N 1 ATOM 2857 C CA . GLU B 2 39 ? -44.817 49.239 -50.056 1.00 46.45 ? 368 GLU B CA 1 ATOM 2858 C C . GLU B 2 39 ? -45.449 48.056 -49.307 1.00 44.98 ? 368 GLU B C 1 ATOM 2859 O O . GLU B 2 39 ? -45.924 48.207 -48.180 1.00 40.03 ? 368 GLU B O 1 ATOM 2860 C CB . GLU B 2 39 ? -45.707 49.675 -51.222 1.00 53.38 ? 368 GLU B CB 1 ATOM 2861 C CG . GLU B 2 39 ? -47.050 50.257 -50.807 1.00 65.46 ? 368 GLU B CG 1 ATOM 2862 C CD . GLU B 2 39 ? -48.204 49.646 -51.582 1.00 80.44 ? 368 GLU B CD 1 ATOM 2863 O OE1 . GLU B 2 39 ? -47.994 48.576 -52.197 1.00 80.09 ? 368 GLU B OE1 1 ATOM 2864 O OE2 . GLU B 2 39 ? -49.313 50.227 -51.577 1.00 78.94 ? 368 GLU B OE2 1 ATOM 2865 N N . SER B 2 40 ? -45.452 46.878 -49.924 1.00 41.89 ? 369 SER B N 1 ATOM 2866 C CA . SER B 2 40 ? -46.008 45.693 -49.271 1.00 35.70 ? 369 SER B CA 1 ATOM 2867 C C . SER B 2 40 ? -45.112 45.202 -48.129 1.00 35.85 ? 369 SER B C 1 ATOM 2868 O O . SER B 2 40 ? -45.602 44.673 -47.125 1.00 31.25 ? 369 SER B O 1 ATOM 2869 C CB . SER B 2 40 ? -46.239 44.573 -50.281 1.00 28.62 ? 369 SER B CB 1 ATOM 2870 O OG . SER B 2 40 ? -45.010 44.138 -50.825 1.00 33.21 ? 369 SER B OG 1 ATOM 2871 N N . THR B 2 41 ? -43.802 45.372 -48.278 1.00 30.53 ? 370 THR B N 1 ATOM 2872 C CA . THR B 2 41 ? -42.883 45.036 -47.197 1.00 29.60 ? 370 THR B CA 1 ATOM 2873 C C . THR B 2 41 ? -43.139 45.929 -45.989 1.00 32.27 ? 370 THR B C 1 ATOM 2874 O O . THR B 2 41 ? -43.278 45.438 -44.865 1.00 31.63 ? 370 THR B O 1 ATOM 2875 C CB . THR B 2 41 ? -41.402 45.151 -47.627 1.00 28.71 ? 370 THR B CB 1 ATOM 2876 O OG1 . THR B 2 41 ? -41.098 44.133 -48.589 1.00 29.60 ? 370 THR B OG1 1 ATOM 2877 C CG2 . THR B 2 41 ? -40.482 44.971 -46.429 1.00 30.23 ? 370 THR B CG2 1 ATOM 2878 N N . GLN B 2 42 ? -43.206 47.237 -46.220 1.00 33.57 ? 371 GLN B N 1 ATOM 2879 C CA . GLN B 2 42 ? -43.359 48.191 -45.128 1.00 34.77 ? 371 GLN B CA 1 ATOM 2880 C C . GLN B 2 42 ? -44.678 47.965 -44.392 1.00 37.42 ? 371 GLN B C 1 ATOM 2881 O O . GLN B 2 42 ? -44.730 47.959 -43.154 1.00 33.26 ? 371 GLN B O 1 ATOM 2882 C CB . GLN B 2 42 ? -43.274 49.627 -45.651 1.00 31.68 ? 371 GLN B CB 1 ATOM 2883 C CG . GLN B 2 42 ? -43.172 50.667 -44.549 1.00 35.22 ? 371 GLN B CG 1 ATOM 2884 C CD . GLN B 2 42 ? -41.992 50.412 -43.623 1.00 40.31 ? 371 GLN B CD 1 ATOM 2885 O OE1 . GLN B 2 42 ? -40.853 50.258 -44.075 1.00 42.97 ? 371 GLN B OE1 1 ATOM 2886 N NE2 . GLN B 2 42 ? -42.263 50.350 -42.320 1.00 36.23 ? 371 GLN B NE2 1 ATOM 2887 N N . LYS B 2 43 ? -45.736 47.766 -45.171 1.00 27.14 ? 372 LYS B N 1 ATOM 2888 C CA . LYS B 2 43 ? -47.059 47.501 -44.631 1.00 29.87 ? 372 LYS B CA 1 ATOM 2889 C C . LYS B 2 43 ? -47.035 46.260 -43.734 1.00 33.89 ? 372 LYS B C 1 ATOM 2890 O O . LYS B 2 43 ? -47.664 46.234 -42.671 1.00 27.15 ? 372 LYS B O 1 ATOM 2891 C CB . LYS B 2 43 ? -48.050 47.305 -45.776 1.00 33.30 ? 372 LYS B CB 1 ATOM 2892 C CG . LYS B 2 43 ? -49.499 47.274 -45.337 1.00 44.65 ? 372 LYS B CG 1 ATOM 2893 C CD . LYS B 2 43 ? -50.375 46.626 -46.404 1.00 45.33 ? 372 LYS B CD 1 ATOM 2894 C CE . LYS B 2 43 ? -51.802 46.433 -45.900 1.00 53.23 ? 372 LYS B CE 1 ATOM 2895 N NZ . LYS B 2 43 ? -52.619 45.602 -46.835 1.00 58.84 ? 372 LYS B NZ 1 ATOM 2896 N N . ALA B 2 44 ? -46.288 45.239 -44.153 1.00 29.71 ? 373 ALA B N 1 ATOM 2897 C CA . ALA B 2 44 ? -46.178 44.014 -43.365 1.00 24.38 ? 373 ALA B CA 1 ATOM 2898 C C . ALA B 2 44 ? -45.359 44.237 -42.095 1.00 29.32 ? 373 ALA B C 1 ATOM 2899 O O . ALA B 2 44 ? -45.722 43.747 -41.020 1.00 27.40 ? 373 ALA B O 1 ATOM 2900 C CB . ALA B 2 44 ? -45.585 42.903 -44.190 1.00 23.77 ? 373 ALA B CB 1 ATOM 2901 N N . ILE B 2 45 ? -44.247 44.958 -42.227 1.00 29.13 ? 374 ILE B N 1 ATOM 2902 C CA . ILE B 2 45 ? -43.440 45.339 -41.076 1.00 27.84 ? 374 ILE B CA 1 ATOM 2903 C C . ILE B 2 45 ? -44.307 46.096 -40.068 1.00 29.03 ? 374 ILE B C 1 ATOM 2904 O O . ILE B 2 45 ? -44.254 45.816 -38.870 1.00 30.15 ? 374 ILE B O 1 ATOM 2905 C CB . ILE B 2 45 ? -42.227 46.209 -41.484 1.00 32.53 ? 374 ILE B CB 1 ATOM 2906 C CG1 . ILE B 2 45 ? -41.211 45.380 -42.275 1.00 34.35 ? 374 ILE B CG1 1 ATOM 2907 C CG2 . ILE B 2 45 ? -41.544 46.792 -40.261 1.00 24.86 ? 374 ILE B CG2 1 ATOM 2908 C CD1 . ILE B 2 45 ? -40.127 46.216 -42.965 1.00 28.21 ? 374 ILE B CD1 1 ATOM 2909 N N . ASP B 2 46 ? -45.111 47.040 -40.551 1.00 33.83 ? 375 ASP B N 1 ATOM 2910 C CA . ASP B 2 46 ? -45.971 47.821 -39.665 1.00 37.81 ? 375 ASP B CA 1 ATOM 2911 C C . ASP B 2 46 ? -47.023 46.959 -38.955 1.00 34.74 ? 375 ASP B C 1 ATOM 2912 O O . ASP B 2 46 ? -47.218 47.089 -37.747 1.00 33.96 ? 375 ASP B O 1 ATOM 2913 C CB . ASP B 2 46 ? -46.626 48.988 -40.419 1.00 35.71 ? 375 ASP B CB 1 ATOM 2914 C CG . ASP B 2 46 ? -45.611 50.032 -40.888 1.00 46.42 ? 375 ASP B CG 1 ATOM 2915 O OD1 . ASP B 2 46 ? -44.492 50.072 -40.332 1.00 45.73 ? 375 ASP B OD1 1 ATOM 2916 O OD2 . ASP B 2 46 ? -45.938 50.814 -41.812 1.00 46.39 ? 375 ASP B OD2 1 ATOM 2917 N N . GLY B 2 47 ? -47.682 46.073 -39.698 1.00 30.30 ? 376 GLY B N 1 ATOM 2918 C CA . GLY B 2 47 ? -48.675 45.187 -39.112 1.00 28.82 ? 376 GLY B CA 1 ATOM 2919 C C . GLY B 2 47 ? -48.080 44.297 -38.032 1.00 31.66 ? 376 GLY B C 1 ATOM 2920 O O . GLY B 2 47 ? -48.587 44.228 -36.905 1.00 28.39 ? 376 GLY B O 1 ATOM 2921 N N . ILE B 2 48 ? -46.982 43.632 -38.376 1.00 27.74 ? 377 ILE B N 1 ATOM 2922 C CA . ILE B 2 48 ? -46.334 42.686 -37.482 1.00 26.83 ? 377 ILE B CA 1 ATOM 2923 C C . ILE B 2 48 ? -45.719 43.369 -36.257 1.00 31.97 ? 377 ILE B C 1 ATOM 2924 O O . ILE B 2 48 ? -45.805 42.845 -35.136 1.00 28.64 ? 377 ILE B O 1 ATOM 2925 C CB . ILE B 2 48 ? -45.324 41.818 -38.261 1.00 30.03 ? 377 ILE B CB 1 ATOM 2926 C CG1 . ILE B 2 48 ? -46.091 40.760 -39.057 1.00 34.14 ? 377 ILE B CG1 1 ATOM 2927 C CG2 . ILE B 2 48 ? -44.351 41.119 -37.333 1.00 28.34 ? 377 ILE B CG2 1 ATOM 2928 C CD1 . ILE B 2 48 ? -45.389 40.315 -40.304 1.00 37.14 ? 377 ILE B CD1 1 ATOM 2929 N N . THR B 2 49 ? -45.127 44.545 -36.468 1.00 29.53 ? 378 THR B N 1 ATOM 2930 C CA . THR B 2 49 ? -44.628 45.364 -35.366 1.00 28.88 ? 378 THR B CA 1 ATOM 2931 C C . THR B 2 49 ? -45.781 45.738 -34.433 1.00 30.81 ? 378 THR B C 1 ATOM 2932 O O . THR B 2 49 ? -45.622 45.780 -33.208 1.00 32.40 ? 378 THR B O 1 ATOM 2933 C CB . THR B 2 49 ? -43.952 46.649 -35.875 1.00 31.33 ? 378 THR B CB 1 ATOM 2934 O OG1 . THR B 2 49 ? -42.859 46.305 -36.737 1.00 29.60 ? 378 THR B OG1 1 ATOM 2935 C CG2 . THR B 2 49 ? -43.442 47.493 -34.714 1.00 23.80 ? 378 THR B CG2 1 ATOM 2936 N N . ASN B 2 50 ? -46.944 46.006 -35.015 1.00 25.83 ? 379 ASN B N 1 ATOM 2937 C CA . ASN B 2 50 ? -48.111 46.334 -34.216 1.00 27.24 ? 379 ASN B CA 1 ATOM 2938 C C . ASN B 2 50 ? -48.571 45.124 -33.411 1.00 28.38 ? 379 ASN B C 1 ATOM 2939 O O . ASN B 2 50 ? -48.965 45.254 -32.250 1.00 26.29 ? 379 ASN B O 1 ATOM 2940 C CB . ASN B 2 50 ? -49.244 46.844 -35.099 1.00 28.48 ? 379 ASN B CB 1 ATOM 2941 C CG . ASN B 2 50 ? -50.346 47.498 -34.299 1.00 34.85 ? 379 ASN B CG 1 ATOM 2942 O OD1 . ASN B 2 50 ? -50.279 48.692 -33.994 1.00 42.57 ? 379 ASN B OD1 1 ATOM 2943 N ND2 . ASN B 2 50 ? -51.365 46.718 -33.940 1.00 28.93 ? 379 ASN B ND2 1 ATOM 2944 N N . LYS B 2 51 ? -48.517 43.946 -34.029 1.00 29.36 ? 380 LYS B N 1 ATOM 2945 C CA . LYS B 2 51 ? -48.945 42.718 -33.363 1.00 32.50 ? 380 LYS B CA 1 ATOM 2946 C C . LYS B 2 51 ? -48.051 42.414 -32.167 1.00 32.77 ? 380 LYS B C 1 ATOM 2947 O O . LYS B 2 51 ? -48.542 42.114 -31.075 1.00 30.75 ? 380 LYS B O 1 ATOM 2948 C CB . LYS B 2 51 ? -48.948 41.532 -34.330 1.00 29.43 ? 380 LYS B CB 1 ATOM 2949 C CG . LYS B 2 51 ? -49.249 40.210 -33.642 1.00 34.76 ? 380 LYS B CG 1 ATOM 2950 C CD . LYS B 2 51 ? -48.985 39.003 -34.542 1.00 32.98 ? 380 LYS B CD 1 ATOM 2951 C CE . LYS B 2 51 ? -49.942 38.972 -35.718 1.00 36.13 ? 380 LYS B CE 1 ATOM 2952 N NZ . LYS B 2 51 ? -50.018 37.612 -36.325 1.00 36.65 ? 380 LYS B NZ 1 ATOM 2953 N N . VAL B 2 52 ? -46.740 42.504 -32.383 1.00 28.60 ? 381 VAL B N 1 ATOM 2954 C CA . VAL B 2 52 ? -45.769 42.274 -31.324 1.00 28.04 ? 381 VAL B CA 1 ATOM 2955 C C . VAL B 2 52 ? -45.988 43.247 -30.156 1.00 29.84 ? 381 VAL B C 1 ATOM 2956 O O . VAL B 2 52 ? -46.064 42.826 -29.003 1.00 26.45 ? 381 VAL B O 1 ATOM 2957 C CB . VAL B 2 52 ? -44.322 42.343 -31.864 1.00 29.14 ? 381 VAL B CB 1 ATOM 2958 C CG1 . VAL B 2 52 ? -43.318 42.305 -30.726 1.00 28.90 ? 381 VAL B CG1 1 ATOM 2959 C CG2 . VAL B 2 52 ? -44.063 41.186 -32.821 1.00 21.45 ? 381 VAL B CG2 1 ATOM 2960 N N . ASN B 2 53 ? -46.112 44.537 -30.454 1.00 27.69 ? 382 ASN B N 1 ATOM 2961 C CA . ASN B 2 53 ? -46.321 45.527 -29.402 1.00 28.98 ? 382 ASN B CA 1 ATOM 2962 C C . ASN B 2 53 ? -47.656 45.368 -28.679 1.00 31.22 ? 382 ASN B C 1 ATOM 2963 O O . ASN B 2 53 ? -47.741 45.601 -27.477 1.00 33.24 ? 382 ASN B O 1 ATOM 2964 C CB . ASN B 2 53 ? -46.155 46.954 -29.939 1.00 25.94 ? 382 ASN B CB 1 ATOM 2965 C CG . ASN B 2 53 ? -44.719 47.264 -30.351 1.00 36.95 ? 382 ASN B CG 1 ATOM 2966 O OD1 . ASN B 2 53 ? -43.768 46.648 -29.857 1.00 32.87 ? 382 ASN B OD1 1 ATOM 2967 N ND2 . ASN B 2 53 ? -44.557 48.229 -31.261 1.00 33.94 ? 382 ASN B ND2 1 ATOM 2968 N N . SER B 2 54 ? -48.694 44.964 -29.404 1.00 29.76 ? 383 SER B N 1 ATOM 2969 C CA . SER B 2 54 ? -49.997 44.746 -28.785 1.00 31.24 ? 383 SER B CA 1 ATOM 2970 C C . SER B 2 54 ? -49.944 43.585 -27.796 1.00 32.11 ? 383 SER B C 1 ATOM 2971 O O . SER B 2 54 ? -50.541 43.648 -26.721 1.00 36.53 ? 383 SER B O 1 ATOM 2972 C CB . SER B 2 54 ? -51.079 44.494 -29.836 1.00 29.70 ? 383 SER B CB 1 ATOM 2973 O OG . SER B 2 54 ? -51.231 45.614 -30.682 1.00 33.98 ? 383 SER B OG 1 ATOM 2974 N N . ILE B 2 55 ? -49.226 42.528 -28.165 1.00 26.59 ? 384 ILE B N 1 ATOM 2975 C CA . ILE B 2 55 ? -49.041 41.377 -27.283 1.00 27.15 ? 384 ILE B CA 1 ATOM 2976 C C . ILE B 2 55 ? -48.265 41.767 -26.028 1.00 27.25 ? 384 ILE B C 1 ATOM 2977 O O . ILE B 2 55 ? -48.676 41.459 -24.907 1.00 29.90 ? 384 ILE B O 1 ATOM 2978 C CB . ILE B 2 55 ? -48.313 40.230 -28.010 1.00 29.91 ? 384 ILE B CB 1 ATOM 2979 C CG1 . ILE B 2 55 ? -49.215 39.651 -29.104 1.00 22.87 ? 384 ILE B CG1 1 ATOM 2980 C CG2 . ILE B 2 55 ? -47.888 39.144 -27.017 1.00 27.34 ? 384 ILE B CG2 1 ATOM 2981 C CD1 . ILE B 2 55 ? -48.545 38.597 -29.960 1.00 26.85 ? 384 ILE B CD1 1 ATOM 2982 N N . ILE B 2 56 ? -47.144 42.451 -26.227 1.00 27.07 ? 385 ILE B N 1 ATOM 2983 C CA . ILE B 2 56 ? -46.335 42.951 -25.124 1.00 32.24 ? 385 ILE B CA 1 ATOM 2984 C C . ILE B 2 56 ? -47.166 43.827 -24.177 1.00 35.79 ? 385 ILE B C 1 ATOM 2985 O O . ILE B 2 56 ? -47.087 43.682 -22.954 1.00 36.64 ? 385 ILE B O 1 ATOM 2986 C CB . ILE B 2 56 ? -45.108 43.722 -25.658 1.00 31.95 ? 385 ILE B CB 1 ATOM 2987 C CG1 . ILE B 2 56 ? -44.102 42.741 -26.269 1.00 30.51 ? 385 ILE B CG1 1 ATOM 2988 C CG2 . ILE B 2 56 ? -44.452 44.538 -24.554 1.00 23.64 ? 385 ILE B CG2 1 ATOM 2989 C CD1 . ILE B 2 56 ? -42.978 43.419 -27.046 1.00 27.57 ? 385 ILE B CD1 1 ATOM 2990 N N . ASN B 2 57 ? -47.977 44.713 -24.750 1.00 37.51 ? 386 ASN B N 1 ATOM 2991 C CA . ASN B 2 57 ? -48.807 45.620 -23.966 1.00 38.42 ? 386 ASN B CA 1 ATOM 2992 C C . ASN B 2 57 ? -49.886 44.910 -23.134 1.00 38.99 ? 386 ASN B C 1 ATOM 2993 O O . ASN B 2 57 ? -50.225 45.368 -22.043 1.00 43.85 ? 386 ASN B O 1 ATOM 2994 C CB . ASN B 2 57 ? -49.415 46.702 -24.879 1.00 42.82 ? 386 ASN B CB 1 ATOM 2995 C CG . ASN B 2 57 ? -50.272 47.710 -24.116 1.00 58.93 ? 386 ASN B CG 1 ATOM 2996 O OD1 . ASN B 2 57 ? -49.762 48.503 -23.318 1.00 64.92 ? 386 ASN B OD1 1 ATOM 2997 N ND2 . ASN B 2 57 ? -51.581 47.694 -24.375 1.00 52.94 ? 386 ASN B ND2 1 ATOM 2998 N N . LYS B 2 58 ? -50.422 43.797 -23.639 1.00 39.46 ? 387 LYS B N 1 ATOM 2999 C CA . LYS B 2 58 ? -51.471 43.059 -22.922 1.00 40.44 ? 387 LYS B CA 1 ATOM 3000 C C . LYS B 2 58 ? -50.879 42.161 -21.842 1.00 42.41 ? 387 LYS B C 1 ATOM 3001 O O . LYS B 2 58 ? -51.561 41.793 -20.885 1.00 40.55 ? 387 LYS B O 1 ATOM 3002 C CB . LYS B 2 58 ? -52.312 42.198 -23.874 1.00 38.27 ? 387 LYS B CB 1 ATOM 3003 C CG . LYS B 2 58 ? -53.068 42.956 -24.953 1.00 36.96 ? 387 LYS B CG 1 ATOM 3004 C CD . LYS B 2 58 ? -53.760 44.184 -24.395 1.00 40.75 ? 387 LYS B CD 1 ATOM 3005 C CE . LYS B 2 58 ? -54.439 44.969 -25.509 1.00 41.27 ? 387 LYS B CE 1 ATOM 3006 N NZ . LYS B 2 58 ? -54.990 46.255 -24.999 1.00 42.85 ? 387 LYS B NZ 1 ATOM 3007 N N . MET B 2 59 ? -49.610 41.805 -22.019 1.00 38.88 ? 388 MET B N 1 ATOM 3008 C CA . MET B 2 59 ? -48.895 40.945 -21.088 1.00 38.33 ? 388 MET B CA 1 ATOM 3009 C C . MET B 2 59 ? -48.128 41.799 -20.086 1.00 39.17 ? 388 MET B C 1 ATOM 3010 O O . MET B 2 59 ? -47.190 41.330 -19.444 1.00 44.78 ? 388 MET B O 1 ATOM 3011 C CB . MET B 2 59 ? -47.930 40.036 -21.856 1.00 36.53 ? 388 MET B CB 1 ATOM 3012 C CG . MET B 2 59 ? -48.609 38.997 -22.735 1.00 30.39 ? 388 MET B CG 1 ATOM 3013 S SD . MET B 2 59 ? -49.485 37.780 -21.732 1.00 44.20 ? 388 MET B SD 1 ATOM 3014 C CE . MET B 2 59 ? -49.791 36.477 -22.930 1.00 34.55 ? 388 MET B CE 1 ATOM 3015 N N . ASN B 2 60 ? -48.558 43.050 -19.946 1.00 48.03 ? 389 ASN B N 1 ATOM 3016 C CA . ASN B 2 60 ? -47.845 44.059 -19.162 1.00 47.71 ? 389 ASN B CA 1 ATOM 3017 C C . ASN B 2 60 ? -48.341 44.183 -17.717 1.00 49.37 ? 389 ASN B C 1 ATOM 3018 O O . ASN B 2 60 ? -48.136 45.207 -17.062 1.00 51.94 ? 389 ASN B O 1 ATOM 3019 C CB . ASN B 2 60 ? -47.955 45.413 -19.873 1.00 55.95 ? 389 ASN B CB 1 ATOM 3020 C CG . ASN B 2 60 ? -46.975 46.450 -19.342 1.00 75.93 ? 389 ASN B CG 1 ATOM 3021 O OD1 . ASN B 2 60 ? -46.000 46.120 -18.659 1.00 72.65 ? 389 ASN B OD1 1 ATOM 3022 N ND2 . ASN B 2 60 ? -47.236 47.719 -19.657 1.00 78.21 ? 389 ASN B ND2 1 ATOM 3023 N N . THR B 2 61 ? -49.007 43.148 -17.220 1.00 39.36 ? 390 THR B N 1 ATOM 3024 C CA . THR B 2 61 ? -49.325 43.085 -15.796 1.00 41.99 ? 390 THR B CA 1 ATOM 3025 C C . THR B 2 61 ? -48.538 41.929 -15.204 1.00 39.33 ? 390 THR B C 1 ATOM 3026 O O . THR B 2 61 ? -48.064 41.066 -15.941 1.00 38.72 ? 390 THR B O 1 ATOM 3027 C CB . THR B 2 61 ? -50.837 42.914 -15.524 1.00 41.31 ? 390 THR B CB 1 ATOM 3028 O OG1 . THR B 2 61 ? -51.328 41.748 -16.192 1.00 41.62 ? 390 THR B OG1 1 ATOM 3029 C CG2 . THR B 2 61 ? -51.606 44.129 -16.006 1.00 32.81 ? 390 THR B CG2 1 ATOM 3030 N N . GLN B 2 62 ? -48.371 41.915 -13.886 1.00 40.04 ? 391 GLN B N 1 ATOM 3031 C CA . GLN B 2 62 ? -47.734 40.773 -13.237 1.00 39.04 ? 391 GLN B CA 1 ATOM 3032 C C . GLN B 2 62 ? -48.546 40.332 -12.033 1.00 40.26 ? 391 GLN B C 1 ATOM 3033 O O . GLN B 2 62 ? -49.013 41.165 -11.251 1.00 42.01 ? 391 GLN B O 1 ATOM 3034 C CB . GLN B 2 62 ? -46.289 41.087 -12.812 1.00 40.09 ? 391 GLN B CB 1 ATOM 3035 C CG . GLN B 2 62 ? -45.324 41.407 -13.960 1.00 35.64 ? 391 GLN B CG 1 ATOM 3036 C CD . GLN B 2 62 ? -45.439 42.848 -14.434 1.00 40.52 ? 391 GLN B CD 1 ATOM 3037 O OE1 . GLN B 2 62 ? -45.708 43.750 -13.639 1.00 45.88 ? 391 GLN B OE1 1 ATOM 3038 N NE2 . GLN B 2 62 ? -45.245 43.070 -15.734 1.00 42.78 ? 391 GLN B NE2 1 ATOM 3039 N N . PHE B 2 63 ? -48.731 39.023 -11.894 1.00 37.26 ? 392 PHE B N 1 ATOM 3040 C CA . PHE B 2 63 ? -49.246 38.489 -10.647 1.00 33.94 ? 392 PHE B CA 1 ATOM 3041 C C . PHE B 2 63 ? -48.078 38.402 -9.668 1.00 35.80 ? 392 PHE B C 1 ATOM 3042 O O . PHE B 2 63 ? -47.003 37.909 -10.020 1.00 38.39 ? 392 PHE B O 1 ATOM 3043 C CB . PHE B 2 63 ? -49.874 37.114 -10.838 1.00 28.41 ? 392 PHE B CB 1 ATOM 3044 C CG . PHE B 2 63 ? -50.219 36.444 -9.545 1.00 34.79 ? 392 PHE B CG 1 ATOM 3045 C CD1 . PHE B 2 63 ? -51.397 36.759 -8.880 1.00 25.65 ? 392 PHE B CD1 1 ATOM 3046 C CD2 . PHE B 2 63 ? -49.349 35.522 -8.972 1.00 32.72 ? 392 PHE B CD2 1 ATOM 3047 C CE1 . PHE B 2 63 ? -51.707 36.160 -7.672 1.00 29.49 ? 392 PHE B CE1 1 ATOM 3048 C CE2 . PHE B 2 63 ? -49.652 34.915 -7.765 1.00 30.40 ? 392 PHE B CE2 1 ATOM 3049 C CZ . PHE B 2 63 ? -50.835 35.232 -7.116 1.00 34.73 ? 392 PHE B CZ 1 ATOM 3050 N N . GLU B 2 64 ? -48.274 38.874 -8.442 1.00 38.38 ? 393 GLU B N 1 ATOM 3051 C CA . GLU B 2 64 ? -47.160 38.920 -7.503 1.00 50.35 ? 393 GLU B CA 1 ATOM 3052 C C . GLU B 2 64 ? -47.301 37.931 -6.344 1.00 42.54 ? 393 GLU B C 1 ATOM 3053 O O . GLU B 2 64 ? -48.221 38.024 -5.532 1.00 42.97 ? 393 GLU B O 1 ATOM 3054 C CB . GLU B 2 64 ? -46.913 40.359 -7.017 1.00 53.16 ? 393 GLU B CB 1 ATOM 3055 C CG . GLU B 2 64 ? -46.568 41.326 -8.161 1.00 58.09 ? 393 GLU B CG 1 ATOM 3056 C CD . GLU B 2 64 ? -45.961 42.643 -7.693 1.00 68.09 ? 393 GLU B CD 1 ATOM 3057 O OE1 . GLU B 2 64 ? -44.720 42.714 -7.567 1.00 72.10 ? 393 GLU B OE1 1 ATOM 3058 O OE2 . GLU B 2 64 ? -46.718 43.611 -7.463 1.00 75.47 ? 393 GLU B OE2 1 ATOM 3059 N N . ALA B 2 65 ? -46.385 36.967 -6.298 1.00 31.59 ? 394 ALA B N 1 ATOM 3060 C CA . ALA B 2 65 ? -46.325 36.013 -5.202 1.00 36.21 ? 394 ALA B CA 1 ATOM 3061 C C . ALA B 2 65 ? -45.632 36.662 -4.009 1.00 37.47 ? 394 ALA B C 1 ATOM 3062 O O . ALA B 2 65 ? -44.862 37.617 -4.167 1.00 40.83 ? 394 ALA B O 1 ATOM 3063 C CB . ALA B 2 65 ? -45.594 34.762 -5.629 1.00 36.00 ? 394 ALA B CB 1 ATOM 3064 N N . VAL B 2 66 ? -45.900 36.144 -2.815 1.00 38.85 ? 395 VAL B N 1 ATOM 3065 C CA . VAL B 2 66 ? -45.382 36.763 -1.602 1.00 41.19 ? 395 VAL B CA 1 ATOM 3066 C C . VAL B 2 66 ? -44.503 35.828 -0.786 1.00 41.86 ? 395 VAL B C 1 ATOM 3067 O O . VAL B 2 66 ? -44.556 34.606 -0.937 1.00 41.51 ? 395 VAL B O 1 ATOM 3068 C CB . VAL B 2 66 ? -46.523 37.283 -0.713 1.00 45.06 ? 395 VAL B CB 1 ATOM 3069 C CG1 . VAL B 2 66 ? -47.279 38.392 -1.423 1.00 35.71 ? 395 VAL B CG1 1 ATOM 3070 C CG2 . VAL B 2 66 ? -47.465 36.139 -0.334 1.00 41.57 ? 395 VAL B CG2 1 ATOM 3071 N N . ASP B 2 67 ? -43.704 36.424 0.091 1.00 53.50 ? 396 ASP B N 1 ATOM 3072 C CA . ASP B 2 67 ? -42.806 35.677 0.961 1.00 51.98 ? 396 ASP B CA 1 ATOM 3073 C C . ASP B 2 67 ? -43.453 35.395 2.319 1.00 45.35 ? 396 ASP B C 1 ATOM 3074 O O . ASP B 2 67 ? -42.772 34.995 3.269 1.00 46.52 ? 396 ASP B O 1 ATOM 3075 C CB . ASP B 2 67 ? -41.520 36.475 1.165 1.00 51.05 ? 396 ASP B CB 1 ATOM 3076 C CG . ASP B 2 67 ? -41.787 37.957 1.418 1.00 58.06 ? 396 ASP B CG 1 ATOM 3077 O OD1 . ASP B 2 67 ? -41.571 38.768 0.488 1.00 58.31 ? 396 ASP B OD1 1 ATOM 3078 O OD2 . ASP B 2 67 ? -42.220 38.309 2.540 1.00 47.46 ? 396 ASP B OD2 1 ATOM 3079 N N . HIS B 2 68 ? -44.765 35.600 2.406 1.00 33.06 ? 397 HIS B N 1 ATOM 3080 C CA . HIS B 2 68 ? -45.488 35.446 3.670 1.00 32.75 ? 397 HIS B CA 1 ATOM 3081 C C . HIS B 2 68 ? -45.392 34.029 4.212 1.00 30.23 ? 397 HIS B C 1 ATOM 3082 O O . HIS B 2 68 ? -45.426 33.057 3.450 1.00 35.92 ? 397 HIS B O 1 ATOM 3083 C CB . HIS B 2 68 ? -46.954 35.836 3.500 1.00 32.29 ? 397 HIS B CB 1 ATOM 3084 C CG . HIS B 2 68 ? -47.184 37.307 3.400 1.00 30.60 ? 397 HIS B CG 1 ATOM 3085 N ND1 . HIS B 2 68 ? -48.341 37.847 2.890 1.00 34.58 ? 397 HIS B ND1 1 ATOM 3086 C CD2 . HIS B 2 68 ? -46.401 38.357 3.760 1.00 31.09 ? 397 HIS B CD2 1 ATOM 3087 C CE1 . HIS B 2 68 ? -48.266 39.165 2.933 1.00 34.46 ? 397 HIS B CE1 1 ATOM 3088 N NE2 . HIS B 2 68 ? -47.104 39.500 3.454 1.00 33.34 ? 397 HIS B NE2 1 ATOM 3089 N N . GLU B 2 69 ? -45.271 33.914 5.531 1.00 31.00 ? 398 GLU B N 1 ATOM 3090 C CA . GLU B 2 69 ? -45.148 32.612 6.171 1.00 33.13 ? 398 GLU B CA 1 ATOM 3091 C C . GLU B 2 69 ? -46.447 32.196 6.853 1.00 32.09 ? 398 GLU B C 1 ATOM 3092 O O . GLU B 2 69 ? -47.335 33.023 7.091 1.00 28.70 ? 398 GLU B O 1 ATOM 3093 C CB . GLU B 2 69 ? -43.993 32.614 7.179 1.00 37.94 ? 398 GLU B CB 1 ATOM 3094 C CG . GLU B 2 69 ? -42.627 32.876 6.558 1.00 41.67 ? 398 GLU B CG 1 ATOM 3095 C CD . GLU B 2 69 ? -41.476 32.634 7.526 1.00 56.24 ? 398 GLU B CD 1 ATOM 3096 O OE1 . GLU B 2 69 ? -41.697 32.664 8.762 1.00 52.10 ? 398 GLU B OE1 1 ATOM 3097 O OE2 . GLU B 2 69 ? -40.345 32.408 7.042 1.00 60.46 ? 398 GLU B OE2 1 ATOM 3098 N N . PHE B 2 70 ? -46.550 30.910 7.168 1.00 34.17 ? 399 PHE B N 1 ATOM 3099 C CA . PHE B 2 70 ? -47.731 30.386 7.827 1.00 33.23 ? 399 PHE B CA 1 ATOM 3100 C C . PHE B 2 70 ? -47.310 29.366 8.875 1.00 34.71 ? 399 PHE B C 1 ATOM 3101 O O . PHE B 2 70 ? -46.420 28.548 8.626 1.00 38.36 ? 399 PHE B O 1 ATOM 3102 C CB . PHE B 2 70 ? -48.670 29.761 6.792 1.00 28.74 ? 399 PHE B CB 1 ATOM 3103 C CG . PHE B 2 70 ? -49.133 30.732 5.741 1.00 31.36 ? 399 PHE B CG 1 ATOM 3104 C CD1 . PHE B 2 70 ? -50.277 31.499 5.938 1.00 27.37 ? 399 PHE B CD1 1 ATOM 3105 C CD2 . PHE B 2 70 ? -48.414 30.894 4.558 1.00 31.01 ? 399 PHE B CD2 1 ATOM 3106 C CE1 . PHE B 2 70 ? -50.704 32.406 4.969 1.00 26.77 ? 399 PHE B CE1 1 ATOM 3107 C CE2 . PHE B 2 70 ? -48.829 31.801 3.589 1.00 28.08 ? 399 PHE B CE2 1 ATOM 3108 C CZ . PHE B 2 70 ? -49.977 32.557 3.794 1.00 30.59 ? 399 PHE B CZ 1 ATOM 3109 N N . SER B 2 71 ? -47.940 29.424 10.046 1.00 34.42 ? 400 SER B N 1 ATOM 3110 C CA . SER B 2 71 ? -47.605 28.521 11.147 1.00 38.09 ? 400 SER B CA 1 ATOM 3111 C C . SER B 2 71 ? -48.125 27.108 10.891 1.00 40.30 ? 400 SER B C 1 ATOM 3112 O O . SER B 2 71 ? -48.774 26.849 9.872 1.00 36.52 ? 400 SER B O 1 ATOM 3113 C CB . SER B 2 71 ? -48.167 29.048 12.470 1.00 33.13 ? 400 SER B CB 1 ATOM 3114 O OG . SER B 2 71 ? -49.580 28.972 12.503 1.00 33.52 ? 400 SER B OG 1 ATOM 3115 N N . ASN B 2 72 ? -47.829 26.198 11.816 1.00 45.67 ? 401 ASN B N 1 ATOM 3116 C CA . ASN B 2 72 ? -48.302 24.818 11.728 1.00 49.96 ? 401 ASN B CA 1 ATOM 3117 C C . ASN B 2 72 ? -49.823 24.709 11.789 1.00 45.85 ? 401 ASN B C 1 ATOM 3118 O O . ASN B 2 72 ? -50.397 23.736 11.300 1.00 43.57 ? 401 ASN B O 1 ATOM 3119 C CB . ASN B 2 72 ? -47.680 23.961 12.842 1.00 55.02 ? 401 ASN B CB 1 ATOM 3120 C CG . ASN B 2 72 ? -46.238 23.576 12.553 1.00 73.10 ? 401 ASN B CG 1 ATOM 3121 O OD1 . ASN B 2 72 ? -45.838 23.418 11.393 1.00 68.81 ? 401 ASN B OD1 1 ATOM 3122 N ND2 . ASN B 2 72 ? -45.449 23.415 13.613 1.00 73.55 ? 401 ASN B ND2 1 ATOM 3123 N N . LEU B 2 73 ? -50.463 25.706 12.399 1.00 42.90 ? 402 LEU B N 1 ATOM 3124 C CA . LEU B 2 73 ? -51.917 25.723 12.550 1.00 39.67 ? 402 LEU B CA 1 ATOM 3125 C C . LEU B 2 73 ? -52.597 26.631 11.521 1.00 40.24 ? 402 LEU B C 1 ATOM 3126 O O . LEU B 2 73 ? -53.757 27.013 11.687 1.00 37.75 ? 402 LEU B O 1 ATOM 3127 C CB . LEU B 2 73 ? -52.302 26.144 13.973 1.00 38.94 ? 402 LEU B CB 1 ATOM 3128 C CG . LEU B 2 73 ? -51.902 25.155 15.071 1.00 43.94 ? 402 LEU B CG 1 ATOM 3129 C CD1 . LEU B 2 73 ? -52.181 25.725 16.449 1.00 41.55 ? 402 LEU B CD1 1 ATOM 3130 C CD2 . LEU B 2 73 ? -52.629 23.827 14.897 1.00 36.56 ? 402 LEU B CD2 1 ATOM 3131 N N . GLU B 2 74 ? -51.865 26.974 10.462 1.00 37.87 ? 403 GLU B N 1 ATOM 3132 C CA . GLU B 2 74 ? -52.411 27.751 9.355 1.00 36.47 ? 403 GLU B CA 1 ATOM 3133 C C . GLU B 2 74 ? -52.159 27.005 8.055 1.00 35.53 ? 403 GLU B C 1 ATOM 3134 O O . GLU B 2 74 ? -51.899 27.603 7.008 1.00 35.22 ? 403 GLU B O 1 ATOM 3135 C CB . GLU B 2 74 ? -51.788 29.147 9.316 1.00 35.79 ? 403 GLU B CB 1 ATOM 3136 C CG . GLU B 2 74 ? -52.047 29.964 10.564 1.00 34.59 ? 403 GLU B CG 1 ATOM 3137 C CD . GLU B 2 74 ? -51.318 31.290 10.557 1.00 37.05 ? 403 GLU B CD 1 ATOM 3138 O OE1 . GLU B 2 74 ? -50.111 31.309 10.215 1.00 33.31 ? 403 GLU B OE1 1 ATOM 3139 O OE2 . GLU B 2 74 ? -51.957 32.312 10.893 1.00 37.22 ? 403 GLU B OE2 1 ATOM 3140 N N . ARG B 2 75 ? -52.230 25.683 8.147 1.00 36.87 ? 404 ARG B N 1 ATOM 3141 C CA . ARG B 2 75 ? -52.038 24.796 7.008 1.00 34.95 ? 404 ARG B CA 1 ATOM 3142 C C . ARG B 2 75 ? -53.060 25.068 5.907 1.00 36.57 ? 404 ARG B C 1 ATOM 3143 O O . ARG B 2 75 ? -52.719 25.065 4.717 1.00 35.54 ? 404 ARG B O 1 ATOM 3144 C CB . ARG B 2 75 ? -52.127 23.339 7.481 1.00 36.26 ? 404 ARG B CB 1 ATOM 3145 C CG . ARG B 2 75 ? -52.141 22.283 6.384 1.00 46.26 ? 404 ARG B CG 1 ATOM 3146 C CD . ARG B 2 75 ? -52.141 20.866 6.967 1.00 45.80 ? 404 ARG B CD 1 ATOM 3147 N NE . ARG B 2 75 ? -50.932 20.136 6.590 1.00 50.70 ? 404 ARG B NE 1 ATOM 3148 C CZ . ARG B 2 75 ? -49.874 19.974 7.379 1.00 50.43 ? 404 ARG B CZ 1 ATOM 3149 N NH1 . ARG B 2 75 ? -49.869 20.475 8.611 1.00 48.28 ? 404 ARG B NH1 1 ATOM 3150 N NH2 . ARG B 2 75 ? -48.821 19.302 6.936 1.00 51.82 ? 404 ARG B NH2 1 ATOM 3151 N N . ARG B 2 76 ? -54.307 25.326 6.300 1.00 30.18 ? 405 ARG B N 1 ATOM 3152 C CA . ARG B 2 76 ? -55.368 25.598 5.324 1.00 32.64 ? 405 ARG B CA 1 ATOM 3153 C C . ARG B 2 76 ? -55.124 26.874 4.503 1.00 28.20 ? 405 ARG B C 1 ATOM 3154 O O . ARG B 2 76 ? -55.180 26.839 3.272 1.00 28.25 ? 405 ARG B O 1 ATOM 3155 C CB . ARG B 2 76 ? -56.746 25.625 6.001 1.00 27.13 ? 405 ARG B CB 1 ATOM 3156 C CG . ARG B 2 76 ? -57.221 24.252 6.496 1.00 28.21 ? 405 ARG B CG 1 ATOM 3157 C CD . ARG B 2 76 ? -58.401 24.384 7.438 1.00 25.37 ? 405 ARG B CD 1 ATOM 3158 N NE . ARG B 2 76 ? -58.059 25.227 8.580 1.00 28.84 ? 405 ARG B NE 1 ATOM 3159 C CZ . ARG B 2 76 ? -58.889 26.085 9.163 1.00 30.12 ? 405 ARG B CZ 1 ATOM 3160 N NH1 . ARG B 2 76 ? -60.131 26.223 8.717 1.00 29.07 ? 405 ARG B NH1 1 ATOM 3161 N NH2 . ARG B 2 76 ? -58.469 26.808 10.191 1.00 25.42 ? 405 ARG B NH2 1 ATOM 3162 N N . ILE B 2 77 ? -54.842 27.992 5.170 1.00 30.54 ? 406 ILE B N 1 ATOM 3163 C CA . ILE B 2 77 ? -54.600 29.236 4.438 1.00 34.98 ? 406 ILE B CA 1 ATOM 3164 C C . ILE B 2 77 ? -53.254 29.213 3.719 1.00 34.07 ? 406 ILE B C 1 ATOM 3165 O O . ILE B 2 77 ? -53.129 29.774 2.627 1.00 31.79 ? 406 ILE B O 1 ATOM 3166 C CB . ILE B 2 77 ? -54.722 30.497 5.320 1.00 34.96 ? 406 ILE B CB 1 ATOM 3167 C CG1 . ILE B 2 77 ? -53.734 30.448 6.488 1.00 37.20 ? 406 ILE B CG1 1 ATOM 3168 C CG2 . ILE B 2 77 ? -56.149 30.651 5.821 1.00 34.48 ? 406 ILE B CG2 1 ATOM 3169 C CD1 . ILE B 2 77 ? -53.745 31.714 7.343 1.00 36.47 ? 406 ILE B CD1 1 ATOM 3170 N N . GLY B 2 78 ? -52.255 28.573 4.325 1.00 23.95 ? 407 GLY B N 1 ATOM 3171 C CA . GLY B 2 78 ? -50.974 28.378 3.665 1.00 24.28 ? 407 GLY B CA 1 ATOM 3172 C C . GLY B 2 78 ? -51.127 27.672 2.323 1.00 27.04 ? 407 GLY B C 1 ATOM 3173 O O . GLY B 2 78 ? -50.501 28.055 1.332 1.00 26.51 ? 407 GLY B O 1 ATOM 3174 N N . ASN B 2 79 ? -51.975 26.648 2.288 1.00 27.45 ? 408 ASN B N 1 ATOM 3175 C CA . ASN B 2 79 ? -52.179 25.853 1.085 1.00 27.78 ? 408 ASN B CA 1 ATOM 3176 C C . ASN B 2 79 ? -53.111 26.556 0.099 1.00 32.61 ? 408 ASN B C 1 ATOM 3177 O O . ASN B 2 79 ? -53.037 26.343 -1.121 1.00 29.92 ? 408 ASN B O 1 ATOM 3178 C CB . ASN B 2 79 ? -52.710 24.466 1.455 1.00 28.86 ? 408 ASN B CB 1 ATOM 3179 C CG . ASN B 2 79 ? -53.121 23.654 0.241 1.00 43.90 ? 408 ASN B CG 1 ATOM 3180 O OD1 . ASN B 2 79 ? -54.313 23.457 -0.014 1.00 45.57 ? 408 ASN B OD1 1 ATOM 3181 N ND2 . ASN B 2 79 ? -52.134 23.190 -0.527 1.00 44.96 ? 408 ASN B ND2 1 ATOM 3182 N N . LEU B 2 80 ? -53.989 27.399 0.634 1.00 31.21 ? 409 LEU B N 1 ATOM 3183 C CA . LEU B 2 80 ? -54.848 28.231 -0.196 1.00 30.54 ? 409 LEU B CA 1 ATOM 3184 C C . LEU B 2 80 ? -53.968 29.204 -0.981 1.00 32.27 ? 409 LEU B C 1 ATOM 3185 O O . LEU B 2 80 ? -54.105 29.347 -2.203 1.00 33.16 ? 409 LEU B O 1 ATOM 3186 C CB . LEU B 2 80 ? -55.859 28.980 0.676 1.00 32.15 ? 409 LEU B CB 1 ATOM 3187 C CG . LEU B 2 80 ? -57.123 29.588 0.064 1.00 38.42 ? 409 LEU B CG 1 ATOM 3188 C CD1 . LEU B 2 80 ? -58.122 29.917 1.158 1.00 32.20 ? 409 LEU B CD1 1 ATOM 3189 C CD2 . LEU B 2 80 ? -56.803 30.847 -0.719 1.00 42.42 ? 409 LEU B CD2 1 ATOM 3190 N N . ASN B 2 81 ? -53.054 29.861 -0.277 1.00 27.44 ? 410 ASN B N 1 ATOM 3191 C CA . ASN B 2 81 ? -52.133 30.783 -0.922 1.00 30.31 ? 410 ASN B CA 1 ATOM 3192 C C . ASN B 2 81 ? -51.305 30.090 -1.995 1.00 29.58 ? 410 ASN B C 1 ATOM 3193 O O . ASN B 2 81 ? -51.120 30.622 -3.089 1.00 30.35 ? 410 ASN B O 1 ATOM 3194 C CB . ASN B 2 81 ? -51.211 31.438 0.107 1.00 29.30 ? 410 ASN B CB 1 ATOM 3195 C CG . ASN B 2 81 ? -50.270 32.447 -0.520 1.00 30.26 ? 410 ASN B CG 1 ATOM 3196 O OD1 . ASN B 2 81 ? -50.701 33.495 -1.008 1.00 31.68 ? 410 ASN B OD1 1 ATOM 3197 N ND2 . ASN B 2 81 ? -48.979 32.135 -0.515 1.00 29.23 ? 410 ASN B ND2 1 ATOM 3198 N N . LYS B 2 82 ? -50.813 28.898 -1.678 1.00 29.61 ? 411 LYS B N 1 ATOM 3199 C CA . LYS B 2 82 ? -50.005 28.140 -2.621 1.00 32.57 ? 411 LYS B CA 1 ATOM 3200 C C . LYS B 2 82 ? -50.810 27.772 -3.870 1.00 31.38 ? 411 LYS B C 1 ATOM 3201 O O . LYS B 2 82 ? -50.353 27.996 -4.992 1.00 29.72 ? 411 LYS B O 1 ATOM 3202 C CB . LYS B 2 82 ? -49.431 26.883 -1.959 1.00 31.63 ? 411 LYS B CB 1 ATOM 3203 C CG . LYS B 2 82 ? -48.382 26.170 -2.809 1.00 39.95 ? 411 LYS B CG 1 ATOM 3204 C CD . LYS B 2 82 ? -48.689 24.678 -2.947 1.00 50.86 ? 411 LYS B CD 1 ATOM 3205 C CE . LYS B 2 82 ? -47.666 23.952 -3.822 1.00 52.34 ? 411 LYS B CE 1 ATOM 3206 N NZ . LYS B 2 82 ? -46.275 24.066 -3.303 1.00 57.22 ? 411 LYS B NZ 1 ATOM 3207 N N . ARG B 2 83 ? -52.007 27.221 -3.680 1.00 29.23 ? 412 ARG B N 1 ATOM 3208 C CA . ARG B 2 83 ? -52.851 26.829 -4.812 1.00 30.10 ? 412 ARG B CA 1 ATOM 3209 C C . ARG B 2 83 ? -53.256 28.028 -5.660 1.00 30.85 ? 412 ARG B C 1 ATOM 3210 O O . ARG B 2 83 ? -53.404 27.909 -6.876 1.00 25.40 ? 412 ARG B O 1 ATOM 3211 C CB . ARG B 2 83 ? -54.098 26.070 -4.339 1.00 27.68 ? 412 ARG B CB 1 ATOM 3212 C CG . ARG B 2 83 ? -53.851 24.609 -3.986 1.00 34.43 ? 412 ARG B CG 1 ATOM 3213 C CD . ARG B 2 83 ? -54.852 24.106 -2.954 1.00 35.12 ? 412 ARG B CD 1 ATOM 3214 N NE . ARG B 2 83 ? -56.224 24.482 -3.289 1.00 43.96 ? 412 ARG B NE 1 ATOM 3215 C CZ . ARG B 2 83 ? -57.062 25.107 -2.465 1.00 36.47 ? 412 ARG B CZ 1 ATOM 3216 N NH1 . ARG B 2 83 ? -56.687 25.427 -1.234 1.00 28.93 ? 412 ARG B NH1 1 ATOM 3217 N NH2 . ARG B 2 83 ? -58.286 25.404 -2.875 1.00 41.38 ? 412 ARG B NH2 1 ATOM 3218 N N . MET B 2 84 ? -53.437 29.181 -5.020 1.00 32.36 ? 413 MET B N 1 ATOM 3219 C CA . MET B 2 84 ? -53.762 30.399 -5.751 1.00 29.81 ? 413 MET B CA 1 ATOM 3220 C C . MET B 2 84 ? -52.598 30.836 -6.630 1.00 31.96 ? 413 MET B C 1 ATOM 3221 O O . MET B 2 84 ? -52.772 31.085 -7.829 1.00 31.16 ? 413 MET B O 1 ATOM 3222 C CB . MET B 2 84 ? -54.123 31.543 -4.808 1.00 27.43 ? 413 MET B CB 1 ATOM 3223 C CG . MET B 2 84 ? -54.592 32.762 -5.566 1.00 34.78 ? 413 MET B CG 1 ATOM 3224 S SD . MET B 2 84 ? -54.438 34.293 -4.654 1.00 45.81 ? 413 MET B SD 1 ATOM 3225 C CE . MET B 2 84 ? -52.669 34.349 -4.380 1.00 40.77 ? 413 MET B CE 1 ATOM 3226 N N . GLU B 2 85 ? -51.414 30.938 -6.032 1.00 27.68 ? 414 GLU B N 1 ATOM 3227 C CA . GLU B 2 85 ? -50.229 31.332 -6.779 1.00 30.26 ? 414 GLU B CA 1 ATOM 3228 C C . GLU B 2 85 ? -49.966 30.361 -7.930 1.00 29.69 ? 414 GLU B C 1 ATOM 3229 O O . GLU B 2 85 ? -49.808 30.791 -9.074 1.00 29.38 ? 414 GLU B O 1 ATOM 3230 C CB . GLU B 2 85 ? -49.023 31.482 -5.845 1.00 26.40 ? 414 GLU B CB 1 ATOM 3231 C CG . GLU B 2 85 ? -49.148 32.705 -4.920 1.00 35.70 ? 414 GLU B CG 1 ATOM 3232 C CD . GLU B 2 85 ? -48.037 32.806 -3.880 1.00 41.02 ? 414 GLU B CD 1 ATOM 3233 O OE1 . GLU B 2 85 ? -47.200 31.880 -3.801 1.00 46.15 ? 414 GLU B OE1 1 ATOM 3234 O OE2 . GLU B 2 85 ? -48.003 33.816 -3.139 1.00 37.24 ? 414 GLU B OE2 1 ATOM 3235 N N . ASP B 2 86 ? -49.945 29.063 -7.639 1.00 26.35 ? 415 ASP B N 1 ATOM 3236 C CA . ASP B 2 86 ? -49.799 28.066 -8.693 1.00 26.40 ? 415 ASP B CA 1 ATOM 3237 C C . ASP B 2 86 ? -50.936 28.169 -9.717 1.00 28.89 ? 415 ASP B C 1 ATOM 3238 O O . ASP B 2 86 ? -50.725 27.957 -10.908 1.00 28.30 ? 415 ASP B O 1 ATOM 3239 C CB . ASP B 2 86 ? -49.714 26.653 -8.104 1.00 30.59 ? 415 ASP B CB 1 ATOM 3240 C CG . ASP B 2 86 ? -48.442 26.429 -7.301 1.00 42.93 ? 415 ASP B CG 1 ATOM 3241 O OD1 . ASP B 2 86 ? -47.565 27.323 -7.307 1.00 41.53 ? 415 ASP B OD1 1 ATOM 3242 O OD2 . ASP B 2 86 ? -48.320 25.351 -6.674 1.00 46.46 ? 415 ASP B OD2 1 ATOM 3243 N N . GLY B 2 87 ? -52.132 28.517 -9.250 1.00 27.06 ? 416 GLY B N 1 ATOM 3244 C CA . GLY B 2 87 ? -53.260 28.746 -10.134 1.00 22.56 ? 416 GLY B CA 1 ATOM 3245 C C . GLY B 2 87 ? -52.975 29.771 -11.223 1.00 29.63 ? 416 GLY B C 1 ATOM 3246 O O . GLY B 2 87 ? -53.069 29.455 -12.417 1.00 24.42 ? 416 GLY B O 1 ATOM 3247 N N . PHE B 2 88 ? -52.619 30.992 -10.825 1.00 27.78 ? 417 PHE B N 1 ATOM 3248 C CA . PHE B 2 88 ? -52.365 32.062 -11.788 1.00 26.29 ? 417 PHE B CA 1 ATOM 3249 C C . PHE B 2 88 ? -51.136 31.783 -12.649 1.00 28.33 ? 417 PHE B C 1 ATOM 3250 O O . PHE B 2 88 ? -51.121 32.107 -13.841 1.00 28.93 ? 417 PHE B O 1 ATOM 3251 C CB . PHE B 2 88 ? -52.233 33.413 -11.081 1.00 24.47 ? 417 PHE B CB 1 ATOM 3252 C CG . PHE B 2 88 ? -53.539 33.965 -10.587 1.00 26.80 ? 417 PHE B CG 1 ATOM 3253 C CD1 . PHE B 2 88 ? -54.549 34.308 -11.480 1.00 26.15 ? 417 PHE B CD1 1 ATOM 3254 C CD2 . PHE B 2 88 ? -53.760 34.147 -9.230 1.00 26.74 ? 417 PHE B CD2 1 ATOM 3255 C CE1 . PHE B 2 88 ? -55.765 34.821 -11.023 1.00 24.60 ? 417 PHE B CE1 1 ATOM 3256 C CE2 . PHE B 2 88 ? -54.964 34.664 -8.765 1.00 28.91 ? 417 PHE B CE2 1 ATOM 3257 C CZ . PHE B 2 88 ? -55.970 34.998 -9.663 1.00 27.96 ? 417 PHE B CZ 1 ATOM 3258 N N . LEU B 2 89 ? -50.109 31.188 -12.051 1.00 23.37 ? 418 LEU B N 1 ATOM 3259 C CA . LEU B 2 89 ? -48.930 30.783 -12.813 1.00 27.05 ? 418 LEU B CA 1 ATOM 3260 C C . LEU B 2 89 ? -49.322 29.854 -13.968 1.00 27.10 ? 418 LEU B C 1 ATOM 3261 O O . LEU B 2 89 ? -48.811 29.984 -15.091 1.00 27.70 ? 418 LEU B O 1 ATOM 3262 C CB . LEU B 2 89 ? -47.897 30.106 -11.906 1.00 24.38 ? 418 LEU B CB 1 ATOM 3263 C CG . LEU B 2 89 ? -46.668 29.518 -12.600 1.00 28.30 ? 418 LEU B CG 1 ATOM 3264 C CD1 . LEU B 2 89 ? -46.007 30.578 -13.471 1.00 25.91 ? 418 LEU B CD1 1 ATOM 3265 C CD2 . LEU B 2 89 ? -45.682 28.982 -11.576 1.00 25.80 ? 418 LEU B CD2 1 ATOM 3266 N N . ASP B 2 90 ? -50.238 28.930 -13.699 1.00 23.39 ? 419 ASP B N 1 ATOM 3267 C CA . ASP B 2 90 ? -50.690 28.014 -14.737 1.00 26.42 ? 419 ASP B CA 1 ATOM 3268 C C . ASP B 2 90 ? -51.516 28.701 -15.834 1.00 27.30 ? 419 ASP B C 1 ATOM 3269 O O . ASP B 2 90 ? -51.316 28.409 -17.019 1.00 22.42 ? 419 ASP B O 1 ATOM 3270 C CB . ASP B 2 90 ? -51.449 26.821 -14.142 1.00 28.55 ? 419 ASP B CB 1 ATOM 3271 C CG . ASP B 2 90 ? -50.536 25.844 -13.405 1.00 37.94 ? 419 ASP B CG 1 ATOM 3272 O OD1 . ASP B 2 90 ? -49.301 25.900 -13.600 1.00 43.43 ? 419 ASP B OD1 1 ATOM 3273 O OD2 . ASP B 2 90 ? -51.061 25.009 -12.634 1.00 42.33 ? 419 ASP B OD2 1 ATOM 3274 N N . VAL B 2 91 ? -52.427 29.610 -15.475 1.00 21.37 ? 420 VAL B N 1 ATOM 3275 C CA . VAL B 2 91 ? -53.191 30.280 -16.535 1.00 22.62 ? 420 VAL B CA 1 ATOM 3276 C C . VAL B 2 91 ? -52.318 31.200 -17.386 1.00 23.85 ? 420 VAL B C 1 ATOM 3277 O O . VAL B 2 91 ? -52.470 31.239 -18.605 1.00 28.03 ? 420 VAL B O 1 ATOM 3278 C CB . VAL B 2 91 ? -54.536 30.974 -16.076 1.00 27.68 ? 420 VAL B CB 1 ATOM 3279 C CG1 . VAL B 2 91 ? -54.833 30.710 -14.615 1.00 24.08 ? 420 VAL B CG1 1 ATOM 3280 C CG2 . VAL B 2 91 ? -54.537 32.474 -16.381 1.00 24.43 ? 420 VAL B CG2 1 ATOM 3281 N N . TRP B 2 92 ? -51.383 31.913 -16.768 1.00 21.76 ? 421 TRP B N 1 ATOM 3282 C CA . TRP B 2 92 ? -50.531 32.810 -17.549 1.00 24.35 ? 421 TRP B CA 1 ATOM 3283 C C . TRP B 2 92 ? -49.549 32.078 -18.472 1.00 25.94 ? 421 TRP B C 1 ATOM 3284 O O . TRP B 2 92 ? -49.290 32.527 -19.593 1.00 20.48 ? 421 TRP B O 1 ATOM 3285 C CB . TRP B 2 92 ? -49.811 33.815 -16.652 1.00 21.69 ? 421 TRP B CB 1 ATOM 3286 C CG . TRP B 2 92 ? -50.717 34.922 -16.188 1.00 28.20 ? 421 TRP B CG 1 ATOM 3287 C CD1 . TRP B 2 92 ? -51.124 35.175 -14.906 1.00 26.22 ? 421 TRP B CD1 1 ATOM 3288 C CD2 . TRP B 2 92 ? -51.342 35.916 -17.010 1.00 23.23 ? 421 TRP B CD2 1 ATOM 3289 N NE1 . TRP B 2 92 ? -51.954 36.269 -14.883 1.00 20.73 ? 421 TRP B NE1 1 ATOM 3290 C CE2 . TRP B 2 92 ? -52.106 36.743 -16.159 1.00 23.84 ? 421 TRP B CE2 1 ATOM 3291 C CE3 . TRP B 2 92 ? -51.329 36.188 -18.381 1.00 24.07 ? 421 TRP B CE3 1 ATOM 3292 C CZ2 . TRP B 2 92 ? -52.852 37.827 -16.638 1.00 23.35 ? 421 TRP B CZ2 1 ATOM 3293 C CZ3 . TRP B 2 92 ? -52.064 37.261 -18.855 1.00 24.66 ? 421 TRP B CZ3 1 ATOM 3294 C CH2 . TRP B 2 92 ? -52.815 38.070 -17.985 1.00 26.44 ? 421 TRP B CH2 1 ATOM 3295 N N . THR B 2 93 ? -49.005 30.959 -17.996 1.00 23.53 ? 422 THR B N 1 ATOM 3296 C CA . THR B 2 93 ? -48.153 30.111 -18.830 1.00 22.87 ? 422 THR B CA 1 ATOM 3297 C C . THR B 2 93 ? -48.952 29.605 -20.027 1.00 24.74 ? 422 THR B C 1 ATOM 3298 O O . THR B 2 93 ? -48.479 29.638 -21.169 1.00 23.08 ? 422 THR B O 1 ATOM 3299 C CB . THR B 2 93 ? -47.604 28.912 -18.040 1.00 26.37 ? 422 THR B CB 1 ATOM 3300 O OG1 . THR B 2 93 ? -46.889 29.384 -16.887 1.00 26.65 ? 422 THR B OG1 1 ATOM 3301 C CG2 . THR B 2 93 ? -46.686 28.058 -18.916 1.00 23.14 ? 422 THR B CG2 1 ATOM 3302 N N . TYR B 2 94 ? -50.170 29.143 -19.758 1.00 27.76 ? 423 TYR B N 1 ATOM 3303 C CA . TYR B 2 94 ? -51.074 28.694 -20.810 1.00 25.30 ? 423 TYR B CA 1 ATOM 3304 C C . TYR B 2 94 ? -51.316 29.826 -21.802 1.00 28.71 ? 423 TYR B C 1 ATOM 3305 O O . TYR B 2 94 ? -51.132 29.647 -23.010 1.00 27.41 ? 423 TYR B O 1 ATOM 3306 C CB . TYR B 2 94 ? -52.408 28.210 -20.222 1.00 23.41 ? 423 TYR B CB 1 ATOM 3307 C CG . TYR B 2 94 ? -53.487 28.063 -21.267 1.00 31.13 ? 423 TYR B CG 1 ATOM 3308 C CD1 . TYR B 2 94 ? -53.585 26.910 -22.042 1.00 32.23 ? 423 TYR B CD1 1 ATOM 3309 C CD2 . TYR B 2 94 ? -54.404 29.086 -21.495 1.00 29.13 ? 423 TYR B CD2 1 ATOM 3310 C CE1 . TYR B 2 94 ? -54.569 26.780 -23.015 1.00 29.53 ? 423 TYR B CE1 1 ATOM 3311 C CE2 . TYR B 2 94 ? -55.383 28.966 -22.460 1.00 32.19 ? 423 TYR B CE2 1 ATOM 3312 C CZ . TYR B 2 94 ? -55.462 27.813 -23.216 1.00 35.33 ? 423 TYR B CZ 1 ATOM 3313 O OH . TYR B 2 94 ? -56.444 27.708 -24.173 1.00 38.73 ? 423 TYR B OH 1 ATOM 3314 N N . ASN B 2 95 ? -51.734 30.983 -21.292 1.00 25.35 ? 424 ASN B N 1 ATOM 3315 C CA . ASN B 2 95 ? -52.020 32.130 -22.148 1.00 28.13 ? 424 ASN B CA 1 ATOM 3316 C C . ASN B 2 95 ? -50.849 32.487 -23.058 1.00 28.49 ? 424 ASN B C 1 ATOM 3317 O O . ASN B 2 95 ? -51.023 32.679 -24.261 1.00 27.35 ? 424 ASN B O 1 ATOM 3318 C CB . ASN B 2 95 ? -52.421 33.348 -21.314 1.00 25.92 ? 424 ASN B CB 1 ATOM 3319 C CG . ASN B 2 95 ? -53.823 33.243 -20.755 1.00 26.71 ? 424 ASN B CG 1 ATOM 3320 O OD1 . ASN B 2 95 ? -54.621 32.415 -21.186 1.00 30.96 ? 424 ASN B OD1 1 ATOM 3321 N ND2 . ASN B 2 95 ? -54.135 34.103 -19.793 1.00 35.08 ? 424 ASN B ND2 1 ATOM 3322 N N . ALA B 2 96 ? -49.656 32.563 -22.479 1.00 21.06 ? 425 ALA B N 1 ATOM 3323 C CA . ALA B 2 96 ? -48.462 32.898 -23.246 1.00 24.23 ? 425 ALA B CA 1 ATOM 3324 C C . ALA B 2 96 ? -48.104 31.828 -24.292 1.00 26.78 ? 425 ALA B C 1 ATOM 3325 O O . ALA B 2 96 ? -47.876 32.149 -25.459 1.00 27.04 ? 425 ALA B O 1 ATOM 3326 C CB . ALA B 2 96 ? -47.290 33.147 -22.321 1.00 21.94 ? 425 ALA B CB 1 ATOM 3327 N N . GLU B 2 97 ? -48.044 30.564 -23.881 1.00 28.35 ? 426 GLU B N 1 ATOM 3328 C CA . GLU B 2 97 ? -47.621 29.505 -24.793 1.00 28.46 ? 426 GLU B CA 1 ATOM 3329 C C . GLU B 2 97 ? -48.631 29.302 -25.917 1.00 32.47 ? 426 GLU B C 1 ATOM 3330 O O . GLU B 2 97 ? -48.254 29.095 -27.074 1.00 36.46 ? 426 GLU B O 1 ATOM 3331 C CB . GLU B 2 97 ? -47.342 28.194 -24.035 1.00 31.75 ? 426 GLU B CB 1 ATOM 3332 C CG . GLU B 2 97 ? -46.034 28.211 -23.224 1.00 33.82 ? 426 GLU B CG 1 ATOM 3333 C CD . GLU B 2 97 ? -45.842 26.977 -22.339 1.00 44.13 ? 426 GLU B CD 1 ATOM 3334 O OE1 . GLU B 2 97 ? -46.702 26.065 -22.358 1.00 49.64 ? 426 GLU B OE1 1 ATOM 3335 O OE2 . GLU B 2 97 ? -44.825 26.920 -21.613 1.00 43.10 ? 426 GLU B OE2 1 ATOM 3336 N N . LEU B 2 98 ? -49.912 29.377 -25.583 1.00 27.71 ? 427 LEU B N 1 ATOM 3337 C CA . LEU B 2 98 ? -50.958 29.188 -26.585 1.00 25.65 ? 427 LEU B CA 1 ATOM 3338 C C . LEU B 2 98 ? -50.997 30.358 -27.562 1.00 27.11 ? 427 LEU B C 1 ATOM 3339 O O . LEU B 2 98 ? -51.097 30.153 -28.770 1.00 31.30 ? 427 LEU B O 1 ATOM 3340 C CB . LEU B 2 98 ? -52.319 28.999 -25.911 1.00 33.05 ? 427 LEU B CB 1 ATOM 3341 C CG . LEU B 2 98 ? -53.452 28.311 -26.684 1.00 39.37 ? 427 LEU B CG 1 ATOM 3342 C CD1 . LEU B 2 98 ? -54.222 29.292 -27.560 1.00 36.15 ? 427 LEU B CD1 1 ATOM 3343 C CD2 . LEU B 2 98 ? -52.924 27.158 -27.523 1.00 34.86 ? 427 LEU B CD2 1 ATOM 3344 N N . LEU B 2 99 ? -50.904 31.583 -27.050 1.00 30.89 ? 428 LEU B N 1 ATOM 3345 C CA . LEU B 2 99 ? -50.900 32.767 -27.917 1.00 29.35 ? 428 LEU B CA 1 ATOM 3346 C C . LEU B 2 99 ? -49.775 32.707 -28.952 1.00 34.00 ? 428 LEU B C 1 ATOM 3347 O O . LEU B 2 99 ? -49.983 32.995 -30.140 1.00 28.75 ? 428 LEU B O 1 ATOM 3348 C CB . LEU B 2 99 ? -50.764 34.047 -27.094 1.00 26.36 ? 428 LEU B CB 1 ATOM 3349 C CG . LEU B 2 99 ? -50.802 35.343 -27.904 1.00 30.48 ? 428 LEU B CG 1 ATOM 3350 C CD1 . LEU B 2 99 ? -52.135 35.452 -28.627 1.00 30.94 ? 428 LEU B CD1 1 ATOM 3351 C CD2 . LEU B 2 99 ? -50.578 36.560 -27.017 1.00 29.77 ? 428 LEU B CD2 1 ATOM 3352 N N . VAL B 2 100 ? -48.588 32.317 -28.496 1.00 28.34 ? 429 VAL B N 1 ATOM 3353 C CA . VAL B 2 100 ? -47.418 32.265 -29.363 1.00 30.20 ? 429 VAL B CA 1 ATOM 3354 C C . VAL B 2 100 ? -47.585 31.263 -30.505 1.00 29.03 ? 429 VAL B C 1 ATOM 3355 O O . VAL B 2 100 ? -47.221 31.558 -31.647 1.00 25.91 ? 429 VAL B O 1 ATOM 3356 C CB . VAL B 2 100 ? -46.143 31.989 -28.549 1.00 29.40 ? 429 VAL B CB 1 ATOM 3357 C CG1 . VAL B 2 100 ? -44.991 31.575 -29.451 1.00 28.56 ? 429 VAL B CG1 1 ATOM 3358 C CG2 . VAL B 2 100 ? -45.774 33.221 -27.760 1.00 27.84 ? 429 VAL B CG2 1 ATOM 3359 N N . LEU B 2 101 ? -48.143 30.093 -30.202 1.00 24.73 ? 430 LEU B N 1 ATOM 3360 C CA . LEU B 2 101 ? -48.359 29.074 -31.226 1.00 25.59 ? 430 LEU B CA 1 ATOM 3361 C C . LEU B 2 101 ? -49.392 29.559 -32.234 1.00 25.72 ? 430 LEU B C 1 ATOM 3362 O O . LEU B 2 101 ? -49.215 29.414 -33.447 1.00 23.28 ? 430 LEU B O 1 ATOM 3363 C CB . LEU B 2 101 ? -48.809 27.752 -30.604 1.00 24.07 ? 430 LEU B CB 1 ATOM 3364 C CG . LEU B 2 101 ? -47.796 27.032 -29.710 1.00 30.17 ? 430 LEU B CG 1 ATOM 3365 C CD1 . LEU B 2 101 ? -48.376 25.735 -29.128 1.00 24.39 ? 430 LEU B CD1 1 ATOM 3366 C CD2 . LEU B 2 101 ? -46.512 26.750 -30.480 1.00 22.00 ? 430 LEU B CD2 1 ATOM 3367 N N . LEU B 2 102 ? -50.469 30.145 -31.722 1.00 28.54 ? 431 LEU B N 1 ATOM 3368 C CA . LEU B 2 102 ? -51.539 30.659 -32.567 1.00 28.60 ? 431 LEU B CA 1 ATOM 3369 C C . LEU B 2 102 ? -51.032 31.807 -33.435 1.00 28.69 ? 431 LEU B C 1 ATOM 3370 O O . LEU B 2 102 ? -51.240 31.813 -34.649 1.00 32.22 ? 431 LEU B O 1 ATOM 3371 C CB . LEU B 2 102 ? -52.725 31.106 -31.709 1.00 27.52 ? 431 LEU B CB 1 ATOM 3372 C CG . LEU B 2 102 ? -53.846 31.873 -32.412 1.00 37.07 ? 431 LEU B CG 1 ATOM 3373 C CD1 . LEU B 2 102 ? -54.518 31.005 -33.465 1.00 33.25 ? 431 LEU B CD1 1 ATOM 3374 C CD2 . LEU B 2 102 ? -54.868 32.375 -31.402 1.00 37.58 ? 431 LEU B CD2 1 ATOM 3375 N N . GLU B 2 103 ? -50.343 32.762 -32.820 1.00 30.61 ? 432 GLU B N 1 ATOM 3376 C CA . GLU B 2 103 ? -49.846 33.916 -33.560 1.00 30.51 ? 432 GLU B CA 1 ATOM 3377 C C . GLU B 2 103 ? -48.780 33.577 -34.594 1.00 30.69 ? 432 GLU B C 1 ATOM 3378 O O . GLU B 2 103 ? -48.762 34.167 -35.680 1.00 31.55 ? 432 GLU B O 1 ATOM 3379 C CB . GLU B 2 103 ? -49.359 35.011 -32.614 1.00 27.79 ? 432 GLU B CB 1 ATOM 3380 C CG . GLU B 2 103 ? -50.493 35.732 -31.931 1.00 33.08 ? 432 GLU B CG 1 ATOM 3381 C CD . GLU B 2 103 ? -51.638 36.050 -32.889 1.00 47.29 ? 432 GLU B CD 1 ATOM 3382 O OE1 . GLU B 2 103 ? -51.378 36.608 -33.979 1.00 51.26 ? 432 GLU B OE1 1 ATOM 3383 O OE2 . GLU B 2 103 ? -52.803 35.736 -32.557 1.00 54.87 ? 432 GLU B OE2 1 ATOM 3384 N N . ASN B 2 104 ? -47.899 32.634 -34.274 1.00 22.10 ? 433 ASN B N 1 ATOM 3385 C CA . ASN B 2 104 ? -46.896 32.211 -35.243 1.00 25.54 ? 433 ASN B CA 1 ATOM 3386 C C . ASN B 2 104 ? -47.533 31.617 -36.491 1.00 28.67 ? 433 ASN B C 1 ATOM 3387 O O . ASN B 2 104 ? -47.095 31.886 -37.608 1.00 27.54 ? 433 ASN B O 1 ATOM 3388 C CB . ASN B 2 104 ? -45.901 31.222 -34.630 1.00 21.46 ? 433 ASN B CB 1 ATOM 3389 C CG . ASN B 2 104 ? -44.942 31.886 -33.666 1.00 26.17 ? 433 ASN B CG 1 ATOM 3390 O OD1 . ASN B 2 104 ? -44.837 33.118 -33.621 1.00 25.65 ? 433 ASN B OD1 1 ATOM 3391 N ND2 . ASN B 2 104 ? -44.226 31.070 -32.888 1.00 23.65 ? 433 ASN B ND2 1 ATOM 3392 N N . GLU B 2 105 ? -48.570 30.811 -36.297 1.00 29.22 ? 434 GLU B N 1 ATOM 3393 C CA . GLU B 2 105 ? -49.264 30.195 -37.421 1.00 33.95 ? 434 GLU B CA 1 ATOM 3394 C C . GLU B 2 105 ? -49.894 31.257 -38.327 1.00 35.08 ? 434 GLU B C 1 ATOM 3395 O O . GLU B 2 105 ? -49.841 31.156 -39.559 1.00 31.57 ? 434 GLU B O 1 ATOM 3396 C CB . GLU B 2 105 ? -50.339 29.231 -36.919 1.00 33.61 ? 434 GLU B CB 1 ATOM 3397 C CG . GLU B 2 105 ? -51.195 28.630 -38.021 1.00 40.23 ? 434 GLU B CG 1 ATOM 3398 C CD . GLU B 2 105 ? -52.295 27.736 -37.473 1.00 52.49 ? 434 GLU B CD 1 ATOM 3399 O OE1 . GLU B 2 105 ? -52.117 27.200 -36.357 1.00 53.02 ? 434 GLU B OE1 1 ATOM 3400 O OE2 . GLU B 2 105 ? -53.338 27.575 -38.151 1.00 55.17 ? 434 GLU B OE2 1 ATOM 3401 N N . ARG B 2 106 ? -50.473 32.284 -37.716 1.00 26.42 ? 435 ARG B N 1 ATOM 3402 C CA . ARG B 2 106 ? -51.157 33.322 -38.477 1.00 29.18 ? 435 ARG B CA 1 ATOM 3403 C C . ARG B 2 106 ? -50.177 34.320 -39.087 1.00 27.45 ? 435 ARG B C 1 ATOM 3404 O O . ARG B 2 106 ? -50.439 34.883 -40.149 1.00 26.56 ? 435 ARG B O 1 ATOM 3405 C CB . ARG B 2 106 ? -52.189 34.033 -37.597 1.00 27.49 ? 435 ARG B CB 1 ATOM 3406 C CG . ARG B 2 106 ? -53.128 33.084 -36.867 1.00 35.48 ? 435 ARG B CG 1 ATOM 3407 C CD . ARG B 2 106 ? -54.129 33.843 -36.010 1.00 40.67 ? 435 ARG B CD 1 ATOM 3408 N NE . ARG B 2 106 ? -54.908 34.762 -36.830 1.00 48.70 ? 435 ARG B NE 1 ATOM 3409 C CZ . ARG B 2 106 ? -54.762 36.082 -36.826 1.00 46.86 ? 435 ARG B CZ 1 ATOM 3410 N NH1 . ARG B 2 106 ? -53.877 36.661 -36.020 1.00 38.62 ? 435 ARG B NH1 1 ATOM 3411 N NH2 . ARG B 2 106 ? -55.515 36.820 -37.627 1.00 45.99 ? 435 ARG B NH2 1 ATOM 3412 N N . THR B 2 107 ? -49.049 34.544 -38.418 1.00 27.08 ? 436 THR B N 1 ATOM 3413 C CA . THR B 2 107 ? -48.013 35.409 -38.979 1.00 24.98 ? 436 THR B CA 1 ATOM 3414 C C . THR B 2 107 ? -47.484 34.820 -40.291 1.00 25.01 ? 436 THR B C 1 ATOM 3415 O O . THR B 2 107 ? -47.393 35.522 -41.297 1.00 25.02 ? 436 THR B O 1 ATOM 3416 C CB . THR B 2 107 ? -46.863 35.645 -37.978 1.00 25.14 ? 436 THR B CB 1 ATOM 3417 O OG1 . THR B 2 107 ? -47.338 36.469 -36.906 1.00 26.20 ? 436 THR B OG1 1 ATOM 3418 C CG2 . THR B 2 107 ? -45.673 36.329 -38.648 1.00 21.67 ? 436 THR B CG2 1 ATOM 3419 N N . LEU B 2 108 ? -47.171 33.526 -40.288 1.00 23.78 ? 437 LEU B N 1 ATOM 3420 C CA . LEU B 2 108 ? -46.664 32.867 -41.490 1.00 29.22 ? 437 LEU B CA 1 ATOM 3421 C C . LEU B 2 108 ? -47.691 32.869 -42.629 1.00 29.12 ? 437 LEU B C 1 ATOM 3422 O O . LEU B 2 108 ? -47.318 33.018 -43.799 1.00 26.29 ? 437 LEU B O 1 ATOM 3423 C CB . LEU B 2 108 ? -46.182 31.447 -41.171 1.00 23.88 ? 437 LEU B CB 1 ATOM 3424 C CG . LEU B 2 108 ? -45.099 31.389 -40.090 1.00 28.66 ? 437 LEU B CG 1 ATOM 3425 C CD1 . LEU B 2 108 ? -44.570 29.977 -39.887 1.00 29.76 ? 437 LEU B CD1 1 ATOM 3426 C CD2 . LEU B 2 108 ? -43.956 32.346 -40.406 1.00 24.69 ? 437 LEU B CD2 1 ATOM 3427 N N . ASP B 2 109 ? -48.974 32.721 -42.289 1.00 26.58 ? 438 ASP B N 1 ATOM 3428 C CA . ASP B 2 109 ? -50.042 32.808 -43.287 1.00 28.74 ? 438 ASP B CA 1 ATOM 3429 C C . ASP B 2 109 ? -50.122 34.206 -43.896 1.00 28.47 ? 438 ASP B C 1 ATOM 3430 O O . ASP B 2 109 ? -50.309 34.350 -45.107 1.00 27.32 ? 438 ASP B O 1 ATOM 3431 C CB . ASP B 2 109 ? -51.395 32.421 -42.679 1.00 30.27 ? 438 ASP B CB 1 ATOM 3432 C CG . ASP B 2 109 ? -51.504 30.933 -42.388 1.00 36.82 ? 438 ASP B CG 1 ATOM 3433 O OD1 . ASP B 2 109 ? -50.788 30.146 -43.043 1.00 39.30 ? 438 ASP B OD1 1 ATOM 3434 O OD2 . ASP B 2 109 ? -52.312 30.555 -41.509 1.00 47.58 ? 438 ASP B OD2 1 ATOM 3435 N N . LEU B 2 110 ? -49.978 35.228 -43.055 1.00 21.35 ? 439 LEU B N 1 ATOM 3436 C CA . LEU B 2 110 ? -49.975 36.613 -43.526 1.00 27.82 ? 439 LEU B CA 1 ATOM 3437 C C . LEU B 2 110 ? -48.946 36.827 -44.641 1.00 26.48 ? 439 LEU B C 1 ATOM 3438 O O . LEU B 2 110 ? -49.291 37.316 -45.719 1.00 24.84 ? 439 LEU B O 1 ATOM 3439 C CB . LEU B 2 110 ? -49.724 37.588 -42.368 1.00 27.67 ? 439 LEU B CB 1 ATOM 3440 C CG . LEU B 2 110 ? -49.494 39.061 -42.743 1.00 33.67 ? 439 LEU B CG 1 ATOM 3441 C CD1 . LEU B 2 110 ? -50.772 39.714 -43.244 1.00 36.70 ? 439 LEU B CD1 1 ATOM 3442 C CD2 . LEU B 2 110 ? -48.928 39.842 -41.570 1.00 33.29 ? 439 LEU B CD2 1 ATOM 3443 N N . HIS B 2 111 ? -47.696 36.440 -44.386 1.00 22.64 ? 440 HIS B N 1 ATOM 3444 C CA . HIS B 2 111 ? -46.632 36.540 -45.391 1.00 24.54 ? 440 HIS B CA 1 ATOM 3445 C C . HIS B 2 111 ? -46.991 35.785 -46.663 1.00 25.83 ? 440 HIS B C 1 ATOM 3446 O O . HIS B 2 111 ? -46.839 36.307 -47.769 1.00 26.76 ? 440 HIS B O 1 ATOM 3447 C CB . HIS B 2 111 ? -45.311 35.990 -44.851 1.00 21.73 ? 440 HIS B CB 1 ATOM 3448 C CG . HIS B 2 111 ? -44.722 36.799 -43.742 1.00 23.42 ? 440 HIS B CG 1 ATOM 3449 N ND1 . HIS B 2 111 ? -44.478 38.151 -43.851 1.00 25.70 ? 440 HIS B ND1 1 ATOM 3450 C CD2 . HIS B 2 111 ? -44.303 36.436 -42.505 1.00 25.04 ? 440 HIS B CD2 1 ATOM 3451 C CE1 . HIS B 2 111 ? -43.941 38.587 -42.724 1.00 27.32 ? 440 HIS B CE1 1 ATOM 3452 N NE2 . HIS B 2 111 ? -43.826 37.575 -41.894 1.00 24.81 ? 440 HIS B NE2 1 ATOM 3453 N N . ASP B 2 112 ? -47.440 34.545 -46.492 1.00 25.09 ? 441 ASP B N 1 ATOM 3454 C CA . ASP B 2 112 ? -47.895 33.717 -47.605 1.00 27.90 ? 441 ASP B CA 1 ATOM 3455 C C . ASP B 2 112 ? -48.933 34.479 -48.437 1.00 26.56 ? 441 ASP B C 1 ATOM 3456 O O . ASP B 2 112 ? -48.800 34.585 -49.658 1.00 29.84 ? 441 ASP B O 1 ATOM 3457 C CB . ASP B 2 112 ? -48.472 32.400 -47.065 1.00 26.00 ? 441 ASP B CB 1 ATOM 3458 C CG . ASP B 2 112 ? -48.688 31.353 -48.148 1.00 34.09 ? 441 ASP B CG 1 ATOM 3459 O OD1 . ASP B 2 112 ? -48.163 31.522 -49.278 1.00 31.89 ? 441 ASP B OD1 1 ATOM 3460 O OD2 . ASP B 2 112 ? -49.376 30.344 -47.857 1.00 35.74 ? 441 ASP B OD2 1 ATOM 3461 N N . ALA B 2 113 ? -49.937 35.046 -47.772 1.00 18.71 ? 442 ALA B N 1 ATOM 3462 C CA . ALA B 2 113 ? -50.969 35.816 -48.465 1.00 24.66 ? 442 ALA B CA 1 ATOM 3463 C C . ALA B 2 113 ? -50.387 37.031 -49.187 1.00 23.99 ? 442 ALA B C 1 ATOM 3464 O O . ALA B 2 113 ? -50.746 37.313 -50.337 1.00 23.57 ? 442 ALA B O 1 ATOM 3465 C CB . ALA B 2 113 ? -52.067 36.246 -47.496 1.00 17.65 ? 442 ALA B CB 1 ATOM 3466 N N . ASN B 2 114 ? -49.503 37.756 -48.510 1.00 20.02 ? 443 ASN B N 1 ATOM 3467 C CA . ASN B 2 114 ? -48.878 38.925 -49.118 1.00 26.05 ? 443 ASN B CA 1 ATOM 3468 C C . ASN B 2 114 ? -48.082 38.610 -50.390 1.00 28.47 ? 443 ASN B C 1 ATOM 3469 O O . ASN B 2 114 ? -48.168 39.350 -51.374 1.00 29.16 ? 443 ASN B O 1 ATOM 3470 C CB . ASN B 2 114 ? -48.005 39.659 -48.101 1.00 23.12 ? 443 ASN B CB 1 ATOM 3471 C CG . ASN B 2 114 ? -48.819 40.345 -47.029 1.00 23.54 ? 443 ASN B CG 1 ATOM 3472 O OD1 . ASN B 2 114 ? -49.994 40.661 -47.232 1.00 25.37 ? 443 ASN B OD1 1 ATOM 3473 N ND2 . ASN B 2 114 ? -48.197 40.588 -45.877 1.00 24.12 ? 443 ASN B ND2 1 ATOM 3474 N N . VAL B 2 115 ? -47.313 37.521 -50.370 1.00 24.20 ? 444 VAL B N 1 ATOM 3475 C CA . VAL B 2 115 ? -46.579 37.099 -51.557 1.00 26.14 ? 444 VAL B CA 1 ATOM 3476 C C . VAL B 2 115 ? -47.576 36.741 -52.645 1.00 31.37 ? 444 VAL B C 1 ATOM 3477 O O . VAL B 2 115 ? -47.412 37.119 -53.805 1.00 30.05 ? 444 VAL B O 1 ATOM 3478 C CB . VAL B 2 115 ? -45.650 35.898 -51.278 1.00 27.23 ? 444 VAL B CB 1 ATOM 3479 C CG1 . VAL B 2 115 ? -45.056 35.359 -52.574 1.00 23.10 ? 444 VAL B CG1 1 ATOM 3480 C CG2 . VAL B 2 115 ? -44.544 36.303 -50.330 1.00 21.69 ? 444 VAL B CG2 1 ATOM 3481 N N . LYS B 2 116 ? -48.623 36.025 -52.253 1.00 29.63 ? 445 LYS B N 1 ATOM 3482 C CA . LYS B 2 116 ? -49.678 35.629 -53.178 1.00 29.47 ? 445 LYS B CA 1 ATOM 3483 C C . LYS B 2 116 ? -50.325 36.852 -53.824 1.00 30.16 ? 445 LYS B C 1 ATOM 3484 O O . LYS B 2 116 ? -50.470 36.911 -55.044 1.00 30.78 ? 445 LYS B O 1 ATOM 3485 C CB . LYS B 2 116 ? -50.729 34.792 -52.444 1.00 30.23 ? 445 LYS B CB 1 ATOM 3486 C CG . LYS B 2 116 ? -51.919 34.371 -53.288 1.00 30.14 ? 445 LYS B CG 1 ATOM 3487 C CD . LYS B 2 116 ? -51.515 33.410 -54.408 1.00 43.03 ? 445 LYS B CD 1 ATOM 3488 C CE . LYS B 2 116 ? -52.744 32.880 -55.150 1.00 47.39 ? 445 LYS B CE 1 ATOM 3489 N NZ . LYS B 2 116 ? -53.752 32.313 -54.206 1.00 54.54 ? 445 LYS B NZ 1 ATOM 3490 N N . ASN B 2 117 ? -50.686 37.843 -53.015 1.00 28.29 ? 446 ASN B N 1 ATOM 3491 C CA . ASN B 2 117 ? -51.353 39.024 -53.549 1.00 31.48 ? 446 ASN B CA 1 ATOM 3492 C C . ASN B 2 117 ? -50.448 39.854 -54.460 1.00 34.40 ? 446 ASN B C 1 ATOM 3493 O O . ASN B 2 117 ? -50.914 40.436 -55.447 1.00 35.40 ? 446 ASN B O 1 ATOM 3494 C CB . ASN B 2 117 ? -51.962 39.871 -52.423 1.00 27.77 ? 446 ASN B CB 1 ATOM 3495 C CG . ASN B 2 117 ? -53.044 39.121 -51.655 1.00 34.97 ? 446 ASN B CG 1 ATOM 3496 O OD1 . ASN B 2 117 ? -53.834 38.380 -52.243 1.00 37.05 ? 446 ASN B OD1 1 ATOM 3497 N ND2 . ASN B 2 117 ? -53.072 39.296 -50.337 1.00 29.92 ? 446 ASN B ND2 1 ATOM 3498 N N . LEU B 2 118 ? -49.157 39.891 -54.143 1.00 31.78 ? 447 LEU B N 1 ATOM 3499 C CA . LEU B 2 118 ? -48.194 40.583 -54.995 1.00 32.71 ? 447 LEU B CA 1 ATOM 3500 C C . LEU B 2 118 ? -48.120 39.931 -56.377 1.00 34.66 ? 447 LEU B C 1 ATOM 3501 O O . LEU B 2 118 ? -48.126 40.624 -57.398 1.00 35.04 ? 447 LEU B O 1 ATOM 3502 C CB . LEU B 2 118 ? -46.810 40.618 -54.344 1.00 34.74 ? 447 LEU B CB 1 ATOM 3503 C CG . LEU B 2 118 ? -45.808 41.567 -55.004 1.00 36.38 ? 447 LEU B CG 1 ATOM 3504 C CD1 . LEU B 2 118 ? -46.300 42.992 -54.865 1.00 40.41 ? 447 LEU B CD1 1 ATOM 3505 C CD2 . LEU B 2 118 ? -44.429 41.417 -54.378 1.00 37.37 ? 447 LEU B CD2 1 ATOM 3506 N N . TYR B 2 119 ? -48.066 38.600 -56.404 1.00 26.16 ? 448 TYR B N 1 ATOM 3507 C CA . TYR B 2 119 ? -48.112 37.845 -57.656 1.00 27.51 ? 448 TYR B CA 1 ATOM 3508 C C . TYR B 2 119 ? -49.375 38.140 -58.480 1.00 29.56 ? 448 TYR B C 1 ATOM 3509 O O . TYR B 2 119 ? -49.297 38.338 -59.691 1.00 28.14 ? 448 TYR B O 1 ATOM 3510 C CB . TYR B 2 119 ? -47.988 36.341 -57.374 1.00 24.20 ? 448 TYR B CB 1 ATOM 3511 C CG . TYR B 2 119 ? -48.480 35.455 -58.497 1.00 28.70 ? 448 TYR B CG 1 ATOM 3512 C CD1 . TYR B 2 119 ? -47.653 35.119 -59.560 1.00 28.90 ? 448 TYR B CD1 1 ATOM 3513 C CD2 . TYR B 2 119 ? -49.771 34.944 -58.486 1.00 31.84 ? 448 TYR B CD2 1 ATOM 3514 C CE1 . TYR B 2 119 ? -48.105 34.300 -60.588 1.00 31.36 ? 448 TYR B CE1 1 ATOM 3515 C CE2 . TYR B 2 119 ? -50.230 34.134 -59.504 1.00 33.07 ? 448 TYR B CE2 1 ATOM 3516 C CZ . TYR B 2 119 ? -49.394 33.817 -60.552 1.00 33.54 ? 448 TYR B CZ 1 ATOM 3517 O OH . TYR B 2 119 ? -49.862 33.010 -61.556 1.00 31.64 ? 448 TYR B OH 1 ATOM 3518 N N . GLU B 2 120 ? -50.535 38.150 -57.827 1.00 28.19 ? 449 GLU B N 1 ATOM 3519 C CA . GLU B 2 120 ? -51.790 38.450 -58.508 1.00 32.45 ? 449 GLU B CA 1 ATOM 3520 C C . GLU B 2 120 ? -51.782 39.864 -59.084 1.00 33.19 ? 449 GLU B C 1 ATOM 3521 O O . GLU B 2 120 ? -52.258 40.098 -60.197 1.00 33.68 ? 449 GLU B O 1 ATOM 3522 C CB . GLU B 2 120 ? -52.975 38.292 -57.549 1.00 33.01 ? 449 GLU B CB 1 ATOM 3523 C CG . GLU B 2 120 ? -53.174 36.885 -57.014 1.00 34.43 ? 449 GLU B CG 1 ATOM 3524 C CD . GLU B 2 120 ? -53.632 35.911 -58.081 1.00 50.26 ? 449 GLU B CD 1 ATOM 3525 O OE1 . GLU B 2 120 ? -54.364 36.334 -59.004 1.00 57.31 ? 449 GLU B OE1 1 ATOM 3526 O OE2 . GLU B 2 120 ? -53.266 34.716 -57.997 1.00 55.78 ? 449 GLU B OE2 1 ATOM 3527 N N . LYS B 2 121 ? -51.242 40.794 -58.305 1.00 32.40 ? 450 LYS B N 1 ATOM 3528 C CA . LYS B 2 121 ? -51.134 42.203 -58.676 1.00 36.53 ? 450 LYS B CA 1 ATOM 3529 C C . LYS B 2 121 ? -50.370 42.361 -59.998 1.00 40.21 ? 450 LYS B C 1 ATOM 3530 O O . LYS B 2 121 ? -50.730 43.180 -60.847 1.00 40.85 ? 450 LYS B O 1 ATOM 3531 C CB . LYS B 2 121 ? -50.418 42.956 -57.542 1.00 41.88 ? 450 LYS B CB 1 ATOM 3532 C CG . LYS B 2 121 ? -50.621 44.467 -57.488 1.00 50.27 ? 450 LYS B CG 1 ATOM 3533 C CD . LYS B 2 121 ? -49.989 45.050 -56.207 1.00 56.87 ? 450 LYS B CD 1 ATOM 3534 C CE . LYS B 2 121 ? -49.700 46.549 -56.322 1.00 70.13 ? 450 LYS B CE 1 ATOM 3535 N NZ . LYS B 2 121 ? -48.712 46.889 -57.400 1.00 62.58 ? 450 LYS B NZ 1 ATOM 3536 N N . VAL B 2 122 ? -49.328 41.556 -60.175 1.00 28.04 ? 451 VAL B N 1 ATOM 3537 C CA . VAL B 2 122 ? -48.528 41.591 -61.395 1.00 31.86 ? 451 VAL B CA 1 ATOM 3538 C C . VAL B 2 122 ? -49.235 40.884 -62.555 1.00 33.30 ? 451 VAL B C 1 ATOM 3539 O O . VAL B 2 122 ? -49.280 41.409 -63.672 1.00 33.12 ? 451 VAL B O 1 ATOM 3540 C CB . VAL B 2 122 ? -47.114 41.003 -61.151 1.00 32.09 ? 451 VAL B CB 1 ATOM 3541 C CG1 . VAL B 2 122 ? -46.364 40.820 -62.451 1.00 23.07 ? 451 VAL B CG1 1 ATOM 3542 C CG2 . VAL B 2 122 ? -46.331 41.900 -60.203 1.00 29.73 ? 451 VAL B CG2 1 ATOM 3543 N N . LYS B 2 123 ? -49.794 39.706 -62.284 1.00 34.26 ? 452 LYS B N 1 ATOM 3544 C CA . LYS B 2 123 ? -50.558 38.962 -63.288 1.00 35.24 ? 452 LYS B CA 1 ATOM 3545 C C . LYS B 2 123 ? -51.690 39.807 -63.870 1.00 37.13 ? 452 LYS B C 1 ATOM 3546 O O . LYS B 2 123 ? -51.952 39.768 -65.071 1.00 39.07 ? 452 LYS B O 1 ATOM 3547 C CB . LYS B 2 123 ? -51.133 37.676 -62.688 1.00 29.78 ? 452 LYS B CB 1 ATOM 3548 C CG . LYS B 2 123 ? -51.991 36.874 -63.656 1.00 34.22 ? 452 LYS B CG 1 ATOM 3549 C CD . LYS B 2 123 ? -52.944 35.916 -62.935 1.00 45.86 ? 452 LYS B CD 1 ATOM 3550 C CE . LYS B 2 123 ? -52.492 34.458 -63.044 1.00 53.87 ? 452 LYS B CE 1 ATOM 3551 N NZ . LYS B 2 123 ? -52.319 33.987 -64.461 1.00 55.03 ? 452 LYS B NZ 1 ATOM 3552 N N . SER B 2 124 ? -52.345 40.585 -63.016 1.00 35.04 ? 453 SER B N 1 ATOM 3553 C CA . SER B 2 124 ? -53.493 41.384 -63.428 1.00 35.34 ? 453 SER B CA 1 ATOM 3554 C C . SER B 2 124 ? -53.111 42.505 -64.399 1.00 35.44 ? 453 SER B C 1 ATOM 3555 O O . SER B 2 124 ? -53.910 42.885 -65.260 1.00 34.94 ? 453 SER B O 1 ATOM 3556 C CB . SER B 2 124 ? -54.194 41.956 -62.195 1.00 35.23 ? 453 SER B CB 1 ATOM 3557 O OG . SER B 2 124 ? -55.309 42.737 -62.566 1.00 40.07 ? 453 SER B OG 1 ATOM 3558 N N . GLN B 2 125 ? -51.893 43.028 -64.259 1.00 34.02 ? 454 GLN B N 1 ATOM 3559 C CA . GLN B 2 125 ? -51.399 44.080 -65.149 1.00 37.09 ? 454 GLN B CA 1 ATOM 3560 C C . GLN B 2 125 ? -50.958 43.541 -66.508 1.00 40.53 ? 454 GLN B C 1 ATOM 3561 O O . GLN B 2 125 ? -51.247 44.141 -67.545 1.00 39.60 ? 454 GLN B O 1 ATOM 3562 C CB . GLN B 2 125 ? -50.218 44.823 -64.517 1.00 34.09 ? 454 GLN B CB 1 ATOM 3563 C CG . GLN B 2 125 ? -50.548 45.684 -63.314 1.00 36.42 ? 454 GLN B CG 1 ATOM 3564 C CD . GLN B 2 125 ? -49.371 46.540 -62.891 1.00 40.99 ? 454 GLN B CD 1 ATOM 3565 O OE1 . GLN B 2 125 ? -49.262 47.705 -63.283 1.00 45.05 ? 454 GLN B OE1 1 ATOM 3566 N NE2 . GLN B 2 125 ? -48.475 45.963 -62.097 1.00 35.76 ? 454 GLN B NE2 1 ATOM 3567 N N . LEU B 2 126 ? -50.251 42.415 -66.497 1.00 38.11 ? 455 LEU B N 1 ATOM 3568 C CA . LEU B 2 126 ? -49.625 41.895 -67.713 1.00 43.01 ? 455 LEU B CA 1 ATOM 3569 C C . LEU B 2 126 ? -50.769 41.439 -68.610 1.00 43.53 ? 455 LEU B C 1 ATOM 3570 O O . LEU B 2 126 ? -50.917 41.937 -69.725 1.00 44.91 ? 455 LEU B O 1 ATOM 3571 C CB . LEU B 2 126 ? -48.490 40.926 -67.372 1.00 36.66 ? 455 LEU B CB 1 ATOM 3572 C CG . LEU B 2 126 ? -47.419 41.502 -66.446 1.00 36.24 ? 455 LEU B CG 1 ATOM 3573 C CD1 . LEU B 2 126 ? -46.272 40.522 -66.261 1.00 32.97 ? 455 LEU B CD1 1 ATOM 3574 C CD2 . LEU B 2 126 ? -46.904 42.838 -66.969 1.00 33.46 ? 455 LEU B CD2 1 ATOM 3575 N N . ARG B 2 127 ? -51.595 40.523 -68.100 1.00 48.57 ? 456 ARG B N 1 ATOM 3576 C CA . ARG B 2 127 ? -52.604 39.782 -68.872 1.00 48.70 ? 456 ARG B CA 1 ATOM 3577 C C . ARG B 2 127 ? -51.904 39.149 -70.087 1.00 50.88 ? 456 ARG B C 1 ATOM 3578 O O . ARG B 2 127 ? -50.932 38.402 -69.927 1.00 52.39 ? 456 ARG B O 1 ATOM 3579 C CB . ARG B 2 127 ? -53.785 40.688 -69.281 1.00 50.18 ? 456 ARG B CB 1 ATOM 3580 C CG . ARG B 2 127 ? -53.582 42.192 -69.031 1.00 52.47 ? 456 ARG B CG 1 ATOM 3581 C CD . ARG B 2 127 ? -54.854 42.880 -68.569 1.00 53.98 ? 456 ARG B CD 1 ATOM 3582 N NE . ARG B 2 127 ? -55.962 42.674 -69.499 1.00 65.97 ? 456 ARG B NE 1 ATOM 3583 C CZ . ARG B 2 127 ? -57.210 43.070 -69.272 1.00 61.51 ? 456 ARG B CZ 1 ATOM 3584 N NH1 . ARG B 2 127 ? -57.509 43.702 -68.144 1.00 55.92 ? 456 ARG B NH1 1 ATOM 3585 N NH2 . ARG B 2 127 ? -58.155 42.833 -70.171 1.00 62.38 ? 456 ARG B NH2 1 ATOM 3586 N N . ASP B 2 128 ? -52.405 39.445 -71.286 1.00 54.48 ? 457 ASP B N 1 ATOM 3587 C CA . ASP B 2 128 ? -51.914 38.843 -72.533 1.00 56.46 ? 457 ASP B CA 1 ATOM 3588 C C . ASP B 2 128 ? -50.406 38.981 -72.704 1.00 52.51 ? 457 ASP B C 1 ATOM 3589 O O . ASP B 2 128 ? -49.728 38.041 -73.125 1.00 54.85 ? 457 ASP B O 1 ATOM 3590 C CB . ASP B 2 128 ? -52.537 39.544 -73.745 1.00 57.88 ? 457 ASP B CB 1 ATOM 3591 C CG . ASP B 2 128 ? -53.962 39.143 -73.996 1.00 65.91 ? 457 ASP B CG 1 ATOM 3592 O OD1 . ASP B 2 128 ? -54.182 38.008 -74.473 1.00 66.62 ? 457 ASP B OD1 1 ATOM 3593 O OD2 . ASP B 2 128 ? -54.859 39.977 -73.744 1.00 76.56 ? 457 ASP B OD2 1 ATOM 3594 N N . ASN B 2 129 ? -49.903 40.176 -72.405 1.00 39.80 ? 458 ASN B N 1 ATOM 3595 C CA . ASN B 2 129 ? -48.547 40.577 -72.765 1.00 40.87 ? 458 ASN B CA 1 ATOM 3596 C C . ASN B 2 129 ? -47.401 39.727 -72.204 1.00 37.10 ? 458 ASN B C 1 ATOM 3597 O O . ASN B 2 129 ? -46.254 39.878 -72.625 1.00 39.88 ? 458 ASN B O 1 ATOM 3598 C CB . ASN B 2 129 ? -48.332 42.064 -72.451 1.00 37.63 ? 458 ASN B CB 1 ATOM 3599 C CG . ASN B 2 129 ? -49.152 42.978 -73.355 1.00 42.24 ? 458 ASN B CG 1 ATOM 3600 O OD1 . ASN B 2 129 ? -49.776 42.523 -74.314 1.00 41.46 ? 458 ASN B OD1 1 ATOM 3601 N ND2 . ASN B 2 129 ? -49.141 44.276 -73.058 1.00 41.48 ? 458 ASN B ND2 1 ATOM 3602 N N . ALA B 2 130 ? -47.707 38.830 -71.272 1.00 37.00 ? 459 ALA B N 1 ATOM 3603 C CA . ALA B 2 130 ? -46.684 37.960 -70.699 1.00 39.35 ? 459 ALA B CA 1 ATOM 3604 C C . ALA B 2 130 ? -47.203 36.543 -70.497 1.00 39.31 ? 459 ALA B C 1 ATOM 3605 O O . ALA B 2 130 ? -48.411 36.331 -70.363 1.00 41.54 ? 459 ALA B O 1 ATOM 3606 C CB . ALA B 2 130 ? -46.158 38.529 -69.381 1.00 35.20 ? 459 ALA B CB 1 ATOM 3607 N N . ASN B 2 131 ? -46.282 35.583 -70.473 1.00 36.61 ? 460 ASN B N 1 ATOM 3608 C CA . ASN B 2 131 ? -46.609 34.186 -70.220 1.00 37.58 ? 460 ASN B CA 1 ATOM 3609 C C . ASN B 2 131 ? -46.283 33.786 -68.775 1.00 39.10 ? 460 ASN B C 1 ATOM 3610 O O . ASN B 2 131 ? -45.149 33.952 -68.326 1.00 39.21 ? 460 ASN B O 1 ATOM 3611 C CB . ASN B 2 131 ? -45.820 33.300 -71.180 1.00 37.56 ? 460 ASN B CB 1 ATOM 3612 C CG . ASN B 2 131 ? -46.166 31.831 -71.040 1.00 47.90 ? 460 ASN B CG 1 ATOM 3613 O OD1 . ASN B 2 131 ? -47.304 31.477 -70.721 1.00 51.43 ? 460 ASN B OD1 1 ATOM 3614 N ND2 . ASN B 2 131 ? -45.186 30.965 -71.281 1.00 44.31 ? 460 ASN B ND2 1 ATOM 3615 N N . ASP B 2 132 ? -47.272 33.257 -68.057 1.00 43.12 ? 461 ASP B N 1 ATOM 3616 C CA . ASP B 2 132 ? -47.097 32.813 -66.673 1.00 38.50 ? 461 ASP B CA 1 ATOM 3617 C C . ASP B 2 132 ? -46.512 31.401 -66.657 1.00 39.54 ? 461 ASP B C 1 ATOM 3618 O O . ASP B 2 132 ? -47.137 30.462 -67.153 1.00 41.45 ? 461 ASP B O 1 ATOM 3619 C CB . ASP B 2 132 ? -48.455 32.816 -65.969 1.00 38.35 ? 461 ASP B CB 1 ATOM 3620 C CG . ASP B 2 132 ? -48.353 32.604 -64.466 1.00 41.60 ? 461 ASP B CG 1 ATOM 3621 O OD1 . ASP B 2 132 ? -47.303 32.131 -63.968 1.00 39.57 ? 461 ASP B OD1 1 ATOM 3622 O OD2 . ASP B 2 132 ? -49.351 32.904 -63.777 1.00 39.01 ? 461 ASP B OD2 1 ATOM 3623 N N . LEU B 2 133 ? -45.320 31.248 -66.088 1.00 40.27 ? 462 LEU B N 1 ATOM 3624 C CA . LEU B 2 133 ? -44.647 29.949 -66.070 1.00 41.85 ? 462 LEU B CA 1 ATOM 3625 C C . LEU B 2 133 ? -45.083 29.040 -64.911 1.00 45.66 ? 462 LEU B C 1 ATOM 3626 O O . LEU B 2 133 ? -44.629 27.898 -64.814 1.00 46.83 ? 462 LEU B O 1 ATOM 3627 C CB . LEU B 2 133 ? -43.129 30.135 -66.059 1.00 44.01 ? 462 LEU B CB 1 ATOM 3628 C CG . LEU B 2 133 ? -42.577 30.994 -67.199 1.00 51.25 ? 462 LEU B CG 1 ATOM 3629 C CD1 . LEU B 2 133 ? -41.070 31.190 -67.079 1.00 49.10 ? 462 LEU B CD1 1 ATOM 3630 C CD2 . LEU B 2 133 ? -42.929 30.379 -68.548 1.00 46.34 ? 462 LEU B CD2 1 ATOM 3631 N N . GLY B 2 134 ? -45.958 29.539 -64.040 1.00 41.87 ? 463 GLY B N 1 ATOM 3632 C CA . GLY B 2 134 ? -46.465 28.744 -62.932 1.00 43.10 ? 463 GLY B CA 1 ATOM 3633 C C . GLY B 2 134 ? -45.533 28.670 -61.734 1.00 44.36 ? 463 GLY B C 1 ATOM 3634 O O . GLY B 2 134 ? -45.701 27.815 -60.857 1.00 44.48 ? 463 GLY B O 1 ATOM 3635 N N . ASN B 2 135 ? -44.554 29.569 -61.688 1.00 40.69 ? 464 ASN B N 1 ATOM 3636 C CA . ASN B 2 135 ? -43.593 29.592 -60.590 1.00 38.96 ? 464 ASN B CA 1 ATOM 3637 C C . ASN B 2 135 ? -43.299 31.011 -60.111 1.00 35.80 ? 464 ASN B C 1 ATOM 3638 O O . ASN B 2 135 ? -42.248 31.269 -59.519 1.00 30.44 ? 464 ASN B O 1 ATOM 3639 C CB . ASN B 2 135 ? -42.294 28.908 -61.013 1.00 36.14 ? 464 ASN B CB 1 ATOM 3640 C CG . ASN B 2 135 ? -41.603 29.629 -62.165 1.00 45.44 ? 464 ASN B CG 1 ATOM 3641 O OD1 . ASN B 2 135 ? -42.208 30.463 -62.851 1.00 43.89 ? 464 ASN B OD1 1 ATOM 3642 N ND2 . ASN B 2 135 ? -40.330 29.304 -62.385 1.00 37.46 ? 464 ASN B ND2 1 ATOM 3643 N N . GLY B 2 136 ? -44.223 31.928 -60.380 1.00 33.38 ? 465 GLY B N 1 ATOM 3644 C CA . GLY B 2 136 ? -44.044 33.315 -59.999 1.00 32.92 ? 465 GLY B CA 1 ATOM 3645 C C . GLY B 2 136 ? -43.293 34.113 -61.050 1.00 36.03 ? 465 GLY B C 1 ATOM 3646 O O . GLY B 2 136 ? -43.034 35.303 -60.859 1.00 36.61 ? 465 GLY B O 1 ATOM 3647 N N . CYS B 2 137 ? -42.940 33.471 -62.161 1.00 37.23 ? 466 CYS B N 1 ATOM 3648 C CA . CYS B 2 137 ? -42.199 34.167 -63.211 1.00 36.45 ? 466 CYS B CA 1 ATOM 3649 C C . CYS B 2 137 ? -43.056 34.442 -64.442 1.00 39.85 ? 466 CYS B C 1 ATOM 3650 O O . CYS B 2 137 ? -43.856 33.600 -64.863 1.00 40.81 ? 466 CYS B O 1 ATOM 3651 C CB . CYS B 2 137 ? -40.936 33.390 -63.597 1.00 38.91 ? 466 CYS B CB 1 ATOM 3652 S SG . CYS B 2 137 ? -39.619 33.477 -62.349 1.00 52.39 ? 466 CYS B SG 1 ATOM 3653 N N . PHE B 2 138 ? -42.893 35.632 -65.009 1.00 31.57 ? 467 PHE B N 1 ATOM 3654 C CA . PHE B 2 138 ? -43.619 36.010 -66.211 1.00 33.79 ? 467 PHE B CA 1 ATOM 3655 C C . PHE B 2 138 ? -42.648 36.306 -67.353 1.00 34.76 ? 467 PHE B C 1 ATOM 3656 O O . PHE B 2 138 ? -41.774 37.163 -67.218 1.00 34.90 ? 467 PHE B O 1 ATOM 3657 C CB . PHE B 2 138 ? -44.483 37.244 -65.936 1.00 32.41 ? 467 PHE B CB 1 ATOM 3658 C CG . PHE B 2 138 ? -45.569 37.012 -64.925 1.00 32.75 ? 467 PHE B CG 1 ATOM 3659 C CD1 . PHE B 2 138 ? -45.367 37.309 -63.578 1.00 36.29 ? 467 PHE B CD1 1 ATOM 3660 C CD2 . PHE B 2 138 ? -46.797 36.491 -65.319 1.00 35.70 ? 467 PHE B CD2 1 ATOM 3661 C CE1 . PHE B 2 138 ? -46.375 37.090 -62.638 1.00 31.00 ? 467 PHE B CE1 1 ATOM 3662 C CE2 . PHE B 2 138 ? -47.811 36.268 -64.389 1.00 40.16 ? 467 PHE B CE2 1 ATOM 3663 C CZ . PHE B 2 138 ? -47.598 36.569 -63.045 1.00 34.50 ? 467 PHE B CZ 1 ATOM 3664 N N . GLU B 2 139 ? -42.792 35.600 -68.472 1.00 44.00 ? 468 GLU B N 1 ATOM 3665 C CA . GLU B 2 139 ? -41.984 35.895 -69.653 1.00 43.88 ? 468 GLU B CA 1 ATOM 3666 C C . GLU B 2 139 ? -42.731 36.841 -70.578 1.00 41.62 ? 468 GLU B C 1 ATOM 3667 O O . GLU B 2 139 ? -43.826 36.524 -71.045 1.00 48.93 ? 468 GLU B O 1 ATOM 3668 C CB . GLU B 2 139 ? -41.596 34.615 -70.400 1.00 42.70 ? 468 GLU B CB 1 ATOM 3669 C CG . GLU B 2 139 ? -40.470 33.832 -69.738 1.00 54.45 ? 468 GLU B CG 1 ATOM 3670 C CD . GLU B 2 139 ? -40.053 32.601 -70.531 1.00 72.10 ? 468 GLU B CD 1 ATOM 3671 O OE1 . GLU B 2 139 ? -40.695 32.302 -71.568 1.00 70.23 ? 468 GLU B OE1 1 ATOM 3672 O OE2 . GLU B 2 139 ? -39.080 31.934 -70.114 1.00 73.05 ? 468 GLU B OE2 1 ATOM 3673 N N . PHE B 2 140 ? -42.140 38.002 -70.840 1.00 31.38 ? 469 PHE B N 1 ATOM 3674 C CA . PHE B 2 140 ? -42.777 39.008 -71.681 1.00 37.63 ? 469 PHE B CA 1 ATOM 3675 C C . PHE B 2 140 ? -42.825 38.626 -73.167 1.00 42.84 ? 469 PHE B C 1 ATOM 3676 O O . PHE B 2 140 ? -41.852 38.096 -73.715 1.00 39.30 ? 469 PHE B O 1 ATOM 3677 C CB . PHE B 2 140 ? -42.054 40.341 -71.523 1.00 38.77 ? 469 PHE B CB 1 ATOM 3678 C CG . PHE B 2 140 ? -42.277 40.998 -70.195 1.00 34.29 ? 469 PHE B CG 1 ATOM 3679 C CD1 . PHE B 2 140 ? -43.324 41.891 -70.022 1.00 35.45 ? 469 PHE B CD1 1 ATOM 3680 C CD2 . PHE B 2 140 ? -41.436 40.740 -69.123 1.00 29.40 ? 469 PHE B CD2 1 ATOM 3681 C CE1 . PHE B 2 140 ? -43.537 42.508 -68.796 1.00 35.74 ? 469 PHE B CE1 1 ATOM 3682 C CE2 . PHE B 2 140 ? -41.642 41.350 -67.898 1.00 29.90 ? 469 PHE B CE2 1 ATOM 3683 C CZ . PHE B 2 140 ? -42.693 42.234 -67.732 1.00 30.28 ? 469 PHE B CZ 1 ATOM 3684 N N . TRP B 2 141 ? -43.954 38.908 -73.816 1.00 38.61 ? 470 TRP B N 1 ATOM 3685 C CA . TRP B 2 141 ? -44.067 38.737 -75.262 1.00 45.50 ? 470 TRP B CA 1 ATOM 3686 C C . TRP B 2 141 ? -43.555 39.985 -75.970 1.00 49.38 ? 470 TRP B C 1 ATOM 3687 O O . TRP B 2 141 ? -43.761 40.162 -77.173 1.00 53.98 ? 470 TRP B O 1 ATOM 3688 C CB . TRP B 2 141 ? -45.518 38.459 -75.676 1.00 46.42 ? 470 TRP B CB 1 ATOM 3689 C CG . TRP B 2 141 ? -46.016 37.124 -75.230 1.00 46.21 ? 470 TRP B CG 1 ATOM 3690 C CD1 . TRP B 2 141 ? -47.055 36.871 -74.380 1.00 42.70 ? 470 TRP B CD1 1 ATOM 3691 C CD2 . TRP B 2 141 ? -45.479 35.850 -75.600 1.00 49.13 ? 470 TRP B CD2 1 ATOM 3692 N NE1 . TRP B 2 141 ? -47.199 35.514 -74.203 1.00 41.16 ? 470 TRP B NE1 1 ATOM 3693 C CE2 . TRP B 2 141 ? -46.243 34.866 -74.938 1.00 42.56 ? 470 TRP B CE2 1 ATOM 3694 C CE3 . TRP B 2 141 ? -44.428 35.446 -76.428 1.00 49.93 ? 470 TRP B CE3 1 ATOM 3695 C CZ2 . TRP B 2 141 ? -45.986 33.500 -75.082 1.00 43.39 ? 470 TRP B CZ2 1 ATOM 3696 C CZ3 . TRP B 2 141 ? -44.172 34.095 -76.569 1.00 53.05 ? 470 TRP B CZ3 1 ATOM 3697 C CH2 . TRP B 2 141 ? -44.948 33.136 -75.898 1.00 48.56 ? 470 TRP B CH2 1 ATOM 3698 N N . HIS B 2 142 ? -42.899 40.858 -75.214 1.00 44.98 ? 471 HIS B N 1 ATOM 3699 C CA . HIS B 2 142 ? -42.342 42.079 -75.776 1.00 44.67 ? 471 HIS B CA 1 ATOM 3700 C C . HIS B 2 142 ? -41.086 42.499 -75.030 1.00 47.70 ? 471 HIS B C 1 ATOM 3701 O O . HIS B 2 142 ? -40.703 41.876 -74.037 1.00 47.12 ? 471 HIS B O 1 ATOM 3702 C CB . HIS B 2 142 ? -43.376 43.201 -75.738 1.00 43.63 ? 471 HIS B CB 1 ATOM 3703 C CG . HIS B 2 142 ? -43.740 43.641 -74.358 1.00 43.37 ? 471 HIS B CG 1 ATOM 3704 N ND1 . HIS B 2 142 ? -43.000 44.560 -73.647 1.00 44.29 ? 471 HIS B ND1 1 ATOM 3705 C CD2 . HIS B 2 142 ? -44.772 43.285 -73.552 1.00 43.67 ? 471 HIS B CD2 1 ATOM 3706 C CE1 . HIS B 2 142 ? -43.559 44.754 -72.465 1.00 41.15 ? 471 HIS B CE1 1 ATOM 3707 N NE2 . HIS B 2 142 ? -44.632 43.994 -72.381 1.00 40.50 ? 471 HIS B NE2 1 ATOM 3708 N N . LYS B 2 143 ? -40.437 43.553 -75.513 1.00 51.77 ? 472 LYS B N 1 ATOM 3709 C CA . LYS B 2 143 ? -39.249 44.062 -74.844 1.00 49.24 ? 472 LYS B CA 1 ATOM 3710 C C . LYS B 2 143 ? -39.623 44.956 -73.669 1.00 49.32 ? 472 LYS B C 1 ATOM 3711 O O . LYS B 2 143 ? -40.362 45.938 -73.824 1.00 46.47 ? 472 LYS B O 1 ATOM 3712 C CB . LYS B 2 143 ? -38.348 44.811 -75.829 1.00 52.92 ? 472 LYS B CB 1 ATOM 3713 C CG . LYS B 2 143 ? -37.462 43.890 -76.661 1.00 51.91 ? 472 LYS B CG 1 ATOM 3714 C CD . LYS B 2 143 ? -36.305 43.348 -75.826 1.00 66.85 ? 472 LYS B CD 1 ATOM 3715 C CE . LYS B 2 143 ? -36.070 41.863 -76.083 1.00 73.84 ? 472 LYS B CE 1 ATOM 3716 N NZ . LYS B 2 143 ? -35.892 41.538 -77.530 1.00 79.22 ? 472 LYS B NZ 1 ATOM 3717 N N . CYS B 2 144 ? -39.117 44.605 -72.491 1.00 46.24 ? 473 CYS B N 1 ATOM 3718 C CA . CYS B 2 144 ? -39.382 45.390 -71.299 1.00 42.72 ? 473 CYS B CA 1 ATOM 3719 C C . CYS B 2 144 ? -38.077 45.934 -70.740 1.00 43.66 ? 473 CYS B C 1 ATOM 3720 O O . CYS B 2 144 ? -37.354 45.225 -70.026 1.00 45.40 ? 473 CYS B O 1 ATOM 3721 C CB . CYS B 2 144 ? -40.107 44.545 -70.244 1.00 40.56 ? 473 CYS B CB 1 ATOM 3722 S SG . CYS B 2 144 ? -40.987 45.517 -68.997 1.00 52.64 ? 473 CYS B SG 1 ATOM 3723 N N . ASP B 2 145 ? -37.770 47.189 -71.066 1.00 42.13 ? 474 ASP B N 1 ATOM 3724 C CA . ASP B 2 145 ? -36.569 47.840 -70.535 1.00 44.41 ? 474 ASP B CA 1 ATOM 3725 C C . ASP B 2 145 ? -36.737 48.208 -69.051 1.00 42.11 ? 474 ASP B C 1 ATOM 3726 O O . ASP B 2 145 ? -37.716 47.806 -68.420 1.00 43.04 ? 474 ASP B O 1 ATOM 3727 C CB . ASP B 2 145 ? -36.174 49.060 -71.382 1.00 42.69 ? 474 ASP B CB 1 ATOM 3728 C CG . ASP B 2 145 ? -37.272 50.120 -71.459 1.00 49.39 ? 474 ASP B CG 1 ATOM 3729 O OD1 . ASP B 2 145 ? -38.163 50.153 -70.581 1.00 50.09 ? 474 ASP B OD1 1 ATOM 3730 O OD2 . ASP B 2 145 ? -37.226 50.950 -72.397 1.00 49.26 ? 474 ASP B OD2 1 ATOM 3731 N N . ASN B 2 146 ? -35.793 48.969 -68.504 1.00 38.26 ? 475 ASN B N 1 ATOM 3732 C CA . ASN B 2 146 ? -35.806 49.308 -67.083 1.00 35.79 ? 475 ASN B CA 1 ATOM 3733 C C . ASN B 2 146 ? -37.032 50.102 -66.622 1.00 39.91 ? 475 ASN B C 1 ATOM 3734 O O . ASN B 2 146 ? -37.491 49.936 -65.488 1.00 39.50 ? 475 ASN B O 1 ATOM 3735 C CB . ASN B 2 146 ? -34.530 50.066 -66.702 1.00 33.11 ? 475 ASN B CB 1 ATOM 3736 C CG . ASN B 2 146 ? -33.302 49.187 -66.718 1.00 33.52 ? 475 ASN B CG 1 ATOM 3737 O OD1 . ASN B 2 146 ? -33.380 47.988 -67.006 1.00 29.94 ? 475 ASN B OD1 1 ATOM 3738 N ND2 . ASN B 2 146 ? -32.149 49.784 -66.416 1.00 34.34 ? 475 ASN B ND2 1 ATOM 3739 N N . GLU B 2 147 ? -37.544 50.975 -67.485 1.00 42.76 ? 476 GLU B N 1 ATOM 3740 C CA . GLU B 2 147 ? -38.712 51.784 -67.137 1.00 44.66 ? 476 GLU B CA 1 ATOM 3741 C C . GLU B 2 147 ? -39.999 50.968 -67.232 1.00 43.92 ? 476 GLU B C 1 ATOM 3742 O O . GLU B 2 147 ? -40.938 51.174 -66.459 1.00 41.37 ? 476 GLU B O 1 ATOM 3743 C CB . GLU B 2 147 ? -38.794 53.054 -67.998 1.00 42.64 ? 476 GLU B CB 1 ATOM 3744 C CG . GLU B 2 147 ? -37.843 54.168 -67.558 1.00 47.48 ? 476 GLU B CG 1 ATOM 3745 C CD . GLU B 2 147 ? -37.916 55.408 -68.447 1.00 66.35 ? 476 GLU B CD 1 ATOM 3746 O OE1 . GLU B 2 147 ? -38.587 55.359 -69.508 1.00 64.32 ? 476 GLU B OE1 1 ATOM 3747 O OE2 . GLU B 2 147 ? -37.295 56.432 -68.077 1.00 61.51 ? 476 GLU B OE2 1 ATOM 3748 N N . CYS B 2 148 ? -40.036 50.042 -68.183 1.00 39.38 ? 477 CYS B N 1 ATOM 3749 C CA . CYS B 2 148 ? -41.140 49.097 -68.283 1.00 40.55 ? 477 CYS B CA 1 ATOM 3750 C C . CYS B 2 148 ? -41.169 48.202 -67.043 1.00 43.04 ? 477 CYS B C 1 ATOM 3751 O O . CYS B 2 148 ? -42.232 47.982 -66.458 1.00 41.83 ? 477 CYS B O 1 ATOM 3752 C CB . CYS B 2 148 ? -41.012 48.261 -69.556 1.00 40.33 ? 477 CYS B CB 1 ATOM 3753 S SG . CYS B 2 148 ? -42.243 46.955 -69.743 1.00 51.23 ? 477 CYS B SG 1 ATOM 3754 N N . MET B 2 149 ? -40.000 47.702 -66.638 1.00 43.97 ? 478 MET B N 1 ATOM 3755 C CA . MET B 2 149 ? -39.878 46.927 -65.401 1.00 43.91 ? 478 MET B CA 1 ATOM 3756 C C . MET B 2 149 ? -40.397 47.723 -64.208 1.00 44.92 ? 478 MET B C 1 ATOM 3757 O O . MET B 2 149 ? -41.196 47.222 -63.413 1.00 42.45 ? 478 MET B O 1 ATOM 3758 C CB . MET B 2 149 ? -38.425 46.501 -65.145 1.00 38.02 ? 478 MET B CB 1 ATOM 3759 C CG . MET B 2 149 ? -37.898 45.413 -66.081 1.00 42.83 ? 478 MET B CG 1 ATOM 3760 S SD . MET B 2 149 ? -38.890 43.904 -66.047 1.00 43.28 ? 478 MET B SD 1 ATOM 3761 C CE . MET B 2 149 ? -37.914 42.831 -67.107 1.00 35.33 ? 478 MET B CE 1 ATOM 3762 N N . GLU B 2 150 ? -39.960 48.972 -64.099 1.00 39.96 ? 479 GLU B N 1 ATOM 3763 C CA . GLU B 2 150 ? -40.338 49.813 -62.968 1.00 41.31 ? 479 GLU B CA 1 ATOM 3764 C C . GLU B 2 150 ? -41.836 50.126 -62.971 1.00 43.54 ? 479 GLU B C 1 ATOM 3765 O O . GLU B 2 150 ? -42.447 50.285 -61.912 1.00 43.85 ? 479 GLU B O 1 ATOM 3766 C CB . GLU B 2 150 ? -39.508 51.097 -62.967 1.00 39.83 ? 479 GLU B CB 1 ATOM 3767 C CG . GLU B 2 150 ? -39.525 51.864 -61.658 1.00 48.81 ? 479 GLU B CG 1 ATOM 3768 C CD . GLU B 2 150 ? -39.084 51.021 -60.466 1.00 59.24 ? 479 GLU B CD 1 ATOM 3769 O OE1 . GLU B 2 150 ? -39.722 51.146 -59.395 1.00 57.83 ? 479 GLU B OE1 1 ATOM 3770 O OE2 . GLU B 2 150 ? -38.104 50.247 -60.590 1.00 51.94 ? 479 GLU B OE2 1 ATOM 3771 N N . SER B 2 151 ? -42.431 50.194 -64.160 1.00 40.25 ? 480 SER B N 1 ATOM 3772 C CA . SER B 2 151 ? -43.863 50.459 -64.265 1.00 39.25 ? 480 SER B CA 1 ATOM 3773 C C . SER B 2 151 ? -44.676 49.280 -63.724 1.00 38.82 ? 480 SER B C 1 ATOM 3774 O O . SER B 2 151 ? -45.690 49.483 -63.052 1.00 40.39 ? 480 SER B O 1 ATOM 3775 C CB . SER B 2 151 ? -44.266 50.793 -65.706 1.00 36.42 ? 480 SER B CB 1 ATOM 3776 O OG . SER B 2 151 ? -44.125 49.675 -66.559 1.00 34.71 ? 480 SER B OG 1 ATOM 3777 N N . VAL B 2 152 ? -44.231 48.057 -64.011 1.00 33.61 ? 481 VAL B N 1 ATOM 3778 C CA . VAL B 2 152 ? -44.863 46.863 -63.448 1.00 36.68 ? 481 VAL B CA 1 ATOM 3779 C C . VAL B 2 152 ? -44.789 46.871 -61.913 1.00 41.73 ? 481 VAL B C 1 ATOM 3780 O O . VAL B 2 152 ? -45.742 46.487 -61.230 1.00 40.16 ? 481 VAL B O 1 ATOM 3781 C CB . VAL B 2 152 ? -44.208 45.573 -63.968 1.00 33.30 ? 481 VAL B CB 1 ATOM 3782 C CG1 . VAL B 2 152 ? -44.889 44.350 -63.368 1.00 30.95 ? 481 VAL B CG1 1 ATOM 3783 C CG2 . VAL B 2 152 ? -44.260 45.518 -65.484 1.00 35.63 ? 481 VAL B CG2 1 ATOM 3784 N N . LYS B 2 153 ? -43.658 47.323 -61.379 1.00 36.33 ? 482 LYS B N 1 ATOM 3785 C CA . LYS B 2 153 ? -43.437 47.329 -59.938 1.00 39.90 ? 482 LYS B CA 1 ATOM 3786 C C . LYS B 2 153 ? -44.203 48.415 -59.177 1.00 41.95 ? 482 LYS B C 1 ATOM 3787 O O . LYS B 2 153 ? -44.527 48.225 -58.003 1.00 44.15 ? 482 LYS B O 1 ATOM 3788 C CB . LYS B 2 153 ? -41.942 47.423 -59.624 1.00 38.94 ? 482 LYS B CB 1 ATOM 3789 C CG . LYS B 2 153 ? -41.114 46.244 -60.116 1.00 37.24 ? 482 LYS B CG 1 ATOM 3790 C CD . LYS B 2 153 ? -39.676 46.382 -59.640 1.00 37.11 ? 482 LYS B CD 1 ATOM 3791 C CE . LYS B 2 153 ? -38.692 46.069 -60.759 1.00 45.80 ? 482 LYS B CE 1 ATOM 3792 N NZ . LYS B 2 153 ? -37.287 46.429 -60.385 1.00 49.73 ? 482 LYS B NZ 1 ATOM 3793 N N . ASN B 2 154 ? -44.478 49.551 -59.821 1.00 44.80 ? 483 ASN B N 1 ATOM 3794 C CA . ASN B 2 154 ? -45.276 50.595 -59.168 1.00 45.43 ? 483 ASN B CA 1 ATOM 3795 C C . ASN B 2 154 ? -46.733 50.617 -59.631 1.00 42.74 ? 483 ASN B C 1 ATOM 3796 O O . ASN B 2 154 ? -47.482 51.546 -59.322 1.00 46.49 ? 483 ASN B O 1 ATOM 3797 C CB . ASN B 2 154 ? -44.621 51.992 -59.244 1.00 47.71 ? 483 ASN B CB 1 ATOM 3798 C CG . ASN B 2 154 ? -44.444 52.513 -60.677 1.00 53.52 ? 483 ASN B CG 1 ATOM 3799 O OD1 . ASN B 2 154 ? -45.159 52.116 -61.608 1.00 49.06 ? 483 ASN B OD1 1 ATOM 3800 N ND2 . ASN B 2 154 ? -43.485 53.438 -60.844 1.00 55.10 ? 483 ASN B ND2 1 ATOM 3801 N N . GLY B 2 155 ? -47.124 49.578 -60.363 1.00 35.25 ? 484 GLY B N 1 ATOM 3802 C CA . GLY B 2 155 ? -48.506 49.398 -60.769 1.00 38.49 ? 484 GLY B CA 1 ATOM 3803 C C . GLY B 2 155 ? -49.013 50.402 -61.786 1.00 42.91 ? 484 GLY B C 1 ATOM 3804 O O . GLY B 2 155 ? -50.180 50.794 -61.740 1.00 47.40 ? 484 GLY B O 1 ATOM 3805 N N . THR B 2 156 ? -48.145 50.810 -62.709 1.00 41.05 ? 485 THR B N 1 ATOM 3806 C CA . THR B 2 156 ? -48.534 51.723 -63.778 1.00 40.11 ? 485 THR B CA 1 ATOM 3807 C C . THR B 2 156 ? -48.219 51.133 -65.147 1.00 41.62 ? 485 THR B C 1 ATOM 3808 O O . THR B 2 156 ? -48.091 51.869 -66.125 1.00 45.90 ? 485 THR B O 1 ATOM 3809 C CB . THR B 2 156 ? -47.831 53.088 -63.649 1.00 45.67 ? 485 THR B CB 1 ATOM 3810 O OG1 . THR B 2 156 ? -46.412 52.909 -63.749 1.00 46.99 ? 485 THR B OG1 1 ATOM 3811 C CG2 . THR B 2 156 ? -48.166 53.746 -62.315 1.00 42.81 ? 485 THR B CG2 1 ATOM 3812 N N . TYR B 2 157 ? -48.085 49.811 -65.211 1.00 39.89 ? 486 TYR B N 1 ATOM 3813 C CA . TYR B 2 157 ? -47.783 49.128 -66.470 1.00 40.03 ? 486 TYR B CA 1 ATOM 3814 C C . TYR B 2 157 ? -48.803 49.459 -67.562 1.00 45.90 ? 486 TYR B C 1 ATOM 3815 O O . TYR B 2 157 ? -50.012 49.489 -67.310 1.00 47.10 ? 486 TYR B O 1 ATOM 3816 C CB . TYR B 2 157 ? -47.712 47.615 -66.258 1.00 39.18 ? 486 TYR B CB 1 ATOM 3817 C CG . TYR B 2 157 ? -47.526 46.823 -67.531 1.00 41.21 ? 486 TYR B CG 1 ATOM 3818 C CD1 . TYR B 2 157 ? -46.288 46.764 -68.159 1.00 38.13 ? 486 TYR B CD1 1 ATOM 3819 C CD2 . TYR B 2 157 ? -48.584 46.129 -68.102 1.00 36.86 ? 486 TYR B CD2 1 ATOM 3820 C CE1 . TYR B 2 157 ? -46.111 46.042 -69.325 1.00 36.80 ? 486 TYR B CE1 1 ATOM 3821 C CE2 . TYR B 2 157 ? -48.417 45.403 -69.269 1.00 37.95 ? 486 TYR B CE2 1 ATOM 3822 C CZ . TYR B 2 157 ? -47.177 45.365 -69.876 1.00 38.84 ? 486 TYR B CZ 1 ATOM 3823 O OH . TYR B 2 157 ? -47.000 44.644 -71.034 1.00 37.80 ? 486 TYR B OH 1 ATOM 3824 N N . ASP B 2 158 ? -48.307 49.703 -68.773 1.00 51.64 ? 487 ASP B N 1 ATOM 3825 C CA . ASP B 2 158 ? -49.144 50.164 -69.874 1.00 49.76 ? 487 ASP B CA 1 ATOM 3826 C C . ASP B 2 158 ? -49.459 49.015 -70.830 1.00 54.06 ? 487 ASP B C 1 ATOM 3827 O O . ASP B 2 158 ? -48.764 48.830 -71.832 1.00 57.42 ? 487 ASP B O 1 ATOM 3828 C CB . ASP B 2 158 ? -48.419 51.287 -70.622 1.00 56.55 ? 487 ASP B CB 1 ATOM 3829 C CG . ASP B 2 158 ? -49.360 52.182 -71.409 1.00 61.36 ? 487 ASP B CG 1 ATOM 3830 O OD1 . ASP B 2 158 ? -50.250 51.659 -72.118 1.00 62.40 ? 487 ASP B OD1 1 ATOM 3831 O OD2 . ASP B 2 158 ? -49.198 53.418 -71.316 1.00 59.03 ? 487 ASP B OD2 1 ATOM 3832 N N . TYR B 2 159 ? -50.503 48.246 -70.525 1.00 46.04 ? 488 TYR B N 1 ATOM 3833 C CA . TYR B 2 159 ? -50.885 47.106 -71.367 1.00 47.55 ? 488 TYR B CA 1 ATOM 3834 C C . TYR B 2 159 ? -51.105 47.429 -72.860 1.00 51.88 ? 488 TYR B C 1 ATOM 3835 O O . TYR B 2 159 ? -50.527 46.755 -73.718 1.00 53.44 ? 488 TYR B O 1 ATOM 3836 C CB . TYR B 2 159 ? -52.096 46.349 -70.790 1.00 41.41 ? 488 TYR B CB 1 ATOM 3837 C CG . TYR B 2 159 ? -52.614 45.261 -71.708 1.00 43.64 ? 488 TYR B CG 1 ATOM 3838 C CD1 . TYR B 2 159 ? -52.061 43.988 -71.689 1.00 43.07 ? 488 TYR B CD1 1 ATOM 3839 C CD2 . TYR B 2 159 ? -53.647 45.510 -72.601 1.00 47.82 ? 488 TYR B CD2 1 ATOM 3840 C CE1 . TYR B 2 159 ? -52.524 42.994 -72.533 1.00 43.20 ? 488 TYR B CE1 1 ATOM 3841 C CE2 . TYR B 2 159 ? -54.113 44.525 -73.451 1.00 48.88 ? 488 TYR B CE2 1 ATOM 3842 C CZ . TYR B 2 159 ? -53.552 43.270 -73.412 1.00 49.87 ? 488 TYR B CZ 1 ATOM 3843 O OH . TYR B 2 159 ? -54.029 42.295 -74.257 1.00 46.67 ? 488 TYR B OH 1 ATOM 3844 N N . PRO B 2 160 ? -51.941 48.444 -73.178 1.00 63.97 ? 489 PRO B N 1 ATOM 3845 C CA . PRO B 2 160 ? -52.209 48.685 -74.605 1.00 69.94 ? 489 PRO B CA 1 ATOM 3846 C C . PRO B 2 160 ? -50.989 49.180 -75.387 1.00 69.44 ? 489 PRO B C 1 ATOM 3847 O O . PRO B 2 160 ? -50.948 49.020 -76.612 1.00 71.26 ? 489 PRO B O 1 ATOM 3848 C CB . PRO B 2 160 ? -53.303 49.762 -74.584 1.00 66.92 ? 489 PRO B CB 1 ATOM 3849 C CG . PRO B 2 160 ? -53.123 50.459 -73.277 1.00 69.22 ? 489 PRO B CG 1 ATOM 3850 C CD . PRO B 2 160 ? -52.690 49.385 -72.318 1.00 62.94 ? 489 PRO B CD 1 ATOM 3851 N N . LYS B 2 161 ? -50.021 49.773 -74.692 1.00 55.15 ? 490 LYS B N 1 ATOM 3852 C CA . LYS B 2 161 ? -48.782 50.232 -75.324 1.00 51.74 ? 490 LYS B CA 1 ATOM 3853 C C . LYS B 2 161 ? -47.981 49.073 -75.929 1.00 52.98 ? 490 LYS B C 1 ATOM 3854 O O . LYS B 2 161 ? -47.280 49.244 -76.929 1.00 59.47 ? 490 LYS B O 1 ATOM 3855 C CB . LYS B 2 161 ? -47.929 51.009 -74.313 1.00 51.25 ? 490 LYS B CB 1 ATOM 3856 C CG . LYS B 2 161 ? -46.487 51.279 -74.746 1.00 49.88 ? 490 LYS B CG 1 ATOM 3857 C CD . LYS B 2 161 ? -45.757 52.172 -73.733 1.00 52.92 ? 490 LYS B CD 1 ATOM 3858 C CE . LYS B 2 161 ? -44.283 52.328 -74.100 1.00 51.07 ? 490 LYS B CE 1 ATOM 3859 N NZ . LYS B 2 161 ? -43.584 53.352 -73.273 1.00 53.43 ? 490 LYS B NZ 1 ATOM 3860 N N . TYR B 2 162 ? -48.115 47.887 -75.342 1.00 46.96 ? 491 TYR B N 1 ATOM 3861 C CA . TYR B 2 162 ? -47.314 46.742 -75.762 1.00 45.37 ? 491 TYR B CA 1 ATOM 3862 C C . TYR B 2 162 ? -48.114 45.596 -76.381 1.00 45.88 ? 491 TYR B C 1 ATOM 3863 O O . TYR B 2 162 ? -47.533 44.566 -76.730 1.00 46.99 ? 491 TYR B O 1 ATOM 3864 C CB . TYR B 2 162 ? -46.511 46.198 -74.571 1.00 45.32 ? 491 TYR B CB 1 ATOM 3865 C CG . TYR B 2 162 ? -45.552 47.188 -73.961 1.00 45.31 ? 491 TYR B CG 1 ATOM 3866 C CD1 . TYR B 2 162 ? -45.873 47.868 -72.796 1.00 42.29 ? 491 TYR B CD1 1 ATOM 3867 C CD2 . TYR B 2 162 ? -44.319 47.438 -74.551 1.00 45.17 ? 491 TYR B CD2 1 ATOM 3868 C CE1 . TYR B 2 162 ? -44.992 48.774 -72.236 1.00 43.41 ? 491 TYR B CE1 1 ATOM 3869 C CE2 . TYR B 2 162 ? -43.433 48.342 -73.997 1.00 40.84 ? 491 TYR B CE2 1 ATOM 3870 C CZ . TYR B 2 162 ? -43.774 49.006 -72.843 1.00 43.98 ? 491 TYR B CZ 1 ATOM 3871 O OH . TYR B 2 162 ? -42.888 49.906 -72.296 1.00 51.57 ? 491 TYR B OH 1 ATOM 3872 N N . GLN B 2 163 ? -49.429 45.750 -76.519 1.00 49.98 ? 492 GLN B N 1 ATOM 3873 C CA . GLN B 2 163 ? -50.242 44.602 -76.932 1.00 58.98 ? 492 GLN B CA 1 ATOM 3874 C C . GLN B 2 163 ? -50.066 44.155 -78.387 1.00 62.09 ? 492 GLN B C 1 ATOM 3875 O O . GLN B 2 163 ? -50.128 42.955 -78.666 1.00 65.35 ? 492 GLN B O 1 ATOM 3876 C CB . GLN B 2 163 ? -51.726 44.761 -76.565 1.00 59.20 ? 492 GLN B CB 1 ATOM 3877 C CG . GLN B 2 163 ? -52.483 45.870 -77.274 1.00 68.01 ? 492 GLN B CG 1 ATOM 3878 C CD . GLN B 2 163 ? -53.991 45.651 -77.218 1.00 75.96 ? 492 GLN B CD 1 ATOM 3879 O OE1 . GLN B 2 163 ? -54.492 44.606 -77.646 1.00 71.43 ? 492 GLN B OE1 1 ATOM 3880 N NE2 . GLN B 2 163 ? -54.720 46.631 -76.683 1.00 71.51 ? 492 GLN B NE2 1 ATOM 3881 N N . LYS B 2 164 ? -49.834 45.098 -79.301 1.00 60.84 ? 493 LYS B N 1 ATOM 3882 C CA . LYS B 2 164 ? -49.589 44.752 -80.704 1.00 66.34 ? 493 LYS B CA 1 ATOM 3883 C C . LYS B 2 164 ? -48.325 43.905 -80.839 1.00 64.13 ? 493 LYS B C 1 ATOM 3884 O O . LYS B 2 164 ? -48.339 42.838 -81.457 1.00 65.02 ? 493 LYS B O 1 ATOM 3885 C CB . LYS B 2 164 ? -49.453 46.015 -81.561 1.00 78.26 ? 493 LYS B CB 1 ATOM 3886 C CG . LYS B 2 164 ? -50.591 47.017 -81.424 1.00 84.42 ? 493 LYS B CG 1 ATOM 3887 C CD . LYS B 2 164 ? -50.350 48.233 -82.320 1.00 88.13 ? 493 LYS B CD 1 ATOM 3888 C CE . LYS B 2 164 ? -51.410 49.311 -82.118 1.00 96.33 ? 493 LYS B CE 1 ATOM 3889 N NZ . LYS B 2 164 ? -51.370 49.901 -80.750 1.00 86.07 ? 493 LYS B NZ 1 ATOM 3890 N N . GLU B 2 165 ? -47.235 44.400 -80.256 1.00 53.27 ? 494 GLU B N 1 ATOM 3891 C CA . GLU B 2 165 ? -45.946 43.714 -80.259 1.00 54.49 ? 494 GLU B CA 1 ATOM 3892 C C . GLU B 2 165 ? -46.044 42.343 -79.579 1.00 58.98 ? 494 GLU B C 1 ATOM 3893 O O . GLU B 2 165 ? -45.492 41.352 -80.071 1.00 59.47 ? 494 GLU B O 1 ATOM 3894 C CB . GLU B 2 165 ? -44.896 44.593 -79.565 1.00 52.87 ? 494 GLU B CB 1 ATOM 3895 C CG . GLU B 2 165 ? -43.519 43.960 -79.389 1.00 50.69 ? 494 GLU B CG 1 ATOM 3896 C CD . GLU B 2 165 ? -42.562 44.864 -78.621 1.00 54.66 ? 494 GLU B CD 1 ATOM 3897 O OE1 . GLU B 2 165 ? -41.443 44.409 -78.283 1.00 50.27 ? 494 GLU B OE1 1 ATOM 3898 O OE2 . GLU B 2 165 ? -42.933 46.032 -78.354 1.00 49.35 ? 494 GLU B OE2 1 ATOM 3899 N N . SER B 2 166 ? -46.761 42.291 -78.459 1.00 58.41 ? 495 SER B N 1 ATOM 3900 C CA . SER B 2 166 ? -46.955 41.047 -77.720 1.00 62.70 ? 495 SER B CA 1 ATOM 3901 C C . SER B 2 166 ? -47.753 40.025 -78.525 1.00 60.27 ? 495 SER B C 1 ATOM 3902 O O . SER B 2 166 ? -47.339 38.874 -78.666 1.00 59.79 ? 495 SER B O 1 ATOM 3903 C CB . SER B 2 166 ? -47.662 41.313 -76.388 1.00 57.44 ? 495 SER B CB 1 ATOM 3904 O OG . SER B 2 166 ? -46.966 42.263 -75.603 1.00 53.46 ? 495 SER B OG 1 ATOM 3905 N N . LYS B 2 167 ? -48.902 40.459 -79.037 1.00 67.29 ? 496 LYS B N 1 ATOM 3906 C CA . LYS B 2 167 ? -49.801 39.608 -79.817 1.00 74.76 ? 496 LYS B CA 1 ATOM 3907 C C . LYS B 2 167 ? -49.097 38.979 -81.022 1.00 73.45 ? 496 LYS B C 1 ATOM 3908 O O . LYS B 2 167 ? -49.318 37.809 -81.343 1.00 72.23 ? 496 LYS B O 1 ATOM 3909 C CB . LYS B 2 167 ? -51.018 40.424 -80.272 1.00 73.80 ? 496 LYS B CB 1 ATOM 3910 C CG . LYS B 2 167 ? -52.033 39.676 -81.122 1.00 82.58 ? 496 LYS B CG 1 ATOM 3911 C CD . LYS B 2 167 ? -53.174 40.611 -81.534 1.00 93.00 ? 496 LYS B CD 1 ATOM 3912 C CE . LYS B 2 167 ? -54.133 39.951 -82.524 1.00 96.58 ? 496 LYS B CE 1 ATOM 3913 N NZ . LYS B 2 167 ? -55.156 40.910 -83.046 1.00 93.63 ? 496 LYS B NZ 1 ATOM 3914 N N . LEU B 2 168 ? -48.241 39.764 -81.672 1.00 63.02 ? 497 LEU B N 1 ATOM 3915 C CA . LEU B 2 168 ? -47.447 39.289 -82.800 1.00 65.35 ? 497 LEU B CA 1 ATOM 3916 C C . LEU B 2 168 ? -46.533 38.132 -82.388 1.00 67.79 ? 497 LEU B C 1 ATOM 3917 O O . LEU B 2 168 ? -46.510 37.086 -83.041 1.00 68.26 ? 497 LEU B O 1 ATOM 3918 C CB . LEU B 2 168 ? -46.618 40.439 -83.379 1.00 66.86 ? 497 LEU B CB 1 ATOM 3919 C CG . LEU B 2 168 ? -46.638 40.616 -84.899 1.00 79.99 ? 497 LEU B CG 1 ATOM 3920 C CD1 . LEU B 2 168 ? -47.051 42.039 -85.272 1.00 74.92 ? 497 LEU B CD1 1 ATOM 3921 C CD2 . LEU B 2 168 ? -45.282 40.267 -85.504 1.00 77.10 ? 497 LEU B CD2 1 ATOM 3922 N N . ASN B 2 169 ? -45.787 38.325 -81.302 1.00 72.71 ? 498 ASN B N 1 ATOM 3923 C CA . ASN B 2 169 ? -44.869 37.301 -80.806 1.00 72.60 ? 498 ASN B CA 1 ATOM 3924 C C . ASN B 2 169 ? -45.586 36.106 -80.164 1.00 71.85 ? 498 ASN B C 1 ATOM 3925 O O . ASN B 2 169 ? -45.117 34.969 -80.257 1.00 69.00 ? 498 ASN B O 1 ATOM 3926 C CB . ASN B 2 169 ? -43.853 37.910 -79.824 1.00 66.71 ? 498 ASN B CB 1 ATOM 3927 C CG . ASN B 2 169 ? -42.942 38.942 -80.481 1.00 72.43 ? 498 ASN B CG 1 ATOM 3928 O OD1 . ASN B 2 169 ? -42.447 38.735 -81.591 1.00 76.59 ? 498 ASN B OD1 1 ATOM 3929 N ND2 . ASN B 2 169 ? -42.719 40.059 -79.794 1.00 64.23 ? 498 ASN B ND2 1 ATOM 3930 N N . ARG B 2 170 ? -46.722 36.370 -79.518 1.00 69.68 ? 499 ARG B N 1 ATOM 3931 C CA . ARG B 2 170 ? -47.501 35.332 -78.836 1.00 69.98 ? 499 ARG B CA 1 ATOM 3932 C C . ARG B 2 170 ? -48.099 34.319 -79.819 1.00 74.51 ? 499 ARG B C 1 ATOM 3933 O O . ARG B 2 170 ? -48.019 33.108 -79.600 1.00 74.20 ? 499 ARG B O 1 ATOM 3934 C CB . ARG B 2 170 ? -48.622 35.964 -77.995 1.00 67.61 ? 499 ARG B CB 1 ATOM 3935 C CG . ARG B 2 170 ? -49.381 34.985 -77.090 1.00 62.44 ? 499 ARG B CG 1 ATOM 3936 C CD . ARG B 2 170 ? -50.653 35.613 -76.524 1.00 64.56 ? 499 ARG B CD 1 ATOM 3937 N NE . ARG B 2 170 ? -50.512 37.056 -76.323 1.00 68.81 ? 499 ARG B NE 1 ATOM 3938 C CZ . ARG B 2 170 ? -51.325 37.973 -76.844 1.00 70.15 ? 499 ARG B CZ 1 ATOM 3939 N NH1 . ARG B 2 170 ? -52.359 37.601 -77.590 1.00 69.10 ? 499 ARG B NH1 1 ATOM 3940 N NH2 . ARG B 2 170 ? -51.110 39.265 -76.617 1.00 61.81 ? 499 ARG B NH2 1 ATOM 3941 N N . GLN B 2 171 ? -48.688 34.823 -80.901 1.00 93.18 ? 500 GLN B N 1 ATOM 3942 C CA . GLN B 2 171 ? -49.379 33.976 -81.877 1.00 100.94 ? 500 GLN B CA 1 ATOM 3943 C C . GLN B 2 171 ? -48.466 33.447 -82.988 1.00 98.36 ? 500 GLN B C 1 ATOM 3944 O O . GLN B 2 171 ? -47.423 34.029 -83.293 1.00 97.81 ? 500 GLN B O 1 ATOM 3945 C CB . GLN B 2 171 ? -50.573 34.726 -82.481 1.00 98.97 ? 500 GLN B CB 1 ATOM 3946 C CG . GLN B 2 171 ? -51.684 35.031 -81.476 1.00 99.34 ? 500 GLN B CG 1 ATOM 3947 C CD . GLN B 2 171 ? -52.670 36.072 -81.980 1.00 106.08 ? 500 GLN B CD 1 ATOM 3948 O OE1 . GLN B 2 171 ? -52.510 36.623 -83.074 1.00 103.79 ? 500 GLN B OE1 1 ATOM 3949 N NE2 . GLN B 2 171 ? -53.697 36.350 -81.180 1.00 99.08 ? 500 GLN B NE2 1 HETATM 3950 C C1 . NAG C 3 . ? -36.784 20.389 -32.652 0.00 44.62 ? 601 NAG A C1 1 HETATM 3951 C C2 . NAG C 3 . ? -35.301 20.356 -33.008 0.00 44.66 ? 601 NAG A C2 1 HETATM 3952 C C3 . NAG C 3 . ? -34.490 19.868 -31.820 0.00 45.01 ? 601 NAG A C3 1 HETATM 3953 C C4 . NAG C 3 . ? -34.698 20.857 -30.689 0.00 44.78 ? 601 NAG A C4 1 HETATM 3954 C C5 . NAG C 3 . ? -36.175 20.899 -30.315 0.00 44.68 ? 601 NAG A C5 1 HETATM 3955 C C6 . NAG C 3 . ? -36.431 22.033 -29.325 0.00 44.32 ? 601 NAG A C6 1 HETATM 3956 C C7 . NAG C 3 . ? -34.504 20.026 -35.273 0.00 44.31 ? 601 NAG A C7 1 HETATM 3957 C C8 . NAG C 3 . ? -35.391 20.157 -36.476 0.00 43.49 ? 601 NAG A C8 1 HETATM 3958 N N2 . NAG C 3 . ? -35.063 19.527 -34.173 0.00 44.73 ? 601 NAG A N2 1 HETATM 3959 O O3 . NAG C 3 . ? -33.126 19.776 -32.161 0.00 44.96 ? 601 NAG A O3 1 HETATM 3960 O O4 . NAG C 3 . ? -33.928 20.485 -29.567 0.00 44.66 ? 601 NAG A O4 1 HETATM 3961 O O5 . NAG C 3 . ? -37.039 21.072 -31.429 0.00 44.62 ? 601 NAG A O5 1 HETATM 3962 O O6 . NAG C 3 . ? -37.808 22.105 -29.025 0.00 43.93 ? 601 NAG A O6 1 HETATM 3963 O O7 . NAG C 3 . ? -33.324 20.369 -35.329 0.00 44.48 ? 601 NAG A O7 1 HETATM 3964 C C1 . NAG D 3 . ? -50.727 62.995 25.334 0.00 59.25 ? 602 NAG A C1 1 HETATM 3965 C C2 . NAG D 3 . ? -51.124 64.134 24.402 0.00 58.97 ? 602 NAG A C2 1 HETATM 3966 C C3 . NAG D 3 . ? -52.524 64.642 24.727 0.00 59.03 ? 602 NAG A C3 1 HETATM 3967 C C4 . NAG D 3 . ? -53.513 63.488 24.833 0.00 58.67 ? 602 NAG A C4 1 HETATM 3968 C C5 . NAG D 3 . ? -52.974 62.388 25.738 0.00 58.60 ? 602 NAG A C5 1 HETATM 3969 C C6 . NAG D 3 . ? -53.928 61.201 25.784 0.00 57.96 ? 602 NAG A C6 1 HETATM 3970 C C7 . NAG D 3 . ? -50.268 66.311 23.758 0.00 58.89 ? 602 NAG A C7 1 HETATM 3971 C C8 . NAG D 3 . ? -49.175 67.323 23.932 0.00 59.15 ? 602 NAG A C8 1 HETATM 3972 N N2 . NAG D 3 . ? -50.166 65.217 24.508 0.00 59.14 ? 602 NAG A N2 1 HETATM 3973 O O3 . NAG D 3 . ? -52.952 65.546 23.703 0.00 58.74 ? 602 NAG A O3 1 HETATM 3974 O O4 . NAG D 3 . ? -54.755 63.971 25.357 0.00 58.58 ? 602 NAG A O4 1 HETATM 3975 O O5 . NAG D 3 . ? -51.702 61.957 25.257 0.00 58.61 ? 602 NAG A O5 1 HETATM 3976 O O6 . NAG D 3 . ? -53.852 60.576 27.070 0.00 57.90 ? 602 NAG A O6 1 HETATM 3977 O O7 . NAG D 3 . ? -51.191 66.480 22.978 0.00 58.71 ? 602 NAG A O7 1 HETATM 3978 C C1 . SIA E 4 . ? -29.628 31.912 33.826 1.00 71.37 ? 603 SIA A C1 1 HETATM 3979 C C2 . SIA E 4 . ? -29.718 31.481 35.265 1.00 74.11 ? 603 SIA A C2 1 HETATM 3980 C C3 . SIA E 4 . ? -28.957 32.485 36.120 1.00 68.73 ? 603 SIA A C3 1 HETATM 3981 C C4 . SIA E 4 . ? -29.522 33.903 35.962 1.00 68.46 ? 603 SIA A C4 1 HETATM 3982 C C5 . SIA E 4 . ? -30.948 34.099 36.321 1.00 64.97 ? 603 SIA A C5 1 HETATM 3983 C C6 . SIA E 4 . ? -31.742 32.964 35.713 1.00 62.79 ? 603 SIA A C6 1 HETATM 3984 C C7 . SIA E 4 . ? -33.156 32.835 36.263 1.00 64.20 ? 603 SIA A C7 1 HETATM 3985 C C8 . SIA E 4 . ? -33.830 31.630 35.617 1.00 62.79 ? 603 SIA A C8 1 HETATM 3986 C C9 . SIA E 4 . ? -35.340 31.653 35.803 1.00 54.60 ? 603 SIA A C9 1 HETATM 3987 C C10 . SIA E 4 . ? -32.462 35.981 36.364 1.00 58.07 ? 603 SIA A C10 1 HETATM 3988 C C11 . SIA E 4 . ? -32.716 37.385 35.906 1.00 58.30 ? 603 SIA A C11 1 HETATM 3989 N N5 . SIA E 4 . ? -31.417 35.372 35.817 1.00 56.70 ? 603 SIA A N5 1 HETATM 3990 O O1A . SIA E 4 . ? -30.685 32.091 33.187 1.00 66.76 ? 603 SIA A O1A 1 HETATM 3991 O O1B . SIA E 4 . ? -28.497 32.079 33.326 1.00 70.10 ? 603 SIA A O1B 1 HETATM 3992 O O4 . SIA E 4 . ? -28.735 34.797 36.760 1.00 63.31 ? 603 SIA A O4 1 HETATM 3993 O O6 . SIA E 4 . ? -31.077 31.659 35.751 1.00 68.36 ? 603 SIA A O6 1 HETATM 3994 O O7 . SIA E 4 . ? -33.107 32.669 37.681 1.00 64.85 ? 603 SIA A O7 1 HETATM 3995 O O8 . SIA E 4 . ? -33.536 31.603 34.217 1.00 57.40 ? 603 SIA A O8 1 HETATM 3996 O O9 . SIA E 4 . ? -35.875 30.414 35.329 1.00 57.38 ? 603 SIA A O9 1 HETATM 3997 O O10 . SIA E 4 . ? -33.170 35.432 37.186 1.00 65.20 ? 603 SIA A O10 1 HETATM 3998 C C1 . GAL F 5 . ? -30.719 26.831 36.156 1.00 87.95 ? 604 GAL A C1 1 HETATM 3999 C C2 . GAL F 5 . ? -30.305 28.247 36.540 1.00 88.16 ? 604 GAL A C2 1 HETATM 4000 C C3 . GAL F 5 . ? -29.831 29.068 35.342 1.00 81.78 ? 604 GAL A C3 1 HETATM 4001 C C4 . GAL F 5 . ? -28.917 28.282 34.408 1.00 78.88 ? 604 GAL A C4 1 HETATM 4002 C C5 . GAL F 5 . ? -29.470 26.885 34.152 1.00 77.77 ? 604 GAL A C5 1 HETATM 4003 C C6 . GAL F 5 . ? -28.513 26.068 33.292 1.00 78.08 ? 604 GAL A C6 1 HETATM 4004 O O2 . GAL F 5 . ? -31.414 28.910 37.158 1.00 86.07 ? 604 GAL A O2 1 HETATM 4005 O O3 . GAL F 5 . ? -29.188 30.255 35.776 1.00 78.94 ? 604 GAL A O3 1 HETATM 4006 O O4 . GAL F 5 . ? -27.612 28.180 34.990 1.00 82.10 ? 604 GAL A O4 1 HETATM 4007 O O5 . GAL F 5 . ? -29.677 26.220 35.396 1.00 91.02 ? 604 GAL A O5 1 HETATM 4008 O O6 . GAL F 5 . ? -28.393 26.675 32.001 1.00 76.70 ? 604 GAL A O6 1 HETATM 4009 C C1 . NAG G 3 . ? -32.516 22.469 38.307 1.00 125.76 ? 605 NAG A C1 1 HETATM 4010 C C2 . NAG G 3 . ? -31.685 22.491 37.026 1.00 122.21 ? 605 NAG A C2 1 HETATM 4011 C C3 . NAG G 3 . ? -30.864 23.770 36.900 1.00 117.12 ? 605 NAG A C3 1 HETATM 4012 C C4 . NAG G 3 . ? -31.664 25.023 37.248 1.00 112.82 ? 605 NAG A C4 1 HETATM 4013 C C5 . NAG G 3 . ? -32.465 24.831 38.532 1.00 116.10 ? 605 NAG A C5 1 HETATM 4014 C C6 . NAG G 3 . ? -33.374 26.026 38.813 1.00 110.65 ? 605 NAG A C6 1 HETATM 4015 C C7 . NAG G 3 . ? -30.805 20.547 35.864 1.00 127.48 ? 605 NAG A C7 1 HETATM 4016 C C8 . NAG G 3 . ? -29.704 19.532 35.760 1.00 122.89 ? 605 NAG A C8 1 HETATM 4017 N N2 . NAG G 3 . ? -30.806 21.336 36.940 1.00 127.47 ? 605 NAG A N2 1 HETATM 4018 O O3 . NAG G 3 . ? -30.369 23.854 35.582 1.00 110.90 ? 605 NAG A O3 1 HETATM 4019 O O4 . NAG G 3 . ? -30.779 26.109 37.417 1.00 105.84 ? 605 NAG A O4 1 HETATM 4020 O O5 . NAG G 3 . ? -33.254 23.667 38.433 1.00 124.89 ? 605 NAG A O5 1 HETATM 4021 O O6 . NAG G 3 . ? -34.346 25.686 39.779 1.00 105.05 ? 605 NAG A O6 1 HETATM 4022 O O7 . NAG G 3 . ? -31.659 20.630 34.982 1.00 122.57 ? 605 NAG A O7 1 HETATM 4023 C C1 . GAL H 5 . ? -32.718 18.272 40.450 1.00 140.32 ? 606 GAL A C1 1 HETATM 4024 C C2 . GAL H 5 . ? -32.615 19.269 39.295 1.00 138.23 ? 606 GAL A C2 1 HETATM 4025 C C3 . GAL H 5 . ? -33.219 20.631 39.631 1.00 137.74 ? 606 GAL A C3 1 HETATM 4026 C C4 . GAL H 5 . ? -34.546 20.485 40.365 1.00 141.25 ? 606 GAL A C4 1 HETATM 4027 C C5 . GAL H 5 . ? -34.397 19.503 41.523 1.00 142.08 ? 606 GAL A C5 1 HETATM 4028 C C6 . GAL H 5 . ? -35.692 19.379 42.320 1.00 139.67 ? 606 GAL A C6 1 HETATM 4029 O O1 . GAL H 5 . ? -32.426 16.982 39.961 1.00 140.52 ? 606 GAL A O1 1 HETATM 4030 O O2 . GAL H 5 . ? -31.253 19.443 38.978 1.00 134.46 ? 606 GAL A O2 1 HETATM 4031 O O3 . GAL H 5 . ? -33.431 21.384 38.453 1.00 131.31 ? 606 GAL A O3 1 HETATM 4032 O O4 . GAL H 5 . ? -35.532 20.030 39.461 1.00 140.32 ? 606 GAL A O4 1 HETATM 4033 O O5 . GAL H 5 . ? -34.018 18.248 41.001 1.00 139.71 ? 606 GAL A O5 1 HETATM 4034 O O6 . GAL H 5 . ? -35.604 18.305 43.229 1.00 134.12 ? 606 GAL A O6 1 HETATM 4035 C C1 . NAG I 3 . ? -43.679 54.229 -62.033 0.00 49.80 ? 601 NAG B C1 1 HETATM 4036 C C2 . NAG I 3 . ? -43.700 55.706 -61.626 0.00 50.95 ? 601 NAG B C2 1 HETATM 4037 C C3 . NAG I 3 . ? -43.457 56.682 -62.781 0.00 52.33 ? 601 NAG B C3 1 HETATM 4038 C C4 . NAG I 3 . ? -42.566 56.161 -63.905 0.00 52.98 ? 601 NAG B C4 1 HETATM 4039 C C5 . NAG I 3 . ? -42.805 54.682 -64.171 0.00 50.75 ? 601 NAG B C5 1 HETATM 4040 C C6 . NAG I 3 . ? -41.824 54.125 -65.199 0.00 49.91 ? 601 NAG B C6 1 HETATM 4041 C C7 . NAG I 3 . ? -45.153 56.256 -59.732 0.00 50.04 ? 601 NAG B C7 1 HETATM 4042 C C8 . NAG I 3 . ? -46.410 55.723 -59.110 0.00 49.17 ? 601 NAG B C8 1 HETATM 4043 N N2 . NAG I 3 . ? -44.991 56.011 -61.031 0.00 50.35 ? 601 NAG B N2 1 HETATM 4044 O O3 . NAG I 3 . ? -42.879 57.863 -62.272 0.00 53.06 ? 601 NAG B O3 1 HETATM 4045 O O4 . NAG I 3 . ? -42.873 56.899 -65.068 0.00 54.63 ? 601 NAG B O4 1 HETATM 4046 O O5 . NAG I 3 . ? -42.652 53.974 -62.966 0.00 49.37 ? 601 NAG B O5 1 HETATM 4047 O O6 . NAG I 3 . ? -40.501 54.323 -64.754 0.00 50.26 ? 601 NAG B O6 1 HETATM 4048 O O7 . NAG I 3 . ? -44.341 56.882 -59.054 0.00 50.51 ? 601 NAG B O7 1 HETATM 4049 C C1 . NAG J 3 . ? -41.736 57.643 -65.542 0.00 56.16 ? 602 NAG B C1 1 HETATM 4050 C C2 . NAG J 3 . ? -42.042 58.066 -66.967 0.00 57.55 ? 602 NAG B C2 1 HETATM 4051 C C3 . NAG J 3 . ? -40.787 58.641 -67.585 0.00 59.82 ? 602 NAG B C3 1 HETATM 4052 C C4 . NAG J 3 . ? -40.383 59.862 -66.766 0.00 60.35 ? 602 NAG B C4 1 HETATM 4053 C C5 . NAG J 3 . ? -40.340 59.580 -65.260 0.00 59.28 ? 602 NAG B C5 1 HETATM 4054 C C6 . NAG J 3 . ? -40.384 60.898 -64.496 0.00 60.33 ? 602 NAG B C6 1 HETATM 4055 C C7 . NAG J 3 . ? -43.784 57.018 -68.282 0.00 57.09 ? 602 NAG B C7 1 HETATM 4056 C C8 . NAG J 3 . ? -44.844 57.745 -67.507 0.00 57.02 ? 602 NAG B C8 1 HETATM 4057 N N2 . NAG J 3 . ? -42.569 56.961 -67.741 0.00 57.33 ? 602 NAG B N2 1 HETATM 4058 O O3 . NAG J 3 . ? -41.057 58.979 -68.926 0.00 60.88 ? 602 NAG B O3 1 HETATM 4059 O O4 . NAG J 3 . ? -39.128 60.344 -67.206 0.00 62.22 ? 602 NAG B O4 1 HETATM 4060 O O5 . NAG J 3 . ? -41.418 58.787 -64.781 0.00 57.02 ? 602 NAG B O5 1 HETATM 4061 O O6 . NAG J 3 . ? -41.659 61.053 -63.912 0.00 58.60 ? 602 NAG B O6 1 HETATM 4062 O O7 . NAG J 3 . ? -44.053 56.508 -69.368 0.00 57.49 ? 602 NAG B O7 1 HETATM 4063 C C1 . BMA K 6 . ? -39.341 61.408 -68.156 0.00 63.19 ? 603 BMA B C1 1 HETATM 4064 C C2 . BMA K 6 . ? -38.237 62.454 -68.068 0.00 64.68 ? 603 BMA B C2 1 HETATM 4065 C C3 . BMA K 6 . ? -38.588 63.631 -68.965 0.00 65.56 ? 603 BMA B C3 1 HETATM 4066 C C4 . BMA K 6 . ? -38.886 63.149 -70.380 0.00 65.63 ? 603 BMA B C4 1 HETATM 4067 C C5 . BMA K 6 . ? -39.897 62.004 -70.381 0.00 64.71 ? 603 BMA B C5 1 HETATM 4068 C C6 . BMA K 6 . ? -40.082 61.440 -71.785 0.00 65.10 ? 603 BMA B C6 1 HETATM 4069 O O2 . BMA K 6 . ? -36.996 61.883 -68.499 0.00 65.25 ? 603 BMA B O2 1 HETATM 4070 O O3 . BMA K 6 . ? -37.495 64.555 -68.991 0.00 66.72 ? 603 BMA B O3 1 HETATM 4071 O O4 . BMA K 6 . ? -39.421 64.240 -71.137 0.00 66.45 ? 603 BMA B O4 1 HETATM 4072 O O5 . BMA K 6 . ? -39.476 60.957 -69.505 0.00 63.69 ? 603 BMA B O5 1 HETATM 4073 O O6 . BMA K 6 . ? -41.074 60.410 -71.766 0.00 64.47 ? 603 BMA B O6 1 HETATM 4074 O O . HOH L 7 . ? -46.592 35.153 43.160 1.00 52.95 ? 701 HOH A O 1 HETATM 4075 O O . HOH L 7 . ? -31.363 51.367 -7.542 1.00 52.03 ? 702 HOH A O 1 HETATM 4076 O O . HOH L 7 . ? -35.035 28.426 -20.563 1.00 49.47 ? 703 HOH A O 1 HETATM 4077 O O . HOH L 7 . ? -51.647 48.818 16.755 1.00 55.92 ? 704 HOH A O 1 HETATM 4078 O O . HOH L 7 . ? -29.649 36.495 8.343 1.00 32.34 ? 705 HOH A O 1 HETATM 4079 O O . HOH L 7 . ? -31.673 58.196 14.929 1.00 54.32 ? 706 HOH A O 1 HETATM 4080 O O . HOH L 7 . ? -37.837 50.030 30.251 1.00 47.03 ? 707 HOH A O 1 HETATM 4081 O O . HOH L 7 . ? -34.292 26.002 -48.078 1.00 54.38 ? 708 HOH A O 1 HETATM 4082 O O . HOH L 7 . ? -29.924 23.371 27.618 1.00 61.48 ? 709 HOH A O 1 HETATM 4083 O O . HOH L 7 . ? -50.864 40.640 -18.360 1.00 44.29 ? 710 HOH A O 1 HETATM 4084 O O . HOH L 7 . ? -56.490 54.385 18.408 1.00 58.73 ? 711 HOH A O 1 HETATM 4085 O O . HOH L 7 . ? -29.713 45.928 31.164 1.00 47.11 ? 712 HOH A O 1 HETATM 4086 O O . HOH L 7 . ? -32.071 47.079 16.379 1.00 44.01 ? 713 HOH A O 1 HETATM 4087 O O . HOH L 7 . ? -43.378 38.944 -6.439 1.00 40.23 ? 714 HOH A O 1 HETATM 4088 O O . HOH L 7 . ? -33.089 42.875 31.636 1.00 35.71 ? 715 HOH A O 1 HETATM 4089 O O . HOH L 7 . ? -36.502 34.007 10.982 1.00 55.57 ? 716 HOH A O 1 HETATM 4090 O O . HOH L 7 . ? -46.629 48.898 7.088 1.00 46.33 ? 717 HOH A O 1 HETATM 4091 O O . HOH L 7 . ? -34.397 28.436 33.422 1.00 65.20 ? 718 HOH A O 1 HETATM 4092 O O . HOH L 7 . ? -30.993 37.335 -47.896 1.00 42.00 ? 719 HOH A O 1 HETATM 4093 O O . HOH L 7 . ? -30.952 44.645 16.831 1.00 43.72 ? 720 HOH A O 1 HETATM 4094 O O . HOH L 7 . ? -38.636 45.726 0.354 1.00 50.21 ? 721 HOH A O 1 HETATM 4095 O O . HOH L 7 . ? -46.629 34.613 22.553 1.00 60.71 ? 722 HOH A O 1 HETATM 4096 O O . HOH L 7 . ? -50.276 48.885 20.700 1.00 35.50 ? 723 HOH A O 1 HETATM 4097 O O . HOH L 7 . ? -52.666 50.271 20.214 1.00 46.57 ? 724 HOH A O 1 HETATM 4098 O O . HOH L 7 . ? -39.760 47.445 22.894 1.00 38.86 ? 725 HOH A O 1 HETATM 4099 O O . HOH L 7 . ? -31.107 38.972 -16.904 1.00 43.86 ? 726 HOH A O 1 HETATM 4100 O O . HOH L 7 . ? -23.678 32.012 27.891 1.00 57.27 ? 727 HOH A O 1 HETATM 4101 O O . HOH L 7 . ? -54.347 48.456 18.606 1.00 50.20 ? 728 HOH A O 1 HETATM 4102 O O . HOH L 7 . ? -42.876 52.369 38.222 1.00 62.78 ? 729 HOH A O 1 HETATM 4103 O O . HOH L 7 . ? -38.653 48.377 1.984 1.00 42.59 ? 730 HOH A O 1 HETATM 4104 O O . HOH L 7 . ? -46.683 23.011 -31.900 1.00 43.12 ? 731 HOH A O 1 HETATM 4105 O O . HOH L 7 . ? -45.875 35.753 -34.798 1.00 23.04 ? 732 HOH A O 1 HETATM 4106 O O . HOH L 7 . ? -40.703 41.412 36.029 1.00 33.20 ? 733 HOH A O 1 HETATM 4107 O O . HOH L 7 . ? -31.870 48.011 13.739 1.00 40.95 ? 734 HOH A O 1 HETATM 4108 O O . HOH L 7 . ? -28.756 43.505 19.281 1.00 38.94 ? 735 HOH A O 1 HETATM 4109 O O . HOH L 7 . ? -31.762 32.529 -3.434 1.00 39.95 ? 736 HOH A O 1 HETATM 4110 O O . HOH L 7 . ? -49.484 32.965 12.888 1.00 48.33 ? 737 HOH A O 1 HETATM 4111 O O . HOH L 7 . ? -45.145 54.660 8.372 1.00 46.32 ? 738 HOH A O 1 HETATM 4112 O O . HOH L 7 . ? -37.433 32.092 -47.437 1.00 24.83 ? 739 HOH A O 1 HETATM 4113 O O . HOH L 7 . ? -27.486 35.580 22.700 1.00 49.66 ? 740 HOH A O 1 HETATM 4114 O O . HOH L 7 . ? -36.765 49.378 -9.828 1.00 42.94 ? 741 HOH A O 1 HETATM 4115 O O . HOH L 7 . ? -44.970 29.953 14.380 1.00 47.90 ? 742 HOH A O 1 HETATM 4116 O O . HOH L 7 . ? -45.679 42.260 3.804 1.00 35.83 ? 743 HOH A O 1 HETATM 4117 O O . HOH L 7 . ? -29.538 51.365 7.177 1.00 44.17 ? 744 HOH A O 1 HETATM 4118 O O . HOH L 7 . ? -42.239 25.817 25.070 1.00 49.74 ? 745 HOH A O 1 HETATM 4119 O O . HOH L 7 . ? -53.588 36.887 8.321 1.00 38.72 ? 746 HOH A O 1 HETATM 4120 O O . HOH L 7 . ? -45.062 36.318 7.186 1.00 34.67 ? 747 HOH A O 1 HETATM 4121 O O . HOH L 7 . ? -34.914 44.153 -16.039 1.00 47.43 ? 748 HOH A O 1 HETATM 4122 O O . HOH L 7 . ? -23.727 42.117 3.167 1.00 52.69 ? 749 HOH A O 1 HETATM 4123 O O . HOH L 7 . ? -49.266 35.535 13.017 1.00 29.83 ? 750 HOH A O 1 HETATM 4124 O O . HOH L 7 . ? -44.198 19.294 -36.503 1.00 56.98 ? 751 HOH A O 1 HETATM 4125 O O . HOH L 7 . ? -34.162 31.783 -27.207 1.00 44.72 ? 752 HOH A O 1 HETATM 4126 O O . HOH L 7 . ? -40.377 33.411 -58.811 1.00 40.51 ? 753 HOH A O 1 HETATM 4127 O O . HOH L 7 . ? -35.148 38.422 -29.672 1.00 36.71 ? 754 HOH A O 1 HETATM 4128 O O . HOH L 7 . ? -42.127 29.341 -30.786 1.00 28.63 ? 755 HOH A O 1 HETATM 4129 O O . HOH L 7 . ? -35.175 34.039 -36.832 1.00 39.85 ? 756 HOH A O 1 HETATM 4130 O O . HOH L 7 . ? -46.963 19.341 -39.615 1.00 41.58 ? 757 HOH A O 1 HETATM 4131 O O . HOH L 7 . ? -45.768 37.251 -12.645 1.00 42.64 ? 758 HOH A O 1 HETATM 4132 O O . HOH L 7 . ? -38.818 44.796 3.044 1.00 41.48 ? 759 HOH A O 1 HETATM 4133 O O . HOH L 7 . ? -47.836 26.715 -39.654 1.00 29.65 ? 760 HOH A O 1 HETATM 4134 O O . HOH L 7 . ? -44.598 31.669 17.067 1.00 48.70 ? 761 HOH A O 1 HETATM 4135 O O . HOH L 7 . ? -23.042 39.381 1.097 1.00 48.77 ? 762 HOH A O 1 HETATM 4136 O O . HOH L 7 . ? -47.954 39.670 19.858 1.00 40.48 ? 763 HOH A O 1 HETATM 4137 O O . HOH L 7 . ? -34.468 38.012 -36.040 1.00 40.97 ? 764 HOH A O 1 HETATM 4138 O O . HOH L 7 . ? -41.404 28.973 -28.248 1.00 43.40 ? 765 HOH A O 1 HETATM 4139 O O . HOH L 7 . ? -47.120 32.573 15.828 1.00 52.67 ? 766 HOH A O 1 HETATM 4140 O O . HOH L 7 . ? -30.011 54.096 8.458 1.00 50.70 ? 767 HOH A O 1 HETATM 4141 O O . HOH L 7 . ? -47.517 34.969 -13.082 1.00 37.46 ? 768 HOH A O 1 HETATM 4142 O O . HOH L 7 . ? -28.447 53.053 0.279 1.00 45.40 ? 769 HOH A O 1 HETATM 4143 O O . HOH L 7 . ? -37.255 40.694 -35.635 1.00 44.47 ? 770 HOH A O 1 HETATM 4144 O O . HOH L 7 . ? -45.372 29.844 -44.734 1.00 30.18 ? 771 HOH A O 1 HETATM 4145 O O . HOH L 7 . ? -47.609 28.601 -43.035 1.00 44.07 ? 772 HOH A O 1 HETATM 4146 O O . HOH L 7 . ? -28.199 38.862 -16.740 1.00 53.20 ? 773 HOH A O 1 HETATM 4147 O O . HOH L 7 . ? -50.552 40.703 21.526 1.00 46.31 ? 774 HOH A O 1 HETATM 4148 O O . HOH L 7 . ? -52.077 42.499 22.284 1.00 57.05 ? 775 HOH A O 1 HETATM 4149 O O . HOH M 7 . ? -44.092 47.799 -78.615 1.00 65.00 ? 701 HOH B O 1 HETATM 4150 O O . HOH M 7 . ? -40.480 24.718 -51.499 1.00 48.82 ? 702 HOH B O 1 HETATM 4151 O O . HOH M 7 . ? -47.904 30.338 0.467 1.00 45.46 ? 703 HOH B O 1 HETATM 4152 O O . HOH M 7 . ? -52.814 45.833 -67.316 1.00 56.34 ? 704 HOH B O 1 HETATM 4153 O O . HOH M 7 . ? -51.197 28.060 -42.077 1.00 36.81 ? 705 HOH B O 1 HETATM 4154 O O . HOH M 7 . ? -40.920 42.305 -79.259 1.00 62.72 ? 706 HOH B O 1 HETATM 4155 O O . HOH M 7 . ? -51.409 37.703 -38.256 1.00 38.60 ? 707 HOH B O 1 HETATM 4156 O O . HOH M 7 . ? -50.357 37.199 1.784 1.00 33.86 ? 708 HOH B O 1 HETATM 4157 O O . HOH M 7 . ? -27.599 41.957 -71.490 1.00 52.96 ? 709 HOH B O 1 HETATM 4158 O O . HOH M 7 . ? -45.363 36.255 -9.179 1.00 38.93 ? 710 HOH B O 1 HETATM 4159 O O . HOH M 7 . ? -47.983 43.957 -47.001 1.00 43.04 ? 711 HOH B O 1 HETATM 4160 O O . HOH M 7 . ? -48.119 27.472 -60.359 1.00 45.75 ? 712 HOH B O 1 HETATM 4161 O O . HOH M 7 . ? -52.455 44.929 -60.419 1.00 37.48 ? 713 HOH B O 1 HETATM 4162 O O . HOH M 7 . ? -47.693 28.095 -49.123 1.00 51.29 ? 714 HOH B O 1 HETATM 4163 O O . HOH M 7 . ? -38.713 33.689 -53.723 1.00 33.65 ? 715 HOH B O 1 HETATM 4164 O O . HOH M 7 . ? -56.217 27.930 11.385 1.00 47.81 ? 716 HOH B O 1 HETATM 4165 O O . HOH M 7 . ? -46.883 29.576 -2.541 1.00 55.40 ? 717 HOH B O 1 HETATM 4166 O O . HOH M 7 . ? -51.463 41.413 -49.312 1.00 42.67 ? 718 HOH B O 1 HETATM 4167 O O . HOH M 7 . ? -53.917 42.968 -20.371 1.00 34.37 ? 719 HOH B O 1 HETATM 4168 O O . HOH M 7 . ? -49.018 41.901 -51.214 1.00 38.38 ? 720 HOH B O 1 HETATM 4169 O O . HOH M 7 . ? -53.221 25.315 -11.050 1.00 44.99 ? 721 HOH B O 1 HETATM 4170 O O . HOH M 7 . ? -44.756 32.327 -2.391 1.00 44.39 ? 722 HOH B O 1 HETATM 4171 O O . HOH M 7 . ? -32.415 31.346 -52.111 1.00 48.18 ? 723 HOH B O 1 HETATM 4172 O O . HOH M 7 . ? -45.689 50.329 -69.144 1.00 50.03 ? 724 HOH B O 1 HETATM 4173 O O . HOH M 7 . ? -56.463 47.250 -27.064 1.00 40.33 ? 725 HOH B O 1 HETATM 4174 O O . HOH M 7 . ? -41.214 47.203 -76.592 1.00 43.70 ? 726 HOH B O 1 HETATM 4175 O O . HOH M 7 . ? -54.638 38.367 -60.845 1.00 40.11 ? 727 HOH B O 1 HETATM 4176 O O . HOH M 7 . ? -53.504 28.032 -40.872 1.00 39.16 ? 728 HOH B O 1 HETATM 4177 O O . HOH M 7 . ? -51.700 42.258 -45.754 1.00 30.45 ? 729 HOH B O 1 HETATM 4178 O O . HOH M 7 . ? -53.133 25.413 -8.063 1.00 39.72 ? 730 HOH B O 1 HETATM 4179 O O . HOH M 7 . ? -50.480 25.846 -17.718 1.00 29.51 ? 731 HOH B O 1 HETATM 4180 O O . HOH M 7 . ? -36.263 43.880 -59.865 1.00 47.22 ? 732 HOH B O 1 HETATM 4181 O O . HOH M 7 . ? -50.805 39.706 -14.344 1.00 53.19 ? 733 HOH B O 1 HETATM 4182 O O . HOH M 7 . ? -58.314 29.696 -24.857 1.00 38.00 ? 734 HOH B O 1 HETATM 4183 O O . HOH M 7 . ? -55.560 38.963 -54.405 1.00 62.76 ? 735 HOH B O 1 HETATM 4184 O O . HOH M 7 . ? -43.308 23.495 -53.594 1.00 45.11 ? 736 HOH B O 1 HETATM 4185 O O . HOH M 7 . ? -48.897 28.684 -40.617 1.00 28.61 ? 737 HOH B O 1 HETATM 4186 O O . HOH M 7 . ? -53.174 37.857 -12.847 1.00 27.30 ? 738 HOH B O 1 HETATM 4187 O O . HOH M 7 . ? -55.464 29.427 -51.313 1.00 52.09 ? 739 HOH B O 1 HETATM 4188 O O . HOH M 7 . ? -49.941 52.974 -58.691 1.00 52.24 ? 740 HOH B O 1 HETATM 4189 O O . HOH M 7 . ? -29.623 42.498 -57.210 1.00 43.43 ? 741 HOH B O 1 HETATM 4190 O O . HOH M 7 . ? -46.730 47.091 -79.241 1.00 53.75 ? 742 HOH B O 1 HETATM 4191 O O . HOH M 7 . ? -53.743 41.202 -55.560 1.00 40.81 ? 743 HOH B O 1 HETATM 4192 O O . HOH M 7 . ? -31.230 34.427 -54.422 1.00 48.17 ? 744 HOH B O 1 HETATM 4193 O O . HOH M 7 . ? -44.691 29.163 5.650 1.00 41.12 ? 745 HOH B O 1 HETATM 4194 O O . HOH M 7 . ? -46.388 49.603 -36.389 1.00 47.18 ? 746 HOH B O 1 HETATM 4195 O O . HOH M 7 . ? -44.820 30.842 -5.324 1.00 56.64 ? 747 HOH B O 1 HETATM 4196 O O . HOH M 7 . ? -39.738 47.473 -56.477 1.00 52.80 ? 748 HOH B O 1 HETATM 4197 O O . HOH M 7 . ? -45.310 28.222 -27.272 1.00 36.60 ? 749 HOH B O 1 HETATM 4198 O O . HOH M 7 . ? -44.455 31.974 -44.308 1.00 34.84 ? 750 HOH B O 1 HETATM 4199 O O . HOH M 7 . ? -42.696 37.496 5.491 1.00 39.78 ? 751 HOH B O 1 HETATM 4200 O O . HOH M 7 . ? -33.585 49.256 -73.649 1.00 43.69 ? 752 HOH B O 1 HETATM 4201 O O . HOH M 7 . ? -55.042 32.582 10.641 1.00 37.32 ? 753 HOH B O 1 HETATM 4202 O O . HOH M 7 . ? -40.057 49.037 -73.244 1.00 48.70 ? 754 HOH B O 1 HETATM 4203 O O . HOH M 7 . ? -53.240 35.909 -41.027 1.00 32.84 ? 755 HOH B O 1 HETATM 4204 O O . HOH M 7 . ? -54.593 41.787 -57.820 1.00 31.68 ? 756 HOH B O 1 HETATM 4205 O O . HOH M 7 . ? -49.917 43.523 -53.175 1.00 36.08 ? 757 HOH B O 1 HETATM 4206 O O . HOH M 7 . ? -43.539 50.088 -78.350 1.00 64.97 ? 758 HOH B O 1 HETATM 4207 O O . HOH M 7 . ? -30.621 31.670 -54.968 1.00 47.24 ? 759 HOH B O 1 HETATM 4208 O O . HOH M 7 . ? -54.420 44.448 -58.754 1.00 40.75 ? 760 HOH B O 1 HETATM 4209 O O . HOH M 7 . ? -56.016 30.450 9.891 1.00 32.85 ? 761 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 0.3643 0.4562 0.3356 -0.0328 0.0482 0.0220 1 ASP A N 2 C CA . ASP A 1 ? 0.5634 0.6540 0.5390 -0.0344 0.0464 0.0242 1 ASP A CA 3 C C . ASP A 1 ? 0.5471 0.6348 0.5256 -0.0327 0.0424 0.0234 1 ASP A C 4 O O . ASP A 1 ? 0.4477 0.5320 0.4220 -0.0315 0.0401 0.0227 1 ASP A O 5 C CB . ASP A 1 ? 0.5102 0.5967 0.4803 -0.0369 0.0461 0.0276 1 ASP A CB 6 C CG . ASP A 1 ? 0.6535 0.7428 0.6225 -0.0399 0.0501 0.0290 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.5909 0.6865 0.5632 -0.0398 0.0531 0.0272 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.6134 0.6986 0.5780 -0.0422 0.0502 0.0320 1 ASP A OD2 9 N N . LYS A 2 ? 0.4832 0.5725 0.4687 -0.0328 0.0416 0.0235 2 LYS A N 10 C CA . LYS A 2 ? 0.5268 0.6139 0.5155 -0.0311 0.0382 0.0224 2 LYS A CA 11 C C . LYS A 2 ? 0.5112 0.5989 0.5065 -0.0319 0.0370 0.0235 2 LYS A C 12 O O . LYS A 2 ? 0.4725 0.5638 0.4716 -0.0334 0.0391 0.0241 2 LYS A O 13 C CB . LYS A 2 ? 0.5906 0.6791 0.5803 -0.0285 0.0385 0.0191 2 LYS A CB 14 C CG . LYS A 2 ? 0.6472 0.7414 0.6413 -0.0275 0.0416 0.0177 2 LYS A CG 15 C CD . LYS A 2 ? 0.8048 0.8989 0.7982 -0.0242 0.0419 0.0144 2 LYS A CD 16 C CE . LYS A 2 ? 0.7379 0.8285 0.7338 -0.0229 0.0387 0.0133 2 LYS A CE 17 N NZ . LYS A 2 ? 0.8447 0.9340 0.8391 -0.0197 0.0391 0.0102 2 LYS A NZ 18 N N . ILE A 3 ? 0.4224 0.5071 0.4190 -0.0311 0.0336 0.0236 3 ILE A N 19 C CA . ILE A 3 ? 0.3461 0.4310 0.3487 -0.0314 0.0322 0.0242 3 ILE A CA 20 C C . ILE A 3 ? 0.3782 0.4625 0.3837 -0.0293 0.0298 0.0220 3 ILE A C 21 O O . ILE A 3 ? 0.3884 0.4703 0.3902 -0.0284 0.0280 0.0211 3 ILE A O 22 C CB . ILE A 3 ? 0.3473 0.4283 0.3481 -0.0328 0.0305 0.0271 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.3588 0.4400 0.3656 -0.0334 0.0296 0.0277 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.3578 0.4355 0.3543 -0.0315 0.0275 0.0275 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.3630 0.4401 0.3675 -0.0349 0.0289 0.0308 3 ILE A CD1 26 N N . CYS A 4 ? 0.4216 0.5082 0.4333 -0.0288 0.0298 0.0211 4 CYS A N 27 C CA . CYS A 4 ? 0.3919 0.4775 0.4062 -0.0270 0.0278 0.0192 4 CYS A CA 28 C C . CYS A 4 ? 0.3970 0.4819 0.4162 -0.0275 0.0257 0.0202 4 CYS A C 29 O O . CYS A 4 ? 0.3895 0.4759 0.4115 -0.0290 0.0266 0.0218 4 CYS A O 30 C CB . CYS A 4 ? 0.4150 0.5038 0.4319 -0.0250 0.0297 0.0168 4 CYS A CB 31 S SG . CYS A 4 ? 0.5909 0.6808 0.6023 -0.0238 0.0327 0.0151 4 CYS A SG 32 N N . ILE A 5 ? 0.3343 0.4169 0.3540 -0.0266 0.0231 0.0193 5 ILE A N 33 C CA . ILE A 5 ? 0.2974 0.3795 0.3218 -0.0267 0.0212 0.0200 5 ILE A CA 34 C C . ILE A 5 ? 0.3724 0.4557 0.4007 -0.0252 0.0213 0.0178 5 ILE A C 35 O O . ILE A 5 ? 0.3800 0.4622 0.4059 -0.0237 0.0216 0.0157 5 ILE A O 36 C CB . ILE A 5 ? 0.3368 0.4160 0.3591 -0.0268 0.0182 0.0206 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.3558 0.4338 0.3745 -0.0278 0.0179 0.0231 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.2999 0.3787 0.3269 -0.0266 0.0163 0.0207 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.3788 0.4564 0.3915 -0.0279 0.0187 0.0231 5 ILE A CD1 40 N N . GLY A 6 ? 0.2700 0.3550 0.3038 -0.0254 0.0212 0.0182 6 GLY A N 41 C CA . GLY A 6 ? 0.2610 0.3475 0.2985 -0.0236 0.0212 0.0164 6 GLY A CA 42 C C . GLY A 6 ? 0.3123 0.3998 0.3553 -0.0241 0.0201 0.0170 6 GLY A C 43 O O . GLY A 6 ? 0.3003 0.3866 0.3440 -0.0258 0.0191 0.0189 6 GLY A O 44 N N . TYR A 7 ? 0.2960 0.3853 0.3424 -0.0223 0.0203 0.0155 7 TYR A N 45 C CA . TYR A 7 ? 0.2928 0.3828 0.3441 -0.0225 0.0190 0.0158 7 TYR A CA 46 C C . TYR A 7 ? 0.3212 0.4167 0.3771 -0.0214 0.0204 0.0149 7 TYR A C 47 O O . TYR A 7 ? 0.2821 0.3804 0.3372 -0.0195 0.0222 0.0135 7 TYR A O 48 C CB . TYR A 7 ? 0.2584 0.3441 0.3090 -0.0215 0.0165 0.0150 7 TYR A CB 49 C CG . TYR A 7 ? 0.2779 0.3612 0.3251 -0.0193 0.0167 0.0129 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.2806 0.3608 0.3222 -0.0196 0.0166 0.0124 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.3196 0.4034 0.3686 -0.0169 0.0168 0.0113 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.3298 0.4068 0.3674 -0.0179 0.0168 0.0104 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.2990 0.3791 0.3436 -0.0147 0.0170 0.0094 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.3329 0.4093 0.3717 -0.0154 0.0171 0.0089 7 TYR A CZ 55 O OH . TYR A 7 ? 0.3341 0.4058 0.3677 -0.0135 0.0174 0.0069 7 TYR A OH 56 N N . HIS A 8 ? 0.3291 0.4262 0.3894 -0.0224 0.0196 0.0156 8 HIS A N 57 C CA . HIS A 8 ? 0.3263 0.4297 0.3916 -0.0218 0.0206 0.0148 8 HIS A CA 58 C C . HIS A 8 ? 0.3446 0.4487 0.4106 -0.0179 0.0203 0.0128 8 HIS A C 59 O O . HIS A 8 ? 0.3429 0.4418 0.4072 -0.0165 0.0184 0.0122 8 HIS A O 60 C CB . HIS A 8 ? 0.3363 0.4400 0.4054 -0.0240 0.0194 0.0160 8 HIS A CB 61 C CG . HIS A 8 ? 0.4018 0.5126 0.4761 -0.0242 0.0203 0.0154 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.4427 0.5600 0.5185 -0.0261 0.0226 0.0156 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.3356 0.4486 0.4139 -0.0231 0.0190 0.0147 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.3917 0.5155 0.4725 -0.0261 0.0228 0.0149 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.4018 0.5230 0.4841 -0.0242 0.0206 0.0144 8 HIS A NE2 66 N N . ALA A 9 ? 0.3286 0.4392 0.3968 -0.0161 0.0222 0.0117 9 ALA A N 67 C CA . ALA A 9 ? 0.3229 0.4353 0.3925 -0.0120 0.0219 0.0100 9 ALA A CA 68 C C . ALA A 9 ? 0.3162 0.4379 0.3918 -0.0121 0.0228 0.0098 9 ALA A C 69 O O . ALA A 9 ? 0.3667 0.4939 0.4445 -0.0151 0.0244 0.0107 9 ALA A O 70 C CB . ALA A 9 ? 0.2947 0.4057 0.3597 -0.0085 0.0233 0.0084 9 ALA A CB 71 N N . ASN A 10 ? 0.3080 0.4318 0.3862 -0.0089 0.0218 0.0087 10 ASN A N 72 C CA . ASN A 10 ? 0.3100 0.4439 0.3942 -0.0088 0.0224 0.0085 10 ASN A CA 73 C C . ASN A 10 ? 0.3042 0.4413 0.3895 -0.0032 0.0221 0.0067 10 ASN A C 74 O O . ASN A 10 ? 0.3350 0.4661 0.4156 0.0007 0.0219 0.0057 10 ASN A O 75 C CB . ASN A 10 ? 0.2246 0.3590 0.3126 -0.0130 0.0209 0.0098 10 ASN A CB 76 C CG . ASN A 10 ? 0.3342 0.4615 0.4215 -0.0119 0.0181 0.0098 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.2777 0.4011 0.3625 -0.0078 0.0173 0.0086 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.2800 0.4052 0.3690 -0.0156 0.0168 0.0110 10 ASN A ND2 79 N N . ASN A 11 ? 0.3066 0.4528 0.3977 -0.0029 0.0219 0.0065 11 ASN A N 80 C CA . ASN A 11 ? 0.3516 0.5022 0.4439 0.0029 0.0216 0.0049 11 ASN A CA 81 C C . ASN A 11 ? 0.3827 0.5274 0.4746 0.0048 0.0188 0.0048 11 ASN A C 82 O O . ASN A 11 ? 0.3859 0.5340 0.4789 0.0095 0.0182 0.0038 11 ASN A O 83 C CB . ASN A 11 ? 0.2992 0.4644 0.3979 0.0028 0.0230 0.0044 11 ASN A CB 84 C CG . ASN A 11 ? 0.4850 0.6549 0.5892 -0.0021 0.0217 0.0054 11 ASN A CG 85 O OD1 . ASN A 11 ? 0.4594 0.6213 0.5623 -0.0056 0.0200 0.0066 11 ASN A OD1 86 N ND2 . ASN A 11 ? 0.5102 0.6933 0.6201 -0.0024 0.0225 0.0048 11 ASN A ND2 87 N N . SER A 12 ? 0.4433 0.5794 0.5335 0.0012 0.0172 0.0060 12 SER A N 88 C CA . SER A 12 ? 0.4320 0.5625 0.5218 0.0022 0.0147 0.0060 12 SER A CA 89 C C . SER A 12 ? 0.4218 0.5453 0.5062 0.0078 0.0141 0.0048 12 SER A C 90 O O . SER A 12 ? 0.3970 0.5146 0.4760 0.0092 0.0151 0.0043 12 SER A O 91 C CB . SER A 12 ? 0.4042 0.5269 0.4926 -0.0025 0.0133 0.0074 12 SER A CB 92 O OG . SER A 12 ? 0.4295 0.5462 0.5168 -0.0015 0.0111 0.0074 12 SER A OG 93 N N . THR A 13 ? 0.3299 0.4538 0.4155 0.0108 0.0125 0.0043 13 THR A N 94 C CA . THR A 13 ? 0.3633 0.4789 0.4430 0.0157 0.0116 0.0034 13 THR A CA 95 C C . THR A 13 ? 0.3605 0.4688 0.4392 0.0140 0.0092 0.0041 13 THR A C 96 O O . THR A 13 ? 0.3693 0.4705 0.4434 0.0174 0.0082 0.0035 13 THR A O 97 C CB . THR A 13 ? 0.3950 0.5172 0.4757 0.0221 0.0119 0.0022 13 THR A CB 98 O OG1 . THR A 13 ? 0.3674 0.4988 0.4550 0.0213 0.0107 0.0026 13 THR A OG1 99 C CG2 . THR A 13 ? 0.3578 0.4871 0.4390 0.0245 0.0145 0.0014 13 THR A CG2 100 N N . THR A 14 ? 0.3627 0.4726 0.4454 0.0087 0.0084 0.0053 14 THR A N 101 C CA . THR A 14 ? 0.3909 0.4947 0.4730 0.0067 0.0063 0.0059 14 THR A CA 102 C C . THR A 14 ? 0.4060 0.4986 0.4819 0.0053 0.0059 0.0061 14 THR A C 103 O O . THR A 14 ? 0.3867 0.4778 0.4610 0.0029 0.0070 0.0064 14 THR A O 104 C CB . THR A 14 ? 0.4123 0.5207 0.4999 0.0017 0.0056 0.0071 14 THR A CB 105 O OG1 . THR A 14 ? 0.4742 0.5933 0.5675 0.0024 0.0058 0.0068 14 THR A OG1 106 C CG2 . THR A 14 ? 0.3842 0.4864 0.4710 0.0001 0.0036 0.0077 14 THR A CG2 107 N N . GLN A 15 ? 0.3195 0.4047 0.3917 0.0067 0.0045 0.0058 15 GLN A N 108 C CA . GLN A 15 ? 0.3367 0.4117 0.4026 0.0053 0.0042 0.0057 15 GLN A CA 109 C C . GLN A 15 ? 0.3096 0.3805 0.3758 0.0019 0.0024 0.0065 15 GLN A C 110 O O . GLN A 15 ? 0.2717 0.3455 0.3415 0.0020 0.0012 0.0069 15 GLN A O 111 C CB . GLN A 15 ? 0.3122 0.3799 0.3710 0.0098 0.0044 0.0045 15 GLN A CB 112 C CG . GLN A 15 ? 0.3676 0.4390 0.4254 0.0142 0.0061 0.0035 15 GLN A CG 113 C CD . GLN A 15 ? 0.4824 0.5457 0.5325 0.0194 0.0062 0.0023 15 GLN A CD 114 O OE1 . GLN A 15 ? 0.5401 0.5992 0.5883 0.0213 0.0048 0.0023 15 GLN A OE1 115 N NE2 . GLN A 15 ? 0.5150 0.5752 0.5601 0.0218 0.0079 0.0012 15 GLN A NE2 116 N N . VAL A 16 ? 0.2839 0.3488 0.3464 -0.0010 0.0023 0.0067 16 VAL A N 117 C CA . VAL A 16 ? 0.2777 0.3385 0.3397 -0.0039 0.0008 0.0073 16 VAL A CA 118 C C . VAL A 16 ? 0.2871 0.3387 0.3416 -0.0041 0.0007 0.0065 16 VAL A C 119 O O . VAL A 16 ? 0.2810 0.3293 0.3308 -0.0026 0.0018 0.0056 16 VAL A O 120 C CB . VAL A 16 ? 0.2583 0.3222 0.3238 -0.0080 0.0006 0.0085 16 VAL A CB 121 C CG1 . VAL A 16 ? 0.2476 0.3194 0.3194 -0.0085 0.0009 0.0093 16 VAL A CG1 122 C CG2 . VAL A 16 ? 0.2032 0.2652 0.2653 -0.0095 0.0016 0.0083 16 VAL A CG2 123 N N . ASP A 17 ? 0.3260 0.3732 0.3789 -0.0061 -0.0006 0.0068 17 ASP A N 124 C CA . ASP A 17 ? 0.3084 0.3473 0.3542 -0.0077 -0.0007 0.0061 17 ASP A CA 125 C C . ASP A 17 ? 0.3489 0.3891 0.3958 -0.0123 -0.0011 0.0067 17 ASP A C 126 O O . ASP A 17 ? 0.3322 0.3778 0.3848 -0.0138 -0.0017 0.0078 17 ASP A O 127 C CB . ASP A 17 ? 0.2909 0.3233 0.3327 -0.0066 -0.0016 0.0058 17 ASP A CB 128 C CG . ASP A 17 ? 0.4780 0.5079 0.5170 -0.0014 -0.0012 0.0051 17 ASP A CG 129 O OD1 . ASP A 17 ? 0.5079 0.5388 0.5457 0.0012 0.0000 0.0044 17 ASP A OD1 130 O OD2 . ASP A 17 ? 0.4722 0.4991 0.5098 0.0004 -0.0021 0.0051 17 ASP A OD2 131 N N . THR A 18 ? 0.3652 0.4006 0.4065 -0.0144 -0.0007 0.0060 18 THR A N 132 C CA . THR A 18 ? 0.3371 0.3737 0.3786 -0.0187 -0.0013 0.0064 18 THR A CA 133 C C . THR A 18 ? 0.3935 0.4226 0.4282 -0.0210 -0.0017 0.0055 18 THR A C 134 O O . THR A 18 ? 0.3694 0.3915 0.3986 -0.0192 -0.0013 0.0046 18 THR A O 135 C CB . THR A 18 ? 0.3150 0.3546 0.3564 -0.0199 -0.0006 0.0064 18 THR A CB 136 O OG1 . THR A 18 ? 0.3649 0.3980 0.3988 -0.0204 0.0001 0.0051 18 THR A OG1 137 C CG2 . THR A 18 ? 0.3194 0.3643 0.3652 -0.0173 0.0003 0.0070 18 THR A CG2 138 N N . LEU A 19 ? 0.3672 0.3978 0.4018 -0.0250 -0.0023 0.0057 19 LEU A N 139 C CA . LEU A 19 ? 0.3746 0.3988 0.4026 -0.0281 -0.0025 0.0047 19 LEU A CA 140 C C . LEU A 19 ? 0.3953 0.4126 0.4153 -0.0286 -0.0016 0.0033 19 LEU A C 141 O O . LEU A 19 ? 0.4237 0.4324 0.4365 -0.0295 -0.0013 0.0023 19 LEU A O 142 C CB . LEU A 19 ? 0.3919 0.4211 0.4221 -0.0323 -0.0034 0.0052 19 LEU A CB 143 C CG . LEU A 19 ? 0.3731 0.4059 0.4081 -0.0327 -0.0043 0.0061 19 LEU A CG 144 C CD1 . LEU A 19 ? 0.4427 0.4823 0.4807 -0.0358 -0.0050 0.0066 19 LEU A CD1 145 C CD2 . LEU A 19 ? 0.3823 0.4080 0.4124 -0.0337 -0.0044 0.0055 19 LEU A CD2 146 N N . LEU A 20 ? 0.3789 0.3992 0.3997 -0.0279 -0.0009 0.0032 20 LEU A N 147 C CA . LEU A 20 ? 0.4101 0.4239 0.4231 -0.0284 0.0001 0.0017 20 LEU A CA 148 C C . LEU A 20 ? 0.4285 0.4374 0.4385 -0.0234 0.0012 0.0011 20 LEU A C 149 O O . LEU A 20 ? 0.4269 0.4281 0.4289 -0.0231 0.0021 -0.0003 20 LEU A O 150 C CB . LEU A 20 ? 0.4079 0.4272 0.4223 -0.0303 0.0002 0.0018 20 LEU A CB 151 C CG . LEU A 20 ? 0.4088 0.4337 0.4253 -0.0349 -0.0009 0.0023 20 LEU A CG 152 C CD1 . LEU A 20 ? 0.4289 0.4601 0.4476 -0.0355 -0.0008 0.0026 20 LEU A CD1 153 C CD2 . LEU A 20 ? 0.3675 0.3862 0.3766 -0.0393 -0.0011 0.0009 20 LEU A CD2 154 N N . GLU A 21 ? 0.4486 0.4619 0.4647 -0.0194 0.0012 0.0020 21 GLU A N 155 C CA . GLU A 21 ? 0.4446 0.4570 0.4598 -0.0144 0.0024 0.0016 21 GLU A CA 156 C C . GLU A 21 ? 0.4285 0.4440 0.4487 -0.0104 0.0020 0.0023 21 GLU A C 157 O O . GLU A 21 ? 0.4049 0.4280 0.4328 -0.0111 0.0012 0.0035 21 GLU A O 158 C CB . GLU A 21 ? 0.4781 0.4975 0.4972 -0.0142 0.0032 0.0019 21 GLU A CB 159 C CG . GLU A 21 ? 0.5924 0.6077 0.6056 -0.0117 0.0048 0.0006 21 GLU A CG 160 C CD . GLU A 21 ? 0.6973 0.7190 0.7134 -0.0128 0.0055 0.0009 21 GLU A CD 161 O OE1 . GLU A 21 ? 0.6463 0.6687 0.6613 -0.0096 0.0069 0.0004 21 GLU A OE1 162 O OE2 . GLU A 21 ? 0.6695 0.6954 0.6885 -0.0167 0.0047 0.0017 21 GLU A OE2 163 N N . LYS A 22 ? 0.3696 0.3793 0.3850 -0.0060 0.0026 0.0015 22 LYS A N 164 C CA . LYS A 22 ? 0.4023 0.4160 0.4223 -0.0016 0.0022 0.0021 22 LYS A CA 165 C C . LYS A 22 ? 0.4098 0.4300 0.4333 0.0025 0.0034 0.0019 22 LYS A C 166 O O . LYS A 22 ? 0.3809 0.3993 0.4007 0.0031 0.0047 0.0010 22 LYS A O 167 C CB . LYS A 22 ? 0.4309 0.4350 0.4437 0.0013 0.0019 0.0015 22 LYS A CB 168 C CG . LYS A 22 ? 0.4808 0.4803 0.4918 -0.0023 0.0006 0.0019 22 LYS A CG 169 C CD . LYS A 22 ? 0.5984 0.5870 0.6009 0.0007 0.0005 0.0013 22 LYS A CD 170 C CE . LYS A 22 ? 0.7138 0.6972 0.7135 -0.0035 -0.0005 0.0017 22 LYS A CE 171 N NZ . LYS A 22 ? 0.8675 0.8382 0.8568 -0.0012 -0.0004 0.0012 22 LYS A NZ 172 N N . ASN A 23 ? 0.4610 0.4889 0.4915 0.0051 0.0030 0.0026 23 ASN A N 173 C CA . ASN A 23 ? 0.4414 0.4767 0.4757 0.0091 0.0041 0.0024 23 ASN A CA 174 C C . ASN A 23 ? 0.4383 0.4784 0.4745 0.0073 0.0055 0.0024 23 ASN A C 175 O O . ASN A 23 ? 0.3932 0.4323 0.4259 0.0102 0.0070 0.0014 23 ASN A O 176 C CB . ASN A 23 ? 0.4519 0.4817 0.4800 0.0153 0.0047 0.0013 23 ASN A CB 177 C CG . ASN A 23 ? 0.6338 0.6621 0.6621 0.0179 0.0033 0.0016 23 ASN A CG 178 O OD1 . ASN A 23 ? 0.6485 0.6828 0.6835 0.0158 0.0020 0.0026 23 ASN A OD1 179 N ND2 . ASN A 23 ? 0.5913 0.6108 0.6115 0.0226 0.0034 0.0007 23 ASN A ND2 180 N N . VAL A 24 ? 0.4105 0.4554 0.4518 0.0027 0.0050 0.0035 24 VAL A N 181 C CA . VAL A 24 ? 0.3605 0.4105 0.4042 0.0007 0.0061 0.0038 24 VAL A CA 182 C C . VAL A 24 ? 0.3579 0.4184 0.4096 0.0014 0.0066 0.0047 24 VAL A C 183 O O . VAL A 24 ? 0.3336 0.3982 0.3907 -0.0004 0.0055 0.0057 24 VAL A O 184 C CB . VAL A 24 ? 0.3547 0.4036 0.3986 -0.0045 0.0053 0.0047 24 VAL A CB 185 C CG1 . VAL A 24 ? 0.3365 0.3899 0.3819 -0.0063 0.0063 0.0051 24 VAL A CG1 186 C CG2 . VAL A 24 ? 0.3815 0.4209 0.4178 -0.0061 0.0047 0.0038 24 VAL A CG2 187 N N . THR A 25 ? 0.3245 0.3895 0.3767 0.0039 0.0083 0.0041 25 THR A N 188 C CA . THR A 25 ? 0.3308 0.4062 0.3901 0.0040 0.0091 0.0048 25 THR A CA 189 C C . THR A 25 ? 0.3268 0.4055 0.3894 -0.0009 0.0092 0.0061 25 THR A C 190 O O . THR A 25 ? 0.2961 0.3720 0.3552 -0.0025 0.0099 0.0062 25 THR A O 191 C CB . THR A 25 ? 0.3851 0.4648 0.4437 0.0079 0.0111 0.0038 25 THR A CB 192 O OG1 . THR A 25 ? 0.4172 0.4929 0.4717 0.0131 0.0110 0.0025 25 THR A OG1 193 C CG2 . THR A 25 ? 0.3096 0.4011 0.3757 0.0076 0.0119 0.0044 25 THR A CG2 194 N N . VAL A 26 ? 0.2763 0.3605 0.3448 -0.0030 0.0085 0.0073 26 VAL A N 195 C CA . VAL A 26 ? 0.2955 0.3818 0.3664 -0.0072 0.0087 0.0087 26 VAL A CA 196 C C . VAL A 26 ? 0.3266 0.4217 0.4029 -0.0082 0.0098 0.0093 26 VAL A C 197 O O . VAL A 26 ? 0.3462 0.4466 0.4261 -0.0065 0.0098 0.0089 26 VAL A O 198 C CB . VAL A 26 ? 0.2920 0.3749 0.3638 -0.0099 0.0067 0.0096 26 VAL A CB 199 C CG1 . VAL A 26 ? 0.2222 0.2973 0.2885 -0.0102 0.0058 0.0092 26 VAL A CG1 200 C CG2 . VAL A 26 ? 0.2483 0.3333 0.3237 -0.0090 0.0055 0.0096 26 VAL A CG2 201 N N . THR A 27 ? 0.2990 0.3956 0.3755 -0.0112 0.0108 0.0103 27 THR A N 202 C CA . THR A 27 ? 0.2702 0.3742 0.3507 -0.0130 0.0122 0.0110 27 THR A CA 203 C C . THR A 27 ? 0.3351 0.4420 0.4202 -0.0152 0.0112 0.0117 27 THR A C 204 O O . THR A 27 ? 0.3979 0.5122 0.4870 -0.0157 0.0120 0.0116 27 THR A O 205 C CB . THR A 27 ? 0.3080 0.4114 0.3865 -0.0159 0.0135 0.0121 27 THR A CB 206 O OG1 . THR A 27 ? 0.2653 0.3635 0.3425 -0.0185 0.0121 0.0134 27 THR A OG1 207 C CG2 . THR A 27 ? 0.2580 0.3589 0.3318 -0.0139 0.0146 0.0112 27 THR A CG2 208 N N . HIS A 28 ? 0.3115 0.4130 0.3959 -0.0167 0.0094 0.0125 28 HIS A N 209 C CA . HIS A 28 ? 0.2688 0.3716 0.3567 -0.0188 0.0083 0.0131 28 HIS A CA 210 C C . HIS A 28 ? 0.3248 0.4219 0.4115 -0.0178 0.0061 0.0130 28 HIS A C 211 O O . HIS A 28 ? 0.2973 0.3887 0.3803 -0.0175 0.0056 0.0130 28 HIS A O 212 C CB . HIS A 28 ? 0.2590 0.3610 0.3468 -0.0228 0.0088 0.0147 28 HIS A CB 213 C CG . HIS A 28 ? 0.3531 0.4596 0.4410 -0.0243 0.0110 0.0150 28 HIS A CG 214 N ND1 . HIS A 28 ? 0.3137 0.4185 0.3981 -0.0239 0.0122 0.0152 28 HIS A ND1 215 C CD2 . HIS A 28 ? 0.2664 0.3795 0.3574 -0.0265 0.0123 0.0151 28 HIS A CD2 216 C CE1 . HIS A 28 ? 0.3729 0.4826 0.4581 -0.0257 0.0142 0.0155 28 HIS A CE1 217 N NE2 . HIS A 28 ? 0.3899 0.5048 0.4791 -0.0275 0.0144 0.0155 28 HIS A NE2 218 N N . SER A 29 ? 0.2700 0.3691 0.3597 -0.0176 0.0050 0.0127 29 SER A N 219 C CA . SER A 29 ? 0.2843 0.3784 0.3730 -0.0170 0.0031 0.0126 29 SER A CA 220 C C . SER A 29 ? 0.3149 0.4115 0.4072 -0.0184 0.0021 0.0128 29 SER A C 221 O O . SER A 29 ? 0.3251 0.4276 0.4206 -0.0199 0.0028 0.0129 29 SER A O 222 C CB . SER A 29 ? 0.2416 0.3335 0.3281 -0.0132 0.0026 0.0113 29 SER A CB 223 O OG . SER A 29 ? 0.2997 0.3974 0.3886 -0.0107 0.0030 0.0105 29 SER A OG 224 N N . VAL A 30 ? 0.3835 0.4760 0.4751 -0.0181 0.0004 0.0128 30 VAL A N 225 C CA . VAL A 30 ? 0.3927 0.4868 0.4871 -0.0195 -0.0006 0.0130 30 VAL A CA 226 C C . VAL A 30 ? 0.3653 0.4564 0.4588 -0.0173 -0.0023 0.0124 30 VAL A C 227 O O . VAL A 30 ? 0.3854 0.4707 0.4758 -0.0167 -0.0029 0.0124 30 VAL A O 228 C CB . VAL A 30 ? 0.3628 0.4539 0.4568 -0.0229 -0.0007 0.0142 30 VAL A CB 229 C CG1 . VAL A 30 ? 0.3254 0.4104 0.4160 -0.0227 -0.0012 0.0148 30 VAL A CG1 230 C CG2 . VAL A 30 ? 0.4132 0.5047 0.5092 -0.0242 -0.0019 0.0142 30 VAL A CG2 231 N N . GLU A 31 ? 0.3860 0.4814 0.4822 -0.0162 -0.0030 0.0117 31 GLU A N 232 C CA . GLU A 31 ? 0.3356 0.4284 0.4307 -0.0140 -0.0046 0.0112 31 GLU A CA 233 C C . GLU A 31 ? 0.3479 0.4384 0.4438 -0.0165 -0.0058 0.0117 31 GLU A C 234 O O . GLU A 31 ? 0.3683 0.4624 0.4669 -0.0189 -0.0058 0.0119 31 GLU A O 235 C CB . GLU A 31 ? 0.3728 0.4717 0.4701 -0.0111 -0.0049 0.0103 31 GLU A CB 236 C CG . GLU A 31 ? 0.4036 0.5004 0.5000 -0.0088 -0.0067 0.0099 31 GLU A CG 237 C CD . GLU A 31 ? 0.4211 0.5097 0.5121 -0.0064 -0.0070 0.0097 31 GLU A CD 238 O OE1 . GLU A 31 ? 0.4308 0.5136 0.5197 -0.0078 -0.0079 0.0101 31 GLU A OE1 239 O OE2 . GLU A 31 ? 0.4325 0.5202 0.5210 -0.0032 -0.0063 0.0091 31 GLU A OE2 240 N N . LEU A 32 ? 0.3746 0.4589 0.4676 -0.0160 -0.0067 0.0118 32 LEU A N 241 C CA . LEU A 32 ? 0.3524 0.4341 0.4455 -0.0180 -0.0077 0.0123 32 LEU A CA 242 C C . LEU A 32 ? 0.3507 0.4324 0.4441 -0.0167 -0.0092 0.0117 32 LEU A C 243 O O . LEU A 32 ? 0.3585 0.4387 0.4522 -0.0183 -0.0101 0.0119 32 LEU A O 244 C CB . LEU A 32 ? 0.3340 0.4098 0.4239 -0.0187 -0.0077 0.0128 32 LEU A CB 245 C CG . LEU A 32 ? 0.3526 0.4276 0.4414 -0.0198 -0.0065 0.0134 32 LEU A CG 246 C CD1 . LEU A 32 ? 0.3244 0.3947 0.4102 -0.0201 -0.0069 0.0137 32 LEU A CD1 247 C CD2 . LEU A 32 ? 0.2731 0.3501 0.3638 -0.0221 -0.0059 0.0142 32 LEU A CD2 248 N N . LEU A 33 ? 0.3560 0.4390 0.4487 -0.0135 -0.0096 0.0110 33 LEU A N 249 C CA . LEU A 33 ? 0.3804 0.4627 0.4725 -0.0117 -0.0111 0.0106 33 LEU A CA 250 C C . LEU A 33 ? 0.3973 0.4873 0.4929 -0.0104 -0.0117 0.0100 33 LEU A C 251 O O . LEU A 33 ? 0.4853 0.5803 0.5824 -0.0086 -0.0109 0.0096 33 LEU A O 252 C CB . LEU A 33 ? 0.4124 0.4891 0.4998 -0.0086 -0.0113 0.0103 33 LEU A CB 253 C CG . LEU A 33 ? 0.3967 0.4709 0.4819 -0.0064 -0.0128 0.0100 33 LEU A CG 254 C CD1 . LEU A 33 ? 0.3838 0.4493 0.4634 -0.0062 -0.0128 0.0101 33 LEU A CD1 255 C CD2 . LEU A 33 ? 0.3714 0.4497 0.4570 -0.0023 -0.0132 0.0094 33 LEU A CD2 256 N N . GLU A 34 ? 0.4112 0.5026 0.5082 -0.0113 -0.0130 0.0099 34 GLU A N 257 C CA . GLU A 34 ? 0.4172 0.5165 0.5174 -0.0101 -0.0140 0.0092 34 GLU A CA 258 C C . GLU A 34 ? 0.3841 0.4817 0.4817 -0.0057 -0.0154 0.0088 34 GLU A C 259 O O . GLU A 34 ? 0.3764 0.4679 0.4710 -0.0056 -0.0164 0.0091 34 GLU A O 260 C CB . GLU A 34 ? 0.4200 0.5223 0.5229 -0.0139 -0.0147 0.0092 34 GLU A CB 261 C CG . GLU A 34 ? 0.4097 0.5218 0.5165 -0.0134 -0.0156 0.0084 34 GLU A CG 262 C CD . GLU A 34 ? 0.5511 0.6710 0.6607 -0.0121 -0.0144 0.0080 34 GLU A CD 263 O OE1 . GLU A 34 ? 0.5818 0.7061 0.6941 -0.0158 -0.0132 0.0081 34 GLU A OE1 264 O OE2 . GLU A 34 ? 0.5460 0.6674 0.6546 -0.0074 -0.0145 0.0077 34 GLU A OE2 265 N N . ASN A 35 ? 0.3411 0.4444 0.4397 -0.0019 -0.0154 0.0083 35 ASN A N 266 C CA . ASN A 35 ? 0.3820 0.4841 0.4778 0.0029 -0.0169 0.0080 35 ASN A CA 267 C C . ASN A 35 ? 0.3767 0.4891 0.4765 0.0043 -0.0183 0.0073 35 ASN A C 268 O O . ASN A 35 ? 0.4052 0.5180 0.5029 0.0089 -0.0196 0.0071 35 ASN A O 269 C CB . ASN A 35 ? 0.3499 0.4485 0.4418 0.0074 -0.0159 0.0078 35 ASN A CB 270 C CG . ASN A 35 ? 0.4462 0.5534 0.5417 0.0087 -0.0146 0.0073 35 ASN A CG 271 O OD1 . ASN A 35 ? 0.4155 0.5310 0.5164 0.0054 -0.0141 0.0072 35 ASN A OD1 272 N ND2 . ASN A 35 ? 0.4039 0.5085 0.4958 0.0131 -0.0137 0.0070 35 ASN A ND2 273 N N . GLN A 36 ? 0.3716 0.4918 0.4766 0.0002 -0.0181 0.0071 36 GLN A N 274 C CA . GLN A 36 ? 0.4210 0.5527 0.5305 0.0006 -0.0193 0.0063 36 GLN A CA 275 C C . GLN A 36 ? 0.4266 0.5586 0.5371 -0.0030 -0.0209 0.0062 36 GLN A C 276 O O . GLN A 36 ? 0.3876 0.5143 0.4976 -0.0077 -0.0204 0.0067 36 GLN A O 277 C CB . GLN A 36 ? 0.4435 0.5849 0.5580 -0.0019 -0.0177 0.0060 36 GLN A CB 278 C CG . GLN A 36 ? 0.5878 0.7409 0.7055 0.0023 -0.0179 0.0051 36 GLN A CG 279 C CD . GLN A 36 ? 0.5729 0.7221 0.6867 0.0089 -0.0173 0.0052 36 GLN A CD 280 O OE1 . GLN A 36 ? 0.5826 0.7217 0.6923 0.0092 -0.0162 0.0057 36 GLN A OE1 281 N NE2 . GLN A 36 ? 0.6463 0.8036 0.7612 0.0144 -0.0182 0.0045 36 GLN A NE2 282 N N . LYS A 37 ? 0.4520 0.5902 0.5636 -0.0007 -0.0229 0.0057 37 LYS A N 283 C CA . LYS A 37 ? 0.4604 0.6001 0.5730 -0.0041 -0.0246 0.0053 37 LYS A CA 284 C C . LYS A 37 ? 0.4566 0.6100 0.5737 -0.0036 -0.0261 0.0043 37 LYS A C 285 O O . LYS A 37 ? 0.5292 0.6898 0.6476 0.0013 -0.0264 0.0040 37 LYS A O 286 C CB . LYS A 37 ? 0.4340 0.5638 0.5414 -0.0022 -0.0260 0.0058 37 LYS A CB 287 C CG . LYS A 37 ? 0.3828 0.5133 0.4875 0.0044 -0.0276 0.0058 37 LYS A CG 288 C CD . LYS A 37 ? 0.5333 0.6565 0.6337 0.0088 -0.0263 0.0063 37 LYS A CD 289 C CE . LYS A 37 ? 0.5077 0.6319 0.6050 0.0160 -0.0276 0.0062 37 LYS A CE 290 N NZ . LYS A 37 ? 0.5648 0.6833 0.6578 0.0173 -0.0296 0.0065 37 LYS A NZ 291 N N . GLU A 38 ? 0.4919 0.6490 0.6112 -0.0088 -0.0270 0.0038 38 GLU A N 292 C CA . GLU A 38 ? 0.4678 0.6376 0.5909 -0.0088 -0.0289 0.0028 38 GLU A CA 293 C C . GLU A 38 ? 0.4874 0.6537 0.6071 -0.0056 -0.0314 0.0028 38 GLU A C 294 O O . GLU A 38 ? 0.4983 0.6566 0.6152 -0.0088 -0.0320 0.0030 38 GLU A O 295 C CB . GLU A 38 ? 0.5180 0.6930 0.6443 -0.0165 -0.0286 0.0020 38 GLU A CB 296 C CG . GLU A 38 ? 0.4947 0.6727 0.6237 -0.0205 -0.0260 0.0021 38 GLU A CG 297 C CD . GLU A 38 ? 0.6050 0.7845 0.7352 -0.0286 -0.0256 0.0016 38 GLU A CD 298 O OE1 . GLU A 38 ? 0.5614 0.7385 0.6900 -0.0313 -0.0272 0.0011 38 GLU A OE1 299 O OE2 . GLU A 38 ? 0.6564 0.8390 0.7886 -0.0325 -0.0236 0.0016 38 GLU A OE2 300 N N . LYS A 39 ? 0.4614 0.6333 0.5810 0.0008 -0.0328 0.0026 39 LYS A N 301 C CA . LYS A 39 ? 0.4609 0.6283 0.5762 0.0047 -0.0352 0.0028 39 LYS A CA 302 C C . LYS A 39 ? 0.4964 0.6708 0.6137 0.0012 -0.0374 0.0019 39 LYS A C 303 O O . LYS A 39 ? 0.4770 0.6623 0.5964 0.0044 -0.0395 0.0013 39 LYS A O 304 C CB . LYS A 39 ? 0.4282 0.5986 0.5418 0.0132 -0.0360 0.0030 39 LYS A CB 305 C CG . LYS A 39 ? 0.5432 0.7082 0.6549 0.0165 -0.0337 0.0036 39 LYS A CG 306 C CD . LYS A 39 ? 0.5936 0.7491 0.6984 0.0237 -0.0342 0.0044 39 LYS A CD 307 C CE . LYS A 39 ? 0.7235 0.8881 0.8283 0.0306 -0.0364 0.0040 39 LYS A CE 308 N NZ . LYS A 39 ? 0.7690 0.9223 0.8655 0.0374 -0.0372 0.0049 39 LYS A NZ 309 N N . ARG A 40 ? 0.4580 0.6261 0.5744 -0.0050 -0.0371 0.0019 40 ARG A N 310 C CA . ARG A 40 ? 0.4333 0.6063 0.5508 -0.0094 -0.0390 0.0009 40 ARG A CA 311 C C . ARG A 40 ? 0.4381 0.5996 0.5524 -0.0149 -0.0382 0.0011 40 ARG A C 312 O O . ARG A 40 ? 0.4002 0.5524 0.5128 -0.0163 -0.0361 0.0019 40 ARG A O 313 C CB . ARG A 40 ? 0.4490 0.6368 0.5728 -0.0136 -0.0389 -0.0003 40 ARG A CB 314 C CG . ARG A 40 ? 0.4822 0.6677 0.6078 -0.0192 -0.0361 -0.0002 40 ARG A CG 315 C CD . ARG A 40 ? 0.5452 0.7456 0.6767 -0.0234 -0.0358 -0.0014 40 ARG A CD 316 N NE . ARG A 40 ? 0.5823 0.7794 0.7145 -0.0293 -0.0331 -0.0012 40 ARG A NE 317 C CZ . ARG A 40 ? 0.6166 0.8236 0.7528 -0.0350 -0.0323 -0.0021 40 ARG A CZ 318 N NH1 . ARG A 40 ? 0.5759 0.7979 0.7162 -0.0359 -0.0340 -0.0034 40 ARG A NH1 319 N NH2 . ARG A 40 ? 0.5746 0.7767 0.7104 -0.0401 -0.0298 -0.0017 40 ARG A NH2 320 N N . PHE A 41 ? 0.4727 0.6350 0.5859 -0.0180 -0.0400 0.0004 41 PHE A N 321 C CA . PHE A 41 ? 0.4279 0.5804 0.5381 -0.0235 -0.0393 0.0003 41 PHE A CA 322 C C . PHE A 41 ? 0.4508 0.6093 0.5641 -0.0308 -0.0388 -0.0008 41 PHE A C 323 O O . PHE A 41 ? 0.5089 0.6798 0.6258 -0.0323 -0.0402 -0.0020 41 PHE A O 324 C CB . PHE A 41 ? 0.3708 0.5180 0.4767 -0.0224 -0.0414 0.0002 41 PHE A CB 325 C CG . PHE A 41 ? 0.3678 0.5061 0.4692 -0.0165 -0.0414 0.0014 41 PHE A CG 326 C CD1 . PHE A 41 ? 0.3630 0.4898 0.4615 -0.0164 -0.0393 0.0024 41 PHE A CD1 327 C CD2 . PHE A 41 ? 0.3530 0.4943 0.4527 -0.0112 -0.0437 0.0015 41 PHE A CD2 328 C CE1 . PHE A 41 ? 0.3512 0.4699 0.4453 -0.0117 -0.0392 0.0035 41 PHE A CE1 329 C CE2 . PHE A 41 ? 0.3887 0.5207 0.4834 -0.0061 -0.0436 0.0027 41 PHE A CE2 330 C CZ . PHE A 41 ? 0.3508 0.4716 0.4427 -0.0067 -0.0413 0.0036 41 PHE A CZ 331 N N . CYS A 42 ? 0.3762 0.5259 0.4877 -0.0352 -0.0367 -0.0005 42 CYS A N 332 C CA . CYS A 42 ? 0.3876 0.5401 0.5004 -0.0425 -0.0359 -0.0014 42 CYS A CA 333 C C . CYS A 42 ? 0.4219 0.5628 0.5296 -0.0466 -0.0355 -0.0016 42 CYS A C 334 O O . CYS A 42 ? 0.3791 0.5112 0.4829 -0.0438 -0.0360 -0.0011 42 CYS A O 335 C CB . CYS A 42 ? 0.4117 0.5648 0.5268 -0.0439 -0.0332 -0.0008 42 CYS A CB 336 S SG . CYS A 42 ? 0.6018 0.7686 0.7227 -0.0393 -0.0331 -0.0007 42 CYS A SG 337 N N . LYS A 43 ? 0.4481 0.5887 0.5554 -0.0533 -0.0346 -0.0023 43 LYS A N 338 C CA . LYS A 43 ? 0.4663 0.5951 0.5680 -0.0573 -0.0339 -0.0026 43 LYS A CA 339 C C . LYS A 43 ? 0.4910 0.6081 0.5900 -0.0564 -0.0314 -0.0012 43 LYS A C 340 O O . LYS A 43 ? 0.4832 0.6022 0.5846 -0.0557 -0.0297 -0.0004 43 LYS A O 341 C CB . LYS A 43 ? 0.5213 0.6534 0.6225 -0.0651 -0.0340 -0.0040 43 LYS A CB 342 C CG . LYS A 43 ? 0.5916 0.7350 0.6949 -0.0666 -0.0367 -0.0056 43 LYS A CG 343 C CD . LYS A 43 ? 0.6239 0.7704 0.7261 -0.0752 -0.0367 -0.0072 43 LYS A CD 344 C CE . LYS A 43 ? 0.7833 0.9430 0.8912 -0.0781 -0.0360 -0.0076 43 LYS A CE 345 N NZ . LYS A 43 ? 0.9563 1.1198 1.0630 -0.0872 -0.0360 -0.0092 43 LYS A NZ 346 N N . ILE A 44 ? 0.4540 0.5596 0.5477 -0.0563 -0.0311 -0.0010 44 ILE A N 347 C CA . ILE A 44 ? 0.4310 0.5257 0.5217 -0.0553 -0.0290 0.0002 44 ILE A CA 348 C C . ILE A 44 ? 0.5014 0.5874 0.5868 -0.0604 -0.0281 -0.0004 44 ILE A C 349 O O . ILE A 44 ? 0.4851 0.5678 0.5672 -0.0616 -0.0294 -0.0013 44 ILE A O 350 C CB . ILE A 44 ? 0.4369 0.5256 0.5257 -0.0498 -0.0293 0.0011 44 ILE A CB 351 C CG1 . ILE A 44 ? 0.4245 0.5196 0.5171 -0.0447 -0.0298 0.0018 44 ILE A CG1 352 C CG2 . ILE A 44 ? 0.3567 0.4345 0.4419 -0.0492 -0.0272 0.0021 44 ILE A CG2 353 C CD1 . ILE A 44 ? 0.3818 0.4792 0.4774 -0.0441 -0.0279 0.0027 44 ILE A CD1 354 N N . MET A 45 ? 0.7024 0.7840 0.7865 -0.0631 -0.0260 0.0002 45 MET A N 355 C CA . MET A 45 ? 0.7378 0.8104 0.8160 -0.0682 -0.0250 -0.0004 45 MET A CA 356 C C . MET A 45 ? 0.7740 0.8523 0.8520 -0.0739 -0.0265 -0.0022 45 MET A C 357 O O . MET A 45 ? 0.7578 0.8293 0.8305 -0.0769 -0.0269 -0.0032 45 MET A O 358 C CB . MET A 45 ? 0.7899 0.8507 0.8624 -0.0658 -0.0248 -0.0002 45 MET A CB 359 C CG . MET A 45 ? 0.8603 0.9165 0.9330 -0.0603 -0.0236 0.0014 45 MET A CG 360 S SD . MET A 45 ? 1.1599 1.2083 1.2297 -0.0613 -0.0208 0.0028 45 MET A SD 361 C CE . MET A 45 ? 1.0531 1.0874 1.1142 -0.0619 -0.0201 0.0024 45 MET A CE 362 N N . ASN A 46 ? 0.7376 0.8287 0.8213 -0.0754 -0.0271 -0.0026 46 ASN A N 363 C CA . ASN A 46 ? 0.7554 0.8555 0.8405 -0.0805 -0.0288 -0.0043 46 ASN A CA 364 C C . ASN A 46 ? 0.7161 0.8157 0.7991 -0.0798 -0.0312 -0.0055 46 ASN A C 365 O O . ASN A 46 ? 0.7021 0.8040 0.7832 -0.0853 -0.0323 -0.0071 46 ASN A O 366 C CB . ASN A 46 ? 0.8230 0.9197 0.9044 -0.0885 -0.0273 -0.0051 46 ASN A CB 367 C CG . ASN A 46 ? 0.9667 1.0774 1.0522 -0.0941 -0.0284 -0.0066 46 ASN A CG 368 O OD1 . ASN A 46 ? 0.9675 1.0777 1.0496 -0.0998 -0.0294 -0.0083 46 ASN A OD1 369 N ND2 . ASN A 46 ? 0.8563 0.9798 0.9488 -0.0924 -0.0283 -0.0062 46 ASN A ND2 370 N N . LYS A 47 ? 0.6982 0.7949 0.7813 -0.0734 -0.0319 -0.0047 47 LYS A N 371 C CA . LYS A 47 ? 0.6021 0.6980 0.6830 -0.0720 -0.0341 -0.0056 47 LYS A CA 372 C C . LYS A 47 ? 0.5682 0.6746 0.6543 -0.0665 -0.0361 -0.0053 47 LYS A C 373 O O . LYS A 47 ? 0.5850 0.6912 0.6734 -0.0612 -0.0354 -0.0039 47 LYS A O 374 C CB . LYS A 47 ? 0.6368 0.7187 0.7117 -0.0695 -0.0332 -0.0050 47 LYS A CB 375 C CG . LYS A 47 ? 0.6761 0.7557 0.7477 -0.0686 -0.0352 -0.0060 47 LYS A CG 376 C CD . LYS A 47 ? 0.6665 0.7319 0.7313 -0.0676 -0.0339 -0.0058 47 LYS A CD 377 C CE . LYS A 47 ? 0.7347 0.7980 0.7957 -0.0675 -0.0358 -0.0070 47 LYS A CE 378 N NZ . LYS A 47 ? 0.7504 0.8005 0.8046 -0.0667 -0.0345 -0.0070 47 LYS A NZ 379 N N . ALA A 48 ? 0.5087 0.6240 0.5962 -0.0679 -0.0386 -0.0066 48 ALA A N 380 C CA . ALA A 48 ? 0.4844 0.6101 0.5763 -0.0626 -0.0407 -0.0064 48 ALA A CA 381 C C . ALA A 48 ? 0.4189 0.5374 0.5077 -0.0568 -0.0415 -0.0055 48 ALA A C 382 O O . ALA A 48 ? 0.4335 0.5421 0.5169 -0.0578 -0.0414 -0.0058 48 ALA A O 383 C CB . ALA A 48 ? 0.4865 0.6242 0.5803 -0.0659 -0.0433 -0.0081 48 ALA A CB 384 N N . PRO A 49 ? 0.3449 0.4682 0.4366 -0.0505 -0.0421 -0.0045 49 PRO A N 385 C CA . PRO A 49 ? 0.3583 0.4756 0.4467 -0.0453 -0.0430 -0.0037 49 PRO A CA 386 C C . PRO A 49 ? 0.4163 0.5385 0.5033 -0.0450 -0.0460 -0.0048 49 PRO A C 387 O O . PRO A 49 ? 0.3784 0.5110 0.4681 -0.0480 -0.0476 -0.0061 49 PRO A O 388 C CB . PRO A 49 ? 0.2828 0.4038 0.3744 -0.0393 -0.0427 -0.0024 49 PRO A CB 389 C CG . PRO A 49 ? 0.2829 0.4168 0.3802 -0.0407 -0.0430 -0.0030 49 PRO A CG 390 C CD . PRO A 49 ? 0.2855 0.4186 0.3829 -0.0480 -0.0418 -0.0039 49 PRO A CD 391 N N . LEU A 50 ? 0.3851 0.5002 0.4677 -0.0416 -0.0467 -0.0043 50 LEU A N 392 C CA . LEU A 50 ? 0.3424 0.4614 0.4230 -0.0406 -0.0496 -0.0051 50 LEU A CA 393 C C . LEU A 50 ? 0.3948 0.5194 0.4768 -0.0338 -0.0512 -0.0041 50 LEU A C 394 O O . LEU A 50 ? 0.4355 0.5525 0.5148 -0.0293 -0.0503 -0.0027 50 LEU A O 395 C CB . LEU A 50 ? 0.4082 0.5157 0.4824 -0.0412 -0.0495 -0.0052 50 LEU A CB 396 C CG . LEU A 50 ? 0.4256 0.5352 0.4966 -0.0400 -0.0523 -0.0059 50 LEU A CG 397 C CD1 . LEU A 50 ? 0.3763 0.4955 0.4491 -0.0449 -0.0544 -0.0078 50 LEU A CD1 398 C CD2 . LEU A 50 ? 0.3670 0.4645 0.4313 -0.0403 -0.0517 -0.0059 50 LEU A CD2 399 N N . ASP A 51 ? 0.4694 0.6071 0.5551 -0.0330 -0.0535 -0.0048 51 ASP A N 400 C CA . ASP A 51 ? 0.4107 0.5537 0.4968 -0.0259 -0.0553 -0.0039 51 ASP A CA 401 C C . ASP A 51 ? 0.4557 0.5964 0.5368 -0.0240 -0.0578 -0.0041 51 ASP A C 402 O O . ASP A 51 ? 0.5120 0.6581 0.5929 -0.0276 -0.0598 -0.0056 51 ASP A O 403 C CB . ASP A 51 ? 0.4205 0.5796 0.5128 -0.0252 -0.0567 -0.0046 51 ASP A CB 404 C CG . ASP A 51 ? 0.4841 0.6479 0.5770 -0.0170 -0.0579 -0.0035 51 ASP A CG 405 O OD1 . ASP A 51 ? 0.4777 0.6316 0.5655 -0.0122 -0.0578 -0.0021 51 ASP A OD1 406 O OD2 . ASP A 51 ? 0.5000 0.6773 0.5979 -0.0153 -0.0590 -0.0040 51 ASP A OD2 407 N N . LEU A 52 ? 0.4490 0.5817 0.5257 -0.0185 -0.0577 -0.0026 52 LEU A N 408 C CA . LEU A 52 ? 0.4857 0.6151 0.5568 -0.0162 -0.0599 -0.0026 52 LEU A CA 409 C C . LEU A 52 ? 0.4849 0.6266 0.5577 -0.0117 -0.0632 -0.0028 52 LEU A C 410 O O . LEU A 52 ? 0.4361 0.5802 0.5059 -0.0114 -0.0658 -0.0033 52 LEU A O 411 C CB . LEU A 52 ? 0.4660 0.5812 0.5311 -0.0134 -0.0583 -0.0011 52 LEU A CB 412 C CG . LEU A 52 ? 0.4236 0.5282 0.4866 -0.0181 -0.0557 -0.0013 52 LEU A CG 413 C CD1 . LEU A 52 ? 0.4016 0.4940 0.4585 -0.0152 -0.0544 0.0001 52 LEU A CD1 414 C CD2 . LEU A 52 ? 0.4222 0.5276 0.4840 -0.0236 -0.0567 -0.0030 52 LEU A CD2 415 N N . LYS A 53 ? 0.4194 0.5690 0.4968 -0.0081 -0.0630 -0.0023 53 LYS A N 416 C CA . LYS A 53 ? 0.5029 0.6638 0.5816 -0.0023 -0.0658 -0.0022 53 LYS A CA 417 C C . LYS A 53 ? 0.5335 0.6862 0.6047 0.0040 -0.0672 -0.0008 53 LYS A C 418 O O . LYS A 53 ? 0.4996 0.6405 0.5666 0.0071 -0.0653 0.0007 53 LYS A O 419 C CB . LYS A 53 ? 0.4937 0.6689 0.5761 -0.0061 -0.0685 -0.0041 53 LYS A CB 420 C CG . LYS A 53 ? 0.5440 0.7319 0.6343 -0.0101 -0.0678 -0.0053 53 LYS A CG 421 C CD . LYS A 53 ? 0.5824 0.7749 0.6744 -0.0189 -0.0684 -0.0073 53 LYS A CD 422 C CE . LYS A 53 ? 0.6991 0.9037 0.7985 -0.0236 -0.0673 -0.0084 53 LYS A CE 423 N NZ . LYS A 53 ? 0.7105 0.9166 0.8103 -0.0331 -0.0673 -0.0103 53 LYS A NZ 424 N N . ASP A 54 ? 0.4867 0.6455 0.5559 0.0057 -0.0705 -0.0013 54 ASP A N 425 C CA . ASP A 54 ? 0.5200 0.6727 0.5819 0.0125 -0.0721 0.0001 54 ASP A CA 426 C C . ASP A 54 ? 0.5029 0.6418 0.5576 0.0101 -0.0716 0.0005 54 ASP A C 427 O O . ASP A 54 ? 0.5308 0.6642 0.5787 0.0145 -0.0732 0.0015 54 ASP A O 428 C CB . ASP A 54 ? 0.5174 0.6839 0.5803 0.0167 -0.0761 -0.0004 54 ASP A CB 429 C CG . ASP A 54 ? 0.7374 0.8989 0.7934 0.0257 -0.0776 0.0013 54 ASP A CG 430 O OD1 . ASP A 54 ? 0.6810 0.8318 0.7334 0.0296 -0.0754 0.0029 54 ASP A OD1 431 O OD2 . ASP A 54 ? 0.8438 1.0116 0.8973 0.0288 -0.0810 0.0012 54 ASP A OD2 432 N N . CYS A 55 ? 0.5117 0.6447 0.5675 0.0032 -0.0693 -0.0003 55 CYS A N 433 C CA . CYS A 55 ? 0.5166 0.6364 0.5659 0.0009 -0.0683 0.0000 55 CYS A CA 434 C C . CYS A 55 ? 0.4987 0.6060 0.5462 0.0008 -0.0646 0.0013 55 CYS A C 435 O O . CYS A 55 ? 0.4846 0.5936 0.5371 -0.0006 -0.0626 0.0013 55 CYS A O 436 C CB . CYS A 55 ? 0.4872 0.6086 0.5378 -0.0066 -0.0684 -0.0019 55 CYS A CB 437 S SG . CYS A 55 ? 0.7790 0.9124 0.8293 -0.0075 -0.0729 -0.0036 55 CYS A SG 438 N N . THR A 56 ? 0.4718 0.5672 0.5121 0.0022 -0.0638 0.0023 56 THR A N 439 C CA . THR A 56 ? 0.4524 0.5363 0.4906 0.0011 -0.0604 0.0033 56 THR A CA 440 C C . THR A 56 ? 0.4939 0.5739 0.5326 -0.0053 -0.0588 0.0021 56 THR A C 441 O O . THR A 56 ? 0.5186 0.6032 0.5578 -0.0084 -0.0605 0.0007 56 THR A O 442 C CB . THR A 56 ? 0.5025 0.5755 0.5324 0.0051 -0.0600 0.0050 56 THR A CB 443 O OG1 . THR A 56 ? 0.4892 0.5578 0.5137 0.0033 -0.0610 0.0046 56 THR A OG1 444 C CG2 . THR A 56 ? 0.4931 0.5689 0.5207 0.0119 -0.0620 0.0061 56 THR A CG2 445 N N . ILE A 57 ? 0.5026 0.5743 0.5408 -0.0070 -0.0557 0.0027 57 ILE A N 446 C CA . ILE A 57 ? 0.4972 0.5643 0.5351 -0.0122 -0.0540 0.0017 57 ILE A CA 447 C C . ILE A 57 ? 0.4876 0.5503 0.5194 -0.0131 -0.0552 0.0012 57 ILE A C 448 O O . ILE A 57 ? 0.4701 0.5341 0.5021 -0.0171 -0.0556 -0.0003 57 ILE A O 449 C CB . ILE A 57 ? 0.4911 0.5502 0.5288 -0.0130 -0.0505 0.0026 57 ILE A CB 450 C CG1 . ILE A 57 ? 0.5096 0.5734 0.5537 -0.0133 -0.0493 0.0027 57 ILE A CG1 451 C CG2 . ILE A 57 ? 0.4258 0.4793 0.4618 -0.0171 -0.0488 0.0017 57 ILE A CG2 452 C CD1 . ILE A 57 ? 0.5664 0.6235 0.6108 -0.0140 -0.0461 0.0035 57 ILE A CD1 453 N N . GLU A 58 ? 0.4749 0.5323 0.5007 -0.0093 -0.0557 0.0024 58 GLU A N 454 C CA . GLU A 58 ? 0.5277 0.5806 0.5471 -0.0098 -0.0567 0.0022 58 GLU A CA 455 C C . GLU A 58 ? 0.5072 0.5682 0.5271 -0.0104 -0.0601 0.0008 58 GLU A C 456 O O . GLU A 58 ? 0.4961 0.5557 0.5135 -0.0137 -0.0606 -0.0005 58 GLU A O 457 C CB . GLU A 58 ? 0.5380 0.5834 0.5503 -0.0056 -0.0566 0.0040 58 GLU A CB 458 C CG . GLU A 58 ? 0.5591 0.5967 0.5704 -0.0054 -0.0533 0.0052 58 GLU A CG 459 C CD . GLU A 58 ? 0.6432 0.6820 0.6561 -0.0015 -0.0532 0.0065 58 GLU A CD 460 O OE1 . GLU A 58 ? 0.5637 0.6090 0.5835 -0.0020 -0.0530 0.0060 58 GLU A OE1 461 O OE2 . GLU A 58 ? 0.6397 0.6724 0.6465 0.0020 -0.0533 0.0079 58 GLU A OE2 462 N N . GLY A 59 ? 0.4855 0.5553 0.5082 -0.0072 -0.0625 0.0011 59 GLY A N 463 C CA . GLY A 59 ? 0.4939 0.5734 0.5178 -0.0076 -0.0660 -0.0002 59 GLY A CA 464 C C . GLY A 59 ? 0.4991 0.5844 0.5279 -0.0138 -0.0659 -0.0024 59 GLY A C 465 O O . GLY A 59 ? 0.4672 0.5557 0.4944 -0.0166 -0.0679 -0.0038 59 GLY A O 466 N N . TRP A 60 ? 0.4401 0.5263 0.4744 -0.0161 -0.0636 -0.0025 60 TRP A N 467 C CA . TRP A 60 ? 0.3986 0.4884 0.4368 -0.0222 -0.0631 -0.0043 60 TRP A CA 468 C C . TRP A 60 ? 0.4369 0.5175 0.4703 -0.0263 -0.0617 -0.0053 60 TRP A C 469 O O . TRP A 60 ? 0.4797 0.5627 0.5121 -0.0305 -0.0631 -0.0071 60 TRP A O 470 C CB . TRP A 60 ? 0.3717 0.4629 0.4159 -0.0233 -0.0607 -0.0040 60 TRP A CB 471 C CG . TRP A 60 ? 0.4082 0.4975 0.4542 -0.0295 -0.0589 -0.0054 60 TRP A CG 472 C CD1 . TRP A 60 ? 0.4994 0.5931 0.5458 -0.0347 -0.0602 -0.0073 60 TRP A CD1 473 C CD2 . TRP A 60 ? 0.4305 0.5127 0.4776 -0.0311 -0.0555 -0.0049 60 TRP A CD2 474 N NE1 . TRP A 60 ? 0.4551 0.5436 0.5021 -0.0393 -0.0577 -0.0080 60 TRP A NE1 475 C CE2 . TRP A 60 ? 0.4274 0.5092 0.4751 -0.0369 -0.0549 -0.0065 60 TRP A CE2 476 C CE3 . TRP A 60 ? 0.4356 0.5117 0.4829 -0.0282 -0.0531 -0.0033 60 TRP A CE3 477 C CZ2 . TRP A 60 ? 0.3813 0.4565 0.4295 -0.0394 -0.0519 -0.0064 60 TRP A CZ2 478 C CZ3 . TRP A 60 ? 0.3852 0.4561 0.4337 -0.0308 -0.0502 -0.0033 60 TRP A CZ3 479 C CH2 . TRP A 60 ? 0.3741 0.4444 0.4230 -0.0361 -0.0497 -0.0048 60 TRP A CH2 480 N N . ILE A 61 ? 0.4291 0.4991 0.4591 -0.0251 -0.0591 -0.0042 61 ILE A N 481 C CA . ILE A 61 ? 0.4146 0.4761 0.4407 -0.0286 -0.0572 -0.0051 61 ILE A CA 482 C C . ILE A 61 ? 0.4379 0.4953 0.4570 -0.0282 -0.0586 -0.0056 61 ILE A C 483 O O . ILE A 61 ? 0.4915 0.5438 0.5070 -0.0315 -0.0579 -0.0069 61 ILE A O 484 C CB . ILE A 61 ? 0.4195 0.4728 0.4456 -0.0278 -0.0536 -0.0039 61 ILE A CB 485 C CG1 . ILE A 61 ? 0.4340 0.4818 0.4593 -0.0320 -0.0514 -0.0052 61 ILE A CG1 486 C CG2 . ILE A 61 ? 0.4139 0.4603 0.4346 -0.0242 -0.0528 -0.0025 61 ILE A CG2 487 C CD1 . ILE A 61 ? 0.4863 0.5391 0.5167 -0.0356 -0.0513 -0.0062 61 ILE A CD1 488 N N . LEU A 62 ? 0.4547 0.5139 0.4712 -0.0240 -0.0607 -0.0045 62 LEU A N 489 C CA . LEU A 62 ? 0.4937 0.5497 0.5033 -0.0234 -0.0623 -0.0048 62 LEU A CA 490 C C . LEU A 62 ? 0.5048 0.5693 0.5150 -0.0258 -0.0657 -0.0066 62 LEU A C 491 O O . LEU A 62 ? 0.5221 0.5840 0.5269 -0.0275 -0.0668 -0.0077 62 LEU A O 492 C CB . LEU A 62 ? 0.4742 0.5276 0.4795 -0.0179 -0.0631 -0.0028 62 LEU A CB 493 C CG . LEU A 62 ? 0.5253 0.5685 0.5272 -0.0163 -0.0599 -0.0012 62 LEU A CG 494 C CD1 . LEU A 62 ? 0.5089 0.5489 0.5055 -0.0113 -0.0608 0.0007 62 LEU A CD1 495 C CD2 . LEU A 62 ? 0.4743 0.5098 0.4718 -0.0195 -0.0579 -0.0021 62 LEU A CD2 496 N N . GLY A 63 ? 0.4714 0.5465 0.4879 -0.0260 -0.0673 -0.0070 63 GLY A N 497 C CA . GLY A 63 ? 0.5104 0.5956 0.5282 -0.0283 -0.0707 -0.0087 63 GLY A CA 498 C C . GLY A 63 ? 0.5237 0.6158 0.5401 -0.0232 -0.0741 -0.0078 63 GLY A C 499 O O . GLY A 63 ? 0.5641 0.6603 0.5774 -0.0241 -0.0770 -0.0089 63 GLY A O 500 N N . ASN A 64 ? 0.4481 0.5409 0.4661 -0.0176 -0.0738 -0.0058 64 ASN A N 501 C CA . ASN A 64 ? 0.4723 0.5724 0.4894 -0.0118 -0.0770 -0.0048 64 ASN A CA 502 C C . ASN A 64 ? 0.4911 0.6064 0.5134 -0.0140 -0.0802 -0.0066 64 ASN A C 503 O O . ASN A 64 ? 0.4719 0.5944 0.5011 -0.0172 -0.0795 -0.0075 64 ASN A O 504 C CB . ASN A 64 ? 0.4190 0.5183 0.4385 -0.0064 -0.0757 -0.0027 64 ASN A CB 505 C CG . ASN A 64 ? 0.4722 0.5774 0.4898 0.0007 -0.0787 -0.0015 64 ASN A CG 506 O OD1 . ASN A 64 ? 0.5364 0.6537 0.5563 0.0014 -0.0821 -0.0025 64 ASN A OD1 507 N ND2 . ASN A 64 ? 0.4601 0.5567 0.4732 0.0061 -0.0775 0.0007 64 ASN A ND2 508 N N . PRO A 65 ? 0.5388 0.6594 0.5574 -0.0124 -0.0838 -0.0071 65 PRO A N 509 C CA . PRO A 65 ? 0.5569 0.6923 0.5795 -0.0152 -0.0872 -0.0091 65 PRO A CA 510 C C . PRO A 65 ? 0.5512 0.7007 0.5821 -0.0130 -0.0881 -0.0090 65 PRO A C 511 O O . PRO A 65 ? 0.5912 0.7539 0.6269 -0.0168 -0.0902 -0.0109 65 PRO A O 512 C CB . PRO A 65 ? 0.5947 0.7320 0.6110 -0.0113 -0.0908 -0.0088 65 PRO A CB 513 C CG . PRO A 65 ? 0.5922 0.7130 0.6001 -0.0094 -0.0888 -0.0073 65 PRO A CG 514 C CD . PRO A 65 ? 0.5438 0.6563 0.5538 -0.0079 -0.0849 -0.0057 65 PRO A CD 515 N N . LYS A 66 ? 0.5615 0.7083 0.5938 -0.0072 -0.0866 -0.0069 66 LYS A N 516 C CA . LYS A 66 ? 0.5786 0.7378 0.6185 -0.0047 -0.0870 -0.0068 66 LYS A CA 517 C C . LYS A 66 ? 0.5562 0.7134 0.6020 -0.0091 -0.0834 -0.0071 66 LYS A C 518 O O . LYS A 66 ? 0.5503 0.7164 0.6025 -0.0073 -0.0830 -0.0069 66 LYS A O 519 C CB . LYS A 66 ? 0.5834 0.7416 0.6209 0.0048 -0.0878 -0.0044 66 LYS A CB 520 C CG . LYS A 66 ? 0.6586 0.8239 0.6921 0.0101 -0.0920 -0.0042 66 LYS A CG 521 C CD . LYS A 66 ? 0.7222 0.8863 0.7529 0.0200 -0.0927 -0.0019 66 LYS A CD 522 C CE . LYS A 66 ? 0.7342 0.9065 0.7610 0.0258 -0.0972 -0.0016 66 LYS A CE 523 N NZ . LYS A 66 ? 0.7827 0.9509 0.8046 0.0359 -0.0977 0.0008 66 LYS A NZ 524 N N . CYS A 67 ? 0.5203 0.6660 0.5637 -0.0146 -0.0807 -0.0076 67 CYS A N 525 C CA . CYS A 67 ? 0.5386 0.6815 0.5867 -0.0190 -0.0773 -0.0079 67 CYS A CA 526 C C . CYS A 67 ? 0.5716 0.7179 0.6215 -0.0276 -0.0774 -0.0104 67 CYS A C 527 O O . CYS A 67 ? 0.5726 0.7118 0.6232 -0.0323 -0.0744 -0.0108 67 CYS A O 528 C CB . CYS A 67 ? 0.4861 0.6127 0.5300 -0.0181 -0.0739 -0.0065 67 CYS A CB 529 S SG . CYS A 67 ? 0.5973 0.7177 0.6373 -0.0090 -0.0736 -0.0037 67 CYS A SG 530 N N . ASP A 68 ? 0.5499 0.7069 0.6000 -0.0296 -0.0808 -0.0120 68 ASP A N 531 C CA . ASP A 68 ? 0.5282 0.6881 0.5787 -0.0381 -0.0812 -0.0145 68 ASP A CA 532 C C . ASP A 68 ? 0.5052 0.6717 0.5625 -0.0433 -0.0794 -0.0154 68 ASP A C 533 O O . ASP A 68 ? 0.5110 0.6738 0.5675 -0.0507 -0.0782 -0.0170 68 ASP A O 534 C CB . ASP A 68 ? 0.5968 0.7681 0.6462 -0.0390 -0.0855 -0.0160 68 ASP A CB 535 C CG . ASP A 68 ? 0.6842 0.8459 0.7250 -0.0380 -0.0867 -0.0160 68 ASP A CG 536 O OD1 . ASP A 68 ? 0.6755 0.8217 0.7112 -0.0384 -0.0839 -0.0154 68 ASP A OD1 537 O OD2 . ASP A 68 ? 0.7011 0.8712 0.7401 -0.0366 -0.0904 -0.0167 68 ASP A OD2 538 N N . LEU A 69 ? 0.3867 0.5624 0.4503 -0.0393 -0.0793 -0.0144 69 LEU A N 539 C CA . LEU A 69 ? 0.4031 0.5843 0.4731 -0.0437 -0.0773 -0.0150 69 LEU A CA 540 C C . LEU A 69 ? 0.4108 0.5768 0.4787 -0.0470 -0.0732 -0.0145 69 LEU A C 541 O O . LEU A 69 ? 0.4343 0.6007 0.5043 -0.0536 -0.0716 -0.0156 69 LEU A O 542 C CB . LEU A 69 ? 0.4481 0.6398 0.5244 -0.0377 -0.0774 -0.0137 69 LEU A CB 543 C CG . LEU A 69 ? 0.5672 0.7642 0.6501 -0.0414 -0.0749 -0.0139 69 LEU A CG 544 C CD1 . LEU A 69 ? 0.4527 0.6605 0.5387 -0.0501 -0.0759 -0.0164 69 LEU A CD1 545 C CD2 . LEU A 69 ? 0.5275 0.7341 0.6158 -0.0344 -0.0751 -0.0126 69 LEU A CD2 546 N N . LEU A 70 ? 0.5263 0.6789 0.5896 -0.0426 -0.0717 -0.0128 70 LEU A N 547 C CA . LEU A 70 ? 0.5631 0.7017 0.6243 -0.0446 -0.0679 -0.0122 70 LEU A CA 548 C C . LEU A 70 ? 0.5254 0.6535 0.5802 -0.0496 -0.0674 -0.0135 70 LEU A C 549 O O . LEU A 70 ? 0.5279 0.6462 0.5810 -0.0530 -0.0645 -0.0137 70 LEU A O 550 C CB . LEU A 70 ? 0.5628 0.6929 0.6223 -0.0377 -0.0663 -0.0098 70 LEU A CB 551 C CG . LEU A 70 ? 0.5988 0.7366 0.6636 -0.0323 -0.0663 -0.0084 70 LEU A CG 552 C CD1 . LEU A 70 ? 0.5848 0.7130 0.6462 -0.0258 -0.0651 -0.0063 70 LEU A CD1 553 C CD2 . LEU A 70 ? 0.4958 0.6373 0.5665 -0.0357 -0.0641 -0.0087 70 LEU A CD2 554 N N . LEU A 71 ? 0.4539 0.5840 0.5047 -0.0498 -0.0702 -0.0145 71 LEU A N 555 C CA . LEU A 71 ? 0.4559 0.5753 0.4994 -0.0534 -0.0699 -0.0157 71 LEU A CA 556 C C . LEU A 71 ? 0.4337 0.5484 0.4760 -0.0612 -0.0681 -0.0175 71 LEU A C 557 O O . LEU A 71 ? 0.4541 0.5779 0.4996 -0.0665 -0.0691 -0.0190 71 LEU A O 558 C CB . LEU A 71 ? 0.5083 0.6336 0.5485 -0.0531 -0.0736 -0.0168 71 LEU A CB 559 C CG . LEU A 71 ? 0.4887 0.6022 0.5205 -0.0551 -0.0734 -0.0177 71 LEU A CG 560 C CD1 . LEU A 71 ? 0.4467 0.5501 0.4746 -0.0487 -0.0720 -0.0156 71 LEU A CD1 561 C CD2 . LEU A 71 ? 0.4611 0.5819 0.4901 -0.0573 -0.0771 -0.0195 71 LEU A CD2 562 N N . GLY A 72 ? 0.3873 0.4875 0.4246 -0.0620 -0.0653 -0.0173 72 GLY A N 563 C CA . GLY A 72 ? 0.4228 0.5159 0.4570 -0.0688 -0.0635 -0.0189 72 GLY A CA 564 C C . GLY A 72 ? 0.4485 0.5331 0.4839 -0.0684 -0.0597 -0.0177 72 GLY A C 565 O O . GLY A 72 ? 0.4565 0.5351 0.4918 -0.0631 -0.0580 -0.0159 72 GLY A O 566 N N . ASP A 73 ? 0.5730 0.6568 0.6090 -0.0742 -0.0584 -0.0188 73 ASP A N 567 C CA . ASP A 73 ? 0.5535 0.6293 0.5901 -0.0742 -0.0550 -0.0178 73 ASP A CA 568 C C . ASP A 73 ? 0.5672 0.6516 0.6117 -0.0713 -0.0545 -0.0161 73 ASP A C 569 O O . ASP A 73 ? 0.5432 0.6406 0.5930 -0.0725 -0.0564 -0.0165 73 ASP A O 570 C CB . ASP A 73 ? 0.5315 0.6014 0.5643 -0.0816 -0.0536 -0.0195 73 ASP A CB 571 C CG . ASP A 73 ? 0.6217 0.6826 0.6459 -0.0849 -0.0542 -0.0214 73 ASP A CG 572 O OD1 . ASP A 73 ? 0.6325 0.6889 0.6533 -0.0807 -0.0546 -0.0210 73 ASP A OD1 573 O OD2 . ASP A 73 ? 0.6413 0.6994 0.6617 -0.0918 -0.0540 -0.0233 73 ASP A OD2 574 N N . GLN A 74 ? 0.4463 0.5241 0.4917 -0.0673 -0.0519 -0.0143 74 GLN A N 575 C CA . GLN A 74 ? 0.4055 0.4896 0.4577 -0.0648 -0.0509 -0.0128 74 GLN A CA 576 C C . GLN A 74 ? 0.4062 0.4809 0.4577 -0.0651 -0.0475 -0.0118 74 GLN A C 577 O O . GLN A 74 ? 0.4060 0.4696 0.4527 -0.0634 -0.0459 -0.0114 74 GLN A O 578 C CB . GLN A 74 ? 0.3697 0.4581 0.4246 -0.0577 -0.0519 -0.0111 74 GLN A CB 579 C CG . GLN A 74 ? 0.3831 0.4825 0.4395 -0.0563 -0.0555 -0.0117 74 GLN A CG 580 C CD . GLN A 74 ? 0.4093 0.5230 0.4722 -0.0585 -0.0568 -0.0124 74 GLN A CD 581 O OE1 . GLN A 74 ? 0.4594 0.5748 0.5258 -0.0611 -0.0550 -0.0122 74 GLN A OE1 582 N NE2 . GLN A 74 ? 0.4426 0.5672 0.5070 -0.0573 -0.0600 -0.0130 74 GLN A NE2 583 N N . SER A 75 ? 0.4283 0.5080 0.4844 -0.0671 -0.0465 -0.0115 75 SER A N 584 C CA . SER A 75 ? 0.4337 0.5067 0.4903 -0.0662 -0.0435 -0.0102 75 SER A CA 585 C C . SER A 75 ? 0.4489 0.5304 0.5124 -0.0621 -0.0434 -0.0087 75 SER A C 586 O O . SER A 75 ? 0.4899 0.5832 0.5580 -0.0621 -0.0452 -0.0090 75 SER A O 587 C CB . SER A 75 ? 0.4371 0.5071 0.4920 -0.0727 -0.0421 -0.0112 75 SER A CB 588 O OG . SER A 75 ? 0.5384 0.5966 0.5856 -0.0755 -0.0413 -0.0122 75 SER A OG 589 N N . TRP A 76 ? 0.4657 0.5414 0.5296 -0.0585 -0.0412 -0.0070 76 TRP A N 590 C CA . TRP A 76 ? 0.3873 0.4697 0.4570 -0.0545 -0.0409 -0.0056 76 TRP A CA 591 C C . TRP A 76 ? 0.4241 0.5000 0.4940 -0.0529 -0.0381 -0.0042 76 TRP A C 592 O O . TRP A 76 ? 0.4569 0.5227 0.5226 -0.0524 -0.0366 -0.0039 76 TRP A O 593 C CB . TRP A 76 ? 0.3826 0.4680 0.4527 -0.0490 -0.0426 -0.0049 76 TRP A CB 594 C CG . TRP A 76 ? 0.4147 0.4899 0.4803 -0.0458 -0.0416 -0.0041 76 TRP A CG 595 C CD1 . TRP A 76 ? 0.3974 0.4679 0.4632 -0.0421 -0.0398 -0.0026 76 TRP A CD1 596 C CD2 . TRP A 76 ? 0.4199 0.4890 0.4799 -0.0462 -0.0424 -0.0049 76 TRP A CD2 597 N NE1 . TRP A 76 ? 0.3806 0.4431 0.4416 -0.0403 -0.0393 -0.0024 76 TRP A NE1 598 C CE2 . TRP A 76 ? 0.3758 0.4371 0.4332 -0.0427 -0.0408 -0.0037 76 TRP A CE2 599 C CE3 . TRP A 76 ? 0.3617 0.4314 0.4187 -0.0495 -0.0441 -0.0065 76 TRP A CE3 600 C CZ2 . TRP A 76 ? 0.3627 0.4170 0.4146 -0.0421 -0.0409 -0.0041 76 TRP A CZ2 601 C CZ3 . TRP A 76 ? 0.4230 0.4851 0.4742 -0.0488 -0.0443 -0.0069 76 TRP A CZ3 602 C CH2 . TRP A 76 ? 0.4081 0.4628 0.4569 -0.0450 -0.0426 -0.0057 76 TRP A CH2 603 N N . SER A 77 ? 0.4910 0.5732 0.5660 -0.0520 -0.0375 -0.0034 77 SER A N 604 C CA . SER A 77 ? 0.4510 0.5286 0.5269 -0.0499 -0.0351 -0.0020 77 SER A CA 605 C C . SER A 77 ? 0.4386 0.5157 0.5152 -0.0440 -0.0352 -0.0007 77 SER A C 606 O O . SER A 77 ? 0.4593 0.5305 0.5351 -0.0418 -0.0334 0.0004 77 SER A O 607 C CB . SER A 77 ? 0.4519 0.5364 0.5324 -0.0519 -0.0342 -0.0018 77 SER A CB 608 O OG . SER A 77 ? 0.4123 0.5085 0.4975 -0.0505 -0.0360 -0.0021 77 SER A OG 609 N N . TYR A 78 ? 0.3862 0.4695 0.4640 -0.0414 -0.0374 -0.0009 78 TYR A N 610 C CA . TYR A 78 ? 0.3968 0.4785 0.4736 -0.0361 -0.0378 0.0001 78 TYR A CA 611 C C . TYR A 78 ? 0.4127 0.5008 0.4896 -0.0341 -0.0406 -0.0004 78 TYR A C 612 O O . TYR A 78 ? 0.4141 0.5098 0.4929 -0.0367 -0.0422 -0.0015 78 TYR A O 613 C CB . TYR A 78 ? 0.3632 0.4464 0.4431 -0.0330 -0.0364 0.0014 78 TYR A CB 614 C CG . TYR A 78 ? 0.3459 0.4394 0.4309 -0.0330 -0.0370 0.0012 78 TYR A CG 615 C CD1 . TYR A 78 ? 0.3228 0.4190 0.4106 -0.0369 -0.0357 0.0009 78 TYR A CD1 616 C CD2 . TYR A 78 ? 0.3046 0.4048 0.3914 -0.0290 -0.0386 0.0014 78 TYR A CD2 617 C CE1 . TYR A 78 ? 0.3528 0.4591 0.4454 -0.0371 -0.0360 0.0006 78 TYR A CE1 618 C CE2 . TYR A 78 ? 0.3113 0.4217 0.4029 -0.0286 -0.0390 0.0011 78 TYR A CE2 619 C CZ . TYR A 78 ? 0.3477 0.4615 0.4425 -0.0328 -0.0376 0.0007 78 TYR A CZ 620 O OH . TYR A 78 ? 0.3770 0.5017 0.4767 -0.0326 -0.0378 0.0004 78 TYR A OH 621 N N . ILE A 79 ? 0.3619 0.4471 0.4364 -0.0296 -0.0411 0.0005 79 ILE A N 622 C CA . ILE A 79 ? 0.3565 0.4464 0.4299 -0.0270 -0.0438 0.0002 79 ILE A CA 623 C C . ILE A 79 ? 0.3777 0.4725 0.4530 -0.0218 -0.0445 0.0012 79 ILE A C 624 O O . ILE A 79 ? 0.4482 0.5378 0.5223 -0.0189 -0.0430 0.0024 79 ILE A O 625 C CB . ILE A 79 ? 0.3849 0.4667 0.4523 -0.0260 -0.0442 0.0004 79 ILE A CB 626 C CG1 . ILE A 79 ? 0.3629 0.4405 0.4279 -0.0307 -0.0439 -0.0008 79 ILE A CG1 627 C CG2 . ILE A 79 ? 0.3586 0.4442 0.4241 -0.0225 -0.0469 0.0004 79 ILE A CG2 628 C CD1 . ILE A 79 ? 0.3888 0.4579 0.4479 -0.0299 -0.0437 -0.0008 79 ILE A CD1 629 N N . VAL A 80 ? 0.3210 0.4263 0.3992 -0.0207 -0.0467 0.0006 80 VAL A N 630 C CA . VAL A 80 ? 0.3347 0.4446 0.4138 -0.0150 -0.0476 0.0014 80 VAL A CA 631 C C . VAL A 80 ? 0.3657 0.4755 0.4406 -0.0113 -0.0501 0.0015 80 VAL A C 632 O O . VAL A 80 ? 0.4184 0.5349 0.4938 -0.0127 -0.0524 0.0004 80 VAL A O 633 C CB . VAL A 80 ? 0.3908 0.5137 0.4762 -0.0152 -0.0482 0.0007 80 VAL A CB 634 C CG1 . VAL A 80 ? 0.3591 0.4868 0.4448 -0.0084 -0.0493 0.0015 80 VAL A CG1 635 C CG2 . VAL A 80 ? 0.3248 0.4473 0.4138 -0.0187 -0.0456 0.0007 80 VAL A CG2 636 N N . GLU A 81 ? 0.4441 0.5458 0.5141 -0.0069 -0.0497 0.0028 81 GLU A N 637 C CA . GLU A 81 ? 0.4581 0.5584 0.5231 -0.0029 -0.0520 0.0033 81 GLU A CA 638 C C . GLU A 81 ? 0.4956 0.6002 0.5607 0.0036 -0.0529 0.0041 81 GLU A C 639 O O . GLU A 81 ? 0.5285 0.6298 0.5940 0.0056 -0.0511 0.0049 81 GLU A O 640 C CB . GLU A 81 ? 0.4941 0.5813 0.5523 -0.0026 -0.0508 0.0042 81 GLU A CB 641 C CG . GLU A 81 ? 0.6418 0.7264 0.6938 0.0007 -0.0531 0.0046 81 GLU A CG 642 C CD . GLU A 81 ? 0.7742 0.8460 0.8192 0.0009 -0.0516 0.0056 81 GLU A CD 643 O OE1 . GLU A 81 ? 0.7451 0.8137 0.7844 0.0029 -0.0533 0.0059 81 GLU A OE1 644 O OE2 . GLU A 81 ? 0.7929 0.8583 0.8380 -0.0011 -0.0489 0.0060 81 GLU A OE2 645 N N . ARG A 82 ? 0.4088 0.5207 0.4733 0.0070 -0.0558 0.0038 82 ARG A N 646 C CA . ARG A 82 ? 0.4454 0.5623 0.5099 0.0138 -0.0570 0.0045 82 ARG A CA 647 C C . ARG A 82 ? 0.4905 0.5960 0.5463 0.0192 -0.0571 0.0060 82 ARG A C 648 O O . ARG A 82 ? 0.5141 0.6133 0.5645 0.0187 -0.0581 0.0063 82 ARG A O 649 C CB . ARG A 82 ? 0.4150 0.5469 0.4835 0.0153 -0.0600 0.0034 82 ARG A CB 650 C CG . ARG A 82 ? 0.3704 0.5138 0.4469 0.0091 -0.0599 0.0018 82 ARG A CG 651 C CD . ARG A 82 ? 0.4209 0.5648 0.5019 0.0076 -0.0570 0.0019 82 ARG A CD 652 N NE . ARG A 82 ? 0.3454 0.5002 0.4335 0.0018 -0.0568 0.0004 82 ARG A NE 653 C CZ . ARG A 82 ? 0.3770 0.5364 0.4701 0.0007 -0.0548 0.0003 82 ARG A CZ 654 N NH1 . ARG A 82 ? 0.3526 0.5067 0.4446 0.0051 -0.0531 0.0015 82 ARG A NH1 655 N NH2 . ARG A 82 ? 0.3419 0.5108 0.4407 -0.0050 -0.0546 -0.0010 82 ARG A NH2 656 N N . PRO A 83 ? 0.6457 0.7480 0.6997 0.0243 -0.0561 0.0070 83 PRO A N 657 C CA . PRO A 83 ? 0.7168 0.8060 0.7618 0.0287 -0.0556 0.0086 83 PRO A CA 658 C C . PRO A 83 ? 0.7581 0.8458 0.7965 0.0334 -0.0584 0.0092 83 PRO A C 659 O O . PRO A 83 ? 0.7598 0.8354 0.7902 0.0336 -0.0579 0.0102 83 PRO A O 660 C CB . PRO A 83 ? 0.6088 0.6990 0.6544 0.0337 -0.0546 0.0091 83 PRO A CB 661 C CG . PRO A 83 ? 0.6275 0.7281 0.6826 0.0299 -0.0535 0.0080 83 PRO A CG 662 C CD . PRO A 83 ? 0.6098 0.7211 0.6700 0.0259 -0.0554 0.0067 83 PRO A CD 663 N N . ASN A 84 ? 0.7139 0.8139 0.7552 0.0370 -0.0612 0.0086 84 ASN A N 664 C CA . ASN A 84 ? 0.8411 0.9404 0.8760 0.0420 -0.0641 0.0092 84 ASN A CA 665 C C . ASN A 84 ? 0.7784 0.8864 0.8161 0.0384 -0.0666 0.0080 84 ASN A C 666 O O . ASN A 84 ? 0.7927 0.9085 0.8294 0.0427 -0.0697 0.0079 84 ASN A O 667 C CB . ASN A 84 ? 0.9194 1.0244 0.9531 0.0507 -0.0657 0.0098 84 ASN A CB 668 C CG . ASN A 84 ? 1.0243 1.1177 1.0524 0.0550 -0.0634 0.0111 84 ASN A CG 669 O OD1 . ASN A 84 ? 0.9372 1.0153 0.9579 0.0537 -0.0617 0.0122 84 ASN A OD1 670 N ND2 . ASN A 84 ? 1.0744 1.1751 1.1059 0.0598 -0.0633 0.0110 84 ASN A ND2 671 N N . ALA A 85 ? 0.6147 0.7212 0.6555 0.0307 -0.0653 0.0071 85 ALA A N 672 C CA . ALA A 85 ? 0.5883 0.7005 0.6306 0.0263 -0.0672 0.0058 85 ALA A CA 673 C C . ALA A 85 ? 0.6259 0.7301 0.6591 0.0291 -0.0690 0.0067 85 ALA A C 674 O O . ALA A 85 ? 0.5869 0.6772 0.6129 0.0301 -0.0673 0.0080 85 ALA A O 675 C CB . ALA A 85 ? 0.4691 0.5780 0.5146 0.0182 -0.0650 0.0048 85 ALA A CB 676 N N . GLN A 86 ? 0.5819 0.6951 0.6152 0.0301 -0.0723 0.0059 86 GLN A N 677 C CA . GLN A 86 ? 0.6192 0.7263 0.6437 0.0339 -0.0745 0.0069 86 GLN A CA 678 C C . GLN A 86 ? 0.4949 0.5983 0.5169 0.0280 -0.0748 0.0060 86 GLN A C 679 O O . GLN A 86 ? 0.5028 0.5966 0.5165 0.0296 -0.0753 0.0070 86 GLN A O 680 C CB . GLN A 86 ? 0.6052 0.7245 0.6300 0.0404 -0.0783 0.0068 86 GLN A CB 681 C CG . GLN A 86 ? 0.6668 0.7883 0.6916 0.0481 -0.0783 0.0080 86 GLN A CG 682 C CD . GLN A 86 ? 0.7903 0.8954 0.8043 0.0539 -0.0772 0.0102 86 GLN A CD 683 O OE1 . GLN A 86 ? 0.7764 0.8679 0.7869 0.0509 -0.0741 0.0109 86 GLN A OE1 684 N NE2 . GLN A 86 ? 0.8877 0.9939 0.8959 0.0622 -0.0798 0.0113 86 GLN A NE2 685 N N . ASN A 87 ? 0.5034 0.6140 0.5323 0.0213 -0.0745 0.0041 87 ASN A N 686 C CA . ASN A 87 ? 0.5094 0.6179 0.5361 0.0158 -0.0752 0.0030 87 ASN A CA 687 C C . ASN A 87 ? 0.5394 0.6350 0.5636 0.0108 -0.0717 0.0031 87 ASN A C 688 O O . ASN A 87 ? 0.5194 0.6164 0.5490 0.0052 -0.0698 0.0019 87 ASN A O 689 C CB . ASN A 87 ? 0.4849 0.6078 0.5188 0.0112 -0.0770 0.0007 87 ASN A CB 690 C CG . ASN A 87 ? 0.6077 0.7450 0.6440 0.0161 -0.0807 0.0005 87 ASN A CG 691 O OD1 . ASN A 87 ? 0.5776 0.7137 0.6080 0.0218 -0.0830 0.0015 87 ASN A OD1 692 N ND2 . ASN A 87 ? 0.5673 0.7183 0.6121 0.0140 -0.0811 -0.0008 87 ASN A ND2 693 N N . GLY A 88 ? 0.4423 0.5256 0.4582 0.0129 -0.0709 0.0045 88 GLY A N 694 C CA . GLY A 88 ? 0.4650 0.5368 0.4782 0.0087 -0.0677 0.0046 88 GLY A CA 695 C C . GLY A 88 ? 0.5092 0.5748 0.5151 0.0075 -0.0686 0.0045 88 GLY A C 696 O O . GLY A 88 ? 0.5219 0.5932 0.5287 0.0046 -0.0705 0.0029 88 GLY A O 697 N N . ILE A 89 ? 0.5069 0.5606 0.5052 0.0093 -0.0670 0.0060 89 ILE A N 698 C CA . ILE A 89 ? 0.6073 0.6545 0.5978 0.0086 -0.0677 0.0061 89 ILE A CA 699 C C . ILE A 89 ? 0.5728 0.6226 0.5580 0.0143 -0.0712 0.0070 89 ILE A C 700 O O . ILE A 89 ? 0.6461 0.6907 0.6264 0.0195 -0.0713 0.0089 89 ILE A O 701 C CB . ILE A 89 ? 0.5662 0.6001 0.5507 0.0076 -0.0643 0.0074 89 ILE A CB 702 C CG1 . ILE A 89 ? 0.5591 0.5917 0.5486 0.0020 -0.0611 0.0062 89 ILE A CG1 703 C CG2 . ILE A 89 ? 0.5512 0.5781 0.5265 0.0080 -0.0650 0.0078 89 ILE A CG2 704 C CD1 . ILE A 89 ? 0.5449 0.5665 0.5300 0.0009 -0.0576 0.0073 89 ILE A CD1 705 N N . CYS A 90 ? 0.6224 0.6800 0.6081 0.0134 -0.0743 0.0057 90 CYS A N 706 C CA . CYS A 90 ? 0.7542 0.8161 0.7355 0.0189 -0.0781 0.0064 90 CYS A CA 707 C C . CYS A 90 ? 0.7207 0.7716 0.6909 0.0207 -0.0784 0.0076 90 CYS A C 708 O O . CYS A 90 ? 0.6933 0.7397 0.6568 0.0267 -0.0795 0.0095 90 CYS A O 709 C CB . CYS A 90 ? 0.7296 0.8062 0.7166 0.0172 -0.0815 0.0043 90 CYS A CB 710 S SG . CYS A 90 ? 0.9583 1.0351 0.9465 0.0086 -0.0809 0.0018 90 CYS A SG 711 N N . TYR A 91 ? 0.5620 0.6080 0.5295 0.0156 -0.0773 0.0066 91 TYR A N 712 C CA . TYR A 91 ? 0.6226 0.6573 0.5794 0.0166 -0.0768 0.0079 91 TYR A CA 713 C C . TYR A 91 ? 0.6124 0.6347 0.5658 0.0160 -0.0727 0.0094 91 TYR A C 714 O O . TYR A 91 ? 0.5708 0.5911 0.5283 0.0112 -0.0696 0.0085 91 TYR A O 715 C CB . TYR A 91 ? 0.6078 0.6422 0.5627 0.0116 -0.0771 0.0061 91 TYR A CB 716 C CG . TYR A 91 ? 0.6294 0.6557 0.5731 0.0134 -0.0781 0.0071 91 TYR A CG 717 C CD1 . TYR A 91 ? 0.5804 0.5938 0.5171 0.0122 -0.0748 0.0083 91 TYR A CD1 718 C CD2 . TYR A 91 ? 0.6823 0.7143 0.6224 0.0162 -0.0822 0.0069 91 TYR A CD2 719 C CE1 . TYR A 91 ? 0.6754 0.6812 0.6016 0.0136 -0.0755 0.0093 91 TYR A CE1 720 C CE2 . TYR A 91 ? 0.6590 0.6834 0.5886 0.0179 -0.0831 0.0079 91 TYR A CE2 721 C CZ . TYR A 91 ? 0.7475 0.7584 0.6699 0.0166 -0.0797 0.0092 91 TYR A CZ 722 O OH . TYR A 91 ? 0.6868 0.6900 0.5984 0.0180 -0.0804 0.0102 91 TYR A OH 723 N N . PRO A 92 ? 0.6687 0.6827 0.6141 0.0208 -0.0726 0.0116 92 PRO A N 724 C CA . PRO A 92 ? 0.6485 0.6512 0.5902 0.0206 -0.0689 0.0132 92 PRO A CA 725 C C . PRO A 92 ? 0.6933 0.6890 0.6336 0.0146 -0.0654 0.0126 92 PRO A C 726 O O . PRO A 92 ? 0.6211 0.6157 0.5578 0.0123 -0.0658 0.0118 92 PRO A O 727 C CB . PRO A 92 ? 0.6516 0.6452 0.5818 0.0262 -0.0701 0.0155 92 PRO A CB 728 C CG . PRO A 92 ? 0.7176 0.7164 0.6444 0.0282 -0.0740 0.0151 92 PRO A CG 729 C CD . PRO A 92 ? 0.6841 0.6981 0.6220 0.0266 -0.0761 0.0128 92 PRO A CD 730 N N . GLY A 93 ? 0.5977 0.5893 0.5408 0.0124 -0.0619 0.0130 93 GLY A N 731 C CA . GLY A 93 ? 0.5819 0.5682 0.5246 0.0071 -0.0583 0.0124 93 GLY A CA 732 C C . GLY A 93 ? 0.6012 0.5897 0.5521 0.0044 -0.0555 0.0118 93 GLY A C 733 O O . GLY A 93 ? 0.6185 0.6138 0.5764 0.0059 -0.0565 0.0115 93 GLY A O 734 N N . VAL A 94 ? 0.6557 0.6390 0.6057 0.0005 -0.0520 0.0117 94 VAL A N 735 C CA . VAL A 94 ? 0.6393 0.6240 0.5962 -0.0019 -0.0492 0.0114 94 VAL A CA 736 C C . VAL A 94 ? 0.5242 0.5155 0.4888 -0.0056 -0.0486 0.0093 94 VAL A C 737 O O . VAL A 94 ? 0.5450 0.5354 0.5073 -0.0079 -0.0483 0.0083 94 VAL A O 738 C CB . VAL A 94 ? 0.6354 0.6113 0.5871 -0.0040 -0.0457 0.0125 94 VAL A CB 739 C CG1 . VAL A 94 ? 0.6271 0.6051 0.5858 -0.0066 -0.0429 0.0120 94 VAL A CG1 740 C CG2 . VAL A 94 ? 0.6348 0.6025 0.5779 -0.0007 -0.0460 0.0145 94 VAL A CG2 741 N N . LEU A 95 ? 0.6015 0.5988 0.5745 -0.0061 -0.0484 0.0086 95 LEU A N 742 C CA . LEU A 95 ? 0.5673 0.5688 0.5468 -0.0098 -0.0471 0.0069 95 LEU A CA 743 C C . LEU A 95 ? 0.5669 0.5639 0.5466 -0.0120 -0.0432 0.0073 95 LEU A C 744 O O . LEU A 95 ? 0.5290 0.5251 0.5108 -0.0114 -0.0419 0.0083 95 LEU A O 745 C CB . LEU A 95 ? 0.5042 0.5141 0.4923 -0.0096 -0.0484 0.0061 95 LEU A CB 746 C CG . LEU A 95 ? 0.5464 0.5618 0.5389 -0.0126 -0.0492 0.0041 95 LEU A CG 747 C CD1 . LEU A 95 ? 0.5223 0.5453 0.5231 -0.0131 -0.0499 0.0034 95 LEU A CD1 748 C CD2 . LEU A 95 ? 0.5138 0.5251 0.5054 -0.0159 -0.0465 0.0032 95 LEU A CD2 749 N N . ASN A 96 ? 0.5274 0.5218 0.5048 -0.0146 -0.0415 0.0065 96 ASN A N 750 C CA . ASN A 96 ? 0.4893 0.4804 0.4665 -0.0166 -0.0379 0.0068 96 ASN A CA 751 C C . ASN A 96 ? 0.4823 0.4776 0.4675 -0.0179 -0.0364 0.0062 96 ASN A C 752 O O . ASN A 96 ? 0.4330 0.4329 0.4231 -0.0186 -0.0374 0.0049 96 ASN A O 753 C CB . ASN A 96 ? 0.5536 0.5421 0.5267 -0.0186 -0.0364 0.0059 96 ASN A CB 754 C CG . ASN A 96 ? 0.7322 0.7152 0.6999 -0.0197 -0.0336 0.0070 96 ASN A CG 755 O OD1 . ASN A 96 ? 0.7257 0.7038 0.6868 -0.0186 -0.0341 0.0083 96 ASN A OD1 756 N ND2 . ASN A 96 ? 0.5802 0.5642 0.5504 -0.0218 -0.0306 0.0064 96 ASN A ND2 757 N N . GLU A 97 ? 0.4981 0.4916 0.4841 -0.0184 -0.0340 0.0071 97 GLU A N 758 C CA . GLU A 97 ? 0.4184 0.4156 0.4114 -0.0195 -0.0324 0.0067 97 GLU A CA 759 C C . GLU A 97 ? 0.4176 0.4199 0.4165 -0.0182 -0.0346 0.0064 97 GLU A C 760 O O . GLU A 97 ? 0.3862 0.3924 0.3906 -0.0193 -0.0343 0.0054 97 GLU A O 761 C CB . GLU A 97 ? 0.3977 0.3962 0.3927 -0.0215 -0.0306 0.0054 97 GLU A CB 762 C CG . GLU A 97 ? 0.4540 0.4489 0.4437 -0.0227 -0.0282 0.0055 97 GLU A CG 763 C CD . GLU A 97 ? 0.6494 0.6437 0.6397 -0.0237 -0.0255 0.0064 97 GLU A CD 764 O OE1 . GLU A 97 ? 0.7200 0.7123 0.7063 -0.0251 -0.0233 0.0065 97 GLU A OE1 765 O OE2 . GLU A 97 ? 0.6316 0.6280 0.6263 -0.0234 -0.0255 0.0070 97 GLU A OE2 766 N N . LEU A 98 ? 0.3891 0.3911 0.3862 -0.0157 -0.0366 0.0074 98 LEU A N 767 C CA . LEU A 98 ? 0.3845 0.3921 0.3867 -0.0141 -0.0388 0.0072 98 LEU A CA 768 C C . LEU A 98 ? 0.4017 0.4125 0.4106 -0.0149 -0.0373 0.0071 98 LEU A C 769 O O . LEU A 98 ? 0.4214 0.4376 0.4360 -0.0156 -0.0381 0.0062 98 LEU A O 770 C CB . LEU A 98 ? 0.3982 0.4043 0.3966 -0.0106 -0.0408 0.0084 98 LEU A CB 771 C CG . LEU A 98 ? 0.4510 0.4639 0.4548 -0.0084 -0.0429 0.0082 98 LEU A CG 772 C CD1 . LEU A 98 ? 0.3737 0.3933 0.3812 -0.0096 -0.0450 0.0067 98 LEU A CD1 773 C CD2 . LEU A 98 ? 0.3364 0.3473 0.3357 -0.0040 -0.0447 0.0095 98 LEU A CD2 774 N N . GLU A 99 ? 0.4366 0.4439 0.4445 -0.0150 -0.0352 0.0081 99 GLU A N 775 C CA . GLU A 99 ? 0.4472 0.4573 0.4609 -0.0155 -0.0338 0.0082 99 GLU A CA 776 C C . GLU A 99 ? 0.4372 0.4501 0.4554 -0.0180 -0.0324 0.0071 99 GLU A C 777 O O . GLU A 99 ? 0.4070 0.4240 0.4309 -0.0184 -0.0324 0.0067 99 GLU A O 778 C CB . GLU A 99 ? 0.4195 0.4250 0.4303 -0.0155 -0.0318 0.0094 99 GLU A CB 779 C CG . GLU A 99 ? 0.4582 0.4599 0.4643 -0.0126 -0.0331 0.0106 99 GLU A CG 780 C CD . GLU A 99 ? 0.6117 0.6083 0.6099 -0.0116 -0.0342 0.0111 99 GLU A CD 781 O OE1 . GLU A 99 ? 0.5143 0.5094 0.5101 -0.0136 -0.0334 0.0106 99 GLU A OE1 782 O OE2 . GLU A 99 ? 0.5989 0.5929 0.5931 -0.0084 -0.0358 0.0119 99 GLU A OE2 783 N N . GLU A 100 ? 0.3786 0.3888 0.3938 -0.0195 -0.0311 0.0066 100 GLU A N 784 C CA . GLU A 100 ? 0.4099 0.4219 0.4282 -0.0213 -0.0298 0.0055 100 GLU A CA 785 C C . GLU A 100 ? 0.4201 0.4350 0.4407 -0.0217 -0.0317 0.0043 100 GLU A C 786 O O . GLU A 100 ? 0.4131 0.4301 0.4377 -0.0228 -0.0311 0.0036 100 GLU A O 787 C CB . GLU A 100 ? 0.3886 0.3973 0.4025 -0.0223 -0.0279 0.0052 100 GLU A CB 788 C CG . GLU A 100 ? 0.4473 0.4551 0.4610 -0.0230 -0.0253 0.0060 100 GLU A CG 789 C CD . GLU A 100 ? 0.4632 0.4743 0.4825 -0.0235 -0.0238 0.0057 100 GLU A CD 790 O OE1 . GLU A 100 ? 0.4920 0.5043 0.5132 -0.0237 -0.0237 0.0047 100 GLU A OE1 791 O OE2 . GLU A 100 ? 0.4451 0.4572 0.4664 -0.0236 -0.0227 0.0065 100 GLU A OE2 792 N N . LEU A 101 ? 0.3631 0.3781 0.3808 -0.0210 -0.0341 0.0040 101 LEU A N 793 C CA . LEU A 101 ? 0.3882 0.4068 0.4079 -0.0219 -0.0362 0.0028 101 LEU A CA 794 C C . LEU A 101 ? 0.3593 0.3833 0.3852 -0.0217 -0.0370 0.0029 101 LEU A C 795 O O . LEU A 101 ? 0.3646 0.3911 0.3937 -0.0237 -0.0372 0.0018 101 LEU A O 796 C CB . LEU A 101 ? 0.4149 0.4334 0.4303 -0.0208 -0.0388 0.0027 101 LEU A CB 797 C CG . LEU A 101 ? 0.3925 0.4161 0.4101 -0.0219 -0.0414 0.0014 101 LEU A CG 798 C CD1 . LEU A 101 ? 0.3785 0.4005 0.3957 -0.0249 -0.0405 -0.0002 101 LEU A CD1 799 C CD2 . LEU A 101 ? 0.4317 0.4565 0.4454 -0.0202 -0.0442 0.0015 101 LEU A CD2 800 N N . LYS A 102 ? 0.3335 0.3589 0.3605 -0.0195 -0.0375 0.0041 102 LYS A N 801 C CA . LYS A 102 ? 0.3787 0.4096 0.4115 -0.0191 -0.0381 0.0042 102 LYS A CA 802 C C . LYS A 102 ? 0.3854 0.4164 0.4222 -0.0208 -0.0358 0.0041 102 LYS A C 803 O O . LYS A 102 ? 0.4106 0.4458 0.4518 -0.0222 -0.0361 0.0035 102 LYS A O 804 C CB . LYS A 102 ? 0.3625 0.3937 0.3946 -0.0159 -0.0387 0.0055 102 LYS A CB 805 C CG . LYS A 102 ? 0.4452 0.4777 0.4739 -0.0134 -0.0415 0.0057 102 LYS A CG 806 C CD . LYS A 102 ? 0.4367 0.4685 0.4641 -0.0097 -0.0419 0.0070 102 LYS A CD 807 C CE . LYS A 102 ? 0.5190 0.5527 0.5432 -0.0064 -0.0448 0.0072 102 LYS A CE 808 N NZ . LYS A 102 ? 0.5790 0.6111 0.6010 -0.0022 -0.0452 0.0085 102 LYS A NZ 809 N N . ALA A 103 ? 0.3110 0.3378 0.3462 -0.0209 -0.0335 0.0047 103 ALA A N 810 C CA . ALA A 103 ? 0.3454 0.3723 0.3840 -0.0222 -0.0314 0.0046 103 ALA A CA 811 C C . ALA A 103 ? 0.3435 0.3703 0.3827 -0.0243 -0.0312 0.0034 103 ALA A C 812 O O . ALA A 103 ? 0.3689 0.3972 0.4115 -0.0254 -0.0305 0.0031 103 ALA A O 813 C CB . ALA A 103 ? 0.3000 0.3234 0.3365 -0.0219 -0.0291 0.0054 103 ALA A CB 814 N N . PHE A 104 ? 0.3450 0.3690 0.3799 -0.0248 -0.0317 0.0026 104 PHE A N 815 C CA . PHE A 104 ? 0.3747 0.3972 0.4087 -0.0268 -0.0315 0.0012 104 PHE A CA 816 C C . PHE A 104 ? 0.4094 0.4358 0.4463 -0.0286 -0.0333 0.0004 104 PHE A C 817 O O . PHE A 104 ? 0.4168 0.4430 0.4556 -0.0303 -0.0326 -0.0001 104 PHE A O 818 C CB . PHE A 104 ? 0.3129 0.3317 0.3414 -0.0270 -0.0318 0.0005 104 PHE A CB 819 C CG . PHE A 104 ? 0.3686 0.3851 0.3952 -0.0290 -0.0318 -0.0011 104 PHE A CG 820 C CD1 . PHE A 104 ? 0.4040 0.4170 0.4300 -0.0293 -0.0296 -0.0015 104 PHE A CD1 821 C CD2 . PHE A 104 ? 0.3572 0.3747 0.3820 -0.0305 -0.0342 -0.0022 104 PHE A CD2 822 C CE1 . PHE A 104 ? 0.4340 0.4434 0.4571 -0.0311 -0.0296 -0.0030 104 PHE A CE1 823 C CE2 . PHE A 104 ? 0.3831 0.3975 0.4052 -0.0328 -0.0342 -0.0038 104 PHE A CE2 824 C CZ . PHE A 104 ? 0.4191 0.4289 0.4401 -0.0331 -0.0318 -0.0042 104 PHE A CZ 825 N N . ILE A 105 ? 0.3491 0.3791 0.3860 -0.0280 -0.0358 0.0004 105 ILE A N 826 C CA . ILE A 105 ? 0.3666 0.4021 0.4065 -0.0298 -0.0377 -0.0005 105 ILE A CA 827 C C . ILE A 105 ? 0.3891 0.4283 0.4345 -0.0302 -0.0368 0.0000 105 ILE A C 828 O O . ILE A 105 ? 0.3782 0.4194 0.4256 -0.0330 -0.0370 -0.0008 105 ILE A O 829 C CB . ILE A 105 ? 0.3880 0.4280 0.4272 -0.0283 -0.0405 -0.0004 105 ILE A CB 830 C CG1 . ILE A 105 ? 0.3487 0.3854 0.3824 -0.0289 -0.0416 -0.0013 105 ILE A CG1 831 C CG2 . ILE A 105 ? 0.3195 0.3674 0.3631 -0.0297 -0.0424 -0.0011 105 ILE A CG2 832 C CD1 . ILE A 105 ? 0.3554 0.3959 0.3874 -0.0270 -0.0444 -0.0012 105 ILE A CD1 833 N N . GLY A 106 ? 0.4544 0.4940 0.5016 -0.0277 -0.0359 0.0014 106 GLY A N 834 C CA . GLY A 106 ? 0.3842 0.4269 0.4362 -0.0278 -0.0349 0.0020 106 GLY A CA 835 C C . GLY A 106 ? 0.4146 0.4543 0.4673 -0.0299 -0.0329 0.0017 106 GLY A C 836 O O . GLY A 106 ? 0.4347 0.4773 0.4911 -0.0312 -0.0325 0.0017 106 GLY A O 837 N N . SER A 107 ? 0.3657 0.3995 0.4147 -0.0301 -0.0316 0.0014 107 SER A N 838 C CA . SER A 107 ? 0.4026 0.4327 0.4513 -0.0314 -0.0296 0.0012 107 SER A CA 839 C C . SER A 107 ? 0.4587 0.4875 0.5059 -0.0346 -0.0303 -0.0002 107 SER A C 840 O O . SER A 107 ? 0.5248 0.5491 0.5703 -0.0357 -0.0288 -0.0005 107 SER A O 841 C CB . SER A 107 ? 0.4119 0.4369 0.4571 -0.0299 -0.0279 0.0014 107 SER A CB 842 O OG . SER A 107 ? 0.3979 0.4195 0.4385 -0.0305 -0.0284 0.0003 107 SER A OG 843 N N . GLY A 108 ? 0.4145 0.4471 0.4618 -0.0360 -0.0325 -0.0010 108 GLY A N 844 C CA . GLY A 108 ? 0.4134 0.4449 0.4587 -0.0397 -0.0334 -0.0025 108 GLY A CA 845 C C . GLY A 108 ? 0.4331 0.4701 0.4823 -0.0425 -0.0341 -0.0028 108 GLY A C 846 O O . GLY A 108 ? 0.4019 0.4439 0.4558 -0.0413 -0.0338 -0.0018 108 GLY A O 847 N N . GLU A 109 ? 0.4911 0.5274 0.5381 -0.0466 -0.0349 -0.0043 109 GLU A N 848 C CA . GLU A 109 ? 0.5178 0.5577 0.5674 -0.0504 -0.0349 -0.0048 109 GLU A CA 849 C C . GLU A 109 ? 0.5098 0.5531 0.5579 -0.0546 -0.0371 -0.0066 109 GLU A C 850 O O . GLU A 109 ? 0.4840 0.5347 0.5356 -0.0576 -0.0381 -0.0070 109 GLU A O 851 C CB . GLU A 109 ? 0.5397 0.5713 0.5864 -0.0519 -0.0325 -0.0047 109 GLU A CB 852 C CG . GLU A 109 ? 0.6387 0.6714 0.6863 -0.0564 -0.0320 -0.0051 109 GLU A CG 853 C CD . GLU A 109 ? 0.7135 0.7361 0.7566 -0.0572 -0.0296 -0.0049 109 GLU A CD 854 O OE1 . GLU A 109 ? 0.7614 0.7798 0.8009 -0.0618 -0.0292 -0.0059 109 GLU A OE1 855 O OE2 . GLU A 109 ? 0.7896 0.8085 0.8326 -0.0532 -0.0280 -0.0036 109 GLU A OE2 856 N N . ARG A 110 ? 0.4334 0.4716 0.4762 -0.0549 -0.0378 -0.0076 110 ARG A N 857 C CA . ARG A 110 ? 0.4466 0.4869 0.4869 -0.0592 -0.0398 -0.0094 110 ARG A CA 858 C C . ARG A 110 ? 0.4466 0.4829 0.4819 -0.0576 -0.0408 -0.0101 110 ARG A C 859 O O . ARG A 110 ? 0.4754 0.5032 0.5066 -0.0553 -0.0391 -0.0098 110 ARG A O 860 C CB . ARG A 110 ? 0.4825 0.5167 0.5189 -0.0646 -0.0386 -0.0107 110 ARG A CB 861 C CG . ARG A 110 ? 0.5531 0.5864 0.5848 -0.0694 -0.0403 -0.0128 110 ARG A CG 862 C CD . ARG A 110 ? 0.6034 0.6326 0.6319 -0.0758 -0.0394 -0.0141 110 ARG A CD 863 N NE . ARG A 110 ? 0.8018 0.8316 0.8262 -0.0810 -0.0414 -0.0163 110 ARG A NE 864 C CZ . ARG A 110 ? 0.7353 0.7771 0.7636 -0.0839 -0.0440 -0.0172 110 ARG A CZ 865 N NH1 . ARG A 110 ? 0.7559 0.7977 0.7798 -0.0888 -0.0457 -0.0194 110 ARG A NH1 866 N NH2 . ARG A 110 ? 0.5454 0.5992 0.5818 -0.0819 -0.0448 -0.0161 110 ARG A NH2 867 N N . VAL A 111 ? 0.4186 0.4615 0.4541 -0.0586 -0.0436 -0.0111 111 VAL A N 868 C CA . VAL A 111 ? 0.4834 0.5223 0.5132 -0.0581 -0.0447 -0.0120 111 VAL A CA 869 C C . VAL A 111 ? 0.5087 0.5488 0.5353 -0.0638 -0.0466 -0.0143 111 VAL A C 870 O O . VAL A 111 ? 0.5274 0.5767 0.5579 -0.0670 -0.0482 -0.0149 111 VAL A O 871 C CB . VAL A 111 ? 0.4416 0.4857 0.4730 -0.0535 -0.0465 -0.0110 111 VAL A CB 872 C CG1 . VAL A 111 ? 0.4127 0.4535 0.4455 -0.0485 -0.0445 -0.0090 111 VAL A CG1 873 C CG2 . VAL A 111 ? 0.4147 0.4713 0.4517 -0.0536 -0.0491 -0.0109 111 VAL A CG2 874 N N . GLU A 112 ? 0.4879 0.5191 0.5072 -0.0653 -0.0462 -0.0156 112 GLU A N 875 C CA . GLU A 112 ? 0.4979 0.5293 0.5129 -0.0706 -0.0481 -0.0179 112 GLU A CA 876 C C . GLU A 112 ? 0.4964 0.5278 0.5077 -0.0685 -0.0500 -0.0184 112 GLU A C 877 O O . GLU A 112 ? 0.5118 0.5341 0.5178 -0.0660 -0.0486 -0.0183 112 GLU A O 878 C CB . GLU A 112 ? 0.5599 0.5793 0.5679 -0.0746 -0.0460 -0.0193 112 GLU A CB 879 C CG . GLU A 112 ? 0.6901 0.7085 0.7000 -0.0782 -0.0444 -0.0191 112 GLU A CG 880 C CD . GLU A 112 ? 0.9724 0.9774 0.9739 -0.0819 -0.0424 -0.0205 112 GLU A CD 881 O OE1 . GLU A 112 ? 0.9165 0.9146 0.9107 -0.0831 -0.0428 -0.0221 112 GLU A OE1 882 O OE2 . GLU A 112 ? 0.9125 0.9132 0.9140 -0.0835 -0.0403 -0.0200 112 GLU A OE2 883 N N . ARG A 113 ? 0.4498 0.4918 0.4637 -0.0693 -0.0532 -0.0189 113 ARG A N 884 C CA . ARG A 113 ? 0.4434 0.4861 0.4535 -0.0675 -0.0554 -0.0194 113 ARG A CA 885 C C . ARG A 113 ? 0.5206 0.5562 0.5227 -0.0724 -0.0558 -0.0219 113 ARG A C 886 O O . ARG A 113 ? 0.5199 0.5555 0.5210 -0.0784 -0.0559 -0.0236 113 ARG A O 887 C CB . ARG A 113 ? 0.4120 0.4685 0.4271 -0.0665 -0.0588 -0.0192 113 ARG A CB 888 C CG . ARG A 113 ? 0.4252 0.4833 0.4368 -0.0634 -0.0612 -0.0192 113 ARG A CG 889 C CD . ARG A 113 ? 0.4281 0.4994 0.4454 -0.0602 -0.0641 -0.0182 113 ARG A CD 890 N NE . ARG A 113 ? 0.5187 0.5916 0.5321 -0.0572 -0.0666 -0.0181 113 ARG A NE 891 C CZ . ARG A 113 ? 0.4973 0.5759 0.5083 -0.0601 -0.0697 -0.0199 113 ARG A CZ 892 N NH1 . ARG A 113 ? 0.4415 0.5248 0.4536 -0.0666 -0.0706 -0.0220 113 ARG A NH1 893 N NH2 . ARG A 113 ? 0.5240 0.6033 0.5310 -0.0569 -0.0719 -0.0196 113 ARG A NH2 894 N N . PHE A 114 ? 0.5088 0.5381 0.5049 -0.0702 -0.0558 -0.0222 114 PHE A N 895 C CA . PHE A 114 ? 0.5261 0.5479 0.5138 -0.0742 -0.0562 -0.0246 114 PHE A CA 896 C C . PHE A 114 ? 0.6125 0.6326 0.5955 -0.0709 -0.0575 -0.0246 114 PHE A C 897 O O . PHE A 114 ? 0.5885 0.6084 0.5731 -0.0653 -0.0567 -0.0226 114 PHE A O 898 C CB . PHE A 114 ? 0.5054 0.5137 0.4878 -0.0755 -0.0527 -0.0252 114 PHE A CB 899 C CG . PHE A 114 ? 0.5991 0.5996 0.5794 -0.0698 -0.0501 -0.0238 114 PHE A CG 900 C CD1 . PHE A 114 ? 0.5379 0.5406 0.5243 -0.0653 -0.0484 -0.0214 114 PHE A CD1 901 C CD2 . PHE A 114 ? 0.5504 0.5416 0.5226 -0.0689 -0.0492 -0.0249 114 PHE A CD2 902 C CE1 . PHE A 114 ? 0.5117 0.5082 0.4963 -0.0604 -0.0459 -0.0201 114 PHE A CE1 903 C CE2 . PHE A 114 ? 0.6175 0.6026 0.5880 -0.0638 -0.0466 -0.0236 114 PHE A CE2 904 C CZ . PHE A 114 ? 0.5623 0.5504 0.5392 -0.0597 -0.0450 -0.0213 114 PHE A CZ 905 N N . GLU A 115 ? 0.6584 0.6769 0.6352 -0.0747 -0.0593 -0.0269 115 GLU A N 906 C CA . GLU A 115 ? 0.6459 0.6622 0.6173 -0.0720 -0.0605 -0.0271 115 GLU A CA 907 C C . GLU A 115 ? 0.6909 0.6937 0.6558 -0.0696 -0.0571 -0.0270 115 GLU A C 908 O O . GLU A 115 ? 0.7158 0.7093 0.6749 -0.0728 -0.0555 -0.0288 115 GLU A O 909 C CB . GLU A 115 ? 0.6854 0.7046 0.6520 -0.0771 -0.0637 -0.0296 115 GLU A CB 910 C CG . GLU A 115 ? 0.7405 0.7619 0.7034 -0.0742 -0.0660 -0.0295 115 GLU A CG 911 C CD . GLU A 115 ? 0.7603 0.7860 0.7190 -0.0794 -0.0695 -0.0321 115 GLU A CD 912 O OE1 . GLU A 115 ? 0.6988 0.7319 0.6573 -0.0773 -0.0726 -0.0318 115 GLU A OE1 913 O OE2 . GLU A 115 ? 0.8290 0.8503 0.7839 -0.0856 -0.0691 -0.0344 115 GLU A OE2 914 N N . MET A 116 ? 0.6788 0.6807 0.6446 -0.0638 -0.0560 -0.0250 116 MET A N 915 C CA . MET A 116 ? 0.6615 0.6527 0.6223 -0.0609 -0.0526 -0.0247 116 MET A CA 916 C C . MET A 116 ? 0.6626 0.6489 0.6151 -0.0606 -0.0533 -0.0260 116 MET A C 917 O O . MET A 116 ? 0.7083 0.6848 0.6539 -0.0613 -0.0513 -0.0275 116 MET A O 918 C CB . MET A 116 ? 0.6426 0.6357 0.6086 -0.0555 -0.0508 -0.0220 116 MET A CB 919 C CG . MET A 116 ? 0.6213 0.6054 0.5843 -0.0525 -0.0469 -0.0215 116 MET A CG 920 S SD . MET A 116 ? 0.6115 0.5992 0.5807 -0.0471 -0.0451 -0.0183 116 MET A SD 921 C CE . MET A 116 ? 0.5198 0.4979 0.4854 -0.0448 -0.0406 -0.0184 116 MET A CE 922 N N . PHE A 117 ? 0.6202 0.6133 0.5731 -0.0592 -0.0562 -0.0254 117 PHE A N 923 C CA . PHE A 117 ? 0.6185 0.6082 0.5635 -0.0594 -0.0574 -0.0267 117 PHE A CA 924 C C . PHE A 117 ? 0.6209 0.6193 0.5661 -0.0623 -0.0618 -0.0277 117 PHE A C 925 O O . PHE A 117 ? 0.5945 0.6017 0.5440 -0.0597 -0.0642 -0.0261 117 PHE A O 926 C CB . PHE A 117 ? 0.6217 0.6102 0.5654 -0.0540 -0.0564 -0.0246 117 PHE A CB 927 C CG . PHE A 117 ? 0.6291 0.6101 0.5720 -0.0511 -0.0521 -0.0237 117 PHE A CG 928 C CD1 . PHE A 117 ? 0.5974 0.5689 0.5329 -0.0515 -0.0498 -0.0253 117 PHE A CD1 929 C CD2 . PHE A 117 ? 0.5852 0.5689 0.5347 -0.0479 -0.0504 -0.0213 117 PHE A CD2 930 C CE1 . PHE A 117 ? 0.6249 0.5907 0.5600 -0.0484 -0.0458 -0.0245 117 PHE A CE1 931 C CE2 . PHE A 117 ? 0.6206 0.5986 0.5697 -0.0454 -0.0466 -0.0206 117 PHE A CE2 932 C CZ . PHE A 117 ? 0.6170 0.5865 0.5590 -0.0455 -0.0443 -0.0221 117 PHE A CZ 933 N N . PRO A 118 ? 0.7050 0.7009 0.6452 -0.0677 -0.0630 -0.0305 118 PRO A N 934 C CA . PRO A 118 ? 0.6757 0.6803 0.6152 -0.0708 -0.0674 -0.0318 118 PRO A CA 935 C C . PRO A 118 ? 0.6931 0.6981 0.6280 -0.0671 -0.0690 -0.0311 118 PRO A C 936 O O . PRO A 118 ? 0.6860 0.6819 0.6157 -0.0643 -0.0664 -0.0307 118 PRO A O 937 C CB . PRO A 118 ? 0.6883 0.6862 0.6207 -0.0773 -0.0674 -0.0351 118 PRO A CB 938 C CG . PRO A 118 ? 0.7265 0.7145 0.6585 -0.0778 -0.0634 -0.0353 118 PRO A CG 939 C CD . PRO A 118 ? 0.7104 0.6951 0.6446 -0.0711 -0.0605 -0.0326 118 PRO A CD 940 N N . LYS A 119 ? 0.7020 0.7175 0.6387 -0.0668 -0.0730 -0.0309 119 LYS A N 941 C CA . LYS A 119 ? 0.7494 0.7652 0.6813 -0.0630 -0.0747 -0.0300 119 LYS A CA 942 C C . LYS A 119 ? 0.7691 0.7756 0.6906 -0.0652 -0.0743 -0.0322 119 LYS A C 943 O O . LYS A 119 ? 0.8005 0.8037 0.7167 -0.0619 -0.0743 -0.0314 119 LYS A O 944 C CB . LYS A 119 ? 0.6948 0.7240 0.6301 -0.0623 -0.0794 -0.0295 119 LYS A CB 945 C CG . LYS A 119 ? 0.6966 0.7362 0.6421 -0.0610 -0.0802 -0.0280 119 LYS A CG 946 C CD . LYS A 119 ? 0.6762 0.7267 0.6241 -0.0567 -0.0840 -0.0264 119 LYS A CD 947 C CE . LYS A 119 ? 0.6731 0.7376 0.6298 -0.0581 -0.0864 -0.0265 119 LYS A CE 948 N NZ . LYS A 119 ? 0.7258 0.8003 0.6854 -0.0522 -0.0895 -0.0244 119 LYS A NZ 949 N N . SER A 120 ? 0.7152 0.7171 0.6335 -0.0709 -0.0737 -0.0350 120 SER A N 950 C CA . SER A 120 ? 0.7470 0.7389 0.6549 -0.0733 -0.0730 -0.0374 120 SER A CA 951 C C . SER A 120 ? 0.7966 0.7767 0.7003 -0.0693 -0.0685 -0.0365 120 SER A C 952 O O . SER A 120 ? 0.8294 0.8015 0.7243 -0.0694 -0.0676 -0.0379 120 SER A O 953 C CB . SER A 120 ? 0.7938 0.7823 0.6987 -0.0805 -0.0731 -0.0405 120 SER A CB 954 O OG . SER A 120 ? 0.8499 0.8282 0.7542 -0.0808 -0.0689 -0.0407 120 SER A OG 955 N N . THR A 121 ? 0.8028 0.7825 0.7128 -0.0659 -0.0657 -0.0342 121 THR A N 956 C CA . THR A 121 ? 0.8501 0.8208 0.7575 -0.0619 -0.0614 -0.0332 121 THR A CA 957 C C . THR A 121 ? 0.8217 0.7916 0.7244 -0.0581 -0.0617 -0.0320 121 THR A C 958 O O . THR A 121 ? 0.7755 0.7369 0.6717 -0.0566 -0.0589 -0.0325 121 THR A O 959 C CB . THR A 121 ? 0.7563 0.7289 0.6722 -0.0588 -0.0589 -0.0308 121 THR A CB 960 O OG1 . THR A 121 ? 0.8106 0.7782 0.7276 -0.0615 -0.0567 -0.0320 121 THR A OG1 961 N N . TRP A 122 ? 0.6976 0.6763 0.6032 -0.0564 -0.0649 -0.0304 122 TRP A N 962 C CA . TRP A 122 ? 0.7836 0.7616 0.6852 -0.0523 -0.0651 -0.0287 122 TRP A CA 963 C C . TRP A 122 ? 0.7961 0.7734 0.6891 -0.0540 -0.0680 -0.0304 122 TRP A C 964 O O . TRP A 122 ? 0.7342 0.7197 0.6282 -0.0549 -0.0723 -0.0305 122 TRP A O 965 C CB . TRP A 122 ? 0.7540 0.7401 0.6624 -0.0487 -0.0667 -0.0257 122 TRP A CB 966 C CG . TRP A 122 ? 0.7758 0.7643 0.6932 -0.0480 -0.0647 -0.0244 122 TRP A CG 967 C CD1 . TRP A 122 ? 0.7496 0.7467 0.6749 -0.0490 -0.0667 -0.0241 122 TRP A CD1 968 C CD2 . TRP A 122 ? 0.7103 0.6928 0.6296 -0.0463 -0.0602 -0.0235 122 TRP A CD2 969 N NE1 . TRP A 122 ? 0.6911 0.6872 0.6227 -0.0480 -0.0638 -0.0229 122 TRP A NE1 970 C CE2 . TRP A 122 ? 0.7029 0.6903 0.6310 -0.0463 -0.0599 -0.0225 122 TRP A CE2 971 C CE3 . TRP A 122 ? 0.7174 0.6916 0.6317 -0.0446 -0.0565 -0.0234 122 TRP A CE3 972 C CZ2 . TRP A 122 ? 0.7045 0.6884 0.6364 -0.0448 -0.0561 -0.0214 122 TRP A CZ2 973 C CZ3 . TRP A 122 ? 0.7345 0.7061 0.6530 -0.0430 -0.0528 -0.0223 122 TRP A CZ3 974 C CH2 . TRP A 122 ? 0.6739 0.6502 0.6011 -0.0431 -0.0527 -0.0213 122 TRP A CH2 975 N N . ALA A 123 ? 0.7765 0.7447 0.6612 -0.0540 -0.0657 -0.0317 123 ALA A N 976 C CA . ALA A 123 ? 0.8650 0.8309 0.7405 -0.0562 -0.0680 -0.0338 123 ALA A CA 977 C C . ALA A 123 ? 0.8768 0.8435 0.7475 -0.0526 -0.0692 -0.0320 123 ALA A C 978 O O . ALA A 123 ? 0.8347 0.7969 0.7038 -0.0490 -0.0661 -0.0302 123 ALA A O 979 C CB . ALA A 123 ? 0.8199 0.7749 0.6880 -0.0583 -0.0649 -0.0365 123 ALA A CB 980 N N . GLY A 124 ? 0.8710 0.8433 0.7388 -0.0537 -0.0737 -0.0327 124 GLY A N 981 C CA . GLY A 124 ? 0.9229 0.8954 0.7847 -0.0505 -0.0753 -0.0311 124 GLY A CA 982 C C . GLY A 124 ? 0.9414 0.9206 0.8086 -0.0461 -0.0768 -0.0277 124 GLY A C 983 O O . GLY A 124 ? 0.9329 0.9097 0.7953 -0.0425 -0.0766 -0.0256 124 GLY A O 984 N N . VAL A 125 ? 0.7944 0.7817 0.6709 -0.0463 -0.0783 -0.0271 125 VAL A N 985 C CA . VAL A 125 ? 0.7673 0.7611 0.6492 -0.0420 -0.0798 -0.0240 125 VAL A CA 986 C C . VAL A 125 ? 0.7981 0.8040 0.6870 -0.0432 -0.0840 -0.0245 125 VAL A C 987 O O . VAL A 125 ? 0.7671 0.7759 0.6582 -0.0481 -0.0849 -0.0271 125 VAL A O 988 C CB . VAL A 125 ? 0.7838 0.7741 0.6714 -0.0396 -0.0756 -0.0218 125 VAL A CB 989 C CG1 . VAL A 125 ? 0.6718 0.6532 0.5531 -0.0368 -0.0722 -0.0202 125 VAL A CG1 990 C CG2 . VAL A 125 ? 0.7250 0.7132 0.6174 -0.0432 -0.0729 -0.0237 125 VAL A CG2 991 N N . ASP A 126 ? 0.7745 0.7873 0.6667 -0.0389 -0.0864 -0.0220 126 ASP A N 992 C CA . ASP A 126 ? 0.8217 0.8474 0.7210 -0.0394 -0.0903 -0.0223 126 ASP A CA 993 C C . ASP A 126 ? 0.8619 0.8914 0.7715 -0.0386 -0.0886 -0.0211 126 ASP A C 994 O O . ASP A 126 ? 0.7573 0.7834 0.6688 -0.0344 -0.0863 -0.0185 126 ASP A O 995 C CB . ASP A 126 ? 0.8161 0.8484 0.7126 -0.0348 -0.0947 -0.0206 126 ASP A CB 996 C CG . ASP A 126 ? 0.9289 0.9760 0.8319 -0.0355 -0.0991 -0.0215 126 ASP A CG 997 O OD1 . ASP A 126 ? 0.9805 1.0325 0.8869 -0.0413 -0.0999 -0.0243 126 ASP A OD1 998 O OD2 . ASP A 126 ? 0.9529 1.0069 0.8575 -0.0303 -0.1018 -0.0193 126 ASP A OD2 999 N N . THR A 127 ? 0.7816 0.8182 0.6974 -0.0430 -0.0897 -0.0231 127 THR A N 1000 C CA . THR A 127 ? 0.7208 0.7612 0.6461 -0.0431 -0.0880 -0.0224 127 THR A CA 1001 C C . THR A 127 ? 0.7586 0.8138 0.6910 -0.0428 -0.0919 -0.0224 127 THR A C 1002 O O . THR A 127 ? 0.8007 0.8610 0.7411 -0.0442 -0.0912 -0.0225 127 THR A O 1003 C CB . THR A 127 ? 0.7472 0.7823 0.6741 -0.0489 -0.0850 -0.0247 127 THR A CB 1004 O OG1 . THR A 127 ? 0.7230 0.7634 0.6488 -0.0546 -0.0878 -0.0277 127 THR A OG1 1005 C CG2 . THR A 127 ? 0.6413 0.6626 0.5611 -0.0490 -0.0810 -0.0250 127 THR A CG2 1006 N N . SER A 128 ? 0.6562 0.7185 0.5854 -0.0407 -0.0962 -0.0223 128 SER A N 1007 C CA . SER A 128 ? 0.6865 0.7644 0.6218 -0.0406 -0.1004 -0.0227 128 SER A CA 1008 C C . SER A 128 ? 0.6729 0.7568 0.6090 -0.0328 -0.1028 -0.0199 128 SER A C 1009 O O . SER A 128 ? 0.6416 0.7393 0.5832 -0.0313 -0.1062 -0.0199 128 SER A O 1010 C CB . SER A 128 ? 0.7094 0.7936 0.6411 -0.0458 -0.1040 -0.0258 128 SER A CB 1011 O OG . SER A 128 ? 0.7717 0.8485 0.6934 -0.0447 -0.1048 -0.0259 128 SER A OG 1012 N N . ARG A 129 ? 0.9727 1.0463 0.9029 -0.0278 -0.1010 -0.0174 129 ARG A N 1013 C CA . ARG A 129 ? 1.0697 1.1462 0.9978 -0.0202 -0.1033 -0.0146 129 ARG A CA 1014 C C . ARG A 129 ? 1.0508 1.1206 0.9813 -0.0156 -0.0999 -0.0118 129 ARG A C 1015 O O . ARG A 129 ? 1.0000 1.0678 0.9269 -0.0092 -0.1008 -0.0092 129 ARG A O 1016 C CB . ARG A 129 ? 1.0979 1.1681 1.0149 -0.0182 -0.1049 -0.0142 129 ARG A CB 1017 C CG . ARG A 129 ? 1.2484 1.3271 1.1626 -0.0123 -0.1097 -0.0128 129 ARG A CG 1018 C CD . ARG A 129 ? 1.3016 1.3778 1.2057 -0.0128 -0.1123 -0.0136 129 ARG A CD 1019 N NE . ARG A 129 ? 1.3841 1.4674 1.2895 -0.0197 -0.1144 -0.0172 129 ARG A NE 1020 C CZ . ARG A 129 ? 1.3912 1.4661 1.2910 -0.0253 -0.1126 -0.0194 129 ARG A CZ 1021 N NH1 . ARG A 129 ? 1.3185 1.3787 1.2118 -0.0245 -0.1088 -0.0183 129 ARG A NH1 1022 N NH2 . ARG A 129 ? 1.2972 1.3785 1.1977 -0.0316 -0.1147 -0.0227 129 ARG A NH2 1023 N N . GLY A 130 ? 0.9823 1.0484 0.9184 -0.0190 -0.0961 -0.0123 130 GLY A N 1024 C CA . GLY A 130 ? 0.7815 0.8412 0.7201 -0.0156 -0.0927 -0.0099 130 GLY A CA 1025 C C . GLY A 130 ? 0.8076 0.8770 0.7547 -0.0125 -0.0937 -0.0088 130 GLY A C 1026 O O . GLY A 130 ? 0.7655 0.8357 0.7198 -0.0147 -0.0912 -0.0091 130 GLY A O 1027 N N . VAL A 131 ? 0.6694 0.7463 0.6155 -0.0070 -0.0974 -0.0075 131 VAL A N 1028 C CA . VAL A 131 ? 0.6110 0.6972 0.5642 -0.0029 -0.0986 -0.0064 131 VAL A CA 1029 C C . VAL A 131 ? 0.6629 0.7438 0.6109 0.0052 -0.0988 -0.0032 131 VAL A C 1030 O O . VAL A 131 ? 0.6481 0.7190 0.5868 0.0073 -0.0985 -0.0019 131 VAL A O 1031 C CB . VAL A 131 ? 0.6685 0.7720 0.6269 -0.0035 -0.1031 -0.0081 131 VAL A CB 1032 C CG1 . VAL A 131 ? 0.5441 0.6524 0.5072 -0.0121 -0.1028 -0.0113 131 VAL A CG1 1033 C CG2 . VAL A 131 ? 0.6562 0.7628 0.6071 0.0002 -0.1074 -0.0078 131 VAL A CG2 1034 N N . THR A 132 ? 0.6486 0.7360 0.6023 0.0096 -0.0993 -0.0020 132 THR A N 1035 C CA . THR A 132 ? 0.6192 0.7011 0.5679 0.0174 -0.0994 0.0010 132 THR A CA 1036 C C . THR A 132 ? 0.6656 0.7594 0.6215 0.0222 -0.1013 0.0015 132 THR A C 1037 O O . THR A 132 ? 0.6527 0.7551 0.6182 0.0187 -0.1005 0.0001 132 THR A O 1038 C CB . THR A 132 ? 0.6195 0.6858 0.5650 0.0172 -0.0946 0.0027 132 THR A CB 1039 O OG1 . THR A 132 ? 0.6526 0.7141 0.5940 0.0245 -0.0946 0.0055 132 THR A OG1 1040 C CG2 . THR A 132 ? 0.6401 0.7077 0.5948 0.0123 -0.0912 0.0015 132 THR A CG2 1041 N N . ASN A 133 ? 0.6449 0.7390 0.5957 0.0302 -0.1036 0.0036 133 ASN A N 1042 C CA . ASN A 133 ? 0.6794 0.7840 0.6361 0.0359 -0.1051 0.0043 133 ASN A CA 1043 C C . ASN A 133 ? 0.7022 0.7978 0.6604 0.0378 -0.1011 0.0060 133 ASN A C 1044 O O . ASN A 133 ? 0.6307 0.7326 0.5931 0.0428 -0.1017 0.0067 133 ASN A O 1045 C CB . ASN A 133 ? 0.6965 0.8059 0.6472 0.0445 -0.1094 0.0058 133 ASN A CB 1046 C CG . ASN A 133 ? 0.8208 0.9139 0.7582 0.0484 -0.1089 0.0082 133 ASN A CG 1047 O OD1 . ASN A 133 ? 0.8469 0.9247 0.7798 0.0461 -0.1050 0.0092 133 ASN A OD1 1048 N ND2 . ASN A 133 ? 0.8251 0.9215 0.7557 0.0545 -0.1130 0.0091 133 ASN A ND2 1049 N N . ALA A 134 ? 0.7966 0.8778 0.7513 0.0337 -0.0972 0.0064 134 ALA A N 1050 C CA . ALA A 134 ? 0.8654 0.9392 0.8229 0.0335 -0.0931 0.0075 134 ALA A CA 1051 C C . ALA A 134 ? 0.7930 0.8769 0.7624 0.0282 -0.0919 0.0054 134 ALA A C 1052 O O . ALA A 134 ? 0.7387 0.8236 0.7133 0.0296 -0.0901 0.0059 134 ALA A O 1053 C CB . ALA A 134 ? 0.8187 0.8759 0.7694 0.0303 -0.0894 0.0084 134 ALA A CB 1054 N N . CYS A 135 ? 0.6777 0.7685 0.6509 0.0220 -0.0930 0.0030 135 CYS A N 1055 C CA . CYS A 135 ? 0.6503 0.7497 0.6337 0.0161 -0.0918 0.0009 135 CYS A CA 1056 C C . CYS A 135 ? 0.6368 0.7535 0.6259 0.0148 -0.0957 -0.0011 135 CYS A C 1057 O O . CYS A 135 ? 0.6326 0.7526 0.6225 0.0087 -0.0965 -0.0032 135 CYS A O 1058 C CB . CYS A 135 ? 0.6321 0.7231 0.6150 0.0086 -0.0888 -0.0004 135 CYS A CB 1059 S SG . CYS A 135 ? 0.8034 0.8760 0.7808 0.0089 -0.0839 0.0016 135 CYS A SG 1060 N N . PRO A 136 ? 0.5270 0.6551 0.5201 0.0204 -0.0980 -0.0005 136 PRO A N 1061 C CA . PRO A 136 ? 0.5700 0.7165 0.5695 0.0189 -0.1016 -0.0025 136 PRO A CA 1062 C C . PRO A 136 ? 0.6124 0.7667 0.6219 0.0121 -0.0998 -0.0045 136 PRO A C 1063 O O . PRO A 136 ? 0.5975 0.7460 0.6102 0.0116 -0.0963 -0.0037 136 PRO A O 1064 C CB . PRO A 136 ? 0.6067 0.7617 0.6068 0.0281 -0.1041 -0.0009 136 PRO A CB 1065 C CG . PRO A 136 ? 0.5021 0.6450 0.5005 0.0321 -0.1005 0.0013 136 PRO A CG 1066 C CD . PRO A 136 ? 0.5919 0.7166 0.5833 0.0284 -0.0974 0.0019 136 PRO A CD 1067 N N . SER A 137 ? 0.6405 0.8075 0.6544 0.0067 -0.1021 -0.0069 137 SER A N 1068 C CA . SER A 137 ? 0.5721 0.7496 0.5956 0.0011 -0.1011 -0.0087 137 SER A CA 1069 C C . SER A 137 ? 0.6325 0.8278 0.6622 0.0063 -0.1039 -0.0086 137 SER A C 1070 O O . SER A 137 ? 0.6327 0.8294 0.6588 0.0148 -0.1060 -0.0069 137 SER A O 1071 C CB . SER A 137 ? 0.5970 0.7783 0.6215 -0.0083 -0.1018 -0.0116 137 SER A CB 1072 O OG . SER A 137 ? 0.7004 0.8943 0.7240 -0.0081 -0.1063 -0.0129 137 SER A OG 1073 N N . TYR A 138 ? 0.6266 0.8353 0.6651 0.0015 -0.1038 -0.0104 138 TYR A N 1074 C CA . TYR A 138 ? 0.6648 0.8924 0.7098 0.0060 -0.1064 -0.0105 138 TYR A CA 1075 C C . TYR A 138 ? 0.6930 0.9361 0.7381 0.0054 -0.1113 -0.0122 138 TYR A C 1076 O O . TYR A 138 ? 0.6591 0.9200 0.7094 0.0094 -0.1140 -0.0125 138 TYR A O 1077 C CB . TYR A 138 ? 0.6108 0.8470 0.6655 0.0013 -0.1041 -0.0116 138 TYR A CB 1078 C CG . TYR A 138 ? 0.6738 0.8998 0.7297 0.0049 -0.1002 -0.0097 138 TYR A CG 1079 C CD1 . TYR A 138 ? 0.6679 0.8875 0.7273 -0.0017 -0.0964 -0.0102 138 TYR A CD1 1080 C CD2 . TYR A 138 ? 0.6712 0.8939 0.7242 0.0150 -0.1005 -0.0073 138 TYR A CD2 1081 C CE1 . TYR A 138 ? 0.6105 0.8214 0.6710 0.0015 -0.0930 -0.0085 138 TYR A CE1 1082 C CE2 . TYR A 138 ? 0.6903 0.9035 0.7440 0.0179 -0.0969 -0.0057 138 TYR A CE2 1083 C CZ . TYR A 138 ? 0.7297 0.9375 0.7874 0.0111 -0.0933 -0.0063 138 TYR A CZ 1084 O OH . TYR A 138 ? 0.6600 0.8589 0.7183 0.0139 -0.0899 -0.0047 138 TYR A OH 1085 N N . THR A 139 ? 0.6514 0.8881 0.6905 0.0006 -0.1123 -0.0133 139 THR A N 1086 C CA . THR A 139 ? 0.7110 0.9617 0.7496 -0.0012 -0.1169 -0.0151 139 THR A CA 1087 C C . THR A 139 ? 0.7596 1.0022 0.7880 0.0033 -0.1194 -0.0141 139 THR A C 1088 O O . THR A 139 ? 0.7920 1.0474 0.8195 0.0057 -0.1238 -0.0148 139 THR A O 1089 C CB . THR A 139 ? 0.7051 0.9605 0.7468 -0.0132 -0.1167 -0.0183 139 THR A CB 1090 O OG1 . THR A 139 ? 0.7500 0.9858 0.7863 -0.0186 -0.1132 -0.0184 139 THR A OG1 1091 C CG2 . THR A 139 ? 0.6059 0.8743 0.6579 -0.0173 -0.1153 -0.0195 139 THR A CG2 1092 N N . LEU A 140 ? 0.7713 0.9933 0.7921 0.0042 -0.1167 -0.0125 140 LEU A N 1093 C CA . LEU A 140 ? 0.7828 0.9956 0.7933 0.0088 -0.1185 -0.0113 140 LEU A CA 1094 C C . LEU A 140 ? 0.8095 1.0061 0.8139 0.0165 -0.1161 -0.0080 140 LEU A C 1095 O O . LEU A 140 ? 0.7578 0.9446 0.7642 0.0156 -0.1120 -0.0071 140 LEU A O 1096 C CB . LEU A 140 ? 0.7580 0.9613 0.7629 0.0009 -0.1180 -0.0130 140 LEU A CB 1097 C CG . LEU A 140 ? 0.8357 1.0359 0.8448 -0.0094 -0.1150 -0.0153 140 LEU A CG 1098 C CD1 . LEU A 140 ? 0.7596 0.9421 0.7604 -0.0136 -0.1128 -0.0156 140 LEU A CD1 1099 C CD2 . LEU A 140 ? 0.8859 1.1039 0.9008 -0.0162 -0.1178 -0.0183 140 LEU A CD2 1100 N N . ASP A 141 ? 0.9345 1.1283 0.9310 0.0240 -0.1188 -0.0063 141 ASP A N 1101 C CA . ASP A 141 ? 0.9336 1.1121 0.9229 0.0315 -0.1169 -0.0032 141 ASP A CA 1102 C C . ASP A 141 ? 0.8454 1.0037 0.8277 0.0273 -0.1132 -0.0026 141 ASP A C 1103 O O . ASP A 141 ? 0.8387 0.9833 0.8172 0.0306 -0.1101 -0.0005 141 ASP A O 1104 C CB . ASP A 141 ? 0.9850 1.1663 0.9669 0.0406 -0.1209 -0.0015 141 ASP A CB 1105 C CG . ASP A 141 ? 1.1866 1.3897 1.1753 0.0451 -0.1250 -0.0023 141 ASP A CG 1106 O OD1 . ASP A 141 ? 1.1445 1.3511 1.1359 0.0522 -0.1246 -0.0008 141 ASP A OD1 1107 O OD2 . ASP A 141 ? 1.2089 1.4260 1.2001 0.0416 -0.1285 -0.0044 141 ASP A OD2 1108 N N . SER A 142 ? 0.6426 0.7995 0.6234 0.0198 -0.1134 -0.0047 142 SER A N 1109 C CA . SER A 142 ? 0.6499 0.7889 0.6241 0.0159 -0.1100 -0.0044 142 SER A CA 1110 C C . SER A 142 ? 0.6818 0.8196 0.6606 0.0061 -0.1075 -0.0069 142 SER A C 1111 O O . SER A 142 ? 0.7304 0.8745 0.7094 0.0006 -0.1096 -0.0093 142 SER A O 1112 C CB . SER A 142 ? 0.6536 0.7866 0.6172 0.0178 -0.1123 -0.0039 142 SER A CB 1113 O OG . SER A 142 ? 0.6620 0.7932 0.6198 0.0272 -0.1142 -0.0012 142 SER A OG 1114 N N . SER A 143 ? 0.6761 0.8054 0.6581 0.0040 -0.1032 -0.0064 143 SER A N 1115 C CA . SER A 143 ? 0.6765 0.8022 0.6619 -0.0045 -0.1003 -0.0085 143 SER A CA 1116 C C . SER A 143 ? 0.6668 0.7752 0.6482 -0.0051 -0.0957 -0.0071 143 SER A C 1117 O O . SER A 143 ? 0.6756 0.7742 0.6497 -0.0004 -0.0951 -0.0051 143 SER A O 1118 C CB . SER A 143 ? 0.6109 0.7483 0.6069 -0.0074 -0.0998 -0.0096 143 SER A CB 1119 O OG . SER A 143 ? 0.6459 0.7830 0.6444 -0.0161 -0.0985 -0.0121 143 SER A OG 1120 N N . PHE A 144 ? 0.5794 0.6842 0.5652 -0.0107 -0.0924 -0.0083 144 PHE A N 1121 C CA . PHE A 144 ? 0.5427 0.6328 0.5256 -0.0116 -0.0879 -0.0072 144 PHE A CA 1122 C C . PHE A 144 ? 0.5610 0.6511 0.5510 -0.0166 -0.0849 -0.0083 144 PHE A C 1123 O O . PHE A 144 ? 0.5466 0.6469 0.5427 -0.0204 -0.0861 -0.0101 144 PHE A O 1124 C CB . PHE A 144 ? 0.4871 0.5672 0.4617 -0.0142 -0.0873 -0.0080 144 PHE A CB 1125 C CG . PHE A 144 ? 0.5079 0.5736 0.4776 -0.0129 -0.0834 -0.0063 144 PHE A CG 1126 C CD1 . PHE A 144 ? 0.5099 0.5703 0.4755 -0.0069 -0.0830 -0.0036 144 PHE A CD1 1127 C CD2 . PHE A 144 ? 0.4493 0.5066 0.4178 -0.0177 -0.0801 -0.0075 144 PHE A CD2 1128 C CE1 . PHE A 144 ? 0.4355 0.4832 0.3964 -0.0063 -0.0794 -0.0022 144 PHE A CE1 1129 C CE2 . PHE A 144 ? 0.4648 0.5104 0.4291 -0.0166 -0.0765 -0.0060 144 PHE A CE2 1130 C CZ . PHE A 144 ? 0.4374 0.4784 0.3980 -0.0113 -0.0762 -0.0034 144 PHE A CZ 1131 N N . TYR A 145 ? 0.5711 0.6500 0.5600 -0.0167 -0.0809 -0.0073 145 TYR A N 1132 C CA . TYR A 145 ? 0.5742 0.6514 0.5688 -0.0209 -0.0777 -0.0080 145 TYR A CA 1133 C C . TYR A 145 ? 0.5608 0.6395 0.5560 -0.0279 -0.0778 -0.0108 145 TYR A C 1134 O O . TYR A 145 ? 0.5994 0.6726 0.5883 -0.0301 -0.0782 -0.0119 145 TYR A O 1135 C CB . TYR A 145 ? 0.5634 0.6279 0.5552 -0.0199 -0.0737 -0.0066 145 TYR A CB 1136 C CG . TYR A 145 ? 0.5446 0.6060 0.5346 -0.0137 -0.0733 -0.0039 145 TYR A CG 1137 C CD1 . TYR A 145 ? 0.5279 0.5933 0.5238 -0.0112 -0.0726 -0.0028 145 TYR A CD1 1138 C CD2 . TYR A 145 ? 0.5534 0.6074 0.5352 -0.0105 -0.0736 -0.0026 145 TYR A CD2 1139 C CE1 . TYR A 145 ? 0.5437 0.6052 0.5372 -0.0056 -0.0722 -0.0005 145 TYR A CE1 1140 C CE2 . TYR A 145 ? 0.5677 0.6176 0.5468 -0.0051 -0.0731 -0.0002 145 TYR A CE2 1141 C CZ . TYR A 145 ? 0.5500 0.6035 0.5348 -0.0027 -0.0724 0.0008 145 TYR A CZ 1142 O OH . TYR A 145 ? 0.5707 0.6190 0.5520 0.0025 -0.0719 0.0031 145 TYR A OH 1143 N N . ARG A 146 ? 0.5517 0.6371 0.5538 -0.0315 -0.0775 -0.0119 146 ARG A N 1144 C CA . ARG A 146 ? 0.5869 0.6736 0.5894 -0.0386 -0.0776 -0.0146 146 ARG A CA 1145 C C . ARG A 146 ? 0.6004 0.6737 0.5984 -0.0417 -0.0740 -0.0152 146 ARG A C 1146 O O . ARG A 146 ? 0.6385 0.7089 0.6330 -0.0468 -0.0742 -0.0173 146 ARG A O 1147 C CB . ARG A 146 ? 0.5797 0.6760 0.5904 -0.0417 -0.0775 -0.0153 146 ARG A CB 1148 C CG . ARG A 146 ? 0.5924 0.7035 0.6087 -0.0384 -0.0806 -0.0148 146 ARG A CG 1149 C CD . ARG A 146 ? 0.6324 0.7529 0.6467 -0.0397 -0.0849 -0.0163 146 ARG A CD 1150 N NE . ARG A 146 ? 0.6899 0.8254 0.7095 -0.0357 -0.0879 -0.0157 146 ARG A NE 1151 C CZ . ARG A 146 ? 0.7084 0.8533 0.7263 -0.0339 -0.0920 -0.0163 146 ARG A CZ 1152 N NH1 . ARG A 146 ? 0.6535 0.7941 0.6645 -0.0362 -0.0935 -0.0175 146 ARG A NH1 1153 N NH2 . ARG A 146 ? 0.6243 0.7832 0.6473 -0.0296 -0.0945 -0.0157 146 ARG A NH2 1154 N N . ASN A 147 ? 0.5396 0.6046 0.5374 -0.0385 -0.0709 -0.0133 147 ASN A N 1155 C CA . ASN A 147 ? 0.5338 0.5872 0.5283 -0.0407 -0.0673 -0.0138 147 ASN A CA 1156 C C . ASN A 147 ? 0.5638 0.6082 0.5505 -0.0384 -0.0665 -0.0132 147 ASN A C 1157 O O . ASN A 147 ? 0.5131 0.5482 0.4963 -0.0397 -0.0635 -0.0136 147 ASN A O 1158 C CB . ASN A 147 ? 0.4825 0.5332 0.4819 -0.0395 -0.0640 -0.0123 147 ASN A CB 1159 C CG . ASN A 147 ? 0.5540 0.6126 0.5607 -0.0422 -0.0643 -0.0129 147 ASN A CG 1160 O OD1 . ASN A 147 ? 0.5023 0.5652 0.5094 -0.0469 -0.0658 -0.0149 147 ASN A OD1 1161 N ND2 . ASN A 147 ? 0.4853 0.5457 0.4973 -0.0395 -0.0628 -0.0113 147 ASN A ND2 1162 N N . LEU A 148 ? 0.6041 0.6513 0.5878 -0.0349 -0.0690 -0.0122 148 LEU A N 1163 C CA . LEU A 148 ? 0.6267 0.6658 0.6024 -0.0328 -0.0684 -0.0116 148 LEU A CA 1164 C C . LEU A 148 ? 0.6244 0.6670 0.5950 -0.0334 -0.0721 -0.0128 148 LEU A C 1165 O O . LEU A 148 ? 0.6362 0.6890 0.6100 -0.0338 -0.0755 -0.0134 148 LEU A O 1166 C CB . LEU A 148 ? 0.6126 0.6492 0.5878 -0.0274 -0.0675 -0.0088 148 LEU A CB 1167 C CG . LEU A 148 ? 0.6153 0.6479 0.5946 -0.0267 -0.0638 -0.0076 148 LEU A CG 1168 C CD1 . LEU A 148 ? 0.5717 0.6010 0.5491 -0.0218 -0.0631 -0.0050 148 LEU A CD1 1169 C CD2 . LEU A 148 ? 0.5981 0.6223 0.5749 -0.0296 -0.0604 -0.0086 148 LEU A CD2 1170 N N . VAL A 149 ? 0.5322 0.5671 0.4950 -0.0335 -0.0715 -0.0132 149 VAL A N 1171 C CA . VAL A 149 ? 0.5943 0.6318 0.5514 -0.0335 -0.0750 -0.0140 149 VAL A CA 1172 C C . VAL A 149 ? 0.5186 0.5492 0.4681 -0.0295 -0.0746 -0.0123 149 VAL A C 1173 O O . VAL A 149 ? 0.5035 0.5246 0.4487 -0.0299 -0.0714 -0.0121 149 VAL A O 1174 C CB . VAL A 149 ? 0.6041 0.6404 0.5580 -0.0393 -0.0755 -0.0171 149 VAL A CB 1175 C CG1 . VAL A 149 ? 0.6155 0.6404 0.5661 -0.0413 -0.0713 -0.0179 149 VAL A CG1 1176 C CG2 . VAL A 149 ? 0.5970 0.6349 0.5440 -0.0391 -0.0789 -0.0179 149 VAL A CG2 1177 N N . TRP A 150 ? 0.5251 0.5607 0.4729 -0.0256 -0.0778 -0.0110 150 TRP A N 1178 C CA . TRP A 150 ? 0.6129 0.6420 0.5528 -0.0216 -0.0778 -0.0091 150 TRP A CA 1179 C C . TRP A 150 ? 0.6256 0.6518 0.5576 -0.0238 -0.0792 -0.0108 150 TRP A C 1180 O O . TRP A 150 ? 0.6974 0.7309 0.6284 -0.0244 -0.0831 -0.0119 150 TRP A O 1181 C CB . TRP A 150 ? 0.6143 0.6496 0.5548 -0.0162 -0.0809 -0.0071 150 TRP A CB 1182 C CG . TRP A 150 ? 0.5994 0.6268 0.5318 -0.0116 -0.0805 -0.0046 150 TRP A CG 1183 C CD1 . TRP A 150 ? 0.5930 0.6103 0.5172 -0.0122 -0.0785 -0.0043 150 TRP A CD1 1184 C CD2 . TRP A 150 ? 0.5826 0.6112 0.5138 -0.0056 -0.0821 -0.0021 150 TRP A CD2 1185 N NE1 . TRP A 150 ? 0.5832 0.5952 0.5010 -0.0075 -0.0786 -0.0017 150 TRP A NE1 1186 C CE2 . TRP A 150 ? 0.6045 0.6228 0.5262 -0.0033 -0.0809 -0.0003 150 TRP A CE2 1187 C CE3 . TRP A 150 ? 0.6035 0.6408 0.5404 -0.0020 -0.0843 -0.0012 150 TRP A CE3 1188 C CZ2 . TRP A 150 ? 0.6581 0.6732 0.5750 0.0025 -0.0818 0.0024 150 TRP A CZ2 1189 C CZ3 . TRP A 150 ? 0.6632 0.6977 0.5956 0.0043 -0.0853 0.0014 150 TRP A CZ3 1190 C CH2 . TRP A 150 ? 0.6737 0.6967 0.5959 0.0064 -0.0841 0.0032 150 TRP A CH2 1191 N N . LEU A 151 ? 0.7386 0.7546 0.6648 -0.0250 -0.0760 -0.0109 151 LEU A N 1192 C CA . LEU A 151 ? 0.7899 0.8019 0.7081 -0.0273 -0.0767 -0.0126 151 LEU A CA 1193 C C . LEU A 151 ? 0.8244 0.8329 0.7341 -0.0234 -0.0782 -0.0109 151 LEU A C 1194 O O . LEU A 151 ? 0.8379 0.8403 0.7449 -0.0203 -0.0760 -0.0085 151 LEU A O 1195 C CB . LEU A 151 ? 0.7922 0.7952 0.7082 -0.0303 -0.0724 -0.0139 151 LEU A CB 1196 C CG . LEU A 151 ? 0.8012 0.8060 0.7246 -0.0338 -0.0706 -0.0155 151 LEU A CG 1197 C CD1 . LEU A 151 ? 0.7393 0.7352 0.6599 -0.0361 -0.0665 -0.0168 151 LEU A CD1 1198 C CD2 . LEU A 151 ? 0.8728 0.8855 0.7987 -0.0373 -0.0742 -0.0178 151 LEU A CD2 1199 N N . VAL A 152 ? 0.8261 0.8386 0.7313 -0.0239 -0.0820 -0.0120 152 VAL A N 1200 C CA . VAL A 152 ? 0.8448 0.8540 0.7408 -0.0204 -0.0838 -0.0106 152 VAL A CA 1201 C C . VAL A 152 ? 0.8056 0.8106 0.6938 -0.0238 -0.0841 -0.0128 152 VAL A C 1202 O O . VAL A 152 ? 0.7681 0.7767 0.6583 -0.0282 -0.0851 -0.0156 152 VAL A O 1203 C CB . VAL A 152 ? 0.8233 0.8422 0.7205 -0.0166 -0.0888 -0.0095 152 VAL A CB 1204 C CG1 . VAL A 152 ? 0.9757 0.9913 0.8627 -0.0131 -0.0911 -0.0082 152 VAL A CG1 1205 C CG2 . VAL A 152 ? 0.8133 0.8350 0.7170 -0.0126 -0.0882 -0.0071 152 VAL A CG2 1206 N N . LYS A 153 ? 0.8045 0.8014 0.6834 -0.0219 -0.0830 -0.0116 153 LYS A N 1207 C CA . LYS A 153 ? 0.8813 0.8740 0.7519 -0.0246 -0.0834 -0.0137 153 LYS A CA 1208 C C . LYS A 153 ? 0.8534 0.8548 0.7225 -0.0254 -0.0888 -0.0152 153 LYS A C 1209 O O . LYS A 153 ? 0.7643 0.7739 0.6364 -0.0222 -0.0924 -0.0139 153 LYS A O 1210 C CB . LYS A 153 ? 0.8603 0.8433 0.7210 -0.0223 -0.0813 -0.0118 153 LYS A CB 1211 C CG . LYS A 153 ? 0.8865 0.8706 0.7405 -0.0179 -0.0850 -0.0097 153 LYS A CG 1212 C CD . LYS A 153 ? 0.9117 0.8851 0.7557 -0.0160 -0.0822 -0.0077 153 LYS A CD 1213 C CE . LYS A 153 ? 1.0266 0.9997 0.8612 -0.0127 -0.0861 -0.0064 153 LYS A CE 1214 N NZ . LYS A 153 ? 1.0005 0.9810 0.8382 -0.0081 -0.0903 -0.0045 153 LYS A NZ 1215 N N . THR A 154 ? 0.9768 0.9765 0.8410 -0.0295 -0.0894 -0.0181 154 THR A N 1216 C CA . THR A 154 ? 1.1319 1.1403 0.9948 -0.0314 -0.0945 -0.0201 154 THR A CA 1217 C C . THR A 154 ? 1.1929 1.2017 1.0469 -0.0279 -0.0979 -0.0188 154 THR A C 1218 O O . THR A 154 ? 1.1816 1.1815 1.0283 -0.0251 -0.0959 -0.0169 154 THR A O 1219 C CB . THR A 154 ? 1.1248 1.1311 0.9858 -0.0378 -0.0939 -0.0239 154 THR A CB 1220 O OG1 . THR A 154 ? 1.1074 1.1017 0.9642 -0.0389 -0.0888 -0.0242 154 THR A OG1 1221 C CG2 . THR A 154 ? 0.9970 1.0109 0.8675 -0.0418 -0.0945 -0.0258 154 THR A CG2 1222 N N . ASP A 155 ? 1.6906 1.7101 1.5453 -0.0284 -0.1031 -0.0200 155 ASP A N 1223 C CA . ASP A 155 ? 1.8273 1.8497 1.6740 -0.0253 -0.1075 -0.0193 155 ASP A CA 1224 C C . ASP A 155 ? 1.8177 1.8303 1.6548 -0.0202 -0.1062 -0.0163 155 ASP A C 1225 O O . ASP A 155 ? 1.8216 1.8372 1.6571 -0.0145 -0.1087 -0.0136 155 ASP A O 1226 C CB . ASP A 155 ? 1.8351 1.8601 1.6768 -0.0306 -0.1101 -0.0228 155 ASP A CB 1227 C CG . ASP A 155 ? 1.8830 1.8956 1.7184 -0.0348 -0.1059 -0.0248 155 ASP A CG 1228 O OD1 . ASP A 155 ? 1.7751 1.7769 1.6058 -0.0324 -0.1020 -0.0229 155 ASP A OD1 1229 O OD2 . ASP A 155 ? 1.8691 1.8828 1.7040 -0.0407 -0.1064 -0.0283 155 ASP A OD2 1230 N N . SER A 156 ? 1.5053 1.5062 1.3356 -0.0223 -0.1023 -0.0168 156 SER A N 1231 C CA . SER A 156 ? 1.5115 1.5025 1.3315 -0.0187 -0.1007 -0.0143 156 SER A CA 1232 C C . SER A 156 ? 1.4537 1.4329 1.2702 -0.0214 -0.0949 -0.0148 156 SER A C 1233 O O . SER A 156 ? 1.4220 1.3923 1.2304 -0.0193 -0.0926 -0.0129 156 SER A O 1234 C CB . SER A 156 ? 1.5600 1.5525 1.3701 -0.0179 -0.1050 -0.0148 156 SER A CB 1235 O OG . SER A 156 ? 1.5513 1.5556 1.3643 -0.0148 -0.1106 -0.0142 156 SER A OG 1236 N N . ALA A 157 ? 1.2164 1.1957 1.0386 -0.0261 -0.0925 -0.0175 157 ALA A N 1237 C CA . ALA A 157 ? 1.1906 1.1600 1.0098 -0.0285 -0.0871 -0.0185 157 ALA A CA 1238 C C . ALA A 157 ? 1.2067 1.1708 1.0291 -0.0260 -0.0826 -0.0157 157 ALA A C 1239 O O . ALA A 157 ? 1.2296 1.1959 1.0543 -0.0222 -0.0837 -0.0128 157 ALA A O 1240 C CB . ALA A 157 ? 1.1449 1.1155 0.9690 -0.0337 -0.0860 -0.0220 157 ALA A CB 1241 N N . THR A 158 ? 1.1433 1.1005 0.9653 -0.0281 -0.0776 -0.0166 158 THR A N 1242 C CA . THR A 158 ? 1.0441 0.9976 0.8703 -0.0266 -0.0732 -0.0145 158 THR A CA 1243 C C . THR A 158 ? 1.0152 0.9733 0.8529 -0.0284 -0.0721 -0.0156 158 THR A C 1244 O O . THR A 158 ? 0.9984 0.9603 0.8391 -0.0315 -0.0737 -0.0183 158 THR A O 1245 C CB . THR A 158 ? 1.0357 0.9802 0.8557 -0.0276 -0.0681 -0.0147 158 THR A CB 1246 O OG1 . THR A 158 ? 1.0109 0.9540 0.8320 -0.0310 -0.0661 -0.0180 158 THR A OG1 1247 C CG2 . THR A 158 ? 1.0106 0.9502 0.8186 -0.0264 -0.0689 -0.0139 158 THR A CG2 1248 N N . TYR A 159 ? 1.1038 1.0614 0.9473 -0.0267 -0.0694 -0.0135 159 TYR A N 1249 C CA . TYR A 159 ? 0.9861 0.9469 0.8399 -0.0282 -0.0676 -0.0143 159 TYR A CA 1250 C C . TYR A 159 ? 0.9624 0.9169 0.8148 -0.0304 -0.0627 -0.0159 159 TYR A C 1251 O O . TYR A 159 ? 0.9331 0.8827 0.7832 -0.0292 -0.0589 -0.0143 159 TYR A O 1252 C CB . TYR A 159 ? 0.9446 0.9074 0.8046 -0.0253 -0.0669 -0.0114 159 TYR A CB 1253 C CG . TYR A 159 ? 0.9246 0.8927 0.7957 -0.0263 -0.0664 -0.0119 159 TYR A CG 1254 C CD1 . TYR A 159 ? 0.9051 0.8798 0.7824 -0.0241 -0.0692 -0.0104 159 TYR A CD1 1255 C CD2 . TYR A 159 ? 0.9012 0.8675 0.7763 -0.0291 -0.0632 -0.0138 159 TYR A CD2 1256 C CE1 . TYR A 159 ? 0.8477 0.8274 0.7349 -0.0251 -0.0686 -0.0108 159 TYR A CE1 1257 C CE2 . TYR A 159 ? 0.8637 0.8344 0.7484 -0.0300 -0.0627 -0.0141 159 TYR A CE2 1258 C CZ . TYR A 159 ? 0.8750 0.8525 0.7658 -0.0281 -0.0654 -0.0126 159 TYR A CZ 1259 O OH . TYR A 159 ? 0.8592 0.8411 0.7594 -0.0291 -0.0649 -0.0129 159 TYR A OH 1260 N N . PRO A 160 ? 0.7997 0.7543 0.6530 -0.0336 -0.0627 -0.0190 160 PRO A N 1261 C CA . PRO A 160 ? 0.8223 0.7706 0.6732 -0.0351 -0.0583 -0.0208 160 PRO A CA 1262 C C . PRO A 160 ? 0.8354 0.7843 0.6949 -0.0348 -0.0548 -0.0202 160 PRO A C 1263 O O . PRO A 160 ? 0.8049 0.7588 0.6719 -0.0337 -0.0560 -0.0184 160 PRO A O 1264 C CB . PRO A 160 ? 0.7877 0.7359 0.6362 -0.0385 -0.0603 -0.0242 160 PRO A CB 1265 C CG . PRO A 160 ? 0.8047 0.7611 0.6600 -0.0395 -0.0646 -0.0242 160 PRO A CG 1266 C CD . PRO A 160 ? 0.7939 0.7546 0.6504 -0.0360 -0.0668 -0.0210 160 PRO A CD 1267 N N . VAL A 161 ? 0.8547 0.7989 0.7131 -0.0355 -0.0507 -0.0216 161 VAL A N 1268 C CA . VAL A 161 ? 0.8183 0.7632 0.6846 -0.0352 -0.0477 -0.0214 161 VAL A CA 1269 C C . VAL A 161 ? 0.8464 0.7935 0.7177 -0.0377 -0.0494 -0.0234 161 VAL A C 1270 O O . VAL A 161 ? 0.8342 0.7776 0.7011 -0.0398 -0.0495 -0.0262 161 VAL A O 1271 C CB . VAL A 161 ? 0.7995 0.7391 0.6628 -0.0345 -0.0425 -0.0221 161 VAL A CB 1272 C CG1 . VAL A 161 ? 0.7647 0.7057 0.6362 -0.0340 -0.0397 -0.0219 161 VAL A CG1 1273 C CG2 . VAL A 161 ? 0.8176 0.7556 0.6762 -0.0328 -0.0405 -0.0200 161 VAL A CG2 1274 N N . ILE A 162 ? 0.8368 0.7896 0.7167 -0.0375 -0.0508 -0.0221 162 ILE A N 1275 C CA . ILE A 162 ? 0.8010 0.7563 0.6863 -0.0400 -0.0522 -0.0238 162 ILE A CA 1276 C C . ILE A 162 ? 0.7833 0.7368 0.6742 -0.0395 -0.0484 -0.0237 162 ILE A C 1277 O O . ILE A 162 ? 0.7554 0.7091 0.6491 -0.0370 -0.0457 -0.0216 162 ILE A O 1278 C CB . ILE A 162 ? 0.7860 0.7497 0.6774 -0.0402 -0.0563 -0.0226 162 ILE A CB 1279 C CG1 . ILE A 162 ? 0.7330 0.6998 0.6303 -0.0370 -0.0553 -0.0195 162 ILE A CG1 1280 C CG2 . ILE A 162 ? 0.7375 0.7037 0.6233 -0.0406 -0.0605 -0.0230 162 ILE A CG2 1281 C CD1 . ILE A 162 ? 0.6850 0.6599 0.5875 -0.0362 -0.0593 -0.0181 162 ILE A CD1 1282 N N . LYS A 163 ? 0.7533 0.7049 0.6453 -0.0420 -0.0481 -0.0259 163 LYS A N 1283 C CA . LYS A 163 ? 0.7483 0.6974 0.6446 -0.0413 -0.0446 -0.0259 163 LYS A CA 1284 C C . LYS A 163 ? 0.7590 0.7102 0.6607 -0.0440 -0.0460 -0.0269 163 LYS A C 1285 O O . LYS A 163 ? 0.7537 0.7062 0.6537 -0.0473 -0.0492 -0.0286 163 LYS A O 1286 C CB . LYS A 163 ? 0.7418 0.6828 0.6312 -0.0407 -0.0411 -0.0278 163 LYS A CB 1287 C CG . LYS A 163 ? 0.7771 0.7165 0.6625 -0.0377 -0.0383 -0.0266 163 LYS A CG 1288 C CD . LYS A 163 ? 0.8232 0.7554 0.7023 -0.0367 -0.0347 -0.0286 163 LYS A CD 1289 C CE . LYS A 163 ? 0.9383 0.8699 0.8136 -0.0341 -0.0318 -0.0275 163 LYS A CE 1290 N NZ . LYS A 163 ? 0.9371 0.8622 0.8056 -0.0328 -0.0283 -0.0297 163 LYS A NZ 1291 N N . GLY A 164 ? 0.6386 0.5902 0.5466 -0.0429 -0.0436 -0.0260 164 GLY A N 1292 C CA . GLY A 164 ? 0.5819 0.5351 0.4950 -0.0454 -0.0444 -0.0267 164 GLY A CA 1293 C C . GLY A 164 ? 0.6050 0.5543 0.5207 -0.0438 -0.0406 -0.0264 164 GLY A C 1294 O O . GLY A 164 ? 0.6055 0.5547 0.5227 -0.0404 -0.0378 -0.0249 164 GLY A O 1295 N N . THR A 165 ? 0.6742 0.6204 0.5902 -0.0463 -0.0405 -0.0280 165 THR A N 1296 C CA . THR A 165 ? 0.7060 0.6480 0.6240 -0.0447 -0.0371 -0.0278 165 THR A CA 1297 C C . THR A 165 ? 0.7107 0.6538 0.6332 -0.0477 -0.0381 -0.0281 165 THR A C 1298 O O . THR A 165 ? 0.6890 0.6312 0.6089 -0.0520 -0.0405 -0.0299 165 THR A O 1299 C CB . THR A 165 ? 0.7588 0.6909 0.6680 -0.0436 -0.0343 -0.0299 165 THR A CB 1300 O OG1 . THR A 165 ? 0.8411 0.7729 0.7464 -0.0407 -0.0330 -0.0295 165 THR A OG1 1301 C CG2 . THR A 165 ? 0.7196 0.6474 0.6303 -0.0412 -0.0309 -0.0296 165 THR A CG2 1302 N N . TYR A 166 ? 0.5794 0.5248 0.5086 -0.0458 -0.0364 -0.0264 166 TYR A N 1303 C CA . TYR A 166 ? 0.6028 0.5478 0.5354 -0.0484 -0.0367 -0.0267 166 TYR A CA 1304 C C . TYR A 166 ? 0.6460 0.5859 0.5792 -0.0455 -0.0330 -0.0262 166 TYR A C 1305 O O . TYR A 166 ? 0.6480 0.5910 0.5853 -0.0415 -0.0311 -0.0244 166 TYR A O 1306 C CB . TYR A 166 ? 0.5662 0.5214 0.5078 -0.0495 -0.0391 -0.0250 166 TYR A CB 1307 C CG . TYR A 166 ? 0.5861 0.5416 0.5311 -0.0529 -0.0395 -0.0254 166 TYR A CG 1308 C CD1 . TYR A 166 ? 0.5776 0.5327 0.5274 -0.0510 -0.0372 -0.0240 166 TYR A CD1 1309 C CD2 . TYR A 166 ? 0.5380 0.4941 0.4810 -0.0581 -0.0421 -0.0272 166 TYR A CD2 1310 C CE1 . TYR A 166 ? 0.5894 0.5444 0.5418 -0.0541 -0.0374 -0.0244 166 TYR A CE1 1311 C CE2 . TYR A 166 ? 0.5548 0.5112 0.5004 -0.0617 -0.0423 -0.0276 166 TYR A CE2 1312 C CZ . TYR A 166 ? 0.6078 0.5633 0.5580 -0.0596 -0.0399 -0.0261 166 TYR A CZ 1313 O OH . TYR A 166 ? 0.6082 0.5634 0.5605 -0.0632 -0.0399 -0.0264 166 TYR A OH 1314 N N . ASN A 167 ? 0.7091 0.6410 0.6377 -0.0474 -0.0320 -0.0279 167 ASN A N 1315 C CA . ASN A 167 ? 0.6826 0.6089 0.6109 -0.0445 -0.0288 -0.0275 167 ASN A CA 1316 C C . ASN A 167 ? 0.7180 0.6463 0.6519 -0.0468 -0.0293 -0.0267 167 ASN A C 1317 O O . ASN A 167 ? 0.7251 0.6496 0.6560 -0.0515 -0.0306 -0.0282 167 ASN A O 1318 C CB . ASN A 167 ? 0.7849 0.6989 0.7024 -0.0442 -0.0270 -0.0299 167 ASN A CB 1319 C CG . ASN A 167 ? 0.8750 0.7825 0.7910 -0.0404 -0.0235 -0.0296 167 ASN A CG 1320 O OD1 . ASN A 167 ? 0.8116 0.7244 0.7348 -0.0376 -0.0224 -0.0275 167 ASN A OD1 1321 N ND2 . ASN A 167 ? 0.8770 0.7726 0.7829 -0.0401 -0.0220 -0.0317 167 ASN A ND2 1322 N N . ASN A 168 ? 0.6404 0.5747 0.5822 -0.0439 -0.0282 -0.0244 168 ASN A N 1323 C CA . ASN A 168 ? 0.5804 0.5168 0.5276 -0.0456 -0.0284 -0.0234 168 ASN A CA 1324 C C . ASN A 168 ? 0.6418 0.5676 0.5834 -0.0451 -0.0260 -0.0243 168 ASN A C 1325 O O . ASN A 168 ? 0.6538 0.5773 0.5957 -0.0406 -0.0233 -0.0234 168 ASN A O 1326 C CB . ASN A 168 ? 0.5804 0.5256 0.5368 -0.0425 -0.0278 -0.0208 168 ASN A CB 1327 C CG . ASN A 168 ? 0.5519 0.5012 0.5148 -0.0447 -0.0286 -0.0198 168 ASN A CG 1328 O OD1 . ASN A 168 ? 0.5749 0.5194 0.5351 -0.0483 -0.0289 -0.0209 168 ASN A OD1 1329 N ND2 . ASN A 168 ? 0.4897 0.4474 0.4607 -0.0428 -0.0288 -0.0177 168 ASN A ND2 1330 N N . THR A 169 ? 0.6919 0.6111 0.6279 -0.0500 -0.0270 -0.0262 169 THR A N 1331 C CA . THR A 169 ? 0.7647 0.6720 0.6936 -0.0501 -0.0249 -0.0271 169 THR A CA 1332 C C . THR A 169 ? 0.8104 0.7194 0.7441 -0.0528 -0.0251 -0.0261 169 THR A C 1333 O O . THR A 169 ? 0.8552 0.7544 0.7834 -0.0533 -0.0234 -0.0266 169 THR A O 1334 C CB . THR A 169 ? 0.8332 0.7302 0.7512 -0.0542 -0.0255 -0.0300 169 THR A CB 1335 O OG1 . THR A 169 ? 0.8014 0.7039 0.7214 -0.0607 -0.0287 -0.0309 169 THR A OG1 1336 C CG2 . THR A 169 ? 0.7168 0.6106 0.6290 -0.0509 -0.0248 -0.0311 169 THR A CG2 1337 N N . GLY A 170 ? 0.6802 0.6012 0.6236 -0.0542 -0.0270 -0.0246 170 GLY A N 1338 C CA . GLY A 170 ? 0.6332 0.5574 0.5820 -0.0567 -0.0272 -0.0235 170 GLY A CA 1339 C C . GLY A 170 ? 0.6632 0.5887 0.6168 -0.0516 -0.0249 -0.0212 170 GLY A C 1340 O O . GLY A 170 ? 0.6935 0.6176 0.6462 -0.0462 -0.0231 -0.0206 170 GLY A O 1341 N N . THR A 171 ? 0.6595 0.5883 0.6182 -0.0536 -0.0250 -0.0201 171 THR A N 1342 C CA . THR A 171 ? 0.6912 0.6217 0.6547 -0.0494 -0.0231 -0.0180 171 THR A CA 1343 C C . THR A 171 ? 0.7032 0.6469 0.6773 -0.0477 -0.0242 -0.0161 171 THR A C 1344 O O . THR A 171 ? 0.6565 0.6029 0.6351 -0.0440 -0.0228 -0.0143 171 THR A O 1345 C CB . THR A 171 ? 0.7798 0.7050 0.7417 -0.0523 -0.0223 -0.0177 171 THR A CB 1346 O OG1 . THR A 171 ? 0.7220 0.6535 0.6879 -0.0584 -0.0246 -0.0181 171 THR A OG1 1347 C CG2 . THR A 171 ? 0.7167 0.6269 0.6671 -0.0530 -0.0207 -0.0194 171 THR A CG2 1348 N N . GLN A 172 ? 0.6067 0.5582 0.5843 -0.0504 -0.0268 -0.0164 172 GLN A N 1349 C CA . GLN A 172 ? 0.6025 0.5656 0.5893 -0.0491 -0.0280 -0.0147 172 GLN A CA 1350 C C . GLN A 172 ? 0.5497 0.5165 0.5371 -0.0458 -0.0285 -0.0144 172 GLN A C 1351 O O . GLN A 172 ? 0.5838 0.5473 0.5657 -0.0466 -0.0291 -0.0159 172 GLN A O 1352 C CB . GLN A 172 ? 0.6012 0.5715 0.5921 -0.0539 -0.0306 -0.0151 172 GLN A CB 1353 C CG . GLN A 172 ? 0.6693 0.6367 0.6595 -0.0582 -0.0303 -0.0155 172 GLN A CG 1354 C CD . GLN A 172 ? 0.8430 0.8114 0.8306 -0.0645 -0.0325 -0.0174 172 GLN A CD 1355 O OE1 . GLN A 172 ? 0.8237 0.7980 0.8154 -0.0684 -0.0336 -0.0174 172 GLN A OE1 1356 N NE2 . GLN A 172 ? 0.7324 0.6956 0.7131 -0.0656 -0.0332 -0.0192 172 GLN A NE2 1357 N N . PRO A 173 ? 0.4798 0.4533 0.4734 -0.0425 -0.0280 -0.0125 173 PRO A N 1358 C CA . PRO A 173 ? 0.4701 0.4476 0.4644 -0.0401 -0.0286 -0.0120 173 PRO A CA 1359 C C . PRO A 173 ? 0.4607 0.4439 0.4563 -0.0428 -0.0317 -0.0125 173 PRO A C 1360 O O . PRO A 173 ? 0.4290 0.4164 0.4282 -0.0457 -0.0333 -0.0125 173 PRO A O 1361 C CB . PRO A 173 ? 0.4658 0.4489 0.4666 -0.0370 -0.0275 -0.0099 173 PRO A CB 1362 C CG . PRO A 173 ? 0.4028 0.3875 0.4078 -0.0386 -0.0275 -0.0093 173 PRO A CG 1363 C CD . PRO A 173 ? 0.4216 0.3982 0.4210 -0.0410 -0.0268 -0.0108 173 PRO A CD 1364 N N . ILE A 174 ? 0.4737 0.4572 0.4663 -0.0417 -0.0326 -0.0128 174 ILE A N 1365 C CA . ILE A 174 ? 0.4439 0.4325 0.4368 -0.0437 -0.0357 -0.0133 174 ILE A CA 1366 C C . ILE A 174 ? 0.4371 0.4317 0.4334 -0.0408 -0.0366 -0.0116 174 ILE A C 1367 O O . ILE A 174 ? 0.4342 0.4264 0.4278 -0.0382 -0.0353 -0.0111 174 ILE A O 1368 C CB . ILE A 174 ? 0.4871 0.4704 0.4724 -0.0456 -0.0365 -0.0154 174 ILE A CB 1369 C CG1 . ILE A 174 ? 0.5051 0.4825 0.4865 -0.0495 -0.0363 -0.0172 174 ILE A CG1 1370 C CG2 . ILE A 174 ? 0.4151 0.4044 0.4004 -0.0467 -0.0398 -0.0157 174 ILE A CG2 1371 C CD1 . ILE A 174 ? 0.5153 0.4860 0.4883 -0.0513 -0.0367 -0.0194 174 ILE A CD1 1372 N N . LEU A 175 ? 0.4368 0.4388 0.4384 -0.0413 -0.0386 -0.0108 175 LEU A N 1373 C CA . LEU A 175 ? 0.4778 0.4846 0.4815 -0.0385 -0.0397 -0.0092 175 LEU A CA 1374 C C . LEU A 175 ? 0.4672 0.4759 0.4673 -0.0391 -0.0425 -0.0100 175 LEU A C 1375 O O . LEU A 175 ? 0.4998 0.5126 0.5007 -0.0417 -0.0449 -0.0111 175 LEU A O 1376 C CB . LEU A 175 ? 0.4504 0.4642 0.4613 -0.0379 -0.0404 -0.0079 175 LEU A CB 1377 C CG . LEU A 175 ? 0.4556 0.4740 0.4684 -0.0349 -0.0417 -0.0063 175 LEU A CG 1378 C CD1 . LEU A 175 ? 0.3908 0.4051 0.4018 -0.0321 -0.0394 -0.0050 175 LEU A CD1 1379 C CD2 . LEU A 175 ? 0.3734 0.3985 0.3929 -0.0346 -0.0424 -0.0054 175 LEU A CD2 1380 N N . TYR A 176 ? 0.4323 0.4384 0.4283 -0.0368 -0.0422 -0.0095 176 TYR A N 1381 C CA . TYR A 176 ? 0.4367 0.4439 0.4284 -0.0371 -0.0448 -0.0102 176 TYR A CA 1382 C C . TYR A 176 ? 0.4550 0.4632 0.4453 -0.0337 -0.0453 -0.0084 176 TYR A C 1383 O O . TYR A 176 ? 0.4256 0.4322 0.4173 -0.0315 -0.0431 -0.0069 176 TYR A O 1384 C CB . TYR A 176 ? 0.4166 0.4173 0.4012 -0.0388 -0.0442 -0.0120 176 TYR A CB 1385 C CG . TYR A 176 ? 0.4577 0.4522 0.4385 -0.0366 -0.0411 -0.0116 176 TYR A CG 1386 C CD1 . TYR A 176 ? 0.4392 0.4299 0.4211 -0.0362 -0.0380 -0.0116 176 TYR A CD1 1387 C CD2 . TYR A 176 ? 0.4719 0.4646 0.4479 -0.0349 -0.0413 -0.0111 176 TYR A CD2 1388 C CE1 . TYR A 176 ? 0.4749 0.4613 0.4536 -0.0341 -0.0352 -0.0113 176 TYR A CE1 1389 C CE2 . TYR A 176 ? 0.4608 0.4488 0.4335 -0.0332 -0.0383 -0.0108 176 TYR A CE2 1390 C CZ . TYR A 176 ? 0.4825 0.4679 0.4568 -0.0328 -0.0353 -0.0110 176 TYR A CZ 1391 O OH . TYR A 176 ? 0.5061 0.4881 0.4774 -0.0310 -0.0324 -0.0107 176 TYR A OH 1392 N N . PHE A 177 ? 0.5157 0.5263 0.5030 -0.0334 -0.0481 -0.0086 177 PHE A N 1393 C CA . PHE A 177 ? 0.5309 0.5420 0.5162 -0.0301 -0.0490 -0.0068 177 PHE A CA 1394 C C . PHE A 177 ? 0.5876 0.5954 0.5652 -0.0299 -0.0502 -0.0074 177 PHE A C 1395 O O . PHE A 177 ? 0.5688 0.5763 0.5436 -0.0324 -0.0515 -0.0093 177 PHE A O 1396 C CB . PHE A 177 ? 0.4949 0.5137 0.4847 -0.0286 -0.0517 -0.0060 177 PHE A CB 1397 C CG . PHE A 177 ? 0.5082 0.5308 0.5054 -0.0290 -0.0508 -0.0056 177 PHE A CG 1398 C CD1 . PHE A 177 ? 0.4927 0.5191 0.4937 -0.0323 -0.0514 -0.0071 177 PHE A CD1 1399 C CD2 . PHE A 177 ? 0.5468 0.5689 0.5467 -0.0264 -0.0492 -0.0037 177 PHE A CD2 1400 C CE1 . PHE A 177 ? 0.5075 0.5373 0.5150 -0.0328 -0.0504 -0.0067 177 PHE A CE1 1401 C CE2 . PHE A 177 ? 0.5118 0.5373 0.5182 -0.0267 -0.0483 -0.0033 177 PHE A CE2 1402 C CZ . PHE A 177 ? 0.4915 0.5210 0.5017 -0.0298 -0.0489 -0.0048 177 PHE A CZ 1403 N N . TRP A 178 ? 0.5050 0.5101 0.4789 -0.0272 -0.0498 -0.0058 178 TRP A N 1404 C CA . TRP A 178 ? 0.5389 0.5411 0.5052 -0.0266 -0.0511 -0.0060 178 TRP A CA 1405 C C . TRP A 178 ? 0.5413 0.5420 0.5047 -0.0232 -0.0514 -0.0037 178 TRP A C 1406 O O . TRP A 178 ? 0.5350 0.5361 0.5018 -0.0216 -0.0502 -0.0021 178 TRP A O 1407 C CB . TRP A 178 ? 0.5097 0.5055 0.4708 -0.0282 -0.0486 -0.0072 178 TRP A CB 1408 C CG . TRP A 178 ? 0.5575 0.5485 0.5171 -0.0270 -0.0450 -0.0060 178 TRP A CG 1409 C CD1 . TRP A 178 ? 0.5937 0.5806 0.5472 -0.0257 -0.0440 -0.0049 178 TRP A CD1 1410 C CD2 . TRP A 178 ? 0.5437 0.5340 0.5079 -0.0273 -0.0418 -0.0058 178 TRP A CD2 1411 N NE1 . TRP A 178 ? 0.5707 0.5550 0.5250 -0.0255 -0.0403 -0.0041 178 TRP A NE1 1412 C CE2 . TRP A 178 ? 0.5755 0.5621 0.5364 -0.0263 -0.0390 -0.0046 178 TRP A CE2 1413 C CE3 . TRP A 178 ? 0.5512 0.5439 0.5217 -0.0284 -0.0411 -0.0064 178 TRP A CE3 1414 C CZ2 . TRP A 178 ? 0.5352 0.5212 0.4994 -0.0262 -0.0357 -0.0042 178 TRP A CZ2 1415 C CZ3 . TRP A 178 ? 0.5103 0.5017 0.4837 -0.0280 -0.0378 -0.0058 178 TRP A CZ3 1416 C CH2 . TRP A 178 ? 0.5484 0.5370 0.5188 -0.0269 -0.0352 -0.0048 178 TRP A CH2 1417 N N . GLY A 179 ? 0.4882 0.4866 0.4446 -0.0222 -0.0530 -0.0035 179 GLY A N 1418 C CA . GLY A 179 ? 0.4846 0.4804 0.4367 -0.0190 -0.0534 -0.0012 179 GLY A CA 1419 C C . GLY A 179 ? 0.5371 0.5266 0.4799 -0.0188 -0.0529 -0.0010 179 GLY A C 1420 O O . GLY A 179 ? 0.5590 0.5471 0.4987 -0.0209 -0.0528 -0.0027 179 GLY A O 1421 N N . VAL A 180 ? 0.6180 0.6032 0.5559 -0.0163 -0.0525 0.0012 180 VAL A N 1422 C CA . VAL A 180 ? 0.6444 0.6236 0.5727 -0.0159 -0.0524 0.0018 180 VAL A CA 1423 C C . VAL A 180 ? 0.6532 0.6319 0.5772 -0.0121 -0.0554 0.0037 180 VAL A C 1424 O O . VAL A 180 ? 0.6423 0.6206 0.5681 -0.0099 -0.0552 0.0054 180 VAL A O 1425 C CB . VAL A 180 ? 0.6956 0.6682 0.6206 -0.0170 -0.0481 0.0027 180 VAL A CB 1426 C CG1 . VAL A 180 ? 0.6713 0.6376 0.5859 -0.0166 -0.0479 0.0035 180 VAL A CG1 1427 C CG2 . VAL A 180 ? 0.5928 0.5663 0.5221 -0.0199 -0.0451 0.0009 180 VAL A CG2 1428 N N . HIS A 181 ? 0.6326 0.6115 0.5507 -0.0111 -0.0583 0.0033 181 HIS A N 1429 C CA . HIS A 181 ? 0.6628 0.6412 0.5760 -0.0068 -0.0614 0.0052 181 HIS A CA 1430 C C . HIS A 181 ? 0.6430 0.6115 0.5463 -0.0055 -0.0596 0.0073 181 HIS A C 1431 O O . HIS A 181 ? 0.7389 0.7022 0.6365 -0.0078 -0.0575 0.0069 181 HIS A O 1432 C CB . HIS A 181 ? 0.6885 0.6723 0.5996 -0.0060 -0.0657 0.0040 181 HIS A CB 1433 C CG . HIS A 181 ? 0.6924 0.6779 0.5999 -0.0009 -0.0694 0.0057 181 HIS A CG 1434 N ND1 . HIS A 181 ? 0.7121 0.6941 0.6100 0.0013 -0.0716 0.0065 181 HIS A ND1 1435 C CD2 . HIS A 181 ? 0.7068 0.6969 0.6186 0.0028 -0.0712 0.0068 181 HIS A CD2 1436 C CE1 . HIS A 181 ? 0.7366 0.7211 0.6330 0.0064 -0.0747 0.0081 181 HIS A CE1 1437 N NE2 . HIS A 181 ? 0.7408 0.7304 0.6456 0.0075 -0.0744 0.0083 181 HIS A NE2 1438 N N . HIS A 182 ? 0.6868 0.6523 0.5875 -0.0019 -0.0602 0.0096 182 HIS A N 1439 C CA . HIS A 182 ? 0.7482 0.7031 0.6383 -0.0006 -0.0587 0.0119 182 HIS A CA 1440 C C . HIS A 182 ? 0.7642 0.7177 0.6472 0.0046 -0.0626 0.0135 182 HIS A C 1441 O O . HIS A 182 ? 0.7785 0.7319 0.6621 0.0085 -0.0638 0.0150 182 HIS A O 1442 C CB . HIS A 182 ? 0.7538 0.7041 0.6455 -0.0010 -0.0554 0.0133 182 HIS A CB 1443 C CG . HIS A 182 ? 0.7378 0.6904 0.6368 -0.0055 -0.0517 0.0119 182 HIS A CG 1444 N ND1 . HIS A 182 ? 0.7508 0.6986 0.6461 -0.0091 -0.0481 0.0116 182 HIS A ND1 1445 C CD2 . HIS A 182 ? 0.7661 0.7254 0.6757 -0.0067 -0.0511 0.0107 182 HIS A CD2 1446 C CE1 . HIS A 182 ? 0.7786 0.7303 0.6819 -0.0119 -0.0455 0.0104 182 HIS A CE1 1447 N NE2 . HIS A 182 ? 0.7774 0.7356 0.6893 -0.0106 -0.0473 0.0098 182 HIS A NE2 1448 N N . PRO A 183 ? 0.7546 0.7067 0.6304 0.0050 -0.0646 0.0132 183 PRO A N 1449 C CA . PRO A 183 ? 0.7518 0.7027 0.6200 0.0102 -0.0686 0.0147 183 PRO A CA 1450 C C . PRO A 183 ? 0.7444 0.6840 0.6028 0.0134 -0.0674 0.0178 183 PRO A C 1451 O O . PRO A 183 ? 0.7277 0.6588 0.5823 0.0104 -0.0633 0.0186 183 PRO A O 1452 C CB . PRO A 183 ? 0.7521 0.7020 0.6137 0.0085 -0.0696 0.0137 183 PRO A CB 1453 C CG . PRO A 183 ? 0.7813 0.7361 0.6504 0.0031 -0.0676 0.0110 183 PRO A CG 1454 C CD . PRO A 183 ? 0.7391 0.6914 0.6137 0.0007 -0.0633 0.0113 183 PRO A CD 1455 N N . LEU A 184 ? 0.7612 0.7003 0.6149 0.0194 -0.0709 0.0194 184 LEU A N 1456 C CA . LEU A 184 ? 0.8287 0.7558 0.6718 0.0230 -0.0700 0.0223 184 LEU A CA 1457 C C . LEU A 184 ? 0.8388 0.7543 0.6681 0.0220 -0.0688 0.0237 184 LEU A C 1458 O O . LEU A 184 ? 0.8750 0.7785 0.6959 0.0215 -0.0659 0.0257 184 LEU A O 1459 C CB . LEU A 184 ? 0.8773 0.8073 0.7191 0.0306 -0.0741 0.0237 184 LEU A CB 1460 C CG . LEU A 184 ? 0.9713 0.9063 0.8085 0.0348 -0.0790 0.0236 184 LEU A CG 1461 C CD1 . LEU A 184 ? 1.0053 0.9340 0.8328 0.0428 -0.0815 0.0264 184 LEU A CD1 1462 C CD2 . LEU A 184 ? 0.9147 0.8665 0.7645 0.0346 -0.0822 0.0210 184 LEU A CD2 1463 N N . ASP A 185 ? 0.9132 0.8321 0.7399 0.0215 -0.0710 0.0227 185 ASP A N 1464 C CA . ASP A 185 ? 0.9450 0.8537 0.7586 0.0204 -0.0699 0.0238 185 ASP A CA 1465 C C . ASP A 185 ? 0.9599 0.8730 0.7753 0.0155 -0.0693 0.0215 185 ASP A C 1466 O O . ASP A 185 ? 0.9617 0.8854 0.7879 0.0132 -0.0700 0.0189 185 ASP A O 1467 C CB . ASP A 185 ? 0.9571 0.8610 0.7594 0.0270 -0.0739 0.0260 185 ASP A CB 1468 C CG . ASP A 185 ? 1.0518 0.9685 0.8591 0.0306 -0.0793 0.0246 185 ASP A CG 1469 O OD1 . ASP A 185 ? 1.0424 0.9666 0.8540 0.0271 -0.0801 0.0222 185 ASP A OD1 1470 O OD2 . ASP A 185 ? 1.0847 1.0041 0.8913 0.0371 -0.0827 0.0258 185 ASP A OD2 1471 N N . THR A 186 ? 0.8452 0.7494 0.6492 0.0140 -0.0679 0.0223 186 THR A N 1472 C CA . THR A 186 ? 0.9121 0.8188 0.7160 0.0096 -0.0669 0.0202 186 THR A CA 1473 C C . THR A 186 ? 0.8626 0.7769 0.6662 0.0117 -0.0717 0.0188 186 THR A C 1474 O O . THR A 186 ? 0.8644 0.7829 0.6701 0.0081 -0.0715 0.0164 186 THR A O 1475 C CB . THR A 186 ? 0.9811 0.8759 0.7728 0.0067 -0.0632 0.0215 186 THR A CB 1476 O OG1 . THR A 186 ? 0.9841 0.8689 0.7630 0.0110 -0.0648 0.0246 186 THR A OG1 1477 C CG2 . THR A 186 ? 0.8782 0.7693 0.6732 0.0020 -0.0577 0.0216 186 THR A CG2 1478 N N . THR A 187 ? 0.8952 0.8115 0.6960 0.0177 -0.0762 0.0201 187 THR A N 1479 C CA . THR A 187 ? 0.9714 0.8964 0.7724 0.0199 -0.0812 0.0188 187 THR A CA 1480 C C . THR A 187 ? 0.9857 0.9250 0.8013 0.0183 -0.0829 0.0160 187 THR A C 1481 O O . THR A 187 ? 0.9704 0.9164 0.7892 0.0151 -0.0842 0.0134 187 THR A O 1482 C CB . THR A 187 ? 1.0187 0.9422 0.8118 0.0274 -0.0857 0.0212 187 THR A CB 1483 O OG1 . THR A 187 ? 1.0983 1.0292 0.9000 0.0313 -0.0876 0.0215 187 THR A OG1 1484 C CG2 . THR A 187 ? 1.0218 0.9295 0.8005 0.0294 -0.0835 0.0245 187 THR A CG2 1485 N N . VAL A 188 ? 0.8335 0.7768 0.6574 0.0202 -0.0829 0.0164 188 VAL A N 1486 C CA . VAL A 188 ? 0.7798 0.7358 0.6176 0.0183 -0.0839 0.0140 188 VAL A CA 1487 C C . VAL A 188 ? 0.7047 0.6615 0.5481 0.0114 -0.0803 0.0114 188 VAL A C 1488 O O . VAL A 188 ? 0.6652 0.6309 0.5151 0.0086 -0.0819 0.0088 188 VAL A O 1489 C CB . VAL A 188 ? 0.8184 0.7764 0.6632 0.0211 -0.0833 0.0151 188 VAL A CB 1490 C CG1 . VAL A 188 ? 0.7188 0.6894 0.5779 0.0183 -0.0838 0.0126 188 VAL A CG1 1491 C CG2 . VAL A 188 ? 0.8538 0.8121 0.6934 0.0286 -0.0871 0.0174 188 VAL A CG2 1492 N N . GLN A 189 ? 0.7137 0.6610 0.5539 0.0087 -0.0756 0.0123 189 GLN A N 1493 C CA . GLN A 189 ? 0.7518 0.6986 0.5956 0.0029 -0.0718 0.0102 189 GLN A CA 1494 C C . GLN A 189 ? 0.7758 0.7242 0.6152 0.0007 -0.0734 0.0081 189 GLN A C 1495 O O . GLN A 189 ? 0.7358 0.6910 0.5819 -0.0024 -0.0739 0.0054 189 GLN A O 1496 C CB . GLN A 189 ? 0.7653 0.7013 0.6035 0.0009 -0.0668 0.0118 189 GLN A CB 1497 C CG . GLN A 189 ? 0.7557 0.6906 0.5954 -0.0044 -0.0629 0.0097 189 GLN A CG 1498 C CD . GLN A 189 ? 0.7484 0.6900 0.6006 -0.0071 -0.0610 0.0078 189 GLN A CD 1499 O OE1 . GLN A 189 ? 0.7267 0.6729 0.5864 -0.0054 -0.0622 0.0082 189 GLN A OE1 1500 N NE2 . GLN A 189 ? 0.7347 0.6764 0.5887 -0.0111 -0.0581 0.0058 189 GLN A NE2 1501 N N . ASP A 190 ? 0.9743 0.9159 0.8019 0.0025 -0.0743 0.0096 190 ASP A N 1502 C CA . ASP A 190 ? 0.9684 0.9104 0.7901 0.0008 -0.0758 0.0079 190 ASP A CA 1503 C C . ASP A 190 ? 0.9132 0.8665 0.7399 0.0016 -0.0810 0.0059 190 ASP A C 1504 O O . ASP A 190 ? 0.9033 0.8602 0.7312 -0.0019 -0.0815 0.0031 190 ASP A O 1505 C CB . ASP A 190 ? 1.0095 0.9421 0.8170 0.0033 -0.0763 0.0103 190 ASP A CB 1506 C CG . ASP A 190 ? 1.1946 1.1236 0.9947 0.0002 -0.0752 0.0088 190 ASP A CG 1507 O OD1 . ASP A 190 ? 1.1610 1.0962 0.9614 -0.0004 -0.0786 0.0066 190 ASP A OD1 1508 O OD2 . ASP A 190 ? 1.2881 1.2082 1.0816 -0.0019 -0.0710 0.0097 190 ASP A OD2 1509 N N . ASN A 191 ? 0.8165 0.7754 0.6459 0.0062 -0.0846 0.0072 191 ASN A N 1510 C CA . ASN A 191 ? 0.8867 0.8578 0.7210 0.0071 -0.0897 0.0054 191 ASN A CA 1511 C C . ASN A 191 ? 0.9273 0.9075 0.7741 0.0028 -0.0892 0.0025 191 ASN A C 1512 O O . ASN A 191 ? 0.9118 0.9014 0.7620 0.0012 -0.0927 0.0002 191 ASN A O 1513 C CB . ASN A 191 ? 0.8883 0.8638 0.7224 0.0138 -0.0936 0.0076 191 ASN A CB 1514 C CG . ASN A 191 ? 1.1232 1.0920 0.9440 0.0185 -0.0958 0.0100 191 ASN A CG 1515 O OD1 . ASN A 191 ? 1.1556 1.1138 0.9668 0.0169 -0.0934 0.0107 191 ASN A OD1 1516 N ND2 . ASN A 191 ? 1.1448 1.1200 0.9648 0.0244 -0.1005 0.0111 191 ASN A ND2 1517 N N . LEU A 192 ? 0.8596 0.8369 0.7127 0.0006 -0.0850 0.0025 192 LEU A N 1518 C CA . LEU A 192 ? 0.7796 0.7645 0.6442 -0.0032 -0.0842 0.0001 192 LEU A CA 1519 C C . LEU A 192 ? 0.7821 0.7625 0.6471 -0.0087 -0.0804 -0.0021 192 LEU A C 1520 O O . LEU A 192 ? 0.7916 0.7775 0.6616 -0.0124 -0.0811 -0.0049 192 LEU A O 1521 C CB . LEU A 192 ? 0.7419 0.7282 0.6144 -0.0013 -0.0826 0.0016 192 LEU A CB 1522 C CG . LEU A 192 ? 0.8136 0.8105 0.6928 0.0022 -0.0864 0.0020 192 LEU A CG 1523 C CD1 . LEU A 192 ? 0.7930 0.7927 0.6653 0.0070 -0.0911 0.0031 192 LEU A CD1 1524 C CD2 . LEU A 192 ? 0.7752 0.7702 0.6590 0.0049 -0.0843 0.0041 192 LEU A CD2 1525 N N . TYR A 193 ? 0.8149 0.7854 0.6742 -0.0092 -0.0763 -0.0009 193 TYR A N 1526 C CA . TYR A 193 ? 0.8325 0.7988 0.6926 -0.0136 -0.0721 -0.0028 193 TYR A CA 1527 C C . TYR A 193 ? 0.8852 0.8438 0.7344 -0.0145 -0.0706 -0.0029 193 TYR A C 1528 O O . TYR A 193 ? 0.9331 0.8883 0.7815 -0.0177 -0.0674 -0.0046 193 TYR A O 1529 C CB . TYR A 193 ? 0.8157 0.7792 0.6815 -0.0139 -0.0678 -0.0016 193 TYR A CB 1530 C CG . TYR A 193 ? 0.7447 0.7146 0.6195 -0.0119 -0.0693 -0.0007 193 TYR A CG 1531 C CD1 . TYR A 193 ? 0.7406 0.7187 0.6248 -0.0139 -0.0706 -0.0027 193 TYR A CD1 1532 C CD2 . TYR A 193 ? 0.7198 0.6871 0.5932 -0.0081 -0.0693 0.0022 193 TYR A CD2 1533 C CE1 . TYR A 193 ? 0.7381 0.7224 0.6304 -0.0121 -0.0718 -0.0019 193 TYR A CE1 1534 C CE2 . TYR A 193 ? 0.7519 0.7249 0.6332 -0.0060 -0.0706 0.0030 193 TYR A CE2 1535 C CZ . TYR A 193 ? 0.7549 0.7369 0.6459 -0.0080 -0.0718 0.0009 193 TYR A CZ 1536 O OH . TYR A 193 ? 0.6629 0.6510 0.5617 -0.0060 -0.0730 0.0016 193 TYR A OH 1537 N N . GLY A 194 ? 1.0161 0.9718 0.8565 -0.0114 -0.0730 -0.0010 194 GLY A N 1538 C CA . GLY A 194 ? 1.0093 0.9575 0.8385 -0.0120 -0.0719 -0.0009 194 GLY A CA 1539 C C . GLY A 194 ? 1.0575 0.9966 0.8817 -0.0120 -0.0672 0.0013 194 GLY A C 1540 O O . GLY A 194 ? 1.1074 1.0455 0.9360 -0.0109 -0.0653 0.0030 194 GLY A O 1541 N N . SER A 195 ? 1.0395 0.9720 0.8542 -0.0134 -0.0652 0.0011 195 SER A N 1542 C CA . SER A 195 ? 1.0643 0.9884 0.8733 -0.0141 -0.0606 0.0030 195 SER A CA 1543 C C . SER A 195 ? 0.9975 0.9218 0.8123 -0.0177 -0.0556 0.0013 195 SER A C 1544 O O . SER A 195 ? 0.9858 0.9150 0.8068 -0.0195 -0.0558 -0.0015 195 SER A O 1545 C CB . SER A 195 ? 1.1480 1.0651 0.9437 -0.0138 -0.0606 0.0038 195 SER A CB 1546 O OG . SER A 195 ? 1.0330 0.9463 0.8255 -0.0172 -0.0560 0.0026 195 SER A OG 1547 N N . GLY A 196 ? 0.8261 0.7452 0.6388 -0.0186 -0.0512 0.0029 196 GLY A N 1548 C CA . GLY A 196 ? 0.7973 0.7171 0.6148 -0.0216 -0.0463 0.0015 196 GLY A CA 1549 C C . GLY A 196 ? 0.8384 0.7605 0.6650 -0.0217 -0.0443 0.0025 196 GLY A C 1550 O O . GLY A 196 ? 0.7823 0.7065 0.6129 -0.0195 -0.0470 0.0038 196 GLY A O 1551 N N . ASP A 197 ? 1.0451 0.9674 0.8750 -0.0240 -0.0396 0.0018 197 ASP A N 1552 C CA . ASP A 197 ? 1.0439 0.9690 0.8827 -0.0244 -0.0376 0.0025 197 ASP A CA 1553 C C . ASP A 197 ? 1.0010 0.9330 0.8505 -0.0245 -0.0388 0.0002 197 ASP A C 1554 O O . ASP A 197 ? 0.9583 0.8920 0.8093 -0.0259 -0.0373 -0.0022 197 ASP A O 1555 C CB . ASP A 197 ? 1.0447 0.9679 0.8823 -0.0269 -0.0321 0.0029 197 ASP A CB 1556 C CG . ASP A 197 ? 1.2362 1.1522 1.0633 -0.0275 -0.0307 0.0054 197 ASP A CG 1557 O OD1 . ASP A 197 ? 1.2459 1.1582 1.0690 -0.0254 -0.0336 0.0075 197 ASP A OD1 1558 O OD2 . ASP A 197 ? 1.2257 1.1397 1.0482 -0.0298 -0.0267 0.0053 197 ASP A OD2 1559 N N . LYS A 198 ? 0.7900 0.7255 0.6462 -0.0229 -0.0413 0.0011 198 LYS A N 1560 C CA . LYS A 198 ? 0.7651 0.7069 0.6309 -0.0231 -0.0428 -0.0009 198 LYS A CA 1561 C C . LYS A 198 ? 0.7295 0.6742 0.6043 -0.0240 -0.0397 -0.0009 198 LYS A C 1562 O O . LYS A 198 ? 0.6967 0.6393 0.5713 -0.0241 -0.0372 0.0010 198 LYS A O 1563 C CB . LYS A 198 ? 0.7297 0.6751 0.5976 -0.0209 -0.0479 -0.0004 198 LYS A CB 1564 C CG . LYS A 198 ? 0.8432 0.7870 0.7026 -0.0198 -0.0514 -0.0005 198 LYS A CG 1565 C CD . LYS A 198 ? 0.7816 0.7248 0.6376 -0.0220 -0.0510 -0.0033 198 LYS A CD 1566 C CE . LYS A 198 ? 0.8305 0.7732 0.6788 -0.0210 -0.0550 -0.0036 198 LYS A CE 1567 N NZ . LYS A 198 ? 0.8646 0.8070 0.7097 -0.0234 -0.0550 -0.0066 198 LYS A NZ 1568 N N . TYR A 199 ? 0.8294 0.7785 0.7114 -0.0248 -0.0400 -0.0030 199 TYR A N 1569 C CA . TYR A 199 ? 0.7960 0.7480 0.6865 -0.0255 -0.0372 -0.0032 199 TYR A CA 1570 C C . TYR A 199 ? 0.8050 0.7618 0.7034 -0.0256 -0.0393 -0.0048 199 TYR A C 1571 O O . TYR A 199 ? 0.7764 0.7343 0.6735 -0.0261 -0.0420 -0.0065 199 TYR A O 1572 C CB . TYR A 199 ? 0.7932 0.7437 0.6821 -0.0269 -0.0327 -0.0043 199 TYR A CB 1573 C CG . TYR A 199 ? 0.8739 0.8237 0.7601 -0.0276 -0.0328 -0.0070 199 TYR A CG 1574 C CD1 . TYR A 199 ? 0.8756 0.8215 0.7526 -0.0278 -0.0333 -0.0076 199 TYR A CD1 1575 C CD2 . TYR A 199 ? 0.8560 0.8081 0.7480 -0.0280 -0.0324 -0.0091 199 TYR A CD2 1576 C CE1 . TYR A 199 ? 0.8628 0.8074 0.7366 -0.0285 -0.0333 -0.0102 199 TYR A CE1 1577 C CE2 . TYR A 199 ? 0.8824 0.8326 0.7709 -0.0287 -0.0324 -0.0117 199 TYR A CE2 1578 C CZ . TYR A 199 ? 0.9314 0.8779 0.8108 -0.0290 -0.0329 -0.0123 199 TYR A CZ 1579 O OH . TYR A 199 ? 0.9615 0.9054 0.8367 -0.0297 -0.0329 -0.0149 199 TYR A OH 1580 N N . VAL A 200 ? 0.7824 0.7423 0.6888 -0.0256 -0.0379 -0.0043 200 VAL A N 1581 C CA . VAL A 200 ? 0.6422 0.6061 0.5561 -0.0262 -0.0388 -0.0059 200 VAL A CA 1582 C C . VAL A 200 ? 0.6523 0.6166 0.5706 -0.0269 -0.0348 -0.0064 200 VAL A C 1583 O O . VAL A 200 ? 0.6763 0.6413 0.5976 -0.0264 -0.0327 -0.0048 200 VAL A O 1584 C CB . VAL A 200 ? 0.6445 0.6127 0.5644 -0.0251 -0.0417 -0.0047 200 VAL A CB 1585 C CG1 . VAL A 200 ? 0.6136 0.5859 0.5415 -0.0262 -0.0420 -0.0062 200 VAL A CG1 1586 C CG2 . VAL A 200 ? 0.6269 0.5960 0.5428 -0.0240 -0.0459 -0.0043 200 VAL A CG2 1587 N N . ARG A 201 ? 0.7212 0.6848 0.6395 -0.0277 -0.0337 -0.0087 201 ARG A N 1588 C CA . ARG A 201 ? 0.7229 0.6869 0.6448 -0.0277 -0.0300 -0.0093 201 ARG A CA 1589 C C . ARG A 201 ? 0.6992 0.6645 0.6264 -0.0282 -0.0306 -0.0109 201 ARG A C 1590 O O . ARG A 201 ? 0.6933 0.6575 0.6185 -0.0293 -0.0329 -0.0126 201 ARG A O 1591 C CB . ARG A 201 ? 0.6990 0.6598 0.6147 -0.0276 -0.0268 -0.0103 201 ARG A CB 1592 C CG . ARG A 201 ? 0.7135 0.6735 0.6252 -0.0275 -0.0249 -0.0084 201 ARG A CG 1593 C CD . ARG A 201 ? 0.7680 0.7251 0.6723 -0.0276 -0.0224 -0.0095 201 ARG A CD 1594 N NE . ARG A 201 ? 0.8338 0.7896 0.7331 -0.0281 -0.0210 -0.0077 201 ARG A NE 1595 C CZ . ARG A 201 ? 0.8902 0.8424 0.7810 -0.0285 -0.0209 -0.0078 201 ARG A CZ 1596 N NH1 . ARG A 201 ? 0.8238 0.7735 0.7100 -0.0284 -0.0222 -0.0098 201 ARG A NH1 1597 N NH2 . ARG A 201 ? 0.8655 0.8161 0.7517 -0.0293 -0.0194 -0.0059 201 ARG A NH2 1598 N N . MET A 202 ? 0.7470 0.7148 0.6807 -0.0277 -0.0286 -0.0103 202 MET A N 1599 C CA . MET A 202 ? 0.7257 0.6944 0.6645 -0.0282 -0.0289 -0.0115 202 MET A CA 1600 C C . MET A 202 ? 0.7254 0.6944 0.6672 -0.0270 -0.0252 -0.0116 202 MET A C 1601 O O . MET A 202 ? 0.7132 0.6843 0.6563 -0.0261 -0.0229 -0.0102 202 MET A O 1602 C CB . MET A 202 ? 0.7057 0.6785 0.6508 -0.0286 -0.0317 -0.0104 202 MET A CB 1603 C CG . MET A 202 ? 0.7256 0.6992 0.6685 -0.0297 -0.0358 -0.0109 202 MET A CG 1604 S SD . MET A 202 ? 0.9199 0.8996 0.8708 -0.0299 -0.0387 -0.0098 202 MET A SD 1605 C CE . MET A 202 ? 0.7639 0.7452 0.7119 -0.0317 -0.0431 -0.0114 202 MET A CE 1606 N N . GLY A 203 ? 0.5993 0.5664 0.5418 -0.0269 -0.0245 -0.0133 203 GLY A N 1607 C CA . GLY A 203 ? 0.5759 0.5432 0.5206 -0.0252 -0.0210 -0.0135 203 GLY A CA 1608 C C . GLY A 203 ? 0.6068 0.5716 0.5532 -0.0252 -0.0211 -0.0149 203 GLY A C 1609 O O . GLY A 203 ? 0.6018 0.5627 0.5448 -0.0268 -0.0229 -0.0165 203 GLY A O 1610 N N . THR A 204 ? 0.5807 0.5478 0.5323 -0.0237 -0.0191 -0.0142 204 THR A N 1611 C CA . THR A 204 ? 0.6083 0.5723 0.5607 -0.0232 -0.0184 -0.0153 204 THR A CA 1612 C C . THR A 204 ? 0.6217 0.5860 0.5738 -0.0199 -0.0147 -0.0154 204 THR A C 1613 O O . THR A 204 ? 0.6536 0.6203 0.6040 -0.0186 -0.0128 -0.0151 204 THR A O 1614 C CB . THR A 204 ? 0.6088 0.5757 0.5682 -0.0243 -0.0199 -0.0142 204 THR A CB 1615 O OG1 . THR A 204 ? 0.6495 0.6221 0.6148 -0.0228 -0.0184 -0.0123 204 THR A OG1 1616 C CG2 . THR A 204 ? 0.5420 0.5108 0.5026 -0.0271 -0.0235 -0.0139 204 THR A CG2 1617 N N . GLU A 205 ? 0.6795 0.6418 0.6331 -0.0184 -0.0135 -0.0159 205 GLU A N 1618 C CA . GLU A 205 ? 0.6676 0.6310 0.6213 -0.0147 -0.0102 -0.0159 205 GLU A CA 1619 C C . GLU A 205 ? 0.6804 0.6524 0.6411 -0.0139 -0.0090 -0.0139 205 GLU A C 1620 O O . GLU A 205 ? 0.7336 0.7090 0.6944 -0.0112 -0.0062 -0.0138 205 GLU A O 1621 C CB . GLU A 205 ? 0.6512 0.6096 0.6043 -0.0131 -0.0095 -0.0168 205 GLU A CB 1622 C CG . GLU A 205 ? 0.6513 0.6000 0.5957 -0.0129 -0.0095 -0.0192 205 GLU A CG 1623 C CD . GLU A 205 ? 0.7937 0.7379 0.7362 -0.0173 -0.0127 -0.0200 205 GLU A CD 1624 O OE1 . GLU A 205 ? 0.7708 0.7065 0.7062 -0.0180 -0.0129 -0.0220 205 GLU A OE1 1625 O OE2 . GLU A 205 ? 0.7687 0.7180 0.7165 -0.0202 -0.0151 -0.0187 205 GLU A OE2 1626 N N . SER A 206 ? 0.7171 0.6925 0.6830 -0.0163 -0.0111 -0.0124 206 SER A N 1627 C CA . SER A 206 ? 0.7634 0.7459 0.7356 -0.0160 -0.0101 -0.0105 206 SER A CA 1628 C C . SER A 206 ? 0.7465 0.7319 0.7198 -0.0184 -0.0116 -0.0091 206 SER A C 1629 O O . SER A 206 ? 0.7532 0.7437 0.7307 -0.0187 -0.0109 -0.0076 206 SER A O 1630 C CB . SER A 206 ? 0.7355 0.7192 0.7135 -0.0158 -0.0107 -0.0098 206 SER A CB 1631 O OG . SER A 206 ? 0.7357 0.7178 0.7153 -0.0185 -0.0138 -0.0095 206 SER A OG 1632 N N . MET A 207 ? 0.7146 0.6965 0.6838 -0.0201 -0.0138 -0.0097 207 MET A N 1633 C CA . MET A 207 ? 0.7042 0.6877 0.6735 -0.0220 -0.0156 -0.0083 207 MET A CA 1634 C C . MET A 207 ? 0.6980 0.6784 0.6602 -0.0225 -0.0159 -0.0091 207 MET A C 1635 O O . MET A 207 ? 0.7039 0.6800 0.6617 -0.0224 -0.0165 -0.0109 207 MET A O 1636 C CB . MET A 207 ? 0.6924 0.6759 0.6651 -0.0235 -0.0189 -0.0079 207 MET A CB 1637 C CG . MET A 207 ? 0.7092 0.6946 0.6825 -0.0246 -0.0209 -0.0064 207 MET A CG 1638 S SD . MET A 207 ? 0.7734 0.7554 0.7394 -0.0256 -0.0232 -0.0069 207 MET A SD 1639 C CE . MET A 207 ? 0.6616 0.6421 0.6279 -0.0269 -0.0263 -0.0085 207 MET A CE 1640 N N . ASN A 208 ? 0.5945 0.5764 0.5550 -0.0232 -0.0155 -0.0079 208 ASN A N 1641 C CA . ASN A 208 ? 0.6654 0.6441 0.6190 -0.0240 -0.0165 -0.0082 208 ASN A CA 1642 C C . ASN A 208 ? 0.6815 0.6609 0.6346 -0.0252 -0.0180 -0.0063 208 ASN A C 1643 O O . ASN A 208 ? 0.6788 0.6611 0.6351 -0.0254 -0.0169 -0.0047 208 ASN A O 1644 C CB . ASN A 208 ? 0.6589 0.6368 0.6073 -0.0231 -0.0134 -0.0092 208 ASN A CB 1645 C CG . ASN A 208 ? 0.7867 0.7694 0.7376 -0.0226 -0.0101 -0.0082 208 ASN A CG 1646 O OD1 . ASN A 208 ? 0.8287 0.8129 0.7789 -0.0241 -0.0098 -0.0067 208 ASN A OD1 1647 N ND2 . ASN A 208 ? 0.7648 0.7498 0.7181 -0.0207 -0.0077 -0.0091 208 ASN A ND2 1648 N N . PHE A 209 ? 0.5956 0.5721 0.5441 -0.0258 -0.0207 -0.0065 209 PHE A N 1649 C CA . PHE A 209 ? 0.5874 0.5637 0.5347 -0.0263 -0.0228 -0.0047 209 PHE A CA 1650 C C . PHE A 209 ? 0.6146 0.5871 0.5536 -0.0266 -0.0235 -0.0048 209 PHE A C 1651 O O . PHE A 209 ? 0.6232 0.5935 0.5585 -0.0267 -0.0244 -0.0065 209 PHE A O 1652 C CB . PHE A 209 ? 0.5763 0.5539 0.5278 -0.0262 -0.0263 -0.0046 209 PHE A CB 1653 C CG . PHE A 209 ? 0.5568 0.5338 0.5060 -0.0260 -0.0291 -0.0032 209 PHE A CG 1654 C CD1 . PHE A 209 ? 0.5788 0.5539 0.5227 -0.0260 -0.0318 -0.0038 209 PHE A CD1 1655 C CD2 . PHE A 209 ? 0.5621 0.5405 0.5142 -0.0255 -0.0292 -0.0012 209 PHE A CD2 1656 C CE1 . PHE A 209 ? 0.5628 0.5376 0.5044 -0.0251 -0.0346 -0.0023 209 PHE A CE1 1657 C CE2 . PHE A 209 ? 0.5838 0.5610 0.5332 -0.0245 -0.0318 0.0001 209 PHE A CE2 1658 C CZ . PHE A 209 ? 0.6373 0.6129 0.5815 -0.0241 -0.0345 -0.0004 209 PHE A CZ 1659 N N . ALA A 210 ? 0.5935 0.5647 0.5290 -0.0269 -0.0232 -0.0030 210 ALA A N 1660 C CA . ALA A 210 ? 0.6161 0.5833 0.5432 -0.0272 -0.0240 -0.0028 210 ALA A CA 1661 C C . ALA A 210 ? 0.6298 0.5950 0.5543 -0.0270 -0.0256 -0.0005 210 ALA A C 1662 O O . ALA A 210 ? 0.6296 0.5953 0.5558 -0.0275 -0.0238 0.0010 210 ALA A O 1663 C CB . ALA A 210 ? 0.5395 0.5057 0.4619 -0.0279 -0.0203 -0.0033 210 ALA A CB 1664 N N . LYS A 211 ? 0.7029 0.6659 0.6230 -0.0262 -0.0289 -0.0003 211 LYS A N 1665 C CA . LYS A 211 ? 0.7350 0.6950 0.6510 -0.0253 -0.0306 0.0019 211 LYS A CA 1666 C C . LYS A 211 ? 0.7937 0.7498 0.7010 -0.0246 -0.0328 0.0020 211 LYS A C 1667 O O . LYS A 211 ? 0.7541 0.7110 0.6601 -0.0247 -0.0343 0.0003 211 LYS A O 1668 C CB . LYS A 211 ? 0.7414 0.7044 0.6636 -0.0237 -0.0333 0.0026 211 LYS A CB 1669 C CG . LYS A 211 ? 0.7976 0.7589 0.7203 -0.0235 -0.0321 0.0048 211 LYS A CG 1670 C CD . LYS A 211 ? 0.8450 0.8053 0.7665 -0.0209 -0.0356 0.0063 211 LYS A CD 1671 C CE . LYS A 211 ? 0.8669 0.8215 0.7832 -0.0207 -0.0343 0.0086 211 LYS A CE 1672 N NZ . LYS A 211 ? 0.8360 0.7916 0.7569 -0.0226 -0.0310 0.0090 211 LYS A NZ 1673 N N . SER A 212 ? 0.8516 0.8030 0.7523 -0.0240 -0.0330 0.0041 212 SER A N 1674 C CA . SER A 212 ? 0.8030 0.7501 0.6946 -0.0230 -0.0352 0.0047 212 SER A CA 1675 C C . SER A 212 ? 0.8137 0.7587 0.7032 -0.0204 -0.0382 0.0068 212 SER A C 1676 O O . SER A 212 ? 0.8690 0.8130 0.7608 -0.0201 -0.0371 0.0083 212 SER A O 1677 C CB . SER A 212 ? 0.8013 0.7432 0.6844 -0.0248 -0.0320 0.0053 212 SER A CB 1678 O OG . SER A 212 ? 0.9186 0.8630 0.8038 -0.0267 -0.0291 0.0032 212 SER A OG 1679 N N . PRO A 213 ? 0.7514 0.6958 0.6363 -0.0183 -0.0420 0.0069 213 PRO A N 1680 C CA . PRO A 213 ? 0.7358 0.6788 0.6186 -0.0149 -0.0452 0.0088 213 PRO A CA 1681 C C . PRO A 213 ? 0.7676 0.7021 0.6421 -0.0145 -0.0434 0.0114 213 PRO A C 1682 O O . PRO A 213 ? 0.7700 0.6989 0.6368 -0.0164 -0.0409 0.0119 213 PRO A O 1683 C CB . PRO A 213 ? 0.7471 0.6910 0.6250 -0.0130 -0.0492 0.0082 213 PRO A CB 1684 C CG . PRO A 213 ? 0.7529 0.6953 0.6268 -0.0158 -0.0473 0.0065 213 PRO A CG 1685 C CD . PRO A 213 ? 0.7388 0.6842 0.6203 -0.0187 -0.0437 0.0051 213 PRO A CD 1686 N N . GLU A 214 ? 0.8368 0.7702 0.7126 -0.0120 -0.0445 0.0130 214 GLU A N 1687 C CA . GLU A 214 ? 0.8694 0.7938 0.7371 -0.0115 -0.0429 0.0156 214 GLU A CA 1688 C C . GLU A 214 ? 0.8661 0.7871 0.7274 -0.0066 -0.0469 0.0172 214 GLU A C 1689 O O . GLU A 214 ? 0.8347 0.7585 0.7004 -0.0033 -0.0492 0.0177 214 GLU A O 1690 C CB . GLU A 214 ? 0.8168 0.7418 0.6908 -0.0128 -0.0405 0.0160 214 GLU A CB 1691 C CG . GLU A 214 ? 0.8829 0.8122 0.7636 -0.0171 -0.0366 0.0144 214 GLU A CG 1692 C CD . GLU A 214 ? 1.0282 0.9614 0.9180 -0.0178 -0.0352 0.0143 214 GLU A CD 1693 O OE1 . GLU A 214 ? 0.9257 0.8589 0.8175 -0.0150 -0.0372 0.0152 214 GLU A OE1 1694 O OE2 . GLU A 214 ? 1.0090 0.9457 0.9040 -0.0210 -0.0321 0.0132 214 GLU A OE2 1695 N N . ILE A 215 ? 0.8026 0.7175 0.6531 -0.0058 -0.0478 0.0181 215 ILE A N 1696 C CA . ILE A 215 ? 0.7654 0.6779 0.6092 -0.0007 -0.0520 0.0195 215 ILE A CA 1697 C C . ILE A 215 ? 0.7702 0.6722 0.6049 0.0021 -0.0517 0.0224 215 ILE A C 1698 O O . ILE A 215 ? 0.7600 0.6519 0.5848 0.0000 -0.0489 0.0239 215 ILE A O 1699 C CB . ILE A 215 ? 0.7821 0.6926 0.6177 -0.0007 -0.0535 0.0191 215 ILE A CB 1700 C CG1 . ILE A 215 ? 0.8053 0.7253 0.6491 -0.0033 -0.0539 0.0161 215 ILE A CG1 1701 C CG2 . ILE A 215 ? 0.7472 0.6561 0.5760 0.0050 -0.0581 0.0206 215 ILE A CG2 1702 C CD1 . ILE A 215 ? 0.8520 0.7708 0.6882 -0.0035 -0.0555 0.0154 215 ILE A CD1 1703 N N . ALA A 216 ? 0.7392 0.6435 0.5769 0.0069 -0.0545 0.0231 216 ALA A N 1704 C CA . ALA A 216 ? 0.7928 0.6871 0.6218 0.0105 -0.0547 0.0258 216 ALA A CA 1705 C C . ALA A 216 ? 0.7940 0.6941 0.6276 0.0168 -0.0587 0.0260 216 ALA A C 1706 O O . ALA A 216 ? 0.7727 0.6850 0.6184 0.0169 -0.0603 0.0241 216 ALA A O 1707 C CB . ALA A 216 ? 0.8496 0.7381 0.6793 0.0066 -0.0502 0.0264 216 ALA A CB 1708 N N . ALA A 217 ? 0.8059 0.6973 0.6294 0.0221 -0.0603 0.0284 217 ALA A N 1709 C CA . ALA A 217 ? 0.8571 0.7538 0.6841 0.0288 -0.0640 0.0288 217 ALA A CA 1710 C C . ALA A 217 ? 0.8162 0.7113 0.6480 0.0288 -0.0619 0.0292 217 ALA A C 1711 O O . ALA A 217 ? 0.8401 0.7226 0.6632 0.0282 -0.0592 0.0310 217 ALA A O 1712 C CB . ALA A 217 ? 0.8912 0.7796 0.7049 0.0354 -0.0670 0.0312 217 ALA A CB 1713 N N . ARG A 218 ? 0.8514 0.7591 0.6967 0.0293 -0.0630 0.0275 218 ARG A N 1714 C CA . ARG A 218 ? 0.8793 0.7867 0.7297 0.0301 -0.0615 0.0277 218 ARG A CA 1715 C C . ARG A 218 ? 0.8881 0.7982 0.7375 0.0383 -0.0653 0.0287 218 ARG A C 1716 O O . ARG A 218 ? 0.8906 0.8062 0.7386 0.0424 -0.0691 0.0286 218 ARG A O 1717 C CB . ARG A 218 ? 0.8137 0.7332 0.6794 0.0255 -0.0601 0.0253 218 ARG A CB 1718 C CG . ARG A 218 ? 0.8207 0.7381 0.6883 0.0180 -0.0561 0.0243 218 ARG A CG 1719 C CD . ARG A 218 ? 0.8030 0.7252 0.6713 0.0153 -0.0569 0.0229 218 ARG A CD 1720 N NE . ARG A 218 ? 0.8497 0.7708 0.7200 0.0087 -0.0529 0.0218 218 ARG A NE 1721 C CZ . ARG A 218 ? 0.8844 0.8097 0.7566 0.0055 -0.0528 0.0202 218 ARG A CZ 1722 N NH1 . ARG A 218 ? 0.8107 0.7415 0.6828 0.0079 -0.0564 0.0195 218 ARG A NH1 1723 N NH2 . ARG A 218 ? 0.9275 0.8519 0.8013 0.0002 -0.0490 0.0194 218 ARG A NH2 1724 N N . PRO A 219 ? 0.8634 0.7695 0.7129 0.0409 -0.0642 0.0295 219 PRO A N 1725 C CA . PRO A 219 ? 0.8621 0.7722 0.7118 0.0491 -0.0677 0.0302 219 PRO A CA 1726 C C . PRO A 219 ? 0.8824 0.8110 0.7451 0.0505 -0.0711 0.0282 219 PRO A C 1727 O O . PRO A 219 ? 0.8666 0.8045 0.7403 0.0447 -0.0699 0.0261 219 PRO A O 1728 C CB . PRO A 219 ? 0.8823 0.7880 0.7342 0.0492 -0.0651 0.0306 219 PRO A CB 1729 C CG . PRO A 219 ? 0.8510 0.7434 0.6957 0.0429 -0.0608 0.0314 219 PRO A CG 1730 C CD . PRO A 219 ? 0.8234 0.7202 0.6712 0.0366 -0.0599 0.0301 219 PRO A CD 1731 N N . ALA A 220 ? 0.8396 0.7737 0.7006 0.0579 -0.0752 0.0287 220 ALA A N 1732 C CA . ALA A 220 ? 0.8078 0.7601 0.6804 0.0589 -0.0786 0.0267 220 ALA A CA 1733 C C . ALA A 220 ? 0.7986 0.7618 0.6844 0.0584 -0.0780 0.0252 220 ALA A C 1734 O O . ALA A 220 ? 0.7695 0.7294 0.6540 0.0629 -0.0775 0.0263 220 ALA A O 1735 C CB . ALA A 220 ? 0.8146 0.7707 0.6814 0.0671 -0.0833 0.0276 220 ALA A CB 1736 N N . VAL A 221 ? 0.7492 0.7248 0.6470 0.0529 -0.0780 0.0229 221 VAL A N 1737 C CA . VAL A 221 ? 0.7008 0.6886 0.6117 0.0520 -0.0778 0.0213 221 VAL A CA 1738 C C . VAL A 221 ? 0.6662 0.6707 0.5859 0.0511 -0.0812 0.0192 221 VAL A C 1739 O O . VAL A 221 ? 0.6634 0.6699 0.5842 0.0458 -0.0813 0.0179 221 VAL A O 1740 C CB . VAL A 221 ? 0.7130 0.6980 0.6301 0.0447 -0.0735 0.0203 221 VAL A CB 1741 C CG1 . VAL A 221 ? 0.5566 0.5541 0.4869 0.0438 -0.0734 0.0188 221 VAL A CG1 1742 C CG2 . VAL A 221 ? 0.6268 0.5959 0.5353 0.0447 -0.0701 0.0222 221 VAL A CG2 1743 N N . ASN A 222 ? 0.7308 0.7473 0.6563 0.0561 -0.0840 0.0188 222 ASN A N 1744 C CA . ASN A 222 ? 0.7880 0.8213 0.7210 0.0557 -0.0877 0.0169 222 ASN A CA 1745 C C . ASN A 222 ? 0.8356 0.8685 0.7611 0.0566 -0.0907 0.0170 222 ASN A C 1746 O O . ASN A 222 ? 0.8495 0.8921 0.7800 0.0524 -0.0924 0.0150 222 ASN A O 1747 C CB . ASN A 222 ? 0.7802 0.8225 0.7252 0.0477 -0.0861 0.0144 222 ASN A CB 1748 C CG . ASN A 222 ? 0.7986 0.8446 0.7521 0.0474 -0.0839 0.0141 222 ASN A CG 1749 O OD1 . ASN A 222 ? 0.8553 0.9025 0.8083 0.0537 -0.0846 0.0152 222 ASN A OD1 1750 N ND2 . ASN A 222 ? 0.7257 0.7733 0.6868 0.0402 -0.0812 0.0126 222 ASN A ND2 1751 N N . GLY A 223 ? 0.7299 0.7508 0.6428 0.0620 -0.0912 0.0194 223 GLY A N 1752 C CA . GLY A 223 ? 0.6988 0.7180 0.6031 0.0639 -0.0941 0.0198 223 GLY A CA 1753 C C . GLY A 223 ? 0.7529 0.7617 0.6517 0.0573 -0.0918 0.0196 223 GLY A C 1754 O O . GLY A 223 ? 0.7858 0.7939 0.6781 0.0577 -0.0940 0.0197 223 GLY A O 1755 N N . GLN A 224 ? 0.7866 0.7877 0.6875 0.0515 -0.0873 0.0194 224 GLN A N 1756 C CA . GLN A 224 ? 0.7330 0.7261 0.6302 0.0449 -0.0848 0.0189 224 GLN A CA 1757 C C . GLN A 224 ? 0.7718 0.7478 0.6600 0.0437 -0.0808 0.0208 224 GLN A C 1758 O O . GLN A 224 ? 0.7772 0.7492 0.6680 0.0435 -0.0781 0.0214 224 GLN A O 1759 C CB . GLN A 224 ? 0.7111 0.7128 0.6201 0.0374 -0.0832 0.0162 224 GLN A CB 1760 C CG . GLN A 224 ? 0.7571 0.7760 0.6762 0.0376 -0.0866 0.0141 224 GLN A CG 1761 C CD . GLN A 224 ? 0.7829 0.8081 0.6981 0.0394 -0.0909 0.0136 224 GLN A CD 1762 O OE1 . GLN A 224 ? 0.7511 0.7690 0.6584 0.0375 -0.0907 0.0137 224 GLN A OE1 1763 N NE2 . GLN A 224 ? 0.7405 0.7797 0.6611 0.0430 -0.0947 0.0128 224 GLN A NE2 1764 N N . ARG A 225 ? 0.8066 0.7728 0.6842 0.0427 -0.0803 0.0218 225 ARG A N 1765 C CA . ARG A 225 ? 0.8126 0.7629 0.6810 0.0405 -0.0764 0.0235 225 ARG A CA 1766 C C . ARG A 225 ? 0.7732 0.7230 0.6455 0.0323 -0.0730 0.0218 225 ARG A C 1767 O O . ARG A 225 ? 0.7752 0.7145 0.6428 0.0288 -0.0692 0.0226 225 ARG A O 1768 C CB . ARG A 225 ? 0.9224 0.8615 0.7757 0.0445 -0.0777 0.0257 225 ARG A CB 1769 C CG . ARG A 225 ? 0.9872 0.9271 0.8353 0.0536 -0.0816 0.0273 225 ARG A CG 1770 C CD . ARG A 225 ? 1.0653 0.9918 0.9052 0.0573 -0.0796 0.0298 225 ARG A CD 1771 N NE . ARG A 225 ? 1.1419 1.0512 0.9678 0.0553 -0.0769 0.0317 225 ARG A NE 1772 C CZ . ARG A 225 ? 1.1993 1.0936 1.0148 0.0575 -0.0748 0.0339 225 ARG A CZ 1773 N NH1 . ARG A 225 ? 1.1262 1.0204 0.9438 0.0622 -0.0750 0.0345 225 ARG A NH1 1774 N NH2 . ARG A 225 ? 1.1306 1.0099 0.9333 0.0547 -0.0723 0.0355 225 ARG A NH2 1775 N N . SER A 226 ? 0.6545 0.6157 0.5350 0.0294 -0.0746 0.0194 226 SER A N 1776 C CA . SER A 226 ? 0.6904 0.6525 0.5757 0.0223 -0.0717 0.0175 226 SER A CA 1777 C C . SER A 226 ? 0.6650 0.6322 0.5616 0.0194 -0.0693 0.0164 226 SER A C 1778 O O . SER A 226 ? 0.6488 0.6206 0.5504 0.0228 -0.0704 0.0168 226 SER A O 1779 C CB . SER A 226 ? 0.6482 0.6193 0.5364 0.0203 -0.0743 0.0154 226 SER A CB 1780 O OG . SER A 226 ? 0.8037 0.7704 0.6813 0.0228 -0.0766 0.0163 226 SER A OG 1781 N N . ARG A 227 ? 0.5759 0.5425 0.4764 0.0135 -0.0661 0.0151 227 ARG A N 1782 C CA . ARG A 227 ? 0.5816 0.5529 0.4926 0.0106 -0.0637 0.0140 227 ARG A CA 1783 C C . ARG A 227 ? 0.5953 0.5728 0.5131 0.0055 -0.0629 0.0114 227 ARG A C 1784 O O . ARG A 227 ? 0.6078 0.5841 0.5214 0.0036 -0.0633 0.0105 227 ARG A O 1785 C CB . ARG A 227 ? 0.5558 0.5174 0.4637 0.0089 -0.0595 0.0154 227 ARG A CB 1786 C CG . ARG A 227 ? 0.6023 0.5571 0.5044 0.0135 -0.0598 0.0177 227 ARG A CG 1787 C CD . ARG A 227 ? 0.5679 0.5308 0.4781 0.0169 -0.0617 0.0175 227 ARG A CD 1788 N NE . ARG A 227 ? 0.5940 0.5495 0.4987 0.0212 -0.0613 0.0196 227 ARG A NE 1789 C CZ . ARG A 227 ? 0.6564 0.6094 0.5541 0.0274 -0.0642 0.0211 227 ARG A CZ 1790 N NH1 . ARG A 227 ? 0.6949 0.6531 0.5907 0.0299 -0.0678 0.0207 227 ARG A NH1 1791 N NH2 . ARG A 227 ? 0.6309 0.5759 0.5230 0.0312 -0.0636 0.0229 227 ARG A NH2 1792 N N . ILE A 228 ? 0.6223 0.6058 0.5501 0.0034 -0.0617 0.0103 228 ILE A N 1793 C CA . ILE A 228 ? 0.5870 0.5740 0.5206 -0.0015 -0.0601 0.0081 228 ILE A CA 1794 C C . ILE A 228 ? 0.6056 0.5905 0.5442 -0.0039 -0.0562 0.0082 228 ILE A C 1795 O O . ILE A 228 ? 0.6346 0.6216 0.5779 -0.0022 -0.0560 0.0090 228 ILE A O 1796 C CB . ILE A 228 ? 0.5879 0.5858 0.5290 -0.0023 -0.0630 0.0061 228 ILE A CB 1797 C CG1 . ILE A 228 ? 0.6601 0.6608 0.5961 -0.0008 -0.0667 0.0056 228 ILE A CG1 1798 C CG2 . ILE A 228 ? 0.5619 0.5619 0.5087 -0.0073 -0.0608 0.0039 228 ILE A CG2 1799 C CD1 . ILE A 228 ? 0.6246 0.6363 0.5673 -0.0025 -0.0696 0.0034 228 ILE A CD1 1800 N N . ASP A 229 ? 0.6724 0.6534 0.6098 -0.0075 -0.0530 0.0075 229 ASP A N 1801 C CA . ASP A 229 ? 0.6405 0.6214 0.5837 -0.0100 -0.0496 0.0073 229 ASP A CA 1802 C C . ASP A 229 ? 0.6348 0.6228 0.5863 -0.0124 -0.0498 0.0051 229 ASP A C 1803 O O . ASP A 229 ? 0.5988 0.5866 0.5491 -0.0148 -0.0494 0.0035 229 ASP A O 1804 C CB . ASP A 229 ? 0.6900 0.6640 0.6282 -0.0124 -0.0459 0.0077 229 ASP A CB 1805 C CG . ASP A 229 ? 0.8440 0.8108 0.7760 -0.0111 -0.0445 0.0099 229 ASP A CG 1806 O OD1 . ASP A 229 ? 0.8598 0.8270 0.7938 -0.0087 -0.0454 0.0111 229 ASP A OD1 1807 O OD2 . ASP A 229 ? 0.8744 0.8349 0.7992 -0.0125 -0.0424 0.0106 229 ASP A OD2 1808 N N . TYR A 230 ? 0.4998 0.4934 0.4589 -0.0117 -0.0505 0.0050 230 TYR A N 1809 C CA . TYR A 230 ? 0.4464 0.4461 0.4130 -0.0142 -0.0506 0.0031 230 TYR A CA 1810 C C . TYR A 230 ? 0.4396 0.4369 0.4093 -0.0167 -0.0468 0.0027 230 TYR A C 1811 O O . TYR A 230 ? 0.4731 0.4668 0.4421 -0.0162 -0.0444 0.0041 230 TYR A O 1812 C CB . TYR A 230 ? 0.4208 0.4278 0.3941 -0.0126 -0.0527 0.0032 230 TYR A CB 1813 C CG . TYR A 230 ? 0.4780 0.4888 0.4489 -0.0094 -0.0566 0.0036 230 TYR A CG 1814 C CD1 . TYR A 230 ? 0.5057 0.5133 0.4722 -0.0053 -0.0573 0.0056 230 TYR A CD1 1815 C CD2 . TYR A 230 ? 0.4554 0.4729 0.4279 -0.0105 -0.0596 0.0020 230 TYR A CD2 1816 C CE1 . TYR A 230 ? 0.5182 0.5295 0.4822 -0.0016 -0.0609 0.0061 230 TYR A CE1 1817 C CE2 . TYR A 230 ? 0.4772 0.4994 0.4478 -0.0073 -0.0633 0.0023 230 TYR A CE2 1818 C CZ . TYR A 230 ? 0.5415 0.5607 0.5079 -0.0025 -0.0640 0.0045 230 TYR A CZ 1819 O OH . TYR A 230 ? 0.5469 0.5709 0.5110 0.0014 -0.0677 0.0049 230 TYR A OH 1820 N N . TYR A 231 ? 0.4041 0.4033 0.3767 -0.0194 -0.0461 0.0008 231 TYR A N 1821 C CA . TYR A 231 ? 0.4372 0.4346 0.4126 -0.0213 -0.0427 0.0004 231 TYR A CA 1822 C C . TYR A 231 ? 0.3925 0.3941 0.3741 -0.0231 -0.0430 -0.0012 231 TYR A C 1823 O O . TYR A 231 ? 0.4088 0.4142 0.3915 -0.0239 -0.0456 -0.0022 231 TYR A O 1824 C CB . TYR A 231 ? 0.4385 0.4307 0.4080 -0.0225 -0.0405 -0.0002 231 TYR A CB 1825 C CG . TYR A 231 ? 0.4853 0.4728 0.4483 -0.0213 -0.0396 0.0014 231 TYR A CG 1826 C CD1 . TYR A 231 ? 0.5125 0.4978 0.4758 -0.0214 -0.0367 0.0027 231 TYR A CD1 1827 C CD2 . TYR A 231 ? 0.5437 0.5287 0.4998 -0.0204 -0.0416 0.0016 231 TYR A CD2 1828 C CE1 . TYR A 231 ? 0.5535 0.5338 0.5101 -0.0210 -0.0357 0.0041 231 TYR A CE1 1829 C CE2 . TYR A 231 ? 0.5121 0.4918 0.4613 -0.0195 -0.0406 0.0032 231 TYR A CE2 1830 C CZ . TYR A 231 ? 0.6193 0.5965 0.5687 -0.0200 -0.0376 0.0044 231 TYR A CZ 1831 O OH . TYR A 231 ? 0.6704 0.6418 0.6123 -0.0198 -0.0365 0.0059 231 TYR A OH 1832 N N . TRP A 232 ? 0.4606 0.4616 0.4460 -0.0241 -0.0402 -0.0013 232 TRP A N 1833 C CA . TRP A 232 ? 0.4310 0.4347 0.4215 -0.0259 -0.0401 -0.0026 232 TRP A CA 1834 C C . TRP A 232 ? 0.4332 0.4337 0.4240 -0.0266 -0.0366 -0.0030 232 TRP A C 1835 O O . TRP A 232 ? 0.4439 0.4423 0.4333 -0.0257 -0.0344 -0.0020 232 TRP A O 1836 C CB . TRP A 232 ? 0.4334 0.4422 0.4305 -0.0253 -0.0409 -0.0018 232 TRP A CB 1837 C CG . TRP A 232 ? 0.4818 0.4898 0.4815 -0.0241 -0.0385 -0.0003 232 TRP A CG 1838 C CD1 . TRP A 232 ? 0.4327 0.4395 0.4309 -0.0221 -0.0383 0.0014 232 TRP A CD1 1839 C CD2 . TRP A 232 ? 0.4284 0.4364 0.4323 -0.0249 -0.0360 -0.0004 232 TRP A CD2 1840 N NE1 . TRP A 232 ? 0.4274 0.4337 0.4285 -0.0220 -0.0359 0.0022 232 TRP A NE1 1841 C CE2 . TRP A 232 ? 0.4274 0.4350 0.4324 -0.0236 -0.0345 0.0012 232 TRP A CE2 1842 C CE3 . TRP A 232 ? 0.4266 0.4345 0.4328 -0.0266 -0.0350 -0.0016 232 TRP A CE3 1843 C CZ2 . TRP A 232 ? 0.3983 0.4063 0.4072 -0.0239 -0.0321 0.0015 232 TRP A CZ2 1844 C CZ3 . TRP A 232 ? 0.4277 0.4357 0.4376 -0.0265 -0.0325 -0.0012 232 TRP A CZ3 1845 C CH2 . TRP A 232 ? 0.3947 0.4032 0.4061 -0.0251 -0.0312 0.0004 232 TRP A CH2 1846 N N . SER A 233 ? 0.4658 0.4658 0.4578 -0.0283 -0.0362 -0.0046 233 SER A N 1847 C CA . SER A 233 ? 0.4357 0.4329 0.4280 -0.0284 -0.0331 -0.0050 233 SER A CA 1848 C C . SER A 233 ? 0.4567 0.4540 0.4518 -0.0301 -0.0333 -0.0062 233 SER A C 1849 O O . SER A 233 ? 0.4692 0.4692 0.4660 -0.0317 -0.0357 -0.0068 233 SER A O 1850 C CB . SER A 233 ? 0.4267 0.4192 0.4125 -0.0283 -0.0317 -0.0059 233 SER A CB 1851 O OG . SER A 233 ? 0.4923 0.4827 0.4784 -0.0277 -0.0287 -0.0063 233 SER A OG 1852 N N . VAL A 234 ? 0.4377 0.4324 0.4332 -0.0298 -0.0306 -0.0066 234 VAL A N 1853 C CA . VAL A 234 ? 0.4436 0.4367 0.4404 -0.0313 -0.0304 -0.0077 234 VAL A CA 1854 C C . VAL A 234 ? 0.4969 0.4836 0.4880 -0.0311 -0.0286 -0.0092 234 VAL A C 1855 O O . VAL A 234 ? 0.5067 0.4919 0.4967 -0.0289 -0.0260 -0.0088 234 VAL A O 1856 C CB . VAL A 234 ? 0.4004 0.3958 0.4030 -0.0305 -0.0290 -0.0065 234 VAL A CB 1857 C CG1 . VAL A 234 ? 0.4163 0.4085 0.4189 -0.0318 -0.0282 -0.0076 234 VAL A CG1 1858 C CG2 . VAL A 234 ? 0.3860 0.3874 0.3939 -0.0308 -0.0309 -0.0053 234 VAL A CG2 1859 N N . LEU A 235 ? 0.4959 0.4792 0.4830 -0.0334 -0.0299 -0.0109 235 LEU A N 1860 C CA . LEU A 235 ? 0.4875 0.4637 0.4683 -0.0332 -0.0282 -0.0126 235 LEU A CA 1861 C C . LEU A 235 ? 0.5063 0.4790 0.4880 -0.0333 -0.0267 -0.0130 235 LEU A C 1862 O O . LEU A 235 ? 0.5314 0.5037 0.5141 -0.0362 -0.0281 -0.0135 235 LEU A O 1863 C CB . LEU A 235 ? 0.5265 0.4997 0.5016 -0.0359 -0.0304 -0.0145 235 LEU A CB 1864 C CG . LEU A 235 ? 0.6004 0.5654 0.5676 -0.0356 -0.0288 -0.0164 235 LEU A CG 1865 C CD1 . LEU A 235 ? 0.5588 0.5232 0.5231 -0.0325 -0.0269 -0.0160 235 LEU A CD1 1866 C CD2 . LEU A 235 ? 0.5578 0.5196 0.5197 -0.0392 -0.0311 -0.0184 235 LEU A CD2 1867 N N . ARG A 236 ? 0.6268 0.5973 0.6079 -0.0303 -0.0238 -0.0126 236 ARG A N 1868 C CA . ARG A 236 ? 0.6531 0.6202 0.6349 -0.0296 -0.0222 -0.0126 236 ARG A CA 1869 C C . ARG A 236 ? 0.6615 0.6197 0.6362 -0.0312 -0.0221 -0.0146 236 ARG A C 1870 O O . ARG A 236 ? 0.6939 0.6481 0.6625 -0.0317 -0.0224 -0.0161 236 ARG A O 1871 C CB . ARG A 236 ? 0.7050 0.6731 0.6879 -0.0254 -0.0193 -0.0116 236 ARG A CB 1872 C CG . ARG A 236 ? 0.7843 0.7605 0.7735 -0.0242 -0.0192 -0.0097 236 ARG A CG 1873 C CD . ARG A 236 ? 0.9273 0.9049 0.9166 -0.0205 -0.0163 -0.0091 236 ARG A CD 1874 N NE . ARG A 236 ? 0.9847 0.9689 0.9776 -0.0200 -0.0160 -0.0078 236 ARG A NE 1875 C CZ . ARG A 236 ? 1.0472 1.0342 1.0400 -0.0176 -0.0136 -0.0073 236 ARG A CZ 1876 N NH1 . ARG A 236 ? 0.9648 0.9494 0.9548 -0.0148 -0.0114 -0.0082 236 ARG A NH1 1877 N NH2 . ARG A 236 ? 1.0500 1.0423 1.0455 -0.0181 -0.0135 -0.0061 236 ARG A NH2 1878 N N . PRO A 237 ? 0.5518 0.5063 0.5266 -0.0321 -0.0215 -0.0147 237 PRO A N 1879 C CA . PRO A 237 ? 0.5471 0.4915 0.5140 -0.0337 -0.0211 -0.0166 237 PRO A CA 1880 C C . PRO A 237 ? 0.6227 0.5604 0.5825 -0.0297 -0.0187 -0.0175 237 PRO A C 1881 O O . PRO A 237 ? 0.5812 0.5200 0.5427 -0.0253 -0.0164 -0.0165 237 PRO A O 1882 C CB . PRO A 237 ? 0.5382 0.4802 0.5069 -0.0338 -0.0201 -0.0158 237 PRO A CB 1883 C CG . PRO A 237 ? 0.4992 0.4512 0.4773 -0.0345 -0.0213 -0.0139 237 PRO A CG 1884 C CD . PRO A 237 ? 0.4869 0.4459 0.4685 -0.0319 -0.0213 -0.0130 237 PRO A CD 1885 N N . GLY A 238 ? 0.6523 0.5839 0.6047 -0.0312 -0.0192 -0.0195 238 GLY A N 1886 C CA . GLY A 238 ? 0.6349 0.5600 0.5801 -0.0274 -0.0169 -0.0207 238 GLY A CA 1887 C C . GLY A 238 ? 0.7137 0.6438 0.6589 -0.0259 -0.0170 -0.0207 238 GLY A C 1888 O O . GLY A 238 ? 0.7316 0.6564 0.6699 -0.0238 -0.0155 -0.0221 238 GLY A O 1889 N N . GLU A 239 ? 0.6989 0.6385 0.6513 -0.0270 -0.0185 -0.0192 239 GLU A N 1890 C CA . GLU A 239 ? 0.6723 0.6163 0.6245 -0.0262 -0.0188 -0.0190 239 GLU A CA 1891 C C . GLU A 239 ? 0.6784 0.6200 0.6259 -0.0299 -0.0213 -0.0205 239 GLU A C 1892 O O . GLU A 239 ? 0.6355 0.5758 0.5829 -0.0337 -0.0235 -0.0212 239 GLU A O 1893 C CB . GLU A 239 ? 0.6168 0.5706 0.5774 -0.0258 -0.0194 -0.0167 239 GLU A CB 1894 C CG . GLU A 239 ? 0.6827 0.6404 0.6473 -0.0219 -0.0167 -0.0153 239 GLU A CG 1895 C CD . GLU A 239 ? 0.7577 0.7241 0.7292 -0.0220 -0.0173 -0.0133 239 GLU A CD 1896 O OE1 . GLU A 239 ? 0.6458 0.6151 0.6200 -0.0248 -0.0199 -0.0127 239 GLU A OE1 1897 O OE2 . GLU A 239 ? 0.8022 0.7725 0.7761 -0.0194 -0.0152 -0.0122 239 GLU A OE2 1898 N N . THR A 240 ? 0.6484 0.5900 0.5918 -0.0288 -0.0210 -0.0211 240 THR A N 1899 C CA . THR A 240 ? 0.6940 0.6349 0.6335 -0.0320 -0.0237 -0.0223 240 THR A CA 1900 C C . THR A 240 ? 0.6784 0.6265 0.6208 -0.0313 -0.0246 -0.0208 240 THR A C 1901 O O . THR A 240 ? 0.6660 0.6169 0.6101 -0.0282 -0.0224 -0.0196 240 THR A O 1902 C CB . THR A 240 ? 0.7465 0.6781 0.6757 -0.0321 -0.0228 -0.0248 240 THR A CB 1903 O OG1 . THR A 240 ? 0.7676 0.7004 0.6936 -0.0299 -0.0218 -0.0248 240 THR A OG1 1904 C CG2 . THR A 240 ? 0.7073 0.6311 0.6327 -0.0297 -0.0200 -0.0257 240 THR A CG2 1905 N N . LEU A 241 ? 0.7131 0.6641 0.6557 -0.0342 -0.0278 -0.0209 241 LEU A N 1906 C CA . LEU A 241 ? 0.6991 0.6557 0.6433 -0.0335 -0.0290 -0.0194 241 LEU A CA 1907 C C . LEU A 241 ? 0.7324 0.6857 0.6688 -0.0343 -0.0300 -0.0209 241 LEU A C 1908 O O . LEU A 241 ? 0.7233 0.6731 0.6553 -0.0371 -0.0318 -0.0228 241 LEU A O 1909 C CB . LEU A 241 ? 0.6488 0.6121 0.5993 -0.0354 -0.0321 -0.0181 241 LEU A CB 1910 C CG . LEU A 241 ? 0.6687 0.6366 0.6192 -0.0350 -0.0342 -0.0169 241 LEU A CG 1911 C CD1 . LEU A 241 ? 0.6777 0.6475 0.6299 -0.0321 -0.0318 -0.0149 241 LEU A CD1 1912 C CD2 . LEU A 241 ? 0.6358 0.6100 0.5915 -0.0366 -0.0375 -0.0161 241 LEU A CD2 1913 N N . ASN A 242 ? 0.7168 0.6711 0.6511 -0.0322 -0.0287 -0.0200 242 ASN A N 1914 C CA . ASN A 242 ? 0.7035 0.6555 0.6306 -0.0328 -0.0297 -0.0210 242 ASN A CA 1915 C C . ASN A 242 ? 0.6883 0.6455 0.6171 -0.0328 -0.0319 -0.0191 242 ASN A C 1916 O O . ASN A 242 ? 0.7522 0.7130 0.6849 -0.0311 -0.0307 -0.0170 242 ASN A O 1917 C CB . ASN A 242 ? 0.7322 0.6799 0.6535 -0.0304 -0.0263 -0.0218 242 ASN A CB 1918 C CG . ASN A 242 ? 0.7851 0.7256 0.7015 -0.0302 -0.0247 -0.0242 242 ASN A CG 1919 O OD1 . ASN A 242 ? 0.8420 0.7790 0.7566 -0.0329 -0.0266 -0.0257 242 ASN A OD1 1920 N ND2 . ASN A 242 ? 0.8253 0.7634 0.7391 -0.0271 -0.0210 -0.0246 242 ASN A ND2 1921 N N . VAL A 243 ? 0.6074 0.5649 0.5327 -0.0348 -0.0352 -0.0199 243 VAL A N 1922 C CA . VAL A 243 ? 0.6254 0.5870 0.5508 -0.0343 -0.0376 -0.0182 243 VAL A CA 1923 C C . VAL A 243 ? 0.6872 0.6451 0.6039 -0.0342 -0.0377 -0.0189 243 VAL A C 1924 O O . VAL A 243 ? 0.7377 0.6913 0.6487 -0.0357 -0.0381 -0.0213 243 VAL A O 1925 C CB . VAL A 243 ? 0.6322 0.5988 0.5612 -0.0363 -0.0417 -0.0182 243 VAL A CB 1926 C CG1 . VAL A 243 ? 0.5800 0.5506 0.5089 -0.0348 -0.0441 -0.0162 243 VAL A CG1 1927 C CG2 . VAL A 243 ? 0.6617 0.6316 0.5988 -0.0368 -0.0415 -0.0177 243 VAL A CG2 1928 N N . GLU A 244 ? 0.8062 0.7652 0.7213 -0.0325 -0.0372 -0.0171 244 GLU A N 1929 C CA . GLU A 244 ? 0.8355 0.7911 0.7420 -0.0323 -0.0373 -0.0175 244 GLU A CA 1930 C C . GLU A 244 ? 0.8373 0.7952 0.7429 -0.0311 -0.0388 -0.0150 244 GLU A C 1931 O O . GLU A 244 ? 0.8039 0.7631 0.7125 -0.0298 -0.0369 -0.0130 244 GLU A O 1932 C CB . GLU A 244 ? 0.8149 0.7664 0.7175 -0.0311 -0.0329 -0.0182 244 GLU A CB 1933 C CG . GLU A 244 ? 0.9218 0.8693 0.8149 -0.0311 -0.0326 -0.0190 244 GLU A CG 1934 C CD . GLU A 244 ? 1.0609 1.0059 0.9507 -0.0297 -0.0280 -0.0194 244 GLU A CD 1935 O OE1 . GLU A 244 ? 0.9557 0.8992 0.8395 -0.0293 -0.0270 -0.0188 244 GLU A OE1 1936 O OE2 . GLU A 244 ? 1.0065 0.9512 0.8997 -0.0288 -0.0254 -0.0202 244 GLU A OE2 1937 N N . SER A 245 ? 0.7153 0.6734 0.6163 -0.0317 -0.0423 -0.0153 245 SER A N 1938 C CA . SER A 245 ? 0.7446 0.7040 0.6434 -0.0301 -0.0441 -0.0130 245 SER A CA 1939 C C . SER A 245 ? 0.7730 0.7299 0.6629 -0.0305 -0.0464 -0.0138 245 SER A C 1940 O O . SER A 245 ? 0.7447 0.7003 0.6315 -0.0323 -0.0475 -0.0162 245 SER A O 1941 C CB . SER A 245 ? 0.6510 0.6161 0.5564 -0.0295 -0.0474 -0.0117 245 SER A CB 1942 O OG . SER A 245 ? 0.6579 0.6234 0.5600 -0.0275 -0.0493 -0.0096 245 SER A OG 1943 N N . ASN A 246 ? 0.8240 0.7795 0.7090 -0.0288 -0.0469 -0.0117 246 ASN A N 1944 C CA . ASN A 246 ? 0.8547 0.8083 0.7311 -0.0287 -0.0495 -0.0120 246 ASN A CA 1945 C C . ASN A 246 ? 0.8807 0.8372 0.7569 -0.0266 -0.0532 -0.0098 246 ASN A C 1946 O O . ASN A 246 ? 0.9119 0.8661 0.7804 -0.0255 -0.0550 -0.0090 246 ASN A O 1947 C CB . ASN A 246 ? 0.8226 0.7702 0.6906 -0.0286 -0.0463 -0.0118 246 ASN A CB 1948 C CG . ASN A 246 ? 0.8838 0.8296 0.7512 -0.0271 -0.0440 -0.0089 246 ASN A CG 1949 O OD1 . ASN A 246 ? 0.8974 0.8458 0.7714 -0.0263 -0.0437 -0.0073 246 ASN A OD1 1950 N ND2 . ASN A 246 ? 0.9157 0.8567 0.7745 -0.0270 -0.0422 -0.0081 246 ASN A ND2 1951 N N . GLY A 247 ? 0.8371 0.7984 0.7215 -0.0257 -0.0543 -0.0087 247 GLY A N 1952 C CA . GLY A 247 ? 0.8323 0.7967 0.7169 -0.0230 -0.0577 -0.0067 247 GLY A CA 1953 C C . GLY A 247 ? 0.8427 0.8091 0.7344 -0.0213 -0.0567 -0.0047 247 GLY A C 1954 O O . GLY A 247 ? 0.8525 0.8170 0.7477 -0.0222 -0.0529 -0.0044 247 GLY A O 1955 N N . ASN A 248 ? 0.8090 0.7797 0.7027 -0.0188 -0.0601 -0.0033 248 ASN A N 1956 C CA . ASN A 248 ? 0.7974 0.7700 0.6972 -0.0168 -0.0596 -0.0014 248 ASN A CA 1957 C C . ASN A 248 ? 0.7656 0.7431 0.6757 -0.0187 -0.0583 -0.0027 248 ASN A C 1958 O O . ASN A 248 ? 0.7626 0.7404 0.6776 -0.0177 -0.0567 -0.0013 248 ASN A O 1959 C CB . ASN A 248 ? 0.7501 0.7154 0.6454 -0.0157 -0.0563 0.0009 248 ASN A CB 1960 C CG . ASN A 248 ? 0.7927 0.7523 0.6771 -0.0138 -0.0574 0.0024 248 ASN A CG 1961 O OD1 . ASN A 248 ? 0.8539 0.8095 0.7317 -0.0154 -0.0563 0.0016 248 ASN A OD1 1962 N ND2 . ASN A 248 ? 0.7917 0.7505 0.6736 -0.0102 -0.0596 0.0047 248 ASN A ND2 1963 N N . LEU A 249 ? 0.6347 0.6154 0.5474 -0.0215 -0.0591 -0.0052 249 LEU A N 1964 C CA . LEU A 249 ? 0.6121 0.5966 0.5336 -0.0235 -0.0579 -0.0064 249 LEU A CA 1965 C C . LEU A 249 ? 0.6232 0.6163 0.5512 -0.0232 -0.0615 -0.0068 249 LEU A C 1966 O O . LEU A 249 ? 0.6558 0.6530 0.5822 -0.0241 -0.0649 -0.0082 249 LEU A O 1967 C CB . LEU A 249 ? 0.6408 0.6228 0.5612 -0.0269 -0.0562 -0.0091 249 LEU A CB 1968 C CG . LEU A 249 ? 0.5872 0.5723 0.5154 -0.0292 -0.0553 -0.0105 249 LEU A CG 1969 C CD1 . LEU A 249 ? 0.5985 0.5826 0.5320 -0.0281 -0.0519 -0.0090 249 LEU A CD1 1970 C CD2 . LEU A 249 ? 0.5812 0.5626 0.5065 -0.0323 -0.0540 -0.0132 249 LEU A CD2 1971 N N . ILE A 250 ? 0.7113 0.7074 0.6464 -0.0221 -0.0607 -0.0057 250 ILE A N 1972 C CA . ILE A 250 ? 0.6510 0.6557 0.5937 -0.0228 -0.0631 -0.0065 250 ILE A CA 1973 C C . ILE A 250 ? 0.6504 0.6545 0.5976 -0.0267 -0.0608 -0.0084 250 ILE A C 1974 O O . ILE A 250 ? 0.6801 0.6816 0.6308 -0.0266 -0.0575 -0.0077 250 ILE A O 1975 C CB . ILE A 250 ? 0.6252 0.6335 0.5732 -0.0195 -0.0634 -0.0044 250 ILE A CB 1976 C CG1 . ILE A 250 ? 0.6445 0.6500 0.5862 -0.0152 -0.0648 -0.0021 250 ILE A CG1 1977 C CG2 . ILE A 250 ? 0.5992 0.6176 0.5545 -0.0200 -0.0663 -0.0052 250 ILE A CG2 1978 C CD1 . ILE A 250 ? 0.6105 0.6196 0.5474 -0.0139 -0.0690 -0.0025 250 ILE A CD1 1979 N N . ALA A 251 ? 0.5982 0.6043 0.5447 -0.0300 -0.0623 -0.0108 251 ALA A N 1980 C CA . ALA A 251 ? 0.6238 0.6268 0.5718 -0.0336 -0.0599 -0.0128 251 ALA A CA 1981 C C . ALA A 251 ? 0.5745 0.5826 0.5309 -0.0353 -0.0598 -0.0131 251 ALA A C 1982 O O . ALA A 251 ? 0.5829 0.5991 0.5438 -0.0351 -0.0626 -0.0129 251 ALA A O 1983 C CB . ALA A 251 ? 0.6119 0.6130 0.5541 -0.0369 -0.0613 -0.0153 251 ALA A CB 1984 N N . PRO A 252 ? 0.5050 0.5086 0.4634 -0.0368 -0.0564 -0.0137 252 PRO A N 1985 C CA . PRO A 252 ? 0.5409 0.5485 0.5061 -0.0391 -0.0563 -0.0144 252 PRO A CA 1986 C C . PRO A 252 ? 0.5687 0.5789 0.5324 -0.0434 -0.0588 -0.0169 252 PRO A C 1987 O O . PRO A 252 ? 0.5943 0.5991 0.5512 -0.0453 -0.0587 -0.0186 252 PRO A O 1988 C CB . PRO A 252 ? 0.4673 0.4679 0.4326 -0.0394 -0.0522 -0.0145 252 PRO A CB 1989 C CG . PRO A 252 ? 0.5148 0.5081 0.4724 -0.0385 -0.0505 -0.0149 252 PRO A CG 1990 C CD . PRO A 252 ? 0.5053 0.5007 0.4598 -0.0361 -0.0526 -0.0136 252 PRO A CD 1991 N N . TRP A 253 ? 0.5605 0.5789 0.5300 -0.0452 -0.0609 -0.0172 253 TRP A N 1992 C CA . TRP A 253 ? 0.5074 0.5297 0.4760 -0.0500 -0.0634 -0.0196 253 TRP A CA 1993 C C . TRP A 253 ? 0.5320 0.5553 0.5056 -0.0536 -0.0621 -0.0205 253 TRP A C 1994 O O . TRP A 253 ? 0.5103 0.5270 0.4804 -0.0573 -0.0606 -0.0223 253 TRP A O 1995 C CB . TRP A 253 ? 0.5004 0.5336 0.4711 -0.0490 -0.0677 -0.0193 253 TRP A CB 1996 C CG . TRP A 253 ? 0.5685 0.6073 0.5382 -0.0543 -0.0707 -0.0219 253 TRP A CG 1997 C CD1 . TRP A 253 ? 0.5221 0.5553 0.4875 -0.0596 -0.0700 -0.0244 253 TRP A CD1 1998 C CD2 . TRP A 253 ? 0.5591 0.6104 0.5320 -0.0547 -0.0748 -0.0222 253 TRP A CD2 1999 N NE1 . TRP A 253 ? 0.5666 0.6079 0.5321 -0.0640 -0.0734 -0.0264 253 TRP A NE1 2000 C CE2 . TRP A 253 ? 0.5628 0.6161 0.5333 -0.0610 -0.0765 -0.0251 253 TRP A CE2 2001 C CE3 . TRP A 253 ? 0.5303 0.5914 0.5074 -0.0501 -0.0773 -0.0204 253 TRP A CE3 2002 C CZ2 . TRP A 253 ? 0.5165 0.5824 0.4893 -0.0632 -0.0805 -0.0262 253 TRP A CZ2 2003 C CZ3 . TRP A 253 ? 0.5541 0.6276 0.5336 -0.0517 -0.0814 -0.0215 253 TRP A CZ3 2004 C CH2 . TRP A 253 ? 0.5205 0.5970 0.4982 -0.0583 -0.0830 -0.0244 253 TRP A CH2 2005 N N . TYR A 254 ? 0.5382 0.5693 0.5196 -0.0523 -0.0626 -0.0191 254 TYR A N 2006 C CA . TYR A 254 ? 0.5757 0.6076 0.5622 -0.0551 -0.0610 -0.0194 254 TYR A CA 2007 C C . TYR A 254 ? 0.5258 0.5534 0.5156 -0.0514 -0.0577 -0.0173 254 TYR A C 2008 O O . TYR A 254 ? 0.5003 0.5291 0.4913 -0.0468 -0.0575 -0.0153 254 TYR A O 2009 C CB . TYR A 254 ? 0.5877 0.6322 0.5808 -0.0567 -0.0638 -0.0195 254 TYR A CB 2010 C CG . TYR A 254 ? 0.6297 0.6793 0.6207 -0.0620 -0.0667 -0.0220 254 TYR A CG 2011 C CD1 . TYR A 254 ? 0.6506 0.7057 0.6388 -0.0611 -0.0701 -0.0225 254 TYR A CD1 2012 C CD2 . TYR A 254 ? 0.6449 0.6937 0.6362 -0.0682 -0.0660 -0.0239 254 TYR A CD2 2013 C CE1 . TYR A 254 ? 0.6244 0.6849 0.6106 -0.0664 -0.0729 -0.0249 254 TYR A CE1 2014 C CE2 . TYR A 254 ? 0.6547 0.7082 0.6437 -0.0738 -0.0687 -0.0263 254 TYR A CE2 2015 C CZ . TYR A 254 ? 0.6800 0.7398 0.6667 -0.0729 -0.0721 -0.0268 254 TYR A CZ 2016 O OH . TYR A 254 ? 0.6485 0.7137 0.6329 -0.0789 -0.0748 -0.0294 254 TYR A OH 2017 N N . ALA A 255 ? 0.5168 0.5393 0.5074 -0.0536 -0.0550 -0.0178 255 ALA A N 2018 C CA . ALA A 255 ? 0.4633 0.4823 0.4571 -0.0505 -0.0519 -0.0160 255 ALA A CA 2019 C C . ALA A 255 ? 0.4256 0.4470 0.4248 -0.0531 -0.0509 -0.0160 255 ALA A C 2020 O O . ALA A 255 ? 0.4665 0.4928 0.4671 -0.0572 -0.0527 -0.0173 255 ALA A O 2021 C CB . ALA A 255 ? 0.4902 0.4985 0.4782 -0.0494 -0.0489 -0.0162 255 ALA A CB 2022 N N . TYR A 256 ? 0.4547 0.4726 0.4565 -0.0509 -0.0481 -0.0146 256 TYR A N 2023 C CA . TYR A 256 ? 0.4481 0.4681 0.4549 -0.0529 -0.0470 -0.0144 256 TYR A CA 2024 C C . TYR A 256 ? 0.4283 0.4391 0.4327 -0.0531 -0.0437 -0.0145 256 TYR A C 2025 O O . TYR A 256 ? 0.4819 0.4882 0.4854 -0.0495 -0.0416 -0.0134 256 TYR A O 2026 C CB . TYR A 256 ? 0.4025 0.4301 0.4165 -0.0496 -0.0472 -0.0124 256 TYR A CB 2027 C CG . TYR A 256 ? 0.3940 0.4316 0.4110 -0.0489 -0.0505 -0.0122 256 TYR A CG 2028 C CD1 . TYR A 256 ? 0.4402 0.4863 0.4611 -0.0522 -0.0524 -0.0131 256 TYR A CD1 2029 C CD2 . TYR A 256 ? 0.4065 0.4452 0.4221 -0.0447 -0.0516 -0.0110 256 TYR A CD2 2030 C CE1 . TYR A 256 ? 0.4095 0.4658 0.4333 -0.0509 -0.0555 -0.0129 256 TYR A CE1 2031 C CE2 . TYR A 256 ? 0.4572 0.5048 0.4749 -0.0433 -0.0547 -0.0107 256 TYR A CE2 2032 C CZ . TYR A 256 ? 0.4563 0.5131 0.4784 -0.0461 -0.0567 -0.0117 256 TYR A CZ 2033 O OH . TYR A 256 ? 0.5201 0.5866 0.5443 -0.0441 -0.0598 -0.0115 256 TYR A OH 2034 N N . LYS A 257 ? 0.4584 0.4664 0.4615 -0.0575 -0.0433 -0.0158 257 LYS A N 2035 C CA . LYS A 257 ? 0.5262 0.5264 0.5279 -0.0573 -0.0403 -0.0155 257 LYS A CA 2036 C C . LYS A 257 ? 0.4636 0.4694 0.4728 -0.0556 -0.0394 -0.0136 257 LYS A C 2037 O O . LYS A 257 ? 0.4790 0.4926 0.4932 -0.0578 -0.0409 -0.0136 257 LYS A O 2038 C CB . LYS A 257 ? 0.5809 0.5749 0.5776 -0.0626 -0.0400 -0.0175 257 LYS A CB 2039 C CG . LYS A 257 ? 0.5946 0.5786 0.5821 -0.0629 -0.0393 -0.0192 257 LYS A CG 2040 C CD . LYS A 257 ? 0.7047 0.6859 0.6869 -0.0692 -0.0408 -0.0216 257 LYS A CD 2041 C CE . LYS A 257 ? 0.7265 0.6978 0.6994 -0.0691 -0.0403 -0.0233 257 LYS A CE 2042 N NZ . LYS A 257 ? 0.8802 0.8479 0.8469 -0.0756 -0.0417 -0.0259 257 LYS A NZ 2043 N N . PHE A 258 ? 0.5148 0.5172 0.5249 -0.0515 -0.0370 -0.0122 258 PHE A N 2044 C CA . PHE A 258 ? 0.5017 0.5094 0.5185 -0.0491 -0.0363 -0.0103 258 PHE A CA 2045 C C . PHE A 258 ? 0.4868 0.4898 0.5040 -0.0494 -0.0339 -0.0098 258 PHE A C 2046 O O . PHE A 258 ? 0.5429 0.5382 0.5560 -0.0477 -0.0317 -0.0099 258 PHE A O 2047 C CB . PHE A 258 ? 0.4881 0.4966 0.5056 -0.0444 -0.0358 -0.0089 258 PHE A CB 2048 C CG . PHE A 258 ? 0.5102 0.5241 0.5339 -0.0419 -0.0353 -0.0070 258 PHE A CG 2049 C CD1 . PHE A 258 ? 0.4934 0.5151 0.5212 -0.0412 -0.0374 -0.0064 258 PHE A CD1 2050 C CD2 . PHE A 258 ? 0.5004 0.5115 0.5256 -0.0400 -0.0328 -0.0060 258 PHE A CD2 2051 C CE1 . PHE A 258 ? 0.5270 0.5529 0.5598 -0.0387 -0.0369 -0.0047 258 PHE A CE1 2052 C CE2 . PHE A 258 ? 0.5401 0.5560 0.5707 -0.0380 -0.0323 -0.0043 258 PHE A CE2 2053 C CZ . PHE A 258 ? 0.5099 0.5326 0.5440 -0.0374 -0.0343 -0.0038 258 PHE A CZ 2054 N N . VAL A 259 ? 0.3998 0.4076 0.4219 -0.0513 -0.0341 -0.0093 259 VAL A N 2055 C CA . VAL A 259 ? 0.4583 0.4623 0.4811 -0.0513 -0.0318 -0.0085 259 VAL A CA 2056 C C . VAL A 259 ? 0.4741 0.4830 0.5029 -0.0475 -0.0310 -0.0066 259 VAL A C 2057 O O . VAL A 259 ? 0.4784 0.4954 0.5127 -0.0475 -0.0323 -0.0059 259 VAL A O 2058 C CB . VAL A 259 ? 0.4986 0.5041 0.5224 -0.0563 -0.0323 -0.0092 259 VAL A CB 2059 C CG1 . VAL A 259 ? 0.4636 0.4625 0.4859 -0.0564 -0.0298 -0.0086 259 VAL A CG1 2060 C CG2 . VAL A 259 ? 0.5321 0.5347 0.5505 -0.0610 -0.0337 -0.0114 259 VAL A CG2 2061 N N . SER A 260 ? 0.5799 0.5840 0.6073 -0.0441 -0.0288 -0.0057 260 SER A N 2062 C CA . SER A 260 ? 0.6155 0.6236 0.6479 -0.0408 -0.0279 -0.0039 260 SER A CA 2063 C C . SER A 260 ? 0.7140 0.7235 0.7498 -0.0419 -0.0270 -0.0031 260 SER A C 2064 O O . SER A 260 ? 0.7046 0.7082 0.7373 -0.0434 -0.0257 -0.0035 260 SER A O 2065 C CB . SER A 260 ? 0.6246 0.6284 0.6545 -0.0372 -0.0259 -0.0034 260 SER A CB 2066 O OG . SER A 260 ? 0.7686 0.7758 0.8029 -0.0347 -0.0248 -0.0018 260 SER A OG 2067 N N . THR A 261 ? 1.0716 1.0883 1.1133 -0.0410 -0.0275 -0.0020 261 THR A N 2068 C CA . THR A 261 ? 1.1278 1.1464 1.1730 -0.0418 -0.0266 -0.0012 261 THR A CA 2069 C C . THR A 261 ? 1.2022 1.2164 1.2465 -0.0389 -0.0243 -0.0001 261 THR A C 2070 O O . THR A 261 ? 1.1775 1.1919 1.2220 -0.0357 -0.0237 0.0005 261 THR A O 2071 C CB . THR A 261 ? 1.1214 1.1491 1.1729 -0.0414 -0.0277 -0.0004 261 THR A CB 2072 O OG1 . THR A 261 ? 1.2511 1.2809 1.3053 -0.0434 -0.0271 0.0000 261 THR A OG1 2073 C CG2 . THR A 261 ? 1.1276 1.1573 1.1814 -0.0373 -0.0272 0.0009 261 THR A CG2 2074 N N . ASN A 262 ? 1.5100 1.5203 1.5530 -0.0402 -0.0230 0.0001 262 ASN A N 2075 C CA . ASN A 262 ? 1.6343 1.6417 1.6770 -0.0373 -0.0210 0.0012 262 ASN A CA 2076 C C . ASN A 262 ? 1.6396 1.6539 1.6883 -0.0357 -0.0210 0.0026 262 ASN A C 2077 O O . ASN A 262 ? 1.6222 1.6368 1.6719 -0.0327 -0.0198 0.0035 262 ASN A O 2078 C CB . ASN A 262 ? 1.7125 1.7134 1.7517 -0.0391 -0.0198 0.0012 262 ASN A CB 2079 C CG . ASN A 262 ? 1.7715 1.7725 1.8125 -0.0368 -0.0182 0.0027 262 ASN A CG 2080 O OD1 . ASN A 262 ? 1.8107 1.8148 1.8548 -0.0385 -0.0182 0.0033 262 ASN A OD1 2081 N ND2 . ASN A 262 ? 1.7068 1.7050 1.7459 -0.0330 -0.0169 0.0032 262 ASN A ND2 2082 N N . LYS A 263 ? 1.2686 1.2889 1.3213 -0.0378 -0.0223 0.0025 263 LYS A N 2083 C CA . LYS A 263 ? 1.2360 1.2625 1.2940 -0.0365 -0.0222 0.0036 263 LYS A CA 2084 C C . LYS A 263 ? 1.2192 1.2490 1.2789 -0.0337 -0.0228 0.0041 263 LYS A C 2085 O O . LYS A 263 ? 1.2099 1.2367 1.2670 -0.0317 -0.0222 0.0041 263 LYS A O 2086 C CB . LYS A 263 ? 1.2800 1.3121 1.3414 -0.0393 -0.0233 0.0034 263 LYS A CB 2087 C CG . LYS A 263 ? 1.3190 1.3481 1.3781 -0.0433 -0.0230 0.0026 263 LYS A CG 2088 C CD . LYS A 263 ? 1.4515 1.4743 1.5080 -0.0431 -0.0210 0.0034 263 LYS A CD 2089 C CE . LYS A 263 ? 1.5071 1.5249 1.5596 -0.0474 -0.0206 0.0026 263 LYS A CE 2090 N NZ . LYS A 263 ? 1.4548 1.4629 1.5017 -0.0464 -0.0188 0.0030 263 LYS A NZ 2091 N N . LYS A 264 ? 1.1733 1.2091 1.2367 -0.0335 -0.0238 0.0044 264 LYS A N 2092 C CA . LYS A 264 ? 1.1132 1.1514 1.1778 -0.0308 -0.0242 0.0050 264 LYS A CA 2093 C C . LYS A 264 ? 1.0797 1.1196 1.1432 -0.0306 -0.0261 0.0043 264 LYS A C 2094 O O . LYS A 264 ? 1.1061 1.1435 1.1668 -0.0292 -0.0262 0.0043 264 LYS A O 2095 C CB . LYS A 264 ? 1.0364 1.0791 1.1050 -0.0300 -0.0240 0.0058 264 LYS A CB 2096 C CG . LYS A 264 ? 0.9884 1.0324 1.0573 -0.0274 -0.0241 0.0065 264 LYS A CG 2097 C CD . LYS A 264 ? 0.9568 1.0047 1.0293 -0.0267 -0.0238 0.0072 264 LYS A CD 2098 C CE . LYS A 264 ? 0.9074 0.9558 0.9794 -0.0243 -0.0240 0.0078 264 LYS A CE 2099 N NZ . LYS A 264 ? 0.7591 0.8109 0.8340 -0.0235 -0.0236 0.0082 264 LYS A NZ 2100 N N . GLY A 265 ? 0.7419 0.7865 0.8075 -0.0321 -0.0276 0.0038 265 GLY A N 2101 C CA . GLY A 265 ? 0.6284 0.6757 0.6932 -0.0316 -0.0297 0.0032 265 GLY A CA 2102 C C . GLY A 265 ? 0.5261 0.5768 0.5924 -0.0286 -0.0305 0.0040 265 GLY A C 2103 O O . GLY A 265 ? 0.5675 0.6155 0.6329 -0.0265 -0.0294 0.0049 265 GLY A O 2104 N N . ALA A 266 ? 0.4515 0.5084 0.5200 -0.0283 -0.0323 0.0037 266 ALA A N 2105 C CA . ALA A 266 ? 0.4427 0.5025 0.5120 -0.0248 -0.0331 0.0044 266 ALA A CA 2106 C C . ALA A 266 ? 0.4203 0.4839 0.4885 -0.0235 -0.0356 0.0039 266 ALA A C 2107 O O . ALA A 266 ? 0.3604 0.4279 0.4295 -0.0258 -0.0369 0.0028 266 ALA A O 2108 C CB . ALA A 266 ? 0.4025 0.4674 0.4762 -0.0244 -0.0325 0.0048 266 ALA A CB 2109 N N . VAL A 267 ? 0.5161 0.5781 0.5818 -0.0199 -0.0362 0.0047 267 VAL A N 2110 C CA . VAL A 267 ? 0.4389 0.5049 0.5035 -0.0176 -0.0387 0.0045 267 VAL A CA 2111 C C . VAL A 267 ? 0.4706 0.5395 0.5365 -0.0137 -0.0389 0.0053 267 VAL A C 2112 O O . VAL A 267 ? 0.5263 0.5896 0.5890 -0.0112 -0.0380 0.0063 267 VAL A O 2113 C CB . VAL A 267 ? 0.4951 0.5551 0.5538 -0.0165 -0.0394 0.0047 267 VAL A CB 2114 C CG1 . VAL A 267 ? 0.4326 0.4965 0.4897 -0.0133 -0.0420 0.0047 267 VAL A CG1 2115 C CG2 . VAL A 267 ? 0.4764 0.5335 0.5335 -0.0200 -0.0392 0.0037 267 VAL A CG2 2116 N N . PHE A 268 ? 0.4414 0.5192 0.5117 -0.0132 -0.0401 0.0048 268 PHE A N 2117 C CA . PHE A 268 ? 0.4009 0.4823 0.4726 -0.0091 -0.0402 0.0054 268 PHE A CA 2118 C C . PHE A 268 ? 0.4505 0.5346 0.5195 -0.0047 -0.0427 0.0056 268 PHE A C 2119 O O . PHE A 268 ? 0.4885 0.5795 0.5590 -0.0052 -0.0448 0.0047 268 PHE A O 2120 C CB . PHE A 268 ? 0.4093 0.4996 0.4873 -0.0106 -0.0398 0.0048 268 PHE A CB 2121 C CG . PHE A 268 ? 0.4416 0.5286 0.5215 -0.0139 -0.0373 0.0050 268 PHE A CG 2122 C CD1 . PHE A 268 ? 0.4414 0.5196 0.5183 -0.0135 -0.0355 0.0059 268 PHE A CD1 2123 C CD2 . PHE A 268 ? 0.4195 0.5125 0.5041 -0.0176 -0.0367 0.0043 268 PHE A CD2 2124 C CE1 . PHE A 268 ? 0.3817 0.4575 0.4603 -0.0161 -0.0333 0.0061 268 PHE A CE1 2125 C CE2 . PHE A 268 ? 0.4034 0.4929 0.4891 -0.0203 -0.0345 0.0046 268 PHE A CE2 2126 C CZ . PHE A 268 ? 0.4149 0.4960 0.4977 -0.0193 -0.0328 0.0055 268 PHE A CZ 2127 N N . LYS A 269 ? 0.5178 0.5961 0.5824 -0.0003 -0.0424 0.0066 269 LYS A N 2128 C CA . LYS A 269 ? 0.5178 0.5977 0.5791 0.0049 -0.0446 0.0070 269 LYS A CA 2129 C C . LYS A 269 ? 0.5384 0.6255 0.6032 0.0086 -0.0447 0.0071 269 LYS A C 2130 O O . LYS A 269 ? 0.5787 0.6608 0.6415 0.0111 -0.0432 0.0078 269 LYS A O 2131 C CB . LYS A 269 ? 0.5473 0.6156 0.6006 0.0075 -0.0440 0.0082 269 LYS A CB 2132 C CG . LYS A 269 ? 0.7260 0.7919 0.7739 0.0094 -0.0462 0.0084 269 LYS A CG 2133 C CD . LYS A 269 ? 0.8298 0.8847 0.8719 0.0070 -0.0448 0.0089 269 LYS A CD 2134 C CE . LYS A 269 ? 0.8255 0.8806 0.8716 0.0012 -0.0431 0.0082 269 LYS A CE 2135 N NZ . LYS A 269 ? 0.8007 0.8461 0.8429 -0.0007 -0.0407 0.0088 269 LYS A NZ 2136 N N . SER A 270 ? 0.4266 0.5256 0.4962 0.0090 -0.0465 0.0061 270 SER A N 2137 C CA . SER A 270 ? 0.4464 0.5541 0.5203 0.0121 -0.0465 0.0060 270 SER A CA 2138 C C . SER A 270 ? 0.4918 0.6124 0.5688 0.0145 -0.0493 0.0051 270 SER A C 2139 O O . SER A 270 ? 0.4948 0.6192 0.5724 0.0117 -0.0510 0.0044 270 SER A O 2140 C CB . SER A 270 ? 0.4094 0.5207 0.4893 0.0075 -0.0443 0.0054 270 SER A CB 2141 O OG . SER A 270 ? 0.4076 0.5280 0.4919 0.0103 -0.0441 0.0052 270 SER A OG 2142 N N . ASP A 271 ? 0.5369 0.6645 0.6157 0.0197 -0.0497 0.0052 271 ASP A N 2143 C CA . ASP A 271 ? 0.5874 0.7295 0.6700 0.0223 -0.0523 0.0044 271 ASP A CA 2144 C C . ASP A 271 ? 0.5644 0.7193 0.6554 0.0196 -0.0513 0.0033 271 ASP A C 2145 O O . ASP A 271 ? 0.5869 0.7554 0.6820 0.0224 -0.0529 0.0026 271 ASP A O 2146 C CB . ASP A 271 ? 0.6193 0.7611 0.6973 0.0313 -0.0538 0.0052 271 ASP A CB 2147 C CG . ASP A 271 ? 0.9117 1.0479 0.9878 0.0355 -0.0515 0.0060 271 ASP A CG 2148 O OD1 . ASP A 271 ? 0.9295 1.0710 1.0050 0.0425 -0.0524 0.0062 271 ASP A OD1 2149 O OD2 . ASP A 271 ? 0.9253 1.0518 1.0003 0.0319 -0.0489 0.0064 271 ASP A OD2 2150 N N . LEU A 272 ? 0.4736 0.6243 0.5670 0.0140 -0.0487 0.0033 272 LEU A N 2151 C CA . LEU A 272 ? 0.4782 0.6390 0.5786 0.0106 -0.0474 0.0024 272 LEU A CA 2152 C C . LEU A 272 ? 0.4414 0.6130 0.5467 0.0046 -0.0487 0.0010 272 LEU A C 2153 O O . LEU A 272 ? 0.4154 0.5823 0.5184 0.0006 -0.0496 0.0007 272 LEU A O 2154 C CB . LEU A 272 ? 0.3779 0.5297 0.4784 0.0067 -0.0442 0.0029 272 LEU A CB 2155 C CG . LEU A 272 ? 0.4611 0.6051 0.5586 0.0113 -0.0424 0.0040 272 LEU A CG 2156 C CD1 . LEU A 272 ? 0.3659 0.5033 0.4643 0.0067 -0.0395 0.0043 272 LEU A CD1 2157 C CD2 . LEU A 272 ? 0.4177 0.5720 0.5180 0.0169 -0.0427 0.0038 272 LEU A CD2 2158 N N . PRO A 273 ? 0.3841 0.5703 0.4958 0.0037 -0.0488 0.0000 273 PRO A N 2159 C CA . PRO A 273 ? 0.3923 0.5900 0.5086 -0.0025 -0.0500 -0.0015 273 PRO A CA 2160 C C . PRO A 273 ? 0.4017 0.5930 0.5184 -0.0110 -0.0481 -0.0019 273 PRO A C 2161 O O . PRO A 273 ? 0.3967 0.5813 0.5134 -0.0123 -0.0454 -0.0012 273 PRO A O 2162 C CB . PRO A 273 ? 0.4297 0.6437 0.5525 -0.0010 -0.0499 -0.0022 273 PRO A CB 2163 C CG . PRO A 273 ? 0.4278 0.6356 0.5499 0.0032 -0.0473 -0.0011 273 PRO A CG 2164 C CD . PRO A 273 ? 0.4064 0.5992 0.5210 0.0084 -0.0477 0.0002 273 PRO A CD 2165 N N . ILE A 274 ? 0.4640 0.6568 0.5803 -0.0166 -0.0494 -0.0029 274 ILE A N 2166 C CA . ILE A 274 ? 0.4429 0.6310 0.5594 -0.0249 -0.0477 -0.0035 274 ILE A CA 2167 C C . ILE A 274 ? 0.4971 0.7001 0.6196 -0.0299 -0.0477 -0.0049 274 ILE A C 2168 O O . ILE A 274 ? 0.5669 0.7818 0.6917 -0.0309 -0.0501 -0.0061 274 ILE A O 2169 C CB . ILE A 274 ? 0.4478 0.6284 0.5597 -0.0286 -0.0490 -0.0041 274 ILE A CB 2170 C CG1 . ILE A 274 ? 0.4331 0.6007 0.5391 -0.0236 -0.0493 -0.0028 274 ILE A CG1 2171 C CG2 . ILE A 274 ? 0.3921 0.5661 0.5031 -0.0366 -0.0471 -0.0046 274 ILE A CG2 2172 C CD1 . ILE A 274 ? 0.4170 0.5765 0.5182 -0.0270 -0.0502 -0.0033 274 ILE A CD1 2173 N N . GLU A 275 ? 0.5580 0.7606 0.6829 -0.0331 -0.0450 -0.0047 275 GLU A N 2174 C CA . GLU A 275 ? 0.5428 0.7596 0.6733 -0.0380 -0.0445 -0.0059 275 GLU A CA 2175 C C . GLU A 275 ? 0.5766 0.7879 0.7056 -0.0474 -0.0430 -0.0066 275 GLU A C 2176 O O . GLU A 275 ? 0.5647 0.7612 0.6885 -0.0493 -0.0421 -0.0060 275 GLU A O 2177 C CB . GLU A 275 ? 0.5613 0.7842 0.6958 -0.0342 -0.0427 -0.0052 275 GLU A CB 2178 C CG . GLU A 275 ? 0.5351 0.7638 0.6705 -0.0247 -0.0442 -0.0047 275 GLU A CG 2179 C CD . GLU A 275 ? 0.6905 0.9256 0.8296 -0.0209 -0.0422 -0.0043 275 GLU A CD 2180 O OE1 . GLU A 275 ? 0.6400 0.8773 0.7818 -0.0260 -0.0399 -0.0045 275 GLU A OE1 2181 O OE2 . GLU A 275 ? 0.6385 0.8757 0.7772 -0.0126 -0.0430 -0.0037 275 GLU A OE2 2182 N N . ASN A 276 ? 0.5926 0.8157 0.7258 -0.0532 -0.0425 -0.0077 276 ASN A N 2183 C CA . ASN A 276 ? 0.6438 0.8615 0.7748 -0.0624 -0.0409 -0.0084 276 ASN A CA 2184 C C . ASN A 276 ? 0.7131 0.9245 0.8441 -0.0639 -0.0375 -0.0073 276 ASN A C 2185 O O . ASN A 276 ? 0.7173 0.9386 0.8523 -0.0671 -0.0361 -0.0077 276 ASN A O 2186 C CB . ASN A 276 ? 0.6396 0.8725 0.7741 -0.0692 -0.0420 -0.0104 276 ASN A CB 2187 C CG . ASN A 276 ? 0.7310 0.9561 0.8613 -0.0791 -0.0408 -0.0112 276 ASN A CG 2188 O OD1 . ASN A 276 ? 0.6953 0.9037 0.8195 -0.0802 -0.0399 -0.0106 276 ASN A OD1 2189 N ND2 . ASN A 276 ? 0.7544 0.9917 0.8877 -0.0864 -0.0406 -0.0127 276 ASN A ND2 2190 N N . CYS A 277 ? 0.8425 1.0378 0.9689 -0.0614 -0.0361 -0.0059 277 CYS A N 2191 C CA . CYS A 277 ? 0.7773 0.9657 0.9032 -0.0619 -0.0331 -0.0047 277 CYS A CA 2192 C C . CYS A 277 ? 0.7153 0.8855 0.8348 -0.0628 -0.0319 -0.0037 277 CYS A C 2193 O O . CYS A 277 ? 0.7332 0.8960 0.8491 -0.0611 -0.0333 -0.0038 277 CYS A O 2194 C CB . CYS A 277 ? 0.7629 0.9553 0.8920 -0.0542 -0.0325 -0.0036 277 CYS A CB 2195 S SG . CYS A 277 ? 0.9943 1.1805 1.1209 -0.0450 -0.0345 -0.0028 277 CYS A SG 2196 N N . ASP A 278 ? 0.5603 0.7236 0.6783 -0.0653 -0.0292 -0.0029 278 ASP A N 2197 C CA . ASP A 278 ? 0.5301 0.6771 0.6424 -0.0654 -0.0279 -0.0018 278 ASP A CA 2198 C C . ASP A 278 ? 0.5620 0.7040 0.6746 -0.0592 -0.0266 -0.0002 278 ASP A C 2199 O O . ASP A 278 ? 0.5139 0.6636 0.6306 -0.0566 -0.0259 0.0001 278 ASP A O 2200 C CB . ASP A 278 ? 0.4957 0.6366 0.6046 -0.0726 -0.0259 -0.0019 278 ASP A CB 2201 C CG . ASP A 278 ? 0.7130 0.8458 0.8164 -0.0772 -0.0267 -0.0029 278 ASP A CG 2202 O OD1 . ASP A 278 ? 0.7561 0.8814 0.8565 -0.0738 -0.0278 -0.0027 278 ASP A OD1 2203 O OD2 . ASP A 278 ? 0.8278 0.9613 0.9295 -0.0844 -0.0261 -0.0038 278 ASP A OD2 2204 N N . ALA A 279 ? 0.4456 0.5749 0.5537 -0.0569 -0.0263 0.0006 279 ALA A N 2205 C CA . ALA A 279 ? 0.3799 0.5037 0.4877 -0.0518 -0.0251 0.0021 279 ALA A CA 2206 C C . ALA A 279 ? 0.3596 0.4695 0.4621 -0.0524 -0.0239 0.0029 279 ALA A C 2207 O O . ALA A 279 ? 0.3874 0.4913 0.4861 -0.0551 -0.0245 0.0024 279 ALA A O 2208 C CB . ALA A 279 ? 0.3547 0.4814 0.4638 -0.0454 -0.0267 0.0023 279 ALA A CB 2209 N N . THR A 280 ? 0.4429 0.5480 0.5449 -0.0495 -0.0224 0.0042 280 THR A N 2210 C CA . THR A 280 ? 0.4220 0.5153 0.5194 -0.0488 -0.0214 0.0050 280 THR A CA 2211 C C . THR A 280 ? 0.3949 0.4852 0.4918 -0.0433 -0.0220 0.0056 280 THR A C 2212 O O . THR A 280 ? 0.4301 0.5122 0.5234 -0.0423 -0.0219 0.0060 280 THR A O 2213 C CB . THR A 280 ? 0.4966 0.5862 0.5932 -0.0502 -0.0191 0.0061 280 THR A CB 2214 O OG1 . THR A 280 ? 0.5423 0.6398 0.6432 -0.0485 -0.0185 0.0064 280 THR A OG1 2215 C CG2 . THR A 280 ? 0.3962 0.4835 0.4904 -0.0562 -0.0182 0.0057 280 THR A CG2 2216 N N . CYS A 281 ? 0.4210 0.5180 0.5212 -0.0398 -0.0226 0.0057 281 CYS A N 2217 C CA . CYS A 281 ? 0.4054 0.4996 0.5046 -0.0348 -0.0231 0.0062 281 CYS A CA 2218 C C . CYS A 281 ? 0.3817 0.4825 0.4826 -0.0319 -0.0251 0.0056 281 CYS A C 2219 O O . CYS A 281 ? 0.4153 0.5246 0.5196 -0.0307 -0.0253 0.0053 281 CYS A O 2220 C CB . CYS A 281 ? 0.3993 0.4926 0.4992 -0.0325 -0.0215 0.0072 281 CYS A CB 2221 S SG . CYS A 281 ? 0.4798 0.5703 0.5782 -0.0269 -0.0220 0.0077 281 CYS A SG 2222 N N . GLN A 282 ? 0.3252 0.4223 0.4234 -0.0304 -0.0265 0.0054 282 GLN A N 2223 C CA . GLN A 282 ? 0.3183 0.4206 0.4171 -0.0272 -0.0285 0.0050 282 GLN A CA 2224 C C . GLN A 282 ? 0.3322 0.4281 0.4275 -0.0228 -0.0288 0.0057 282 GLN A C 2225 O O . GLN A 282 ? 0.3286 0.4175 0.4204 -0.0233 -0.0289 0.0059 282 GLN A O 2226 C CB . GLN A 282 ? 0.2846 0.3891 0.3828 -0.0299 -0.0303 0.0039 282 GLN A CB 2227 C CG . GLN A 282 ? 0.3138 0.4239 0.4123 -0.0265 -0.0326 0.0035 282 GLN A CG 2228 C CD . GLN A 282 ? 0.3837 0.5058 0.4869 -0.0253 -0.0333 0.0030 282 GLN A CD 2229 O OE1 . GLN A 282 ? 0.4111 0.5407 0.5173 -0.0293 -0.0335 0.0021 282 GLN A OE1 2230 N NE2 . GLN A 282 ? 0.3571 0.4811 0.4604 -0.0198 -0.0336 0.0035 282 GLN A NE2 2231 N N . THR A 283 ? 0.2646 0.3628 0.3605 -0.0187 -0.0287 0.0061 283 THR A N 2232 C CA . THR A 283 ? 0.3117 0.4038 0.4035 -0.0147 -0.0291 0.0067 283 THR A CA 2233 C C . THR A 283 ? 0.3416 0.4372 0.4324 -0.0117 -0.0314 0.0063 283 THR A C 2234 O O . THR A 283 ? 0.3360 0.4404 0.4300 -0.0122 -0.0327 0.0055 283 THR A O 2235 C CB . THR A 283 ? 0.2958 0.3862 0.3871 -0.0116 -0.0278 0.0074 283 THR A CB 2236 O OG1 . THR A 283 ? 0.3074 0.4052 0.4006 -0.0081 -0.0286 0.0070 283 THR A OG1 2237 C CG2 . THR A 283 ? 0.2980 0.3877 0.3913 -0.0144 -0.0257 0.0077 283 THR A CG2 2238 N N . ILE A 284 ? 0.3498 0.4387 0.4357 -0.0087 -0.0319 0.0069 284 ILE A N 2239 C CA . ILE A 284 ? 0.3792 0.4701 0.4630 -0.0054 -0.0341 0.0067 284 ILE A CA 2240 C C . ILE A 284 ? 0.3886 0.4870 0.4744 -0.0009 -0.0349 0.0066 284 ILE A C 2241 O O . ILE A 284 ? 0.3906 0.4944 0.4763 0.0017 -0.0370 0.0062 284 ILE A O 2242 C CB . ILE A 284 ? 0.3860 0.4667 0.4632 -0.0033 -0.0342 0.0074 284 ILE A CB 2243 C CG1 . ILE A 284 ? 0.3954 0.4772 0.4697 -0.0005 -0.0366 0.0073 284 ILE A CG1 2244 C CG2 . ILE A 284 ? 0.3654 0.4408 0.4398 -0.0002 -0.0329 0.0082 284 ILE A CG2 2245 C CD1 . ILE A 284 ? 0.3805 0.4520 0.4477 0.0013 -0.0366 0.0081 284 ILE A CD1 2246 N N . THR A 285 ? 0.3899 0.4889 0.4772 0.0001 -0.0332 0.0068 285 THR A N 2247 C CA . THR A 285 ? 0.4147 0.5205 0.5036 0.0048 -0.0336 0.0067 285 THR A CA 2248 C C . THR A 285 ? 0.4019 0.5193 0.4976 0.0026 -0.0332 0.0059 285 THR A C 2249 O O . THR A 285 ? 0.4368 0.5613 0.5346 0.0062 -0.0332 0.0057 285 THR A O 2250 C CB . THR A 285 ? 0.4660 0.5645 0.5509 0.0084 -0.0321 0.0074 285 THR A CB 2251 O OG1 . THR A 285 ? 0.5219 0.6174 0.6083 0.0048 -0.0299 0.0076 285 THR A OG1 2252 C CG2 . THR A 285 ? 0.4641 0.5514 0.5415 0.0106 -0.0326 0.0082 285 THR A CG2 2253 N N . GLY A 286 ? 0.3171 0.4362 0.4159 -0.0033 -0.0326 0.0055 286 GLY A N 2254 C CA . GLY A 286 ? 0.3880 0.5175 0.4926 -0.0064 -0.0321 0.0048 286 GLY A CA 2255 C C . GLY A 286 ? 0.4047 0.5308 0.5105 -0.0123 -0.0301 0.0049 286 GLY A C 2256 O O . GLY A 286 ? 0.3466 0.4626 0.4492 -0.0136 -0.0292 0.0055 286 GLY A O 2257 N N . VAL A 287 ? 0.3861 0.5209 0.4966 -0.0157 -0.0295 0.0043 287 VAL A N 2258 C CA . VAL A 287 ? 0.3644 0.4964 0.4757 -0.0213 -0.0277 0.0044 287 VAL A CA 2259 C C . VAL A 287 ? 0.4014 0.5312 0.5132 -0.0205 -0.0254 0.0051 287 VAL A C 2260 O O . VAL A 287 ? 0.4089 0.5447 0.5226 -0.0170 -0.0251 0.0051 287 VAL A O 2261 C CB . VAL A 287 ? 0.4342 0.5765 0.5497 -0.0261 -0.0280 0.0034 287 VAL A CB 2262 C CG1 . VAL A 287 ? 0.3775 0.5153 0.4925 -0.0320 -0.0261 0.0036 287 VAL A CG1 2263 C CG2 . VAL A 287 ? 0.4430 0.5887 0.5582 -0.0272 -0.0304 0.0024 287 VAL A CG2 2264 N N . LEU A 288 ? 0.4366 0.5580 0.5462 -0.0233 -0.0239 0.0058 288 LEU A N 2265 C CA . LEU A 288 ? 0.4833 0.6031 0.5934 -0.0234 -0.0217 0.0064 288 LEU A CA 2266 C C . LEU A 288 ? 0.4389 0.5611 0.5509 -0.0290 -0.0204 0.0063 288 LEU A C 2267 O O . LEU A 288 ? 0.5050 0.6222 0.6151 -0.0329 -0.0204 0.0064 288 LEU A O 2268 C CB . LEU A 288 ? 0.4808 0.5896 0.5869 -0.0221 -0.0209 0.0074 288 LEU A CB 2269 C CG . LEU A 288 ? 0.4524 0.5565 0.5552 -0.0176 -0.0219 0.0076 288 LEU A CG 2270 C CD1 . LEU A 288 ? 0.3880 0.4827 0.4873 -0.0173 -0.0207 0.0084 288 LEU A CD1 2271 C CD2 . LEU A 288 ? 0.4234 0.5331 0.5273 -0.0130 -0.0223 0.0073 288 LEU A CD2 2272 N N . ARG A 289 ? 0.3594 0.4888 0.4745 -0.0294 -0.0191 0.0062 289 ARG A N 2273 C CA . ARG A 289 ? 0.4534 0.5835 0.5693 -0.0345 -0.0174 0.0064 289 ARG A CA 2274 C C . ARG A 289 ? 0.4064 0.5328 0.5214 -0.0333 -0.0154 0.0073 289 ARG A C 2275 O O . ARG A 289 ? 0.3769 0.5100 0.4945 -0.0316 -0.0145 0.0072 289 ARG A O 2276 C CB . ARG A 289 ? 0.4497 0.5922 0.5699 -0.0373 -0.0175 0.0054 289 ARG A CB 2277 C CG . ARG A 289 ? 0.4686 0.6148 0.5894 -0.0398 -0.0195 0.0044 289 ARG A CG 2278 C CD . ARG A 289 ? 0.4339 0.5933 0.5591 -0.0434 -0.0195 0.0033 289 ARG A CD 2279 N NE . ARG A 289 ? 0.5432 0.7087 0.6697 -0.0431 -0.0220 0.0022 289 ARG A NE 2280 C CZ . ARG A 289 ? 0.4642 0.6257 0.5883 -0.0471 -0.0232 0.0017 289 ARG A CZ 2281 N NH1 . ARG A 289 ? 0.3606 0.5116 0.4808 -0.0516 -0.0219 0.0022 289 ARG A NH1 2282 N NH2 . ARG A 289 ? 0.5143 0.6820 0.6396 -0.0465 -0.0255 0.0007 289 ARG A NH2 2283 N N . THR A 290 ? 0.4504 0.5666 0.5618 -0.0339 -0.0147 0.0082 290 THR A N 2284 C CA . THR A 290 ? 0.5094 0.6216 0.6195 -0.0327 -0.0130 0.0092 290 THR A CA 2285 C C . THR A 290 ? 0.4607 0.5645 0.5675 -0.0357 -0.0119 0.0101 290 THR A C 2286 O O . THR A 290 ? 0.4586 0.5574 0.5632 -0.0377 -0.0126 0.0101 290 THR A O 2287 C CB . THR A 290 ? 0.4679 0.5757 0.5761 -0.0278 -0.0135 0.0094 290 THR A CB 2288 O OG1 . THR A 290 ? 0.5789 0.6877 0.6870 -0.0253 -0.0154 0.0088 290 THR A OG1 2289 C CG2 . THR A 290 ? 0.4442 0.5559 0.5535 -0.0250 -0.0124 0.0095 290 THR A CG2 2290 N N . ASN A 291 ? 0.5361 0.6384 0.6422 -0.0356 -0.0103 0.0108 291 ASN A N 2291 C CA . ASN A 291 ? 0.6100 0.7041 0.7126 -0.0370 -0.0093 0.0119 291 ASN A CA 2292 C C . ASN A 291 ? 0.5738 0.6637 0.6748 -0.0332 -0.0093 0.0124 291 ASN A C 2293 O O . ASN A 291 ? 0.6129 0.6973 0.7113 -0.0333 -0.0084 0.0133 291 ASN A O 2294 C CB . ASN A 291 ? 0.5158 0.6114 0.6183 -0.0401 -0.0074 0.0125 291 ASN A CB 2295 C CG . ASN A 291 ? 0.6691 0.7705 0.7739 -0.0380 -0.0064 0.0124 291 ASN A CG 2296 O OD1 . ASN A 291 ? 0.6639 0.7708 0.7712 -0.0349 -0.0072 0.0116 291 ASN A OD1 2297 N ND2 . ASN A 291 ? 0.7941 0.8940 0.8975 -0.0393 -0.0047 0.0133 291 ASN A ND2 2298 N N . LYS A 292 ? 0.4437 0.5362 0.5458 -0.0298 -0.0102 0.0118 292 LYS A N 2299 C CA . LYS A 292 ? 0.4648 0.5535 0.5650 -0.0265 -0.0101 0.0121 292 LYS A CA 2300 C C . LYS A 292 ? 0.4458 0.5278 0.5432 -0.0259 -0.0110 0.0124 292 LYS A C 2301 O O . LYS A 292 ? 0.4794 0.5600 0.5765 -0.0270 -0.0120 0.0121 292 LYS A O 2302 C CB . LYS A 292 ? 0.4504 0.5433 0.5517 -0.0230 -0.0106 0.0114 292 LYS A CB 2303 C CG . LYS A 292 ? 0.4748 0.5730 0.5779 -0.0226 -0.0091 0.0113 292 LYS A CG 2304 C CD . LYS A 292 ? 0.5036 0.6066 0.6078 -0.0187 -0.0096 0.0105 292 LYS A CD 2305 C CE . LYS A 292 ? 0.5602 0.6707 0.6670 -0.0186 -0.0082 0.0102 292 LYS A CE 2306 N NZ . LYS A 292 ? 0.6718 0.7882 0.7799 -0.0144 -0.0086 0.0093 292 LYS A NZ 2307 N N . THR A 293 ? 0.3873 0.4655 0.4825 -0.0244 -0.0105 0.0128 293 THR A N 2308 C CA . THR A 293 ? 0.3830 0.4557 0.4756 -0.0241 -0.0110 0.0131 293 THR A CA 2309 C C . THR A 293 ? 0.3631 0.4344 0.4545 -0.0220 -0.0121 0.0126 293 THR A C 2310 O O . THR A 293 ? 0.3210 0.3889 0.4108 -0.0222 -0.0128 0.0126 293 THR A O 2311 C CB . THR A 293 ? 0.4302 0.5005 0.5210 -0.0237 -0.0100 0.0138 293 THR A CB 2312 O OG1 . THR A 293 ? 0.5213 0.5933 0.6129 -0.0251 -0.0088 0.0144 293 THR A OG1 2313 C CG2 . THR A 293 ? 0.4384 0.5044 0.5270 -0.0240 -0.0103 0.0142 293 THR A CG2 2314 N N . PHE A 294 ? 0.2757 0.3492 0.3673 -0.0199 -0.0122 0.0121 294 PHE A N 2315 C CA . PHE A 294 ? 0.2948 0.3658 0.3842 -0.0176 -0.0132 0.0116 294 PHE A CA 2316 C C . PHE A 294 ? 0.3060 0.3813 0.3970 -0.0157 -0.0141 0.0110 294 PHE A C 2317 O O . PHE A 294 ? 0.2807 0.3618 0.3748 -0.0159 -0.0138 0.0108 294 PHE A O 2318 C CB . PHE A 294 ? 0.2741 0.3420 0.3605 -0.0161 -0.0125 0.0116 294 PHE A CB 2319 C CG . PHE A 294 ? 0.3074 0.3722 0.3922 -0.0178 -0.0117 0.0122 294 PHE A CG 2320 C CD1 . PHE A 294 ? 0.2662 0.3272 0.3488 -0.0185 -0.0121 0.0123 294 PHE A CD1 2321 C CD2 . PHE A 294 ? 0.3312 0.3975 0.4168 -0.0186 -0.0106 0.0125 294 PHE A CD2 2322 C CE1 . PHE A 294 ? 0.2488 0.3083 0.3302 -0.0199 -0.0115 0.0127 294 PHE A CE1 2323 C CE2 . PHE A 294 ? 0.3290 0.3932 0.4132 -0.0198 -0.0100 0.0130 294 PHE A CE2 2324 C CZ . PHE A 294 ? 0.2908 0.3520 0.3730 -0.0204 -0.0105 0.0131 294 PHE A CZ 2325 N N . GLN A 295 ? 0.2621 0.3349 0.3508 -0.0138 -0.0153 0.0107 295 GLN A N 2326 C CA . GLN A 295 ? 0.2499 0.3265 0.3393 -0.0111 -0.0164 0.0101 295 GLN A CA 2327 C C . GLN A 295 ? 0.3001 0.3710 0.3848 -0.0083 -0.0172 0.0101 295 GLN A C 2328 O O . GLN A 295 ? 0.3031 0.3683 0.3848 -0.0095 -0.0173 0.0104 295 GLN A O 2329 C CB . GLN A 295 ? 0.2347 0.3157 0.3271 -0.0129 -0.0175 0.0099 295 GLN A CB 2330 C CG . GLN A 295 ? 0.2350 0.3113 0.3257 -0.0148 -0.0182 0.0101 295 GLN A CG 2331 C CD . GLN A 295 ? 0.2622 0.3364 0.3503 -0.0127 -0.0198 0.0098 295 GLN A CD 2332 O OE1 . GLN A 295 ? 0.2785 0.3550 0.3661 -0.0095 -0.0205 0.0095 295 GLN A OE1 2333 N NE2 . GLN A 295 ? 0.2171 0.2869 0.3032 -0.0141 -0.0202 0.0099 295 GLN A NE2 2334 N N . ASN A 296 ? 0.2755 0.3481 0.3592 -0.0045 -0.0176 0.0097 296 ASN A N 2335 C CA . ASN A 296 ? 0.2762 0.3424 0.3543 -0.0016 -0.0183 0.0097 296 ASN A CA 2336 C C . ASN A 296 ? 0.3116 0.3809 0.3899 0.0013 -0.0201 0.0094 296 ASN A C 2337 O O . ASN A 296 ? 0.2810 0.3470 0.3550 0.0053 -0.0207 0.0094 296 ASN A O 2338 C CB . ASN A 296 ? 0.2605 0.3231 0.3349 0.0012 -0.0172 0.0096 296 ASN A CB 2339 C CG . ASN A 296 ? 0.3470 0.4167 0.4242 0.0045 -0.0171 0.0091 296 ASN A CG 2340 O OD1 . ASN A 296 ? 0.3532 0.4314 0.4355 0.0043 -0.0178 0.0089 296 ASN A OD1 2341 N ND2 . ASN A 296 ? 0.3597 0.4263 0.4334 0.0073 -0.0161 0.0089 296 ASN A ND2 2342 N N . VAL A 297 ? 0.3167 0.3923 0.3995 -0.0008 -0.0210 0.0092 297 VAL A N 2343 C CA . VAL A 297 ? 0.3169 0.3974 0.4008 0.0014 -0.0228 0.0089 297 VAL A CA 2344 C C . VAL A 297 ? 0.3485 0.4230 0.4284 0.0012 -0.0241 0.0091 297 VAL A C 2345 O O . VAL A 297 ? 0.3610 0.4340 0.4376 0.0049 -0.0254 0.0091 297 VAL A O 2346 C CB . VAL A 297 ? 0.3753 0.4656 0.4656 -0.0013 -0.0232 0.0084 297 VAL A CB 2347 C CG1 . VAL A 297 ? 0.3087 0.4046 0.4000 0.0004 -0.0253 0.0079 297 VAL A CG1 2348 C CG2 . VAL A 297 ? 0.3143 0.4113 0.4082 -0.0008 -0.0219 0.0081 297 VAL A CG2 2349 N N . SER A 298 ? 0.3707 0.4419 0.4508 -0.0028 -0.0237 0.0093 298 SER A N 2350 C CA . SER A 298 ? 0.3524 0.4183 0.4289 -0.0035 -0.0247 0.0095 298 SER A CA 2351 C C . SER A 298 ? 0.3732 0.4350 0.4494 -0.0075 -0.0237 0.0098 298 SER A C 2352 O O . SER A 298 ? 0.3526 0.4174 0.4325 -0.0103 -0.0229 0.0097 298 SER A O 2353 C CB . SER A 298 ? 0.3804 0.4519 0.4589 -0.0031 -0.0266 0.0090 298 SER A CB 2354 O OG . SER A 298 ? 0.3483 0.4148 0.4235 -0.0042 -0.0274 0.0092 298 SER A OG 2355 N N . PRO A 299 ? 0.3546 0.4095 0.4261 -0.0077 -0.0237 0.0101 299 PRO A N 2356 C CA . PRO A 299 ? 0.3279 0.3796 0.3989 -0.0110 -0.0229 0.0102 299 PRO A CA 2357 C C . PRO A 299 ? 0.3658 0.4195 0.4381 -0.0125 -0.0241 0.0098 299 PRO A C 2358 O O . PRO A 299 ? 0.4010 0.4531 0.4735 -0.0150 -0.0235 0.0098 299 PRO A O 2359 C CB . PRO A 299 ? 0.3288 0.3731 0.3939 -0.0105 -0.0225 0.0106 299 PRO A CB 2360 C CG . PRO A 299 ? 0.3307 0.3735 0.3924 -0.0069 -0.0239 0.0106 299 PRO A CG 2361 C CD . PRO A 299 ? 0.3220 0.3712 0.3876 -0.0047 -0.0243 0.0103 299 PRO A CD 2362 N N . LEU A 300 ? 0.3527 0.4097 0.4254 -0.0107 -0.0258 0.0095 300 LEU A N 2363 C CA . LEU A 300 ? 0.3712 0.4301 0.4446 -0.0121 -0.0271 0.0090 300 LEU A CA 2364 C C . LEU A 300 ? 0.3429 0.4090 0.4214 -0.0140 -0.0275 0.0084 300 LEU A C 2365 O O . LEU A 300 ? 0.3387 0.4109 0.4198 -0.0124 -0.0283 0.0081 300 LEU A O 2366 C CB . LEU A 300 ? 0.3571 0.4153 0.4272 -0.0093 -0.0289 0.0089 300 LEU A CB 2367 C CG . LEU A 300 ? 0.4888 0.5405 0.5538 -0.0096 -0.0292 0.0092 300 LEU A CG 2368 C CD1 . LEU A 300 ? 0.4875 0.5334 0.5504 -0.0114 -0.0272 0.0096 300 LEU A CD1 2369 C CD2 . LEU A 300 ? 0.4940 0.5429 0.5542 -0.0058 -0.0305 0.0096 300 LEU A CD2 2370 N N . TRP A 301 ? 0.2724 0.3378 0.3521 -0.0174 -0.0268 0.0081 301 TRP A N 2371 C CA . TRP A 301 ? 0.3371 0.4081 0.4206 -0.0199 -0.0270 0.0075 301 TRP A CA 2372 C C . TRP A 301 ? 0.3566 0.4251 0.4393 -0.0232 -0.0270 0.0070 301 TRP A C 2373 O O . TRP A 301 ? 0.3830 0.4457 0.4625 -0.0234 -0.0266 0.0072 301 TRP A O 2374 C CB . TRP A 301 ? 0.3099 0.3829 0.3963 -0.0206 -0.0254 0.0079 301 TRP A CB 2375 C CG . TRP A 301 ? 0.3513 0.4188 0.4364 -0.0221 -0.0236 0.0085 301 TRP A CG 2376 C CD1 . TRP A 301 ? 0.3319 0.3970 0.4167 -0.0249 -0.0230 0.0084 301 TRP A CD1 2377 C CD2 . TRP A 301 ? 0.2952 0.3591 0.3788 -0.0206 -0.0224 0.0092 301 TRP A CD2 2378 N NE1 . TRP A 301 ? 0.3488 0.4097 0.4324 -0.0248 -0.0215 0.0090 301 TRP A NE1 2379 C CE2 . TRP A 301 ? 0.3713 0.4318 0.4543 -0.0225 -0.0211 0.0095 301 TRP A CE2 2380 C CE3 . TRP A 301 ? 0.2945 0.3573 0.3767 -0.0180 -0.0223 0.0095 301 TRP A CE3 2381 C CZ2 . TRP A 301 ? 0.3745 0.4319 0.4562 -0.0219 -0.0199 0.0101 301 TRP A CZ2 2382 C CZ3 . TRP A 301 ? 0.3749 0.4339 0.4554 -0.0179 -0.0209 0.0101 301 TRP A CZ3 2383 C CH2 . TRP A 301 ? 0.3682 0.4251 0.4488 -0.0199 -0.0198 0.0104 301 TRP A CH2 2384 N N . ILE A 302 ? 0.4304 0.5035 0.5157 -0.0260 -0.0273 0.0064 302 ILE A N 2385 C CA . ILE A 302 ? 0.4134 0.4835 0.4974 -0.0295 -0.0270 0.0058 302 ILE A CA 2386 C C . ILE A 302 ? 0.4183 0.4907 0.5049 -0.0322 -0.0257 0.0059 302 ILE A C 2387 O O . ILE A 302 ? 0.4598 0.5386 0.5498 -0.0318 -0.0257 0.0059 302 ILE A O 2388 C CB . ILE A 302 ? 0.4765 0.5492 0.5597 -0.0310 -0.0290 0.0047 302 ILE A CB 2389 C CG1 . ILE A 302 ? 0.4982 0.5654 0.5784 -0.0342 -0.0287 0.0041 302 ILE A CG1 2390 C CG2 . ILE A 302 ? 0.4430 0.5250 0.5302 -0.0322 -0.0301 0.0041 302 ILE A CG2 2391 C CD1 . ILE A 302 ? 0.6141 0.6735 0.6905 -0.0327 -0.0278 0.0046 302 ILE A CD1 2392 N N . GLY A 303 ? 0.3906 0.4577 0.4751 -0.0347 -0.0245 0.0060 303 GLY A N 2393 C CA . GLY A 303 ? 0.3930 0.4607 0.4788 -0.0373 -0.0231 0.0062 303 GLY A CA 2394 C C . GLY A 303 ? 0.4124 0.4771 0.4982 -0.0355 -0.0214 0.0074 303 GLY A C 2395 O O . GLY A 303 ? 0.4286 0.4899 0.5129 -0.0328 -0.0212 0.0079 303 GLY A O 2396 N N . GLU A 304 ? 0.5664 0.6326 0.6536 -0.0373 -0.0202 0.0077 304 GLU A N 2397 C CA . GLU A 304 ? 0.5901 0.6538 0.6772 -0.0358 -0.0186 0.0088 304 GLU A CA 2398 C C . GLU A 304 ? 0.5571 0.6266 0.6476 -0.0337 -0.0185 0.0092 304 GLU A C 2399 O O . GLU A 304 ? 0.5767 0.6513 0.6697 -0.0351 -0.0181 0.0091 304 GLU A O 2400 C CB . GLU A 304 ? 0.5662 0.6268 0.6518 -0.0387 -0.0172 0.0092 304 GLU A CB 2401 C CG . GLU A 304 ? 0.7302 0.7838 0.8115 -0.0407 -0.0171 0.0089 304 GLU A CG 2402 C CD . GLU A 304 ? 0.9474 0.9952 1.0257 -0.0378 -0.0170 0.0093 304 GLU A CD 2403 O OE1 . GLU A 304 ? 0.9930 1.0369 1.0696 -0.0365 -0.0157 0.0102 304 GLU A OE1 2404 O OE2 . GLU A 304 ? 0.8554 0.9031 0.9332 -0.0367 -0.0181 0.0086 304 GLU A OE2 2405 N N . CYS A 305 ? 0.4524 0.5208 0.5424 -0.0305 -0.0188 0.0095 305 CYS A N 2406 C CA . CYS A 305 ? 0.4376 0.5103 0.5297 -0.0280 -0.0188 0.0096 305 CYS A CA 2407 C C . CYS A 305 ? 0.3664 0.4365 0.4578 -0.0266 -0.0174 0.0105 305 CYS A C 2408 O O . CYS A 305 ? 0.3950 0.4602 0.4842 -0.0269 -0.0167 0.0109 305 CYS A O 2409 C CB . CYS A 305 ? 0.3834 0.4568 0.4748 -0.0253 -0.0203 0.0092 305 CYS A CB 2410 S SG . CYS A 305 ? 0.5696 0.6490 0.6628 -0.0262 -0.0222 0.0082 305 CYS A SG 2411 N N . PRO A 306 ? 0.3701 0.4437 0.4631 -0.0251 -0.0170 0.0106 306 PRO A N 2412 C CA . PRO A 306 ? 0.3462 0.4173 0.4381 -0.0238 -0.0158 0.0112 306 PRO A CA 2413 C C . PRO A 306 ? 0.3411 0.4083 0.4302 -0.0217 -0.0163 0.0112 306 PRO A C 2414 O O . PRO A 306 ? 0.3416 0.4088 0.4299 -0.0204 -0.0175 0.0108 306 PRO A O 2415 C CB . PRO A 306 ? 0.3249 0.4010 0.4190 -0.0227 -0.0153 0.0111 306 PRO A CB 2416 C CG . PRO A 306 ? 0.3757 0.4576 0.4727 -0.0244 -0.0158 0.0105 306 PRO A CG 2417 C CD . PRO A 306 ? 0.2975 0.3782 0.3936 -0.0249 -0.0173 0.0101 306 PRO A CD 2418 N N . LYS A 307 ? 0.3162 0.3803 0.4036 -0.0214 -0.0154 0.0117 307 LYS A N 2419 C CA . LYS A 307 ? 0.3545 0.4147 0.4387 -0.0202 -0.0156 0.0117 307 LYS A CA 2420 C C . LYS A 307 ? 0.3282 0.3885 0.4112 -0.0179 -0.0161 0.0114 307 LYS A C 2421 O O . LYS A 307 ? 0.3146 0.3771 0.3985 -0.0168 -0.0156 0.0113 307 LYS A O 2422 C CB . LYS A 307 ? 0.3616 0.4199 0.4446 -0.0208 -0.0144 0.0123 307 LYS A CB 2423 C CG . LYS A 307 ? 0.3855 0.4406 0.4652 -0.0201 -0.0143 0.0122 307 LYS A CG 2424 C CD . LYS A 307 ? 0.4305 0.4850 0.5094 -0.0212 -0.0133 0.0126 307 LYS A CD 2425 C CE . LYS A 307 ? 0.4838 0.5380 0.5628 -0.0221 -0.0133 0.0128 307 LYS A CE 2426 N NZ . LYS A 307 ? 0.4647 0.5203 0.5446 -0.0226 -0.0125 0.0134 307 LYS A NZ 2427 N N . TYR A 308 ? 0.2790 0.3365 0.3594 -0.0169 -0.0170 0.0112 308 TYR A N 2428 C CA . TYR A 308 ? 0.3077 0.3637 0.3855 -0.0143 -0.0176 0.0109 308 TYR A CA 2429 C C . TYR A 308 ? 0.3055 0.3570 0.3796 -0.0140 -0.0166 0.0111 308 TYR A C 2430 O O . TYR A 308 ? 0.2756 0.3240 0.3478 -0.0158 -0.0160 0.0113 308 TYR A O 2431 C CB . TYR A 308 ? 0.2849 0.3388 0.3604 -0.0133 -0.0189 0.0107 308 TYR A CB 2432 C CG . TYR A 308 ? 0.3051 0.3564 0.3769 -0.0100 -0.0196 0.0106 308 TYR A CG 2433 C CD1 . TYR A 308 ? 0.3192 0.3749 0.3928 -0.0073 -0.0200 0.0104 308 TYR A CD1 2434 C CD2 . TYR A 308 ? 0.3100 0.3546 0.3762 -0.0096 -0.0196 0.0108 308 TYR A CD2 2435 C CE1 . TYR A 308 ? 0.3154 0.3682 0.3850 -0.0036 -0.0206 0.0103 308 TYR A CE1 2436 C CE2 . TYR A 308 ? 0.3126 0.3535 0.3744 -0.0064 -0.0201 0.0108 308 TYR A CE2 2437 C CZ . TYR A 308 ? 0.3628 0.4076 0.4261 -0.0031 -0.0206 0.0105 308 TYR A CZ 2438 O OH . TYR A 308 ? 0.3896 0.4303 0.4479 0.0008 -0.0212 0.0106 308 TYR A OH 2439 N N . VAL A 309 ? 0.3013 0.3525 0.3741 -0.0117 -0.0164 0.0109 309 VAL A N 2440 C CA . VAL A 309 ? 0.2974 0.3442 0.3663 -0.0115 -0.0154 0.0109 309 VAL A CA 2441 C C . VAL A 309 ? 0.3486 0.3928 0.4140 -0.0079 -0.0157 0.0106 309 VAL A C 2442 O O . VAL A 309 ? 0.3676 0.4161 0.4354 -0.0054 -0.0165 0.0104 309 VAL A O 2443 C CB . VAL A 309 ? 0.3008 0.3510 0.3728 -0.0129 -0.0142 0.0110 309 VAL A CB 2444 C CG1 . VAL A 309 ? 0.3081 0.3591 0.3795 -0.0106 -0.0136 0.0107 309 VAL A CG1 2445 C CG2 . VAL A 309 ? 0.2900 0.3373 0.3600 -0.0155 -0.0134 0.0112 309 VAL A CG2 2446 N N . LYS A 310 ? 0.3175 0.3548 0.3769 -0.0076 -0.0151 0.0105 310 LYS A N 2447 C CA . LYS A 310 ? 0.3365 0.3696 0.3911 -0.0037 -0.0154 0.0102 310 LYS A CA 2448 C C . LYS A 310 ? 0.3651 0.4000 0.4200 -0.0014 -0.0145 0.0098 310 LYS A C 2449 O O . LYS A 310 ? 0.4649 0.4975 0.5164 0.0027 -0.0147 0.0095 310 LYS A O 2450 C CB . LYS A 310 ? 0.2894 0.3126 0.3358 -0.0044 -0.0151 0.0102 310 LYS A CB 2451 C CG . LYS A 310 ? 0.4779 0.4995 0.5236 -0.0070 -0.0157 0.0106 310 LYS A CG 2452 C CD . LYS A 310 ? 0.5528 0.5660 0.5908 -0.0054 -0.0163 0.0107 310 LYS A CD 2453 C CE . LYS A 310 ? 0.6024 0.6066 0.6325 -0.0069 -0.0151 0.0106 310 LYS A CE 2454 N NZ . LYS A 310 ? 0.6994 0.6944 0.7212 -0.0060 -0.0154 0.0108 310 LYS A NZ 2455 N N . SER A 311 ? 0.3099 0.3488 0.3686 -0.0037 -0.0135 0.0098 311 SER A N 2456 C CA . SER A 311 ? 0.3988 0.4392 0.4576 -0.0021 -0.0125 0.0094 311 SER A CA 2457 C C . SER A 311 ? 0.3889 0.4361 0.4514 0.0017 -0.0128 0.0092 311 SER A C 2458 O O . SER A 311 ? 0.4582 0.5114 0.5254 0.0018 -0.0138 0.0093 311 SER A O 2459 C CB . SER A 311 ? 0.3939 0.4380 0.4565 -0.0055 -0.0114 0.0097 311 SER A CB 2460 O OG . SER A 311 ? 0.4287 0.4700 0.4902 -0.0091 -0.0115 0.0100 311 SER A OG 2461 N N . GLU A 312 ? 0.4595 0.5059 0.5197 0.0048 -0.0120 0.0087 312 GLU A N 2462 C CA . GLU A 312 ? 0.5320 0.5863 0.5961 0.0084 -0.0120 0.0083 312 GLU A CA 2463 C C . GLU A 312 ? 0.5276 0.5898 0.5979 0.0060 -0.0110 0.0084 312 GLU A C 2464 O O . GLU A 312 ? 0.5038 0.5748 0.5793 0.0070 -0.0111 0.0082 312 GLU A O 2465 C CB . GLU A 312 ? 0.5521 0.6021 0.6105 0.0135 -0.0115 0.0077 312 GLU A CB 2466 C CG . GLU A 312 ? 0.6936 0.7362 0.7455 0.0170 -0.0127 0.0078 312 GLU A CG 2467 C CD . GLU A 312 ? 0.7815 0.8309 0.8372 0.0196 -0.0144 0.0079 312 GLU A CD 2468 O OE1 . GLU A 312 ? 0.7849 0.8453 0.8483 0.0190 -0.0146 0.0078 312 GLU A OE1 2469 O OE2 . GLU A 312 ? 0.9486 0.9922 0.9993 0.0220 -0.0155 0.0081 312 GLU A OE2 2470 N N . SER A 313 ? 0.4698 0.5288 0.5390 0.0027 -0.0099 0.0086 313 SER A N 2471 C CA . SER A 313 ? 0.4697 0.5347 0.5435 0.0004 -0.0088 0.0088 313 SER A CA 2472 C C . SER A 313 ? 0.4143 0.4758 0.4873 -0.0037 -0.0082 0.0093 313 SER A C 2473 O O . SER A 313 ? 0.4814 0.5357 0.5491 -0.0044 -0.0081 0.0091 313 SER A O 2474 C CB . SER A 313 ? 0.4413 0.5081 0.5140 0.0035 -0.0074 0.0081 313 SER A CB 2475 O OG . SER A 313 ? 0.4979 0.5704 0.5747 0.0011 -0.0062 0.0084 313 SER A OG 2476 N N . LEU A 314 ? 0.3144 0.3809 0.3921 -0.0066 -0.0080 0.0098 314 LEU A N 2477 C CA . LEU A 314 ? 0.3392 0.4038 0.4166 -0.0100 -0.0075 0.0104 314 LEU A CA 2478 C C . LEU A 314 ? 0.3466 0.4163 0.4271 -0.0111 -0.0063 0.0107 314 LEU A C 2479 O O . LEU A 314 ? 0.3467 0.4200 0.4309 -0.0133 -0.0063 0.0114 314 LEU A O 2480 C CB . LEU A 314 ? 0.3271 0.3911 0.4060 -0.0124 -0.0085 0.0110 314 LEU A CB 2481 C CG . LEU A 314 ? 0.3718 0.4302 0.4469 -0.0119 -0.0095 0.0107 314 LEU A CG 2482 C CD1 . LEU A 314 ? 0.2686 0.3274 0.3456 -0.0136 -0.0105 0.0112 314 LEU A CD1 2483 C CD2 . LEU A 314 ? 0.2802 0.3330 0.3505 -0.0131 -0.0089 0.0106 314 LEU A CD2 2484 N N . ARG A 315 ? 0.3234 0.3930 0.4020 -0.0095 -0.0052 0.0102 315 ARG A N 2485 C CA . ARG A 315 ? 0.3087 0.3832 0.3897 -0.0101 -0.0039 0.0104 315 ARG A CA 2486 C C . ARG A 315 ? 0.3119 0.3839 0.3910 -0.0125 -0.0032 0.0110 315 ARG A C 2487 O O . ARG A 315 ? 0.2489 0.3162 0.3236 -0.0122 -0.0029 0.0105 315 ARG A O 2488 C CB . ARG A 315 ? 0.3627 0.4393 0.4427 -0.0066 -0.0029 0.0096 315 ARG A CB 2489 C CG . ARG A 315 ? 0.3022 0.3842 0.3845 -0.0072 -0.0013 0.0097 315 ARG A CG 2490 C CD . ARG A 315 ? 0.3133 0.4019 0.3980 -0.0041 -0.0007 0.0090 315 ARG A CD 2491 N NE . ARG A 315 ? 0.4363 0.5329 0.5261 -0.0064 0.0000 0.0094 315 ARG A NE 2492 C CZ . ARG A 315 ? 0.4528 0.5566 0.5470 -0.0060 -0.0004 0.0092 315 ARG A CZ 2493 N NH1 . ARG A 315 ? 0.3460 0.4502 0.4400 -0.0028 -0.0016 0.0086 315 ARG A NH1 2494 N NH2 . ARG A 315 ? 0.5770 0.6875 0.6752 -0.0089 0.0005 0.0096 315 ARG A NH2 2495 N N . LEU A 316 ? 0.3139 0.3888 0.3959 -0.0150 -0.0029 0.0119 316 LEU A N 2496 C CA . LEU A 316 ? 0.2943 0.3675 0.3748 -0.0171 -0.0025 0.0126 316 LEU A CA 2497 C C . LEU A 316 ? 0.3390 0.4153 0.4198 -0.0172 -0.0010 0.0128 316 LEU A C 2498 O O . LEU A 316 ? 0.3327 0.4135 0.4165 -0.0176 -0.0003 0.0130 316 LEU A O 2499 C CB . LEU A 316 ? 0.3461 0.4197 0.4287 -0.0193 -0.0032 0.0137 316 LEU A CB 2500 C CG . LEU A 316 ? 0.3725 0.4433 0.4533 -0.0207 -0.0036 0.0143 316 LEU A CG 2501 C CD1 . LEU A 316 ? 0.3281 0.3953 0.4057 -0.0203 -0.0043 0.0136 316 LEU A CD1 2502 C CD2 . LEU A 316 ? 0.3090 0.3796 0.3916 -0.0218 -0.0044 0.0151 316 LEU A CD2 2503 N N . ALA A 317 ? 0.2879 0.3617 0.3651 -0.0171 -0.0004 0.0125 317 ALA A N 2504 C CA . ALA A 317 ? 0.2835 0.3597 0.3603 -0.0174 0.0011 0.0128 317 ALA A CA 2505 C C . ALA A 317 ? 0.2747 0.3524 0.3531 -0.0198 0.0013 0.0142 317 ALA A C 2506 O O . ALA A 317 ? 0.2229 0.2983 0.3007 -0.0210 0.0003 0.0149 317 ALA A O 2507 C CB . ALA A 317 ? 0.3001 0.3727 0.3722 -0.0169 0.0015 0.0121 317 ALA A CB 2508 N N . THR A 318 ? 0.2960 0.3774 0.3758 -0.0204 0.0027 0.0146 318 THR A N 2509 C CA . THR A 318 ? 0.3121 0.3938 0.3921 -0.0227 0.0031 0.0161 318 THR A CA 2510 C C . THR A 318 ? 0.3302 0.4129 0.4080 -0.0228 0.0047 0.0163 318 THR A C 2511 O O . THR A 318 ? 0.3504 0.4311 0.4257 -0.0237 0.0047 0.0172 318 THR A O 2512 C CB . THR A 318 ? 0.3246 0.4090 0.4079 -0.0243 0.0034 0.0166 318 THR A CB 2513 O OG1 . THR A 318 ? 0.3800 0.4697 0.4657 -0.0237 0.0045 0.0158 318 THR A OG1 2514 C CG2 . THR A 318 ? 0.2612 0.3440 0.3460 -0.0242 0.0018 0.0164 318 THR A CG2 2515 N N . GLY A 319 ? 0.2989 0.3853 0.3777 -0.0217 0.0060 0.0154 319 GLY A N 2516 C CA . GLY A 319 ? 0.2825 0.3700 0.3590 -0.0215 0.0076 0.0153 319 GLY A CA 2517 C C . GLY A 319 ? 0.3126 0.3964 0.3850 -0.0199 0.0073 0.0144 319 GLY A C 2518 O O . GLY A 319 ? 0.2737 0.3539 0.3448 -0.0195 0.0058 0.0140 319 GLY A O 2519 N N . LEU A 320 ? 0.3870 0.4717 0.4570 -0.0193 0.0087 0.0140 320 LEU A N 2520 C CA . LEU A 320 ? 0.3880 0.4688 0.4532 -0.0183 0.0086 0.0130 320 LEU A CA 2521 C C . LEU A 320 ? 0.3794 0.4598 0.4433 -0.0153 0.0093 0.0112 320 LEU A C 2522 O O . LEU A 320 ? 0.4084 0.4928 0.4755 -0.0137 0.0099 0.0108 320 LEU A O 2523 C CB . LEU A 320 ? 0.4017 0.4825 0.4639 -0.0195 0.0096 0.0136 320 LEU A CB 2524 C CG . LEU A 320 ? 0.4108 0.4962 0.4744 -0.0200 0.0117 0.0143 320 LEU A CG 2525 C CD1 . LEU A 320 ? 0.4477 0.5326 0.5071 -0.0197 0.0130 0.0139 320 LEU A CD1 2526 C CD2 . LEU A 320 ? 0.4176 0.5037 0.4829 -0.0226 0.0114 0.0162 320 LEU A CD2 2527 N N . ARG A 321 ? 0.2807 0.3563 0.3395 -0.0145 0.0091 0.0101 321 ARG A N 2528 C CA . ARG A 321 ? 0.2920 0.3654 0.3477 -0.0114 0.0099 0.0084 321 ARG A CA 2529 C C . ARG A 321 ? 0.3392 0.4178 0.3961 -0.0095 0.0121 0.0081 321 ARG A C 2530 O O . ARG A 321 ? 0.3377 0.4181 0.3936 -0.0109 0.0133 0.0086 321 ARG A O 2531 C CB . ARG A 321 ? 0.2821 0.3488 0.3311 -0.0118 0.0096 0.0074 321 ARG A CB 2532 C CG . ARG A 321 ? 0.3616 0.4236 0.4056 -0.0086 0.0104 0.0055 321 ARG A CG 2533 C CD . ARG A 321 ? 0.4060 0.4612 0.4427 -0.0100 0.0103 0.0045 321 ARG A CD 2534 N NE . ARG A 321 ? 0.4210 0.4723 0.4562 -0.0129 0.0084 0.0047 321 ARG A NE 2535 C CZ . ARG A 321 ? 0.4067 0.4517 0.4383 -0.0125 0.0076 0.0038 321 ARG A CZ 2536 N NH1 . ARG A 321 ? 0.3482 0.3896 0.3770 -0.0088 0.0084 0.0026 321 ARG A NH1 2537 N NH2 . ARG A 321 ? 0.3896 0.4322 0.4203 -0.0156 0.0060 0.0040 321 ARG A NH2 2538 N N . ASN A 322 ? 0.3613 0.4430 0.4203 -0.0064 0.0127 0.0072 322 ASN A N 2539 C CA . ASN A 322 ? 0.4040 0.4923 0.4650 -0.0045 0.0148 0.0069 322 ASN A CA 2540 C C . ASN A 322 ? 0.4548 0.5397 0.5098 -0.0014 0.0162 0.0053 322 ASN A C 2541 O O . ASN A 322 ? 0.5001 0.5807 0.5518 0.0021 0.0159 0.0040 322 ASN A O 2542 C CB . ASN A 322 ? 0.3773 0.4717 0.4434 -0.0023 0.0147 0.0066 322 ASN A CB 2543 C CG . ASN A 322 ? 0.4466 0.5505 0.5165 -0.0016 0.0168 0.0066 322 ASN A CG 2544 O OD1 . ASN A 322 ? 0.4249 0.5316 0.4953 -0.0045 0.0181 0.0074 322 ASN A OD1 2545 N ND2 . ASN A 322 ? 0.4473 0.5566 0.5197 0.0021 0.0172 0.0056 322 ASN A ND2 2546 N N . VAL A 323 ? 0.3530 0.4393 0.4061 -0.0026 0.0178 0.0054 323 VAL A N 2547 C CA . VAL A 323 ? 0.4358 0.5187 0.4828 0.0000 0.0193 0.0039 323 VAL A CA 2548 C C . VAL A 323 ? 0.4477 0.5384 0.4966 0.0010 0.0219 0.0038 323 VAL A C 2549 O O . VAL A 323 ? 0.4220 0.5127 0.4687 -0.0012 0.0230 0.0043 323 VAL A O 2550 C CB . VAL A 323 ? 0.4554 0.5311 0.4964 -0.0027 0.0187 0.0039 323 VAL A CB 2551 C CG1 . VAL A 323 ? 0.4134 0.4830 0.4467 0.0001 0.0198 0.0020 323 VAL A CG1 2552 C CG2 . VAL A 323 ? 0.3672 0.4376 0.4078 -0.0051 0.0162 0.0044 323 VAL A CG2 2553 N N . PRO A 324 ? 0.5646 0.6625 0.6177 0.0041 0.0229 0.0033 324 PRO A N 2554 C CA . PRO A 324 ? 0.6394 0.7461 0.6949 0.0048 0.0255 0.0032 324 PRO A CA 2555 C C . PRO A 324 ? 0.6192 0.7229 0.6682 0.0084 0.0274 0.0015 324 PRO A C 2556 O O . PRO A 324 ? 0.5880 0.6841 0.6316 0.0118 0.0268 0.0001 324 PRO A O 2557 C CB . PRO A 324 ? 0.6220 0.7376 0.6837 0.0074 0.0257 0.0029 324 PRO A CB 2558 C CG . PRO A 324 ? 0.4906 0.6021 0.5539 0.0072 0.0230 0.0032 324 PRO A CG 2559 C CD . PRO A 324 ? 0.5201 0.6195 0.5763 0.0070 0.0217 0.0029 324 PRO A CD 2560 N N . GLN A 325 ? 0.7056 0.8146 0.7546 0.0076 0.0298 0.0016 325 GLN A N 2561 C CA . GLN A 325 ? 0.8262 0.9330 0.8691 0.0111 0.0319 0.0000 325 GLN A CA 2562 C C . GLN A 325 ? 0.8022 0.9201 0.8483 0.0122 0.0349 -0.0003 325 GLN A C 2563 O O . GLN A 325 ? 0.8480 0.9732 0.8976 0.0162 0.0358 -0.0012 325 GLN A O 2564 C CB . GLN A 325 ? 0.7695 0.8676 0.8056 0.0081 0.0316 0.0001 325 GLN A CB 2565 C CG . GLN A 325 ? 0.7838 0.8833 0.8225 0.0022 0.0307 0.0023 325 GLN A CG 2566 C CD . GLN A 325 ? 0.7929 0.8851 0.8249 -0.0003 0.0303 0.0025 325 GLN A CD 2567 O OE1 . GLN A 325 ? 0.7751 0.8602 0.8003 0.0017 0.0304 0.0008 325 GLN A OE1 2568 N NE2 . GLN A 325 ? 0.6304 0.7240 0.6640 -0.0048 0.0299 0.0044 325 GLN A NE2 2569 N N . GLY B 1 ? 0.7803 0.8215 0.7964 -0.0269 0.0051 0.0028 330 GLY B N 2570 C CA . GLY B 1 ? 0.7123 0.7603 0.7342 -0.0285 0.0038 0.0046 330 GLY B CA 2571 C C . GLY B 1 ? 0.6757 0.7254 0.6949 -0.0321 0.0025 0.0044 330 GLY B C 2572 O O . GLY B 1 ? 0.6374 0.6855 0.6513 -0.0333 0.0029 0.0034 330 GLY B O 2573 N N . ILE B 2 ? 0.5173 0.5710 0.5401 -0.0338 0.0009 0.0054 331 ILE B N 2574 C CA . ILE B 2 ? 0.4683 0.5253 0.4892 -0.0372 -0.0006 0.0053 331 ILE B CA 2575 C C . ILE B 2 ? 0.3893 0.4518 0.4110 -0.0369 -0.0008 0.0065 331 ILE B C 2576 O O . ILE B 2 ? 0.4175 0.4830 0.4368 -0.0394 -0.0019 0.0062 331 ILE B O 2577 C CB . ILE B 2 ? 0.3925 0.4529 0.4171 -0.0387 -0.0021 0.0059 331 ILE B CB 2578 C CG1 . ILE B 2 ? 0.3907 0.4563 0.4222 -0.0363 -0.0025 0.0081 331 ILE B CG1 2579 C CG2 . ILE B 2 ? 0.3805 0.4348 0.4033 -0.0393 -0.0019 0.0047 331 ILE B CG2 2580 C CD1 . ILE B 2 ? 0.4544 0.5233 0.4894 -0.0373 -0.0039 0.0087 331 ILE B CD1 2581 N N . PHE B 3 ? 0.3771 0.4411 0.4020 -0.0340 0.0003 0.0079 332 PHE B N 2582 C CA . PHE B 3 ? 0.4100 0.4779 0.4344 -0.0337 0.0003 0.0091 332 PHE B CA 2583 C C . PHE B 3 ? 0.3668 0.4317 0.3867 -0.0331 0.0020 0.0081 332 PHE B C 2584 O O . PHE B 3 ? 0.5350 0.6022 0.5530 -0.0332 0.0022 0.0087 332 PHE B O 2585 C CB . PHE B 3 ? 0.3883 0.4601 0.4183 -0.0316 0.0003 0.0115 332 PHE B CB 2586 C CG . PHE B 3 ? 0.3681 0.4433 0.4018 -0.0320 -0.0014 0.0125 332 PHE B CG 2587 C CD1 . PHE B 3 ? 0.3369 0.4107 0.3742 -0.0315 -0.0015 0.0124 332 PHE B CD1 2588 C CD2 . PHE B 3 ? 0.3161 0.3961 0.3494 -0.0327 -0.0030 0.0134 332 PHE B CD2 2589 C CE1 . PHE B 3 ? 0.3328 0.4097 0.3732 -0.0317 -0.0030 0.0132 332 PHE B CE1 2590 C CE2 . PHE B 3 ? 0.3414 0.4249 0.3779 -0.0326 -0.0045 0.0142 332 PHE B CE2 2591 C CZ . PHE B 3 ? 0.3431 0.4250 0.3832 -0.0322 -0.0044 0.0141 332 PHE B CZ 2592 N N . GLY B 4 ? 0.3511 0.4106 0.3689 -0.0321 0.0034 0.0066 333 GLY B N 2593 C CA . GLY B 4 ? 0.3164 0.3720 0.3286 -0.0316 0.0049 0.0051 333 GLY B CA 2594 C C . GLY B 4 ? 0.3444 0.4019 0.3582 -0.0289 0.0068 0.0060 333 GLY B C 2595 O O . GLY B 4 ? 0.3791 0.4341 0.3882 -0.0282 0.0083 0.0048 333 GLY B O 2596 N N . ALA B 5 ? 0.2973 0.3591 0.3173 -0.0277 0.0069 0.0080 334 ALA B N 2597 C CA . ALA B 5 ? 0.2950 0.3592 0.3167 -0.0258 0.0088 0.0090 334 ALA B CA 2598 C C . ALA B 5 ? 0.3484 0.4117 0.3725 -0.0232 0.0105 0.0082 334 ALA B C 2599 O O . ALA B 5 ? 0.3211 0.3828 0.3422 -0.0216 0.0123 0.0070 334 ALA B O 2600 C CB . ALA B 5 ? 0.2865 0.3553 0.3126 -0.0261 0.0082 0.0115 334 ALA B CB 2601 N N . ILE B 6 ? 0.3123 0.3768 0.3417 -0.0226 0.0099 0.0089 335 ILE B N 2602 C CA . ILE B 6 ? 0.3181 0.3830 0.3503 -0.0200 0.0112 0.0084 335 ILE B CA 2603 C C . ILE B 6 ? 0.3688 0.4282 0.3964 -0.0184 0.0117 0.0061 335 ILE B C 2604 O O . ILE B 6 ? 0.3295 0.3844 0.3542 -0.0196 0.0103 0.0052 335 ILE B O 2605 C CB . ILE B 6 ? 0.3603 0.4274 0.3987 -0.0199 0.0102 0.0095 335 ILE B CB 2606 C CG1 . ILE B 6 ? 0.3746 0.4462 0.4167 -0.0212 0.0102 0.0117 335 ILE B CG1 2607 C CG2 . ILE B 6 ? 0.2893 0.3570 0.3302 -0.0172 0.0112 0.0087 335 ILE B CG2 2608 C CD1 . ILE B 6 ? 0.3178 0.3915 0.3656 -0.0212 0.0095 0.0128 335 ILE B CD1 2609 N N . ALA B 7 ? 0.4175 0.4771 0.4439 -0.0156 0.0137 0.0052 336 ALA B N 2610 C CA . ALA B 7 ? 0.4630 0.5164 0.4835 -0.0133 0.0144 0.0030 336 ALA B CA 2611 C C . ALA B 7 ? 0.4544 0.5018 0.4675 -0.0159 0.0136 0.0018 336 ALA B C 2612 O O . ALA B 7 ? 0.4145 0.4549 0.4225 -0.0159 0.0131 0.0003 336 ALA B O 2613 C CB . ALA B 7 ? 0.3090 0.3599 0.3311 -0.0114 0.0137 0.0024 336 ALA B CB 2614 N N . GLY B 8 ? 0.4152 0.4653 0.4274 -0.0182 0.0135 0.0026 337 GLY B N 2615 C CA . GLY B 8 ? 0.3377 0.3839 0.3434 -0.0211 0.0127 0.0016 337 GLY B CA 2616 C C . GLY B 8 ? 0.4047 0.4523 0.4070 -0.0209 0.0142 0.0015 337 GLY B C 2617 O O . GLY B 8 ? 0.3906 0.4364 0.3902 -0.0181 0.0163 0.0003 337 GLY B O 2618 N N . PHE B 9 ? 0.3325 0.3835 0.3348 -0.0235 0.0133 0.0027 338 PHE B N 2619 C CA . PHE B 9 ? 0.3611 0.4133 0.3598 -0.0234 0.0147 0.0026 338 PHE B CA 2620 C C . PHE B 9 ? 0.4070 0.4645 0.4106 -0.0211 0.0167 0.0041 338 PHE B C 2621 O O . PHE B 9 ? 0.4395 0.4979 0.4403 -0.0202 0.0186 0.0038 338 PHE B O 2622 C CB . PHE B 9 ? 0.3607 0.4148 0.3569 -0.0266 0.0130 0.0034 338 PHE B CB 2623 C CG . PHE B 9 ? 0.4179 0.4780 0.4200 -0.0273 0.0118 0.0061 338 PHE B CG 2624 C CD1 . PHE B 9 ? 0.3717 0.4355 0.3751 -0.0266 0.0131 0.0078 338 PHE B CD1 2625 C CD2 . PHE B 9 ? 0.3820 0.4435 0.3875 -0.0288 0.0096 0.0068 338 PHE B CD2 2626 C CE1 . PHE B 9 ? 0.3543 0.4223 0.3620 -0.0271 0.0120 0.0103 338 PHE B CE1 2627 C CE2 . PHE B 9 ? 0.3674 0.4336 0.3775 -0.0289 0.0086 0.0093 338 PHE B CE2 2628 C CZ . PHE B 9 ? 0.3631 0.4320 0.3741 -0.0280 0.0098 0.0110 338 PHE B CZ 2629 N N . ILE B 10 ? 0.3617 0.4228 0.3723 -0.0205 0.0163 0.0055 339 ILE B N 2630 C CA . ILE B 10 ? 0.3732 0.4390 0.3884 -0.0185 0.0183 0.0064 339 ILE B CA 2631 C C . ILE B 10 ? 0.3847 0.4492 0.4017 -0.0156 0.0190 0.0050 339 ILE B C 2632 O O . ILE B 10 ? 0.3930 0.4582 0.4147 -0.0155 0.0177 0.0056 339 ILE B O 2633 C CB . ILE B 10 ? 0.3588 0.4295 0.3800 -0.0199 0.0177 0.0090 339 ILE B CB 2634 C CG1 . ILE B 10 ? 0.3576 0.4287 0.3760 -0.0223 0.0167 0.0104 339 ILE B CG1 2635 C CG2 . ILE B 10 ? 0.3138 0.3894 0.3387 -0.0187 0.0201 0.0097 339 ILE B CG2 2636 C CD1 . ILE B 10 ? 0.3540 0.4282 0.3767 -0.0235 0.0158 0.0130 339 ILE B CD1 2637 N N . GLU B 11 ? 0.5211 0.5837 0.5343 -0.0128 0.0209 0.0032 340 GLU B N 2638 C CA . GLU B 11 ? 0.4913 0.5505 0.5035 -0.0095 0.0213 0.0015 340 GLU B CA 2639 C C . GLU B 11 ? 0.4568 0.5212 0.4763 -0.0073 0.0216 0.0022 340 GLU B C 2640 O O . GLU B 11 ? 0.5212 0.5824 0.5410 -0.0055 0.0207 0.0014 340 GLU B O 2641 C CB . GLU B 11 ? 0.6286 0.6849 0.6346 -0.0064 0.0236 -0.0005 340 GLU B CB 2642 C CG . GLU B 11 ? 0.8087 0.8578 0.8059 -0.0083 0.0232 -0.0019 340 GLU B CG 2643 C CD . GLU B 11 ? 1.0461 1.0935 1.0372 -0.0057 0.0258 -0.0035 340 GLU B CD 2644 O OE1 . GLU B 11 ? 0.9819 1.0302 0.9700 -0.0077 0.0263 -0.0033 340 GLU B OE1 2645 O OE2 . GLU B 11 ? 0.9896 1.0347 0.9788 -0.0013 0.0273 -0.0051 340 GLU B OE2 2646 N N . GLY B 12 ? 0.3539 0.4260 0.3788 -0.0077 0.0228 0.0036 341 GLY B N 2647 C CA . GLY B 12 ? 0.2943 0.3722 0.3261 -0.0061 0.0231 0.0041 341 GLY B CA 2648 C C . GLY B 12 ? 0.3321 0.4162 0.3699 -0.0091 0.0230 0.0064 341 GLY B C 2649 O O . GLY B 12 ? 0.2449 0.3290 0.2814 -0.0120 0.0229 0.0076 341 GLY B O 2650 N N . GLY B 13 ? 0.2993 0.3884 0.3433 -0.0085 0.0229 0.0068 342 GLY B N 2651 C CA . GLY B 13 ? 0.2831 0.3777 0.3323 -0.0114 0.0230 0.0088 342 GLY B CA 2652 C C . GLY B 13 ? 0.3403 0.4423 0.3913 -0.0112 0.0258 0.0088 342 GLY B C 2653 O O . GLY B 13 ? 0.3296 0.4328 0.3780 -0.0084 0.0277 0.0074 342 GLY B O 2654 N N . TRP B 14 ? 0.3480 0.4547 0.4032 -0.0143 0.0263 0.0105 343 TRP B N 2655 C CA . TRP B 14 ? 0.3378 0.4521 0.3950 -0.0153 0.0290 0.0109 343 TRP B CA 2656 C C . TRP B 14 ? 0.3861 0.5078 0.4501 -0.0160 0.0292 0.0111 343 TRP B C 2657 O O . TRP B 14 ? 0.3837 0.5050 0.4503 -0.0193 0.0281 0.0126 343 TRP B O 2658 C CB . TRP B 14 ? 0.3204 0.4331 0.3752 -0.0194 0.0296 0.0129 343 TRP B CB 2659 C CG . TRP B 14 ? 0.3465 0.4539 0.3948 -0.0191 0.0297 0.0128 343 TRP B CG 2660 C CD1 . TRP B 14 ? 0.3186 0.4241 0.3628 -0.0160 0.0304 0.0109 343 TRP B CD1 2661 C CD2 . TRP B 14 ? 0.3527 0.4559 0.3972 -0.0219 0.0291 0.0146 343 TRP B CD2 2662 N NE1 . TRP B 14 ? 0.3547 0.4554 0.3931 -0.0172 0.0302 0.0114 343 TRP B NE1 2663 C CE2 . TRP B 14 ? 0.3083 0.4078 0.3469 -0.0206 0.0294 0.0137 343 TRP B CE2 2664 C CE3 . TRP B 14 ? 0.3265 0.4282 0.3715 -0.0252 0.0283 0.0169 343 TRP B CE3 2665 C CZ2 . TRP B 14 ? 0.3225 0.4179 0.3561 -0.0225 0.0287 0.0150 343 TRP B CZ2 2666 C CZ3 . TRP B 14 ? 0.3167 0.4139 0.3566 -0.0267 0.0278 0.0183 343 TRP B CZ3 2667 C CH2 . TRP B 14 ? 0.3319 0.4264 0.3664 -0.0253 0.0279 0.0174 343 TRP B CH2 2668 N N . THR B 15 ? 0.3787 0.5072 0.4454 -0.0128 0.0306 0.0095 344 THR B N 2669 C CA . THR B 15 ? 0.4456 0.5831 0.5190 -0.0137 0.0310 0.0096 344 THR B CA 2670 C C . THR B 15 ? 0.4547 0.5976 0.5297 -0.0186 0.0329 0.0110 344 THR B C 2671 O O . THR B 15 ? 0.4068 0.5548 0.4864 -0.0216 0.0328 0.0117 344 THR B O 2672 C CB . THR B 15 ? 0.4443 0.5892 0.5200 -0.0087 0.0321 0.0075 344 THR B CB 2673 O OG1 . THR B 15 ? 0.4567 0.6040 0.5291 -0.0068 0.0347 0.0067 344 THR B OG1 2674 C CG2 . THR B 15 ? 0.3705 0.5094 0.4446 -0.0041 0.0300 0.0063 344 THR B CG2 2675 N N . GLY B 16 ? 0.4288 0.5699 0.4993 -0.0198 0.0347 0.0115 345 GLY B N 2676 C CA . GLY B 16 ? 0.3913 0.5360 0.4617 -0.0246 0.0369 0.0130 345 GLY B CA 2677 C C . GLY B 16 ? 0.4216 0.5599 0.4906 -0.0292 0.0355 0.0153 345 GLY B C 2678 O O . GLY B 16 ? 0.4749 0.6156 0.5439 -0.0337 0.0371 0.0166 345 GLY B O 2679 N N . MET B 17 ? 0.3941 0.5238 0.4611 -0.0283 0.0327 0.0157 346 MET B N 2680 C CA . MET B 17 ? 0.4225 0.5461 0.4881 -0.0319 0.0313 0.0178 346 MET B CA 2681 C C . MET B 17 ? 0.4288 0.5534 0.4993 -0.0325 0.0295 0.0177 346 MET B C 2682 O O . MET B 17 ? 0.4226 0.5435 0.4939 -0.0300 0.0271 0.0171 346 MET B O 2683 C CB . MET B 17 ? 0.3402 0.4547 0.4007 -0.0308 0.0294 0.0185 346 MET B CB 2684 C CG . MET B 17 ? 0.3974 0.5059 0.4554 -0.0339 0.0283 0.0207 346 MET B CG 2685 S SD . MET B 17 ? 0.5247 0.6246 0.5769 -0.0323 0.0261 0.0214 346 MET B SD 2686 C CE . MET B 17 ? 0.3200 0.4185 0.3753 -0.0291 0.0233 0.0197 346 MET B CE 2687 N N . ILE B 18 ? 0.4808 0.6105 0.5543 -0.0362 0.0306 0.0183 347 ILE B N 2688 C CA . ILE B 18 ? 0.5409 0.6736 0.6196 -0.0369 0.0292 0.0179 347 ILE B CA 2689 C C . ILE B 18 ? 0.5309 0.6567 0.6082 -0.0405 0.0278 0.0196 347 ILE B C 2690 O O . ILE B 18 ? 0.6048 0.7310 0.6855 -0.0408 0.0261 0.0193 347 ILE B O 2691 C CB . ILE B 18 ? 0.5470 0.6912 0.6305 -0.0387 0.0313 0.0170 347 ILE B CB 2692 C CG1 . ILE B 18 ? 0.5736 0.7188 0.6551 -0.0445 0.0336 0.0185 347 ILE B CG1 2693 C CG2 . ILE B 18 ? 0.5120 0.6634 0.5968 -0.0343 0.0328 0.0151 347 ILE B CG2 2694 C CD1 . ILE B 18 ? 0.5720 0.7298 0.6581 -0.0468 0.0361 0.0175 347 ILE B CD1 2695 N N . ASP B 19 ? 0.6245 0.7438 0.6965 -0.0428 0.0283 0.0215 348 ASP B N 2696 C CA . ASP B 19 ? 0.7153 0.8277 0.7850 -0.0462 0.0274 0.0233 348 ASP B CA 2697 C C . ASP B 19 ? 0.7110 0.8144 0.7776 -0.0438 0.0247 0.0241 348 ASP B C 2698 O O . ASP B 19 ? 0.6863 0.7830 0.7497 -0.0458 0.0240 0.0257 348 ASP B O 2699 C CB . ASP B 19 ? 0.7031 0.8137 0.7683 -0.0506 0.0297 0.0250 348 ASP B CB 2700 C CG . ASP B 19 ? 0.8670 0.9750 0.9271 -0.0492 0.0308 0.0257 348 ASP B CG 2701 O OD1 . ASP B 19 ? 0.8082 0.9201 0.8697 -0.0456 0.0309 0.0242 348 ASP B OD1 2702 O OD2 . ASP B 19 ? 0.8512 0.9531 0.9055 -0.0516 0.0316 0.0276 348 ASP B OD2 2703 N N . GLY B 20 ? 0.4758 0.5791 0.5432 -0.0397 0.0233 0.0229 349 GLY B N 2704 C CA . GLY B 20 ? 0.4043 0.5006 0.4695 -0.0376 0.0208 0.0234 349 GLY B CA 2705 C C . GLY B 20 ? 0.3969 0.4935 0.4626 -0.0337 0.0196 0.0218 349 GLY B C 2706 O O . GLY B 20 ? 0.4487 0.5501 0.5159 -0.0320 0.0207 0.0203 349 GLY B O 2707 N N . TRP B 21 ? 0.3727 0.4640 0.4367 -0.0323 0.0173 0.0221 350 TRP B N 2708 C CA . TRP B 21 ? 0.3449 0.4354 0.4087 -0.0293 0.0160 0.0206 350 TRP B CA 2709 C C . TRP B 21 ? 0.3315 0.4203 0.3905 -0.0284 0.0165 0.0206 350 TRP B C 2710 O O . TRP B 21 ? 0.3405 0.4304 0.3988 -0.0265 0.0168 0.0190 350 TRP B O 2711 C CB . TRP B 21 ? 0.2879 0.3744 0.3522 -0.0286 0.0135 0.0209 350 TRP B CB 2712 C CG . TRP B 21 ? 0.3058 0.3941 0.3746 -0.0283 0.0127 0.0201 350 TRP B CG 2713 C CD1 . TRP B 21 ? 0.3361 0.4294 0.4085 -0.0276 0.0135 0.0187 350 TRP B CD1 2714 C CD2 . TRP B 21 ? 0.2871 0.3725 0.3572 -0.0285 0.0108 0.0205 350 TRP B CD2 2715 N NE1 . TRP B 21 ? 0.2959 0.3895 0.3717 -0.0275 0.0122 0.0184 350 TRP B NE1 2716 C CE2 . TRP B 21 ? 0.2964 0.3850 0.3708 -0.0282 0.0105 0.0194 350 TRP B CE2 2717 C CE3 . TRP B 21 ? 0.2891 0.3700 0.3571 -0.0287 0.0093 0.0217 350 TRP B CE3 2718 C CZ2 . TRP B 21 ? 0.2324 0.3192 0.3087 -0.0283 0.0089 0.0195 350 TRP B CZ2 2719 C CZ3 . TRP B 21 ? 0.2738 0.3532 0.3439 -0.0287 0.0078 0.0217 350 TRP B CZ3 2720 C CH2 . TRP B 21 ? 0.2965 0.3786 0.3707 -0.0286 0.0076 0.0206 350 TRP B CH2 2721 N N . TYR B 22 ? 0.3097 0.3953 0.3650 -0.0297 0.0164 0.0224 351 TYR B N 2722 C CA . TYR B 22 ? 0.3391 0.4232 0.3896 -0.0291 0.0167 0.0225 351 TYR B CA 2723 C C . TYR B 22 ? 0.3723 0.4568 0.4199 -0.0310 0.0188 0.0240 351 TYR B C 2724 O O . TYR B 22 ? 0.3982 0.4815 0.4459 -0.0331 0.0193 0.0256 351 TYR B O 2725 C CB . TYR B 22 ? 0.3259 0.4059 0.3736 -0.0284 0.0143 0.0234 351 TYR B CB 2726 C CG . TYR B 22 ? 0.3097 0.3887 0.3605 -0.0276 0.0122 0.0228 351 TYR B CG 2727 C CD1 . TYR B 22 ? 0.2958 0.3757 0.3485 -0.0263 0.0115 0.0208 351 TYR B CD1 2728 C CD2 . TYR B 22 ? 0.3085 0.3851 0.3597 -0.0281 0.0110 0.0243 351 TYR B CD2 2729 C CE1 . TYR B 22 ? 0.2651 0.3439 0.3202 -0.0258 0.0097 0.0204 351 TYR B CE1 2730 C CE2 . TYR B 22 ? 0.3154 0.3914 0.3693 -0.0273 0.0091 0.0238 351 TYR B CE2 2731 C CZ . TYR B 22 ? 0.3335 0.4108 0.3895 -0.0263 0.0085 0.0218 351 TYR B CZ 2732 O OH . TYR B 22 ? 0.3069 0.3834 0.3652 -0.0258 0.0068 0.0213 351 TYR B OH 2733 N N . GLY B 23 ? 0.3412 0.4268 0.3856 -0.0305 0.0202 0.0235 352 GLY B N 2734 C CA . GLY B 23 ? 0.3535 0.4391 0.3945 -0.0324 0.0223 0.0250 352 GLY B CA 2735 C C . GLY B 23 ? 0.3236 0.4102 0.3606 -0.0316 0.0236 0.0243 352 GLY B C 2736 O O . GLY B 23 ? 0.3190 0.4045 0.3543 -0.0297 0.0224 0.0230 352 GLY B O 2737 N N . TYR B 24 ? 0.3505 0.4393 0.3860 -0.0334 0.0263 0.0250 353 TYR B N 2738 C CA . TYR B 24 ? 0.3554 0.4446 0.3861 -0.0329 0.0277 0.0246 353 TYR B CA 2739 C C . TYR B 24 ? 0.3731 0.4683 0.4056 -0.0333 0.0308 0.0234 353 TYR B C 2740 O O . TYR B 24 ? 0.4358 0.5349 0.4722 -0.0351 0.0323 0.0236 353 TYR B O 2741 C CB . TYR B 24 ? 0.3503 0.4354 0.3753 -0.0347 0.0280 0.0271 353 TYR B CB 2742 C CG . TYR B 24 ? 0.3645 0.4442 0.3876 -0.0343 0.0253 0.0288 353 TYR B CG 2743 C CD1 . TYR B 24 ? 0.3544 0.4318 0.3791 -0.0357 0.0248 0.0303 353 TYR B CD1 2744 C CD2 . TYR B 24 ? 0.3850 0.4623 0.4044 -0.0325 0.0232 0.0288 353 TYR B CD2 2745 C CE1 . TYR B 24 ? 0.3715 0.4441 0.3941 -0.0348 0.0224 0.0318 353 TYR B CE1 2746 C CE2 . TYR B 24 ? 0.3394 0.4130 0.3573 -0.0317 0.0207 0.0303 353 TYR B CE2 2747 C CZ . TYR B 24 ? 0.3807 0.4519 0.4002 -0.0327 0.0204 0.0318 353 TYR B CZ 2748 O OH . TYR B 24 ? 0.4175 0.4850 0.4352 -0.0314 0.0180 0.0333 353 TYR B OH 2749 N N . HIS B 25 ? 0.3507 0.4468 0.3800 -0.0317 0.0319 0.0221 354 HIS B N 2750 C CA . HIS B 25 ? 0.3681 0.4695 0.3972 -0.0320 0.0352 0.0214 354 HIS B CA 2751 C C . HIS B 25 ? 0.4019 0.5007 0.4241 -0.0329 0.0363 0.0224 354 HIS B C 2752 O O . HIS B 25 ? 0.4022 0.4973 0.4202 -0.0312 0.0349 0.0218 354 HIS B O 2753 C CB . HIS B 25 ? 0.3480 0.4531 0.3793 -0.0286 0.0359 0.0186 354 HIS B CB 2754 C CG . HIS B 25 ? 0.4610 0.5724 0.4922 -0.0283 0.0393 0.0176 354 HIS B CG 2755 N ND1 . HIS B 25 ? 0.4484 0.5676 0.4850 -0.0292 0.0413 0.0173 354 HIS B ND1 2756 C CD2 . HIS B 25 ? 0.4273 0.5391 0.4536 -0.0273 0.0412 0.0168 354 HIS B CD2 2757 C CE1 . HIS B 25 ? 0.4394 0.5639 0.4747 -0.0286 0.0444 0.0164 354 HIS B CE1 2758 N NE2 . HIS B 25 ? 0.4772 0.5969 0.5061 -0.0273 0.0444 0.0161 354 HIS B NE2 2759 N N . HIS B 26 ? 0.3587 0.4593 0.3793 -0.0358 0.0388 0.0240 355 HIS B N 2760 C CA . HIS B 26 ? 0.3511 0.4491 0.3647 -0.0367 0.0400 0.0251 355 HIS B CA 2761 C C . HIS B 26 ? 0.4169 0.5209 0.4299 -0.0370 0.0437 0.0240 355 HIS B C 2762 O O . HIS B 26 ? 0.3788 0.4896 0.3971 -0.0371 0.0455 0.0229 355 HIS B O 2763 C CB . HIS B 26 ? 0.3610 0.4544 0.3710 -0.0399 0.0399 0.0282 355 HIS B CB 2764 C CG . HIS B 26 ? 0.4764 0.5733 0.4876 -0.0436 0.0431 0.0292 355 HIS B CG 2765 N ND1 . HIS B 26 ? 0.4975 0.5965 0.5140 -0.0457 0.0431 0.0295 355 HIS B ND1 2766 C CD2 . HIS B 26 ? 0.4758 0.5749 0.4833 -0.0460 0.0463 0.0299 355 HIS B CD2 2767 C CE1 . HIS B 26 ? 0.5275 0.6299 0.5435 -0.0494 0.0462 0.0303 355 HIS B CE1 2768 N NE2 . HIS B 26 ? 0.5440 0.6466 0.5547 -0.0497 0.0483 0.0306 355 HIS B NE2 2769 N N . GLU B 27 ? 0.4467 0.5487 0.4532 -0.0370 0.0448 0.0244 356 GLU B N 2770 C CA . GLU B 27 ? 0.4870 0.5946 0.4922 -0.0368 0.0484 0.0232 356 GLU B CA 2771 C C . GLU B 27 ? 0.4846 0.5887 0.4818 -0.0386 0.0497 0.0249 356 GLU B C 2772 O O . GLU B 27 ? 0.5011 0.6000 0.4929 -0.0371 0.0479 0.0249 356 GLU B O 2773 C CB . GLU B 27 ? 0.4965 0.6057 0.5024 -0.0326 0.0481 0.0201 356 GLU B CB 2774 C CG . GLU B 27 ? 0.6298 0.7467 0.6370 -0.0313 0.0517 0.0182 356 GLU B CG 2775 C CD . GLU B 27 ? 0.9017 1.0182 0.9082 -0.0265 0.0513 0.0152 356 GLU B CD 2776 O OE1 . GLU B 27 ? 0.7666 0.8808 0.7762 -0.0245 0.0487 0.0142 356 GLU B OE1 2777 O OE2 . GLU B 27 ? 0.9191 1.0372 0.9215 -0.0250 0.0536 0.0138 356 GLU B OE2 2778 N N . ASN B 28 ? 0.4492 0.5562 0.4453 -0.0420 0.0528 0.0263 357 ASN B N 2779 C CA . ASN B 28 ? 0.4234 0.5271 0.4114 -0.0439 0.0544 0.0281 357 ASN B CA 2780 C C . ASN B 28 ? 0.4444 0.5551 0.4324 -0.0466 0.0590 0.0280 357 ASN B C 2781 O O . ASN B 28 ? 0.4507 0.5697 0.4449 -0.0461 0.0608 0.0261 357 ASN B O 2782 C CB . ASN B 28 ? 0.3501 0.4459 0.3337 -0.0464 0.0526 0.0314 357 ASN B CB 2783 C CG . ASN B 28 ? 0.3717 0.4684 0.3589 -0.0501 0.0536 0.0329 357 ASN B CG 2784 O OD1 . ASN B 28 ? 0.4140 0.5183 0.4070 -0.0515 0.0558 0.0316 357 ASN B OD1 2785 N ND2 . ASN B 28 ? 0.3633 0.4521 0.3467 -0.0517 0.0519 0.0356 357 ASN B ND2 2786 N N . SER B 29 ? 0.4787 0.5862 0.4595 -0.0494 0.0608 0.0301 358 SER B N 2787 C CA . SER B 29 ? 0.5493 0.6631 0.5289 -0.0525 0.0654 0.0302 358 SER B CA 2788 C C . SER B 29 ? 0.5186 0.6386 0.5044 -0.0563 0.0673 0.0305 358 SER B C 2789 O O . SER B 29 ? 0.5420 0.6714 0.5308 -0.0578 0.0709 0.0293 358 SER B O 2790 C CB . SER B 29 ? 0.5023 0.6098 0.4721 -0.0552 0.0666 0.0328 358 SER B CB 2791 O OG . SER B 29 ? 0.6051 0.7081 0.5692 -0.0517 0.0650 0.0323 358 SER B OG 2792 N N . GLN B 30 ? 0.4180 0.5334 0.4059 -0.0581 0.0650 0.0320 359 GLN B N 2793 C CA . GLN B 30 ? 0.4236 0.5443 0.4174 -0.0620 0.0663 0.0322 359 GLN B CA 2794 C C . GLN B 30 ? 0.4348 0.5635 0.4383 -0.0589 0.0652 0.0295 359 GLN B C 2795 O O . GLN B 30 ? 0.4024 0.5375 0.4118 -0.0617 0.0662 0.0291 359 GLN B O 2796 C CB . GLN B 30 ? 0.4239 0.5353 0.4147 -0.0653 0.0645 0.0351 359 GLN B CB 2797 C CG . GLN B 30 ? 0.4497 0.5552 0.4318 -0.0705 0.0669 0.0380 359 GLN B CG 2798 C CD . GLN B 30 ? 0.4733 0.5745 0.4469 -0.0688 0.0676 0.0389 359 GLN B CD 2799 O OE1 . GLN B 30 ? 0.4238 0.5310 0.3959 -0.0699 0.0710 0.0381 359 GLN B OE1 2800 N NE2 . GLN B 30 ? 0.4850 0.5763 0.4531 -0.0661 0.0643 0.0404 359 GLN B NE2 2801 N N . GLY B 31 ? 0.4592 0.5874 0.4640 -0.0533 0.0631 0.0275 360 GLY B N 2802 C CA . GLY B 31 ? 0.5077 0.6430 0.5207 -0.0498 0.0622 0.0248 360 GLY B CA 2803 C C . GLY B 31 ? 0.4766 0.6062 0.4922 -0.0466 0.0579 0.0243 360 GLY B C 2804 O O . GLY B 31 ? 0.5143 0.6347 0.5252 -0.0460 0.0553 0.0257 360 GLY B O 2805 N N . SER B 32 ? 0.4399 0.5756 0.4630 -0.0446 0.0573 0.0225 361 SER B N 2806 C CA . SER B 32 ? 0.4146 0.5461 0.4407 -0.0413 0.0535 0.0216 361 SER B CA 2807 C C . SER B 32 ? 0.4597 0.5919 0.4912 -0.0438 0.0521 0.0225 361 SER B C 2808 O O . SER B 32 ? 0.4497 0.5872 0.4835 -0.0479 0.0542 0.0232 361 SER B O 2809 C CB . SER B 32 ? 0.3784 0.5152 0.4080 -0.0361 0.0536 0.0186 361 SER B CB 2810 O OG . SER B 32 ? 0.6637 0.8000 0.6881 -0.0338 0.0552 0.0175 361 SER B OG 2811 N N . GLY B 33 ? 0.4602 0.5872 0.4934 -0.0417 0.0486 0.0224 362 GLY B N 2812 C CA . GLY B 33 ? 0.4382 0.5650 0.4761 -0.0438 0.0471 0.0231 362 GLY B CA 2813 C C . GLY B 33 ? 0.4698 0.5898 0.5084 -0.0413 0.0432 0.0231 362 GLY B C 2814 O O . GLY B 33 ? 0.4695 0.5828 0.5034 -0.0394 0.0415 0.0234 362 GLY B O 2815 N N . TYR B 34 ? 0.4622 0.5843 0.5065 -0.0415 0.0418 0.0226 363 TYR B N 2816 C CA . TYR B 34 ? 0.4043 0.5203 0.4495 -0.0398 0.0383 0.0228 363 TYR B CA 2817 C C . TYR B 34 ? 0.4286 0.5392 0.4726 -0.0435 0.0374 0.0251 363 TYR B C 2818 O O . TYR B 34 ? 0.4784 0.5914 0.5227 -0.0475 0.0393 0.0261 363 TYR B O 2819 C CB . TYR B 34 ? 0.3732 0.4941 0.4250 -0.0371 0.0372 0.0207 363 TYR B CB 2820 C CG . TYR B 34 ? 0.4003 0.5247 0.4526 -0.0326 0.0378 0.0184 363 TYR B CG 2821 C CD1 . TYR B 34 ? 0.4091 0.5275 0.4585 -0.0293 0.0357 0.0175 363 TYR B CD1 2822 C CD2 . TYR B 34 ? 0.3666 0.5001 0.4218 -0.0317 0.0404 0.0169 363 TYR B CD2 2823 C CE1 . TYR B 34 ? 0.4184 0.5384 0.4670 -0.0253 0.0363 0.0153 363 TYR B CE1 2824 C CE2 . TYR B 34 ? 0.3770 0.5128 0.4317 -0.0271 0.0410 0.0147 363 TYR B CE2 2825 C CZ . TYR B 34 ? 0.4544 0.5827 0.5055 -0.0239 0.0389 0.0139 363 TYR B CZ 2826 O OH . TYR B 34 ? 0.4506 0.5798 0.5002 -0.0193 0.0396 0.0117 363 TYR B OH 2827 N N . ALA B 35 ? 0.4720 0.5753 0.5141 -0.0421 0.0345 0.0259 364 ALA B N 2828 C CA . ALA B 35 ? 0.4707 0.5681 0.5115 -0.0446 0.0333 0.0279 364 ALA B CA 2829 C C . ALA B 35 ? 0.4094 0.5021 0.4511 -0.0419 0.0299 0.0278 364 ALA B C 2830 O O . ALA B 35 ? 0.4023 0.4923 0.4415 -0.0391 0.0284 0.0274 364 ALA B O 2831 C CB . ALA B 35 ? 0.4235 0.5150 0.4570 -0.0470 0.0343 0.0304 364 ALA B CB 2832 N N . ALA B 36 ? 0.4499 0.5418 0.4951 -0.0428 0.0286 0.0279 365 ALA B N 2833 C CA . ALA B 36 ? 0.4350 0.5226 0.4810 -0.0405 0.0255 0.0279 365 ALA B CA 2834 C C . ALA B 36 ? 0.4266 0.5064 0.4665 -0.0405 0.0244 0.0301 365 ALA B C 2835 O O . ALA B 36 ? 0.4602 0.5366 0.4960 -0.0431 0.0258 0.0320 365 ALA B O 2836 C CB . ALA B 36 ? 0.4476 0.5364 0.4985 -0.0415 0.0247 0.0274 365 ALA B CB 2837 N N . ASP B 37 ? 0.3994 0.4765 0.4385 -0.0376 0.0219 0.0299 366 ASP B N 2838 C CA . ASP B 37 ? 0.4251 0.4957 0.4596 -0.0369 0.0203 0.0319 366 ASP B CA 2839 C C . ASP B 37 ? 0.4534 0.5215 0.4905 -0.0374 0.0190 0.0323 366 ASP B C 2840 O O . ASP B 37 ? 0.5025 0.5720 0.5435 -0.0356 0.0171 0.0310 366 ASP B O 2841 C CB . ASP B 37 ? 0.4381 0.5083 0.4711 -0.0338 0.0181 0.0314 366 ASP B CB 2842 C CG . ASP B 37 ? 0.5033 0.5682 0.5312 -0.0325 0.0165 0.0335 366 ASP B CG 2843 O OD1 . ASP B 37 ? 0.5896 0.6519 0.6118 -0.0330 0.0174 0.0351 366 ASP B OD1 2844 O OD2 . ASP B 37 ? 0.4945 0.5581 0.5238 -0.0309 0.0142 0.0335 366 ASP B OD2 2845 N N . ARG B 38 ? 0.5077 0.5719 0.5423 -0.0401 0.0202 0.0339 367 ARG B N 2846 C CA . ARG B 38 ? 0.6475 0.7092 0.6842 -0.0411 0.0193 0.0340 367 ARG B CA 2847 C C . ARG B 38 ? 0.5586 0.6160 0.5943 -0.0380 0.0166 0.0346 367 ARG B C 2848 O O . ARG B 38 ? 0.5484 0.6065 0.5881 -0.0374 0.0153 0.0337 367 ARG B O 2849 C CB . ARG B 38 ? 0.7553 0.8122 0.7879 -0.0450 0.0212 0.0358 367 ARG B CB 2850 C CG . ARG B 38 ? 0.9208 0.9830 0.9552 -0.0489 0.0241 0.0351 367 ARG B CG 2851 C CD . ARG B 38 ? 1.1585 1.2153 1.1886 -0.0535 0.0258 0.0367 367 ARG B CD 2852 N NE . ARG B 38 ? 1.3130 1.3592 1.3351 -0.0525 0.0250 0.0391 367 ARG B NE 2853 C CZ . ARG B 38 ? 1.2602 1.3019 1.2753 -0.0523 0.0260 0.0409 367 ARG B CZ 2854 N NH1 . ARG B 38 ? 1.0990 1.1458 1.1142 -0.0532 0.0278 0.0405 367 ARG B NH1 2855 N NH2 . ARG B 38 ? 1.1494 1.1814 1.1572 -0.0507 0.0251 0.0431 367 ARG B NH2 2856 N N . GLU B 39 ? 0.5240 0.5778 0.5544 -0.0359 0.0158 0.0360 368 GLU B N 2857 C CA . GLU B 39 ? 0.5619 0.6123 0.5907 -0.0327 0.0133 0.0367 368 GLU B CA 2858 C C . GLU B 39 ? 0.5397 0.5952 0.5741 -0.0305 0.0113 0.0347 368 GLU B C 2859 O O . GLU B 39 ? 0.4766 0.5311 0.5133 -0.0295 0.0099 0.0344 368 GLU B O 2860 C CB . GLU B 39 ? 0.6531 0.7001 0.6752 -0.0307 0.0129 0.0386 368 GLU B CB 2861 C CG . GLU B 39 ? 0.8082 0.8514 0.8276 -0.0272 0.0106 0.0398 368 GLU B CG 2862 C CD . GLU B 39 ? 0.9974 1.0438 1.0152 -0.0241 0.0088 0.0398 368 GLU B CD 2863 O OE1 . GLU B 39 ? 0.9905 1.0420 1.0103 -0.0248 0.0092 0.0384 368 GLU B OE1 2864 O OE2 . GLU B 39 ? 0.9804 1.0242 0.9948 -0.0210 0.0072 0.0412 368 GLU B OE2 2865 N N . SER B 40 ? 0.4984 0.5587 0.5343 -0.0299 0.0113 0.0334 369 SER B N 2866 C CA . SER B 40 ? 0.4173 0.4815 0.4575 -0.0284 0.0096 0.0314 369 SER B CA 2867 C C . SER B 40 ? 0.4165 0.4832 0.4624 -0.0295 0.0100 0.0297 369 SER B C 2868 O O . SER B 40 ? 0.3568 0.4246 0.4060 -0.0284 0.0084 0.0287 369 SER B O 2869 C CB . SER B 40 ? 0.3269 0.3944 0.3660 -0.0277 0.0096 0.0303 369 SER B CB 2870 O OG . SER B 40 ? 0.3840 0.4538 0.4239 -0.0292 0.0119 0.0295 369 SER B OG 2871 N N . THR B 41 ? 0.3482 0.4164 0.3954 -0.0317 0.0121 0.0296 370 THR B N 2872 C CA . THR B 41 ? 0.3337 0.4049 0.3862 -0.0327 0.0124 0.0281 370 THR B CA 2873 C C . THR B 41 ? 0.3683 0.4362 0.4218 -0.0331 0.0113 0.0288 370 THR B C 2874 O O . THR B 41 ? 0.3584 0.4276 0.4157 -0.0323 0.0101 0.0276 370 THR B O 2875 C CB . THR B 41 ? 0.3208 0.3955 0.3745 -0.0352 0.0150 0.0278 370 THR B CB 2876 O OG1 . THR B 41 ? 0.3310 0.4093 0.3843 -0.0342 0.0160 0.0268 370 THR B OG1 2877 C CG2 . THR B 41 ? 0.3371 0.4153 0.3962 -0.0361 0.0150 0.0265 370 THR B CG2 2878 N N . GLN B 42 ? 0.3878 0.4507 0.4372 -0.0345 0.0119 0.0307 371 GLN B N 2879 C CA . GLN B 42 ? 0.4044 0.4631 0.4537 -0.0351 0.0112 0.0313 371 GLN B CA 2880 C C . GLN B 42 ? 0.4382 0.4955 0.4881 -0.0320 0.0088 0.0312 371 GLN B C 2881 O O . GLN B 42 ? 0.3846 0.4418 0.4375 -0.0318 0.0078 0.0304 371 GLN B O 2882 C CB . GLN B 42 ? 0.3696 0.4215 0.4127 -0.0368 0.0124 0.0335 371 GLN B CB 2883 C CG . GLN B 42 ? 0.4163 0.4631 0.4586 -0.0382 0.0121 0.0340 371 GLN B CG 2884 C CD . GLN B 42 ? 0.4775 0.5288 0.5252 -0.0411 0.0127 0.0324 371 GLN B CD 2885 O OE1 . GLN B 42 ? 0.5094 0.5648 0.5586 -0.0439 0.0145 0.0319 371 GLN B OE1 2886 N NE2 . GLN B 42 ? 0.4249 0.4759 0.4756 -0.0402 0.0112 0.0315 371 GLN B NE2 2887 N N . LYS B 43 ? 0.3092 0.3660 0.3561 -0.0296 0.0079 0.0318 372 LYS B N 2888 C CA . LYS B 43 ? 0.3436 0.4004 0.3909 -0.0268 0.0057 0.0316 372 LYS B CA 2889 C C . LYS B 43 ? 0.3910 0.4526 0.4439 -0.0265 0.0047 0.0295 372 LYS B C 2890 O O . LYS B 43 ? 0.3052 0.3664 0.3599 -0.0254 0.0033 0.0291 372 LYS B O 2891 C CB . LYS B 43 ? 0.3880 0.4455 0.4316 -0.0247 0.0050 0.0324 372 LYS B CB 2892 C CG . LYS B 43 ? 0.5317 0.5899 0.5751 -0.0218 0.0028 0.0326 372 LYS B CG 2893 C CD . LYS B 43 ? 0.5398 0.6014 0.5812 -0.0204 0.0019 0.0325 372 LYS B CD 2894 C CE . LYS B 43 ? 0.6387 0.7030 0.6808 -0.0180 -0.0003 0.0323 372 LYS B CE 2895 N NZ . LYS B 43 ? 0.7085 0.7775 0.7494 -0.0173 -0.0013 0.0317 372 LYS B NZ 2896 N N . ALA B 44 ? 0.3361 0.4015 0.3911 -0.0274 0.0056 0.0281 373 ALA B N 2897 C CA . ALA B 44 ? 0.2661 0.3348 0.3253 -0.0270 0.0049 0.0261 373 ALA B CA 2898 C C . ALA B 44 ? 0.3274 0.3963 0.3904 -0.0281 0.0050 0.0255 373 ALA B C 2899 O O . ALA B 44 ? 0.3020 0.3714 0.3675 -0.0272 0.0037 0.0246 373 ALA B O 2900 C CB . ALA B 44 ? 0.2573 0.3292 0.3168 -0.0272 0.0059 0.0249 373 ALA B CB 2901 N N . ILE B 45 ? 0.3250 0.3936 0.3881 -0.0301 0.0066 0.0261 374 ILE B N 2902 C CA . ILE B 45 ? 0.3075 0.3765 0.3737 -0.0316 0.0067 0.0256 374 ILE B CA 2903 C C . ILE B 45 ? 0.3243 0.3891 0.3897 -0.0309 0.0052 0.0262 374 ILE B C 2904 O O . ILE B 45 ? 0.3372 0.4028 0.4057 -0.0307 0.0043 0.0252 374 ILE B O 2905 C CB . ILE B 45 ? 0.3670 0.4363 0.4325 -0.0346 0.0087 0.0262 374 ILE B CB 2906 C CG1 . ILE B 45 ? 0.3876 0.4626 0.4550 -0.0351 0.0102 0.0253 374 ILE B CG1 2907 C CG2 . ILE B 45 ? 0.2691 0.3383 0.3372 -0.0366 0.0085 0.0259 374 ILE B CG2 2908 C CD1 . ILE B 45 ? 0.3099 0.3858 0.3760 -0.0384 0.0125 0.0260 374 ILE B CD1 2909 N N . ASP B 46 ? 0.3881 0.4483 0.4490 -0.0303 0.0051 0.0279 375 ASP B N 2910 C CA . ASP B 46 ? 0.4404 0.4963 0.4998 -0.0291 0.0038 0.0285 375 ASP B CA 2911 C C . ASP B 46 ? 0.4000 0.4582 0.4618 -0.0267 0.0020 0.0275 375 ASP B C 2912 O O . ASP B 46 ? 0.3898 0.4471 0.4533 -0.0263 0.0011 0.0270 375 ASP B O 2913 C CB . ASP B 46 ? 0.4177 0.4680 0.4711 -0.0282 0.0041 0.0306 375 ASP B CB 2914 C CG . ASP B 46 ? 0.5558 0.6020 0.6059 -0.0312 0.0060 0.0317 375 ASP B CG 2915 O OD1 . ASP B 46 ? 0.5457 0.5933 0.5984 -0.0341 0.0068 0.0309 375 ASP B OD1 2916 O OD2 . ASP B 46 ? 0.5589 0.6006 0.6033 -0.0307 0.0066 0.0335 375 ASP B OD2 2917 N N . GLY B 47 ? 0.3428 0.4040 0.4044 -0.0253 0.0015 0.0272 376 GLY B N 2918 C CA . GLY B 47 ? 0.3226 0.3863 0.3860 -0.0237 -0.0001 0.0262 376 GLY B CA 2919 C C . GLY B 47 ? 0.3566 0.4223 0.4241 -0.0245 -0.0003 0.0245 376 GLY B C 2920 O O . GLY B 47 ? 0.3148 0.3802 0.3839 -0.0238 -0.0014 0.0240 376 GLY B O 2921 N N . ILE B 48 ? 0.3057 0.3734 0.3748 -0.0256 0.0007 0.0236 377 ILE B N 2922 C CA . ILE B 48 ? 0.2924 0.3622 0.3649 -0.0258 0.0005 0.0220 377 ILE B CA 2923 C C . ILE B 48 ? 0.3571 0.4259 0.4318 -0.0267 0.0003 0.0220 377 ILE B C 2924 O O . ILE B 48 ? 0.3141 0.3833 0.3909 -0.0262 -0.0007 0.0210 377 ILE B O 2925 C CB . ILE B 48 ? 0.3317 0.4043 0.4049 -0.0261 0.0017 0.0211 377 ILE B CB 2926 C CG1 . ILE B 48 ? 0.3844 0.4575 0.4555 -0.0251 0.0014 0.0205 377 ILE B CG1 2927 C CG2 . ILE B 48 ? 0.3085 0.3833 0.3851 -0.0260 0.0017 0.0198 377 ILE B CG2 2928 C CD1 . ILE B 48 ? 0.4222 0.4969 0.4920 -0.0253 0.0029 0.0203 377 ILE B CD1 2929 N N . THR B 49 ? 0.3271 0.3942 0.4008 -0.0282 0.0013 0.0230 378 THR B N 2930 C CA . THR B 49 ? 0.3191 0.3845 0.3939 -0.0295 0.0011 0.0231 378 THR B CA 2931 C C . THR B 49 ? 0.3449 0.4071 0.4187 -0.0281 -0.0003 0.0233 378 THR B C 2932 O O . THR B 49 ? 0.3645 0.4263 0.4401 -0.0283 -0.0011 0.0226 378 THR B O 2933 C CB . THR B 49 ? 0.3517 0.4145 0.4241 -0.0319 0.0025 0.0243 378 THR B CB 2934 O OG1 . THR B 49 ? 0.3281 0.3949 0.4017 -0.0334 0.0040 0.0240 378 THR B OG1 2935 C CG2 . THR B 49 ? 0.2569 0.3176 0.3299 -0.0337 0.0023 0.0241 378 THR B CG2 2936 N N . ASN B 50 ? 0.2834 0.3437 0.3543 -0.0264 -0.0007 0.0243 379 ASN B N 2937 C CA . ASN B 50 ? 0.3023 0.3606 0.3723 -0.0247 -0.0020 0.0245 379 ASN B CA 2938 C C . ASN B 50 ? 0.3146 0.3762 0.3875 -0.0239 -0.0031 0.0231 379 ASN B C 2939 O O . ASN B 50 ? 0.2882 0.3488 0.3619 -0.0233 -0.0039 0.0227 379 ASN B O 2940 C CB . ASN B 50 ? 0.3196 0.3766 0.3859 -0.0227 -0.0022 0.0258 379 ASN B CB 2941 C CG . ASN B 50 ? 0.4015 0.4563 0.4664 -0.0206 -0.0032 0.0263 379 ASN B CG 2942 O OD1 . ASN B 50 ? 0.5019 0.5516 0.5640 -0.0203 -0.0029 0.0272 379 ASN B OD1 2943 N ND2 . ASN B 50 ? 0.3248 0.3832 0.3913 -0.0191 -0.0043 0.0255 379 ASN B ND2 2944 N N . LYS B 51 ? 0.3257 0.3904 0.3995 -0.0239 -0.0030 0.0223 380 LYS B N 2945 C CA . LYS B 51 ? 0.3643 0.4310 0.4397 -0.0234 -0.0039 0.0210 380 LYS B CA 2946 C C . LYS B 51 ? 0.3669 0.4335 0.4449 -0.0241 -0.0041 0.0200 380 LYS B C 2947 O O . LYS B 51 ? 0.3412 0.4073 0.4199 -0.0236 -0.0050 0.0194 380 LYS B O 2948 C CB . LYS B 51 ? 0.3248 0.3936 0.3997 -0.0235 -0.0036 0.0203 380 LYS B CB 2949 C CG . LYS B 51 ? 0.3920 0.4614 0.4674 -0.0235 -0.0043 0.0189 380 LYS B CG 2950 C CD . LYS B 51 ? 0.3695 0.4398 0.4437 -0.0237 -0.0037 0.0180 380 LYS B CD 2951 C CE . LYS B 51 ? 0.4100 0.4813 0.4816 -0.0238 -0.0038 0.0184 380 LYS B CE 2952 N NZ . LYS B 51 ? 0.4173 0.4885 0.4868 -0.0243 -0.0036 0.0171 380 LYS B NZ 2953 N N . VAL B 52 ? 0.3133 0.3807 0.3926 -0.0250 -0.0032 0.0198 381 VAL B N 2954 C CA . VAL B 52 ? 0.3051 0.3734 0.3870 -0.0255 -0.0034 0.0190 381 VAL B CA 2955 C C . VAL B 52 ? 0.3286 0.3945 0.4107 -0.0260 -0.0041 0.0193 381 VAL B C 2956 O O . VAL B 52 ? 0.2853 0.3511 0.3685 -0.0255 -0.0050 0.0185 381 VAL B O 2957 C CB . VAL B 52 ? 0.3175 0.3886 0.4010 -0.0266 -0.0023 0.0188 381 VAL B CB 2958 C CG1 . VAL B 52 ? 0.3130 0.3859 0.3993 -0.0271 -0.0027 0.0179 381 VAL B CG1 2959 C CG2 . VAL B 52 ? 0.2195 0.2929 0.3027 -0.0256 -0.0016 0.0181 381 VAL B CG2 2960 N N . ASN B 53 ? 0.3029 0.3661 0.3830 -0.0267 -0.0036 0.0204 382 ASN B N 2961 C CA . ASN B 53 ? 0.3206 0.3805 0.4000 -0.0271 -0.0041 0.0206 382 ASN B CA 2962 C C . ASN B 53 ? 0.3496 0.4083 0.4281 -0.0252 -0.0052 0.0205 382 ASN B C 2963 O O . ASN B 53 ? 0.3756 0.4328 0.4545 -0.0251 -0.0059 0.0201 382 ASN B O 2964 C CB . ASN B 53 ? 0.2844 0.3404 0.3606 -0.0282 -0.0032 0.0219 382 ASN B CB 2965 C CG . ASN B 53 ? 0.4231 0.4805 0.5002 -0.0310 -0.0021 0.0218 382 ASN B CG 2966 O OD1 . ASN B 53 ? 0.3691 0.4304 0.4496 -0.0320 -0.0022 0.0207 382 ASN B OD1 2967 N ND2 . ASN B 53 ? 0.3871 0.4415 0.4610 -0.0323 -0.0009 0.0230 382 ASN B ND2 2968 N N . SER B 54 ? 0.3313 0.3910 0.4086 -0.0237 -0.0053 0.0209 383 SER B N 2969 C CA . SER B 54 ? 0.3500 0.4100 0.4269 -0.0221 -0.0062 0.0207 383 SER B CA 2970 C C . SER B 54 ? 0.3597 0.4215 0.4387 -0.0224 -0.0069 0.0194 383 SER B C 2971 O O . SER B 54 ? 0.4159 0.4770 0.4950 -0.0219 -0.0076 0.0191 383 SER B O 2972 C CB . SER B 54 ? 0.3304 0.3925 0.4058 -0.0209 -0.0063 0.0213 383 SER B CB 2973 O OG . SER B 54 ? 0.3862 0.4460 0.4589 -0.0201 -0.0058 0.0227 383 SER B OG 2974 N N . ILE B 55 ? 0.2888 0.3524 0.3690 -0.0231 -0.0067 0.0187 384 ILE B N 2975 C CA . ILE B 55 ? 0.2954 0.3596 0.3767 -0.0232 -0.0073 0.0175 384 ILE B CA 2976 C C . ILE B 55 ? 0.2965 0.3596 0.3792 -0.0236 -0.0078 0.0171 384 ILE B C 2977 O O . ILE B 55 ? 0.3304 0.3927 0.4131 -0.0233 -0.0085 0.0166 384 ILE B O 2978 C CB . ILE B 55 ? 0.3298 0.3954 0.4114 -0.0233 -0.0069 0.0169 384 ILE B CB 2979 C CG1 . ILE B 55 ? 0.2410 0.3074 0.3206 -0.0232 -0.0066 0.0170 384 ILE B CG1 2980 C CG2 . ILE B 55 ? 0.2972 0.3623 0.3792 -0.0230 -0.0075 0.0158 384 ILE B CG2 2981 C CD1 . ILE B 55 ? 0.2914 0.3584 0.3704 -0.0232 -0.0060 0.0163 384 ILE B CD1 2982 N N . ILE B 56 ? 0.2938 0.3571 0.3775 -0.0244 -0.0073 0.0174 385 ILE B N 2983 C CA . ILE B 56 ? 0.3591 0.4218 0.4440 -0.0252 -0.0077 0.0170 385 ILE B CA 2984 C C . ILE B 56 ? 0.4056 0.4651 0.4890 -0.0250 -0.0082 0.0172 385 ILE B C 2985 O O . ILE B 56 ? 0.4165 0.4754 0.5004 -0.0250 -0.0090 0.0166 385 ILE B O 2986 C CB . ILE B 56 ? 0.3547 0.4185 0.4406 -0.0269 -0.0069 0.0172 385 ILE B CB 2987 C CG1 . ILE B 56 ? 0.3345 0.4025 0.4224 -0.0267 -0.0065 0.0166 385 ILE B CG1 2988 C CG2 . ILE B 56 ? 0.2497 0.3125 0.3361 -0.0284 -0.0074 0.0169 385 ILE B CG2 2989 C CD1 . ILE B 56 ? 0.2962 0.3665 0.3850 -0.0286 -0.0053 0.0170 385 ILE B CD1 2990 N N . ASN B 57 ? 0.4288 0.4863 0.5102 -0.0246 -0.0078 0.0182 386 ASN B N 2991 C CA . ASN B 57 ? 0.4421 0.4963 0.5215 -0.0238 -0.0081 0.0185 386 ASN B CA 2992 C C . ASN B 57 ? 0.4488 0.5042 0.5284 -0.0224 -0.0088 0.0179 386 ASN B C 2993 O O . ASN B 57 ? 0.5114 0.5647 0.5901 -0.0220 -0.0092 0.0176 386 ASN B O 2994 C CB . ASN B 57 ? 0.4996 0.5513 0.5761 -0.0229 -0.0074 0.0197 386 ASN B CB 2995 C CG . ASN B 57 ? 0.7058 0.7537 0.7796 -0.0214 -0.0076 0.0200 386 ASN B CG 2996 O OD1 . ASN B 57 ? 0.7833 0.8274 0.8558 -0.0223 -0.0076 0.0198 386 ASN B OD1 2997 N ND2 . ASN B 57 ? 0.6300 0.6790 0.7026 -0.0190 -0.0077 0.0205 386 ASN B ND2 2998 N N . LYS B 58 ? 0.4536 0.5118 0.5338 -0.0221 -0.0089 0.0177 387 LYS B N 2999 C CA . LYS B 58 ? 0.4657 0.5252 0.5456 -0.0215 -0.0094 0.0171 387 LYS B CA 3000 C C . LYS B 58 ? 0.4905 0.5497 0.5713 -0.0222 -0.0100 0.0161 387 LYS B C 3001 O O . LYS B 58 ? 0.4672 0.5262 0.5474 -0.0220 -0.0104 0.0157 387 LYS B O 3002 C CB . LYS B 58 ? 0.4374 0.4998 0.5169 -0.0214 -0.0093 0.0172 387 LYS B CB 3003 C CG . LYS B 58 ? 0.4208 0.4844 0.4992 -0.0203 -0.0089 0.0182 387 LYS B CG 3004 C CD . LYS B 58 ? 0.4696 0.5319 0.5469 -0.0186 -0.0090 0.0187 387 LYS B CD 3005 C CE . LYS B 58 ? 0.4764 0.5394 0.5520 -0.0169 -0.0087 0.0199 387 LYS B CE 3006 N NZ . LYS B 58 ? 0.4981 0.5585 0.5716 -0.0146 -0.0087 0.0205 387 LYS B NZ 3007 N N . MET B 59 ? 0.4453 0.5046 0.5274 -0.0229 -0.0100 0.0158 388 MET B N 3008 C CA . MET B 59 ? 0.4382 0.4973 0.5209 -0.0230 -0.0106 0.0150 388 MET B CA 3009 C C . MET B 59 ? 0.4490 0.5069 0.5323 -0.0235 -0.0111 0.0148 388 MET B C 3010 O O . MET B 59 ? 0.5195 0.5781 0.6038 -0.0235 -0.0117 0.0142 388 MET B O 3011 C CB . MET B 59 ? 0.4146 0.4752 0.4980 -0.0229 -0.0104 0.0147 388 MET B CB 3012 C CG . MET B 59 ? 0.3373 0.3982 0.4193 -0.0227 -0.0100 0.0146 388 MET B CG 3013 S SD . MET B 59 ? 0.5137 0.5725 0.5931 -0.0228 -0.0106 0.0139 388 MET B SD 3014 C CE . MET B 59 ? 0.3924 0.4509 0.4696 -0.0231 -0.0100 0.0136 388 MET B CE 3015 N N . ASN B 60 ? 0.5621 0.6183 0.6446 -0.0236 -0.0109 0.0153 389 ASN B N 3016 C CA . ASN B 60 ? 0.5586 0.6130 0.6410 -0.0245 -0.0112 0.0151 389 ASN B CA 3017 C C . ASN B 60 ? 0.5808 0.6331 0.6620 -0.0242 -0.0119 0.0146 389 ASN B C 3018 O O . ASN B 60 ? 0.6146 0.6644 0.6947 -0.0248 -0.0120 0.0144 389 ASN B O 3019 C CB . ASN B 60 ? 0.6643 0.7163 0.7453 -0.0250 -0.0104 0.0159 389 ASN B CB 3020 C CG . ASN B 60 ? 0.9182 0.9680 0.9986 -0.0268 -0.0105 0.0157 389 ASN B CG 3021 O OD1 . ASN B 60 ? 0.8755 0.9271 0.9576 -0.0280 -0.0111 0.0149 389 ASN B OD1 3022 N ND2 . ASN B 60 ? 0.9495 0.9951 1.0270 -0.0272 -0.0098 0.0164 389 ASN B ND2 3023 N N . THR B 61 ? 0.4538 0.5070 0.5348 -0.0233 -0.0122 0.0142 390 THR B N 3024 C CA . THR B 61 ? 0.4880 0.5397 0.5679 -0.0232 -0.0129 0.0136 390 THR B CA 3025 C C . THR B 61 ? 0.4537 0.5063 0.5342 -0.0233 -0.0137 0.0130 390 THR B C 3026 O O . THR B 61 ? 0.4452 0.4994 0.5266 -0.0231 -0.0136 0.0131 390 THR B O 3027 C CB . THR B 61 ? 0.4799 0.5315 0.5582 -0.0222 -0.0125 0.0137 390 THR B CB 3028 O OG1 . THR B 61 ? 0.4830 0.5368 0.5615 -0.0223 -0.0123 0.0138 390 THR B OG1 3029 C CG2 . THR B 61 ? 0.3728 0.4237 0.4502 -0.0213 -0.0118 0.0143 390 THR B CG2 3030 N N . GLN B 62 ? 0.4635 0.5147 0.5430 -0.0233 -0.0145 0.0125 391 GLN B N 3031 C CA . GLN B 62 ? 0.4508 0.5024 0.5301 -0.0229 -0.0154 0.0120 391 GLN B CA 3032 C C . GLN B 62 ? 0.4678 0.5172 0.5446 -0.0227 -0.0157 0.0117 391 GLN B C 3033 O O . GLN B 62 ? 0.4908 0.5388 0.5666 -0.0229 -0.0157 0.0115 391 GLN B O 3034 C CB . GLN B 62 ? 0.4631 0.5162 0.5440 -0.0233 -0.0164 0.0116 391 GLN B CB 3035 C CG . GLN B 62 ? 0.4049 0.4610 0.4883 -0.0239 -0.0160 0.0117 391 GLN B CG 3036 C CD . GLN B 62 ? 0.4669 0.5221 0.5506 -0.0254 -0.0152 0.0121 391 GLN B CD 3037 O OE1 . GLN B 62 ? 0.5361 0.5887 0.6183 -0.0261 -0.0154 0.0119 391 GLN B OE1 3038 N NE2 . GLN B 62 ? 0.4947 0.5513 0.5796 -0.0258 -0.0143 0.0126 391 GLN B NE2 3039 N N . PHE B 63 ? 0.4306 0.4793 0.5058 -0.0222 -0.0159 0.0116 392 PHE B N 3040 C CA . PHE B 63 ? 0.3904 0.4366 0.4627 -0.0222 -0.0162 0.0114 392 PHE B CA 3041 C C . PHE B 63 ? 0.4141 0.4599 0.4862 -0.0216 -0.0176 0.0110 392 PHE B C 3042 O O . PHE B 63 ? 0.4462 0.4933 0.5193 -0.0207 -0.0182 0.0109 392 PHE B O 3043 C CB . PHE B 63 ? 0.3218 0.3664 0.3914 -0.0224 -0.0158 0.0115 392 PHE B CB 3044 C CG . PHE B 63 ? 0.4048 0.4463 0.4707 -0.0226 -0.0162 0.0113 392 PHE B CG 3045 C CD1 . PHE B 63 ? 0.2896 0.3309 0.3542 -0.0236 -0.0155 0.0112 392 PHE B CD1 3046 C CD2 . PHE B 63 ? 0.3803 0.4192 0.4439 -0.0215 -0.0171 0.0112 392 PHE B CD2 3047 C CE1 . PHE B 63 ? 0.3404 0.3788 0.4013 -0.0240 -0.0157 0.0110 392 PHE B CE1 3048 C CE2 . PHE B 63 ? 0.3533 0.3888 0.4129 -0.0216 -0.0175 0.0111 392 PHE B CE2 3049 C CZ . PHE B 63 ? 0.4088 0.4439 0.4670 -0.0232 -0.0167 0.0110 392 PHE B CZ 3050 N N . GLU B 64 ? 0.4478 0.4921 0.5184 -0.0219 -0.0181 0.0106 393 GLU B N 3051 C CA . GLU B 64 ? 0.5994 0.6438 0.6698 -0.0214 -0.0196 0.0102 393 GLU B CA 3052 C C . GLU B 64 ? 0.5027 0.5443 0.5694 -0.0207 -0.0203 0.0101 393 GLU B C 3053 O O . GLU B 64 ? 0.5097 0.5490 0.5739 -0.0213 -0.0199 0.0100 393 GLU B O 3054 C CB . GLU B 64 ? 0.6344 0.6794 0.7060 -0.0225 -0.0199 0.0098 393 GLU B CB 3055 C CG . GLU B 64 ? 0.6952 0.7421 0.7697 -0.0233 -0.0192 0.0099 393 GLU B CG 3056 C CD . GLU B 64 ? 0.8218 0.8686 0.8966 -0.0248 -0.0197 0.0094 393 GLU B CD 3057 O OE1 . GLU B 64 ? 0.8712 0.9207 0.9476 -0.0254 -0.0208 0.0090 393 GLU B OE1 3058 O OE2 . GLU B 64 ? 0.9168 0.9608 0.9901 -0.0253 -0.0190 0.0093 393 GLU B OE2 3059 N N . ALA B 65 ? 0.3643 0.4059 0.4302 -0.0191 -0.0213 0.0102 394 ALA B N 3060 C CA . ALA B 65 ? 0.4253 0.4635 0.4869 -0.0180 -0.0221 0.0102 394 ALA B CA 3061 C C . ALA B 65 ? 0.4409 0.4802 0.5025 -0.0179 -0.0236 0.0097 394 ALA B C 3062 O O . ALA B 65 ? 0.4810 0.5242 0.5462 -0.0184 -0.0242 0.0093 394 ALA B O 3063 C CB . ALA B 65 ? 0.4235 0.4608 0.4836 -0.0158 -0.0226 0.0105 394 ALA B CB 3064 N N . VAL B 66 ? 0.4610 0.4968 0.5184 -0.0175 -0.0242 0.0097 395 VAL B N 3065 C CA . VAL B 66 ? 0.4905 0.5270 0.5473 -0.0175 -0.0256 0.0092 395 VAL B CA 3066 C C . VAL B 66 ? 0.5004 0.5360 0.5542 -0.0152 -0.0274 0.0093 395 VAL B C 3067 O O . VAL B 66 ? 0.4981 0.5305 0.5486 -0.0135 -0.0273 0.0099 395 VAL B O 3068 C CB . VAL B 66 ? 0.5415 0.5750 0.5957 -0.0191 -0.0248 0.0090 395 VAL B CB 3069 C CG1 . VAL B 66 ? 0.4216 0.4564 0.4787 -0.0208 -0.0233 0.0088 395 VAL B CG1 3070 C CG2 . VAL B 66 ? 0.5004 0.5292 0.5498 -0.0190 -0.0239 0.0096 395 VAL B CG2 3071 N N . ASP B 67 ? 0.6467 0.6849 0.7011 -0.0151 -0.0291 0.0087 396 ASP B N 3072 C CA . ASP B 67 ? 0.6284 0.6666 0.6800 -0.0126 -0.0311 0.0088 396 ASP B CA 3073 C C . ASP B 67 ? 0.5480 0.5810 0.5939 -0.0128 -0.0313 0.0089 396 ASP B C 3074 O O . ASP B 67 ? 0.5638 0.5966 0.6069 -0.0110 -0.0332 0.0089 396 ASP B O 3075 C CB . ASP B 67 ? 0.6130 0.6580 0.6685 -0.0127 -0.0329 0.0080 396 ASP B CB 3076 C CG . ASP B 67 ? 0.7007 0.7470 0.7583 -0.0161 -0.0325 0.0071 396 ASP B CG 3077 O OD1 . ASP B 67 ? 0.7014 0.7510 0.7633 -0.0178 -0.0318 0.0068 396 ASP B OD1 3078 O OD2 . ASP B 67 ? 0.5685 0.6118 0.6230 -0.0171 -0.0329 0.0068 396 ASP B OD2 3079 N N . HIS B 68 ? 0.3943 0.4234 0.4385 -0.0148 -0.0295 0.0091 397 HIS B N 3080 C CA . HIS B 68 ? 0.3936 0.4182 0.4325 -0.0155 -0.0294 0.0091 397 HIS B CA 3081 C C . HIS B 68 ? 0.3654 0.3849 0.3982 -0.0134 -0.0300 0.0100 397 HIS B C 3082 O O . HIS B 68 ? 0.4386 0.4559 0.4701 -0.0122 -0.0294 0.0106 397 HIS B O 3083 C CB . HIS B 68 ? 0.3887 0.4111 0.4272 -0.0179 -0.0271 0.0091 397 HIS B CB 3084 C CG . HIS B 68 ? 0.3650 0.3904 0.4073 -0.0195 -0.0266 0.0082 397 HIS B CG 3085 N ND1 . HIS B 68 ? 0.4150 0.4404 0.4586 -0.0210 -0.0245 0.0082 397 HIS B ND1 3086 C CD2 . HIS B 68 ? 0.3695 0.3977 0.4140 -0.0200 -0.0278 0.0074 397 HIS B CD2 3087 C CE1 . HIS B 68 ? 0.4120 0.4392 0.4580 -0.0218 -0.0245 0.0074 397 HIS B CE1 3088 N NE2 . HIS B 68 ? 0.3974 0.4259 0.4437 -0.0216 -0.0265 0.0069 397 HIS B NE2 3089 N N . GLU B 69 ? 0.3775 0.3945 0.4058 -0.0128 -0.0312 0.0099 398 GLU B N 3090 C CA . GLU B 69 ? 0.4087 0.4200 0.4301 -0.0107 -0.0318 0.0108 398 GLU B CA 3091 C C . GLU B 69 ? 0.3996 0.4045 0.4150 -0.0128 -0.0301 0.0113 398 GLU B C 3092 O O . GLU B 69 ? 0.3558 0.3618 0.3728 -0.0154 -0.0287 0.0107 398 GLU B O 3093 C CB . GLU B 69 ? 0.4696 0.4827 0.4894 -0.0082 -0.0346 0.0107 398 GLU B CB 3094 C CG . GLU B 69 ? 0.5125 0.5329 0.5378 -0.0060 -0.0364 0.0103 398 GLU B CG 3095 C CD . GLU B 69 ? 0.6971 0.7197 0.7201 -0.0030 -0.0393 0.0102 398 GLU B CD 3096 O OE1 . GLU B 69 ? 0.6473 0.6668 0.6656 -0.0033 -0.0400 0.0102 398 GLU B OE1 3097 O OE2 . GLU B 69 ? 0.7477 0.7758 0.7737 -0.0002 -0.0408 0.0102 398 GLU B OE2 3098 N N . PHE B 70 ? 0.4306 0.4288 0.4390 -0.0115 -0.0300 0.0122 399 PHE B N 3099 C CA . PHE B 70 ? 0.4229 0.4147 0.4249 -0.0138 -0.0283 0.0127 399 PHE B CA 3100 C C . PHE B 70 ? 0.4468 0.4318 0.4402 -0.0116 -0.0296 0.0136 399 PHE B C 3101 O O . PHE B 70 ? 0.4946 0.4772 0.4855 -0.0081 -0.0309 0.0143 399 PHE B O 3102 C CB . PHE B 70 ? 0.3672 0.3564 0.3686 -0.0160 -0.0259 0.0131 399 PHE B CB 3103 C CG . PHE B 70 ? 0.3954 0.3913 0.4048 -0.0179 -0.0247 0.0123 399 PHE B CG 3104 C CD1 . PHE B 70 ? 0.3435 0.3417 0.3547 -0.0209 -0.0230 0.0118 399 PHE B CD1 3105 C CD2 . PHE B 70 ? 0.3878 0.3877 0.4026 -0.0163 -0.0253 0.0122 399 PHE B CD2 3106 C CE1 . PHE B 70 ? 0.3317 0.3356 0.3496 -0.0221 -0.0219 0.0112 399 PHE B CE1 3107 C CE2 . PHE B 70 ? 0.3466 0.3521 0.3682 -0.0180 -0.0242 0.0116 399 PHE B CE2 3108 C CZ . PHE B 70 ? 0.3774 0.3846 0.4003 -0.0207 -0.0226 0.0111 399 PHE B CZ 3109 N N . SER B 71 ? 0.4459 0.4275 0.4343 -0.0132 -0.0291 0.0137 400 SER B N 3110 C CA . SER B 71 ? 0.4977 0.4722 0.4771 -0.0113 -0.0303 0.0146 400 SER B CA 3111 C C . SER B 71 ? 0.5316 0.4967 0.5028 -0.0117 -0.0288 0.0159 400 SER B C 3112 O O . SER B 71 ? 0.4833 0.4479 0.4562 -0.0139 -0.0268 0.0158 400 SER B O 3113 C CB . SER B 71 ? 0.4362 0.4100 0.4126 -0.0132 -0.0300 0.0143 400 SER B CB 3114 O OG . SER B 71 ? 0.4427 0.4139 0.4169 -0.0173 -0.0271 0.0143 400 SER B OG 3115 N N . ASN B 72 ? 0.6054 0.5626 0.5673 -0.0097 -0.0297 0.0169 401 ASN B N 3116 C CA . ASN B 72 ? 0.6666 0.6129 0.6188 -0.0103 -0.0283 0.0181 401 ASN B CA 3117 C C . ASN B 72 ? 0.6164 0.5598 0.5659 -0.0162 -0.0251 0.0180 401 ASN B C 3118 O O . ASN B 72 ? 0.5918 0.5280 0.5356 -0.0182 -0.0233 0.0187 401 ASN B O 3119 C CB . ASN B 72 ? 0.7370 0.6749 0.6788 -0.0068 -0.0300 0.0193 401 ASN B CB 3120 C CG . ASN B 72 ? 0.9656 0.9043 0.9077 -0.0005 -0.0328 0.0197 401 ASN B CG 3121 O OD1 . ASN B 72 ? 0.9091 0.8501 0.8554 0.0011 -0.0328 0.0195 401 ASN B OD1 3122 N ND2 . ASN B 72 ? 0.9734 0.9104 0.9107 0.0033 -0.0352 0.0203 401 ASN B ND2 3123 N N . LEU B 73 ? 0.5759 0.5248 0.5292 -0.0189 -0.0244 0.0172 402 LEU B N 3124 C CA . LEU B 73 ? 0.5359 0.4841 0.4874 -0.0243 -0.0214 0.0170 402 LEU B CA 3125 C C . LEU B 73 ? 0.5367 0.4941 0.4982 -0.0268 -0.0198 0.0158 402 LEU B C 3126 O O . LEU B 73 ? 0.5038 0.4642 0.4664 -0.0306 -0.0176 0.0153 402 LEU B O 3127 C CB . LEU B 73 ? 0.5279 0.4758 0.4759 -0.0255 -0.0212 0.0169 402 LEU B CB 3128 C CG . LEU B 73 ? 0.5985 0.5361 0.5350 -0.0238 -0.0222 0.0182 402 LEU B CG 3129 C CD1 . LEU B 73 ? 0.5687 0.5072 0.5027 -0.0247 -0.0222 0.0179 402 LEU B CD1 3130 C CD2 . LEU B 73 ? 0.5116 0.4391 0.4385 -0.0269 -0.0200 0.0193 402 LEU B CD2 3131 N N . GLU B 74 ? 0.5027 0.4649 0.4712 -0.0243 -0.0210 0.0155 403 GLU B N 3132 C CA . GLU B 74 ? 0.4795 0.4494 0.4567 -0.0262 -0.0198 0.0146 403 GLU B CA 3133 C C . GLU B 74 ? 0.4681 0.4360 0.4458 -0.0256 -0.0196 0.0149 403 GLU B C 3134 O O . GLU B 74 ? 0.4596 0.4338 0.4450 -0.0248 -0.0198 0.0143 403 GLU B O 3135 C CB . GLU B 74 ? 0.4652 0.4436 0.4511 -0.0242 -0.0213 0.0136 403 GLU B CB 3136 C CG . GLU B 74 ? 0.4496 0.4297 0.4349 -0.0248 -0.0214 0.0130 403 GLU B CG 3137 C CD . GLU B 74 ? 0.4761 0.4630 0.4686 -0.0229 -0.0231 0.0120 403 GLU B CD 3138 O OE1 . GLU B 74 ? 0.4275 0.4158 0.4225 -0.0201 -0.0253 0.0121 403 GLU B OE1 3139 O OE2 . GLU B 74 ? 0.4760 0.4669 0.4714 -0.0244 -0.0221 0.0111 403 GLU B OE2 3140 N N . ARG B 75 ? 0.4913 0.4498 0.4600 -0.0260 -0.0191 0.0159 404 ARG B N 3141 C CA . ARG B 75 ? 0.4689 0.4234 0.4358 -0.0256 -0.0187 0.0162 404 ARG B CA 3142 C C . ARG B 75 ? 0.4859 0.4455 0.4580 -0.0296 -0.0166 0.0155 404 ARG B C 3143 O O . ARG B 75 ? 0.4706 0.4327 0.4470 -0.0285 -0.0168 0.0152 404 ARG B O 3144 C CB . ARG B 75 ? 0.4938 0.4356 0.4482 -0.0261 -0.0181 0.0173 404 ARG B CB 3145 C CG . ARG B 75 ? 0.6241 0.5594 0.5742 -0.0265 -0.0172 0.0176 404 ARG B CG 3146 C CD . ARG B 75 ? 0.6276 0.5486 0.5639 -0.0266 -0.0168 0.0188 404 ARG B CD 3147 N NE . ARG B 75 ? 0.6930 0.6079 0.6253 -0.0208 -0.0186 0.0194 404 ARG B NE 3148 C CZ . ARG B 75 ? 0.6918 0.6037 0.6207 -0.0154 -0.0209 0.0201 404 ARG B CZ 3149 N NH1 . ARG B 75 ? 0.6641 0.5779 0.5926 -0.0152 -0.0217 0.0204 404 ARG B NH1 3150 N NH2 . ARG B 75 ? 0.7120 0.6193 0.6377 -0.0099 -0.0223 0.0206 404 ARG B NH2 3151 N N . ARG B 76 ? 0.4044 0.3663 0.3761 -0.0341 -0.0145 0.0152 405 ARG B N 3152 C CA . ARG B 76 ? 0.4319 0.3997 0.4084 -0.0379 -0.0126 0.0145 405 ARG B CA 3153 C C . ARG B 76 ? 0.3685 0.3467 0.3563 -0.0360 -0.0133 0.0137 405 ARG B C 3154 O O . ARG B 76 ? 0.3670 0.3479 0.3586 -0.0363 -0.0129 0.0134 405 ARG B O 3155 C CB . ARG B 76 ? 0.3625 0.3318 0.3364 -0.0428 -0.0103 0.0142 405 ARG B CB 3156 C CG . ARG B 76 ? 0.3835 0.3424 0.3460 -0.0463 -0.0089 0.0150 405 ARG B CG 3157 C CD . ARG B 76 ? 0.3477 0.3087 0.3075 -0.0506 -0.0069 0.0148 405 ARG B CD 3158 N NE . ARG B 76 ? 0.3902 0.3537 0.3517 -0.0480 -0.0079 0.0147 405 ARG B NE 3159 C CZ . ARG B 76 ? 0.4028 0.3737 0.3679 -0.0496 -0.0067 0.0140 405 ARG B CZ 3160 N NH1 . ARG B 76 ? 0.3864 0.3639 0.3542 -0.0538 -0.0044 0.0133 405 ARG B NH1 3161 N NH2 . ARG B 76 ? 0.3427 0.3147 0.3086 -0.0470 -0.0078 0.0139 405 ARG B NH2 3162 N N . ILE B 77 ? 0.3949 0.3782 0.3872 -0.0341 -0.0143 0.0132 406 ILE B N 3163 C CA . ILE B 77 ? 0.4450 0.4370 0.4469 -0.0325 -0.0148 0.0125 406 ILE B CA 3164 C C . ILE B 77 ? 0.4326 0.4244 0.4374 -0.0288 -0.0168 0.0127 406 ILE B C 3165 O O . ILE B 77 ? 0.3999 0.3969 0.4112 -0.0283 -0.0168 0.0123 406 ILE B O 3166 C CB . ILE B 77 ? 0.4420 0.4389 0.4474 -0.0318 -0.0151 0.0119 406 ILE B CB 3167 C CG1 . ILE B 77 ? 0.4729 0.4657 0.4747 -0.0293 -0.0171 0.0121 406 ILE B CG1 3168 C CG2 . ILE B 77 ? 0.4357 0.4348 0.4397 -0.0352 -0.0129 0.0115 406 ILE B CG2 3169 C CD1 . ILE B 77 ? 0.4614 0.4584 0.4661 -0.0286 -0.0176 0.0114 406 ILE B CD1 3170 N N . GLY B 78 ? 0.3080 0.2941 0.3080 -0.0261 -0.0185 0.0133 407 GLY B N 3171 C CA . GLY B 78 ? 0.3114 0.2977 0.3135 -0.0224 -0.0202 0.0134 407 GLY B CA 3172 C C . GLY B 78 ? 0.3469 0.3316 0.3489 -0.0230 -0.0192 0.0136 407 GLY B C 3173 O O . GLY B 78 ? 0.3367 0.3259 0.3446 -0.0213 -0.0198 0.0133 407 GLY B O 3174 N N . ASN B 79 ? 0.3564 0.3347 0.3517 -0.0259 -0.0176 0.0139 408 ASN B N 3175 C CA . ASN B 79 ? 0.3620 0.3375 0.3558 -0.0269 -0.0166 0.0140 408 ASN B CA 3176 C C . ASN B 79 ? 0.4186 0.4016 0.4190 -0.0300 -0.0151 0.0133 408 ASN B C 3177 O O . ASN B 79 ? 0.3834 0.3675 0.3860 -0.0300 -0.0148 0.0131 408 ASN B O 3178 C CB . ASN B 79 ? 0.3830 0.3478 0.3658 -0.0292 -0.0154 0.0146 408 ASN B CB 3179 C CG . ASN B 79 ? 0.5754 0.5369 0.5557 -0.0314 -0.0141 0.0144 408 ASN B CG 3180 O OD1 . ASN B 79 ? 0.5969 0.5588 0.5758 -0.0363 -0.0122 0.0141 408 ASN B OD1 3181 N ND2 . ASN B 79 ? 0.5900 0.5486 0.5698 -0.0277 -0.0151 0.0146 408 ASN B ND2 3182 N N . LEU B 80 ? 0.3979 0.3863 0.4015 -0.0323 -0.0143 0.0129 409 LEU B N 3183 C CA . LEU B 80 ? 0.3845 0.3811 0.3948 -0.0344 -0.0131 0.0123 409 LEU B CA 3184 C C . LEU B 80 ? 0.4020 0.4043 0.4201 -0.0312 -0.0144 0.0120 409 LEU B C 3185 O O . LEU B 80 ? 0.4108 0.4165 0.4327 -0.0316 -0.0140 0.0118 409 LEU B O 3186 C CB . LEU B 80 ? 0.4031 0.4040 0.4146 -0.0365 -0.0121 0.0119 409 LEU B CB 3187 C CG . LEU B 80 ? 0.4783 0.4871 0.4945 -0.0392 -0.0104 0.0114 409 LEU B CG 3188 C CD1 . LEU B 80 ? 0.3993 0.4103 0.4138 -0.0413 -0.0092 0.0111 409 LEU B CD1 3189 C CD2 . LEU B 80 ? 0.5239 0.5397 0.5483 -0.0367 -0.0111 0.0110 409 LEU B CD2 3190 N N . ASN B 81 ? 0.3397 0.3430 0.3598 -0.0283 -0.0160 0.0120 410 ASN B N 3191 C CA . ASN B 81 ? 0.3721 0.3806 0.3990 -0.0258 -0.0172 0.0118 410 ASN B CA 3192 C C . ASN B 81 ? 0.3634 0.3702 0.3904 -0.0240 -0.0177 0.0120 410 ASN B C 3193 O O . ASN B 81 ? 0.3697 0.3812 0.4021 -0.0236 -0.0176 0.0118 410 ASN B O 3194 C CB . ASN B 81 ? 0.3587 0.3680 0.3865 -0.0235 -0.0190 0.0116 410 ASN B CB 3195 C CG . ASN B 81 ? 0.3668 0.3816 0.4014 -0.0216 -0.0201 0.0113 410 ASN B CG 3196 O OD1 . ASN B 81 ? 0.3815 0.4010 0.4210 -0.0226 -0.0194 0.0109 410 ASN B OD1 3197 N ND2 . ASN B 81 ? 0.3539 0.3683 0.3885 -0.0189 -0.0218 0.0114 410 ASN B ND2 3198 N N . LYS B 82 ? 0.3682 0.3682 0.3888 -0.0227 -0.0183 0.0125 411 LYS B N 3199 C CA . LYS B 82 ? 0.4067 0.4043 0.4264 -0.0204 -0.0187 0.0127 411 LYS B CA 3200 C C . LYS B 82 ? 0.3916 0.3891 0.4114 -0.0230 -0.0170 0.0125 411 LYS B C 3201 O O . LYS B 82 ? 0.3680 0.3690 0.3921 -0.0218 -0.0171 0.0123 411 LYS B O 3202 C CB . LYS B 82 ? 0.4006 0.3895 0.4118 -0.0182 -0.0194 0.0132 411 LYS B CB 3203 C CG . LYS B 82 ? 0.5070 0.4937 0.5171 -0.0146 -0.0201 0.0134 411 LYS B CG 3204 C CD . LYS B 82 ? 0.6520 0.6281 0.6524 -0.0149 -0.0192 0.0138 411 LYS B CD 3205 C CE . LYS B 82 ? 0.6722 0.6456 0.6709 -0.0108 -0.0197 0.0138 411 LYS B CE 3206 N NZ . LYS B 82 ? 0.7328 0.7085 0.7328 -0.0054 -0.0219 0.0141 411 LYS B NZ 3207 N N . ARG B 83 ? 0.3670 0.3612 0.3823 -0.0267 -0.0155 0.0125 412 ARG B N 3208 C CA . ARG B 83 ? 0.3780 0.3725 0.3930 -0.0297 -0.0140 0.0122 412 ARG B CA 3209 C C . ARG B 83 ? 0.3815 0.3855 0.4051 -0.0304 -0.0136 0.0118 412 ARG B C 3210 O O . ARG B 83 ? 0.3114 0.3171 0.3368 -0.0311 -0.0130 0.0116 412 ARG B O 3211 C CB . ARG B 83 ? 0.3511 0.3412 0.3595 -0.0343 -0.0124 0.0122 412 ARG B CB 3212 C CG . ARG B 83 ? 0.4438 0.4224 0.4419 -0.0344 -0.0122 0.0127 412 ARG B CG 3213 C CD . ARG B 83 ? 0.4563 0.4305 0.4477 -0.0384 -0.0110 0.0128 412 ARG B CD 3214 N NE . ARG B 83 ? 0.5650 0.5458 0.5595 -0.0433 -0.0093 0.0123 412 ARG B NE 3215 C CZ . ARG B 83 ? 0.4678 0.4536 0.4642 -0.0455 -0.0086 0.0121 412 ARG B CZ 3216 N NH1 . ARG B 83 ? 0.3731 0.3576 0.3685 -0.0435 -0.0094 0.0125 412 ARG B NH1 3217 N NH2 . ARG B 83 ? 0.5267 0.5194 0.5260 -0.0495 -0.0071 0.0115 412 ARG B NH2 3218 N N . MET B 84 ? 0.3974 0.4068 0.4256 -0.0302 -0.0139 0.0117 413 MET B N 3219 C CA . MET B 84 ? 0.3599 0.3772 0.3954 -0.0303 -0.0137 0.0114 413 MET B CA 3220 C C . MET B 84 ? 0.3849 0.4045 0.4249 -0.0274 -0.0147 0.0114 413 MET B C 3221 O O . MET B 84 ? 0.3725 0.3955 0.4158 -0.0278 -0.0142 0.0113 413 MET B O 3222 C CB . MET B 84 ? 0.3275 0.3488 0.3658 -0.0302 -0.0138 0.0112 413 MET B CB 3223 C CG . MET B 84 ? 0.4161 0.4445 0.4608 -0.0301 -0.0133 0.0110 413 MET B CG 3224 S SD . MET B 84 ? 0.5536 0.5852 0.6017 -0.0285 -0.0139 0.0107 413 MET B SD 3225 C CE . MET B 84 ? 0.4904 0.5194 0.5392 -0.0258 -0.0159 0.0108 413 MET B CE 3226 N N . GLU B 85 ? 0.3310 0.3493 0.3712 -0.0246 -0.0161 0.0115 414 GLU B N 3227 C CA . GLU B 85 ? 0.3614 0.3826 0.4058 -0.0221 -0.0171 0.0115 414 GLU B CA 3228 C C . GLU B 85 ? 0.3556 0.3744 0.3981 -0.0215 -0.0166 0.0116 414 GLU B C 3229 O O . GLU B 85 ? 0.3490 0.3717 0.3957 -0.0214 -0.0163 0.0115 414 GLU B O 3230 C CB . GLU B 85 ? 0.3126 0.3334 0.3569 -0.0194 -0.0188 0.0115 414 GLU B CB 3231 C CG . GLU B 85 ? 0.4284 0.4525 0.4756 -0.0200 -0.0193 0.0113 414 GLU B CG 3232 C CD . GLU B 85 ? 0.4961 0.5199 0.5426 -0.0178 -0.0211 0.0112 414 GLU B CD 3233 O OE1 . GLU B 85 ? 0.5628 0.5841 0.6065 -0.0155 -0.0220 0.0114 414 GLU B OE1 3234 O OE2 . GLU B 85 ? 0.4467 0.4729 0.4952 -0.0183 -0.0216 0.0108 414 GLU B OE2 3235 N N . ASP B 86 ? 0.3179 0.3297 0.3537 -0.0212 -0.0165 0.0118 415 ASP B N 3236 C CA . ASP B 86 ? 0.3208 0.3289 0.3535 -0.0209 -0.0159 0.0117 415 ASP B CA 3237 C C . ASP B 86 ? 0.3511 0.3616 0.3852 -0.0243 -0.0144 0.0115 415 ASP B C 3238 O O . ASP B 86 ? 0.3430 0.3542 0.3781 -0.0239 -0.0140 0.0113 415 ASP B O 3239 C CB . ASP B 86 ? 0.3800 0.3785 0.4036 -0.0203 -0.0159 0.0120 415 ASP B CB 3240 C CG . ASP B 86 ? 0.5376 0.5341 0.5596 -0.0159 -0.0175 0.0123 415 ASP B CG 3241 O OD1 . ASP B 86 ? 0.5155 0.5187 0.5438 -0.0137 -0.0187 0.0121 415 ASP B OD1 3242 O OD2 . ASP B 86 ? 0.5876 0.5758 0.6017 -0.0148 -0.0177 0.0126 415 ASP B OD2 3243 N N . GLY B 87 ? 0.3273 0.3395 0.3614 -0.0275 -0.0136 0.0114 416 GLY B N 3244 C CA . GLY B 87 ? 0.2683 0.2845 0.3043 -0.0306 -0.0124 0.0111 416 GLY B CA 3245 C C . GLY B 87 ? 0.3532 0.3762 0.3962 -0.0293 -0.0126 0.0111 416 GLY B C 3246 O O . GLY B 87 ? 0.2870 0.3105 0.3303 -0.0299 -0.0121 0.0109 416 GLY B O 3247 N N . PHE B 88 ? 0.3266 0.3542 0.3748 -0.0278 -0.0133 0.0112 417 PHE B N 3248 C CA . PHE B 88 ? 0.3038 0.3371 0.3579 -0.0268 -0.0133 0.0113 417 PHE B CA 3249 C C . PHE B 88 ? 0.3296 0.3622 0.3847 -0.0246 -0.0138 0.0114 417 PHE B C 3250 O O . PHE B 88 ? 0.3352 0.3709 0.3931 -0.0246 -0.0133 0.0114 417 PHE B O 3251 C CB . PHE B 88 ? 0.2783 0.3151 0.3363 -0.0259 -0.0138 0.0114 417 PHE B CB 3252 C CG . PHE B 88 ? 0.3069 0.3462 0.3652 -0.0276 -0.0131 0.0113 417 PHE B CG 3253 C CD1 . PHE B 88 ? 0.2966 0.3401 0.3568 -0.0288 -0.0122 0.0113 417 PHE B CD1 3254 C CD2 . PHE B 88 ? 0.3071 0.3450 0.3637 -0.0277 -0.0133 0.0112 417 PHE B CD2 3255 C CE1 . PHE B 88 ? 0.2757 0.3225 0.3362 -0.0299 -0.0115 0.0112 417 PHE B CE1 3256 C CE2 . PHE B 88 ? 0.3336 0.3744 0.3905 -0.0290 -0.0125 0.0110 417 PHE B CE2 3257 C CZ . PHE B 88 ? 0.3194 0.3649 0.3783 -0.0299 -0.0116 0.0110 417 PHE B CZ 3258 N N . LEU B 89 ? 0.2686 0.2977 0.3215 -0.0225 -0.0146 0.0113 418 LEU B N 3259 C CA . LEU B 89 ? 0.3152 0.3440 0.3685 -0.0200 -0.0150 0.0113 418 LEU B CA 3260 C C . LEU B 89 ? 0.3177 0.3439 0.3680 -0.0209 -0.0140 0.0111 418 LEU B C 3261 O O . LEU B 89 ? 0.3237 0.3523 0.3764 -0.0199 -0.0137 0.0110 418 LEU B O 3262 C CB . LEU B 89 ? 0.2836 0.3088 0.3338 -0.0172 -0.0161 0.0113 418 LEU B CB 3263 C CG . LEU B 89 ? 0.3333 0.3584 0.3834 -0.0139 -0.0165 0.0112 418 LEU B CG 3264 C CD1 . LEU B 89 ? 0.2984 0.3309 0.3554 -0.0135 -0.0165 0.0111 418 LEU B CD1 3265 C CD2 . LEU B 89 ? 0.3035 0.3261 0.3508 -0.0107 -0.0178 0.0113 418 LEU B CD2 3266 N N . ASP B 90 ? 0.2744 0.2954 0.3190 -0.0230 -0.0133 0.0110 419 ASP B N 3267 C CA . ASP B 90 ? 0.3151 0.3328 0.3559 -0.0245 -0.0123 0.0107 419 ASP B CA 3268 C C . ASP B 90 ? 0.3230 0.3466 0.3679 -0.0268 -0.0116 0.0106 419 ASP B C 3269 O O . ASP B 90 ? 0.2612 0.2848 0.3059 -0.0266 -0.0111 0.0103 419 ASP B O 3270 C CB . ASP B 90 ? 0.3473 0.3573 0.3801 -0.0269 -0.0118 0.0105 419 ASP B CB 3271 C CG . ASP B 90 ? 0.4708 0.4730 0.4976 -0.0240 -0.0124 0.0106 419 ASP B CG 3272 O OD1 . ASP B 90 ? 0.5395 0.5425 0.5681 -0.0200 -0.0132 0.0107 419 ASP B OD1 3273 O OD2 . ASP B 90 ? 0.5310 0.5263 0.5509 -0.0258 -0.0121 0.0107 419 ASP B OD2 3274 N N . VAL B 91 ? 0.2452 0.2736 0.2934 -0.0286 -0.0115 0.0107 420 VAL B N 3275 C CA . VAL B 91 ? 0.2578 0.2920 0.3096 -0.0301 -0.0109 0.0107 420 VAL B CA 3276 C C . VAL B 91 ? 0.2703 0.3086 0.3273 -0.0278 -0.0112 0.0111 420 VAL B C 3277 O O . VAL B 91 ? 0.3222 0.3625 0.3801 -0.0282 -0.0107 0.0110 420 VAL B O 3278 C CB . VAL B 91 ? 0.3198 0.3587 0.3734 -0.0324 -0.0105 0.0108 420 VAL B CB 3279 C CG1 . VAL B 91 ? 0.2760 0.3121 0.3268 -0.0332 -0.0107 0.0108 420 VAL B CG1 3280 C CG2 . VAL B 91 ? 0.2744 0.3196 0.3341 -0.0309 -0.0108 0.0112 420 VAL B CG2 3281 N N . TRP B 92 ? 0.2425 0.2818 0.3024 -0.0255 -0.0120 0.0113 421 TRP B N 3282 C CA . TRP B 92 ? 0.2725 0.3157 0.3370 -0.0239 -0.0121 0.0116 421 TRP B CA 3283 C C . TRP B 92 ? 0.2935 0.3352 0.3570 -0.0223 -0.0119 0.0114 421 TRP B C 3284 O O . TRP B 92 ? 0.2224 0.2673 0.2885 -0.0221 -0.0115 0.0116 421 TRP B O 3285 C CB . TRP B 92 ? 0.2371 0.2821 0.3048 -0.0226 -0.0129 0.0118 421 TRP B CB 3286 C CG . TRP B 92 ? 0.3181 0.3656 0.3878 -0.0237 -0.0128 0.0121 421 TRP B CG 3287 C CD1 . TRP B 92 ? 0.2936 0.3402 0.3624 -0.0240 -0.0132 0.0120 421 TRP B CD1 3288 C CD2 . TRP B 92 ? 0.2531 0.3042 0.3253 -0.0242 -0.0123 0.0125 421 TRP B CD2 3289 N NE1 . TRP B 92 ? 0.2224 0.2718 0.2932 -0.0245 -0.0129 0.0122 421 TRP B NE1 3290 C CE2 . TRP B 92 ? 0.2603 0.3124 0.3330 -0.0245 -0.0123 0.0126 421 TRP B CE2 3291 C CE3 . TRP B 92 ? 0.2625 0.3158 0.3362 -0.0241 -0.0117 0.0128 421 TRP B CE3 3292 C CZ2 . TRP B 92 ? 0.2525 0.3075 0.3270 -0.0243 -0.0119 0.0130 421 TRP B CZ2 3293 C CZ3 . TRP B 92 ? 0.2684 0.3246 0.3439 -0.0243 -0.0114 0.0133 421 TRP B CZ3 3294 C CH2 . TRP B 92 ? 0.2906 0.3476 0.3664 -0.0242 -0.0115 0.0134 421 TRP B CH2 3295 N N . THR B 93 ? 0.2659 0.3027 0.3253 -0.0211 -0.0122 0.0111 422 THR B N 3296 C CA . THR B 93 ? 0.2590 0.2937 0.3163 -0.0191 -0.0119 0.0107 422 THR B CA 3297 C C . THR B 93 ? 0.2839 0.3174 0.3388 -0.0211 -0.0109 0.0105 422 THR B C 3298 O O . THR B 93 ? 0.2618 0.2972 0.3181 -0.0202 -0.0104 0.0104 422 THR B O 3299 C CB . THR B 93 ? 0.3073 0.3357 0.3592 -0.0171 -0.0123 0.0105 422 THR B CB 3300 O OG1 . THR B 93 ? 0.3094 0.3395 0.3635 -0.0153 -0.0135 0.0107 422 THR B OG1 3301 C CG2 . THR B 93 ? 0.2678 0.2939 0.3173 -0.0144 -0.0120 0.0101 422 THR B CG2 3302 N N . TYR B 94 ? 0.3241 0.3550 0.3756 -0.0240 -0.0105 0.0103 423 TYR B N 3303 C CA . TYR B 94 ? 0.2939 0.3243 0.3430 -0.0265 -0.0097 0.0099 423 TYR B CA 3304 C C . TYR B 94 ? 0.3329 0.3703 0.3875 -0.0269 -0.0095 0.0103 423 TYR B C 3305 O O . TYR B 94 ? 0.3164 0.3544 0.3707 -0.0267 -0.0090 0.0101 423 TYR B O 3306 C CB . TYR B 94 ? 0.2719 0.3002 0.3172 -0.0302 -0.0094 0.0097 423 TYR B CB 3307 C CG . TYR B 94 ? 0.3692 0.3999 0.4136 -0.0334 -0.0088 0.0093 423 TYR B CG 3308 C CD1 . TYR B 94 ? 0.3869 0.4123 0.4255 -0.0348 -0.0081 0.0086 423 TYR B CD1 3309 C CD2 . TYR B 94 ? 0.3399 0.3780 0.3889 -0.0348 -0.0088 0.0096 423 TYR B CD2 3310 C CE1 . TYR B 94 ? 0.3521 0.3802 0.3898 -0.0381 -0.0076 0.0081 423 TYR B CE1 3311 C CE2 . TYR B 94 ? 0.3778 0.4191 0.4262 -0.0375 -0.0084 0.0093 423 TYR B CE2 3312 C CZ . TYR B 94 ? 0.4210 0.4576 0.4639 -0.0393 -0.0078 0.0085 423 TYR B CZ 3313 O OH . TYR B 94 ? 0.4630 0.5034 0.5053 -0.0423 -0.0075 0.0081 423 TYR B OH 3314 N N . ASN B 95 ? 0.2873 0.3295 0.3462 -0.0272 -0.0099 0.0109 424 ASN B N 3315 C CA . ASN B 95 ? 0.3192 0.3671 0.3825 -0.0273 -0.0097 0.0114 424 ASN B CA 3316 C C . ASN B 95 ? 0.3225 0.3718 0.3882 -0.0252 -0.0095 0.0116 424 ASN B C 3317 O O . ASN B 95 ? 0.3071 0.3586 0.3734 -0.0256 -0.0090 0.0117 424 ASN B O 3318 C CB . ASN B 95 ? 0.2888 0.3402 0.3556 -0.0271 -0.0102 0.0119 424 ASN B CB 3319 C CG . ASN B 95 ? 0.2990 0.3515 0.3644 -0.0293 -0.0101 0.0118 424 ASN B CG 3320 O OD1 . ASN B 95 ? 0.3539 0.4060 0.4164 -0.0315 -0.0096 0.0113 424 ASN B OD1 3321 N ND2 . ASN B 95 ? 0.4037 0.4580 0.4711 -0.0288 -0.0104 0.0121 424 ASN B ND2 3322 N N . ALA B 96 ? 0.2283 0.2767 0.2952 -0.0231 -0.0099 0.0116 425 ALA B N 3323 C CA . ALA B 96 ? 0.2668 0.3174 0.3362 -0.0213 -0.0097 0.0118 425 ALA B CA 3324 C C . ALA B 96 ? 0.3010 0.3493 0.3673 -0.0206 -0.0090 0.0112 425 ALA B C 3325 O O . ALA B 96 ? 0.3029 0.3538 0.3706 -0.0206 -0.0083 0.0114 425 ALA B O 3326 C CB . ALA B 96 ? 0.2369 0.2882 0.3084 -0.0195 -0.0104 0.0117 425 ALA B CB 3327 N N . GLU B 97 ? 0.3242 0.3672 0.3857 -0.0200 -0.0090 0.0106 426 GLU B N 3328 C CA . GLU B 97 ? 0.3281 0.3677 0.3857 -0.0189 -0.0083 0.0099 426 GLU B CA 3329 C C . GLU B 97 ? 0.3796 0.4190 0.4351 -0.0215 -0.0076 0.0097 426 GLU B C 3330 O O . GLU B 97 ? 0.4302 0.4701 0.4851 -0.0208 -0.0069 0.0094 426 GLU B O 3331 C CB . GLU B 97 ? 0.3741 0.4066 0.4257 -0.0175 -0.0085 0.0093 426 GLU B CB 3332 C CG . GLU B 97 ? 0.3995 0.4328 0.4528 -0.0138 -0.0092 0.0094 426 GLU B CG 3333 C CD . GLU B 97 ? 0.5347 0.5603 0.5816 -0.0120 -0.0096 0.0090 426 GLU B CD 3334 O OE1 . GLU B 97 ? 0.6089 0.6277 0.6495 -0.0140 -0.0091 0.0087 426 GLU B OE1 3335 O OE2 . GLU B 97 ? 0.5212 0.5476 0.5689 -0.0088 -0.0103 0.0091 426 GLU B OE2 3336 N N . LEU B 98 ? 0.3197 0.3590 0.3741 -0.0245 -0.0078 0.0098 427 LEU B N 3337 C CA . LEU B 98 ? 0.2939 0.3341 0.3465 -0.0272 -0.0074 0.0095 427 LEU B CA 3338 C C . LEU B 98 ? 0.3088 0.3553 0.3661 -0.0270 -0.0072 0.0102 427 LEU B C 3339 O O . LEU B 98 ? 0.3620 0.4091 0.4180 -0.0275 -0.0067 0.0100 427 LEU B O 3340 C CB . LEU B 98 ? 0.3884 0.4283 0.4391 -0.0304 -0.0076 0.0093 427 LEU B CB 3341 C CG . LEU B 98 ? 0.4700 0.5093 0.5166 -0.0340 -0.0072 0.0086 427 LEU B CG 3342 C CD1 . LEU B 98 ? 0.4253 0.4722 0.4760 -0.0350 -0.0074 0.0091 427 LEU B CD1 3343 C CD2 . LEU B 98 ? 0.4167 0.4499 0.4577 -0.0337 -0.0066 0.0077 427 LEU B CD2 3344 N N . LEU B 99 ? 0.3536 0.4043 0.4159 -0.0262 -0.0077 0.0111 428 LEU B N 3345 C CA . LEU B 99 ? 0.3311 0.3868 0.3972 -0.0259 -0.0075 0.0119 428 LEU B CA 3346 C C . LEU B 99 ? 0.3898 0.4457 0.4562 -0.0243 -0.0068 0.0119 428 LEU B C 3347 O O . LEU B 99 ? 0.3227 0.3807 0.3891 -0.0248 -0.0063 0.0121 428 LEU B O 3348 C CB . LEU B 99 ? 0.2910 0.3493 0.3612 -0.0251 -0.0080 0.0127 428 LEU B CB 3349 C CG . LEU B 99 ? 0.3410 0.4031 0.4140 -0.0247 -0.0077 0.0137 428 LEU B CG 3350 C CD1 . LEU B 99 ? 0.3465 0.4109 0.4183 -0.0260 -0.0078 0.0139 428 LEU B CD1 3351 C CD2 . LEU B 99 ? 0.3307 0.3937 0.4066 -0.0241 -0.0081 0.0144 428 LEU B CD2 3352 N N . VAL B 100 ? 0.3186 0.3728 0.3852 -0.0223 -0.0067 0.0115 429 VAL B N 3353 C CA . VAL B 100 ? 0.3415 0.3969 0.4089 -0.0206 -0.0059 0.0114 429 VAL B CA 3354 C C . VAL B 100 ? 0.3291 0.3819 0.3921 -0.0208 -0.0051 0.0107 429 VAL B C 3355 O O . VAL B 100 ? 0.2885 0.3437 0.3523 -0.0205 -0.0043 0.0108 429 VAL B O 3356 C CB . VAL B 100 ? 0.3311 0.3862 0.3997 -0.0181 -0.0061 0.0111 429 VAL B CB 3357 C CG1 . VAL B 100 ? 0.3202 0.3765 0.3886 -0.0160 -0.0051 0.0106 429 VAL B CG1 3358 C CG2 . VAL B 100 ? 0.3086 0.3674 0.3819 -0.0183 -0.0067 0.0118 429 VAL B CG2 3359 N N . LEU B 101 ? 0.2779 0.3255 0.3360 -0.0215 -0.0052 0.0098 430 LEU B N 3360 C CA . LEU B 101 ? 0.2918 0.3358 0.3447 -0.0221 -0.0045 0.0089 430 LEU B CA 3361 C C . LEU B 101 ? 0.2923 0.3395 0.3455 -0.0247 -0.0044 0.0092 430 LEU B C 3362 O O . LEU B 101 ? 0.2617 0.3093 0.3134 -0.0246 -0.0037 0.0089 430 LEU B O 3363 C CB . LEU B 101 ? 0.2772 0.3139 0.3237 -0.0229 -0.0046 0.0079 430 LEU B CB 3364 C CG . LEU B 101 ? 0.3566 0.3887 0.4010 -0.0198 -0.0047 0.0076 430 LEU B CG 3365 C CD1 . LEU B 101 ? 0.2888 0.3123 0.3257 -0.0211 -0.0048 0.0067 430 LEU B CD1 3366 C CD2 . LEU B 101 ? 0.2530 0.2854 0.2973 -0.0162 -0.0039 0.0072 430 LEU B CD2 3367 N N . LEU B 102 ? 0.3266 0.3763 0.3815 -0.0267 -0.0052 0.0097 431 LEU B N 3368 C CA . LEU B 102 ? 0.3259 0.3796 0.3813 -0.0288 -0.0054 0.0101 431 LEU B CA 3369 C C . LEU B 102 ? 0.3243 0.3824 0.3834 -0.0274 -0.0050 0.0112 431 LEU B C 3370 O O . LEU B 102 ? 0.3691 0.4285 0.4268 -0.0279 -0.0046 0.0111 431 LEU B O 3371 C CB . LEU B 102 ? 0.3109 0.3672 0.3677 -0.0306 -0.0062 0.0105 431 LEU B CB 3372 C CG . LEU B 102 ? 0.4294 0.4914 0.4877 -0.0319 -0.0066 0.0111 431 LEU B CG 3373 C CD1 . LEU B 102 ? 0.3826 0.4443 0.4366 -0.0343 -0.0065 0.0102 431 LEU B CD1 3374 C CD2 . LEU B 102 ? 0.4342 0.4993 0.4944 -0.0329 -0.0074 0.0114 431 LEU B CD2 3375 N N . GLU B 103 ? 0.3466 0.4066 0.4100 -0.0258 -0.0051 0.0120 432 GLU B N 3376 C CA . GLU B 103 ? 0.3431 0.4066 0.4094 -0.0249 -0.0047 0.0131 432 GLU B CA 3377 C C . GLU B 103 ? 0.3458 0.4090 0.4112 -0.0238 -0.0035 0.0128 432 GLU B C 3378 O O . GLU B 103 ? 0.3560 0.4213 0.4216 -0.0239 -0.0030 0.0134 432 GLU B O 3379 C CB . GLU B 103 ? 0.3068 0.3717 0.3772 -0.0240 -0.0050 0.0140 432 GLU B CB 3380 C CG . GLU B 103 ? 0.3731 0.4392 0.4444 -0.0248 -0.0059 0.0146 432 GLU B CG 3381 C CD . GLU B 103 ? 0.5527 0.6213 0.6228 -0.0256 -0.0060 0.0151 432 GLU B CD 3382 O OE1 . GLU B 103 ? 0.6025 0.6725 0.6726 -0.0252 -0.0055 0.0158 432 GLU B OE1 3383 O OE2 . GLU B 103 ? 0.6487 0.7184 0.7177 -0.0267 -0.0067 0.0148 432 GLU B OE2 3384 N N . ASN B 104 ? 0.2384 0.2988 0.3024 -0.0224 -0.0031 0.0118 433 ASN B N 3385 C CA . ASN B 104 ? 0.2823 0.3428 0.3452 -0.0210 -0.0019 0.0113 433 ASN B CA 3386 C C . ASN B 104 ? 0.3239 0.3829 0.3826 -0.0221 -0.0014 0.0108 433 ASN B C 3387 O O . ASN B 104 ? 0.3089 0.3699 0.3675 -0.0217 -0.0005 0.0110 433 ASN B O 3388 C CB . ASN B 104 ? 0.2320 0.2897 0.2937 -0.0186 -0.0016 0.0103 433 ASN B CB 3389 C CG . ASN B 104 ? 0.2891 0.3499 0.3555 -0.0172 -0.0019 0.0108 433 ASN B CG 3390 O OD1 . ASN B 104 ? 0.2798 0.3445 0.3502 -0.0181 -0.0020 0.0118 433 ASN B OD1 3391 N ND2 . ASN B 104 ? 0.2582 0.3169 0.3236 -0.0150 -0.0021 0.0100 433 ASN B ND2 3392 N N . GLU B 105 ? 0.3332 0.3890 0.3881 -0.0238 -0.0021 0.0100 434 GLU B N 3393 C CA . GLU B 105 ? 0.3950 0.4494 0.4454 -0.0255 -0.0018 0.0094 434 GLU B CA 3394 C C . GLU B 105 ? 0.4070 0.4664 0.4594 -0.0266 -0.0020 0.0105 434 GLU B C 3395 O O . GLU B 105 ? 0.3632 0.4231 0.4133 -0.0268 -0.0013 0.0103 434 GLU B O 3396 C CB . GLU B 105 ? 0.3935 0.4441 0.4396 -0.0279 -0.0025 0.0084 434 GLU B CB 3397 C CG . GLU B 105 ? 0.4792 0.5288 0.5204 -0.0304 -0.0024 0.0075 434 GLU B CG 3398 C CD . GLU B 105 ? 0.6370 0.6833 0.6740 -0.0337 -0.0031 0.0065 434 GLU B CD 3399 O OE1 . GLU B 105 ? 0.6455 0.6877 0.6814 -0.0334 -0.0032 0.0062 434 GLU B OE1 3400 O OE2 . GLU B 105 ? 0.6711 0.7194 0.7058 -0.0367 -0.0035 0.0061 434 GLU B OE2 3401 N N . ARG B 106 ? 0.2950 0.3577 0.3510 -0.0270 -0.0029 0.0116 435 ARG B N 3402 C CA . ARG B 106 ? 0.3282 0.3951 0.3854 -0.0275 -0.0032 0.0128 435 ARG B CA 3403 C C . ARG B 106 ? 0.3049 0.3736 0.3645 -0.0260 -0.0023 0.0140 435 ARG B C 3404 O O . ARG B 106 ? 0.2932 0.3639 0.3520 -0.0262 -0.0021 0.0148 435 ARG B O 3405 C CB . ARG B 106 ? 0.3051 0.3746 0.3647 -0.0281 -0.0044 0.0136 435 ARG B CB 3406 C CG . ARG B 106 ? 0.4074 0.4757 0.4649 -0.0301 -0.0052 0.0125 435 ARG B CG 3407 C CD . ARG B 106 ? 0.4711 0.5429 0.5312 -0.0304 -0.0062 0.0132 435 ARG B CD 3408 N NE . ARG B 106 ? 0.5710 0.6477 0.6318 -0.0301 -0.0067 0.0142 435 ARG B NE 3409 C CZ . ARG B 106 ? 0.5462 0.6246 0.6096 -0.0280 -0.0068 0.0157 435 ARG B CZ 3410 N NH1 . ARG B 106 ? 0.4417 0.5179 0.5076 -0.0267 -0.0064 0.0163 435 ARG B NH1 3411 N NH2 . ARG B 106 ? 0.5341 0.6163 0.5971 -0.0274 -0.0072 0.0167 435 ARG B NH2 3412 N N . THR B 107 ? 0.2995 0.3676 0.3618 -0.0247 -0.0017 0.0141 436 THR B N 3413 C CA . THR B 107 ? 0.2716 0.3416 0.3359 -0.0238 -0.0006 0.0150 436 THR B CA 3414 C C . THR B 107 ? 0.2730 0.3428 0.3345 -0.0235 0.0006 0.0144 436 THR B C 3415 O O . THR B 107 ? 0.2727 0.3442 0.3338 -0.0238 0.0013 0.0153 436 THR B O 3416 C CB . THR B 107 ? 0.2725 0.3427 0.3402 -0.0228 -0.0003 0.0149 436 THR B CB 3417 O OG1 . THR B 107 ? 0.2849 0.3554 0.3550 -0.0232 -0.0014 0.0157 436 THR B OG1 3418 C CG2 . THR B 107 ? 0.2271 0.2998 0.2966 -0.0225 0.0011 0.0156 436 THR B CG2 3419 N N . LEU B 108 ? 0.2591 0.3263 0.3181 -0.0229 0.0010 0.0129 437 LEU B N 3420 C CA . LEU B 108 ? 0.3293 0.3958 0.3850 -0.0223 0.0023 0.0121 437 LEU B CA 3421 C C . LEU B 108 ? 0.3292 0.3958 0.3815 -0.0239 0.0020 0.0122 437 LEU B C 3422 O O . LEU B 108 ? 0.2935 0.3612 0.3442 -0.0237 0.0031 0.0124 437 LEU B O 3423 C CB . LEU B 108 ? 0.2641 0.3266 0.3168 -0.0209 0.0027 0.0103 437 LEU B CB 3424 C CG . LEU B 108 ? 0.3233 0.3863 0.3793 -0.0188 0.0029 0.0102 437 LEU B CG 3425 C CD1 . LEU B 108 ? 0.3402 0.3986 0.3922 -0.0166 0.0033 0.0085 437 LEU B CD1 3426 C CD2 . LEU B 108 ? 0.2699 0.3381 0.3301 -0.0179 0.0040 0.0110 437 LEU B CD2 3427 N N . ASP B 109 ? 0.2976 0.3637 0.3486 -0.0256 0.0006 0.0122 438 ASP B N 3428 C CA . ASP B 109 ? 0.3254 0.3930 0.3736 -0.0272 0.0000 0.0124 438 ASP B CA 3429 C C . ASP B 109 ? 0.3200 0.3913 0.3703 -0.0268 0.0000 0.0143 438 ASP B C 3430 O O . ASP B 109 ? 0.3060 0.3783 0.3536 -0.0271 0.0004 0.0146 438 ASP B O 3431 C CB . ASP B 109 ? 0.3450 0.4128 0.3921 -0.0292 -0.0016 0.0119 438 ASP B CB 3432 C CG . ASP B 109 ? 0.4310 0.4940 0.4739 -0.0304 -0.0015 0.0099 438 ASP B CG 3433 O OD1 . ASP B 109 ? 0.4647 0.5243 0.5041 -0.0298 -0.0003 0.0089 438 ASP B OD1 3434 O OD2 . ASP B 109 ? 0.5677 0.6300 0.6103 -0.0320 -0.0025 0.0094 438 ASP B OD2 3435 N N . LEU B 110 ? 0.2281 0.3006 0.2823 -0.0261 -0.0003 0.0155 439 LEU B N 3436 C CA . LEU B 110 ? 0.3091 0.3836 0.3644 -0.0255 -0.0001 0.0174 439 LEU B CA 3437 C C . LEU B 110 ? 0.2926 0.3670 0.3467 -0.0252 0.0016 0.0178 439 LEU B C 3438 O O . LEU B 110 ? 0.2723 0.3476 0.3240 -0.0253 0.0017 0.0187 439 LEU B O 3439 C CB . LEU B 110 ? 0.3059 0.3803 0.3651 -0.0249 -0.0004 0.0184 439 LEU B CB 3440 C CG . LEU B 110 ? 0.3817 0.4564 0.4413 -0.0244 0.0000 0.0204 439 LEU B CG 3441 C CD1 . LEU B 110 ? 0.4204 0.4962 0.4778 -0.0240 -0.0011 0.0216 439 LEU B CD1 3442 C CD2 . LEU B 110 ? 0.3761 0.4497 0.4389 -0.0242 0.0001 0.0209 439 LEU B CD2 3443 N N . HIS B 111 ? 0.2435 0.3174 0.2992 -0.0246 0.0029 0.0170 440 HIS B N 3444 C CA . HIS B 111 ? 0.2677 0.3424 0.3225 -0.0243 0.0048 0.0171 440 HIS B CA 3445 C C . HIS B 111 ? 0.2857 0.3598 0.3358 -0.0246 0.0051 0.0164 440 HIS B C 3446 O O . HIS B 111 ? 0.2978 0.3729 0.3460 -0.0248 0.0060 0.0173 440 HIS B O 3447 C CB . HIS B 111 ? 0.2311 0.3063 0.2883 -0.0233 0.0059 0.0160 440 HIS B CB 3448 C CG . HIS B 111 ? 0.2506 0.3271 0.3122 -0.0233 0.0058 0.0168 440 HIS B CG 3449 N ND1 . HIS B 111 ? 0.2787 0.3563 0.3417 -0.0243 0.0062 0.0184 440 HIS B ND1 3450 C CD2 . HIS B 111 ? 0.2702 0.3467 0.3347 -0.0226 0.0053 0.0160 440 HIS B CD2 3451 C CE1 . HIS B 111 ? 0.2977 0.3760 0.3643 -0.0245 0.0060 0.0185 440 HIS B CE1 3452 N NE2 . HIS B 111 ? 0.2657 0.3437 0.3335 -0.0233 0.0053 0.0171 440 HIS B NE2 3453 N N . ASP B 112 ? 0.2778 0.3499 0.3257 -0.0247 0.0045 0.0147 441 ASP B N 3454 C CA . ASP B 112 ? 0.3155 0.3863 0.3583 -0.0253 0.0047 0.0136 441 ASP B CA 3455 C C . ASP B 112 ? 0.2984 0.3713 0.3394 -0.0264 0.0037 0.0150 441 ASP B C 3456 O O . ASP B 112 ? 0.3408 0.4142 0.3788 -0.0265 0.0046 0.0152 441 ASP B O 3457 C CB . ASP B 112 ? 0.2934 0.3609 0.3336 -0.0260 0.0038 0.0118 441 ASP B CB 3458 C CG . ASP B 112 ? 0.3988 0.4637 0.4329 -0.0268 0.0043 0.0102 441 ASP B CG 3459 O OD1 . ASP B 112 ? 0.3712 0.4370 0.4035 -0.0262 0.0056 0.0104 441 ASP B OD1 3460 O OD2 . ASP B 112 ? 0.4218 0.4835 0.4525 -0.0282 0.0035 0.0088 441 ASP B OD2 3461 N N . ALA B 113 ? 0.1979 0.2722 0.2407 -0.0269 0.0020 0.0158 442 ALA B N 3462 C CA . ALA B 113 ? 0.2729 0.3498 0.3142 -0.0272 0.0009 0.0172 442 ALA B CA 3463 C C . ALA B 113 ? 0.2643 0.3416 0.3055 -0.0262 0.0020 0.0191 442 ALA B C 3464 O O . ALA B 113 ? 0.2598 0.3382 0.2977 -0.0263 0.0020 0.0199 442 ALA B O 3465 C CB . ALA B 113 ? 0.1828 0.2616 0.2263 -0.0273 -0.0010 0.0178 442 ALA B CB 3466 N N . ASN B 114 ? 0.2131 0.2897 0.2577 -0.0256 0.0029 0.0200 443 ASN B N 3467 C CA . ASN B 114 ? 0.2899 0.3662 0.3339 -0.0253 0.0041 0.0218 443 ASN B CA 3468 C C . ASN B 114 ? 0.3214 0.3977 0.3625 -0.0256 0.0060 0.0215 443 ASN B C 3469 O O . ASN B 114 ? 0.3312 0.4074 0.3694 -0.0257 0.0064 0.0230 443 ASN B O 3470 C CB . ASN B 114 ? 0.2516 0.3271 0.2996 -0.0252 0.0048 0.0225 443 ASN B CB 3471 C CG . ASN B 114 ? 0.2565 0.3315 0.3065 -0.0247 0.0032 0.0233 443 ASN B CG 3472 O OD1 . ASN B 114 ? 0.2801 0.3556 0.3282 -0.0241 0.0017 0.0241 443 ASN B OD1 3473 N ND2 . ASN B 114 ? 0.2629 0.3372 0.3165 -0.0249 0.0034 0.0232 443 ASN B ND2 3474 N N . VAL B 115 ? 0.2673 0.3435 0.3088 -0.0256 0.0070 0.0197 444 VAL B N 3475 C CA . VAL B 115 ? 0.2927 0.3691 0.3312 -0.0256 0.0089 0.0191 444 VAL B CA 3476 C C . VAL B 115 ? 0.3608 0.4369 0.3943 -0.0261 0.0080 0.0189 444 VAL B C 3477 O O . VAL B 115 ? 0.3450 0.4215 0.3753 -0.0262 0.0090 0.0198 444 VAL B O 3478 C CB . VAL B 115 ? 0.3064 0.3825 0.3458 -0.0248 0.0101 0.0170 444 VAL B CB 3479 C CG1 . VAL B 115 ? 0.2553 0.3315 0.2908 -0.0245 0.0120 0.0161 444 VAL B CG1 3480 C CG2 . VAL B 115 ? 0.2341 0.3117 0.2784 -0.0243 0.0111 0.0172 444 VAL B CG2 3481 N N . LYS B 116 ? 0.3391 0.4149 0.3719 -0.0265 0.0062 0.0178 445 LYS B N 3482 C CA . LYS B 116 ? 0.3384 0.4148 0.3666 -0.0274 0.0050 0.0175 445 LYS B CA 3483 C C . LYS B 116 ? 0.3470 0.4253 0.3739 -0.0270 0.0042 0.0197 445 LYS B C 3484 O O . LYS B 116 ? 0.3560 0.4348 0.3787 -0.0272 0.0045 0.0201 445 LYS B O 3485 C CB . LYS B 116 ? 0.3479 0.4244 0.3762 -0.0284 0.0031 0.0160 445 LYS B CB 3486 C CG . LYS B 116 ? 0.3477 0.4259 0.3716 -0.0299 0.0016 0.0154 445 LYS B CG 3487 C CD . LYS B 116 ? 0.5135 0.5894 0.5321 -0.0307 0.0028 0.0138 445 LYS B CD 3488 C CE . LYS B 116 ? 0.5697 0.6473 0.5837 -0.0327 0.0011 0.0129 445 LYS B CE 3489 N NZ . LYS B 116 ? 0.6595 0.7382 0.6746 -0.0346 -0.0007 0.0118 445 LYS B NZ 3490 N N . ASN B 117 ? 0.3220 0.4010 0.3520 -0.0262 0.0032 0.0213 446 ASN B N 3491 C CA . ASN B 117 ? 0.3628 0.4427 0.3908 -0.0253 0.0023 0.0236 446 ASN B CA 3492 C C . ASN B 117 ? 0.4011 0.4792 0.4267 -0.0250 0.0043 0.0252 446 ASN B C 3493 O O . ASN B 117 ? 0.4151 0.4933 0.4366 -0.0244 0.0039 0.0267 446 ASN B O 3494 C CB . ASN B 117 ? 0.3145 0.3949 0.3457 -0.0242 0.0009 0.0248 446 ASN B CB 3495 C CG . ASN B 117 ? 0.4041 0.4873 0.4371 -0.0246 -0.0011 0.0234 446 ASN B CG 3496 O OD1 . ASN B 117 ? 0.4305 0.5162 0.4610 -0.0256 -0.0022 0.0223 446 ASN B OD1 3497 N ND2 . ASN B 117 ? 0.3390 0.4218 0.3760 -0.0243 -0.0015 0.0233 446 ASN B ND2 3498 N N . LEU B 118 ? 0.3677 0.4443 0.3957 -0.0255 0.0064 0.0250 447 LEU B N 3499 C CA . LEU B 118 ? 0.3807 0.4559 0.4064 -0.0259 0.0086 0.0262 447 LEU B CA 3500 C C . LEU B 118 ? 0.4066 0.4825 0.4277 -0.0263 0.0094 0.0255 447 LEU B C 3501 O O . LEU B 118 ? 0.4131 0.4882 0.4301 -0.0263 0.0101 0.0271 447 LEU B O 3502 C CB . LEU B 118 ? 0.4050 0.4802 0.4347 -0.0267 0.0106 0.0257 447 LEU B CB 3503 C CG . LEU B 118 ? 0.4267 0.5009 0.4547 -0.0277 0.0130 0.0273 447 LEU B CG 3504 C CD1 . LEU B 118 ? 0.4794 0.5505 0.5056 -0.0276 0.0122 0.0299 447 LEU B CD1 3505 C CD2 . LEU B 118 ? 0.4371 0.5131 0.4696 -0.0286 0.0149 0.0264 447 LEU B CD2 3506 N N . TYR B 119 ? 0.2987 0.3755 0.3199 -0.0266 0.0095 0.0231 448 TYR B N 3507 C CA . TYR B 119 ? 0.3174 0.3943 0.3337 -0.0269 0.0101 0.0220 448 TYR B CA 3508 C C . TYR B 119 ? 0.3445 0.4223 0.3564 -0.0269 0.0081 0.0230 448 TYR B C 3509 O O . TYR B 119 ? 0.3282 0.4058 0.3354 -0.0270 0.0089 0.0237 448 TYR B O 3510 C CB . TYR B 119 ? 0.2756 0.3519 0.2919 -0.0272 0.0102 0.0191 448 TYR B CB 3511 C CG . TYR B 119 ? 0.3347 0.4106 0.3453 -0.0278 0.0099 0.0177 448 TYR B CG 3512 C CD1 . TYR B 119 ? 0.3387 0.4138 0.3457 -0.0277 0.0122 0.0171 448 TYR B CD1 3513 C CD2 . TYR B 119 ? 0.3749 0.4514 0.3834 -0.0288 0.0075 0.0169 448 TYR B CD2 3514 C CE1 . TYR B 119 ? 0.3721 0.4462 0.3732 -0.0284 0.0119 0.0156 448 TYR B CE1 3515 C CE2 . TYR B 119 ? 0.3925 0.4685 0.3954 -0.0299 0.0072 0.0155 448 TYR B CE2 3516 C CZ . TYR B 119 ? 0.4003 0.4748 0.3993 -0.0296 0.0094 0.0148 448 TYR B CZ 3517 O OH . TYR B 119 ? 0.3785 0.4521 0.3714 -0.0308 0.0091 0.0133 448 TYR B OH 3518 N N . GLU B 120 ? 0.3262 0.4054 0.3394 -0.0267 0.0056 0.0230 449 GLU B N 3519 C CA . GLU B 120 ? 0.3806 0.4621 0.3902 -0.0263 0.0034 0.0239 449 GLU B CA 3520 C C . GLU B 120 ? 0.3911 0.4717 0.3984 -0.0249 0.0037 0.0269 449 GLU B C 3521 O O . GLU B 120 ? 0.3986 0.4800 0.4010 -0.0244 0.0031 0.0278 449 GLU B O 3522 C CB . GLU B 120 ? 0.3858 0.4702 0.3983 -0.0262 0.0009 0.0235 449 GLU B CB 3523 C CG . GLU B 120 ? 0.4034 0.4880 0.4169 -0.0281 0.0004 0.0206 449 GLU B CG 3524 C CD . GLU B 120 ? 0.6053 0.6908 0.6136 -0.0298 0.0000 0.0190 449 GLU B CD 3525 O OE1 . GLU B 120 ? 0.6947 0.7831 0.6997 -0.0295 -0.0013 0.0200 449 GLU B OE1 3526 O OE2 . GLU B 120 ? 0.6763 0.7595 0.6836 -0.0313 0.0008 0.0166 449 GLU B OE2 3527 N N . LYS B 121 ? 0.3808 0.4591 0.3910 -0.0242 0.0045 0.0284 450 LYS B N 3528 C CA . LYS B 121 ? 0.4349 0.5107 0.4425 -0.0230 0.0050 0.0312 450 LYS B CA 3529 C C . LYS B 121 ? 0.4837 0.5576 0.4863 -0.0237 0.0071 0.0319 450 LYS B C 3530 O O . LYS B 121 ? 0.4940 0.5665 0.4915 -0.0227 0.0068 0.0340 450 LYS B O 3531 C CB . LYS B 121 ? 0.5023 0.5753 0.5139 -0.0230 0.0060 0.0321 450 LYS B CB 3532 C CG . LYS B 121 ? 0.6106 0.6798 0.6196 -0.0216 0.0058 0.0350 450 LYS B CG 3533 C CD . LYS B 121 ? 0.6936 0.7603 0.7069 -0.0221 0.0066 0.0352 450 LYS B CD 3534 C CE . LYS B 121 ? 0.8648 0.9256 0.8741 -0.0218 0.0076 0.0380 450 LYS B CE 3535 N NZ . LYS B 121 ? 0.7715 0.8298 0.7766 -0.0236 0.0101 0.0390 450 LYS B NZ 3536 N N . VAL B 122 ? 0.3291 0.4033 0.3330 -0.0253 0.0093 0.0302 451 VAL B N 3537 C CA . VAL B 122 ? 0.3793 0.4524 0.3788 -0.0262 0.0116 0.0305 451 VAL B CA 3538 C C . VAL B 122 ? 0.3987 0.4734 0.3931 -0.0260 0.0106 0.0297 451 VAL B C 3539 O O . VAL B 122 ? 0.3986 0.4722 0.3875 -0.0258 0.0111 0.0312 451 VAL B O 3540 C CB . VAL B 122 ? 0.3809 0.4545 0.3837 -0.0275 0.0144 0.0289 451 VAL B CB 3541 C CG1 . VAL B 122 ? 0.2682 0.3417 0.2665 -0.0282 0.0168 0.0288 451 VAL B CG1 3542 C CG2 . VAL B 122 ? 0.3502 0.4225 0.3570 -0.0280 0.0156 0.0301 451 VAL B CG2 3543 N N . LYS B 123 ? 0.4096 0.4866 0.4054 -0.0264 0.0092 0.0272 452 LYS B N 3544 C CA . LYS B 123 ? 0.4232 0.5017 0.4140 -0.0268 0.0080 0.0261 452 LYS B CA 3545 C C . LYS B 123 ? 0.4479 0.5279 0.4350 -0.0255 0.0057 0.0282 452 LYS B C 3546 O O . LYS B 123 ? 0.4742 0.5547 0.4556 -0.0255 0.0055 0.0286 452 LYS B O 3547 C CB . LYS B 123 ? 0.3528 0.4330 0.3456 -0.0278 0.0065 0.0233 452 LYS B CB 3548 C CG . LYS B 123 ? 0.4103 0.4922 0.3978 -0.0288 0.0050 0.0219 452 LYS B CG 3549 C CD . LYS B 123 ? 0.5564 0.6404 0.5456 -0.0302 0.0028 0.0197 452 LYS B CD 3550 C CE . LYS B 123 ? 0.6594 0.7407 0.6466 -0.0319 0.0040 0.0166 452 LYS B CE 3551 N NZ . LYS B 123 ? 0.6768 0.7570 0.6571 -0.0327 0.0049 0.0157 452 LYS B NZ 3552 N N . SER B 124 ? 0.4203 0.5010 0.4102 -0.0240 0.0039 0.0297 453 SER B N 3553 C CA . SER B 124 ? 0.4245 0.5072 0.4112 -0.0220 0.0015 0.0317 453 SER B CA 3554 C C . SER B 124 ? 0.4289 0.5079 0.4099 -0.0208 0.0028 0.0346 453 SER B C 3555 O O . SER B 124 ? 0.4237 0.5041 0.3997 -0.0193 0.0012 0.0359 453 SER B O 3556 C CB . SER B 124 ? 0.4212 0.5051 0.4123 -0.0204 -0.0003 0.0326 453 SER B CB 3557 O OG . SER B 124 ? 0.4828 0.5690 0.4707 -0.0177 -0.0027 0.0345 453 SER B OG 3558 N N . GLN B 125 ? 0.4122 0.4867 0.3939 -0.0216 0.0056 0.0355 454 GLN B N 3559 C CA . GLN B 125 ? 0.4545 0.5246 0.4303 -0.0211 0.0072 0.0381 454 GLN B CA 3560 C C . GLN B 125 ? 0.4997 0.5700 0.4704 -0.0224 0.0088 0.0374 454 GLN B C 3561 O O . GLN B 125 ? 0.4906 0.5593 0.4547 -0.0214 0.0085 0.0394 454 GLN B O 3562 C CB . GLN B 125 ? 0.4171 0.4828 0.3953 -0.0223 0.0099 0.0391 454 GLN B CB 3563 C CG . GLN B 125 ? 0.4463 0.5099 0.4276 -0.0209 0.0088 0.0404 454 GLN B CG 3564 C CD . GLN B 125 ? 0.5056 0.5642 0.4875 -0.0226 0.0115 0.0417 454 GLN B CD 3565 O OE1 . GLN B 125 ? 0.5607 0.6139 0.5372 -0.0222 0.0122 0.0443 454 GLN B OE1 3566 N NE2 . GLN B 125 ? 0.4368 0.4971 0.4249 -0.0247 0.0129 0.0398 454 GLN B NE2 3567 N N . LEU B 126 ? 0.4676 0.5396 0.4409 -0.0244 0.0103 0.0347 455 LEU B N 3568 C CA . LEU B 126 ? 0.5313 0.6030 0.5000 -0.0257 0.0124 0.0339 455 LEU B CA 3569 C C . LEU B 126 ? 0.5387 0.6130 0.5024 -0.0250 0.0099 0.0334 455 LEU B C 3570 O O . LEU B 126 ? 0.5587 0.6319 0.5160 -0.0244 0.0100 0.0351 455 LEU B O 3571 C CB . LEU B 126 ? 0.4492 0.5216 0.4219 -0.0273 0.0149 0.0313 455 LEU B CB 3572 C CG . LEU B 126 ? 0.4427 0.5137 0.4206 -0.0279 0.0171 0.0320 455 LEU B CG 3573 C CD1 . LEU B 126 ? 0.3996 0.4722 0.3808 -0.0289 0.0196 0.0294 455 LEU B CD1 3574 C CD2 . LEU B 126 ? 0.4099 0.4775 0.3839 -0.0284 0.0188 0.0350 455 LEU B CD2 3575 N N . ARG B 127 ? 0.6003 0.6781 0.5668 -0.0252 0.0075 0.0312 456 ARG B N 3576 C CA . ARG B 127 ? 0.6022 0.6835 0.5648 -0.0256 0.0053 0.0299 456 ARG B CA 3577 C C . ARG B 127 ? 0.6321 0.7118 0.5892 -0.0269 0.0075 0.0286 456 ARG B C 3578 O O . ARG B 127 ? 0.6512 0.7293 0.6101 -0.0282 0.0099 0.0266 456 ARG B O 3579 C CB . ARG B 127 ? 0.6213 0.7049 0.5804 -0.0233 0.0024 0.0323 456 ARG B CB 3580 C CG . ARG B 127 ? 0.6516 0.7316 0.6102 -0.0210 0.0029 0.0358 456 ARG B CG 3581 C CD . ARG B 127 ? 0.6696 0.7526 0.6288 -0.0182 -0.0004 0.0374 456 ARG B CD 3582 N NE . ARG B 127 ? 0.8214 0.9092 0.7758 -0.0172 -0.0031 0.0374 456 ARG B NE 3583 C CZ . ARG B 127 ? 0.7633 0.8559 0.7179 -0.0146 -0.0064 0.0384 456 ARG B CZ 3584 N NH1 . ARG B 127 ? 0.6910 0.7836 0.6502 -0.0126 -0.0072 0.0394 456 ARG B NH1 3585 N NH2 . ARG B 127 ? 0.7739 0.8719 0.7242 -0.0140 -0.0088 0.0382 456 ARG B NH2 3586 N N . ASP B 128 ? 0.6798 0.7601 0.6301 -0.0264 0.0066 0.0298 457 ASP B N 3587 C CA . ASP B 128 ? 0.7072 0.7864 0.6515 -0.0277 0.0084 0.0285 457 ASP B CA 3588 C C . ASP B 128 ? 0.6584 0.7339 0.6029 -0.0282 0.0125 0.0287 457 ASP B C 3589 O O . ASP B 128 ? 0.6887 0.7636 0.6318 -0.0294 0.0146 0.0264 457 ASP B O 3590 C CB . ASP B 128 ? 0.7276 0.8073 0.6644 -0.0265 0.0071 0.0308 457 ASP B CB 3591 C CG . ASP B 128 ? 0.8282 0.9130 0.7630 -0.0264 0.0032 0.0299 457 ASP B CG 3592 O OD1 . ASP B 128 ? 0.8375 0.9239 0.7699 -0.0285 0.0027 0.0271 457 ASP B OD1 3593 O OD2 . ASP B 128 ? 0.9621 1.0493 0.8973 -0.0242 0.0006 0.0321 457 ASP B OD2 3594 N N . ASN B 129 ? 0.4976 0.5709 0.4435 -0.0274 0.0138 0.0315 458 ASN B N 3595 C CA . ASN B 129 ? 0.5125 0.5831 0.4574 -0.0283 0.0177 0.0323 458 ASN B CA 3596 C C . ASN B 129 ? 0.4629 0.5340 0.4129 -0.0294 0.0205 0.0298 458 ASN B C 3597 O O . ASN B 129 ? 0.4987 0.5690 0.4478 -0.0302 0.0239 0.0300 458 ASN B O 3598 C CB . ASN B 129 ? 0.4724 0.5399 0.4174 -0.0276 0.0183 0.0359 458 ASN B CB 3599 C CG . ASN B 129 ? 0.5340 0.5996 0.4715 -0.0261 0.0166 0.0387 458 ASN B CG 3600 O OD1 . ASN B 129 ? 0.5253 0.5925 0.4575 -0.0258 0.0152 0.0381 458 ASN B OD1 3601 N ND2 . ASN B 129 ? 0.5260 0.5877 0.4623 -0.0252 0.0167 0.0418 458 ASN B ND2 3602 N N . ALA B 130 ? 0.4593 0.5321 0.4144 -0.0293 0.0190 0.0274 459 ALA B N 3603 C CA . ALA B 130 ? 0.4875 0.5607 0.4470 -0.0297 0.0213 0.0249 459 ALA B CA 3604 C C . ALA B 130 ? 0.4869 0.5604 0.4463 -0.0298 0.0199 0.0217 459 ALA B C 3605 O O . ALA B 130 ? 0.5151 0.5895 0.4737 -0.0301 0.0167 0.0214 459 ALA B O 3606 C CB . ALA B 130 ? 0.4323 0.5057 0.3993 -0.0295 0.0218 0.0258 459 ALA B CB 3607 N N . ASN B 131 ? 0.4526 0.5256 0.4127 -0.0297 0.0222 0.0192 460 ASN B N 3608 C CA . ASN B 131 ? 0.4656 0.5373 0.4249 -0.0299 0.0213 0.0160 460 ASN B CA 3609 C C . ASN B 131 ? 0.4826 0.5542 0.4488 -0.0293 0.0212 0.0149 460 ASN B C 3610 O O . ASN B 131 ? 0.4824 0.5547 0.4527 -0.0283 0.0236 0.0150 460 ASN B O 3611 C CB . ASN B 131 ? 0.4677 0.5377 0.4217 -0.0296 0.0241 0.0138 460 ASN B CB 3612 C CG . ASN B 131 ? 0.6006 0.6677 0.5519 -0.0298 0.0233 0.0103 460 ASN B CG 3613 O OD1 . ASN B 131 ? 0.6457 0.7123 0.5962 -0.0311 0.0203 0.0097 460 ASN B OD1 3614 N ND2 . ASN B 131 ? 0.5564 0.6214 0.5057 -0.0285 0.0261 0.0081 460 ASN B ND2 3615 N N . ASP B 132 ? 0.5332 0.6043 0.5007 -0.0299 0.0184 0.0138 461 ASP B N 3616 C CA . ASP B 132 ? 0.4730 0.5434 0.4463 -0.0294 0.0180 0.0127 461 ASP B CA 3617 C C . ASP B 132 ? 0.4881 0.5552 0.4590 -0.0288 0.0196 0.0095 461 ASP B C 3618 O O . ASP B 132 ? 0.5151 0.5795 0.4803 -0.0300 0.0186 0.0075 461 ASP B O 3619 C CB . ASP B 132 ? 0.4703 0.5416 0.4452 -0.0306 0.0145 0.0129 461 ASP B CB 3620 C CG . ASP B 132 ? 0.5095 0.5804 0.4908 -0.0302 0.0139 0.0124 461 ASP B CG 3621 O OD1 . ASP B 132 ? 0.4834 0.5528 0.4671 -0.0290 0.0159 0.0112 461 ASP B OD1 3622 O OD2 . ASP B 132 ? 0.4752 0.5478 0.4590 -0.0309 0.0113 0.0131 461 ASP B OD2 3623 N N . LEU B 133 ? 0.4961 0.5631 0.4708 -0.0270 0.0219 0.0090 462 LEU B N 3624 C CA . LEU B 133 ? 0.5182 0.5818 0.4902 -0.0255 0.0236 0.0061 462 LEU B CA 3625 C C . LEU B 133 ? 0.5671 0.6273 0.5405 -0.0255 0.0220 0.0043 462 LEU B C 3626 O O . LEU B 133 ? 0.5843 0.6403 0.5546 -0.0241 0.0231 0.0019 462 LEU B O 3627 C CB . LEU B 133 ? 0.5436 0.6097 0.5188 -0.0231 0.0270 0.0062 462 LEU B CB 3628 C CG . LEU B 133 ? 0.6348 0.7042 0.6083 -0.0234 0.0291 0.0078 462 LEU B CG 3629 C CD1 . LEU B 133 ? 0.6051 0.6782 0.5824 -0.0215 0.0325 0.0078 462 LEU B CD1 3630 C CD2 . LEU B 133 ? 0.5765 0.6430 0.5412 -0.0239 0.0296 0.0065 462 LEU B CD2 3631 N N . GLY B 134 ? 0.5172 0.5788 0.4948 -0.0269 0.0193 0.0056 463 GLY B N 3632 C CA . GLY B 134 ? 0.5334 0.5920 0.5122 -0.0274 0.0177 0.0042 463 GLY B CA 3633 C C . GLY B 134 ? 0.5474 0.6060 0.5320 -0.0251 0.0188 0.0041 463 GLY B C 3634 O O . GLY B 134 ? 0.5503 0.6051 0.5347 -0.0249 0.0180 0.0025 463 GLY B O 3635 N N . ASN B 135 ? 0.4979 0.5608 0.4874 -0.0236 0.0205 0.0057 464 ASN B N 3636 C CA . ASN B 135 ? 0.4735 0.5377 0.4690 -0.0214 0.0215 0.0057 464 ASN B CA 3637 C C . ASN B 135 ? 0.4294 0.4989 0.4317 -0.0219 0.0214 0.0084 464 ASN B C 3638 O O . ASN B 135 ? 0.3590 0.4313 0.3662 -0.0204 0.0229 0.0087 464 ASN B O 3639 C CB . ASN B 135 ? 0.4385 0.5024 0.4321 -0.0185 0.0245 0.0041 464 ASN B CB 3640 C CG . ASN B 135 ? 0.5552 0.6233 0.5481 -0.0185 0.0268 0.0052 464 ASN B CG 3641 O OD1 . ASN B 135 ? 0.5356 0.6050 0.5272 -0.0207 0.0261 0.0069 464 ASN B OD1 3642 N ND2 . ASN B 135 ? 0.4532 0.5235 0.4466 -0.0158 0.0296 0.0042 464 ASN B ND2 3643 N N . GLY B 136 ? 0.3984 0.4691 0.4007 -0.0239 0.0197 0.0103 465 GLY B N 3644 C CA . GLY B 136 ? 0.3898 0.4639 0.3971 -0.0245 0.0196 0.0129 465 GLY B CA 3645 C C . GLY B 136 ? 0.4289 0.5054 0.4347 -0.0248 0.0220 0.0143 465 GLY B C 3646 O O . GLY B 136 ? 0.4346 0.5131 0.4434 -0.0255 0.0223 0.0165 465 GLY B O 3647 N N . CYS B 137 ? 0.4460 0.5218 0.4467 -0.0243 0.0237 0.0130 466 CYS B N 3648 C CA . CYS B 137 ? 0.4360 0.5141 0.4348 -0.0247 0.0261 0.0143 466 CYS B CA 3649 C C . CYS B 137 ? 0.4817 0.5583 0.4741 -0.0259 0.0253 0.0152 466 CYS B C 3650 O O . CYS B 137 ? 0.4963 0.5703 0.4841 -0.0260 0.0240 0.0137 466 CYS B O 3651 C CB . CYS B 137 ? 0.4668 0.5465 0.4650 -0.0228 0.0292 0.0124 466 CYS B CB 3652 S SG . CYS B 137 ? 0.6334 0.7175 0.6396 -0.0213 0.0307 0.0120 466 CYS B SG 3653 N N . PHE B 138 ? 0.3766 0.4545 0.3683 -0.0270 0.0262 0.0177 467 PHE B N 3654 C CA . PHE B 138 ? 0.4074 0.4840 0.3926 -0.0279 0.0255 0.0189 467 PHE B CA 3655 C C . PHE B 138 ? 0.4203 0.4981 0.4021 -0.0282 0.0288 0.0194 467 PHE B C 3656 O O . PHE B 138 ? 0.4206 0.5004 0.4051 -0.0289 0.0308 0.0209 467 PHE B O 3657 C CB . PHE B 138 ? 0.3898 0.4658 0.3757 -0.0286 0.0233 0.0217 467 PHE B CB 3658 C CG . PHE B 138 ? 0.3932 0.4688 0.3821 -0.0284 0.0201 0.0213 467 PHE B CG 3659 C CD1 . PHE B 138 ? 0.4358 0.5119 0.4312 -0.0281 0.0195 0.0216 467 PHE B CD1 3660 C CD2 . PHE B 138 ? 0.4320 0.5071 0.4171 -0.0286 0.0175 0.0206 467 PHE B CD2 3661 C CE1 . PHE B 138 ? 0.3680 0.4440 0.3660 -0.0279 0.0167 0.0212 467 PHE B CE1 3662 C CE2 . PHE B 138 ? 0.4876 0.5631 0.4754 -0.0286 0.0147 0.0201 467 PHE B CE2 3663 C CZ . PHE B 138 ? 0.4136 0.4895 0.4079 -0.0282 0.0143 0.0205 467 PHE B CZ 3664 N N . GLU B 139 ? 0.5399 0.6166 0.5155 -0.0280 0.0294 0.0180 468 GLU B N 3665 C CA . GLU B 139 ? 0.5394 0.6171 0.5108 -0.0284 0.0325 0.0186 468 GLU B CA 3666 C C . GLU B 139 ? 0.5131 0.5892 0.4790 -0.0296 0.0314 0.0211 468 GLU B C 3667 O O . GLU B 139 ? 0.6077 0.6821 0.5692 -0.0296 0.0290 0.0208 468 GLU B O 3668 C CB . GLU B 139 ? 0.5261 0.6032 0.4931 -0.0272 0.0341 0.0156 468 GLU B CB 3669 C CG . GLU B 139 ? 0.6727 0.7518 0.6441 -0.0253 0.0364 0.0134 468 GLU B CG 3670 C CD . GLU B 139 ? 0.8986 0.9763 0.8646 -0.0235 0.0382 0.0105 468 GLU B CD 3671 O OE1 . GLU B 139 ? 0.8783 0.9531 0.8371 -0.0242 0.0377 0.0101 468 GLU B OE1 3672 O OE2 . GLU B 139 ? 0.9091 0.9885 0.8778 -0.0213 0.0403 0.0087 468 GLU B OE2 3673 N N . PHE B 140 ? 0.3832 0.4600 0.3490 -0.0308 0.0333 0.0237 469 PHE B N 3674 C CA . PHE B 140 ? 0.4651 0.5396 0.4252 -0.0316 0.0324 0.0265 469 PHE B CA 3675 C C . PHE B 140 ? 0.5340 0.6078 0.4861 -0.0317 0.0336 0.0260 469 PHE B C 3676 O O . PHE B 140 ? 0.4890 0.5644 0.4399 -0.0318 0.0367 0.0244 469 PHE B O 3677 C CB . PHE B 140 ? 0.4792 0.5534 0.4405 -0.0332 0.0344 0.0292 469 PHE B CB 3678 C CG . PHE B 140 ? 0.4207 0.4943 0.3880 -0.0333 0.0327 0.0304 469 PHE B CG 3679 C CD1 . PHE B 140 ? 0.4372 0.5074 0.4024 -0.0329 0.0300 0.0328 469 PHE B CD1 3680 C CD2 . PHE B 140 ? 0.3553 0.4318 0.3300 -0.0335 0.0339 0.0291 469 PHE B CD2 3681 C CE1 . PHE B 140 ? 0.4395 0.5088 0.4098 -0.0328 0.0286 0.0338 469 PHE B CE1 3682 C CE2 . PHE B 140 ? 0.3602 0.4359 0.3400 -0.0337 0.0323 0.0301 469 PHE B CE2 3683 C CZ . PHE B 140 ? 0.3670 0.4388 0.3445 -0.0334 0.0297 0.0324 469 PHE B CZ 3684 N N . TRP B 141 ? 0.4829 0.5547 0.4294 -0.0316 0.0310 0.0272 470 TRP B N 3685 C CA . TRP B 141 ? 0.5733 0.6441 0.5115 -0.0318 0.0318 0.0272 470 TRP B CA 3686 C C . TRP B 141 ? 0.6242 0.6935 0.5584 -0.0329 0.0340 0.0304 470 TRP B C 3687 O O . TRP B 141 ? 0.6855 0.7534 0.6121 -0.0331 0.0344 0.0313 470 TRP B O 3688 C CB . TRP B 141 ? 0.5867 0.6567 0.5204 -0.0312 0.0280 0.0271 470 TRP B CB 3689 C CG . TRP B 141 ? 0.5831 0.6540 0.5187 -0.0310 0.0262 0.0237 470 TRP B CG 3690 C CD1 . TRP B 141 ? 0.5372 0.6089 0.4762 -0.0307 0.0227 0.0231 470 TRP B CD1 3691 C CD2 . TRP B 141 ? 0.6208 0.6914 0.5545 -0.0310 0.0280 0.0204 470 TRP B CD2 3692 N NE1 . TRP B 141 ? 0.5178 0.5892 0.4567 -0.0310 0.0222 0.0197 470 TRP B NE1 3693 C CE2 . TRP B 141 ? 0.5371 0.6074 0.4726 -0.0310 0.0254 0.0180 470 TRP B CE2 3694 C CE3 . TRP B 141 ? 0.6322 0.7025 0.5625 -0.0309 0.0316 0.0192 470 TRP B CE3 3695 C CZ2 . TRP B 141 ? 0.5489 0.6175 0.4822 -0.0310 0.0264 0.0145 470 TRP B CZ2 3696 C CZ3 . TRP B 141 ? 0.6727 0.7419 0.6011 -0.0303 0.0326 0.0157 470 TRP B CZ3 3697 C CH2 . TRP B 141 ? 0.6158 0.6837 0.5454 -0.0304 0.0299 0.0134 470 TRP B CH2 3698 N N . HIS B 142 ? 0.5670 0.6362 0.5058 -0.0338 0.0354 0.0321 471 HIS B N 3699 C CA . HIS B 142 ? 0.5652 0.6321 0.4999 -0.0355 0.0377 0.0351 471 HIS B CA 3700 C C . HIS B 142 ? 0.6010 0.6699 0.5416 -0.0373 0.0408 0.0353 471 HIS B C 3701 O O . HIS B 142 ? 0.5900 0.6622 0.5382 -0.0368 0.0408 0.0332 471 HIS B O 3702 C CB . HIS B 142 ? 0.5548 0.6172 0.4858 -0.0348 0.0349 0.0383 471 HIS B CB 3703 C CG . HIS B 142 ? 0.5494 0.6113 0.4870 -0.0343 0.0328 0.0390 471 HIS B CG 3704 N ND1 . HIS B 142 ? 0.5606 0.6209 0.5012 -0.0359 0.0346 0.0406 471 HIS B ND1 3705 C CD2 . HIS B 142 ? 0.5517 0.6145 0.4930 -0.0324 0.0291 0.0382 471 HIS B CD2 3706 C CE1 . HIS B 142 ? 0.5193 0.5791 0.4652 -0.0348 0.0320 0.0407 471 HIS B CE1 3707 N NE2 . HIS B 142 ? 0.5103 0.5718 0.4568 -0.0326 0.0288 0.0393 471 HIS B NE2 3708 N N . LYS B 143 ? 0.6544 0.7213 0.5913 -0.0396 0.0434 0.0377 472 LYS B N 3709 C CA . LYS B 143 ? 0.6198 0.6891 0.5619 -0.0421 0.0464 0.0381 472 LYS B CA 3710 C C . LYS B 143 ? 0.6206 0.6868 0.5665 -0.0425 0.0443 0.0398 472 LYS B C 3711 O O . LYS B 143 ? 0.5883 0.6483 0.5289 -0.0424 0.0427 0.0427 472 LYS B O 3712 C CB . LYS B 143 ? 0.6686 0.7372 0.6050 -0.0451 0.0503 0.0398 472 LYS B CB 3713 C CG . LYS B 143 ? 0.6542 0.7283 0.5899 -0.0452 0.0536 0.0374 472 LYS B CG 3714 C CD . LYS B 143 ? 0.8380 0.9195 0.7827 -0.0457 0.0559 0.0350 472 LYS B CD 3715 C CE . LYS B 143 ? 0.9243 1.0105 0.8708 -0.0428 0.0564 0.0314 472 LYS B CE 3716 N NZ . LYS B 143 ? 0.9950 1.0812 0.9338 -0.0427 0.0587 0.0310 472 LYS B NZ 3717 N N . CYS B 144 ? 0.5775 0.6475 0.5319 -0.0426 0.0444 0.0381 473 CYS B N 3718 C CA . CYS B 144 ? 0.5325 0.5999 0.4909 -0.0431 0.0427 0.0395 473 CYS B CA 3719 C C . CYS B 144 ? 0.5420 0.6122 0.5047 -0.0464 0.0458 0.0397 473 CYS B C 3720 O O . CYS B 144 ? 0.5594 0.6359 0.5296 -0.0463 0.0467 0.0373 473 CYS B O 3721 C CB . CYS B 144 ? 0.5023 0.5716 0.4671 -0.0403 0.0394 0.0374 473 CYS B CB 3722 S SG . CYS B 144 ? 0.6562 0.7206 0.6233 -0.0397 0.0361 0.0394 473 CYS B SG 3723 N N . ASP B 145 ? 0.5259 0.5915 0.4834 -0.0496 0.0476 0.0425 474 ASP B N 3724 C CA . ASP B 145 ? 0.5528 0.6208 0.5137 -0.0537 0.0505 0.0428 474 ASP B CA 3725 C C . ASP B 145 ? 0.5220 0.5889 0.4891 -0.0538 0.0485 0.0428 474 ASP B C 3726 O O . ASP B 145 ? 0.5334 0.5988 0.5030 -0.0504 0.0450 0.0422 474 ASP B O 3727 C CB . ASP B 145 ? 0.5357 0.5982 0.4881 -0.0576 0.0532 0.0458 474 ASP B CB 3728 C CG . ASP B 145 ? 0.6268 0.6783 0.5715 -0.0568 0.0508 0.0490 474 ASP B CG 3729 O OD1 . ASP B 145 ? 0.6356 0.6845 0.5830 -0.0540 0.0473 0.0491 474 ASP B OD1 3730 O OD2 . ASP B 145 ? 0.6301 0.6757 0.5657 -0.0588 0.0525 0.0515 474 ASP B OD2 3731 N N . ASN B 146 ? 0.4722 0.5401 0.4415 -0.0579 0.0507 0.0434 475 ASN B N 3732 C CA . ASN B 146 ? 0.4391 0.5065 0.4143 -0.0584 0.0491 0.0432 475 ASN B CA 3733 C C . ASN B 146 ? 0.4958 0.5535 0.4670 -0.0567 0.0458 0.0454 475 ASN B C 3734 O O . ASN B 146 ? 0.4888 0.5466 0.4654 -0.0548 0.0433 0.0445 475 ASN B O 3735 C CB . ASN B 146 ? 0.4036 0.4737 0.3807 -0.0639 0.0522 0.0435 475 ASN B CB 3736 C CG . ASN B 146 ? 0.4025 0.4846 0.3866 -0.0649 0.0549 0.0408 475 ASN B CG 3737 O OD1 . ASN B 146 ? 0.3543 0.4418 0.3414 -0.0611 0.0544 0.0387 475 ASN B OD1 3738 N ND2 . ASN B 146 ? 0.4106 0.4970 0.3970 -0.0699 0.0577 0.0409 475 ASN B ND2 3739 N N . GLU B 147 ? 0.5380 0.5874 0.4995 -0.0571 0.0460 0.0482 476 GLU B N 3740 C CA . GLU B 147 ? 0.5667 0.6068 0.5235 -0.0548 0.0430 0.0504 476 GLU B CA 3741 C C . GLU B 147 ? 0.5566 0.5977 0.5143 -0.0493 0.0393 0.0496 476 GLU B C 3742 O O . GLU B 147 ? 0.5251 0.5629 0.4839 -0.0466 0.0363 0.0500 476 GLU B O 3743 C CB . GLU B 147 ? 0.5483 0.5784 0.4936 -0.0568 0.0444 0.0538 476 GLU B CB 3744 C CG . GLU B 147 ? 0.6117 0.6374 0.5549 -0.0624 0.0472 0.0551 476 GLU B CG 3745 C CD . GLU B 147 ? 0.8587 0.8732 0.7893 -0.0646 0.0488 0.0586 476 GLU B CD 3746 O OE1 . GLU B 147 ? 0.8364 0.8475 0.7600 -0.0618 0.0481 0.0600 476 GLU B OE1 3747 O OE2 . GLU B 147 ? 0.8005 0.8091 0.7276 -0.0693 0.0508 0.0600 476 GLU B OE2 3748 N N . CYS B 148 ? 0.4979 0.5436 0.4548 -0.0479 0.0397 0.0483 477 CYS B N 3749 C CA . CYS B 148 ? 0.5115 0.5595 0.4697 -0.0436 0.0365 0.0470 477 CYS B CA 3750 C C . CYS B 148 ? 0.5379 0.5915 0.5060 -0.0423 0.0348 0.0442 477 CYS B C 3751 O O . CYS B 148 ? 0.5222 0.5751 0.4921 -0.0393 0.0315 0.0440 477 CYS B O 3752 C CB . CYS B 148 ? 0.5086 0.5602 0.4637 -0.0431 0.0377 0.0459 477 CYS B CB 3753 S SG . CYS B 148 ? 0.6449 0.7000 0.6014 -0.0387 0.0340 0.0437 477 CYS B SG 3754 N N . MET B 149 ? 0.5456 0.6052 0.5198 -0.0444 0.0372 0.0423 478 MET B N 3755 C CA . MET B 149 ? 0.5402 0.6047 0.5235 -0.0433 0.0359 0.0398 478 MET B CA 3756 C C . MET B 149 ? 0.5538 0.6140 0.5391 -0.0431 0.0338 0.0410 478 MET B C 3757 O O . MET B 149 ? 0.5209 0.5818 0.5101 -0.0405 0.0309 0.0400 478 MET B O 3758 C CB . MET B 149 ? 0.4614 0.5329 0.4503 -0.0456 0.0390 0.0380 478 MET B CB 3759 C CG . MET B 149 ? 0.5206 0.5976 0.5092 -0.0448 0.0409 0.0360 478 MET B CG 3760 S SD . MET B 149 ? 0.5252 0.6037 0.5154 -0.0403 0.0379 0.0334 478 MET B SD 3761 C CE . MET B 149 ? 0.4229 0.5072 0.4121 -0.0399 0.0411 0.0311 478 MET B CE 3762 N N . GLU B 150 ? 0.4936 0.5490 0.4756 -0.0460 0.0353 0.0432 479 GLU B N 3763 C CA . GLU B 150 ? 0.5120 0.5625 0.4951 -0.0461 0.0336 0.0443 479 GLU B CA 3764 C C . GLU B 150 ? 0.5435 0.5884 0.5225 -0.0423 0.0303 0.0458 479 GLU B C 3765 O O . GLU B 150 ? 0.5469 0.5902 0.5290 -0.0406 0.0280 0.0457 479 GLU B O 3766 C CB . GLU B 150 ? 0.4963 0.5418 0.4754 -0.0506 0.0363 0.0463 479 GLU B CB 3767 C CG . GLU B 150 ? 0.6105 0.6520 0.5919 -0.0517 0.0353 0.0468 479 GLU B CG 3768 C CD . GLU B 150 ? 0.7365 0.7859 0.7283 -0.0515 0.0346 0.0440 479 GLU B CD 3769 O OE1 . GLU B 150 ? 0.7186 0.7657 0.7131 -0.0497 0.0321 0.0439 479 GLU B OE1 3770 O OE2 . GLU B 150 ? 0.6396 0.6973 0.6365 -0.0530 0.0365 0.0421 479 GLU B OE2 3771 N N . SER B 151 ? 0.5050 0.5473 0.4770 -0.0407 0.0300 0.0471 480 SER B N 3772 C CA . SER B 151 ? 0.4951 0.5334 0.4630 -0.0367 0.0267 0.0485 480 SER B CA 3773 C C . SER B 151 ? 0.4854 0.5299 0.4597 -0.0337 0.0239 0.0461 480 SER B C 3774 O O . SER B 151 ? 0.5055 0.5486 0.4806 -0.0310 0.0211 0.0465 480 SER B O 3775 C CB . SER B 151 ? 0.4634 0.4982 0.4220 -0.0357 0.0270 0.0505 480 SER B CB 3776 O OG . SER B 151 ? 0.4394 0.4804 0.3990 -0.0356 0.0275 0.0486 480 SER B OG 3777 N N . VAL B 152 ? 0.4159 0.4670 0.3941 -0.0342 0.0246 0.0436 481 VAL B N 3778 C CA . VAL B 152 ? 0.4512 0.5075 0.4352 -0.0321 0.0223 0.0410 481 VAL B CA 3779 C C . VAL B 152 ? 0.5125 0.5696 0.5036 -0.0322 0.0213 0.0401 481 VAL B C 3780 O O . VAL B 152 ? 0.4913 0.5496 0.4851 -0.0300 0.0186 0.0394 481 VAL B O 3781 C CB . VAL B 152 ? 0.4058 0.4676 0.3920 -0.0329 0.0238 0.0384 481 VAL B CB 3782 C CG1 . VAL B 152 ? 0.3731 0.4387 0.3640 -0.0310 0.0215 0.0359 481 VAL B CG1 3783 C CG2 . VAL B 152 ? 0.4378 0.4990 0.4170 -0.0329 0.0249 0.0391 481 VAL B CG2 3784 N N . LYS B 153 ? 0.4433 0.5001 0.4371 -0.0349 0.0236 0.0402 482 LYS B N 3785 C CA . LYS B 153 ? 0.4860 0.5438 0.4864 -0.0352 0.0229 0.0392 482 LYS B CA 3786 C C . LYS B 153 ? 0.5144 0.5664 0.5131 -0.0341 0.0211 0.0411 482 LYS B C 3787 O O . LYS B 153 ? 0.5403 0.5934 0.5440 -0.0332 0.0194 0.0402 482 LYS B O 3788 C CB . LYS B 153 ? 0.4716 0.5321 0.4756 -0.0386 0.0259 0.0385 482 LYS B CB 3789 C CG . LYS B 153 ? 0.4469 0.5141 0.4539 -0.0389 0.0276 0.0362 482 LYS B CG 3790 C CD . LYS B 153 ? 0.4424 0.5137 0.4538 -0.0419 0.0303 0.0354 482 LYS B CD 3791 C CE . LYS B 153 ? 0.5518 0.6271 0.5614 -0.0435 0.0334 0.0349 482 LYS B CE 3792 N NZ . LYS B 153 ? 0.5987 0.6786 0.6121 -0.0469 0.0362 0.0345 482 LYS B NZ 3793 N N . ASN B 154 ? 0.5552 0.6007 0.5464 -0.0342 0.0215 0.0438 483 ASN B N 3794 C CA . ASN B 154 ? 0.5662 0.6053 0.5546 -0.0324 0.0197 0.0457 483 ASN B CA 3795 C C . ASN B 154 ? 0.5338 0.5720 0.5182 -0.0281 0.0169 0.0468 483 ASN B C 3796 O O . ASN B 154 ? 0.5844 0.6171 0.5649 -0.0258 0.0155 0.0486 483 ASN B O 3797 C CB . ASN B 154 ? 0.5997 0.6308 0.5822 -0.0351 0.0218 0.0481 483 ASN B CB 3798 C CG . ASN B 154 ? 0.6775 0.7045 0.6513 -0.0360 0.0236 0.0502 483 ASN B CG 3799 O OD1 . ASN B 154 ? 0.6217 0.6501 0.5923 -0.0334 0.0224 0.0505 483 ASN B OD1 3800 N ND2 . ASN B 154 ? 0.7007 0.7224 0.6703 -0.0400 0.0264 0.0516 483 ASN B ND2 3801 N N . GLY B 155 ? 0.4369 0.4806 0.4220 -0.0270 0.0161 0.0454 484 GLY B N 3802 C CA . GLY B 155 ? 0.4784 0.5234 0.4608 -0.0233 0.0132 0.0459 484 GLY B CA 3803 C C . GLY B 155 ? 0.5393 0.5786 0.5123 -0.0214 0.0130 0.0488 484 GLY B C 3804 O O . GLY B 155 ? 0.5974 0.6359 0.5678 -0.0177 0.0104 0.0500 484 GLY B O 3805 N N . THR B 156 ? 0.5187 0.5545 0.4866 -0.0238 0.0156 0.0500 485 THR B N 3806 C CA . THR B 156 ? 0.5121 0.5418 0.4701 -0.0222 0.0157 0.0529 485 THR B CA 3807 C C . THR B 156 ? 0.5315 0.5639 0.4860 -0.0235 0.0170 0.0526 485 THR B C 3808 O O . THR B 156 ? 0.5903 0.6172 0.5365 -0.0236 0.0181 0.0549 485 THR B O 3809 C CB . THR B 156 ? 0.5877 0.6077 0.5400 -0.0242 0.0179 0.0554 485 THR B CB 3810 O OG1 . THR B 156 ? 0.6034 0.6243 0.5579 -0.0293 0.0214 0.0545 485 THR B OG1 3811 C CG2 . THR B 156 ? 0.5519 0.5681 0.5066 -0.0229 0.0167 0.0558 485 THR B CG2 3812 N N . TYR B 157 ? 0.5050 0.5453 0.4654 -0.0243 0.0168 0.0497 486 TYR B N 3813 C CA . TYR B 157 ? 0.5069 0.5500 0.4642 -0.0254 0.0180 0.0490 486 TYR B CA 3814 C C . TYR B 157 ? 0.5844 0.6259 0.5337 -0.0225 0.0161 0.0509 486 TYR B C 3815 O O . TYR B 157 ? 0.5991 0.6422 0.5484 -0.0191 0.0129 0.0512 486 TYR B O 3816 C CB . TYR B 157 ? 0.4912 0.5420 0.4553 -0.0260 0.0176 0.0455 486 TYR B CB 3817 C CG . TYR B 157 ? 0.5171 0.5708 0.4778 -0.0267 0.0186 0.0444 486 TYR B CG 3818 C CD1 . TYR B 157 ? 0.4788 0.5321 0.4380 -0.0295 0.0221 0.0442 486 TYR B CD1 3819 C CD2 . TYR B 157 ? 0.4617 0.5187 0.4203 -0.0247 0.0160 0.0435 486 TYR B CD2 3820 C CE1 . TYR B 157 ? 0.4623 0.5179 0.4179 -0.0299 0.0231 0.0431 486 TYR B CE1 3821 C CE2 . TYR B 157 ? 0.4760 0.5351 0.4308 -0.0255 0.0169 0.0424 486 TYR B CE2 3822 C CZ . TYR B 157 ? 0.4882 0.5462 0.4413 -0.0279 0.0205 0.0422 486 TYR B CZ 3823 O OH . TYR B 157 ? 0.4758 0.5357 0.4249 -0.0285 0.0215 0.0411 486 TYR B OH 3824 N N . ASP B 158 ? 0.6603 0.6991 0.6027 -0.0238 0.0182 0.0521 487 ASP B N 3825 C CA . ASP B 158 ? 0.6403 0.6766 0.5738 -0.0211 0.0167 0.0543 487 ASP B CA 3826 C C . ASP B 158 ? 0.6928 0.7354 0.6257 -0.0210 0.0159 0.0523 487 ASP B C 3827 O O . ASP B 158 ? 0.7370 0.7790 0.6658 -0.0230 0.0183 0.0523 487 ASP B O 3828 C CB . ASP B 158 ? 0.7320 0.7598 0.6568 -0.0227 0.0195 0.0572 487 ASP B CB 3829 C CG . ASP B 158 ? 0.7980 0.8204 0.7129 -0.0190 0.0176 0.0604 487 ASP B CG 3830 O OD1 . ASP B 158 ? 0.8104 0.8373 0.7231 -0.0164 0.0152 0.0600 487 ASP B OD1 3831 O OD2 . ASP B 158 ? 0.7736 0.7869 0.6823 -0.0187 0.0186 0.0633 487 ASP B OD2 3832 N N . TYR B 159 ? 0.5880 0.6367 0.5247 -0.0189 0.0127 0.0506 488 TYR B N 3833 C CA . TYR B 159 ? 0.6054 0.6599 0.5413 -0.0191 0.0117 0.0484 488 TYR B CA 3834 C C . TYR B 159 ? 0.6642 0.7167 0.5904 -0.0183 0.0117 0.0502 488 TYR B C 3835 O O . TYR B 159 ? 0.6842 0.7381 0.6083 -0.0204 0.0136 0.0489 488 TYR B O 3836 C CB . TYR B 159 ? 0.5239 0.5850 0.4645 -0.0173 0.0079 0.0465 488 TYR B CB 3837 C CG . TYR B 159 ? 0.5511 0.6176 0.4896 -0.0178 0.0066 0.0445 488 TYR B CG 3838 C CD1 . TYR B 159 ? 0.5416 0.6110 0.4837 -0.0206 0.0079 0.0412 488 TYR B CD1 3839 C CD2 . TYR B 159 ? 0.6054 0.6738 0.5376 -0.0155 0.0041 0.0458 488 TYR B CD2 3840 C CE1 . TYR B 159 ? 0.5430 0.6163 0.4822 -0.0213 0.0068 0.0391 488 TYR B CE1 3841 C CE2 . TYR B 159 ? 0.6181 0.6914 0.5479 -0.0164 0.0028 0.0438 488 TYR B CE2 3842 C CZ . TYR B 159 ? 0.6288 0.7041 0.5619 -0.0195 0.0043 0.0404 488 TYR B CZ 3843 O OH . TYR B 159 ? 0.5880 0.6673 0.5179 -0.0206 0.0031 0.0383 488 TYR B OH 3844 N N . PRO B 160 ? 0.8204 0.8697 0.7404 -0.0149 0.0097 0.0532 489 PRO B N 3845 C CA . PRO B 160 ? 0.8997 0.9475 0.8102 -0.0139 0.0095 0.0549 489 PRO B CA 3846 C C . PRO B 160 ? 0.8975 0.9388 0.8021 -0.0166 0.0136 0.0563 489 PRO B C 3847 O O . PRO B 160 ? 0.9228 0.9639 0.8207 -0.0169 0.0141 0.0567 489 PRO B O 3848 C CB . PRO B 160 ? 0.8642 0.9092 0.7694 -0.0091 0.0066 0.0580 489 PRO B CB 3849 C CG . PRO B 160 ? 0.8930 0.9341 0.8028 -0.0085 0.0069 0.0588 489 PRO B CG 3850 C CD . PRO B 160 ? 0.8080 0.8548 0.7285 -0.0115 0.0076 0.0552 489 PRO B CD 3851 N N . LYS B 161 ? 0.7173 0.7537 0.6244 -0.0188 0.0164 0.0571 490 LYS B N 3852 C CA . LYS B 161 ? 0.6774 0.7086 0.5797 -0.0222 0.0206 0.0583 490 LYS B CA 3853 C C . LYS B 161 ? 0.6906 0.7272 0.5953 -0.0252 0.0229 0.0554 490 LYS B C 3854 O O . LYS B 161 ? 0.7756 0.8097 0.6743 -0.0272 0.0257 0.0562 490 LYS B O 3855 C CB . LYS B 161 ? 0.6719 0.6980 0.5774 -0.0245 0.0229 0.0592 490 LYS B CB 3856 C CG . LYS B 161 ? 0.6562 0.6794 0.5596 -0.0291 0.0275 0.0595 490 LYS B CG 3857 C CD . LYS B 161 ? 0.6956 0.7137 0.6013 -0.0316 0.0294 0.0606 490 LYS B CD 3858 C CE . LYS B 161 ? 0.6728 0.6901 0.5776 -0.0368 0.0342 0.0605 490 LYS B CE 3859 N NZ . LYS B 161 ? 0.7045 0.7158 0.6096 -0.0398 0.0361 0.0620 490 LYS B NZ 3860 N N . TYR B 162 ? 0.6092 0.6528 0.5222 -0.0254 0.0218 0.0520 491 TYR B N 3861 C CA . TYR B 162 ? 0.5867 0.6348 0.5022 -0.0279 0.0241 0.0490 491 TYR B CA 3862 C C . TYR B 162 ? 0.5918 0.6450 0.5063 -0.0267 0.0218 0.0466 491 TYR B C 3863 O O . TYR B 162 ? 0.6044 0.6608 0.5204 -0.0283 0.0235 0.0439 491 TYR B O 3864 C CB . TYR B 162 ? 0.5818 0.6329 0.5072 -0.0296 0.0256 0.0466 491 TYR B CB 3865 C CG . TYR B 162 ? 0.5825 0.6296 0.5094 -0.0317 0.0282 0.0483 491 TYR B CG 3866 C CD1 . TYR B 162 ? 0.5439 0.5886 0.4745 -0.0309 0.0267 0.0494 491 TYR B CD1 3867 C CD2 . TYR B 162 ? 0.5819 0.6279 0.5063 -0.0348 0.0324 0.0488 491 TYR B CD2 3868 C CE1 . TYR B 162 ? 0.5591 0.5998 0.4906 -0.0333 0.0292 0.0509 491 TYR B CE1 3869 C CE2 . TYR B 162 ? 0.5278 0.5706 0.4534 -0.0374 0.0348 0.0502 491 TYR B CE2 3870 C CZ . TYR B 162 ? 0.5674 0.6073 0.4964 -0.0368 0.0332 0.0512 491 TYR B CZ 3871 O OH . TYR B 162 ? 0.6645 0.7009 0.5942 -0.0398 0.0356 0.0526 491 TYR B OH 3872 N N . GLN B 163 ? 0.6444 0.6986 0.5562 -0.0239 0.0179 0.0475 492 GLN B N 3873 C CA . GLN B 163 ? 0.7564 0.8163 0.6682 -0.0234 0.0154 0.0449 492 GLN B CA 3874 C C . GLN B 163 ? 0.7983 0.8584 0.7025 -0.0243 0.0165 0.0444 492 GLN B C 3875 O O . GLN B 163 ? 0.8380 0.9018 0.7431 -0.0254 0.0163 0.0412 492 GLN B O 3876 C CB . GLN B 163 ? 0.7579 0.8210 0.6703 -0.0205 0.0108 0.0455 492 GLN B CB 3877 C CG . GLN B 163 ? 0.8731 0.9335 0.7775 -0.0174 0.0089 0.0491 492 GLN B CG 3878 C CD . GLN B 163 ? 0.9717 1.0381 0.8762 -0.0146 0.0042 0.0487 492 GLN B CD 3879 O OE1 . GLN B 163 ? 0.9124 0.9845 0.8169 -0.0157 0.0027 0.0462 492 GLN B OE1 3880 N NE2 . GLN B 163 ? 0.9158 0.9811 0.8201 -0.0111 0.0021 0.0512 492 GLN B NE2 3881 N N . LYS B 164 ? 0.7867 0.8421 0.6828 -0.0239 0.0178 0.0474 493 LYS B N 3882 C CA . LYS B 164 ? 0.8591 0.9142 0.7474 -0.0248 0.0192 0.0471 493 LYS B CA 3883 C C . LYS B 164 ? 0.8299 0.8860 0.7209 -0.0278 0.0233 0.0444 493 LYS B C 3884 O O . LYS B 164 ? 0.8406 0.8996 0.7301 -0.0285 0.0234 0.0416 493 LYS B O 3885 C CB . LYS B 164 ? 1.0151 1.0641 0.8942 -0.0240 0.0204 0.0511 493 LYS B CB 3886 C CG . LYS B 164 ? 1.0951 1.1419 0.9705 -0.0204 0.0168 0.0542 493 LYS B CG 3887 C CD . LYS B 164 ? 1.1481 1.1873 1.0130 -0.0197 0.0183 0.0582 493 LYS B CD 3888 C CE . LYS B 164 ? 1.2545 1.2903 1.1152 -0.0153 0.0149 0.0615 493 LYS B CE 3889 N NZ . LYS B 164 ? 1.1232 1.1567 0.9904 -0.0146 0.0147 0.0622 493 LYS B NZ 3890 N N . GLU B 165 ? 0.6918 0.7456 0.5866 -0.0294 0.0265 0.0451 494 GLU B N 3891 C CA . GLU B 165 ? 0.7055 0.7611 0.6037 -0.0318 0.0305 0.0428 494 GLU B CA 3892 C C . GLU B 165 ? 0.7584 0.8187 0.6637 -0.0316 0.0295 0.0388 494 GLU B C 3893 O O . GLU B 165 ? 0.7643 0.8266 0.6689 -0.0324 0.0314 0.0361 494 GLU B O 3894 C CB . GLU B 165 ? 0.6846 0.7378 0.5864 -0.0335 0.0336 0.0444 494 GLU B CB 3895 C CG . GLU B 165 ? 0.6542 0.7108 0.5610 -0.0358 0.0376 0.0420 494 GLU B CG 3896 C CD . GLU B 165 ? 0.7036 0.7588 0.6144 -0.0379 0.0402 0.0436 494 GLU B CD 3897 O OE1 . GLU B 165 ? 0.6449 0.7041 0.5612 -0.0395 0.0433 0.0417 494 GLU B OE1 3898 O OE2 . GLU B 165 ? 0.6388 0.6890 0.5471 -0.0379 0.0392 0.0467 494 GLU B OE2 3899 N N . SER B 166 ? 0.7487 0.8103 0.6601 -0.0305 0.0265 0.0384 495 SER B N 3900 C CA . SER B 166 ? 0.7998 0.8650 0.7174 -0.0304 0.0253 0.0349 495 SER B CA 3901 C C . SER B 166 ? 0.7700 0.8371 0.6830 -0.0302 0.0233 0.0326 495 SER B C 3902 O O . SER B 166 ? 0.7634 0.8316 0.6768 -0.0310 0.0246 0.0294 495 SER B O 3903 C CB . SER B 166 ? 0.7307 0.7968 0.6551 -0.0294 0.0224 0.0353 495 SER B CB 3904 O OG . SER B 166 ? 0.6797 0.7436 0.6080 -0.0297 0.0241 0.0372 495 SER B OG 3905 N N . LYS B 167 ? 0.8604 0.9277 0.7684 -0.0291 0.0201 0.0342 496 LYS B N 3906 C CA . LYS B 167 ? 0.9560 1.0256 0.8590 -0.0292 0.0176 0.0323 496 LYS B CA 3907 C C . LYS B 167 ? 0.9420 1.0104 0.8386 -0.0305 0.0204 0.0308 496 LYS B C 3908 O O . LYS B 167 ? 0.9266 0.9962 0.8215 -0.0314 0.0199 0.0276 496 LYS B O 3909 C CB . LYS B 167 ? 0.9451 1.0158 0.8434 -0.0274 0.0140 0.0350 496 LYS B CB 3910 C CG . LYS B 167 ? 1.0569 1.1310 0.9498 -0.0277 0.0111 0.0333 496 LYS B CG 3911 C CD . LYS B 167 ? 1.1897 1.2657 1.0782 -0.0253 0.0076 0.0363 496 LYS B CD 3912 C CE . LYS B 167 ? 1.2357 1.3158 1.1180 -0.0258 0.0047 0.0348 496 LYS B CE 3913 N NZ . LYS B 167 ? 1.1993 1.2816 1.0766 -0.0229 0.0015 0.0379 496 LYS B NZ 3914 N N . LEU B 168 ? 0.8120 0.8777 0.7048 -0.0306 0.0236 0.0330 497 LEU B N 3915 C CA . LEU B 168 ? 0.8439 0.9084 0.7307 -0.0317 0.0268 0.0318 497 LEU B CA 3916 C C . LEU B 168 ? 0.8730 0.9385 0.7643 -0.0325 0.0295 0.0281 497 LEU B C 3917 O O . LEU B 168 ? 0.8803 0.9459 0.7676 -0.0330 0.0300 0.0253 497 LEU B O 3918 C CB . LEU B 168 ? 0.8653 0.9269 0.7482 -0.0321 0.0300 0.0350 497 LEU B CB 3919 C CG . LEU B 168 ? 1.0357 1.0956 0.9081 -0.0324 0.0309 0.0360 497 LEU B CG 3920 C CD1 . LEU B 168 ? 0.9744 1.0308 0.8414 -0.0314 0.0299 0.0405 497 LEU B CD1 3921 C CD2 . LEU B 168 ? 0.9998 1.0593 0.8704 -0.0339 0.0359 0.0348 497 LEU B CD2 3922 N N . ASN B 169 ? 0.9324 0.9984 0.8317 -0.0326 0.0311 0.0282 498 ASN B N 3923 C CA . ASN B 169 ? 0.9291 0.9963 0.8331 -0.0327 0.0337 0.0250 498 ASN B CA 3924 C C . ASN B 169 ? 0.9186 0.9863 0.8252 -0.0323 0.0310 0.0218 498 ASN B C 3925 O O . ASN B 169 ? 0.8828 0.9500 0.7888 -0.0322 0.0325 0.0186 498 ASN B O 3926 C CB . ASN B 169 ? 0.8516 0.9198 0.7632 -0.0328 0.0361 0.0261 498 ASN B CB 3927 C CG . ASN B 169 ? 0.9253 0.9929 0.8339 -0.0339 0.0395 0.0287 498 ASN B CG 3928 O OD1 . ASN B 169 ? 0.9800 1.0475 0.8825 -0.0344 0.0421 0.0282 498 ASN B OD1 3929 N ND2 . ASN B 169 ? 0.8203 0.8873 0.7327 -0.0346 0.0398 0.0314 498 ASN B ND2 3930 N N . ARG B 170 ? 0.8900 0.9584 0.7991 -0.0322 0.0270 0.0227 499 ARG B N 3931 C CA . ARG B 170 ? 0.8927 0.9618 0.8044 -0.0324 0.0243 0.0199 499 ARG B CA 3932 C C . ARG B 170 ? 0.9529 1.0212 0.8569 -0.0334 0.0231 0.0174 499 ARG B C 3933 O O . ARG B 170 ? 0.9495 1.0164 0.8533 -0.0340 0.0234 0.0140 499 ARG B O 3934 C CB . ARG B 170 ? 0.8607 0.9317 0.7766 -0.0321 0.0204 0.0217 499 ARG B CB 3935 C CG . ARG B 170 ? 0.7936 0.8657 0.7132 -0.0328 0.0178 0.0191 499 ARG B CG 3936 C CD . ARG B 170 ? 0.8185 0.8937 0.7408 -0.0325 0.0137 0.0208 499 ARG B CD 3937 N NE . ARG B 170 ? 0.8717 0.9469 0.7960 -0.0308 0.0139 0.0246 499 ARG B NE 3938 C CZ . ARG B 170 ? 0.8894 0.9659 0.8100 -0.0297 0.0117 0.0273 499 ARG B CZ 3939 N NH1 . ARG B 170 ? 0.8769 0.9561 0.7923 -0.0301 0.0090 0.0266 499 ARG B NH1 3940 N NH2 . ARG B 170 ? 0.7840 0.8589 0.7056 -0.0282 0.0122 0.0307 499 ARG B NH2 3941 N N . GLN B 171 ? 1.1915 1.2603 1.0887 -0.0337 0.0219 0.0190 500 GLN B N 3942 C CA . GLN B 171 ? 1.2923 1.3609 1.1818 -0.0349 0.0203 0.0168 500 GLN B CA 3943 C C . GLN B 171 ? 1.2629 1.3288 1.1456 -0.0351 0.0239 0.0152 500 GLN B C 3944 O O . GLN B 171 ? 1.2561 1.3212 1.1388 -0.0343 0.0274 0.0167 500 GLN B O 3945 C CB . GLN B 171 ? 1.2679 1.3393 1.1532 -0.0349 0.0167 0.0191 500 GLN B CB 3946 C CG . GLN B 171 ? 1.2695 1.3446 1.1606 -0.0346 0.0127 0.0200 500 GLN B CG 3947 C CD . GLN B 171 ? 1.3549 1.4331 1.2427 -0.0333 0.0096 0.0232 500 GLN B CD 3948 O OE1 . GLN B 171 ? 1.3286 1.4055 1.2096 -0.0326 0.0105 0.0249 500 GLN B OE1 3949 N NE2 . GLN B 171 ? 1.2633 1.3455 1.1557 -0.0327 0.0061 0.0239 500 GLN B NE2 3950 C C1 . NAG C . ? 0.5514 0.5722 0.5718 0.0283 0.0027 0.0007 601 NAG A C1 3951 C C2 . NAG C . ? 0.5480 0.5774 0.5716 0.0346 0.0036 0.0002 601 NAG A C2 3952 C C3 . NAG C . ? 0.5527 0.5822 0.5754 0.0404 0.0024 0.0003 601 NAG A C3 3953 C C4 . NAG C . ? 0.5452 0.5810 0.5754 0.0369 0.0006 0.0015 601 NAG A C4 3954 C C5 . NAG C . ? 0.5480 0.5748 0.5748 0.0307 -0.0002 0.0021 601 NAG A C5 3955 C C6 . NAG C . ? 0.5385 0.5721 0.5732 0.0269 -0.0018 0.0032 601 NAG A C6 3956 C C7 . NAG C . ? 0.5429 0.5762 0.5645 0.0378 0.0070 -0.0013 601 NAG A C7 3957 C C8 . NAG C . ? 0.5345 0.5642 0.5537 0.0329 0.0082 -0.0016 601 NAG A C8 3958 N N2 . NAG C . ? 0.5526 0.5771 0.5696 0.0376 0.0055 -0.0010 601 NAG A N2 3959 O O3 . NAG C . ? 0.5481 0.5864 0.5737 0.0466 0.0032 -0.0003 601 NAG A O3 3960 O O4 . NAG C . ? 0.5434 0.5803 0.5731 0.0421 -0.0007 0.0016 601 NAG A O4 3961 O O5 . NAG C . ? 0.5485 0.5728 0.5740 0.0261 0.0010 0.0018 601 NAG A O5 3962 O O6 . NAG C . ? 0.5369 0.5634 0.5689 0.0214 -0.0023 0.0036 601 NAG A O6 3963 O O7 . NAG C . ? 0.5395 0.5837 0.5669 0.0417 0.0075 -0.0014 601 NAG A O7 3964 C C1 . NAG D . ? 0.8220 0.7091 0.7199 -0.0355 -0.0190 -0.0328 602 NAG A C1 3965 C C2 . NAG D . ? 0.8231 0.7005 0.7170 -0.0336 -0.0167 -0.0331 602 NAG A C2 3966 C C3 . NAG D . ? 0.8279 0.6992 0.7157 -0.0270 -0.0132 -0.0336 602 NAG A C3 3967 C C4 . NAG D . ? 0.8173 0.6998 0.7123 -0.0223 -0.0120 -0.0318 602 NAG A C4 3968 C C5 . NAG D . ? 0.8124 0.7033 0.7110 -0.0253 -0.0144 -0.0316 602 NAG A C5 3969 C C6 . NAG D . ? 0.7985 0.6999 0.7038 -0.0214 -0.0131 -0.0297 602 NAG A C6 3970 C C7 . NAG D . ? 0.8333 0.6902 0.7141 -0.0387 -0.0163 -0.0356 602 NAG A C7 3971 C C8 . NAG D . ? 0.8426 0.6895 0.7152 -0.0455 -0.0178 -0.0378 602 NAG A C8 3972 N N2 . NAG D . ? 0.8313 0.6986 0.7174 -0.0390 -0.0179 -0.0352 602 NAG A N2 3973 O O3 . NAG D . ? 0.8276 0.6914 0.7128 -0.0242 -0.0111 -0.0333 602 NAG A O3 3974 O O4 . NAG D . ? 0.8197 0.6974 0.7084 -0.0164 -0.0088 -0.0328 602 NAG A O4 3975 O O5 . NAG D . ? 0.8089 0.7047 0.7133 -0.0307 -0.0175 -0.0309 602 NAG A O5 3976 O O6 . NAG D . ? 0.7976 0.7016 0.7005 -0.0224 -0.0140 -0.0303 602 NAG A O6 3977 O O7 . NAG D . ? 0.8310 0.6865 0.7130 -0.0334 -0.0138 -0.0343 602 NAG A O7 3978 C C1 . SIA E . ? 0.9114 0.9695 0.8309 0.0335 -0.1022 0.0074 603 SIA A C1 3979 C C2 . SIA E . ? 0.9522 1.0038 0.8598 0.0360 -0.1043 0.0085 603 SIA A C2 3980 C C3 . SIA E . ? 0.8796 0.9428 0.7891 0.0327 -0.1079 0.0059 603 SIA A C3 3981 C C4 . SIA E . ? 0.8740 0.9379 0.7894 0.0235 -0.1055 0.0031 603 SIA A C4 3982 C C5 . SIA E . ? 0.8368 0.8856 0.7462 0.0195 -0.1013 0.0034 603 SIA A C5 3983 C C6 . SIA E . ? 0.8143 0.8514 0.7202 0.0233 -0.0980 0.0062 603 SIA A C6 3984 C C7 . SIA E . ? 0.8401 0.8617 0.7376 0.0207 -0.0941 0.0071 603 SIA A C7 3985 C C8 . SIA E . ? 0.8269 0.8378 0.7208 0.0243 -0.0912 0.0099 603 SIA A C8 3986 C C9 . SIA E . ? 0.7294 0.7269 0.6182 0.0202 -0.0864 0.0104 603 SIA A C9 3987 C C10 . SIA E . ? 0.7511 0.7919 0.6633 0.0072 -0.0958 0.0000 603 SIA A C10 3988 C C11 . SIA E . ? 0.7507 0.7944 0.6699 0.0001 -0.0939 -0.0028 603 SIA A C11 3989 N N5 . SIA E . ? 0.7292 0.7793 0.6457 0.0120 -0.0986 0.0009 603 SIA A N5 3990 O O1A . SIA E . ? 0.8554 0.9046 0.7766 0.0296 -0.0978 0.0076 603 SIA A O1A 3991 O O1B . SIA E . ? 0.8879 0.9604 0.8151 0.0353 -0.1049 0.0065 603 SIA A O1B 3992 O O4 . SIA E . ? 0.8048 0.8794 0.7212 0.0203 -0.1091 0.0007 603 SIA A O4 3993 O O6 . SIA E . ? 0.8864 0.9236 0.7876 0.0315 -0.1005 0.0087 603 SIA A O6 3994 O O7 . SIA E . ? 0.8529 0.8708 0.7403 0.0219 -0.0963 0.0074 603 SIA A O7 3995 O O8 . SIA E . ? 0.7535 0.7702 0.6572 0.0249 -0.0902 0.0098 603 SIA A O8 3996 O O9 . SIA E . ? 0.7696 0.7571 0.6534 0.0237 -0.0842 0.0131 603 SIA A O9 3997 O O10 . SIA E . ? 0.8482 0.8784 0.7508 0.0088 -0.0948 0.0014 603 SIA A O10 3998 C C1 . GAL F . ? 1.1543 1.1632 1.0241 0.0577 -0.1028 0.0191 604 GAL A C1 3999 C C2 . GAL F . ? 1.1496 1.1721 1.0278 0.0519 -0.1047 0.0159 604 GAL A C2 4000 C C3 . GAL F . ? 1.0595 1.0953 0.9524 0.0487 -0.1044 0.0137 604 GAL A C3 4001 C C4 . GAL F . ? 1.0190 1.0619 0.9161 0.0557 -0.1059 0.0149 604 GAL A C4 4002 C C5 . GAL F . ? 1.0134 1.0407 0.9009 0.0614 -0.1038 0.0180 604 GAL A C5 4003 C C6 . GAL F . ? 1.0141 1.0479 0.9046 0.0692 -0.1056 0.0191 604 GAL A C6 4004 O O2 . GAL F . ? 1.1272 1.1412 1.0020 0.0449 -0.1018 0.0150 604 GAL A O2 4005 O O3 . GAL F . ? 1.0170 1.0663 0.9161 0.0444 -0.1070 0.0109 604 GAL A O3 4006 O O4 . GAL F . ? 1.0556 1.1114 0.9525 0.0610 -0.1112 0.0146 604 GAL A O4 4007 O O5 . GAL F . ? 1.1891 1.2062 1.0629 0.0647 -0.1051 0.0198 604 GAL A O5 4008 O O6 . GAL F . ? 0.9894 1.0321 0.8929 0.0657 -0.1038 0.0175 604 GAL A O6 4009 C C1 . NAG G . ? 1.6718 1.6199 1.4868 0.0727 -0.0995 0.0300 605 NAG A C1 4010 C C2 . NAG G . ? 1.6190 1.5788 1.4456 0.0760 -0.1006 0.0292 605 NAG A C2 4011 C C3 . NAG G . ? 1.5430 1.5232 1.3838 0.0733 -0.1034 0.0261 605 NAG A C3 4012 C C4 . NAG G . ? 1.4862 1.4682 1.3322 0.0636 -0.1012 0.0237 605 NAG A C4 4013 C C5 . NAG G . ? 1.5363 1.5056 1.3695 0.0616 -0.1002 0.0247 605 NAG A C5 4014 C C6 . NAG G . ? 1.4655 1.4353 1.3032 0.0523 -0.0975 0.0224 605 NAG A C6 4015 C C7 . NAG G . ? 1.6905 1.6429 1.5103 0.0898 -0.1016 0.0326 605 NAG A C7 4016 C C8 . NAG G . ? 1.6339 1.5874 1.4481 0.1010 -0.1051 0.0345 605 NAG A C8 4017 N N2 . NAG G . ? 1.6887 1.6464 1.5083 0.0862 -0.1034 0.0314 605 NAG A N2 4018 O O3 . NAG G . ? 1.4574 1.4469 1.3096 0.0745 -0.1030 0.0252 605 NAG A O3 4019 O O4 . NAG G . ? 1.3887 1.3882 1.2444 0.0617 -0.1045 0.0210 605 NAG A O4 4020 O O5 . NAG G . ? 1.6570 1.6089 1.4792 0.0636 -0.0972 0.0275 605 NAG A O5 4021 O O6 . NAG G . ? 1.4034 1.3590 1.2289 0.0502 -0.0953 0.0237 605 NAG A O6 4022 O O7 . NAG G . ? 1.6288 1.5757 1.4528 0.0846 -0.0973 0.0323 605 NAG A O7 4023 C C1 . GAL H . ? 1.8924 1.7881 1.6508 0.0927 -0.1011 0.0406 606 GAL A C1 4024 C C2 . GAL H . ? 1.8544 1.7657 1.6319 0.0880 -0.1000 0.0377 606 GAL A C2 4025 C C3 . GAL H . ? 1.8426 1.7619 1.6292 0.0784 -0.0986 0.0349 606 GAL A C3 4026 C C4 . GAL H . ? 1.8957 1.7993 1.6717 0.0724 -0.0946 0.0358 606 GAL A C4 4027 C C5 . GAL H . ? 1.9163 1.8074 1.6745 0.0780 -0.0965 0.0386 606 GAL A C5 4028 C C6 . GAL H . ? 1.8944 1.7706 1.6419 0.0717 -0.0926 0.0395 606 GAL A C6 4029 O O1 . GAL H . ? 1.9017 1.7864 1.6509 0.1004 -0.1011 0.0432 606 GAL A O1 4030 O O2 . GAL H . ? 1.7985 1.7261 1.5841 0.0945 -0.1046 0.0368 606 GAL A O2 4031 O O3 . GAL H . ? 1.7531 1.6814 1.5547 0.0733 -0.0963 0.0327 606 GAL A O3 4032 O O4 . GAL H . ? 1.8876 1.7806 1.6634 0.0687 -0.0897 0.0365 606 GAL A O4 4033 O O5 . GAL H . ? 1.8921 1.7739 1.6425 0.0855 -0.0969 0.0412 606 GAL A O5 4034 O O6 . GAL H . ? 1.8347 1.6967 1.5644 0.0770 -0.0938 0.0425 606 GAL A O6 4035 C C1 . NAG I . ? 0.6394 0.6540 0.5987 -0.0398 0.0273 0.0542 601 NAG B C1 4036 C C2 . NAG I . ? 0.6601 0.6633 0.6123 -0.0408 0.0278 0.0568 601 NAG B C2 4037 C C3 . NAG I . ? 0.6845 0.6787 0.6250 -0.0425 0.0300 0.0597 601 NAG B C3 4038 C C4 . NAG I . ? 0.6912 0.6905 0.6312 -0.0459 0.0328 0.0592 601 NAG B C4 4039 C C5 . NAG I . ? 0.6565 0.6673 0.6042 -0.0436 0.0315 0.0565 601 NAG B C5 4040 C C6 . NAG I . ? 0.6441 0.6603 0.5918 -0.0469 0.0345 0.0557 601 NAG B C6 4041 C C7 . NAG I . ? 0.6494 0.6476 0.6044 -0.0351 0.0234 0.0569 601 NAG B C7 4042 C C8 . NAG I . ? 0.6354 0.6378 0.5949 -0.0298 0.0199 0.0559 601 NAG B C8 4043 N N2 . NAG I . ? 0.6542 0.6538 0.6052 -0.0356 0.0246 0.0576 601 NAG B N2 4044 O O3 . NAG I . ? 0.6985 0.6835 0.6342 -0.0462 0.0318 0.0612 601 NAG B O3 4045 O O4 . NAG I . ? 0.7185 0.7098 0.6472 -0.0452 0.0335 0.0620 601 NAG B O4 4046 O O5 . NAG I . ? 0.6334 0.6509 0.5915 -0.0435 0.0304 0.0539 601 NAG B O5 4047 O O6 . NAG I . ? 0.6467 0.6651 0.5979 -0.0522 0.0375 0.0549 601 NAG B O6 4048 O O7 . NAG I . ? 0.6567 0.6508 0.6118 -0.0390 0.0251 0.0569 601 NAG B O7 4049 C C1 . NAG J . ? 0.7416 0.7278 0.6645 -0.0511 0.0373 0.0633 602 NAG B C1 4050 C C2 . NAG J . ? 0.7649 0.7451 0.6767 -0.0501 0.0381 0.0659 602 NAG B C2 4051 C C3 . NAG J . ? 0.7966 0.7735 0.7030 -0.0568 0.0424 0.0669 602 NAG B C3 4052 C C4 . NAG J . ? 0.8081 0.7747 0.7101 -0.0605 0.0437 0.0683 602 NAG B C4 4053 C C5 . NAG J . ? 0.7896 0.7608 0.7018 -0.0604 0.0421 0.0660 602 NAG B C5 4054 C C6 . NAG J . ? 0.8095 0.7677 0.7148 -0.0621 0.0423 0.0679 602 NAG B C6 4055 C C7 . NAG J . ? 0.7580 0.7437 0.6674 -0.0411 0.0338 0.0660 602 NAG B C7 4056 C C8 . NAG J . ? 0.7604 0.7391 0.6671 -0.0366 0.0308 0.0675 602 NAG B C8 4057 N N2 . NAG J . ? 0.7583 0.7469 0.6730 -0.0466 0.0366 0.0646 602 NAG B N2 4058 O O3 . NAG J . ? 0.8153 0.7866 0.7112 -0.0559 0.0432 0.0692 602 NAG B O3 4059 O O4 . NAG J . ? 0.8336 0.7985 0.7318 -0.0678 0.0479 0.0688 602 NAG B O4 4060 O O5 . NAG J . ? 0.7569 0.7337 0.6758 -0.0540 0.0383 0.0646 602 NAG B O5 4061 O O6 . NAG J . ? 0.7893 0.7432 0.6939 -0.0554 0.0386 0.0685 602 NAG B O6 4062 O O7 . NAG J . ? 0.7629 0.7519 0.6695 -0.0396 0.0335 0.0661 602 NAG B O7 4063 C C1 . BMA K . ? 0.8553 0.8068 0.7387 -0.0683 0.0492 0.0723 603 BMA B C1 4064 C C2 . BMA K . ? 0.8789 0.8226 0.7558 -0.0764 0.0531 0.0736 603 BMA B C2 4065 C C3 . BMA K . ? 0.9012 0.8285 0.7613 -0.0764 0.0541 0.0775 603 BMA B C3 4066 C C4 . BMA K . ? 0.9026 0.8327 0.7584 -0.0737 0.0543 0.0785 603 BMA B C4 4067 C C5 . BMA K . ? 0.8847 0.8249 0.7490 -0.0660 0.0504 0.0767 603 BMA B C5 4068 C C6 . BMA K . ? 0.8895 0.8337 0.7502 -0.0641 0.0507 0.0772 603 BMA B C6 4069 O O2 . BMA K . ? 0.8808 0.8354 0.7632 -0.0823 0.0565 0.0718 603 BMA B O2 4070 O O3 . BMA K . ? 0.9206 0.8406 0.7739 -0.0849 0.0582 0.0786 603 BMA B O3 4071 O O4 . BMA K . ? 0.9236 0.8376 0.7634 -0.0722 0.0545 0.0823 603 BMA B O4 4072 O O5 . BMA K . ? 0.8620 0.8164 0.7415 -0.0668 0.0498 0.0730 603 BMA B O5 4073 O O6 . BMA K . ? 0.8762 0.8292 0.7441 -0.0574 0.0469 0.0756 603 BMA B O6 4074 O O . HOH L . ? 0.7504 0.6789 0.5824 -0.0152 -0.0540 0.0047 701 HOH A O 4075 O O . HOH L . ? 0.5948 0.6957 0.6864 -0.0693 -0.0263 -0.0009 702 HOH A O 4076 O O . HOH L . ? 0.5758 0.6528 0.6512 0.0157 -0.0141 0.0077 703 HOH A O 4077 O O . HOH L . ? 0.7136 0.7031 0.7081 -0.0256 -0.0226 -0.0066 704 HOH A O 4078 O O . HOH L . ? 0.3483 0.4687 0.4116 0.0022 -0.0604 0.0017 705 HOH A O 4079 O O . HOH L . ? 0.6732 0.7122 0.6784 -0.0995 -0.0531 -0.0265 706 HOH A O 4080 O O . HOH L . ? 0.6096 0.6195 0.5578 -0.0514 -0.0652 -0.0227 707 HOH A O 4081 O O . HOH L . ? 0.6479 0.7306 0.6876 0.0127 0.0230 -0.0003 708 HOH A O 4082 O O . HOH L . ? 0.8088 0.8177 0.7093 0.0757 -0.0919 0.0231 709 HOH A O 4083 O O . HOH L . ? 0.5155 0.5720 0.5953 -0.0226 -0.0117 0.0142 710 HOH A O 4084 O O . HOH L . ? 0.7648 0.7313 0.7352 -0.0134 -0.0105 -0.0131 711 HOH A O 4085 O O . HOH L . ? 0.5771 0.6664 0.5463 -0.0425 -0.0919 -0.0205 712 HOH A O 4086 O O . HOH L . ? 0.5172 0.6041 0.5511 -0.0472 -0.0631 -0.0126 713 HOH A O 4087 O O . HOH L . ? 0.4674 0.5197 0.5416 -0.0198 -0.0237 0.0091 714 HOH A O 4088 O O . HOH L . ? 0.4481 0.5049 0.4036 -0.0263 -0.0845 -0.0126 715 HOH A O 4089 O O . HOH L . ? 0.6780 0.7287 0.7045 0.0033 -0.0521 0.0073 716 HOH A O 4090 O O . HOH L . ? 0.5714 0.5836 0.6052 -0.0318 -0.0266 -0.0014 717 HOH A O 4091 O O . HOH L . ? 0.8657 0.8577 0.7539 0.0361 -0.0866 0.0164 718 HOH A O 4092 O O . HOH L . ? 0.4575 0.5975 0.5408 -0.0214 0.0274 0.0121 719 HOH A O 4093 O O . HOH L . ? 0.5078 0.6088 0.5447 -0.0366 -0.0675 -0.0102 720 HOH A O 4094 O O . HOH L . ? 0.5921 0.6533 0.6625 -0.0360 -0.0330 0.0015 721 HOH A O 4095 O O . HOH L . ? 0.7895 0.7699 0.7474 -0.0148 -0.0402 0.0079 722 HOH A O 4096 O O . HOH L . ? 0.4626 0.4450 0.4412 -0.0285 -0.0271 -0.0096 723 HOH A O 4097 O O . HOH L . ? 0.6051 0.5829 0.5815 -0.0248 -0.0210 -0.0105 724 HOH A O 4098 O O . HOH L . ? 0.4909 0.5090 0.4766 -0.0400 -0.0539 -0.0126 725 HOH A O 4099 O O . HOH L . ? 0.4720 0.6069 0.5878 -0.0175 -0.0190 0.0063 726 HOH A O 4100 O O . HOH L . ? 0.6854 0.8280 0.6625 0.0459 -0.1098 0.0036 727 HOH A O 4101 O O . HOH L . ? 0.6446 0.6324 0.6304 -0.0221 -0.0176 -0.0071 728 HOH A O 4102 O O . HOH L . ? 0.8481 0.8033 0.7341 -0.0505 -0.0566 -0.0308 729 HOH A O 4103 O O . HOH L . ? 0.5011 0.5534 0.5637 -0.0435 -0.0334 -0.0011 730 HOH A O 4104 O O . HOH L . ? 0.5362 0.5452 0.5571 -0.0153 -0.0017 0.0038 731 HOH A O 4105 O O . HOH L . ? 0.2441 0.3136 0.3177 -0.0215 -0.0018 0.0144 732 HOH A O 4106 O O . HOH L . ? 0.4545 0.4438 0.3631 -0.0225 -0.0670 -0.0079 733 HOH A O 4107 O O . HOH L . ? 0.4741 0.5640 0.5178 -0.0519 -0.0591 -0.0124 734 HOH A O 4108 O O . HOH L . ? 0.4419 0.5628 0.4750 -0.0314 -0.0768 -0.0112 735 HOH A O 4109 O O . HOH L . ? 0.4456 0.5487 0.5237 0.0138 -0.0401 0.0069 736 HOH A O 4110 O O . HOH L . ? 0.6178 0.6082 0.6102 -0.0192 -0.0280 0.0106 737 HOH A O 4111 O O . HOH L . ? 0.5860 0.5735 0.6003 -0.0429 -0.0265 -0.0076 738 HOH A O 4112 O O . HOH L . ? 0.2649 0.3562 0.3224 -0.0103 0.0179 0.0088 739 HOH A O 4113 O O . HOH L . ? 0.5873 0.7063 0.5933 0.0143 -0.0890 -0.0002 740 HOH A O 4114 O O . HOH L . ? 0.4917 0.5623 0.5777 -0.0500 -0.0212 0.0051 741 HOH A O 4115 O O . HOH L . ? 0.6200 0.6025 0.5976 -0.0050 -0.0382 0.0136 742 HOH A O 4116 O O . HOH L . ? 0.4266 0.4584 0.4764 -0.0245 -0.0281 0.0047 743 HOH A O 4117 O O . HOH L . ? 0.5018 0.6092 0.5672 -0.0726 -0.0507 -0.0135 744 HOH A O 4118 O O . HOH L . ? 0.6819 0.6230 0.5850 0.0145 -0.0534 0.0207 745 HOH A O 4119 O O . HOH L . ? 0.4797 0.4918 0.4994 -0.0259 -0.0186 0.0078 746 HOH A O 4120 O O . HOH L . ? 0.4215 0.4433 0.4523 -0.0158 -0.0326 0.0079 747 HOH A O 4121 O O . HOH L . ? 0.5317 0.6336 0.6370 -0.0362 -0.0170 0.0082 748 HOH A O 4122 O O . HOH L . ? 0.5648 0.7635 0.6737 -0.0280 -0.0582 -0.0069 749 HOH A O 4123 O O . HOH L . ? 0.3775 0.3769 0.3791 -0.0204 -0.0286 0.0081 750 HOH A O 4124 O O . HOH L . ? 0.7281 0.7150 0.7219 -0.0042 0.0043 -0.0014 751 HOH A O 4125 O O . HOH L . ? 0.5012 0.6038 0.5940 0.0036 -0.0054 0.0077 752 HOH A O 4126 O O . HOH L . ? 0.4794 0.5619 0.4980 -0.0206 0.0256 0.0120 753 HOH A O 4127 O O . HOH L . ? 0.3935 0.5041 0.4971 -0.0201 -0.0014 0.0116 754 HOH A O 4128 O O . HOH L . ? 0.3230 0.3783 0.3866 -0.0077 -0.0029 0.0085 755 HOH A O 4129 O O . HOH L . ? 0.4395 0.5462 0.5283 -0.0087 0.0071 0.0097 756 HOH A O 4130 O O . HOH L . ? 0.5356 0.5222 0.5222 -0.0180 0.0050 -0.0031 757 HOH A O 4131 O O . HOH L . ? 0.4971 0.5488 0.5742 -0.0195 -0.0173 0.0113 758 HOH A O 4132 O O . HOH L . ? 0.4845 0.5431 0.5485 -0.0330 -0.0361 0.0009 759 HOH A O 4133 O O . HOH L . ? 0.3513 0.3908 0.3846 -0.0228 0.0014 0.0052 760 HOH A O 4134 O O . HOH L . ? 0.6296 0.6164 0.6044 -0.0065 -0.0412 0.0117 761 HOH A O 4135 O O . HOH L . ? 0.5100 0.7184 0.6247 -0.0112 -0.0565 -0.0043 762 HOH A O 4136 O O . HOH L . ? 0.5196 0.5152 0.5033 -0.0224 -0.0348 0.0019 763 HOH A O 4137 O O . HOH L . ? 0.4473 0.5637 0.5455 -0.0204 0.0072 0.0124 764 HOH A O 4138 O O . HOH L . ? 0.5102 0.5641 0.5747 -0.0046 -0.0051 0.0085 765 HOH A O 4139 O O . HOH L . ? 0.6780 0.6644 0.6589 -0.0137 -0.0347 0.0109 766 HOH A O 4140 O O . HOH L . ? 0.5960 0.6837 0.6467 -0.0849 -0.0498 -0.0170 767 HOH A O 4141 O O . HOH L . ? 0.4361 0.4810 0.5061 -0.0194 -0.0161 0.0115 768 HOH A O 4142 O O . HOH L . ? 0.5096 0.6250 0.5905 -0.0843 -0.0397 -0.0105 769 HOH A O 4143 O O . HOH L . ? 0.4989 0.5987 0.5920 -0.0280 0.0054 0.0159 770 HOH A O 4144 O O . HOH L . ? 0.3487 0.4080 0.3899 -0.0196 0.0063 0.0080 771 HOH A O 4145 O O . HOH L . ? 0.5288 0.5803 0.5654 -0.0234 0.0031 0.0068 772 HOH A O 4146 O O . HOH L . ? 0.5783 0.7399 0.7032 -0.0161 -0.0202 0.0044 773 HOH A O 4147 O O . HOH L . ? 0.5985 0.5877 0.5734 -0.0246 -0.0293 0.0004 774 HOH A O 4148 O O . HOH L . ? 0.7361 0.7234 0.7082 -0.0255 -0.0256 -0.0021 775 HOH A O 4149 O O . HOH M . ? 0.8435 0.8840 0.7421 -0.0360 0.0363 0.0521 701 HOH B O 4150 O O . HOH M . ? 0.5996 0.6464 0.6090 -0.0042 0.0194 -0.0013 702 HOH B O 4151 O O . HOH M . ? 0.5655 0.5712 0.5906 -0.0153 -0.0236 0.0122 703 HOH B O 4152 O O . HOH M . ? 0.7046 0.7714 0.6645 -0.0165 0.0048 0.0435 704 HOH B O 4153 O O . HOH M . ? 0.4387 0.4890 0.4710 -0.0318 -0.0006 0.0062 705 HOH B O 4154 O O . HOH M . ? 0.8005 0.8662 0.7163 -0.0384 0.0453 0.0364 706 HOH B O 4155 O O . HOH M . ? 0.4424 0.5164 0.5079 -0.0249 -0.0038 0.0178 707 HOH B O 4156 O O . HOH M . ? 0.4063 0.4308 0.4495 -0.0225 -0.0212 0.0089 708 HOH B O 4157 O O . HOH M . ? 0.6230 0.7691 0.6202 -0.0512 0.0737 0.0239 709 HOH B O 4158 O O . HOH M . ? 0.4540 0.5004 0.5247 -0.0177 -0.0202 0.0106 710 HOH B O 4159 O O . HOH M . ? 0.5064 0.5750 0.5541 -0.0250 0.0049 0.0283 711 HOH B O 4160 O O . HOH M . ? 0.5677 0.6209 0.5495 -0.0302 0.0132 0.0021 712 HOH B O 4161 O O . HOH M . ? 0.4528 0.5239 0.4474 -0.0183 0.0033 0.0377 713 HOH B O 4162 O O . HOH M . ? 0.6252 0.6776 0.6458 -0.0254 0.0069 0.0052 714 HOH B O 4163 O O . HOH M . ? 0.3828 0.4724 0.4233 -0.0177 0.0232 0.0117 715 HOH B O 4164 O O . HOH M . ? 0.6258 0.5964 0.5942 -0.0381 -0.0128 0.0139 716 HOH B O 4165 O O . HOH M . ? 0.6885 0.6974 0.7190 -0.0125 -0.0229 0.0123 717 HOH B O 4166 O O . HOH M . ? 0.5011 0.5782 0.5417 -0.0228 0.0006 0.0262 718 HOH B O 4167 O O . HOH M . ? 0.3890 0.4496 0.4674 -0.0199 -0.0102 0.0162 719 HOH B O 4168 O O . HOH M . ? 0.4493 0.5230 0.4859 -0.0246 0.0053 0.0273 720 HOH B O 4169 O O . HOH M . ? 0.5651 0.5616 0.5828 -0.0329 -0.0110 0.0108 721 HOH B O 4170 O O . HOH M . ? 0.5382 0.5644 0.5838 -0.0108 -0.0259 0.0110 722 HOH B O 4171 O O . HOH M . ? 0.5523 0.6703 0.6079 -0.0027 0.0308 0.0054 723 HOH B O 4172 O O . HOH M . ? 0.6420 0.6761 0.5829 -0.0314 0.0256 0.0527 724 HOH B O 4173 O O . HOH M . ? 0.4664 0.5297 0.5363 -0.0104 -0.0085 0.0226 725 HOH B O 4174 O O . HOH M . ? 0.5642 0.6138 0.4825 -0.0425 0.0433 0.0478 726 HOH B O 4175 O O . HOH M . ? 0.4786 0.5683 0.4771 -0.0262 -0.0016 0.0245 727 HOH B O 4176 O O . HOH M . ? 0.4673 0.5208 0.4999 -0.0372 -0.0030 0.0062 728 HOH B O 4177 O O . HOH M . ? 0.3441 0.4193 0.3937 -0.0217 -0.0010 0.0261 729 HOH B O 4178 O O . HOH M . ? 0.5015 0.4931 0.5145 -0.0320 -0.0121 0.0116 730 HOH B O 4179 O O . HOH M . ? 0.3601 0.3691 0.3919 -0.0248 -0.0104 0.0095 731 HOH B O 4180 O O . HOH M . ? 0.5588 0.6525 0.5830 -0.0426 0.0367 0.0290 732 HOH B O 4181 O O . HOH M . ? 0.6309 0.6826 0.7074 -0.0228 -0.0135 0.0127 733 HOH B O 4182 O O . HOH M . ? 0.4447 0.5029 0.4962 -0.0435 -0.0081 0.0089 734 HOH B O 4183 O O . HOH M . ? 0.7567 0.8485 0.7794 -0.0245 -0.0046 0.0240 735 HOH B O 4184 O O . HOH M . ? 0.5634 0.5958 0.5546 -0.0126 0.0177 -0.0035 736 HOH B O 4185 O O . HOH M . ? 0.3323 0.3826 0.3721 -0.0257 0.0006 0.0073 737 HOH B O 4186 O O . HOH M . ? 0.3053 0.3556 0.3762 -0.0245 -0.0129 0.0121 738 HOH B O 4187 O O . HOH M . ? 0.6307 0.7040 0.6446 -0.0415 -0.0032 0.0066 739 HOH B O 4188 O O . HOH M . ? 0.6621 0.6874 0.6355 -0.0171 0.0105 0.0519 740 HOH B O 4189 O O . HOH M . ? 0.4842 0.6260 0.5399 -0.0456 0.0458 0.0210 741 HOH B O 4190 O O . HOH M . ? 0.7020 0.7450 0.5954 -0.0295 0.0282 0.0517 742 HOH B O 4191 O O . HOH M . ? 0.4827 0.5665 0.5014 -0.0217 -0.0011 0.0285 743 HOH B O 4192 O O . HOH M . ? 0.5460 0.6791 0.6051 -0.0133 0.0364 0.0092 744 HOH B O 4193 O O . HOH M . ? 0.5193 0.5162 0.5268 -0.0045 -0.0319 0.0133 745 HOH B O 4194 O O . HOH M . ? 0.5621 0.6090 0.6216 -0.0291 0.0020 0.0284 746 HOH B O 4195 O O . HOH M . ? 0.6939 0.7183 0.7399 -0.0094 -0.0235 0.0115 747 HOH B O 4196 O O . HOH M . ? 0.6390 0.7073 0.6599 -0.0431 0.0273 0.0355 748 HOH B O 4197 O O . HOH M . ? 0.4324 0.4714 0.4870 -0.0131 -0.0063 0.0087 749 HOH B O 4198 O O . HOH M . ? 0.4018 0.4696 0.4525 -0.0194 0.0066 0.0106 750 HOH B O 4199 O O . HOH M . ? 0.4777 0.5131 0.5208 -0.0155 -0.0349 0.0068 751 HOH B O 4200 O O . HOH M . ? 0.5475 0.6195 0.4928 -0.0659 0.0636 0.0458 752 HOH B O 4201 O O . HOH M . ? 0.4758 0.4708 0.4715 -0.0309 -0.0161 0.0105 753 HOH B O 4202 O O . HOH M . ? 0.6235 0.6699 0.5568 -0.0472 0.0443 0.0495 754 HOH B O 4203 O O . HOH M . ? 0.3712 0.4486 0.4281 -0.0276 -0.0044 0.0163 755 HOH B O 4204 O O . HOH M . ? 0.3696 0.4552 0.3788 -0.0201 -0.0021 0.0305 756 HOH B O 4205 O O . HOH M . ? 0.4241 0.4953 0.4513 -0.0230 0.0050 0.0310 757 HOH B O 4206 O O . HOH M . ? 0.8497 0.8779 0.7409 -0.0386 0.0388 0.0577 758 HOH B O 4207 O O . HOH M . ? 0.5369 0.6682 0.5899 -0.0026 0.0379 0.0048 759 HOH B O 4208 O O . HOH M . ? 0.4894 0.5680 0.4909 -0.0158 -0.0014 0.0362 760 HOH B O 4209 O O . HOH M . ? 0.4237 0.4122 0.4121 -0.0350 -0.0137 0.0119 761 HOH B O # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 LYS 2 2 2 LYS LYS A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 THR 14 14 14 THR THR A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 SER 29 29 29 SER SER A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 GLU 31 31 31 GLU GLU A . n A 1 32 LEU 32 32 32 LEU LEU A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 ASN 35 35 35 ASN ASN A . n A 1 36 GLN 36 36 36 GLN GLN A . n A 1 37 LYS 37 37 37 LYS LYS A . n A 1 38 GLU 38 38 38 GLU GLU A . n A 1 39 LYS 39 39 39 LYS LYS A . n A 1 40 ARG 40 40 40 ARG ARG A . n A 1 41 PHE 41 41 41 PHE PHE A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 ILE 44 44 44 ILE ILE A . n A 1 45 MET 45 45 45 MET MET A . n A 1 46 ASN 46 46 46 ASN ASN A . n A 1 47 LYS 47 47 47 LYS LYS A . n A 1 48 ALA 48 48 48 ALA ALA A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ASP 51 51 51 ASP ASP A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 LYS 53 53 53 LYS LYS A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 THR 56 56 56 THR THR A . n A 1 57 ILE 57 57 57 ILE ILE A . n A 1 58 GLU 58 58 58 GLU GLU A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 ILE 61 61 61 ILE ILE A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 LYS 66 66 66 LYS LYS A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 LEU 71 71 71 LEU LEU A . n A 1 72 GLY 72 72 72 GLY GLY A . n A 1 73 ASP 73 73 73 ASP ASP A . n A 1 74 GLN 74 74 74 GLN GLN A . n A 1 75 SER 75 75 75 SER SER A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 ARG 82 82 82 ARG ARG A . n A 1 83 PRO 83 83 83 PRO PRO A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 ALA 85 85 85 ALA ALA A . n A 1 86 GLN 86 86 86 GLN GLN A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 GLY 88 88 88 GLY GLY A . n A 1 89 ILE 89 89 89 ILE ILE A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 VAL 94 94 94 VAL VAL A . n A 1 95 LEU 95 95 95 LEU LEU A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 GLU 97 97 97 GLU GLU A . n A 1 98 LEU 98 98 98 LEU LEU A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 ALA 103 103 103 ALA ALA A . n A 1 104 PHE 104 104 104 PHE PHE A . n A 1 105 ILE 105 105 105 ILE ILE A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 SER 107 107 107 SER SER A . n A 1 108 GLY 108 108 108 GLY GLY A . n A 1 109 GLU 109 109 109 GLU GLU A . n A 1 110 ARG 110 110 110 ARG ARG A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 PHE 114 114 114 PHE PHE A . n A 1 115 GLU 115 115 115 GLU GLU A . n A 1 116 MET 116 116 116 MET MET A . n A 1 117 PHE 117 117 117 PHE PHE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 THR 121 121 121 THR THR A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 ALA 123 123 123 ALA ALA A . n A 1 124 GLY 124 124 124 GLY GLY A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 ASP 126 126 126 ASP ASP A . n A 1 127 THR 127 127 127 THR THR A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 ARG 129 129 129 ARG ARG A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 THR 132 132 132 THR THR A . n A 1 133 ASN 133 133 133 ASN ASN A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 SER 137 137 137 SER SER A . n A 1 138 TYR 138 138 138 TYR TYR A . n A 1 139 THR 139 139 139 THR THR A . n A 1 140 LEU 140 140 140 LEU LEU A . n A 1 141 ASP 141 141 141 ASP ASP A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 SER 143 143 143 SER SER A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 TYR 145 145 145 TYR TYR A . n A 1 146 ARG 146 146 146 ARG ARG A . n A 1 147 ASN 147 147 147 ASN ASN A . n A 1 148 LEU 148 148 148 LEU LEU A . n A 1 149 VAL 149 149 149 VAL VAL A . n A 1 150 TRP 150 150 150 TRP TRP A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 VAL 152 152 152 VAL VAL A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 THR 154 154 154 THR THR A . n A 1 155 ASP 155 155 155 ASP ASP A . n A 1 156 SER 156 156 156 SER SER A . n A 1 157 ALA 157 157 157 ALA ALA A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 TYR 159 159 159 TYR TYR A . n A 1 160 PRO 160 160 160 PRO PRO A . n A 1 161 VAL 161 161 161 VAL VAL A . n A 1 162 ILE 162 162 162 ILE ILE A . n A 1 163 LYS 163 163 163 LYS LYS A . n A 1 164 GLY 164 164 164 GLY GLY A . n A 1 165 THR 165 165 165 THR THR A . n A 1 166 TYR 166 166 166 TYR TYR A . n A 1 167 ASN 167 167 167 ASN ASN A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 THR 169 169 169 THR THR A . n A 1 170 GLY 170 170 170 GLY GLY A . n A 1 171 THR 171 171 171 THR THR A . n A 1 172 GLN 172 172 172 GLN GLN A . n A 1 173 PRO 173 173 173 PRO PRO A . n A 1 174 ILE 174 174 174 ILE ILE A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TYR 176 176 176 TYR TYR A . n A 1 177 PHE 177 177 177 PHE PHE A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 HIS 181 181 181 HIS HIS A . n A 1 182 HIS 182 182 182 HIS HIS A . n A 1 183 PRO 183 183 183 PRO PRO A . n A 1 184 LEU 184 184 184 LEU LEU A . n A 1 185 ASP 185 185 185 ASP ASP A . n A 1 186 THR 186 186 186 THR THR A . n A 1 187 THR 187 187 187 THR THR A . n A 1 188 VAL 188 188 188 VAL VAL A . n A 1 189 GLN 189 189 189 GLN GLN A . n A 1 190 ASP 190 190 190 ASP ASP A . n A 1 191 ASN 191 191 191 ASN ASN A . n A 1 192 LEU 192 192 192 LEU LEU A . n A 1 193 TYR 193 193 193 TYR TYR A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 GLY 196 196 196 GLY GLY A . n A 1 197 ASP 197 197 197 ASP ASP A . n A 1 198 LYS 198 198 198 LYS LYS A . n A 1 199 TYR 199 199 199 TYR TYR A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 ARG 201 201 201 ARG ARG A . n A 1 202 MET 202 202 202 MET MET A . n A 1 203 GLY 203 203 203 GLY GLY A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 GLU 205 205 205 GLU GLU A . n A 1 206 SER 206 206 206 SER SER A . n A 1 207 MET 207 207 207 MET MET A . n A 1 208 ASN 208 208 208 ASN ASN A . n A 1 209 PHE 209 209 209 PHE PHE A . n A 1 210 ALA 210 210 210 ALA ALA A . n A 1 211 LYS 211 211 211 LYS LYS A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 PRO 213 213 213 PRO PRO A . n A 1 214 GLU 214 214 214 GLU GLU A . n A 1 215 ILE 215 215 215 ILE ILE A . n A 1 216 ALA 216 216 216 ALA ALA A . n A 1 217 ALA 217 217 217 ALA ALA A . n A 1 218 ARG 218 218 218 ARG ARG A . n A 1 219 PRO 219 219 219 PRO PRO A . n A 1 220 ALA 220 220 220 ALA ALA A . n A 1 221 VAL 221 221 221 VAL VAL A . n A 1 222 ASN 222 222 222 ASN ASN A . n A 1 223 GLY 223 223 223 GLY GLY A . n A 1 224 GLN 224 224 224 GLN GLN A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 SER 226 226 226 SER SER A . n A 1 227 ARG 227 227 227 ARG ARG A . n A 1 228 ILE 228 228 228 ILE ILE A . n A 1 229 ASP 229 229 229 ASP ASP A . n A 1 230 TYR 230 230 230 TYR TYR A . n A 1 231 TYR 231 231 231 TYR TYR A . n A 1 232 TRP 232 232 232 TRP TRP A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 LEU 235 235 235 LEU LEU A . n A 1 236 ARG 236 236 236 ARG ARG A . n A 1 237 PRO 237 237 237 PRO PRO A . n A 1 238 GLY 238 238 238 GLY GLY A . n A 1 239 GLU 239 239 239 GLU GLU A . n A 1 240 THR 240 240 240 THR THR A . n A 1 241 LEU 241 241 241 LEU LEU A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 VAL 243 243 243 VAL VAL A . n A 1 244 GLU 244 244 244 GLU GLU A . n A 1 245 SER 245 245 245 SER SER A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 GLY 247 247 247 GLY GLY A . n A 1 248 ASN 248 248 248 ASN ASN A . n A 1 249 LEU 249 249 249 LEU LEU A . n A 1 250 ILE 250 250 250 ILE ILE A . n A 1 251 ALA 251 251 251 ALA ALA A . n A 1 252 PRO 252 252 252 PRO PRO A . n A 1 253 TRP 253 253 253 TRP TRP A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 ALA 255 255 255 ALA ALA A . n A 1 256 TYR 256 256 256 TYR TYR A . n A 1 257 LYS 257 257 257 LYS LYS A . n A 1 258 PHE 258 258 258 PHE PHE A . n A 1 259 VAL 259 259 259 VAL VAL A . n A 1 260 SER 260 260 260 SER SER A . n A 1 261 THR 261 261 261 THR THR A . n A 1 262 ASN 262 262 262 ASN ASN A . n A 1 263 LYS 263 263 263 LYS LYS A . n A 1 264 LYS 264 264 264 LYS LYS A . n A 1 265 GLY 265 265 265 GLY GLY A . n A 1 266 ALA 266 266 266 ALA ALA A . n A 1 267 VAL 267 267 267 VAL VAL A . n A 1 268 PHE 268 268 268 PHE PHE A . n A 1 269 LYS 269 269 269 LYS LYS A . n A 1 270 SER 270 270 270 SER SER A . n A 1 271 ASP 271 271 271 ASP ASP A . n A 1 272 LEU 272 272 272 LEU LEU A . n A 1 273 PRO 273 273 273 PRO PRO A . n A 1 274 ILE 274 274 274 ILE ILE A . n A 1 275 GLU 275 275 275 GLU GLU A . n A 1 276 ASN 276 276 276 ASN ASN A . n A 1 277 CYS 277 277 277 CYS CYS A . n A 1 278 ASP 278 278 278 ASP ASP A . n A 1 279 ALA 279 279 279 ALA ALA A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 CYS 281 281 281 CYS CYS A . n A 1 282 GLN 282 282 282 GLN GLN A . n A 1 283 THR 283 283 283 THR THR A . n A 1 284 ILE 284 284 284 ILE ILE A . n A 1 285 THR 285 285 285 THR THR A . n A 1 286 GLY 286 286 286 GLY GLY A . n A 1 287 VAL 287 287 287 VAL VAL A . n A 1 288 LEU 288 288 288 LEU LEU A . n A 1 289 ARG 289 289 289 ARG ARG A . n A 1 290 THR 290 290 290 THR THR A . n A 1 291 ASN 291 291 291 ASN ASN A . n A 1 292 LYS 292 292 292 LYS LYS A . n A 1 293 THR 293 293 293 THR THR A . n A 1 294 PHE 294 294 294 PHE PHE A . n A 1 295 GLN 295 295 295 GLN GLN A . n A 1 296 ASN 296 296 296 ASN ASN A . n A 1 297 VAL 297 297 297 VAL VAL A . n A 1 298 SER 298 298 298 SER SER A . n A 1 299 PRO 299 299 299 PRO PRO A . n A 1 300 LEU 300 300 300 LEU LEU A . n A 1 301 TRP 301 301 301 TRP TRP A . n A 1 302 ILE 302 302 302 ILE ILE A . n A 1 303 GLY 303 303 303 GLY GLY A . n A 1 304 GLU 304 304 304 GLU GLU A . n A 1 305 CYS 305 305 305 CYS CYS A . n A 1 306 PRO 306 306 306 PRO PRO A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 TYR 308 308 308 TYR TYR A . n A 1 309 VAL 309 309 309 VAL VAL A . n A 1 310 LYS 310 310 310 LYS LYS A . n A 1 311 SER 311 311 311 SER SER A . n A 1 312 GLU 312 312 312 GLU GLU A . n A 1 313 SER 313 313 313 SER SER A . n A 1 314 LEU 314 314 314 LEU LEU A . n A 1 315 ARG 315 315 315 ARG ARG A . n A 1 316 LEU 316 316 316 LEU LEU A . n A 1 317 ALA 317 317 317 ALA ALA A . n A 1 318 THR 318 318 318 THR THR A . n A 1 319 GLY 319 319 319 GLY GLY A . n A 1 320 LEU 320 320 320 LEU LEU A . n A 1 321 ARG 321 321 321 ARG ARG A . n A 1 322 ASN 322 322 322 ASN ASN A . n A 1 323 VAL 323 323 323 VAL VAL A . n A 1 324 PRO 324 324 324 PRO PRO A . n A 1 325 GLN 325 325 325 GLN GLN A . n B 2 1 GLY 1 330 330 GLY GLY B . n B 2 2 ILE 2 331 331 ILE ILE B . n B 2 3 PHE 3 332 332 PHE PHE B . n B 2 4 GLY 4 333 333 GLY GLY B . n B 2 5 ALA 5 334 334 ALA ALA B . n B 2 6 ILE 6 335 335 ILE ILE B . n B 2 7 ALA 7 336 336 ALA ALA B . n B 2 8 GLY 8 337 337 GLY GLY B . n B 2 9 PHE 9 338 338 PHE PHE B . n B 2 10 ILE 10 339 339 ILE ILE B . n B 2 11 GLU 11 340 340 GLU GLU B . n B 2 12 GLY 12 341 341 GLY GLY B . n B 2 13 GLY 13 342 342 GLY GLY B . n B 2 14 TRP 14 343 343 TRP TRP B . n B 2 15 THR 15 344 344 THR THR B . n B 2 16 GLY 16 345 345 GLY GLY B . n B 2 17 MET 17 346 346 MET MET B . n B 2 18 ILE 18 347 347 ILE ILE B . n B 2 19 ASP 19 348 348 ASP ASP B . n B 2 20 GLY 20 349 349 GLY GLY B . n B 2 21 TRP 21 350 350 TRP TRP B . n B 2 22 TYR 22 351 351 TYR TYR B . n B 2 23 GLY 23 352 352 GLY GLY B . n B 2 24 TYR 24 353 353 TYR TYR B . n B 2 25 HIS 25 354 354 HIS HIS B . n B 2 26 HIS 26 355 355 HIS HIS B . n B 2 27 GLU 27 356 356 GLU GLU B . n B 2 28 ASN 28 357 357 ASN ASN B . n B 2 29 SER 29 358 358 SER SER B . n B 2 30 GLN 30 359 359 GLN GLN B . n B 2 31 GLY 31 360 360 GLY GLY B . n B 2 32 SER 32 361 361 SER SER B . n B 2 33 GLY 33 362 362 GLY GLY B . n B 2 34 TYR 34 363 363 TYR TYR B . n B 2 35 ALA 35 364 364 ALA ALA B . n B 2 36 ALA 36 365 365 ALA ALA B . n B 2 37 ASP 37 366 366 ASP ASP B . n B 2 38 ARG 38 367 367 ARG ARG B . n B 2 39 GLU 39 368 368 GLU GLU B . n B 2 40 SER 40 369 369 SER SER B . n B 2 41 THR 41 370 370 THR THR B . n B 2 42 GLN 42 371 371 GLN GLN B . n B 2 43 LYS 43 372 372 LYS LYS B . n B 2 44 ALA 44 373 373 ALA ALA B . n B 2 45 ILE 45 374 374 ILE ILE B . n B 2 46 ASP 46 375 375 ASP ASP B . n B 2 47 GLY 47 376 376 GLY GLY B . n B 2 48 ILE 48 377 377 ILE ILE B . n B 2 49 THR 49 378 378 THR THR B . n B 2 50 ASN 50 379 379 ASN ASN B . n B 2 51 LYS 51 380 380 LYS LYS B . n B 2 52 VAL 52 381 381 VAL VAL B . n B 2 53 ASN 53 382 382 ASN ASN B . n B 2 54 SER 54 383 383 SER SER B . n B 2 55 ILE 55 384 384 ILE ILE B . n B 2 56 ILE 56 385 385 ILE ILE B . n B 2 57 ASN 57 386 386 ASN ASN B . n B 2 58 LYS 58 387 387 LYS LYS B . n B 2 59 MET 59 388 388 MET MET B . n B 2 60 ASN 60 389 389 ASN ASN B . n B 2 61 THR 61 390 390 THR THR B . n B 2 62 GLN 62 391 391 GLN GLN B . n B 2 63 PHE 63 392 392 PHE PHE B . n B 2 64 GLU 64 393 393 GLU GLU B . n B 2 65 ALA 65 394 394 ALA ALA B . n B 2 66 VAL 66 395 395 VAL VAL B . n B 2 67 ASP 67 396 396 ASP ASP B . n B 2 68 HIS 68 397 397 HIS HIS B . n B 2 69 GLU 69 398 398 GLU GLU B . n B 2 70 PHE 70 399 399 PHE PHE B . n B 2 71 SER 71 400 400 SER SER B . n B 2 72 ASN 72 401 401 ASN ASN B . n B 2 73 LEU 73 402 402 LEU LEU B . n B 2 74 GLU 74 403 403 GLU GLU B . n B 2 75 ARG 75 404 404 ARG ARG B . n B 2 76 ARG 76 405 405 ARG ARG B . n B 2 77 ILE 77 406 406 ILE ILE B . n B 2 78 GLY 78 407 407 GLY GLY B . n B 2 79 ASN 79 408 408 ASN ASN B . n B 2 80 LEU 80 409 409 LEU LEU B . n B 2 81 ASN 81 410 410 ASN ASN B . n B 2 82 LYS 82 411 411 LYS LYS B . n B 2 83 ARG 83 412 412 ARG ARG B . n B 2 84 MET 84 413 413 MET MET B . n B 2 85 GLU 85 414 414 GLU GLU B . n B 2 86 ASP 86 415 415 ASP ASP B . n B 2 87 GLY 87 416 416 GLY GLY B . n B 2 88 PHE 88 417 417 PHE PHE B . n B 2 89 LEU 89 418 418 LEU LEU B . n B 2 90 ASP 90 419 419 ASP ASP B . n B 2 91 VAL 91 420 420 VAL VAL B . n B 2 92 TRP 92 421 421 TRP TRP B . n B 2 93 THR 93 422 422 THR THR B . n B 2 94 TYR 94 423 423 TYR TYR B . n B 2 95 ASN 95 424 424 ASN ASN B . n B 2 96 ALA 96 425 425 ALA ALA B . n B 2 97 GLU 97 426 426 GLU GLU B . n B 2 98 LEU 98 427 427 LEU LEU B . n B 2 99 LEU 99 428 428 LEU LEU B . n B 2 100 VAL 100 429 429 VAL VAL B . n B 2 101 LEU 101 430 430 LEU LEU B . n B 2 102 LEU 102 431 431 LEU LEU B . n B 2 103 GLU 103 432 432 GLU GLU B . n B 2 104 ASN 104 433 433 ASN ASN B . n B 2 105 GLU 105 434 434 GLU GLU B . n B 2 106 ARG 106 435 435 ARG ARG B . n B 2 107 THR 107 436 436 THR THR B . n B 2 108 LEU 108 437 437 LEU LEU B . n B 2 109 ASP 109 438 438 ASP ASP B . n B 2 110 LEU 110 439 439 LEU LEU B . n B 2 111 HIS 111 440 440 HIS HIS B . n B 2 112 ASP 112 441 441 ASP ASP B . n B 2 113 ALA 113 442 442 ALA ALA B . n B 2 114 ASN 114 443 443 ASN ASN B . n B 2 115 VAL 115 444 444 VAL VAL B . n B 2 116 LYS 116 445 445 LYS LYS B . n B 2 117 ASN 117 446 446 ASN ASN B . n B 2 118 LEU 118 447 447 LEU LEU B . n B 2 119 TYR 119 448 448 TYR TYR B . n B 2 120 GLU 120 449 449 GLU GLU B . n B 2 121 LYS 121 450 450 LYS LYS B . n B 2 122 VAL 122 451 451 VAL VAL B . n B 2 123 LYS 123 452 452 LYS LYS B . n B 2 124 SER 124 453 453 SER SER B . n B 2 125 GLN 125 454 454 GLN GLN B . n B 2 126 LEU 126 455 455 LEU LEU B . n B 2 127 ARG 127 456 456 ARG ARG B . n B 2 128 ASP 128 457 457 ASP ASP B . n B 2 129 ASN 129 458 458 ASN ASN B . n B 2 130 ALA 130 459 459 ALA ALA B . n B 2 131 ASN 131 460 460 ASN ASN B . n B 2 132 ASP 132 461 461 ASP ASP B . n B 2 133 LEU 133 462 462 LEU LEU B . n B 2 134 GLY 134 463 463 GLY GLY B . n B 2 135 ASN 135 464 464 ASN ASN B . n B 2 136 GLY 136 465 465 GLY GLY B . n B 2 137 CYS 137 466 466 CYS CYS B . n B 2 138 PHE 138 467 467 PHE PHE B . n B 2 139 GLU 139 468 468 GLU GLU B . n B 2 140 PHE 140 469 469 PHE PHE B . n B 2 141 TRP 141 470 470 TRP TRP B . n B 2 142 HIS 142 471 471 HIS HIS B . n B 2 143 LYS 143 472 472 LYS LYS B . n B 2 144 CYS 144 473 473 CYS CYS B . n B 2 145 ASP 145 474 474 ASP ASP B . n B 2 146 ASN 146 475 475 ASN ASN B . n B 2 147 GLU 147 476 476 GLU GLU B . n B 2 148 CYS 148 477 477 CYS CYS B . n B 2 149 MET 149 478 478 MET MET B . n B 2 150 GLU 150 479 479 GLU GLU B . n B 2 151 SER 151 480 480 SER SER B . n B 2 152 VAL 152 481 481 VAL VAL B . n B 2 153 LYS 153 482 482 LYS LYS B . n B 2 154 ASN 154 483 483 ASN ASN B . n B 2 155 GLY 155 484 484 GLY GLY B . n B 2 156 THR 156 485 485 THR THR B . n B 2 157 TYR 157 486 486 TYR TYR B . n B 2 158 ASP 158 487 487 ASP ASP B . n B 2 159 TYR 159 488 488 TYR TYR B . n B 2 160 PRO 160 489 489 PRO PRO B . n B 2 161 LYS 161 490 490 LYS LYS B . n B 2 162 TYR 162 491 491 TYR TYR B . n B 2 163 GLN 163 492 492 GLN GLN B . n B 2 164 LYS 164 493 493 LYS LYS B . n B 2 165 GLU 165 494 494 GLU GLU B . n B 2 166 SER 166 495 495 SER SER B . n B 2 167 LYS 167 496 496 LYS LYS B . n B 2 168 LEU 168 497 497 LEU LEU B . n B 2 169 ASN 169 498 498 ASN ASN B . n B 2 170 ARG 170 499 499 ARG ARG B . n B 2 171 GLN 171 500 500 GLN GLN 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 3 NAG 1 601 601 NAG NAG A . D 3 NAG 1 602 602 NAG NAG A . E 4 SIA 1 603 801 SIA SIA A . F 5 GAL 2 604 802 GAL GAL A . G 3 NAG 3 605 803 NAG NAG A . H 5 GAL 4 606 804 GAL GAL A . I 3 NAG 1 601 604 NAG NAG B . J 3 NAG 2 602 605 NAG NAG B . K 6 BMA 3 603 606 BMA BMA B . L 7 HOH 1 701 115 HOH HOH A . L 7 HOH 2 702 9 HOH HOH A . L 7 HOH 3 703 75 HOH HOH A . L 7 HOH 4 704 72 HOH HOH A . L 7 HOH 5 705 5 HOH HOH A . L 7 HOH 6 706 85 HOH HOH A . L 7 HOH 7 707 17 HOH HOH A . L 7 HOH 8 708 37 HOH HOH A . L 7 HOH 9 709 129 HOH HOH A . L 7 HOH 10 710 2 HOH HOH A . L 7 HOH 11 711 98 HOH HOH A . L 7 HOH 12 712 84 HOH HOH A . L 7 HOH 13 713 107 HOH HOH A . L 7 HOH 14 714 23 HOH HOH A . L 7 HOH 15 715 27 HOH HOH A . L 7 HOH 16 716 78 HOH HOH A . L 7 HOH 17 717 21 HOH HOH A . L 7 HOH 18 718 35 HOH HOH A . L 7 HOH 19 719 14 HOH HOH A . L 7 HOH 20 720 52 HOH HOH A . L 7 HOH 21 721 20 HOH HOH A . L 7 HOH 22 722 49 HOH HOH A . L 7 HOH 23 723 16 HOH HOH A . L 7 HOH 24 724 111 HOH HOH A . L 7 HOH 25 725 38 HOH HOH A . L 7 HOH 26 726 109 HOH HOH A . L 7 HOH 27 727 122 HOH HOH A . L 7 HOH 28 728 117 HOH HOH A . L 7 HOH 29 729 125 HOH HOH A . L 7 HOH 30 730 118 HOH HOH A . L 7 HOH 31 731 30 HOH HOH A . L 7 HOH 32 732 19 HOH HOH A . L 7 HOH 33 733 3 HOH HOH A . L 7 HOH 34 734 4 HOH HOH A . L 7 HOH 35 735 8 HOH HOH A . L 7 HOH 36 736 48 HOH HOH A . L 7 HOH 37 737 18 HOH HOH A . L 7 HOH 38 738 69 HOH HOH A . L 7 HOH 39 739 1 HOH HOH A . L 7 HOH 40 740 99 HOH HOH A . L 7 HOH 41 741 53 HOH HOH A . L 7 HOH 42 742 124 HOH HOH A . L 7 HOH 43 743 57 HOH HOH A . L 7 HOH 44 744 120 HOH HOH A . L 7 HOH 45 745 56 HOH HOH A . L 7 HOH 46 746 31 HOH HOH A . L 7 HOH 47 747 43 HOH HOH A . L 7 HOH 48 748 45 HOH HOH A . L 7 HOH 49 749 105 HOH HOH A . L 7 HOH 50 750 7 HOH HOH A . L 7 HOH 51 751 123 HOH HOH A . L 7 HOH 52 752 87 HOH HOH A . L 7 HOH 53 753 61 HOH HOH A . L 7 HOH 54 754 76 HOH HOH A . L 7 HOH 55 755 12 HOH HOH A . L 7 HOH 56 756 79 HOH HOH A . L 7 HOH 57 757 70 HOH HOH A . L 7 HOH 58 758 110 HOH HOH A . L 7 HOH 59 759 104 HOH HOH A . L 7 HOH 60 760 36 HOH HOH A . L 7 HOH 61 761 64 HOH HOH A . L 7 HOH 62 762 91 HOH HOH A . L 7 HOH 63 763 6 HOH HOH A . L 7 HOH 64 764 71 HOH HOH A . L 7 HOH 65 765 113 HOH HOH A . L 7 HOH 66 766 82 HOH HOH A . L 7 HOH 67 767 130 HOH HOH A . L 7 HOH 68 768 39 HOH HOH A . L 7 HOH 69 769 103 HOH HOH A . L 7 HOH 70 770 92 HOH HOH A . L 7 HOH 71 771 26 HOH HOH A . L 7 HOH 72 772 128 HOH HOH A . L 7 HOH 73 773 131 HOH HOH A . L 7 HOH 74 774 114 HOH HOH A . L 7 HOH 75 775 136 HOH HOH A . M 7 HOH 1 701 46 HOH HOH B . M 7 HOH 2 702 86 HOH HOH B . M 7 HOH 3 703 102 HOH HOH B . M 7 HOH 4 704 90 HOH HOH B . M 7 HOH 5 705 77 HOH HOH B . M 7 HOH 6 706 119 HOH HOH B . M 7 HOH 7 707 32 HOH HOH B . M 7 HOH 8 708 13 HOH HOH B . M 7 HOH 9 709 97 HOH HOH B . M 7 HOH 10 710 34 HOH HOH B . M 7 HOH 11 711 66 HOH HOH B . M 7 HOH 12 712 58 HOH HOH B . M 7 HOH 13 713 51 HOH HOH B . M 7 HOH 14 714 15 HOH HOH B . M 7 HOH 15 715 11 HOH HOH B . M 7 HOH 16 716 106 HOH HOH B . M 7 HOH 17 717 133 HOH HOH B . M 7 HOH 18 718 74 HOH HOH B . M 7 HOH 19 719 42 HOH HOH B . M 7 HOH 20 720 81 HOH HOH B . M 7 HOH 21 721 112 HOH HOH B . M 7 HOH 22 722 116 HOH HOH B . M 7 HOH 23 723 93 HOH HOH B . M 7 HOH 24 724 67 HOH HOH B . M 7 HOH 25 725 126 HOH HOH B . M 7 HOH 26 726 41 HOH HOH B . M 7 HOH 27 727 60 HOH HOH B . M 7 HOH 28 728 101 HOH HOH B . M 7 HOH 29 729 47 HOH HOH B . M 7 HOH 30 730 50 HOH HOH B . M 7 HOH 31 731 10 HOH HOH B . M 7 HOH 32 732 44 HOH HOH B . M 7 HOH 33 733 88 HOH HOH B . M 7 HOH 34 734 29 HOH HOH B . M 7 HOH 35 735 134 HOH HOH B . M 7 HOH 36 736 40 HOH HOH B . M 7 HOH 37 737 62 HOH HOH B . M 7 HOH 38 738 22 HOH HOH B . M 7 HOH 39 739 65 HOH HOH B . M 7 HOH 40 740 89 HOH HOH B . M 7 HOH 41 741 96 HOH HOH B . M 7 HOH 42 742 68 HOH HOH B . M 7 HOH 43 743 94 HOH HOH B . M 7 HOH 44 744 33 HOH HOH B . M 7 HOH 45 745 55 HOH HOH B . M 7 HOH 46 746 95 HOH HOH B . M 7 HOH 47 747 135 HOH HOH B . M 7 HOH 48 748 132 HOH HOH B . M 7 HOH 49 749 73 HOH HOH B . M 7 HOH 50 750 63 HOH HOH B . M 7 HOH 51 751 28 HOH HOH B . M 7 HOH 52 752 83 HOH HOH B . M 7 HOH 53 753 80 HOH HOH B . M 7 HOH 54 754 24 HOH HOH B . M 7 HOH 55 755 59 HOH HOH B . M 7 HOH 56 756 100 HOH HOH B . M 7 HOH 57 757 121 HOH HOH B . M 7 HOH 58 758 25 HOH HOH B . M 7 HOH 59 759 127 HOH HOH B . M 7 HOH 60 760 108 HOH HOH B . M 7 HOH 61 761 54 HOH HOH B . # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 35510 ? 1 MORE -102 ? 1 'SSA (A^2)' 61810 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_565 -y,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 -57.0970000000 0.8660254038 -0.5000000000 0.0000000000 98.8949049598 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038 0.0000000000 -114.1940000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 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 2016-04-13 2 'Structure model' 1 1 2016-04-20 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # _pdbx_refine_tls.id 1 _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x -40.9282 _pdbx_refine_tls.origin_y 39.6371 _pdbx_refine_tls.origin_z -10.1962 _pdbx_refine_tls.T[1][1] 0.1573 _pdbx_refine_tls.T[1][1]_esd ? _pdbx_refine_tls.T[1][2] -0.0207 _pdbx_refine_tls.T[1][2]_esd ? _pdbx_refine_tls.T[1][3] -0.0221 _pdbx_refine_tls.T[1][3]_esd ? _pdbx_refine_tls.T[2][2] 0.2237 _pdbx_refine_tls.T[2][2]_esd ? _pdbx_refine_tls.T[2][3] 0.0092 _pdbx_refine_tls.T[2][3]_esd ? _pdbx_refine_tls.T[3][3] 0.2427 _pdbx_refine_tls.T[3][3]_esd ? _pdbx_refine_tls.L[1][1] 0.1321 _pdbx_refine_tls.L[1][1]_esd ? _pdbx_refine_tls.L[1][2] 0.0041 _pdbx_refine_tls.L[1][2]_esd ? _pdbx_refine_tls.L[1][3] -0.0509 _pdbx_refine_tls.L[1][3]_esd ? _pdbx_refine_tls.L[2][2] 0.1797 _pdbx_refine_tls.L[2][2]_esd ? _pdbx_refine_tls.L[2][3] 0.0444 _pdbx_refine_tls.L[2][3]_esd ? _pdbx_refine_tls.L[3][3] 0.7490 _pdbx_refine_tls.L[3][3]_esd ? _pdbx_refine_tls.S[1][1] 0.0019 _pdbx_refine_tls.S[1][1]_esd ? _pdbx_refine_tls.S[1][2] -0.0087 _pdbx_refine_tls.S[1][2]_esd ? _pdbx_refine_tls.S[1][3] 0.0167 _pdbx_refine_tls.S[1][3]_esd ? _pdbx_refine_tls.S[2][1] 0.0395 _pdbx_refine_tls.S[2][1]_esd ? _pdbx_refine_tls.S[2][2] 0.0092 _pdbx_refine_tls.S[2][2]_esd ? _pdbx_refine_tls.S[2][3] -0.0555 _pdbx_refine_tls.S[2][3]_esd ? _pdbx_refine_tls.S[3][1] 0.0124 _pdbx_refine_tls.S[3][1]_esd ? _pdbx_refine_tls.S[3][2] 0.1233 _pdbx_refine_tls.S[3][2]_esd ? _pdbx_refine_tls.S[3][3] 0.0000 _pdbx_refine_tls.S[3][3]_esd ? # _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.refine_tls_id 1 _pdbx_refine_tls_group.beg_label_asym_id ? _pdbx_refine_tls_group.beg_label_seq_id ? _pdbx_refine_tls_group.beg_auth_asym_id ? _pdbx_refine_tls_group.beg_auth_seq_id ? _pdbx_refine_tls_group.end_label_asym_id ? _pdbx_refine_tls_group.end_label_seq_id ? _pdbx_refine_tls_group.end_auth_asym_id ? _pdbx_refine_tls_group.end_auth_seq_id ? _pdbx_refine_tls_group.selection ? _pdbx_refine_tls_group.selection_details all # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? 'data processing' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? . 1 ? phasing ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? . 2 ? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 3 ? refinement ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.8.3_1479 4 ? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? SCALA ? ? ? . 5 ? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? SCALEPACK ? ? ? . 6 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O A GLY 196 ? ? O A HOH 701 ? ? 1.96 2 1 N A ASN 46 ? ? O A HOH 702 ? ? 2.06 3 1 OE1 A GLU 312 ? ? O A HOH 703 ? ? 2.10 4 1 OE2 B GLU 494 ? ? O B HOH 701 ? ? 2.13 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 46 ? ? 46.75 29.59 2 1 LYS A 53 ? ? 58.15 -122.73 3 1 GLU A 109 ? ? -148.88 -29.24 4 1 CYS A 135 ? ? -119.40 76.58 5 1 SER A 143 ? ? -135.36 -157.59 6 1 ASP A 155 ? ? 12.68 -62.61 7 1 SER A 156 ? ? -160.83 -5.08 8 1 ALA A 157 ? ? -69.70 -169.21 9 1 THR A 204 ? ? -128.06 -166.26 10 1 TRP A 253 ? ? -122.45 -67.60 11 1 LYS A 263 ? ? -76.37 -136.33 12 1 ARG B 456 ? ? 52.34 -124.34 # _pdbx_unobs_or_zero_occ_atoms.id 1 _pdbx_unobs_or_zero_occ_atoms.PDB_model_num 1 _pdbx_unobs_or_zero_occ_atoms.polymer_flag Y _pdbx_unobs_or_zero_occ_atoms.occupancy_flag 1 _pdbx_unobs_or_zero_occ_atoms.auth_asym_id A _pdbx_unobs_or_zero_occ_atoms.auth_comp_id THR _pdbx_unobs_or_zero_occ_atoms.auth_seq_id 121 _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code ? _pdbx_unobs_or_zero_occ_atoms.auth_atom_id CG2 _pdbx_unobs_or_zero_occ_atoms.label_alt_id ? _pdbx_unobs_or_zero_occ_atoms.label_asym_id A _pdbx_unobs_or_zero_occ_atoms.label_comp_id THR _pdbx_unobs_or_zero_occ_atoms.label_seq_id 121 _pdbx_unobs_or_zero_occ_atoms.label_atom_id CG2 # 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 N 0 A NAG 601 ? C NAG ? 2 1 N 0 A NAG 602 ? D NAG ? 3 1 N 0 B NAG 601 ? I NAG ? 4 1 N 0 B NAG 602 ? J NAG ? 5 1 N 0 B BMA 603 ? K BMA ? # loop_ _pdbx_audit_support.funding_organization _pdbx_audit_support.country _pdbx_audit_support.grant_number _pdbx_audit_support.ordinal 'China Ministry of Science and Technology National 973 Project' China 2011CB504703 1 'Intramural Special Grant for Influenza Virus Research from the Chinese Academy of Sciences' China KJZD-EW-L09 2 'Intramural Special Grant for Strategic Priority Research Program of the Chinese Academy of Sciences' China XDB08020100 3 'National Natural Science Foundation of China' China 31402196 4 'China National Grand S&T Special Project' China 2014ZX10004002 5 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'O-SIALIC ACID' SIA 5 BETA-D-GALACTOSE GAL 6 BETA-D-MANNOSE BMA 7 water HOH #