data_5EFI # _entry.id 5EFI # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.286 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5EFI WWPDB D_1000214635 # _pdbx_database_related.db_name PDB _pdbx_database_related.details '5fkp contains the same structure complexed with the p99 peptide' _pdbx_database_related.db_id 5fkp _pdbx_database_related.content_type 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 5EFI _pdbx_database_status.recvd_initial_deposition_date 2015-10-23 _pdbx_database_status.SG_entry N _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Girardi, E.' 1 'Wang, J.' 2 'Zajonc, D.M.' 3 # _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 US _citation.database_id_Medline ? _citation.details ? _citation.id primary _citation.journal_abbrev J.Biol.Chem. _citation.journal_id_ASTM JBCHA3 _citation.journal_id_CSD 0071 _citation.journal_id_ISSN 1083-351X _citation.journal_full ? _citation.journal_issue ? _citation.journal_volume 291 _citation.language ? _citation.page_first 10677 _citation.page_last 10683 _citation.title ;Structure of an alpha-Helical Peptide and Lipopeptide Bound to the Nonclassical Major Histocompatibility Complex (MHC) Class I Molecule CD1d. ; _citation.year 2016 _citation.database_id_CSD ? _citation.pdbx_database_id_DOI 10.1074/jbc.M115.702118 _citation.pdbx_database_id_PubMed 27006394 _citation.unpublished_flag ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Girardi, E.' 1 primary 'Wang, J.' 2 primary 'Zajonc, D.M.' 3 # _cell.angle_alpha 90.00 _cell.angle_alpha_esd ? _cell.angle_beta 90.00 _cell.angle_beta_esd ? _cell.angle_gamma 90.00 _cell.angle_gamma_esd ? _cell.entry_id 5EFI _cell.details ? _cell.formula_units_Z ? _cell.length_a 42.190 _cell.length_a_esd ? _cell.length_b 107.850 _cell.length_b_esd ? _cell.length_c 110.340 _cell.length_c_esd ? _cell.volume ? _cell.volume_esd ? _cell.Z_PDB 4 _cell.reciprocal_angle_alpha ? _cell.reciprocal_angle_beta ? _cell.reciprocal_angle_gamma ? _cell.reciprocal_angle_alpha_esd ? _cell.reciprocal_angle_beta_esd ? _cell.reciprocal_angle_gamma_esd ? _cell.reciprocal_length_a ? _cell.reciprocal_length_b ? _cell.reciprocal_length_c ? _cell.reciprocal_length_a_esd ? _cell.reciprocal_length_b_esd ? _cell.reciprocal_length_c_esd ? _cell.pdbx_unique_axis ? # _symmetry.entry_id 5EFI _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 _symmetry.space_group_name_Hall ? _symmetry.space_group_name_H-M 'P 21 21 21' _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 'Antigen-presenting glycoprotein CD1d1' 32609.609 1 ? ? ? ? 2 polymer man Beta-2-microglobulin 11660.350 1 ? ? ? ? 3 polymer syn p99p 2816.180 1 ? ? ? 'Palmitate residue covalently linked to Lys 12' 4 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? 5 non-polymer man BETA-D-MANNOSE 180.156 1 ? ? ? ? 6 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 7 non-polymer man ALPHA-L-FUCOSE 164.156 1 ? ? ? ? 8 non-polymer syn 'CITRIC ACID' 192.124 1 ? ? ? ? 9 non-polymer syn 'SODIUM ION' 22.990 1 ? ? ? ? 10 non-polymer man 'PALMITIC ACID' 256.424 1 ? ? ? ? 11 non-polymer syn 'OCTANOIC ACID (CAPRYLIC ACID)' 144.211 1 ? ? ? ? 12 water nat water 18.015 204 ? ? ? ? # 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 ;SEAQQKNYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRD IQELVKMMSPKEDYPIEIQLSAGCEMYPGNASESFLHVAFQGKYVVRFWGTSWQTVPGAPSWLDLPIKVLNADQGTSATV QMLLNDTCPLFVRGLLEAGKSDLEKQEKPVAWLSSVPSSADGHRQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPN ADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWHHHHHH ; ;SEAQQKNYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRD IQELVKMMSPKEDYPIEIQLSAGCEMYPGNASESFLHVAFQGKYVVRFWGTSWQTVPGAPSWLDLPIKVLNADQGTSATV QMLLNDTCPLFVRGLLEAGKSDLEKQEKPVAWLSSVPSSADGHRQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPN ADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWHHHHHH ; A ? 2 'polypeptide(L)' no no ;IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYAC RVKHASMAEPKTVYWDRDM ; ;IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYAC RVKHASMAEPKTVYWDRDM ; B ? 3 'polypeptide(L)' no no YEHDFHHIREKGNHWKNFLAVM YEHDFHHIREKGNHWKNFLAVM C ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 SER n 1 2 GLU n 1 3 ALA n 1 4 GLN n 1 5 GLN n 1 6 LYS n 1 7 ASN n 1 8 TYR n 1 9 THR n 1 10 PHE n 1 11 ARG n 1 12 CYS n 1 13 LEU n 1 14 GLN n 1 15 MET n 1 16 SER n 1 17 SER n 1 18 PHE n 1 19 ALA n 1 20 ASN n 1 21 ARG n 1 22 SER n 1 23 TRP n 1 24 SER n 1 25 ARG n 1 26 THR n 1 27 ASP n 1 28 SER n 1 29 VAL n 1 30 VAL n 1 31 TRP n 1 32 LEU n 1 33 GLY n 1 34 ASP n 1 35 LEU n 1 36 GLN n 1 37 THR n 1 38 HIS n 1 39 ARG n 1 40 TRP n 1 41 SER n 1 42 ASN n 1 43 ASP n 1 44 SER n 1 45 ALA n 1 46 THR n 1 47 ILE n 1 48 SER n 1 49 PHE n 1 50 THR n 1 51 LYS n 1 52 PRO n 1 53 TRP n 1 54 SER n 1 55 GLN n 1 56 GLY n 1 57 LYS n 1 58 LEU n 1 59 SER n 1 60 ASN n 1 61 GLN n 1 62 GLN n 1 63 TRP n 1 64 GLU n 1 65 LYS n 1 66 LEU n 1 67 GLN n 1 68 HIS n 1 69 MET n 1 70 PHE n 1 71 GLN n 1 72 VAL n 1 73 TYR n 1 74 ARG n 1 75 VAL n 1 76 SER n 1 77 PHE n 1 78 THR n 1 79 ARG n 1 80 ASP n 1 81 ILE n 1 82 GLN n 1 83 GLU n 1 84 LEU n 1 85 VAL n 1 86 LYS n 1 87 MET n 1 88 MET n 1 89 SER n 1 90 PRO n 1 91 LYS n 1 92 GLU n 1 93 ASP n 1 94 TYR n 1 95 PRO n 1 96 ILE n 1 97 GLU n 1 98 ILE n 1 99 GLN n 1 100 LEU n 1 101 SER n 1 102 ALA n 1 103 GLY n 1 104 CYS n 1 105 GLU n 1 106 MET n 1 107 TYR n 1 108 PRO n 1 109 GLY n 1 110 ASN n 1 111 ALA n 1 112 SER n 1 113 GLU n 1 114 SER n 1 115 PHE n 1 116 LEU n 1 117 HIS n 1 118 VAL n 1 119 ALA n 1 120 PHE n 1 121 GLN n 1 122 GLY n 1 123 LYS n 1 124 TYR n 1 125 VAL n 1 126 VAL n 1 127 ARG n 1 128 PHE n 1 129 TRP n 1 130 GLY n 1 131 THR n 1 132 SER n 1 133 TRP n 1 134 GLN n 1 135 THR n 1 136 VAL n 1 137 PRO n 1 138 GLY n 1 139 ALA n 1 140 PRO n 1 141 SER n 1 142 TRP n 1 143 LEU n 1 144 ASP n 1 145 LEU n 1 146 PRO n 1 147 ILE n 1 148 LYS n 1 149 VAL n 1 150 LEU n 1 151 ASN n 1 152 ALA n 1 153 ASP n 1 154 GLN n 1 155 GLY n 1 156 THR n 1 157 SER n 1 158 ALA n 1 159 THR n 1 160 VAL n 1 161 GLN n 1 162 MET n 1 163 LEU n 1 164 LEU n 1 165 ASN n 1 166 ASP n 1 167 THR n 1 168 CYS n 1 169 PRO n 1 170 LEU n 1 171 PHE n 1 172 VAL n 1 173 ARG n 1 174 GLY n 1 175 LEU n 1 176 LEU n 1 177 GLU n 1 178 ALA n 1 179 GLY n 1 180 LYS n 1 181 SER n 1 182 ASP n 1 183 LEU n 1 184 GLU n 1 185 LYS n 1 186 GLN n 1 187 GLU n 1 188 LYS n 1 189 PRO n 1 190 VAL n 1 191 ALA n 1 192 TRP n 1 193 LEU n 1 194 SER n 1 195 SER n 1 196 VAL n 1 197 PRO n 1 198 SER n 1 199 SER n 1 200 ALA n 1 201 ASP n 1 202 GLY n 1 203 HIS n 1 204 ARG n 1 205 GLN n 1 206 LEU n 1 207 VAL n 1 208 CYS n 1 209 HIS n 1 210 VAL n 1 211 SER n 1 212 GLY n 1 213 PHE n 1 214 TYR n 1 215 PRO n 1 216 LYS n 1 217 PRO n 1 218 VAL n 1 219 TRP n 1 220 VAL n 1 221 MET n 1 222 TRP n 1 223 MET n 1 224 ARG n 1 225 GLY n 1 226 ASP n 1 227 GLN n 1 228 GLU n 1 229 GLN n 1 230 GLN n 1 231 GLY n 1 232 THR n 1 233 HIS n 1 234 ARG n 1 235 GLY n 1 236 ASP n 1 237 PHE n 1 238 LEU n 1 239 PRO n 1 240 ASN n 1 241 ALA n 1 242 ASP n 1 243 GLU n 1 244 THR n 1 245 TRP n 1 246 TYR n 1 247 LEU n 1 248 GLN n 1 249 ALA n 1 250 THR n 1 251 LEU n 1 252 ASP n 1 253 VAL n 1 254 GLU n 1 255 ALA n 1 256 GLY n 1 257 GLU n 1 258 GLU n 1 259 ALA n 1 260 GLY n 1 261 LEU n 1 262 ALA n 1 263 CYS n 1 264 ARG n 1 265 VAL n 1 266 LYS n 1 267 HIS n 1 268 SER n 1 269 SER n 1 270 LEU n 1 271 GLY n 1 272 GLY n 1 273 GLN n 1 274 ASP n 1 275 ILE n 1 276 ILE n 1 277 LEU n 1 278 TYR n 1 279 TRP n 1 280 HIS n 1 281 HIS n 1 282 HIS n 1 283 HIS n 1 284 HIS n 1 285 HIS n 2 1 ILE n 2 2 GLN n 2 3 LYS n 2 4 THR n 2 5 PRO n 2 6 GLN n 2 7 ILE n 2 8 GLN n 2 9 VAL n 2 10 TYR n 2 11 SER n 2 12 ARG n 2 13 HIS n 2 14 PRO n 2 15 PRO n 2 16 GLU n 2 17 ASN n 2 18 GLY n 2 19 LYS n 2 20 PRO n 2 21 ASN n 2 22 ILE n 2 23 LEU n 2 24 ASN n 2 25 CYS n 2 26 TYR n 2 27 VAL n 2 28 THR n 2 29 GLN n 2 30 PHE n 2 31 HIS n 2 32 PRO n 2 33 PRO n 2 34 HIS n 2 35 ILE n 2 36 GLU n 2 37 ILE n 2 38 GLN n 2 39 MET n 2 40 LEU n 2 41 LYS n 2 42 ASN n 2 43 GLY n 2 44 LYS n 2 45 LYS n 2 46 ILE n 2 47 PRO n 2 48 LYS n 2 49 VAL n 2 50 GLU n 2 51 MET n 2 52 SER n 2 53 ASP n 2 54 MET n 2 55 SER n 2 56 PHE n 2 57 SER n 2 58 LYS n 2 59 ASP n 2 60 TRP n 2 61 SER n 2 62 PHE n 2 63 TYR n 2 64 ILE n 2 65 LEU n 2 66 ALA n 2 67 HIS n 2 68 THR n 2 69 GLU n 2 70 PHE n 2 71 THR n 2 72 PRO n 2 73 THR n 2 74 GLU n 2 75 THR n 2 76 ASP n 2 77 THR n 2 78 TYR n 2 79 ALA n 2 80 CYS n 2 81 ARG n 2 82 VAL n 2 83 LYS n 2 84 HIS n 2 85 ALA n 2 86 SER n 2 87 MET n 2 88 ALA n 2 89 GLU n 2 90 PRO n 2 91 LYS n 2 92 THR n 2 93 VAL n 2 94 TYR n 2 95 TRP n 2 96 ASP n 2 97 ARG n 2 98 ASP n 2 99 MET n 3 1 TYR n 3 2 GLU n 3 3 HIS n 3 4 ASP n 3 5 PHE n 3 6 HIS n 3 7 HIS n 3 8 ILE n 3 9 ARG n 3 10 GLU n 3 11 LYS n 3 12 GLY n 3 13 ASN n 3 14 HIS n 3 15 TRP n 3 16 LYS n 3 17 ASN n 3 18 PHE n 3 19 LEU n 3 20 ALA n 3 21 VAL n 3 22 MET 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' 1 285 Mouse ? 'Cd1d1, Cd1.1' ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Sf9 ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample 'Biological sequence' 1 99 Mouse ? B2m ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? Sf9 ? ? ? ? ? ? ? ? ? ? ? ? ? ? # _pdbx_entity_src_syn.entity_id 3 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num 1 _pdbx_entity_src_syn.pdbx_end_seq_num 22 _pdbx_entity_src_syn.organism_scientific Mus _pdbx_entity_src_syn.organism_common_name ? _pdbx_entity_src_syn.ncbi_taxonomy_id 10088 _pdbx_entity_src_syn.details ? # 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 UNP CD1D1_MOUSE P11609 ? 1 ;SEAQQKNYTFRCLQMSSFANRSWSRTDSVVWLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRD IQELVKMMSPKEDYPIEIQLSAGCEMYPGNASESFLHVAFQGKYVVRFWGTSWQTVPGAPSWLDLPIKVLNADQGTSATV QMLLNDTCPLFVRGLLEAGKSDLEKQEKPVAWLSSVPSSADGHRQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPN ADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYW ; 19 2 UNP B2MG_MOUSE P01887 ? 2 ;IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYAC RVKHASMAEPKTVYWDRDM ; 21 3 PDB 5EFI 5EFI ? 3 ? 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 5EFI A 1 ? 279 ? P11609 19 ? 297 ? 1 279 2 2 5EFI B 1 ? 99 ? P01887 21 ? 119 ? 1 99 3 3 5EFI C 1 ? 22 ? 5EFI -3 ? 18 ? -3 18 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 5EFI HIS A 280 ? UNP P11609 ? ? 'expression tag' 280 1 1 5EFI HIS A 281 ? UNP P11609 ? ? 'expression tag' 281 2 1 5EFI HIS A 282 ? UNP P11609 ? ? 'expression tag' 282 3 1 5EFI HIS A 283 ? UNP P11609 ? ? 'expression tag' 283 4 1 5EFI HIS A 284 ? UNP P11609 ? ? 'expression tag' 284 5 1 5EFI HIS A 285 ? UNP P11609 ? ? 'expression tag' 285 6 # 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 CIT non-polymer . 'CITRIC ACID' ? 'C6 H8 O7' 192.124 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 OCA non-polymer . 'OCTANOIC ACID (CAPRYLIC ACID)' ? 'C8 H16 O2' 144.211 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PLM non-polymer . 'PALMITIC ACID' ? 'C16 H32 O2' 256.424 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.absorpt_coefficient_mu ? _exptl.absorpt_correction_T_max ? _exptl.absorpt_correction_T_min ? _exptl.absorpt_correction_type ? _exptl.absorpt_process_details ? _exptl.entry_id 5EFI _exptl.crystals_number ? _exptl.details ? _exptl.method 'X-RAY DIFFRACTION' _exptl.method_details ? # _exptl_crystal.colour ? _exptl_crystal.density_diffrn ? _exptl_crystal.density_Matthews 2.67 _exptl_crystal.density_method ? _exptl_crystal.density_percent_sol 53.86 _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 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.temp_esd ? _exptl_crystal_grow.time ? _exptl_crystal_grow.pdbx_details 'ammonium citrate, 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 PIXEL _diffrn_detector.diffrn_id 1 _diffrn_detector.type 'PSI PILATUS 6M' _diffrn_detector.area_resol_mean ? _diffrn_detector.dtime ? _diffrn_detector.pdbx_frames_total ? _diffrn_detector.pdbx_collection_time_total ? _diffrn_detector.pdbx_collection_date 2014-01-31 # _diffrn_radiation.collimation ? _diffrn_radiation.diffrn_id 1 _diffrn_radiation.filter_edge ? _diffrn_radiation.inhomogeneity ? _diffrn_radiation.monochromator ? _diffrn_radiation.polarisn_norm ? _diffrn_radiation.polarisn_ratio ? _diffrn_radiation.probe ? _diffrn_radiation.type ? _diffrn_radiation.xray_symbol ? _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_wavelength_list ? _diffrn_radiation.pdbx_wavelength ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_analyzer ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9794 _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 'SSRL BEAMLINE BL11-1' _diffrn_source.voltage ? _diffrn_source.take-off_angle ? _diffrn_source.pdbx_wavelength_list 0.9794 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_synchrotron_beamline BL11-1 _diffrn_source.pdbx_synchrotron_site SSRL # _reflns.B_iso_Wilson_estimate ? _reflns.entry_id 5EFI _reflns.data_reduction_details ? _reflns.data_reduction_method ? _reflns.d_resolution_high 1.8 _reflns.d_resolution_low 49.12 _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 46178 _reflns.observed_criterion ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.observed_criterion_I_max ? _reflns.observed_criterion_I_min ? _reflns.observed_criterion_sigma_F ? _reflns.observed_criterion_sigma_I ? _reflns.percent_possible_obs 97.4 _reflns.R_free_details ? _reflns.Rmerge_F_all ? _reflns.Rmerge_F_obs ? _reflns.Friedel_coverage ? _reflns.number_gt ? _reflns.threshold_expression ? _reflns.pdbx_redundancy 3.5 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rmerge_I_all ? _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_av_sigmaI ? _reflns.pdbx_netI_over_sigmaI 10.9 _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 ? # _refine.aniso_B[1][1] -1.61 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][2] 0.20 _refine.aniso_B[2][3] 0.00 _refine.aniso_B[3][3] 1.41 _refine.B_iso_max ? _refine.B_iso_mean 34.966 _refine.B_iso_min ? _refine.correlation_coeff_Fo_to_Fc 0.947 _refine.correlation_coeff_Fo_to_Fc_free 0.933 _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _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 5EFI _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.ls_abs_structure_details ? _refine.ls_abs_structure_Flack ? _refine.ls_abs_structure_Flack_esd ? _refine.ls_abs_structure_Rogers ? _refine.ls_abs_structure_Rogers_esd ? _refine.ls_d_res_high 1.80 _refine.ls_d_res_low 49.12 _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 43789 _refine.ls_number_reflns_R_free 2345 _refine.ls_number_reflns_R_work ? _refine.ls_number_restraints ? _refine.ls_percent_reflns_obs 96.89 _refine.ls_percent_reflns_R_free 5.1 _refine.ls_R_factor_all ? _refine.ls_R_factor_obs 0.21988 _refine.ls_R_factor_R_free 0.24387 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_R_factor_R_work 0.21857 _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 MASK _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 ? _refine.pdbx_ls_sigma_Fsqd ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_starting_model 3G08 _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_overall_ESU_R 0.135 _refine.pdbx_overall_ESU_R_Free 0.125 _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_real_space_R ? _refine.pdbx_density_correlation ? _refine.pdbx_pd_number_of_powder_patterns ? _refine.pdbx_pd_number_of_points ? _refine.pdbx_pd_meas_number_of_points ? _refine.pdbx_pd_proc_ls_prof_R_factor ? _refine.pdbx_pd_proc_ls_prof_wR_factor ? _refine.pdbx_pd_Marquardt_correlation_coeff ? _refine.pdbx_pd_Fsqrd_R_factor ? _refine.pdbx_pd_ls_matrix_band_width ? _refine.pdbx_overall_phase_error ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _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 7.029 _refine.overall_SU_ML 0.108 _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 2980 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 154 _refine_hist.number_atoms_solvent 204 _refine_hist.number_atoms_total 3338 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 49.12 # 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' ? 0.008 0.019 3264 ? r_bond_refined_d ? ? 'X-RAY DIFFRACTION' ? 0.002 0.020 2919 ? r_bond_other_d ? ? 'X-RAY DIFFRACTION' ? 1.334 1.966 4447 ? r_angle_refined_deg ? ? 'X-RAY DIFFRACTION' ? 0.847 3.000 6729 ? r_angle_other_deg ? ? 'X-RAY DIFFRACTION' ? 6.448 5.000 378 ? r_dihedral_angle_1_deg ? ? 'X-RAY DIFFRACTION' ? 34.069 23.759 141 ? r_dihedral_angle_2_deg ? ? 'X-RAY DIFFRACTION' ? 12.120 15.000 479 ? r_dihedral_angle_3_deg ? ? 'X-RAY DIFFRACTION' ? 16.734 15.000 14 ? r_dihedral_angle_4_deg ? ? 'X-RAY DIFFRACTION' ? 0.073 0.200 490 ? r_chiral_restr ? ? 'X-RAY DIFFRACTION' ? 0.004 0.021 3579 ? r_gen_planes_refined ? ? 'X-RAY DIFFRACTION' ? 0.001 0.020 774 ? r_gen_planes_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_nbtor_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_xyhbond_nbd_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_vdw_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_hbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_refined ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_symmetry_metal_ion_other ? ? 'X-RAY DIFFRACTION' ? 0.426 1.490 1521 ? r_mcbond_it ? ? 'X-RAY DIFFRACTION' ? 0.426 1.489 1520 ? r_mcbond_other ? ? 'X-RAY DIFFRACTION' ? 0.758 2.225 1896 ? r_mcangle_it ? ? 'X-RAY DIFFRACTION' ? 0.758 2.226 1897 ? r_mcangle_other ? ? 'X-RAY DIFFRACTION' ? 0.365 1.572 1743 ? r_scbond_it ? ? 'X-RAY DIFFRACTION' ? 0.364 1.569 1741 ? r_scbond_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_scangle_it ? ? 'X-RAY DIFFRACTION' ? 0.639 2.330 2551 ? r_scangle_other ? ? 'X-RAY DIFFRACTION' ? 5.149 13.007 3650 ? r_long_range_B_refined ? ? 'X-RAY DIFFRACTION' ? 5.149 13.014 3651 ? r_long_range_B_other ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_rigid_bond_restr ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_free ? ? 'X-RAY DIFFRACTION' ? ? ? ? ? r_sphericity_bonded ? ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.d_res_high 1.800 _refine_ls_shell.d_res_low 1.847 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.number_reflns_R_free 142 _refine_ls_shell.number_reflns_R_work 3235 _refine_ls_shell.percent_reflns_obs 96.73 _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 0.366 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.R_factor_R_work 0.316 _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 20 _refine_ls_shell.pdbx_phase_error ? _refine_ls_shell.pdbx_fsc_work ? _refine_ls_shell.pdbx_fsc_free ? # _struct.entry_id 5EFI _struct.title 'Crystal structure of mouse CD1d in complex with the p99p lipopeptide' _struct.pdbx_descriptor 'Antigen-presenting glycoprotein CD1d1, Beta-2-microglobulin, p99p' _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 5EFI _struct_keywords.text 'CD1d, lipopeptide, alpha-helical peptide, 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 4 ? E N N 4 ? F N N 4 ? G N N 4 ? H N N 5 ? I N N 6 ? J N N 7 ? K N N 6 ? L N N 4 ? M N N 8 ? N N N 9 ? O N N 10 ? P N N 11 ? Q N N 12 ? R N N 12 ? S N N 12 ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 AA1 SER A 59 ? MET A 88 ? SER A 59 MET A 88 1 ? 30 HELX_P HELX_P2 AA2 PRO A 140 ? TRP A 142 ? PRO A 140 TRP A 142 5 ? 3 HELX_P HELX_P3 AA3 LEU A 143 ? ALA A 152 ? LEU A 143 ALA A 152 1 ? 10 HELX_P HELX_P4 AA4 ASP A 153 ? ASP A 166 ? ASP A 153 ASP A 166 1 ? 14 HELX_P HELX_P5 AA5 ASP A 166 ? GLY A 179 ? ASP A 166 GLY A 179 1 ? 14 HELX_P HELX_P6 AA6 GLY A 179 ? GLU A 184 ? GLY A 179 GLU A 184 1 ? 6 HELX_P HELX_P7 AA7 HIS A 267 ? GLY A 271 ? HIS A 267 GLY A 271 5 ? 5 HELX_P HELX_P8 AA8 PHE C 5 ? TRP C 15 ? PHE C 1 TRP C 11 1 ? 11 # _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 104 SG ? ? ? 1_555 A CYS 168 SG ? ? A CYS 104 A CYS 168 1_555 ? ? ? ? ? ? ? 2.035 ? disulf2 disulf ? ? A CYS 208 SG ? ? ? 1_555 A CYS 263 SG ? ? A CYS 208 A CYS 263 1_555 ? ? ? ? ? ? ? 2.038 ? disulf3 disulf ? ? B CYS 25 SG ? ? ? 1_555 B CYS 80 SG ? ? B CYS 25 B CYS 80 1_555 ? ? ? ? ? ? ? 2.026 ? covale1 covale one ? A ASN 20 ND2 ? ? ? 1_555 L NAG . C1 ? ? A ASN 20 A NAG 309 1_555 ? ? ? ? ? ? ? 1.446 ? metalc1 metalc ? ? A THR 26 O ? ? ? 1_555 N NA . NA ? ? A THR 26 A NA 311 1_555 ? ? ? ? ? ? ? 2.862 ? metalc2 metalc ? ? A TRP 40 O ? ? ? 1_555 N NA . NA ? ? A TRP 40 A NA 311 1_555 ? ? ? ? ? ? ? 2.628 ? covale2 covale one ? A ASN 42 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 42 A NAG 301 1_555 ? ? ? ? ? ? ? 1.439 ? covale3 covale one ? A ASN 165 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 165 A NAG 303 1_555 ? ? ? ? ? ? ? 1.441 ? covale4 covale one ? C LYS 11 NZ ? ? ? 1_555 O PLM . C1 ? ? C LYS 7 C PLM 101 1_555 ? ? ? ? ? ? ? 1.351 ? covale5 covale both ? D NAG . O4 ? ? ? 1_555 E NAG . C1 ? ? A NAG 301 A NAG 302 1_555 ? ? ? ? ? ? ? 1.448 ? covale6 covale both ? F NAG . O4 ? ? ? 1_555 G NAG . C1 ? ? A NAG 303 A NAG 304 1_555 ? ? ? ? ? ? ? 1.447 ? covale7 covale one ? F NAG . O6 ? ? ? 1_555 J FUC . C1 ? ? A NAG 303 A FUC 307 1_555 ? ? ? ? ? ? ? 1.455 ? covale8 covale both ? G NAG . O4 ? ? ? 1_555 H BMA . C1 ? ? A NAG 304 A BMA 305 1_555 ? ? ? ? ? ? ? 1.444 ? covale9 covale one ? H BMA . O3 ? ? ? 1_555 K MAN . C1 ? ? A BMA 305 A MAN 308 1_555 ? ? ? ? ? ? ? 1.440 ? covale10 covale one ? H BMA . O6 ? ? ? 1_555 I MAN . C1 ? ? A BMA 305 A MAN 306 1_555 ? ? ? ? ? ? ? 1.442 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 TYR 94 A . ? TYR 94 A PRO 95 A ? PRO 95 A 1 1.01 2 TYR 214 A . ? TYR 214 A PRO 215 A ? PRO 215 A 1 0.21 3 HIS 31 B . ? HIS 31 B PRO 32 B ? PRO 32 B 1 3.28 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA1 ? 8 ? AA2 ? 4 ? AA3 ? 4 ? AA4 ? 4 ? AA5 ? 4 ? AA6 ? 4 ? AA7 ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA1 1 2 ? anti-parallel AA1 2 3 ? anti-parallel AA1 3 4 ? anti-parallel AA1 4 5 ? anti-parallel AA1 5 6 ? anti-parallel AA1 6 7 ? anti-parallel AA1 7 8 ? anti-parallel AA2 1 2 ? anti-parallel AA2 2 3 ? anti-parallel AA2 3 4 ? anti-parallel AA3 1 2 ? anti-parallel AA3 2 3 ? anti-parallel AA3 3 4 ? anti-parallel AA4 1 2 ? anti-parallel AA4 2 3 ? anti-parallel AA4 3 4 ? anti-parallel AA5 1 2 ? anti-parallel AA5 2 3 ? anti-parallel AA5 3 4 ? anti-parallel AA6 1 2 ? anti-parallel AA6 2 3 ? anti-parallel AA6 3 4 ? anti-parallel AA7 1 2 ? anti-parallel AA7 2 3 ? anti-parallel AA7 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA1 1 SER A 48 ? PHE A 49 ? SER A 48 PHE A 49 AA1 2 LEU A 35 ? TRP A 40 ? LEU A 35 TRP A 40 AA1 3 TRP A 23 ? LEU A 32 ? TRP A 23 LEU A 32 AA1 4 THR A 9 ? ASN A 20 ? THR A 9 ASN A 20 AA1 5 ILE A 96 ? GLU A 105 ? ILE A 96 GLU A 105 AA1 6 GLU A 113 ? PHE A 120 ? GLU A 113 PHE A 120 AA1 7 LYS A 123 ? TRP A 129 ? LYS A 123 TRP A 129 AA1 8 SER A 132 ? THR A 135 ? SER A 132 THR A 135 AA2 1 VAL A 190 ? VAL A 196 ? VAL A 190 VAL A 196 AA2 2 ARG A 204 ? PHE A 213 ? ARG A 204 PHE A 213 AA2 3 TRP A 245 ? VAL A 253 ? TRP A 245 VAL A 253 AA2 4 HIS A 233 ? ARG A 234 ? HIS A 233 ARG A 234 AA3 1 VAL A 190 ? VAL A 196 ? VAL A 190 VAL A 196 AA3 2 ARG A 204 ? PHE A 213 ? ARG A 204 PHE A 213 AA3 3 TRP A 245 ? VAL A 253 ? TRP A 245 VAL A 253 AA3 4 LEU A 238 ? PRO A 239 ? LEU A 238 PRO A 239 AA4 1 GLN A 227 ? GLU A 228 ? GLN A 227 GLU A 228 AA4 2 TRP A 219 ? ARG A 224 ? TRP A 219 ARG A 224 AA4 3 LEU A 261 ? LYS A 266 ? LEU A 261 LYS A 266 AA4 4 ILE A 275 ? TYR A 278 ? ILE A 275 TYR A 278 AA5 1 GLN B 6 ? SER B 11 ? GLN B 6 SER B 11 AA5 2 ASN B 21 ? PHE B 30 ? ASN B 21 PHE B 30 AA5 3 PHE B 62 ? PHE B 70 ? PHE B 62 PHE B 70 AA5 4 GLU B 50 ? MET B 51 ? GLU B 50 MET B 51 AA6 1 GLN B 6 ? SER B 11 ? GLN B 6 SER B 11 AA6 2 ASN B 21 ? PHE B 30 ? ASN B 21 PHE B 30 AA6 3 PHE B 62 ? PHE B 70 ? PHE B 62 PHE B 70 AA6 4 SER B 55 ? PHE B 56 ? SER B 55 PHE B 56 AA7 1 LYS B 44 ? LYS B 45 ? LYS B 44 LYS B 45 AA7 2 GLU B 36 ? LYS B 41 ? GLU B 36 LYS B 41 AA7 3 TYR B 78 ? LYS B 83 ? TYR B 78 LYS B 83 AA7 4 LYS B 91 ? TYR B 94 ? LYS B 91 TYR B 94 # 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 SER A 48 ? O SER A 48 N ARG A 39 ? N ARG A 39 AA1 2 3 O TRP A 40 ? O TRP A 40 N SER A 28 ? N SER A 28 AA1 3 4 O VAL A 29 ? O VAL A 29 N LEU A 13 ? N LEU A 13 AA1 4 5 N CYS A 12 ? N CYS A 12 O ALA A 102 ? O ALA A 102 AA1 5 6 N GLU A 105 ? N GLU A 105 O GLU A 113 ? O GLU A 113 AA1 6 7 N VAL A 118 ? N VAL A 118 O VAL A 126 ? O VAL A 126 AA1 7 8 N ARG A 127 ? N ARG A 127 O GLN A 134 ? O GLN A 134 AA2 1 2 N SER A 194 ? N SER A 194 O VAL A 207 ? O VAL A 207 AA2 2 3 N ARG A 204 ? N ARG A 204 O VAL A 253 ? O VAL A 253 AA2 3 4 O THR A 250 ? O THR A 250 N HIS A 233 ? N HIS A 233 AA3 1 2 N SER A 194 ? N SER A 194 O VAL A 207 ? O VAL A 207 AA3 2 3 N ARG A 204 ? N ARG A 204 O VAL A 253 ? O VAL A 253 AA3 3 4 O TYR A 246 ? O TYR A 246 N LEU A 238 ? N LEU A 238 AA4 1 2 O GLN A 227 ? O GLN A 227 N ARG A 224 ? N ARG A 224 AA4 2 3 N MET A 223 ? N MET A 223 O ALA A 262 ? O ALA A 262 AA4 3 4 N CYS A 263 ? N CYS A 263 O LEU A 277 ? O LEU A 277 AA5 1 2 N TYR B 10 ? N TYR B 10 O ASN B 24 ? O ASN B 24 AA5 2 3 N CYS B 25 ? N CYS B 25 O ALA B 66 ? O ALA B 66 AA5 3 4 O HIS B 67 ? O HIS B 67 N GLU B 50 ? N GLU B 50 AA6 1 2 N TYR B 10 ? N TYR B 10 O ASN B 24 ? O ASN B 24 AA6 2 3 N CYS B 25 ? N CYS B 25 O ALA B 66 ? O ALA B 66 AA6 3 4 O TYR B 63 ? O TYR B 63 N SER B 55 ? N SER B 55 AA7 1 2 O LYS B 44 ? O LYS B 44 N LYS B 41 ? N LYS B 41 AA7 2 3 N GLN B 38 ? N GLN B 38 O ARG B 81 ? O ARG B 81 AA7 3 4 N VAL B 82 ? N VAL B 82 O LYS B 91 ? O LYS B 91 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software A CIT 310 ? 8 'binding site for residue CIT A 310' AC2 Software A NA 311 ? 4 'binding site for residue NA A 311' AC3 Software C PLM 101 ? 4 'binding site for residue PLM C 101' AC4 Software C OCA 102 ? 2 'binding site for residue OCA C 102' AC5 Software A NAG 309 ? 3 'binding site for Mono-Saccharide NAG A 309 bound to ASN A 20' AC6 Software A ASN 42 ? 3 'binding site for Poly-Saccharide residues NAG A 301 through NAG A 302 bound to ASN A 42' AC7 Software A ASN 165 ? 15 'binding site for Poly-Saccharide residues NAG A 303 through MAN A 308 bound to ASN A 165' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 8 CYS A 12 ? CYS A 12 . ? 1_555 ? 2 AC1 8 GLN A 14 ? GLN A 14 . ? 1_555 ? 3 AC1 8 SER A 28 ? SER A 28 . ? 1_555 ? 4 AC1 8 TRP A 40 ? TRP A 40 . ? 1_555 ? 5 AC1 8 PHE A 70 ? PHE A 70 . ? 1_555 ? 6 AC1 8 TYR A 73 ? TYR A 73 . ? 1_555 ? 7 AC1 8 NA N . ? NA A 311 . ? 1_555 ? 8 AC1 8 PLM O . ? PLM C 101 . ? 1_555 ? 9 AC2 4 THR A 26 ? THR A 26 . ? 1_555 ? 10 AC2 4 TRP A 40 ? TRP A 40 . ? 1_555 ? 11 AC2 4 ARG A 74 ? ARG A 74 . ? 1_555 ? 12 AC2 4 CIT M . ? CIT A 310 . ? 1_555 ? 13 AC3 4 TYR A 73 ? TYR A 73 . ? 1_555 ? 14 AC3 4 THR A 159 ? THR A 159 . ? 1_555 ? 15 AC3 4 CIT M . ? CIT A 310 . ? 1_555 ? 16 AC3 4 LYS C 11 ? LYS C 7 . ? 1_555 ? 17 AC4 2 TRP A 133 ? TRP A 133 . ? 1_555 ? 18 AC4 2 ILE C 8 ? ILE C 4 . ? 1_555 ? 19 AC5 3 ALA A 19 ? ALA A 19 . ? 1_555 ? 20 AC5 3 ASN A 20 ? ASN A 20 . ? 1_555 ? 21 AC5 3 TRP A 23 ? TRP A 23 . ? 1_555 ? 22 AC6 3 TRP A 23 ? TRP A 23 . ? 1_555 ? 23 AC6 3 SER A 24 ? SER A 24 . ? 1_555 ? 24 AC6 3 ASN A 42 ? ASN A 42 . ? 1_555 ? 25 AC7 15 LYS A 57 ? LYS A 57 . ? 1_655 ? 26 AC7 15 SER A 114 ? SER A 114 . ? 1_555 ? 27 AC7 15 TRP A 129 ? TRP A 129 . ? 1_555 ? 28 AC7 15 GLY A 130 ? GLY A 130 . ? 1_555 ? 29 AC7 15 THR A 131 ? THR A 131 . ? 1_555 ? 30 AC7 15 GLN A 161 ? GLN A 161 . ? 1_555 ? 31 AC7 15 ASN A 165 ? ASN A 165 . ? 1_555 ? 32 AC7 15 GLU A 177 ? GLU A 177 . ? 1_655 ? 33 AC7 15 ALA A 178 ? ALA A 178 . ? 1_655 ? 34 AC7 15 LYS A 180 ? LYS A 180 . ? 1_655 ? 35 AC7 15 SER A 181 ? SER A 181 . ? 1_655 ? 36 AC7 15 HOH Q . ? HOH A 417 . ? 1_555 ? 37 AC7 15 ASN B 42 ? ASN B 42 . ? 3_645 ? 38 AC7 15 GLY B 43 ? GLY B 43 . ? 3_645 ? 39 AC7 15 THR B 77 ? THR B 77 . ? 3_645 ? # _atom_sites.entry_id 5EFI _atom_sites.fract_transf_matrix[1][1] 0.023702 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.009272 _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] 0.009063 _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 NA 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 . LYS A 1 6 ? 17.346 -0.583 9.492 1.00 61.86 ? 6 LYS A N 1 ATOM 2 C CA . LYS A 1 6 ? 18.111 0.530 10.144 1.00 59.34 ? 6 LYS A CA 1 ATOM 3 C C . LYS A 1 6 ? 19.025 0.017 11.252 1.00 57.57 ? 6 LYS A C 1 ATOM 4 O O . LYS A 1 6 ? 18.762 -1.034 11.845 1.00 57.97 ? 6 LYS A O 1 ATOM 5 C CB . LYS A 1 6 ? 17.158 1.589 10.715 1.00 57.88 ? 6 LYS A CB 1 ATOM 6 N N . ASN A 1 7 ? 20.085 0.779 11.524 1.00 55.82 ? 7 ASN A N 1 ATOM 7 C CA . ASN A 1 7 ? 21.094 0.428 12.522 1.00 54.03 ? 7 ASN A CA 1 ATOM 8 C C . ASN A 1 7 ? 20.939 1.262 13.793 1.00 51.14 ? 7 ASN A C 1 ATOM 9 O O . ASN A 1 7 ? 21.353 2.425 13.825 1.00 51.10 ? 7 ASN A O 1 ATOM 10 C CB . ASN A 1 7 ? 22.495 0.636 11.933 1.00 54.60 ? 7 ASN A CB 1 ATOM 11 N N . TYR A 1 8 ? 20.364 0.669 14.842 1.00 49.28 ? 8 TYR A N 1 ATOM 12 C CA . TYR A 1 8 ? 20.107 1.393 16.098 1.00 46.27 ? 8 TYR A CA 1 ATOM 13 C C . TYR A 1 8 ? 21.354 1.486 16.962 1.00 44.14 ? 8 TYR A C 1 ATOM 14 O O . TYR A 1 8 ? 22.163 0.546 17.007 1.00 44.90 ? 8 TYR A O 1 ATOM 15 C CB . TYR A 1 8 ? 19.000 0.720 16.917 1.00 46.41 ? 8 TYR A CB 1 ATOM 16 C CG . TYR A 1 8 ? 17.630 0.751 16.278 1.00 47.50 ? 8 TYR A CG 1 ATOM 17 C CD1 . TYR A 1 8 ? 17.242 -0.237 15.375 1.00 49.71 ? 8 TYR A CD1 1 ATOM 18 C CD2 . TYR A 1 8 ? 16.716 1.760 16.582 1.00 46.83 ? 8 TYR A CD2 1 ATOM 19 C CE1 . TYR A 1 8 ? 15.985 -0.222 14.785 1.00 51.03 ? 8 TYR A CE1 1 ATOM 20 C CE2 . TYR A 1 8 ? 15.455 1.782 16.000 1.00 48.01 ? 8 TYR A CE2 1 ATOM 21 C CZ . TYR A 1 8 ? 15.097 0.791 15.100 1.00 50.00 ? 8 TYR A CZ 1 ATOM 22 O OH . TYR A 1 8 ? 13.852 0.794 14.516 1.00 51.47 ? 8 TYR A OH 1 ATOM 23 N N . THR A 1 9 ? 21.487 2.620 17.651 1.00 41.25 ? 9 THR A N 1 ATOM 24 C CA . THR A 1 9 ? 22.503 2.814 18.679 1.00 39.07 ? 9 THR A CA 1 ATOM 25 C C . THR A 1 9 ? 21.828 2.773 20.042 1.00 36.49 ? 9 THR A C 1 ATOM 26 O O . THR A 1 9 ? 20.963 3.602 20.335 1.00 35.71 ? 9 THR A O 1 ATOM 27 C CB . THR A 1 9 ? 23.219 4.169 18.514 1.00 38.79 ? 9 THR A CB 1 ATOM 28 O OG1 . THR A 1 9 ? 23.889 4.194 17.252 1.00 40.82 ? 9 THR A OG1 1 ATOM 29 C CG2 . THR A 1 9 ? 24.251 4.395 19.632 1.00 38.04 ? 9 THR A CG2 1 ATOM 30 N N . PHE A 1 10 ? 22.231 1.816 20.876 1.00 34.80 ? 10 PHE A N 1 ATOM 31 C CA . PHE A 1 10 ? 21.747 1.729 22.244 1.00 33.19 ? 10 PHE A CA 1 ATOM 32 C C . PHE A 1 10 ? 22.772 2.411 23.157 1.00 31.76 ? 10 PHE A C 1 ATOM 33 O O . PHE A 1 10 ? 23.947 2.063 23.124 1.00 31.34 ? 10 PHE A O 1 ATOM 34 C CB . PHE A 1 10 ? 21.551 0.259 22.615 1.00 33.95 ? 10 PHE A CB 1 ATOM 35 C CG . PHE A 1 10 ? 21.113 0.037 24.027 1.00 33.37 ? 10 PHE A CG 1 ATOM 36 C CD1 . PHE A 1 10 ? 19.807 0.304 24.409 1.00 33.39 ? 10 PHE A CD1 1 ATOM 37 C CD2 . PHE A 1 10 ? 21.999 -0.463 24.976 1.00 33.27 ? 10 PHE A CD2 1 ATOM 38 C CE1 . PHE A 1 10 ? 19.390 0.089 25.713 1.00 33.52 ? 10 PHE A CE1 1 ATOM 39 C CE2 . PHE A 1 10 ? 21.590 -0.679 26.284 1.00 33.31 ? 10 PHE A CE2 1 ATOM 40 C CZ . PHE A 1 10 ? 20.279 -0.406 26.651 1.00 33.54 ? 10 PHE A CZ 1 ATOM 41 N N . ARG A 1 11 ? 22.347 3.398 23.944 1.00 30.74 ? 11 ARG A N 1 ATOM 42 C CA . ARG A 1 11 ? 23.271 4.056 24.866 1.00 29.90 ? 11 ARG A CA 1 ATOM 43 C C . ARG A 1 11 ? 22.695 4.273 26.261 1.00 29.20 ? 11 ARG A C 1 ATOM 44 O O . ARG A 1 11 ? 21.580 4.773 26.424 1.00 28.99 ? 11 ARG A O 1 ATOM 45 C CB . ARG A 1 11 ? 23.866 5.360 24.290 1.00 29.75 ? 11 ARG A CB 1 ATOM 46 C CG . ARG A 1 11 ? 22.978 6.203 23.418 1.00 30.42 ? 11 ARG A CG 1 ATOM 47 C CD . ARG A 1 11 ? 23.664 7.511 22.982 1.00 30.52 ? 11 ARG A CD 1 ATOM 48 N NE . ARG A 1 11 ? 22.715 8.628 22.936 1.00 30.91 ? 11 ARG A NE 1 ATOM 49 C CZ . ARG A 1 11 ? 22.965 9.901 23.288 1.00 30.92 ? 11 ARG A CZ 1 ATOM 50 N NH1 . ARG A 1 11 ? 24.173 10.313 23.752 1.00 30.29 ? 11 ARG A NH1 1 ATOM 51 N NH2 . ARG A 1 11 ? 21.974 10.789 23.190 1.00 31.24 ? 11 ARG A NH2 1 ATOM 52 N N . CYS A 1 12 ? 23.487 3.857 27.245 1.00 28.59 ? 12 CYS A N 1 ATOM 53 C CA . CYS A 1 12 ? 23.251 4.111 28.655 1.00 28.48 ? 12 CYS A CA 1 ATOM 54 C C . CYS A 1 12 ? 24.166 5.265 29.036 1.00 27.28 ? 12 CYS A C 1 ATOM 55 O O . CYS A 1 12 ? 25.391 5.154 28.897 1.00 26.80 ? 12 CYS A O 1 ATOM 56 C CB . CYS A 1 12 ? 23.590 2.872 29.487 1.00 29.61 ? 12 CYS A CB 1 ATOM 57 S SG . CYS A 1 12 ? 22.799 1.349 28.895 1.00 31.33 ? 12 CYS A SG 1 ATOM 58 N N . LEU A 1 13 ? 23.562 6.356 29.505 1.00 26.65 ? 13 LEU A N 1 ATOM 59 C CA . LEU A 1 13 ? 24.264 7.598 29.793 1.00 25.93 ? 13 LEU A CA 1 ATOM 60 C C . LEU A 1 13 ? 24.161 7.876 31.277 1.00 26.30 ? 13 LEU A C 1 ATOM 61 O O . LEU A 1 13 ? 23.060 8.087 31.790 1.00 26.66 ? 13 LEU A O 1 ATOM 62 C CB . LEU A 1 13 ? 23.638 8.751 28.994 1.00 25.67 ? 13 LEU A CB 1 ATOM 63 C CG . LEU A 1 13 ? 23.476 8.544 27.487 1.00 25.31 ? 13 LEU A CG 1 ATOM 64 C CD1 . LEU A 1 13 ? 22.916 9.803 26.827 1.00 25.40 ? 13 LEU A CD1 1 ATOM 65 C CD2 . LEU A 1 13 ? 24.801 8.160 26.851 1.00 25.09 ? 13 LEU A CD2 1 ATOM 66 N N . GLN A 1 14 ? 25.307 7.874 31.961 1.00 26.06 ? 14 GLN A N 1 ATOM 67 C CA . GLN A 1 14 ? 25.383 8.197 33.373 1.00 26.90 ? 14 GLN A CA 1 ATOM 68 C C . GLN A 1 14 ? 25.992 9.578 33.546 1.00 26.77 ? 14 GLN A C 1 ATOM 69 O O . GLN A 1 14 ? 26.990 9.906 32.900 1.00 26.09 ? 14 GLN A O 1 ATOM 70 C CB . GLN A 1 14 ? 26.246 7.160 34.092 1.00 27.49 ? 14 GLN A CB 1 ATOM 71 C CG . GLN A 1 14 ? 26.530 7.426 35.564 1.00 28.81 ? 14 GLN A CG 1 ATOM 72 C CD . GLN A 1 14 ? 27.648 6.540 36.084 1.00 29.38 ? 14 GLN A CD 1 ATOM 73 O OE1 . GLN A 1 14 ? 27.870 5.452 35.559 1.00 29.41 ? 14 GLN A OE1 1 ATOM 74 N NE2 . GLN A 1 14 ? 28.370 7.005 37.084 1.00 30.16 ? 14 GLN A NE2 1 ATOM 75 N N . MET A 1 15 ? 25.404 10.357 34.443 1.00 27.56 ? 15 MET A N 1 ATOM 76 C CA . MET A 1 15 ? 25.830 11.724 34.714 1.00 27.89 ? 15 MET A CA 1 ATOM 77 C C . MET A 1 15 ? 26.014 11.852 36.211 1.00 29.23 ? 15 MET A C 1 ATOM 78 O O . MET A 1 15 ? 25.026 11.839 36.951 1.00 30.06 ? 15 MET A O 1 ATOM 79 C CB . MET A 1 15 ? 24.764 12.714 34.233 1.00 28.09 ? 15 MET A CB 1 ATOM 80 C CG . MET A 1 15 ? 24.453 12.601 32.755 1.00 27.10 ? 15 MET A CG 1 ATOM 81 S SD . MET A 1 15 ? 22.800 13.218 32.336 1.00 27.50 ? 15 MET A SD 1 ATOM 82 C CE . MET A 1 15 ? 21.891 11.682 32.448 1.00 27.53 ? 15 MET A CE 1 ATOM 83 N N . SER A 1 16 ? 27.276 11.960 36.645 1.00 29.35 ? 16 SER A N 1 ATOM 84 C CA . SER A 1 16 ? 27.635 12.075 38.048 1.00 31.08 ? 16 SER A CA 1 ATOM 85 C C . SER A 1 16 ? 28.275 13.437 38.347 1.00 31.98 ? 16 SER A C 1 ATOM 86 O O . SER A 1 16 ? 29.264 13.811 37.718 1.00 31.08 ? 16 SER A O 1 ATOM 87 C CB . SER A 1 16 ? 28.593 10.947 38.440 1.00 31.11 ? 16 SER A CB 1 ATOM 88 O OG . SER A 1 16 ? 27.970 9.691 38.239 1.00 30.73 ? 16 SER A OG 1 ATOM 89 N N . SER A 1 17 ? 27.696 14.160 39.302 1.00 33.90 ? 17 SER A N 1 ATOM 90 C CA . SER A 1 17 ? 28.200 15.451 39.756 1.00 35.38 ? 17 SER A CA 1 ATOM 91 C C . SER A 1 17 ? 28.634 15.310 41.193 1.00 37.86 ? 17 SER A C 1 ATOM 92 O O . SER A 1 17 ? 27.870 14.805 42.005 1.00 39.24 ? 17 SER A O 1 ATOM 93 C CB . SER A 1 17 ? 27.095 16.499 39.690 1.00 36.03 ? 17 SER A CB 1 ATOM 94 O OG . SER A 1 17 ? 26.620 16.645 38.372 1.00 34.14 ? 17 SER A OG 1 ATOM 95 N N . PHE A 1 18 ? 29.847 15.758 41.507 1.00 38.89 ? 18 PHE A N 1 ATOM 96 C CA . PHE A 1 18 ? 30.342 15.790 42.884 1.00 41.63 ? 18 PHE A CA 1 ATOM 97 C C . PHE A 1 18 ? 30.663 17.238 43.219 1.00 43.56 ? 18 PHE A C 1 ATOM 98 O O . PHE A 1 18 ? 31.535 17.832 42.599 1.00 42.79 ? 18 PHE A O 1 ATOM 99 C CB . PHE A 1 18 ? 31.587 14.918 43.041 1.00 41.30 ? 18 PHE A CB 1 ATOM 100 C CG . PHE A 1 18 ? 31.395 13.491 42.595 1.00 39.83 ? 18 PHE A CG 1 ATOM 101 C CD1 . PHE A 1 18 ? 31.414 13.160 41.249 1.00 37.44 ? 18 PHE A CD1 1 ATOM 102 C CD2 . PHE A 1 18 ? 31.214 12.470 43.531 1.00 41.19 ? 18 PHE A CD2 1 ATOM 103 C CE1 . PHE A 1 18 ? 31.234 11.841 40.833 1.00 36.42 ? 18 PHE A CE1 1 ATOM 104 C CE2 . PHE A 1 18 ? 31.045 11.153 43.129 1.00 40.09 ? 18 PHE A CE2 1 ATOM 105 C CZ . PHE A 1 18 ? 31.056 10.834 41.780 1.00 37.77 ? 18 PHE A CZ 1 ATOM 106 N N . ALA A 1 19 ? 29.945 17.799 44.186 1.00 46.42 ? 19 ALA A N 1 ATOM 107 C CA . ALA A 1 19 ? 30.100 19.207 44.563 1.00 48.76 ? 19 ALA A CA 1 ATOM 108 C C . ALA A 1 19 ? 31.146 19.371 45.657 1.00 51.49 ? 19 ALA A C 1 ATOM 109 O O . ALA A 1 19 ? 31.889 20.349 45.677 1.00 52.44 ? 19 ALA A O 1 ATOM 110 C CB . ALA A 1 19 ? 28.769 19.778 45.021 1.00 50.47 ? 19 ALA A CB 1 ATOM 111 N N . ASN A 1 20 ? 31.159 18.423 46.586 1.00 53.29 ? 20 ASN A N 1 ATOM 112 C CA . ASN A 1 20 ? 32.120 18.382 47.680 1.00 56.07 ? 20 ASN A CA 1 ATOM 113 C C . ASN A 1 20 ? 32.115 16.964 48.266 1.00 56.46 ? 20 ASN A C 1 ATOM 114 O O . ASN A 1 20 ? 31.502 16.061 47.681 1.00 54.72 ? 20 ASN A O 1 ATOM 115 C CB . ASN A 1 20 ? 31.785 19.461 48.736 1.00 59.94 ? 20 ASN A CB 1 ATOM 116 C CG . ASN A 1 20 ? 30.295 19.536 49.060 1.00 61.46 ? 20 ASN A CG 1 ATOM 117 O OD1 . ASN A 1 20 ? 29.654 18.513 49.294 1.00 61.48 ? 20 ASN A OD1 1 ATOM 118 N ND2 . ASN A 1 20 ? 29.740 20.753 49.075 1.00 63.23 ? 20 ASN A ND2 1 ATOM 119 N N . ARG A 1 21 ? 32.817 16.756 49.377 1.00 58.91 ? 21 ARG A N 1 ATOM 120 C CA . ARG A 1 21 ? 32.591 15.577 50.214 1.00 60.27 ? 21 ARG A CA 1 ATOM 121 C C . ARG A 1 21 ? 31.164 15.684 50.764 1.00 62.00 ? 21 ARG A C 1 ATOM 122 O O . ARG A 1 21 ? 30.735 16.764 51.168 1.00 64.13 ? 21 ARG A O 1 ATOM 123 C CB . ARG A 1 21 ? 33.617 15.514 51.353 1.00 63.04 ? 21 ARG A CB 1 ATOM 124 N N . SER A 1 22 ? 30.421 14.581 50.746 1.00 61.38 ? 22 SER A N 1 ATOM 125 C CA . SER A 1 22 ? 29.024 14.561 51.213 1.00 62.89 ? 22 SER A CA 1 ATOM 126 C C . SER A 1 22 ? 28.019 15.399 50.384 1.00 61.27 ? 22 SER A C 1 ATOM 127 O O . SER A 1 22 ? 27.007 15.854 50.922 1.00 63.37 ? 22 SER A O 1 ATOM 128 C CB . SER A 1 22 ? 28.946 14.959 52.693 1.00 67.39 ? 22 SER A CB 1 ATOM 129 N N . TRP A 1 23 ? 28.303 15.616 49.100 1.00 57.67 ? 23 TRP A N 1 ATOM 130 C CA . TRP A 1 23 ? 27.261 15.968 48.117 1.00 55.66 ? 23 TRP A CA 1 ATOM 131 C C . TRP A 1 23 ? 27.671 15.440 46.760 1.00 51.91 ? 23 TRP A C 1 ATOM 132 O O . TRP A 1 23 ? 28.670 15.882 46.184 1.00 50.54 ? 23 TRP A O 1 ATOM 133 C CB . TRP A 1 23 ? 26.992 17.478 48.008 1.00 56.47 ? 23 TRP A CB 1 ATOM 134 C CG . TRP A 1 23 ? 25.677 17.841 47.268 1.00 55.41 ? 23 TRP A CG 1 ATOM 135 C CD1 . TRP A 1 23 ? 24.493 18.210 47.852 1.00 57.57 ? 23 TRP A CD1 1 ATOM 136 C CD2 . TRP A 1 23 ? 25.434 17.868 45.839 1.00 52.23 ? 23 TRP A CD2 1 ATOM 137 N NE1 . TRP A 1 23 ? 23.542 18.465 46.891 1.00 55.79 ? 23 TRP A NE1 1 ATOM 138 C CE2 . TRP A 1 23 ? 24.089 18.266 45.652 1.00 52.60 ? 23 TRP A CE2 1 ATOM 139 C CE3 . TRP A 1 23 ? 26.220 17.603 44.705 1.00 49.28 ? 23 TRP A CE3 1 ATOM 140 C CZ2 . TRP A 1 23 ? 23.513 18.398 44.379 1.00 50.14 ? 23 TRP A CZ2 1 ATOM 141 C CZ3 . TRP A 1 23 ? 25.649 17.736 43.442 1.00 47.00 ? 23 TRP A CZ3 1 ATOM 142 C CH2 . TRP A 1 23 ? 24.305 18.131 43.292 1.00 47.48 ? 23 TRP A CH2 1 ATOM 143 N N . SER A 1 24 ? 26.911 14.467 46.275 1.00 50.40 ? 24 SER A N 1 ATOM 144 C CA . SER A 1 24 ? 26.962 14.069 44.891 1.00 47.15 ? 24 SER A CA 1 ATOM 145 C C . SER A 1 24 ? 25.616 13.480 44.507 1.00 46.38 ? 24 SER A C 1 ATOM 146 O O . SER A 1 24 ? 24.847 13.056 45.375 1.00 48.16 ? 24 SER A O 1 ATOM 147 C CB . SER A 1 24 ? 28.087 13.055 44.646 1.00 46.03 ? 24 SER A CB 1 ATOM 148 O OG . SER A 1 24 ? 27.765 11.774 45.159 1.00 46.96 ? 24 SER A OG 1 ATOM 149 N N . ARG A 1 25 ? 25.333 13.497 43.209 1.00 43.74 ? 25 ARG A N 1 ATOM 150 C CA . ARG A 1 25 ? 24.227 12.738 42.644 1.00 42.72 ? 25 ARG A CA 1 ATOM 151 C C . ARG A 1 25 ? 24.652 12.110 41.330 1.00 39.67 ? 25 ARG A C 1 ATOM 152 O O . ARG A 1 25 ? 25.520 12.635 40.624 1.00 38.17 ? 25 ARG A O 1 ATOM 153 C CB . ARG A 1 25 ? 22.978 13.604 42.442 1.00 43.42 ? 25 ARG A CB 1 ATOM 154 C CG . ARG A 1 25 ? 23.143 14.768 41.482 1.00 42.37 ? 25 ARG A CG 1 ATOM 155 C CD . ARG A 1 25 ? 21.926 15.678 41.503 1.00 43.65 ? 25 ARG A CD 1 ATOM 156 N NE . ARG A 1 25 ? 20.745 15.042 40.909 1.00 43.11 ? 25 ARG A NE 1 ATOM 157 C CZ . ARG A 1 25 ? 19.676 14.565 41.563 1.00 44.82 ? 25 ARG A CZ 1 ATOM 158 N NH1 . ARG A 1 25 ? 19.567 14.618 42.890 1.00 47.43 ? 25 ARG A NH1 1 ATOM 159 N NH2 . ARG A 1 25 ? 18.683 14.017 40.863 1.00 44.05 ? 25 ARG A NH2 1 ATOM 160 N N . THR A 1 26 ? 24.044 10.966 41.032 1.00 38.75 ? 26 THR A N 1 ATOM 161 C CA . THR A 1 26 ? 24.235 10.256 39.783 1.00 36.40 ? 26 THR A CA 1 ATOM 162 C C . THR A 1 26 ? 22.852 9.985 39.193 1.00 35.90 ? 26 THR A C 1 ATOM 163 O O . THR A 1 26 ? 22.009 9.352 39.844 1.00 37.14 ? 26 THR A O 1 ATOM 164 C CB . THR A 1 26 ? 24.987 8.939 40.018 1.00 36.43 ? 26 THR A CB 1 ATOM 165 O OG1 . THR A 1 26 ? 26.292 9.234 40.530 1.00 36.73 ? 26 THR A OG1 1 ATOM 166 C CG2 . THR A 1 26 ? 25.122 8.131 38.726 1.00 34.58 ? 26 THR A CG2 1 ATOM 167 N N . ASP A 1 27 ? 22.621 10.488 37.987 1.00 33.94 ? 27 ASP A N 1 ATOM 168 C CA . ASP A 1 27 ? 21.382 10.266 37.250 1.00 33.25 ? 27 ASP A CA 1 ATOM 169 C C . ASP A 1 27 ? 21.729 9.620 35.936 1.00 31.24 ? 27 ASP A C 1 ATOM 170 O O . ASP A 1 27 ? 22.733 9.976 35.322 1.00 30.04 ? 27 ASP A O 1 ATOM 171 C CB . ASP A 1 27 ? 20.669 11.577 37.005 1.00 33.41 ? 27 ASP A CB 1 ATOM 172 C CG . ASP A 1 27 ? 20.349 12.293 38.283 1.00 35.48 ? 27 ASP A CG 1 ATOM 173 O OD1 . ASP A 1 27 ? 19.352 11.935 38.939 1.00 36.87 ? 27 ASP A OD1 1 ATOM 174 O OD2 . ASP A 1 27 ? 21.116 13.209 38.649 1.00 36.06 ? 27 ASP A OD2 1 ATOM 175 N N . SER A 1 28 ? 20.892 8.682 35.499 1.00 30.78 ? 28 SER A N 1 ATOM 176 C CA . SER A 1 28 ? 21.112 7.979 34.249 1.00 29.41 ? 28 SER A CA 1 ATOM 177 C C . SER A 1 28 ? 19.863 7.971 33.384 1.00 28.89 ? 28 SER A C 1 ATOM 178 O O . SER A 1 28 ? 18.739 8.001 33.897 1.00 29.66 ? 28 SER A O 1 ATOM 179 C CB . SER A 1 28 ? 21.579 6.554 34.502 1.00 29.99 ? 28 SER A CB 1 ATOM 180 O OG . SER A 1 28 ? 22.858 6.556 35.099 1.00 30.29 ? 28 SER A OG 1 ATOM 181 N N . VAL A 1 29 ? 20.089 7.953 32.071 1.00 27.50 ? 29 VAL A N 1 ATOM 182 C CA . VAL A 1 29 ? 19.028 7.783 31.078 1.00 27.21 ? 29 VAL A CA 1 ATOM 183 C C . VAL A 1 29 ? 19.502 6.747 30.067 1.00 26.55 ? 29 VAL A C 1 ATOM 184 O O . VAL A 1 29 ? 20.708 6.582 29.854 1.00 26.19 ? 29 VAL A O 1 ATOM 185 C CB . VAL A 1 29 ? 18.641 9.101 30.357 1.00 26.78 ? 29 VAL A CB 1 ATOM 186 C CG1 . VAL A 1 29 ? 17.993 10.071 31.330 1.00 27.56 ? 29 VAL A CG1 1 ATOM 187 C CG2 . VAL A 1 29 ? 19.846 9.755 29.682 1.00 25.98 ? 29 VAL A CG2 1 ATOM 188 N N . VAL A 1 30 ? 18.558 6.039 29.463 1.00 26.60 ? 30 VAL A N 1 ATOM 189 C CA . VAL A 1 30 ? 18.866 5.033 28.445 1.00 26.38 ? 30 VAL A CA 1 ATOM 190 C C . VAL A 1 30 ? 18.039 5.335 27.200 1.00 26.18 ? 30 VAL A C 1 ATOM 191 O O . VAL A 1 30 ? 16.847 5.603 27.301 1.00 26.41 ? 30 VAL A O 1 ATOM 192 C CB . VAL A 1 30 ? 18.586 3.607 28.956 1.00 27.38 ? 30 VAL A CB 1 ATOM 193 C CG1 . VAL A 1 30 ? 18.946 2.561 27.911 1.00 27.48 ? 30 VAL A CG1 1 ATOM 194 C CG2 . VAL A 1 30 ? 19.380 3.357 30.234 1.00 27.69 ? 30 VAL A CG2 1 ATOM 195 N N . TRP A 1 31 ? 18.698 5.262 26.045 1.00 25.80 ? 31 TRP A N 1 ATOM 196 C CA . TRP A 1 31 ? 18.121 5.586 24.755 1.00 25.94 ? 31 TRP A CA 1 ATOM 197 C C . TRP A 1 31 ? 18.311 4.412 23.820 1.00 26.55 ? 31 TRP A C 1 ATOM 198 O O . TRP A 1 31 ? 19.382 3.817 23.792 1.00 26.56 ? 31 TRP A O 1 ATOM 199 C CB . TRP A 1 31 ? 18.831 6.793 24.122 1.00 25.28 ? 31 TRP A CB 1 ATOM 200 C CG . TRP A 1 31 ? 18.699 8.041 24.891 1.00 24.93 ? 31 TRP A CG 1 ATOM 201 C CD1 . TRP A 1 31 ? 19.563 8.517 25.828 1.00 24.55 ? 31 TRP A CD1 1 ATOM 202 C CD2 . TRP A 1 31 ? 17.638 8.993 24.797 1.00 25.12 ? 31 TRP A CD2 1 ATOM 203 N NE1 . TRP A 1 31 ? 19.104 9.710 26.328 1.00 24.66 ? 31 TRP A NE1 1 ATOM 204 C CE2 . TRP A 1 31 ? 17.925 10.026 25.709 1.00 24.93 ? 31 TRP A CE2 1 ATOM 205 C CE3 . TRP A 1 31 ? 16.472 9.076 24.024 1.00 25.65 ? 31 TRP A CE3 1 ATOM 206 C CZ2 . TRP A 1 31 ? 17.088 11.130 25.877 1.00 25.31 ? 31 TRP A CZ2 1 ATOM 207 C CZ3 . TRP A 1 31 ? 15.641 10.166 24.187 1.00 25.88 ? 31 TRP A CZ3 1 ATOM 208 C CH2 . TRP A 1 31 ? 15.947 11.180 25.113 1.00 25.72 ? 31 TRP A CH2 1 ATOM 209 N N . LEU A 1 32 ? 17.271 4.083 23.063 1.00 27.26 ? 32 LEU A N 1 ATOM 210 C CA . LEU A 1 32 ? 17.401 3.164 21.932 1.00 28.09 ? 32 LEU A CA 1 ATOM 211 C C . LEU A 1 32 ? 17.085 3.982 20.706 1.00 28.21 ? 32 LEU A C 1 ATOM 212 O O . LEU A 1 32 ? 15.922 4.320 20.466 1.00 28.42 ? 32 LEU A O 1 ATOM 213 C CB . LEU A 1 32 ? 16.445 1.975 22.048 1.00 29.31 ? 32 LEU A CB 1 ATOM 214 C CG . LEU A 1 32 ? 16.484 0.973 20.890 1.00 30.62 ? 32 LEU A CG 1 ATOM 215 C CD1 . LEU A 1 32 ? 17.892 0.449 20.641 1.00 30.69 ? 32 LEU A CD1 1 ATOM 216 C CD2 . LEU A 1 32 ? 15.534 -0.173 21.207 1.00 31.96 ? 32 LEU A CD2 1 ATOM 217 N N . GLY A 1 33 ? 18.121 4.303 19.934 1.00 28.11 ? 33 GLY A N 1 ATOM 218 C CA . GLY A 1 33 ? 17.993 5.300 18.870 1.00 28.46 ? 33 GLY A CA 1 ATOM 219 C C . GLY A 1 33 ? 17.653 6.610 19.533 1.00 27.47 ? 33 GLY A C 1 ATOM 220 O O . GLY A 1 33 ? 18.356 7.047 20.453 1.00 26.59 ? 33 GLY A O 1 ATOM 221 N N . ASP A 1 34 ? 16.548 7.214 19.110 1.00 27.87 ? 34 ASP A N 1 ATOM 222 C CA . ASP A 1 34 ? 16.075 8.473 19.688 1.00 27.32 ? 34 ASP A CA 1 ATOM 223 C C . ASP A 1 34 ? 14.870 8.319 20.648 1.00 27.33 ? 34 ASP A C 1 ATOM 224 O O . ASP A 1 34 ? 14.250 9.312 21.009 1.00 27.16 ? 34 ASP A O 1 ATOM 225 C CB . ASP A 1 34 ? 15.756 9.473 18.563 1.00 28.07 ? 34 ASP A CB 1 ATOM 226 C CG . ASP A 1 34 ? 14.641 9.000 17.635 1.00 29.32 ? 34 ASP A CG 1 ATOM 227 O OD1 . ASP A 1 34 ? 14.076 7.909 17.857 1.00 29.67 ? 34 ASP A OD1 1 ATOM 228 O OD2 . ASP A 1 34 ? 14.316 9.726 16.673 1.00 30.42 ? 34 ASP A OD2 1 ATOM 229 N N . LEU A 1 35 ? 14.543 7.085 21.059 1.00 27.65 ? 35 LEU A N 1 ATOM 230 C CA . LEU A 1 35 ? 13.466 6.855 22.027 1.00 27.90 ? 35 LEU A CA 1 ATOM 231 C C . LEU A 1 35 ? 14.041 6.491 23.380 1.00 27.26 ? 35 LEU A C 1 ATOM 232 O O . LEU A 1 35 ? 14.851 5.581 23.484 1.00 27.20 ? 35 LEU A O 1 ATOM 233 C CB . LEU A 1 35 ? 12.517 5.752 21.537 1.00 29.17 ? 35 LEU A CB 1 ATOM 234 C CG . LEU A 1 35 ? 11.776 6.066 20.241 1.00 30.09 ? 35 LEU A CG 1 ATOM 235 C CD1 . LEU A 1 35 ? 10.950 4.865 19.808 1.00 31.46 ? 35 LEU A CD1 1 ATOM 236 C CD2 . LEU A 1 35 ? 10.886 7.292 20.366 1.00 30.10 ? 35 LEU A CD2 1 ATOM 237 N N . GLN A 1 36 ? 13.649 7.229 24.417 1.00 27.13 ? 36 GLN A N 1 ATOM 238 C CA . GLN A 1 36 ? 14.078 6.928 25.774 1.00 27.07 ? 36 GLN A CA 1 ATOM 239 C C . GLN A 1 36 ? 13.413 5.626 26.262 1.00 28.07 ? 36 GLN A C 1 ATOM 240 O O . GLN A 1 36 ? 12.205 5.470 26.147 1.00 28.74 ? 36 GLN A O 1 ATOM 241 C CB . GLN A 1 36 ? 13.729 8.075 26.721 1.00 27.02 ? 36 GLN A CB 1 ATOM 242 C CG . GLN A 1 36 ? 14.331 7.883 28.105 1.00 27.11 ? 36 GLN A CG 1 ATOM 243 C CD . GLN A 1 36 ? 14.192 9.094 28.999 1.00 27.34 ? 36 GLN A CD 1 ATOM 244 O OE1 . GLN A 1 36 ? 13.673 10.137 28.585 1.00 27.37 ? 36 GLN A OE1 1 ATOM 245 N NE2 . GLN A 1 36 ? 14.667 8.970 30.228 1.00 27.65 ? 36 GLN A NE2 1 ATOM 246 N N . THR A 1 37 ? 14.212 4.710 26.798 1.00 28.34 ? 37 THR A N 1 ATOM 247 C CA . THR A 1 37 ? 13.699 3.439 27.337 1.00 29.69 ? 37 THR A CA 1 ATOM 248 C C . THR A 1 37 ? 13.735 3.346 28.858 1.00 30.58 ? 37 THR A C 1 ATOM 249 O O . THR A 1 37 ? 12.932 2.609 29.450 1.00 31.77 ? 37 THR A O 1 ATOM 250 C CB . THR A 1 37 ? 14.476 2.255 26.770 1.00 29.87 ? 37 THR A CB 1 ATOM 251 O OG1 . THR A 1 37 ? 15.871 2.398 27.082 1.00 29.10 ? 37 THR A OG1 1 ATOM 252 C CG2 . THR A 1 37 ? 14.283 2.156 25.275 1.00 29.85 ? 37 THR A CG2 1 ATOM 253 N N . HIS A 1 38 ? 14.675 4.053 29.495 1.00 30.13 ? 38 HIS A N 1 ATOM 254 C CA . HIS A 1 38 ? 14.788 4.052 30.954 1.00 31.18 ? 38 HIS A CA 1 ATOM 255 C C . HIS A 1 38 ? 15.193 5.419 31.488 1.00 31.05 ? 38 HIS A C 1 ATOM 256 O O . HIS A 1 38 ? 15.796 6.223 30.779 1.00 29.59 ? 38 HIS A O 1 ATOM 257 C CB . HIS A 1 38 ? 15.818 3.018 31.423 1.00 31.48 ? 38 HIS A CB 1 ATOM 258 C CG . HIS A 1 38 ? 15.634 1.647 30.841 1.00 32.12 ? 38 HIS A CG 1 ATOM 259 N ND1 . HIS A 1 38 ? 15.976 1.327 29.543 1.00 31.40 ? 38 HIS A ND1 1 ATOM 260 C CD2 . HIS A 1 38 ? 15.167 0.501 31.397 1.00 33.71 ? 38 HIS A CD2 1 ATOM 261 C CE1 . HIS A 1 38 ? 15.719 0.051 29.320 1.00 32.61 ? 38 HIS A CE1 1 ATOM 262 N NE2 . HIS A 1 38 ? 15.234 -0.477 30.430 1.00 33.93 ? 38 HIS A NE2 1 ATOM 263 N N . ARG A 1 39 ? 14.828 5.673 32.737 1.00 32.79 ? 39 ARG A N 1 ATOM 264 C CA . ARG A 1 39 ? 15.458 6.706 33.546 1.00 33.28 ? 39 ARG A CA 1 ATOM 265 C C . ARG A 1 39 ? 15.793 6.124 34.908 1.00 35.14 ? 39 ARG A C 1 ATOM 266 O O . ARG A 1 39 ? 15.068 5.275 35.439 1.00 36.34 ? 39 ARG A O 1 ATOM 267 C CB . ARG A 1 39 ? 14.585 7.966 33.666 1.00 33.82 ? 39 ARG A CB 1 ATOM 268 C CG . ARG A 1 39 ? 13.396 7.891 34.615 1.00 35.82 ? 39 ARG A CG 1 ATOM 269 C CD . ARG A 1 39 ? 12.767 9.258 34.825 1.00 36.39 ? 39 ARG A CD 1 ATOM 270 N NE . ARG A 1 39 ? 12.132 9.757 33.601 1.00 35.67 ? 39 ARG A NE 1 ATOM 271 C CZ . ARG A 1 39 ? 10.972 9.327 33.104 1.00 36.23 ? 39 ARG A CZ 1 ATOM 272 N NH1 . ARG A 1 39 ? 10.247 8.401 33.732 1.00 37.51 ? 39 ARG A NH1 1 ATOM 273 N NH2 . ARG A 1 39 ? 10.509 9.864 31.971 1.00 35.65 ? 39 ARG A NH2 1 ATOM 274 N N . TRP A 1 40 ? 16.904 6.567 35.472 1.00 35.51 ? 40 TRP A N 1 ATOM 275 C CA . TRP A 1 40 ? 17.265 6.133 36.801 1.00 37.54 ? 40 TRP A CA 1 ATOM 276 C C . TRP A 1 40 ? 17.793 7.292 37.618 1.00 38.32 ? 40 TRP A C 1 ATOM 277 O O . TRP A 1 40 ? 18.989 7.620 37.573 1.00 37.55 ? 40 TRP A O 1 ATOM 278 C CB . TRP A 1 40 ? 18.235 4.965 36.740 1.00 37.56 ? 40 TRP A CB 1 ATOM 279 C CG . TRP A 1 40 ? 18.488 4.342 38.072 1.00 39.69 ? 40 TRP A CG 1 ATOM 280 C CD1 . TRP A 1 40 ? 17.681 4.380 39.179 1.00 41.81 ? 40 TRP A CD1 1 ATOM 281 C CD2 . TRP A 1 40 ? 19.624 3.571 38.434 1.00 40.05 ? 40 TRP A CD2 1 ATOM 282 N NE1 . TRP A 1 40 ? 18.255 3.689 40.206 1.00 43.55 ? 40 TRP A NE1 1 ATOM 283 C CE2 . TRP A 1 40 ? 19.451 3.180 39.779 1.00 42.40 ? 40 TRP A CE2 1 ATOM 284 C CE3 . TRP A 1 40 ? 20.777 3.174 37.754 1.00 38.82 ? 40 TRP A CE3 1 ATOM 285 C CZ2 . TRP A 1 40 ? 20.380 2.413 40.453 1.00 43.42 ? 40 TRP A CZ2 1 ATOM 286 C CZ3 . TRP A 1 40 ? 21.706 2.416 38.425 1.00 39.80 ? 40 TRP A CZ3 1 ATOM 287 C CH2 . TRP A 1 40 ? 21.499 2.040 39.765 1.00 42.04 ? 40 TRP A CH2 1 ATOM 288 N N . SER A 1 41 ? 16.876 7.910 38.354 1.00 40.02 ? 41 SER A N 1 ATOM 289 C CA . SER A 1 41 ? 17.165 9.077 39.160 1.00 41.37 ? 41 SER A CA 1 ATOM 290 C C . SER A 1 41 ? 18.015 8.703 40.375 1.00 43.11 ? 41 SER A C 1 ATOM 291 O O . SER A 1 41 ? 17.961 7.564 40.871 1.00 44.11 ? 41 SER A O 1 ATOM 292 C CB . SER A 1 41 ? 15.853 9.736 39.594 1.00 43.00 ? 41 SER A CB 1 ATOM 293 O OG . SER A 1 41 ? 16.090 10.892 40.370 1.00 44.52 ? 41 SER A OG 1 ATOM 294 N N . ASN A 1 42 ? 18.806 9.666 40.838 1.00 43.73 ? 42 ASN A N 1 ATOM 295 C CA . ASN A 1 42 ? 19.642 9.481 42.016 1.00 45.70 ? 42 ASN A CA 1 ATOM 296 C C . ASN A 1 42 ? 18.834 9.065 43.255 1.00 48.79 ? 42 ASN A C 1 ATOM 297 O O . ASN A 1 42 ? 19.224 8.151 43.984 1.00 50.11 ? 42 ASN A O 1 ATOM 298 C CB . ASN A 1 42 ? 20.411 10.758 42.341 1.00 46.06 ? 42 ASN A CB 1 ATOM 299 C CG . ASN A 1 42 ? 21.381 10.552 43.478 1.00 47.95 ? 42 ASN A CG 1 ATOM 300 O OD1 . ASN A 1 42 ? 22.377 9.850 43.315 1.00 46.90 ? 42 ASN A OD1 1 ATOM 301 N ND2 . ASN A 1 42 ? 21.094 11.144 44.639 1.00 50.88 ? 42 ASN A ND2 1 ATOM 302 N N . ASP A 1 43 ? 17.717 9.756 43.469 1.00 50.11 ? 43 ASP A N 1 ATOM 303 C CA . ASP A 1 43 ? 16.832 9.522 44.628 1.00 53.45 ? 43 ASP A CA 1 ATOM 304 C C . ASP A 1 43 ? 15.900 8.306 44.487 1.00 53.86 ? 43 ASP A C 1 ATOM 305 O O . ASP A 1 43 ? 15.248 7.916 45.458 1.00 56.66 ? 43 ASP A O 1 ATOM 306 C CB . ASP A 1 43 ? 16.017 10.790 44.978 1.00 55.04 ? 43 ASP A CB 1 ATOM 307 C CG . ASP A 1 43 ? 15.551 11.555 43.753 1.00 53.02 ? 43 ASP A CG 1 ATOM 308 O OD1 . ASP A 1 43 ? 16.407 12.200 43.103 1.00 51.47 ? 43 ASP A OD1 1 ATOM 309 O OD2 . ASP A 1 43 ? 14.347 11.506 43.431 1.00 53.52 ? 43 ASP A OD2 1 ATOM 310 N N . SER A 1 44 ? 15.835 7.716 43.294 1.00 51.33 ? 44 SER A N 1 ATOM 311 C CA . SER A 1 44 ? 15.123 6.457 43.077 1.00 51.63 ? 44 SER A CA 1 ATOM 312 C C . SER A 1 44 ? 16.055 5.257 43.277 1.00 51.36 ? 44 SER A C 1 ATOM 313 O O . SER A 1 44 ? 17.141 5.208 42.697 1.00 49.56 ? 44 SER A O 1 ATOM 314 C CB . SER A 1 44 ? 14.534 6.430 41.666 1.00 49.54 ? 44 SER A CB 1 ATOM 315 O OG . SER A 1 44 ? 13.819 5.230 41.436 1.00 50.34 ? 44 SER A OG 1 ATOM 316 N N . ALA A 1 45 ? 15.626 4.297 44.097 1.00 53.38 ? 45 ALA A N 1 ATOM 317 C CA . ALA A 1 45 ? 16.364 3.039 44.309 1.00 53.61 ? 45 ALA A CA 1 ATOM 318 C C . ALA A 1 45 ? 16.335 2.114 43.086 1.00 51.42 ? 45 ALA A C 1 ATOM 319 O O . ALA A 1 45 ? 17.264 1.329 42.869 1.00 50.64 ? 45 ALA A O 1 ATOM 320 C CB . ALA A 1 45 ? 15.807 2.301 45.526 1.00 57.20 ? 45 ALA A CB 1 ATOM 321 N N . THR A 1 46 ? 15.256 2.205 42.311 1.00 50.57 ? 46 THR A N 1 ATOM 322 C CA . THR A 1 46 ? 14.986 1.314 41.180 1.00 49.29 ? 46 THR A CA 1 ATOM 323 C C . THR A 1 46 ? 15.067 2.076 39.849 1.00 46.17 ? 46 THR A C 1 ATOM 324 O O . THR A 1 46 ? 14.786 3.271 39.802 1.00 45.62 ? 46 THR A O 1 ATOM 325 C CB . THR A 1 46 ? 13.575 0.703 41.310 1.00 51.13 ? 46 THR A CB 1 ATOM 326 O OG1 . THR A 1 46 ? 12.602 1.750 41.394 1.00 51.42 ? 46 THR A OG1 1 ATOM 327 C CG2 . THR A 1 46 ? 13.474 -0.156 42.566 1.00 54.43 ? 46 THR A CG2 1 ATOM 328 N N . ILE A 1 47 ? 15.431 1.358 38.785 1.00 44.57 ? 47 ILE A N 1 ATOM 329 C CA . ILE A 1 47 ? 15.444 1.881 37.415 1.00 42.13 ? 47 ILE A CA 1 ATOM 330 C C . ILE A 1 47 ? 14.006 1.934 36.892 1.00 42.15 ? 47 ILE A C 1 ATOM 331 O O . ILE A 1 47 ? 13.270 0.945 36.982 1.00 43.60 ? 47 ILE A O 1 ATOM 332 C CB . ILE A 1 47 ? 16.299 0.994 36.475 1.00 41.12 ? 47 ILE A CB 1 ATOM 333 C CG1 . ILE A 1 47 ? 17.756 0.939 36.950 1.00 40.92 ? 47 ILE A CG1 1 ATOM 334 C CG2 . ILE A 1 47 ? 16.243 1.506 35.036 1.00 39.20 ? 47 ILE A CG2 1 ATOM 335 C CD1 . ILE A 1 47 ? 18.545 -0.222 36.383 1.00 40.77 ? 47 ILE A CD1 1 ATOM 336 N N . SER A 1 48 ? 13.626 3.087 36.344 1.00 40.52 ? 48 SER A N 1 ATOM 337 C CA . SER A 1 48 ? 12.255 3.370 35.929 1.00 40.55 ? 48 SER A CA 1 ATOM 338 C C . SER A 1 48 ? 12.070 3.157 34.415 1.00 38.76 ? 48 SER A C 1 ATOM 339 O O . SER A 1 48 ? 12.845 3.684 33.609 1.00 36.91 ? 48 SER A O 1 ATOM 340 C CB . SER A 1 48 ? 11.878 4.795 36.355 1.00 40.70 ? 48 SER A CB 1 ATOM 341 O OG . SER A 1 48 ? 10.703 5.260 35.707 1.00 40.85 ? 48 SER A OG 1 ATOM 342 N N . PHE A 1 49 ? 11.051 2.374 34.042 1.00 39.22 ? 49 PHE A N 1 ATOM 343 C CA . PHE A 1 49 ? 10.725 2.096 32.638 1.00 37.94 ? 49 PHE A CA 1 ATOM 344 C C . PHE A 1 49 ? 9.967 3.284 32.037 1.00 36.86 ? 49 PHE A C 1 ATOM 345 O O . PHE A 1 49 ? 9.003 3.777 32.636 1.00 37.88 ? 49 PHE A O 1 ATOM 346 C CB . PHE A 1 49 ? 9.837 0.835 32.497 1.00 39.58 ? 49 PHE A CB 1 ATOM 347 C CG . PHE A 1 49 ? 10.473 -0.464 32.957 1.00 40.75 ? 49 PHE A CG 1 ATOM 348 C CD1 . PHE A 1 49 ? 11.852 -0.670 32.931 1.00 39.83 ? 49 PHE A CD1 1 ATOM 349 C CD2 . PHE A 1 49 ? 9.656 -1.527 33.362 1.00 42.91 ? 49 PHE A CD2 1 ATOM 350 C CE1 . PHE A 1 49 ? 12.399 -1.873 33.339 1.00 41.16 ? 49 PHE A CE1 1 ATOM 351 C CE2 . PHE A 1 49 ? 10.207 -2.737 33.765 1.00 44.18 ? 49 PHE A CE2 1 ATOM 352 C CZ . PHE A 1 49 ? 11.582 -2.913 33.755 1.00 43.24 ? 49 PHE A CZ 1 ATOM 353 N N . THR A 1 50 ? 10.402 3.749 30.865 1.00 34.83 ? 50 THR A N 1 ATOM 354 C CA . THR A 1 50 ? 9.701 4.810 30.135 1.00 34.00 ? 50 THR A CA 1 ATOM 355 C C . THR A 1 50 ? 9.001 4.288 28.872 1.00 33.95 ? 50 THR A C 1 ATOM 356 O O . THR A 1 50 ? 8.514 5.084 28.058 1.00 33.58 ? 50 THR A O 1 ATOM 357 C CB . THR A 1 50 ? 10.660 5.962 29.750 1.00 32.47 ? 50 THR A CB 1 ATOM 358 O OG1 . THR A 1 50 ? 11.700 5.458 28.913 1.00 31.41 ? 50 THR A OG1 1 ATOM 359 C CG2 . THR A 1 50 ? 11.274 6.591 30.998 1.00 32.58 ? 50 THR A CG2 1 ATOM 360 N N . LYS A 1 51 ? 8.972 2.964 28.709 1.00 34.44 ? 51 LYS A N 1 ATOM 361 C CA . LYS A 1 51 ? 8.165 2.298 27.696 1.00 34.97 ? 51 LYS A CA 1 ATOM 362 C C . LYS A 1 51 ? 7.547 1.027 28.295 1.00 36.63 ? 51 LYS A C 1 ATOM 363 O O . LYS A 1 51 ? 8.074 0.494 29.269 1.00 37.11 ? 51 LYS A O 1 ATOM 364 C CB . LYS A 1 51 ? 9.021 1.912 26.490 1.00 34.15 ? 51 LYS A CB 1 ATOM 365 C CG . LYS A 1 51 ? 9.589 3.081 25.701 1.00 32.67 ? 51 LYS A CG 1 ATOM 366 C CD . LYS A 1 51 ? 8.509 3.850 24.951 1.00 32.86 ? 51 LYS A CD 1 ATOM 367 C CE . LYS A 1 51 ? 9.078 5.060 24.221 1.00 31.65 ? 51 LYS A CE 1 ATOM 368 N NZ . LYS A 1 51 ? 9.580 6.078 25.181 1.00 30.77 ? 51 LYS A NZ 1 ATOM 369 N N . PRO A 1 52 ? 6.447 0.519 27.697 1.00 37.72 ? 52 PRO A N 1 ATOM 370 C CA . PRO A 1 52 ? 5.899 -0.781 28.104 1.00 39.61 ? 52 PRO A CA 1 ATOM 371 C C . PRO A 1 52 ? 6.908 -1.917 27.960 1.00 39.73 ? 52 PRO A C 1 ATOM 372 O O . PRO A 1 52 ? 6.885 -2.865 28.742 1.00 41.43 ? 52 PRO A O 1 ATOM 373 C CB . PRO A 1 52 ? 4.734 -0.998 27.120 1.00 40.54 ? 52 PRO A CB 1 ATOM 374 C CG . PRO A 1 52 ? 4.387 0.353 26.630 1.00 39.41 ? 52 PRO A CG 1 ATOM 375 C CD . PRO A 1 52 ? 5.667 1.115 26.597 1.00 37.52 ? 52 PRO A CD 1 ATOM 376 N N . TRP A 1 53 ? 7.806 -1.778 26.990 1.00 38.33 ? 53 TRP A N 1 ATOM 377 C CA . TRP A 1 53 ? 8.711 -2.830 26.535 1.00 38.59 ? 53 TRP A CA 1 ATOM 378 C C . TRP A 1 53 ? 10.165 -2.640 27.023 1.00 37.36 ? 53 TRP A C 1 ATOM 379 O O . TRP A 1 53 ? 11.085 -3.262 26.495 1.00 37.19 ? 53 TRP A O 1 ATOM 380 C CB . TRP A 1 53 ? 8.660 -2.896 24.995 1.00 38.42 ? 53 TRP A CB 1 ATOM 381 C CG . TRP A 1 53 ? 8.698 -1.539 24.259 1.00 36.76 ? 53 TRP A CG 1 ATOM 382 C CD1 . TRP A 1 53 ? 7.615 -0.794 23.847 1.00 36.83 ? 53 TRP A CD1 1 ATOM 383 C CD2 . TRP A 1 53 ? 9.861 -0.805 23.839 1.00 35.09 ? 53 TRP A CD2 1 ATOM 384 N NE1 . TRP A 1 53 ? 8.037 0.342 23.200 1.00 35.41 ? 53 TRP A NE1 1 ATOM 385 C CE2 . TRP A 1 53 ? 9.407 0.366 23.183 1.00 34.35 ? 53 TRP A CE2 1 ATOM 386 C CE3 . TRP A 1 53 ? 11.239 -1.028 23.938 1.00 34.35 ? 53 TRP A CE3 1 ATOM 387 C CZ2 . TRP A 1 53 ? 10.287 1.315 22.636 1.00 32.97 ? 53 TRP A CZ2 1 ATOM 388 C CZ3 . TRP A 1 53 ? 12.119 -0.066 23.401 1.00 32.86 ? 53 TRP A CZ3 1 ATOM 389 C CH2 . TRP A 1 53 ? 11.630 1.082 22.752 1.00 32.28 ? 53 TRP A CH2 1 ATOM 390 N N . SER A 1 54 ? 10.361 -1.814 28.053 1.00 36.70 ? 54 SER A N 1 ATOM 391 C CA . SER A 1 54 ? 11.710 -1.462 28.543 1.00 35.61 ? 54 SER A CA 1 ATOM 392 C C . SER A 1 54 ? 12.478 -2.607 29.189 1.00 36.82 ? 54 SER A C 1 ATOM 393 O O . SER A 1 54 ? 13.692 -2.504 29.373 1.00 35.94 ? 54 SER A O 1 ATOM 394 C CB . SER A 1 54 ? 11.623 -0.299 29.531 1.00 34.97 ? 54 SER A CB 1 ATOM 395 O OG . SER A 1 54 ? 11.114 0.864 28.909 1.00 33.78 ? 54 SER A OG 1 ATOM 396 N N . GLN A 1 55 ? 11.781 -3.694 29.536 1.00 38.96 ? 55 GLN A N 1 ATOM 397 C CA . GLN A 1 55 ? 12.437 -4.920 30.010 1.00 40.58 ? 55 GLN A CA 1 ATOM 398 C C . GLN A 1 55 ? 12.950 -5.814 28.865 1.00 41.01 ? 55 GLN A C 1 ATOM 399 O O . GLN A 1 55 ? 13.640 -6.806 29.126 1.00 42.09 ? 55 GLN A O 1 ATOM 400 C CB . GLN A 1 55 ? 11.474 -5.715 30.906 1.00 42.98 ? 55 GLN A CB 1 ATOM 401 C CG . GLN A 1 55 ? 12.160 -6.586 31.949 1.00 44.44 ? 55 GLN A CG 1 ATOM 402 C CD . GLN A 1 55 ? 11.173 -7.174 32.946 1.00 46.97 ? 55 GLN A CD 1 ATOM 403 O OE1 . GLN A 1 55 ? 10.465 -6.441 33.642 1.00 47.18 ? 55 GLN A OE1 1 ATOM 404 N NE2 . GLN A 1 55 ? 11.126 -8.493 33.027 1.00 49.19 ? 55 GLN A NE2 1 ATOM 405 N N . GLY A 1 56 ? 12.611 -5.480 27.612 1.00 40.52 ? 56 GLY A N 1 ATOM 406 C CA . GLY A 1 56 ? 13.018 -6.274 26.452 1.00 41.29 ? 56 GLY A CA 1 ATOM 407 C C . GLY A 1 56 ? 12.436 -7.678 26.560 1.00 44.15 ? 56 GLY A C 1 ATOM 408 O O . GLY A 1 56 ? 11.261 -7.829 26.882 1.00 45.23 ? 56 GLY A O 1 ATOM 409 N N . LYS A 1 57 ? 13.265 -8.692 26.324 1.00 45.52 ? 57 LYS A N 1 ATOM 410 C CA . LYS A 1 57 ? 12.858 -10.091 26.515 1.00 48.61 ? 57 LYS A CA 1 ATOM 411 C C . LYS A 1 57 ? 13.382 -10.700 27.828 1.00 49.85 ? 57 LYS A C 1 ATOM 412 O O . LYS A 1 57 ? 13.257 -11.903 28.031 1.00 52.11 ? 57 LYS A O 1 ATOM 413 C CB . LYS A 1 57 ? 13.302 -10.946 25.315 1.00 49.86 ? 57 LYS A CB 1 ATOM 414 C CG . LYS A 1 57 ? 12.612 -10.631 23.990 1.00 49.93 ? 57 LYS A CG 1 ATOM 415 C CD . LYS A 1 57 ? 11.099 -10.830 23.985 1.00 51.47 ? 57 LYS A CD 1 ATOM 416 C CE . LYS A 1 57 ? 10.650 -12.248 24.307 1.00 54.57 ? 57 LYS A CE 1 ATOM 417 N NZ . LYS A 1 57 ? 11.089 -13.256 23.301 1.00 56.48 ? 57 LYS A NZ 1 ATOM 418 N N . LEU A 1 58 ? 13.929 -9.883 28.729 1.00 48.62 ? 58 LEU A N 1 ATOM 419 C CA . LEU A 1 58 ? 14.473 -10.395 29.992 1.00 50.04 ? 58 LEU A CA 1 ATOM 420 C C . LEU A 1 58 ? 13.358 -10.737 30.987 1.00 52.22 ? 58 LEU A C 1 ATOM 421 O O . LEU A 1 58 ? 12.346 -10.038 31.055 1.00 51.80 ? 58 LEU A O 1 ATOM 422 C CB . LEU A 1 58 ? 15.432 -9.383 30.627 1.00 47.99 ? 58 LEU A CB 1 ATOM 423 C CG . LEU A 1 58 ? 16.585 -8.826 29.777 1.00 45.99 ? 58 LEU A CG 1 ATOM 424 C CD1 . LEU A 1 58 ? 17.556 -8.071 30.673 1.00 44.73 ? 58 LEU A CD1 1 ATOM 425 C CD2 . LEU A 1 58 ? 17.312 -9.904 28.983 1.00 47.06 ? 58 LEU A CD2 1 ATOM 426 N N . SER A 1 59 ? 13.561 -11.799 31.767 1.00 54.89 ? 59 SER A N 1 ATOM 427 C CA . SER A 1 59 ? 12.603 -12.202 32.803 1.00 57.45 ? 59 SER A CA 1 ATOM 428 C C . SER A 1 59 ? 12.634 -11.237 33.986 1.00 57.03 ? 59 SER A C 1 ATOM 429 O O . SER A 1 59 ? 13.620 -10.523 34.180 1.00 55.23 ? 59 SER A O 1 ATOM 430 C CB . SER A 1 59 ? 12.912 -13.618 33.292 1.00 60.38 ? 59 SER A CB 1 ATOM 431 O OG . SER A 1 59 ? 14.198 -13.685 33.898 1.00 59.88 ? 59 SER A OG 1 ATOM 432 N N . ASN A 1 60 ? 11.553 -11.225 34.767 1.00 59.20 ? 60 ASN A N 1 ATOM 433 C CA . ASN A 1 60 ? 11.483 -10.453 36.019 1.00 59.75 ? 60 ASN A CA 1 ATOM 434 C C . ASN A 1 60 ? 12.661 -10.716 36.956 1.00 60.83 ? 60 ASN A C 1 ATOM 435 O O . ASN A 1 60 ? 13.200 -9.776 37.553 1.00 59.55 ? 60 ASN A O 1 ATOM 436 C CB . ASN A 1 60 ? 10.173 -10.739 36.776 1.00 62.46 ? 60 ASN A CB 1 ATOM 437 C CG . ASN A 1 60 ? 8.960 -10.066 36.146 1.00 61.63 ? 60 ASN A CG 1 ATOM 438 O OD1 . ASN A 1 60 ? 9.083 -9.265 35.217 1.00 58.99 ? 60 ASN A OD1 1 ATOM 439 N ND2 . ASN A 1 60 ? 7.779 -10.383 36.661 1.00 63.97 ? 60 ASN A ND2 1 ATOM 440 N N . GLN A 1 61 ? 13.056 -11.986 37.066 1.00 63.50 ? 61 GLN A N 1 ATOM 441 C CA . GLN A 1 61 ? 14.182 -12.400 37.912 1.00 64.98 ? 61 GLN A CA 1 ATOM 442 C C . GLN A 1 61 ? 15.523 -11.861 37.402 1.00 62.72 ? 61 GLN A C 1 ATOM 443 O O . GLN A 1 61 ? 16.281 -11.269 38.170 1.00 62.16 ? 61 GLN A O 1 ATOM 444 C CB . GLN A 1 61 ? 14.229 -13.923 38.036 1.00 68.04 ? 61 GLN A CB 1 ATOM 445 N N . GLN A 1 62 ? 15.806 -12.070 36.114 1.00 61.93 ? 62 GLN A N 1 ATOM 446 C CA . GLN A 1 62 ? 17.031 -11.551 35.478 1.00 59.75 ? 62 GLN A CA 1 ATOM 447 C C . GLN A 1 62 ? 17.150 -10.028 35.617 1.00 57.18 ? 62 GLN A C 1 ATOM 448 O O . GLN A 1 62 ? 18.207 -9.516 35.999 1.00 56.00 ? 62 GLN A O 1 ATOM 449 C CB . GLN A 1 62 ? 17.059 -11.887 33.985 1.00 59.11 ? 62 GLN A CB 1 ATOM 450 C CG . GLN A 1 62 ? 17.288 -13.355 33.651 1.00 61.47 ? 62 GLN A CG 1 ATOM 451 C CD . GLN A 1 62 ? 16.951 -13.685 32.198 1.00 61.47 ? 62 GLN A CD 1 ATOM 452 O OE1 . GLN A 1 62 ? 16.149 -12.996 31.547 1.00 60.35 ? 62 GLN A OE1 1 ATOM 453 N NE2 . GLN A 1 62 ? 17.566 -14.740 31.680 1.00 62.91 ? 62 GLN A NE2 1 ATOM 454 N N . TRP A 1 63 ? 16.063 -9.328 35.300 1.00 56.47 ? 63 TRP A N 1 ATOM 455 C CA . TRP A 1 63 ? 16.006 -7.869 35.418 1.00 54.51 ? 63 TRP A CA 1 ATOM 456 C C . TRP A 1 63 ? 16.215 -7.376 36.860 1.00 55.61 ? 63 TRP A C 1 ATOM 457 O O . TRP A 1 63 ? 16.955 -6.404 37.075 1.00 53.79 ? 63 TRP A O 1 ATOM 458 C CB . TRP A 1 63 ? 14.686 -7.301 34.879 1.00 53.83 ? 63 TRP A CB 1 ATOM 459 C CG . TRP A 1 63 ? 14.652 -5.830 35.047 1.00 51.91 ? 63 TRP A CG 1 ATOM 460 C CD1 . TRP A 1 63 ? 13.979 -5.122 36.001 1.00 52.51 ? 63 TRP A CD1 1 ATOM 461 C CD2 . TRP A 1 63 ? 15.413 -4.880 34.300 1.00 49.08 ? 63 TRP A CD2 1 ATOM 462 N NE1 . TRP A 1 63 ? 14.247 -3.782 35.870 1.00 50.49 ? 63 TRP A NE1 1 ATOM 463 C CE2 . TRP A 1 63 ? 15.128 -3.605 34.834 1.00 48.46 ? 63 TRP A CE2 1 ATOM 464 C CE3 . TRP A 1 63 ? 16.294 -4.981 33.214 1.00 47.55 ? 63 TRP A CE3 1 ATOM 465 C CZ2 . TRP A 1 63 ? 15.698 -2.423 34.312 1.00 46.00 ? 63 TRP A CZ2 1 ATOM 466 C CZ3 . TRP A 1 63 ? 16.864 -3.804 32.696 1.00 45.33 ? 63 TRP A CZ3 1 ATOM 467 C CH2 . TRP A 1 63 ? 16.558 -2.549 33.248 1.00 44.50 ? 63 TRP A CH2 1 ATOM 468 N N . GLU A 1 64 ? 15.569 -8.041 37.826 1.00 58.41 ? 64 GLU A N 1 ATOM 469 C CA . GLU A 1 64 ? 15.638 -7.647 39.246 1.00 59.90 ? 64 GLU A CA 1 ATOM 470 C C . GLU A 1 64 ? 17.071 -7.657 39.783 1.00 59.90 ? 64 GLU A C 1 ATOM 471 O O . GLU A 1 64 ? 17.462 -6.785 40.567 1.00 59.21 ? 64 GLU A O 1 ATOM 472 C CB . GLU A 1 64 ? 14.759 -8.559 40.108 1.00 63.42 ? 64 GLU A CB 1 ATOM 473 N N . LYS A 1 65 ? 17.847 -8.639 39.336 1.00 60.55 ? 65 LYS A N 1 ATOM 474 C CA . LYS A 1 65 ? 19.220 -8.807 39.793 1.00 60.93 ? 65 LYS A CA 1 ATOM 475 C C . LYS A 1 65 ? 20.146 -7.853 39.058 1.00 57.81 ? 65 LYS A C 1 ATOM 476 O O . LYS A 1 65 ? 21.088 -7.324 39.652 1.00 57.71 ? 65 LYS A O 1 ATOM 477 C CB . LYS A 1 65 ? 19.687 -10.267 39.644 1.00 62.76 ? 65 LYS A CB 1 ATOM 478 C CG . LYS A 1 65 ? 19.422 -11.172 40.847 1.00 66.31 ? 65 LYS A CG 1 ATOM 479 C CD . LYS A 1 65 ? 18.165 -12.028 40.721 1.00 68.60 ? 65 LYS A CD 1 ATOM 480 C CE . LYS A 1 65 ? 16.913 -11.315 41.219 1.00 69.01 ? 65 LYS A CE 1 ATOM 481 N NZ . LYS A 1 65 ? 15.696 -12.169 41.126 1.00 71.35 ? 65 LYS A NZ 1 ATOM 482 N N . LEU A 1 66 ? 19.893 -7.621 37.773 1.00 56.14 ? 66 LEU A N 1 ATOM 483 C CA . LEU A 1 66 ? 20.614 -6.551 37.060 1.00 53.31 ? 66 LEU A CA 1 ATOM 484 C C . LEU A 1 66 ? 20.410 -5.187 37.720 1.00 52.01 ? 66 LEU A C 1 ATOM 485 O O . LEU A 1 66 ? 21.376 -4.449 37.919 1.00 50.97 ? 66 LEU A O 1 ATOM 486 C CB . LEU A 1 66 ? 20.265 -6.493 35.569 1.00 52.11 ? 66 LEU A CB 1 ATOM 487 C CG . LEU A 1 66 ? 21.279 -7.173 34.644 1.00 51.94 ? 66 LEU A CG 1 ATOM 488 C CD1 . LEU A 1 66 ? 20.812 -7.052 33.202 1.00 50.94 ? 66 LEU A CD1 1 ATOM 489 C CD2 . LEU A 1 66 ? 22.674 -6.578 34.811 1.00 50.73 ? 66 LEU A CD2 1 ATOM 490 N N . GLN A 1 67 ? 19.168 -4.876 38.087 1.00 52.33 ? 67 GLN A N 1 ATOM 491 C CA . GLN A 1 67 ? 18.874 -3.662 38.844 1.00 51.85 ? 67 GLN A CA 1 ATOM 492 C C . GLN A 1 67 ? 19.697 -3.589 40.132 1.00 53.17 ? 67 GLN A C 1 ATOM 493 O O . GLN A 1 67 ? 20.347 -2.575 40.396 1.00 51.53 ? 67 GLN A O 1 ATOM 494 C CB . GLN A 1 67 ? 17.390 -3.567 39.180 1.00 53.11 ? 67 GLN A CB 1 ATOM 495 C CG . GLN A 1 67 ? 17.032 -2.311 39.949 1.00 53.17 ? 67 GLN A CG 1 ATOM 496 C CD . GLN A 1 67 ? 15.543 -2.084 40.038 1.00 54.22 ? 67 GLN A CD 1 ATOM 497 O OE1 . GLN A 1 67 ? 14.990 -1.273 39.293 1.00 52.61 ? 67 GLN A OE1 1 ATOM 498 N NE2 . GLN A 1 67 ? 14.884 -2.785 40.954 1.00 56.78 ? 67 GLN A NE2 1 ATOM 499 N N . HIS A 1 68 ? 19.662 -4.664 40.923 1.00 55.65 ? 68 HIS A N 1 ATOM 500 C CA . HIS A 1 68 ? 20.426 -4.722 42.170 1.00 57.54 ? 68 HIS A CA 1 ATOM 501 C C . HIS A 1 68 ? 21.932 -4.567 41.896 1.00 55.99 ? 68 HIS A C 1 ATOM 502 O O . HIS A 1 68 ? 22.597 -3.802 42.582 1.00 55.99 ? 68 HIS A O 1 ATOM 503 C CB . HIS A 1 68 ? 20.105 -6.010 42.951 1.00 61.07 ? 68 HIS A CB 1 ATOM 504 C CG . HIS A 1 68 ? 20.620 -6.020 44.361 1.00 63.65 ? 68 HIS A CG 1 ATOM 505 N ND1 . HIS A 1 68 ? 20.679 -7.170 45.122 1.00 66.93 ? 68 HIS A ND1 1 ATOM 506 C CD2 . HIS A 1 68 ? 21.099 -5.026 45.147 1.00 63.77 ? 68 HIS A CD2 1 ATOM 507 C CE1 . HIS A 1 68 ? 21.167 -6.883 46.316 1.00 68.72 ? 68 HIS A CE1 1 ATOM 508 N NE2 . HIS A 1 68 ? 21.433 -5.590 46.356 1.00 67.01 ? 68 HIS A NE2 1 ATOM 509 N N . MET A 1 69 ? 22.454 -5.245 40.873 1.00 54.91 ? 69 MET A N 1 ATOM 510 C CA . MET A 1 69 ? 23.855 -5.075 40.469 1.00 53.66 ? 69 MET A CA 1 ATOM 511 C C . MET A 1 69 ? 24.230 -3.616 40.155 1.00 51.06 ? 69 MET A C 1 ATOM 512 O O . MET A 1 69 ? 25.301 -3.139 40.549 1.00 50.66 ? 69 MET A O 1 ATOM 513 C CB . MET A 1 69 ? 24.168 -5.906 39.225 1.00 53.37 ? 69 MET A CB 1 ATOM 514 C CG . MET A 1 69 ? 25.587 -5.690 38.715 1.00 52.50 ? 69 MET A CG 1 ATOM 515 S SD . MET A 1 69 ? 25.924 -6.570 37.196 1.00 52.77 ? 69 MET A SD 1 ATOM 516 C CE . MET A 1 69 ? 26.509 -5.243 36.152 1.00 49.31 ? 69 MET A CE 1 ATOM 517 N N . PHE A 1 70 ? 23.375 -2.942 39.396 1.00 49.09 ? 70 PHE A N 1 ATOM 518 C CA . PHE A 1 70 ? 23.604 -1.543 39.062 1.00 46.82 ? 70 PHE A CA 1 ATOM 519 C C . PHE A 1 70 ? 23.484 -0.644 40.305 1.00 47.53 ? 70 PHE A C 1 ATOM 520 O O . PHE A 1 70 ? 24.223 0.340 40.425 1.00 46.36 ? 70 PHE A O 1 ATOM 521 C CB . PHE A 1 70 ? 22.663 -1.081 37.934 1.00 45.47 ? 70 PHE A CB 1 ATOM 522 C CG . PHE A 1 70 ? 23.119 -1.483 36.550 1.00 44.15 ? 70 PHE A CG 1 ATOM 523 C CD1 . PHE A 1 70 ? 24.343 -1.044 36.050 1.00 42.93 ? 70 PHE A CD1 1 ATOM 524 C CD2 . PHE A 1 70 ? 22.318 -2.276 35.733 1.00 44.62 ? 70 PHE A CD2 1 ATOM 525 C CE1 . PHE A 1 70 ? 24.766 -1.397 34.771 1.00 42.00 ? 70 PHE A CE1 1 ATOM 526 C CE2 . PHE A 1 70 ? 22.732 -2.633 34.454 1.00 43.67 ? 70 PHE A CE2 1 ATOM 527 C CZ . PHE A 1 70 ? 23.957 -2.188 33.969 1.00 42.53 ? 70 PHE A CZ 1 ATOM 528 N N . GLN A 1 71 ? 22.566 -0.982 41.219 1.00 49.21 ? 71 GLN A N 1 ATOM 529 C CA . GLN A 1 71 ? 22.414 -0.272 42.508 1.00 50.60 ? 71 GLN A CA 1 ATOM 530 C C . GLN A 1 71 ? 23.708 -0.266 43.324 1.00 51.26 ? 71 GLN A C 1 ATOM 531 O O . GLN A 1 71 ? 24.036 0.742 43.960 1.00 51.37 ? 71 GLN A O 1 ATOM 532 C CB . GLN A 1 71 ? 21.300 -0.894 43.368 1.00 53.28 ? 71 GLN A CB 1 ATOM 533 C CG . GLN A 1 71 ? 19.866 -0.567 42.962 1.00 53.11 ? 71 GLN A CG 1 ATOM 534 C CD . GLN A 1 71 ? 18.839 -1.488 43.631 1.00 55.95 ? 71 GLN A CD 1 ATOM 535 O OE1 . GLN A 1 71 ? 19.185 -2.308 44.476 1.00 58.35 ? 71 GLN A OE1 1 ATOM 536 N NE2 . GLN A 1 71 ? 17.574 -1.347 43.257 1.00 55.95 ? 71 GLN A NE2 1 ATOM 537 N N . VAL A 1 72 ? 24.417 -1.398 43.311 1.00 51.73 ? 72 VAL A N 1 ATOM 538 C CA . VAL A 1 72 ? 25.680 -1.556 44.041 1.00 52.67 ? 72 VAL A CA 1 ATOM 539 C C . VAL A 1 72 ? 26.796 -0.820 43.303 1.00 50.09 ? 72 VAL A C 1 ATOM 540 O O . VAL A 1 72 ? 27.635 -0.182 43.940 1.00 50.32 ? 72 VAL A O 1 ATOM 541 C CB . VAL A 1 72 ? 26.052 -3.044 44.257 1.00 54.38 ? 72 VAL A CB 1 ATOM 542 C CG1 . VAL A 1 72 ? 27.399 -3.177 44.969 1.00 55.45 ? 72 VAL A CG1 1 ATOM 543 C CG2 . VAL A 1 72 ? 24.972 -3.744 45.078 1.00 57.19 ? 72 VAL A CG2 1 ATOM 544 N N . TYR A 1 73 ? 26.803 -0.935 41.974 1.00 47.78 ? 73 TYR A N 1 ATOM 545 C CA . TYR A 1 73 ? 27.683 -0.131 41.113 1.00 45.35 ? 73 TYR A CA 1 ATOM 546 C C . TYR A 1 73 ? 27.567 1.358 41.418 1.00 44.50 ? 73 TYR A C 1 ATOM 547 O O . TYR A 1 73 ? 28.575 2.029 41.607 1.00 43.88 ? 73 TYR A O 1 ATOM 548 C CB . TYR A 1 73 ? 27.380 -0.363 39.628 1.00 43.54 ? 73 TYR A CB 1 ATOM 549 C CG . TYR A 1 73 ? 27.993 0.696 38.743 1.00 41.35 ? 73 TYR A CG 1 ATOM 550 C CD1 . TYR A 1 73 ? 29.367 0.746 38.549 1.00 40.88 ? 73 TYR A CD1 1 ATOM 551 C CD2 . TYR A 1 73 ? 27.210 1.683 38.144 1.00 40.20 ? 73 TYR A CD2 1 ATOM 552 C CE1 . TYR A 1 73 ? 29.952 1.729 37.762 1.00 39.12 ? 73 TYR A CE1 1 ATOM 553 C CE2 . TYR A 1 73 ? 27.784 2.664 37.349 1.00 38.47 ? 73 TYR A CE2 1 ATOM 554 C CZ . TYR A 1 73 ? 29.153 2.689 37.162 1.00 37.98 ? 73 TYR A CZ 1 ATOM 555 O OH . TYR A 1 73 ? 29.724 3.668 36.379 1.00 36.23 ? 73 TYR A OH 1 ATOM 556 N N . ARG A 1 74 ? 26.339 1.862 41.456 1.00 44.39 ? 74 ARG A N 1 ATOM 557 C CA . ARG A 1 74 ? 26.100 3.287 41.683 1.00 44.05 ? 74 ARG A CA 1 ATOM 558 C C . ARG A 1 74 ? 26.685 3.773 43.011 1.00 45.65 ? 74 ARG A C 1 ATOM 559 O O . ARG A 1 74 ? 27.357 4.803 43.043 1.00 45.00 ? 74 ARG A O 1 ATOM 560 C CB . ARG A 1 74 ? 24.609 3.605 41.629 1.00 44.50 ? 74 ARG A CB 1 ATOM 561 C CG . ARG A 1 74 ? 24.288 5.068 41.905 1.00 44.71 ? 74 ARG A CG 1 ATOM 562 C CD . ARG A 1 74 ? 22.835 5.390 41.621 1.00 45.00 ? 74 ARG A CD 1 ATOM 563 N NE . ARG A 1 74 ? 21.910 4.679 42.505 1.00 47.46 ? 74 ARG A NE 1 ATOM 564 C CZ . ARG A 1 74 ? 20.616 4.966 42.664 1.00 48.53 ? 74 ARG A CZ 1 ATOM 565 N NH1 . ARG A 1 74 ? 20.035 5.973 42.015 1.00 47.25 ? 74 ARG A NH1 1 ATOM 566 N NH2 . ARG A 1 74 ? 19.886 4.228 43.499 1.00 50.89 ? 74 ARG A NH2 1 ATOM 567 N N . VAL A 1 75 ? 26.410 3.041 44.092 1.00 47.92 ? 75 VAL A N 1 ATOM 568 C CA . VAL A 1 75 ? 26.960 3.357 45.413 1.00 49.99 ? 75 VAL A CA 1 ATOM 569 C C . VAL A 1 75 ? 28.485 3.224 45.412 1.00 49.37 ? 75 VAL A C 1 ATOM 570 O O . VAL A 1 75 ? 29.195 4.104 45.905 1.00 49.86 ? 75 VAL A O 1 ATOM 571 C CB . VAL A 1 75 ? 26.365 2.447 46.512 1.00 53.11 ? 75 VAL A CB 1 ATOM 572 N N . SER A 1 76 ? 28.973 2.131 44.835 1.00 48.43 ? 76 SER A N 1 ATOM 573 C CA . SER A 1 76 ? 30.405 1.867 44.713 1.00 47.90 ? 76 SER A CA 1 ATOM 574 C C . SER A 1 76 ? 31.160 2.947 43.946 1.00 45.56 ? 76 SER A C 1 ATOM 575 O O . SER A 1 76 ? 32.235 3.392 44.362 1.00 45.78 ? 76 SER A O 1 ATOM 576 C CB . SER A 1 76 ? 30.630 0.528 44.009 1.00 47.43 ? 76 SER A CB 1 ATOM 577 O OG . SER A 1 76 ? 30.226 -0.548 44.838 1.00 49.99 ? 76 SER A OG 1 ATOM 578 N N . PHE A 1 77 ? 30.586 3.342 42.814 1.00 43.15 ? 77 PHE A N 1 ATOM 579 C CA . PHE A 1 77 ? 31.171 4.356 41.949 1.00 41.04 ? 77 PHE A CA 1 ATOM 580 C C . PHE A 1 77 ? 31.347 5.650 42.722 1.00 41.96 ? 77 PHE A C 1 ATOM 581 O O . PHE A 1 77 ? 32.441 6.207 42.758 1.00 41.89 ? 77 PHE A O 1 ATOM 582 C CB . PHE A 1 77 ? 30.279 4.588 40.727 1.00 39.04 ? 77 PHE A CB 1 ATOM 583 C CG . PHE A 1 77 ? 30.787 5.652 39.798 1.00 37.03 ? 77 PHE A CG 1 ATOM 584 C CD1 . PHE A 1 77 ? 31.714 5.345 38.812 1.00 35.67 ? 77 PHE A CD1 1 ATOM 585 C CD2 . PHE A 1 77 ? 30.345 6.963 39.914 1.00 36.92 ? 77 PHE A CD2 1 ATOM 586 C CE1 . PHE A 1 77 ? 32.182 6.328 37.943 1.00 34.23 ? 77 PHE A CE1 1 ATOM 587 C CE2 . PHE A 1 77 ? 30.808 7.948 39.050 1.00 35.48 ? 77 PHE A CE2 1 ATOM 588 C CZ . PHE A 1 77 ? 31.733 7.629 38.072 1.00 34.14 ? 77 PHE A CZ 1 ATOM 589 N N . THR A 1 78 ? 30.261 6.102 43.341 1.00 43.19 ? 78 THR A N 1 ATOM 590 C CA . THR A 1 78 ? 30.241 7.336 44.119 1.00 44.61 ? 78 THR A CA 1 ATOM 591 C C . THR A 1 78 ? 31.336 7.350 45.188 1.00 46.86 ? 78 THR A C 1 ATOM 592 O O . THR A 1 78 ? 32.103 8.310 45.275 1.00 46.97 ? 78 THR A O 1 ATOM 593 C CB . THR A 1 78 ? 28.862 7.532 44.778 1.00 46.15 ? 78 THR A CB 1 ATOM 594 O OG1 . THR A 1 78 ? 27.857 7.620 43.759 1.00 44.34 ? 78 THR A OG1 1 ATOM 595 C CG2 . THR A 1 78 ? 28.824 8.790 45.651 1.00 47.84 ? 78 THR A CG2 1 ATOM 596 N N . ARG A 1 79 ? 31.413 6.280 45.977 1.00 48.84 ? 79 ARG A N 1 ATOM 597 C CA . ARG A 1 79 ? 32.401 6.184 47.058 1.00 51.26 ? 79 ARG A CA 1 ATOM 598 C C . ARG A 1 79 ? 33.842 6.216 46.528 1.00 50.08 ? 79 ARG A C 1 ATOM 599 O O . ARG A 1 79 ? 34.698 6.891 47.097 1.00 51.05 ? 79 ARG A O 1 ATOM 600 C CB . ARG A 1 79 ? 32.170 4.916 47.884 1.00 53.46 ? 79 ARG A CB 1 ATOM 601 N N . ASP A 1 80 ? 34.090 5.505 45.431 1.00 48.27 ? 80 ASP A N 1 ATOM 602 C CA . ASP A 1 80 ? 35.425 5.446 44.822 1.00 47.35 ? 80 ASP A CA 1 ATOM 603 C C . ASP A 1 80 ? 35.922 6.768 44.237 1.00 46.28 ? 80 ASP A C 1 ATOM 604 O O . ASP A 1 80 ? 37.108 7.075 44.347 1.00 46.43 ? 80 ASP A O 1 ATOM 605 C CB . ASP A 1 80 ? 35.472 4.373 43.733 1.00 45.73 ? 80 ASP A CB 1 ATOM 606 C CG . ASP A 1 80 ? 35.401 2.969 44.294 1.00 47.50 ? 80 ASP A CG 1 ATOM 607 O OD1 . ASP A 1 80 ? 35.524 2.781 45.525 1.00 49.46 ? 80 ASP A OD1 1 ATOM 608 O OD2 . ASP A 1 80 ? 35.233 2.034 43.490 1.00 46.72 ? 80 ASP A OD2 1 ATOM 609 N N . ILE A 1 81 ? 35.031 7.537 43.614 1.00 45.32 ? 81 ILE A N 1 ATOM 610 C CA . ILE A 1 81 ? 35.414 8.834 43.051 1.00 44.65 ? 81 ILE A CA 1 ATOM 611 C C . ILE A 1 81 ? 35.748 9.835 44.170 1.00 47.28 ? 81 ILE A C 1 ATOM 612 O O . ILE A 1 81 ? 36.744 10.554 44.081 1.00 47.20 ? 81 ILE A O 1 ATOM 613 C CB . ILE A 1 81 ? 34.319 9.397 42.109 1.00 42.88 ? 81 ILE A CB 1 ATOM 614 C CG1 . ILE A 1 81 ? 34.127 8.486 40.876 1.00 40.90 ? 81 ILE A CG1 1 ATOM 615 C CG2 . ILE A 1 81 ? 34.631 10.829 41.686 1.00 42.37 ? 81 ILE A CG2 1 ATOM 616 C CD1 . ILE A 1 81 ? 35.343 8.289 39.990 1.00 39.64 ? 81 ILE A CD1 1 ATOM 617 N N . GLN A 1 82 ? 34.934 9.866 45.223 1.00 50.12 ? 82 GLN A N 1 ATOM 618 C CA . GLN A 1 82 ? 35.176 10.780 46.347 1.00 53.28 ? 82 GLN A CA 1 ATOM 619 C C . GLN A 1 82 ? 36.449 10.395 47.101 1.00 55.54 ? 82 GLN A C 1 ATOM 620 O O . GLN A 1 82 ? 37.153 11.264 47.620 1.00 56.80 ? 82 GLN A O 1 ATOM 621 C CB . GLN A 1 82 ? 33.965 10.850 47.283 1.00 55.39 ? 82 GLN A CB 1 ATOM 622 C CG . GLN A 1 82 ? 32.692 11.269 46.562 1.00 54.15 ? 82 GLN A CG 1 ATOM 623 C CD . GLN A 1 82 ? 31.794 12.180 47.368 1.00 56.56 ? 82 GLN A CD 1 ATOM 624 O OE1 . GLN A 1 82 ? 30.807 11.734 47.959 1.00 58.43 ? 82 GLN A OE1 1 ATOM 625 N NE2 . GLN A 1 82 ? 32.122 13.467 47.389 1.00 57.05 ? 82 GLN A NE2 1 ATOM 626 N N . GLU A 1 83 ? 36.738 9.094 47.139 1.00 56.44 ? 83 GLU A N 1 ATOM 627 C CA . GLU A 1 83 ? 38.027 8.593 47.620 1.00 58.47 ? 83 GLU A CA 1 ATOM 628 C C . GLU A 1 83 ? 39.183 9.001 46.710 1.00 57.21 ? 83 GLU A C 1 ATOM 629 O O . GLU A 1 83 ? 40.199 9.506 47.190 1.00 58.50 ? 83 GLU A O 1 ATOM 630 C CB . GLU A 1 83 ? 38.007 7.060 47.768 1.00 59.07 ? 83 GLU A CB 1 ATOM 631 C CG . GLU A 1 83 ? 37.536 6.579 49.132 1.00 62.55 ? 83 GLU A CG 1 ATOM 632 C CD . GLU A 1 83 ? 38.469 6.990 50.260 1.00 65.54 ? 83 GLU A CD 1 ATOM 633 O OE1 . GLU A 1 83 ? 39.643 7.322 49.986 1.00 65.20 ? 83 GLU A OE1 1 ATOM 634 O OE2 . GLU A 1 83 ? 38.030 6.986 51.429 1.00 69.09 ? 83 GLU A OE2 1 ATOM 635 N N . LEU A 1 84 ? 39.021 8.760 45.411 1.00 55.28 ? 84 LEU A N 1 ATOM 636 C CA . LEU A 1 84 ? 40.027 9.121 44.402 1.00 54.57 ? 84 LEU A CA 1 ATOM 637 C C . LEU A 1 84 ? 40.390 10.605 44.466 1.00 55.85 ? 84 LEU A C 1 ATOM 638 O O . LEU A 1 84 ? 41.571 10.964 44.442 1.00 56.55 ? 84 LEU A O 1 ATOM 639 C CB . LEU A 1 84 ? 39.532 8.763 42.997 1.00 52.01 ? 84 LEU A CB 1 ATOM 640 C CG . LEU A 1 84 ? 40.415 9.135 41.798 1.00 50.52 ? 84 LEU A CG 1 ATOM 641 C CD1 . LEU A 1 84 ? 41.806 8.531 41.936 1.00 51.10 ? 84 LEU A CD1 1 ATOM 642 C CD2 . LEU A 1 84 ? 39.765 8.695 40.498 1.00 48.41 ? 84 LEU A CD2 1 ATOM 643 N N . VAL A 1 85 ? 39.366 11.449 44.558 1.00 56.72 ? 85 VAL A N 1 ATOM 644 C CA . VAL A 1 85 ? 39.548 12.891 44.730 1.00 58.16 ? 85 VAL A CA 1 ATOM 645 C C . VAL A 1 85 ? 40.307 13.204 46.032 1.00 61.61 ? 85 VAL A C 1 ATOM 646 O O . VAL A 1 85 ? 41.269 13.972 46.013 1.00 62.15 ? 85 VAL A O 1 ATOM 647 C CB . VAL A 1 85 ? 38.187 13.638 44.680 1.00 57.93 ? 85 VAL A CB 1 ATOM 648 C CG1 . VAL A 1 85 ? 38.314 15.091 45.134 1.00 59.69 ? 85 VAL A CG1 1 ATOM 649 C CG2 . VAL A 1 85 ? 37.608 13.584 43.273 1.00 55.20 ? 85 VAL A CG2 1 ATOM 650 N N . LYS A 1 86 ? 39.881 12.605 47.145 1.00 64.46 ? 86 LYS A N 1 ATOM 651 C CA . LYS A 1 86 ? 40.495 12.864 48.457 1.00 68.30 ? 86 LYS A CA 1 ATOM 652 C C . LYS A 1 86 ? 41.938 12.359 48.538 1.00 69.28 ? 86 LYS A C 1 ATOM 653 O O . LYS A 1 86 ? 42.805 13.057 49.062 1.00 70.88 ? 86 LYS A O 1 ATOM 654 C CB . LYS A 1 86 ? 39.662 12.247 49.589 1.00 70.60 ? 86 LYS A CB 1 ATOM 655 N N . MET A 1 87 ? 42.190 11.162 48.002 1.00 68.95 ? 87 MET A N 1 ATOM 656 C CA . MET A 1 87 ? 43.542 10.580 47.954 1.00 69.98 ? 87 MET A CA 1 ATOM 657 C C . MET A 1 87 ? 44.521 11.438 47.149 1.00 69.85 ? 87 MET A C 1 ATOM 658 O O . MET A 1 87 ? 45.736 11.319 47.326 1.00 70.78 ? 87 MET A O 1 ATOM 659 C CB . MET A 1 87 ? 43.510 9.161 47.379 1.00 68.50 ? 87 MET A CB 1 ATOM 660 N N . MET A 1 88 ? 43.986 12.277 46.259 1.00 69.21 ? 88 MET A N 1 ATOM 661 C CA . MET A 1 88 ? 44.728 13.390 45.671 1.00 69.73 ? 88 MET A CA 1 ATOM 662 C C . MET A 1 88 ? 44.256 14.702 46.293 1.00 71.32 ? 88 MET A C 1 ATOM 663 O O . MET A 1 88 ? 45.029 15.645 46.457 1.00 72.75 ? 88 MET A O 1 ATOM 664 C CB . MET A 1 88 ? 44.500 13.421 44.167 1.00 67.94 ? 88 MET A CB 1 ATOM 665 C CG . MET A 1 88 ? 44.781 12.095 43.481 1.00 67.15 ? 88 MET A CG 1 ATOM 666 S SD . MET A 1 88 ? 44.837 12.280 41.695 1.00 66.12 ? 88 MET A SD 1 ATOM 667 C CE . MET A 1 88 ? 43.234 13.014 41.364 1.00 64.90 ? 88 MET A CE 1 ATOM 668 N N . ASP A 1 93 ? 40.298 18.991 42.211 1.00 44.77 ? 93 ASP A N 1 ATOM 669 C CA . ASP A 1 93 ? 39.463 19.841 43.056 1.00 46.79 ? 93 ASP A CA 1 ATOM 670 C C . ASP A 1 93 ? 38.004 19.793 42.630 1.00 45.63 ? 93 ASP A C 1 ATOM 671 O O . ASP A 1 93 ? 37.696 19.565 41.463 1.00 43.52 ? 93 ASP A O 1 ATOM 672 C CB . ASP A 1 93 ? 39.940 21.297 43.012 1.00 48.38 ? 93 ASP A CB 1 ATOM 673 N N . TYR A 1 94 ? 37.114 20.035 43.586 1.00 47.29 ? 94 TYR A N 1 ATOM 674 C CA . TYR A 1 94 ? 35.684 20.138 43.311 1.00 46.62 ? 94 TYR A CA 1 ATOM 675 C C . TYR A 1 94 ? 35.359 21.496 42.665 1.00 46.69 ? 94 TYR A C 1 ATOM 676 O O . TYR A 1 94 ? 36.058 22.478 42.940 1.00 48.28 ? 94 TYR A O 1 ATOM 677 C CB . TYR A 1 94 ? 34.893 20.015 44.605 1.00 49.03 ? 94 TYR A CB 1 ATOM 678 C CG . TYR A 1 94 ? 34.977 18.666 45.273 1.00 49.22 ? 94 TYR A CG 1 ATOM 679 C CD1 . TYR A 1 94 ? 34.337 17.558 44.726 1.00 47.26 ? 94 TYR A CD1 1 ATOM 680 C CD2 . TYR A 1 94 ? 35.669 18.501 46.474 1.00 51.71 ? 94 TYR A CD2 1 ATOM 681 C CE1 . TYR A 1 94 ? 34.396 16.316 45.341 1.00 47.69 ? 94 TYR A CE1 1 ATOM 682 C CE2 . TYR A 1 94 ? 35.732 17.262 47.100 1.00 52.15 ? 94 TYR A CE2 1 ATOM 683 C CZ . TYR A 1 94 ? 35.093 16.174 46.530 1.00 50.18 ? 94 TYR A CZ 1 ATOM 684 O OH . TYR A 1 94 ? 35.151 14.947 47.147 1.00 51.00 ? 94 TYR A OH 1 ATOM 685 N N . PRO A 1 95 ? 34.298 21.592 41.857 1.00 44.90 ? 95 PRO A N 1 ATOM 686 C CA . PRO A 1 95 ? 33.382 20.490 41.542 1.00 43.03 ? 95 PRO A CA 1 ATOM 687 C C . PRO A 1 95 ? 33.918 19.571 40.444 1.00 40.16 ? 95 PRO A C 1 ATOM 688 O O . PRO A 1 95 ? 34.725 20.004 39.626 1.00 39.32 ? 95 PRO A O 1 ATOM 689 C CB . PRO A 1 95 ? 32.121 21.217 41.075 1.00 43.05 ? 95 PRO A CB 1 ATOM 690 C CG . PRO A 1 95 ? 32.623 22.486 40.474 1.00 43.58 ? 95 PRO A CG 1 ATOM 691 C CD . PRO A 1 95 ? 33.896 22.847 41.195 1.00 45.18 ? 95 PRO A CD 1 ATOM 692 N N . ILE A 1 96 ? 33.458 18.318 40.462 1.00 38.83 ? 96 ILE A N 1 ATOM 693 C CA . ILE A 1 96 ? 33.847 17.263 39.521 1.00 36.50 ? 96 ILE A CA 1 ATOM 694 C C . ILE A 1 96 ? 32.598 16.783 38.764 1.00 34.77 ? 96 ILE A C 1 ATOM 695 O O . ILE A 1 96 ? 31.572 16.498 39.386 1.00 35.31 ? 96 ILE A O 1 ATOM 696 C CB . ILE A 1 96 ? 34.406 16.026 40.271 1.00 36.97 ? 96 ILE A CB 1 ATOM 697 C CG1 . ILE A 1 96 ? 35.597 16.384 41.179 1.00 38.78 ? 96 ILE A CG1 1 ATOM 698 C CG2 . ILE A 1 96 ? 34.768 14.907 39.302 1.00 35.04 ? 96 ILE A CG2 1 ATOM 699 C CD1 . ILE A 1 96 ? 36.907 16.639 40.464 1.00 38.14 ? 96 ILE A CD1 1 ATOM 700 N N . GLU A 1 97 ? 32.698 16.679 37.440 1.00 32.65 ? 97 GLU A N 1 ATOM 701 C CA . GLU A 1 97 ? 31.642 16.108 36.599 1.00 31.15 ? 97 GLU A CA 1 ATOM 702 C C . GLU A 1 97 ? 32.201 14.903 35.887 1.00 29.66 ? 97 GLU A C 1 ATOM 703 O O . GLU A 1 97 ? 33.258 14.993 35.264 1.00 29.18 ? 97 GLU A O 1 ATOM 704 C CB . GLU A 1 97 ? 31.158 17.137 35.567 1.00 30.56 ? 97 GLU A CB 1 ATOM 705 C CG . GLU A 1 97 ? 30.578 18.404 36.179 1.00 32.04 ? 97 GLU A CG 1 ATOM 706 C CD . GLU A 1 97 ? 29.283 18.179 36.946 1.00 32.67 ? 97 GLU A CD 1 ATOM 707 O OE1 . GLU A 1 97 ? 28.579 17.185 36.700 1.00 31.72 ? 97 GLU A OE1 1 ATOM 708 O OE2 . GLU A 1 97 ? 28.959 19.009 37.798 1.00 34.36 ? 97 GLU A OE2 1 ATOM 709 N N . ILE A 1 98 ? 31.512 13.766 35.991 1.00 29.16 ? 98 ILE A N 1 ATOM 710 C CA . ILE A 1 98 ? 31.884 12.560 35.259 1.00 27.98 ? 98 ILE A CA 1 ATOM 711 C C . ILE A 1 98 ? 30.672 12.075 34.469 1.00 27.23 ? 98 ILE A C 1 ATOM 712 O O . ILE A 1 98 ? 29.540 12.093 34.973 1.00 27.52 ? 98 ILE A O 1 ATOM 713 C CB . ILE A 1 98 ? 32.402 11.436 36.191 1.00 28.62 ? 98 ILE A CB 1 ATOM 714 C CG1 . ILE A 1 98 ? 33.712 11.865 36.860 1.00 29.46 ? 98 ILE A CG1 1 ATOM 715 C CG2 . ILE A 1 98 ? 32.618 10.138 35.409 1.00 27.68 ? 98 ILE A CG2 1 ATOM 716 C CD1 . ILE A 1 98 ? 34.186 10.936 37.959 1.00 30.55 ? 98 ILE A CD1 1 ATOM 717 N N . GLN A 1 99 ? 30.926 11.659 33.230 1.00 26.22 ? 99 GLN A N 1 ATOM 718 C CA . GLN A 1 99 ? 29.904 11.117 32.339 1.00 25.71 ? 99 GLN A CA 1 ATOM 719 C C . GLN A 1 99 ? 30.403 9.799 31.779 1.00 25.56 ? 99 GLN A C 1 ATOM 720 O O . GLN A 1 99 ? 31.585 9.665 31.495 1.00 25.40 ? 99 GLN A O 1 ATOM 721 C CB . GLN A 1 99 ? 29.616 12.082 31.184 1.00 25.17 ? 99 GLN A CB 1 ATOM 722 C CG . GLN A 1 99 ? 29.027 13.401 31.620 1.00 25.71 ? 99 GLN A CG 1 ATOM 723 C CD . GLN A 1 99 ? 29.263 14.513 30.614 1.00 25.60 ? 99 GLN A CD 1 ATOM 724 O OE1 . GLN A 1 99 ? 30.218 15.270 30.747 1.00 26.02 ? 99 GLN A OE1 1 ATOM 725 N NE2 . GLN A 1 99 ? 28.408 14.603 29.604 1.00 25.07 ? 99 GLN A NE2 1 ATOM 726 N N . LEU A 1 100 ? 29.514 8.813 31.664 1.00 25.80 ? 100 LEU A N 1 ATOM 727 C CA . LEU A 1 100 ? 29.831 7.536 31.029 1.00 26.02 ? 100 LEU A CA 1 ATOM 728 C C . LEU A 1 100 ? 28.795 7.320 29.960 1.00 25.69 ? 100 LEU A C 1 ATOM 729 O O . LEU A 1 100 ? 27.617 7.619 30.180 1.00 25.98 ? 100 LEU A O 1 ATOM 730 C CB . LEU A 1 100 ? 29.803 6.363 32.024 1.00 27.07 ? 100 LEU A CB 1 ATOM 731 C CG . LEU A 1 100 ? 31.020 6.106 32.912 1.00 27.91 ? 100 LEU A CG 1 ATOM 732 C CD1 . LEU A 1 100 ? 31.072 7.066 34.084 1.00 28.67 ? 100 LEU A CD1 1 ATOM 733 C CD2 . LEU A 1 100 ? 31.011 4.669 33.426 1.00 28.77 ? 100 LEU A CD2 1 ATOM 734 N N . SER A 1 101 ? 29.247 6.902 28.784 1.00 25.43 ? 101 SER A N 1 ATOM 735 C CA . SER A 1 101 ? 28.389 6.503 27.689 1.00 25.60 ? 101 SER A CA 1 ATOM 736 C C . SER A 1 101 ? 28.776 5.068 27.358 1.00 26.47 ? 101 SER A C 1 ATOM 737 O O . SER A 1 101 ? 29.901 4.807 26.896 1.00 26.49 ? 101 SER A O 1 ATOM 738 C CB . SER A 1 101 ? 28.597 7.421 26.481 1.00 25.43 ? 101 SER A CB 1 ATOM 739 O OG . SER A 1 101 ? 27.788 7.049 25.380 1.00 25.53 ? 101 SER A OG 1 ATOM 740 N N . ALA A 1 102 ? 27.853 4.144 27.623 1.00 27.15 ? 102 ALA A N 1 ATOM 741 C CA . ALA A 1 102 ? 28.069 2.708 27.424 1.00 28.15 ? 102 ALA A CA 1 ATOM 742 C C . ALA A 1 102 ? 26.884 2.097 26.682 1.00 29.03 ? 102 ALA A C 1 ATOM 743 O O . ALA A 1 102 ? 25.736 2.412 26.977 1.00 28.82 ? 102 ALA A O 1 ATOM 744 C CB . ALA A 1 102 ? 28.239 2.011 28.761 1.00 28.81 ? 102 ALA A CB 1 ATOM 745 N N . GLY A 1 103 ? 27.165 1.214 25.734 1.00 29.95 ? 103 GLY A N 1 ATOM 746 C CA . GLY A 1 103 ? 26.106 0.604 24.958 1.00 31.13 ? 103 GLY A CA 1 ATOM 747 C C . GLY A 1 103 ? 26.652 -0.153 23.778 1.00 32.48 ? 103 GLY A C 1 ATOM 748 O O . GLY A 1 103 ? 27.808 -0.580 23.786 1.00 32.43 ? 103 GLY A O 1 ATOM 749 N N . CYS A 1 104 ? 25.808 -0.338 22.770 1.00 33.84 ? 104 CYS A N 1 ATOM 750 C CA . CYS A 1 104 ? 26.216 -1.028 21.563 1.00 35.82 ? 104 CYS A CA 1 ATOM 751 C C . CYS A 1 104 ? 25.493 -0.509 20.320 1.00 37.54 ? 104 CYS A C 1 ATOM 752 O O . CYS A 1 104 ? 24.339 -0.080 20.393 1.00 37.16 ? 104 CYS A O 1 ATOM 753 C CB . CYS A 1 104 ? 26.034 -2.544 21.729 1.00 37.09 ? 104 CYS A CB 1 ATOM 754 S SG . CYS A 1 104 ? 24.488 -3.046 22.511 1.00 36.98 ? 104 CYS A SG 1 ATOM 755 N N . GLU A 1 105 ? 26.209 -0.536 19.194 1.00 40.16 ? 105 GLU A N 1 ATOM 756 C CA . GLU A 1 105 ? 25.709 -0.103 17.886 1.00 42.82 ? 105 GLU A CA 1 ATOM 757 C C . GLU A 1 105 ? 25.392 -1.365 17.092 1.00 45.73 ? 105 GLU A C 1 ATOM 758 O O . GLU A 1 105 ? 26.269 -2.220 16.922 1.00 46.58 ? 105 GLU A O 1 ATOM 759 C CB . GLU A 1 105 ? 26.769 0.767 17.175 1.00 43.69 ? 105 GLU A CB 1 ATOM 760 C CG . GLU A 1 105 ? 26.578 0.990 15.666 1.00 46.13 ? 105 GLU A CG 1 ATOM 761 C CD . GLU A 1 105 ? 27.305 -0.036 14.787 1.00 48.74 ? 105 GLU A CD 1 ATOM 762 O OE1 . GLU A 1 105 ? 28.543 -0.190 14.917 1.00 49.58 ? 105 GLU A OE1 1 ATOM 763 O OE2 . GLU A 1 105 ? 26.640 -0.690 13.945 1.00 51.39 ? 105 GLU A OE2 1 ATOM 764 N N . MET A 1 106 ? 24.150 -1.478 16.612 1.00 47.60 ? 106 MET A N 1 ATOM 765 C CA . MET A 1 106 ? 23.651 -2.708 15.983 1.00 50.77 ? 106 MET A CA 1 ATOM 766 C C . MET A 1 106 ? 23.649 -2.616 14.461 1.00 53.32 ? 106 MET A C 1 ATOM 767 O O . MET A 1 106 ? 22.990 -1.745 13.901 1.00 53.53 ? 106 MET A O 1 ATOM 768 C CB . MET A 1 106 ? 22.221 -3.023 16.452 1.00 51.09 ? 106 MET A CB 1 ATOM 769 C CG . MET A 1 106 ? 21.992 -2.956 17.959 1.00 49.75 ? 106 MET A CG 1 ATOM 770 S SD . MET A 1 106 ? 22.978 -4.088 18.972 1.00 50.47 ? 106 MET A SD 1 ATOM 771 C CE . MET A 1 106 ? 22.325 -5.695 18.489 1.00 52.84 ? 106 MET A CE 1 ATOM 772 N N . TYR A 1 107 ? 24.380 -3.520 13.806 1.00 56.00 ? 107 TYR A N 1 ATOM 773 C CA . TYR A 1 107 ? 24.299 -3.699 12.351 1.00 58.97 ? 107 TYR A CA 1 ATOM 774 C C . TYR A 1 107 ? 23.140 -4.634 12.001 1.00 60.95 ? 107 TYR A C 1 ATOM 775 O O . TYR A 1 107 ? 23.047 -5.747 12.525 1.00 61.88 ? 107 TYR A O 1 ATOM 776 C CB . TYR A 1 107 ? 25.605 -4.278 11.796 1.00 60.71 ? 107 TYR A CB 1 ATOM 777 N N . ALA A 1 111 ? 25.069 -8.336 13.506 1.00 55.23 ? 111 ALA A N 1 ATOM 778 C CA . ALA A 1 111 ? 26.347 -7.942 14.100 1.00 53.65 ? 111 ALA A CA 1 ATOM 779 C C . ALA A 1 111 ? 26.234 -6.646 14.898 1.00 50.42 ? 111 ALA A C 1 ATOM 780 O O . ALA A 1 111 ? 25.267 -5.891 14.748 1.00 49.82 ? 111 ALA A O 1 ATOM 781 C CB . ALA A 1 111 ? 27.406 -7.796 13.017 1.00 55.20 ? 111 ALA A CB 1 ATOM 782 N N . SER A 1 112 ? 27.228 -6.396 15.749 1.00 48.63 ? 112 SER A N 1 ATOM 783 C CA . SER A 1 112 ? 27.270 -5.181 16.565 1.00 45.66 ? 112 SER A CA 1 ATOM 784 C C . SER A 1 112 ? 28.636 -4.934 17.206 1.00 43.99 ? 112 SER A C 1 ATOM 785 O O . SER A 1 112 ? 29.428 -5.865 17.382 1.00 44.98 ? 112 SER A O 1 ATOM 786 C CB . SER A 1 112 ? 26.209 -5.235 17.674 1.00 44.78 ? 112 SER A CB 1 ATOM 787 O OG . SER A 1 112 ? 26.378 -6.375 18.483 1.00 45.91 ? 112 SER A OG 1 ATOM 788 N N . GLU A 1 113 ? 28.888 -3.667 17.547 1.00 41.28 ? 113 GLU A N 1 ATOM 789 C CA . GLU A 1 113 ? 30.069 -3.253 18.306 1.00 39.57 ? 113 GLU A CA 1 ATOM 790 C C . GLU A 1 113 ? 29.618 -2.547 19.566 1.00 37.02 ? 113 GLU A C 1 ATOM 791 O O . GLU A 1 113 ? 28.598 -1.844 19.570 1.00 36.43 ? 113 GLU A O 1 ATOM 792 C CB . GLU A 1 113 ? 30.947 -2.308 17.492 1.00 39.72 ? 113 GLU A CB 1 ATOM 793 N N . SER A 1 114 ? 30.394 -2.714 20.629 1.00 35.58 ? 114 SER A N 1 ATOM 794 C CA . SER A 1 114 ? 30.086 -2.126 21.917 1.00 33.53 ? 114 SER A CA 1 ATOM 795 C C . SER A 1 114 ? 31.118 -1.080 22.268 1.00 31.91 ? 114 SER A C 1 ATOM 796 O O . SER A 1 114 ? 32.209 -1.057 21.707 1.00 32.17 ? 114 SER A O 1 ATOM 797 C CB . SER A 1 114 ? 30.031 -3.203 22.995 1.00 34.06 ? 114 SER A CB 1 ATOM 798 O OG . SER A 1 114 ? 28.916 -4.032 22.770 1.00 35.18 ? 114 SER A OG 1 ATOM 799 N N . PHE A 1 115 ? 30.741 -0.205 23.192 1.00 30.27 ? 115 PHE A N 1 ATOM 800 C CA . PHE A 1 115 ? 31.594 0.885 23.632 1.00 29.12 ? 115 PHE A CA 1 ATOM 801 C C . PHE A 1 115 ? 31.301 1.211 25.074 1.00 28.31 ? 115 PHE A C 1 ATOM 802 O O . PHE A 1 115 ? 30.186 1.022 25.553 1.00 28.02 ? 115 PHE A O 1 ATOM 803 C CB . PHE A 1 115 ? 31.347 2.145 22.794 1.00 28.68 ? 115 PHE A CB 1 ATOM 804 C CG . PHE A 1 115 ? 29.902 2.567 22.756 1.00 28.19 ? 115 PHE A CG 1 ATOM 805 C CD1 . PHE A 1 115 ? 29.027 2.020 21.815 1.00 29.02 ? 115 PHE A CD1 1 ATOM 806 C CD2 . PHE A 1 115 ? 29.405 3.484 23.679 1.00 27.25 ? 115 PHE A CD2 1 ATOM 807 C CE1 . PHE A 1 115 ? 27.688 2.398 21.786 1.00 28.82 ? 115 PHE A CE1 1 ATOM 808 C CE2 . PHE A 1 115 ? 28.070 3.871 23.647 1.00 27.08 ? 115 PHE A CE2 1 ATOM 809 C CZ . PHE A 1 115 ? 27.212 3.326 22.704 1.00 27.74 ? 115 PHE A CZ 1 ATOM 810 N N . LEU A 1 116 ? 32.311 1.746 25.743 1.00 27.90 ? 116 LEU A N 1 ATOM 811 C CA . LEU A 1 116 ? 32.167 2.271 27.076 1.00 27.49 ? 116 LEU A CA 1 ATOM 812 C C . LEU A 1 116 ? 33.169 3.408 27.176 1.00 26.99 ? 116 LEU A C 1 ATOM 813 O O . LEU A 1 116 ? 34.363 3.151 27.318 1.00 27.02 ? 116 LEU A O 1 ATOM 814 C CB . LEU A 1 116 ? 32.455 1.171 28.099 1.00 28.35 ? 116 LEU A CB 1 ATOM 815 C CG . LEU A 1 116 ? 32.020 1.414 29.548 1.00 28.51 ? 116 LEU A CG 1 ATOM 816 C CD1 . LEU A 1 116 ? 32.302 0.147 30.338 1.00 29.66 ? 116 LEU A CD1 1 ATOM 817 C CD2 . LEU A 1 116 ? 32.704 2.607 30.201 1.00 27.98 ? 116 LEU A CD2 1 ATOM 818 N N . HIS A 1 117 ? 32.676 4.645 27.081 1.00 26.25 ? 117 HIS A N 1 ATOM 819 C CA . HIS A 1 117 ? 33.514 5.861 27.140 1.00 26.02 ? 117 HIS A CA 1 ATOM 820 C C . HIS A 1 117 ? 33.221 6.671 28.394 1.00 25.52 ? 117 HIS A C 1 ATOM 821 O O . HIS A 1 117 ? 32.080 6.697 28.856 1.00 25.15 ? 117 HIS A O 1 ATOM 822 C CB . HIS A 1 117 ? 33.281 6.729 25.909 1.00 26.22 ? 117 HIS A CB 1 ATOM 823 C CG . HIS A 1 117 ? 33.642 6.053 24.627 1.00 27.18 ? 117 HIS A CG 1 ATOM 824 N ND1 . HIS A 1 117 ? 33.214 6.511 23.402 1.00 27.99 ? 117 HIS A ND1 1 ATOM 825 C CD2 . HIS A 1 117 ? 34.368 4.941 24.377 1.00 27.94 ? 117 HIS A CD2 1 ATOM 826 C CE1 . HIS A 1 117 ? 33.679 5.721 22.452 1.00 28.70 ? 117 HIS A CE1 1 ATOM 827 N NE2 . HIS A 1 117 ? 34.387 4.764 23.019 1.00 28.84 ? 117 HIS A NE2 1 ATOM 828 N N . VAL A 1 118 ? 34.263 7.306 28.942 1.00 25.23 ? 118 VAL A N 1 ATOM 829 C CA . VAL A 1 118 ? 34.168 8.080 30.168 1.00 25.19 ? 118 VAL A CA 1 ATOM 830 C C . VAL A 1 118 ? 34.730 9.482 29.903 1.00 25.09 ? 118 VAL A C 1 ATOM 831 O O . VAL A 1 118 ? 35.791 9.611 29.297 1.00 25.19 ? 118 VAL A O 1 ATOM 832 C CB . VAL A 1 118 ? 34.968 7.438 31.311 1.00 25.85 ? 118 VAL A CB 1 ATOM 833 C CG1 . VAL A 1 118 ? 34.778 8.220 32.612 1.00 26.41 ? 118 VAL A CG1 1 ATOM 834 C CG2 . VAL A 1 118 ? 34.593 5.968 31.475 1.00 26.15 ? 118 VAL A CG2 1 ATOM 835 N N . ALA A 1 119 ? 34.015 10.505 30.358 1.00 24.84 ? 119 ALA A N 1 ATOM 836 C CA . ALA A 1 119 ? 34.490 11.891 30.284 1.00 25.16 ? 119 ALA A CA 1 ATOM 837 C C . ALA A 1 119 ? 34.620 12.478 31.683 1.00 25.90 ? 119 ALA A C 1 ATOM 838 O O . ALA A 1 119 ? 33.803 12.198 32.565 1.00 26.14 ? 119 ALA A O 1 ATOM 839 C CB . ALA A 1 119 ? 33.562 12.722 29.431 1.00 24.94 ? 119 ALA A CB 1 ATOM 840 N N . PHE A 1 120 ? 35.668 13.280 31.879 1.00 26.42 ? 120 PHE A N 1 ATOM 841 C CA . PHE A 1 120 ? 35.954 13.948 33.144 1.00 27.42 ? 120 PHE A CA 1 ATOM 842 C C . PHE A 1 120 ? 35.953 15.449 32.835 1.00 27.97 ? 120 PHE A C 1 ATOM 843 O O . PHE A 1 120 ? 36.662 15.873 31.935 1.00 27.80 ? 120 PHE A O 1 ATOM 844 C CB . PHE A 1 120 ? 37.331 13.496 33.646 1.00 28.00 ? 120 PHE A CB 1 ATOM 845 C CG . PHE A 1 120 ? 37.831 14.247 34.857 1.00 29.46 ? 120 PHE A CG 1 ATOM 846 C CD1 . PHE A 1 120 ? 37.245 14.059 36.103 1.00 30.36 ? 120 PHE A CD1 1 ATOM 847 C CD2 . PHE A 1 120 ? 38.910 15.131 34.757 1.00 30.21 ? 120 PHE A CD2 1 ATOM 848 C CE1 . PHE A 1 120 ? 37.708 14.751 37.220 1.00 31.95 ? 120 PHE A CE1 1 ATOM 849 C CE2 . PHE A 1 120 ? 39.380 15.817 35.873 1.00 31.70 ? 120 PHE A CE2 1 ATOM 850 C CZ . PHE A 1 120 ? 38.779 15.628 37.105 1.00 32.55 ? 120 PHE A CZ 1 ATOM 851 N N . GLN A 1 121 ? 35.150 16.227 33.558 1.00 28.69 ? 121 GLN A N 1 ATOM 852 C CA . GLN A 1 121 ? 35.032 17.672 33.329 1.00 29.66 ? 121 GLN A CA 1 ATOM 853 C C . GLN A 1 121 ? 34.694 18.018 31.874 1.00 29.29 ? 121 GLN A C 1 ATOM 854 O O . GLN A 1 121 ? 35.232 18.965 31.319 1.00 29.93 ? 121 GLN A O 1 ATOM 855 C CB . GLN A 1 121 ? 36.310 18.403 33.790 1.00 30.68 ? 121 GLN A CB 1 ATOM 856 C CG . GLN A 1 121 ? 36.809 18.036 35.186 1.00 31.51 ? 121 GLN A CG 1 ATOM 857 C CD . GLN A 1 121 ? 35.894 18.512 36.311 1.00 32.68 ? 121 GLN A CD 1 ATOM 858 O OE1 . GLN A 1 121 ? 34.690 18.251 36.304 1.00 32.15 ? 121 GLN A OE1 1 ATOM 859 N NE2 . GLN A 1 121 ? 36.468 19.196 37.294 1.00 34.33 ? 121 GLN A NE2 1 ATOM 860 N N . GLY A 1 122 ? 33.810 17.230 31.262 1.00 28.58 ? 122 GLY A N 1 ATOM 861 C CA . GLY A 1 122 ? 33.333 17.478 29.901 1.00 28.53 ? 122 GLY A CA 1 ATOM 862 C C . GLY A 1 122 ? 34.189 16.939 28.764 1.00 28.43 ? 122 GLY A C 1 ATOM 863 O O . GLY A 1 122 ? 33.830 17.116 27.605 1.00 28.59 ? 122 GLY A O 1 ATOM 864 N N . LYS A 1 123 ? 35.288 16.260 29.091 1.00 28.64 ? 123 LYS A N 1 ATOM 865 C CA . LYS A 1 123 ? 36.273 15.797 28.114 1.00 28.90 ? 123 LYS A CA 1 ATOM 866 C C . LYS A 1 123 ? 36.464 14.279 28.184 1.00 27.54 ? 123 LYS A C 1 ATOM 867 O O . LYS A 1 123 ? 36.695 13.730 29.251 1.00 27.20 ? 123 LYS A O 1 ATOM 868 C CB . LYS A 1 123 ? 37.618 16.470 28.403 1.00 30.63 ? 123 LYS A CB 1 ATOM 869 C CG . LYS A 1 123 ? 38.679 16.304 27.321 1.00 31.72 ? 123 LYS A CG 1 ATOM 870 C CD . LYS A 1 123 ? 38.744 17.491 26.377 1.00 33.24 ? 123 LYS A CD 1 ATOM 871 C CE . LYS A 1 123 ? 39.746 17.245 25.252 1.00 34.32 ? 123 LYS A CE 1 ATOM 872 N NZ . LYS A 1 123 ? 41.140 17.147 25.747 1.00 35.03 ? 123 LYS A NZ 1 ATOM 873 N N . TYR A 1 124 ? 36.442 13.628 27.027 1.00 26.89 ? 124 TYR A N 1 ATOM 874 C CA . TYR A 1 124 ? 36.709 12.182 26.901 1.00 26.27 ? 124 TYR A CA 1 ATOM 875 C C . TYR A 1 124 ? 38.110 11.854 27.400 1.00 26.50 ? 124 TYR A C 1 ATOM 876 O O . TYR A 1 124 ? 39.071 12.430 26.906 1.00 26.95 ? 124 TYR A O 1 ATOM 877 C CB . TYR A 1 124 ? 36.544 11.801 25.427 1.00 26.42 ? 124 TYR A CB 1 ATOM 878 C CG . TYR A 1 124 ? 36.817 10.371 25.023 1.00 26.44 ? 124 TYR A CG 1 ATOM 879 C CD1 . TYR A 1 124 ? 36.386 9.288 25.801 1.00 25.99 ? 124 TYR A CD1 1 ATOM 880 C CD2 . TYR A 1 124 ? 37.458 10.101 23.809 1.00 27.14 ? 124 TYR A CD2 1 ATOM 881 C CE1 . TYR A 1 124 ? 36.628 7.980 25.387 1.00 26.29 ? 124 TYR A CE1 1 ATOM 882 C CE2 . TYR A 1 124 ? 37.691 8.814 23.382 1.00 27.39 ? 124 TYR A CE2 1 ATOM 883 C CZ . TYR A 1 124 ? 37.275 7.752 24.168 1.00 27.06 ? 124 TYR A CZ 1 ATOM 884 O OH . TYR A 1 124 ? 37.522 6.489 23.733 1.00 27.52 ? 124 TYR A OH 1 ATOM 885 N N . VAL A 1 125 ? 38.217 10.973 28.404 1.00 26.01 ? 125 VAL A N 1 ATOM 886 C CA . VAL A 1 125 ? 39.520 10.596 29.001 1.00 26.47 ? 125 VAL A CA 1 ATOM 887 C C . VAL A 1 125 ? 39.836 9.100 29.048 1.00 26.48 ? 125 VAL A C 1 ATOM 888 O O . VAL A 1 125 ? 41.015 8.737 29.093 1.00 27.09 ? 125 VAL A O 1 ATOM 889 C CB . VAL A 1 125 ? 39.705 11.152 30.444 1.00 26.86 ? 125 VAL A CB 1 ATOM 890 C CG1 . VAL A 1 125 ? 39.769 12.664 30.434 1.00 27.33 ? 125 VAL A CG1 1 ATOM 891 C CG2 . VAL A 1 125 ? 38.611 10.671 31.403 1.00 26.65 ? 125 VAL A CG2 1 ATOM 892 N N . VAL A 1 126 ? 38.819 8.234 29.070 1.00 26.07 ? 126 VAL A N 1 ATOM 893 C CA . VAL A 1 126 ? 39.023 6.794 29.295 1.00 26.56 ? 126 VAL A CA 1 ATOM 894 C C . VAL A 1 126 ? 38.000 5.981 28.497 1.00 26.51 ? 126 VAL A C 1 ATOM 895 O O . VAL A 1 126 ? 36.850 6.390 28.348 1.00 26.03 ? 126 VAL A O 1 ATOM 896 C CB . VAL A 1 126 ? 38.923 6.452 30.809 1.00 26.76 ? 126 VAL A CB 1 ATOM 897 C CG1 . VAL A 1 126 ? 38.788 4.945 31.054 1.00 27.17 ? 126 VAL A CG1 1 ATOM 898 C CG2 . VAL A 1 126 ? 40.124 7.005 31.569 1.00 27.32 ? 126 VAL A CG2 1 ATOM 899 N N . ARG A 1 127 ? 38.438 4.846 27.968 1.00 27.36 ? 127 ARG A N 1 ATOM 900 C CA . ARG A 1 127 ? 37.529 3.838 27.421 1.00 27.74 ? 127 ARG A CA 1 ATOM 901 C C . ARG A 1 127 ? 37.886 2.462 27.958 1.00 28.34 ? 127 ARG A C 1 ATOM 902 O O . ARG A 1 127 ? 39.016 2.228 28.384 1.00 28.65 ? 127 ARG A O 1 ATOM 903 C CB . ARG A 1 127 ? 37.574 3.811 25.890 1.00 28.36 ? 127 ARG A CB 1 ATOM 904 C CG . ARG A 1 127 ? 38.902 3.388 25.277 1.00 29.70 ? 127 ARG A CG 1 ATOM 905 C CD . ARG A 1 127 ? 38.775 3.207 23.770 1.00 30.92 ? 127 ARG A CD 1 ATOM 906 N NE . ARG A 1 127 ? 40.045 2.791 23.175 1.00 32.48 ? 127 ARG A NE 1 ATOM 907 C CZ . ARG A 1 127 ? 40.223 2.452 21.897 1.00 33.90 ? 127 ARG A CZ 1 ATOM 908 N NH1 . ARG A 1 127 ? 39.216 2.478 21.036 1.00 34.51 ? 127 ARG A NH1 1 ATOM 909 N NH2 . ARG A 1 127 ? 41.430 2.090 21.477 1.00 35.10 ? 127 ARG A NH2 1 ATOM 910 N N . PHE A 1 128 ? 36.901 1.569 27.945 1.00 28.51 ? 128 PHE A N 1 ATOM 911 C CA . PHE A 1 128 ? 37.165 0.149 28.054 1.00 29.47 ? 128 PHE A CA 1 ATOM 912 C C . PHE A 1 128 ? 37.268 -0.376 26.632 1.00 30.17 ? 128 PHE A C 1 ATOM 913 O O . PHE A 1 128 ? 36.411 -0.091 25.798 1.00 29.90 ? 128 PHE A O 1 ATOM 914 C CB . PHE A 1 128 ? 36.060 -0.586 28.799 1.00 29.68 ? 128 PHE A CB 1 ATOM 915 C CG . PHE A 1 128 ? 36.439 -1.982 29.166 1.00 30.93 ? 128 PHE A CG 1 ATOM 916 C CD1 . PHE A 1 128 ? 37.170 -2.232 30.322 1.00 31.46 ? 128 PHE A CD1 1 ATOM 917 C CD2 . PHE A 1 128 ? 36.107 -3.046 28.339 1.00 31.83 ? 128 PHE A CD2 1 ATOM 918 C CE1 . PHE A 1 128 ? 37.541 -3.523 30.662 1.00 32.88 ? 128 PHE A CE1 1 ATOM 919 C CE2 . PHE A 1 128 ? 36.469 -4.341 28.677 1.00 33.20 ? 128 PHE A CE2 1 ATOM 920 C CZ . PHE A 1 128 ? 37.194 -4.579 29.836 1.00 33.79 ? 128 PHE A CZ 1 ATOM 921 N N . TRP A 1 129 ? 38.317 -1.137 26.355 1.00 31.29 ? 129 TRP A N 1 ATOM 922 C CA . TRP A 1 129 ? 38.568 -1.627 25.006 1.00 32.46 ? 129 TRP A CA 1 ATOM 923 C C . TRP A 1 129 ? 39.209 -2.996 25.089 1.00 33.87 ? 129 TRP A C 1 ATOM 924 O O . TRP A 1 129 ? 40.263 -3.144 25.701 1.00 33.99 ? 129 TRP A O 1 ATOM 925 C CB . TRP A 1 129 ? 39.484 -0.654 24.254 1.00 32.59 ? 129 TRP A CB 1 ATOM 926 C CG . TRP A 1 129 ? 39.743 -1.056 22.853 1.00 34.15 ? 129 TRP A CG 1 ATOM 927 C CD1 . TRP A 1 129 ? 40.915 -1.526 22.335 1.00 35.64 ? 129 TRP A CD1 1 ATOM 928 C CD2 . TRP A 1 129 ? 38.802 -1.059 21.788 1.00 34.82 ? 129 TRP A CD2 1 ATOM 929 N NE1 . TRP A 1 129 ? 40.764 -1.803 21.002 1.00 36.99 ? 129 TRP A NE1 1 ATOM 930 C CE2 . TRP A 1 129 ? 39.475 -1.528 20.638 1.00 36.52 ? 129 TRP A CE2 1 ATOM 931 C CE3 . TRP A 1 129 ? 37.452 -0.693 21.683 1.00 34.24 ? 129 TRP A CE3 1 ATOM 932 C CZ2 . TRP A 1 129 ? 38.845 -1.643 19.398 1.00 37.72 ? 129 TRP A CZ2 1 ATOM 933 C CZ3 . TRP A 1 129 ? 36.824 -0.807 20.446 1.00 35.28 ? 129 TRP A CZ3 1 ATOM 934 C CH2 . TRP A 1 129 ? 37.522 -1.283 19.321 1.00 36.94 ? 129 TRP A CH2 1 ATOM 935 N N . GLY A 1 130 ? 38.579 -3.984 24.456 1.00 34.93 ? 130 GLY A N 1 ATOM 936 C CA . GLY A 1 130 ? 39.042 -5.362 24.518 1.00 36.68 ? 130 GLY A CA 1 ATOM 937 C C . GLY A 1 130 ? 38.859 -5.978 25.896 1.00 36.78 ? 130 GLY A C 1 ATOM 938 O O . GLY A 1 130 ? 37.775 -6.439 26.238 1.00 36.97 ? 130 GLY A O 1 ATOM 939 N N . THR A 1 131 ? 39.930 -5.969 26.681 1.00 37.06 ? 131 THR A N 1 ATOM 940 C CA . THR A 1 131 ? 39.948 -6.592 28.011 1.00 37.70 ? 131 THR A CA 1 ATOM 941 C C . THR A 1 131 ? 40.398 -5.635 29.121 1.00 36.69 ? 131 THR A C 1 ATOM 942 O O . THR A 1 131 ? 40.599 -6.064 30.259 1.00 37.26 ? 131 THR A O 1 ATOM 943 C CB . THR A 1 131 ? 40.904 -7.808 28.024 1.00 39.63 ? 131 THR A CB 1 ATOM 944 O OG1 . THR A 1 131 ? 42.245 -7.357 27.830 1.00 39.49 ? 131 THR A OG1 1 ATOM 945 C CG2 . THR A 1 131 ? 40.547 -8.811 26.931 1.00 41.17 ? 131 THR A CG2 1 ATOM 946 N N . SER A 1 132 ? 40.565 -4.352 28.809 1.00 35.42 ? 132 SER A N 1 ATOM 947 C CA . SER A 1 132 ? 41.159 -3.425 29.766 1.00 34.85 ? 132 SER A CA 1 ATOM 948 C C . SER A 1 132 ? 40.709 -1.981 29.570 1.00 33.21 ? 132 SER A C 1 ATOM 949 O O . SER A 1 132 ? 40.236 -1.583 28.491 1.00 32.44 ? 132 SER A O 1 ATOM 950 C CB . SER A 1 132 ? 42.698 -3.516 29.723 1.00 35.71 ? 132 SER A CB 1 ATOM 951 O OG . SER A 1 132 ? 43.219 -2.927 28.547 1.00 35.60 ? 132 SER A OG 1 ATOM 952 N N . TRP A 1 133 ? 40.841 -1.227 30.655 1.00 32.66 ? 133 TRP A N 1 ATOM 953 C CA . TRP A 1 133 ? 40.595 0.199 30.661 1.00 31.68 ? 133 TRP A CA 1 ATOM 954 C C . TRP A 1 133 ? 41.834 0.881 30.103 1.00 31.66 ? 133 TRP A C 1 ATOM 955 O O . TRP A 1 133 ? 42.959 0.479 30.401 1.00 31.94 ? 133 TRP A O 1 ATOM 956 C CB . TRP A 1 133 ? 40.336 0.691 32.077 1.00 31.71 ? 133 TRP A CB 1 ATOM 957 C CG . TRP A 1 133 ? 39.159 0.079 32.716 1.00 32.19 ? 133 TRP A CG 1 ATOM 958 C CD1 . TRP A 1 133 ? 39.138 -1.046 33.494 1.00 33.54 ? 133 TRP A CD1 1 ATOM 959 C CD2 . TRP A 1 133 ? 37.816 0.550 32.653 1.00 31.63 ? 133 TRP A CD2 1 ATOM 960 N NE1 . TRP A 1 133 ? 37.860 -1.301 33.916 1.00 33.81 ? 133 TRP A NE1 1 ATOM 961 C CE2 . TRP A 1 133 ? 37.027 -0.338 33.416 1.00 32.56 ? 133 TRP A CE2 1 ATOM 962 C CE3 . TRP A 1 133 ? 37.198 1.637 32.028 1.00 30.54 ? 133 TRP A CE3 1 ATOM 963 C CZ2 . TRP A 1 133 ? 35.644 -0.173 33.569 1.00 32.43 ? 133 TRP A CZ2 1 ATOM 964 C CZ3 . TRP A 1 133 ? 35.810 1.799 32.176 1.00 30.43 ? 133 TRP A CZ3 1 ATOM 965 C CH2 . TRP A 1 133 ? 35.056 0.892 32.944 1.00 31.14 ? 133 TRP A CH2 1 ATOM 966 N N . GLN A 1 134 ? 41.625 1.899 29.285 1.00 31.26 ? 134 GLN A N 1 ATOM 967 C CA . GLN A 1 134 ? 42.718 2.595 28.623 1.00 31.83 ? 134 GLN A CA 1 ATOM 968 C C . GLN A 1 134 ? 42.473 4.094 28.668 1.00 31.14 ? 134 GLN A C 1 ATOM 969 O O . GLN A 1 134 ? 41.373 4.546 28.349 1.00 30.40 ? 134 GLN A O 1 ATOM 970 C CB . GLN A 1 134 ? 42.837 2.119 27.171 1.00 32.68 ? 134 GLN A CB 1 ATOM 971 C CG . GLN A 1 134 ? 43.037 0.612 27.034 1.00 34.23 ? 134 GLN A CG 1 ATOM 972 C CD . GLN A 1 134 ? 43.158 0.137 25.596 1.00 35.40 ? 134 GLN A CD 1 ATOM 973 O OE1 . GLN A 1 134 ? 43.176 0.929 24.665 1.00 35.74 ? 134 GLN A OE1 1 ATOM 974 N NE2 . GLN A 1 134 ? 43.216 -1.173 25.417 1.00 36.87 ? 134 GLN A NE2 1 ATOM 975 N N . THR A 1 135 ? 43.486 4.856 29.090 1.00 31.45 ? 135 THR A N 1 ATOM 976 C CA . THR A 1 135 ? 43.463 6.305 28.957 1.00 31.31 ? 135 THR A CA 1 ATOM 977 C C . THR A 1 135 ? 43.646 6.657 27.493 1.00 31.64 ? 135 THR A C 1 ATOM 978 O O . THR A 1 135 ? 44.349 5.957 26.761 1.00 32.94 ? 135 THR A O 1 ATOM 979 C CB . THR A 1 135 ? 44.572 7.004 29.765 1.00 31.92 ? 135 THR A CB 1 ATOM 980 O OG1 . THR A 1 135 ? 45.840 6.400 29.474 1.00 33.22 ? 135 THR A OG1 1 ATOM 981 C CG2 . THR A 1 135 ? 44.294 6.895 31.251 1.00 32.01 ? 135 THR A CG2 1 ATOM 982 N N . VAL A 1 136 ? 43.024 7.743 27.079 1.00 31.05 ? 136 VAL A N 1 ATOM 983 C CA . VAL A 1 136 ? 43.105 8.195 25.695 1.00 31.63 ? 136 VAL A CA 1 ATOM 984 C C . VAL A 1 136 ? 44.314 9.135 25.568 1.00 32.16 ? 136 VAL A C 1 ATOM 985 O O . VAL A 1 136 ? 44.642 9.836 26.535 1.00 32.31 ? 136 VAL A O 1 ATOM 986 C CB . VAL A 1 136 ? 41.809 8.882 25.239 1.00 31.25 ? 136 VAL A CB 1 ATOM 987 C CG1 . VAL A 1 136 ? 40.614 7.987 25.537 1.00 30.73 ? 136 VAL A CG1 1 ATOM 988 C CG2 . VAL A 1 136 ? 41.623 10.259 25.865 1.00 31.10 ? 136 VAL A CG2 1 ATOM 989 N N . PRO A 1 137 ? 44.980 9.151 24.394 1.00 32.68 ? 137 PRO A N 1 ATOM 990 C CA . PRO A 1 137 ? 46.106 10.092 24.275 1.00 33.31 ? 137 PRO A CA 1 ATOM 991 C C . PRO A 1 137 ? 45.668 11.513 24.602 1.00 32.59 ? 137 PRO A C 1 ATOM 992 O O . PRO A 1 137 ? 44.612 11.944 24.156 1.00 32.09 ? 137 PRO A O 1 ATOM 993 C CB . PRO A 1 137 ? 46.524 9.945 22.811 1.00 34.57 ? 137 PRO A CB 1 ATOM 994 C CG . PRO A 1 137 ? 46.186 8.515 22.501 1.00 34.58 ? 137 PRO A CG 1 ATOM 995 C CD . PRO A 1 137 ? 44.854 8.317 23.181 1.00 33.23 ? 137 PRO A CD 1 ATOM 996 N N . GLY A 1 138 ? 46.452 12.198 25.432 1.00 32.73 ? 138 GLY A N 1 ATOM 997 C CA . GLY A 1 138 ? 46.132 13.560 25.863 1.00 32.67 ? 138 GLY A CA 1 ATOM 998 C C . GLY A 1 138 ? 45.382 13.679 27.178 1.00 31.76 ? 138 GLY A C 1 ATOM 999 O O . GLY A 1 138 ? 45.174 14.794 27.657 1.00 31.87 ? 138 GLY A O 1 ATOM 1000 N N . ALA A 1 139 ? 44.955 12.551 27.762 1.00 31.02 ? 139 ALA A N 1 ATOM 1001 C CA . ALA A 1 139 ? 44.332 12.567 29.087 1.00 30.77 ? 139 ALA A CA 1 ATOM 1002 C C . ALA A 1 139 ? 45.351 12.987 30.159 1.00 31.86 ? 139 ALA A C 1 ATOM 1003 O O . ALA A 1 139 ? 46.549 12.758 29.986 1.00 32.44 ? 139 ALA A O 1 ATOM 1004 C CB . ALA A 1 139 ? 43.765 11.196 29.424 1.00 30.04 ? 139 ALA A CB 1 ATOM 1005 N N . PRO A 1 140 ? 44.884 13.577 31.277 1.00 32.37 ? 140 PRO A N 1 ATOM 1006 C CA . PRO A 1 140 ? 45.812 13.937 32.366 1.00 33.59 ? 140 PRO A CA 1 ATOM 1007 C C . PRO A 1 140 ? 46.603 12.740 32.870 1.00 33.91 ? 140 PRO A C 1 ATOM 1008 O O . PRO A 1 140 ? 46.033 11.665 33.045 1.00 33.47 ? 140 PRO A O 1 ATOM 1009 C CB . PRO A 1 140 ? 44.885 14.457 33.465 1.00 33.76 ? 140 PRO A CB 1 ATOM 1010 C CG . PRO A 1 140 ? 43.658 14.900 32.755 1.00 33.07 ? 140 PRO A CG 1 ATOM 1011 C CD . PRO A 1 140 ? 43.497 13.966 31.592 1.00 31.94 ? 140 PRO A CD 1 ATOM 1012 N N . SER A 1 141 ? 47.900 12.919 33.097 1.00 35.09 ? 141 SER A N 1 ATOM 1013 C CA . SER A 1 141 ? 48.772 11.797 33.453 1.00 35.54 ? 141 SER A CA 1 ATOM 1014 C C . SER A 1 141 ? 48.439 11.182 34.813 1.00 35.91 ? 141 SER A C 1 ATOM 1015 O O . SER A 1 141 ? 48.770 10.020 35.051 1.00 35.84 ? 141 SER A O 1 ATOM 1016 C CB . SER A 1 141 ? 50.237 12.229 33.421 1.00 36.88 ? 141 SER A CB 1 ATOM 1017 O OG . SER A 1 141 ? 50.401 13.426 34.153 1.00 38.03 ? 141 SER A OG 1 ATOM 1018 N N . TRP A 1 142 ? 47.787 11.946 35.698 1.00 36.61 ? 142 TRP A N 1 ATOM 1019 C CA . TRP A 1 142 ? 47.368 11.407 37.000 1.00 37.47 ? 142 TRP A CA 1 ATOM 1020 C C . TRP A 1 142 ? 46.382 10.239 36.906 1.00 36.44 ? 142 TRP A C 1 ATOM 1021 O O . TRP A 1 142 ? 46.240 9.504 37.868 1.00 37.01 ? 142 TRP A O 1 ATOM 1022 C CB . TRP A 1 142 ? 46.817 12.501 37.934 1.00 38.73 ? 142 TRP A CB 1 ATOM 1023 C CG . TRP A 1 142 ? 45.584 13.190 37.467 1.00 38.18 ? 142 TRP A CG 1 ATOM 1024 C CD1 . TRP A 1 142 ? 45.515 14.413 36.864 1.00 38.43 ? 142 TRP A CD1 1 ATOM 1025 C CD2 . TRP A 1 142 ? 44.233 12.718 37.569 1.00 37.68 ? 142 TRP A CD2 1 ATOM 1026 N NE1 . TRP A 1 142 ? 44.212 14.728 36.575 1.00 37.77 ? 142 TRP A NE1 1 ATOM 1027 C CE2 . TRP A 1 142 ? 43.404 13.704 36.991 1.00 37.34 ? 142 TRP A CE2 1 ATOM 1028 C CE3 . TRP A 1 142 ? 43.641 11.555 38.083 1.00 37.81 ? 142 TRP A CE3 1 ATOM 1029 C CZ2 . TRP A 1 142 ? 42.019 13.570 36.919 1.00 36.71 ? 142 TRP A CZ2 1 ATOM 1030 C CZ3 . TRP A 1 142 ? 42.252 11.417 38.004 1.00 37.23 ? 142 TRP A CZ3 1 ATOM 1031 C CH2 . TRP A 1 142 ? 41.461 12.423 37.427 1.00 36.71 ? 142 TRP A CH2 1 ATOM 1032 N N . LEU A 1 143 ? 45.700 10.080 35.768 1.00 35.21 ? 143 LEU A N 1 ATOM 1033 C CA . LEU A 1 143 ? 44.835 8.914 35.523 1.00 34.51 ? 143 LEU A CA 1 ATOM 1034 C C . LEU A 1 143 ? 45.567 7.576 35.382 1.00 34.91 ? 143 LEU A C 1 ATOM 1035 O O . LEU A 1 143 ? 44.949 6.532 35.597 1.00 34.56 ? 143 LEU A O 1 ATOM 1036 C CB . LEU A 1 143 ? 43.972 9.131 34.272 1.00 33.36 ? 143 LEU A CB 1 ATOM 1037 C CG . LEU A 1 143 ? 42.775 10.064 34.442 1.00 33.20 ? 143 LEU A CG 1 ATOM 1038 C CD1 . LEU A 1 143 ? 42.291 10.624 33.110 1.00 32.22 ? 143 LEU A CD1 1 ATOM 1039 C CD2 . LEU A 1 143 ? 41.649 9.318 35.151 1.00 33.32 ? 143 LEU A CD2 1 ATOM 1040 N N . ASP A 1 144 ? 46.857 7.588 35.032 1.00 35.54 ? 144 ASP A N 1 ATOM 1041 C CA . ASP A 1 144 ? 47.589 6.341 34.739 1.00 36.10 ? 144 ASP A CA 1 ATOM 1042 C C . ASP A 1 144 ? 47.648 5.373 35.927 1.00 37.16 ? 144 ASP A C 1 ATOM 1043 O O . ASP A 1 144 ? 47.440 4.164 35.755 1.00 37.07 ? 144 ASP A O 1 ATOM 1044 C CB . ASP A 1 144 ? 49.013 6.638 34.235 1.00 36.89 ? 144 ASP A CB 1 ATOM 1045 C CG . ASP A 1 144 ? 49.035 7.279 32.840 1.00 36.59 ? 144 ASP A CG 1 ATOM 1046 O OD1 . ASP A 1 144 ? 47.987 7.373 32.172 1.00 35.71 ? 144 ASP A OD1 1 ATOM 1047 O OD2 . ASP A 1 144 ? 50.126 7.691 32.407 1.00 37.73 ? 144 ASP A OD2 1 ATOM 1048 N N . LEU A 1 145 ? 47.919 5.914 37.115 1.00 38.26 ? 145 LEU A N 1 ATOM 1049 C CA . LEU A 1 145 ? 47.973 5.123 38.352 1.00 39.65 ? 145 LEU A CA 1 ATOM 1050 C C . LEU A 1 145 ? 46.632 4.425 38.661 1.00 39.40 ? 145 LEU A C 1 ATOM 1051 O O . LEU A 1 145 ? 46.585 3.199 38.671 1.00 39.81 ? 145 LEU A O 1 ATOM 1052 C CB . LEU A 1 145 ? 48.434 5.987 39.539 1.00 40.93 ? 145 LEU A CB 1 ATOM 1053 N N . PRO A 1 146 ? 45.538 5.193 38.871 1.00 39.09 ? 146 PRO A N 1 ATOM 1054 C CA . PRO A 1 146 ? 44.245 4.546 39.180 1.00 39.08 ? 146 PRO A CA 1 ATOM 1055 C C . PRO A 1 146 ? 43.694 3.602 38.094 1.00 37.93 ? 146 PRO A C 1 ATOM 1056 O O . PRO A 1 146 ? 43.023 2.621 38.434 1.00 38.31 ? 146 PRO A O 1 ATOM 1057 C CB . PRO A 1 146 ? 43.295 5.727 39.409 1.00 38.81 ? 146 PRO A CB 1 ATOM 1058 C CG . PRO A 1 146 ? 43.958 6.905 38.788 1.00 38.23 ? 146 PRO A CG 1 ATOM 1059 C CD . PRO A 1 146 ? 45.427 6.663 38.899 1.00 38.85 ? 146 PRO A CD 1 ATOM 1060 N N . ILE A 1 147 ? 43.986 3.880 36.820 1.00 36.47 ? 147 ILE A N 1 ATOM 1061 C CA . ILE A 1 147 ? 43.583 2.983 35.721 1.00 35.77 ? 147 ILE A CA 1 ATOM 1062 C C . ILE A 1 147 ? 44.365 1.658 35.764 1.00 36.94 ? 147 ILE A C 1 ATOM 1063 O O . ILE A 1 147 ? 43.790 0.587 35.537 1.00 36.94 ? 147 ILE A O 1 ATOM 1064 C CB . ILE A 1 147 ? 43.688 3.694 34.336 1.00 34.51 ? 147 ILE A CB 1 ATOM 1065 C CG1 . ILE A 1 147 ? 42.673 4.845 34.245 1.00 33.67 ? 147 ILE A CG1 1 ATOM 1066 C CG2 . ILE A 1 147 ? 43.488 2.727 33.169 1.00 34.19 ? 147 ILE A CG2 1 ATOM 1067 C CD1 . ILE A 1 147 ? 41.214 4.446 34.318 1.00 33.39 ? 147 ILE A CD1 1 ATOM 1068 N N . LYS A 1 148 ? 45.660 1.727 36.076 1.00 37.86 ? 148 LYS A N 1 ATOM 1069 C CA . LYS A 1 148 ? 46.462 0.521 36.253 1.00 39.33 ? 148 LYS A CA 1 ATOM 1070 C C . LYS A 1 148 ? 45.915 -0.329 37.417 1.00 40.67 ? 148 LYS A C 1 ATOM 1071 O O . LYS A 1 148 ? 45.849 -1.555 37.315 1.00 41.55 ? 148 LYS A O 1 ATOM 1072 C CB . LYS A 1 148 ? 47.938 0.881 36.463 1.00 40.25 ? 148 LYS A CB 1 ATOM 1073 C CG . LYS A 1 148 ? 48.871 -0.317 36.608 1.00 41.85 ? 148 LYS A CG 1 ATOM 1074 C CD . LYS A 1 148 ? 50.325 0.137 36.676 1.00 42.74 ? 148 LYS A CD 1 ATOM 1075 C CE . LYS A 1 148 ? 51.276 -1.045 36.733 1.00 44.35 ? 148 LYS A CE 1 ATOM 1076 N NZ . LYS A 1 148 ? 51.298 -1.716 38.066 1.00 46.15 ? 148 LYS A NZ 1 ATOM 1077 N N . VAL A 1 149 ? 45.503 0.333 38.497 1.00 41.13 ? 149 VAL A N 1 ATOM 1078 C CA . VAL A 1 149 ? 44.912 -0.343 39.651 1.00 42.83 ? 149 VAL A CA 1 ATOM 1079 C C . VAL A 1 149 ? 43.585 -0.995 39.267 1.00 42.41 ? 149 VAL A C 1 ATOM 1080 O O . VAL A 1 149 ? 43.352 -2.169 39.567 1.00 43.65 ? 149 VAL A O 1 ATOM 1081 C CB . VAL A 1 149 ? 44.720 0.624 40.845 1.00 43.79 ? 149 VAL A CB 1 ATOM 1082 C CG1 . VAL A 1 149 ? 43.912 -0.031 41.959 1.00 45.72 ? 149 VAL A CG1 1 ATOM 1083 C CG2 . VAL A 1 149 ? 46.076 1.061 41.389 1.00 44.74 ? 149 VAL A CG2 1 ATOM 1084 N N . LEU A 1 150 ? 42.730 -0.238 38.590 1.00 40.87 ? 150 LEU A N 1 ATOM 1085 C CA . LEU A 1 150 ? 41.454 -0.761 38.098 1.00 40.34 ? 150 LEU A CA 1 ATOM 1086 C C . LEU A 1 150 ? 41.646 -1.988 37.196 1.00 40.44 ? 150 LEU A C 1 ATOM 1087 O O . LEU A 1 150 ? 40.885 -2.946 37.285 1.00 41.09 ? 150 LEU A O 1 ATOM 1088 C CB . LEU A 1 150 ? 40.694 0.336 37.347 1.00 38.57 ? 150 LEU A CB 1 ATOM 1089 C CG . LEU A 1 150 ? 39.268 0.037 36.892 1.00 38.11 ? 150 LEU A CG 1 ATOM 1090 C CD1 . LEU A 1 150 ? 38.382 -0.371 38.057 1.00 39.48 ? 150 LEU A CD1 1 ATOM 1091 C CD2 . LEU A 1 150 ? 38.714 1.266 36.190 1.00 36.72 ? 150 LEU A CD2 1 ATOM 1092 N N . ASN A 1 151 ? 42.671 -1.952 36.346 1.00 39.96 ? 151 ASN A N 1 ATOM 1093 C CA . ASN A 1 151 ? 42.999 -3.080 35.467 1.00 40.42 ? 151 ASN A CA 1 ATOM 1094 C C . ASN A 1 151 ? 43.503 -4.327 36.201 1.00 42.44 ? 151 ASN A C 1 ATOM 1095 O O . ASN A 1 151 ? 43.367 -5.429 35.684 1.00 43.28 ? 151 ASN A O 1 ATOM 1096 C CB . ASN A 1 151 ? 43.986 -2.655 34.368 1.00 39.56 ? 151 ASN A CB 1 ATOM 1097 C CG . ASN A 1 151 ? 43.306 -1.918 33.229 1.00 38.08 ? 151 ASN A CG 1 ATOM 1098 O OD1 . ASN A 1 151 ? 42.178 -2.249 32.848 1.00 37.78 ? 151 ASN A OD1 1 ATOM 1099 N ND2 . ASN A 1 151 ? 43.988 -0.927 32.666 1.00 37.08 ? 151 ASN A ND2 1 ATOM 1100 N N . ALA A 1 152 ? 44.047 -4.154 37.405 1.00 43.57 ? 152 ALA A N 1 ATOM 1101 C CA . ALA A 1 152 ? 44.416 -5.276 38.273 1.00 45.91 ? 152 ALA A CA 1 ATOM 1102 C C . ALA A 1 152 ? 43.212 -6.114 38.754 1.00 47.24 ? 152 ALA A C 1 ATOM 1103 O O . ALA A 1 152 ? 43.381 -7.259 39.174 1.00 48.90 ? 152 ALA A O 1 ATOM 1104 C CB . ALA A 1 152 ? 45.213 -4.775 39.474 1.00 46.88 ? 152 ALA A CB 1 ATOM 1105 N N . ASP A 1 153 ? 42.011 -5.538 38.700 1.00 46.57 ? 153 ASP A N 1 ATOM 1106 C CA . ASP A 1 153 ? 40.791 -6.215 39.140 1.00 47.93 ? 153 ASP A CA 1 ATOM 1107 C C . ASP A 1 153 ? 40.172 -7.028 37.997 1.00 47.58 ? 153 ASP A C 1 ATOM 1108 O O . ASP A 1 153 ? 39.450 -6.476 37.153 1.00 45.54 ? 153 ASP A O 1 ATOM 1109 C CB . ASP A 1 153 ? 39.807 -5.166 39.668 1.00 47.52 ? 153 ASP A CB 1 ATOM 1110 C CG . ASP A 1 153 ? 38.464 -5.747 40.048 1.00 48.87 ? 153 ASP A CG 1 ATOM 1111 O OD1 . ASP A 1 153 ? 38.365 -6.939 40.383 1.00 51.18 ? 153 ASP A OD1 1 ATOM 1112 O OD2 . ASP A 1 153 ? 37.486 -4.992 39.985 1.00 48.41 ? 153 ASP A OD2 1 ATOM 1113 N N . GLN A 1 154 ? 40.445 -8.336 37.984 1.00 49.33 ? 154 GLN A N 1 ATOM 1114 C CA . GLN A 1 154 ? 39.944 -9.211 36.910 1.00 49.73 ? 154 GLN A CA 1 ATOM 1115 C C . GLN A 1 154 ? 38.436 -9.452 36.969 1.00 49.56 ? 154 GLN A C 1 ATOM 1116 O O . GLN A 1 154 ? 37.796 -9.611 35.925 1.00 48.43 ? 154 GLN A O 1 ATOM 1117 C CB . GLN A 1 154 ? 40.706 -10.541 36.867 1.00 52.24 ? 154 GLN A CB 1 ATOM 1118 C CG . GLN A 1 154 ? 42.180 -10.385 36.497 1.00 52.53 ? 154 GLN A CG 1 ATOM 1119 C CD . GLN A 1 154 ? 42.391 -9.625 35.191 1.00 51.02 ? 154 GLN A CD 1 ATOM 1120 O OE1 . GLN A 1 154 ? 41.700 -9.869 34.197 1.00 50.76 ? 154 GLN A OE1 1 ATOM 1121 N NE2 . GLN A 1 154 ? 43.327 -8.674 35.198 1.00 50.42 ? 154 GLN A NE2 1 ATOM 1122 N N . GLY A 1 155 ? 37.880 -9.477 38.178 1.00 50.58 ? 155 GLY A N 1 ATOM 1123 C CA . GLY A 1 155 ? 36.432 -9.552 38.374 1.00 50.65 ? 155 GLY A CA 1 ATOM 1124 C C . GLY A 1 155 ? 35.665 -8.522 37.570 1.00 47.77 ? 155 GLY A C 1 ATOM 1125 O O . GLY A 1 155 ? 34.868 -8.882 36.704 1.00 47.35 ? 155 GLY A O 1 ATOM 1126 N N . THR A 1 156 ? 35.914 -7.240 37.843 1.00 46.07 ? 156 THR A N 1 ATOM 1127 C CA . THR A 1 156 ? 35.325 -6.133 37.070 1.00 43.60 ? 156 THR A CA 1 ATOM 1128 C C . THR A 1 156 ? 35.639 -6.207 35.575 1.00 41.48 ? 156 THR A C 1 ATOM 1129 O O . THR A 1 156 ? 34.759 -5.965 34.767 1.00 39.93 ? 156 THR A O 1 ATOM 1130 C CB . THR A 1 156 ? 35.776 -4.750 37.589 1.00 42.93 ? 156 THR A CB 1 ATOM 1131 O OG1 . THR A 1 156 ? 35.470 -4.643 38.984 1.00 45.05 ? 156 THR A OG1 1 ATOM 1132 C CG2 . THR A 1 156 ? 35.091 -3.618 36.842 1.00 41.12 ? 156 THR A CG2 1 ATOM 1133 N N . SER A 1 157 ? 36.879 -6.546 35.221 1.00 41.19 ? 157 SER A N 1 ATOM 1134 C CA . SER A 1 157 ? 37.264 -6.694 33.810 1.00 40.17 ? 157 SER A CA 1 ATOM 1135 C C . SER A 1 157 ? 36.388 -7.720 33.097 1.00 40.52 ? 157 SER A C 1 ATOM 1136 O O . SER A 1 157 ? 35.823 -7.437 32.045 1.00 39.35 ? 157 SER A O 1 ATOM 1137 C CB . SER A 1 157 ? 38.723 -7.132 33.668 1.00 41.09 ? 157 SER A CB 1 ATOM 1138 O OG . SER A 1 157 ? 39.080 -7.157 32.292 1.00 40.67 ? 157 SER A OG 1 ATOM 1139 N N . ALA A 1 158 ? 36.284 -8.907 33.688 1.00 42.06 ? 158 ALA A N 1 ATOM 1140 C CA . ALA A 1 158 ? 35.452 -9.977 33.139 1.00 43.01 ? 158 ALA A CA 1 ATOM 1141 C C . ALA A 1 158 ? 33.970 -9.579 33.114 1.00 42.15 ? 158 ALA A C 1 ATOM 1142 O O . ALA A 1 158 ? 33.265 -9.851 32.144 1.00 41.89 ? 158 ALA A O 1 ATOM 1143 C CB . ALA A 1 158 ? 35.661 -11.270 33.927 1.00 45.60 ? 158 ALA A CB 1 ATOM 1144 N N . THR A 1 159 ? 33.507 -8.924 34.174 1.00 41.62 ? 159 THR A N 1 ATOM 1145 C CA . THR A 1 159 ? 32.125 -8.459 34.254 1.00 41.09 ? 159 THR A CA 1 ATOM 1146 C C . THR A 1 159 ? 31.823 -7.426 33.143 1.00 38.69 ? 159 THR A C 1 ATOM 1147 O O . THR A 1 159 ? 30.786 -7.523 32.485 1.00 38.46 ? 159 THR A O 1 ATOM 1148 C CB . THR A 1 159 ? 31.811 -7.900 35.663 1.00 41.61 ? 159 THR A CB 1 ATOM 1149 O OG1 . THR A 1 159 ? 31.838 -8.974 36.612 1.00 44.18 ? 159 THR A OG1 1 ATOM 1150 C CG2 . THR A 1 159 ? 30.444 -7.244 35.715 1.00 41.13 ? 159 THR A CG2 1 ATOM 1151 N N . VAL A 1 160 ? 32.737 -6.480 32.919 1.00 37.00 ? 160 VAL A N 1 ATOM 1152 C CA . VAL A 1 160 ? 32.567 -5.475 31.845 1.00 35.20 ? 160 VAL A CA 1 ATOM 1153 C C . VAL A 1 160 ? 32.622 -6.138 30.465 1.00 35.50 ? 160 VAL A C 1 ATOM 1154 O O . VAL A 1 160 ? 31.798 -5.851 29.610 1.00 34.60 ? 160 VAL A O 1 ATOM 1155 C CB . VAL A 1 160 ? 33.600 -4.323 31.951 1.00 33.92 ? 160 VAL A CB 1 ATOM 1156 C CG1 . VAL A 1 160 ? 33.552 -3.409 30.730 1.00 32.43 ? 160 VAL A CG1 1 ATOM 1157 C CG2 . VAL A 1 160 ? 33.345 -3.508 33.207 1.00 33.75 ? 160 VAL A CG2 1 ATOM 1158 N N . GLN A 1 161 ? 33.575 -7.050 30.266 1.00 36.80 ? 161 GLN A N 1 ATOM 1159 C CA . GLN A 1 161 ? 33.650 -7.805 29.013 1.00 37.80 ? 161 GLN A CA 1 ATOM 1160 C C . GLN A 1 161 ? 32.335 -8.531 28.703 1.00 39.04 ? 161 GLN A C 1 ATOM 1161 O O . GLN A 1 161 ? 31.874 -8.494 27.566 1.00 38.72 ? 161 GLN A O 1 ATOM 1162 C CB . GLN A 1 161 ? 34.803 -8.808 29.044 1.00 39.44 ? 161 GLN A CB 1 ATOM 1163 C CG . GLN A 1 161 ? 36.183 -8.180 28.970 1.00 38.67 ? 161 GLN A CG 1 ATOM 1164 C CD . GLN A 1 161 ? 37.267 -9.227 29.094 1.00 40.54 ? 161 GLN A CD 1 ATOM 1165 O OE1 . GLN A 1 161 ? 37.282 -10.189 28.328 1.00 42.10 ? 161 GLN A OE1 1 ATOM 1166 N NE2 . GLN A 1 161 ? 38.163 -9.070 30.065 1.00 40.61 ? 161 GLN A NE2 1 ATOM 1167 N N . MET A 1 162 ? 31.737 -9.171 29.714 1.00 40.57 ? 162 MET A N 1 ATOM 1168 C CA . MET A 1 162 ? 30.445 -9.874 29.550 1.00 42.22 ? 162 MET A CA 1 ATOM 1169 C C . MET A 1 162 ? 29.326 -8.893 29.193 1.00 40.78 ? 162 MET A C 1 ATOM 1170 O O . MET A 1 162 ? 28.560 -9.126 28.260 1.00 41.12 ? 162 MET A O 1 ATOM 1171 C CB . MET A 1 162 ? 30.076 -10.673 30.820 1.00 44.34 ? 162 MET A CB 1 ATOM 1172 C CG . MET A 1 162 ? 30.994 -11.859 31.089 1.00 46.73 ? 162 MET A CG 1 ATOM 1173 S SD . MET A 1 162 ? 30.873 -12.702 32.701 1.00 49.86 ? 162 MET A SD 1 ATOM 1174 C CE . MET A 1 162 ? 32.566 -13.226 32.919 1.00 50.77 ? 162 MET A CE 1 ATOM 1175 N N . LEU A 1 163 ? 29.252 -7.786 29.923 1.00 39.39 ? 163 LEU A N 1 ATOM 1176 C CA . LEU A 1 163 ? 28.222 -6.772 29.673 1.00 38.15 ? 163 LEU A CA 1 ATOM 1177 C C . LEU A 1 163 ? 28.291 -6.213 28.261 1.00 36.92 ? 163 LEU A C 1 ATOM 1178 O O . LEU A 1 163 ? 27.266 -6.123 27.591 1.00 36.83 ? 163 LEU A O 1 ATOM 1179 C CB . LEU A 1 163 ? 28.284 -5.654 30.713 1.00 37.21 ? 163 LEU A CB 1 ATOM 1180 C CG . LEU A 1 163 ? 27.825 -6.122 32.101 1.00 38.68 ? 163 LEU A CG 1 ATOM 1181 C CD1 . LEU A 1 163 ? 28.280 -5.161 33.189 1.00 38.14 ? 163 LEU A CD1 1 ATOM 1182 C CD2 . LEU A 1 163 ? 26.308 -6.312 32.149 1.00 39.36 ? 163 LEU A CD2 1 ATOM 1183 N N . LEU A 1 164 ? 29.496 -5.895 27.794 1.00 36.36 ? 164 LEU A N 1 ATOM 1184 C CA . LEU A 1 164 ? 29.684 -5.327 26.454 1.00 35.76 ? 164 LEU A CA 1 ATOM 1185 C C . LEU A 1 164 ? 29.566 -6.364 25.333 1.00 37.55 ? 164 LEU A C 1 ATOM 1186 O O . LEU A 1 164 ? 28.813 -6.148 24.374 1.00 37.61 ? 164 LEU A O 1 ATOM 1187 C CB . LEU A 1 164 ? 31.024 -4.590 26.363 1.00 34.77 ? 164 LEU A CB 1 ATOM 1188 C CG . LEU A 1 164 ? 31.179 -3.418 27.340 1.00 33.36 ? 164 LEU A CG 1 ATOM 1189 C CD1 . LEU A 1 164 ? 32.593 -2.863 27.273 1.00 32.88 ? 164 LEU A CD1 1 ATOM 1190 C CD2 . LEU A 1 164 ? 30.155 -2.322 27.054 1.00 32.31 ? 164 LEU A CD2 1 ATOM 1191 N N . ASN A 1 165 ? 30.287 -7.480 25.452 1.00 39.19 ? 165 ASN A N 1 ATOM 1192 C CA . ASN A 1 165 ? 30.330 -8.481 24.376 1.00 41.28 ? 165 ASN A CA 1 ATOM 1193 C C . ASN A 1 165 ? 29.014 -9.258 24.180 1.00 42.46 ? 165 ASN A C 1 ATOM 1194 O O . ASN A 1 165 ? 28.588 -9.509 22.990 1.00 43.51 ? 165 ASN A O 1 ATOM 1195 C CB . ASN A 1 165 ? 31.479 -9.482 24.575 1.00 43.10 ? 165 ASN A CB 1 ATOM 1196 C CG . ASN A 1 165 ? 32.859 -8.837 24.519 1.00 42.65 ? 165 ASN A CG 1 ATOM 1197 O OD1 . ASN A 1 165 ? 33.009 -7.617 24.658 1.00 40.86 ? 165 ASN A OD1 1 ATOM 1198 N ND2 . ASN A 1 165 ? 33.881 -9.674 24.317 1.00 44.82 ? 165 ASN A ND2 1 ATOM 1199 N N . ASP A 1 166 ? 28.380 -9.627 25.313 1.00 42.65 ? 166 ASP A N 1 ATOM 1200 C CA . ASP A 1 166 ? 27.203 -10.509 25.326 1.00 44.17 ? 166 ASP A CA 1 ATOM 1201 C C . ASP A 1 166 ? 25.905 -9.786 25.658 1.00 43.09 ? 166 ASP A C 1 ATOM 1202 O O . ASP A 1 166 ? 24.974 -9.763 24.851 1.00 43.37 ? 166 ASP A O 1 ATOM 1203 C CB . ASP A 1 166 ? 27.398 -11.633 26.360 1.00 45.97 ? 166 ASP A CB 1 ATOM 1204 C CG . ASP A 1 166 ? 28.524 -12.573 26.006 1.00 47.62 ? 166 ASP A CG 1 ATOM 1205 O OD1 . ASP A 1 166 ? 29.205 -12.328 24.982 1.00 47.32 ? 166 ASP A OD1 1 ATOM 1206 O OD2 . ASP A 1 166 ? 28.720 -13.570 26.756 1.00 49.51 ? 166 ASP A OD2 1 ATOM 1207 N N . THR A 1 167 ? 25.849 -9.205 26.853 1.00 41.98 ? 167 THR A N 1 ATOM 1208 C CA . THR A 1 167 ? 24.599 -8.699 27.418 1.00 41.58 ? 167 THR A CA 1 ATOM 1209 C C . THR A 1 167 ? 23.991 -7.549 26.599 1.00 39.99 ? 167 THR A C 1 ATOM 1210 O O . THR A 1 167 ? 22.788 -7.555 26.337 1.00 40.13 ? 167 THR A O 1 ATOM 1211 C CB . THR A 1 167 ? 24.803 -8.240 28.878 1.00 41.09 ? 167 THR A CB 1 ATOM 1212 O OG1 . THR A 1 167 ? 25.567 -9.222 29.582 1.00 42.51 ? 167 THR A OG1 1 ATOM 1213 C CG2 . THR A 1 167 ? 23.473 -8.028 29.590 1.00 41.43 ? 167 THR A CG2 1 ATOM 1214 N N . CYS A 1 168 ? 24.818 -6.589 26.184 1.00 38.42 ? 168 CYS A N 1 ATOM 1215 C CA . CYS A 1 168 ? 24.321 -5.441 25.399 1.00 37.30 ? 168 CYS A CA 1 ATOM 1216 C C . CYS A 1 168 ? 23.592 -5.872 24.114 1.00 38.06 ? 168 CYS A C 1 ATOM 1217 O O . CYS A 1 168 ? 22.387 -5.636 24.001 1.00 38.18 ? 168 CYS A O 1 ATOM 1218 C CB . CYS A 1 168 ? 25.433 -4.413 25.105 1.00 36.13 ? 168 CYS A CB 1 ATOM 1219 S SG . CYS A 1 168 ? 24.826 -2.815 24.504 1.00 35.08 ? 168 CYS A SG 1 ATOM 1220 N N . PRO A 1 169 ? 24.292 -6.522 23.159 1.00 38.91 ? 169 PRO A N 1 ATOM 1221 C CA . PRO A 1 169 ? 23.580 -6.904 21.929 1.00 40.15 ? 169 PRO A CA 1 ATOM 1222 C C . PRO A 1 169 ? 22.379 -7.825 22.159 1.00 41.60 ? 169 PRO A C 1 ATOM 1223 O O . PRO A 1 169 ? 21.341 -7.632 21.530 1.00 42.02 ? 169 PRO A O 1 ATOM 1224 C CB . PRO A 1 169 ? 24.662 -7.581 21.081 1.00 41.43 ? 169 PRO A CB 1 ATOM 1225 C CG . PRO A 1 169 ? 25.716 -7.990 22.043 1.00 41.37 ? 169 PRO A CG 1 ATOM 1226 C CD . PRO A 1 169 ? 25.704 -6.935 23.106 1.00 39.30 ? 169 PRO A CD 1 ATOM 1227 N N . LEU A 1 170 ? 22.526 -8.789 23.070 1.00 42.54 ? 170 LEU A N 1 ATOM 1228 C CA . LEU A 1 170 ? 21.430 -9.667 23.479 1.00 44.19 ? 170 LEU A CA 1 ATOM 1229 C C . LEU A 1 170 ? 20.219 -8.878 23.969 1.00 43.05 ? 170 LEU A C 1 ATOM 1230 O O . LEU A 1 170 ? 19.103 -9.101 23.491 1.00 43.93 ? 170 LEU A O 1 ATOM 1231 C CB . LEU A 1 170 ? 21.915 -10.648 24.563 1.00 45.54 ? 170 LEU A CB 1 ATOM 1232 C CG . LEU A 1 170 ? 20.916 -11.574 25.243 1.00 47.54 ? 170 LEU A CG 1 ATOM 1233 C CD1 . LEU A 1 170 ? 20.232 -12.448 24.213 1.00 49.79 ? 170 LEU A CD1 1 ATOM 1234 C CD2 . LEU A 1 170 ? 21.634 -12.435 26.272 1.00 48.92 ? 170 LEU A CD2 1 ATOM 1235 N N . PHE A 1 171 ? 20.448 -7.947 24.898 1.00 41.09 ? 171 PHE A N 1 ATOM 1236 C CA . PHE A 1 171 ? 19.375 -7.099 25.438 1.00 40.12 ? 171 PHE A CA 1 ATOM 1237 C C . PHE A 1 171 ? 18.698 -6.264 24.349 1.00 39.26 ? 171 PHE A C 1 ATOM 1238 O O . PHE A 1 171 ? 17.461 -6.192 24.292 1.00 39.38 ? 171 PHE A O 1 ATOM 1239 C CB . PHE A 1 171 ? 19.895 -6.181 26.552 1.00 38.58 ? 171 PHE A CB 1 ATOM 1240 C CG . PHE A 1 171 ? 18.819 -5.345 27.197 1.00 38.03 ? 171 PHE A CG 1 ATOM 1241 C CD1 . PHE A 1 171 ? 17.756 -5.953 27.855 1.00 39.43 ? 171 PHE A CD1 1 ATOM 1242 C CD2 . PHE A 1 171 ? 18.861 -3.954 27.142 1.00 36.29 ? 171 PHE A CD2 1 ATOM 1243 C CE1 . PHE A 1 171 ? 16.758 -5.203 28.453 1.00 39.18 ? 171 PHE A CE1 1 ATOM 1244 C CE2 . PHE A 1 171 ? 17.863 -3.188 27.739 1.00 36.03 ? 171 PHE A CE2 1 ATOM 1245 C CZ . PHE A 1 171 ? 16.805 -3.812 28.391 1.00 37.41 ? 171 PHE A CZ 1 ATOM 1246 N N . VAL A 1 172 ? 19.513 -5.667 23.479 1.00 38.34 ? 172 VAL A N 1 ATOM 1247 C CA . VAL A 1 172 ? 19.009 -4.795 22.415 1.00 37.83 ? 172 VAL A CA 1 ATOM 1248 C C . VAL A 1 172 ? 18.145 -5.563 21.411 1.00 39.58 ? 172 VAL A C 1 ATOM 1249 O O . VAL A 1 172 ? 17.137 -5.034 20.957 1.00 39.54 ? 172 VAL A O 1 ATOM 1250 C CB . VAL A 1 172 ? 20.147 -4.031 21.700 1.00 36.90 ? 172 VAL A CB 1 ATOM 1251 C CG1 . VAL A 1 172 ? 19.622 -3.261 20.490 1.00 36.97 ? 172 VAL A CG1 1 ATOM 1252 C CG2 . VAL A 1 172 ? 20.808 -3.058 22.671 1.00 35.10 ? 172 VAL A CG2 1 ATOM 1253 N N . ARG A 1 173 ? 18.520 -6.801 21.085 1.00 41.33 ? 173 ARG A N 1 ATOM 1254 C CA . ARG A 1 173 ? 17.690 -7.636 20.211 1.00 43.41 ? 173 ARG A CA 1 ATOM 1255 C C . ARG A 1 173 ? 16.275 -7.794 20.788 1.00 43.88 ? 173 ARG A C 1 ATOM 1256 O O . ARG A 1 173 ? 15.270 -7.570 20.070 1.00 44.48 ? 173 ARG A O 1 ATOM 1257 C CB . ARG A 1 173 ? 18.350 -8.992 19.923 1.00 45.57 ? 173 ARG A CB 1 ATOM 1258 C CG . ARG A 1 173 ? 19.535 -8.887 18.965 1.00 45.73 ? 173 ARG A CG 1 ATOM 1259 C CD . ARG A 1 173 ? 20.064 -10.243 18.521 1.00 48.30 ? 173 ARG A CD 1 ATOM 1260 N NE . ARG A 1 173 ? 20.533 -11.097 19.620 1.00 48.79 ? 173 ARG A NE 1 ATOM 1261 C CZ . ARG A 1 173 ? 21.795 -11.208 20.068 1.00 48.34 ? 173 ARG A CZ 1 ATOM 1262 N NH1 . ARG A 1 173 ? 22.798 -10.478 19.572 1.00 47.11 ? 173 ARG A NH1 1 ATOM 1263 N NH2 . ARG A 1 173 ? 22.059 -12.063 21.063 1.00 49.05 ? 173 ARG A NH2 1 ATOM 1264 N N . GLY A 1 174 ? 16.200 -8.123 22.084 1.00 43.67 ? 174 GLY A N 1 ATOM 1265 C CA . GLY A 1 174 ? 14.921 -8.201 22.787 1.00 44.15 ? 174 GLY A CA 1 ATOM 1266 C C . GLY A 1 174 ? 14.128 -6.901 22.795 1.00 42.52 ? 174 GLY A C 1 ATOM 1267 O O . GLY A 1 174 ? 12.908 -6.905 22.619 1.00 43.01 ? 174 GLY A O 1 ATOM 1268 N N . LEU A 1 175 ? 14.817 -5.784 23.001 1.00 40.51 ? 175 LEU A N 1 ATOM 1269 C CA . LEU A 1 175 ? 14.161 -4.470 22.947 1.00 39.26 ? 175 LEU A CA 1 ATOM 1270 C C . LEU A 1 175 ? 13.532 -4.202 21.588 1.00 39.93 ? 175 LEU A C 1 ATOM 1271 O O . LEU A 1 175 ? 12.411 -3.700 21.525 1.00 39.86 ? 175 LEU A O 1 ATOM 1272 C CB . LEU A 1 175 ? 15.138 -3.346 23.270 1.00 37.15 ? 175 LEU A CB 1 ATOM 1273 C CG . LEU A 1 175 ? 15.512 -3.118 24.726 1.00 36.36 ? 175 LEU A CG 1 ATOM 1274 C CD1 . LEU A 1 175 ? 16.495 -1.956 24.777 1.00 34.53 ? 175 LEU A CD1 1 ATOM 1275 C CD2 . LEU A 1 175 ? 14.279 -2.834 25.572 1.00 36.64 ? 175 LEU A CD2 1 ATOM 1276 N N . LEU A 1 176 ? 14.245 -4.554 20.519 1.00 40.90 ? 176 LEU A N 1 ATOM 1277 C CA . LEU A 1 176 ? 13.752 -4.337 19.155 1.00 42.22 ? 176 LEU A CA 1 ATOM 1278 C C . LEU A 1 176 ? 12.492 -5.160 18.853 1.00 44.46 ? 176 LEU A C 1 ATOM 1279 O O . LEU A 1 176 ? 11.556 -4.659 18.225 1.00 44.96 ? 176 LEU A O 1 ATOM 1280 C CB . LEU A 1 176 ? 14.854 -4.617 18.127 1.00 43.01 ? 176 LEU A CB 1 ATOM 1281 C CG . LEU A 1 176 ? 16.062 -3.670 18.166 1.00 41.42 ? 176 LEU A CG 1 ATOM 1282 C CD1 . LEU A 1 176 ? 17.268 -4.291 17.467 1.00 42.57 ? 176 LEU A CD1 1 ATOM 1283 C CD2 . LEU A 1 176 ? 15.739 -2.322 17.563 1.00 40.62 ? 176 LEU A CD2 1 ATOM 1284 N N . GLU A 1 177 ? 12.466 -6.411 19.312 1.00 45.98 ? 177 GLU A N 1 ATOM 1285 C CA . GLU A 1 177 ? 11.271 -7.258 19.195 1.00 48.22 ? 177 GLU A CA 1 ATOM 1286 C C . GLU A 1 177 ? 10.112 -6.660 19.988 1.00 47.60 ? 177 GLU A C 1 ATOM 1287 O O . GLU A 1 177 ? 9.031 -6.425 19.435 1.00 48.43 ? 177 GLU A O 1 ATOM 1288 C CB . GLU A 1 177 ? 11.544 -8.693 19.680 1.00 50.20 ? 177 GLU A CB 1 ATOM 1289 C CG . GLU A 1 177 ? 10.384 -9.671 19.459 1.00 52.91 ? 177 GLU A CG 1 ATOM 1290 C CD . GLU A 1 177 ? 10.566 -11.010 20.167 1.00 54.95 ? 177 GLU A CD 1 ATOM 1291 O OE1 . GLU A 1 177 ? 11.661 -11.602 20.062 1.00 55.36 ? 177 GLU A OE1 1 ATOM 1292 O OE2 . GLU A 1 177 ? 9.600 -11.494 20.808 1.00 56.25 ? 177 GLU A OE2 1 ATOM 1293 N N . ALA A 1 178 ? 10.353 -6.412 21.274 1.00 46.32 ? 178 ALA A N 1 ATOM 1294 C CA . ALA A 1 178 ? 9.300 -6.019 22.200 1.00 46.22 ? 178 ALA A CA 1 ATOM 1295 C C . ALA A 1 178 ? 8.765 -4.604 21.929 1.00 44.86 ? 178 ALA A C 1 ATOM 1296 O O . ALA A 1 178 ? 7.608 -4.325 22.229 1.00 45.28 ? 178 ALA A O 1 ATOM 1297 C CB . ALA A 1 178 ? 9.786 -6.142 23.635 1.00 45.71 ? 178 ALA A CB 1 ATOM 1298 N N . GLY A 1 179 ? 9.605 -3.745 21.349 1.00 43.53 ? 179 GLY A N 1 ATOM 1299 C CA . GLY A 1 179 ? 9.257 -2.358 21.046 1.00 42.68 ? 179 GLY A CA 1 ATOM 1300 C C . GLY A 1 179 ? 8.950 -2.031 19.600 1.00 43.68 ? 179 GLY A C 1 ATOM 1301 O O . GLY A 1 179 ? 8.903 -0.853 19.237 1.00 42.59 ? 179 GLY A O 1 ATOM 1302 N N . LYS A 1 180 ? 8.709 -3.061 18.790 1.00 46.02 ? 180 LYS A N 1 ATOM 1303 C CA . LYS A 1 180 ? 8.538 -2.916 17.348 1.00 47.49 ? 180 LYS A CA 1 ATOM 1304 C C . LYS A 1 180 ? 7.513 -1.836 16.979 1.00 47.46 ? 180 LYS A C 1 ATOM 1305 O O . LYS A 1 180 ? 7.814 -0.956 16.176 1.00 47.03 ? 180 LYS A O 1 ATOM 1306 C CB . LYS A 1 180 ? 8.124 -4.264 16.743 1.00 50.14 ? 180 LYS A CB 1 ATOM 1307 C CG . LYS A 1 180 ? 8.154 -4.316 15.229 1.00 51.95 ? 180 LYS A CG 1 ATOM 1308 C CD . LYS A 1 180 ? 7.466 -5.570 14.714 1.00 54.96 ? 180 LYS A CD 1 ATOM 1309 C CE . LYS A 1 180 ? 7.410 -5.592 13.193 1.00 57.01 ? 180 LYS A CE 1 ATOM 1310 N NZ . LYS A 1 180 ? 8.768 -5.762 12.601 1.00 57.34 ? 180 LYS A NZ 1 ATOM 1311 N N . SER A 1 181 ? 6.320 -1.913 17.575 1.00 43.68 ? 181 SER A N 1 ATOM 1312 C CA . SER A 1 181 ? 5.235 -0.925 17.344 1.00 41.85 ? 181 SER A CA 1 ATOM 1313 C C . SER A 1 181 ? 5.693 0.521 17.447 1.00 38.49 ? 181 SER A C 1 ATOM 1314 O O . SER A 1 181 ? 5.417 1.332 16.558 1.00 36.87 ? 181 SER A O 1 ATOM 1315 C CB . SER A 1 181 ? 4.096 -1.118 18.356 1.00 42.60 ? 181 SER A CB 1 ATOM 1316 O OG . SER A 1 181 ? 3.314 -2.237 18.034 1.00 46.14 ? 181 SER A OG 1 ATOM 1317 N N . ASP A 1 182 ? 6.368 0.837 18.552 1.00 37.61 ? 182 ASP A N 1 ATOM 1318 C CA . ASP A 1 182 ? 6.862 2.193 18.803 1.00 34.94 ? 182 ASP A CA 1 ATOM 1319 C C . ASP A 1 182 ? 8.057 2.542 17.942 1.00 33.97 ? 182 ASP A C 1 ATOM 1320 O O . ASP A 1 182 ? 8.140 3.652 17.400 1.00 31.67 ? 182 ASP A O 1 ATOM 1321 C CB . ASP A 1 182 ? 7.251 2.377 20.273 1.00 35.23 ? 182 ASP A CB 1 ATOM 1322 C CG . ASP A 1 182 ? 6.057 2.435 21.193 1.00 35.60 ? 182 ASP A CG 1 ATOM 1323 O OD1 . ASP A 1 182 ? 4.908 2.593 20.714 1.00 35.85 ? 182 ASP A OD1 1 ATOM 1324 O OD2 . ASP A 1 182 ? 6.277 2.334 22.414 1.00 36.42 ? 182 ASP A OD2 1 ATOM 1325 N N . LEU A 1 183 ? 8.992 1.604 17.826 1.00 35.44 ? 183 LEU A N 1 ATOM 1326 C CA . LEU A 1 183 ? 10.192 1.834 17.026 1.00 35.17 ? 183 LEU A CA 1 ATOM 1327 C C . LEU A 1 183 ? 9.875 2.106 15.566 1.00 34.65 ? 183 LEU A C 1 ATOM 1328 O O . LEU A 1 183 ? 10.538 2.927 14.944 1.00 33.20 ? 183 LEU A O 1 ATOM 1329 C CB . LEU A 1 183 ? 11.153 0.649 17.120 1.00 38.08 ? 183 LEU A CB 1 ATOM 1330 C CG . LEU A 1 183 ? 11.783 0.445 18.497 1.00 38.76 ? 183 LEU A CG 1 ATOM 1331 C CD1 . LEU A 1 183 ? 12.388 -0.951 18.576 1.00 42.18 ? 183 LEU A CD1 1 ATOM 1332 C CD2 . LEU A 1 183 ? 12.825 1.512 18.785 1.00 37.26 ? 183 LEU A CD2 1 ATOM 1333 N N . GLU A 1 184 ? 8.871 1.415 15.029 1.00 35.85 ? 184 GLU A N 1 ATOM 1334 C CA . GLU A 1 184 ? 8.489 1.571 13.624 1.00 36.03 ? 184 GLU A CA 1 ATOM 1335 C C . GLU A 1 184 ? 7.277 2.499 13.402 1.00 33.94 ? 184 GLU A C 1 ATOM 1336 O O . GLU A 1 184 ? 6.698 2.511 12.316 1.00 34.05 ? 184 GLU A O 1 ATOM 1337 C CB . GLU A 1 184 ? 8.213 0.198 13.022 1.00 39.53 ? 184 GLU A CB 1 ATOM 1338 C CG . GLU A 1 184 ? 9.416 -0.731 13.053 1.00 42.34 ? 184 GLU A CG 1 ATOM 1339 C CD . GLU A 1 184 ? 9.106 -2.101 12.479 1.00 46.35 ? 184 GLU A CD 1 ATOM 1340 O OE1 . GLU A 1 184 ? 8.021 -2.273 11.880 1.00 47.32 ? 184 GLU A OE1 1 ATOM 1341 O OE2 . GLU A 1 184 ? 9.940 -3.021 12.632 1.00 49.48 ? 184 GLU A OE2 1 ATOM 1342 N N . LYS A 1 185 ? 6.910 3.295 14.406 1.00 32.07 ? 185 LYS A N 1 ATOM 1343 C CA . LYS A 1 185 ? 5.753 4.175 14.271 1.00 30.66 ? 185 LYS A CA 1 ATOM 1344 C C . LYS A 1 185 ? 6.003 5.194 13.170 1.00 29.20 ? 185 LYS A C 1 ATOM 1345 O O . LYS A 1 185 ? 7.150 5.545 12.880 1.00 28.48 ? 185 LYS A O 1 ATOM 1346 C CB . LYS A 1 185 ? 5.427 4.883 15.588 1.00 29.23 ? 185 LYS A CB 1 ATOM 1347 C CG . LYS A 1 185 ? 6.373 6.009 15.952 1.00 27.33 ? 185 LYS A CG 1 ATOM 1348 C CD . LYS A 1 185 ? 6.019 6.628 17.291 1.00 26.58 ? 185 LYS A CD 1 ATOM 1349 C CE . LYS A 1 185 ? 6.878 7.850 17.540 1.00 25.00 ? 185 LYS A CE 1 ATOM 1350 N NZ . LYS A 1 185 ? 6.515 8.557 18.795 1.00 24.64 ? 185 LYS A NZ 1 ATOM 1351 N N . GLN A 1 186 ? 4.924 5.658 12.554 1.00 28.98 ? 186 GLN A N 1 ATOM 1352 C CA . GLN A 1 186 ? 4.993 6.742 11.590 1.00 27.84 ? 186 GLN A CA 1 ATOM 1353 C C . GLN A 1 186 ? 4.060 7.835 12.075 1.00 26.74 ? 186 GLN A C 1 ATOM 1354 O O . GLN A 1 186 ? 2.885 7.563 12.328 1.00 27.38 ? 186 GLN A O 1 ATOM 1355 C CB . GLN A 1 186 ? 4.567 6.273 10.212 1.00 29.24 ? 186 GLN A CB 1 ATOM 1356 C CG . GLN A 1 186 ? 5.506 5.262 9.577 1.00 31.00 ? 186 GLN A CG 1 ATOM 1357 C CD . GLN A 1 186 ? 6.774 5.878 8.997 1.00 30.02 ? 186 GLN A CD 1 ATOM 1358 O OE1 . GLN A 1 186 ? 6.768 7.002 8.482 1.00 28.63 ? 186 GLN A OE1 1 ATOM 1359 N NE2 . GLN A 1 186 ? 7.865 5.125 9.054 1.00 31.19 ? 186 GLN A NE2 1 ATOM 1360 N N . GLU A 1 187 ? 4.587 9.046 12.243 1.00 25.02 ? 187 GLU A N 1 ATOM 1361 C CA . GLU A 1 187 ? 3.767 10.210 12.584 1.00 24.39 ? 187 GLU A CA 1 ATOM 1362 C C . GLU A 1 187 ? 3.979 11.269 11.495 1.00 23.19 ? 187 GLU A C 1 ATOM 1363 O O . GLU A 1 187 ? 5.111 11.522 11.077 1.00 22.21 ? 187 GLU A O 1 ATOM 1364 C CB . GLU A 1 187 ? 4.144 10.772 13.954 1.00 24.07 ? 187 GLU A CB 1 ATOM 1365 C CG . GLU A 1 187 ? 4.013 9.789 15.116 1.00 25.56 ? 187 GLU A CG 1 ATOM 1366 C CD . GLU A 1 187 ? 2.575 9.424 15.443 1.00 27.13 ? 187 GLU A CD 1 ATOM 1367 O OE1 . GLU A 1 187 ? 1.638 10.115 14.992 1.00 27.99 ? 187 GLU A OE1 1 ATOM 1368 O OE2 . GLU A 1 187 ? 2.378 8.431 16.159 1.00 29.01 ? 187 GLU A OE2 1 ATOM 1369 N N . LYS A 1 188 ? 2.894 11.889 11.047 1.00 23.22 ? 188 LYS A N 1 ATOM 1370 C CA . LYS A 1 188 ? 2.964 12.821 9.915 1.00 23.29 ? 188 LYS A CA 1 ATOM 1371 C C . LYS A 1 188 ? 3.430 14.205 10.294 1.00 21.82 ? 188 LYS A C 1 ATOM 1372 O O . LYS A 1 188 ? 2.975 14.753 11.293 1.00 21.97 ? 188 LYS A O 1 ATOM 1373 C CB . LYS A 1 188 ? 1.615 12.945 9.228 1.00 24.48 ? 188 LYS A CB 1 ATOM 1374 C CG . LYS A 1 188 ? 1.170 11.657 8.582 1.00 26.83 ? 188 LYS A CG 1 ATOM 1375 C CD . LYS A 1 188 ? -0.190 11.842 7.940 1.00 28.38 ? 188 LYS A CD 1 ATOM 1376 C CE . LYS A 1 188 ? -0.585 10.611 7.153 1.00 30.84 ? 188 LYS A CE 1 ATOM 1377 N NZ . LYS A 1 188 ? -1.848 10.863 6.423 1.00 32.55 ? 188 LYS A NZ 1 ATOM 1378 N N . PRO A 1 189 ? 4.308 14.806 9.465 1.00 21.19 ? 189 PRO A N 1 ATOM 1379 C CA . PRO A 1 189 ? 4.616 16.218 9.660 1.00 19.94 ? 189 PRO A CA 1 ATOM 1380 C C . PRO A 1 189 ? 3.395 17.095 9.374 1.00 19.77 ? 189 PRO A C 1 ATOM 1381 O O . PRO A 1 189 ? 2.572 16.748 8.521 1.00 20.24 ? 189 PRO A O 1 ATOM 1382 C CB . PRO A 1 189 ? 5.682 16.496 8.611 1.00 19.72 ? 189 PRO A CB 1 ATOM 1383 C CG . PRO A 1 189 ? 5.421 15.516 7.539 1.00 20.96 ? 189 PRO A CG 1 ATOM 1384 C CD . PRO A 1 189 ? 4.909 14.283 8.221 1.00 21.55 ? 189 PRO A CD 1 ATOM 1385 N N . VAL A 1 190 ? 3.272 18.173 10.139 1.00 19.24 ? 190 VAL A N 1 ATOM 1386 C CA . VAL A 1 190 ? 2.401 19.300 9.810 1.00 19.31 ? 190 VAL A CA 1 ATOM 1387 C C . VAL A 1 190 ? 3.331 20.485 9.589 1.00 18.42 ? 190 VAL A C 1 ATOM 1388 O O . VAL A 1 190 ? 4.245 20.724 10.392 1.00 17.52 ? 190 VAL A O 1 ATOM 1389 C CB . VAL A 1 190 ? 1.389 19.595 10.929 1.00 19.97 ? 190 VAL A CB 1 ATOM 1390 C CG1 . VAL A 1 190 ? 0.690 20.935 10.713 1.00 20.74 ? 190 VAL A CG1 1 ATOM 1391 C CG2 . VAL A 1 190 ? 0.356 18.470 11.024 1.00 21.13 ? 190 VAL A CG2 1 ATOM 1392 N N . ALA A 1 191 ? 3.098 21.214 8.497 1.00 18.56 ? 191 ALA A N 1 ATOM 1393 C CA . ALA A 1 191 ? 3.967 22.318 8.118 1.00 18.07 ? 191 ALA A CA 1 ATOM 1394 C C . ALA A 1 191 ? 3.232 23.632 8.090 1.00 18.41 ? 191 ALA A C 1 ATOM 1395 O O . ALA A 1 191 ? 2.006 23.666 7.910 1.00 18.84 ? 191 ALA A O 1 ATOM 1396 C CB . ALA A 1 191 ? 4.634 22.056 6.773 1.00 18.24 ? 191 ALA A CB 1 ATOM 1397 N N . TRP A 1 192 ? 3.987 24.715 8.297 1.00 17.98 ? 192 TRP A N 1 ATOM 1398 C CA . TRP A 1 192 ? 3.447 26.065 8.127 1.00 19.17 ? 192 TRP A CA 1 ATOM 1399 C C . TRP A 1 192 ? 4.532 27.065 7.778 1.00 19.35 ? 192 TRP A C 1 ATOM 1400 O O . TRP A 1 192 ? 5.701 26.843 8.096 1.00 18.93 ? 192 TRP A O 1 ATOM 1401 C CB . TRP A 1 192 ? 2.676 26.531 9.361 1.00 20.10 ? 192 TRP A CB 1 ATOM 1402 C CG . TRP A 1 192 ? 3.478 26.768 10.643 1.00 19.90 ? 192 TRP A CG 1 ATOM 1403 C CD1 . TRP A 1 192 ? 3.857 27.978 11.160 1.00 20.93 ? 192 TRP A CD1 1 ATOM 1404 C CD2 . TRP A 1 192 ? 3.926 25.777 11.583 1.00 19.26 ? 192 TRP A CD2 1 ATOM 1405 N NE1 . TRP A 1 192 ? 4.512 27.801 12.362 1.00 20.62 ? 192 TRP A NE1 1 ATOM 1406 C CE2 . TRP A 1 192 ? 4.585 26.463 12.637 1.00 19.72 ? 192 TRP A CE2 1 ATOM 1407 C CE3 . TRP A 1 192 ? 3.854 24.382 11.631 1.00 18.84 ? 192 TRP A CE3 1 ATOM 1408 C CZ2 . TRP A 1 192 ? 5.150 25.799 13.730 1.00 19.46 ? 192 TRP A CZ2 1 ATOM 1409 C CZ3 . TRP A 1 192 ? 4.425 23.706 12.736 1.00 18.55 ? 192 TRP A CZ3 1 ATOM 1410 C CH2 . TRP A 1 192 ? 5.054 24.424 13.765 1.00 18.84 ? 192 TRP A CH2 1 ATOM 1411 N N . LEU A 1 193 ? 4.113 28.151 7.133 1.00 20.41 ? 193 LEU A N 1 ATOM 1412 C CA . LEU A 1 193 ? 5.001 29.183 6.615 1.00 21.08 ? 193 LEU A CA 1 ATOM 1413 C C . LEU A 1 193 ? 4.850 30.456 7.415 1.00 22.74 ? 193 LEU A C 1 ATOM 1414 O O . LEU A 1 193 ? 3.735 30.856 7.792 1.00 23.46 ? 193 LEU A O 1 ATOM 1415 C CB . LEU A 1 193 ? 4.704 29.479 5.136 1.00 21.67 ? 193 LEU A CB 1 ATOM 1416 C CG . LEU A 1 193 ? 4.618 28.287 4.178 1.00 20.94 ? 193 LEU A CG 1 ATOM 1417 C CD1 . LEU A 1 193 ? 4.443 28.784 2.744 1.00 22.01 ? 193 LEU A CD1 1 ATOM 1418 C CD2 . LEU A 1 193 ? 5.855 27.409 4.299 1.00 19.83 ? 193 LEU A CD2 1 ATOM 1419 N N . SER A 1 194 ? 5.974 31.114 7.648 1.00 23.47 ? 194 SER A N 1 ATOM 1420 C CA . SER A 1 194 ? 5.978 32.436 8.246 1.00 25.95 ? 194 SER A CA 1 ATOM 1421 C C . SER A 1 194 ? 7.145 33.222 7.677 1.00 27.57 ? 194 SER A C 1 ATOM 1422 O O . SER A 1 194 ? 7.959 32.678 6.929 1.00 26.32 ? 194 SER A O 1 ATOM 1423 C CB . SER A 1 194 ? 6.087 32.341 9.762 1.00 25.91 ? 194 SER A CB 1 ATOM 1424 O OG . SER A 1 194 ? 7.360 31.846 10.151 1.00 24.72 ? 194 SER A OG 1 ATOM 1425 N N . SER A 1 195 ? 7.218 34.504 8.009 1.00 30.84 ? 195 SER A N 1 ATOM 1426 C CA . SER A 1 195 ? 8.394 35.281 7.633 1.00 33.07 ? 195 SER A CA 1 ATOM 1427 C C . SER A 1 195 ? 8.699 36.408 8.589 1.00 36.28 ? 195 SER A C 1 ATOM 1428 O O . SER A 1 195 ? 7.791 36.992 9.181 1.00 37.66 ? 195 SER A O 1 ATOM 1429 C CB . SER A 1 195 ? 8.284 35.811 6.199 1.00 34.08 ? 195 SER A CB 1 ATOM 1430 O OG . SER A 1 195 ? 7.395 36.911 6.098 1.00 36.58 ? 195 SER A OG 1 ATOM 1431 N N . VAL A 1 196 ? 9.998 36.677 8.736 1.00 38.26 ? 196 VAL A N 1 ATOM 1432 C CA . VAL A 1 196 ? 10.511 37.854 9.433 1.00 41.49 ? 196 VAL A CA 1 ATOM 1433 C C . VAL A 1 196 ? 10.743 38.950 8.408 1.00 44.41 ? 196 VAL A C 1 ATOM 1434 O O . VAL A 1 196 ? 11.446 38.736 7.412 1.00 44.79 ? 196 VAL A O 1 ATOM 1435 C CB . VAL A 1 196 ? 11.811 37.516 10.148 1.00 41.31 ? 196 VAL A CB 1 ATOM 1436 N N . ASP A 1 201 ? 17.093 46.422 4.322 1.00 66.16 ? 201 ASP A N 1 ATOM 1437 C CA . ASP A 1 201 ? 16.112 47.078 3.459 1.00 67.26 ? 201 ASP A CA 1 ATOM 1438 C C . ASP A 1 201 ? 15.649 46.140 2.335 1.00 64.28 ? 201 ASP A C 1 ATOM 1439 O O . ASP A 1 201 ? 16.423 45.827 1.429 1.00 64.20 ? 201 ASP A O 1 ATOM 1440 C CB . ASP A 1 201 ? 16.695 48.364 2.868 1.00 71.13 ? 201 ASP A CB 1 ATOM 1441 N N . GLY A 1 202 ? 14.402 45.671 2.417 1.00 62.06 ? 202 GLY A N 1 ATOM 1442 C CA . GLY A 1 202 ? 13.774 44.892 1.342 1.00 59.52 ? 202 GLY A CA 1 ATOM 1443 C C . GLY A 1 202 ? 13.816 43.380 1.507 1.00 55.25 ? 202 GLY A C 1 ATOM 1444 O O . GLY A 1 202 ? 12.848 42.694 1.150 1.00 53.85 ? 202 GLY A O 1 ATOM 1445 N N . HIS A 1 203 ? 14.916 42.852 2.051 1.00 53.69 ? 203 HIS A N 1 ATOM 1446 C CA . HIS A 1 203 ? 15.092 41.395 2.180 1.00 50.18 ? 203 HIS A CA 1 ATOM 1447 C C . HIS A 1 203 ? 14.228 40.779 3.279 1.00 47.83 ? 203 HIS A C 1 ATOM 1448 O O . HIS A 1 203 ? 13.992 41.377 4.331 1.00 49.05 ? 203 HIS A O 1 ATOM 1449 C CB . HIS A 1 203 ? 16.564 41.009 2.388 1.00 50.36 ? 203 HIS A CB 1 ATOM 1450 C CG . HIS A 1 203 ? 17.399 41.156 1.153 1.00 51.80 ? 203 HIS A CG 1 ATOM 1451 N ND1 . HIS A 1 203 ? 17.795 42.383 0.666 1.00 54.91 ? 203 HIS A ND1 1 ATOM 1452 C CD2 . HIS A 1 203 ? 17.900 40.232 0.298 1.00 50.53 ? 203 HIS A CD2 1 ATOM 1453 C CE1 . HIS A 1 203 ? 18.509 42.210 -0.433 1.00 55.34 ? 203 HIS A CE1 1 ATOM 1454 N NE2 . HIS A 1 203 ? 18.584 40.914 -0.680 1.00 52.88 ? 203 HIS A NE2 1 ATOM 1455 N N . ARG A 1 204 ? 13.782 39.562 3.002 1.00 44.37 ? 204 ARG A N 1 ATOM 1456 C CA . ARG A 1 204 ? 12.827 38.837 3.826 1.00 42.35 ? 204 ARG A CA 1 ATOM 1457 C C . ARG A 1 204 ? 13.389 37.461 4.099 1.00 38.19 ? 204 ARG A C 1 ATOM 1458 O O . ARG A 1 204 ? 13.967 36.867 3.200 1.00 36.35 ? 204 ARG A O 1 ATOM 1459 C CB . ARG A 1 204 ? 11.541 38.672 3.028 1.00 42.93 ? 204 ARG A CB 1 ATOM 1460 C CG . ARG A 1 204 ? 10.896 39.991 2.651 1.00 46.60 ? 204 ARG A CG 1 ATOM 1461 C CD . ARG A 1 204 ? 9.880 40.370 3.699 1.00 48.38 ? 204 ARG A CD 1 ATOM 1462 N NE . ARG A 1 204 ? 8.646 39.618 3.496 1.00 47.78 ? 204 ARG A NE 1 ATOM 1463 C CZ . ARG A 1 204 ? 7.743 39.354 4.437 1.00 48.40 ? 204 ARG A CZ 1 ATOM 1464 N NH1 . ARG A 1 204 ? 7.911 39.736 5.707 1.00 49.80 ? 204 ARG A NH1 1 ATOM 1465 N NH2 . ARG A 1 204 ? 6.653 38.679 4.103 1.00 47.67 ? 204 ARG A NH2 1 ATOM 1466 N N . GLN A 1 205 ? 13.219 36.958 5.319 1.00 36.13 ? 205 GLN A N 1 ATOM 1467 C CA . GLN A 1 205 ? 13.534 35.560 5.617 1.00 33.41 ? 205 GLN A CA 1 ATOM 1468 C C . GLN A 1 205 ? 12.234 34.765 5.745 1.00 30.59 ? 205 GLN A C 1 ATOM 1469 O O . GLN A 1 205 ? 11.482 34.954 6.700 1.00 30.42 ? 205 GLN A O 1 ATOM 1470 C CB . GLN A 1 205 ? 14.360 35.444 6.896 1.00 34.40 ? 205 GLN A CB 1 ATOM 1471 C CG . GLN A 1 205 ? 14.724 34.011 7.241 1.00 33.19 ? 205 GLN A CG 1 ATOM 1472 C CD . GLN A 1 205 ? 15.829 33.900 8.275 1.00 34.53 ? 205 GLN A CD 1 ATOM 1473 O OE1 . GLN A 1 205 ? 15.575 33.548 9.428 1.00 35.28 ? 205 GLN A OE1 1 ATOM 1474 N NE2 . GLN A 1 205 ? 17.056 34.204 7.873 1.00 35.92 ? 205 GLN A NE2 1 ATOM 1475 N N . LEU A 1 206 ? 11.990 33.878 4.785 1.00 28.09 ? 206 LEU A N 1 ATOM 1476 C CA . LEU A 1 206 ? 10.824 32.991 4.807 1.00 25.93 ? 206 LEU A CA 1 ATOM 1477 C C . LEU A 1 206 ? 11.175 31.764 5.641 1.00 23.85 ? 206 LEU A C 1 ATOM 1478 O O . LEU A 1 206 ? 12.297 31.276 5.541 1.00 23.16 ? 206 LEU A O 1 ATOM 1479 C CB . LEU A 1 206 ? 10.444 32.576 3.388 1.00 25.68 ? 206 LEU A CB 1 ATOM 1480 C CG . LEU A 1 206 ? 10.286 33.698 2.360 1.00 27.59 ? 206 LEU A CG 1 ATOM 1481 C CD1 . LEU A 1 206 ? 9.832 33.133 1.026 1.00 27.47 ? 206 LEU A CD1 1 ATOM 1482 C CD2 . LEU A 1 206 ? 9.336 34.767 2.857 1.00 28.88 ? 206 LEU A CD2 1 ATOM 1483 N N . VAL A 1 207 ? 10.228 31.270 6.439 1.00 22.55 ? 207 VAL A N 1 ATOM 1484 C CA . VAL A 1 207 ? 10.473 30.135 7.348 1.00 20.93 ? 207 VAL A CA 1 ATOM 1485 C C . VAL A 1 207 ? 9.426 29.066 7.090 1.00 20.00 ? 207 VAL A C 1 ATOM 1486 O O . VAL A 1 207 ? 8.235 29.327 7.173 1.00 20.19 ? 207 VAL A O 1 ATOM 1487 C CB . VAL A 1 207 ? 10.455 30.536 8.848 1.00 21.27 ? 207 VAL A CB 1 ATOM 1488 C CG1 . VAL A 1 207 ? 10.823 29.343 9.741 1.00 20.05 ? 207 VAL A CG1 1 ATOM 1489 C CG2 . VAL A 1 207 ? 11.386 31.708 9.116 1.00 22.88 ? 207 VAL A CG2 1 ATOM 1490 N N . CYS A 1 208 ? 9.895 27.880 6.730 1.00 19.12 ? 208 CYS A N 1 ATOM 1491 C CA . CYS A 1 208 ? 9.054 26.712 6.604 1.00 18.50 ? 208 CYS A CA 1 ATOM 1492 C C . CYS A 1 208 ? 9.286 25.847 7.834 1.00 17.87 ? 208 CYS A C 1 ATOM 1493 O O . CYS A 1 208 ? 10.390 25.327 8.037 1.00 17.55 ? 208 CYS A O 1 ATOM 1494 C CB . CYS A 1 208 ? 9.397 25.957 5.338 1.00 18.65 ? 208 CYS A CB 1 ATOM 1495 S SG . CYS A 1 208 ? 8.344 24.533 5.063 1.00 18.91 ? 208 CYS A SG 1 ATOM 1496 N N . HIS A 1 209 ? 8.234 25.725 8.635 1.00 17.66 ? 209 HIS A N 1 ATOM 1497 C CA . HIS A 1 209 ? 8.229 24.976 9.887 1.00 17.16 ? 209 HIS A CA 1 ATOM 1498 C C . HIS A 1 209 ? 7.598 23.618 9.625 1.00 16.78 ? 209 HIS A C 1 ATOM 1499 O O . HIS A 1 209 ? 6.575 23.545 8.950 1.00 16.43 ? 209 HIS A O 1 ATOM 1500 C CB . HIS A 1 209 ? 7.350 25.653 10.915 1.00 17.82 ? 209 HIS A CB 1 ATOM 1501 C CG . HIS A 1 209 ? 7.646 27.094 11.154 1.00 18.82 ? 209 HIS A CG 1 ATOM 1502 N ND1 . HIS A 1 209 ? 8.323 27.529 12.270 1.00 19.57 ? 209 HIS A ND1 1 ATOM 1503 C CD2 . HIS A 1 209 ? 7.269 28.210 10.485 1.00 19.77 ? 209 HIS A CD2 1 ATOM 1504 C CE1 . HIS A 1 209 ? 8.396 28.847 12.253 1.00 20.82 ? 209 HIS A CE1 1 ATOM 1505 N NE2 . HIS A 1 209 ? 7.764 29.285 11.180 1.00 21.01 ? 209 HIS A NE2 1 ATOM 1506 N N . VAL A 1 210 ? 8.190 22.564 10.184 1.00 16.33 ? 210 VAL A N 1 ATOM 1507 C CA . VAL A 1 210 ? 7.712 21.191 9.996 1.00 16.53 ? 210 VAL A CA 1 ATOM 1508 C C . VAL A 1 210 ? 7.747 20.502 11.357 1.00 16.31 ? 210 VAL A C 1 ATOM 1509 O O . VAL A 1 210 ? 8.817 20.372 11.924 1.00 16.35 ? 210 VAL A O 1 ATOM 1510 C CB . VAL A 1 210 ? 8.612 20.425 9.013 1.00 16.81 ? 210 VAL A CB 1 ATOM 1511 C CG1 . VAL A 1 210 ? 7.994 19.092 8.649 1.00 17.41 ? 210 VAL A CG1 1 ATOM 1512 C CG2 . VAL A 1 210 ? 8.905 21.267 7.770 1.00 17.32 ? 210 VAL A CG2 1 ATOM 1513 N N . SER A 1 211 ? 6.597 20.070 11.875 1.00 16.42 ? 211 SER A N 1 ATOM 1514 C CA . SER A 1 211 ? 6.531 19.567 13.245 1.00 16.35 ? 211 SER A CA 1 ATOM 1515 C C . SER A 1 211 ? 5.694 18.325 13.372 1.00 16.93 ? 211 SER A C 1 ATOM 1516 O O . SER A 1 211 ? 4.664 18.183 12.697 1.00 17.48 ? 211 SER A O 1 ATOM 1517 C CB . SER A 1 211 ? 5.980 20.628 14.189 1.00 16.83 ? 211 SER A CB 1 ATOM 1518 O OG . SER A 1 211 ? 6.219 20.275 15.540 1.00 16.75 ? 211 SER A OG 1 ATOM 1519 N N . GLY A 1 212 ? 6.125 17.443 14.274 1.00 16.86 ? 212 GLY A N 1 ATOM 1520 C CA . GLY A 1 212 ? 5.314 16.291 14.650 1.00 17.47 ? 212 GLY A CA 1 ATOM 1521 C C . GLY A 1 212 ? 5.625 15.034 13.875 1.00 17.88 ? 212 GLY A C 1 ATOM 1522 O O . GLY A 1 212 ? 4.883 14.062 13.981 1.00 18.73 ? 212 GLY A O 1 ATOM 1523 N N . PHE A 1 213 ? 6.743 15.018 13.148 1.00 17.58 ? 213 PHE A N 1 ATOM 1524 C CA . PHE A 1 213 ? 7.079 13.866 12.307 1.00 18.05 ? 213 PHE A CA 1 ATOM 1525 C C . PHE A 1 213 ? 7.927 12.858 13.079 1.00 18.51 ? 213 PHE A C 1 ATOM 1526 O O . PHE A 1 213 ? 8.655 13.192 14.017 1.00 17.86 ? 213 PHE A O 1 ATOM 1527 C CB . PHE A 1 213 ? 7.738 14.249 10.967 1.00 18.13 ? 213 PHE A CB 1 ATOM 1528 C CG . PHE A 1 213 ? 9.000 15.054 11.105 1.00 17.78 ? 213 PHE A CG 1 ATOM 1529 C CD1 . PHE A 1 213 ? 8.934 16.446 11.209 1.00 17.25 ? 213 PHE A CD1 1 ATOM 1530 C CD2 . PHE A 1 213 ? 10.239 14.436 11.119 1.00 18.46 ? 213 PHE A CD2 1 ATOM 1531 C CE1 . PHE A 1 213 ? 10.084 17.203 11.353 1.00 17.11 ? 213 PHE A CE1 1 ATOM 1532 C CE2 . PHE A 1 213 ? 11.398 15.193 11.243 1.00 18.36 ? 213 PHE A CE2 1 ATOM 1533 C CZ . PHE A 1 213 ? 11.316 16.574 11.373 1.00 17.69 ? 213 PHE A CZ 1 ATOM 1534 N N . TYR A 1 214 ? 7.750 11.602 12.701 1.00 19.57 ? 214 TYR A N 1 ATOM 1535 C CA . TYR A 1 214 ? 8.561 10.503 13.192 1.00 20.61 ? 214 TYR A CA 1 ATOM 1536 C C . TYR A 1 214 ? 8.477 9.378 12.156 1.00 22.36 ? 214 TYR A C 1 ATOM 1537 O O . TYR A 1 214 ? 7.384 9.126 11.666 1.00 22.57 ? 214 TYR A O 1 ATOM 1538 C CB . TYR A 1 214 ? 8.053 9.995 14.537 1.00 20.92 ? 214 TYR A CB 1 ATOM 1539 C CG . TYR A 1 214 ? 9.065 9.116 15.188 1.00 21.83 ? 214 TYR A CG 1 ATOM 1540 C CD1 . TYR A 1 214 ? 9.134 7.757 14.894 1.00 23.65 ? 214 TYR A CD1 1 ATOM 1541 C CD2 . TYR A 1 214 ? 10.006 9.650 16.058 1.00 21.50 ? 214 TYR A CD2 1 ATOM 1542 C CE1 . TYR A 1 214 ? 10.099 6.947 15.484 1.00 24.92 ? 214 TYR A CE1 1 ATOM 1543 C CE2 . TYR A 1 214 ? 10.969 8.860 16.653 1.00 22.60 ? 214 TYR A CE2 1 ATOM 1544 C CZ . TYR A 1 214 ? 11.023 7.508 16.359 1.00 24.46 ? 214 TYR A CZ 1 ATOM 1545 O OH . TYR A 1 214 ? 11.999 6.725 16.950 1.00 25.89 ? 214 TYR A OH 1 ATOM 1546 N N . PRO A 1 215 ? 9.577 8.692 11.817 1.00 24.10 ? 215 PRO A N 1 ATOM 1547 C CA . PRO A 1 215 ? 10.922 8.905 12.357 1.00 24.34 ? 215 PRO A CA 1 ATOM 1548 C C . PRO A 1 215 ? 11.621 10.145 11.811 1.00 24.05 ? 215 PRO A C 1 ATOM 1549 O O . PRO A 1 215 ? 11.062 10.907 11.007 1.00 22.78 ? 215 PRO A O 1 ATOM 1550 C CB . PRO A 1 215 ? 11.671 7.618 11.954 1.00 26.64 ? 215 PRO A CB 1 ATOM 1551 C CG . PRO A 1 215 ? 10.954 7.099 10.766 1.00 27.48 ? 215 PRO A CG 1 ATOM 1552 C CD . PRO A 1 215 ? 9.524 7.557 10.874 1.00 26.20 ? 215 PRO A CD 1 ATOM 1553 N N . LYS A 1 216 ? 12.847 10.327 12.276 1.00 25.04 ? 216 LYS A N 1 ATOM 1554 C CA . LYS A 1 216 ? 13.596 11.544 12.062 1.00 25.14 ? 216 LYS A CA 1 ATOM 1555 C C . LYS A 1 216 ? 13.878 11.914 10.595 1.00 25.30 ? 216 LYS A C 1 ATOM 1556 O O . LYS A 1 216 ? 13.789 13.101 10.249 1.00 24.14 ? 216 LYS A O 1 ATOM 1557 C CB . LYS A 1 216 ? 14.912 11.445 12.836 1.00 26.87 ? 216 LYS A CB 1 ATOM 1558 C CG . LYS A 1 216 ? 15.531 12.761 13.202 1.00 26.59 ? 216 LYS A CG 1 ATOM 1559 C CD . LYS A 1 216 ? 16.640 12.517 14.200 1.00 28.47 ? 216 LYS A CD 1 ATOM 1560 C CE . LYS A 1 216 ? 17.375 13.792 14.526 1.00 28.81 ? 216 LYS A CE 1 ATOM 1561 N NZ . LYS A 1 216 ? 18.580 13.466 15.329 1.00 30.69 ? 216 LYS A NZ 1 ATOM 1562 N N . PRO A 1 217 ? 14.217 10.928 9.737 1.00 26.72 ? 217 PRO A N 1 ATOM 1563 C CA . PRO A 1 217 ? 14.582 11.325 8.367 1.00 27.27 ? 217 PRO A CA 1 ATOM 1564 C C . PRO A 1 217 ? 13.462 12.082 7.635 1.00 26.12 ? 217 PRO A C 1 ATOM 1565 O O . PRO A 1 217 ? 12.323 11.628 7.614 1.00 25.68 ? 217 PRO A O 1 ATOM 1566 C CB . PRO A 1 217 ? 14.897 9.994 7.677 1.00 29.38 ? 217 PRO A CB 1 ATOM 1567 C CG . PRO A 1 217 ? 15.264 9.070 8.791 1.00 30.45 ? 217 PRO A CG 1 ATOM 1568 C CD . PRO A 1 217 ? 14.419 9.483 9.957 1.00 28.71 ? 217 PRO A CD 1 ATOM 1569 N N . VAL A 1 218 ? 13.800 13.236 7.067 1.00 25.69 ? 218 VAL A N 1 ATOM 1570 C CA . VAL A 1 218 ? 12.815 14.137 6.447 1.00 24.62 ? 218 VAL A CA 1 ATOM 1571 C C . VAL A 1 218 ? 13.532 14.975 5.393 1.00 25.02 ? 218 VAL A C 1 ATOM 1572 O O . VAL A 1 218 ? 14.756 15.144 5.455 1.00 26.19 ? 218 VAL A O 1 ATOM 1573 C CB . VAL A 1 218 ? 12.120 15.027 7.506 1.00 22.73 ? 218 VAL A CB 1 ATOM 1574 C CG1 . VAL A 1 218 ? 13.056 16.101 8.060 1.00 22.50 ? 218 VAL A CG1 1 ATOM 1575 C CG2 . VAL A 1 218 ? 10.851 15.662 6.959 1.00 22.06 ? 218 VAL A CG2 1 ATOM 1576 N N . TRP A 1 219 ? 12.780 15.454 4.415 1.00 24.39 ? 219 TRP A N 1 ATOM 1577 C CA . TRP A 1 219 ? 13.315 16.291 3.348 1.00 24.70 ? 219 TRP A CA 1 ATOM 1578 C C . TRP A 1 219 ? 12.438 17.527 3.278 1.00 23.13 ? 219 TRP A C 1 ATOM 1579 O O . TRP A 1 219 ? 11.207 17.417 3.232 1.00 21.92 ? 219 TRP A O 1 ATOM 1580 C CB . TRP A 1 219 ? 13.266 15.503 2.056 1.00 26.62 ? 219 TRP A CB 1 ATOM 1581 C CG . TRP A 1 219 ? 13.919 16.113 0.855 1.00 27.88 ? 219 TRP A CG 1 ATOM 1582 C CD1 . TRP A 1 219 ? 15.174 15.855 0.386 1.00 29.47 ? 219 TRP A CD1 1 ATOM 1583 C CD2 . TRP A 1 219 ? 13.318 17.026 -0.075 1.00 27.81 ? 219 TRP A CD2 1 ATOM 1584 N NE1 . TRP A 1 219 ? 15.403 16.568 -0.769 1.00 30.31 ? 219 TRP A NE1 1 ATOM 1585 C CE2 . TRP A 1 219 ? 14.279 17.300 -1.069 1.00 29.24 ? 219 TRP A CE2 1 ATOM 1586 C CE3 . TRP A 1 219 ? 12.064 17.655 -0.151 1.00 26.94 ? 219 TRP A CE3 1 ATOM 1587 C CZ2 . TRP A 1 219 ? 14.029 18.171 -2.136 1.00 29.59 ? 219 TRP A CZ2 1 ATOM 1588 C CZ3 . TRP A 1 219 ? 11.815 18.522 -1.207 1.00 27.57 ? 219 TRP A CZ3 1 ATOM 1589 C CH2 . TRP A 1 219 ? 12.794 18.758 -2.202 1.00 28.75 ? 219 TRP A CH2 1 ATOM 1590 N N . VAL A 1 220 ? 13.075 18.694 3.340 1.00 22.74 ? 220 VAL A N 1 ATOM 1591 C CA . VAL A 1 220 ? 12.390 19.981 3.331 1.00 21.89 ? 220 VAL A CA 1 ATOM 1592 C C . VAL A 1 220 ? 13.154 20.896 2.387 1.00 22.52 ? 220 VAL A C 1 ATOM 1593 O O . VAL A 1 220 ? 14.365 21.029 2.497 1.00 22.95 ? 220 VAL A O 1 ATOM 1594 C CB . VAL A 1 220 ? 12.326 20.626 4.737 1.00 21.13 ? 220 VAL A CB 1 ATOM 1595 C CG1 . VAL A 1 220 ? 11.529 21.920 4.703 1.00 20.86 ? 220 VAL A CG1 1 ATOM 1596 C CG2 . VAL A 1 220 ? 11.729 19.665 5.759 1.00 20.90 ? 220 VAL A CG2 1 ATOM 1597 N N . MET A 1 221 ? 12.462 21.497 1.433 1.00 22.63 ? 221 MET A N 1 ATOM 1598 C CA . MET A 1 221 ? 13.122 22.369 0.464 1.00 23.89 ? 221 MET A CA 1 ATOM 1599 C C . MET A 1 221 ? 12.189 23.471 0.005 1.00 22.64 ? 221 MET A C 1 ATOM 1600 O O . MET A 1 221 ? 11.017 23.218 -0.270 1.00 21.93 ? 221 MET A O 1 ATOM 1601 C CB . MET A 1 221 ? 13.574 21.550 -0.749 1.00 26.32 ? 221 MET A CB 1 ATOM 1602 C CG . MET A 1 221 ? 14.650 22.217 -1.575 1.00 28.93 ? 221 MET A CG 1 ATOM 1603 S SD . MET A 1 221 ? 16.212 22.310 -0.686 1.00 31.09 ? 221 MET A SD 1 ATOM 1604 C CE . MET A 1 221 ? 16.772 20.622 -0.848 1.00 31.98 ? 221 MET A CE 1 ATOM 1605 N N . TRP A 1 222 ? 12.713 24.692 -0.075 1.00 22.24 ? 222 TRP A N 1 ATOM 1606 C CA . TRP A 1 222 ? 12.039 25.750 -0.809 1.00 22.46 ? 222 TRP A CA 1 ATOM 1607 C C . TRP A 1 222 ? 12.208 25.494 -2.300 1.00 23.75 ? 222 TRP A C 1 ATOM 1608 O O . TRP A 1 222 ? 13.296 25.139 -2.757 1.00 23.70 ? 222 TRP A O 1 ATOM 1609 C CB . TRP A 1 222 ? 12.565 27.142 -0.440 1.00 22.88 ? 222 TRP A CB 1 ATOM 1610 C CG . TRP A 1 222 ? 12.089 27.569 0.928 1.00 22.00 ? 222 TRP A CG 1 ATOM 1611 C CD1 . TRP A 1 222 ? 12.717 27.376 2.125 1.00 21.55 ? 222 TRP A CD1 1 ATOM 1612 C CD2 . TRP A 1 222 ? 10.839 28.202 1.229 1.00 22.10 ? 222 TRP A CD2 1 ATOM 1613 N NE1 . TRP A 1 222 ? 11.951 27.884 3.151 1.00 21.03 ? 222 TRP A NE1 1 ATOM 1614 C CE2 . TRP A 1 222 ? 10.794 28.399 2.628 1.00 21.66 ? 222 TRP A CE2 1 ATOM 1615 C CE3 . TRP A 1 222 ? 9.761 28.635 0.449 1.00 22.94 ? 222 TRP A CE3 1 ATOM 1616 C CZ2 . TRP A 1 222 ? 9.701 29.014 3.269 1.00 21.87 ? 222 TRP A CZ2 1 ATOM 1617 C CZ3 . TRP A 1 222 ? 8.670 29.254 1.084 1.00 23.00 ? 222 TRP A CZ3 1 ATOM 1618 C CH2 . TRP A 1 222 ? 8.653 29.441 2.476 1.00 22.63 ? 222 TRP A CH2 1 ATOM 1619 N N . MET A 1 223 ? 11.124 25.714 -3.043 1.00 24.24 ? 223 MET A N 1 ATOM 1620 C CA . MET A 1 223 ? 11.031 25.373 -4.443 1.00 25.91 ? 223 MET A CA 1 ATOM 1621 C C . MET A 1 223 ? 10.476 26.553 -5.228 1.00 27.16 ? 223 MET A C 1 ATOM 1622 O O . MET A 1 223 ? 9.676 27.334 -4.713 1.00 26.63 ? 223 MET A O 1 ATOM 1623 C CB . MET A 1 223 ? 10.073 24.191 -4.616 1.00 26.18 ? 223 MET A CB 1 ATOM 1624 C CG . MET A 1 223 ? 10.389 22.954 -3.791 1.00 25.60 ? 223 MET A CG 1 ATOM 1625 S SD . MET A 1 223 ? 11.881 22.084 -4.269 1.00 27.23 ? 223 MET A SD 1 ATOM 1626 C CE . MET A 1 223 ? 11.347 21.468 -5.867 1.00 29.14 ? 223 MET A CE 1 ATOM 1627 N N . ARG A 1 224 ? 10.914 26.680 -6.466 1.00 29.10 ? 224 ARG A N 1 ATOM 1628 C CA . ARG A 1 224 ? 10.249 27.527 -7.449 1.00 31.21 ? 224 ARG A CA 1 ATOM 1629 C C . ARG A 1 224 ? 9.886 26.561 -8.571 1.00 32.33 ? 224 ARG A C 1 ATOM 1630 O O . ARG A 1 224 ? 10.732 26.178 -9.378 1.00 33.22 ? 224 ARG A O 1 ATOM 1631 C CB . ARG A 1 224 ? 11.158 28.668 -7.894 1.00 32.82 ? 224 ARG A CB 1 ATOM 1632 C CG . ARG A 1 224 ? 10.442 29.745 -8.695 1.00 35.16 ? 224 ARG A CG 1 ATOM 1633 C CD . ARG A 1 224 ? 11.379 30.889 -9.063 1.00 36.79 ? 224 ARG A CD 1 ATOM 1634 N NE . ARG A 1 224 ? 11.908 31.601 -7.893 1.00 36.51 ? 224 ARG A NE 1 ATOM 1635 C CZ . ARG A 1 224 ? 11.251 32.518 -7.173 1.00 36.59 ? 224 ARG A CZ 1 ATOM 1636 N NH1 . ARG A 1 224 ? 9.989 32.841 -7.453 1.00 37.25 ? 224 ARG A NH1 1 ATOM 1637 N NH2 . ARG A 1 224 ? 11.864 33.093 -6.131 1.00 36.37 ? 224 ARG A NH2 1 ATOM 1638 N N . GLY A 1 225 ? 8.633 26.108 -8.561 1.00 32.61 ? 225 GLY A N 1 ATOM 1639 C CA . GLY A 1 225 ? 8.209 25.002 -9.413 1.00 33.94 ? 225 GLY A CA 1 ATOM 1640 C C . GLY A 1 225 ? 8.947 23.733 -9.005 1.00 33.46 ? 225 GLY A C 1 ATOM 1641 O O . GLY A 1 225 ? 8.964 23.371 -7.824 1.00 32.44 ? 225 GLY A O 1 ATOM 1642 N N . ASP A 1 226 ? 9.588 23.084 -9.973 1.00 35.00 ? 226 ASP A N 1 ATOM 1643 C CA . ASP A 1 226 ? 10.404 21.893 -9.710 1.00 34.99 ? 226 ASP A CA 1 ATOM 1644 C C . ASP A 1 226 ? 11.896 22.221 -9.474 1.00 34.11 ? 226 ASP A C 1 ATOM 1645 O O . ASP A 1 226 ? 12.713 21.314 -9.432 1.00 34.32 ? 226 ASP A O 1 ATOM 1646 C CB . ASP A 1 226 ? 10.226 20.839 -10.832 1.00 37.88 ? 226 ASP A CB 1 ATOM 1647 C CG . ASP A 1 226 ? 10.709 21.318 -12.204 1.00 40.39 ? 226 ASP A CG 1 ATOM 1648 O OD1 . ASP A 1 226 ? 11.305 22.413 -12.306 1.00 40.65 ? 226 ASP A OD1 1 ATOM 1649 O OD2 . ASP A 1 226 ? 10.469 20.603 -13.211 1.00 43.39 ? 226 ASP A OD2 1 ATOM 1650 N N . GLN A 1 227 ? 12.235 23.503 -9.313 1.00 33.21 ? 227 GLN A N 1 ATOM 1651 C CA . GLN A 1 227 ? 13.612 23.925 -9.036 1.00 33.12 ? 227 GLN A CA 1 ATOM 1652 C C . GLN A 1 227 ? 13.839 24.138 -7.551 1.00 30.73 ? 227 GLN A C 1 ATOM 1653 O O . GLN A 1 227 ? 13.195 24.980 -6.922 1.00 29.27 ? 227 GLN A O 1 ATOM 1654 C CB . GLN A 1 227 ? 13.948 25.213 -9.795 1.00 34.48 ? 227 GLN A CB 1 ATOM 1655 C CG . GLN A 1 227 ? 13.808 25.088 -11.303 1.00 36.98 ? 227 GLN A CG 1 ATOM 1656 C CD . GLN A 1 227 ? 14.667 23.967 -11.873 1.00 38.75 ? 227 GLN A CD 1 ATOM 1657 O OE1 . GLN A 1 227 ? 15.893 24.031 -11.824 1.00 39.71 ? 227 GLN A OE1 1 ATOM 1658 N NE2 . GLN A 1 227 ? 14.026 22.926 -12.398 1.00 39.74 ? 227 GLN A NE2 1 ATOM 1659 N N . GLU A 1 228 ? 14.783 23.383 -7.005 1.00 30.24 ? 228 GLU A N 1 ATOM 1660 C CA . GLU A 1 228 ? 15.170 23.511 -5.609 1.00 28.71 ? 228 GLU A CA 1 ATOM 1661 C C . GLU A 1 228 ? 15.888 24.836 -5.411 1.00 27.99 ? 228 GLU A C 1 ATOM 1662 O O . GLU A 1 228 ? 16.756 25.195 -6.208 1.00 29.57 ? 228 GLU A O 1 ATOM 1663 C CB . GLU A 1 228 ? 16.058 22.338 -5.185 1.00 29.70 ? 228 GLU A CB 1 ATOM 1664 C CG . GLU A 1 228 ? 15.353 20.991 -5.306 1.00 30.55 ? 228 GLU A CG 1 ATOM 1665 C CD . GLU A 1 228 ? 16.195 19.805 -4.864 1.00 32.06 ? 228 GLU A CD 1 ATOM 1666 O OE1 . GLU A 1 228 ? 15.799 18.674 -5.200 1.00 33.96 ? 228 GLU A OE1 1 ATOM 1667 O OE2 . GLU A 1 228 ? 17.226 19.986 -4.187 1.00 32.71 ? 228 GLU A OE2 1 ATOM 1668 N N . GLN A 1 229 ? 15.501 25.576 -4.376 1.00 25.79 ? 229 GLN A N 1 ATOM 1669 C CA . GLN A 1 229 ? 16.158 26.843 -4.048 1.00 25.59 ? 229 GLN A CA 1 ATOM 1670 C C . GLN A 1 229 ? 17.358 26.558 -3.138 1.00 25.00 ? 229 GLN A C 1 ATOM 1671 O O . GLN A 1 229 ? 17.191 26.170 -1.976 1.00 23.46 ? 229 GLN A O 1 ATOM 1672 C CB . GLN A 1 229 ? 15.175 27.812 -3.405 1.00 24.91 ? 229 GLN A CB 1 ATOM 1673 C CG . GLN A 1 229 ? 13.990 28.147 -4.313 1.00 25.27 ? 229 GLN A CG 1 ATOM 1674 C CD . GLN A 1 229 ? 14.406 28.662 -5.691 1.00 27.18 ? 229 GLN A CD 1 ATOM 1675 O OE1 . GLN A 1 229 ? 14.374 27.926 -6.693 1.00 28.17 ? 229 GLN A OE1 1 ATOM 1676 N NE2 . GLN A 1 229 ? 14.814 29.915 -5.747 1.00 27.99 ? 229 GLN A NE2 1 ATOM 1677 N N . GLN A 1 230 ? 18.566 26.742 -3.674 1.00 25.92 ? 230 GLN A N 1 ATOM 1678 C CA . GLN A 1 230 ? 19.791 26.353 -2.950 1.00 26.14 ? 230 GLN A CA 1 ATOM 1679 C C . GLN A 1 230 ? 20.141 27.256 -1.754 1.00 25.76 ? 230 GLN A C 1 ATOM 1680 O O . GLN A 1 230 ? 20.985 26.900 -0.929 1.00 25.74 ? 230 GLN A O 1 ATOM 1681 C CB . GLN A 1 230 ? 20.970 26.208 -3.912 1.00 28.18 ? 230 GLN A CB 1 ATOM 1682 C CG . GLN A 1 230 ? 20.745 25.099 -4.925 1.00 28.66 ? 230 GLN A CG 1 ATOM 1683 C CD . GLN A 1 230 ? 21.896 24.897 -5.877 1.00 30.98 ? 230 GLN A CD 1 ATOM 1684 O OE1 . GLN A 1 230 ? 22.507 25.860 -6.367 1.00 32.10 ? 230 GLN A OE1 1 ATOM 1685 N NE2 . GLN A 1 230 ? 22.211 23.630 -6.156 1.00 31.82 ? 230 GLN A NE2 1 ATOM 1686 N N . GLY A 1 231 ? 19.453 28.391 -1.631 1.00 25.41 ? 231 GLY A N 1 ATOM 1687 C CA . GLY A 1 231 ? 19.472 29.177 -0.399 1.00 25.19 ? 231 GLY A CA 1 ATOM 1688 C C . GLY A 1 231 ? 18.758 28.551 0.793 1.00 23.67 ? 231 GLY A C 1 ATOM 1689 O O . GLY A 1 231 ? 18.904 29.044 1.920 1.00 23.61 ? 231 GLY A O 1 ATOM 1690 N N . THR A 1 232 ? 17.984 27.482 0.570 1.00 22.67 ? 232 THR A N 1 ATOM 1691 C CA . THR A 1 232 ? 17.291 26.784 1.652 1.00 21.58 ? 232 THR A CA 1 ATOM 1692 C C . THR A 1 232 ? 18.303 26.452 2.731 1.00 22.10 ? 232 THR A C 1 ATOM 1693 O O . THR A 1 232 ? 19.299 25.797 2.450 1.00 23.06 ? 232 THR A O 1 ATOM 1694 C CB . THR A 1 232 ? 16.623 25.475 1.197 1.00 20.79 ? 232 THR A CB 1 ATOM 1695 O OG1 . THR A 1 232 ? 15.627 25.749 0.207 1.00 20.77 ? 232 THR A OG1 1 ATOM 1696 C CG2 . THR A 1 232 ? 15.965 24.756 2.390 1.00 19.47 ? 232 THR A CG2 1 ATOM 1697 N N . HIS A 1 233 ? 18.061 26.952 3.938 1.00 22.28 ? 233 HIS A N 1 ATOM 1698 C CA . HIS A 1 233 ? 18.955 26.754 5.071 1.00 23.37 ? 233 HIS A CA 1 ATOM 1699 C C . HIS A 1 233 ? 18.205 25.957 6.126 1.00 22.46 ? 233 HIS A C 1 ATOM 1700 O O . HIS A 1 233 ? 17.372 26.500 6.849 1.00 21.51 ? 233 HIS A O 1 ATOM 1701 C CB . HIS A 1 233 ? 19.439 28.094 5.633 1.00 24.96 ? 233 HIS A CB 1 ATOM 1702 C CG . HIS A 1 233 ? 20.511 27.966 6.668 1.00 26.39 ? 233 HIS A CG 1 ATOM 1703 N ND1 . HIS A 1 233 ? 20.950 29.034 7.418 1.00 28.16 ? 233 HIS A ND1 1 ATOM 1704 C CD2 . HIS A 1 233 ? 21.243 26.898 7.069 1.00 27.01 ? 233 HIS A CD2 1 ATOM 1705 C CE1 . HIS A 1 233 ? 21.904 28.629 8.241 1.00 29.22 ? 233 HIS A CE1 1 ATOM 1706 N NE2 . HIS A 1 233 ? 22.093 27.334 8.056 1.00 28.48 ? 233 HIS A NE2 1 ATOM 1707 N N A ARG A 1 234 ? 18.516 24.665 6.202 0.50 22.53 ? 234 ARG A N 1 ATOM 1708 N N B ARG A 1 234 ? 18.491 24.664 6.202 0.50 22.46 ? 234 ARG A N 1 ATOM 1709 C CA A ARG A 1 234 ? 17.901 23.764 7.167 0.50 21.98 ? 234 ARG A CA 1 ATOM 1710 C CA B ARG A 1 234 ? 17.821 23.798 7.160 0.50 21.79 ? 234 ARG A CA 1 ATOM 1711 C C A ARG A 1 234 ? 18.493 23.985 8.557 0.50 22.35 ? 234 ARG A C 1 ATOM 1712 C C B ARG A 1 234 ? 18.471 23.916 8.544 0.50 22.25 ? 234 ARG A C 1 ATOM 1713 O O A ARG A 1 234 ? 19.713 24.093 8.703 0.50 23.27 ? 234 ARG A O 1 ATOM 1714 O O B ARG A 1 234 ? 19.697 23.917 8.667 0.50 23.14 ? 234 ARG A O 1 ATOM 1715 C CB A ARG A 1 234 ? 18.151 22.317 6.746 0.50 22.68 ? 234 ARG A CB 1 ATOM 1716 C CB B ARG A 1 234 ? 17.798 22.361 6.630 0.50 22.15 ? 234 ARG A CB 1 ATOM 1717 C CG A ARG A 1 234 ? 17.103 21.346 7.243 0.50 22.19 ? 234 ARG A CG 1 ATOM 1718 C CG B ARG A 1 234 ? 16.577 22.132 5.746 0.50 21.78 ? 234 ARG A CG 1 ATOM 1719 C CD A ARG A 1 234 ? 17.698 19.975 7.449 0.50 23.35 ? 234 ARG A CD 1 ATOM 1720 C CD B ARG A 1 234 ? 16.744 21.071 4.670 0.50 22.83 ? 234 ARG A CD 1 ATOM 1721 N NE A ARG A 1 234 ? 18.597 19.964 8.596 0.50 24.53 ? 234 ARG A NE 1 ATOM 1722 N NE B ARG A 1 234 ? 17.320 21.588 3.428 0.50 24.21 ? 234 ARG A NE 1 ATOM 1723 C CZ A ARG A 1 234 ? 19.423 18.971 8.882 0.50 26.02 ? 234 ARG A CZ 1 ATOM 1724 C CZ B ARG A 1 234 ? 18.596 21.417 3.081 0.50 25.94 ? 234 ARG A CZ 1 ATOM 1725 N NH1 A ARG A 1 234 ? 19.486 17.916 8.085 0.50 26.92 ? 234 ARG A NH1 1 ATOM 1726 N NH1 B ARG A 1 234 ? 19.396 20.725 3.864 0.50 27.02 ? 234 ARG A NH1 1 ATOM 1727 N NH2 A ARG A 1 234 ? 20.198 19.045 9.950 0.50 27.01 ? 234 ARG A NH2 1 ATOM 1728 N NH2 B ARG A 1 234 ? 19.071 21.916 1.950 0.50 27.21 ? 234 ARG A NH2 1 ATOM 1729 N N . GLY A 1 235 ? 17.633 24.048 9.570 1.00 21.53 ? 235 GLY A N 1 ATOM 1730 C CA . GLY A 1 235 ? 18.081 24.161 10.956 1.00 22.31 ? 235 GLY A CA 1 ATOM 1731 C C . GLY A 1 235 ? 18.391 22.776 11.505 1.00 22.74 ? 235 GLY A C 1 ATOM 1732 O O . GLY A 1 235 ? 18.457 21.796 10.760 1.00 23.43 ? 235 GLY A O 1 ATOM 1733 N N . ASP A 1 236 ? 18.579 22.691 12.813 1.00 23.17 ? 236 ASP A N 1 ATOM 1734 C CA . ASP A 1 236 ? 18.841 21.406 13.464 1.00 23.24 ? 236 ASP A CA 1 ATOM 1735 C C . ASP A 1 236 ? 17.534 20.690 13.754 1.00 21.59 ? 236 ASP A C 1 ATOM 1736 O O . ASP A 1 236 ? 16.472 21.312 13.807 1.00 20.09 ? 236 ASP A O 1 ATOM 1737 C CB . ASP A 1 236 ? 19.614 21.602 14.765 1.00 24.58 ? 236 ASP A CB 1 ATOM 1738 C CG . ASP A 1 236 ? 21.002 22.174 14.552 1.00 26.66 ? 236 ASP A CG 1 ATOM 1739 O OD1 . ASP A 1 236 ? 21.576 22.045 13.447 1.00 27.36 ? 236 ASP A OD1 1 ATOM 1740 O OD2 . ASP A 1 236 ? 21.522 22.762 15.509 1.00 27.89 ? 236 ASP A OD2 1 ATOM 1741 N N . PHE A 1 237 ? 17.608 19.375 13.955 1.00 21.72 ? 237 PHE A N 1 ATOM 1742 C CA . PHE A 1 237 ? 16.432 18.629 14.436 1.00 20.77 ? 237 PHE A CA 1 ATOM 1743 C C . PHE A 1 237 ? 16.209 18.933 15.909 1.00 20.03 ? 237 PHE A C 1 ATOM 1744 O O . PHE A 1 237 ? 17.112 18.748 16.724 1.00 20.51 ? 237 PHE A O 1 ATOM 1745 C CB . PHE A 1 237 ? 16.605 17.120 14.229 1.00 22.01 ? 237 PHE A CB 1 ATOM 1746 C CG . PHE A 1 237 ? 16.478 16.702 12.802 1.00 22.73 ? 237 PHE A CG 1 ATOM 1747 C CD1 . PHE A 1 237 ? 17.587 16.720 11.959 1.00 24.47 ? 237 PHE A CD1 1 ATOM 1748 C CD2 . PHE A 1 237 ? 15.248 16.314 12.282 1.00 22.45 ? 237 PHE A CD2 1 ATOM 1749 C CE1 . PHE A 1 237 ? 17.467 16.346 10.626 1.00 25.06 ? 237 PHE A CE1 1 ATOM 1750 C CE2 . PHE A 1 237 ? 15.127 15.927 10.950 1.00 22.72 ? 237 PHE A CE2 1 ATOM 1751 C CZ . PHE A 1 237 ? 16.233 15.945 10.126 1.00 24.09 ? 237 PHE A CZ 1 ATOM 1752 N N . LEU A 1 238 ? 15.007 19.414 16.228 1.00 18.40 ? 238 LEU A N 1 ATOM 1753 C CA . LEU A 1 238 ? 14.622 19.820 17.580 1.00 18.28 ? 238 LEU A CA 1 ATOM 1754 C C . LEU A 1 238 ? 13.531 18.872 18.076 1.00 17.54 ? 238 LEU A C 1 ATOM 1755 O O . LEU A 1 238 ? 12.566 18.623 17.345 1.00 16.64 ? 238 LEU A O 1 ATOM 1756 C CB . LEU A 1 238 ? 14.098 21.260 17.559 1.00 18.05 ? 238 LEU A CB 1 ATOM 1757 C CG . LEU A 1 238 ? 14.981 22.299 16.835 1.00 18.63 ? 238 LEU A CG 1 ATOM 1758 C CD1 . LEU A 1 238 ? 14.458 23.717 17.042 1.00 19.08 ? 238 LEU A CD1 1 ATOM 1759 C CD2 . LEU A 1 238 ? 16.417 22.242 17.321 1.00 20.07 ? 238 LEU A CD2 1 ATOM 1760 N N . PRO A 1 239 ? 13.647 18.381 19.321 1.00 17.97 ? 239 PRO A N 1 ATOM 1761 C CA . PRO A 1 239 ? 12.631 17.463 19.810 1.00 17.91 ? 239 PRO A CA 1 ATOM 1762 C C . PRO A 1 239 ? 11.349 18.150 20.267 1.00 17.66 ? 239 PRO A C 1 ATOM 1763 O O . PRO A 1 239 ? 11.400 19.199 20.911 1.00 18.09 ? 239 PRO A O 1 ATOM 1764 C CB . PRO A 1 239 ? 13.321 16.797 21.007 1.00 18.99 ? 239 PRO A CB 1 ATOM 1765 C CG . PRO A 1 239 ? 14.198 17.865 21.553 1.00 19.73 ? 239 PRO A CG 1 ATOM 1766 C CD . PRO A 1 239 ? 14.662 18.671 20.356 1.00 19.32 ? 239 PRO A CD 1 ATOM 1767 N N . ASN A 1 240 ? 10.214 17.550 19.919 1.00 17.23 ? 240 ASN A N 1 ATOM 1768 C CA . ASN A 1 240 ? 8.978 17.806 20.618 1.00 17.74 ? 240 ASN A CA 1 ATOM 1769 C C . ASN A 1 240 ? 8.910 16.906 21.845 1.00 18.81 ? 240 ASN A C 1 ATOM 1770 O O . ASN A 1 240 ? 9.662 15.928 21.967 1.00 19.79 ? 240 ASN A O 1 ATOM 1771 C CB . ASN A 1 240 ? 7.770 17.593 19.704 1.00 17.12 ? 240 ASN A CB 1 ATOM 1772 C CG . ASN A 1 240 ? 7.676 18.653 18.621 1.00 16.58 ? 240 ASN A CG 1 ATOM 1773 O OD1 . ASN A 1 240 ? 7.876 19.839 18.892 1.00 16.86 ? 240 ASN A OD1 1 ATOM 1774 N ND2 . ASN A 1 240 ? 7.371 18.240 17.400 1.00 15.75 ? 240 ASN A ND2 1 ATOM 1775 N N . ALA A 1 241 ? 8.005 17.233 22.746 1.00 19.29 ? 241 ALA A N 1 ATOM 1776 C CA . ALA A 1 241 ? 7.873 16.516 24.004 1.00 20.52 ? 241 ALA A CA 1 ATOM 1777 C C . ALA A 1 241 ? 7.075 15.203 23.876 1.00 20.67 ? 241 ALA A C 1 ATOM 1778 O O . ALA A 1 241 ? 6.948 14.468 24.837 1.00 21.55 ? 241 ALA A O 1 ATOM 1779 C CB . ALA A 1 241 ? 7.260 17.437 25.058 1.00 21.38 ? 241 ALA A CB 1 ATOM 1780 N N . ASP A 1 242 ? 6.570 14.909 22.680 1.00 20.01 ? 242 ASP A N 1 ATOM 1781 C CA . ASP A 1 242 ? 5.724 13.746 22.450 1.00 20.56 ? 242 ASP A CA 1 ATOM 1782 C C . ASP A 1 242 ? 6.383 12.734 21.515 1.00 20.24 ? 242 ASP A C 1 ATOM 1783 O O . ASP A 1 242 ? 5.713 12.047 20.758 1.00 20.35 ? 242 ASP A O 1 ATOM 1784 C CB . ASP A 1 242 ? 4.353 14.204 21.925 1.00 20.74 ? 242 ASP A CB 1 ATOM 1785 C CG . ASP A 1 242 ? 4.419 14.855 20.543 1.00 20.06 ? 242 ASP A CG 1 ATOM 1786 O OD1 . ASP A 1 242 ? 5.513 15.242 20.086 1.00 19.26 ? 242 ASP A OD1 1 ATOM 1787 O OD2 . ASP A 1 242 ? 3.346 14.992 19.917 1.00 20.97 ? 242 ASP A OD2 1 ATOM 1788 N N . GLU A 1 243 ? 7.703 12.646 21.589 1.00 20.33 ? 243 GLU A N 1 ATOM 1789 C CA . GLU A 1 243 ? 8.492 11.727 20.772 1.00 20.85 ? 243 GLU A CA 1 ATOM 1790 C C . GLU A 1 243 ? 8.195 11.904 19.279 1.00 20.28 ? 243 GLU A C 1 ATOM 1791 O O . GLU A 1 243 ? 7.981 10.937 18.528 1.00 21.31 ? 243 GLU A O 1 ATOM 1792 C CB . GLU A 1 243 ? 8.328 10.279 21.302 1.00 22.36 ? 243 GLU A CB 1 ATOM 1793 C CG . GLU A 1 243 ? 8.817 10.166 22.734 1.00 23.23 ? 243 GLU A CG 1 ATOM 1794 C CD . GLU A 1 243 ? 8.682 8.780 23.341 1.00 24.96 ? 243 GLU A CD 1 ATOM 1795 O OE1 . GLU A 1 243 ? 9.606 8.369 24.059 1.00 25.88 ? 243 GLU A OE1 1 ATOM 1796 O OE2 . GLU A 1 243 ? 7.660 8.101 23.109 1.00 25.60 ? 243 GLU A OE2 1 ATOM 1797 N N . THR A 1 244 ? 8.135 13.176 18.875 1.00 18.99 ? 244 THR A N 1 ATOM 1798 C CA . THR A 1 244 ? 8.147 13.576 17.472 1.00 18.21 ? 244 THR A CA 1 ATOM 1799 C C . THR A 1 244 ? 9.201 14.675 17.315 1.00 17.75 ? 244 THR A C 1 ATOM 1800 O O . THR A 1 244 ? 9.771 15.163 18.316 1.00 18.30 ? 244 THR A O 1 ATOM 1801 C CB . THR A 1 244 ? 6.790 14.097 16.977 1.00 17.70 ? 244 THR A CB 1 ATOM 1802 O OG1 . THR A 1 244 ? 6.452 15.319 17.659 1.00 17.04 ? 244 THR A OG1 1 ATOM 1803 C CG2 . THR A 1 244 ? 5.700 13.069 17.175 1.00 18.62 ? 244 THR A CG2 1 ATOM 1804 N N . TRP A 1 245 ? 9.464 15.030 16.062 1.00 17.06 ? 245 TRP A N 1 ATOM 1805 C CA . TRP A 1 245 ? 10.541 15.945 15.711 1.00 16.90 ? 245 TRP A CA 1 ATOM 1806 C C . TRP A 1 245 ? 9.985 17.233 15.113 1.00 16.16 ? 245 TRP A C 1 ATOM 1807 O O . TRP A 1 245 ? 8.865 17.272 14.593 1.00 15.46 ? 245 TRP A O 1 ATOM 1808 C CB . TRP A 1 245 ? 11.508 15.277 14.739 1.00 17.43 ? 245 TRP A CB 1 ATOM 1809 C CG . TRP A 1 245 ? 12.351 14.251 15.407 1.00 18.88 ? 245 TRP A CG 1 ATOM 1810 C CD1 . TRP A 1 245 ? 12.202 12.890 15.342 1.00 19.71 ? 245 TRP A CD1 1 ATOM 1811 C CD2 . TRP A 1 245 ? 13.471 14.497 16.261 1.00 19.57 ? 245 TRP A CD2 1 ATOM 1812 N NE1 . TRP A 1 245 ? 13.173 12.277 16.097 1.00 21.13 ? 245 TRP A NE1 1 ATOM 1813 C CE2 . TRP A 1 245 ? 13.968 13.236 16.673 1.00 20.90 ? 245 TRP A CE2 1 ATOM 1814 C CE3 . TRP A 1 245 ? 14.109 15.663 16.718 1.00 19.74 ? 245 TRP A CE3 1 ATOM 1815 C CZ2 . TRP A 1 245 ? 15.063 13.106 17.534 1.00 22.22 ? 245 TRP A CZ2 1 ATOM 1816 C CZ3 . TRP A 1 245 ? 15.216 15.543 17.557 1.00 20.94 ? 245 TRP A CZ3 1 ATOM 1817 C CH2 . TRP A 1 245 ? 15.687 14.261 17.958 1.00 22.54 ? 245 TRP A CH2 1 ATOM 1818 N N . TYR A 1 246 ? 10.803 18.268 15.223 1.00 16.37 ? 246 TYR A N 1 ATOM 1819 C CA . TYR A 1 246 ? 10.556 19.602 14.673 1.00 16.47 ? 246 TYR A CA 1 ATOM 1820 C C . TYR A 1 246 ? 11.804 19.988 13.884 1.00 16.94 ? 246 TYR A C 1 ATOM 1821 O O . TYR A 1 246 ? 12.923 19.715 14.315 1.00 17.18 ? 246 TYR A O 1 ATOM 1822 C CB . TYR A 1 246 ? 10.325 20.617 15.805 1.00 16.98 ? 246 TYR A CB 1 ATOM 1823 C CG . TYR A 1 246 ? 10.150 22.060 15.355 1.00 17.40 ? 246 TYR A CG 1 ATOM 1824 C CD1 . TYR A 1 246 ? 11.248 22.848 15.027 1.00 18.02 ? 246 TYR A CD1 1 ATOM 1825 C CD2 . TYR A 1 246 ? 8.883 22.645 15.279 1.00 17.76 ? 246 TYR A CD2 1 ATOM 1826 C CE1 . TYR A 1 246 ? 11.094 24.176 14.633 1.00 18.85 ? 246 TYR A CE1 1 ATOM 1827 C CE2 . TYR A 1 246 ? 8.721 23.967 14.879 1.00 18.40 ? 246 TYR A CE2 1 ATOM 1828 C CZ . TYR A 1 246 ? 9.826 24.723 14.542 1.00 19.13 ? 246 TYR A CZ 1 ATOM 1829 O OH . TYR A 1 246 ? 9.672 26.037 14.150 1.00 20.27 ? 246 TYR A OH 1 ATOM 1830 N N . LEU A 1 247 ? 11.589 20.615 12.730 1.00 17.31 ? 247 LEU A N 1 ATOM 1831 C CA . LEU A 1 247 ? 12.669 21.138 11.906 1.00 18.50 ? 247 LEU A CA 1 ATOM 1832 C C . LEU A 1 247 ? 12.135 22.353 11.171 1.00 18.03 ? 247 LEU A C 1 ATOM 1833 O O . LEU A 1 247 ? 10.982 22.367 10.769 1.00 18.02 ? 247 LEU A O 1 ATOM 1834 C CB . LEU A 1 247 ? 13.087 20.066 10.902 1.00 19.34 ? 247 LEU A CB 1 ATOM 1835 C CG . LEU A 1 247 ? 14.200 20.343 9.896 1.00 21.17 ? 247 LEU A CG 1 ATOM 1836 C CD1 . LEU A 1 247 ? 15.548 20.281 10.562 1.00 22.22 ? 247 LEU A CD1 1 ATOM 1837 C CD2 . LEU A 1 247 ? 14.161 19.310 8.763 1.00 22.12 ? 247 LEU A CD2 1 ATOM 1838 N N . GLN A 1 248 ? 12.958 23.380 10.996 1.00 18.30 ? 248 GLN A N 1 ATOM 1839 C CA . GLN A 1 248 ? 12.568 24.459 10.108 1.00 18.50 ? 248 GLN A CA 1 ATOM 1840 C C . GLN A 1 248 ? 13.670 24.740 9.097 1.00 18.82 ? 248 GLN A C 1 ATOM 1841 O O . GLN A 1 248 ? 14.852 24.468 9.346 1.00 18.85 ? 248 GLN A O 1 ATOM 1842 C CB . GLN A 1 248 ? 12.128 25.714 10.872 1.00 19.58 ? 248 GLN A CB 1 ATOM 1843 C CG . GLN A 1 248 ? 13.116 26.229 11.889 1.00 20.97 ? 248 GLN A CG 1 ATOM 1844 C CD . GLN A 1 248 ? 12.662 27.531 12.540 1.00 22.41 ? 248 GLN A CD 1 ATOM 1845 O OE1 . GLN A 1 248 ? 11.696 27.561 13.305 1.00 23.31 ? 248 GLN A OE1 1 ATOM 1846 N NE2 . GLN A 1 248 ? 13.380 28.593 12.272 1.00 23.51 ? 248 GLN A NE2 1 ATOM 1847 N N . ALA A 1 249 ? 13.248 25.249 7.943 1.00 18.65 ? 249 ALA A N 1 ATOM 1848 C CA . ALA A 1 249 ? 14.146 25.602 6.862 1.00 19.42 ? 249 ALA A CA 1 ATOM 1849 C C . ALA A 1 249 ? 13.821 27.016 6.392 1.00 20.17 ? 249 ALA A C 1 ATOM 1850 O O . ALA A 1 249 ? 12.658 27.329 6.133 1.00 19.36 ? 249 ALA A O 1 ATOM 1851 C CB . ALA A 1 249 ? 14.004 24.619 5.729 1.00 19.30 ? 249 ALA A CB 1 ATOM 1852 N N . THR A 1 250 ? 14.843 27.864 6.324 1.00 21.39 ? 250 THR A N 1 ATOM 1853 C CA . THR A 1 250 ? 14.655 29.277 5.980 1.00 22.69 ? 250 THR A CA 1 ATOM 1854 C C . THR A 1 250 ? 15.176 29.595 4.573 1.00 23.78 ? 250 THR A C 1 ATOM 1855 O O . THR A 1 250 ? 15.991 28.855 4.020 1.00 23.47 ? 250 THR A O 1 ATOM 1856 C CB . THR A 1 250 ? 15.330 30.203 7.011 1.00 23.99 ? 250 THR A CB 1 ATOM 1857 O OG1 . THR A 1 250 ? 16.751 30.055 6.949 1.00 24.81 ? 250 THR A OG1 1 ATOM 1858 C CG2 . THR A 1 250 ? 14.863 29.869 8.423 1.00 23.48 ? 250 THR A CG2 1 ATOM 1859 N N . LEU A 1 251 ? 14.681 30.692 3.989 1.00 24.64 ? 251 LEU A N 1 ATOM 1860 C CA . LEU A 1 251 ? 15.166 31.175 2.696 1.00 26.06 ? 251 LEU A CA 1 ATOM 1861 C C . LEU A 1 251 ? 15.152 32.689 2.690 1.00 28.23 ? 251 LEU A C 1 ATOM 1862 O O . LEU A 1 251 ? 14.101 33.304 2.884 1.00 27.99 ? 251 LEU A O 1 ATOM 1863 C CB . LEU A 1 251 ? 14.319 30.638 1.531 1.00 25.57 ? 251 LEU A CB 1 ATOM 1864 C CG . LEU A 1 251 ? 14.761 31.053 0.111 1.00 26.78 ? 251 LEU A CG 1 ATOM 1865 C CD1 . LEU A 1 251 ? 16.063 30.385 -0.298 1.00 27.30 ? 251 LEU A CD1 1 ATOM 1866 C CD2 . LEU A 1 251 ? 13.703 30.788 -0.949 1.00 26.77 ? 251 LEU A CD2 1 ATOM 1867 N N A ASP A 1 252 ? 16.316 33.297 2.476 0.50 29.97 ? 252 ASP A N 1 ATOM 1868 N N B ASP A 1 252 ? 16.325 33.285 2.472 0.50 29.89 ? 252 ASP A N 1 ATOM 1869 C CA A ASP A 1 252 ? 16.399 34.740 2.364 0.50 32.42 ? 252 ASP A CA 1 ATOM 1870 C CA B ASP A 1 252 ? 16.444 34.720 2.304 0.50 32.33 ? 252 ASP A CA 1 ATOM 1871 C C A ASP A 1 252 ? 16.060 35.132 0.919 0.50 33.54 ? 252 ASP A C 1 ATOM 1872 C C B ASP A 1 252 ? 15.998 35.067 0.889 0.50 33.34 ? 252 ASP A C 1 ATOM 1873 O O A ASP A 1 252 ? 16.659 34.618 -0.026 0.50 33.45 ? 252 ASP A O 1 ATOM 1874 O O B ASP A 1 252 ? 16.461 34.452 -0.072 0.50 33.00 ? 252 ASP A O 1 ATOM 1875 C CB A ASP A 1 252 ? 17.780 35.232 2.808 0.50 34.16 ? 252 ASP A CB 1 ATOM 1876 C CB B ASP A 1 252 ? 17.889 35.168 2.523 0.50 34.02 ? 252 ASP A CB 1 ATOM 1877 C CG A ASP A 1 252 ? 17.973 35.138 4.323 0.50 34.05 ? 252 ASP A CG 1 ATOM 1878 C CG B ASP A 1 252 ? 18.031 36.673 2.532 0.50 36.44 ? 252 ASP A CG 1 ATOM 1879 O OD1 A ASP A 1 252 ? 17.173 34.462 5.005 0.50 32.66 ? 252 ASP A OD1 1 ATOM 1880 O OD1 B ASP A 1 252 ? 17.423 37.322 3.407 0.50 36.95 ? 252 ASP A OD1 1 ATOM 1881 O OD2 A ASP A 1 252 ? 18.923 35.743 4.843 0.50 36.12 ? 252 ASP A OD2 1 ATOM 1882 O OD2 B ASP A 1 252 ? 18.751 37.203 1.664 0.50 38.20 ? 252 ASP A OD2 1 ATOM 1883 N N . VAL A 1 253 ? 15.084 36.025 0.761 1.00 34.80 ? 253 VAL A N 1 ATOM 1884 C CA . VAL A 1 253 ? 14.583 36.447 -0.561 1.00 36.58 ? 253 VAL A CA 1 ATOM 1885 C C . VAL A 1 253 ? 14.496 37.961 -0.643 1.00 40.01 ? 253 VAL A C 1 ATOM 1886 O O . VAL A 1 253 ? 14.187 38.622 0.346 1.00 40.93 ? 253 VAL A O 1 ATOM 1887 C CB . VAL A 1 253 ? 13.193 35.865 -0.884 1.00 35.68 ? 253 VAL A CB 1 ATOM 1888 C CG1 . VAL A 1 253 ? 13.238 34.345 -0.901 1.00 33.80 ? 253 VAL A CG1 1 ATOM 1889 C CG2 . VAL A 1 253 ? 12.142 36.340 0.109 1.00 35.94 ? 253 VAL A CG2 1 ATOM 1890 N N . GLU A 1 254 ? 14.760 38.493 -1.829 1.00 42.53 ? 254 GLU A N 1 ATOM 1891 C CA . GLU A 1 254 ? 14.569 39.914 -2.093 1.00 46.44 ? 254 GLU A CA 1 ATOM 1892 C C . GLU A 1 254 ? 13.073 40.189 -2.258 1.00 47.70 ? 254 GLU A C 1 ATOM 1893 O O . GLU A 1 254 ? 12.308 39.289 -2.636 1.00 45.65 ? 254 GLU A O 1 ATOM 1894 C CB . GLU A 1 254 ? 15.327 40.343 -3.351 1.00 48.15 ? 254 GLU A CB 1 ATOM 1895 N N . ALA A 1 255 ? 12.672 41.429 -1.967 1.00 51.44 ? 255 ALA A N 1 ATOM 1896 C CA . ALA A 1 255 ? 11.281 41.884 -2.137 1.00 53.24 ? 255 ALA A CA 1 ATOM 1897 C C . ALA A 1 255 ? 10.807 41.628 -3.564 1.00 54.18 ? 255 ALA A C 1 ATOM 1898 O O . ALA A 1 255 ? 11.537 41.922 -4.513 1.00 55.37 ? 255 ALA A O 1 ATOM 1899 C CB . ALA A 1 255 ? 11.169 43.368 -1.815 1.00 56.32 ? 255 ALA A CB 1 ATOM 1900 N N . GLY A 1 256 ? 9.616 41.043 -3.714 1.00 54.23 ? 256 GLY A N 1 ATOM 1901 C CA . GLY A 1 256 ? 9.030 40.783 -5.043 1.00 55.05 ? 256 GLY A CA 1 ATOM 1902 C C . GLY A 1 256 ? 9.290 39.359 -5.502 1.00 53.25 ? 256 GLY A C 1 ATOM 1903 O O . GLY A 1 256 ? 8.377 38.681 -6.004 1.00 53.30 ? 256 GLY A O 1 ATOM 1904 N N . GLU A 1 257 ? 10.536 38.913 -5.318 1.00 51.85 ? 257 GLU A N 1 ATOM 1905 C CA . GLU A 1 257 ? 10.951 37.515 -5.525 1.00 49.07 ? 257 GLU A CA 1 ATOM 1906 C C . GLU A 1 257 ? 10.178 36.457 -4.737 1.00 45.79 ? 257 GLU A C 1 ATOM 1907 O O . GLU A 1 257 ? 10.248 35.272 -5.087 1.00 44.66 ? 257 GLU A O 1 ATOM 1908 C CB . GLU A 1 257 ? 12.444 37.359 -5.205 1.00 49.03 ? 257 GLU A CB 1 ATOM 1909 N N . GLU A 1 258 ? 9.472 36.861 -3.674 1.00 44.63 ? 258 GLU A N 1 ATOM 1910 C CA . GLU A 1 258 ? 8.640 35.941 -2.888 1.00 42.11 ? 258 GLU A CA 1 ATOM 1911 C C . GLU A 1 258 ? 7.604 35.191 -3.706 1.00 40.14 ? 258 GLU A C 1 ATOM 1912 O O . GLU A 1 258 ? 7.298 34.044 -3.399 1.00 37.48 ? 258 GLU A O 1 ATOM 1913 C CB . GLU A 1 258 ? 7.870 36.664 -1.781 1.00 43.66 ? 258 GLU A CB 1 ATOM 1914 C CG . GLU A 1 258 ? 8.718 37.327 -0.723 1.00 44.80 ? 258 GLU A CG 1 ATOM 1915 C CD . GLU A 1 258 ? 8.545 38.825 -0.695 1.00 48.10 ? 258 GLU A CD 1 ATOM 1916 O OE1 . GLU A 1 258 ? 8.587 39.458 -1.767 1.00 50.88 ? 258 GLU A OE1 1 ATOM 1917 O OE2 . GLU A 1 258 ? 8.364 39.364 0.410 1.00 49.84 ? 258 GLU A OE2 1 ATOM 1918 N N . ALA A 1 259 ? 7.044 35.864 -4.713 1.00 40.43 ? 259 ALA A N 1 ATOM 1919 C CA . ALA A 1 259 ? 5.999 35.282 -5.548 1.00 39.59 ? 259 ALA A CA 1 ATOM 1920 C C . ALA A 1 259 ? 6.496 34.026 -6.249 1.00 37.17 ? 259 ALA A C 1 ATOM 1921 O O . ALA A 1 259 ? 7.586 34.021 -6.823 1.00 37.14 ? 259 ALA A O 1 ATOM 1922 C CB . ALA A 1 259 ? 5.516 36.294 -6.578 1.00 42.09 ? 259 ALA A CB 1 ATOM 1923 N N . GLY A 1 260 ? 5.692 32.968 -6.183 1.00 35.17 ? 260 GLY A N 1 ATOM 1924 C CA . GLY A 1 260 ? 6.006 31.695 -6.824 1.00 33.88 ? 260 GLY A CA 1 ATOM 1925 C C . GLY A 1 260 ? 6.768 30.688 -5.973 1.00 31.04 ? 260 GLY A C 1 ATOM 1926 O O . GLY A 1 260 ? 7.028 29.577 -6.433 1.00 30.86 ? 260 GLY A O 1 ATOM 1927 N N . LEU A 1 261 ? 7.124 31.042 -4.741 1.00 29.12 ? 261 LEU A N 1 ATOM 1928 C CA . LEU A 1 261 ? 7.864 30.111 -3.881 1.00 26.74 ? 261 LEU A CA 1 ATOM 1929 C C . LEU A 1 261 ? 6.929 29.165 -3.140 1.00 25.34 ? 261 LEU A C 1 ATOM 1930 O O . LEU A 1 261 ? 5.800 29.542 -2.773 1.00 25.00 ? 261 LEU A O 1 ATOM 1931 C CB . LEU A 1 261 ? 8.730 30.848 -2.865 1.00 26.41 ? 261 LEU A CB 1 ATOM 1932 C CG . LEU A 1 261 ? 9.972 31.524 -3.437 1.00 27.40 ? 261 LEU A CG 1 ATOM 1933 C CD1 . LEU A 1 261 ? 10.540 32.464 -2.394 1.00 27.61 ? 261 LEU A CD1 1 ATOM 1934 C CD2 . LEU A 1 261 ? 11.029 30.519 -3.878 1.00 27.16 ? 261 LEU A CD2 1 ATOM 1935 N N . ALA A 1 262 ? 7.433 27.951 -2.924 1.00 23.61 ? 262 ALA A N 1 ATOM 1936 C CA . ALA A 1 262 ? 6.741 26.894 -2.195 1.00 22.64 ? 262 ALA A CA 1 ATOM 1937 C C . ALA A 1 262 ? 7.702 26.163 -1.276 1.00 21.42 ? 262 ALA A C 1 ATOM 1938 O O . ALA A 1 262 ? 8.903 26.090 -1.552 1.00 20.76 ? 262 ALA A O 1 ATOM 1939 C CB . ALA A 1 262 ? 6.130 25.908 -3.177 1.00 23.34 ? 262 ALA A CB 1 ATOM 1940 N N . CYS A 1 263 ? 7.189 25.619 -0.176 1.00 20.94 ? 263 CYS A N 1 ATOM 1941 C CA . CYS A 1 263 ? 7.976 24.696 0.647 1.00 20.30 ? 263 CYS A CA 1 ATOM 1942 C C . CYS A 1 263 ? 7.429 23.307 0.423 1.00 20.32 ? 263 CYS A C 1 ATOM 1943 O O . CYS A 1 263 ? 6.229 23.091 0.587 1.00 20.11 ? 263 CYS A O 1 ATOM 1944 C CB . CYS A 1 263 ? 7.882 25.041 2.124 1.00 20.05 ? 263 CYS A CB 1 ATOM 1945 S SG . CYS A 1 263 ? 8.873 23.949 3.183 1.00 19.98 ? 263 CYS A SG 1 ATOM 1946 N N . ARG A 1 264 ? 8.303 22.387 0.043 1.00 20.39 ? 264 ARG A N 1 ATOM 1947 C CA . ARG A 1 264 ? 7.938 21.003 -0.184 1.00 21.23 ? 264 ARG A CA 1 ATOM 1948 C C . ARG A 1 264 ? 8.575 20.140 0.891 1.00 20.07 ? 264 ARG A C 1 ATOM 1949 O O . ARG A 1 264 ? 9.761 20.278 1.173 1.00 19.74 ? 264 ARG A O 1 ATOM 1950 C CB . ARG A 1 264 ? 8.383 20.530 -1.562 1.00 23.19 ? 264 ARG A CB 1 ATOM 1951 C CG . ARG A 1 264 ? 7.976 19.088 -1.843 1.00 24.93 ? 264 ARG A CG 1 ATOM 1952 C CD . ARG A 1 264 ? 8.597 18.544 -3.107 1.00 27.43 ? 264 ARG A CD 1 ATOM 1953 N NE . ARG A 1 264 ? 7.910 19.014 -4.290 1.00 29.16 ? 264 ARG A NE 1 ATOM 1954 C CZ . ARG A 1 264 ? 7.044 18.327 -5.044 1.00 31.28 ? 264 ARG A CZ 1 ATOM 1955 N NH1 . ARG A 1 264 ? 6.681 17.068 -4.774 1.00 32.37 ? 264 ARG A NH1 1 ATOM 1956 N NH2 . ARG A 1 264 ? 6.528 18.928 -6.108 1.00 32.22 ? 264 ARG A NH2 1 ATOM 1957 N N . VAL A 1 265 ? 7.772 19.244 1.455 1.00 19.86 ? 265 VAL A N 1 ATOM 1958 C CA . VAL A 1 265 ? 8.187 18.333 2.506 1.00 19.51 ? 265 VAL A CA 1 ATOM 1959 C C . VAL A 1 265 ? 7.926 16.902 2.073 1.00 20.76 ? 265 VAL A C 1 ATOM 1960 O O . VAL A 1 265 ? 6.814 16.570 1.682 1.00 20.98 ? 265 VAL A O 1 ATOM 1961 C CB . VAL A 1 265 ? 7.437 18.600 3.821 1.00 18.68 ? 265 VAL A CB 1 ATOM 1962 C CG1 . VAL A 1 265 ? 7.852 17.607 4.899 1.00 18.52 ? 265 VAL A CG1 1 ATOM 1963 C CG2 . VAL A 1 265 ? 7.672 20.033 4.280 1.00 18.14 ? 265 VAL A CG2 1 ATOM 1964 N N . LYS A 1 266 ? 8.964 16.064 2.146 1.00 21.46 ? 266 LYS A N 1 ATOM 1965 C CA . LYS A 1 266 ? 8.828 14.632 1.895 1.00 23.02 ? 266 LYS A CA 1 ATOM 1966 C C . LYS A 1 266 ? 9.075 13.906 3.209 1.00 22.31 ? 266 LYS A C 1 ATOM 1967 O O . LYS A 1 266 ? 9.982 14.281 3.973 1.00 21.56 ? 266 LYS A O 1 ATOM 1968 C CB . LYS A 1 266 ? 9.830 14.138 0.844 1.00 25.03 ? 266 LYS A CB 1 ATOM 1969 C CG . LYS A 1 266 ? 9.819 14.883 -0.475 1.00 26.08 ? 266 LYS A CG 1 ATOM 1970 C CD . LYS A 1 266 ? 10.994 14.458 -1.349 1.00 27.93 ? 266 LYS A CD 1 ATOM 1971 C CE . LYS A 1 266 ? 10.955 15.097 -2.723 1.00 29.11 ? 266 LYS A CE 1 ATOM 1972 N NZ . LYS A 1 266 ? 9.765 14.673 -3.504 1.00 30.41 ? 266 LYS A NZ 1 ATOM 1973 N N . HIS A 1 267 ? 8.254 12.895 3.492 1.00 22.62 ? 267 HIS A N 1 ATOM 1974 C CA . HIS A 1 267 ? 8.425 12.090 4.689 1.00 22.37 ? 267 HIS A CA 1 ATOM 1975 C C . HIS A 1 267 ? 7.782 10.729 4.506 1.00 23.98 ? 267 HIS A C 1 ATOM 1976 O O . HIS A 1 267 ? 6.741 10.610 3.861 1.00 24.80 ? 267 HIS A O 1 ATOM 1977 C CB . HIS A 1 267 ? 7.847 12.805 5.918 1.00 20.70 ? 267 HIS A CB 1 ATOM 1978 C CG . HIS A 1 267 ? 8.152 12.115 7.210 1.00 20.70 ? 267 HIS A CG 1 ATOM 1979 N ND1 . HIS A 1 267 ? 7.242 11.306 7.852 1.00 21.20 ? 267 HIS A ND1 1 ATOM 1980 C CD2 . HIS A 1 267 ? 9.279 12.079 7.962 1.00 20.40 ? 267 HIS A CD2 1 ATOM 1981 C CE1 . HIS A 1 267 ? 7.787 10.809 8.950 1.00 21.05 ? 267 HIS A CE1 1 ATOM 1982 N NE2 . HIS A 1 267 ? 9.022 11.271 9.045 1.00 20.62 ? 267 HIS A NE2 1 ATOM 1983 N N . SER A 1 268 ? 8.402 9.717 5.105 1.00 24.93 ? 268 SER A N 1 ATOM 1984 C CA . SER A 1 268 ? 7.965 8.319 5.008 1.00 26.89 ? 268 SER A CA 1 ATOM 1985 C C . SER A 1 268 ? 6.484 8.089 5.354 1.00 27.18 ? 268 SER A C 1 ATOM 1986 O O . SER A 1 268 ? 5.847 7.211 4.806 1.00 29.06 ? 268 SER A O 1 ATOM 1987 C CB . SER A 1 268 ? 8.833 7.449 5.932 1.00 27.57 ? 268 SER A CB 1 ATOM 1988 O OG . SER A 1 268 ? 8.856 8.010 7.242 1.00 25.72 ? 268 SER A OG 1 ATOM 1989 N N . SER A 1 269 ? 5.967 8.857 6.300 1.00 25.62 ? 269 SER A N 1 ATOM 1990 C CA . SER A 1 269 ? 4.567 8.774 6.745 1.00 26.01 ? 269 SER A CA 1 ATOM 1991 C C . SER A 1 269 ? 3.524 9.271 5.753 1.00 27.05 ? 269 SER A C 1 ATOM 1992 O O . SER A 1 269 ? 2.332 9.031 5.952 1.00 27.79 ? 269 SER A O 1 ATOM 1993 C CB . SER A 1 269 ? 4.386 9.596 8.018 1.00 23.99 ? 269 SER A CB 1 ATOM 1994 O OG . SER A 1 269 ? 4.614 10.956 7.736 1.00 22.04 ? 269 SER A OG 1 ATOM 1995 N N . LEU A 1 270 ? 3.952 9.986 4.717 1.00 27.39 ? 270 LEU A N 1 ATOM 1996 C CA . LEU A 1 270 ? 3.016 10.665 3.833 1.00 28.53 ? 270 LEU A CA 1 ATOM 1997 C C . LEU A 1 270 ? 2.526 9.840 2.648 1.00 31.51 ? 270 LEU A C 1 ATOM 1998 O O . LEU A 1 270 ? 1.777 10.359 1.821 1.00 32.27 ? 270 LEU A O 1 ATOM 1999 C CB . LEU A 1 270 ? 3.637 11.970 3.345 1.00 27.03 ? 270 LEU A CB 1 ATOM 2000 C CG . LEU A 1 270 ? 3.895 12.988 4.443 1.00 25.06 ? 270 LEU A CG 1 ATOM 2001 C CD1 . LEU A 1 270 ? 4.540 14.211 3.826 1.00 24.36 ? 270 LEU A CD1 1 ATOM 2002 C CD2 . LEU A 1 270 ? 2.616 13.355 5.189 1.00 25.08 ? 270 LEU A CD2 1 ATOM 2003 N N . GLY A 1 271 ? 2.948 8.581 2.552 1.00 33.92 ? 271 GLY A N 1 ATOM 2004 C CA . GLY A 1 271 ? 2.509 7.672 1.481 1.00 37.13 ? 271 GLY A CA 1 ATOM 2005 C C . GLY A 1 271 ? 2.774 8.156 0.061 1.00 38.17 ? 271 GLY A C 1 ATOM 2006 O O . GLY A 1 271 ? 1.954 7.939 -0.835 1.00 40.17 ? 271 GLY A O 1 ATOM 2007 N N . GLY A 1 272 ? 3.912 8.820 -0.137 1.00 36.93 ? 272 GLY A N 1 ATOM 2008 C CA . GLY A 1 272 ? 4.272 9.395 -1.436 1.00 37.50 ? 272 GLY A CA 1 ATOM 2009 C C . GLY A 1 272 ? 3.662 10.754 -1.780 1.00 36.28 ? 272 GLY A C 1 ATOM 2010 O O . GLY A 1 272 ? 3.963 11.294 -2.836 1.00 37.26 ? 272 GLY A O 1 ATOM 2011 N N . GLN A 1 273 ? 2.817 11.311 -0.907 1.00 34.43 ? 273 GLN A N 1 ATOM 2012 C CA . GLN A 1 273 ? 2.102 12.559 -1.192 1.00 33.23 ? 273 GLN A CA 1 ATOM 2013 C C . GLN A 1 273 ? 2.765 13.675 -0.409 1.00 29.94 ? 273 GLN A C 1 ATOM 2014 O O . GLN A 1 273 ? 2.461 13.872 0.759 1.00 28.99 ? 273 GLN A O 1 ATOM 2015 C CB . GLN A 1 273 ? 0.628 12.447 -0.789 1.00 34.02 ? 273 GLN A CB 1 ATOM 2016 N N . ASP A 1 274 ? 3.676 14.393 -1.056 1.00 28.76 ? 274 ASP A N 1 ATOM 2017 C CA . ASP A 1 274 ? 4.442 15.446 -0.390 1.00 26.52 ? 274 ASP A CA 1 ATOM 2018 C C . ASP A 1 274 ? 3.533 16.584 0.068 1.00 25.16 ? 274 ASP A C 1 ATOM 2019 O O . ASP A 1 274 ? 2.511 16.871 -0.559 1.00 25.89 ? 274 ASP A O 1 ATOM 2020 C CB . ASP A 1 274 ? 5.508 16.014 -1.328 1.00 26.90 ? 274 ASP A CB 1 ATOM 2021 C CG . ASP A 1 274 ? 6.525 14.980 -1.772 1.00 28.35 ? 274 ASP A CG 1 ATOM 2022 O OD1 . ASP A 1 274 ? 6.528 13.854 -1.236 1.00 29.00 ? 274 ASP A OD1 1 ATOM 2023 O OD2 . ASP A 1 274 ? 7.335 15.305 -2.665 1.00 29.32 ? 274 ASP A OD2 1 ATOM 2024 N N . ILE A 1 275 ? 3.890 17.218 1.173 1.00 23.03 ? 275 ILE A N 1 ATOM 2025 C CA . ILE A 1 275 ? 3.246 18.466 1.545 1.00 22.42 ? 275 ILE A CA 1 ATOM 2026 C C . ILE A 1 275 ? 3.874 19.544 0.654 1.00 22.04 ? 275 ILE A C 1 ATOM 2027 O O . ILE A 1 275 ? 5.083 19.585 0.512 1.00 21.35 ? 275 ILE A O 1 ATOM 2028 C CB . ILE A 1 275 ? 3.461 18.808 3.033 1.00 21.30 ? 275 ILE A CB 1 ATOM 2029 C CG1 . ILE A 1 275 ? 2.768 17.758 3.912 1.00 21.75 ? 275 ILE A CG1 1 ATOM 2030 C CG2 . ILE A 1 275 ? 2.936 20.210 3.350 1.00 21.29 ? 275 ILE A CG2 1 ATOM 2031 C CD1 . ILE A 1 275 ? 3.205 17.790 5.358 1.00 20.96 ? 275 ILE A CD1 1 ATOM 2032 N N . ILE A 1 276 ? 3.057 20.375 0.023 1.00 22.54 ? 276 ILE A N 1 ATOM 2033 C CA . ILE A 1 276 ? 3.562 21.579 -0.631 1.00 22.68 ? 276 ILE A CA 1 ATOM 2034 C C . ILE A 1 276 ? 2.722 22.764 -0.159 1.00 22.61 ? 276 ILE A C 1 ATOM 2035 O O . ILE A 1 276 ? 1.503 22.773 -0.342 1.00 23.71 ? 276 ILE A O 1 ATOM 2036 C CB . ILE A 1 276 ? 3.570 21.497 -2.177 1.00 24.47 ? 276 ILE A CB 1 ATOM 2037 C CG1 . ILE A 1 276 ? 4.349 20.272 -2.677 1.00 25.11 ? 276 ILE A CG1 1 ATOM 2038 C CG2 . ILE A 1 276 ? 4.201 22.758 -2.764 1.00 24.49 ? 276 ILE A CG2 1 ATOM 2039 C CD1 . ILE A 1 276 ? 4.169 19.985 -4.147 1.00 27.34 ? 276 ILE A CD1 1 ATOM 2040 N N . LEU A 1 277 ? 3.376 23.736 0.472 1.00 21.46 ? 277 LEU A N 1 ATOM 2041 C CA . LEU A 1 277 ? 2.725 24.990 0.858 1.00 21.77 ? 277 LEU A CA 1 ATOM 2042 C C . LEU A 1 277 ? 3.249 26.094 -0.019 1.00 22.30 ? 277 LEU A C 1 ATOM 2043 O O . LEU A 1 277 ? 4.452 26.141 -0.278 1.00 21.31 ? 277 LEU A O 1 ATOM 2044 C CB . LEU A 1 277 ? 3.011 25.318 2.319 1.00 20.90 ? 277 LEU A CB 1 ATOM 2045 C CG . LEU A 1 277 ? 2.643 24.226 3.314 1.00 20.46 ? 277 LEU A CG 1 ATOM 2046 C CD1 . LEU A 1 277 ? 2.925 24.722 4.724 1.00 20.16 ? 277 LEU A CD1 1 ATOM 2047 C CD2 . LEU A 1 277 ? 1.198 23.783 3.155 1.00 21.52 ? 277 LEU A CD2 1 ATOM 2048 N N . TYR A 1 278 ? 2.355 26.987 -0.447 1.00 23.68 ? 278 TYR A N 1 ATOM 2049 C CA . TYR A 1 278 ? 2.679 28.093 -1.332 1.00 24.76 ? 278 TYR A CA 1 ATOM 2050 C C . TYR A 1 278 ? 2.692 29.420 -0.569 1.00 25.44 ? 278 TYR A C 1 ATOM 2051 O O . TYR A 1 278 ? 1.712 29.785 0.086 1.00 25.89 ? 278 TYR A O 1 ATOM 2052 C CB . TYR A 1 278 ? 1.667 28.138 -2.492 1.00 26.60 ? 278 TYR A CB 1 ATOM 2053 C CG . TYR A 1 278 ? 1.763 26.900 -3.341 1.00 26.73 ? 278 TYR A CG 1 ATOM 2054 C CD1 . TYR A 1 278 ? 0.995 25.761 -3.054 1.00 26.87 ? 278 TYR A CD1 1 ATOM 2055 C CD2 . TYR A 1 278 ? 2.694 26.819 -4.371 1.00 27.13 ? 278 TYR A CD2 1 ATOM 2056 C CE1 . TYR A 1 278 ? 1.109 24.607 -3.819 1.00 27.26 ? 278 TYR A CE1 1 ATOM 2057 C CE2 . TYR A 1 278 ? 2.817 25.668 -5.136 1.00 27.46 ? 278 TYR A CE2 1 ATOM 2058 C CZ . TYR A 1 278 ? 2.034 24.570 -4.850 1.00 27.60 ? 278 TYR A CZ 1 ATOM 2059 O OH . TYR A 1 278 ? 2.188 23.436 -5.593 1.00 28.66 ? 278 TYR A OH 1 ATOM 2060 N N . TRP A 1 279 ? 3.785 30.167 -0.685 1.00 25.68 ? 279 TRP A N 1 ATOM 2061 C CA . TRP A 1 279 ? 3.877 31.472 -0.034 1.00 27.23 ? 279 TRP A CA 1 ATOM 2062 C C . TRP A 1 279 ? 2.956 32.495 -0.716 1.00 29.37 ? 279 TRP A C 1 ATOM 2063 O O . TRP A 1 279 ? 2.755 32.450 -1.927 1.00 30.09 ? 279 TRP A O 1 ATOM 2064 C CB . TRP A 1 279 ? 5.336 31.956 0.001 1.00 27.59 ? 279 TRP A CB 1 ATOM 2065 C CG . TRP A 1 279 ? 5.493 33.251 0.707 1.00 29.68 ? 279 TRP A CG 1 ATOM 2066 C CD1 . TRP A 1 279 ? 5.646 34.460 0.136 1.00 32.07 ? 279 TRP A CD1 1 ATOM 2067 C CD2 . TRP A 1 279 ? 5.462 33.474 2.121 1.00 30.20 ? 279 TRP A CD2 1 ATOM 2068 N NE1 . TRP A 1 279 ? 5.720 35.439 1.097 1.00 33.46 ? 279 TRP A NE1 1 ATOM 2069 C CE2 . TRP A 1 279 ? 5.621 34.855 2.329 1.00 32.10 ? 279 TRP A CE2 1 ATOM 2070 C CE3 . TRP A 1 279 ? 5.308 32.641 3.231 1.00 29.39 ? 279 TRP A CE3 1 ATOM 2071 C CZ2 . TRP A 1 279 ? 5.631 35.429 3.605 1.00 33.05 ? 279 TRP A CZ2 1 ATOM 2072 C CZ3 . TRP A 1 279 ? 5.326 33.213 4.510 1.00 30.06 ? 279 TRP A CZ3 1 ATOM 2073 C CH2 . TRP A 1 279 ? 5.489 34.594 4.680 1.00 31.86 ? 279 TRP A CH2 1 ATOM 2074 N N . ILE B 2 1 ? 35.799 22.091 30.936 1.00 39.85 ? 1 ILE B N 1 ATOM 2075 C CA . ILE B 2 1 ? 35.585 23.540 30.627 1.00 40.06 ? 1 ILE B CA 1 ATOM 2076 C C . ILE B 2 1 ? 34.100 23.854 30.628 1.00 38.09 ? 1 ILE B C 1 ATOM 2077 O O . ILE B 2 1 ? 33.285 22.967 30.363 1.00 37.02 ? 1 ILE B O 1 ATOM 2078 C CB . ILE B 2 1 ? 36.170 23.930 29.250 1.00 40.50 ? 1 ILE B CB 1 ATOM 2079 N N . GLN B 2 2 ? 33.756 25.105 30.938 1.00 38.13 ? 2 GLN B N 1 ATOM 2080 C CA . GLN B 2 2 ? 32.361 25.561 30.898 1.00 36.94 ? 2 GLN B CA 1 ATOM 2081 C C . GLN B 2 2 ? 31.905 25.762 29.454 1.00 35.32 ? 2 GLN B C 1 ATOM 2082 O O . GLN B 2 2 ? 32.681 26.201 28.615 1.00 36.22 ? 2 GLN B O 1 ATOM 2083 C CB . GLN B 2 2 ? 32.175 26.855 31.704 1.00 38.58 ? 2 GLN B CB 1 ATOM 2084 C CG . GLN B 2 2 ? 32.374 26.647 33.196 1.00 40.14 ? 2 GLN B CG 1 ATOM 2085 C CD . GLN B 2 2 ? 31.935 27.828 34.040 1.00 41.93 ? 2 GLN B CD 1 ATOM 2086 O OE1 . GLN B 2 2 ? 32.101 28.989 33.652 1.00 42.87 ? 2 GLN B OE1 1 ATOM 2087 N NE2 . GLN B 2 2 ? 31.388 27.537 35.220 1.00 42.60 ? 2 GLN B NE2 1 ATOM 2088 N N . LYS B 2 3 ? 30.657 25.406 29.165 1.00 32.87 ? 3 LYS B N 1 ATOM 2089 C CA . LYS B 2 3 ? 30.073 25.620 27.840 1.00 31.63 ? 3 LYS B CA 1 ATOM 2090 C C . LYS B 2 3 ? 28.739 26.329 28.010 1.00 29.94 ? 3 LYS B C 1 ATOM 2091 O O . LYS B 2 3 ? 27.941 25.950 28.868 1.00 28.61 ? 3 LYS B O 1 ATOM 2092 C CB . LYS B 2 3 ? 29.898 24.302 27.098 1.00 31.33 ? 3 LYS B CB 1 ATOM 2093 C CG . LYS B 2 3 ? 31.218 23.611 26.776 1.00 33.05 ? 3 LYS B CG 1 ATOM 2094 C CD . LYS B 2 3 ? 31.027 22.282 26.058 1.00 33.37 ? 3 LYS B CD 1 ATOM 2095 C CE . LYS B 2 3 ? 32.336 21.805 25.430 1.00 35.36 ? 3 LYS B CE 1 ATOM 2096 N NZ . LYS B 2 3 ? 32.202 20.514 24.684 1.00 35.65 ? 3 LYS B NZ 1 ATOM 2097 N N . THR B 2 4 ? 28.520 27.354 27.180 1.00 29.29 ? 4 THR B N 1 ATOM 2098 C CA . THR B 2 4 ? 27.372 28.251 27.295 1.00 28.58 ? 4 THR B CA 1 ATOM 2099 C C . THR B 2 4 ? 26.128 27.641 26.652 1.00 26.34 ? 4 THR B C 1 ATOM 2100 O O . THR B 2 4 ? 26.211 27.149 25.526 1.00 25.51 ? 4 THR B O 1 ATOM 2101 C CB . THR B 2 4 ? 27.700 29.611 26.646 1.00 29.87 ? 4 THR B CB 1 ATOM 2102 O OG1 . THR B 2 4 ? 28.822 30.167 27.326 1.00 31.45 ? 4 THR B OG1 1 ATOM 2103 C CG2 . THR B 2 4 ? 26.553 30.580 26.757 1.00 30.14 ? 4 THR B CG2 1 ATOM 2104 N N . PRO B 2 5 ? 24.970 27.684 27.353 1.00 25.56 ? 5 PRO B N 1 ATOM 2105 C CA . PRO B 2 5 ? 23.774 27.090 26.744 1.00 24.24 ? 5 PRO B CA 1 ATOM 2106 C C . PRO B 2 5 ? 23.275 27.854 25.521 1.00 24.57 ? 5 PRO B C 1 ATOM 2107 O O . PRO B 2 5 ? 23.335 29.091 25.487 1.00 24.91 ? 5 PRO B O 1 ATOM 2108 C CB . PRO B 2 5 ? 22.727 27.141 27.855 1.00 24.06 ? 5 PRO B CB 1 ATOM 2109 C CG . PRO B 2 5 ? 23.219 28.143 28.825 1.00 25.78 ? 5 PRO B CG 1 ATOM 2110 C CD . PRO B 2 5 ? 24.713 28.148 28.726 1.00 26.33 ? 5 PRO B CD 1 ATOM 2111 N N . GLN B 2 6 ? 22.800 27.097 24.537 1.00 23.88 ? 6 GLN B N 1 ATOM 2112 C CA . GLN B 2 6 ? 22.072 27.631 23.403 1.00 24.51 ? 6 GLN B CA 1 ATOM 2113 C C . GLN B 2 6 ? 20.599 27.347 23.641 1.00 22.69 ? 6 GLN B C 1 ATOM 2114 O O . GLN B 2 6 ? 20.254 26.351 24.274 1.00 21.56 ? 6 GLN B O 1 ATOM 2115 C CB . GLN B 2 6 ? 22.592 27.012 22.102 1.00 25.64 ? 6 GLN B CB 1 ATOM 2116 C CG . GLN B 2 6 ? 24.116 27.173 21.932 1.00 28.14 ? 6 GLN B CG 1 ATOM 2117 C CD . GLN B 2 6 ? 24.612 28.617 22.056 1.00 30.99 ? 6 GLN B CD 1 ATOM 2118 O OE1 . GLN B 2 6 ? 25.529 28.929 22.846 1.00 33.64 ? 6 GLN B OE1 1 ATOM 2119 N NE2 . GLN B 2 6 ? 24.016 29.505 21.279 1.00 32.14 ? 6 GLN B NE2 1 ATOM 2120 N N . ILE B 2 7 ? 19.748 28.261 23.188 1.00 22.68 ? 7 ILE B N 1 ATOM 2121 C CA . ILE B 2 7 ? 18.316 28.224 23.492 1.00 21.89 ? 7 ILE B CA 1 ATOM 2122 C C . ILE B 2 7 ? 17.518 28.396 22.220 1.00 21.61 ? 7 ILE B C 1 ATOM 2123 O O . ILE B 2 7 ? 17.734 29.345 21.478 1.00 22.22 ? 7 ILE B O 1 ATOM 2124 C CB . ILE B 2 7 ? 17.906 29.345 24.471 1.00 22.83 ? 7 ILE B CB 1 ATOM 2125 C CG1 . ILE B 2 7 ? 18.722 29.259 25.768 1.00 23.48 ? 7 ILE B CG1 1 ATOM 2126 C CG2 . ILE B 2 7 ? 16.396 29.282 24.767 1.00 22.29 ? 7 ILE B CG2 1 ATOM 2127 C CD1 . ILE B 2 7 ? 18.560 30.477 26.651 1.00 25.05 ? 7 ILE B CD1 1 ATOM 2128 N N . GLN B 2 8 ? 16.564 27.493 21.995 1.00 20.50 ? 8 GLN B N 1 ATOM 2129 C CA . GLN B 2 8 ? 15.650 27.586 20.865 1.00 20.35 ? 8 GLN B CA 1 ATOM 2130 C C . GLN B 2 8 ? 14.224 27.397 21.367 1.00 19.28 ? 8 GLN B C 1 ATOM 2131 O O . GLN B 2 8 ? 13.938 26.477 22.157 1.00 17.99 ? 8 GLN B O 1 ATOM 2132 C CB . GLN B 2 8 ? 16.010 26.549 19.816 1.00 20.96 ? 8 GLN B CB 1 ATOM 2133 C CG . GLN B 2 8 ? 17.408 26.767 19.267 1.00 22.19 ? 8 GLN B CG 1 ATOM 2134 C CD . GLN B 2 8 ? 17.883 25.591 18.452 1.00 22.80 ? 8 GLN B CD 1 ATOM 2135 O OE1 . GLN B 2 8 ? 18.505 24.657 18.988 1.00 23.43 ? 8 GLN B OE1 1 ATOM 2136 N NE2 . GLN B 2 8 ? 17.579 25.610 17.159 1.00 23.18 ? 8 GLN B NE2 1 ATOM 2137 N N . VAL B 2 9 ? 13.348 28.300 20.930 1.00 19.18 ? 9 VAL B N 1 ATOM 2138 C CA . VAL B 2 9 ? 11.965 28.356 21.401 1.00 18.97 ? 9 VAL B CA 1 ATOM 2139 C C . VAL B 2 9 ? 11.060 28.227 20.178 1.00 18.86 ? 9 VAL B C 1 ATOM 2140 O O . VAL B 2 9 ? 11.195 28.992 19.222 1.00 19.51 ? 9 VAL B O 1 ATOM 2141 C CB . VAL B 2 9 ? 11.683 29.684 22.148 1.00 19.78 ? 9 VAL B CB 1 ATOM 2142 C CG1 . VAL B 2 9 ? 10.245 29.753 22.661 1.00 20.08 ? 9 VAL B CG1 1 ATOM 2143 C CG2 . VAL B 2 9 ? 12.662 29.868 23.299 1.00 20.07 ? 9 VAL B CG2 1 ATOM 2144 N N . TYR B 2 10 ? 10.135 27.268 20.212 1.00 18.24 ? 10 TYR B N 1 ATOM 2145 C CA . TYR B 2 10 ? 9.325 26.917 19.046 1.00 18.24 ? 10 TYR B CA 1 ATOM 2146 C C . TYR B 2 10 ? 8.024 26.274 19.504 1.00 17.92 ? 10 TYR B C 1 ATOM 2147 O O . TYR B 2 10 ? 7.967 25.672 20.588 1.00 17.62 ? 10 TYR B O 1 ATOM 2148 C CB . TYR B 2 10 ? 10.096 25.967 18.120 1.00 18.43 ? 10 TYR B CB 1 ATOM 2149 C CG . TYR B 2 10 ? 10.725 24.766 18.820 1.00 17.94 ? 10 TYR B CG 1 ATOM 2150 C CD1 . TYR B 2 10 ? 11.874 24.907 19.591 1.00 17.86 ? 10 TYR B CD1 1 ATOM 2151 C CD2 . TYR B 2 10 ? 10.195 23.491 18.682 1.00 18.03 ? 10 TYR B CD2 1 ATOM 2152 C CE1 . TYR B 2 10 ? 12.456 23.817 20.228 1.00 17.51 ? 10 TYR B CE1 1 ATOM 2153 C CE2 . TYR B 2 10 ? 10.784 22.394 19.306 1.00 17.69 ? 10 TYR B CE2 1 ATOM 2154 C CZ . TYR B 2 10 ? 11.907 22.568 20.086 1.00 17.55 ? 10 TYR B CZ 1 ATOM 2155 O OH . TYR B 2 10 ? 12.514 21.499 20.720 1.00 17.65 ? 10 TYR B OH 1 ATOM 2156 N N . SER B 2 11 ? 6.974 26.414 18.703 1.00 17.95 ? 11 SER B N 1 ATOM 2157 C CA . SER B 2 11 ? 5.680 25.803 19.036 1.00 18.16 ? 11 SER B CA 1 ATOM 2158 C C . SER B 2 11 ? 5.542 24.384 18.448 1.00 17.91 ? 11 SER B C 1 ATOM 2159 O O . SER B 2 11 ? 6.096 24.074 17.377 1.00 17.99 ? 11 SER B O 1 ATOM 2160 C CB . SER B 2 11 ? 4.514 26.692 18.582 1.00 18.86 ? 11 SER B CB 1 ATOM 2161 O OG . SER B 2 11 ? 4.455 26.751 17.168 1.00 19.37 ? 11 SER B OG 1 ATOM 2162 N N . ARG B 2 12 ? 4.793 23.535 19.158 1.00 17.83 ? 12 ARG B N 1 ATOM 2163 C CA . ARG B 2 12 ? 4.520 22.159 18.723 1.00 18.18 ? 12 ARG B CA 1 ATOM 2164 C C . ARG B 2 12 ? 3.636 22.111 17.475 1.00 19.07 ? 12 ARG B C 1 ATOM 2165 O O . ARG B 2 12 ? 3.854 21.280 16.583 1.00 19.51 ? 12 ARG B O 1 ATOM 2166 C CB . ARG B 2 12 ? 3.863 21.355 19.856 1.00 18.57 ? 12 ARG B CB 1 ATOM 2167 C CG . ARG B 2 12 ? 3.304 19.992 19.465 1.00 19.34 ? 12 ARG B CG 1 ATOM 2168 C CD . ARG B 2 12 ? 4.430 19.045 19.076 1.00 19.11 ? 12 ARG B CD 1 ATOM 2169 N NE . ARG B 2 12 ? 3.932 17.729 18.693 1.00 20.13 ? 12 ARG B NE 1 ATOM 2170 C CZ . ARG B 2 12 ? 3.385 17.427 17.513 1.00 20.92 ? 12 ARG B CZ 1 ATOM 2171 N NH1 . ARG B 2 12 ? 3.202 18.349 16.578 1.00 20.86 ? 12 ARG B NH1 1 ATOM 2172 N NH2 . ARG B 2 12 ? 2.961 16.186 17.279 1.00 22.37 ? 12 ARG B NH2 1 ATOM 2173 N N . HIS B 2 13 ? 2.635 22.993 17.435 1.00 19.55 ? 13 HIS B N 1 ATOM 2174 C CA . HIS B 2 13 ? 1.675 23.056 16.354 1.00 20.65 ? 13 HIS B CA 1 ATOM 2175 C C . HIS B 2 13 ? 1.719 24.453 15.728 1.00 20.71 ? 13 HIS B C 1 ATOM 2176 O O . HIS B 2 13 ? 2.207 25.397 16.363 1.00 19.87 ? 13 HIS B O 1 ATOM 2177 C CB . HIS B 2 13 ? 0.265 22.779 16.896 1.00 21.59 ? 13 HIS B CB 1 ATOM 2178 C CG . HIS B 2 13 ? 0.134 21.465 17.599 1.00 22.07 ? 13 HIS B CG 1 ATOM 2179 N ND1 . HIS B 2 13 ? 0.124 20.261 16.927 1.00 22.92 ? 13 HIS B ND1 1 ATOM 2180 C CD2 . HIS B 2 13 ? -0.034 21.169 18.911 1.00 22.22 ? 13 HIS B CD2 1 ATOM 2181 C CE1 . HIS B 2 13 ? -0.007 19.273 17.800 1.00 23.35 ? 13 HIS B CE1 1 ATOM 2182 N NE2 . HIS B 2 13 ? -0.113 19.799 19.011 1.00 22.99 ? 13 HIS B NE2 1 ATOM 2183 N N . PRO B 2 14 ? 1.170 24.591 14.507 1.00 21.91 ? 14 PRO B N 1 ATOM 2184 C CA . PRO B 2 14 ? 1.072 25.932 13.928 1.00 22.54 ? 14 PRO B CA 1 ATOM 2185 C C . PRO B 2 14 ? 0.322 26.892 14.856 1.00 23.18 ? 14 PRO B C 1 ATOM 2186 O O . PRO B 2 14 ? -0.750 26.547 15.357 1.00 23.40 ? 14 PRO B O 1 ATOM 2187 C CB . PRO B 2 14 ? 0.277 25.732 12.631 1.00 23.78 ? 14 PRO B CB 1 ATOM 2188 C CG . PRO B 2 14 ? 0.271 24.281 12.356 1.00 23.97 ? 14 PRO B CG 1 ATOM 2189 C CD . PRO B 2 14 ? 0.587 23.555 13.635 1.00 22.91 ? 14 PRO B CD 1 ATOM 2190 N N . PRO B 2 15 ? 0.873 28.091 15.071 1.00 23.50 ? 15 PRO B N 1 ATOM 2191 C CA . PRO B 2 15 ? 0.231 29.016 15.987 1.00 24.21 ? 15 PRO B CA 1 ATOM 2192 C C . PRO B 2 15 ? -1.044 29.607 15.409 1.00 25.92 ? 15 PRO B C 1 ATOM 2193 O O . PRO B 2 15 ? -1.077 30.018 14.237 1.00 26.26 ? 15 PRO B O 1 ATOM 2194 C CB . PRO B 2 15 ? 1.291 30.093 16.221 1.00 24.01 ? 15 PRO B CB 1 ATOM 2195 C CG . PRO B 2 15 ? 2.206 30.007 15.064 1.00 23.97 ? 15 PRO B CG 1 ATOM 2196 C CD . PRO B 2 15 ? 2.162 28.597 14.562 1.00 23.47 ? 15 PRO B CD 1 ATOM 2197 N N . GLU B 2 16 ? -2.090 29.589 16.229 1.00 27.00 ? 16 GLU B N 1 ATOM 2198 C CA . GLU B 2 16 ? -3.367 30.213 15.894 1.00 29.21 ? 16 GLU B CA 1 ATOM 2199 C C . GLU B 2 16 ? -3.841 30.932 17.135 1.00 29.50 ? 16 GLU B C 1 ATOM 2200 O O . GLU B 2 16 ? -3.934 30.322 18.207 1.00 28.56 ? 16 GLU B O 1 ATOM 2201 C CB . GLU B 2 16 ? -4.411 29.178 15.509 1.00 30.68 ? 16 GLU B CB 1 ATOM 2202 C CG . GLU B 2 16 ? -4.051 28.317 14.315 1.00 31.75 ? 16 GLU B CG 1 ATOM 2203 C CD . GLU B 2 16 ? -5.158 27.334 13.953 1.00 33.77 ? 16 GLU B CD 1 ATOM 2204 O OE1 . GLU B 2 16 ? -4.831 26.269 13.382 1.00 35.37 ? 16 GLU B OE1 1 ATOM 2205 O OE2 . GLU B 2 16 ? -6.342 27.610 14.245 1.00 34.98 ? 16 GLU B OE2 1 ATOM 2206 N N . ASN B 2 17 ? -4.146 32.222 17.008 1.00 30.74 ? 17 ASN B N 1 ATOM 2207 C CA . ASN B 2 17 ? -4.505 32.989 18.199 1.00 31.51 ? 17 ASN B CA 1 ATOM 2208 C C . ASN B 2 17 ? -5.769 32.416 18.829 1.00 32.05 ? 17 ASN B C 1 ATOM 2209 O O . ASN B 2 17 ? -6.674 31.966 18.128 1.00 32.46 ? 17 ASN B O 1 ATOM 2210 C CB . ASN B 2 17 ? -4.653 34.478 17.896 1.00 33.17 ? 17 ASN B CB 1 ATOM 2211 C CG . ASN B 2 17 ? -3.310 35.172 17.663 1.00 32.86 ? 17 ASN B CG 1 ATOM 2212 O OD1 . ASN B 2 17 ? -2.247 34.735 18.145 1.00 31.61 ? 17 ASN B OD1 1 ATOM 2213 N ND2 . ASN B 2 17 ? -3.354 36.267 16.913 1.00 34.35 ? 17 ASN B ND2 1 ATOM 2214 N N . GLY B 2 18 ? -5.786 32.372 20.156 1.00 32.19 ? 18 GLY B N 1 ATOM 2215 C CA . GLY B 2 18 ? -6.895 31.788 20.908 1.00 33.14 ? 18 GLY B CA 1 ATOM 2216 C C . GLY B 2 18 ? -6.969 30.269 20.936 1.00 32.55 ? 18 GLY B C 1 ATOM 2217 O O . GLY B 2 18 ? -7.886 29.724 21.552 1.00 33.44 ? 18 GLY B O 1 ATOM 2218 N N . LYS B 2 19 ? -6.022 29.571 20.298 1.00 31.34 ? 19 LYS B N 1 ATOM 2219 C CA . LYS B 2 19 ? -6.043 28.108 20.254 1.00 31.13 ? 19 LYS B CA 1 ATOM 2220 C C . LYS B 2 19 ? -4.935 27.491 21.116 1.00 29.60 ? 19 LYS B C 1 ATOM 2221 O O . LYS B 2 19 ? -3.758 27.832 20.948 1.00 28.11 ? 19 LYS B O 1 ATOM 2222 C CB . LYS B 2 19 ? -5.946 27.610 18.813 1.00 31.37 ? 19 LYS B CB 1 ATOM 2223 C CG . LYS B 2 19 ? -7.069 28.121 17.906 1.00 33.41 ? 19 LYS B CG 1 ATOM 2224 C CD . LYS B 2 19 ? -8.446 27.650 18.384 1.00 35.59 ? 19 LYS B CD 1 ATOM 2225 C CE . LYS B 2 19 ? -9.517 27.816 17.330 1.00 37.43 ? 19 LYS B CE 1 ATOM 2226 N NZ . LYS B 2 19 ? -10.755 27.092 17.734 1.00 39.42 ? 19 LYS B NZ 1 ATOM 2227 N N . PRO B 2 20 ? -5.306 26.584 22.053 1.00 29.69 ? 20 PRO B N 1 ATOM 2228 C CA . PRO B 2 20 ? -4.324 25.864 22.876 1.00 28.40 ? 20 PRO B CA 1 ATOM 2229 C C . PRO B 2 20 ? -3.234 25.158 22.063 1.00 26.48 ? 20 PRO B C 1 ATOM 2230 O O . PRO B 2 20 ? -3.520 24.562 21.033 1.00 26.63 ? 20 PRO B O 1 ATOM 2231 C CB . PRO B 2 20 ? -5.175 24.836 23.619 1.00 29.95 ? 20 PRO B CB 1 ATOM 2232 C CG . PRO B 2 20 ? -6.515 25.464 23.737 1.00 31.68 ? 20 PRO B CG 1 ATOM 2233 C CD . PRO B 2 20 ? -6.690 26.339 22.524 1.00 31.48 ? 20 PRO B CD 1 ATOM 2234 N N . ASN B 2 21 ? -2.002 25.251 22.544 1.00 24.67 ? 21 ASN B N 1 ATOM 2235 C CA . ASN B 2 21 ? -0.813 24.784 21.837 1.00 22.97 ? 21 ASN B CA 1 ATOM 2236 C C . ASN B 2 21 ? 0.179 24.411 22.934 1.00 22.30 ? 21 ASN B C 1 ATOM 2237 O O . ASN B 2 21 ? -0.159 24.476 24.135 1.00 22.54 ? 21 ASN B O 1 ATOM 2238 C CB . ASN B 2 21 ? -0.275 25.934 20.954 1.00 22.32 ? 21 ASN B CB 1 ATOM 2239 C CG . ASN B 2 21 ? 0.575 25.476 19.760 1.00 21.53 ? 21 ASN B CG 1 ATOM 2240 O OD1 . ASN B 2 21 ? 1.315 24.495 19.829 1.00 21.07 ? 21 ASN B OD1 1 ATOM 2241 N ND2 . ASN B 2 21 ? 0.497 26.229 18.660 1.00 21.45 ? 21 ASN B ND2 1 ATOM 2242 N N . ILE B 2 22 ? 1.385 24.023 22.519 1.00 20.97 ? 22 ILE B N 1 ATOM 2243 C CA . ILE B 2 22 ? 2.488 23.745 23.428 1.00 20.56 ? 22 ILE B CA 1 ATOM 2244 C C . ILE B 2 22 ? 3.737 24.495 22.949 1.00 19.59 ? 22 ILE B C 1 ATOM 2245 O O . ILE B 2 22 ? 4.075 24.477 21.747 1.00 18.94 ? 22 ILE B O 1 ATOM 2246 C CB . ILE B 2 22 ? 2.752 22.217 23.523 1.00 20.60 ? 22 ILE B CB 1 ATOM 2247 C CG1 . ILE B 2 22 ? 1.545 21.522 24.193 1.00 22.11 ? 22 ILE B CG1 1 ATOM 2248 C CG2 . ILE B 2 22 ? 4.040 21.945 24.296 1.00 19.87 ? 22 ILE B CG2 1 ATOM 2249 C CD1 . ILE B 2 22 ? 1.480 20.018 23.980 1.00 22.94 ? 22 ILE B CD1 1 ATOM 2250 N N . LEU B 2 23 ? 4.407 25.142 23.900 1.00 19.62 ? 23 LEU B N 1 ATOM 2251 C CA . LEU B 2 23 ? 5.621 25.922 23.638 1.00 19.34 ? 23 LEU B CA 1 ATOM 2252 C C . LEU B 2 23 ? 6.810 25.164 24.193 1.00 18.86 ? 23 LEU B C 1 ATOM 2253 O O . LEU B 2 23 ? 6.795 24.787 25.355 1.00 19.64 ? 23 LEU B O 1 ATOM 2254 C CB . LEU B 2 23 ? 5.547 27.306 24.298 1.00 20.15 ? 23 LEU B CB 1 ATOM 2255 C CG . LEU B 2 23 ? 6.668 28.284 23.892 1.00 19.96 ? 23 LEU B CG 1 ATOM 2256 C CD1 . LEU B 2 23 ? 6.620 28.560 22.397 1.00 19.90 ? 23 LEU B CD1 1 ATOM 2257 C CD2 . LEU B 2 23 ? 6.563 29.579 24.680 1.00 21.03 ? 23 LEU B CD2 1 ATOM 2258 N N . ASN B 2 24 ? 7.808 24.953 23.341 1.00 18.24 ? 24 ASN B N 1 ATOM 2259 C CA . ASN B 2 24 ? 9.029 24.227 23.649 1.00 17.99 ? 24 ASN B CA 1 ATOM 2260 C C . ASN B 2 24 ? 10.198 25.180 23.823 1.00 17.98 ? 24 ASN B C 1 ATOM 2261 O O . ASN B 2 24 ? 10.327 26.140 23.078 1.00 17.92 ? 24 ASN B O 1 ATOM 2262 C CB . ASN B 2 24 ? 9.364 23.267 22.506 1.00 17.79 ? 24 ASN B CB 1 ATOM 2263 C CG . ASN B 2 24 ? 8.318 22.182 22.326 1.00 18.46 ? 24 ASN B CG 1 ATOM 2264 O OD1 . ASN B 2 24 ? 7.746 21.696 23.305 1.00 19.16 ? 24 ASN B OD1 1 ATOM 2265 N ND2 . ASN B 2 24 ? 8.056 21.803 21.074 1.00 18.64 ? 24 ASN B ND2 1 ATOM 2266 N N . CYS B 2 25 ? 11.037 24.891 24.811 1.00 18.22 ? 25 CYS B N 1 ATOM 2267 C CA . CYS B 2 25 ? 12.291 25.566 24.999 1.00 18.47 ? 25 CYS B CA 1 ATOM 2268 C C . CYS B 2 25 ? 13.354 24.496 25.086 1.00 18.05 ? 25 CYS B C 1 ATOM 2269 O O . CYS B 2 25 ? 13.370 23.742 26.054 1.00 18.65 ? 25 CYS B O 1 ATOM 2270 C CB . CYS B 2 25 ? 12.278 26.399 26.269 1.00 19.59 ? 25 CYS B CB 1 ATOM 2271 S SG . CYS B 2 25 ? 13.897 27.154 26.514 1.00 20.54 ? 25 CYS B SG 1 ATOM 2272 N N . TYR B 2 26 ? 14.193 24.407 24.053 1.00 17.58 ? 26 TYR B N 1 ATOM 2273 C CA . TYR B 2 26 ? 15.208 23.361 23.933 1.00 17.41 ? 26 TYR B CA 1 ATOM 2274 C C . TYR B 2 26 ? 16.536 24.008 24.225 1.00 17.71 ? 26 TYR B C 1 ATOM 2275 O O . TYR B 2 26 ? 16.905 24.962 23.545 1.00 18.11 ? 26 TYR B O 1 ATOM 2276 C CB . TYR B 2 26 ? 15.199 22.762 22.521 1.00 17.33 ? 26 TYR B CB 1 ATOM 2277 C CG . TYR B 2 26 ? 16.107 21.558 22.327 1.00 17.82 ? 26 TYR B CG 1 ATOM 2278 C CD1 . TYR B 2 26 ? 16.124 20.514 23.252 1.00 18.11 ? 26 TYR B CD1 1 ATOM 2279 C CD2 . TYR B 2 26 ? 16.915 21.434 21.192 1.00 18.28 ? 26 TYR B CD2 1 ATOM 2280 C CE1 . TYR B 2 26 ? 16.925 19.397 23.064 1.00 18.64 ? 26 TYR B CE1 1 ATOM 2281 C CE2 . TYR B 2 26 ? 17.714 20.308 21.009 1.00 18.73 ? 26 TYR B CE2 1 ATOM 2282 C CZ . TYR B 2 26 ? 17.703 19.302 21.954 1.00 18.73 ? 26 TYR B CZ 1 ATOM 2283 O OH . TYR B 2 26 ? 18.481 18.182 21.810 1.00 20.35 ? 26 TYR B OH 1 ATOM 2284 N N . VAL B 2 27 ? 17.226 23.509 25.247 1.00 17.61 ? 27 VAL B N 1 ATOM 2285 C CA . VAL B 2 27 ? 18.464 24.101 25.715 1.00 18.42 ? 27 VAL B CA 1 ATOM 2286 C C . VAL B 2 27 ? 19.576 23.079 25.547 1.00 18.54 ? 27 VAL B C 1 ATOM 2287 O O . VAL B 2 27 ? 19.461 21.948 26.032 1.00 18.06 ? 27 VAL B O 1 ATOM 2288 C CB . VAL B 2 27 ? 18.344 24.565 27.176 1.00 18.97 ? 27 VAL B CB 1 ATOM 2289 C CG1 . VAL B 2 27 ? 19.586 25.335 27.616 1.00 19.80 ? 27 VAL B CG1 1 ATOM 2290 C CG2 . VAL B 2 27 ? 17.107 25.429 27.334 1.00 19.29 ? 27 VAL B CG2 1 ATOM 2291 N N . THR B 2 28 ? 20.654 23.495 24.888 1.00 18.87 ? 28 THR B N 1 ATOM 2292 C CA . THR B 2 28 ? 21.691 22.586 24.426 1.00 19.37 ? 28 THR B CA 1 ATOM 2293 C C . THR B 2 28 ? 23.076 23.158 24.654 1.00 20.47 ? 28 THR B C 1 ATOM 2294 O O . THR B 2 28 ? 23.230 24.351 24.957 1.00 20.87 ? 28 THR B O 1 ATOM 2295 C CB . THR B 2 28 ? 21.541 22.327 22.917 1.00 19.27 ? 28 THR B CB 1 ATOM 2296 O OG1 . THR B 2 28 ? 21.575 23.569 22.214 1.00 19.93 ? 28 THR B OG1 1 ATOM 2297 C CG2 . THR B 2 28 ? 20.229 21.635 22.611 1.00 18.69 ? 28 THR B CG2 1 ATOM 2298 N N . GLN B 2 29 ? 24.074 22.290 24.492 1.00 21.22 ? 29 GLN B N 1 ATOM 2299 C CA . GLN B 2 29 ? 25.475 22.671 24.386 1.00 22.82 ? 29 GLN B CA 1 ATOM 2300 C C . GLN B 2 29 ? 26.040 23.296 25.644 1.00 23.10 ? 29 GLN B C 1 ATOM 2301 O O . GLN B 2 29 ? 26.933 24.133 25.570 1.00 24.15 ? 29 GLN B O 1 ATOM 2302 C CB . GLN B 2 29 ? 25.724 23.581 23.163 1.00 24.21 ? 29 GLN B CB 1 ATOM 2303 C CG . GLN B 2 29 ? 25.583 22.853 21.833 1.00 25.28 ? 29 GLN B CG 1 ATOM 2304 C CD . GLN B 2 29 ? 26.709 21.844 21.569 1.00 26.88 ? 29 GLN B CD 1 ATOM 2305 O OE1 . GLN B 2 29 ? 27.858 22.034 21.976 1.00 28.55 ? 29 GLN B OE1 1 ATOM 2306 N NE2 . GLN B 2 29 ? 26.377 20.770 20.858 1.00 27.94 ? 29 GLN B NE2 1 ATOM 2307 N N . PHE B 2 30 ? 25.565 22.850 26.802 1.00 22.38 ? 30 PHE B N 1 ATOM 2308 C CA . PHE B 2 30 ? 26.020 23.428 28.057 1.00 22.79 ? 30 PHE B CA 1 ATOM 2309 C C . PHE B 2 30 ? 26.765 22.419 28.920 1.00 23.21 ? 30 PHE B C 1 ATOM 2310 O O . PHE B 2 30 ? 26.617 21.194 28.755 1.00 22.58 ? 30 PHE B O 1 ATOM 2311 C CB . PHE B 2 30 ? 24.888 24.114 28.820 1.00 22.55 ? 30 PHE B CB 1 ATOM 2312 C CG . PHE B 2 30 ? 23.768 23.209 29.231 1.00 21.75 ? 30 PHE B CG 1 ATOM 2313 C CD1 . PHE B 2 30 ? 22.680 23.008 28.394 1.00 20.78 ? 30 PHE B CD1 1 ATOM 2314 C CD2 . PHE B 2 30 ? 23.775 22.592 30.482 1.00 22.19 ? 30 PHE B CD2 1 ATOM 2315 C CE1 . PHE B 2 30 ? 21.638 22.181 28.779 1.00 20.62 ? 30 PHE B CE1 1 ATOM 2316 C CE2 . PHE B 2 30 ? 22.731 21.776 30.877 1.00 22.03 ? 30 PHE B CE2 1 ATOM 2317 C CZ . PHE B 2 30 ? 21.658 21.562 30.026 1.00 21.27 ? 30 PHE B CZ 1 ATOM 2318 N N . HIS B 2 31 ? 27.596 22.967 29.798 1.00 24.32 ? 31 HIS B N 1 ATOM 2319 C CA . HIS B 2 31 ? 28.358 22.215 30.794 1.00 25.32 ? 31 HIS B CA 1 ATOM 2320 C C . HIS B 2 31 ? 28.845 23.235 31.826 1.00 26.54 ? 31 HIS B C 1 ATOM 2321 O O . HIS B 2 31 ? 29.359 24.282 31.417 1.00 26.52 ? 31 HIS B O 1 ATOM 2322 C CB . HIS B 2 31 ? 29.581 21.530 30.173 1.00 25.84 ? 31 HIS B CB 1 ATOM 2323 C CG . HIS B 2 31 ? 30.370 20.739 31.165 1.00 27.09 ? 31 HIS B CG 1 ATOM 2324 N ND1 . HIS B 2 31 ? 30.198 19.386 31.338 1.00 27.12 ? 31 HIS B ND1 1 ATOM 2325 C CD2 . HIS B 2 31 ? 31.286 21.123 32.087 1.00 28.80 ? 31 HIS B CD2 1 ATOM 2326 C CE1 . HIS B 2 31 ? 30.983 18.963 32.309 1.00 28.24 ? 31 HIS B CE1 1 ATOM 2327 N NE2 . HIS B 2 31 ? 31.658 19.996 32.780 1.00 29.48 ? 31 HIS B NE2 1 ATOM 2328 N N . PRO B 2 32 ? 28.752 22.952 33.132 1.00 27.47 ? 32 PRO B N 1 ATOM 2329 C CA . PRO B 2 32 ? 28.271 21.684 33.727 1.00 27.19 ? 32 PRO B CA 1 ATOM 2330 C C . PRO B 2 32 ? 26.753 21.518 33.647 1.00 26.23 ? 32 PRO B C 1 ATOM 2331 O O . PRO B 2 32 ? 26.067 22.428 33.188 1.00 25.86 ? 32 PRO B O 1 ATOM 2332 C CB . PRO B 2 32 ? 28.761 21.780 35.187 1.00 28.91 ? 32 PRO B CB 1 ATOM 2333 C CG . PRO B 2 32 ? 28.883 23.237 35.453 1.00 29.83 ? 32 PRO B CG 1 ATOM 2334 C CD . PRO B 2 32 ? 29.240 23.896 34.152 1.00 29.06 ? 32 PRO B CD 1 ATOM 2335 N N . PRO B 2 33 ? 26.218 20.347 34.057 1.00 26.40 ? 33 PRO B N 1 ATOM 2336 C CA . PRO B 2 33 ? 24.779 20.131 33.809 1.00 25.72 ? 33 PRO B CA 1 ATOM 2337 C C . PRO B 2 33 ? 23.782 20.907 34.696 1.00 26.44 ? 33 PRO B C 1 ATOM 2338 O O . PRO B 2 33 ? 22.588 20.935 34.369 1.00 26.68 ? 33 PRO B O 1 ATOM 2339 C CB . PRO B 2 33 ? 24.603 18.625 34.014 1.00 25.85 ? 33 PRO B CB 1 ATOM 2340 C CG . PRO B 2 33 ? 25.722 18.216 34.907 1.00 27.08 ? 33 PRO B CG 1 ATOM 2341 C CD . PRO B 2 33 ? 26.858 19.168 34.669 1.00 27.24 ? 33 PRO B CD 1 ATOM 2342 N N A HIS B 2 34 ? 24.251 21.499 35.800 0.50 27.91 ? 34 HIS B N 1 ATOM 2343 N N B HIS B 2 34 ? 24.251 21.538 35.762 0.50 27.63 ? 34 HIS B N 1 ATOM 2344 C CA A HIS B 2 34 ? 23.389 22.304 36.677 0.50 28.76 ? 34 HIS B CA 1 ATOM 2345 C CA B HIS B 2 34 ? 23.387 22.291 36.663 0.50 28.35 ? 34 HIS B CA 1 ATOM 2346 C C A HIS B 2 34 ? 22.909 23.538 35.933 0.50 27.82 ? 34 HIS B C 1 ATOM 2347 C C B HIS B 2 34 ? 22.916 23.579 35.999 0.50 27.71 ? 34 HIS B C 1 ATOM 2348 O O A HIS B 2 34 ? 23.712 24.270 35.376 0.50 27.78 ? 34 HIS B O 1 ATOM 2349 O O B HIS B 2 34 ? 23.726 24.381 35.557 0.50 27.88 ? 34 HIS B O 1 ATOM 2350 C CB A HIS B 2 34 ? 24.115 22.746 37.946 0.50 30.93 ? 34 HIS B CB 1 ATOM 2351 C CB B HIS B 2 34 ? 24.170 22.536 37.935 0.50 30.19 ? 34 HIS B CB 1 ATOM 2352 C CG A HIS B 2 34 ? 23.311 23.695 38.786 0.50 32.31 ? 34 HIS B CG 1 ATOM 2353 C CG B HIS B 2 34 ? 24.938 21.330 38.360 0.50 30.61 ? 34 HIS B CG 1 ATOM 2354 N ND1 A HIS B 2 34 ? 22.393 23.268 39.720 0.50 33.42 ? 34 HIS B ND1 1 ATOM 2355 N ND1 B HIS B 2 34 ? 24.334 20.245 38.957 0.50 31.10 ? 34 HIS B ND1 1 ATOM 2356 C CD2 A HIS B 2 34 ? 23.263 25.048 38.804 0.50 32.95 ? 34 HIS B CD2 1 ATOM 2357 C CD2 B HIS B 2 34 ? 26.236 20.991 38.185 0.50 30.75 ? 34 HIS B CD2 1 ATOM 2358 C CE1 A HIS B 2 34 ? 21.824 24.316 40.289 0.50 34.57 ? 34 HIS B CE1 1 ATOM 2359 C CE1 B HIS B 2 34 ? 25.239 19.310 39.181 0.50 31.61 ? 34 HIS B CE1 1 ATOM 2360 N NE2 A HIS B 2 34 ? 22.335 25.409 39.751 0.50 34.35 ? 34 HIS B NE2 1 ATOM 2361 N NE2 B HIS B 2 34 ? 26.402 19.739 38.722 0.50 31.44 ? 34 HIS B NE2 1 ATOM 2362 N N . ILE B 2 35 ? 21.600 23.750 35.912 1.00 27.29 ? 35 ILE B N 1 ATOM 2363 C CA . ILE B 2 35 ? 21.001 24.821 35.105 1.00 26.63 ? 35 ILE B CA 1 ATOM 2364 C C . ILE B 2 35 ? 19.621 25.166 35.646 1.00 27.49 ? 35 ILE B C 1 ATOM 2365 O O . ILE B 2 35 ? 18.965 24.321 36.270 1.00 27.45 ? 35 ILE B O 1 ATOM 2366 C CB . ILE B 2 35 ? 20.935 24.393 33.612 1.00 24.66 ? 35 ILE B CB 1 ATOM 2367 C CG1 . ILE B 2 35 ? 20.674 25.588 32.686 1.00 24.03 ? 35 ILE B CG1 1 ATOM 2368 C CG2 . ILE B 2 35 ? 19.911 23.265 33.395 1.00 23.91 ? 35 ILE B CG2 1 ATOM 2369 C CD1 . ILE B 2 35 ? 21.166 25.344 31.284 1.00 23.08 ? 35 ILE B CD1 1 ATOM 2370 N N . GLU B 2 36 ? 19.195 26.410 35.430 1.00 28.15 ? 36 GLU B N 1 ATOM 2371 C CA . GLU B 2 36 ? 17.828 26.806 35.745 1.00 29.17 ? 36 GLU B CA 1 ATOM 2372 C C . GLU B 2 36 ? 17.174 27.302 34.482 1.00 27.75 ? 36 GLU B C 1 ATOM 2373 O O . GLU B 2 36 ? 17.717 28.172 33.808 1.00 27.05 ? 36 GLU B O 1 ATOM 2374 C CB . GLU B 2 36 ? 17.782 27.884 36.825 1.00 32.06 ? 36 GLU B CB 1 ATOM 2375 C CG . GLU B 2 36 ? 16.371 28.109 37.347 1.00 33.80 ? 36 GLU B CG 1 ATOM 2376 C CD . GLU B 2 36 ? 16.256 29.226 38.365 1.00 36.82 ? 36 GLU B CD 1 ATOM 2377 O OE1 . GLU B 2 36 ? 17.237 29.509 39.090 1.00 38.93 ? 36 GLU B OE1 1 ATOM 2378 O OE2 . GLU B 2 36 ? 15.152 29.810 38.445 1.00 38.27 ? 36 GLU B OE2 1 ATOM 2379 N N . ILE B 2 37 ? 15.997 26.755 34.179 1.00 27.04 ? 37 ILE B N 1 ATOM 2380 C CA . ILE B 2 37 ? 15.249 27.116 32.983 1.00 26.23 ? 37 ILE B CA 1 ATOM 2381 C C . ILE B 2 37 ? 13.857 27.576 33.412 1.00 27.40 ? 37 ILE B C 1 ATOM 2382 O O . ILE B 2 37 ? 13.166 26.879 34.161 1.00 27.53 ? 37 ILE B O 1 ATOM 2383 C CB . ILE B 2 37 ? 15.164 25.929 32.002 1.00 24.77 ? 37 ILE B CB 1 ATOM 2384 C CG1 . ILE B 2 37 ? 16.572 25.486 31.578 1.00 24.26 ? 37 ILE B CG1 1 ATOM 2385 C CG2 . ILE B 2 37 ? 14.343 26.297 30.771 1.00 23.95 ? 37 ILE B CG2 1 ATOM 2386 C CD1 . ILE B 2 37 ? 16.605 24.148 30.872 1.00 23.41 ? 37 ILE B CD1 1 ATOM 2387 N N . GLN B 2 38 ? 13.476 28.774 32.967 1.00 27.87 ? 38 GLN B N 1 ATOM 2388 C CA . GLN B 2 38 ? 12.161 29.341 33.258 1.00 29.20 ? 38 GLN B CA 1 ATOM 2389 C C . GLN B 2 38 ? 11.495 29.631 31.943 1.00 27.62 ? 38 GLN B C 1 ATOM 2390 O O . GLN B 2 38 ? 12.159 30.002 30.982 1.00 26.82 ? 38 GLN B O 1 ATOM 2391 C CB . GLN B 2 38 ? 12.286 30.666 34.000 1.00 31.79 ? 38 GLN B CB 1 ATOM 2392 C CG . GLN B 2 38 ? 12.962 30.589 35.356 1.00 34.29 ? 38 GLN B CG 1 ATOM 2393 C CD . GLN B 2 38 ? 13.439 31.939 35.850 1.00 37.13 ? 38 GLN B CD 1 ATOM 2394 O OE1 . GLN B 2 38 ? 13.212 32.979 35.214 1.00 38.46 ? 38 GLN B OE1 1 ATOM 2395 N NE2 . GLN B 2 38 ? 14.098 31.936 36.998 1.00 39.34 ? 38 GLN B NE2 1 ATOM 2396 N N . MET B 2 39 ? 10.183 29.467 31.896 1.00 27.15 ? 39 MET B N 1 ATOM 2397 C CA . MET B 2 39 ? 9.412 29.918 30.754 1.00 26.42 ? 39 MET B CA 1 ATOM 2398 C C . MET B 2 39 ? 8.526 31.029 31.265 1.00 27.58 ? 39 MET B C 1 ATOM 2399 O O . MET B 2 39 ? 8.001 30.947 32.378 1.00 28.83 ? 39 MET B O 1 ATOM 2400 C CB . MET B 2 39 ? 8.641 28.771 30.110 1.00 25.27 ? 39 MET B CB 1 ATOM 2401 C CG . MET B 2 39 ? 9.576 27.712 29.548 1.00 24.04 ? 39 MET B CG 1 ATOM 2402 S SD . MET B 2 39 ? 8.733 26.456 28.572 1.00 23.33 ? 39 MET B SD 1 ATOM 2403 C CE . MET B 2 39 ? 8.484 27.334 27.030 1.00 22.57 ? 39 MET B CE 1 ATOM 2404 N N . LEU B 2 40 ? 8.428 32.093 30.473 1.00 27.56 ? 40 LEU B N 1 ATOM 2405 C CA . LEU B 2 40 ? 7.821 33.342 30.907 1.00 29.38 ? 40 LEU B CA 1 ATOM 2406 C C . LEU B 2 40 ? 6.638 33.722 30.023 1.00 29.01 ? 40 LEU B C 1 ATOM 2407 O O . LEU B 2 40 ? 6.686 33.525 28.817 1.00 27.23 ? 40 LEU B O 1 ATOM 2408 C CB . LEU B 2 40 ? 8.863 34.467 30.882 1.00 30.54 ? 40 LEU B CB 1 ATOM 2409 C CG . LEU B 2 40 ? 10.210 34.200 31.563 1.00 30.88 ? 40 LEU B CG 1 ATOM 2410 C CD1 . LEU B 2 40 ? 11.121 35.424 31.476 1.00 32.43 ? 40 LEU B CD1 1 ATOM 2411 C CD2 . LEU B 2 40 ? 10.014 33.812 33.018 1.00 32.13 ? 40 LEU B CD2 1 ATOM 2412 N N . LYS B 2 41 ? 5.588 34.258 30.649 1.00 30.64 ? 41 LYS B N 1 ATOM 2413 C CA . LYS B 2 41 ? 4.439 34.856 29.965 1.00 31.21 ? 41 LYS B CA 1 ATOM 2414 C C . LYS B 2 41 ? 4.371 36.321 30.397 1.00 33.35 ? 41 LYS B C 1 ATOM 2415 O O . LYS B 2 41 ? 4.203 36.593 31.578 1.00 34.68 ? 41 LYS B O 1 ATOM 2416 C CB . LYS B 2 41 ? 3.148 34.135 30.360 1.00 31.82 ? 41 LYS B CB 1 ATOM 2417 C CG . LYS B 2 41 ? 1.887 34.746 29.766 1.00 32.98 ? 41 LYS B CG 1 ATOM 2418 C CD . LYS B 2 41 ? 0.665 33.865 29.978 1.00 33.61 ? 41 LYS B CD 1 ATOM 2419 C CE . LYS B 2 41 ? -0.579 34.547 29.440 1.00 35.13 ? 41 LYS B CE 1 ATOM 2420 N NZ . LYS B 2 41 ? -1.834 33.899 29.919 1.00 36.50 ? 41 LYS B NZ 1 ATOM 2421 N N . ASN B 2 42 ? 4.509 37.253 29.453 1.00 33.78 ? 42 ASN B N 1 ATOM 2422 C CA . ASN B 2 42 ? 4.577 38.703 29.767 1.00 36.22 ? 42 ASN B CA 1 ATOM 2423 C C . ASN B 2 42 ? 5.553 39.016 30.910 1.00 37.55 ? 42 ASN B C 1 ATOM 2424 O O . ASN B 2 42 ? 5.258 39.821 31.800 1.00 39.72 ? 42 ASN B O 1 ATOM 2425 C CB . ASN B 2 42 ? 3.179 39.262 30.066 1.00 37.96 ? 42 ASN B CB 1 ATOM 2426 C CG . ASN B 2 42 ? 2.183 38.967 28.957 1.00 37.04 ? 42 ASN B CG 1 ATOM 2427 O OD1 . ASN B 2 42 ? 2.518 39.042 27.775 1.00 36.11 ? 42 ASN B OD1 1 ATOM 2428 N ND2 . ASN B 2 42 ? 0.952 38.628 29.332 1.00 37.61 ? 42 ASN B ND2 1 ATOM 2429 N N . GLY B 2 43 ? 6.709 38.347 30.879 1.00 36.32 ? 43 GLY B N 1 ATOM 2430 C CA . GLY B 2 43 ? 7.743 38.495 31.900 1.00 37.72 ? 43 GLY B CA 1 ATOM 2431 C C . GLY B 2 43 ? 7.567 37.740 33.215 1.00 38.47 ? 43 GLY B C 1 ATOM 2432 O O . GLY B 2 43 ? 8.457 37.791 34.059 1.00 39.04 ? 43 GLY B O 1 ATOM 2433 N N . LYS B 2 44 ? 6.445 37.037 33.391 1.00 38.34 ? 44 LYS B N 1 ATOM 2434 C CA . LYS B 2 44 ? 6.099 36.390 34.657 1.00 39.70 ? 44 LYS B CA 1 ATOM 2435 C C . LYS B 2 44 ? 6.313 34.900 34.507 1.00 38.03 ? 44 LYS B C 1 ATOM 2436 O O . LYS B 2 44 ? 5.948 34.335 33.481 1.00 36.27 ? 44 LYS B O 1 ATOM 2437 C CB . LYS B 2 44 ? 4.636 36.652 35.014 1.00 41.15 ? 44 LYS B CB 1 ATOM 2438 N N . LYS B 2 45 ? 6.892 34.269 35.526 1.00 39.10 ? 45 LYS B N 1 ATOM 2439 C CA . LYS B 2 45 ? 7.201 32.835 35.482 1.00 38.15 ? 45 LYS B CA 1 ATOM 2440 C C . LYS B 2 45 ? 5.941 32.001 35.258 1.00 37.86 ? 45 LYS B C 1 ATOM 2441 O O . LYS B 2 45 ? 4.945 32.196 35.944 1.00 39.15 ? 45 LYS B O 1 ATOM 2442 C CB . LYS B 2 45 ? 7.881 32.389 36.774 1.00 39.94 ? 45 LYS B CB 1 ATOM 2443 C CG . LYS B 2 45 ? 9.330 32.826 36.872 1.00 40.47 ? 45 LYS B CG 1 ATOM 2444 C CD . LYS B 2 45 ? 9.803 32.877 38.317 1.00 43.32 ? 45 LYS B CD 1 ATOM 2445 C CE . LYS B 2 45 ? 11.296 32.619 38.414 1.00 43.03 ? 45 LYS B CE 1 ATOM 2446 N NZ . LYS B 2 45 ? 11.786 32.695 39.818 1.00 45.72 ? 45 LYS B NZ 1 ATOM 2447 N N . ILE B 2 46 ? 5.981 31.112 34.271 1.00 36.02 ? 46 ILE B N 1 ATOM 2448 C CA . ILE B 2 46 ? 4.902 30.152 34.047 1.00 36.09 ? 46 ILE B CA 1 ATOM 2449 C C . ILE B 2 46 ? 5.088 29.022 35.066 1.00 37.39 ? 46 ILE B C 1 ATOM 2450 O O . ILE B 2 46 ? 6.144 28.404 35.102 1.00 36.18 ? 46 ILE B O 1 ATOM 2451 C CB . ILE B 2 46 ? 4.916 29.607 32.601 1.00 33.98 ? 46 ILE B CB 1 ATOM 2452 C CG1 . ILE B 2 46 ? 4.663 30.755 31.614 1.00 33.52 ? 46 ILE B CG1 1 ATOM 2453 C CG2 . ILE B 2 46 ? 3.882 28.484 32.422 1.00 33.86 ? 46 ILE B CG2 1 ATOM 2454 C CD1 . ILE B 2 46 ? 4.782 30.386 30.152 1.00 31.79 ? 46 ILE B CD1 1 ATOM 2455 N N . PRO B 2 47 ? 4.068 28.748 35.898 1.00 40.59 ? 47 PRO B N 1 ATOM 2456 C CA . PRO B 2 47 ? 4.296 27.818 37.011 1.00 42.54 ? 47 PRO B CA 1 ATOM 2457 C C . PRO B 2 47 ? 4.488 26.335 36.640 1.00 42.29 ? 47 PRO B C 1 ATOM 2458 O O . PRO B 2 47 ? 5.321 25.676 37.260 1.00 43.77 ? 47 PRO B O 1 ATOM 2459 C CB . PRO B 2 47 ? 3.050 28.006 37.889 1.00 44.84 ? 47 PRO B CB 1 ATOM 2460 C CG . PRO B 2 47 ? 1.993 28.471 36.955 1.00 44.26 ? 47 PRO B CG 1 ATOM 2461 C CD . PRO B 2 47 ? 2.679 29.248 35.869 1.00 42.06 ? 47 PRO B CD 1 ATOM 2462 N N . LYS B 2 48 ? 3.758 25.810 35.655 1.00 41.70 ? 48 LYS B N 1 ATOM 2463 C CA . LYS B 2 48 ? 3.656 24.339 35.485 1.00 41.98 ? 48 LYS B CA 1 ATOM 2464 C C . LYS B 2 48 ? 4.568 23.723 34.407 1.00 39.94 ? 48 LYS B C 1 ATOM 2465 O O . LYS B 2 48 ? 4.172 22.764 33.729 1.00 41.13 ? 48 LYS B O 1 ATOM 2466 C CB . LYS B 2 48 ? 2.199 23.949 35.207 1.00 42.81 ? 48 LYS B CB 1 ATOM 2467 N N . VAL B 2 49 ? 5.789 24.232 34.272 1.00 37.76 ? 49 VAL B N 1 ATOM 2468 C CA . VAL B 2 49 ? 6.658 23.836 33.164 1.00 35.09 ? 49 VAL B CA 1 ATOM 2469 C C . VAL B 2 49 ? 7.182 22.405 33.376 1.00 34.59 ? 49 VAL B C 1 ATOM 2470 O O . VAL B 2 49 ? 7.666 22.072 34.456 1.00 35.54 ? 49 VAL B O 1 ATOM 2471 C CB . VAL B 2 49 ? 7.811 24.839 32.981 1.00 33.92 ? 49 VAL B CB 1 ATOM 2472 C CG1 . VAL B 2 49 ? 8.759 24.376 31.886 1.00 32.20 ? 49 VAL B CG1 1 ATOM 2473 C CG2 . VAL B 2 49 ? 7.239 26.213 32.652 1.00 34.01 ? 49 VAL B CG2 1 ATOM 2474 N N . GLU B 2 50 ? 7.042 21.567 32.350 1.00 32.98 ? 50 GLU B N 1 ATOM 2475 C CA . GLU B 2 50 ? 7.501 20.176 32.392 1.00 32.94 ? 50 GLU B CA 1 ATOM 2476 C C . GLU B 2 50 ? 8.873 20.118 31.734 1.00 30.83 ? 50 GLU B C 1 ATOM 2477 O O . GLU B 2 50 ? 9.100 20.777 30.712 1.00 28.58 ? 50 GLU B O 1 ATOM 2478 C CB . GLU B 2 50 ? 6.517 19.254 31.659 1.00 33.61 ? 50 GLU B CB 1 ATOM 2479 C CG . GLU B 2 50 ? 5.208 18.976 32.398 1.00 36.50 ? 50 GLU B CG 1 ATOM 2480 C CD . GLU B 2 50 ? 5.359 18.054 33.616 1.00 39.14 ? 50 GLU B CD 1 ATOM 2481 O OE1 . GLU B 2 50 ? 4.516 18.140 34.542 1.00 42.10 ? 50 GLU B OE1 1 ATOM 2482 O OE2 . GLU B 2 50 ? 6.311 17.237 33.665 1.00 39.64 ? 50 GLU B OE2 1 ATOM 2483 N N . MET B 2 51 ? 9.781 19.355 32.336 1.00 30.68 ? 51 MET B N 1 ATOM 2484 C CA . MET B 2 51 ? 11.160 19.193 31.836 1.00 29.80 ? 51 MET B CA 1 ATOM 2485 C C . MET B 2 51 ? 11.387 17.736 31.480 1.00 28.62 ? 51 MET B C 1 ATOM 2486 O O . MET B 2 51 ? 11.014 16.851 32.247 1.00 29.56 ? 51 MET B O 1 ATOM 2487 C CB . MET B 2 51 ? 12.182 19.524 32.930 1.00 31.63 ? 51 MET B CB 1 ATOM 2488 C CG . MET B 2 51 ? 12.015 20.879 33.584 1.00 33.46 ? 51 MET B CG 1 ATOM 2489 S SD . MET B 2 51 ? 12.690 22.173 32.539 1.00 33.55 ? 51 MET B SD 1 ATOM 2490 C CE . MET B 2 51 ? 12.045 23.598 33.410 1.00 34.79 ? 51 MET B CE 1 ATOM 2491 N N . SER B 2 52 ? 12.035 17.486 30.354 1.00 26.73 ? 52 SER B N 1 ATOM 2492 C CA . SER B 2 52 ? 12.570 16.159 30.064 1.00 26.50 ? 52 SER B CA 1 ATOM 2493 C C . SER B 2 52 ? 13.692 15.827 31.049 1.00 26.63 ? 52 SER B C 1 ATOM 2494 O O . SER B 2 52 ? 14.168 16.695 31.786 1.00 26.33 ? 52 SER B O 1 ATOM 2495 C CB . SER B 2 52 ? 13.129 16.110 28.637 1.00 25.40 ? 52 SER B CB 1 ATOM 2496 O OG . SER B 2 52 ? 14.316 16.889 28.524 1.00 24.42 ? 52 SER B OG 1 ATOM 2497 N N . ASP B 2 53 ? 14.132 14.577 31.031 1.00 27.04 ? 53 ASP B N 1 ATOM 2498 C CA . ASP B 2 53 ? 15.313 14.170 31.793 1.00 27.63 ? 53 ASP B CA 1 ATOM 2499 C C . ASP B 2 53 ? 16.540 14.796 31.160 1.00 26.64 ? 53 ASP B C 1 ATOM 2500 O O . ASP B 2 53 ? 16.603 14.911 29.951 1.00 26.36 ? 53 ASP B O 1 ATOM 2501 C CB . ASP B 2 53 ? 15.468 12.660 31.786 1.00 28.66 ? 53 ASP B CB 1 ATOM 2502 C CG . ASP B 2 53 ? 14.345 11.970 32.487 1.00 30.35 ? 53 ASP B CG 1 ATOM 2503 O OD1 . ASP B 2 53 ? 13.939 12.456 33.562 1.00 31.16 ? 53 ASP B OD1 1 ATOM 2504 O OD2 . ASP B 2 53 ? 13.871 10.935 31.975 1.00 30.93 ? 53 ASP B OD2 1 ATOM 2505 N N . MET B 2 54 ? 17.478 15.242 31.988 1.00 26.90 ? 54 MET B N 1 ATOM 2506 C CA . MET B 2 54 ? 18.763 15.722 31.514 1.00 26.32 ? 54 MET B CA 1 ATOM 2507 C C . MET B 2 54 ? 19.411 14.614 30.688 1.00 25.20 ? 54 MET B C 1 ATOM 2508 O O . MET B 2 54 ? 19.376 13.445 31.081 1.00 25.69 ? 54 MET B O 1 ATOM 2509 C CB . MET B 2 54 ? 19.637 16.072 32.722 1.00 28.48 ? 54 MET B CB 1 ATOM 2510 C CG . MET B 2 54 ? 21.029 16.603 32.417 1.00 29.22 ? 54 MET B CG 1 ATOM 2511 S SD . MET B 2 54 ? 20.968 18.233 31.682 1.00 30.17 ? 54 MET B SD 1 ATOM 2512 C CE . MET B 2 54 ? 20.385 19.241 33.049 1.00 30.52 ? 54 MET B CE 1 ATOM 2513 N N . SER B 2 55 ? 19.979 14.968 29.541 1.00 23.33 ? 55 SER B N 1 ATOM 2514 C CA . SER B 2 55 ? 20.754 14.001 28.759 1.00 23.24 ? 55 SER B CA 1 ATOM 2515 C C . SER B 2 55 ? 21.980 14.689 28.160 1.00 22.34 ? 55 SER B C 1 ATOM 2516 O O . SER B 2 55 ? 22.188 15.890 28.369 1.00 21.26 ? 55 SER B O 1 ATOM 2517 C CB . SER B 2 55 ? 19.856 13.353 27.699 1.00 23.26 ? 55 SER B CB 1 ATOM 2518 O OG . SER B 2 55 ? 20.464 12.236 27.096 1.00 23.94 ? 55 SER B OG 1 ATOM 2519 N N . PHE B 2 56 ? 22.812 13.923 27.465 1.00 22.32 ? 56 PHE B N 1 ATOM 2520 C CA . PHE B 2 56 ? 23.926 14.514 26.752 1.00 22.09 ? 56 PHE B CA 1 ATOM 2521 C C . PHE B 2 56 ? 24.163 13.867 25.402 1.00 22.99 ? 56 PHE B C 1 ATOM 2522 O O . PHE B 2 56 ? 23.686 12.762 25.131 1.00 23.21 ? 56 PHE B O 1 ATOM 2523 C CB . PHE B 2 56 ? 25.198 14.566 27.614 1.00 22.21 ? 56 PHE B CB 1 ATOM 2524 C CG . PHE B 2 56 ? 25.759 13.219 28.008 1.00 22.95 ? 56 PHE B CG 1 ATOM 2525 C CD1 . PHE B 2 56 ? 26.594 12.508 27.151 1.00 23.45 ? 56 PHE B CD1 1 ATOM 2526 C CD2 . PHE B 2 56 ? 25.501 12.690 29.274 1.00 23.58 ? 56 PHE B CD2 1 ATOM 2527 C CE1 . PHE B 2 56 ? 27.135 11.278 27.536 1.00 24.70 ? 56 PHE B CE1 1 ATOM 2528 C CE2 . PHE B 2 56 ? 26.042 11.476 29.664 1.00 24.64 ? 56 PHE B CE2 1 ATOM 2529 C CZ . PHE B 2 56 ? 26.854 10.763 28.796 1.00 25.24 ? 56 PHE B CZ 1 ATOM 2530 N N . SER B 2 57 ? 24.868 14.607 24.546 1.00 23.49 ? 57 SER B N 1 ATOM 2531 C CA . SER B 2 57 ? 25.063 14.256 23.149 1.00 24.66 ? 57 SER B CA 1 ATOM 2532 C C . SER B 2 57 ? 26.396 13.545 22.971 1.00 25.92 ? 57 SER B C 1 ATOM 2533 O O . SER B 2 57 ? 27.179 13.424 23.907 1.00 26.02 ? 57 SER B O 1 ATOM 2534 C CB . SER B 2 57 ? 25.023 15.518 22.268 1.00 24.74 ? 57 SER B CB 1 ATOM 2535 O OG . SER B 2 57 ? 23.775 16.191 22.391 1.00 25.08 ? 57 SER B OG 1 ATOM 2536 N N . LYS B 2 58 ? 26.646 13.080 21.752 1.00 27.03 ? 58 LYS B N 1 ATOM 2537 C CA . LYS B 2 58 ? 27.897 12.413 21.387 1.00 28.88 ? 58 LYS B CA 1 ATOM 2538 C C . LYS B 2 58 ? 29.133 13.248 21.745 1.00 28.36 ? 58 LYS B C 1 ATOM 2539 O O . LYS B 2 58 ? 30.147 12.700 22.178 1.00 29.21 ? 58 LYS B O 1 ATOM 2540 C CB . LYS B 2 58 ? 27.868 12.082 19.888 1.00 30.68 ? 58 LYS B CB 1 ATOM 2541 C CG . LYS B 2 58 ? 28.917 11.106 19.398 1.00 33.24 ? 58 LYS B CG 1 ATOM 2542 C CD . LYS B 2 58 ? 28.458 10.493 18.075 1.00 35.03 ? 58 LYS B CD 1 ATOM 2543 C CE . LYS B 2 58 ? 29.587 9.804 17.332 1.00 37.77 ? 58 LYS B CE 1 ATOM 2544 N NZ . LYS B 2 58 ? 29.137 9.435 15.953 1.00 39.56 ? 58 LYS B NZ 1 ATOM 2545 N N . ASP B 2 59 ? 29.023 14.572 21.622 1.00 27.06 ? 59 ASP B N 1 ATOM 2546 C CA . ASP B 2 59 ? 30.112 15.486 21.999 1.00 26.99 ? 59 ASP B CA 1 ATOM 2547 C C . ASP B 2 59 ? 30.199 15.803 23.513 1.00 25.86 ? 59 ASP B C 1 ATOM 2548 O O . ASP B 2 59 ? 30.986 16.660 23.915 1.00 25.50 ? 59 ASP B O 1 ATOM 2549 C CB . ASP B 2 59 ? 30.041 16.779 21.163 1.00 27.16 ? 59 ASP B CB 1 ATOM 2550 C CG . ASP B 2 59 ? 28.941 17.752 21.627 1.00 26.31 ? 59 ASP B CG 1 ATOM 2551 O OD1 . ASP B 2 59 ? 28.243 17.518 22.643 1.00 25.02 ? 59 ASP B OD1 1 ATOM 2552 O OD2 . ASP B 2 59 ? 28.787 18.786 20.945 1.00 26.62 ? 59 ASP B OD2 1 ATOM 2553 N N . TRP B 2 60 ? 29.377 15.123 24.324 1.00 24.61 ? 60 TRP B N 1 ATOM 2554 C CA . TRP B 2 60 ? 29.367 15.204 25.800 1.00 24.14 ? 60 TRP B CA 1 ATOM 2555 C C . TRP B 2 60 ? 28.611 16.388 26.410 1.00 23.22 ? 60 TRP B C 1 ATOM 2556 O O . TRP B 2 60 ? 28.372 16.408 27.618 1.00 23.26 ? 60 TRP B O 1 ATOM 2557 C CB . TRP B 2 60 ? 30.765 15.094 26.420 1.00 25.01 ? 60 TRP B CB 1 ATOM 2558 C CG . TRP B 2 60 ? 31.510 13.889 25.998 1.00 25.86 ? 60 TRP B CG 1 ATOM 2559 C CD1 . TRP B 2 60 ? 32.440 13.802 25.010 1.00 26.63 ? 60 TRP B CD1 1 ATOM 2560 C CD2 . TRP B 2 60 ? 31.396 12.576 26.566 1.00 26.29 ? 60 TRP B CD2 1 ATOM 2561 N NE1 . TRP B 2 60 ? 32.913 12.512 24.916 1.00 27.68 ? 60 TRP B NE1 1 ATOM 2562 C CE2 . TRP B 2 60 ? 32.287 11.738 25.858 1.00 27.42 ? 60 TRP B CE2 1 ATOM 2563 C CE3 . TRP B 2 60 ? 30.619 12.030 27.597 1.00 26.04 ? 60 TRP B CE3 1 ATOM 2564 C CZ2 . TRP B 2 60 ? 32.439 10.372 26.156 1.00 28.47 ? 60 TRP B CZ2 1 ATOM 2565 C CZ3 . TRP B 2 60 ? 30.768 10.662 27.898 1.00 27.13 ? 60 TRP B CZ3 1 ATOM 2566 C CH2 . TRP B 2 60 ? 31.672 9.855 27.172 1.00 28.25 ? 60 TRP B CH2 1 ATOM 2567 N N . SER B 2 61 ? 28.211 17.348 25.589 1.00 22.75 ? 61 SER B N 1 ATOM 2568 C CA . SER B 2 61 ? 27.474 18.498 26.065 1.00 22.29 ? 61 SER B CA 1 ATOM 2569 C C . SER B 2 61 ? 26.035 18.108 26.404 1.00 21.39 ? 61 SER B C 1 ATOM 2570 O O . SER B 2 61 ? 25.435 17.230 25.763 1.00 21.22 ? 61 SER B O 1 ATOM 2571 C CB . SER B 2 61 ? 27.512 19.635 25.026 1.00 22.34 ? 61 SER B CB 1 ATOM 2572 O OG . SER B 2 61 ? 26.741 19.320 23.872 1.00 22.21 ? 61 SER B OG 1 ATOM 2573 N N . PHE B 2 62 ? 25.485 18.781 27.405 1.00 20.93 ? 62 PHE B N 1 ATOM 2574 C CA . PHE B 2 62 ? 24.167 18.460 27.920 1.00 20.60 ? 62 PHE B CA 1 ATOM 2575 C C . PHE B 2 62 ? 23.039 19.145 27.156 1.00 20.24 ? 62 PHE B C 1 ATOM 2576 O O . PHE B 2 62 ? 23.229 20.209 26.535 1.00 19.76 ? 62 PHE B O 1 ATOM 2577 C CB . PHE B 2 62 ? 24.088 18.830 29.400 1.00 21.01 ? 62 PHE B CB 1 ATOM 2578 C CG . PHE B 2 62 ? 24.960 17.975 30.280 1.00 21.78 ? 62 PHE B CG 1 ATOM 2579 C CD1 . PHE B 2 62 ? 24.487 16.775 30.776 1.00 21.99 ? 62 PHE B CD1 1 ATOM 2580 C CD2 . PHE B 2 62 ? 26.258 18.367 30.609 1.00 22.28 ? 62 PHE B CD2 1 ATOM 2581 C CE1 . PHE B 2 62 ? 25.284 15.979 31.584 1.00 23.07 ? 62 PHE B CE1 1 ATOM 2582 C CE2 . PHE B 2 62 ? 27.059 17.577 31.412 1.00 23.34 ? 62 PHE B CE2 1 ATOM 2583 C CZ . PHE B 2 62 ? 26.569 16.380 31.914 1.00 23.77 ? 62 PHE B CZ 1 ATOM 2584 N N . TYR B 2 63 ? 21.868 18.518 27.207 1.00 20.09 ? 63 TYR B N 1 ATOM 2585 C CA . TYR B 2 63 ? 20.651 19.107 26.673 1.00 19.97 ? 63 TYR B CA 1 ATOM 2586 C C . TYR B 2 63 ? 19.434 18.705 27.489 1.00 20.13 ? 63 TYR B C 1 ATOM 2587 O O . TYR B 2 63 ? 19.408 17.659 28.156 1.00 20.32 ? 63 TYR B O 1 ATOM 2588 C CB . TYR B 2 63 ? 20.449 18.757 25.193 1.00 20.17 ? 63 TYR B CB 1 ATOM 2589 C CG . TYR B 2 63 ? 20.259 17.282 24.902 1.00 21.13 ? 63 TYR B CG 1 ATOM 2590 C CD1 . TYR B 2 63 ? 18.990 16.695 24.946 1.00 21.68 ? 63 TYR B CD1 1 ATOM 2591 C CD2 . TYR B 2 63 ? 21.349 16.473 24.584 1.00 22.28 ? 63 TYR B CD2 1 ATOM 2592 C CE1 . TYR B 2 63 ? 18.822 15.340 24.672 1.00 23.04 ? 63 TYR B CE1 1 ATOM 2593 C CE2 . TYR B 2 63 ? 21.191 15.115 24.326 1.00 23.33 ? 63 TYR B CE2 1 ATOM 2594 C CZ . TYR B 2 63 ? 19.931 14.554 24.370 1.00 23.75 ? 63 TYR B CZ 1 ATOM 2595 O OH . TYR B 2 63 ? 19.796 13.200 24.114 1.00 26.20 ? 63 TYR B OH 1 ATOM 2596 N N . ILE B 2 64 ? 18.413 19.542 27.394 1.00 19.97 ? 64 ILE B N 1 ATOM 2597 C CA . ILE B 2 64 ? 17.171 19.316 28.096 1.00 20.11 ? 64 ILE B CA 1 ATOM 2598 C C . ILE B 2 64 ? 16.074 20.095 27.354 1.00 19.45 ? 64 ILE B C 1 ATOM 2599 O O . ILE B 2 64 ? 16.351 21.145 26.726 1.00 18.42 ? 64 ILE B O 1 ATOM 2600 C CB . ILE B 2 64 ? 17.328 19.715 29.584 1.00 21.38 ? 64 ILE B CB 1 ATOM 2601 C CG1 . ILE B 2 64 ? 16.129 19.248 30.414 1.00 22.37 ? 64 ILE B CG1 1 ATOM 2602 C CG2 . ILE B 2 64 ? 17.578 21.203 29.732 1.00 21.48 ? 64 ILE B CG2 1 ATOM 2603 C CD1 . ILE B 2 64 ? 16.433 19.137 31.894 1.00 23.72 ? 64 ILE B CD1 1 ATOM 2604 N N . LEU B 2 65 ? 14.864 19.535 27.371 1.00 19.56 ? 65 LEU B N 1 ATOM 2605 C CA . LEU B 2 65 ? 13.681 20.171 26.778 1.00 19.40 ? 65 LEU B CA 1 ATOM 2606 C C . LEU B 2 65 ? 12.725 20.591 27.877 1.00 19.95 ? 65 LEU B C 1 ATOM 2607 O O . LEU B 2 65 ? 12.311 19.762 28.678 1.00 20.63 ? 65 LEU B O 1 ATOM 2608 C CB . LEU B 2 65 ? 12.959 19.185 25.860 1.00 19.55 ? 65 LEU B CB 1 ATOM 2609 C CG . LEU B 2 65 ? 11.710 19.679 25.134 1.00 19.32 ? 65 LEU B CG 1 ATOM 2610 C CD1 . LEU B 2 65 ? 12.049 20.811 24.180 1.00 18.82 ? 65 LEU B CD1 1 ATOM 2611 C CD2 . LEU B 2 65 ? 11.049 18.538 24.404 1.00 19.73 ? 65 LEU B CD2 1 ATOM 2612 N N . ALA B 2 66 ? 12.355 21.869 27.891 1.00 19.76 ? 66 ALA B N 1 ATOM 2613 C CA . ALA B 2 66 ? 11.250 22.338 28.720 1.00 20.52 ? 66 ALA B CA 1 ATOM 2614 C C . ALA B 2 66 ? 10.068 22.524 27.792 1.00 20.28 ? 66 ALA B C 1 ATOM 2615 O O . ALA B 2 66 ? 10.249 22.888 26.636 1.00 19.50 ? 66 ALA B O 1 ATOM 2616 C CB . ALA B 2 66 ? 11.604 23.649 29.399 1.00 20.88 ? 66 ALA B CB 1 ATOM 2617 N N . HIS B 2 67 ? 8.858 22.303 28.295 1.00 21.40 ? 67 HIS B N 1 ATOM 2618 C CA . HIS B 2 67 ? 7.656 22.641 27.520 1.00 21.41 ? 67 HIS B CA 1 ATOM 2619 C C . HIS B 2 67 ? 6.488 22.990 28.425 1.00 22.84 ? 67 HIS B C 1 ATOM 2620 O O . HIS B 2 67 ? 6.403 22.528 29.561 1.00 23.71 ? 67 HIS B O 1 ATOM 2621 C CB . HIS B 2 67 ? 7.272 21.519 26.544 1.00 21.47 ? 67 HIS B CB 1 ATOM 2622 C CG . HIS B 2 67 ? 6.613 20.344 27.196 1.00 22.61 ? 67 HIS B CG 1 ATOM 2623 N ND1 . HIS B 2 67 ? 7.327 19.346 27.818 1.00 23.11 ? 67 HIS B ND1 1 ATOM 2624 C CD2 . HIS B 2 67 ? 5.307 20.018 27.340 1.00 24.04 ? 67 HIS B CD2 1 ATOM 2625 C CE1 . HIS B 2 67 ? 6.493 18.449 28.311 1.00 24.39 ? 67 HIS B CE1 1 ATOM 2626 N NE2 . HIS B 2 67 ? 5.259 18.832 28.034 1.00 25.00 ? 67 HIS B NE2 1 ATOM 2627 N N . THR B 2 68 ? 5.576 23.797 27.898 1.00 23.10 ? 68 THR B N 1 ATOM 2628 C CA . THR B 2 68 ? 4.392 24.189 28.641 1.00 24.73 ? 68 THR B CA 1 ATOM 2629 C C . THR B 2 68 ? 3.213 24.369 27.703 1.00 25.19 ? 68 THR B C 1 ATOM 2630 O O . THR B 2 68 ? 3.388 24.670 26.525 1.00 24.08 ? 68 THR B O 1 ATOM 2631 C CB . THR B 2 68 ? 4.654 25.489 29.436 1.00 25.42 ? 68 THR B CB 1 ATOM 2632 O OG1 . THR B 2 68 ? 3.553 25.735 30.314 1.00 27.15 ? 68 THR B OG1 1 ATOM 2633 C CG2 . THR B 2 68 ? 4.858 26.700 28.496 1.00 24.80 ? 68 THR B CG2 1 ATOM 2634 N N . GLU B 2 69 ? 2.014 24.158 28.229 1.00 27.25 ? 69 GLU B N 1 ATOM 2635 C CA . GLU B 2 69 ? 0.797 24.494 27.510 1.00 28.64 ? 69 GLU B CA 1 ATOM 2636 C C . GLU B 2 69 ? 0.725 26.013 27.398 1.00 28.64 ? 69 GLU B C 1 ATOM 2637 O O . GLU B 2 69 ? 1.060 26.728 28.354 1.00 29.71 ? 69 GLU B O 1 ATOM 2638 C CB . GLU B 2 69 ? -0.433 23.950 28.240 1.00 31.30 ? 69 GLU B CB 1 ATOM 2639 C CG . GLU B 2 69 ? -0.479 22.428 28.268 1.00 32.75 ? 69 GLU B CG 1 ATOM 2640 C CD . GLU B 2 69 ? -1.619 21.860 29.089 1.00 35.85 ? 69 GLU B CD 1 ATOM 2641 O OE1 . GLU B 2 69 ? -2.044 22.491 30.094 1.00 38.19 ? 69 GLU B OE1 1 ATOM 2642 O OE2 . GLU B 2 69 ? -2.099 20.761 28.723 1.00 37.25 ? 69 GLU B OE2 1 ATOM 2643 N N . PHE B 2 70 ? 0.356 26.507 26.222 1.00 27.79 ? 70 PHE B N 1 ATOM 2644 C CA . PHE B 2 70 ? 0.128 27.931 26.032 1.00 28.06 ? 70 PHE B CA 1 ATOM 2645 C C . PHE B 2 70 ? -0.895 28.172 24.935 1.00 28.73 ? 70 PHE B C 1 ATOM 2646 O O . PHE B 2 70 ? -1.093 27.343 24.029 1.00 27.59 ? 70 PHE B O 1 ATOM 2647 C CB . PHE B 2 70 ? 1.437 28.712 25.785 1.00 27.02 ? 70 PHE B CB 1 ATOM 2648 C CG . PHE B 2 70 ? 1.891 28.772 24.342 1.00 25.85 ? 70 PHE B CG 1 ATOM 2649 C CD1 . PHE B 2 70 ? 2.053 27.615 23.577 1.00 24.78 ? 70 PHE B CD1 1 ATOM 2650 C CD2 . PHE B 2 70 ? 2.219 30.000 23.757 1.00 25.79 ? 70 PHE B CD2 1 ATOM 2651 C CE1 . PHE B 2 70 ? 2.497 27.687 22.259 1.00 24.00 ? 70 PHE B CE1 1 ATOM 2652 C CE2 . PHE B 2 70 ? 2.664 30.073 22.444 1.00 24.99 ? 70 PHE B CE2 1 ATOM 2653 C CZ . PHE B 2 70 ? 2.799 28.918 21.690 1.00 24.42 ? 70 PHE B CZ 1 ATOM 2654 N N . THR B 2 71 ? -1.549 29.318 25.056 1.00 30.10 ? 71 THR B N 1 ATOM 2655 C CA . THR B 2 71 ? -2.552 29.754 24.112 1.00 30.97 ? 71 THR B CA 1 ATOM 2656 C C . THR B 2 71 ? -2.072 31.105 23.613 1.00 31.11 ? 71 THR B C 1 ATOM 2657 O O . THR B 2 71 ? -2.227 32.103 24.316 1.00 32.69 ? 71 THR B O 1 ATOM 2658 C CB . THR B 2 71 ? -3.926 29.853 24.781 1.00 32.78 ? 71 THR B CB 1 ATOM 2659 O OG1 . THR B 2 71 ? -4.321 28.551 25.236 1.00 32.95 ? 71 THR B OG1 1 ATOM 2660 C CG2 . THR B 2 71 ? -4.968 30.372 23.798 1.00 33.80 ? 71 THR B CG2 1 ATOM 2661 N N . PRO B 2 72 ? -1.463 31.142 22.411 1.00 29.98 ? 72 PRO B N 1 ATOM 2662 C CA . PRO B 2 72 ? -0.975 32.431 21.929 1.00 30.27 ? 72 PRO B CA 1 ATOM 2663 C C . PRO B 2 72 ? -2.113 33.400 21.621 1.00 31.75 ? 72 PRO B C 1 ATOM 2664 O O . PRO B 2 72 ? -3.227 32.969 21.304 1.00 31.99 ? 72 PRO B O 1 ATOM 2665 C CB . PRO B 2 72 ? -0.221 32.075 20.650 1.00 29.30 ? 72 PRO B CB 1 ATOM 2666 C CG . PRO B 2 72 ? -0.765 30.764 20.209 1.00 28.89 ? 72 PRO B CG 1 ATOM 2667 C CD . PRO B 2 72 ? -1.217 30.054 21.444 1.00 29.00 ? 72 PRO B CD 1 ATOM 2668 N N . THR B 2 73 ? -1.815 34.688 21.742 1.00 32.76 ? 73 THR B N 1 ATOM 2669 C CA . THR B 2 73 ? -2.732 35.771 21.403 1.00 34.70 ? 73 THR B CA 1 ATOM 2670 C C . THR B 2 73 ? -1.956 36.821 20.604 1.00 35.45 ? 73 THR B C 1 ATOM 2671 O O . THR B 2 73 ? -0.748 36.689 20.405 1.00 34.38 ? 73 THR B O 1 ATOM 2672 C CB . THR B 2 73 ? -3.287 36.439 22.672 1.00 36.45 ? 73 THR B CB 1 ATOM 2673 O OG1 . THR B 2 73 ? -2.205 37.003 23.424 1.00 36.60 ? 73 THR B OG1 1 ATOM 2674 C CG2 . THR B 2 73 ? -4.046 35.439 23.535 1.00 36.39 ? 73 THR B CG2 1 ATOM 2675 N N . GLU B 2 74 ? -2.641 37.868 20.154 1.00 37.44 ? 74 GLU B N 1 ATOM 2676 C CA . GLU B 2 74 ? -1.956 38.975 19.490 1.00 38.70 ? 74 GLU B CA 1 ATOM 2677 C C . GLU B 2 74 ? -0.992 39.714 20.413 1.00 38.50 ? 74 GLU B C 1 ATOM 2678 O O . GLU B 2 74 ? 0.001 40.245 19.939 1.00 38.63 ? 74 GLU B O 1 ATOM 2679 C CB . GLU B 2 74 ? -2.953 39.981 18.928 1.00 41.69 ? 74 GLU B CB 1 ATOM 2680 C CG . GLU B 2 74 ? -3.711 39.452 17.730 1.00 42.65 ? 74 GLU B CG 1 ATOM 2681 C CD . GLU B 2 74 ? -4.997 40.194 17.471 1.00 45.37 ? 74 GLU B CD 1 ATOM 2682 O OE1 . GLU B 2 74 ? -5.992 39.514 17.140 1.00 46.70 ? 74 GLU B OE1 1 ATOM 2683 O OE2 . GLU B 2 74 ? -5.021 41.441 17.603 1.00 47.91 ? 74 GLU B OE2 1 ATOM 2684 N N . THR B 2 75 ? -1.295 39.748 21.712 1.00 38.34 ? 75 THR B N 1 ATOM 2685 C CA . THR B 2 75 ? -0.627 40.655 22.653 1.00 39.19 ? 75 THR B CA 1 ATOM 2686 C C . THR B 2 75 ? 0.278 40.001 23.707 1.00 37.80 ? 75 THR B C 1 ATOM 2687 O O . THR B 2 75 ? 1.078 40.697 24.328 1.00 39.04 ? 75 THR B O 1 ATOM 2688 C CB . THR B 2 75 ? -1.670 41.520 23.385 1.00 41.34 ? 75 THR B CB 1 ATOM 2689 O OG1 . THR B 2 75 ? -2.608 40.674 24.060 1.00 40.91 ? 75 THR B OG1 1 ATOM 2690 C CG2 . THR B 2 75 ? -2.409 42.417 22.396 1.00 42.73 ? 75 THR B CG2 1 ATOM 2691 N N . ASP B 2 76 ? 0.161 38.697 23.940 1.00 35.39 ? 76 ASP B N 1 ATOM 2692 C CA . ASP B 2 76 ? 0.989 38.068 24.960 1.00 34.41 ? 76 ASP B CA 1 ATOM 2693 C C . ASP B 2 76 ? 2.389 37.795 24.383 1.00 32.71 ? 76 ASP B C 1 ATOM 2694 O O . ASP B 2 76 ? 2.527 37.468 23.209 1.00 31.65 ? 76 ASP B O 1 ATOM 2695 C CB . ASP B 2 76 ? 0.346 36.790 25.501 1.00 33.78 ? 76 ASP B CB 1 ATOM 2696 C CG . ASP B 2 76 ? -0.909 37.062 26.317 1.00 35.65 ? 76 ASP B CG 1 ATOM 2697 O OD1 . ASP B 2 76 ? -0.887 37.909 27.228 1.00 37.34 ? 76 ASP B OD1 1 ATOM 2698 O OD2 . ASP B 2 76 ? -1.930 36.408 26.056 1.00 36.35 ? 76 ASP B OD2 1 ATOM 2699 N N . THR B 2 77 ? 3.417 38.003 25.198 1.00 32.40 ? 77 THR B N 1 ATOM 2700 C CA . THR B 2 77 ? 4.780 37.639 24.836 1.00 30.97 ? 77 THR B CA 1 ATOM 2701 C C . THR B 2 77 ? 5.171 36.412 25.636 1.00 29.30 ? 77 THR B C 1 ATOM 2702 O O . THR B 2 77 ? 4.763 36.272 26.795 1.00 30.24 ? 77 THR B O 1 ATOM 2703 C CB . THR B 2 77 ? 5.791 38.750 25.146 1.00 32.41 ? 77 THR B CB 1 ATOM 2704 O OG1 . THR B 2 77 ? 5.744 39.061 26.545 1.00 34.03 ? 77 THR B OG1 1 ATOM 2705 C CG2 . THR B 2 77 ? 5.498 39.991 24.321 1.00 34.03 ? 77 THR B CG2 1 ATOM 2706 N N . TYR B 2 78 ? 5.962 35.538 25.013 1.00 27.05 ? 78 TYR B N 1 ATOM 2707 C CA . TYR B 2 78 ? 6.474 34.332 25.660 1.00 25.39 ? 78 TYR B CA 1 ATOM 2708 C C . TYR B 2 78 ? 7.984 34.270 25.484 1.00 24.84 ? 78 TYR B C 1 ATOM 2709 O O . TYR B 2 78 ? 8.512 34.694 24.456 1.00 24.44 ? 78 TYR B O 1 ATOM 2710 C CB . TYR B 2 78 ? 5.802 33.084 25.082 1.00 23.92 ? 78 TYR B CB 1 ATOM 2711 C CG . TYR B 2 78 ? 4.344 33.008 25.436 1.00 24.36 ? 78 TYR B CG 1 ATOM 2712 C CD1 . TYR B 2 78 ? 3.937 32.404 26.616 1.00 24.60 ? 78 TYR B CD1 1 ATOM 2713 C CD2 . TYR B 2 78 ? 3.369 33.584 24.614 1.00 24.81 ? 78 TYR B CD2 1 ATOM 2714 C CE1 . TYR B 2 78 ? 2.599 32.340 26.964 1.00 25.48 ? 78 TYR B CE1 1 ATOM 2715 C CE2 . TYR B 2 78 ? 2.029 33.532 24.952 1.00 25.57 ? 78 TYR B CE2 1 ATOM 2716 C CZ . TYR B 2 78 ? 1.651 32.905 26.126 1.00 26.00 ? 78 TYR B CZ 1 ATOM 2717 O OH . TYR B 2 78 ? 0.338 32.846 26.493 1.00 27.25 ? 78 TYR B OH 1 ATOM 2718 N N . ALA B 2 79 ? 8.668 33.752 26.501 1.00 24.57 ? 79 ALA B N 1 ATOM 2719 C CA . ALA B 2 79 ? 10.118 33.681 26.505 1.00 24.50 ? 79 ALA B CA 1 ATOM 2720 C C . ALA B 2 79 ? 10.611 32.469 27.268 1.00 24.05 ? 79 ALA B C 1 ATOM 2721 O O . ALA B 2 79 ? 9.859 31.846 28.028 1.00 23.99 ? 79 ALA B O 1 ATOM 2722 C CB . ALA B 2 79 ? 10.703 34.955 27.110 1.00 26.12 ? 79 ALA B CB 1 ATOM 2723 N N . CYS B 2 80 ? 11.888 32.154 27.054 1.00 23.96 ? 80 CYS B N 1 ATOM 2724 C CA . CYS B 2 80 ? 12.592 31.143 27.826 1.00 23.80 ? 80 CYS B CA 1 ATOM 2725 C C . CYS B 2 80 ? 13.865 31.757 28.383 1.00 24.91 ? 80 CYS B C 1 ATOM 2726 O O . CYS B 2 80 ? 14.667 32.322 27.626 1.00 24.91 ? 80 CYS B O 1 ATOM 2727 C CB . CYS B 2 80 ? 12.935 29.943 26.966 1.00 22.44 ? 80 CYS B CB 1 ATOM 2728 S SG . CYS B 2 80 ? 13.556 28.556 27.936 1.00 22.53 ? 80 CYS B SG 1 ATOM 2729 N N . ARG B 2 81 ? 14.038 31.646 29.698 1.00 26.10 ? 81 ARG B N 1 ATOM 2730 C CA . ARG B 2 81 ? 15.137 32.307 30.400 1.00 28.08 ? 81 ARG B CA 1 ATOM 2731 C C . ARG B 2 81 ? 15.976 31.284 31.124 1.00 27.32 ? 81 ARG B C 1 ATOM 2732 O O . ARG B 2 81 ? 15.445 30.464 31.872 1.00 26.56 ? 81 ARG B O 1 ATOM 2733 C CB . ARG B 2 81 ? 14.609 33.322 31.398 1.00 31.05 ? 81 ARG B CB 1 ATOM 2734 C CG . ARG B 2 81 ? 15.715 34.162 32.030 1.00 33.95 ? 81 ARG B CG 1 ATOM 2735 C CD . ARG B 2 81 ? 15.152 35.404 32.689 1.00 37.34 ? 81 ARG B CD 1 ATOM 2736 N NE . ARG B 2 81 ? 14.705 35.120 34.051 1.00 39.89 ? 81 ARG B NE 1 ATOM 2737 C CZ . ARG B 2 81 ? 15.345 35.456 35.178 1.00 43.08 ? 81 ARG B CZ 1 ATOM 2738 N NH1 . ARG B 2 81 ? 16.501 36.120 35.169 1.00 45.01 ? 81 ARG B NH1 1 ATOM 2739 N NH2 . ARG B 2 81 ? 14.806 35.138 36.355 1.00 45.07 ? 81 ARG B NH2 1 ATOM 2740 N N . VAL B 2 82 ? 17.288 31.360 30.918 1.00 27.18 ? 82 VAL B N 1 ATOM 2741 C CA . VAL B 2 82 ? 18.216 30.352 31.400 1.00 26.94 ? 82 VAL B CA 1 ATOM 2742 C C . VAL B 2 82 ? 19.314 30.983 32.249 1.00 28.35 ? 82 VAL B C 1 ATOM 2743 O O . VAL B 2 82 ? 19.922 31.980 31.846 1.00 28.97 ? 82 VAL B O 1 ATOM 2744 C CB . VAL B 2 82 ? 18.850 29.601 30.213 1.00 25.61 ? 82 VAL B CB 1 ATOM 2745 C CG1 . VAL B 2 82 ? 20.000 28.711 30.665 1.00 25.83 ? 82 VAL B CG1 1 ATOM 2746 C CG2 . VAL B 2 82 ? 17.784 28.791 29.498 1.00 24.31 ? 82 VAL B CG2 1 ATOM 2747 N N . LYS B 2 83 ? 19.554 30.386 33.416 1.00 29.01 ? 83 LYS B N 1 ATOM 2748 C CA . LYS B 2 83 ? 20.656 30.777 34.289 1.00 30.62 ? 83 LYS B CA 1 ATOM 2749 C C . LYS B 2 83 ? 21.611 29.610 34.365 1.00 29.67 ? 83 LYS B C 1 ATOM 2750 O O . LYS B 2 83 ? 21.192 28.480 34.598 1.00 28.53 ? 83 LYS B O 1 ATOM 2751 C CB . LYS B 2 83 ? 20.172 31.101 35.700 1.00 32.74 ? 83 LYS B CB 1 ATOM 2752 C CG . LYS B 2 83 ? 19.039 32.110 35.771 1.00 34.00 ? 83 LYS B CG 1 ATOM 2753 C CD . LYS B 2 83 ? 18.704 32.392 37.226 1.00 36.53 ? 83 LYS B CD 1 ATOM 2754 C CE . LYS B 2 83 ? 17.431 33.204 37.365 1.00 37.75 ? 83 LYS B CE 1 ATOM 2755 N NZ . LYS B 2 83 ? 17.078 33.358 38.802 1.00 40.17 ? 83 LYS B NZ 1 ATOM 2756 N N . HIS B 2 84 ? 22.898 29.900 34.217 1.00 30.14 ? 84 HIS B N 1 ATOM 2757 C CA . HIS B 2 84 ? 23.922 28.874 34.149 1.00 29.75 ? 84 HIS B CA 1 ATOM 2758 C C . HIS B 2 84 ? 25.243 29.533 34.533 1.00 31.38 ? 84 HIS B C 1 ATOM 2759 O O . HIS B 2 84 ? 25.415 30.737 34.307 1.00 32.39 ? 84 HIS B O 1 ATOM 2760 C CB . HIS B 2 84 ? 23.965 28.310 32.724 1.00 28.07 ? 84 HIS B CB 1 ATOM 2761 C CG . HIS B 2 84 ? 24.877 27.134 32.557 1.00 27.86 ? 84 HIS B CG 1 ATOM 2762 N ND1 . HIS B 2 84 ? 26.123 27.240 31.984 1.00 28.34 ? 84 HIS B ND1 1 ATOM 2763 C CD2 . HIS B 2 84 ? 24.728 25.833 32.887 1.00 27.26 ? 84 HIS B CD2 1 ATOM 2764 C CE1 . HIS B 2 84 ? 26.707 26.057 31.973 1.00 27.92 ? 84 HIS B CE1 1 ATOM 2765 N NE2 . HIS B 2 84 ? 25.878 25.182 32.513 1.00 27.19 ? 84 HIS B NE2 1 ATOM 2766 N N . ALA B 2 85 ? 26.156 28.761 35.126 1.00 31.89 ? 85 ALA B N 1 ATOM 2767 C CA . ALA B 2 85 ? 27.420 29.312 35.644 1.00 34.15 ? 85 ALA B CA 1 ATOM 2768 C C . ALA B 2 85 ? 28.327 29.903 34.563 1.00 34.22 ? 85 ALA B C 1 ATOM 2769 O O . ALA B 2 85 ? 29.153 30.743 34.854 1.00 35.89 ? 85 ALA B O 1 ATOM 2770 C CB . ALA B 2 85 ? 28.181 28.263 36.444 1.00 34.70 ? 85 ALA B CB 1 ATOM 2771 N N . SER B 2 86 ? 28.182 29.425 33.329 1.00 32.74 ? 86 SER B N 1 ATOM 2772 C CA . SER B 2 86 ? 28.909 29.962 32.170 1.00 33.29 ? 86 SER B CA 1 ATOM 2773 C C . SER B 2 86 ? 28.580 31.414 31.790 1.00 34.58 ? 86 SER B C 1 ATOM 2774 O O . SER B 2 86 ? 29.311 32.006 31.007 1.00 35.37 ? 86 SER B O 1 ATOM 2775 C CB . SER B 2 86 ? 28.655 29.093 30.942 1.00 31.24 ? 86 SER B CB 1 ATOM 2776 O OG . SER B 2 86 ? 27.293 29.180 30.555 1.00 30.00 ? 86 SER B OG 1 ATOM 2777 N N . MET B 2 87 ? 27.468 31.952 32.290 1.00 35.04 ? 87 MET B N 1 ATOM 2778 C CA . MET B 2 87 ? 27.025 33.305 31.951 1.00 36.50 ? 87 MET B CA 1 ATOM 2779 C C . MET B 2 87 ? 26.846 34.119 33.216 1.00 38.30 ? 87 MET B C 1 ATOM 2780 O O . MET B 2 87 ? 26.212 33.657 34.164 1.00 38.16 ? 87 MET B O 1 ATOM 2781 C CB . MET B 2 87 ? 25.689 33.246 31.209 1.00 35.31 ? 87 MET B CB 1 ATOM 2782 C CG . MET B 2 87 ? 25.617 32.161 30.152 1.00 33.73 ? 87 MET B CG 1 ATOM 2783 S SD . MET B 2 87 ? 24.089 32.201 29.216 1.00 32.83 ? 87 MET B SD 1 ATOM 2784 C CE . MET B 2 87 ? 22.944 31.359 30.304 1.00 31.59 ? 87 MET B CE 1 ATOM 2785 N N . ALA B 2 88 ? 27.385 35.335 33.226 1.00 40.36 ? 88 ALA B N 1 ATOM 2786 C CA . ALA B 2 88 ? 27.166 36.252 34.341 1.00 42.52 ? 88 ALA B CA 1 ATOM 2787 C C . ALA B 2 88 ? 25.701 36.684 34.401 1.00 42.00 ? 88 ALA B C 1 ATOM 2788 O O . ALA B 2 88 ? 25.156 36.863 35.489 1.00 43.23 ? 88 ALA B O 1 ATOM 2789 C CB . ALA B 2 88 ? 28.087 37.464 34.242 1.00 45.25 ? 88 ALA B CB 1 ATOM 2790 N N . GLU B 2 89 ? 25.068 36.833 33.237 1.00 40.33 ? 89 GLU B N 1 ATOM 2791 C CA . GLU B 2 89 ? 23.678 37.259 33.160 1.00 40.03 ? 89 GLU B CA 1 ATOM 2792 C C . GLU B 2 89 ? 22.795 36.134 32.640 1.00 37.09 ? 89 GLU B C 1 ATOM 2793 O O . GLU B 2 89 ? 23.228 35.357 31.789 1.00 35.03 ? 89 GLU B O 1 ATOM 2794 C CB . GLU B 2 89 ? 23.546 38.478 32.246 1.00 41.25 ? 89 GLU B CB 1 ATOM 2795 C CG . GLU B 2 89 ? 24.116 39.758 32.848 1.00 44.53 ? 89 GLU B CG 1 ATOM 2796 C CD . GLU B 2 89 ? 23.285 40.325 33.998 1.00 46.20 ? 89 GLU B CD 1 ATOM 2797 O OE1 . GLU B 2 89 ? 22.138 39.869 34.219 1.00 45.07 ? 89 GLU B OE1 1 ATOM 2798 O OE2 . GLU B 2 89 ? 23.777 41.242 34.687 1.00 48.86 ? 89 GLU B OE2 1 ATOM 2799 N N . PRO B 2 90 ? 21.548 36.053 33.140 1.00 37.03 ? 90 PRO B N 1 ATOM 2800 C CA . PRO B 2 90 ? 20.597 35.117 32.535 1.00 34.78 ? 90 PRO B CA 1 ATOM 2801 C C . PRO B 2 90 ? 20.349 35.455 31.079 1.00 33.86 ? 90 PRO B C 1 ATOM 2802 O O . PRO B 2 90 ? 20.316 36.637 30.711 1.00 35.27 ? 90 PRO B O 1 ATOM 2803 C CB . PRO B 2 90 ? 19.319 35.318 33.361 1.00 35.49 ? 90 PRO B CB 1 ATOM 2804 C CG . PRO B 2 90 ? 19.801 35.861 34.657 1.00 38.03 ? 90 PRO B CG 1 ATOM 2805 C CD . PRO B 2 90 ? 20.970 36.729 34.314 1.00 39.25 ? 90 PRO B CD 1 ATOM 2806 N N . LYS B 2 91 ? 20.202 34.424 30.261 1.00 31.84 ? 91 LYS B N 1 ATOM 2807 C CA . LYS B 2 91 ? 19.939 34.573 28.842 1.00 31.39 ? 91 LYS B CA 1 ATOM 2808 C C . LYS B 2 91 ? 18.465 34.319 28.582 1.00 30.03 ? 91 LYS B C 1 ATOM 2809 O O . LYS B 2 91 ? 17.910 33.315 29.041 1.00 28.20 ? 91 LYS B O 1 ATOM 2810 C CB . LYS B 2 91 ? 20.780 33.586 28.024 1.00 30.97 ? 91 LYS B CB 1 ATOM 2811 C CG . LYS B 2 91 ? 20.660 33.776 26.511 1.00 31.40 ? 91 LYS B CG 1 ATOM 2812 C CD . LYS B 2 91 ? 21.944 33.412 25.753 1.00 32.16 ? 91 LYS B CD 1 ATOM 2813 C CE . LYS B 2 91 ? 21.980 31.942 25.374 1.00 30.68 ? 91 LYS B CE 1 ATOM 2814 N NZ . LYS B 2 91 ? 23.149 31.604 24.501 1.00 31.47 ? 91 LYS B NZ 1 ATOM 2815 N N . THR B 2 92 ? 17.844 35.240 27.850 1.00 30.12 ? 92 THR B N 1 ATOM 2816 C CA . THR B 2 92 ? 16.426 35.163 27.518 1.00 29.22 ? 92 THR B CA 1 ATOM 2817 C C . THR B 2 92 ? 16.270 35.140 26.004 1.00 28.44 ? 92 THR B C 1 ATOM 2818 O O . THR B 2 92 ? 16.839 35.981 25.300 1.00 29.25 ? 92 THR B O 1 ATOM 2819 C CB . THR B 2 92 ? 15.655 36.356 28.122 1.00 30.96 ? 92 THR B CB 1 ATOM 2820 O OG1 . THR B 2 92 ? 15.871 36.391 29.538 1.00 31.90 ? 92 THR B OG1 1 ATOM 2821 C CG2 . THR B 2 92 ? 14.163 36.251 27.850 1.00 30.46 ? 92 THR B CG2 1 ATOM 2822 N N . VAL B 2 93 ? 15.507 34.169 25.509 1.00 26.77 ? 93 VAL B N 1 ATOM 2823 C CA . VAL B 2 93 ? 15.129 34.117 24.107 1.00 26.59 ? 93 VAL B CA 1 ATOM 2824 C C . VAL B 2 93 ? 13.601 34.207 24.057 1.00 26.48 ? 93 VAL B C 1 ATOM 2825 O O . VAL B 2 93 ? 12.917 33.460 24.742 1.00 25.69 ? 93 VAL B O 1 ATOM 2826 C CB . VAL B 2 93 ? 15.688 32.833 23.454 1.00 25.15 ? 93 VAL B CB 1 ATOM 2827 C CG1 . VAL B 2 93 ? 15.063 32.565 22.093 1.00 24.83 ? 93 VAL B CG1 1 ATOM 2828 C CG2 . VAL B 2 93 ? 17.208 32.948 23.340 1.00 25.78 ? 93 VAL B CG2 1 ATOM 2829 N N . TYR B 2 94 ? 13.071 35.151 23.292 1.00 27.61 ? 94 TYR B N 1 ATOM 2830 C CA . TYR B 2 94 ? 11.614 35.284 23.151 1.00 27.98 ? 94 TYR B CA 1 ATOM 2831 C C . TYR B 2 94 ? 11.118 34.386 22.038 1.00 26.74 ? 94 TYR B C 1 ATOM 2832 O O . TYR B 2 94 ? 11.812 34.168 21.037 1.00 26.08 ? 94 TYR B O 1 ATOM 2833 C CB . TYR B 2 94 ? 11.193 36.722 22.867 1.00 30.24 ? 94 TYR B CB 1 ATOM 2834 C CG . TYR B 2 94 ? 11.237 37.602 24.093 1.00 32.13 ? 94 TYR B CG 1 ATOM 2835 C CD1 . TYR B 2 94 ? 12.429 38.146 24.535 1.00 33.31 ? 94 TYR B CD1 1 ATOM 2836 C CD2 . TYR B 2 94 ? 10.076 37.867 24.824 1.00 33.12 ? 94 TYR B CD2 1 ATOM 2837 C CE1 . TYR B 2 94 ? 12.476 38.955 25.661 1.00 35.29 ? 94 TYR B CE1 1 ATOM 2838 C CE2 . TYR B 2 94 ? 10.108 38.666 25.953 1.00 34.90 ? 94 TYR B CE2 1 ATOM 2839 C CZ . TYR B 2 94 ? 11.313 39.201 26.368 1.00 35.96 ? 94 TYR B CZ 1 ATOM 2840 O OH . TYR B 2 94 ? 11.346 39.999 27.478 1.00 38.23 ? 94 TYR B OH 1 ATOM 2841 N N . TRP B 2 95 ? 9.918 33.860 22.226 1.00 26.22 ? 95 TRP B N 1 ATOM 2842 C CA . TRP B 2 95 ? 9.219 33.173 21.159 1.00 26.26 ? 95 TRP B CA 1 ATOM 2843 C C . TRP B 2 95 ? 8.812 34.213 20.132 1.00 28.07 ? 95 TRP B C 1 ATOM 2844 O O . TRP B 2 95 ? 8.286 35.271 20.490 1.00 29.12 ? 95 TRP B O 1 ATOM 2845 C CB . TRP B 2 95 ? 7.975 32.474 21.680 1.00 25.63 ? 95 TRP B CB 1 ATOM 2846 C CG . TRP B 2 95 ? 7.132 31.866 20.604 1.00 25.18 ? 95 TRP B CG 1 ATOM 2847 C CD1 . TRP B 2 95 ? 7.517 30.928 19.696 1.00 24.54 ? 95 TRP B CD1 1 ATOM 2848 C CD2 . TRP B 2 95 ? 5.753 32.150 20.326 1.00 25.89 ? 95 TRP B CD2 1 ATOM 2849 N NE1 . TRP B 2 95 ? 6.471 30.607 18.871 1.00 24.62 ? 95 TRP B NE1 1 ATOM 2850 C CE2 . TRP B 2 95 ? 5.370 31.327 19.243 1.00 25.43 ? 95 TRP B CE2 1 ATOM 2851 C CE3 . TRP B 2 95 ? 4.803 33.008 20.891 1.00 26.95 ? 95 TRP B CE3 1 ATOM 2852 C CZ2 . TRP B 2 95 ? 4.081 31.347 18.703 1.00 26.11 ? 95 TRP B CZ2 1 ATOM 2853 C CZ3 . TRP B 2 95 ? 3.505 33.025 20.355 1.00 27.75 ? 95 TRP B CZ3 1 ATOM 2854 C CH2 . TRP B 2 95 ? 3.164 32.196 19.268 1.00 27.00 ? 95 TRP B CH2 1 ATOM 2855 N N . ASP B 2 96 ? 9.082 33.910 18.873 1.00 28.94 ? 96 ASP B N 1 ATOM 2856 C CA . ASP B 2 96 ? 8.630 34.713 17.756 1.00 31.89 ? 96 ASP B CA 1 ATOM 2857 C C . ASP B 2 96 ? 7.992 33.758 16.746 1.00 32.90 ? 96 ASP B C 1 ATOM 2858 O O . ASP B 2 96 ? 8.704 32.989 16.089 1.00 32.82 ? 96 ASP B O 1 ATOM 2859 C CB . ASP B 2 96 ? 9.820 35.425 17.142 1.00 33.14 ? 96 ASP B CB 1 ATOM 2860 C CG . ASP B 2 96 ? 9.424 36.414 16.072 1.00 35.01 ? 96 ASP B CG 1 ATOM 2861 O OD1 . ASP B 2 96 ? 8.260 36.402 15.593 1.00 35.30 ? 96 ASP B OD1 1 ATOM 2862 O OD2 . ASP B 2 96 ? 10.304 37.211 15.718 1.00 36.93 ? 96 ASP B OD2 1 ATOM 2863 N N . ARG B 2 97 ? 6.672 33.819 16.612 1.00 34.47 ? 97 ARG B N 1 ATOM 2864 C CA . ARG B 2 97 ? 5.954 32.935 15.685 1.00 35.65 ? 97 ARG B CA 1 ATOM 2865 C C . ARG B 2 97 ? 6.436 33.094 14.235 1.00 37.22 ? 97 ARG B C 1 ATOM 2866 O O . ARG B 2 97 ? 6.383 32.150 13.449 1.00 37.42 ? 97 ARG B O 1 ATOM 2867 C CB . ARG B 2 97 ? 4.430 33.147 15.768 1.00 36.59 ? 97 ARG B CB 1 ATOM 2868 C CG . ARG B 2 97 ? 3.845 34.227 14.861 1.00 38.72 ? 97 ARG B CG 1 ATOM 2869 C CD . ARG B 2 97 ? 2.338 34.283 15.002 1.00 39.92 ? 97 ARG B CD 1 ATOM 2870 N NE . ARG B 2 97 ? 1.940 34.714 16.344 1.00 40.16 ? 97 ARG B NE 1 ATOM 2871 C CZ . ARG B 2 97 ? 0.729 34.552 16.883 1.00 40.60 ? 97 ARG B CZ 1 ATOM 2872 N NH1 . ARG B 2 97 ? -0.262 33.946 16.215 1.00 40.51 ? 97 ARG B NH1 1 ATOM 2873 N NH2 . ARG B 2 97 ? 0.509 34.996 18.119 1.00 40.95 ? 97 ARG B NH2 1 ATOM 2874 N N . ASP B 2 98 ? 6.894 34.294 13.890 1.00 38.89 ? 98 ASP B N 1 ATOM 2875 C CA . ASP B 2 98 ? 7.401 34.571 12.549 1.00 40.39 ? 98 ASP B CA 1 ATOM 2876 C C . ASP B 2 98 ? 8.737 33.855 12.256 1.00 40.59 ? 98 ASP B C 1 ATOM 2877 O O . ASP B 2 98 ? 9.047 33.576 11.093 1.00 41.97 ? 98 ASP B O 1 ATOM 2878 C CB . ASP B 2 98 ? 7.542 36.080 12.346 1.00 42.22 ? 98 ASP B CB 1 ATOM 2879 C CG . ASP B 2 98 ? 6.218 36.826 12.528 1.00 43.47 ? 98 ASP B CG 1 ATOM 2880 O OD1 . ASP B 2 98 ? 5.160 36.323 12.078 1.00 42.96 ? 98 ASP B OD1 1 ATOM 2881 O OD2 . ASP B 2 98 ? 6.239 37.918 13.136 1.00 44.97 ? 98 ASP B OD2 1 ATOM 2882 N N . MET B 2 99 ? 9.518 33.576 13.302 1.00 39.80 ? 99 MET B N 1 ATOM 2883 C CA . MET B 2 99 ? 10.847 32.978 13.158 1.00 40.30 ? 99 MET B CA 1 ATOM 2884 C C . MET B 2 99 ? 10.746 31.476 13.341 1.00 39.28 ? 99 MET B C 1 ATOM 2885 O O . MET B 2 99 ? 11.767 30.798 13.447 1.00 41.30 ? 99 MET B O 1 ATOM 2886 C CB . MET B 2 99 ? 11.821 33.574 14.186 1.00 40.14 ? 99 MET B CB 1 ATOM 2887 N N . ASP C 3 4 ? 42.391 3.489 44.871 1.00 64.72 ? 0 ASP C N 1 ATOM 2888 C CA . ASP C 3 4 ? 42.085 2.031 44.805 1.00 64.78 ? 0 ASP C CA 1 ATOM 2889 C C . ASP C 3 4 ? 40.937 1.673 43.839 1.00 63.04 ? 0 ASP C C 1 ATOM 2890 O O . ASP C 3 4 ? 41.001 0.642 43.172 1.00 62.77 ? 0 ASP C O 1 ATOM 2891 C CB . ASP C 3 4 ? 41.763 1.499 46.204 1.00 67.31 ? 0 ASP C CB 1 ATOM 2892 N N . PHE C 3 5 ? 39.909 2.523 43.751 1.00 61.75 ? 1 PHE C N 1 ATOM 2893 C CA . PHE C 3 5 ? 38.587 2.125 43.226 1.00 60.62 ? 1 PHE C CA 1 ATOM 2894 C C . PHE C 3 5 ? 38.033 0.916 44.020 1.00 62.48 ? 1 PHE C C 1 ATOM 2895 O O . PHE C 3 5 ? 37.457 -0.014 43.446 1.00 62.21 ? 1 PHE C O 1 ATOM 2896 C CB . PHE C 3 5 ? 38.617 1.840 41.708 1.00 58.16 ? 1 PHE C CB 1 ATOM 2897 C CG . PHE C 3 5 ? 38.482 3.065 40.851 1.00 56.39 ? 1 PHE C CG 1 ATOM 2898 C CD1 . PHE C 3 5 ? 37.227 3.629 40.619 1.00 55.66 ? 1 PHE C CD1 1 ATOM 2899 C CD2 . PHE C 3 5 ? 39.597 3.644 40.249 1.00 55.36 ? 1 PHE C CD2 1 ATOM 2900 C CE1 . PHE C 3 5 ? 37.087 4.759 39.819 1.00 54.24 ? 1 PHE C CE1 1 ATOM 2901 C CE2 . PHE C 3 5 ? 39.461 4.770 39.439 1.00 54.31 ? 1 PHE C CE2 1 ATOM 2902 C CZ . PHE C 3 5 ? 38.205 5.330 39.224 1.00 53.37 ? 1 PHE C CZ 1 ATOM 2903 N N . HIS C 3 6 ? 38.175 0.978 45.346 1.00 64.71 ? 2 HIS C N 1 ATOM 2904 C CA . HIS C 3 6 ? 37.936 -0.166 46.253 1.00 67.02 ? 2 HIS C CA 1 ATOM 2905 C C . HIS C 3 6 ? 36.532 -0.801 46.178 1.00 67.22 ? 2 HIS C C 1 ATOM 2906 O O . HIS C 3 6 ? 36.403 -2.034 46.182 1.00 68.10 ? 2 HIS C O 1 ATOM 2907 C CB . HIS C 3 6 ? 38.231 0.260 47.702 1.00 69.78 ? 2 HIS C CB 1 ATOM 2908 C CG . HIS C 3 6 ? 37.945 -0.799 48.721 1.00 72.82 ? 2 HIS C CG 1 ATOM 2909 N ND1 . HIS C 3 6 ? 36.732 -0.896 49.371 1.00 74.53 ? 2 HIS C ND1 1 ATOM 2910 C CD2 . HIS C 3 6 ? 38.712 -1.805 49.202 1.00 74.84 ? 2 HIS C CD2 1 ATOM 2911 C CE1 . HIS C 3 6 ? 36.764 -1.918 50.208 1.00 77.58 ? 2 HIS C CE1 1 ATOM 2912 N NE2 . HIS C 3 6 ? 37.956 -2.484 50.129 1.00 77.78 ? 2 HIS C NE2 1 ATOM 2913 N N . HIS C 3 7 ? 35.498 0.038 46.145 1.00 65.97 ? 3 HIS C N 1 ATOM 2914 C CA . HIS C 3 7 ? 34.107 -0.433 46.191 1.00 66.32 ? 3 HIS C CA 1 ATOM 2915 C C . HIS C 3 7 ? 33.650 -1.076 44.881 1.00 64.28 ? 3 HIS C C 1 ATOM 2916 O O . HIS C 3 7 ? 33.010 -2.134 44.905 1.00 65.21 ? 3 HIS C O 1 ATOM 2917 C CB . HIS C 3 7 ? 33.153 0.704 46.569 1.00 66.39 ? 3 HIS C CB 1 ATOM 2918 C CG . HIS C 3 7 ? 33.390 1.259 47.938 1.00 69.04 ? 3 HIS C CG 1 ATOM 2919 N ND1 . HIS C 3 7 ? 34.214 2.339 48.171 1.00 68.88 ? 3 HIS C ND1 1 ATOM 2920 C CD2 . HIS C 3 7 ? 32.912 0.882 49.147 1.00 72.26 ? 3 HIS C CD2 1 ATOM 2921 C CE1 . HIS C 3 7 ? 34.238 2.601 49.466 1.00 71.90 ? 3 HIS C CE1 1 ATOM 2922 N NE2 . HIS C 3 7 ? 33.457 1.730 50.080 1.00 74.12 ? 3 HIS C NE2 1 ATOM 2923 N N . ILE C 3 8 ? 33.966 -0.430 43.753 1.00 61.39 ? 4 ILE C N 1 ATOM 2924 C CA . ILE C 3 8 ? 33.643 -0.951 42.411 1.00 59.31 ? 4 ILE C CA 1 ATOM 2925 C C . ILE C 3 8 ? 34.275 -2.319 42.183 1.00 60.51 ? 4 ILE C C 1 ATOM 2926 O O . ILE C 3 8 ? 33.639 -3.219 41.623 1.00 59.88 ? 4 ILE C O 1 ATOM 2927 C CB . ILE C 3 8 ? 34.098 0.022 41.293 1.00 56.54 ? 4 ILE C CB 1 ATOM 2928 C CG1 . ILE C 3 8 ? 33.195 1.266 41.281 1.00 55.56 ? 4 ILE C CG1 1 ATOM 2929 C CG2 . ILE C 3 8 ? 34.112 -0.653 39.919 1.00 55.19 ? 4 ILE C CG2 1 ATOM 2930 C CD1 . ILE C 3 8 ? 31.825 1.052 40.680 1.00 54.95 ? 4 ILE C CD1 1 ATOM 2931 N N . ARG C 3 9 ? 35.523 -2.459 42.627 1.00 61.84 ? 5 ARG C N 1 ATOM 2932 C CA . ARG C 3 9 ? 36.224 -3.738 42.571 1.00 63.40 ? 5 ARG C CA 1 ATOM 2933 C C . ARG C 3 9 ? 35.517 -4.797 43.435 1.00 66.38 ? 5 ARG C C 1 ATOM 2934 O O . ARG C 3 9 ? 35.380 -5.949 43.013 1.00 67.64 ? 5 ARG C O 1 ATOM 2935 C CB . ARG C 3 9 ? 37.712 -3.563 42.942 1.00 63.76 ? 5 ARG C CB 1 ATOM 2936 C CG . ARG C 3 9 ? 38.493 -2.669 41.963 1.00 61.52 ? 5 ARG C CG 1 ATOM 2937 C CD . ARG C 3 9 ? 39.965 -2.529 42.334 1.00 62.11 ? 5 ARG C CD 1 ATOM 2938 N NE . ARG C 3 9 ? 40.156 -1.930 43.653 1.00 64.03 ? 5 ARG C NE 1 ATOM 2939 N N . GLU C 3 10 ? 35.046 -4.392 44.617 1.00 68.35 ? 6 GLU C N 1 ATOM 2940 C CA . GLU C 3 10 ? 34.195 -5.243 45.465 1.00 71.19 ? 6 GLU C CA 1 ATOM 2941 C C . GLU C 3 10 ? 32.822 -5.545 44.829 1.00 71.19 ? 6 GLU C C 1 ATOM 2942 O O . GLU C 3 10 ? 32.299 -6.648 44.993 1.00 72.67 ? 6 GLU C O 1 ATOM 2943 C CB . GLU C 3 10 ? 34.002 -4.604 46.845 1.00 73.22 ? 6 GLU C CB 1 ATOM 2944 N N . LYS C 3 11 ? 32.245 -4.567 44.123 1.00 69.44 ? 7 LYS C N 1 ATOM 2945 C CA . LYS C 3 11 ? 31.004 -4.759 43.349 1.00 69.68 ? 7 LYS C CA 1 ATOM 2946 C C . LYS C 3 11 ? 31.187 -5.827 42.272 1.00 69.74 ? 7 LYS C C 1 ATOM 2947 O O . LYS C 3 11 ? 30.465 -6.828 42.260 1.00 71.79 ? 7 LYS C O 1 ATOM 2948 C CB . LYS C 3 11 ? 30.547 -3.433 42.699 1.00 67.46 ? 7 LYS C CB 1 ATOM 2949 C CG . LYS C 3 11 ? 29.251 -3.476 41.870 1.00 66.81 ? 7 LYS C CG 1 ATOM 2950 C CD . LYS C 3 11 ? 29.369 -3.912 40.398 1.00 65.22 ? 7 LYS C CD 1 ATOM 2951 C CE . LYS C 3 11 ? 30.232 -3.014 39.511 1.00 63.38 ? 7 LYS C CE 1 ATOM 2952 N NZ . LYS C 3 11 ? 30.576 -3.713 38.276 1.00 62.98 ? 7 LYS C NZ 1 ATOM 2953 N N . GLY C 3 12 ? 32.146 -5.595 41.374 1.00 68.20 ? 8 GLY C N 1 ATOM 2954 C CA . GLY C 3 12 ? 32.432 -6.499 40.253 1.00 67.93 ? 8 GLY C CA 1 ATOM 2955 C C . GLY C 3 12 ? 32.787 -7.921 40.663 1.00 70.67 ? 8 GLY C C 1 ATOM 2956 O O . GLY C 3 12 ? 32.474 -8.866 39.932 1.00 72.14 ? 8 GLY C O 1 ATOM 2957 N N . ASN C 3 13 ? 33.433 -8.071 41.824 1.00 72.04 ? 9 ASN C N 1 ATOM 2958 C CA . ASN C 3 13 ? 33.735 -9.387 42.395 1.00 74.44 ? 9 ASN C CA 1 ATOM 2959 C C . ASN C 3 13 ? 32.494 -10.130 42.916 1.00 76.38 ? 9 ASN C C 1 ATOM 2960 O O . ASN C 3 13 ? 32.439 -11.359 42.837 1.00 78.93 ? 9 ASN C O 1 ATOM 2961 C CB . ASN C 3 13 ? 34.772 -9.266 43.522 1.00 75.95 ? 9 ASN C CB 1 ATOM 2962 N N . HIS C 3 14 ? 31.517 -9.393 43.455 1.00 75.74 ? 10 HIS C N 1 ATOM 2963 C CA . HIS C 3 14 ? 30.265 -9.985 43.967 1.00 77.36 ? 10 HIS C CA 1 ATOM 2964 C C . HIS C 3 14 ? 29.257 -10.284 42.850 1.00 75.77 ? 10 HIS C C 1 ATOM 2965 O O . HIS C 3 14 ? 28.587 -11.322 42.880 1.00 77.50 ? 10 HIS C O 1 ATOM 2966 C CB . HIS C 3 14 ? 29.622 -9.070 45.017 1.00 78.01 ? 10 HIS C CB 1 ATOM 2967 N N . TRP C 3 15 ? 29.162 -9.373 41.876 1.00 72.02 ? 11 TRP C N 1 ATOM 2968 C CA . TRP C 3 15 ? 28.251 -9.504 40.720 1.00 70.70 ? 11 TRP C CA 1 ATOM 2969 C C . TRP C 3 15 ? 28.929 -10.023 39.431 1.00 69.26 ? 11 TRP C C 1 ATOM 2970 O O . TRP C 3 15 ? 28.431 -9.795 38.314 1.00 68.11 ? 11 TRP C O 1 ATOM 2971 C CB . TRP C 3 15 ? 27.535 -8.161 40.474 1.00 68.35 ? 11 TRP C CB 1 ATOM 2972 C CG . TRP C 3 15 ? 26.642 -7.797 41.626 1.00 70.01 ? 11 TRP C CG 1 ATOM 2973 C CD1 . TRP C 3 15 ? 26.993 -7.103 42.749 1.00 70.87 ? 11 TRP C CD1 1 ATOM 2974 C CD2 . TRP C 3 15 ? 25.259 -8.150 41.789 1.00 71.31 ? 11 TRP C CD2 1 ATOM 2975 N NE1 . TRP C 3 15 ? 25.915 -6.989 43.595 1.00 72.82 ? 11 TRP C NE1 1 ATOM 2976 C CE2 . TRP C 3 15 ? 24.837 -7.622 43.032 1.00 72.98 ? 11 TRP C CE2 1 ATOM 2977 C CE3 . TRP C 3 15 ? 24.335 -8.858 41.004 1.00 71.43 ? 11 TRP C CE3 1 ATOM 2978 C CZ2 . TRP C 3 15 ? 23.526 -7.776 43.511 1.00 74.45 ? 11 TRP C CZ2 1 ATOM 2979 C CZ3 . TRP C 3 15 ? 23.029 -9.007 41.478 1.00 73.07 ? 11 TRP C CZ3 1 ATOM 2980 C CH2 . TRP C 3 15 ? 22.642 -8.470 42.723 1.00 74.47 ? 11 TRP C CH2 1 ATOM 2981 N N . LYS C 3 16 ? 30.069 -10.696 39.597 1.00 69.50 ? 12 LYS C N 1 ATOM 2982 C CA . LYS C 3 16 ? 30.649 -11.547 38.559 1.00 68.92 ? 12 LYS C CA 1 ATOM 2983 C C . LYS C 3 16 ? 29.850 -12.849 38.477 1.00 70.77 ? 12 LYS C C 1 ATOM 2984 O O . LYS C 3 16 ? 29.486 -13.292 37.383 1.00 70.20 ? 12 LYS C O 1 ATOM 2985 C CB . LYS C 3 16 ? 32.113 -11.871 38.879 1.00 69.41 ? 12 LYS C CB 1 ATOM 2986 N N . ASN C 3 17 ? 29.578 -13.440 39.645 1.00 72.90 ? 13 ASN C N 1 ATOM 2987 C CA . ASN C 3 17 ? 28.864 -14.717 39.755 1.00 75.44 ? 13 ASN C CA 1 ATOM 2988 C C . ASN C 3 17 ? 27.460 -14.702 39.138 1.00 74.83 ? 13 ASN C C 1 ATOM 2989 O O . ASN C 3 17 ? 27.041 -15.694 38.539 1.00 76.22 ? 13 ASN C O 1 ATOM 2990 C CB . ASN C 3 17 ? 28.783 -15.162 41.221 1.00 78.25 ? 13 ASN C CB 1 ATOM 2991 N N . PHE C 3 18 ? 26.739 -13.591 39.277 1.00 72.90 ? 14 PHE C N 1 ATOM 2992 C CA . PHE C 3 18 ? 25.411 -13.470 38.658 1.00 72.50 ? 14 PHE C CA 1 ATOM 2993 C C . PHE C 3 18 ? 25.483 -13.474 37.124 1.00 70.37 ? 14 PHE C C 1 ATOM 2994 O O . PHE C 3 18 ? 24.724 -14.195 36.466 1.00 71.00 ? 14 PHE C O 1 ATOM 2995 C CB . PHE C 3 18 ? 24.663 -12.218 39.141 1.00 71.21 ? 14 PHE C CB 1 ATOM 2996 C CG . PHE C 3 18 ? 23.386 -11.962 38.384 1.00 70.50 ? 14 PHE C CG 1 ATOM 2997 C CD1 . PHE C 3 18 ? 22.373 -12.921 38.365 1.00 72.86 ? 14 PHE C CD1 1 ATOM 2998 C CD2 . PHE C 3 18 ? 23.207 -10.788 37.662 1.00 67.68 ? 14 PHE C CD2 1 ATOM 2999 C CE1 . PHE C 3 18 ? 21.203 -12.706 37.655 1.00 72.23 ? 14 PHE C CE1 1 ATOM 3000 C CE2 . PHE C 3 18 ? 22.033 -10.565 36.954 1.00 67.07 ? 14 PHE C CE2 1 ATOM 3001 C CZ . PHE C 3 18 ? 21.033 -11.526 36.946 1.00 69.06 ? 14 PHE C CZ 1 ATOM 3002 N N . LEU C 3 19 ? 26.389 -12.671 36.568 1.00 67.78 ? 15 LEU C N 1 ATOM 3003 C CA . LEU C 3 19 ? 26.556 -12.588 35.115 1.00 66.05 ? 15 LEU C CA 1 ATOM 3004 C C . LEU C 3 19 ? 27.283 -13.821 34.582 1.00 67.99 ? 15 LEU C C 1 ATOM 3005 O O . LEU C 3 19 ? 27.205 -14.120 33.390 1.00 67.74 ? 15 LEU C O 1 ATOM 3006 C CB . LEU C 3 19 ? 27.333 -11.331 34.722 1.00 62.85 ? 15 LEU C CB 1 ATOM 3007 C CG . LEU C 3 19 ? 26.733 -9.955 35.035 1.00 60.99 ? 15 LEU C CG 1 ATOM 3008 C CD1 . LEU C 3 19 ? 27.610 -8.892 34.395 1.00 58.31 ? 15 LEU C CD1 1 ATOM 3009 C CD2 . LEU C 3 19 ? 25.293 -9.786 34.552 1.00 60.62 ? 15 LEU C CD2 1 HETATM 3010 C C1 . NAG D 4 . ? 21.936 10.984 45.795 1.00 53.47 ? 301 NAG A C1 1 HETATM 3011 C C2 . NAG D 4 . ? 21.739 11.994 46.920 1.00 56.46 ? 301 NAG A C2 1 HETATM 3012 C C3 . NAG D 4 . ? 22.553 11.612 48.156 1.00 59.20 ? 301 NAG A C3 1 HETATM 3013 C C4 . NAG D 4 . ? 22.268 10.172 48.559 1.00 60.36 ? 301 NAG A C4 1 HETATM 3014 C C5 . NAG D 4 . ? 22.580 9.276 47.360 1.00 57.10 ? 301 NAG A C5 1 HETATM 3015 C C6 . NAG D 4 . ? 22.371 7.791 47.637 1.00 58.00 ? 301 NAG A C6 1 HETATM 3016 C C7 . NAG D 4 . ? 21.351 14.367 46.389 1.00 56.07 ? 301 NAG A C7 1 HETATM 3017 C C8 . NAG D 4 . ? 21.998 15.652 45.967 1.00 55.33 ? 301 NAG A C8 1 HETATM 3018 N N2 . NAG D 4 . ? 22.168 13.319 46.505 1.00 55.51 ? 301 NAG A N2 1 HETATM 3019 O O3 . NAG D 4 . ? 22.264 12.502 49.239 1.00 62.17 ? 301 NAG A O3 1 HETATM 3020 O O4 . NAG D 4 . ? 23.070 9.819 49.700 1.00 63.36 ? 301 NAG A O4 1 HETATM 3021 O O5 . NAG D 4 . ? 21.725 9.655 46.284 1.00 54.76 ? 301 NAG A O5 1 HETATM 3022 O O6 . NAG D 4 . ? 20.991 7.544 47.940 1.00 59.65 ? 301 NAG A O6 1 HETATM 3023 O O7 . NAG D 4 . ? 20.151 14.314 46.601 1.00 57.29 ? 301 NAG A O7 1 HETATM 3024 C C1 . NAG E 4 . ? 22.258 9.466 50.846 1.00 67.38 ? 302 NAG A C1 1 HETATM 3025 C C2 . NAG E 4 . ? 23.142 8.740 51.866 1.00 69.97 ? 302 NAG A C2 1 HETATM 3026 C C3 . NAG E 4 . ? 22.508 8.632 53.259 1.00 74.58 ? 302 NAG A C3 1 HETATM 3027 C C4 . NAG E 4 . ? 21.824 9.928 53.672 1.00 76.28 ? 302 NAG A C4 1 HETATM 3028 C C5 . NAG E 4 . ? 20.832 10.316 52.579 1.00 73.59 ? 302 NAG A C5 1 HETATM 3029 C C6 . NAG E 4 . ? 19.916 11.494 52.927 1.00 75.44 ? 302 NAG A C6 1 HETATM 3030 C C7 . NAG E 4 . ? 24.564 6.988 50.827 1.00 66.91 ? 302 NAG A C7 1 HETATM 3031 C C8 . NAG E 4 . ? 24.572 5.577 50.308 1.00 65.79 ? 302 NAG A C8 1 HETATM 3032 N N2 . NAG E 4 . ? 23.392 7.410 51.324 1.00 68.62 ? 302 NAG A N2 1 HETATM 3033 O O3 . NAG E 4 . ? 23.495 8.306 54.246 1.00 77.14 ? 302 NAG A O3 1 HETATM 3034 O O4 . NAG E 4 . ? 21.175 9.747 54.937 1.00 80.89 ? 302 NAG A O4 1 HETATM 3035 O O5 . NAG E 4 . ? 21.595 10.608 51.401 1.00 69.54 ? 302 NAG A O5 1 HETATM 3036 O O6 . NAG E 4 . ? 20.377 12.219 54.073 1.00 78.82 ? 302 NAG A O6 1 HETATM 3037 O O7 . NAG E 4 . ? 25.578 7.671 50.784 1.00 66.51 ? 302 NAG A O7 1 HETATM 3038 C C1 . NAG F 4 . ? 35.276 -9.321 24.240 1.00 45.68 ? 303 NAG A C1 1 HETATM 3039 C C2 . NAG F 4 . ? 36.200 -10.461 24.678 1.00 47.83 ? 303 NAG A C2 1 HETATM 3040 C C3 . NAG F 4 . ? 37.655 -10.002 24.616 1.00 47.80 ? 303 NAG A C3 1 HETATM 3041 C C4 . NAG F 4 . ? 38.009 -9.316 23.288 1.00 47.98 ? 303 NAG A C4 1 HETATM 3042 C C5 . NAG F 4 . ? 36.938 -8.299 22.883 1.00 46.73 ? 303 NAG A C5 1 HETATM 3043 C C6 . NAG F 4 . ? 37.216 -7.714 21.495 1.00 47.68 ? 303 NAG A C6 1 HETATM 3044 C C7 . NAG F 4 . ? 35.013 -11.933 26.279 1.00 49.22 ? 303 NAG A C7 1 HETATM 3045 C C8 . NAG F 4 . ? 34.817 -12.305 27.718 1.00 49.64 ? 303 NAG A C8 1 HETATM 3046 N N2 . NAG F 4 . ? 35.890 -10.952 26.025 1.00 47.84 ? 303 NAG A N2 1 HETATM 3047 O O3 . NAG F 4 . ? 38.488 -11.143 24.854 1.00 49.47 ? 303 NAG A O3 1 HETATM 3048 O O4 . NAG F 4 . ? 39.248 -8.588 23.416 1.00 47.89 ? 303 NAG A O4 1 HETATM 3049 O O5 . NAG F 4 . ? 35.658 -8.932 22.921 1.00 46.50 ? 303 NAG A O5 1 HETATM 3050 O O6 . NAG F 4 . ? 36.182 -6.793 21.109 1.00 47.67 ? 303 NAG A O6 1 HETATM 3051 O O7 . NAG F 4 . ? 34.375 -12.507 25.412 1.00 50.34 ? 303 NAG A O7 1 HETATM 3052 C C1 . NAG G 4 . ? 40.391 -9.276 22.856 1.00 50.44 ? 304 NAG A C1 1 HETATM 3053 C C2 . NAG G 4 . ? 41.494 -8.294 22.482 1.00 49.99 ? 304 NAG A C2 1 HETATM 3054 C C3 . NAG G 4 . ? 42.692 -9.040 21.886 1.00 52.46 ? 304 NAG A C3 1 HETATM 3055 C C4 . NAG G 4 . ? 43.169 -10.147 22.824 1.00 53.98 ? 304 NAG A C4 1 HETATM 3056 C C5 . NAG G 4 . ? 41.981 -11.027 23.232 1.00 54.52 ? 304 NAG A C5 1 HETATM 3057 C C6 . NAG G 4 . ? 42.357 -12.117 24.244 1.00 56.00 ? 304 NAG A C6 1 HETATM 3058 C C7 . NAG G 4 . ? 41.347 -6.015 21.575 1.00 47.50 ? 304 NAG A C7 1 HETATM 3059 C C8 . NAG G 4 . ? 40.755 -5.144 20.508 1.00 47.01 ? 304 NAG A C8 1 HETATM 3060 N N2 . NAG G 4 . ? 41.002 -7.312 21.533 1.00 48.99 ? 304 NAG A N2 1 HETATM 3061 O O3 . NAG G 4 . ? 43.768 -8.126 21.633 1.00 51.90 ? 304 NAG A O3 1 HETATM 3062 O O4 . NAG G 4 . ? 44.156 -10.956 22.154 1.00 57.21 ? 304 NAG A O4 1 HETATM 3063 O O5 . NAG G 4 . ? 40.939 -10.209 23.780 1.00 52.00 ? 304 NAG A O5 1 HETATM 3064 O O6 . NAG G 4 . ? 42.764 -11.514 25.480 1.00 54.72 ? 304 NAG A O6 1 HETATM 3065 O O7 . NAG G 4 . ? 42.104 -5.539 22.415 1.00 46.45 ? 304 NAG A O7 1 HETATM 3066 C C1 . BMA H 5 . ? 45.532 -10.649 22.468 1.00 57.98 ? 305 BMA A C1 1 HETATM 3067 C C2 . BMA H 5 . ? 46.328 -11.938 22.351 1.00 60.97 ? 305 BMA A C2 1 HETATM 3068 C C3 . BMA H 5 . ? 47.802 -11.669 22.637 1.00 61.67 ? 305 BMA A C3 1 HETATM 3069 C C4 . BMA H 5 . ? 48.353 -10.566 21.747 1.00 60.92 ? 305 BMA A C4 1 HETATM 3070 C C5 . BMA H 5 . ? 47.474 -9.331 21.867 1.00 58.02 ? 305 BMA A C5 1 HETATM 3071 C C6 . BMA H 5 . ? 47.944 -8.278 20.874 1.00 57.67 ? 305 BMA A C6 1 HETATM 3072 O O2 . BMA H 5 . ? 46.171 -12.489 21.039 1.00 62.97 ? 305 BMA A O2 1 HETATM 3073 O O3 . BMA H 5 . ? 48.578 -12.838 22.382 1.00 65.12 ? 305 BMA A O3 1 HETATM 3074 O O4 . BMA H 5 . ? 49.715 -10.278 22.112 1.00 61.22 ? 305 BMA A O4 1 HETATM 3075 O O5 . BMA H 5 . ? 46.102 -9.662 21.602 1.00 57.83 ? 305 BMA A O5 1 HETATM 3076 O O6 . BMA H 5 . ? 47.078 -7.144 20.939 1.00 55.12 ? 305 BMA A O6 1 HETATM 3077 C C1 . MAN I 6 . ? 47.545 -6.101 20.059 1.00 54.95 ? 306 MAN A C1 1 HETATM 3078 C C2 . MAN I 6 . ? 46.816 -4.804 20.396 1.00 52.58 ? 306 MAN A C2 1 HETATM 3079 C C3 . MAN I 6 . ? 45.354 -4.875 19.960 1.00 52.23 ? 306 MAN A C3 1 HETATM 3080 C C4 . MAN I 6 . ? 45.263 -5.314 18.499 1.00 54.40 ? 306 MAN A C4 1 HETATM 3081 C C5 . MAN I 6 . ? 46.019 -6.617 18.279 1.00 56.73 ? 306 MAN A C5 1 HETATM 3082 C C6 . MAN I 6 . ? 45.957 -7.051 16.820 1.00 59.26 ? 306 MAN A C6 1 HETATM 3083 O O2 . MAN I 6 . ? 47.483 -3.712 19.747 1.00 52.42 ? 306 MAN A O2 1 HETATM 3084 O O3 . MAN I 6 . ? 44.703 -3.607 20.125 1.00 50.24 ? 306 MAN A O3 1 HETATM 3085 O O4 . MAN I 6 . ? 43.887 -5.449 18.135 1.00 54.33 ? 306 MAN A O4 1 HETATM 3086 O O5 . MAN I 6 . ? 47.382 -6.424 18.676 1.00 56.85 ? 306 MAN A O5 1 HETATM 3087 O O6 . MAN I 6 . ? 46.976 -8.018 16.543 1.00 61.78 ? 306 MAN A O6 1 HETATM 3088 C C1 . FUC J 7 . ? 36.506 -5.391 21.327 1.00 46.93 ? 307 FUC A C1 1 HETATM 3089 C C2 . FUC J 7 . ? 35.562 -4.533 20.498 1.00 46.65 ? 307 FUC A C2 1 HETATM 3090 C C3 . FUC J 7 . ? 34.124 -4.699 20.998 1.00 46.53 ? 307 FUC A C3 1 HETATM 3091 C C4 . FUC J 7 . ? 34.009 -4.474 22.512 1.00 45.37 ? 307 FUC A C4 1 HETATM 3092 C C5 . FUC J 7 . ? 35.123 -5.173 23.293 1.00 45.80 ? 307 FUC A C5 1 HETATM 3093 C C6 . FUC J 7 . ? 35.147 -4.703 24.748 1.00 44.79 ? 307 FUC A C6 1 HETATM 3094 O O2 . FUC J 7 . ? 35.665 -4.923 19.125 1.00 48.62 ? 307 FUC A O2 1 HETATM 3095 O O3 . FUC J 7 . ? 33.255 -3.795 20.305 1.00 45.89 ? 307 FUC A O3 1 HETATM 3096 O O4 . FUC J 7 . ? 34.025 -3.072 22.806 1.00 43.89 ? 307 FUC A O4 1 HETATM 3097 O O5 . FUC J 7 . ? 36.396 -4.925 22.677 1.00 45.83 ? 307 FUC A O5 1 HETATM 3098 C C1 . MAN K 6 . ? 49.033 -13.443 23.607 1.00 66.38 ? 308 MAN A C1 1 HETATM 3099 C C2 . MAN K 6 . ? 50.126 -14.434 23.247 1.00 69.42 ? 308 MAN A C2 1 HETATM 3100 C C3 . MAN K 6 . ? 49.552 -15.688 22.586 1.00 72.19 ? 308 MAN A C3 1 HETATM 3101 C C4 . MAN K 6 . ? 48.314 -16.242 23.291 1.00 71.91 ? 308 MAN A C4 1 HETATM 3102 C C5 . MAN K 6 . ? 47.314 -15.141 23.650 1.00 68.81 ? 308 MAN A C5 1 HETATM 3103 C C6 . MAN K 6 . ? 46.172 -15.651 24.529 1.00 68.68 ? 308 MAN A C6 1 HETATM 3104 O O2 . MAN K 6 . ? 50.866 -14.769 24.428 1.00 70.17 ? 308 MAN A O2 1 HETATM 3105 O O3 . MAN K 6 . ? 50.563 -16.695 22.566 1.00 74.87 ? 308 MAN A O3 1 HETATM 3106 O O4 . MAN K 6 . ? 47.695 -17.186 22.412 1.00 74.10 ? 308 MAN A O4 1 HETATM 3107 O O5 . MAN K 6 . ? 47.975 -14.072 24.341 1.00 66.65 ? 308 MAN A O5 1 HETATM 3108 O O6 . MAN K 6 . ? 45.098 -14.694 24.508 1.00 66.23 ? 308 MAN A O6 1 HETATM 3109 C C1 . NAG L 4 . ? 28.342 20.995 49.355 1.00 65.27 ? 309 NAG A C1 1 HETATM 3110 C C2 . NAG L 4 . ? 28.173 22.244 50.228 1.00 69.31 ? 309 NAG A C2 1 HETATM 3111 C C3 . NAG L 4 . ? 26.692 22.574 50.423 1.00 70.73 ? 309 NAG A C3 1 HETATM 3112 C C4 . NAG L 4 . ? 25.968 22.676 49.087 1.00 67.61 ? 309 NAG A C4 1 HETATM 3113 C C5 . NAG L 4 . ? 26.230 21.417 48.260 1.00 64.02 ? 309 NAG A C5 1 HETATM 3114 C C6 . NAG L 4 . ? 25.586 21.487 46.873 1.00 61.08 ? 309 NAG A C6 1 HETATM 3115 C C7 . NAG L 4 . ? 30.077 22.402 51.808 1.00 73.60 ? 309 NAG A C7 1 HETATM 3116 C C8 . NAG L 4 . ? 30.516 22.175 53.228 1.00 77.29 ? 309 NAG A C8 1 HETATM 3117 N N2 . NAG L 4 . ? 28.801 22.092 51.538 1.00 72.72 ? 309 NAG A N2 1 HETATM 3118 O O3 . NAG L 4 . ? 26.580 23.814 51.123 1.00 74.31 ? 309 NAG A O3 1 HETATM 3119 O O4 . NAG L 4 . ? 24.557 22.843 49.297 1.00 69.03 ? 309 NAG A O4 1 HETATM 3120 O O5 . NAG L 4 . ? 27.640 21.189 48.122 1.00 62.71 ? 309 NAG A O5 1 HETATM 3121 O O6 . NAG L 4 . ? 25.948 22.686 46.177 1.00 60.84 ? 309 NAG A O6 1 HETATM 3122 O O7 . NAG L 4 . ? 30.851 22.835 50.967 1.00 71.78 ? 309 NAG A O7 1 HETATM 3123 C C1 . CIT M 8 . ? 21.933 1.949 33.765 1.00 61.22 ? 310 CIT A C1 1 HETATM 3124 O O1 . CIT M 8 . ? 21.493 1.038 33.021 1.00 61.40 ? 310 CIT A O1 1 HETATM 3125 O O2 . CIT M 8 . ? 21.212 2.925 34.077 1.00 61.46 ? 310 CIT A O2 1 HETATM 3126 C C2 . CIT M 8 . ? 23.354 1.818 34.319 1.00 60.67 ? 310 CIT A C2 1 HETATM 3127 C C3 . CIT M 8 . ? 24.276 3.062 34.260 1.00 59.17 ? 310 CIT A C3 1 HETATM 3128 O O7 . CIT M 8 . ? 23.562 4.250 33.904 1.00 58.85 ? 310 CIT A O7 1 HETATM 3129 C C4 . CIT M 8 . ? 24.985 3.315 35.603 1.00 59.01 ? 310 CIT A C4 1 HETATM 3130 C C5 . CIT M 8 . ? 24.255 4.028 36.739 1.00 59.79 ? 310 CIT A C5 1 HETATM 3131 O O3 . CIT M 8 . ? 23.252 4.747 36.541 1.00 58.51 ? 310 CIT A O3 1 HETATM 3132 O O4 . CIT M 8 . ? 24.715 3.882 37.897 1.00 60.79 ? 310 CIT A O4 1 HETATM 3133 C C6 . CIT M 8 . ? 25.400 2.865 33.239 1.00 58.76 ? 310 CIT A C6 1 HETATM 3134 O O5 . CIT M 8 . ? 25.417 3.557 32.192 1.00 57.70 ? 310 CIT A O5 1 HETATM 3135 O O6 . CIT M 8 . ? 26.312 2.032 33.475 1.00 59.58 ? 310 CIT A O6 1 HETATM 3136 NA NA . NA N 9 . ? 21.237 6.847 38.694 1.00 45.74 ? 311 NA A NA 1 HETATM 3137 C C1 . PLM O 10 . ? 30.296 -3.392 36.994 1.00 61.04 ? 101 PLM C C1 1 HETATM 3138 O O2 . PLM O 10 . ? 30.662 -4.143 36.110 1.00 62.11 ? 101 PLM C O2 1 HETATM 3139 C C2 . PLM O 10 . ? 29.540 -2.168 36.501 1.00 58.91 ? 101 PLM C C2 1 HETATM 3140 C C3 . PLM O 10 . ? 30.335 -1.459 35.395 1.00 56.27 ? 101 PLM C C3 1 HETATM 3141 C C4 . PLM O 10 . ? 29.648 -0.193 34.880 1.00 54.55 ? 101 PLM C C4 1 HETATM 3142 C C5 . PLM O 10 . ? 29.595 -0.089 33.353 1.00 52.83 ? 101 PLM C C5 1 HETATM 3143 C C6 . PLM O 10 . ? 28.684 -1.143 32.715 1.00 53.10 ? 101 PLM C C6 1 HETATM 3144 C C7 . PLM O 10 . ? 27.888 -0.608 31.519 1.00 51.64 ? 101 PLM C C7 1 HETATM 3145 C C8 . PLM O 10 . ? 27.535 -1.724 30.533 1.00 51.77 ? 101 PLM C C8 1 HETATM 3146 C C9 . PLM O 10 . ? 26.258 -1.412 29.757 1.00 51.02 ? 101 PLM C C9 1 HETATM 3147 C CA . PLM O 10 . ? 26.004 -2.414 28.632 1.00 51.28 ? 101 PLM C CA 1 HETATM 3148 C CB . PLM O 10 . ? 24.509 -2.551 28.352 1.00 51.54 ? 101 PLM C CB 1 HETATM 3149 C CC . PLM O 10 . ? 23.868 -3.686 29.149 1.00 52.96 ? 101 PLM C CC 1 HETATM 3150 C CD . PLM O 10 . ? 22.343 -3.557 29.185 1.00 53.21 ? 101 PLM C CD 1 HETATM 3151 C CE . PLM O 10 . ? 21.876 -2.871 30.474 1.00 53.13 ? 101 PLM C CE 1 HETATM 3152 C CF . PLM O 10 . ? 20.383 -2.541 30.479 1.00 53.03 ? 101 PLM C CF 1 HETATM 3153 C CG . PLM O 10 . ? 20.088 -1.202 31.130 1.00 52.20 ? 101 PLM C CG 1 HETATM 3154 C C1 . OCA P 11 . ? 34.163 1.857 36.886 1.00 59.47 ? 102 OCA C C1 1 HETATM 3155 C C2 . OCA P 11 . ? 34.053 3.000 35.900 1.00 56.68 ? 102 OCA C C2 1 HETATM 3156 C C3 . OCA P 11 . ? 35.425 3.512 35.449 1.00 55.29 ? 102 OCA C C3 1 HETATM 3157 C C4 . OCA P 11 . ? 35.834 4.808 36.150 1.00 54.85 ? 102 OCA C C4 1 HETATM 3158 C C5 . OCA P 11 . ? 36.728 5.710 35.304 1.00 53.43 ? 102 OCA C C5 1 HETATM 3159 C C6 . OCA P 11 . ? 36.686 7.124 35.879 1.00 53.41 ? 102 OCA C C6 1 HETATM 3160 C C7 . OCA P 11 . ? 37.663 8.073 35.200 1.00 52.70 ? 102 OCA C C7 1 HETATM 3161 C C8 . OCA P 11 . ? 37.503 9.476 35.751 1.00 52.99 ? 102 OCA C C8 1 HETATM 3162 O O1 . OCA P 11 . ? 33.518 0.809 36.635 1.00 60.31 ? 102 OCA C O1 1 HETATM 3163 O O2 . OCA P 11 . ? 34.879 2.001 37.913 1.00 61.53 ? 102 OCA C O2 1 HETATM 3164 O O . HOH Q 12 . ? 27.071 9.182 24.050 1.00 28.91 ? 401 HOH A O 1 HETATM 3165 O O . HOH Q 12 . ? 11.942 9.566 24.117 1.00 26.00 ? 402 HOH A O 1 HETATM 3166 O O . HOH Q 12 . ? 4.480 23.281 -6.873 1.00 38.04 ? 403 HOH A O 1 HETATM 3167 O O . HOH Q 12 . ? 18.647 31.562 2.650 1.00 23.19 ? 404 HOH A O 1 HETATM 3168 O O . HOH Q 12 . ? 6.025 9.444 1.340 1.00 40.85 ? 405 HOH A O 1 HETATM 3169 O O . HOH Q 12 . ? 17.934 31.776 5.308 1.00 27.47 ? 406 HOH A O 1 HETATM 3170 O O . HOH Q 12 . ? 43.226 16.377 24.292 1.00 26.66 ? 407 HOH A O 1 HETATM 3171 O O . HOH Q 12 . ? 2.444 14.095 15.060 1.00 21.88 ? 408 HOH A O 1 HETATM 3172 O O . HOH Q 12 . ? 6.599 6.874 25.241 1.00 35.44 ? 409 HOH A O 1 HETATM 3173 O O . HOH Q 12 . ? 26.605 9.936 43.117 1.00 33.96 ? 410 HOH A O 1 HETATM 3174 O O . HOH Q 12 . ? 48.417 14.727 35.444 1.00 35.87 ? 411 HOH A O 1 HETATM 3175 O O . HOH Q 12 . ? 3.844 8.930 18.637 1.00 32.00 ? 412 HOH A O 1 HETATM 3176 O O . HOH Q 12 . ? 6.924 6.732 20.750 1.00 29.26 ? 413 HOH A O 1 HETATM 3177 O O . HOH Q 12 . ? 20.895 6.366 21.096 1.00 32.99 ? 414 HOH A O 1 HETATM 3178 O O . HOH Q 12 . ? 0.025 16.618 7.610 1.00 29.71 ? 415 HOH A O 1 HETATM 3179 O O . HOH Q 12 . ? 40.332 -10.586 30.666 1.00 34.39 ? 416 HOH A O 1 HETATM 3180 O O . HOH Q 12 . ? 41.257 -12.163 27.645 1.00 43.85 ? 417 HOH A O 1 HETATM 3181 O O . HOH Q 12 . ? 0.498 11.312 12.206 1.00 32.30 ? 418 HOH A O 1 HETATM 3182 O O . HOH Q 12 . ? 15.188 32.129 -4.194 1.00 44.91 ? 419 HOH A O 1 HETATM 3183 O O . HOH Q 12 . ? 36.097 14.993 24.681 1.00 25.85 ? 420 HOH A O 1 HETATM 3184 O O . HOH Q 12 . ? 12.707 4.226 16.081 1.00 31.28 ? 421 HOH A O 1 HETATM 3185 O O . HOH Q 12 . ? 34.773 1.496 24.281 1.00 28.19 ? 422 HOH A O 1 HETATM 3186 O O . HOH Q 12 . ? 21.999 2.875 44.598 1.00 36.54 ? 423 HOH A O 1 HETATM 3187 O O . HOH Q 12 . ? -0.109 21.138 -1.838 1.00 23.57 ? 424 HOH A O 1 HETATM 3188 O O . HOH Q 12 . ? 20.035 24.230 0.320 1.00 20.03 ? 425 HOH A O 1 HETATM 3189 O O . HOH Q 12 . ? 20.055 31.602 7.034 1.00 30.47 ? 426 HOH A O 1 HETATM 3190 O O . HOH Q 12 . ? 9.767 4.496 12.821 1.00 26.24 ? 427 HOH A O 1 HETATM 3191 O O . HOH Q 12 . ? 9.968 13.506 23.240 1.00 23.86 ? 428 HOH A O 1 HETATM 3192 O O . HOH Q 12 . ? 8.972 -4.457 29.586 1.00 35.72 ? 429 HOH A O 1 HETATM 3193 O O . HOH Q 12 . ? 48.987 11.222 25.909 1.00 36.81 ? 430 HOH A O 1 HETATM 3194 O O . HOH Q 12 . ? 15.140 23.549 12.883 1.00 17.64 ? 431 HOH A O 1 HETATM 3195 O O . HOH Q 12 . ? 49.316 8.292 37.277 1.00 37.37 ? 432 HOH A O 1 HETATM 3196 O O . HOH Q 12 . ? 18.428 24.870 14.505 1.00 24.13 ? 433 HOH A O 1 HETATM 3197 O O . HOH Q 12 . ? 39.858 13.356 24.423 1.00 24.66 ? 434 HOH A O 1 HETATM 3198 O O . HOH Q 12 . ? 30.186 21.421 38.367 1.00 35.74 ? 435 HOH A O 1 HETATM 3199 O O . HOH Q 12 . ? 7.741 2.266 9.766 1.00 42.61 ? 436 HOH A O 1 HETATM 3200 O O . HOH Q 12 . ? 11.302 9.046 8.017 1.00 32.95 ? 437 HOH A O 1 HETATM 3201 O O . HOH Q 12 . ? 2.551 4.415 13.255 1.00 40.79 ? 438 HOH A O 1 HETATM 3202 O O . HOH Q 12 . ? 24.055 25.366 8.114 1.00 41.27 ? 439 HOH A O 1 HETATM 3203 O O . HOH Q 12 . ? 6.398 19.457 22.294 1.00 17.55 ? 440 HOH A O 1 HETATM 3204 O O . HOH Q 12 . ? 39.223 16.799 31.368 1.00 31.51 ? 441 HOH A O 1 HETATM 3205 O O . HOH Q 12 . ? 32.403 14.916 32.436 1.00 25.57 ? 442 HOH A O 1 HETATM 3206 O O . HOH Q 12 . ? 13.839 8.531 14.200 1.00 25.48 ? 443 HOH A O 1 HETATM 3207 O O . HOH Q 12 . ? 35.703 2.678 21.713 1.00 38.68 ? 444 HOH A O 1 HETATM 3208 O O . HOH Q 12 . ? 3.920 31.061 -4.185 1.00 28.20 ? 445 HOH A O 1 HETATM 3209 O O . HOH Q 12 . ? 17.875 27.677 9.339 1.00 27.41 ? 446 HOH A O 1 HETATM 3210 O O . HOH Q 12 . ? 47.160 -3.471 35.748 1.00 37.46 ? 447 HOH A O 1 HETATM 3211 O O . HOH Q 12 . ? 49.090 15.120 31.838 1.00 40.46 ? 448 HOH A O 1 HETATM 3212 O O . HOH Q 12 . ? 6.424 12.333 1.121 1.00 25.85 ? 449 HOH A O 1 HETATM 3213 O O . HOH Q 12 . ? 0.731 14.644 20.877 1.00 38.60 ? 450 HOH A O 1 HETATM 3214 O O . HOH Q 12 . ? 47.058 4.763 31.404 1.00 35.15 ? 451 HOH A O 1 HETATM 3215 O O . HOH Q 12 . ? 9.010 -6.185 27.262 1.00 33.31 ? 452 HOH A O 1 HETATM 3216 O O . HOH Q 12 . ? 20.574 23.664 4.561 1.00 25.22 ? 453 HOH A O 1 HETATM 3217 O O . HOH Q 12 . ? 0.869 15.380 13.055 1.00 34.89 ? 454 HOH A O 1 HETATM 3218 O O . HOH Q 12 . ? 20.639 5.060 16.527 1.00 38.06 ? 455 HOH A O 1 HETATM 3219 O O . HOH Q 12 . ? 3.210 11.477 19.595 1.00 30.83 ? 456 HOH A O 1 HETATM 3220 O O . HOH Q 12 . ? 18.672 24.482 -8.149 1.00 45.53 ? 457 HOH A O 1 HETATM 3221 O O . HOH Q 12 . ? 17.799 10.428 34.991 1.00 29.97 ? 458 HOH A O 1 HETATM 3222 O O . HOH Q 12 . ? 11.297 13.751 20.241 1.00 24.90 ? 459 HOH A O 1 HETATM 3223 O O . HOH Q 12 . ? 3.803 1.212 14.231 1.00 46.26 ? 460 HOH A O 1 HETATM 3224 O O . HOH Q 12 . ? 6.618 26.668 -6.647 1.00 27.06 ? 461 HOH A O 1 HETATM 3225 O O . HOH Q 12 . ? 17.959 29.918 -3.495 1.00 22.48 ? 462 HOH A O 1 HETATM 3226 O O . HOH Q 12 . ? 43.241 11.453 21.720 1.00 31.18 ? 463 HOH A O 1 HETATM 3227 O O . HOH Q 12 . ? 16.069 28.048 11.544 1.00 28.23 ? 464 HOH A O 1 HETATM 3228 O O . HOH Q 12 . ? 11.532 -3.443 15.659 1.00 44.91 ? 465 HOH A O 1 HETATM 3229 O O . HOH Q 12 . ? 42.669 13.845 24.981 1.00 25.31 ? 466 HOH A O 1 HETATM 3230 O O . HOH Q 12 . ? 12.198 11.275 20.846 1.00 35.23 ? 467 HOH A O 1 HETATM 3231 O O . HOH Q 12 . ? 19.471 19.772 17.955 1.00 24.42 ? 468 HOH A O 1 HETATM 3232 O O . HOH Q 12 . ? 38.845 -3.975 35.579 1.00 36.69 ? 469 HOH A O 1 HETATM 3233 O O . HOH Q 12 . ? 46.766 9.656 30.975 1.00 36.90 ? 470 HOH A O 1 HETATM 3234 O O . HOH Q 12 . ? 7.950 11.858 -2.697 1.00 45.31 ? 471 HOH A O 1 HETATM 3235 O O . HOH Q 12 . ? 29.557 18.811 40.582 1.00 37.91 ? 472 HOH A O 1 HETATM 3236 O O . HOH Q 12 . ? 41.521 13.798 27.524 1.00 29.40 ? 473 HOH A O 1 HETATM 3237 O O . HOH Q 12 . ? 11.233 10.281 5.317 1.00 29.97 ? 474 HOH A O 1 HETATM 3238 O O . HOH Q 12 . ? 16.645 17.241 6.046 1.00 33.20 ? 475 HOH A O 1 HETATM 3239 O O . HOH Q 12 . ? 7.818 -8.153 17.470 1.00 36.98 ? 476 HOH A O 1 HETATM 3240 O O . HOH Q 12 . ? 45.834 16.697 29.730 1.00 44.08 ? 477 HOH A O 1 HETATM 3241 O O . HOH Q 12 . ? 10.479 4.991 7.826 1.00 29.87 ? 478 HOH A O 1 HETATM 3242 O O . HOH Q 12 . ? 20.234 18.153 13.956 1.00 23.75 ? 479 HOH A O 1 HETATM 3243 O O . HOH Q 12 . ? 15.166 28.667 -9.380 1.00 33.30 ? 480 HOH A O 1 HETATM 3244 O O . HOH Q 12 . ? 50.579 9.289 30.030 1.00 50.34 ? 481 HOH A O 1 HETATM 3245 O O . HOH Q 12 . ? 16.803 -10.508 24.575 1.00 38.92 ? 482 HOH A O 1 HETATM 3246 O O . HOH Q 12 . ? 34.952 17.585 24.961 1.00 32.50 ? 483 HOH A O 1 HETATM 3247 O O . HOH Q 12 . ? 1.245 7.254 7.990 1.00 36.19 ? 484 HOH A O 1 HETATM 3248 O O . HOH Q 12 . ? 7.733 21.571 -5.865 1.00 36.97 ? 485 HOH A O 1 HETATM 3249 O O . HOH Q 12 . ? 45.392 17.194 26.016 1.00 31.49 ? 486 HOH A O 1 HETATM 3250 O O . HOH Q 12 . ? 4.724 35.486 9.163 1.00 35.76 ? 487 HOH A O 1 HETATM 3251 O O . HOH Q 12 . ? 18.843 28.074 -6.258 1.00 25.75 ? 488 HOH A O 1 HETATM 3252 O O . HOH Q 12 . ? 42.567 -5.933 32.915 1.00 41.85 ? 489 HOH A O 1 HETATM 3253 O O . HOH Q 12 . ? 0.889 20.611 6.675 1.00 24.44 ? 490 HOH A O 1 HETATM 3254 O O . HOH Q 12 . ? 40.201 -4.403 33.043 1.00 40.15 ? 491 HOH A O 1 HETATM 3255 O O . HOH Q 12 . ? 33.793 9.388 23.172 1.00 36.87 ? 492 HOH A O 1 HETATM 3256 O O . HOH Q 12 . ? 14.296 6.501 38.512 1.00 35.18 ? 493 HOH A O 1 HETATM 3257 O O . HOH Q 12 . ? 2.004 30.945 10.179 1.00 38.77 ? 494 HOH A O 1 HETATM 3258 O O . HOH Q 12 . ? 6.593 7.027 29.171 1.00 44.33 ? 495 HOH A O 1 HETATM 3259 O O . HOH Q 12 . ? 47.035 9.163 28.124 1.00 38.49 ? 496 HOH A O 1 HETATM 3260 O O . HOH Q 12 . ? 28.269 14.874 34.890 1.00 27.27 ? 497 HOH A O 1 HETATM 3261 O O . HOH Q 12 . ? 46.030 3.337 29.166 1.00 32.70 ? 498 HOH A O 1 HETATM 3262 O O . HOH Q 12 . ? 7.886 27.487 16.038 1.00 27.40 ? 499 HOH A O 1 HETATM 3263 O O . HOH Q 12 . ? 18.426 11.939 17.906 1.00 41.45 ? 500 HOH A O 1 HETATM 3264 O O . HOH Q 12 . ? 30.202 7.283 23.607 1.00 38.02 ? 501 HOH A O 1 HETATM 3265 O O . HOH Q 12 . ? 16.535 21.586 -8.660 1.00 32.09 ? 502 HOH A O 1 HETATM 3266 O O . HOH Q 12 . ? 46.754 0.302 32.869 1.00 33.73 ? 503 HOH A O 1 HETATM 3267 O O . HOH Q 12 . ? 19.553 9.631 21.717 1.00 32.72 ? 504 HOH A O 1 HETATM 3268 O O . HOH Q 12 . ? 13.997 32.396 11.788 1.00 37.47 ? 505 HOH A O 1 HETATM 3269 O O . HOH Q 12 . ? 16.141 18.456 3.365 1.00 32.21 ? 506 HOH A O 1 HETATM 3270 O O . HOH Q 12 . ? 0.130 19.938 0.872 1.00 31.45 ? 507 HOH A O 1 HETATM 3271 O O . HOH Q 12 . ? 16.924 13.819 7.257 1.00 31.49 ? 508 HOH A O 1 HETATM 3272 O O . HOH Q 12 . ? 1.709 13.141 17.795 1.00 44.67 ? 509 HOH A O 1 HETATM 3273 O O . HOH Q 12 . ? 1.953 17.111 21.985 1.00 27.27 ? 510 HOH A O 1 HETATM 3274 O O . HOH Q 12 . ? 47.372 4.634 26.972 1.00 41.59 ? 511 HOH A O 1 HETATM 3275 O O . HOH Q 12 . ? 14.080 5.869 14.324 1.00 33.17 ? 512 HOH A O 1 HETATM 3276 O O . HOH Q 12 . ? 1.619 34.909 0.337 1.00 57.37 ? 513 HOH A O 1 HETATM 3277 O O . HOH Q 12 . ? 11.523 -6.305 14.920 1.00 48.33 ? 514 HOH A O 1 HETATM 3278 O O . HOH Q 12 . ? 12.636 11.817 3.192 1.00 46.12 ? 515 HOH A O 1 HETATM 3279 O O . HOH Q 12 . ? 4.329 17.837 23.186 1.00 25.57 ? 516 HOH A O 1 HETATM 3280 O O . HOH Q 12 . ? 19.142 22.824 -2.680 1.00 32.29 ? 517 HOH A O 1 HETATM 3281 O O . HOH Q 12 . ? 16.038 26.163 13.613 1.00 21.92 ? 518 HOH A O 1 HETATM 3282 O O . HOH Q 12 . ? 26.834 7.801 21.655 1.00 37.72 ? 519 HOH A O 1 HETATM 3283 O O . HOH Q 12 . ? 21.764 18.934 16.330 1.00 37.45 ? 520 HOH A O 1 HETATM 3284 O O . HOH Q 12 . ? 41.371 15.879 29.548 1.00 41.13 ? 521 HOH A O 1 HETATM 3285 O O . HOH Q 12 . ? 12.735 6.771 7.340 1.00 38.67 ? 522 HOH A O 1 HETATM 3286 O O . HOH Q 12 . ? 34.741 8.989 20.508 1.00 48.41 ? 523 HOH A O 1 HETATM 3287 O O . HOH Q 12 . ? 9.368 3.662 5.450 1.00 44.64 ? 524 HOH A O 1 HETATM 3288 O O . HOH Q 12 . ? 23.180 23.744 5.874 1.00 45.49 ? 525 HOH A O 1 HETATM 3289 O O . HOH Q 12 . ? 29.726 6.193 20.814 1.00 51.52 ? 526 HOH A O 1 HETATM 3290 O O . HOH Q 12 . ? 18.092 9.938 11.522 1.00 44.39 ? 527 HOH A O 1 HETATM 3291 O O . HOH Q 12 . ? 8.827 -0.061 8.186 1.00 57.35 ? 528 HOH A O 1 HETATM 3292 O O . HOH Q 12 . ? 14.024 5.643 9.705 1.00 42.46 ? 529 HOH A O 1 HETATM 3293 O O . HOH R 12 . ? 2.734 25.452 32.619 1.00 56.04 ? 101 HOH B O 1 HETATM 3294 O O . HOH R 12 . ? 5.428 29.044 16.529 1.00 32.15 ? 102 HOH B O 1 HETATM 3295 O O . HOH R 12 . ? 5.181 29.901 13.822 1.00 30.80 ? 103 HOH B O 1 HETATM 3296 O O . HOH R 12 . ? 9.799 18.588 28.066 1.00 28.21 ? 104 HOH B O 1 HETATM 3297 O O . HOH R 12 . ? 22.300 22.854 19.822 1.00 33.33 ? 105 HOH B O 1 HETATM 3298 O O . HOH R 12 . ? 17.299 15.933 21.140 1.00 26.84 ? 106 HOH B O 1 HETATM 3299 O O . HOH R 12 . ? 20.429 18.192 20.043 1.00 31.36 ? 107 HOH B O 1 HETATM 3300 O O . HOH R 12 . ? 15.797 27.292 16.193 1.00 33.38 ? 108 HOH B O 1 HETATM 3301 O O . HOH R 12 . ? 0.714 20.225 14.352 1.00 22.97 ? 109 HOH B O 1 HETATM 3302 O O . HOH R 12 . ? -0.902 30.905 27.788 1.00 34.62 ? 110 HOH B O 1 HETATM 3303 O O . HOH R 12 . ? 17.118 30.993 19.489 1.00 26.67 ? 111 HOH B O 1 HETATM 3304 O O . HOH R 12 . ? 12.972 12.673 29.562 1.00 31.78 ? 112 HOH B O 1 HETATM 3305 O O . HOH R 12 . ? -8.230 29.395 14.931 1.00 46.14 ? 113 HOH B O 1 HETATM 3306 O O . HOH R 12 . ? -1.503 40.475 26.503 1.00 41.92 ? 114 HOH B O 1 HETATM 3307 O O . HOH R 12 . ? -5.334 37.892 20.191 1.00 37.08 ? 115 HOH B O 1 HETATM 3308 O O . HOH R 12 . ? 10.554 31.387 18.136 1.00 23.72 ? 116 HOH B O 1 HETATM 3309 O O . HOH R 12 . ? 25.698 26.229 36.002 1.00 30.90 ? 117 HOH B O 1 HETATM 3310 O O . HOH R 12 . ? 6.504 36.214 22.315 1.00 27.81 ? 118 HOH B O 1 HETATM 3311 O O . HOH R 12 . ? 24.022 19.433 23.710 1.00 21.01 ? 119 HOH B O 1 HETATM 3312 O O . HOH R 12 . ? 17.318 15.738 27.453 1.00 31.78 ? 120 HOH B O 1 HETATM 3313 O O . HOH R 12 . ? -2.241 23.703 18.782 1.00 24.86 ? 121 HOH B O 1 HETATM 3314 O O . HOH R 12 . ? 29.693 18.552 28.788 1.00 26.51 ? 122 HOH B O 1 HETATM 3315 O O . HOH R 12 . ? 33.269 20.378 34.964 1.00 29.65 ? 123 HOH B O 1 HETATM 3316 O O . HOH R 12 . ? 12.851 32.816 18.890 1.00 35.40 ? 124 HOH B O 1 HETATM 3317 O O . HOH R 12 . ? -3.070 26.750 26.905 1.00 33.59 ? 125 HOH B O 1 HETATM 3318 O O . HOH R 12 . ? -2.747 24.769 14.408 1.00 45.27 ? 126 HOH B O 1 HETATM 3319 O O . HOH R 12 . ? 19.193 24.908 21.780 1.00 20.15 ? 127 HOH B O 1 HETATM 3320 O O . HOH R 12 . ? 30.197 27.722 24.996 1.00 30.69 ? 128 HOH B O 1 HETATM 3321 O O . HOH R 12 . ? 31.721 18.911 26.915 1.00 35.02 ? 129 HOH B O 1 HETATM 3322 O O . HOH R 12 . ? 27.988 26.269 23.551 1.00 33.42 ? 130 HOH B O 1 HETATM 3323 O O . HOH R 12 . ? 33.181 20.833 28.530 1.00 47.74 ? 131 HOH B O 1 HETATM 3324 O O . HOH R 12 . ? -0.586 18.598 21.515 1.00 30.39 ? 132 HOH B O 1 HETATM 3325 O O . HOH R 12 . ? 1.244 35.264 21.996 1.00 35.66 ? 133 HOH B O 1 HETATM 3326 O O . HOH R 12 . ? 9.014 30.158 15.967 1.00 35.13 ? 134 HOH B O 1 HETATM 3327 O O . HOH R 12 . ? 20.910 30.630 22.103 1.00 25.00 ? 135 HOH B O 1 HETATM 3328 O O . HOH R 12 . ? 2.092 17.809 14.005 1.00 23.89 ? 136 HOH B O 1 HETATM 3329 O O . HOH R 12 . ? 34.511 11.953 22.617 1.00 30.48 ? 137 HOH B O 1 HETATM 3330 O O . HOH R 12 . ? -2.564 24.005 25.602 1.00 35.51 ? 138 HOH B O 1 HETATM 3331 O O . HOH R 12 . ? 16.916 15.299 34.793 1.00 38.01 ? 139 HOH B O 1 HETATM 3332 O O . HOH R 12 . ? -0.267 37.566 31.710 1.00 42.50 ? 140 HOH B O 1 HETATM 3333 O O . HOH R 12 . ? 15.178 24.451 35.712 1.00 33.87 ? 141 HOH B O 1 HETATM 3334 O O . HOH R 12 . ? -2.093 27.820 18.582 1.00 18.25 ? 142 HOH B O 1 HETATM 3335 O O . HOH R 12 . ? 20.136 22.428 18.108 1.00 21.32 ? 143 HOH B O 1 HETATM 3336 O O . HOH R 12 . ? 1.799 23.029 30.897 1.00 33.02 ? 144 HOH B O 1 HETATM 3337 O O . HOH R 12 . ? -2.985 25.701 17.017 1.00 35.90 ? 145 HOH B O 1 HETATM 3338 O O . HOH R 12 . ? 18.966 12.809 33.894 1.00 31.03 ? 146 HOH B O 1 HETATM 3339 O O . HOH R 12 . ? 8.975 28.693 34.465 1.00 25.88 ? 147 HOH B O 1 HETATM 3340 O O . HOH R 12 . ? 14.410 30.375 19.171 1.00 20.18 ? 148 HOH B O 1 HETATM 3341 O O . HOH R 12 . ? 15.014 36.744 21.796 1.00 26.32 ? 149 HOH B O 1 HETATM 3342 O O . HOH R 12 . ? 27.110 15.827 19.762 1.00 35.92 ? 150 HOH B O 1 HETATM 3343 O O . HOH R 12 . ? 24.459 12.972 19.762 1.00 39.76 ? 151 HOH B O 1 HETATM 3344 O O . HOH R 12 . ? 26.027 32.333 36.817 1.00 40.02 ? 152 HOH B O 1 HETATM 3345 O O . HOH R 12 . ? 23.273 32.853 34.176 1.00 28.75 ? 153 HOH B O 1 HETATM 3346 O O . HOH R 12 . ? 7.563 37.109 28.282 1.00 30.61 ? 154 HOH B O 1 HETATM 3347 O O . HOH R 12 . ? -3.432 33.505 14.371 1.00 32.78 ? 155 HOH B O 1 HETATM 3348 O O . HOH R 12 . ? 26.255 36.728 30.408 1.00 34.45 ? 156 HOH B O 1 HETATM 3349 O O . HOH R 12 . ? 5.214 35.998 18.209 1.00 34.74 ? 157 HOH B O 1 HETATM 3350 O O . HOH R 12 . ? 14.061 38.153 31.302 1.00 40.41 ? 158 HOH B O 1 HETATM 3351 O O . HOH R 12 . ? 29.386 10.818 24.504 1.00 35.79 ? 159 HOH B O 1 HETATM 3352 O O . HOH R 12 . ? 29.359 36.144 30.846 1.00 47.14 ? 160 HOH B O 1 HETATM 3353 O O . HOH R 12 . ? -6.632 35.380 20.865 1.00 35.65 ? 161 HOH B O 1 HETATM 3354 O O . HOH R 12 . ? 19.430 37.808 26.737 1.00 32.41 ? 162 HOH B O 1 HETATM 3355 O O . HOH R 12 . ? 21.358 15.114 20.540 1.00 42.27 ? 163 HOH B O 1 HETATM 3356 O O . HOH R 12 . ? 13.420 28.447 16.829 1.00 41.53 ? 164 HOH B O 1 HETATM 3357 O O . HOH R 12 . ? 15.507 11.298 36.340 1.00 38.08 ? 165 HOH B O 1 HETATM 3358 O O . HOH R 12 . ? 28.119 21.168 41.556 1.00 52.43 ? 166 HOH B O 1 HETATM 3359 O O . HOH R 12 . ? 29.671 30.689 23.833 1.00 52.73 ? 167 HOH B O 1 HETATM 3360 O O . HOH R 12 . ? -1.792 21.242 22.044 1.00 33.58 ? 168 HOH B O 1 HETATM 3361 O O . HOH R 12 . ? -3.554 21.222 17.747 1.00 35.55 ? 169 HOH B O 1 HETATM 3362 O O . HOH R 12 . ? 16.135 13.974 22.826 1.00 32.97 ? 170 HOH B O 1 HETATM 3363 O O . HOH R 12 . ? -1.800 20.352 13.415 1.00 27.18 ? 171 HOH B O 1 HETATM 3364 O O . HOH R 12 . ? -3.014 22.173 15.169 1.00 39.44 ? 172 HOH B O 1 HETATM 3365 O O . HOH R 12 . ? 27.020 25.052 38.343 1.00 37.99 ? 173 HOH B O 1 HETATM 3366 O O . HOH R 12 . ? 32.059 22.432 36.489 1.00 43.96 ? 174 HOH B O 1 HETATM 3367 O O . HOH S 12 . ? 43.629 4.408 42.668 1.00 38.64 ? 201 HOH C 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 . LYS A 6 ? 0.8948 0.7386 0.7169 0.1914 -0.2987 -0.1701 6 LYS A N 2 C CA . LYS A 6 ? 0.8669 0.7153 0.6722 0.1818 -0.2709 -0.1366 6 LYS A CA 3 C C . LYS A 6 ? 0.8447 0.6748 0.6678 0.1756 -0.2574 -0.1332 6 LYS A C 4 O O . LYS A 6 ? 0.8456 0.6523 0.7045 0.1722 -0.2676 -0.1461 6 LYS A O 5 C CB . LYS A 6 ? 0.8469 0.6847 0.6674 0.1658 -0.2650 -0.1079 6 LYS A CB 6 N N . ASN A 7 ? 0.8259 0.6676 0.6271 0.1739 -0.2354 -0.1139 7 ASN A N 7 C CA . ASN A 7 ? 0.8037 0.6325 0.6164 0.1688 -0.2219 -0.1086 7 ASN A CA 8 C C . ASN A 7 ? 0.7674 0.5806 0.5951 0.1505 -0.2061 -0.0790 7 ASN A C 9 O O . ASN A 7 ? 0.7683 0.5946 0.5786 0.1473 -0.1906 -0.0584 7 ASN A O 10 C CB . ASN A 7 ? 0.8131 0.6680 0.5935 0.1810 -0.2090 -0.1105 7 ASN A CB 11 N N . TYR A 8 ? 0.7408 0.5286 0.6030 0.1391 -0.2101 -0.0771 8 TYR A N 12 C CA . TYR A 8 ? 0.7017 0.4782 0.5781 0.1224 -0.1959 -0.0526 8 TYR A CA 13 C C . TYR A 8 ? 0.6767 0.4524 0.5479 0.1188 -0.1799 -0.0421 8 TYR A C 14 O O . TYR A 8 ? 0.6863 0.4586 0.5609 0.1248 -0.1831 -0.0533 8 TYR A O 15 C CB . TYR A 8 ? 0.6977 0.4530 0.6125 0.1116 -0.2048 -0.0518 8 TYR A CB 16 C CG . TYR A 8 ? 0.7079 0.4613 0.6356 0.1120 -0.2200 -0.0585 8 TYR A CG 17 C CD1 . TYR A 8 ? 0.7334 0.4849 0.6703 0.1227 -0.2418 -0.0828 8 TYR A CD1 18 C CD2 . TYR A 8 ? 0.6969 0.4506 0.6316 0.1021 -0.2138 -0.0426 8 TYR A CD2 19 C CE1 . TYR A 8 ? 0.7461 0.4959 0.6967 0.1233 -0.2579 -0.0898 8 TYR A CE1 20 C CE2 . TYR A 8 ? 0.7075 0.4592 0.6574 0.1023 -0.2288 -0.0482 8 TYR A CE2 21 C CZ . TYR A 8 ? 0.7310 0.4806 0.6879 0.1128 -0.2511 -0.0711 8 TYR A CZ 22 O OH . TYR A 8 ? 0.7447 0.4925 0.7184 0.1132 -0.2680 -0.0775 8 TYR A OH 23 N N . THR A 9 ? 0.6404 0.4193 0.5073 0.1093 -0.1641 -0.0218 9 THR A N 24 C CA . THR A 9 ? 0.6136 0.3906 0.4800 0.1033 -0.1500 -0.0106 9 THR A CA 25 C C . THR A 9 ? 0.5778 0.3413 0.4674 0.0885 -0.1464 0.0000 9 THR A C 26 O O . THR A 9 ? 0.5652 0.3297 0.4618 0.0808 -0.1421 0.0084 9 THR A O 27 C CB . THR A 9 ? 0.6108 0.4038 0.4591 0.1038 -0.1355 0.0029 9 THR A CB 28 O OG1 . THR A 9 ? 0.6380 0.4489 0.4639 0.1178 -0.1369 -0.0035 9 THR A OG1 29 C CG2 . THR A 9 ? 0.6012 0.3919 0.4520 0.0975 -0.1229 0.0128 9 THR A CG2 30 N N . PHE A 10 ? 0.5552 0.3087 0.4581 0.0849 -0.1479 0.0005 10 PHE A N 31 C CA . PHE A 10 ? 0.5309 0.2778 0.4521 0.0713 -0.1426 0.0136 10 PHE A CA 32 C C . PHE A 10 ? 0.5147 0.2690 0.4230 0.0666 -0.1280 0.0247 10 PHE A C 33 O O . PHE A 10 ? 0.5119 0.2670 0.4118 0.0718 -0.1273 0.0230 10 PHE A O 34 C CB . PHE A 10 ? 0.5360 0.2703 0.4835 0.0696 -0.1546 0.0115 10 PHE A CB 35 C CG . PHE A 10 ? 0.5230 0.2555 0.4892 0.0560 -0.1489 0.0288 10 PHE A CG 36 C CD1 . PHE A 10 ? 0.5177 0.2508 0.4999 0.0475 -0.1471 0.0355 10 PHE A CD1 37 C CD2 . PHE A 10 ? 0.5208 0.2537 0.4893 0.0519 -0.1454 0.0394 10 PHE A CD2 38 C CE1 . PHE A 10 ? 0.5128 0.2499 0.5106 0.0355 -0.1401 0.0525 10 PHE A CE1 39 C CE2 . PHE A 10 ? 0.5154 0.2521 0.4980 0.0396 -0.1399 0.0576 10 PHE A CE2 40 C CZ . PHE A 10 ? 0.5126 0.2529 0.5089 0.0316 -0.1365 0.0642 10 PHE A CZ 41 N N . ARG A 11 ? 0.4996 0.2600 0.4084 0.0575 -0.1171 0.0339 11 ARG A N 42 C CA . ARG A 11 ? 0.4895 0.2578 0.3888 0.0532 -0.1054 0.0414 11 ARG A CA 43 C C . ARG A 11 ? 0.4759 0.2492 0.3841 0.0413 -0.0978 0.0499 11 ARG A C 44 O O . ARG A 11 ? 0.4687 0.2452 0.3873 0.0362 -0.0948 0.0501 11 ARG A O 45 C CB . ARG A 11 ? 0.4884 0.2664 0.3753 0.0580 -0.0980 0.0408 11 ARG A CB 46 C CG . ARG A 11 ? 0.4945 0.2763 0.3847 0.0599 -0.0991 0.0392 11 ARG A CG 47 C CD . ARG A 11 ? 0.4937 0.2870 0.3789 0.0633 -0.0917 0.0439 11 ARG A CD 48 N NE . ARG A 11 ? 0.4920 0.2899 0.3922 0.0587 -0.0892 0.0468 11 ARG A NE 49 C CZ . ARG A 11 ? 0.4855 0.2917 0.3976 0.0555 -0.0815 0.0514 11 ARG A CZ 50 N NH1 . ARG A 11 ? 0.4765 0.2878 0.3865 0.0559 -0.0752 0.0540 11 ARG A NH1 51 N NH2 . ARG A 11 ? 0.4821 0.2911 0.4137 0.0517 -0.0813 0.0525 11 ARG A NH2 52 N N . CYS A 12 ? 0.4684 0.2447 0.3728 0.0375 -0.0952 0.0567 12 CYS A N 53 C CA . CYS A 12 ? 0.4628 0.2509 0.3682 0.0276 -0.0868 0.0648 12 CYS A CA 54 C C . CYS A 12 ? 0.4487 0.2471 0.3407 0.0284 -0.0785 0.0612 12 CYS A C 55 O O . CYS A 12 ? 0.4461 0.2426 0.3295 0.0330 -0.0804 0.0614 12 CYS A O 56 C CB . CYS A 12 ? 0.4757 0.2632 0.3862 0.0232 -0.0914 0.0770 12 CYS A CB 57 S SG . CYS A 12 ? 0.4938 0.2656 0.4308 0.0241 -0.1056 0.0806 12 CYS A SG 58 N N . LEU A 13 ? 0.4357 0.2454 0.3311 0.0241 -0.0701 0.0568 13 LEU A N 59 C CA . LEU A 13 ? 0.4245 0.2439 0.3166 0.0251 -0.0639 0.0503 13 LEU A CA 60 C C . LEU A 13 ? 0.4245 0.2615 0.3133 0.0179 -0.0570 0.0491 13 LEU A C 61 O O . LEU A 13 ? 0.4233 0.2700 0.3196 0.0128 -0.0514 0.0468 13 LEU A O 62 C CB . LEU A 13 ? 0.4169 0.2361 0.3224 0.0276 -0.0617 0.0434 13 LEU A CB 63 C CG . LEU A 13 ? 0.4158 0.2232 0.3224 0.0347 -0.0686 0.0452 13 LEU A CG 64 C CD1 . LEU A 13 ? 0.4105 0.2216 0.3327 0.0361 -0.0667 0.0424 13 LEU A CD1 65 C CD2 . LEU A 13 ? 0.4187 0.2219 0.3125 0.0423 -0.0722 0.0479 13 LEU A CD2 66 N N . GLN A 14 ? 0.4230 0.2665 0.3005 0.0180 -0.0576 0.0500 14 GLN A N 67 C CA . GLN A 14 ? 0.4291 0.2937 0.2991 0.0127 -0.0524 0.0467 14 GLN A CA 68 C C . GLN A 14 ? 0.4226 0.2953 0.2989 0.0154 -0.0501 0.0315 14 GLN A C 69 O O . GLN A 14 ? 0.4160 0.2789 0.2962 0.0206 -0.0543 0.0311 14 GLN A O 70 C CB . GLN A 14 ? 0.4405 0.3084 0.2956 0.0106 -0.0575 0.0594 14 GLN A CB 71 C CG . GLN A 14 ? 0.4531 0.3467 0.2945 0.0060 -0.0541 0.0574 14 GLN A CG 72 C CD . GLN A 14 ? 0.4641 0.3585 0.2934 0.0052 -0.0620 0.0710 14 GLN A CD 73 O OE1 . GLN A 14 ? 0.4683 0.3466 0.3023 0.0060 -0.0686 0.0849 14 GLN A OE1 74 N NE2 . GLN A 14 ? 0.4719 0.3851 0.2889 0.0043 -0.0628 0.0655 14 GLN A NE2 75 N N . MET A 15 ? 0.4248 0.3171 0.3051 0.0121 -0.0436 0.0189 15 MET A N 76 C CA . MET A 15 ? 0.4210 0.3227 0.3157 0.0146 -0.0428 0.0005 15 MET A CA 77 C C . MET A 15 ? 0.4338 0.3623 0.3143 0.0116 -0.0404 -0.0096 15 MET A C 78 O O . MET A 15 ? 0.4392 0.3870 0.3156 0.0079 -0.0328 -0.0149 15 MET A O 79 C CB . MET A 15 ? 0.4147 0.3164 0.3362 0.0150 -0.0382 -0.0107 15 MET A CB 80 C CG . MET A 15 ? 0.4056 0.2853 0.3386 0.0180 -0.0413 0.0002 15 MET A CG 81 S SD . MET A 15 ? 0.4016 0.2823 0.3607 0.0161 -0.0366 -0.0061 15 MET A SD 82 C CE . MET A 15 ? 0.4097 0.2871 0.3491 0.0117 -0.0351 0.0078 15 MET A CE 83 N N . SER A 16 ? 0.4367 0.3687 0.3097 0.0136 -0.0469 -0.0121 16 SER A N 84 C CA . SER A 16 ? 0.4551 0.4145 0.3113 0.0118 -0.0474 -0.0224 16 SER A CA 85 C C . SER A 16 ? 0.4567 0.4246 0.3336 0.0160 -0.0517 -0.0476 16 SER A C 86 O O . SER A 16 ? 0.4452 0.3968 0.3386 0.0197 -0.0589 -0.0465 16 SER A O 87 C CB . SER A 16 ? 0.4639 0.4223 0.2958 0.0102 -0.0545 -0.0034 16 SER A CB 88 O OG . SER A 16 ? 0.4650 0.4169 0.2857 0.0061 -0.0520 0.0191 16 SER A OG 89 N N . SER A 17 ? 0.4712 0.4663 0.3505 0.0158 -0.0474 -0.0709 17 SER A N 90 C CA . SER A 17 ? 0.4779 0.4851 0.3812 0.0202 -0.0530 -0.1001 17 SER A CA 91 C C . SER A 17 ? 0.5079 0.5477 0.3828 0.0200 -0.0563 -0.1128 17 SER A C 92 O O . SER A 17 ? 0.5258 0.5914 0.3735 0.0171 -0.0481 -0.1118 17 SER A O 93 C CB . SER A 17 ? 0.4728 0.4884 0.4076 0.0215 -0.0463 -0.1229 17 SER A CB 94 O OG . SER A 17 ? 0.4494 0.4377 0.4098 0.0214 -0.0442 -0.1096 17 SER A OG 95 N N . PHE A 18 ? 0.5180 0.5592 0.4002 0.0234 -0.0684 -0.1238 18 PHE A N 96 C CA . PHE A 18 ? 0.5497 0.6247 0.4072 0.0245 -0.0746 -0.1405 18 PHE A CA 97 C C . PHE A 18 ? 0.5582 0.6440 0.4528 0.0305 -0.0828 -0.1794 18 PHE A C 98 O O . PHE A 18 ? 0.5439 0.6079 0.4738 0.0332 -0.0927 -0.1817 18 PHE A O 99 C CB . PHE A 18 ? 0.5555 0.6232 0.3903 0.0231 -0.0854 -0.1187 18 PHE A CB 100 C CG . PHE A 18 ? 0.5503 0.6029 0.3600 0.0178 -0.0803 -0.0808 18 PHE A CG 101 C CD1 . PHE A 18 ? 0.5261 0.5424 0.3540 0.0176 -0.0781 -0.0614 18 PHE A CD1 102 C CD2 . PHE A 18 ? 0.5726 0.6495 0.3428 0.0133 -0.0787 -0.0642 18 PHE A CD2 103 C CE1 . PHE A 18 ? 0.5237 0.5262 0.3337 0.0137 -0.0753 -0.0309 18 PHE A CE1 104 C CE2 . PHE A 18 ? 0.5682 0.6303 0.3246 0.0084 -0.0761 -0.0295 18 PHE A CE2 105 C CZ . PHE A 18 ? 0.5446 0.5684 0.3221 0.0089 -0.0750 -0.0150 18 PHE A CZ 106 N N . ALA A 19 ? 0.5842 0.7052 0.4743 0.0329 -0.0784 -0.2100 19 ALA A N 107 C CA . ALA A 19 ? 0.5955 0.7298 0.5270 0.0395 -0.0868 -0.2530 19 ALA A CA 108 C C . ALA A 19 ? 0.6270 0.7868 0.5426 0.0433 -0.1018 -0.2738 19 ALA A C 109 O O . ALA A 19 ? 0.6265 0.7822 0.5837 0.0483 -0.1161 -0.2991 19 ALA A O 110 C CB . ALA A 19 ? 0.6054 0.7667 0.5452 0.0415 -0.0747 -0.2807 19 ALA A CB 111 N N . ASN A 20 ? 0.6593 0.8477 0.5176 0.0409 -0.0992 -0.2625 20 ASN A N 112 C CA . ASN A 20 ? 0.6936 0.9103 0.5266 0.0439 -0.1140 -0.2769 20 ASN A CA 113 C C . ASN A 20 ? 0.7131 0.9481 0.4838 0.0380 -0.1090 -0.2416 20 ASN A C 114 O O . ASN A 20 ? 0.7011 0.9195 0.4582 0.0318 -0.0962 -0.2065 20 ASN A O 115 C CB . ASN A 20 ? 0.7252 0.9851 0.5669 0.0519 -0.1177 -0.3302 20 ASN A CB 116 C CG . ASN A 20 ? 0.7392 1.0274 0.5684 0.0522 -0.0977 -0.3425 20 ASN A CG 117 O OD1 . ASN A 20 ? 0.7496 1.0526 0.5337 0.0467 -0.0835 -0.3135 20 ASN A OD1 118 N ND2 . ASN A 20 ? 0.7436 1.0401 0.6185 0.0586 -0.0970 -0.3850 20 ASN A ND2 119 N N . ARG A 21 ? 0.7442 1.0127 0.4813 0.0399 -0.1209 -0.2494 21 ARG A N 120 C CA . ARG A 21 ? 0.7701 1.0714 0.4483 0.0350 -0.1153 -0.2209 21 ARG A CA 121 C C . ARG A 21 ? 0.7855 1.1258 0.4442 0.0355 -0.0956 -0.2335 21 ARG A C 122 O O . ARG A 21 ? 0.7991 1.1632 0.4744 0.0426 -0.0939 -0.2784 21 ARG A O 123 C CB . ARG A 21 ? 0.8040 1.1392 0.4519 0.0380 -0.1338 -0.2313 21 ARG A CB 124 N N . SER A 22 ? 0.7853 1.1315 0.4151 0.0282 -0.0808 -0.1945 22 SER A N 125 C CA . SER A 22 ? 0.7976 1.1807 0.4111 0.0277 -0.0599 -0.1997 22 SER A CA 126 C C . SER A 22 ? 0.7693 1.1307 0.4280 0.0300 -0.0474 -0.2220 22 SER A C 127 O O . SER A 22 ? 0.7847 1.1828 0.4402 0.0332 -0.0334 -0.2459 22 SER A O 128 C CB . SER A 22 ? 0.8442 1.2956 0.4204 0.0338 -0.0601 -0.2308 22 SER A CB 129 N N . TRP A 23 ? 0.7282 1.0336 0.4293 0.0287 -0.0526 -0.2144 23 TRP A N 130 C CA . TRP A 23 ? 0.6992 0.9780 0.4374 0.0276 -0.0399 -0.2154 23 TRP A CA 131 C C . TRP A 23 ? 0.6637 0.8859 0.4228 0.0230 -0.0446 -0.1819 23 TRP A C 132 O O . TRP A 23 ? 0.6477 0.8405 0.4321 0.0255 -0.0583 -0.1870 23 TRP A O 133 C CB . TRP A 23 ? 0.6933 0.9737 0.4784 0.0353 -0.0418 -0.2640 23 TRP A CB 134 C CG . TRP A 23 ? 0.6731 0.9399 0.4921 0.0343 -0.0267 -0.2670 23 TRP A CG 135 C CD1 . TRP A 23 ? 0.6880 0.9913 0.5079 0.0367 -0.0115 -0.2898 23 TRP A CD1 136 C CD2 . TRP A 23 ? 0.6371 0.8537 0.4936 0.0310 -0.0261 -0.2469 23 TRP A CD2 137 N NE1 . TRP A 23 ? 0.6616 0.9381 0.5198 0.0347 -0.0026 -0.2848 23 TRP A NE1 138 C CE2 . TRP A 23 ? 0.6316 0.8557 0.5112 0.0312 -0.0118 -0.2584 23 TRP A CE2 139 C CE3 . TRP A 23 ? 0.6102 0.7796 0.4826 0.0285 -0.0359 -0.2210 23 TRP A CE3 140 C CZ2 . TRP A 23 ? 0.6012 0.7862 0.5176 0.0286 -0.0090 -0.2437 23 TRP A CZ2 141 C CZ3 . TRP A 23 ? 0.5820 0.7157 0.4879 0.0265 -0.0319 -0.2072 23 TRP A CZ3 142 C CH2 . TRP A 23 ? 0.5785 0.7198 0.5056 0.0264 -0.0194 -0.2182 23 TRP A CH2 143 N N . SER A 24 ? 0.6520 0.8617 0.4010 0.0166 -0.0333 -0.1479 24 SER A N 144 C CA . SER A 24 ? 0.6196 0.7794 0.3921 0.0136 -0.0349 -0.1229 24 SER A CA 145 C C . SER A 24 ? 0.6104 0.7677 0.3838 0.0088 -0.0197 -0.1041 24 SER A C 146 O O . SER A 24 ? 0.6288 0.8224 0.3785 0.0061 -0.0086 -0.0993 24 SER A O 147 C CB . SER A 24 ? 0.6183 0.7570 0.3736 0.0106 -0.0463 -0.0915 24 SER A CB 148 O OG . SER A 24 ? 0.6356 0.7903 0.3581 0.0044 -0.0413 -0.0597 24 SER A OG 149 N N . ARG A 25 ? 0.5806 0.6979 0.3831 0.0081 -0.0197 -0.0941 25 ARG A N 150 C CA . ARG A 25 ? 0.5704 0.6765 0.3760 0.0032 -0.0097 -0.0710 25 ARG A CA 151 C C . ARG A 25 ? 0.5431 0.6040 0.3602 0.0021 -0.0175 -0.0467 25 ARG A C 152 O O . ARG A 25 ? 0.5266 0.5634 0.3603 0.0061 -0.0269 -0.0533 25 ARG A O 153 C CB . ARG A 25 ? 0.5675 0.6804 0.4017 0.0047 0.0012 -0.0923 25 ARG A CB 154 C CG . ARG A 25 ? 0.5494 0.6351 0.4252 0.0095 -0.0050 -0.1123 25 ARG A CG 155 C CD . ARG A 25 ? 0.5509 0.6496 0.4577 0.0112 0.0047 -0.1361 25 ARG A CD 156 N NE . ARG A 25 ? 0.5456 0.6335 0.4585 0.0067 0.0136 -0.1158 25 ARG A NE 157 C CZ . ARG A 25 ? 0.5618 0.6771 0.4637 0.0033 0.0273 -0.1113 25 ARG A CZ 158 N NH1 . ARG A 25 ? 0.5875 0.7480 0.4663 0.0041 0.0359 -0.1250 25 ARG A NH1 159 N NH2 . ARG A 25 ? 0.5529 0.6524 0.4681 -0.0006 0.0323 -0.0922 25 ARG A NH2 160 N N . THR A 26 ? 0.5365 0.5890 0.3466 -0.0029 -0.0137 -0.0188 26 THR A N 161 C CA . THR A 26 ? 0.5162 0.5297 0.3372 -0.0032 -0.0204 0.0016 26 THR A CA 162 C C . THR A 26 ? 0.5067 0.5124 0.3447 -0.0059 -0.0126 0.0089 26 THR A C 163 O O . THR A 26 ? 0.5181 0.5445 0.3486 -0.0110 -0.0044 0.0211 26 THR A O 164 C CB . THR A 26 ? 0.5246 0.5340 0.3255 -0.0064 -0.0279 0.0291 26 THR A CB 165 O OG1 . THR A 26 ? 0.5306 0.5464 0.3185 -0.0037 -0.0364 0.0218 26 THR A OG1 166 C CG2 . THR A 26 ? 0.5092 0.4809 0.3236 -0.0056 -0.0349 0.0464 26 THR A CG2 167 N N . ASP A 27 ? 0.4830 0.4613 0.3452 -0.0026 -0.0154 0.0025 27 ASP A N 168 C CA . ASP A 27 ? 0.4717 0.4383 0.3530 -0.0045 -0.0114 0.0087 27 ASP A CA 169 C C . ASP A 27 ? 0.4561 0.3881 0.3428 -0.0022 -0.0216 0.0230 27 ASP A C 170 O O . ASP A 27 ? 0.4459 0.3624 0.3328 0.0025 -0.0288 0.0193 27 ASP A O 171 C CB . ASP A 27 ? 0.4637 0.4340 0.3714 -0.0019 -0.0062 -0.0143 27 ASP A CB 172 C CG . ASP A 27 ? 0.4786 0.4856 0.3837 -0.0023 0.0036 -0.0349 27 ASP A CG 173 O OD1 . ASP A 27 ? 0.4895 0.5194 0.3917 -0.0062 0.0143 -0.0314 27 ASP A OD1 174 O OD2 . ASP A 27 ? 0.4825 0.4977 0.3898 0.0016 0.0004 -0.0553 27 ASP A OD2 175 N N . SER A 28 ? 0.4512 0.3732 0.3447 -0.0051 -0.0222 0.0384 28 SER A N 176 C CA . SER A 28 ? 0.4420 0.3342 0.3410 -0.0020 -0.0328 0.0486 28 SER A CA 177 C C . SER A 28 ? 0.4320 0.3126 0.3528 -0.0021 -0.0332 0.0483 28 SER A C 178 O O . SER A 28 ? 0.4333 0.3280 0.3657 -0.0069 -0.0253 0.0487 28 SER A O 179 C CB . SER A 28 ? 0.4543 0.3421 0.3431 -0.0045 -0.0391 0.0686 28 SER A CB 180 O OG . SER A 28 ? 0.4621 0.3565 0.3323 -0.0034 -0.0416 0.0695 28 SER A OG 181 N N . VAL A 29 ? 0.4204 0.2777 0.3466 0.0034 -0.0424 0.0476 29 VAL A N 182 C CA . VAL A 29 ? 0.4150 0.2588 0.3597 0.0044 -0.0471 0.0484 29 VAL A CA 183 C C . VAL A 29 ? 0.4153 0.2383 0.3550 0.0094 -0.0599 0.0554 29 VAL A C 184 O O . VAL A 29 ? 0.4176 0.2353 0.3422 0.0139 -0.0637 0.0559 29 VAL A O 185 C CB . VAL A 29 ? 0.4053 0.2471 0.3651 0.0077 -0.0462 0.0363 29 VAL A CB 186 C CG1 . VAL A 29 ? 0.4038 0.2663 0.3769 0.0034 -0.0345 0.0255 29 VAL A CG1 187 C CG2 . VAL A 29 ? 0.4003 0.2352 0.3515 0.0143 -0.0503 0.0328 29 VAL A CG2 188 N N . VAL A 30 ? 0.4143 0.2269 0.3694 0.0090 -0.0668 0.0590 30 VAL A N 189 C CA . VAL A 30 ? 0.4177 0.2120 0.3725 0.0150 -0.0806 0.0607 30 VAL A CA 190 C C . VAL A 30 ? 0.4146 0.1992 0.3808 0.0196 -0.0884 0.0532 30 VAL A C 191 O O . VAL A 30 ? 0.4102 0.1978 0.3955 0.0152 -0.0864 0.0531 30 VAL A O 192 C CB . VAL A 30 ? 0.4271 0.2181 0.3948 0.0103 -0.0861 0.0728 30 VAL A CB 193 C CG1 . VAL A 30 ? 0.4329 0.2053 0.4057 0.0177 -0.1021 0.0695 30 VAL A CG1 194 C CG2 . VAL A 30 ? 0.4307 0.2352 0.3862 0.0052 -0.0789 0.0835 30 VAL A CG2 195 N N . TRP A 31 ? 0.4168 0.1923 0.3712 0.0289 -0.0973 0.0475 31 TRP A N 196 C CA . TRP A 31 ? 0.4190 0.1892 0.3773 0.0350 -0.1060 0.0410 31 TRP A CA 197 C C . TRP A 31 ? 0.4314 0.1903 0.3870 0.0429 -0.1210 0.0352 31 TRP A C 198 O O . TRP A 31 ? 0.4365 0.1931 0.3794 0.0475 -0.1228 0.0340 31 TRP A O 199 C CB . TRP A 31 ? 0.4131 0.1901 0.3572 0.0406 -0.1019 0.0393 31 TRP A CB 200 C CG . TRP A 31 ? 0.4022 0.1898 0.3552 0.0346 -0.0898 0.0410 31 TRP A CG 201 C CD1 . TRP A 31 ? 0.3969 0.1926 0.3432 0.0318 -0.0799 0.0416 31 TRP A CD1 202 C CD2 . TRP A 31 ? 0.3961 0.1880 0.3703 0.0312 -0.0878 0.0397 31 TRP A CD2 203 N NE1 . TRP A 31 ? 0.3896 0.1950 0.3523 0.0274 -0.0720 0.0385 31 TRP A NE1 204 C CE2 . TRP A 31 ? 0.3876 0.1905 0.3689 0.0269 -0.0762 0.0377 31 TRP A CE2 205 C CE3 . TRP A 31 ? 0.3986 0.1865 0.3893 0.0317 -0.0960 0.0390 31 TRP A CE3 206 C CZ2 . TRP A 31 ? 0.3814 0.1914 0.3887 0.0233 -0.0719 0.0340 31 TRP A CZ2 207 C CZ3 . TRP A 31 ? 0.3912 0.1854 0.4064 0.0276 -0.0916 0.0382 31 TRP A CZ3 208 C CH2 . TRP A 31 ? 0.3824 0.1875 0.4072 0.0235 -0.0793 0.0352 31 TRP A CH2 209 N N . LEU A 32 ? 0.4375 0.1902 0.4079 0.0449 -0.1328 0.0299 32 LEU A N 210 C CA . LEU A 32 ? 0.4515 0.1965 0.4190 0.0551 -0.1494 0.0185 32 LEU A CA 211 C C . LEU A 32 ? 0.4548 0.2060 0.4108 0.0623 -0.1547 0.0129 32 LEU A C 212 O O . LEU A 32 ? 0.4522 0.2025 0.4250 0.0593 -0.1596 0.0133 32 LEU A O 213 C CB . LEU A 32 ? 0.4604 0.1939 0.4591 0.0521 -0.1624 0.0159 32 LEU A CB 214 C CG . LEU A 32 ? 0.4785 0.2041 0.4807 0.0635 -0.1826 -0.0010 32 LEU A CG 215 C CD1 . LEU A 32 ? 0.4856 0.2121 0.4683 0.0723 -0.1833 -0.0084 32 LEU A CD1 216 C CD2 . LEU A 32 ? 0.4857 0.1990 0.5294 0.0586 -0.1955 -0.0012 32 LEU A CD2 217 N N . GLY A 33 ? 0.4596 0.2194 0.3888 0.0719 -0.1536 0.0098 33 GLY A N 218 C CA . GLY A 33 ? 0.4644 0.2365 0.3802 0.0778 -0.1552 0.0114 33 GLY A CA 219 C C . GLY A 33 ? 0.4464 0.2232 0.3740 0.0685 -0.1426 0.0244 33 GLY A C 220 O O . GLY A 33 ? 0.4349 0.2139 0.3613 0.0634 -0.1292 0.0307 33 GLY A O 221 N N . ASP A 34 ? 0.4458 0.2244 0.3884 0.0663 -0.1481 0.0269 34 ASP A N 222 C CA . ASP A 34 ? 0.4309 0.2139 0.3931 0.0580 -0.1380 0.0364 34 ASP A CA 223 C C . ASP A 34 ? 0.4234 0.1988 0.4159 0.0477 -0.1356 0.0349 34 ASP A C 224 O O . ASP A 34 ? 0.4126 0.1926 0.4267 0.0419 -0.1295 0.0390 34 ASP A O 225 C CB . ASP A 34 ? 0.4363 0.2303 0.3997 0.0625 -0.1442 0.0439 34 ASP A CB 226 C CG . ASP A 34 ? 0.4512 0.2423 0.4203 0.0661 -0.1620 0.0385 34 ASP A CG 227 O OD1 . ASP A 34 ? 0.4571 0.2363 0.4339 0.0650 -0.1698 0.0278 34 ASP A OD1 228 O OD2 . ASP A 34 ? 0.4617 0.2634 0.4307 0.0699 -0.1694 0.0460 34 ASP A OD2 229 N N . LEU A 35 ? 0.4289 0.1944 0.4273 0.0457 -0.1404 0.0296 35 LEU A N 230 C CA . LEU A 35 ? 0.4233 0.1855 0.4512 0.0358 -0.1361 0.0315 35 LEU A CA 231 C C . LEU A 35 ? 0.4154 0.1804 0.4400 0.0294 -0.1224 0.0356 35 LEU A C 232 O O . LEU A 35 ? 0.4208 0.1812 0.4312 0.0321 -0.1252 0.0353 35 LEU A O 233 C CB . LEU A 35 ? 0.4367 0.1882 0.4832 0.0369 -0.1526 0.0264 35 LEU A CB 234 C CG . LEU A 35 ? 0.4471 0.1976 0.4986 0.0429 -0.1687 0.0215 35 LEU A CG 235 C CD1 . LEU A 35 ? 0.4613 0.2006 0.5332 0.0447 -0.1871 0.0133 35 LEU A CD1 236 C CD2 . LEU A 35 ? 0.4376 0.1946 0.5112 0.0372 -0.1629 0.0275 35 LEU A CD2 237 N N . GLN A 36 ? 0.4058 0.1808 0.4438 0.0214 -0.1081 0.0388 36 GLN A N 238 C CA . GLN A 36 ? 0.4039 0.1870 0.4373 0.0151 -0.0951 0.0433 36 GLN A CA 239 C C . GLN A 36 ? 0.4121 0.1913 0.4628 0.0100 -0.0987 0.0501 36 GLN A C 240 O O . GLN A 36 ? 0.4120 0.1896 0.4903 0.0067 -0.1024 0.0511 36 GLN A O 241 C CB . GLN A 36 ? 0.3943 0.1935 0.4387 0.0092 -0.0794 0.0412 36 GLN A CB 242 C CG . GLN A 36 ? 0.3950 0.2079 0.4270 0.0042 -0.0662 0.0442 36 GLN A CG 243 C CD . GLN A 36 ? 0.3892 0.2210 0.4283 0.0009 -0.0517 0.0363 36 GLN A CD 244 O OE1 . GLN A 36 ? 0.3829 0.2159 0.4409 0.0020 -0.0514 0.0287 36 GLN A OE1 245 N NE2 . GLN A 36 ? 0.3922 0.2402 0.4180 -0.0028 -0.0409 0.0371 36 GLN A NE2 246 N N . THR A 37 ? 0.4198 0.1979 0.4590 0.0093 -0.0985 0.0563 37 THR A N 247 C CA . THR A 37 ? 0.4303 0.2063 0.4914 0.0038 -0.1024 0.0672 37 THR A CA 248 C C . THR A 37 ? 0.4351 0.2304 0.4964 -0.0051 -0.0865 0.0806 37 THR A C 249 O O . THR A 37 ? 0.4395 0.2407 0.5267 -0.0120 -0.0851 0.0937 37 THR A O 250 C CB . THR A 37 ? 0.4388 0.1997 0.4962 0.0097 -0.1175 0.0665 37 THR A CB 251 O OG1 . THR A 37 ? 0.4378 0.2022 0.4654 0.0125 -0.1120 0.0667 37 THR A OG1 252 C CG2 . THR A 37 ? 0.4431 0.1895 0.5016 0.0193 -0.1346 0.0519 37 THR A CG2 253 N N . HIS A 38 ? 0.4344 0.2419 0.4683 -0.0050 -0.0753 0.0785 38 HIS A N 254 C CA . HIS A 38 ? 0.4420 0.2729 0.4697 -0.0124 -0.0605 0.0890 38 HIS A CA 255 C C . HIS A 38 ? 0.4412 0.2886 0.4498 -0.0116 -0.0474 0.0768 38 HIS A C 256 O O . HIS A 38 ? 0.4295 0.2678 0.4270 -0.0054 -0.0508 0.0644 38 HIS A O 257 C CB . HIS A 38 ? 0.4503 0.2799 0.4659 -0.0131 -0.0652 0.1021 38 HIS A CB 258 C CG . HIS A 38 ? 0.4567 0.2677 0.4960 -0.0124 -0.0811 0.1112 38 HIS A CG 259 N ND1 . HIS A 38 ? 0.4550 0.2425 0.4955 -0.0037 -0.0970 0.0990 38 HIS A ND1 260 C CD2 . HIS A 38 ? 0.4667 0.2813 0.5328 -0.0190 -0.0844 0.1311 38 HIS A CD2 261 C CE1 . HIS A 38 ? 0.4648 0.2407 0.5333 -0.0043 -0.1104 0.1070 38 HIS A CE1 262 N NE2 . HIS A 38 ? 0.4704 0.2611 0.5577 -0.0140 -0.1035 0.1282 38 HIS A NE2 263 N N . ARG A 39 ? 0.4545 0.3287 0.4625 -0.0178 -0.0326 0.0805 39 ARG A N 264 C CA . ARG A 39 ? 0.4607 0.3550 0.4486 -0.0171 -0.0215 0.0687 39 ARG A CA 265 C C . ARG A 39 ? 0.4811 0.4013 0.4528 -0.0225 -0.0130 0.0822 39 ARG A C 266 O O . ARG A 39 ? 0.4880 0.4204 0.4721 -0.0286 -0.0091 0.1001 39 ARG A O 267 C CB . ARG A 39 ? 0.4576 0.3651 0.4622 -0.0170 -0.0114 0.0516 39 ARG A CB 268 C CG . ARG A 39 ? 0.4684 0.4033 0.4892 -0.0233 0.0027 0.0555 39 ARG A CG 269 C CD . ARG A 39 ? 0.4650 0.4153 0.5023 -0.0217 0.0129 0.0334 39 ARG A CD 270 N NE . ARG A 39 ? 0.4546 0.3813 0.5192 -0.0189 0.0039 0.0266 39 ARG A NE 271 C CZ . ARG A 39 ? 0.4551 0.3739 0.5474 -0.0215 0.0010 0.0343 39 ARG A CZ 272 N NH1 . ARG A 39 ? 0.4636 0.3962 0.5653 -0.0275 0.0076 0.0499 39 ARG A NH1 273 N NH2 . ARG A 39 ? 0.4472 0.3460 0.5612 -0.0182 -0.0091 0.0277 39 ARG A NH2 274 N N . TRP A 40 ? 0.4910 0.4212 0.4368 -0.0204 -0.0110 0.0754 40 TRP A N 275 C CA . TRP A 40 ? 0.5135 0.4727 0.4401 -0.0250 -0.0037 0.0874 40 TRP A CA 276 C C . TRP A 40 ? 0.5217 0.5052 0.4290 -0.0225 0.0046 0.0668 40 TRP A C 277 O O . TRP A 40 ? 0.5200 0.4963 0.4104 -0.0185 -0.0019 0.0590 40 TRP A O 278 C CB . TRP A 40 ? 0.5216 0.4675 0.4380 -0.0256 -0.0155 0.1071 40 TRP A CB 279 C CG . TRP A 40 ? 0.5435 0.5201 0.4442 -0.0316 -0.0099 0.1266 40 TRP A CG 280 C CD1 . TRP A 40 ? 0.5584 0.5729 0.4571 -0.0372 0.0045 0.1347 40 TRP A CD1 281 C CD2 . TRP A 40 ? 0.5536 0.5287 0.4392 -0.0323 -0.0188 0.1425 40 TRP A CD2 282 N NE1 . TRP A 40 ? 0.5786 0.6172 0.4589 -0.0415 0.0049 0.1563 40 TRP A NE1 283 C CE2 . TRP A 40 ? 0.5745 0.5881 0.4481 -0.0389 -0.0101 0.1617 40 TRP A CE2 284 C CE3 . TRP A 40 ? 0.5484 0.4958 0.4307 -0.0278 -0.0331 0.1427 40 TRP A CE3 285 C CZ2 . TRP A 40 ? 0.5889 0.6123 0.4482 -0.0416 -0.0170 0.1827 40 TRP A CZ2 286 C CZ3 . TRP A 40 ? 0.5619 0.5174 0.4328 -0.0303 -0.0394 0.1611 40 TRP A CZ3 287 C CH2 . TRP A 40 ? 0.5816 0.5740 0.4416 -0.0375 -0.0322 0.1818 40 TRP A CH2 288 N N . SER A 41 ? 0.5312 0.5443 0.4447 -0.0244 0.0188 0.0564 41 SER A N 289 C CA . SER A 41 ? 0.5434 0.5833 0.4453 -0.0212 0.0269 0.0310 41 SER A CA 290 C C . SER A 41 ? 0.5668 0.6361 0.4349 -0.0228 0.0288 0.0384 41 SER A C 291 O O . SER A 41 ? 0.5791 0.6598 0.4367 -0.0283 0.0297 0.0665 41 SER A O 292 C CB . SER A 41 ? 0.5487 0.6147 0.4703 -0.0222 0.0420 0.0168 41 SER A CB 293 O OG . SER A 41 ? 0.5609 0.6545 0.4761 -0.0179 0.0490 -0.0126 41 SER A OG 294 N N . ASN A 42 ? 0.5749 0.6566 0.4297 -0.0179 0.0279 0.0140 42 ASN A N 295 C CA . ASN A 42 ? 0.6007 0.7132 0.4224 -0.0183 0.0281 0.0160 42 ASN A CA 296 C C . ASN A 42 ? 0.6287 0.7900 0.4350 -0.0229 0.0433 0.0267 42 ASN A C 297 O O . ASN A 42 ? 0.6469 0.8277 0.4293 -0.0271 0.0423 0.0521 42 ASN A O 298 C CB . ASN A 42 ? 0.6036 0.7252 0.4212 -0.0116 0.0248 -0.0184 42 ASN A CB 299 C CG . ASN A 42 ? 0.6294 0.7804 0.4119 -0.0114 0.0213 -0.0173 42 ASN A CG 300 O OD1 . ASN A 42 ? 0.6263 0.7601 0.3956 -0.0126 0.0097 0.0017 42 ASN A OD1 301 N ND2 . ASN A 42 ? 0.6560 0.8536 0.4236 -0.0093 0.0309 -0.0384 42 ASN A ND2 302 N N . ASP A 43 ? 0.6329 0.8154 0.4555 -0.0218 0.0572 0.0083 43 ASP A N 303 C CA . ASP A 43 ? 0.6616 0.8968 0.4724 -0.0249 0.0752 0.0148 43 ASP A CA 304 C C . ASP A 43 ? 0.6622 0.8971 0.4869 -0.0331 0.0814 0.0539 43 ASP A C 305 O O . ASP A 43 ? 0.6857 0.9664 0.5005 -0.0368 0.0964 0.0687 43 ASP A O 306 C CB . ASP A 43 ? 0.6675 0.9299 0.4940 -0.0195 0.0888 -0.0240 43 ASP A CB 307 C CG . ASP A 43 ? 0.6414 0.8627 0.5103 -0.0166 0.0839 -0.0424 43 ASP A CG 308 O OD1 . ASP A 43 ? 0.6298 0.8201 0.5056 -0.0121 0.0700 -0.0589 43 ASP A OD1 309 O OD2 . ASP A 43 ? 0.6385 0.8596 0.5354 -0.0190 0.0933 -0.0384 43 ASP A OD2 310 N N . SER A 44 ? 0.6380 0.8246 0.4875 -0.0354 0.0698 0.0701 44 SER A N 311 C CA . SER A 44 ? 0.6377 0.8178 0.5061 -0.0429 0.0704 0.1075 44 SER A CA 312 C C . SER A 44 ? 0.6418 0.8151 0.4944 -0.0471 0.0583 0.1406 44 SER A C 313 O O . SER A 44 ? 0.6325 0.7733 0.4771 -0.0438 0.0426 0.1360 44 SER A O 314 C CB . SER A 44 ? 0.6143 0.7473 0.5203 -0.0422 0.0618 0.1045 44 SER A CB 315 O OG . SER A 44 ? 0.6188 0.7445 0.5493 -0.0489 0.0602 0.1374 44 SER A OG 316 N N . ALA A 45 ? 0.6569 0.8625 0.5087 -0.0543 0.0658 0.1752 45 ALA A N 317 C CA . ALA A 45 ? 0.6630 0.8636 0.5103 -0.0596 0.0537 0.2125 45 ALA A CA 318 C C . ALA A 45 ? 0.6402 0.7885 0.5247 -0.0615 0.0371 0.2283 45 ALA A C 319 O O . ALA A 45 ? 0.6375 0.7647 0.5216 -0.0623 0.0214 0.2448 45 ALA A O 320 C CB . ALA A 45 ? 0.6924 0.9461 0.5349 -0.0674 0.0670 0.2489 45 ALA A CB 321 N N . THR A 46 ? 0.6244 0.7542 0.5428 -0.0616 0.0399 0.2219 46 THR A N 322 C CA . THR A 46 ? 0.6096 0.6959 0.5673 -0.0630 0.0246 0.2346 46 THR A CA 323 C C . THR A 46 ? 0.5821 0.6258 0.5462 -0.0551 0.0155 0.2008 46 THR A C 324 O O . THR A 46 ? 0.5760 0.6268 0.5304 -0.0508 0.0248 0.1726 46 THR A O 325 C CB . THR A 46 ? 0.6148 0.7152 0.6124 -0.0700 0.0330 0.2578 46 THR A CB 326 O OG1 . THR A 46 ? 0.6119 0.7301 0.6116 -0.0680 0.0495 0.2346 46 THR A OG1 327 C CG2 . THR A 46 ? 0.6423 0.7868 0.6389 -0.0785 0.0416 0.2985 46 THR A CG2 328 N N . ILE A 47 ? 0.5693 0.5719 0.5522 -0.0529 -0.0028 0.2046 47 ILE A N 329 C CA . ILE A 47 ? 0.5484 0.5127 0.5396 -0.0455 -0.0129 0.1785 47 ILE A CA 330 C C . ILE A 47 ? 0.5387 0.4977 0.5650 -0.0473 -0.0100 0.1764 47 ILE A C 331 O O . ILE A 47 ? 0.5457 0.5063 0.6043 -0.0531 -0.0125 0.1996 47 ILE A O 332 C CB . ILE A 47 ? 0.5451 0.4728 0.5443 -0.0416 -0.0334 0.1826 47 ILE A CB 333 C CG1 . ILE A 47 ? 0.5517 0.4830 0.5201 -0.0396 -0.0372 0.1847 47 ILE A CG1 334 C CG2 . ILE A 47 ? 0.5299 0.4243 0.5350 -0.0335 -0.0430 0.1574 47 ILE A CG2 335 C CD1 . ILE A 47 ? 0.5537 0.4587 0.5365 -0.0377 -0.0554 0.1964 47 ILE A CD1 336 N N . SER A 48 ? 0.5207 0.4733 0.5453 -0.0425 -0.0059 0.1498 48 SER A N 337 C CA . SER A 48 ? 0.5109 0.4621 0.5676 -0.0439 -0.0018 0.1446 48 SER A CA 338 C C . SER A 48 ? 0.4949 0.4057 0.5720 -0.0388 -0.0205 0.1355 48 SER A C 339 O O . SER A 48 ? 0.4843 0.3747 0.5433 -0.0317 -0.0292 0.1182 48 SER A O 340 C CB . SER A 48 ? 0.5085 0.4820 0.5560 -0.0419 0.0140 0.1215 48 SER A CB 341 O OG . SER A 48 ? 0.5024 0.4677 0.5819 -0.0415 0.0148 0.1114 48 SER A OG 342 N N . PHE A 49 ? 0.4908 0.3929 0.6064 -0.0423 -0.0270 0.1477 49 PHE A N 343 C CA . PHE A 49 ? 0.4788 0.3468 0.6160 -0.0373 -0.0462 0.1381 49 PHE A CA 344 C C . PHE A 49 ? 0.4638 0.3289 0.6078 -0.0341 -0.0429 0.1176 49 PHE A C 345 O O . PHE A 49 ? 0.4638 0.3502 0.6251 -0.0387 -0.0287 0.1185 49 PHE A O 346 C CB . PHE A 49 ? 0.4866 0.3472 0.6699 -0.0423 -0.0562 0.1573 49 PHE A CB 347 C CG . PHE A 49 ? 0.4991 0.3591 0.6899 -0.0458 -0.0636 0.1803 49 PHE A CG 348 C CD1 . PHE A 49 ? 0.5007 0.3522 0.6603 -0.0415 -0.0697 0.1778 49 PHE A CD1 349 C CD2 . PHE A 49 ? 0.5088 0.3757 0.7457 -0.0536 -0.0660 0.2062 49 PHE A CD2 350 C CE1 . PHE A 49 ? 0.5134 0.3638 0.6866 -0.0449 -0.0779 0.1997 49 PHE A CE1 351 C CE2 . PHE A 49 ? 0.5199 0.3860 0.7725 -0.0572 -0.0746 0.2300 49 PHE A CE2 352 C CZ . PHE A 49 ? 0.5215 0.3790 0.7421 -0.0528 -0.0809 0.2264 49 PHE A CZ 353 N N . THR A 50 ? 0.4497 0.2913 0.5820 -0.0261 -0.0558 0.1004 50 THR A N 354 C CA . THR A 50 ? 0.4373 0.2738 0.5808 -0.0230 -0.0569 0.0844 50 THR A CA 355 C C . THR A 50 ? 0.4361 0.2485 0.6052 -0.0196 -0.0770 0.0819 50 THR A C 356 O O . THR A 50 ? 0.4312 0.2365 0.6081 -0.0160 -0.0825 0.0702 50 THR A O 357 C CB . THR A 50 ? 0.4289 0.2625 0.5421 -0.0164 -0.0556 0.0685 50 THR A CB 358 O OG1 . THR A 50 ? 0.4293 0.2433 0.5208 -0.0098 -0.0700 0.0672 50 THR A OG1 359 C CG2 . THR A 50 ? 0.4291 0.2874 0.5213 -0.0191 -0.0376 0.0664 50 THR A CG2 360 N N . LYS A 51 ? 0.4409 0.2419 0.6254 -0.0205 -0.0894 0.0924 51 LYS A N 361 C CA . LYS A 51 ? 0.4433 0.2250 0.6600 -0.0182 -0.1095 0.0895 51 LYS A CA 362 C C . LYS A 51 ? 0.4504 0.2346 0.7068 -0.0255 -0.1121 0.1087 51 LYS A C 363 O O . LYS A 51 ? 0.4542 0.2509 0.7047 -0.0304 -0.1027 0.1248 51 LYS A O 364 C CB . LYS A 51 ? 0.4471 0.2071 0.6433 -0.0079 -0.1295 0.0765 51 LYS A CB 365 C CG . LYS A 51 ? 0.4403 0.1983 0.6027 -0.0002 -0.1295 0.0614 51 LYS A CG 366 C CD . LYS A 51 ? 0.4371 0.1929 0.6185 0.0009 -0.1355 0.0538 51 LYS A CD 367 C CE . LYS A 51 ? 0.4309 0.1880 0.5836 0.0076 -0.1350 0.0442 51 LYS A CE 368 N NZ . LYS A 51 ? 0.4192 0.1922 0.5575 0.0037 -0.1139 0.0464 51 LYS A NZ 369 N N . PRO A 52 ? 0.4532 0.2262 0.7534 -0.0262 -0.1266 0.1086 52 PRO A N 370 C CA . PRO A 52 ? 0.4619 0.2340 0.8090 -0.0326 -0.1334 0.1276 52 PRO A CA 371 C C . PRO A 52 ? 0.4691 0.2275 0.8127 -0.0293 -0.1477 0.1310 52 PRO A C 372 O O . PRO A 52 ? 0.4789 0.2445 0.8506 -0.0362 -0.1460 0.1537 52 PRO A O 373 C CB . PRO A 52 ? 0.4646 0.2206 0.8549 -0.0305 -0.1529 0.1181 52 PRO A CB 374 C CG . PRO A 52 ? 0.4562 0.2148 0.8263 -0.0269 -0.1475 0.1020 52 PRO A CG 375 C CD . PRO A 52 ? 0.4508 0.2119 0.7628 -0.0213 -0.1391 0.0920 52 PRO A CD 376 N N . TRP A 53 ? 0.4680 0.2097 0.7784 -0.0186 -0.1607 0.1097 53 TRP A N 377 C CA . TRP A 53 ? 0.4765 0.2019 0.7877 -0.0124 -0.1785 0.1046 53 TRP A CA 378 C C . TRP A 53 ? 0.4742 0.2059 0.7391 -0.0104 -0.1674 0.1069 53 TRP A C 379 O O . TRP A 53 ? 0.4792 0.1979 0.7357 -0.0029 -0.1808 0.0971 53 TRP A O 380 C CB . TRP A 53 ? 0.4819 0.1870 0.7906 -0.0002 -0.2023 0.0765 53 TRP A CB 381 C CG . TRP A 53 ? 0.4738 0.1820 0.7408 0.0060 -0.1973 0.0596 53 TRP A CG 382 C CD1 . TRP A 53 ? 0.4699 0.1800 0.7491 0.0050 -0.1983 0.0549 53 TRP A CD1 383 C CD2 . TRP A 53 ? 0.4696 0.1801 0.6834 0.0139 -0.1919 0.0482 53 TRP A CD2 384 N NE1 . TRP A 53 ? 0.4646 0.1780 0.7026 0.0116 -0.1946 0.0426 53 TRP A NE1 385 C CE2 . TRP A 53 ? 0.4644 0.1786 0.6621 0.0170 -0.1901 0.0389 53 TRP A CE2 386 C CE3 . TRP A 53 ? 0.4709 0.1811 0.6532 0.0187 -0.1889 0.0461 53 TRP A CE3 387 C CZ2 . TRP A 53 ? 0.4603 0.1792 0.6132 0.0243 -0.1850 0.0301 53 TRP A CZ2 388 C CZ3 . TRP A 53 ? 0.4658 0.1806 0.6018 0.0261 -0.1828 0.0356 53 TRP A CZ3 389 C CH2 . TRP A 53 ? 0.4613 0.1808 0.5841 0.0287 -0.1810 0.0287 53 TRP A CH2 390 N N . SER A 54 ? 0.4675 0.2206 0.7061 -0.0167 -0.1438 0.1186 54 SER A N 391 C CA . SER A 54 ? 0.4659 0.2267 0.6601 -0.0149 -0.1333 0.1193 54 SER A CA 392 C C . SER A 54 ? 0.4777 0.2387 0.6823 -0.0179 -0.1375 0.1368 54 SER A C 393 O O . SER A 54 ? 0.4769 0.2390 0.6493 -0.0146 -0.1346 0.1348 54 SER A O 394 C CB . SER A 54 ? 0.4579 0.2437 0.6267 -0.0206 -0.1088 0.1246 54 SER A CB 395 O OG . SER A 54 ? 0.4464 0.2312 0.6058 -0.0170 -0.1056 0.1073 54 SER A OG 396 N N . GLN A 55 ? 0.4885 0.2489 0.7428 -0.0245 -0.1452 0.1557 55 GLN A N 397 C CA . GLN A 55 ? 0.5023 0.2600 0.7795 -0.0272 -0.1542 0.1743 55 GLN A CA 398 C C . GLN A 55 ? 0.5105 0.2402 0.8072 -0.0170 -0.1801 0.1549 55 GLN A C 399 O O . GLN A 55 ? 0.5190 0.2434 0.8366 -0.0174 -0.1899 0.1657 55 GLN A O 400 C CB . GLN A 55 ? 0.5105 0.2824 0.8400 -0.0392 -0.1514 0.2069 55 GLN A CB 401 C CG . GLN A 55 ? 0.5206 0.3055 0.8622 -0.0463 -0.1497 0.2381 55 GLN A CG 402 C CD . GLN A 55 ? 0.5295 0.3374 0.9177 -0.0591 -0.1419 0.2758 55 GLN A CD 403 O OE1 . GLN A 55 ? 0.5279 0.3624 0.9023 -0.0652 -0.1207 0.2855 55 GLN A OE1 404 N NE2 . GLN A 55 ? 0.5409 0.3405 0.9876 -0.0630 -0.1588 0.2975 55 GLN A NE2 405 N N . GLY A 56 ? 0.5112 0.2252 0.8031 -0.0074 -0.1919 0.1262 56 GLY A N 406 C CA . GLY A 56 ? 0.5230 0.2149 0.8309 0.0042 -0.2166 0.1023 56 GLY A CA 407 C C . GLY A 56 ? 0.5388 0.2204 0.9182 0.0002 -0.2357 0.1138 56 GLY A C 408 O O . GLY A 56 ? 0.5381 0.2237 0.9567 -0.0079 -0.2354 0.1286 56 GLY A O 409 N N . LYS A 57 ? 0.5530 0.2223 0.9541 0.0058 -0.2521 0.1080 57 LYS A N 410 C CA . LYS A 57 ? 0.5699 0.2291 1.0477 0.0017 -0.2719 0.1213 57 LYS A CA 411 C C . LYS A 57 ? 0.5748 0.2460 1.0731 -0.0096 -0.2636 0.1602 57 LYS A C 412 O O . LYS A 57 ? 0.5837 0.2471 1.1488 -0.0131 -0.2806 0.1750 57 LYS A O 413 C CB . LYS A 57 ? 0.5844 0.2219 1.0878 0.0163 -0.3003 0.0863 57 LYS A CB 414 C CG . LYS A 57 ? 0.5906 0.2184 1.0881 0.0275 -0.3148 0.0498 57 LYS A CG 415 C CD . LYS A 57 ? 0.5937 0.2185 1.1434 0.0204 -0.3235 0.0581 57 LYS A CD 416 C CE . LYS A 57 ? 0.6062 0.2203 1.2467 0.0149 -0.3445 0.0728 57 LYS A CE 417 N NZ . LYS A 57 ? 0.6245 0.2197 1.3016 0.0291 -0.3756 0.0376 57 LYS A NZ 418 N N . LEU A 58 ? 0.5701 0.2614 1.0155 -0.0154 -0.2389 0.1778 58 LEU A N 419 C CA . LEU A 58 ? 0.5790 0.2859 1.0362 -0.0258 -0.2311 0.2155 58 LEU A CA 420 C C . LEU A 58 ? 0.5855 0.3116 1.0869 -0.0405 -0.2232 0.2551 58 LEU A C 421 O O . LEU A 58 ? 0.5794 0.3162 1.0723 -0.0443 -0.2106 0.2554 58 LEU A O 422 C CB . LEU A 58 ? 0.5712 0.2959 0.9562 -0.0263 -0.2089 0.2185 58 LEU A CB 423 C CG . LEU A 58 ? 0.5667 0.2789 0.9016 -0.0130 -0.2109 0.1843 58 LEU A CG 424 C CD1 . LEU A 58 ? 0.5624 0.2936 0.8433 -0.0163 -0.1915 0.1961 58 LEU A CD1 425 C CD2 . LEU A 58 ? 0.5763 0.2660 0.9455 -0.0031 -0.2350 0.1670 58 LEU A CD2 426 N N . SER A 59 ? 0.6008 0.3334 1.1512 -0.0487 -0.2300 0.2900 59 SER A N 427 C CA . SER A 59 ? 0.6105 0.3671 1.2052 -0.0634 -0.2212 0.3347 59 SER A CA 428 C C . SER A 59 ? 0.6123 0.4066 1.1480 -0.0716 -0.1899 0.3574 59 SER A C 429 O O . SER A 59 ? 0.6089 0.4091 1.0804 -0.0674 -0.1793 0.3454 59 SER A O 430 C CB . SER A 59 ? 0.6243 0.3793 1.2904 -0.0698 -0.2386 0.3691 59 SER A CB 431 O OG . SER A 59 ? 0.6261 0.3897 1.2593 -0.0701 -0.2347 0.3814 59 SER A OG 432 N N . ASN A 60 ? 0.6226 0.4439 1.1828 -0.0827 -0.1757 0.3887 60 ASN A N 433 C CA . ASN A 60 ? 0.6310 0.4955 1.1436 -0.0908 -0.1460 0.4130 60 ASN A CA 434 C C . ASN A 60 ? 0.6474 0.5309 1.1329 -0.0943 -0.1422 0.4379 60 ASN A C 435 O O . ASN A 60 ? 0.6463 0.5521 1.0641 -0.0935 -0.1234 0.4322 60 ASN A O 436 C CB . ASN A 60 ? 0.6397 0.5345 1.1987 -0.1028 -0.1336 0.4508 60 ASN A CB 437 C CG . ASN A 60 ? 0.6288 0.5171 1.1955 -0.1004 -0.1280 0.4271 60 ASN A CG 438 O OD1 . ASN A 60 ? 0.6153 0.4803 1.1456 -0.0903 -0.1313 0.3839 60 ASN A OD1 439 N ND2 . ASN A 60 ? 0.6342 0.5453 1.2508 -0.1100 -0.1193 0.4577 60 ASN A ND2 440 N N . GLN A 61 ? 0.6654 0.5396 1.2077 -0.0979 -0.1618 0.4642 61 GLN A N 441 C CA . GLN A 61 ? 0.6837 0.5736 1.2116 -0.1017 -0.1627 0.4916 61 GLN A CA 442 C C . GLN A 61 ? 0.6812 0.5502 1.1515 -0.0904 -0.1674 0.4546 61 GLN A C 443 O O . GLN A 61 ? 0.6854 0.5777 1.0986 -0.0915 -0.1536 0.4608 61 GLN A O 444 C CB . GLN A 61 ? 0.6963 0.5775 1.3113 -0.1080 -0.1857 0.5280 61 GLN A CB 445 N N . GLN A 62 ? 0.6795 0.5074 1.1661 -0.0791 -0.1869 0.4161 62 GLN A N 446 C CA . GLN A 62 ? 0.6752 0.4834 1.1113 -0.0672 -0.1908 0.3790 62 GLN A CA 447 C C . GLN A 62 ? 0.6647 0.4881 1.0196 -0.0639 -0.1673 0.3567 62 GLN A C 448 O O . GLN A 62 ? 0.6632 0.4951 0.9692 -0.0615 -0.1605 0.3523 62 GLN A O 449 C CB . GLN A 62 ? 0.6715 0.4396 1.1345 -0.0546 -0.2121 0.3379 62 GLN A CB 450 C CG . GLN A 62 ? 0.6823 0.4291 1.2242 -0.0536 -0.2398 0.3465 62 GLN A CG 451 C CD . GLN A 62 ? 0.6826 0.3960 1.2569 -0.0413 -0.2606 0.3042 62 GLN A CD 452 O OE1 . GLN A 62 ? 0.6766 0.3855 1.2307 -0.0372 -0.2554 0.2799 62 GLN A OE1 453 N NE2 . GLN A 62 ? 0.6911 0.3826 1.3167 -0.0348 -0.2852 0.2940 62 GLN A NE2 454 N N . TRP A 63 ? 0.6573 0.4836 1.0045 -0.0638 -0.1568 0.3426 63 TRP A N 455 C CA . TRP A 63 ? 0.6492 0.4903 0.9314 -0.0610 -0.1355 0.3214 63 TRP A CA 456 C C . TRP A 63 ? 0.6619 0.5449 0.9062 -0.0693 -0.1144 0.3471 63 TRP A C 457 O O . TRP A 63 ? 0.6547 0.5463 0.8425 -0.0652 -0.1039 0.3296 63 TRP A O 458 C CB . TRP A 63 ? 0.6383 0.4766 0.9304 -0.0605 -0.1293 0.3058 63 TRP A CB 459 C CG . TRP A 63 ? 0.6282 0.4820 0.8619 -0.0580 -0.1089 0.2854 63 TRP A CG 460 C CD1 . TRP A 63 ? 0.6303 0.5187 0.8461 -0.0648 -0.0866 0.2972 63 TRP A CD1 461 C CD2 . TRP A 63 ? 0.6130 0.4510 0.8009 -0.0476 -0.1088 0.2503 63 TRP A CD2 462 N NE1 . TRP A 63 ? 0.6200 0.5125 0.7856 -0.0590 -0.0743 0.2687 63 TRP A NE1 463 C CE2 . TRP A 63 ? 0.6103 0.4719 0.7591 -0.0490 -0.0877 0.2419 63 TRP A CE2 464 C CE3 . TRP A 63 ? 0.6063 0.4147 0.7854 -0.0369 -0.1242 0.2252 63 TRP A CE3 465 C CZ2 . TRP A 63 ? 0.5957 0.4499 0.7019 -0.0408 -0.0830 0.2114 63 TRP A CZ2 466 C CZ3 . TRP A 63 ? 0.5954 0.3994 0.7275 -0.0288 -0.1175 0.1971 63 TRP A CZ3 467 C CH2 . TRP A 63 ? 0.5887 0.4144 0.6876 -0.0313 -0.0979 0.1918 63 TRP A CH2 468 N N . GLU A 64 ? 0.6771 0.5880 0.9540 -0.0806 -0.1090 0.3883 64 GLU A N 469 C CA . GLU A 64 ? 0.6918 0.6504 0.9336 -0.0885 -0.0885 0.4151 64 GLU A CA 470 C C . GLU A 64 ? 0.7019 0.6673 0.9066 -0.0869 -0.0922 0.4201 64 GLU A C 471 O O . GLU A 64 ? 0.7017 0.6964 0.8516 -0.0870 -0.0765 0.4159 64 GLU A O 472 C CB . GLU A 64 ? 0.7100 0.6986 1.0010 -0.1008 -0.0845 0.4643 64 GLU A CB 473 N N . LYS A 65 ? 0.7083 0.6462 0.9461 -0.0849 -0.1141 0.4265 65 LYS A N 474 C CA . LYS A 65 ? 0.7200 0.6613 0.9336 -0.0837 -0.1208 0.4339 65 LYS A CA 475 C C . LYS A 65 ? 0.7042 0.6229 0.8694 -0.0720 -0.1211 0.3890 65 LYS A C 476 O O . LYS A 65 ? 0.7127 0.6466 0.8333 -0.0708 -0.1159 0.3868 65 LYS A O 477 C CB . LYS A 65 ? 0.7286 0.6510 1.0047 -0.0863 -0.1446 0.4598 65 LYS A CB 478 C CG . LYS A 65 ? 0.7503 0.7078 1.0610 -0.0995 -0.1445 0.5175 65 LYS A CG 479 C CD . LYS A 65 ? 0.7557 0.7125 1.1381 -0.1067 -0.1492 0.5432 65 LYS A CD 480 C CE . LYS A 65 ? 0.7562 0.7465 1.1192 -0.1121 -0.1247 0.5498 65 LYS A CE 481 N NZ . LYS A 65 ? 0.7605 0.7515 1.1988 -0.1197 -0.1294 0.5778 65 LYS A NZ 482 N N . LEU A 66 ? 0.6913 0.5758 0.8658 -0.0632 -0.1275 0.3541 66 LEU A N 483 C CA . LEU A 66 ? 0.6763 0.5450 0.8039 -0.0524 -0.1241 0.3137 66 LEU A CA 484 C C . LEU A 66 ? 0.6682 0.5653 0.7427 -0.0536 -0.1023 0.3035 66 LEU A C 485 O O . LEU A 66 ? 0.6671 0.5689 0.7005 -0.0494 -0.0983 0.2891 66 LEU A O 486 C CB . LEU A 66 ? 0.6673 0.5009 0.8117 -0.0428 -0.1337 0.2806 66 LEU A CB 487 C CG . LEU A 66 ? 0.6695 0.4725 0.8313 -0.0335 -0.1530 0.2649 66 LEU A CG 488 C CD1 . LEU A 66 ? 0.6621 0.4383 0.8350 -0.0235 -0.1612 0.2317 66 LEU A CD1 489 C CD2 . LEU A 66 ? 0.6679 0.4735 0.7861 -0.0283 -0.1495 0.2541 66 LEU A CD2 490 N N . GLN A 67 ? 0.6637 0.5808 0.7438 -0.0592 -0.0889 0.3105 67 GLN A N 491 C CA . GLN A 67 ? 0.6612 0.6105 0.6981 -0.0606 -0.0680 0.3014 67 GLN A CA 492 C C . GLN A 67 ? 0.6775 0.6612 0.6812 -0.0648 -0.0621 0.3198 67 GLN A C 493 O O . GLN A 67 ? 0.6679 0.6614 0.6286 -0.0603 -0.0552 0.2982 67 GLN A O 494 C CB . GLN A 67 ? 0.6635 0.6343 0.7201 -0.0669 -0.0545 0.3123 67 GLN A CB 495 C CG . GLN A 67 ? 0.6658 0.6719 0.6824 -0.0672 -0.0327 0.2986 67 GLN A CG 496 C CD . GLN A 67 ? 0.6662 0.6886 0.7053 -0.0713 -0.0191 0.3014 67 GLN A CD 497 O OE1 . GLN A 67 ? 0.6506 0.6574 0.6908 -0.0663 -0.0158 0.2728 67 GLN A OE1 498 N NE2 . GLN A 67 ? 0.6808 0.7364 0.7402 -0.0804 -0.0109 0.3376 67 GLN A NE2 499 N N . HIS A 68 ? 0.6948 0.6978 0.7218 -0.0733 -0.0662 0.3605 68 HIS A N 500 C CA . HIS A 68 ? 0.7167 0.7557 0.7136 -0.0777 -0.0629 0.3830 68 HIS A CA 501 C C . HIS A 68 ? 0.7116 0.7296 0.6860 -0.0710 -0.0758 0.3664 68 HIS A C 502 O O . HIS A 68 ? 0.7188 0.7593 0.6489 -0.0693 -0.0695 0.3568 68 HIS A O 503 C CB . HIS A 68 ? 0.7413 0.8032 0.7757 -0.0885 -0.0674 0.4351 68 HIS A CB 504 C CG . HIS A 68 ? 0.7690 0.8795 0.7697 -0.0942 -0.0610 0.4633 68 HIS A CG 505 N ND1 . HIS A 68 ? 0.7933 0.9264 0.8232 -0.1037 -0.0681 0.5145 68 HIS A ND1 506 C CD2 . HIS A 68 ? 0.7793 0.9221 0.7213 -0.0915 -0.0497 0.4478 68 HIS A CD2 507 C CE1 . HIS A 68 ? 0.8153 0.9944 0.8011 -0.1066 -0.0608 0.5304 68 HIS A CE1 508 N NE2 . HIS A 68 ? 0.8095 0.9951 0.7411 -0.0989 -0.0500 0.4885 68 HIS A NE2 509 N N . MET A 69 ? 0.7013 0.6775 0.7075 -0.0663 -0.0936 0.3599 69 MET A N 510 C CA . MET A 69 ? 0.6983 0.6528 0.6876 -0.0588 -0.1046 0.3415 69 MET A CA 511 C C . MET A 69 ? 0.6813 0.6333 0.6255 -0.0508 -0.0945 0.3019 69 MET A C 512 O O . MET A 69 ? 0.6837 0.6428 0.5982 -0.0480 -0.0960 0.2943 69 MET A O 513 C CB . MET A 69 ? 0.6951 0.6059 0.7266 -0.0528 -0.1225 0.3323 69 MET A CB 514 C CG . MET A 69 ? 0.6962 0.5863 0.7121 -0.0439 -0.1316 0.3113 69 MET A CG 515 S SD . MET A 69 ? 0.6997 0.5443 0.7609 -0.0344 -0.1502 0.2933 69 MET A SD 516 C CE . MET A 69 ? 0.6750 0.5032 0.6951 -0.0218 -0.1427 0.2481 69 MET A CE 517 N N . PHE A 70 ? 0.6600 0.6000 0.6049 -0.0470 -0.0864 0.2777 70 PHE A N 518 C CA . PHE A 70 ? 0.6431 0.5811 0.5545 -0.0400 -0.0774 0.2429 70 PHE A CA 519 C C . PHE A 70 ? 0.6503 0.6297 0.5257 -0.0436 -0.0627 0.2416 70 PHE A C 520 O O . PHE A 70 ? 0.6436 0.6270 0.4908 -0.0386 -0.0602 0.2191 70 PHE A O 521 C CB . PHE A 70 ? 0.6285 0.5449 0.5541 -0.0356 -0.0739 0.2206 70 PHE A CB 522 C CG . PHE A 70 ? 0.6185 0.4960 0.5629 -0.0275 -0.0878 0.2065 70 PHE A CG 523 C CD1 . PHE A 70 ? 0.6136 0.4770 0.5404 -0.0196 -0.0926 0.1890 70 PHE A CD1 524 C CD2 . PHE A 70 ? 0.6190 0.4764 0.5997 -0.0270 -0.0961 0.2092 70 PHE A CD2 525 C CE1 . PHE A 70 ? 0.6070 0.4404 0.5484 -0.0111 -0.1035 0.1750 70 PHE A CE1 526 C CE2 . PHE A 70 ? 0.6125 0.4388 0.6076 -0.0181 -0.1091 0.1924 70 PHE A CE2 527 C CZ . PHE A 70 ? 0.6088 0.4247 0.5823 -0.0099 -0.1117 0.1754 70 PHE A CZ 528 N N . GLN A 71 ? 0.6595 0.6718 0.5385 -0.0516 -0.0531 0.2649 71 GLN A N 529 C CA . GLN A 71 ? 0.6729 0.7326 0.5169 -0.0546 -0.0388 0.2651 71 GLN A CA 530 C C . GLN A 71 ? 0.6853 0.7620 0.5001 -0.0542 -0.0460 0.2709 71 GLN A C 531 O O . GLN A 71 ? 0.6899 0.7913 0.4705 -0.0511 -0.0391 0.2501 71 GLN A O 532 C CB . GLN A 71 ? 0.6907 0.7871 0.5465 -0.0636 -0.0279 0.2973 71 GLN A CB 533 C CG . GLN A 71 ? 0.6816 0.7780 0.5580 -0.0645 -0.0151 0.2883 71 GLN A CG 534 C CD . GLN A 71 ? 0.6992 0.8252 0.6011 -0.0741 -0.0075 0.3279 71 GLN A CD 535 O OE1 . GLN A 71 ? 0.7216 0.8726 0.6228 -0.0804 -0.0107 0.3636 71 GLN A OE1 536 N NE2 . GLN A 71 ? 0.6912 0.8159 0.6187 -0.0756 0.0021 0.3238 71 GLN A NE2 537 N N . VAL A 72 ? 0.6897 0.7536 0.5221 -0.0571 -0.0611 0.2984 72 VAL A N 538 C CA . VAL A 72 ? 0.7041 0.7816 0.5153 -0.0573 -0.0711 0.3086 72 VAL A CA 539 C C . VAL A 72 ? 0.6850 0.7320 0.4858 -0.0481 -0.0789 0.2751 72 VAL A C 540 O O . VAL A 72 ? 0.6921 0.7567 0.4632 -0.0458 -0.0805 0.2640 72 VAL A O 541 C CB . VAL A 72 ? 0.7168 0.7903 0.5587 -0.0638 -0.0859 0.3511 72 VAL A CB 542 C CG1 . VAL A 72 ? 0.7330 0.8190 0.5547 -0.0638 -0.0979 0.3613 72 VAL A CG1 543 C CG2 . VAL A 72 ? 0.7361 0.8454 0.5912 -0.0737 -0.0776 0.3896 72 VAL A CG2 544 N N . TYR A 73 ? 0.6615 0.6655 0.4882 -0.0428 -0.0841 0.2604 73 TYR A N 545 C CA . TYR A 73 ? 0.6421 0.6190 0.4619 -0.0336 -0.0879 0.2285 73 TYR A CA 546 C C . TYR A 73 ? 0.6349 0.6296 0.4262 -0.0301 -0.0763 0.1988 73 TYR A C 547 O O . TYR A 73 ? 0.6319 0.6285 0.4069 -0.0259 -0.0803 0.1833 73 TYR A O 548 C CB . TYR A 73 ? 0.6230 0.5601 0.4711 -0.0281 -0.0914 0.2161 73 TYR A CB 549 C CG . TYR A 73 ? 0.6050 0.5226 0.4436 -0.0189 -0.0902 0.1841 73 TYR A CG 550 C CD1 . TYR A 73 ? 0.6038 0.5102 0.4391 -0.0138 -0.0990 0.1786 73 TYR A CD1 551 C CD2 . TYR A 73 ? 0.5926 0.5059 0.4286 -0.0157 -0.0801 0.1616 73 TYR A CD2 552 C CE1 . TYR A 73 ? 0.5880 0.4800 0.4182 -0.0059 -0.0971 0.1533 73 TYR A CE1 553 C CE2 . TYR A 73 ? 0.5773 0.4756 0.4088 -0.0079 -0.0793 0.1371 73 TYR A CE2 554 C CZ . TYR A 73 ? 0.5752 0.4637 0.4039 -0.0031 -0.0873 0.1338 73 TYR A CZ 555 O OH . TYR A 73 ? 0.5572 0.4339 0.3854 0.0041 -0.0857 0.1132 73 TYR A OH 556 N N . ARG A 74 ? 0.6296 0.6366 0.4202 -0.0317 -0.0630 0.1902 74 ARG A N 557 C CA . ARG A 74 ? 0.6261 0.6490 0.3986 -0.0279 -0.0523 0.1594 74 ARG A CA 558 C C . ARG A 74 ? 0.6438 0.7055 0.3850 -0.0288 -0.0513 0.1552 74 ARG A C 559 O O . ARG A 74 ? 0.6388 0.7010 0.3697 -0.0232 -0.0531 0.1283 74 ARG A O 560 C CB . ARG A 74 ? 0.6251 0.6590 0.4065 -0.0303 -0.0382 0.1543 74 ARG A CB 561 C CG . ARG A 74 ? 0.6257 0.6776 0.3953 -0.0262 -0.0275 0.1211 74 ARG A CG 562 C CD . ARG A 74 ? 0.6225 0.6783 0.4087 -0.0276 -0.0148 0.1143 74 ARG A CD 563 N NE . ARG A 74 ? 0.6435 0.7324 0.4274 -0.0348 -0.0050 0.1382 74 ARG A NE 564 C CZ . ARG A 74 ? 0.6474 0.7543 0.4422 -0.0370 0.0091 0.1343 74 ARG A CZ 565 N NH1 . ARG A 74 ? 0.6304 0.7247 0.4400 -0.0325 0.0143 0.1061 74 ARG A NH1 566 N NH2 . ARG A 74 ? 0.6665 0.8064 0.4603 -0.0438 0.0182 0.1610 74 ARG A NH2 567 N N . VAL A 75 ? 0.6654 0.7616 0.3936 -0.0355 -0.0491 0.1823 75 VAL A N 568 C CA . VAL A 75 ? 0.6886 0.8276 0.3831 -0.0363 -0.0496 0.1817 75 VAL A CA 569 C C . VAL A 75 ? 0.6875 0.8116 0.3767 -0.0334 -0.0669 0.1823 75 VAL A C 570 O O . VAL A 75 ? 0.6954 0.8343 0.3649 -0.0290 -0.0703 0.1587 75 VAL A O 571 C CB . VAL A 75 ? 0.7178 0.8994 0.4006 -0.0446 -0.0442 0.2185 75 VAL A CB 572 N N . SER A 76 ? 0.6779 0.7727 0.3895 -0.0356 -0.0783 0.2074 76 SER A N 573 C CA . SER A 76 ? 0.6761 0.7532 0.3904 -0.0329 -0.0947 0.2104 76 SER A CA 574 C C . SER A 76 ? 0.6538 0.7054 0.3717 -0.0243 -0.0972 0.1749 76 SER A C 575 O O . SER A 76 ? 0.6582 0.7164 0.3648 -0.0213 -0.1062 0.1646 76 SER A O 576 C CB . SER A 76 ? 0.6696 0.7155 0.4171 -0.0354 -0.1051 0.2383 76 SER A CB 577 O OG . SER A 76 ? 0.6926 0.7634 0.4432 -0.0440 -0.1073 0.2773 76 SER A OG 578 N N . PHE A 77 ? 0.6264 0.6501 0.3628 -0.0205 -0.0900 0.1585 77 PHE A N 579 C CA . PHE A 77 ? 0.6045 0.6045 0.3500 -0.0127 -0.0909 0.1295 77 PHE A CA 580 C C . PHE A 77 ? 0.6133 0.6396 0.3411 -0.0101 -0.0879 0.1025 77 PHE A C 581 O O . PHE A 77 ? 0.6135 0.6356 0.3424 -0.0059 -0.0964 0.0891 77 PHE A O 582 C CB . PHE A 77 ? 0.5812 0.5557 0.3463 -0.0100 -0.0825 0.1195 77 PHE A CB 583 C CG . PHE A 77 ? 0.5587 0.5126 0.3355 -0.0025 -0.0823 0.0945 77 PHE A CG 584 C CD1 . PHE A 77 ? 0.5459 0.4714 0.3379 0.0025 -0.0898 0.0969 77 PHE A CD1 585 C CD2 . PHE A 77 ? 0.5538 0.5190 0.3299 -0.0003 -0.0746 0.0693 77 PHE A CD2 586 C CE1 . PHE A 77 ? 0.5285 0.4391 0.3329 0.0091 -0.0885 0.0784 77 PHE A CE1 587 C CE2 . PHE A 77 ? 0.5357 0.4833 0.3291 0.0059 -0.0752 0.0507 77 PHE A CE2 588 C CZ . PHE A 77 ? 0.5232 0.4445 0.3295 0.0104 -0.0817 0.0571 77 PHE A CZ 589 N N . THR A 78 ? 0.6237 0.6781 0.3390 -0.0124 -0.0762 0.0939 78 THR A N 590 C CA . THR A 78 ? 0.6366 0.7202 0.3382 -0.0092 -0.0727 0.0635 78 THR A CA 591 C C . THR A 78 ? 0.6640 0.7726 0.3436 -0.0088 -0.0847 0.0631 78 THR A C 592 O O . THR A 78 ? 0.6640 0.7726 0.3479 -0.0033 -0.0917 0.0367 78 THR A O 593 C CB . THR A 78 ? 0.6488 0.7660 0.3384 -0.0121 -0.0574 0.0593 78 THR A CB 594 O OG1 . THR A 78 ? 0.6261 0.7190 0.3396 -0.0122 -0.0479 0.0573 78 THR A OG1 595 C CG2 . THR A 78 ? 0.6630 0.8149 0.3397 -0.0076 -0.0542 0.0234 78 THR A CG2 596 N N . ARG A 79 ? 0.6885 0.8186 0.3485 -0.0146 -0.0885 0.0936 79 ARG A N 597 C CA . ARG A 79 ? 0.7177 0.8757 0.3539 -0.0148 -0.1013 0.0976 79 ARG A CA 598 C C . ARG A 79 ? 0.7074 0.8341 0.3611 -0.0111 -0.1176 0.0947 79 ARG A C 599 O O . ARG A 79 ? 0.7178 0.8586 0.3632 -0.0073 -0.1278 0.0754 79 ARG A O 600 C CB . ARG A 79 ? 0.7427 0.9280 0.3603 -0.0227 -0.1027 0.1388 79 ARG A CB 601 N N . ASP A 80 ? 0.6893 0.7752 0.3693 -0.0115 -0.1199 0.1119 80 ASP A N 602 C CA . ASP A 80 ? 0.6808 0.7372 0.3810 -0.0075 -0.1329 0.1111 80 ASP A CA 603 C C . ASP A 80 ? 0.6666 0.7078 0.3838 -0.0001 -0.1329 0.0771 80 ASP A C 604 O O . ASP A 80 ? 0.6672 0.7042 0.3924 0.0030 -0.1451 0.0699 80 ASP A O 605 C CB . ASP A 80 ? 0.6641 0.6839 0.3895 -0.0083 -0.1337 0.1339 80 ASP A CB 606 C CG . ASP A 80 ? 0.6842 0.7142 0.4063 -0.0153 -0.1402 0.1711 80 ASP A CG 607 O OD1 . ASP A 80 ? 0.7052 0.7705 0.4035 -0.0197 -0.1456 0.1837 80 ASP A OD1 608 O OD2 . ASP A 80 ? 0.6752 0.6789 0.4210 -0.0162 -0.1409 0.1882 80 ASP A OD2 609 N N . ILE A 81 ? 0.6538 0.6870 0.3809 0.0021 -0.1203 0.0583 81 ILE A N 610 C CA . ILE A 81 ? 0.6420 0.6626 0.3919 0.0085 -0.1203 0.0291 81 ILE A CA 611 C C . ILE A 81 ? 0.6679 0.7202 0.4080 0.0107 -0.1270 0.0020 81 ILE A C 612 O O . ILE A 81 ? 0.6628 0.7081 0.4224 0.0151 -0.1370 -0.0137 81 ILE A O 613 C CB . ILE A 81 ? 0.6189 0.6246 0.3854 0.0100 -0.1064 0.0184 81 ILE A CB 614 C CG1 . ILE A 81 ? 0.6006 0.5740 0.3793 0.0096 -0.1026 0.0403 81 ILE A CG1 615 C CG2 . ILE A 81 ? 0.6056 0.6045 0.3996 0.0157 -0.1071 -0.0099 81 ILE A CG2 616 C CD1 . ILE A 81 ? 0.5870 0.5336 0.3856 0.0141 -0.1102 0.0468 81 ILE A CD1 617 N N . GLN A 82 ? 0.7011 0.7903 0.4129 0.0081 -0.1219 -0.0037 82 GLN A N 618 C CA . GLN A 82 ? 0.7334 0.8584 0.4325 0.0114 -0.1285 -0.0336 82 GLN A CA 619 C C . GLN A 82 ? 0.7625 0.8996 0.4481 0.0113 -0.1469 -0.0255 82 GLN A C 620 O O . GLN A 82 ? 0.7720 0.9224 0.4635 0.0161 -0.1587 -0.0529 82 GLN A O 621 C CB . GLN A 82 ? 0.7560 0.9231 0.4255 0.0095 -0.1167 -0.0416 82 GLN A CB 622 C CG . GLN A 82 ? 0.7381 0.8938 0.4253 0.0096 -0.0995 -0.0507 82 GLN A CG 623 C CD . GLN A 82 ? 0.7585 0.9532 0.4370 0.0127 -0.0906 -0.0837 82 GLN A CD 624 O OE1 . GLN A 82 ? 0.7805 1.0054 0.4341 0.0093 -0.0782 -0.0745 82 GLN A OE1 625 N NE2 . GLN A 82 ? 0.7561 0.9518 0.4596 0.0194 -0.0968 -0.1227 82 GLN A NE2 626 N N . GLU A 83 ? 0.7801 0.9117 0.4524 0.0060 -0.1506 0.0118 83 GLU A N 627 C CA . GLU A 83 ? 0.8065 0.9407 0.4743 0.0055 -0.1692 0.0255 83 GLU A CA 628 C C . GLU A 83 ? 0.7900 0.8869 0.4966 0.0102 -0.1783 0.0175 83 GLU A C 629 O O . GLU A 83 ? 0.8016 0.9065 0.5145 0.0135 -0.1937 0.0028 83 GLU A O 630 C CB . GLU A 83 ? 0.8186 0.9526 0.4730 -0.0014 -0.1711 0.0699 83 GLU A CB 631 C CG . GLU A 83 ? 0.8599 1.0438 0.4728 -0.0063 -0.1720 0.0849 83 GLU A CG 632 C CD . GLU A 83 ? 0.8937 1.1109 0.4856 -0.0038 -0.1898 0.0716 83 GLU A CD 633 O OE1 . GLU A 83 ? 0.8889 1.0852 0.5030 0.0000 -0.2045 0.0608 83 GLU A OE1 634 O OE2 . GLU A 83 ? 0.9348 1.2018 0.4884 -0.0053 -0.1892 0.0718 83 GLU A OE2 635 N N . LEU A 84 ? 0.7694 0.8286 0.5021 0.0108 -0.1690 0.0277 84 LEU A N 636 C CA . LEU A 84 ? 0.7589 0.7850 0.5295 0.0156 -0.1737 0.0233 84 LEU A CA 637 C C . LEU A 84 ? 0.7659 0.7966 0.5592 0.0211 -0.1780 -0.0113 84 LEU A C 638 O O . LEU A 84 ? 0.7695 0.7930 0.5859 0.0243 -0.1907 -0.0173 84 LEU A O 639 C CB . LEU A 84 ? 0.7312 0.7243 0.5205 0.0164 -0.1602 0.0353 84 LEU A CB 640 C CG . LEU A 84 ? 0.7099 0.6727 0.5367 0.0220 -0.1606 0.0330 84 LEU A CG 641 C CD1 . LEU A 84 ? 0.7160 0.6722 0.5534 0.0230 -0.1747 0.0466 84 LEU A CD1 642 C CD2 . LEU A 84 ? 0.6883 0.6263 0.5244 0.0232 -0.1472 0.0443 84 LEU A CD2 643 N N . VAL A 85 ? 0.7735 0.8163 0.5651 0.0222 -0.1680 -0.0339 85 VAL A N 644 C CA . VAL A 85 ? 0.7803 0.8309 0.5984 0.0273 -0.1730 -0.0696 85 VAL A CA 645 C C . VAL A 85 ? 0.8180 0.8993 0.6234 0.0290 -0.1912 -0.0881 85 VAL A C 646 O O . VAL A 85 ? 0.8157 0.8914 0.6540 0.0332 -0.2043 -0.1053 85 VAL A O 647 C CB . VAL A 85 ? 0.7735 0.8346 0.5927 0.0279 -0.1590 -0.0905 85 VAL A CB 648 C CG1 . VAL A 85 ? 0.7814 0.8579 0.6285 0.0334 -0.1668 -0.1314 85 VAL A CG1 649 C CG2 . VAL A 85 ? 0.7424 0.7710 0.5837 0.0275 -0.1448 -0.0764 85 VAL A CG2 650 N N . LYS A 86 ? 0.8580 0.9735 0.6174 0.0259 -0.1925 -0.0833 86 LYS A N 651 C CA . LYS A 86 ? 0.9012 1.0532 0.6405 0.0279 -0.2101 -0.1014 86 LYS A CA 652 C C . LYS A 86 ? 0.9144 1.0548 0.6629 0.0276 -0.2290 -0.0844 86 LYS A C 653 O O . LYS A 86 ? 0.9262 1.0773 0.6896 0.0319 -0.2468 -0.1081 86 LYS A O 654 C CB . LYS A 86 ? 0.9339 1.1301 0.6182 0.0244 -0.2051 -0.0939 86 LYS A CB 655 N N . MET A 87 ? 0.9189 1.0371 0.6636 0.0229 -0.2260 -0.0453 87 MET A N 656 C CA . MET A 87 ? 0.9319 1.0358 0.6912 0.0225 -0.2425 -0.0262 87 MET A CA 657 C C . MET A 87 ? 0.9220 0.9975 0.7342 0.0279 -0.2487 -0.0420 87 MET A C 658 O O . MET A 87 ? 0.9296 1.0005 0.7592 0.0291 -0.2655 -0.0375 87 MET A O 659 C CB . MET A 87 ? 0.9219 1.0046 0.6761 0.0173 -0.2363 0.0156 87 MET A CB 660 N N . MET A 88 ? 0.9105 0.9682 0.7507 0.0308 -0.2352 -0.0576 88 MET A N 661 C CA . MET A 88 ? 0.9050 0.9458 0.7983 0.0360 -0.2407 -0.0772 88 MET A CA 662 C C . MET A 88 ? 0.9144 0.9777 0.8175 0.0398 -0.2450 -0.1183 88 MET A C 663 O O . MET A 88 ? 0.9191 0.9836 0.8612 0.0441 -0.2595 -0.1416 88 MET A O 664 C CB . MET A 88 ? 0.8837 0.8906 0.8070 0.0369 -0.2235 -0.0627 88 MET A CB 665 C CG . MET A 88 ? 0.8839 0.8701 0.7972 0.0344 -0.2173 -0.0269 88 MET A CG 666 S SD . MET A 88 ? 0.8692 0.8210 0.8221 0.0380 -0.2006 -0.0145 88 MET A SD 667 C CE . MET A 88 ? 0.8549 0.8104 0.8003 0.0374 -0.1841 -0.0298 88 MET A CE 668 N N . ASP A 93 ? 0.5434 0.5468 0.6108 0.0472 -0.1832 -0.1674 93 ASP A N 669 C CA . ASP A 93 ? 0.5592 0.5875 0.6312 0.0493 -0.1856 -0.2051 93 ASP A CA 670 C C . ASP A 93 ? 0.5492 0.5766 0.6078 0.0472 -0.1673 -0.2022 93 ASP A C 671 O O . ASP A 93 ? 0.5273 0.5307 0.5956 0.0453 -0.1557 -0.1764 93 ASP A O 672 C CB . ASP A 93 ? 0.5556 0.5830 0.6995 0.0541 -0.1990 -0.2333 93 ASP A CB 673 N N . TYR A 94 ? 0.5677 0.6238 0.6051 0.0481 -0.1653 -0.2302 94 TYR A N 674 C CA . TYR A 94 ? 0.5601 0.6192 0.5920 0.0467 -0.1490 -0.2331 94 TYR A CA 675 C C . TYR A 94 ? 0.5416 0.5896 0.6426 0.0498 -0.1503 -0.2521 94 TYR A C 676 O O . TYR A 94 ? 0.5446 0.5965 0.6932 0.0541 -0.1654 -0.2769 94 TYR A O 677 C CB . TYR A 94 ? 0.5911 0.6898 0.5817 0.0475 -0.1458 -0.2586 94 TYR A CB 678 C CG . TYR A 94 ? 0.6107 0.7251 0.5343 0.0434 -0.1427 -0.2357 94 TYR A CG 679 C CD1 . TYR A 94 ? 0.6007 0.7020 0.4928 0.0376 -0.1281 -0.1998 94 TYR A CD1 680 C CD2 . TYR A 94 ? 0.6418 0.7862 0.5366 0.0453 -0.1559 -0.2497 94 TYR A CD2 681 C CE1 . TYR A 94 ? 0.6191 0.7350 0.4580 0.0333 -0.1264 -0.1762 94 TYR A CE1 682 C CE2 . TYR A 94 ? 0.6612 0.8223 0.4980 0.0410 -0.1539 -0.2245 94 TYR A CE2 683 C CZ . TYR A 94 ? 0.6495 0.7958 0.4611 0.0347 -0.1390 -0.1868 94 TYR A CZ 684 O OH . TYR A 94 ? 0.6708 0.8335 0.4334 0.0300 -0.1383 -0.1593 94 TYR A OH 685 N N . PRO A 95 ? 0.5195 0.5553 0.6311 0.0478 -0.1364 -0.2414 95 PRO A N 686 C CA . PRO A 95 ? 0.5136 0.5455 0.5758 0.0430 -0.1199 -0.2154 95 PRO A CA 687 C C . PRO A 95 ? 0.4915 0.4939 0.5404 0.0400 -0.1161 -0.1735 95 PRO A C 688 O O . PRO A 95 ? 0.4747 0.4575 0.5617 0.0417 -0.1217 -0.1625 95 PRO A O 689 C CB . PRO A 95 ? 0.5038 0.5341 0.5977 0.0433 -0.1105 -0.2264 95 PRO A CB 690 C CG . PRO A 95 ? 0.4910 0.5076 0.6572 0.0466 -0.1207 -0.2368 95 PRO A CG 691 C CD . PRO A 95 ? 0.5035 0.5293 0.6837 0.0501 -0.1376 -0.2546 95 PRO A CD 692 N N . ILE A 96 ? 0.4918 0.4937 0.4895 0.0361 -0.1067 -0.1512 96 ILE A N 693 C CA . ILE A 96 ? 0.4764 0.4539 0.4562 0.0339 -0.1029 -0.1151 96 ILE A CA 694 C C . ILE A 96 ? 0.4618 0.4289 0.4301 0.0312 -0.0894 -0.0998 96 ILE A C 695 O O . ILE A 96 ? 0.4709 0.4546 0.4159 0.0286 -0.0821 -0.1067 96 ILE A O 696 C CB . ILE A 96 ? 0.4953 0.4815 0.4278 0.0314 -0.1066 -0.1010 96 ILE A CB 697 C CG1 . ILE A 96 ? 0.5119 0.5123 0.4492 0.0338 -0.1218 -0.1166 96 ILE A CG1 698 C CG2 . ILE A 96 ? 0.4834 0.4448 0.4029 0.0300 -0.1034 -0.0675 96 ILE A CG2 699 C CD1 . ILE A 96 ? 0.4995 0.4789 0.4705 0.0366 -0.1307 -0.1068 96 ILE A CD1 700 N N . GLU A 97 ? 0.4378 0.3802 0.4223 0.0321 -0.0862 -0.0791 97 GLU A N 701 C CA . GLU A 97 ? 0.4267 0.3572 0.3996 0.0301 -0.0761 -0.0629 97 GLU A CA 702 C C . GLU A 97 ? 0.4213 0.3345 0.3710 0.0303 -0.0759 -0.0360 97 GLU A C 703 O O . GLU A 97 ? 0.4140 0.3161 0.3783 0.0337 -0.0802 -0.0266 97 GLU A O 704 C CB . GLU A 97 ? 0.4086 0.3285 0.4238 0.0322 -0.0736 -0.0642 97 GLU A CB 705 C CG . GLU A 97 ? 0.4108 0.3460 0.4604 0.0327 -0.0749 -0.0927 97 GLU A CG 706 C CD . GLU A 97 ? 0.4201 0.3723 0.4489 0.0298 -0.0670 -0.1066 97 GLU A CD 707 O OE1 . GLU A 97 ? 0.4199 0.3674 0.4180 0.0268 -0.0596 -0.0900 97 GLU A OE1 708 O OE2 . GLU A 97 ? 0.4288 0.4009 0.4756 0.0310 -0.0683 -0.1352 97 GLU A OE2 709 N N . ILE A 98 ? 0.4258 0.3383 0.3436 0.0270 -0.0712 -0.0242 98 ILE A N 710 C CA . ILE A 98 ? 0.4220 0.3177 0.3231 0.0277 -0.0717 -0.0016 98 ILE A CA 711 C C . ILE A 98 ? 0.4174 0.3031 0.3138 0.0266 -0.0650 0.0069 98 ILE A C 712 O O . ILE A 98 ? 0.4195 0.3155 0.3104 0.0227 -0.0599 0.0008 98 ILE A O 713 C CB . ILE A 98 ? 0.4372 0.3402 0.3097 0.0247 -0.0766 0.0073 98 ILE A CB 714 C CG1 . ILE A 98 ? 0.4433 0.3544 0.3215 0.0264 -0.0856 0.0000 98 ILE A CG1 715 C CG2 . ILE A 98 ? 0.4347 0.3196 0.2971 0.0257 -0.0777 0.0283 98 ILE A CG2 716 C CD1 . ILE A 98 ? 0.4617 0.3857 0.3131 0.0230 -0.0922 0.0078 98 ILE A CD1 717 N N . GLN A 99 ? 0.4094 0.2775 0.3092 0.0307 -0.0653 0.0199 99 GLN A N 718 C CA . GLN A 99 ? 0.4078 0.2653 0.3036 0.0310 -0.0619 0.0275 99 GLN A CA 719 C C . GLN A 99 ? 0.4149 0.2598 0.2963 0.0337 -0.0657 0.0411 99 GLN A C 720 O O . GLN A 99 ? 0.4136 0.2545 0.2967 0.0380 -0.0689 0.0454 99 GLN A O 721 C CB . GLN A 99 ? 0.3953 0.2472 0.3139 0.0350 -0.0596 0.0266 99 GLN A CB 722 C CG . GLN A 99 ? 0.3905 0.2530 0.3332 0.0326 -0.0571 0.0124 99 GLN A CG 723 C CD . GLN A 99 ? 0.3798 0.2390 0.3539 0.0367 -0.0574 0.0153 99 GLN A CD 724 O OE1 . GLN A 99 ? 0.3768 0.2400 0.3716 0.0386 -0.0601 0.0127 99 GLN A OE1 725 N NE2 . GLN A 99 ? 0.3729 0.2261 0.3532 0.0379 -0.0557 0.0225 99 GLN A NE2 726 N N . LEU A 100 ? 0.4230 0.2624 0.2946 0.0314 -0.0660 0.0471 100 LEU A N 727 C CA . LEU A 100 ? 0.4322 0.2587 0.2975 0.0349 -0.0712 0.0568 100 LEU A CA 728 C C . LEU A 100 ? 0.4299 0.2471 0.2991 0.0374 -0.0709 0.0564 100 LEU A C 729 O O . LEU A 100 ? 0.4311 0.2520 0.3041 0.0329 -0.0677 0.0535 100 LEU A O 730 C CB . LEU A 100 ? 0.4477 0.2768 0.3040 0.0292 -0.0756 0.0661 100 LEU A CB 731 C CG . LEU A 100 ? 0.4580 0.2937 0.3086 0.0280 -0.0802 0.0709 100 LEU A CG 732 C CD1 . LEU A 100 ? 0.4631 0.3183 0.3079 0.0234 -0.0771 0.0633 100 LEU A CD1 733 C CD2 . LEU A 100 ? 0.4705 0.3040 0.3187 0.0241 -0.0871 0.0858 100 LEU A CD2 734 N N . SER A 101 ? 0.4297 0.2376 0.2989 0.0453 -0.0741 0.0576 101 SER A N 735 C CA . SER A 101 ? 0.4341 0.2342 0.3044 0.0494 -0.0768 0.0558 101 SER A CA 736 C C . SER A 101 ? 0.4490 0.2393 0.3174 0.0537 -0.0848 0.0572 101 SER A C 737 O O . SER A 101 ? 0.4502 0.2397 0.3166 0.0607 -0.0862 0.0565 101 SER A O 738 C CB . SER A 101 ? 0.4301 0.2334 0.3024 0.0568 -0.0738 0.0540 101 SER A CB 739 O OG . SER A 101 ? 0.4336 0.2324 0.3038 0.0616 -0.0779 0.0515 101 SER A OG 740 N N . ALA A 102 ? 0.4578 0.2418 0.3320 0.0495 -0.0903 0.0591 102 ALA A N 741 C CA . ALA A 102 ? 0.4710 0.2448 0.3534 0.0525 -0.1003 0.0600 102 ALA A CA 742 C C . ALA A 102 ? 0.4816 0.2469 0.3743 0.0542 -0.1075 0.0546 102 ALA A C 743 O O . ALA A 102 ? 0.4768 0.2439 0.3741 0.0478 -0.1052 0.0570 102 ALA A O 744 C CB . ALA A 102 ? 0.4767 0.2524 0.3653 0.0437 -0.1028 0.0726 102 ALA A CB 745 N N . GLY A 103 ? 0.4939 0.2512 0.3927 0.0635 -0.1168 0.0455 103 GLY A N 746 C CA . GLY A 103 ? 0.5074 0.2569 0.4183 0.0666 -0.1265 0.0368 103 GLY A CA 747 C C . GLY A 103 ? 0.5252 0.2708 0.4381 0.0800 -0.1360 0.0207 103 GLY A C 748 O O . GLY A 103 ? 0.5241 0.2702 0.4376 0.0852 -0.1366 0.0187 103 GLY A O 749 N N . CYS A 104 ? 0.5422 0.2858 0.4575 0.0862 -0.1441 0.0079 104 CYS A N 750 C CA . CYS A 104 ? 0.5672 0.3116 0.4822 0.1007 -0.1538 -0.0121 104 CYS A CA 751 C C . CYS A 104 ? 0.5914 0.3442 0.4906 0.1086 -0.1567 -0.0242 104 CYS A C 752 O O . CYS A 104 ? 0.5863 0.3364 0.4890 0.1021 -0.1580 -0.0194 104 CYS A O 753 C CB . CYS A 104 ? 0.5764 0.3065 0.5262 0.1015 -0.1702 -0.0199 104 CYS A CB 754 S SG . CYS A 104 ? 0.5685 0.2857 0.5507 0.0881 -0.1788 -0.0082 104 CYS A SG 755 N N . GLU A 105 ? 0.6261 0.3916 0.5079 0.1230 -0.1573 -0.0391 105 GLU A N 756 C CA . GLU A 105 ? 0.6617 0.4415 0.5237 0.1330 -0.1608 -0.0505 105 GLU A CA 757 C C . GLU A 105 ? 0.6952 0.4714 0.5710 0.1443 -0.1797 -0.0773 105 GLU A C 758 O O . GLU A 105 ? 0.7030 0.4798 0.5868 0.1532 -0.1836 -0.0917 105 GLU A O 759 C CB . GLU A 105 ? 0.6748 0.4780 0.5072 0.1420 -0.1474 -0.0468 105 GLU A CB 760 C CG . GLU A 105 ? 0.7062 0.5321 0.5142 0.1563 -0.1513 -0.0597 105 GLU A CG 761 C CD . GLU A 105 ? 0.7370 0.5747 0.5400 0.1734 -0.1582 -0.0861 105 GLU A CD 762 O OE1 . GLU A 105 ? 0.7459 0.5904 0.5474 0.1781 -0.1489 -0.0862 105 GLU A OE1 763 O OE2 . GLU A 105 ? 0.7695 0.6109 0.5719 0.1829 -0.1738 -0.1089 105 GLU A OE2 764 N N . MET A 106 ? 0.7179 0.4904 0.6001 0.1445 -0.1923 -0.0855 106 MET A N 765 C CA . MET A 106 ? 0.7528 0.5187 0.6573 0.1536 -0.2139 -0.1126 106 MET A CA 766 C C . MET A 106 ? 0.7868 0.5758 0.6633 0.1711 -0.2211 -0.1360 106 MET A C 767 O O . MET A 106 ? 0.7928 0.5937 0.6472 0.1710 -0.2197 -0.1296 106 MET A O 768 C CB . MET A 106 ? 0.7525 0.4997 0.6890 0.1428 -0.2262 -0.1081 106 MET A CB 769 C CG . MET A 106 ? 0.7331 0.4642 0.6929 0.1247 -0.2173 -0.0813 106 MET A CG 770 S SD . MET A 106 ? 0.7363 0.4545 0.7269 0.1211 -0.2185 -0.0765 106 MET A SD 771 C CE . MET A 106 ? 0.7542 0.4576 0.7958 0.1280 -0.2468 -0.1014 106 MET A CE 772 N N . TYR A 107 ? 0.8172 0.6147 0.6959 0.1863 -0.2291 -0.1633 107 TYR A N 773 C CA . TYR A 107 ? 0.8544 0.6765 0.7096 0.2050 -0.2397 -0.1924 107 TYR A CA 774 C C . TYR A 107 ? 0.8736 0.6823 0.7599 0.2082 -0.2664 -0.2174 107 TYR A C 775 O O . TYR A 107 ? 0.8774 0.6640 0.8096 0.2060 -0.2798 -0.2292 107 TYR A O 776 C CB . TYR A 107 ? 0.8733 0.7139 0.7195 0.2215 -0.2362 -0.2150 107 TYR A CB 777 N N . ALA A 111 ? 0.7723 0.5326 0.7933 0.2148 -0.2924 -0.2594 111 ALA A N 778 C CA . ALA A 111 ? 0.7560 0.5212 0.7610 0.2115 -0.2709 -0.2397 111 ALA A CA 779 C C . ALA A 111 ? 0.7257 0.4897 0.7000 0.1947 -0.2493 -0.1983 111 ALA A C 780 O O . ALA A 111 ? 0.7238 0.4898 0.6793 0.1888 -0.2480 -0.1875 111 ALA A O 781 C CB . ALA A 111 ? 0.7769 0.5737 0.7464 0.2314 -0.2627 -0.2641 111 ALA A CB 782 N N . SER A 112 ? 0.7046 0.4658 0.6773 0.1876 -0.2337 -0.1768 112 SER A N 783 C CA . SER A 112 ? 0.6753 0.4367 0.6228 0.1728 -0.2139 -0.1412 112 SER A CA 784 C C . SER A 112 ? 0.6550 0.4200 0.5965 0.1706 -0.1983 -0.1263 112 SER A C 785 O O . SER A 112 ? 0.6603 0.4198 0.6287 0.1756 -0.2043 -0.1368 112 SER A O 786 C CB . SER A 112 ? 0.6627 0.4020 0.6365 0.1545 -0.2183 -0.1189 112 SER A CB 787 O OG . SER A 112 ? 0.6677 0.3886 0.6878 0.1493 -0.2291 -0.1163 112 SER A OG 788 N N . GLU A 113 ? 0.6277 0.4017 0.5388 0.1631 -0.1798 -0.1025 113 GLU A N 789 C CA . GLU A 113 ? 0.6068 0.3829 0.5137 0.1582 -0.1653 -0.0845 113 GLU A CA 790 C C . GLU A 113 ? 0.5779 0.3428 0.4857 0.1398 -0.1580 -0.0559 113 GLU A C 791 O O . GLU A 113 ? 0.5741 0.3388 0.4710 0.1332 -0.1562 -0.0480 113 GLU A O 792 C CB . GLU A 113 ? 0.6114 0.4137 0.4841 0.1681 -0.1494 -0.0842 113 GLU A CB 793 N N . SER A 114 ? 0.5577 0.3154 0.4785 0.1321 -0.1541 -0.0414 114 SER A N 794 C CA . SER A 114 ? 0.5340 0.2850 0.4548 0.1157 -0.1476 -0.0167 114 SER A CA 795 C C . SER A 114 ? 0.5161 0.2784 0.4176 0.1140 -0.1323 -0.0042 114 SER A C 796 O O . SER A 114 ? 0.5180 0.2902 0.4139 0.1240 -0.1277 -0.0111 114 SER A O 797 C CB . SER A 114 ? 0.5347 0.2705 0.4887 0.1069 -0.1579 -0.0072 114 SER A CB 798 O OG . SER A 114 ? 0.5447 0.2697 0.5224 0.1062 -0.1720 -0.0148 114 SER A OG 799 N N . PHE A 115 ? 0.4979 0.2602 0.3920 0.1016 -0.1248 0.0128 115 PHE A N 800 C CA . PHE A 115 ? 0.4843 0.2564 0.3655 0.0986 -0.1122 0.0240 115 PHE A CA 801 C C . PHE A 115 ? 0.4741 0.2426 0.3587 0.0843 -0.1102 0.0393 115 PHE A C 802 O O . PHE A 115 ? 0.4706 0.2336 0.3603 0.0764 -0.1136 0.0432 115 PHE A O 803 C CB . PHE A 115 ? 0.4806 0.2659 0.3432 0.1024 -0.1027 0.0238 115 PHE A CB 804 C CG . PHE A 115 ? 0.4762 0.2586 0.3363 0.0964 -0.1044 0.0249 115 PHE A CG 805 C CD1 . PHE A 115 ? 0.4875 0.2676 0.3473 0.1026 -0.1131 0.0128 115 PHE A CD1 806 C CD2 . PHE A 115 ? 0.4639 0.2467 0.3247 0.0850 -0.0982 0.0359 115 PHE A CD2 807 C CE1 . PHE A 115 ? 0.4856 0.2625 0.3467 0.0968 -0.1155 0.0144 115 PHE A CE1 808 C CE2 . PHE A 115 ? 0.4618 0.2428 0.3243 0.0797 -0.0993 0.0362 115 PHE A CE2 809 C CZ . PHE A 115 ? 0.4711 0.2483 0.3343 0.0852 -0.1079 0.0267 115 PHE A CZ 810 N N . LEU A 116 ? 0.4680 0.2422 0.3498 0.0816 -0.1042 0.0473 116 LEU A N 811 C CA . LEU A 116 ? 0.4625 0.2394 0.3423 0.0697 -0.1012 0.0589 116 LEU A CA 812 C C . LEU A 116 ? 0.4547 0.2418 0.3288 0.0711 -0.0929 0.0608 116 LEU A C 813 O O . LEU A 116 ? 0.4530 0.2411 0.3326 0.0745 -0.0941 0.0627 116 LEU A O 814 C CB . LEU A 116 ? 0.4711 0.2425 0.3633 0.0638 -0.1099 0.0682 116 LEU A CB 815 C CG . LEU A 116 ? 0.4722 0.2505 0.3604 0.0511 -0.1086 0.0810 116 LEU A CG 816 C CD1 . LEU A 116 ? 0.4829 0.2573 0.3865 0.0465 -0.1189 0.0939 116 LEU A CD1 817 C CD2 . LEU A 116 ? 0.4655 0.2558 0.3417 0.0484 -0.1014 0.0819 116 LEU A CD2 818 N N . HIS A 117 ? 0.4448 0.2391 0.3134 0.0688 -0.0854 0.0604 117 HIS A N 819 C CA . HIS A 117 ? 0.4376 0.2417 0.3090 0.0697 -0.0785 0.0626 117 HIS A CA 820 C C . HIS A 117 ? 0.4291 0.2386 0.3020 0.0599 -0.0770 0.0638 117 HIS A C 821 O O . HIS A 117 ? 0.4256 0.2350 0.2949 0.0536 -0.0769 0.0623 117 HIS A O 822 C CB . HIS A 117 ? 0.4379 0.2488 0.3093 0.0762 -0.0722 0.0615 117 HIS A CB 823 C CG . HIS A 117 ? 0.4513 0.2638 0.3175 0.0877 -0.0726 0.0582 117 HIS A CG 824 N ND1 . HIS A 117 ? 0.4606 0.2817 0.3209 0.0944 -0.0689 0.0577 117 HIS A ND1 825 C CD2 . HIS A 117 ? 0.4620 0.2711 0.3285 0.0942 -0.0767 0.0537 117 HIS A CD2 826 C CE1 . HIS A 117 ? 0.4705 0.2958 0.3241 0.1053 -0.0700 0.0516 117 HIS A CE1 827 N NE2 . HIS A 117 ? 0.4730 0.2903 0.3324 0.1056 -0.0746 0.0477 117 HIS A NE2 828 N N . VAL A 118 ? 0.4208 0.2369 0.3008 0.0592 -0.0761 0.0650 118 VAL A N 829 C CA . VAL A 118 ? 0.4167 0.2411 0.2989 0.0516 -0.0763 0.0618 118 VAL A CA 830 C C . VAL A 118 ? 0.4070 0.2386 0.3076 0.0540 -0.0724 0.0589 118 VAL A C 831 O O . VAL A 118 ? 0.4045 0.2366 0.3156 0.0600 -0.0714 0.0637 118 VAL A O 832 C CB . VAL A 118 ? 0.4258 0.2528 0.3034 0.0479 -0.0832 0.0654 118 VAL A CB 833 C CG1 . VAL A 118 ? 0.4293 0.2697 0.3044 0.0409 -0.0841 0.0589 118 VAL A CG1 834 C CG2 . VAL A 118 ? 0.4352 0.2547 0.3037 0.0459 -0.0886 0.0728 118 VAL A CG2 835 N N . ALA A 119 ? 0.3988 0.2372 0.3077 0.0495 -0.0703 0.0514 119 ALA A N 836 C CA . ALA A 119 ? 0.3915 0.2371 0.3273 0.0507 -0.0689 0.0478 119 ALA A CA 837 C C . ALA A 119 ? 0.3957 0.2510 0.3374 0.0453 -0.0734 0.0349 119 ALA A C 838 O O . ALA A 119 ? 0.4023 0.2630 0.3277 0.0401 -0.0738 0.0275 119 ALA A O 839 C CB . ALA A 119 ? 0.3838 0.2299 0.3337 0.0516 -0.0641 0.0485 119 ALA A CB 840 N N . PHE A 120 ? 0.3925 0.2527 0.3586 0.0471 -0.0770 0.0320 120 PHE A N 841 C CA . PHE A 120 ? 0.3980 0.2696 0.3740 0.0437 -0.0837 0.0161 120 PHE A CA 842 C C . PHE A 120 ? 0.3892 0.2649 0.4084 0.0451 -0.0838 0.0084 120 PHE A C 843 O O . PHE A 120 ? 0.3796 0.2515 0.4248 0.0491 -0.0826 0.0204 120 PHE A O 844 C CB . PHE A 120 ? 0.4057 0.2781 0.3799 0.0450 -0.0914 0.0196 120 PHE A CB 845 C CG . PHE A 120 ? 0.4153 0.3010 0.4029 0.0430 -0.1008 0.0021 120 PHE A CG 846 C CD1 . PHE A 120 ? 0.4303 0.3299 0.3934 0.0386 -0.1043 -0.0114 120 PHE A CD1 847 C CD2 . PHE A 120 ? 0.4117 0.2985 0.4377 0.0460 -0.1068 -0.0008 120 PHE A CD2 848 C CE1 . PHE A 120 ? 0.4419 0.3574 0.4146 0.0380 -0.1142 -0.0311 120 PHE A CE1 849 C CE2 . PHE A 120 ? 0.4214 0.3207 0.4623 0.0449 -0.1181 -0.0203 120 PHE A CE2 850 C CZ . PHE A 120 ? 0.4367 0.3509 0.4490 0.0414 -0.1222 -0.0371 120 PHE A CZ 851 N N . GLN A 121 ? 0.3916 0.2768 0.4216 0.0421 -0.0851 -0.0105 121 GLN A N 852 C CA . GLN A 121 ? 0.3862 0.2751 0.4654 0.0431 -0.0871 -0.0198 121 GLN A CA 853 C C . GLN A 121 ? 0.3776 0.2580 0.4772 0.0454 -0.0806 -0.0004 121 GLN A C 854 O O . GLN A 121 ? 0.3707 0.2519 0.5146 0.0476 -0.0827 0.0063 121 GLN A O 855 C CB . GLN A 121 ? 0.3859 0.2798 0.5000 0.0450 -0.0971 -0.0275 121 GLN A CB 856 C CG . GLN A 121 ? 0.4001 0.3049 0.4920 0.0436 -0.1058 -0.0451 121 GLN A CG 857 C CD . GLN A 121 ? 0.4111 0.3325 0.4981 0.0413 -0.1081 -0.0739 121 GLN A CD 858 O OE1 . GLN A 121 ? 0.4104 0.3341 0.4768 0.0390 -0.0998 -0.0758 121 GLN A OE1 859 N NE2 . GLN A 121 ? 0.4208 0.3559 0.5277 0.0425 -0.1196 -0.0978 121 GLN A NE2 860 N N . GLY A 122 ? 0.3810 0.2550 0.4498 0.0450 -0.0736 0.0095 122 GLY A N 861 C CA . GLY A 122 ? 0.3780 0.2472 0.4587 0.0475 -0.0683 0.0269 122 GLY A CA 862 C C . GLY A 122 ? 0.3808 0.2465 0.4528 0.0529 -0.0648 0.0494 122 GLY A C 863 O O . GLY A 122 ? 0.3808 0.2470 0.4584 0.0558 -0.0606 0.0646 122 GLY A O 864 N N . LYS A 123 ? 0.3887 0.2532 0.4463 0.0548 -0.0665 0.0512 123 LYS A N 865 C CA . LYS A 123 ? 0.3930 0.2576 0.4472 0.0610 -0.0626 0.0696 123 LYS A CA 866 C C . LYS A 123 ? 0.3921 0.2498 0.4042 0.0628 -0.0621 0.0697 123 LYS A C 867 O O . LYS A 123 ? 0.3936 0.2485 0.3913 0.0594 -0.0674 0.0599 123 LYS A O 868 C CB . LYS A 123 ? 0.4012 0.2714 0.4909 0.0623 -0.0662 0.0723 123 LYS A CB 869 C CG . LYS A 123 ? 0.4102 0.2859 0.5089 0.0691 -0.0600 0.0933 123 LYS A CG 870 C CD . LYS A 123 ? 0.4116 0.2982 0.5528 0.0710 -0.0559 0.1111 123 LYS A CD 871 C CE . LYS A 123 ? 0.4203 0.3183 0.5652 0.0785 -0.0470 0.1340 123 LYS A CE 872 N NZ . LYS A 123 ? 0.4228 0.3220 0.5862 0.0799 -0.0496 0.1342 123 LYS A NZ 873 N N . TYR A 124 ? 0.3896 0.2466 0.3854 0.0688 -0.0566 0.0811 124 TYR A N 874 C CA . TYR A 124 ? 0.3942 0.2447 0.3591 0.0722 -0.0571 0.0807 124 TYR A CA 875 C C . TYR A 124 ? 0.3943 0.2455 0.3669 0.0739 -0.0599 0.0820 124 TYR A C 876 O O . TYR A 124 ? 0.3895 0.2488 0.3855 0.0782 -0.0564 0.0912 124 TYR A O 877 C CB . TYR A 124 ? 0.3984 0.2532 0.3520 0.0805 -0.0509 0.0899 124 TYR A CB 878 C CG . TYR A 124 ? 0.4084 0.2585 0.3376 0.0865 -0.0516 0.0870 124 TYR A CG 879 C CD1 . TYR A 124 ? 0.4127 0.2502 0.3246 0.0824 -0.0585 0.0777 124 TYR A CD1 880 C CD2 . TYR A 124 ? 0.4145 0.2755 0.3409 0.0968 -0.0454 0.0939 124 TYR A CD2 881 C CE1 . TYR A 124 ? 0.4226 0.2551 0.3211 0.0883 -0.0610 0.0744 124 TYR A CE1 882 C CE2 . TYR A 124 ? 0.4246 0.2827 0.3333 0.1038 -0.0468 0.0871 124 TYR A CE2 883 C CZ . TYR A 124 ? 0.4295 0.2716 0.3270 0.0994 -0.0555 0.0768 124 TYR A CZ 884 O OH . TYR A 124 ? 0.4393 0.2780 0.3281 0.1065 -0.0586 0.0693 124 TYR A OH 885 N N . VAL A 125 ? 0.3960 0.2402 0.3521 0.0701 -0.0667 0.0748 125 VAL A N 886 C CA . VAL A 125 ? 0.3991 0.2434 0.3631 0.0709 -0.0719 0.0761 125 VAL A CA 887 C C . VAL A 125 ? 0.4079 0.2445 0.3535 0.0732 -0.0756 0.0776 125 VAL A C 888 O O . VAL A 125 ? 0.4118 0.2490 0.3684 0.0767 -0.0780 0.0814 125 VAL A O 889 C CB . VAL A 125 ? 0.4003 0.2478 0.3721 0.0636 -0.0806 0.0670 125 VAL A CB 890 C CG1 . VAL A 125 ? 0.3932 0.2483 0.3969 0.0627 -0.0796 0.0636 125 VAL A CG1 891 C CG2 . VAL A 125 ? 0.4068 0.2529 0.3526 0.0565 -0.0846 0.0590 125 VAL A CG2 892 N N . VAL A 126 ? 0.4124 0.2419 0.3362 0.0711 -0.0772 0.0748 126 VAL A N 893 C CA . VAL A 126 ? 0.4244 0.2458 0.3387 0.0717 -0.0836 0.0764 126 VAL A CA 894 C C . VAL A 126 ? 0.4305 0.2450 0.3318 0.0747 -0.0823 0.0739 126 VAL A C 895 O O . VAL A 126 ? 0.4271 0.2417 0.3200 0.0716 -0.0794 0.0711 126 VAL A O 896 C CB . VAL A 126 ? 0.4293 0.2507 0.3364 0.0624 -0.0930 0.0774 126 VAL A CB 897 C CG1 . VAL A 126 ? 0.4394 0.2524 0.3404 0.0612 -0.1005 0.0829 126 VAL A CG1 898 C CG2 . VAL A 126 ? 0.4297 0.2578 0.3504 0.0611 -0.0979 0.0781 126 VAL A CG2 899 N N . ARG A 127 ? 0.4423 0.2512 0.3458 0.0811 -0.0853 0.0731 127 ARG A N 900 C CA . ARG A 127 ? 0.4521 0.2530 0.3486 0.0835 -0.0887 0.0682 127 ARG A CA 901 C C . ARG A 127 ? 0.4596 0.2512 0.3658 0.0824 -0.0994 0.0704 127 ARG A C 902 O O . ARG A 127 ? 0.4593 0.2517 0.3773 0.0833 -0.1029 0.0746 127 ARG A O 903 C CB . ARG A 127 ? 0.4591 0.2650 0.3533 0.0956 -0.0825 0.0610 127 ARG A CB 904 C CG . ARG A 127 ? 0.4703 0.2820 0.3758 0.1061 -0.0802 0.0585 127 ARG A CG 905 C CD . ARG A 127 ? 0.4850 0.3066 0.3831 0.1189 -0.0743 0.0491 127 ARG A CD 906 N NE . ARG A 127 ? 0.4976 0.3289 0.4072 0.1300 -0.0703 0.0451 127 ARG A NE 907 C CZ . ARG A 127 ? 0.5129 0.3580 0.4170 0.1437 -0.0649 0.0342 127 ARG A CZ 908 N NH1 . ARG A 127 ? 0.5249 0.3753 0.4109 0.1480 -0.0644 0.0266 127 ARG A NH1 909 N NH2 . ARG A 127 ? 0.5200 0.3762 0.4371 0.1536 -0.0601 0.0302 127 ARG A NH2 910 N N . PHE A 128 ? 0.4647 0.2477 0.3706 0.0802 -0.1058 0.0688 128 PHE A N 911 C CA . PHE A 128 ? 0.4740 0.2475 0.3981 0.0820 -0.1169 0.0694 128 PHE A CA 912 C C . PHE A 128 ? 0.4814 0.2533 0.4115 0.0955 -0.1163 0.0534 128 PHE A C 913 O O . PHE A 128 ? 0.4813 0.2552 0.3996 0.0993 -0.1124 0.0447 128 PHE A O 914 C CB . PHE A 128 ? 0.4776 0.2440 0.4058 0.0725 -0.1252 0.0776 128 PHE A CB 915 C CG . PHE A 128 ? 0.4874 0.2451 0.4426 0.0719 -0.1386 0.0841 128 PHE A CG 916 C CD1 . PHE A 128 ? 0.4905 0.2511 0.4535 0.0648 -0.1447 0.1003 128 PHE A CD1 917 C CD2 . PHE A 128 ? 0.4951 0.2426 0.4715 0.0790 -0.1466 0.0733 128 PHE A CD2 918 C CE1 . PHE A 128 ? 0.5009 0.2538 0.4944 0.0638 -0.1584 0.1093 128 PHE A CE1 919 C CE2 . PHE A 128 ? 0.5042 0.2428 0.5145 0.0786 -0.1606 0.0793 128 PHE A CE2 920 C CZ . PHE A 128 ? 0.5076 0.2486 0.5276 0.0706 -0.1663 0.0990 128 PHE A CZ 921 N N . TRP A 129 ? 0.4897 0.2603 0.4389 0.1033 -0.1205 0.0485 129 TRP A N 922 C CA . TRP A 129 ? 0.5013 0.2758 0.4561 0.1182 -0.1191 0.0296 129 TRP A CA 923 C C . TRP A 129 ? 0.5112 0.2770 0.4986 0.1229 -0.1313 0.0235 129 TRP A C 924 O O . TRP A 129 ? 0.5076 0.2731 0.5106 0.1212 -0.1334 0.0321 129 TRP A O 925 C CB . TRP A 129 ? 0.5010 0.2928 0.4443 0.1269 -0.1046 0.0271 129 TRP A CB 926 C CG . TRP A 129 ? 0.5170 0.3202 0.4600 0.1431 -0.1007 0.0080 129 TRP A CG 927 C CD1 . TRP A 129 ? 0.5276 0.3400 0.4865 0.1547 -0.0979 -0.0014 129 TRP A CD1 928 C CD2 . TRP A 129 ? 0.5291 0.3386 0.4551 0.1503 -0.0995 -0.0057 129 TRP A CD2 929 N NE1 . TRP A 129 ? 0.5427 0.3696 0.4929 0.1695 -0.0939 -0.0215 129 TRP A NE1 930 C CE2 . TRP A 129 ? 0.5443 0.3697 0.4733 0.1671 -0.0957 -0.0243 129 TRP A CE2 931 C CE3 . TRP A 129 ? 0.5289 0.3343 0.4379 0.1447 -0.1015 -0.0046 129 TRP A CE3 932 C CZ2 . TRP A 129 ? 0.5608 0.3995 0.4726 0.1786 -0.0948 -0.0424 129 TRP A CZ2 933 C CZ3 . TRP A 129 ? 0.5432 0.3589 0.4381 0.1555 -0.1014 -0.0211 129 TRP A CZ3 934 C CH2 . TRP A 129 ? 0.5586 0.3915 0.4533 0.1724 -0.0986 -0.0400 129 TRP A CH2 935 N N . GLY A 130 ? 0.5221 0.2810 0.5240 0.1292 -0.1406 0.0079 130 GLY A N 936 C CA . GLY A 130 ? 0.5341 0.2830 0.5763 0.1338 -0.1550 0.0003 130 GLY A CA 937 C C . GLY A 130 ? 0.5322 0.2675 0.5977 0.1192 -0.1679 0.0233 130 GLY A C 938 O O . GLY A 130 ? 0.5347 0.2609 0.6087 0.1117 -0.1765 0.0295 130 GLY A O 939 N N . THR A 131 ? 0.5316 0.2680 0.6083 0.1152 -0.1690 0.0376 131 THR A N 940 C CA . THR A 131 ? 0.5349 0.2633 0.6341 0.1021 -0.1821 0.0625 131 THR A CA 941 C C . THR A 131 ? 0.5275 0.2645 0.6020 0.0912 -0.1760 0.0840 131 THR A C 942 O O . THR A 131 ? 0.5304 0.2662 0.6189 0.0811 -0.1863 0.1059 131 THR A O 943 C CB . THR A 131 ? 0.5453 0.2662 0.6941 0.1077 -0.1961 0.0599 131 THR A CB 944 O OG1 . THR A 131 ? 0.5413 0.2707 0.6882 0.1149 -0.1885 0.0548 131 THR A OG1 945 C CG2 . THR A 131 ? 0.5569 0.2703 0.7368 0.1202 -0.2044 0.0333 131 THR A CG2 946 N N . SER A 132 ? 0.5190 0.2666 0.5599 0.0934 -0.1608 0.0783 132 SER A N 947 C CA . SER A 132 ? 0.5145 0.2710 0.5387 0.0855 -0.1567 0.0929 132 SER A CA 948 C C . SER A 132 ? 0.5020 0.2682 0.4913 0.0842 -0.1421 0.0887 132 SER A C 949 O O . SER A 132 ? 0.4955 0.2637 0.4731 0.0916 -0.1328 0.0747 132 SER A O 950 C CB . SER A 132 ? 0.5177 0.2768 0.5623 0.0919 -0.1583 0.0920 132 SER A CB 951 O OG . SER A 132 ? 0.5157 0.2821 0.5549 0.1043 -0.1450 0.0749 132 SER A OG 952 N N . TRP A 133 ? 0.4973 0.2709 0.4726 0.0746 -0.1417 0.1011 133 TRP A N 953 C CA . TRP A 133 ? 0.4897 0.2729 0.4410 0.0726 -0.1302 0.0974 133 TRP A CA 954 C C . TRP A 133 ? 0.4847 0.2738 0.4444 0.0808 -0.1235 0.0918 133 TRP A C 955 O O . TRP A 133 ? 0.4820 0.2708 0.4607 0.0826 -0.1297 0.0961 133 TRP A O 956 C CB . TRP A 133 ? 0.4920 0.2835 0.4292 0.0606 -0.1341 0.1089 133 TRP A CB 957 C CG . TRP A 133 ? 0.5007 0.2917 0.4305 0.0520 -0.1387 0.1181 133 TRP A CG 958 C CD1 . TRP A 133 ? 0.5141 0.3035 0.4566 0.0460 -0.1508 0.1343 133 TRP A CD1 959 C CD2 . TRP A 133 ? 0.4985 0.2923 0.4109 0.0481 -0.1315 0.1144 133 TRP A CD2 960 N NE1 . TRP A 133 ? 0.5193 0.3118 0.4532 0.0385 -0.1504 0.1420 133 TRP A NE1 961 C CE2 . TRP A 133 ? 0.5091 0.3038 0.4240 0.0398 -0.1385 0.1288 133 TRP A CE2 962 C CE3 . TRP A 133 ? 0.4884 0.2849 0.3871 0.0505 -0.1201 0.1022 133 TRP A CE3 963 C CZ2 . TRP A 133 ? 0.5099 0.3086 0.4135 0.0342 -0.1333 0.1299 133 TRP A CZ2 964 C CZ3 . TRP A 133 ? 0.4900 0.2887 0.3775 0.0450 -0.1161 0.1020 133 TRP A CZ3 965 C CH2 . TRP A 133 ? 0.4979 0.2977 0.3876 0.0371 -0.1222 0.1151 133 TRP A CH2 966 N N . GLN A 134 ? 0.4809 0.2766 0.4302 0.0855 -0.1111 0.0843 134 GLN A N 967 C CA . GLN A 134 ? 0.4814 0.2859 0.4419 0.0935 -0.1026 0.0820 134 GLN A CA 968 C C . GLN A 134 ? 0.4723 0.2860 0.4246 0.0901 -0.0943 0.0832 134 GLN A C 969 O O . GLN A 134 ? 0.4678 0.2821 0.4049 0.0883 -0.0894 0.0802 134 GLN A O 970 C CB . GLN A 134 ? 0.4899 0.2974 0.4542 0.1066 -0.0951 0.0720 134 GLN A CB 971 C CG . GLN A 134 ? 0.5075 0.3058 0.4872 0.1114 -0.1046 0.0660 134 GLN A CG 972 C CD . GLN A 134 ? 0.5190 0.3240 0.5019 0.1262 -0.0978 0.0506 134 GLN A CD 973 O OE1 . GLN A 134 ? 0.5225 0.3418 0.4935 0.1330 -0.0848 0.0474 134 GLN A OE1 974 N NE2 . GLN A 134 ? 0.5344 0.3311 0.5352 0.1313 -0.1073 0.0410 134 GLN A NE2 975 N N . THR A 135 ? 0.4690 0.2893 0.4366 0.0892 -0.0943 0.0875 135 THR A N 976 C CA . THR A 135 ? 0.4624 0.2921 0.4350 0.0880 -0.0869 0.0883 135 THR A CA 977 C C . THR A 135 ? 0.4615 0.3005 0.4401 0.0982 -0.0735 0.0896 135 THR A C 978 O O . THR A 135 ? 0.4745 0.3167 0.4602 0.1072 -0.0698 0.0891 135 THR A O 979 C CB . THR A 135 ? 0.4611 0.2958 0.4558 0.0850 -0.0924 0.0916 135 THR A CB 980 O OG1 . THR A 135 ? 0.4705 0.3060 0.4853 0.0916 -0.0933 0.0956 135 THR A OG1 981 C CG2 . THR A 135 ? 0.4667 0.2988 0.4505 0.0750 -0.1055 0.0897 135 THR A CG2 982 N N . VAL A 136 ? 0.4522 0.2980 0.4294 0.0971 -0.0664 0.0915 136 VAL A N 983 C CA . VAL A 136 ? 0.4537 0.3131 0.4348 0.1060 -0.0535 0.0970 136 VAL A CA 984 C C . VAL A 136 ? 0.4452 0.3175 0.4591 0.1083 -0.0482 0.1079 136 VAL A C 985 O O . VAL A 136 ? 0.4420 0.3112 0.4745 0.1012 -0.0552 0.1086 136 VAL A O 986 C CB . VAL A 136 ? 0.4526 0.3141 0.4206 0.1035 -0.0496 0.0973 136 VAL A CB 987 C CG1 . VAL A 136 ? 0.4593 0.3073 0.4009 0.0998 -0.0563 0.0871 136 VAL A CG1 988 C CG2 . VAL A 136 ? 0.4435 0.3072 0.4308 0.0957 -0.0510 0.1013 136 VAL A CG2 989 N N . PRO A 137 ? 0.4432 0.3323 0.4659 0.1187 -0.0362 0.1159 137 PRO A N 990 C CA . PRO A 137 ? 0.4342 0.3372 0.4940 0.1202 -0.0305 0.1297 137 PRO A CA 991 C C . PRO A 137 ? 0.4178 0.3224 0.4978 0.1125 -0.0322 0.1371 137 PRO A C 992 O O . PRO A 137 ? 0.4151 0.3219 0.4822 0.1110 -0.0292 0.1387 137 PRO A O 993 C CB . PRO A 137 ? 0.4427 0.3692 0.5015 0.1327 -0.0145 0.1388 137 PRO A CB 994 C CG . PRO A 137 ? 0.4554 0.3752 0.4830 0.1390 -0.0163 0.1226 137 PRO A CG 995 C CD . PRO A 137 ? 0.4534 0.3525 0.4566 0.1299 -0.0276 0.1122 137 PRO A CD 996 N N . GLY A 138 ? 0.4088 0.3116 0.5232 0.1075 -0.0392 0.1395 138 GLY A N 997 C CA . GLY A 138 ? 0.3981 0.3017 0.5413 0.1005 -0.0437 0.1424 138 GLY A CA 998 C C . GLY A 138 ? 0.3957 0.2838 0.5272 0.0910 -0.0579 0.1241 138 GLY A C 999 O O . GLY A 138 ? 0.3874 0.2766 0.5468 0.0858 -0.0635 0.1213 138 GLY A O 1000 N N . ALA A 139 ? 0.4029 0.2791 0.4966 0.0891 -0.0637 0.1118 139 ALA A N 1001 C CA . ALA A 139 ? 0.4074 0.2742 0.4872 0.0806 -0.0762 0.0963 139 ALA A CA 1002 C C . ALA A 139 ? 0.4119 0.2798 0.5188 0.0773 -0.0883 0.0910 139 ALA A C 1003 O O . ALA A 139 ? 0.4116 0.2821 0.5388 0.0814 -0.0887 0.0988 139 ALA A O 1004 C CB . ALA A 139 ? 0.4151 0.2721 0.4538 0.0793 -0.0793 0.0902 139 ALA A CB 1005 N N . PRO A 140 ? 0.4182 0.2859 0.5258 0.0706 -0.0989 0.0761 140 PRO A N 1006 C CA . PRO A 140 ? 0.4252 0.2959 0.5551 0.0681 -0.1133 0.0674 140 PRO A CA 1007 C C . PRO A 140 ? 0.4364 0.3031 0.5489 0.0685 -0.1205 0.0705 140 PRO A C 1008 O O . PRO A 140 ? 0.4452 0.3066 0.5197 0.0670 -0.1200 0.0711 140 PRO A O 1009 C CB . PRO A 140 ? 0.4304 0.3046 0.5477 0.0619 -0.1219 0.0473 140 PRO A CB 1010 C CG . PRO A 140 ? 0.4237 0.2971 0.5355 0.0615 -0.1110 0.0478 140 PRO A CG 1011 C CD . PRO A 140 ? 0.4189 0.2862 0.5085 0.0659 -0.0984 0.0648 140 PRO A CD 1012 N N . SER A 141 ? 0.4396 0.3089 0.5845 0.0705 -0.1279 0.0737 141 SER A N 1013 C CA . SER A 141 ? 0.4494 0.3148 0.5859 0.0716 -0.1350 0.0792 141 SER A CA 1014 C C . SER A 141 ? 0.4650 0.3306 0.5687 0.0652 -0.1499 0.0699 141 SER A C 1015 O O . SER A 141 ? 0.4708 0.3321 0.5588 0.0650 -0.1547 0.0774 141 SER A O 1016 C CB . SER A 141 ? 0.4493 0.3185 0.6333 0.0748 -0.1405 0.0847 141 SER A CB 1017 O OG . SER A 141 ? 0.4523 0.3275 0.6651 0.0715 -0.1521 0.0725 141 SER A OG 1018 N N . TRP A 142 ? 0.4740 0.3472 0.5696 0.0602 -0.1573 0.0542 142 TRP A N 1019 C CA . TRP A 142 ? 0.4945 0.3747 0.5542 0.0544 -0.1696 0.0465 142 TRP A CA 1020 C C . TRP A 142 ? 0.4971 0.3726 0.5149 0.0519 -0.1626 0.0556 142 TRP A C 1021 O O . TRP A 142 ? 0.5109 0.3927 0.5023 0.0473 -0.1722 0.0580 142 TRP A O 1022 C CB . TRP A 142 ? 0.5061 0.4001 0.5651 0.0511 -0.1773 0.0241 142 TRP A CB 1023 C CG . TRP A 142 ? 0.5003 0.3947 0.5556 0.0506 -0.1649 0.0157 142 TRP A CG 1024 C CD1 . TRP A 142 ? 0.4908 0.3844 0.5848 0.0530 -0.1602 0.0088 142 TRP A CD1 1025 C CD2 . TRP A 142 ? 0.5066 0.4026 0.5223 0.0472 -0.1565 0.0149 142 TRP A CD2 1026 N NE1 . TRP A 142 ? 0.4868 0.3809 0.5670 0.0515 -0.1499 0.0032 142 TRP A NE1 1027 C CE2 . TRP A 142 ? 0.4971 0.3925 0.5289 0.0481 -0.1471 0.0061 142 TRP A CE2 1028 C CE3 . TRP A 142 ? 0.5216 0.4202 0.4947 0.0432 -0.1565 0.0229 142 TRP A CE3 1029 C CZ2 . TRP A 142 ? 0.4975 0.3943 0.5028 0.0454 -0.1376 0.0030 142 TRP A CZ2 1030 C CZ3 . TRP A 142 ? 0.5220 0.4226 0.4699 0.0404 -0.1464 0.0209 142 TRP A CZ3 1031 C CH2 . TRP A 142 ? 0.5106 0.4100 0.4739 0.0417 -0.1371 0.0099 142 TRP A CH2 1032 N N . LEU A 143 ? 0.4858 0.3522 0.4997 0.0548 -0.1471 0.0615 143 LEU A N 1033 C CA . LEU A 143 ? 0.4895 0.3493 0.4724 0.0533 -0.1416 0.0701 143 LEU A CA 1034 C C . LEU A 143 ? 0.4970 0.3487 0.4807 0.0554 -0.1463 0.0840 143 LEU A C 1035 O O . LEU A 143 ? 0.5008 0.3491 0.4631 0.0524 -0.1479 0.0911 143 LEU A O 1036 C CB . LEU A 143 ? 0.4777 0.3307 0.4591 0.0570 -0.1258 0.0707 143 LEU A CB 1037 C CG . LEU A 143 ? 0.4764 0.3354 0.4494 0.0534 -0.1209 0.0592 143 LEU A CG 1038 C CD1 . LEU A 143 ? 0.4616 0.3160 0.4465 0.0580 -0.1076 0.0615 143 LEU A CD1 1039 C CD2 . LEU A 143 ? 0.4888 0.3503 0.4269 0.0474 -0.1222 0.0588 143 LEU A CD2 1040 N N . ASP A 144 ? 0.4960 0.3451 0.5092 0.0604 -0.1488 0.0883 144 ASP A N 1041 C CA . ASP A 144 ? 0.5028 0.3439 0.5246 0.0640 -0.1521 0.0995 144 ASP A CA 1042 C C . ASP A 144 ? 0.5206 0.3634 0.5280 0.0574 -0.1682 0.1075 144 ASP A C 1043 O O . ASP A 144 ? 0.5234 0.3585 0.5264 0.0575 -0.1697 0.1169 144 ASP A O 1044 C CB . ASP A 144 ? 0.5001 0.3414 0.5601 0.0706 -0.1516 0.1021 144 ASP A CB 1045 C CG . ASP A 144 ? 0.4905 0.3330 0.5666 0.0784 -0.1336 0.1014 144 ASP A CG 1046 O OD1 . ASP A 144 ? 0.4862 0.3274 0.5431 0.0794 -0.1226 0.0988 144 ASP A OD1 1047 O OD2 . ASP A 144 ? 0.4924 0.3391 0.6019 0.0836 -0.1308 0.1051 144 ASP A OD2 1048 N N . LEU A 145 ? 0.5321 0.3868 0.5345 0.0520 -0.1808 0.1039 145 LEU A N 1049 C CA . LEU A 145 ? 0.5527 0.4156 0.5382 0.0452 -0.1970 0.1139 145 LEU A CA 1050 C C . LEU A 145 ? 0.5595 0.4252 0.5123 0.0395 -0.1936 0.1209 145 LEU A C 1051 O O . LEU A 145 ? 0.5663 0.4258 0.5205 0.0379 -0.1982 0.1368 145 LEU A O 1052 C CB . LEU A 145 ? 0.5642 0.4445 0.5464 0.0417 -0.2110 0.1046 145 LEU A CB 1053 N N . PRO A 146 ? 0.5603 0.4353 0.4897 0.0366 -0.1857 0.1095 146 PRO A N 1054 C CA . PRO A 146 ? 0.5678 0.4474 0.4696 0.0310 -0.1816 0.1174 146 PRO A CA 1055 C C . PRO A 146 ? 0.5570 0.4180 0.4660 0.0337 -0.1727 0.1259 146 PRO A C 1056 O O . PRO A 146 ? 0.5648 0.4269 0.4638 0.0288 -0.1755 0.1402 146 PRO A O 1057 C CB . PRO A 146 ? 0.5661 0.4581 0.4502 0.0294 -0.1728 0.0993 146 PRO A CB 1058 C CG . PRO A 146 ? 0.5523 0.4388 0.4614 0.0354 -0.1694 0.0832 146 PRO A CG 1059 C CD . PRO A 146 ? 0.5535 0.4364 0.4861 0.0381 -0.1812 0.0893 146 PRO A CD 1060 N N . ILE A 147 ? 0.5370 0.3835 0.4650 0.0417 -0.1629 0.1177 147 ILE A N 1061 C CA . ILE A 147 ? 0.5307 0.3616 0.4666 0.0463 -0.1562 0.1214 147 ILE A CA 1062 C C . ILE A 147 ? 0.5413 0.3641 0.4980 0.0477 -0.1672 0.1347 147 ILE A C 1063 O O . ILE A 147 ? 0.5428 0.3575 0.5030 0.0470 -0.1693 0.1423 147 ILE A O 1064 C CB . ILE A 147 ? 0.5133 0.3373 0.4604 0.0554 -0.1422 0.1091 147 ILE A CB 1065 C CG1 . ILE A 147 ? 0.5060 0.3363 0.4369 0.0531 -0.1324 0.0987 147 ILE A CG1 1066 C CG2 . ILE A 147 ? 0.5105 0.3220 0.4663 0.0624 -0.1372 0.1092 147 ILE A CG2 1067 C CD1 . ILE A 147 ? 0.5098 0.3391 0.4198 0.0485 -0.1289 0.0997 147 ILE A CD1 1068 N N . LYS A 148 ? 0.5461 0.3709 0.5214 0.0496 -0.1758 0.1374 148 LYS A N 1069 C CA . LYS A 148 ? 0.5588 0.3771 0.5584 0.0503 -0.1884 0.1507 148 LYS A CA 1070 C C . LYS A 148 ? 0.5772 0.4028 0.5652 0.0402 -0.2015 0.1700 148 LYS A C 1071 O O . LYS A 148 ? 0.5849 0.4018 0.5920 0.0397 -0.2086 0.1826 148 LYS A O 1072 C CB . LYS A 148 ? 0.5618 0.3828 0.5845 0.0535 -0.1957 0.1503 148 LYS A CB 1073 C CG . LYS A 148 ? 0.5738 0.3880 0.6282 0.0549 -0.2093 0.1633 148 LYS A CG 1074 C CD . LYS A 148 ? 0.5753 0.3920 0.6563 0.0590 -0.2147 0.1611 148 LYS A CD 1075 C CE . LYS A 148 ? 0.5858 0.3951 0.7040 0.0613 -0.2278 0.1728 148 LYS A CE 1076 N NZ . LYS A 148 ? 0.6076 0.4237 0.7220 0.0513 -0.2487 0.1938 148 LYS A NZ 1077 N N . VAL A 149 ? 0.5866 0.4302 0.5458 0.0326 -0.2043 0.1721 149 VAL A N 1078 C CA . VAL A 149 ? 0.6087 0.4669 0.5515 0.0228 -0.2143 0.1926 149 VAL A CA 1079 C C . VAL A 149 ? 0.6071 0.4594 0.5446 0.0203 -0.2065 0.1987 149 VAL A C 1080 O O . VAL A 149 ? 0.6187 0.4696 0.5702 0.0157 -0.2155 0.2201 149 VAL A O 1081 C CB . VAL A 149 ? 0.6233 0.5078 0.5324 0.0170 -0.2170 0.1885 149 VAL A CB 1082 C CG1 . VAL A 149 ? 0.6483 0.5539 0.5348 0.0074 -0.2230 0.2107 149 VAL A CG1 1083 C CG2 . VAL A 149 ? 0.6297 0.5211 0.5489 0.0186 -0.2302 0.1856 149 VAL A CG2 1084 N N . LEU A 150 ? 0.5938 0.4426 0.5162 0.0231 -0.1910 0.1809 150 LEU A N 1085 C CA . LEU A 150 ? 0.5902 0.4320 0.5103 0.0216 -0.1835 0.1834 150 LEU A CA 1086 C C . LEU A 150 ? 0.5870 0.4077 0.5418 0.0267 -0.1882 0.1882 150 LEU A C 1087 O O . LEU A 150 ? 0.5928 0.4102 0.5582 0.0225 -0.1924 0.2020 150 LEU A O 1088 C CB . LEU A 150 ? 0.5741 0.4135 0.4778 0.0255 -0.1673 0.1615 150 LEU A CB 1089 C CG . LEU A 150 ? 0.5718 0.4064 0.4699 0.0237 -0.1591 0.1612 150 LEU A CG 1090 C CD1 . LEU A 150 ? 0.5880 0.4408 0.4712 0.0131 -0.1621 0.1797 150 LEU A CD1 1091 C CD2 . LEU A 150 ? 0.5589 0.3927 0.4434 0.0278 -0.1450 0.1401 150 LEU A CD2 1092 N N . ASN A 151 ? 0.5780 0.3863 0.5537 0.0361 -0.1878 0.1761 151 ASN A N 1093 C CA . ASN A 151 ? 0.5778 0.3687 0.5891 0.0432 -0.1927 0.1750 151 ASN A CA 1094 C C . ASN A 151 ? 0.5938 0.3833 0.6353 0.0383 -0.2110 0.1979 151 ASN A C 1095 O O . ASN A 151 ? 0.5979 0.3742 0.6722 0.0415 -0.2174 0.1999 151 ASN A O 1096 C CB . ASN A 151 ? 0.5648 0.3486 0.5894 0.0554 -0.1852 0.1555 151 ASN A CB 1097 C CG . ASN A 151 ? 0.5525 0.3339 0.5603 0.0623 -0.1687 0.1358 151 ASN A CG 1098 O OD1 . ASN A 151 ? 0.5526 0.3291 0.5537 0.0615 -0.1658 0.1328 151 ASN A OD1 1099 N ND2 . ASN A 151 ? 0.5396 0.3254 0.5436 0.0688 -0.1587 0.1241 151 ASN A ND2 1100 N N . ALA A 152 ? 0.6061 0.4103 0.6388 0.0308 -0.2206 0.2148 152 ALA A N 1101 C CA . ALA A 152 ? 0.6261 0.4337 0.6846 0.0241 -0.2392 0.2429 152 ALA A CA 1102 C C . ALA A 152 ? 0.6404 0.4527 0.7016 0.0150 -0.2434 0.2651 152 ALA A C 1103 O O . ALA A 152 ? 0.6504 0.4611 0.7463 0.0105 -0.2588 0.2896 152 ALA A O 1104 C CB . ALA A 152 ? 0.6374 0.4644 0.6791 0.0182 -0.2487 0.2554 152 ALA A CB 1105 N N . ASP A 153 ? 0.6402 0.4591 0.6699 0.0122 -0.2301 0.2583 153 ASP A N 1106 C CA . ASP A 153 ? 0.6542 0.4802 0.6865 0.0036 -0.2315 0.2794 153 ASP A CA 1107 C C . ASP A 153 ? 0.6460 0.4484 0.7132 0.0092 -0.2310 0.2697 153 ASP A C 1108 O O . ASP A 153 ? 0.6280 0.4229 0.6795 0.0143 -0.2178 0.2469 153 ASP A O 1109 C CB . ASP A 153 ? 0.6583 0.5048 0.6421 -0.0016 -0.2173 0.2749 153 ASP A CB 1110 C CG . ASP A 153 ? 0.6716 0.5276 0.6574 -0.0100 -0.2153 0.2951 153 ASP A CG 1111 O OD1 . ASP A 153 ? 0.6895 0.5451 0.7097 -0.0155 -0.2278 0.3232 153 ASP A OD1 1112 O OD2 . ASP A 153 ? 0.6726 0.5366 0.6299 -0.0111 -0.2010 0.2833 153 ASP A OD2 1113 N N . GLN A 154 ? 0.6549 0.4469 0.7723 0.0084 -0.2470 0.2867 154 GLN A N 1114 C CA . GLN A 154 ? 0.6537 0.4235 0.8124 0.0148 -0.2503 0.2744 154 GLN A CA 1115 C C . GLN A 154 ? 0.6509 0.4235 0.8085 0.0083 -0.2463 0.2836 154 GLN A C 1116 O O . GLN A 154 ? 0.6377 0.3946 0.8077 0.0152 -0.2425 0.2617 154 GLN A O 1117 C CB . GLN A 154 ? 0.6686 0.4257 0.8905 0.0167 -0.2703 0.2869 154 GLN A CB 1118 C CG . GLN A 154 ? 0.6710 0.4214 0.9035 0.0262 -0.2732 0.2708 154 GLN A CG 1119 C CD . GLN A 154 ? 0.6616 0.4022 0.8747 0.0402 -0.2575 0.2299 154 GLN A CD 1120 O OE1 . GLN A 154 ? 0.6589 0.3881 0.8814 0.0472 -0.2531 0.2092 154 GLN A OE1 1121 N NE2 . GLN A 154 ? 0.6607 0.4080 0.8470 0.0442 -0.2494 0.2194 154 GLN A NE2 1122 N N . GLY A 155 ? 0.6611 0.4561 0.8042 -0.0045 -0.2471 0.3159 155 GLY A N 1123 C CA . GLY A 155 ? 0.6611 0.4644 0.7988 -0.0117 -0.2404 0.3273 155 GLY A CA 1124 C C . GLY A 155 ? 0.6384 0.4367 0.7399 -0.0059 -0.2225 0.2950 155 GLY A C 1125 O O . GLY A 155 ? 0.6312 0.4138 0.7541 -0.0021 -0.2220 0.2821 155 GLY A O 1126 N N . THR A 156 ? 0.6293 0.4413 0.6798 -0.0050 -0.2094 0.2816 156 THR A N 1127 C CA . THR A 156 ? 0.6101 0.4178 0.6285 0.0007 -0.1931 0.2513 156 THR A CA 1128 C C . THR A 156 ? 0.5862 0.3683 0.6216 0.0138 -0.1930 0.2213 156 THR A C 1129 O O . THR A 156 ? 0.5705 0.3447 0.6018 0.0175 -0.1859 0.2047 156 THR A O 1130 C CB . THR A 156 ? 0.6114 0.4366 0.5829 0.0006 -0.1822 0.2404 156 THR A CB 1131 O OG1 . THR A 156 ? 0.6356 0.4897 0.5864 -0.0100 -0.1820 0.2645 156 THR A OG1 1132 C CG2 . THR A 156 ? 0.5982 0.4201 0.5439 0.0056 -0.1666 0.2133 156 THR A CG2 1133 N N . SER A 157 ? 0.5794 0.3515 0.6340 0.0210 -0.2009 0.2147 157 SER A N 1134 C CA . SER A 157 ? 0.5672 0.3205 0.6382 0.0347 -0.2003 0.1861 157 SER A CA 1135 C C . SER A 157 ? 0.5646 0.3033 0.6717 0.0374 -0.2083 0.1810 157 SER A C 1136 O O . SER A 157 ? 0.5548 0.2860 0.6541 0.0452 -0.2019 0.1572 157 SER A O 1137 C CB . SER A 157 ? 0.5727 0.3201 0.6684 0.0414 -0.2091 0.1833 157 SER A CB 1138 O OG . SER A 157 ? 0.5680 0.3035 0.6737 0.0557 -0.2053 0.1536 157 SER A OG 1139 N N . ALA A 158 ? 0.5708 0.3065 0.7204 0.0309 -0.2237 0.2045 158 ALA A N 1140 C CA . ALA A 158 ? 0.5725 0.2941 0.7674 0.0324 -0.2348 0.2022 158 ALA A CA 1141 C C . ALA A 158 ? 0.5664 0.2925 0.7425 0.0268 -0.2261 0.2034 158 ALA A C 1142 O O . ALA A 158 ? 0.5620 0.2755 0.7539 0.0334 -0.2284 0.1830 158 ALA A O 1143 C CB . ALA A 158 ? 0.5874 0.3074 0.8376 0.0246 -0.2538 0.2335 158 ALA A CB 1144 N N . THR A 159 ? 0.5643 0.3099 0.7071 0.0153 -0.2164 0.2256 159 THR A N 1145 C CA . THR A 159 ? 0.5611 0.3142 0.6858 0.0095 -0.2062 0.2276 159 THR A CA 1146 C C . THR A 159 ? 0.5441 0.2904 0.6355 0.0193 -0.1936 0.1927 159 THR A C 1147 O O . THR A 159 ? 0.5406 0.2792 0.6412 0.0211 -0.1933 0.1819 159 THR A O 1148 C CB . THR A 159 ? 0.5690 0.3499 0.6621 -0.0032 -0.1969 0.2555 159 THR A CB 1149 O OG1 . THR A 159 ? 0.5867 0.3767 0.7150 -0.0129 -0.2093 0.2927 159 THR A OG1 1150 C CG2 . THR A 159 ? 0.5667 0.3576 0.6382 -0.0078 -0.1835 0.2531 159 THR A CG2 1151 N N . VAL A 160 ? 0.5327 0.2824 0.5904 0.0254 -0.1848 0.1770 160 VAL A N 1152 C CA . VAL A 160 ? 0.5207 0.2666 0.5501 0.0347 -0.1733 0.1482 160 VAL A CA 1153 C C . VAL A 160 ? 0.5219 0.2505 0.5761 0.0474 -0.1812 0.1243 160 VAL A C 1154 O O . VAL A 160 ? 0.5144 0.2390 0.5611 0.0521 -0.1777 0.1076 160 VAL A O 1155 C CB . VAL A 160 ? 0.5128 0.2678 0.5082 0.0380 -0.1628 0.1404 160 VAL A CB 1156 C CG1 . VAL A 160 ? 0.5017 0.2535 0.4767 0.0483 -0.1527 0.1146 160 VAL A CG1 1157 C CG2 . VAL A 160 ? 0.5135 0.2879 0.4809 0.0271 -0.1548 0.1560 160 VAL A CG2 1158 N N . GLN A 161 ? 0.5307 0.2509 0.6163 0.0533 -0.1928 0.1218 161 GLN A N 1159 C CA . GLN A 161 ? 0.5384 0.2455 0.6522 0.0665 -0.2019 0.0960 161 GLN A CA 1160 C C . GLN A 161 ? 0.5477 0.2455 0.6900 0.0646 -0.2118 0.0937 161 GLN A C 1161 O O . GLN A 161 ? 0.5461 0.2389 0.6860 0.0747 -0.2127 0.0675 161 GLN A O 1162 C CB . GLN A 161 ? 0.5482 0.2484 0.7019 0.0717 -0.2148 0.0958 161 GLN A CB 1163 C CG . GLN A 161 ? 0.5431 0.2505 0.6757 0.0779 -0.2062 0.0897 161 GLN A CG 1164 C CD . GLN A 161 ? 0.5538 0.2546 0.7319 0.0821 -0.2199 0.0915 161 GLN A CD 1165 O OE1 . GLN A 161 ? 0.5637 0.2544 0.7813 0.0917 -0.2314 0.0727 161 GLN A OE1 1166 N NE2 . GLN A 161 ? 0.5533 0.2600 0.7294 0.0753 -0.2205 0.1127 161 GLN A NE2 1167 N N . MET A 162 ? 0.5580 0.2558 0.7277 0.0518 -0.2195 0.1223 162 MET A N 1168 C CA . MET A 162 ? 0.5700 0.2600 0.7742 0.0481 -0.2294 0.1251 162 MET A CA 1169 C C . MET A 162 ? 0.5622 0.2574 0.7297 0.0468 -0.2166 0.1161 162 MET A C 1170 O O . MET A 162 ? 0.5650 0.2512 0.7460 0.0533 -0.2229 0.0958 162 MET A O 1171 C CB . MET A 162 ? 0.5831 0.2775 0.8241 0.0332 -0.2377 0.1647 162 MET A CB 1172 C CG . MET A 162 ? 0.5984 0.2849 0.8921 0.0341 -0.2554 0.1757 162 MET A CG 1173 S SD . MET A 162 ? 0.6210 0.3193 0.9540 0.0160 -0.2646 0.2307 162 MET A SD 1174 C CE . MET A 162 ? 0.6268 0.3212 0.9810 0.0207 -0.2755 0.2339 162 MET A CE 1175 N N . LEU A 163 ? 0.5543 0.2647 0.6776 0.0390 -0.2000 0.1293 163 LEU A N 1176 C CA . LEU A 163 ? 0.5471 0.2636 0.6388 0.0372 -0.1875 0.1220 163 LEU A CA 1177 C C . LEU A 163 ? 0.5402 0.2508 0.6116 0.0509 -0.1849 0.0893 163 LEU A C 1178 O O . LEU A 163 ? 0.5395 0.2460 0.6137 0.0531 -0.1867 0.0776 163 LEU A O 1179 C CB . LEU A 163 ? 0.5422 0.2777 0.5938 0.0281 -0.1710 0.1376 163 LEU A CB 1180 C CG . LEU A 163 ? 0.5516 0.3004 0.6176 0.0139 -0.1715 0.1711 163 LEU A CG 1181 C CD1 . LEU A 163 ? 0.5507 0.3211 0.5773 0.0074 -0.1582 0.1829 163 LEU A CD1 1182 C CD2 . LEU A 163 ? 0.5537 0.3040 0.6375 0.0075 -0.1707 0.1787 163 LEU A CD2 1183 N N . LEU A 164 ? 0.5385 0.2505 0.5925 0.0602 -0.1814 0.0760 164 LEU A N 1184 C CA . LEU A 164 ? 0.5380 0.2506 0.5700 0.0738 -0.1772 0.0485 164 LEU A CA 1185 C C . LEU A 164 ? 0.5543 0.2565 0.6158 0.0860 -0.1925 0.0244 164 LEU A C 1186 O O . LEU A 164 ? 0.5579 0.2601 0.6107 0.0926 -0.1941 0.0063 164 LEU A O 1187 C CB . LEU A 164 ? 0.5313 0.2528 0.5370 0.0794 -0.1666 0.0451 164 LEU A CB 1188 C CG . LEU A 164 ? 0.5193 0.2523 0.4958 0.0694 -0.1526 0.0623 164 LEU A CG 1189 C CD1 . LEU A 164 ? 0.5157 0.2557 0.4778 0.0751 -0.1456 0.0597 164 LEU A CD1 1190 C CD2 . LEU A 164 ? 0.5121 0.2511 0.4642 0.0670 -0.1426 0.0587 164 LEU A CD2 1191 N N . ASN A 165 ? 0.5653 0.2598 0.6638 0.0895 -0.2050 0.0229 165 ASN A N 1192 C CA . ASN A 165 ? 0.5838 0.2702 0.7143 0.1032 -0.2206 -0.0055 165 ASN A CA 1193 C C . ASN A 165 ? 0.5902 0.2653 0.7576 0.1008 -0.2363 -0.0099 165 ASN A C 1194 O O . ASN A 165 ? 0.6025 0.2760 0.7744 0.1133 -0.2452 -0.0407 165 ASN A O 1195 C CB . ASN A 165 ? 0.5960 0.2768 0.7646 0.1079 -0.2309 -0.0075 165 ASN A CB 1196 C CG . ASN A 165 ? 0.5964 0.2883 0.7358 0.1137 -0.2176 -0.0096 165 ASN A CG 1197 O OD1 . ASN A 165 ? 0.5852 0.2883 0.6788 0.1106 -0.2005 -0.0013 165 ASN A OD1 1198 N ND2 . ASN A 165 ? 0.6140 0.3028 0.7860 0.1225 -0.2263 -0.0210 165 ASN A ND2 1199 N N . ASP A 166 ? 0.5855 0.2555 0.7794 0.0853 -0.2400 0.0202 166 ASP A N 1200 C CA . ASP A 166 ? 0.5922 0.2512 0.8346 0.0808 -0.2562 0.0231 166 ASP A CA 1201 C C . ASP A 166 ? 0.5834 0.2472 0.8065 0.0703 -0.2471 0.0376 166 ASP A C 1202 O O . ASP A 166 ? 0.5869 0.2464 0.8145 0.0751 -0.2535 0.0193 166 ASP A O 1203 C CB . ASP A 166 ? 0.5984 0.2504 0.8978 0.0708 -0.2688 0.0510 166 ASP A CB 1204 C CG . ASP A 166 ? 0.6094 0.2536 0.9460 0.0813 -0.2827 0.0353 166 ASP A CG 1205 O OD1 . ASP A 166 ? 0.6124 0.2589 0.9263 0.0968 -0.2804 0.0018 166 ASP A OD1 1206 O OD2 . ASP A 166 ? 0.6172 0.2549 1.0088 0.0741 -0.2960 0.0577 166 ASP A OD2 1207 N N . THR A 167 ? 0.5726 0.2468 0.7756 0.0564 -0.2329 0.0692 167 THR A N 1208 C CA . THR A 167 ? 0.5674 0.2484 0.7637 0.0447 -0.2245 0.0874 167 THR A CA 1209 C C . THR A 167 ? 0.5599 0.2451 0.7144 0.0499 -0.2142 0.0673 167 THR A C 1210 O O . THR A 167 ? 0.5578 0.2400 0.7266 0.0474 -0.2180 0.0652 167 THR A O 1211 C CB . THR A 167 ? 0.5623 0.2595 0.7394 0.0307 -0.2099 0.1216 167 THR A CB 1212 O OG1 . THR A 167 ? 0.5696 0.2653 0.7802 0.0268 -0.2197 0.1413 167 THR A OG1 1213 C CG2 . THR A 167 ? 0.5609 0.2680 0.7451 0.0182 -0.2029 0.1430 167 THR A CG2 1214 N N . CYS A 168 ? 0.5531 0.2454 0.6612 0.0571 -0.2023 0.0544 168 CYS A N 1215 C CA . CYS A 168 ? 0.5493 0.2474 0.6203 0.0619 -0.1929 0.0391 168 CYS A CA 1216 C C . CYS A 168 ? 0.5566 0.2463 0.6432 0.0722 -0.2076 0.0135 168 CYS A C 1217 O O . CYS A 168 ? 0.5563 0.2449 0.6493 0.0679 -0.2090 0.0148 168 CYS A O 1218 C CB . CYS A 168 ? 0.5458 0.2540 0.5727 0.0684 -0.1793 0.0319 168 CYS A CB 1219 S SG . CYS A 168 ? 0.5425 0.2615 0.5289 0.0698 -0.1654 0.0252 168 CYS A SG 1220 N N . PRO A 169 ? 0.5662 0.2516 0.6606 0.0863 -0.2192 -0.0109 169 PRO A N 1221 C CA . PRO A 169 ? 0.5794 0.2605 0.6855 0.0973 -0.2344 -0.0385 169 PRO A CA 1222 C C . PRO A 169 ? 0.5847 0.2526 0.7433 0.0909 -0.2513 -0.0346 169 PRO A C 1223 O O . PRO A 169 ? 0.5898 0.2567 0.7500 0.0928 -0.2580 -0.0457 169 PRO A O 1224 C CB . PRO A 169 ? 0.5938 0.2758 0.7044 0.1134 -0.2435 -0.0653 169 PRO A CB 1225 C CG . PRO A 169 ? 0.5893 0.2684 0.7142 0.1080 -0.2393 -0.0478 169 PRO A CG 1226 C CD . PRO A 169 ? 0.5709 0.2573 0.6651 0.0939 -0.2196 -0.0173 169 PRO A CD 1227 N N . LEU A 170 ? 0.5844 0.2438 0.7880 0.0827 -0.2585 -0.0164 170 LEU A N 1228 C CA . LEU A 170 ? 0.5896 0.2384 0.8508 0.0741 -0.2729 -0.0043 170 LEU A CA 1229 C C . LEU A 170 ? 0.5771 0.2319 0.8266 0.0621 -0.2614 0.0150 170 LEU A C 1230 O O . LEU A 170 ? 0.5817 0.2304 0.8570 0.0624 -0.2729 0.0064 170 LEU A O 1231 C CB . LEU A 170 ? 0.5931 0.2370 0.8999 0.0650 -0.2782 0.0220 170 LEU A CB 1232 C CG . LEU A 170 ? 0.5989 0.2357 0.9714 0.0532 -0.2906 0.0460 170 LEU A CG 1233 C CD1 . LEU A 170 ? 0.6154 0.2373 1.0387 0.0628 -0.3160 0.0171 170 LEU A CD1 1234 C CD2 . LEU A 170 ? 0.6039 0.2401 1.0146 0.0452 -0.2945 0.0749 170 LEU A CD2 1235 N N . PHE A 171 ? 0.5604 0.2280 0.7728 0.0522 -0.2394 0.0387 171 PHE A N 1236 C CA . PHE A 171 ? 0.5492 0.2261 0.7489 0.0414 -0.2258 0.0554 171 PHE A CA 1237 C C . PHE A 171 ? 0.5465 0.2237 0.7213 0.0489 -0.2259 0.0325 171 PHE A C 1238 O O . PHE A 171 ? 0.5419 0.2175 0.7369 0.0440 -0.2292 0.0355 171 PHE A O 1239 C CB . PHE A 171 ? 0.5371 0.2303 0.6982 0.0323 -0.2030 0.0775 171 PHE A CB 1240 C CG . PHE A 171 ? 0.5289 0.2347 0.6812 0.0217 -0.1883 0.0926 171 PHE A CG 1241 C CD1 . PHE A 171 ? 0.5319 0.2400 0.7261 0.0113 -0.1910 0.1133 171 PHE A CD1 1242 C CD2 . PHE A 171 ? 0.5183 0.2349 0.6254 0.0224 -0.1719 0.0863 171 PHE A CD2 1243 C CE1 . PHE A 171 ? 0.5259 0.2485 0.7143 0.0023 -0.1762 0.1258 171 PHE A CE1 1244 C CE2 . PHE A 171 ? 0.5120 0.2410 0.6158 0.0135 -0.1587 0.0970 171 PHE A CE2 1245 C CZ . PHE A 171 ? 0.5153 0.2480 0.6580 0.0038 -0.1601 0.1158 171 PHE A CZ 1246 N N . VAL A 172 ? 0.5474 0.2279 0.6813 0.0607 -0.2230 0.0117 172 VAL A N 1247 C CA . VAL A 172 ? 0.5489 0.2338 0.6546 0.0682 -0.2227 -0.0065 172 VAL A CA 1248 C C . VAL A 172 ? 0.5637 0.2387 0.7011 0.0760 -0.2456 -0.0283 172 VAL A C 1249 O O . VAL A 172 ? 0.5636 0.2402 0.6983 0.0754 -0.2479 -0.0324 172 VAL A O 1250 C CB . VAL A 172 ? 0.5497 0.2447 0.6074 0.0793 -0.2141 -0.0199 172 VAL A CB 1251 C CG1 . VAL A 172 ? 0.5566 0.2587 0.5893 0.0880 -0.2168 -0.0365 172 VAL A CG1 1252 C CG2 . VAL A 172 ? 0.5331 0.2382 0.5621 0.0710 -0.1923 0.0005 172 VAL A CG2 1253 N N . ARG A 173 ? 0.5780 0.2430 0.7493 0.0832 -0.2638 -0.0430 173 ARG A N 1254 C CA . ARG A 173 ? 0.5947 0.2500 0.8046 0.0907 -0.2887 -0.0663 173 ARG A CA 1255 C C . ARG A 173 ? 0.5889 0.2373 0.8408 0.0777 -0.2929 -0.0479 173 ARG A C 1256 O O . ARG A 173 ? 0.5952 0.2424 0.8522 0.0807 -0.3031 -0.0610 173 ARG A O 1257 C CB . ARG A 173 ? 0.6119 0.2574 0.8621 0.1000 -0.3083 -0.0852 173 ARG A CB 1258 C CG . ARG A 173 ? 0.6234 0.2786 0.8353 0.1172 -0.3081 -0.1138 173 ARG A CG 1259 C CD . ARG A 173 ? 0.6438 0.2904 0.9008 0.1288 -0.3301 -0.1404 173 ARG A CD 1260 N NE . ARG A 173 ? 0.6382 0.2732 0.9424 0.1192 -0.3317 -0.1181 173 ARG A NE 1261 C CZ . ARG A 173 ? 0.6346 0.2725 0.9293 0.1200 -0.3222 -0.1107 173 ARG A CZ 1262 N NH1 . ARG A 173 ? 0.6328 0.2851 0.8718 0.1297 -0.3077 -0.1225 173 ARG A NH1 1263 N NH2 . ARG A 173 ? 0.6305 0.2578 0.9754 0.1104 -0.3274 -0.0879 173 ARG A NH2 1264 N N . GLY A 174 ? 0.5775 0.2243 0.8573 0.0634 -0.2842 -0.0163 174 GLY A N 1265 C CA . GLY A 174 ? 0.5712 0.2171 0.8892 0.0498 -0.2830 0.0067 174 GLY A CA 1266 C C . GLY A 174 ? 0.5584 0.2147 0.8422 0.0450 -0.2671 0.0123 174 GLY A C 1267 O O . GLY A 174 ? 0.5559 0.2093 0.8687 0.0413 -0.2743 0.0129 174 GLY A O 1268 N N . LEU A 175 ? 0.5475 0.2161 0.7753 0.0450 -0.2465 0.0162 175 LEU A N 1269 C CA . LEU A 175 ? 0.5383 0.2169 0.7364 0.0415 -0.2322 0.0191 175 LEU A CA 1270 C C . LEU A 175 ? 0.5497 0.2244 0.7429 0.0518 -0.2475 -0.0056 175 LEU A C 1271 O O . LEU A 175 ? 0.5444 0.2206 0.7492 0.0469 -0.2470 -0.0019 175 LEU A O 1272 C CB . LEU A 175 ? 0.5252 0.2166 0.6696 0.0417 -0.2110 0.0239 175 LEU A CB 1273 C CG . LEU A 175 ? 0.5135 0.2157 0.6521 0.0299 -0.1915 0.0495 175 LEU A CG 1274 C CD1 . LEU A 175 ? 0.5036 0.2164 0.5919 0.0330 -0.1753 0.0468 175 LEU A CD1 1275 C CD2 . LEU A 175 ? 0.5065 0.2172 0.6682 0.0175 -0.1817 0.0678 175 LEU A CD2 1276 N N . LEU A 176 ? 0.5685 0.2402 0.7453 0.0662 -0.2612 -0.0308 176 LEU A N 1277 C CA . LEU A 176 ? 0.5885 0.2612 0.7544 0.0778 -0.2772 -0.0557 176 LEU A CA 1278 C C . LEU A 176 ? 0.6027 0.2636 0.8227 0.0768 -0.3000 -0.0641 176 LEU A C 1279 O O . LEU A 176 ? 0.6085 0.2715 0.8281 0.0782 -0.3074 -0.0709 176 LEU A O 1280 C CB . LEU A 176 ? 0.6068 0.2846 0.7428 0.0945 -0.2857 -0.0817 176 LEU A CB 1281 C CG . LEU A 176 ? 0.6000 0.2919 0.6818 0.0974 -0.2646 -0.0753 176 LEU A CG 1282 C CD1 . LEU A 176 ? 0.6183 0.3146 0.6844 0.1122 -0.2713 -0.0973 176 LEU A CD1 1283 C CD2 . LEU A 176 ? 0.5977 0.3034 0.6420 0.0990 -0.2562 -0.0725 176 LEU A CD2 1284 N N . GLU A 177 ? 0.6089 0.2577 0.8801 0.0739 -0.3120 -0.0621 177 GLU A N 1285 C CA . GLU A 177 ? 0.6203 0.2569 0.9549 0.0710 -0.3336 -0.0658 177 GLU A CA 1286 C C . GLU A 177 ? 0.6051 0.2448 0.9585 0.0559 -0.3204 -0.0385 177 GLU A C 1287 O O . GLU A 177 ? 0.6108 0.2486 0.9806 0.0564 -0.3316 -0.0464 177 GLU A O 1288 C CB . GLU A 177 ? 0.6298 0.2537 1.0235 0.0691 -0.3475 -0.0628 177 GLU A CB 1289 C CG . GLU A 177 ? 0.6436 0.2540 1.1126 0.0675 -0.3737 -0.0690 177 GLU A CG 1290 C CD . GLU A 177 ? 0.6500 0.2492 1.1884 0.0619 -0.3848 -0.0557 177 GLU A CD 1291 O OE1 . GLU A 177 ? 0.6570 0.2530 1.1932 0.0695 -0.3900 -0.0675 177 GLU A OE1 1292 O OE2 . GLU A 177 ? 0.6475 0.2419 1.2477 0.0499 -0.3890 -0.0324 177 GLU A OE2 1293 N N . ALA A 178 ? 0.5875 0.2343 0.9381 0.0431 -0.2970 -0.0078 178 ALA A N 1294 C CA . ALA A 178 ? 0.5757 0.2294 0.9509 0.0286 -0.2827 0.0190 178 ALA A CA 1295 C C . ALA A 178 ? 0.5673 0.2311 0.9058 0.0279 -0.2696 0.0168 178 ALA A C 1296 O O . ALA A 178 ? 0.5620 0.2289 0.9294 0.0198 -0.2663 0.0278 178 ALA A O 1297 C CB . ALA A 178 ? 0.5654 0.2294 0.9419 0.0167 -0.2614 0.0504 178 ALA A CB 1298 N N . GLY A 179 ? 0.5679 0.2375 0.8486 0.0364 -0.2631 0.0035 179 GLY A N 1299 C CA . GLY A 179 ? 0.5648 0.2444 0.8125 0.0365 -0.2517 0.0025 179 GLY A CA 1300 C C . GLY A 179 ? 0.5831 0.2606 0.8159 0.0482 -0.2704 -0.0206 179 GLY A C 1301 O O . GLY A 179 ? 0.5766 0.2636 0.7780 0.0497 -0.2620 -0.0203 179 GLY A O 1302 N N . LYS A 180 ? 0.6077 0.2746 0.8660 0.0565 -0.2967 -0.0402 180 LYS A N 1303 C CA . LYS A 180 ? 0.6319 0.3005 0.8717 0.0701 -0.3176 -0.0657 180 LYS A CA 1304 C C . LYS A 180 ? 0.6304 0.3055 0.8672 0.0670 -0.3169 -0.0606 180 LYS A C 1305 O O . LYS A 180 ? 0.6352 0.3220 0.8295 0.0744 -0.3161 -0.0666 180 LYS A O 1306 C CB . LYS A 180 ? 0.6550 0.3109 0.9392 0.0773 -0.3480 -0.0880 180 LYS A CB 1307 C CG . LYS A 180 ? 0.6840 0.3456 0.9443 0.0942 -0.3719 -0.1201 180 LYS A CG 1308 C CD . LYS A 180 ? 0.7080 0.3566 1.0234 0.1000 -0.4043 -0.1437 180 LYS A CD 1309 C CE . LYS A 180 ? 0.7394 0.3981 1.0285 0.1178 -0.4295 -0.1786 180 LYS A CE 1310 N NZ . LYS A 180 ? 0.7555 0.4269 0.9962 0.1324 -0.4276 -0.1988 180 LYS A NZ 1311 N N . SER A 181 ? 0.8140 0.2201 0.6255 -0.0629 -0.0566 0.0853 181 SER A N 1312 C CA . SER A 181 ? 0.7657 0.2285 0.5959 -0.0905 -0.0626 0.0770 181 SER A CA 1313 C C . SER A 181 ? 0.6853 0.2245 0.5525 -0.0740 -0.0573 0.0734 181 SER A C 1314 O O . SER A 181 ? 0.6538 0.2188 0.5282 -0.0766 -0.0567 0.0583 181 SER A O 1315 C CB . SER A 181 ? 0.7660 0.2492 0.6031 -0.1246 -0.0713 0.0934 181 SER A CB 1316 O OG . SER A 181 ? 0.8426 0.2640 0.6462 -0.1525 -0.0792 0.0939 181 SER A OG 1317 N N . ASP A 182 ? 0.6556 0.2294 0.5439 -0.0593 -0.0543 0.0883 182 ASP A N 1318 C CA . ASP A 182 ? 0.5890 0.2301 0.5083 -0.0467 -0.0501 0.0861 182 ASP A CA 1319 C C . ASP A 182 ? 0.5759 0.2165 0.4983 -0.0165 -0.0426 0.0762 182 ASP A C 1320 O O . ASP A 182 ? 0.5284 0.2080 0.4666 -0.0134 -0.0401 0.0651 182 ASP A O 1321 C CB . ASP A 182 ? 0.5755 0.2519 0.5109 -0.0438 -0.0505 0.1051 182 ASP A CB 1322 C CG . ASP A 182 ? 0.5714 0.2706 0.5105 -0.0728 -0.0554 0.1141 182 ASP A CG 1323 O OD1 . ASP A 182 ? 0.5737 0.2768 0.5113 -0.0947 -0.0581 0.1061 182 ASP A OD1 1324 O OD2 . ASP A 182 ? 0.5738 0.2918 0.5180 -0.0737 -0.0563 0.1308 182 ASP A OD2 1325 N N . LEU A 183 ? 0.6138 0.2111 0.5213 0.0067 -0.0382 0.0819 183 LEU A N 1326 C CA . LEU A 183 ? 0.6085 0.2082 0.5194 0.0383 -0.0291 0.0753 183 LEU A CA 1327 C C . LEU A 183 ? 0.6119 0.1958 0.5088 0.0360 -0.0262 0.0529 183 LEU A C 1328 O O . LEU A 183 ? 0.5779 0.1947 0.4887 0.0515 -0.0205 0.0457 183 LEU A O 1329 C CB . LEU A 183 ? 0.6668 0.2179 0.5619 0.0667 -0.0229 0.0867 183 LEU A CB 1330 C CG . LEU A 183 ? 0.6613 0.2374 0.5739 0.0764 -0.0251 0.1126 183 LEU A CG 1331 C CD1 . LEU A 183 ? 0.7330 0.2456 0.6238 0.1006 -0.0198 0.1255 183 LEU A CD1 1332 C CD2 . LEU A 183 ? 0.6073 0.2553 0.5531 0.0928 -0.0226 0.1192 183 LEU A CD2 1333 N N . GLU A 184 ? 0.6528 0.1880 0.5211 0.0144 -0.0311 0.0431 184 GLU A N 1334 C CA . GLU A 184 ? 0.6676 0.1847 0.5167 0.0084 -0.0302 0.0222 184 GLU A CA 1335 C C . GLU A 184 ? 0.6218 0.1825 0.4850 -0.0219 -0.0388 0.0160 184 GLU A C 1336 O O . GLU A 184 ? 0.6344 0.1799 0.4793 -0.0347 -0.0417 0.0015 184 GLU A O 1337 C CB . GLU A 184 ? 0.7561 0.1873 0.5584 0.0032 -0.0305 0.0138 184 GLU A CB 1338 C CG . GLU A 184 ? 0.8143 0.1953 0.5990 0.0392 -0.0190 0.0186 184 GLU A CG 1339 C CD . GLU A 184 ? 0.9152 0.1990 0.6468 0.0336 -0.0183 0.0086 184 GLU A CD 1340 O OE1 . GLU A 184 ? 0.9443 0.2027 0.6509 -0.0001 -0.0276 -0.0045 184 GLU A OE1 1341 O OE2 . GLU A 184 ? 0.9786 0.2096 0.6917 0.0624 -0.0086 0.0147 184 GLU A OE2 1342 N N . LYS A 185 ? 0.5694 0.1853 0.4638 -0.0318 -0.0423 0.0272 185 LYS A N 1343 C CA . LYS A 185 ? 0.5321 0.1907 0.4420 -0.0559 -0.0481 0.0239 185 LYS A CA 1344 C C . LYS A 185 ? 0.5017 0.1876 0.4200 -0.0460 -0.0444 0.0110 185 LYS A C 1345 O O . LYS A 185 ? 0.4886 0.1811 0.4124 -0.0208 -0.0366 0.0083 185 LYS A O 1346 C CB . LYS A 185 ? 0.4874 0.1971 0.4260 -0.0628 -0.0489 0.0373 185 LYS A CB 1347 C CG . LYS A 185 ? 0.4406 0.1942 0.4037 -0.0423 -0.0423 0.0384 185 LYS A CG 1348 C CD . LYS A 185 ? 0.4108 0.2058 0.3932 -0.0510 -0.0426 0.0492 185 LYS A CD 1349 C CE . LYS A 185 ? 0.3713 0.2058 0.3728 -0.0359 -0.0375 0.0476 185 LYS A CE 1350 N NZ . LYS A 185 ? 0.3504 0.2213 0.3644 -0.0449 -0.0366 0.0545 185 LYS A NZ 1351 N N . GLN A 186 ? 0.4918 0.1969 0.4123 -0.0664 -0.0502 0.0056 186 GLN A N 1352 C CA . GLN A 186 ? 0.4629 0.2002 0.3944 -0.0598 -0.0479 -0.0030 186 GLN A CA 1353 C C . GLN A 186 ? 0.4207 0.2134 0.3817 -0.0722 -0.0503 0.0039 186 GLN A C 1354 O O . GLN A 186 ? 0.4259 0.2263 0.3879 -0.0951 -0.0572 0.0096 186 GLN A O 1355 C CB . GLN A 186 ? 0.5003 0.2076 0.4029 -0.0706 -0.0525 -0.0157 186 GLN A CB 1356 C CG . GLN A 186 ? 0.5541 0.2017 0.4218 -0.0544 -0.0469 -0.0260 186 GLN A CG 1357 C CD . GLN A 186 ? 0.5349 0.1965 0.4093 -0.0239 -0.0356 -0.0313 186 GLN A CD 1358 O OE1 . GLN A 186 ? 0.4966 0.2016 0.3895 -0.0217 -0.0346 -0.0329 186 GLN A OE1 1359 N NE2 . GLN A 186 ? 0.5667 0.1920 0.4261 0.0000 -0.0266 -0.0323 186 GLN A NE2 1360 N N . GLU A 187 ? 0.3788 0.2089 0.3630 -0.0570 -0.0439 0.0046 187 GLU A N 1361 C CA . GLU A 187 ? 0.3467 0.2238 0.3560 -0.0634 -0.0433 0.0094 187 GLU A CA 1362 C C . GLU A 187 ? 0.3225 0.2192 0.3394 -0.0539 -0.0408 0.0031 187 GLU A C 1363 O O . GLU A 187 ? 0.3133 0.2031 0.3273 -0.0373 -0.0360 -0.0016 187 GLU A O 1364 C CB . GLU A 187 ? 0.3302 0.2284 0.3560 -0.0562 -0.0377 0.0164 187 GLU A CB 1365 C CG . GLU A 187 ? 0.3563 0.2395 0.3753 -0.0647 -0.0399 0.0252 187 GLU A CG 1366 C CD . GLU A 187 ? 0.3718 0.2662 0.3928 -0.0872 -0.0446 0.0324 187 GLU A CD 1367 O OE1 . GLU A 187 ? 0.3684 0.2928 0.4021 -0.0942 -0.0449 0.0324 187 GLU A OE1 1368 O OE2 . GLU A 187 ? 0.4052 0.2807 0.4161 -0.0981 -0.0479 0.0403 187 GLU A OE2 1369 N N . LYS A 188 ? 0.3099 0.2345 0.3378 -0.0640 -0.0439 0.0057 188 LYS A N 1370 C CA . LYS A 188 ? 0.3032 0.2450 0.3364 -0.0569 -0.0429 0.0023 188 LYS A CA 1371 C C . LYS A 188 ? 0.2695 0.2361 0.3234 -0.0420 -0.0347 0.0047 188 LYS A C 1372 O O . LYS A 188 ? 0.2602 0.2453 0.3293 -0.0423 -0.0309 0.0103 188 LYS A O 1373 C CB . LYS A 188 ? 0.3091 0.2741 0.3467 -0.0729 -0.0504 0.0072 188 LYS A CB 1374 C CG . LYS A 188 ? 0.3571 0.2943 0.3679 -0.0924 -0.0606 0.0030 188 LYS A CG 1375 C CD . LYS A 188 ? 0.3633 0.3335 0.3813 -0.1116 -0.0701 0.0108 188 LYS A CD 1376 C CE . LYS A 188 ? 0.4159 0.3548 0.4008 -0.1355 -0.0821 0.0048 188 LYS A CE 1377 N NZ . LYS A 188 ? 0.4219 0.4005 0.4143 -0.1560 -0.0933 0.0142 188 LYS A NZ 1378 N N . PRO A 189 ? 0.2624 0.2282 0.3145 -0.0300 -0.0316 0.0004 189 PRO A N 1379 C CA . PRO A 189 ? 0.2340 0.2203 0.3032 -0.0202 -0.0253 0.0034 189 PRO A CA 1380 C C . PRO A 189 ? 0.2181 0.2306 0.3023 -0.0232 -0.0256 0.0101 189 PRO A C 1381 O O . PRO A 189 ? 0.2223 0.2432 0.3036 -0.0318 -0.0322 0.0125 189 PRO A O 1382 C CB . PRO A 189 ? 0.2352 0.2165 0.2974 -0.0107 -0.0235 -0.0003 189 PRO A CB 1383 C CG . PRO A 189 ? 0.2622 0.2292 0.3050 -0.0162 -0.0290 -0.0053 189 PRO A CG 1384 C CD . PRO A 189 ? 0.2796 0.2269 0.3121 -0.0267 -0.0334 -0.0067 189 PRO A CD 1385 N N . VAL A 190 ? 0.2027 0.2270 0.3011 -0.0164 -0.0184 0.0137 190 VAL A N 1386 C CA . VAL A 190 ? 0.1913 0.2374 0.3049 -0.0111 -0.0150 0.0211 190 VAL A CA 1387 C C . VAL A 190 ? 0.1825 0.2203 0.2968 -0.0004 -0.0092 0.0195 190 VAL A C 1388 O O . VAL A 190 ? 0.1775 0.2011 0.2869 0.0014 -0.0051 0.0145 190 VAL A O 1389 C CB . VAL A 190 ? 0.1904 0.2520 0.3164 -0.0103 -0.0088 0.0264 190 VAL A CB 1390 C CG1 . VAL A 190 ? 0.1892 0.2681 0.3307 0.0022 -0.0014 0.0343 190 VAL A CG1 1391 C CG2 . VAL A 190 ? 0.1994 0.2760 0.3273 -0.0243 -0.0157 0.0316 190 VAL A CG2 1392 N N . ALA A 191 ? 0.1791 0.2271 0.2987 0.0042 -0.0101 0.0254 191 ALA A N 1393 C CA . ALA A 191 ? 0.1762 0.2152 0.2951 0.0115 -0.0058 0.0261 191 ALA A CA 1394 C C . ALA A 191 ? 0.1746 0.2193 0.3055 0.0213 0.0005 0.0350 191 ALA A C 1395 O O . ALA A 191 ? 0.1690 0.2346 0.3120 0.0245 0.0002 0.0435 191 ALA A O 1396 C CB . ALA A 191 ? 0.1806 0.2214 0.2911 0.0099 -0.0111 0.0263 191 ALA A CB 1397 N N . TRP A 192 ? 0.1766 0.2025 0.3040 0.0259 0.0066 0.0341 192 TRP A N 1398 C CA . TRP A 192 ? 0.1910 0.2118 0.3253 0.0373 0.0137 0.0428 192 TRP A CA 1399 C C . TRP A 192 ? 0.2036 0.2021 0.3294 0.0362 0.0156 0.0435 192 TRP A C 1400 O O . TRP A 192 ? 0.2053 0.1930 0.3209 0.0266 0.0135 0.0360 192 TRP A O 1401 C CB . TRP A 192 ? 0.2046 0.2172 0.3415 0.0456 0.0242 0.0408 192 TRP A CB 1402 C CG . TRP A 192 ? 0.2172 0.2009 0.3378 0.0403 0.0298 0.0281 192 TRP A CG 1403 C CD1 . TRP A 192 ? 0.2453 0.1963 0.3535 0.0437 0.0383 0.0244 192 TRP A CD1 1404 C CD2 . TRP A 192 ? 0.2115 0.1960 0.3242 0.0295 0.0266 0.0186 192 TRP A CD2 1405 N NE1 . TRP A 192 ? 0.2524 0.1867 0.3443 0.0336 0.0397 0.0123 192 TRP A NE1 1406 C CE2 . TRP A 192 ? 0.2320 0.1889 0.3282 0.0258 0.0325 0.0098 192 TRP A CE2 1407 C CE3 . TRP A 192 ? 0.1991 0.2019 0.3148 0.0217 0.0190 0.0172 192 TRP A CE3 1408 C CZ2 . TRP A 192 ? 0.2333 0.1875 0.3184 0.0152 0.0304 0.0016 192 TRP A CZ2 1409 C CZ3 . TRP A 192 ? 0.2011 0.1970 0.3066 0.0132 0.0179 0.0096 192 TRP A CZ3 1410 C CH2 . TRP A 192 ? 0.2162 0.1915 0.3079 0.0104 0.0233 0.0027 192 TRP A CH2 1411 N N . LEU A 193 ? 0.2167 0.2109 0.3478 0.0459 0.0193 0.0549 193 LEU A N 1412 C CA . LEU A 193 ? 0.2347 0.2079 0.3581 0.0435 0.0204 0.0596 193 LEU A CA 1413 C C . LEU A 193 ? 0.2709 0.2064 0.3866 0.0506 0.0311 0.0589 193 LEU A C 1414 O O . LEU A 193 ? 0.2788 0.2112 0.4010 0.0662 0.0394 0.0626 193 LEU A O 1415 C CB . LEU A 193 ? 0.2332 0.2256 0.3646 0.0483 0.0158 0.0754 193 LEU A CB 1416 C CG . LEU A 193 ? 0.2115 0.2385 0.3453 0.0423 0.0058 0.0761 193 LEU A CG 1417 C CD1 . LEU A 193 ? 0.2188 0.2620 0.3554 0.0452 0.0017 0.0922 193 LEU A CD1 1418 C CD2 . LEU A 193 ? 0.2019 0.2273 0.3242 0.0303 0.0023 0.0638 193 LEU A CD2 1419 N N . SER A 194 ? 0.2949 0.2014 0.3953 0.0391 0.0315 0.0548 194 SER A N 1420 C CA . SER A 194 ? 0.3469 0.2066 0.4323 0.0421 0.0409 0.0535 194 SER A CA 1421 C C . SER A 194 ? 0.3778 0.2174 0.4522 0.0271 0.0368 0.0593 194 SER A C 1422 O O . SER A 194 ? 0.3505 0.2183 0.4310 0.0160 0.0279 0.0636 194 SER A O 1423 C CB . SER A 194 ? 0.3594 0.1965 0.4284 0.0368 0.0464 0.0366 194 SER A CB 1424 O OG . SER A 194 ? 0.3461 0.1874 0.4058 0.0149 0.0379 0.0285 194 SER A OG 1425 N N . SER A 195 ? 0.4416 0.2316 0.4986 0.0270 0.0440 0.0599 195 SER A N 1426 C CA . SER A 195 ? 0.4819 0.2491 0.5254 0.0069 0.0393 0.0653 195 SER A CA 1427 C C . SER A 195 ? 0.5538 0.2574 0.5672 -0.0030 0.0458 0.0563 195 SER A C 1428 O O . SER A 195 ? 0.5875 0.2536 0.5898 0.0142 0.0578 0.0509 195 SER A O 1429 C CB . SER A 195 ? 0.4881 0.2641 0.5425 0.0132 0.0373 0.0862 195 SER A CB 1430 O OG . SER A 195 ? 0.5346 0.2709 0.5840 0.0317 0.0472 0.0950 195 SER A OG 1431 N N . VAL A 196 ? 0.5870 0.2806 0.5861 -0.0315 0.0380 0.0548 196 VAL A N 1432 C CA . VAL A 196 ? 0.6606 0.2900 0.6258 -0.0499 0.0407 0.0483 196 VAL A CA 1433 C C . VAL A 196 ? 0.7085 0.3095 0.6694 -0.0541 0.0405 0.0664 196 VAL A C 1434 O O . VAL A 196 ? 0.6949 0.3346 0.6723 -0.0651 0.0316 0.0815 196 VAL A O 1435 C CB . VAL A 196 ? 0.6581 0.2998 0.6115 -0.0829 0.0298 0.0399 196 VAL A CB 1436 N N . ASP A 201 ? 1.0943 0.4765 0.9427 -0.2706 -0.0030 0.1923 201 ASP A N 1437 C CA . ASP A 201 ? 1.1210 0.4641 0.9704 -0.2394 0.0070 0.2082 201 ASP A CA 1438 C C . ASP A 201 ? 1.0394 0.4696 0.9333 -0.2074 0.0084 0.2224 201 ASP A C 1439 O O . ASP A 201 ? 1.0100 0.5046 0.9246 -0.2227 0.0009 0.2415 201 ASP A O 1440 C CB . ASP A 201 ? 1.1964 0.4837 1.0222 -0.2698 0.0029 0.2320 201 ASP A CB 1441 N N . GLY A 202 ? 1.0057 0.4396 0.9124 -0.1645 0.0181 0.2127 202 GLY A N 1442 C CA . GLY A 202 ? 0.9382 0.4427 0.8805 -0.1341 0.0192 0.2259 202 GLY A CA 1443 C C . GLY A 202 ? 0.8482 0.4337 0.8171 -0.1249 0.0160 0.2106 202 GLY A C 1444 O O . GLY A 202 ? 0.8125 0.4319 0.8016 -0.0930 0.0199 0.2093 202 GLY A O 1445 N N . HIS A 203 ? 0.8183 0.4347 0.7869 -0.1529 0.0085 0.2003 203 HIS A N 1446 C CA . HIS A 203 ? 0.7409 0.4319 0.7335 -0.1448 0.0055 0.1879 203 HIS A CA 1447 C C . HIS A 203 ? 0.7164 0.3936 0.7073 -0.1239 0.0108 0.1626 203 HIS A C 1448 O O . HIS A 203 ? 0.7603 0.3763 0.7268 -0.1284 0.0147 0.1485 203 HIS A O 1449 C CB . HIS A 203 ? 0.7272 0.4622 0.7237 -0.1781 -0.0034 0.1890 203 HIS A CB 1450 C CG . HIS A 203 ? 0.7263 0.5067 0.7351 -0.1924 -0.0073 0.2146 203 HIS A CG 1451 N ND1 . HIS A 203 ? 0.7829 0.5263 0.7769 -0.2148 -0.0094 0.2351 203 HIS A ND1 1452 C CD2 . HIS A 203 ? 0.6764 0.5346 0.7088 -0.1869 -0.0082 0.2232 203 HIS A CD2 1453 C CE1 . HIS A 203 ? 0.7634 0.5655 0.7734 -0.2235 -0.0118 0.2565 203 HIS A CE1 1454 N NE2 . HIS A 203 ? 0.7015 0.5736 0.7340 -0.2056 -0.0104 0.2489 203 HIS A NE2 1455 N N . ARG A 204 ? 0.6455 0.3800 0.6601 -0.1025 0.0111 0.1571 204 ARG A N 1456 C CA . ARG A 204 ? 0.6190 0.3525 0.6374 -0.0801 0.0161 0.1375 204 ARG A CA 1457 C C . ARG A 204 ? 0.5416 0.3342 0.5750 -0.0841 0.0107 0.1266 204 ARG A C 1458 O O . ARG A 204 ? 0.4962 0.3403 0.5446 -0.0867 0.0066 0.1366 204 ARG A O 1459 C CB . ARG A 204 ? 0.6169 0.3633 0.6508 -0.0482 0.0211 0.1461 204 ARG A CB 1460 C CG . ARG A 204 ? 0.6850 0.3775 0.7081 -0.0378 0.0274 0.1611 204 ARG A CG 1461 C CD . ARG A 204 ? 0.7282 0.3702 0.7396 -0.0182 0.0381 0.1473 204 ARG A CD 1462 N NE . ARG A 204 ? 0.7004 0.3802 0.7345 0.0121 0.0417 0.1473 204 ARG A NE 1463 C CZ . ARG A 204 ? 0.7121 0.3807 0.7462 0.0306 0.0500 0.1328 204 ARG A CZ 1464 N NH1 . ARG A 204 ? 0.7545 0.3731 0.7642 0.0239 0.0565 0.1141 204 ARG A NH1 1465 N NH2 . ARG A 204 ? 0.6809 0.3920 0.7384 0.0545 0.0514 0.1374 204 ARG A NH2 1466 N N . GLN A 205 ? 0.5204 0.3041 0.5479 -0.0832 0.0118 0.1070 205 GLN A N 1467 C CA . GLN A 205 ? 0.4638 0.2993 0.5062 -0.0807 0.0079 0.0974 205 GLN A CA 1468 C C . GLN A 205 ? 0.4218 0.2661 0.4742 -0.0533 0.0128 0.0881 205 GLN A C 1469 O O . GLN A 205 ? 0.4337 0.2457 0.4764 -0.0453 0.0183 0.0762 205 GLN A O 1470 C CB . GLN A 205 ? 0.4829 0.3112 0.5128 -0.1022 0.0036 0.0852 205 GLN A CB 1471 C CG . GLN A 205 ? 0.4454 0.3248 0.4907 -0.0980 -0.0001 0.0779 205 GLN A CG 1472 C CD . GLN A 205 ? 0.4622 0.3500 0.4997 -0.1227 -0.0070 0.0734 205 GLN A CD 1473 O OE1 . GLN A 205 ? 0.4788 0.3546 0.5070 -0.1229 -0.0071 0.0592 205 GLN A OE1 1474 N NE2 . GLN A 205 ? 0.4702 0.3830 0.5117 -0.1445 -0.0133 0.0871 205 GLN A NE2 1475 N N . LEU A 206 ? 0.3695 0.2583 0.4394 -0.0405 0.0110 0.0936 206 LEU A N 1476 C CA . LEU A 206 ? 0.3335 0.2380 0.4136 -0.0196 0.0131 0.0866 206 LEU A CA 1477 C C . LEU A 206 ? 0.2991 0.2251 0.3817 -0.0227 0.0104 0.0721 206 LEU A C 1478 O O . LEU A 206 ? 0.2816 0.2321 0.3662 -0.0339 0.0062 0.0730 206 LEU A O 1479 C CB . LEU A 206 ? 0.3151 0.2540 0.4067 -0.0090 0.0108 0.0983 206 LEU A CB 1480 C CG . LEU A 206 ? 0.3433 0.2709 0.4338 -0.0074 0.0118 0.1174 206 LEU A CG 1481 C CD1 . LEU A 206 ? 0.3259 0.2926 0.4250 0.0021 0.0083 0.1275 206 LEU A CD1 1482 C CD2 . LEU A 206 ? 0.3763 0.2588 0.4620 0.0035 0.0183 0.1204 206 LEU A CD2 1483 N N . VAL A 207 ? 0.2845 0.2039 0.3681 -0.0118 0.0133 0.0613 207 VAL A N 1484 C CA . VAL A 207 ? 0.2588 0.1932 0.3430 -0.0147 0.0109 0.0489 207 VAL A CA 1485 C C . VAL A 207 ? 0.2366 0.1921 0.3311 -0.0002 0.0107 0.0460 207 VAL A C 1486 O O . VAL A 207 ? 0.2406 0.1878 0.3386 0.0111 0.0148 0.0469 207 VAL A O 1487 C CB . VAL A 207 ? 0.2781 0.1819 0.3482 -0.0218 0.0141 0.0375 207 VAL A CB 1488 C CG1 . VAL A 207 ? 0.2556 0.1792 0.3268 -0.0260 0.0103 0.0283 207 VAL A CG1 1489 C CG2 . VAL A 207 ? 0.3131 0.1885 0.3675 -0.0403 0.0133 0.0398 207 VAL A CG2 1490 N N . CYS A 208 ? 0.2150 0.1977 0.3137 -0.0009 0.0061 0.0438 208 CYS A N 1491 C CA . CYS A 208 ? 0.2007 0.1983 0.3039 0.0072 0.0042 0.0391 208 CYS A CA 1492 C C . CYS A 208 ? 0.1944 0.1899 0.2946 0.0036 0.0035 0.0290 208 CYS A C 1493 O O . CYS A 208 ? 0.1881 0.1922 0.2863 -0.0015 0.0012 0.0275 208 CYS A O 1494 C CB . CYS A 208 ? 0.1951 0.2152 0.2981 0.0093 0.0006 0.0423 208 CYS A CB 1495 S SG . CYS A 208 ? 0.1953 0.2261 0.2970 0.0142 -0.0033 0.0360 208 CYS A SG 1496 N N . HIS A 209 ? 0.1940 0.1816 0.2952 0.0074 0.0060 0.0245 209 HIS A N 1497 C CA . HIS A 209 ? 0.1898 0.1748 0.2873 0.0039 0.0058 0.0165 209 HIS A CA 1498 C C . HIS A 209 ? 0.1791 0.1781 0.2803 0.0069 0.0020 0.0150 209 HIS A C 1499 O O . HIS A 209 ? 0.1700 0.1773 0.2768 0.0114 0.0013 0.0187 209 HIS A O 1500 C CB . HIS A 209 ? 0.2045 0.1734 0.2988 0.0064 0.0126 0.0130 209 HIS A CB 1501 C CG . HIS A 209 ? 0.2287 0.1722 0.3140 0.0044 0.0180 0.0130 209 HIS A CG 1502 N ND1 . HIS A 209 ? 0.2499 0.1740 0.3196 -0.0062 0.0194 0.0059 209 HIS A ND1 1503 C CD2 . HIS A 209 ? 0.2449 0.1747 0.3313 0.0111 0.0225 0.0195 209 HIS A CD2 1504 C CE1 . HIS A 209 ? 0.2790 0.1741 0.3379 -0.0077 0.0244 0.0061 209 HIS A CE1 1505 N NE2 . HIS A 209 ? 0.2773 0.1741 0.3469 0.0040 0.0269 0.0150 209 HIS A NE2 1506 N N . VAL A 210 ? 0.1743 0.1750 0.2712 0.0035 -0.0010 0.0109 210 VAL A N 1507 C CA . VAL A 210 ? 0.1760 0.1807 0.2711 0.0043 -0.0049 0.0089 210 VAL A CA 1508 C C . VAL A 210 ? 0.1761 0.1756 0.2679 0.0002 -0.0052 0.0059 210 VAL A C 1509 O O . VAL A 210 ? 0.1779 0.1766 0.2665 -0.0012 -0.0058 0.0059 210 VAL A O 1510 C CB . VAL A 210 ? 0.1806 0.1880 0.2700 0.0075 -0.0076 0.0085 210 VAL A CB 1511 C CG1 . VAL A 210 ? 0.1930 0.1942 0.2741 0.0070 -0.0114 0.0048 210 VAL A CG1 1512 C CG2 . VAL A 210 ? 0.1839 0.1994 0.2749 0.0103 -0.0064 0.0128 210 VAL A CG2 1513 N N . SER A 211 ? 0.1767 0.1771 0.2700 -0.0021 -0.0050 0.0057 211 SER A N 1514 C CA . SER A 211 ? 0.1782 0.1754 0.2675 -0.0069 -0.0044 0.0046 211 SER A CA 1515 C C . SER A 211 ? 0.1859 0.1835 0.2738 -0.0116 -0.0081 0.0063 211 SER A C 1516 O O . SER A 211 ? 0.1888 0.1940 0.2814 -0.0135 -0.0099 0.0085 211 SER A O 1517 C CB . SER A 211 ? 0.1842 0.1813 0.2739 -0.0070 0.0028 0.0033 211 SER A CB 1518 O OG . SER A 211 ? 0.1868 0.1813 0.2683 -0.0127 0.0036 0.0017 211 SER A OG 1519 N N . GLY A 212 ? 0.1895 0.1802 0.2707 -0.0153 -0.0103 0.0070 212 GLY A N 1520 C CA . GLY A 212 ? 0.1995 0.1867 0.2773 -0.0229 -0.0137 0.0102 212 GLY A CA 1521 C C . GLY A 212 ? 0.2142 0.1830 0.2820 -0.0235 -0.0198 0.0095 212 GLY A C 1522 O O . GLY A 212 ? 0.2298 0.1900 0.2917 -0.0329 -0.0239 0.0120 212 GLY A O 1523 N N . PHE A 213 ? 0.2145 0.1752 0.2781 -0.0140 -0.0197 0.0065 213 PHE A N 1524 C CA . PHE A 213 ? 0.2329 0.1707 0.2823 -0.0108 -0.0227 0.0037 213 PHE A CA 1525 C C . PHE A 213 ? 0.2468 0.1676 0.2886 -0.0052 -0.0228 0.0078 213 PHE A C 1526 O O . PHE A 213 ? 0.2318 0.1653 0.2812 -0.0014 -0.0212 0.0131 213 PHE A O 1527 C CB . PHE A 213 ? 0.2344 0.1733 0.2809 -0.0012 -0.0206 -0.0009 213 PHE A CB 1528 C CG . PHE A 213 ? 0.2215 0.1762 0.2776 0.0090 -0.0161 0.0017 213 PHE A CG 1529 C CD1 . PHE A 213 ? 0.2040 0.1786 0.2726 0.0064 -0.0141 0.0032 213 PHE A CD1 1530 C CD2 . PHE A 213 ? 0.2332 0.1829 0.2854 0.0210 -0.0136 0.0041 213 PHE A CD2 1531 C CE1 . PHE A 213 ? 0.1955 0.1835 0.2708 0.0106 -0.0116 0.0064 213 PHE A CE1 1532 C CE2 . PHE A 213 ? 0.2206 0.1927 0.2841 0.0274 -0.0107 0.0093 213 PHE A CE2 1533 C CZ . PHE A 213 ? 0.2024 0.1931 0.2766 0.0196 -0.0106 0.0102 213 PHE A CZ 1534 N N . TYR A 214 ? 0.2762 0.1664 0.3009 -0.0063 -0.0255 0.0060 214 TYR A N 1535 C CA . TYR A 214 ? 0.3008 0.1668 0.3154 0.0030 -0.0247 0.0107 214 TYR A CA 1536 C C . TYR A 214 ? 0.3453 0.1694 0.3347 0.0057 -0.0251 0.0033 214 TYR A C 1537 O O . TYR A 214 ? 0.3557 0.1675 0.3343 -0.0106 -0.0302 -0.0018 214 TYR A O 1538 C CB . TYR A 214 ? 0.3054 0.1685 0.3208 -0.0078 -0.0283 0.0197 214 TYR A CB 1539 C CG . TYR A 214 ? 0.3241 0.1710 0.3343 0.0049 -0.0272 0.0288 214 TYR A CG 1540 C CD1 . TYR A 214 ? 0.3691 0.1708 0.3584 0.0096 -0.0277 0.0293 214 TYR A CD1 1541 C CD2 . TYR A 214 ? 0.3056 0.1812 0.3301 0.0128 -0.0258 0.0375 214 TYR A CD2 1542 C CE1 . TYR A 214 ? 0.3915 0.1778 0.3773 0.0257 -0.0256 0.0403 214 TYR A CE1 1543 C CE2 . TYR A 214 ? 0.3225 0.1906 0.3454 0.0260 -0.0255 0.0494 214 TYR A CE2 1544 C CZ . TYR A 214 ? 0.3667 0.1906 0.3718 0.0348 -0.0247 0.0516 214 TYR A CZ 1545 O OH . TYR A 214 ? 0.3874 0.2039 0.3923 0.0519 -0.0234 0.0661 214 TYR A OH 1546 N N . PRO A 215 ? 0.3786 0.1804 0.3567 0.0257 -0.0195 0.0030 215 PRO A N 1547 C CA . PRO A 215 ? 0.3696 0.1925 0.3627 0.0454 -0.0141 0.0125 215 PRO A CA 1548 C C . PRO A 215 ? 0.3467 0.2097 0.3573 0.0526 -0.0101 0.0114 215 PRO A C 1549 O O . PRO A 215 ? 0.3269 0.2003 0.3382 0.0441 -0.0109 0.0034 215 PRO A O 1550 C CB . PRO A 215 ? 0.4196 0.2008 0.3918 0.0661 -0.0080 0.0125 215 PRO A CB 1551 C CG . PRO A 215 ? 0.4530 0.1945 0.3965 0.0592 -0.0080 -0.0027 215 PRO A CG 1552 C CD . PRO A 215 ? 0.4324 0.1839 0.3789 0.0299 -0.0179 -0.0062 215 PRO A CD 1553 N N . LYS A 216 ? 0.3464 0.2335 0.3713 0.0672 -0.0065 0.0218 216 LYS A N 1554 C CA . LYS A 216 ? 0.3273 0.2568 0.3712 0.0694 -0.0045 0.0248 216 LYS A CA 1555 C C . LYS A 216 ? 0.3296 0.2628 0.3686 0.0777 0.0016 0.0170 216 LYS A C 1556 O O . LYS A 216 ? 0.3028 0.2614 0.3526 0.0686 0.0005 0.0155 216 LYS A O 1557 C CB . LYS A 216 ? 0.3350 0.2917 0.3941 0.0822 -0.0031 0.0404 216 LYS A CB 1558 C CG . LYS A 216 ? 0.3096 0.3119 0.3887 0.0731 -0.0058 0.0468 216 LYS A CG 1559 C CD . LYS A 216 ? 0.3195 0.3502 0.4120 0.0800 -0.0080 0.0643 216 LYS A CD 1560 C CE . LYS A 216 ? 0.3032 0.3789 0.4123 0.0674 -0.0120 0.0713 216 LYS A CE 1561 N NZ . LYS A 216 ? 0.3104 0.4215 0.4339 0.0749 -0.0149 0.0911 216 LYS A NZ 1562 N N . PRO A 217 ? 0.3629 0.2687 0.3833 0.0950 0.0087 0.0121 217 PRO A N 1563 C CA . PRO A 217 ? 0.3690 0.2836 0.3832 0.1035 0.0157 0.0055 217 PRO A CA 1564 C C . PRO A 217 ? 0.3567 0.2705 0.3649 0.0840 0.0103 -0.0046 217 PRO A C 1565 O O . PRO A 217 ? 0.3657 0.2511 0.3588 0.0706 0.0043 -0.0123 217 PRO A O 1566 C CB . PRO A 217 ? 0.4190 0.2919 0.4053 0.1240 0.0247 -0.0013 217 PRO A CB 1567 C CG . PRO A 217 ? 0.4370 0.2940 0.4260 0.1342 0.0246 0.0087 217 PRO A CG 1568 C CD . PRO A 217 ? 0.4075 0.2732 0.4099 0.1099 0.0123 0.0131 217 PRO A CD 1569 N N . VAL A 218 ? 0.3357 0.2833 0.3571 0.0820 0.0119 -0.0019 218 VAL A N 1570 C CA . VAL A 218 ? 0.3200 0.2739 0.3412 0.0656 0.0067 -0.0069 218 VAL A CA 1571 C C . VAL A 218 ? 0.3146 0.2957 0.3401 0.0716 0.0125 -0.0040 218 VAL A C 1572 O O . VAL A 218 ? 0.3176 0.3227 0.3547 0.0836 0.0188 0.0043 218 VAL A O 1573 C CB . VAL A 218 ? 0.2854 0.2528 0.3254 0.0491 -0.0005 -0.0020 218 VAL A CB 1574 C CG1 . VAL A 218 ? 0.2646 0.2642 0.3258 0.0490 0.0008 0.0078 218 VAL A CG1 1575 C CG2 . VAL A 218 ? 0.2775 0.2449 0.3157 0.0355 -0.0055 -0.0060 218 VAL A CG2 1576 N N . TRP A 219 ? 0.3098 0.2906 0.3263 0.0630 0.0100 -0.0089 219 TRP A N 1577 C CA . TRP A 219 ? 0.3046 0.3105 0.3232 0.0661 0.0146 -0.0048 219 TRP A CA 1578 C C . TRP A 219 ? 0.2764 0.2951 0.3072 0.0502 0.0075 -0.0003 219 TRP A C 1579 O O . TRP A 219 ? 0.2676 0.2728 0.2921 0.0400 0.0007 -0.0048 219 TRP A O 1580 C CB . TRP A 219 ? 0.3449 0.3332 0.3331 0.0740 0.0197 -0.0151 219 TRP A CB 1581 C CG . TRP A 219 ? 0.3538 0.3674 0.3380 0.0800 0.0268 -0.0113 219 TRP A CG 1582 C CD1 . TRP A 219 ? 0.3698 0.3988 0.3510 0.0986 0.0393 -0.0084 219 TRP A CD1 1583 C CD2 . TRP A 219 ? 0.3489 0.3771 0.3306 0.0683 0.0224 -0.0086 219 TRP A CD2 1584 N NE1 . TRP A 219 ? 0.3741 0.4270 0.3503 0.0976 0.0432 -0.0045 219 TRP A NE1 1585 C CE2 . TRP A 219 ? 0.3611 0.4125 0.3371 0.0787 0.0323 -0.0042 219 TRP A CE2 1586 C CE3 . TRP A 219 ? 0.3367 0.3644 0.3224 0.0514 0.0115 -0.0069 219 TRP A CE3 1587 C CZ2 . TRP A 219 ? 0.3605 0.4315 0.3323 0.0709 0.0308 0.0015 219 TRP A CZ2 1588 C CZ3 . TRP A 219 ? 0.3389 0.3862 0.3221 0.0457 0.0099 -0.0004 219 TRP A CZ3 1589 C CH2 . TRP A 219 ? 0.3501 0.4172 0.3249 0.0546 0.0190 0.0034 219 TRP A CH2 1590 N N . VAL A 220 ? 0.2569 0.3014 0.3056 0.0479 0.0091 0.0101 220 VAL A N 1591 C CA . VAL A 220 ? 0.2399 0.2918 0.2999 0.0360 0.0044 0.0162 220 VAL A CA 1592 C C . VAL A 220 ? 0.2390 0.3140 0.3026 0.0365 0.0084 0.0257 220 VAL A C 1593 O O . VAL A 220 ? 0.2357 0.3292 0.3069 0.0403 0.0133 0.0321 220 VAL A O 1594 C CB . VAL A 220 ? 0.2255 0.2755 0.3019 0.0283 0.0016 0.0197 220 VAL A CB 1595 C CG1 . VAL A 220 ? 0.2199 0.2689 0.3038 0.0199 -0.0009 0.0247 220 VAL A CG1 1596 C CG2 . VAL A 220 ? 0.2295 0.2614 0.3029 0.0279 -0.0013 0.0125 220 VAL A CG2 1597 N N . MET A 221 ? 0.2411 0.3190 0.2996 0.0322 0.0061 0.0288 221 MET A N 1598 C CA . MET A 221 ? 0.2494 0.3488 0.3094 0.0314 0.0097 0.0398 221 MET A CA 1599 C C . MET A 221 ? 0.2326 0.3312 0.2965 0.0236 0.0047 0.0482 221 MET A C 1600 O O . MET A 221 ? 0.2284 0.3189 0.2859 0.0224 -0.0004 0.0446 221 MET A O 1601 C CB . MET A 221 ? 0.2839 0.3923 0.3235 0.0410 0.0157 0.0353 221 MET A CB 1602 C CG . MET A 221 ? 0.3062 0.4441 0.3486 0.0427 0.0226 0.0476 221 MET A CG 1603 S SD . MET A 221 ? 0.3190 0.4799 0.3821 0.0460 0.0288 0.0561 221 MET A SD 1604 C CE . MET A 221 ? 0.3371 0.4941 0.3838 0.0681 0.0386 0.0436 221 MET A CE 1605 N N . TRP A 222 ? 0.2210 0.3286 0.2954 0.0178 0.0060 0.0613 222 TRP A N 1606 C CA . TRP A 222 ? 0.2230 0.3315 0.2987 0.0137 0.0032 0.0731 222 TRP A CA 1607 C C . TRP A 222 ? 0.2375 0.3665 0.2983 0.0165 0.0047 0.0772 222 TRP A C 1608 O O . TRP A 222 ? 0.2330 0.3794 0.2878 0.0196 0.0111 0.0775 222 TRP A O 1609 C CB . TRP A 222 ? 0.2263 0.3297 0.3133 0.0049 0.0042 0.0860 222 TRP A CB 1610 C CG . TRP A 222 ? 0.2214 0.2981 0.3164 0.0018 0.0026 0.0811 222 TRP A CG 1611 C CD1 . TRP A 222 ? 0.2168 0.2862 0.3155 -0.0029 0.0032 0.0741 222 TRP A CD1 1612 C CD2 . TRP A 222 ? 0.2283 0.2844 0.3268 0.0048 0.0010 0.0829 222 TRP A CD2 1613 N NE1 . TRP A 222 ? 0.2186 0.2610 0.3192 -0.0045 0.0025 0.0697 222 TRP A NE1 1614 C CE2 . TRP A 222 ? 0.2292 0.2628 0.3307 0.0018 0.0022 0.0750 222 TRP A CE2 1615 C CE3 . TRP A 222 ? 0.2379 0.2957 0.3377 0.0108 -0.0009 0.0921 222 TRP A CE3 1616 C CZ2 . TRP A 222 ? 0.2387 0.2491 0.3430 0.0067 0.0039 0.0745 222 TRP A CZ2 1617 C CZ3 . TRP A 222 ? 0.2429 0.2812 0.3498 0.0167 0.0000 0.0941 222 TRP A CZ3 1618 C CH2 . TRP A 222 ? 0.2458 0.2595 0.3543 0.0156 0.0035 0.0847 222 TRP A CH2 1619 N N . MET A 223 ? 0.2453 0.3754 0.3003 0.0157 -0.0006 0.0819 223 MET A N 1620 C CA . MET A 223 ? 0.2671 0.4149 0.3025 0.0164 -0.0011 0.0840 223 MET A CA 1621 C C . MET A 223 ? 0.2779 0.4362 0.3178 0.0124 -0.0054 0.1037 223 MET A C 1622 O O . MET A 223 ? 0.2696 0.4167 0.3253 0.0121 -0.0094 0.1121 223 MET A O 1623 C CB . MET A 223 ? 0.2786 0.4188 0.2973 0.0166 -0.0068 0.0695 223 MET A CB 1624 C CG . MET A 223 ? 0.2794 0.4013 0.2919 0.0209 -0.0038 0.0508 223 MET A CG 1625 S SD . MET A 223 ? 0.3046 0.4316 0.2982 0.0314 0.0083 0.0417 223 MET A SD 1626 C CE . MET A 223 ? 0.3403 0.4708 0.2958 0.0288 0.0062 0.0353 223 MET A CE 1627 N N . ARG A 224 ? 0.3002 0.4799 0.3254 0.0110 -0.0034 0.1120 224 ARG A N 1628 C CA . ARG A 224 ? 0.3229 0.5165 0.3461 0.0076 -0.0090 0.1310 224 ARG A CA 1629 C C . ARG A 224 ? 0.3415 0.5513 0.3356 0.0061 -0.0124 0.1229 224 ARG A C 1630 O O . ARG A 224 ? 0.3549 0.5788 0.3284 0.0068 -0.0056 0.1196 224 ARG A O 1631 C CB . ARG A 224 ? 0.3379 0.5417 0.3671 0.0037 -0.0040 0.1508 224 ARG A CB 1632 C CG . ARG A 224 ? 0.3640 0.5757 0.3960 0.0013 -0.0100 0.1748 224 ARG A CG 1633 C CD . ARG A 224 ? 0.3816 0.5978 0.4185 -0.0050 -0.0051 0.1956 224 ARG A CD 1634 N NE . ARG A 224 ? 0.3812 0.5695 0.4361 -0.0087 -0.0017 0.1965 224 ARG A NE 1635 C CZ . ARG A 224 ? 0.3885 0.5448 0.4569 -0.0072 -0.0043 0.2039 224 ARG A CZ 1636 N NH1 . ARG A 224 ? 0.3968 0.5493 0.4689 0.0011 -0.0098 0.2134 224 ARG A NH1 1637 N NH2 . ARG A 224 ? 0.3920 0.5205 0.4692 -0.0137 -0.0009 0.2016 224 ARG A NH2 1638 N N . GLY A 225 ? 0.3469 0.5544 0.3376 0.0034 -0.0224 0.1185 225 GLY A N 1639 C CA . GLY A 225 ? 0.3724 0.5866 0.3306 -0.0022 -0.0275 0.1056 225 GLY A CA 1640 C C . GLY A 225 ? 0.3794 0.5725 0.3194 0.0019 -0.0194 0.0802 225 GLY A C 1641 O O . GLY A 225 ? 0.3681 0.5407 0.3235 0.0055 -0.0178 0.0703 225 GLY A O 1642 N N . ASP A 226 ? 0.4086 0.6062 0.3148 0.0031 -0.0131 0.0707 226 ASP A N 1643 C CA . ASP A 226 ? 0.4225 0.5984 0.3085 0.0120 -0.0023 0.0481 226 ASP A CA 1644 C C . ASP A 226 ? 0.4032 0.5900 0.3028 0.0249 0.0130 0.0528 226 ASP A C 1645 O O . ASP A 226 ? 0.4146 0.5914 0.2980 0.0364 0.0245 0.0382 226 ASP A O 1646 C CB . ASP A 226 ? 0.4789 0.6461 0.3142 0.0080 -0.0022 0.0314 226 ASP A CB 1647 C CG . ASP A 226 ? 0.5086 0.7046 0.3215 0.0078 0.0031 0.0412 226 ASP A CG 1648 O OD1 . ASP A 226 ? 0.4946 0.7176 0.3321 0.0112 0.0078 0.0618 226 ASP A OD1 1649 O OD2 . ASP A 226 ? 0.5636 0.7541 0.3309 0.0020 0.0021 0.0286 226 ASP A OD2 1650 N N . GLN A 227 ? 0.3753 0.5823 0.3041 0.0226 0.0132 0.0741 227 GLN A N 1651 C CA . GLN A 227 ? 0.3633 0.5863 0.3087 0.0294 0.0252 0.0823 227 GLN A CA 1652 C C . GLN A 227 ? 0.3274 0.5359 0.3043 0.0301 0.0242 0.0819 227 GLN A C 1653 O O . GLN A 227 ? 0.3050 0.5039 0.3029 0.0224 0.0158 0.0909 227 GLN A O 1654 C CB . GLN A 227 ? 0.3681 0.6196 0.3221 0.0222 0.0257 0.1070 227 GLN A CB 1655 C CG . GLN A 227 ? 0.4039 0.6755 0.3255 0.0206 0.0271 0.1102 227 GLN A CG 1656 C CD . GLN A 227 ? 0.4345 0.7121 0.3255 0.0330 0.0416 0.0934 227 GLN A CD 1657 O OE1 . GLN A 227 ? 0.4368 0.7352 0.3365 0.0414 0.0550 0.0986 227 GLN A OE1 1658 N NE2 . GLN A 227 ? 0.4655 0.7245 0.3196 0.0342 0.0395 0.0736 227 GLN A NE2 1659 N N . GLU A 228 ? 0.3209 0.5287 0.2994 0.0406 0.0336 0.0722 228 GLU A N 1660 C CA . GLU A 228 ? 0.2953 0.4946 0.3007 0.0405 0.0329 0.0725 228 GLU A CA 1661 C C . GLU A 228 ? 0.2714 0.4915 0.3007 0.0307 0.0332 0.0932 228 GLU A C 1662 O O . GLU A 228 ? 0.2819 0.5322 0.3093 0.0307 0.0405 0.1053 228 GLU A O 1663 C CB . GLU A 228 ? 0.3096 0.5082 0.3104 0.0558 0.0429 0.0605 228 GLU A CB 1664 C CG . GLU A 228 ? 0.3403 0.5073 0.3132 0.0638 0.0424 0.0392 228 GLU A CG 1665 C CD . GLU A 228 ? 0.3643 0.5229 0.3308 0.0821 0.0533 0.0283 228 GLU A CD 1666 O OE1 . GLU A 228 ? 0.4084 0.5375 0.3444 0.0897 0.0557 0.0109 228 GLU A OE1 1667 O OE2 . GLU A 228 ? 0.3574 0.5373 0.3478 0.0884 0.0590 0.0379 228 GLU A OE2 1668 N N . GLN A 229 ? 0.2429 0.4452 0.2917 0.0210 0.0256 0.0973 229 GLN A N 1669 C CA . GLN A 229 ? 0.2313 0.4426 0.2983 0.0080 0.0248 0.1149 229 GLN A CA 1670 C C . GLN A 229 ? 0.2141 0.4402 0.2953 0.0076 0.0289 0.1148 229 GLN A C 1671 O O . GLN A 229 ? 0.1984 0.4062 0.2865 0.0083 0.0256 0.1047 229 GLN A O 1672 C CB . GLN A 229 ? 0.2303 0.4101 0.3057 -0.0011 0.0162 0.1185 229 GLN A CB 1673 C CG . GLN A 229 ? 0.2404 0.4134 0.3063 0.0007 0.0115 0.1235 229 GLN A CG 1674 C CD . GLN A 229 ? 0.2588 0.4579 0.3158 -0.0024 0.0143 0.1401 229 GLN A CD 1675 O OE1 . GLN A 229 ? 0.2711 0.4891 0.3102 0.0041 0.0170 0.1358 229 GLN A OE1 1676 N NE2 . GLN A 229 ? 0.2664 0.4644 0.3325 -0.0136 0.0138 0.1590 229 GLN A NE2 1677 N N . GLN A 230 ? 0.2115 0.4756 0.2977 0.0061 0.0362 0.1281 230 GLN A N 1678 C CA . GLN A 230 ? 0.2000 0.4912 0.3017 0.0078 0.0407 0.1315 230 GLN A CA 1679 C C . GLN A 230 ? 0.1916 0.4757 0.3111 -0.0130 0.0321 0.1396 230 GLN A C 1680 O O . GLN A 230 ? 0.1804 0.4843 0.3133 -0.0138 0.0325 0.1416 230 GLN A O 1681 C CB . GLN A 230 ? 0.2085 0.5504 0.3118 0.0143 0.0525 0.1448 230 GLN A CB 1682 C CG . GLN A 230 ? 0.2216 0.5659 0.3013 0.0376 0.0630 0.1320 230 GLN A CG 1683 C CD . GLN A 230 ? 0.2346 0.6295 0.3130 0.0482 0.0780 0.1438 230 GLN A CD 1684 O OE1 . GLN A 230 ? 0.2342 0.6626 0.3227 0.0339 0.0791 0.1648 230 GLN A OE1 1685 N NE2 . GLN A 230 ? 0.2483 0.6481 0.3125 0.0742 0.0908 0.1310 230 GLN A NE2 1686 N N . GLY A 231 ? 0.1983 0.4514 0.3154 -0.0290 0.0245 0.1440 231 GLY A N 1687 C CA . GLY A 231 ? 0.2017 0.4296 0.3255 -0.0477 0.0163 0.1448 231 GLY A CA 1688 C C . GLY A 231 ? 0.1932 0.3905 0.3154 -0.0409 0.0125 0.1261 231 GLY A C 1689 O O . GLY A 231 ? 0.1973 0.3773 0.3223 -0.0556 0.0068 0.1248 231 GLY A O 1690 N N . THR A 232 ? 0.1856 0.3750 0.3007 -0.0211 0.0152 0.1118 232 THR A N 1691 C CA . THR A 232 ? 0.1808 0.3447 0.2944 -0.0149 0.0120 0.0958 232 THR A CA 1692 C C . THR A 232 ? 0.1782 0.3591 0.3023 -0.0201 0.0107 0.0971 232 THR A C 1693 O O . THR A 232 ? 0.1759 0.3930 0.3071 -0.0121 0.0157 0.1030 232 THR A O 1694 C CB . THR A 232 ? 0.1755 0.3353 0.2791 0.0044 0.0153 0.0824 232 THR A CB 1695 O OG1 . THR A 232 ? 0.1823 0.3310 0.2755 0.0069 0.0144 0.0822 232 THR A OG1 1696 C CG2 . THR A 232 ? 0.1670 0.3024 0.2701 0.0080 0.0116 0.0686 232 THR A CG2 1697 N N . HIS A 233 ? 0.1884 0.3452 0.3126 -0.0333 0.0044 0.0931 233 HIS A N 1698 C CA . HIS A 233 ? 0.1943 0.3671 0.3264 -0.0426 0.0006 0.0955 233 HIS A CA 1699 C C . HIS A 233 ? 0.1923 0.3414 0.3196 -0.0346 -0.0014 0.0807 233 HIS A C 1700 O O . HIS A 233 ? 0.1948 0.3090 0.3133 -0.0424 -0.0046 0.0725 233 HIS A O 1701 C CB . HIS A 233 ? 0.2177 0.3822 0.3482 -0.0705 -0.0058 0.1040 233 HIS A CB 1702 C CG . HIS A 233 ? 0.2245 0.4154 0.3627 -0.0850 -0.0118 0.1102 233 HIS A CG 1703 N ND1 . HIS A 233 ? 0.2530 0.4325 0.3844 -0.1145 -0.0198 0.1149 233 HIS A ND1 1704 C CD2 . HIS A 233 ? 0.2154 0.4443 0.3665 -0.0747 -0.0115 0.1138 233 HIS A CD2 1705 C CE1 . HIS A 233 ? 0.2516 0.4662 0.3922 -0.1240 -0.0257 0.1217 233 HIS A CE1 1706 N NE2 . HIS A 233 ? 0.2270 0.4733 0.3816 -0.0984 -0.0203 0.1222 233 HIS A NE2 1707 N N A ARG A 234 ? 0.1854 0.3529 0.3174 -0.0179 0.0014 0.0782 234 ARG A N 1708 N N B ARG A 234 ? 0.1850 0.3517 0.3167 -0.0178 0.0014 0.0779 234 ARG A N 1709 C CA A ARG A 234 ? 0.1864 0.3345 0.3142 -0.0103 -0.0004 0.0668 234 ARG A CA 1710 C CA B ARG A 234 ? 0.1849 0.3308 0.3120 -0.0106 -0.0005 0.0662 234 ARG A CA 1711 C C A ARG A 234 ? 0.1873 0.3427 0.3191 -0.0253 -0.0072 0.0705 234 ARG A C 1712 C C B ARG A 234 ? 0.1861 0.3413 0.3178 -0.0242 -0.0069 0.0702 234 ARG A C 1713 O O A ARG A 234 ? 0.1831 0.3748 0.3261 -0.0323 -0.0092 0.0837 234 ARG A O 1714 O O B ARG A 234 ? 0.1810 0.3736 0.3245 -0.0290 -0.0084 0.0832 234 ARG A O 1715 C CB A ARG A 234 ? 0.1909 0.3514 0.3194 0.0123 0.0053 0.0648 234 ARG A CB 1716 C CB B ARG A 234 ? 0.1883 0.3396 0.3135 0.0125 0.0053 0.0617 234 ARG A CB 1717 C CG A ARG A 234 ? 0.1984 0.3275 0.3169 0.0213 0.0044 0.0515 234 ARG A CG 1718 C CG B ARG A 234 ? 0.1968 0.3217 0.3088 0.0202 0.0076 0.0510 234 ARG A CG 1719 C CD A ARG A 234 ? 0.2098 0.3479 0.3295 0.0391 0.0081 0.0527 234 ARG A CD 1720 C CD B ARG A 234 ? 0.2114 0.3416 0.3144 0.0389 0.0148 0.0476 234 ARG A CD 1721 N NE A ARG A 234 ? 0.2128 0.3741 0.3451 0.0336 0.0039 0.0630 234 ARG A NE 1722 N NE B ARG A 234 ? 0.2210 0.3747 0.3239 0.0408 0.0202 0.0555 234 ARG A NE 1723 C CZ A ARG A 234 ? 0.2230 0.4033 0.3624 0.0492 0.0069 0.0707 234 ARG A CZ 1724 C CZ B ARG A 234 ? 0.2285 0.4174 0.3396 0.0489 0.0271 0.0660 234 ARG A CZ 1725 N NH1 A ARG A 234 ? 0.2394 0.4118 0.3715 0.0727 0.0160 0.0672 234 ARG A NH1 1726 N NH1 B ARG A 234 ? 0.2338 0.4380 0.3548 0.0573 0.0287 0.0701 234 ARG A NH1 1727 N NH2 A ARG A 234 ? 0.2226 0.4290 0.3745 0.0417 0.0010 0.0825 234 ARG A NH2 1728 N NH2 B ARG A 234 ? 0.2370 0.4495 0.3472 0.0495 0.0327 0.0742 234 ARG A NH2 1729 N N . GLY A 235 ? 0.1904 0.3151 0.3124 -0.0310 -0.0106 0.0600 235 GLY A N 1730 C CA . GLY A 235 ? 0.1995 0.3283 0.3197 -0.0457 -0.0174 0.0614 235 GLY A CA 1731 C C . GLY A 235 ? 0.1970 0.3431 0.3238 -0.0315 -0.0178 0.0636 235 GLY A C 1732 O O . GLY A 235 ? 0.2011 0.3557 0.3334 -0.0108 -0.0121 0.0647 235 GLY A O 1733 N N . ASP A 236 ? 0.2030 0.3512 0.3261 -0.0425 -0.0242 0.0644 236 ASP A N 1734 C CA . ASP A 236 ? 0.1974 0.3596 0.3260 -0.0296 -0.0254 0.0690 236 ASP A CA 1735 C C . ASP A 236 ? 0.1923 0.3183 0.3096 -0.0196 -0.0225 0.0559 236 ASP A C 1736 O O . ASP A 236 ? 0.1870 0.2832 0.2931 -0.0264 -0.0211 0.0442 236 ASP A O 1737 C CB . ASP A 236 ? 0.2068 0.3917 0.3354 -0.0477 -0.0350 0.0780 236 ASP A CB 1738 C CG . ASP A 236 ? 0.2132 0.4438 0.3558 -0.0603 -0.0398 0.0950 236 ASP A CG 1739 O OD1 . ASP A 236 ? 0.2090 0.4639 0.3666 -0.0476 -0.0339 0.1035 236 ASP A OD1 1740 O OD2 . ASP A 236 ? 0.2260 0.4702 0.3633 -0.0847 -0.0497 0.1003 236 ASP A OD2 1741 N N . PHE A 237 ? 0.1920 0.3208 0.3125 -0.0032 -0.0213 0.0593 237 PHE A N 1742 C CA . PHE A 237 ? 0.1941 0.2914 0.3036 0.0012 -0.0205 0.0498 237 PHE A CA 1743 C C . PHE A 237 ? 0.1883 0.2832 0.2895 -0.0152 -0.0265 0.0493 237 PHE A C 1744 O O . PHE A 237 ? 0.1848 0.3044 0.2900 -0.0202 -0.0323 0.0605 237 PHE A O 1745 C CB . PHE A 237 ? 0.2105 0.3040 0.3217 0.0220 -0.0176 0.0543 237 PHE A CB 1746 C CG . PHE A 237 ? 0.2239 0.3064 0.3332 0.0379 -0.0103 0.0492 237 PHE A CG 1747 C CD1 . PHE A 237 ? 0.2339 0.3428 0.3529 0.0499 -0.0054 0.0574 237 PHE A CD1 1748 C CD2 . PHE A 237 ? 0.2358 0.2849 0.3323 0.0394 -0.0084 0.0368 237 PHE A CD2 1749 C CE1 . PHE A 237 ? 0.2474 0.3450 0.3596 0.0644 0.0023 0.0513 237 PHE A CE1 1750 C CE2 . PHE A 237 ? 0.2453 0.2831 0.3347 0.0512 -0.0027 0.0311 237 PHE A CE2 1751 C CZ . PHE A 237 ? 0.2534 0.3132 0.3487 0.0643 0.0031 0.0372 237 PHE A CZ 1752 N N . LEU A 238 ? 0.1805 0.2487 0.2698 -0.0230 -0.0246 0.0372 238 LEU A N 1753 C CA . LEU A 238 ? 0.1858 0.2468 0.2617 -0.0381 -0.0274 0.0334 238 LEU A CA 1754 C C . LEU A 238 ? 0.1838 0.2283 0.2542 -0.0320 -0.0252 0.0299 238 LEU A C 1755 O O . LEU A 238 ? 0.1773 0.2056 0.2493 -0.0240 -0.0205 0.0237 238 LEU A O 1756 C CB . LEU A 238 ? 0.1928 0.2353 0.2577 -0.0501 -0.0241 0.0227 238 LEU A CB 1757 C CG . LEU A 238 ? 0.1959 0.2469 0.2647 -0.0581 -0.0257 0.0259 238 LEU A CG 1758 C CD1 . LEU A 238 ? 0.2167 0.2393 0.2688 -0.0709 -0.0223 0.0156 238 LEU A CD1 1759 C CD2 . LEU A 238 ? 0.2017 0.2855 0.2753 -0.0693 -0.0343 0.0385 238 LEU A CD2 1760 N N . PRO A 239 ? 0.1896 0.2403 0.2527 -0.0383 -0.0293 0.0350 239 PRO A N 1761 C CA . PRO A 239 ? 0.1952 0.2320 0.2532 -0.0348 -0.0274 0.0342 239 PRO A CA 1762 C C . PRO A 239 ? 0.2008 0.2225 0.2475 -0.0424 -0.0213 0.0228 239 PRO A C 1763 O O . PRO A 239 ? 0.2108 0.2312 0.2453 -0.0534 -0.0198 0.0167 239 PRO A O 1764 C CB . PRO A 239 ? 0.2048 0.2578 0.2588 -0.0395 -0.0341 0.0464 239 PRO A CB 1765 C CG . PRO A 239 ? 0.2102 0.2811 0.2581 -0.0545 -0.0388 0.0470 239 PRO A CG 1766 C CD . PRO A 239 ? 0.2011 0.2739 0.2590 -0.0517 -0.0367 0.0431 239 PRO A CD 1767 N N . ASN A 240 ? 0.1982 0.2085 0.2479 -0.0365 -0.0175 0.0206 240 ASN A N 1768 C CA . ASN A 240 ? 0.2088 0.2142 0.2507 -0.0417 -0.0114 0.0154 240 ASN A CA 1769 C C . ASN A 240 ? 0.2234 0.2343 0.2567 -0.0480 -0.0144 0.0233 240 ASN A C 1770 O O . ASN A 240 ? 0.2338 0.2482 0.2697 -0.0458 -0.0212 0.0337 240 ASN A O 1771 C CB . ASN A 240 ? 0.2000 0.1993 0.2513 -0.0355 -0.0073 0.0127 240 ASN A CB 1772 C CG . ASN A 240 ? 0.1920 0.1878 0.2499 -0.0299 -0.0036 0.0063 240 ASN A CG 1773 O OD1 . ASN A 240 ? 0.1990 0.1911 0.2505 -0.0320 0.0005 0.0007 240 ASN A OD1 1774 N ND2 . ASN A 240 ? 0.1789 0.1730 0.2465 -0.0237 -0.0054 0.0072 240 ASN A ND2 1775 N N . ALA A 241 ? 0.2326 0.2448 0.2553 -0.0543 -0.0081 0.0196 241 ALA A N 1776 C CA . ALA A 241 ? 0.2493 0.2692 0.2610 -0.0623 -0.0098 0.0276 241 ALA A CA 1777 C C . ALA A 241 ? 0.2495 0.2669 0.2687 -0.0614 -0.0114 0.0372 241 ALA A C 1778 O O . ALA A 241 ? 0.2616 0.2842 0.2729 -0.0682 -0.0135 0.0468 241 ALA A O 1779 C CB . ALA A 241 ? 0.2656 0.2882 0.2586 -0.0694 -0.0007 0.0191 241 ALA A CB 1780 N N . ASP A 242 ? 0.2398 0.2484 0.2721 -0.0551 -0.0113 0.0354 242 ASP A N 1781 C CA . ASP A 242 ? 0.2476 0.2497 0.2838 -0.0587 -0.0136 0.0430 242 ASP A CA 1782 C C . ASP A 242 ? 0.2495 0.2308 0.2885 -0.0523 -0.0211 0.0469 242 ASP A C 1783 O O . ASP A 242 ? 0.2548 0.2227 0.2955 -0.0546 -0.0231 0.0473 242 ASP A O 1784 C CB . ASP A 242 ? 0.2440 0.2548 0.2891 -0.0601 -0.0071 0.0383 242 ASP A CB 1785 C CG . ASP A 242 ? 0.2335 0.2397 0.2887 -0.0513 -0.0067 0.0298 242 ASP A CG 1786 O OD1 . ASP A 242 ? 0.2262 0.2247 0.2806 -0.0442 -0.0090 0.0254 242 ASP A OD1 1787 O OD2 . ASP A 242 ? 0.2391 0.2539 0.3037 -0.0523 -0.0044 0.0296 242 ASP A OD2 1788 N N . GLU A 243 ? 0.2518 0.2313 0.2894 -0.0446 -0.0248 0.0501 243 GLU A N 1789 C CA . GLU A 243 ? 0.2644 0.2247 0.3031 -0.0334 -0.0290 0.0541 243 GLU A CA 1790 C C . GLU A 243 ? 0.2597 0.2081 0.3027 -0.0277 -0.0272 0.0436 243 GLU A C 1791 O O . GLU A 243 ? 0.2832 0.2063 0.3202 -0.0253 -0.0292 0.0435 243 GLU A O 1792 C CB . GLU A 243 ? 0.2932 0.2331 0.3231 -0.0359 -0.0332 0.0668 243 GLU A CB 1793 C CG . GLU A 243 ? 0.3001 0.2566 0.3259 -0.0401 -0.0358 0.0795 243 GLU A CG 1794 C CD . GLU A 243 ? 0.3317 0.2679 0.3485 -0.0426 -0.0400 0.0952 243 GLU A CD 1795 O OE1 . GLU A 243 ? 0.3418 0.2842 0.3571 -0.0364 -0.0438 0.1092 243 GLU A OE1 1796 O OE2 . GLU A 243 ? 0.3488 0.2638 0.3598 -0.0519 -0.0402 0.0954 243 GLU A OE2 1797 N N . THR A 244 ? 0.2356 0.2001 0.2858 -0.0272 -0.0234 0.0348 244 THR A N 1798 C CA . THR A 244 ? 0.2256 0.1857 0.2805 -0.0205 -0.0220 0.0267 244 THR A CA 1799 C C . THR A 244 ? 0.2124 0.1883 0.2735 -0.0147 -0.0201 0.0244 244 THR A C 1800 O O . THR A 244 ? 0.2152 0.2045 0.2754 -0.0188 -0.0207 0.0277 244 THR A O 1801 C CB . THR A 244 ? 0.2162 0.1811 0.2752 -0.0274 -0.0196 0.0211 244 THR A CB 1802 O OG1 . THR A 244 ? 0.2003 0.1830 0.2639 -0.0301 -0.0142 0.0186 244 THR A OG1 1803 C CG2 . THR A 244 ? 0.2325 0.1882 0.2867 -0.0381 -0.0227 0.0254 244 THR A CG2 1804 N N . TRP A 245 ? 0.2028 0.1775 0.2679 -0.0076 -0.0187 0.0195 245 TRP A N 1805 C CA . TRP A 245 ? 0.1937 0.1831 0.2650 -0.0032 -0.0175 0.0196 245 TRP A CA 1806 C C . TRP A 245 ? 0.1819 0.1752 0.2569 -0.0067 -0.0142 0.0129 245 TRP A C 1807 O O . TRP A 245 ? 0.1748 0.1622 0.2503 -0.0078 -0.0128 0.0091 245 TRP A O 1808 C CB . TRP A 245 ? 0.2009 0.1882 0.2732 0.0103 -0.0172 0.0223 245 TRP A CB 1809 C CG . TRP A 245 ? 0.2196 0.2068 0.2908 0.0179 -0.0191 0.0321 245 TRP A CG 1810 C CD1 . TRP A 245 ? 0.2413 0.2042 0.3034 0.0258 -0.0192 0.0345 245 TRP A CD1 1811 C CD2 . TRP A 245 ? 0.2176 0.2297 0.2962 0.0179 -0.0216 0.0426 245 TRP A CD2 1812 N NE1 . TRP A 245 ? 0.2555 0.2264 0.3207 0.0344 -0.0206 0.0471 245 TRP A NE1 1813 C CE2 . TRP A 245 ? 0.2373 0.2428 0.3140 0.0292 -0.0228 0.0530 245 TRP A CE2 1814 C CE3 . TRP A 245 ? 0.2090 0.2471 0.2938 0.0078 -0.0239 0.0450 245 TRP A CE3 1815 C CZ2 . TRP A 245 ? 0.2426 0.2742 0.3272 0.0323 -0.0264 0.0679 245 TRP A CZ2 1816 C CZ3 . TRP A 245 ? 0.2137 0.2775 0.3041 0.0070 -0.0286 0.0582 245 TRP A CZ3 1817 C CH2 . TRP A 245 ? 0.2333 0.2974 0.3255 0.0201 -0.0300 0.0707 245 TRP A CH2 1818 N N . TYR A 246 ? 0.1799 0.1842 0.2576 -0.0093 -0.0136 0.0136 246 TYR A N 1819 C CA . TYR A 246 ? 0.1807 0.1845 0.2604 -0.0119 -0.0102 0.0094 246 TYR A CA 1820 C C . TYR A 246 ? 0.1809 0.1968 0.2659 -0.0095 -0.0113 0.0139 246 TYR A C 1821 O O . TYR A 246 ? 0.1784 0.2086 0.2656 -0.0106 -0.0144 0.0203 246 TYR A O 1822 C CB . TYR A 246 ? 0.1914 0.1904 0.2632 -0.0218 -0.0078 0.0058 246 TYR A CB 1823 C CG . TYR A 246 ? 0.2004 0.1901 0.2705 -0.0238 -0.0034 0.0020 246 TYR A CG 1824 C CD1 . TYR A 246 ? 0.2075 0.2002 0.2769 -0.0300 -0.0057 0.0047 246 TYR A CD1 1825 C CD2 . TYR A 246 ? 0.2089 0.1873 0.2784 -0.0193 0.0032 -0.0021 246 TYR A CD2 1826 C CE1 . TYR A 246 ? 0.2245 0.2020 0.2896 -0.0330 -0.0018 0.0024 246 TYR A CE1 1827 C CE2 . TYR A 246 ? 0.2224 0.1872 0.2892 -0.0182 0.0082 -0.0039 246 TYR A CE2 1828 C CZ . TYR A 246 ? 0.2342 0.1950 0.2974 -0.0257 0.0054 -0.0020 246 TYR A CZ 1829 O OH . TYR A 246 ? 0.2571 0.1981 0.3151 -0.0259 0.0101 -0.0026 246 TYR A OH 1830 N N . LEU A 247 ? 0.1849 0.1995 0.2731 -0.0062 -0.0089 0.0127 247 LEU A N 1831 C CA . LEU A 247 ? 0.1937 0.2222 0.2869 -0.0056 -0.0088 0.0181 247 LEU A CA 1832 C C . LEU A 247 ? 0.1903 0.2108 0.2836 -0.0083 -0.0061 0.0170 247 LEU A C 1833 O O . LEU A 247 ? 0.1937 0.2044 0.2865 -0.0039 -0.0042 0.0135 247 LEU A O 1834 C CB . LEU A 247 ? 0.2011 0.2374 0.2963 0.0075 -0.0077 0.0202 247 LEU A CB 1835 C CG . LEU A 247 ? 0.2156 0.2722 0.3163 0.0123 -0.0054 0.0270 247 LEU A CG 1836 C CD1 . LEU A 247 ? 0.2179 0.2992 0.3268 0.0103 -0.0071 0.0366 247 LEU A CD1 1837 C CD2 . LEU A 247 ? 0.2307 0.2842 0.3254 0.0273 -0.0015 0.0242 247 LEU A CD2 1838 N N . GLN A 248 ? 0.1916 0.2175 0.2859 -0.0163 -0.0064 0.0219 248 GLN A N 1839 C CA . GLN A 248 ? 0.1972 0.2142 0.2914 -0.0170 -0.0037 0.0238 248 GLN A CA 1840 C C . GLN A 248 ? 0.1927 0.2298 0.2923 -0.0186 -0.0042 0.0331 248 GLN A C 1841 O O . GLN A 248 ? 0.1846 0.2430 0.2886 -0.0230 -0.0064 0.0388 248 GLN A O 1842 C CB . GLN A 248 ? 0.2224 0.2139 0.3076 -0.0262 -0.0016 0.0204 248 GLN A CB 1843 C CG . GLN A 248 ? 0.2437 0.2326 0.3203 -0.0431 -0.0050 0.0205 248 GLN A CG 1844 C CD . GLN A 248 ? 0.2795 0.2325 0.3394 -0.0522 -0.0014 0.0145 248 GLN A CD 1845 O OE1 . GLN A 248 ? 0.3001 0.2340 0.3515 -0.0471 0.0035 0.0059 248 GLN A OE1 1846 N NE2 . GLN A 248 ? 0.2992 0.2417 0.3523 -0.0660 -0.0031 0.0193 248 GLN A NE2 1847 N N . ALA A 249 ? 0.1910 0.2260 0.2915 -0.0144 -0.0019 0.0366 249 ALA A N 1848 C CA . ALA A 249 ? 0.1928 0.2478 0.2972 -0.0159 -0.0011 0.0466 249 ALA A CA 1849 C C . ALA A 249 ? 0.2087 0.2472 0.3102 -0.0232 -0.0003 0.0529 249 ALA A C 1850 O O . ALA A 249 ? 0.2050 0.2260 0.3044 -0.0165 0.0012 0.0509 249 ALA A O 1851 C CB . ALA A 249 ? 0.1866 0.2562 0.2905 -0.0018 0.0011 0.0458 249 ALA A CB 1852 N N . THR A 250 ? 0.2218 0.2668 0.3239 -0.0373 -0.0015 0.0623 250 THR A N 1853 C CA . THR A 250 ? 0.2480 0.2696 0.3443 -0.0467 -0.0009 0.0695 250 THR A CA 1854 C C . THR A 250 ? 0.2528 0.2970 0.3537 -0.0471 0.0001 0.0837 250 THR A C 1855 O O . THR A 250 ? 0.2344 0.3151 0.3421 -0.0436 0.0009 0.0881 250 THR A O 1856 C CB . THR A 250 ? 0.2742 0.2759 0.3613 -0.0685 -0.0041 0.0698 250 THR A CB 1857 O OG1 . THR A 250 ? 0.2704 0.3076 0.3646 -0.0823 -0.0082 0.0796 250 THR A OG1 1858 C CG2 . THR A 250 ? 0.2771 0.2589 0.3560 -0.0687 -0.0046 0.0556 250 THR A CG2 1859 N N . LEU A 251 ? 0.2727 0.2947 0.3689 -0.0495 0.0012 0.0919 251 LEU A N 1860 C CA . LEU A 251 ? 0.2836 0.3246 0.3819 -0.0529 0.0019 0.1079 251 LEU A CA 1861 C C . LEU A 251 ? 0.3255 0.3314 0.4156 -0.0670 0.0014 0.1186 251 LEU A C 1862 O O . LEU A 251 ? 0.3371 0.3052 0.4210 -0.0594 0.0034 0.1163 251 LEU A O 1863 C CB . LEU A 251 ? 0.2722 0.3276 0.3717 -0.0350 0.0039 0.1094 251 LEU A CB 1864 C CG . LEU A 251 ? 0.2798 0.3587 0.3787 -0.0373 0.0051 0.1263 251 LEU A CG 1865 C CD1 . LEU A 251 ? 0.2709 0.3926 0.3737 -0.0403 0.0077 0.1298 251 LEU A CD1 1866 C CD2 . LEU A 251 ? 0.2788 0.3638 0.3742 -0.0230 0.0051 0.1285 251 LEU A CD2 1867 N N A ASP A 252 ? 0.3437 0.3615 0.4335 -0.0872 -0.0008 0.1314 252 ASP A N 1868 N N B ASP A 252 ? 0.3424 0.3608 0.4323 -0.0872 -0.0008 0.1314 252 ASP A N 1869 C CA A ASP A 252 ? 0.3908 0.3711 0.4695 -0.1039 -0.0018 0.1434 252 ASP A CA 1870 C CA B ASP A 252 ? 0.3885 0.3717 0.4679 -0.1040 -0.0019 0.1442 252 ASP A CA 1871 C C A ASP A 252 ? 0.4009 0.3911 0.4822 -0.0955 0.0004 0.1604 252 ASP A C 1872 C C B ASP A 252 ? 0.3977 0.3892 0.4795 -0.0938 0.0006 0.1598 252 ASP A C 1873 O O A ASP A 252 ? 0.3811 0.4188 0.4707 -0.0941 0.0012 0.1696 252 ASP A O 1874 O O B ASP A 252 ? 0.3749 0.4138 0.4651 -0.0893 0.0017 0.1675 252 ASP A O 1875 C CB A ASP A 252 ? 0.4107 0.4004 0.4868 -0.1343 -0.0071 0.1514 252 ASP A CB 1876 C CB B ASP A 252 ? 0.4044 0.4047 0.4835 -0.1334 -0.0067 0.1549 252 ASP A CB 1877 C CG A ASP A 252 ? 0.4193 0.3878 0.4864 -0.1464 -0.0110 0.1358 252 ASP A CG 1878 C CG B ASP A 252 ? 0.4565 0.4088 0.5190 -0.1561 -0.0090 0.1663 252 ASP A CG 1879 O OD1 A ASP A 252 ? 0.4057 0.3630 0.4721 -0.1290 -0.0086 0.1188 252 ASP A OD1 1880 O OD1 B ASP A 252 ? 0.4888 0.3818 0.5334 -0.1589 -0.0086 0.1553 252 ASP A OD1 1881 O OD2 A ASP A 252 ? 0.4495 0.4139 0.5090 -0.1755 -0.0171 0.1414 252 ASP A OD2 1882 O OD2 B ASP A 252 ? 0.4713 0.4432 0.5367 -0.1710 -0.0105 0.1864 252 ASP A OD2 1883 N N . VAL A 253 ? 0.4342 0.3804 0.5073 -0.0882 0.0024 0.1650 253 VAL A N 1884 C CA . VAL A 253 ? 0.4539 0.4071 0.5289 -0.0785 0.0037 0.1831 253 VAL A CA 1885 C C . VAL A 253 ? 0.5188 0.4200 0.5813 -0.0892 0.0042 0.1985 253 VAL A C 1886 O O . VAL A 253 ? 0.5528 0.3994 0.6029 -0.0923 0.0060 0.1898 253 VAL A O 1887 C CB . VAL A 253 ? 0.4386 0.3971 0.5196 -0.0512 0.0056 0.1774 253 VAL A CB 1888 C CG1 . VAL A 253 ? 0.3976 0.4003 0.4863 -0.0421 0.0047 0.1625 253 VAL A CG1 1889 C CG2 . VAL A 253 ? 0.4600 0.3690 0.5366 -0.0399 0.0089 0.1678 253 VAL A CG2 1890 N N . GLU A 254 ? 0.5457 0.4613 0.6087 -0.0942 0.0034 0.2212 254 GLU A N 1891 C CA . GLU A 254 ? 0.6166 0.4806 0.6673 -0.1015 0.0042 0.2397 254 GLU A CA 1892 C C . GLU A 254 ? 0.6414 0.4773 0.6933 -0.0721 0.0083 0.2420 254 GLU A C 1893 O O . GLU A 254 ? 0.5986 0.4725 0.6632 -0.0510 0.0083 0.2369 254 GLU A O 1894 C CB . GLU A 254 ? 0.6278 0.5220 0.6795 -0.1164 0.0019 0.2663 254 GLU A CB 1895 N N . ALA A 255 ? 0.7158 0.4850 0.7536 -0.0713 0.0118 0.2505 255 ALA A N 1896 C CA . ALA A 255 ? 0.7471 0.4879 0.7876 -0.0411 0.0174 0.2581 255 ALA A CA 1897 C C . ALA A 255 ? 0.7371 0.5292 0.7923 -0.0275 0.0140 0.2802 255 ALA A C 1898 O O . ALA A 255 ? 0.7461 0.5587 0.7990 -0.0434 0.0100 0.2996 255 ALA A O 1899 C CB . ALA A 255 ? 0.8208 0.4788 0.8402 -0.0441 0.0227 0.2688 255 ALA A CB 1900 N N . GLY A 256 ? 0.7245 0.5420 0.7939 -0.0005 0.0149 0.2778 256 GLY A N 1901 C CA . GLY A 256 ? 0.7144 0.5817 0.7953 0.0117 0.0101 0.2985 256 GLY A CA 1902 C C . GLY A 256 ? 0.6668 0.6019 0.7543 0.0068 0.0043 0.2855 256 GLY A C 1903 O O . GLY A 256 ? 0.6515 0.6249 0.7486 0.0219 0.0007 0.2869 256 GLY A O 1904 N N . GLU A 257 ? 0.6466 0.5954 0.7280 -0.0144 0.0036 0.2736 257 GLU A N 1905 C CA . GLU A 257 ? 0.5927 0.5947 0.6769 -0.0177 0.0010 0.2568 257 GLU A CA 1906 C C . GLU A 257 ? 0.5464 0.5557 0.6377 -0.0040 0.0009 0.2328 257 GLU A C 1907 O O . GLU A 257 ? 0.5188 0.5682 0.6099 -0.0030 -0.0015 0.2213 257 GLU A O 1908 C CB . GLU A 257 ? 0.5912 0.6011 0.6706 -0.0400 0.0022 0.2498 257 GLU A CB 1909 N N . GLU A 258 ? 0.5441 0.5127 0.6388 0.0058 0.0045 0.2251 258 GLU A N 1910 C CA . GLU A 258 ? 0.5071 0.4831 0.6095 0.0185 0.0050 0.2055 258 GLU A CA 1911 C C . GLU A 258 ? 0.4654 0.4838 0.5759 0.0312 -0.0002 0.2104 258 GLU A C 1912 O O . GLU A 258 ? 0.4234 0.4638 0.5366 0.0329 -0.0027 0.1935 258 GLU A O 1913 C CB . GLU A 258 ? 0.5422 0.4704 0.6463 0.0310 0.0118 0.2015 258 GLU A CB 1914 C CG . GLU A 258 ? 0.5776 0.4563 0.6682 0.0171 0.0166 0.1911 258 GLU A CG 1915 C CD . GLU A 258 ? 0.6415 0.4640 0.7220 0.0205 0.0222 0.2066 258 GLU A CD 1916 O OE1 . GLU A 258 ? 0.6752 0.5016 0.7562 0.0204 0.0200 0.2300 258 GLU A OE1 1917 O OE2 . GLU A 258 ? 0.6842 0.4557 0.7536 0.0234 0.0294 0.1951 258 GLU A OE2 1918 N N . ALA A 259 ? 0.4648 0.4930 0.5782 0.0386 -0.0028 0.2349 259 ALA A N 1919 C CA . ALA A 259 ? 0.4375 0.5089 0.5578 0.0480 -0.0099 0.2435 259 ALA A CA 1920 C C . ALA A 259 ? 0.3971 0.5093 0.5057 0.0357 -0.0160 0.2312 259 ALA A C 1921 O O . ALA A 259 ? 0.3983 0.5180 0.4948 0.0236 -0.0151 0.2324 259 ALA A O 1922 C CB . ALA A 259 ? 0.4662 0.5433 0.5896 0.0558 -0.0124 0.2754 259 ALA A CB 1923 N N . GLY A 260 ? 0.3627 0.4996 0.4737 0.0387 -0.0213 0.2195 260 GLY A N 1924 C CA . GLY A 260 ? 0.3418 0.5089 0.4364 0.0285 -0.0265 0.2054 260 GLY A CA 1925 C C . GLY A 260 ? 0.3121 0.4670 0.4001 0.0228 -0.0223 0.1778 260 GLY A C 1926 O O . GLY A 260 ? 0.3094 0.4816 0.3812 0.0169 -0.0248 0.1643 260 GLY A O 1927 N N . LEU A 261 ? 0.2950 0.4186 0.3926 0.0248 -0.0158 0.1695 261 LEU A N 1928 C CA . LEU A 261 ? 0.2693 0.3842 0.3623 0.0200 -0.0125 0.1465 261 LEU A CA 1929 C C . LEU A 261 ? 0.2501 0.3651 0.3476 0.0239 -0.0155 0.1320 261 LEU A C 1930 O O . LEU A 261 ? 0.2421 0.3548 0.3527 0.0316 -0.0168 0.1388 261 LEU A O 1931 C CB . LEU A 261 ? 0.2734 0.3583 0.3716 0.0162 -0.0060 0.1441 261 LEU A CB 1932 C CG . LEU A 261 ? 0.2870 0.3745 0.3795 0.0063 -0.0032 0.1553 261 LEU A CG 1933 C CD1 . LEU A 261 ? 0.3000 0.3526 0.3963 -0.0007 0.0007 0.1558 261 LEU A CD1 1934 C CD2 . LEU A 261 ? 0.2781 0.3928 0.3610 0.0012 -0.0016 0.1460 261 LEU A CD2 1935 N N . ALA A 262 ? 0.2307 0.3487 0.3175 0.0194 -0.0156 0.1136 262 ALA A N 1936 C CA . ALA A 262 ? 0.2192 0.3343 0.3067 0.0197 -0.0185 0.0988 262 ALA A CA 1937 C C . ALA A 262 ? 0.2101 0.3100 0.2935 0.0178 -0.0137 0.0818 262 ALA A C 1938 O O . ALA A 262 ? 0.2034 0.3056 0.2794 0.0162 -0.0095 0.0799 262 ALA A O 1939 C CB . ALA A 262 ? 0.2263 0.3619 0.2983 0.0147 -0.0264 0.0955 262 ALA A CB 1940 N N . CYS A 263 ? 0.2059 0.2943 0.2952 0.0185 -0.0141 0.0717 263 CYS A N 1941 C CA . CYS A 263 ? 0.2033 0.2804 0.2873 0.0171 -0.0113 0.0568 263 CYS A CA 1942 C C . CYS A 263 ? 0.2074 0.2860 0.2783 0.0146 -0.0163 0.0460 263 CYS A C 1943 O O . CYS A 263 ? 0.2021 0.2844 0.2774 0.0118 -0.0216 0.0471 263 CYS A O 1944 C CB . CYS A 263 ? 0.2020 0.2620 0.2978 0.0176 -0.0082 0.0533 263 CYS A CB 1945 S SG . CYS A 263 ? 0.2059 0.2564 0.2967 0.0159 -0.0061 0.0393 263 CYS A SG 1946 N N . ARG A 264 ? 0.2150 0.2903 0.2691 0.0156 -0.0140 0.0365 264 ARG A N 1947 C CA . ARG A 264 ? 0.2355 0.3010 0.2700 0.0127 -0.0177 0.0240 264 ARG A CA 1948 C C . ARG A 264 ? 0.2273 0.2741 0.2611 0.0166 -0.0136 0.0137 264 ARG A C 1949 O O . ARG A 264 ? 0.2212 0.2696 0.2592 0.0236 -0.0068 0.0143 264 ARG A O 1950 C CB . ARG A 264 ? 0.2675 0.3374 0.2762 0.0135 -0.0165 0.0201 264 ARG A CB 1951 C CG . ARG A 264 ? 0.3056 0.3552 0.2862 0.0086 -0.0203 0.0050 264 ARG A CG 1952 C CD . ARG A 264 ? 0.3492 0.3954 0.2974 0.0120 -0.0159 -0.0027 264 ARG A CD 1953 N NE . ARG A 264 ? 0.3683 0.4340 0.3054 0.0026 -0.0230 0.0042 264 ARG A NE 1954 C CZ . ARG A 264 ? 0.4065 0.4661 0.3157 -0.0106 -0.0322 -0.0025 264 ARG A CZ 1955 N NH1 . ARG A 264 ? 0.4386 0.4667 0.3246 -0.0181 -0.0358 -0.0182 264 ARG A NH1 1956 N NH2 . ARG A 264 ? 0.4121 0.4973 0.3147 -0.0186 -0.0390 0.0078 264 ARG A NH2 1957 N N . VAL A 265 ? 0.2310 0.2635 0.2599 0.0109 -0.0186 0.0066 265 VAL A N 1958 C CA . VAL A 265 ? 0.2338 0.2467 0.2608 0.0136 -0.0162 -0.0011 265 VAL A CA 1959 C C . VAL A 265 ? 0.2668 0.2557 0.2661 0.0101 -0.0191 -0.0127 265 VAL A C 1960 O O . VAL A 265 ? 0.2735 0.2603 0.2633 -0.0024 -0.0274 -0.0142 265 VAL A O 1961 C CB . VAL A 265 ? 0.2170 0.2299 0.2627 0.0084 -0.0187 0.0023 265 VAL A CB 1962 C CG1 . VAL A 265 ? 0.2225 0.2164 0.2646 0.0101 -0.0172 -0.0037 265 VAL A CG1 1963 C CG2 . VAL A 265 ? 0.1987 0.2254 0.2651 0.0115 -0.0149 0.0113 265 VAL A CG2 1964 N N . LYS A 266 ? 0.2865 0.2567 0.2720 0.0212 -0.0122 -0.0199 266 LYS A N 1965 C CA . LYS A 266 ? 0.3284 0.2631 0.2832 0.0201 -0.0130 -0.0323 266 LYS A CA 1966 C C . LYS A 266 ? 0.3236 0.2390 0.2849 0.0240 -0.0117 -0.0327 266 LYS A C 1967 O O . LYS A 266 ? 0.3030 0.2319 0.2841 0.0351 -0.0060 -0.0260 266 LYS A O 1968 C CB . LYS A 266 ? 0.3664 0.2896 0.2950 0.0345 -0.0035 -0.0403 266 LYS A CB 1969 C CG . LYS A 266 ? 0.3747 0.3207 0.2953 0.0326 -0.0030 -0.0384 266 LYS A CG 1970 C CD . LYS A 266 ? 0.4079 0.3478 0.3055 0.0507 0.0101 -0.0449 266 LYS A CD 1971 C CE . LYS A 266 ? 0.4199 0.3818 0.3040 0.0474 0.0107 -0.0432 266 LYS A CE 1972 N NZ . LYS A 266 ? 0.4521 0.3974 0.3060 0.0285 -0.0002 -0.0519 266 LYS A NZ 1973 N N . HIS A 267 ? 0.3428 0.2289 0.2875 0.0123 -0.0181 -0.0386 267 HIS A N 1974 C CA . HIS A 267 ? 0.3462 0.2103 0.2932 0.0148 -0.0174 -0.0376 267 HIS A CA 1975 C C . HIS A 267 ? 0.3928 0.2113 0.3070 0.0034 -0.0226 -0.0470 267 HIS A C 1976 O O . HIS A 267 ? 0.4091 0.2241 0.3089 -0.0158 -0.0315 -0.0510 267 HIS A O 1977 C CB . HIS A 267 ? 0.3064 0.1959 0.2842 0.0060 -0.0218 -0.0272 267 HIS A CB 1978 C CG . HIS A 267 ? 0.3101 0.1842 0.2920 0.0091 -0.0207 -0.0237 267 HIS A CG 1979 N ND1 . HIS A 267 ? 0.3254 0.1799 0.3000 -0.0054 -0.0272 -0.0231 267 HIS A ND1 1980 C CD2 . HIS A 267 ? 0.3017 0.1796 0.2937 0.0241 -0.0147 -0.0184 267 HIS A CD2 1981 C CE1 . HIS A 267 ? 0.3254 0.1698 0.3045 0.0012 -0.0248 -0.0179 267 HIS A CE1 1982 N NE2 . HIS A 267 ? 0.3112 0.1709 0.3013 0.0194 -0.0176 -0.0148 267 HIS A NE2 1983 N N . SER A 268 ? 0.4202 0.2042 0.3227 0.0143 -0.0177 -0.0489 268 SER A N 1984 C CA . SER A 268 ? 0.4758 0.2038 0.3421 0.0052 -0.0211 -0.0578 268 SER A CA 1985 C C . SER A 268 ? 0.4805 0.2063 0.3457 -0.0259 -0.0352 -0.0554 268 SER A C 1986 O O . SER A 268 ? 0.5285 0.2158 0.3598 -0.0433 -0.0418 -0.0642 268 SER A O 1987 C CB . SER A 268 ? 0.4949 0.1932 0.3592 0.0236 -0.0138 -0.0538 268 SER A CB 1988 O OG . SER A 268 ? 0.4479 0.1808 0.3486 0.0226 -0.0161 -0.0394 268 SER A OG 1989 N N . SER A 269 ? 0.4353 0.2019 0.3361 -0.0333 -0.0392 -0.0429 269 SER A N 1990 C CA . SER A 269 ? 0.4340 0.2124 0.3418 -0.0604 -0.0505 -0.0365 269 SER A CA 1991 C C . SER A 269 ? 0.4390 0.2432 0.3453 -0.0792 -0.0596 -0.0371 269 SER A C 1992 O O . SER A 269 ? 0.4442 0.2586 0.3529 -0.1036 -0.0698 -0.0311 269 SER A O 1993 C CB . SER A 269 ? 0.3820 0.2011 0.3281 -0.0580 -0.0487 -0.0233 269 SER A CB 1994 O OG . SER A 269 ? 0.3357 0.1960 0.3056 -0.0472 -0.0444 -0.0206 269 SER A OG 1995 N N . LEU A 270 ? 0.4385 0.2588 0.3432 -0.0687 -0.0561 -0.0416 270 LEU A N 1996 C CA . LEU A 270 ? 0.4398 0.2947 0.3493 -0.0834 -0.0645 -0.0378 270 LEU A CA 1997 C C . LEU A 270 ? 0.5006 0.3279 0.3685 -0.1034 -0.0739 -0.0485 270 LEU A C 1998 O O . LEU A 270 ? 0.4992 0.3580 0.3688 -0.1168 -0.0824 -0.0441 270 LEU A O 1999 C CB . LEU A 270 ? 0.4023 0.2922 0.3322 -0.0644 -0.0572 -0.0340 270 LEU A CB 2000 C CG . LEU A 270 ? 0.3544 0.2744 0.3232 -0.0510 -0.0504 -0.0232 270 LEU A CG 2001 C CD1 . LEU A 270 ? 0.3325 0.2781 0.3147 -0.0359 -0.0441 -0.0199 270 LEU A CD1 2002 C CD2 . LEU A 270 ? 0.3364 0.2864 0.3299 -0.0646 -0.0563 -0.0114 270 LEU A CD2 2003 N N . GLY A 271 ? 0.5642 0.3315 0.3929 -0.1054 -0.0724 -0.0618 271 GLY A N 2004 C CA . GLY A 271 ? 0.6347 0.3624 0.4137 -0.1272 -0.0812 -0.0753 271 GLY A CA 2005 C C . GLY A 271 ? 0.6507 0.3897 0.4096 -0.1231 -0.0801 -0.0834 271 GLY A C 2006 O O . GLY A 271 ? 0.6847 0.4242 0.4173 -0.1493 -0.0928 -0.0871 271 GLY A O 2007 N N . GLY A 272 ? 0.6267 0.3784 0.3977 -0.0924 -0.0657 -0.0844 272 GLY A N 2008 C CA . GLY A 272 ? 0.6334 0.4022 0.3892 -0.0858 -0.0625 -0.0893 272 GLY A CA 2009 C C . GLY A 272 ? 0.5838 0.4195 0.3751 -0.0913 -0.0694 -0.0728 272 GLY A C 2010 O O . GLY A 272 ? 0.5939 0.4470 0.3746 -0.0861 -0.0672 -0.0740 272 GLY A O 2011 N N . GLN A 273 ? 0.5345 0.4071 0.3666 -0.1000 -0.0766 -0.0566 273 GLN A N 2012 C CA . GLN A 273 ? 0.4882 0.4207 0.3536 -0.1037 -0.0827 -0.0392 273 GLN A CA 2013 C C . GLN A 273 ? 0.4241 0.3819 0.3315 -0.0787 -0.0709 -0.0288 273 GLN A C 2014 O O . GLN A 273 ? 0.3992 0.3669 0.3354 -0.0769 -0.0696 -0.0210 273 GLN A O 2015 C CB . GLN A 273 ? 0.4839 0.4431 0.3654 -0.1293 -0.0975 -0.0269 273 GLN A CB 2016 N N . ASP A 274 ? 0.4059 0.3732 0.3137 -0.0614 -0.0622 -0.0288 274 ASP A N 2017 C CA . ASP A 274 ? 0.3600 0.3458 0.3016 -0.0409 -0.0515 -0.0201 274 ASP A CA 2018 C C . ASP A 274 ? 0.3172 0.3423 0.2962 -0.0432 -0.0555 -0.0027 274 ASP A C 2019 O O . ASP A 274 ? 0.3169 0.3680 0.2987 -0.0552 -0.0652 0.0064 274 ASP A O 2020 C CB . ASP A 274 ? 0.3654 0.3581 0.2986 -0.0266 -0.0429 -0.0209 274 ASP A CB 2021 C CG . ASP A 274 ? 0.4074 0.3644 0.3053 -0.0176 -0.0346 -0.0373 274 ASP A CG 2022 O OD1 . ASP A 274 ? 0.4332 0.3540 0.3144 -0.0198 -0.0345 -0.0479 274 ASP A OD1 2023 O OD2 . ASP A 274 ? 0.4208 0.3857 0.3072 -0.0071 -0.0270 -0.0384 274 ASP A OD2 2024 N N . ILE A 275 ? 0.2797 0.3091 0.2860 -0.0313 -0.0479 0.0023 275 ILE A N 2025 C CA . ILE A 275 ? 0.2513 0.3111 0.2892 -0.0272 -0.0473 0.0175 275 ILE A CA 2026 C C . ILE A 275 ? 0.2412 0.3141 0.2820 -0.0171 -0.0432 0.0244 275 ILE A C 2027 O O . ILE A 275 ? 0.2395 0.2996 0.2720 -0.0086 -0.0360 0.0186 275 ILE A O 2028 C CB . ILE A 275 ? 0.2322 0.2861 0.2910 -0.0190 -0.0398 0.0184 275 ILE A CB 2029 C CG1 . ILE A 275 ? 0.2417 0.2864 0.2983 -0.0302 -0.0440 0.0145 275 ILE A CG1 2030 C CG2 . ILE A 275 ? 0.2156 0.2921 0.3012 -0.0108 -0.0358 0.0319 275 ILE A CG2 2031 C CD1 . ILE A 275 ? 0.2318 0.2650 0.2995 -0.0236 -0.0367 0.0123 275 ILE A CD1 2032 N N . ILE A 276 ? 0.2342 0.3351 0.2869 -0.0185 -0.0479 0.0387 276 ILE A N 2033 C CA . ILE A 276 ? 0.2298 0.3422 0.2897 -0.0086 -0.0434 0.0494 276 ILE A CA 2034 C C . ILE A 276 ? 0.2131 0.3435 0.3025 -0.0009 -0.0417 0.0661 276 ILE A C 2035 O O . ILE A 276 ? 0.2153 0.3706 0.3150 -0.0052 -0.0488 0.0767 276 ILE A O 2036 C CB . ILE A 276 ? 0.2547 0.3812 0.2936 -0.0147 -0.0496 0.0526 276 ILE A CB 2037 C CG1 . ILE A 276 ? 0.2821 0.3857 0.2862 -0.0198 -0.0488 0.0340 276 ILE A CG1 2038 C CG2 . ILE A 276 ? 0.2489 0.3855 0.2958 -0.0048 -0.0440 0.0654 276 ILE A CG2 2039 C CD1 . ILE A 276 ? 0.3164 0.4307 0.2917 -0.0292 -0.0557 0.0336 276 ILE A CD1 2040 N N . LEU A 277 ? 0.1988 0.3159 0.3003 0.0102 -0.0321 0.0686 277 LEU A N 2041 C CA . LEU A 277 ? 0.1932 0.3168 0.3169 0.0211 -0.0275 0.0834 277 LEU A CA 2042 C C . LEU A 277 ? 0.2000 0.3240 0.3233 0.0268 -0.0253 0.0957 277 LEU A C 2043 O O . LEU A 277 ? 0.1959 0.3067 0.3071 0.0243 -0.0223 0.0899 277 LEU A O 2044 C CB . LEU A 277 ? 0.1874 0.2873 0.3192 0.0272 -0.0180 0.0760 277 LEU A CB 2045 C CG . LEU A 277 ? 0.1829 0.2803 0.3139 0.0210 -0.0192 0.0645 277 LEU A CG 2046 C CD1 . LEU A 277 ? 0.1844 0.2605 0.3209 0.0272 -0.0094 0.0588 277 LEU A CD1 2047 C CD2 . LEU A 277 ? 0.1830 0.3098 0.3247 0.0172 -0.0257 0.0731 277 LEU A CD2 2048 N N . TYR A 278 ? 0.2069 0.3480 0.3447 0.0351 -0.0262 0.1147 278 TYR A N 2049 C CA . TYR A 278 ? 0.2201 0.3620 0.3584 0.0407 -0.0249 0.1309 278 TYR A CA 2050 C C . TYR A 278 ? 0.2336 0.3485 0.3843 0.0546 -0.0141 0.1388 278 TYR A C 2051 O O . TYR A 278 ? 0.2335 0.3500 0.4001 0.0667 -0.0097 0.1449 278 TYR A O 2052 C CB . TYR A 278 ? 0.2291 0.4094 0.3720 0.0404 -0.0348 0.1497 278 TYR A CB 2053 C CG . TYR A 278 ? 0.2319 0.4304 0.3533 0.0237 -0.0454 0.1398 278 TYR A CG 2054 C CD1 . TYR A 278 ? 0.2301 0.4416 0.3491 0.0133 -0.0529 0.1306 278 TYR A CD1 2055 C CD2 . TYR A 278 ? 0.2445 0.4423 0.3440 0.0172 -0.0468 0.1377 278 TYR A CD2 2056 C CE1 . TYR A 278 ? 0.2420 0.4594 0.3341 -0.0034 -0.0621 0.1190 278 TYR A CE1 2057 C CE2 . TYR A 278 ? 0.2544 0.4613 0.3275 0.0034 -0.0543 0.1256 278 TYR A CE2 2058 C CZ . TYR A 278 ? 0.2560 0.4686 0.3238 -0.0070 -0.0620 0.1153 278 TYR A CZ 2059 O OH . TYR A 278 ? 0.2807 0.4920 0.3162 -0.0216 -0.0688 0.1013 278 TYR A OH 2060 N N . TRP A 279 ? 0.2479 0.3377 0.3899 0.0527 -0.0094 0.1395 279 TRP A N 2061 C CA . TRP A 279 ? 0.2779 0.3322 0.4243 0.0626 0.0002 0.1460 279 TRP A CA 2062 C C . TRP A 279 ? 0.2987 0.3602 0.4571 0.0779 0.0011 0.1711 279 TRP A C 2063 O O . TRP A 279 ? 0.2976 0.3889 0.4567 0.0759 -0.0067 0.1861 279 TRP A O 2064 C CB . TRP A 279 ? 0.2962 0.3234 0.4286 0.0511 0.0030 0.1414 279 TRP A CB 2065 C CG . TRP A 279 ? 0.3386 0.3208 0.4683 0.0561 0.0119 0.1453 279 TRP A CG 2066 C CD1 . TRP A 279 ? 0.3766 0.3381 0.5036 0.0589 0.0143 0.1630 279 TRP A CD1 2067 C CD2 . TRP A 279 ? 0.3579 0.3057 0.4835 0.0584 0.0198 0.1310 279 TRP A CD2 2068 N NE1 . TRP A 279 ? 0.4139 0.3243 0.5331 0.0626 0.0235 0.1596 279 TRP A NE1 2069 C CE2 . TRP A 279 ? 0.4001 0.3023 0.5172 0.0620 0.0271 0.1390 279 TRP A CE2 2070 C CE3 . TRP A 279 ? 0.3473 0.2965 0.4729 0.0569 0.0214 0.1125 279 TRP A CE3 2071 C CZ2 . TRP A 279 ? 0.4316 0.2873 0.5366 0.0640 0.0364 0.1267 279 TRP A CZ2 2072 C CZ3 . TRP A 279 ? 0.3723 0.2813 0.4884 0.0591 0.0304 0.1019 279 TRP A CZ3 2073 C CH2 . TRP A 279 ? 0.4146 0.2766 0.5190 0.0624 0.0380 0.1079 279 TRP A CH2 2074 N N . ILE B 1 ? 0.3630 0.5368 0.6141 -0.0334 -0.0880 0.0342 1 ILE B N 2075 C CA . ILE B 1 ? 0.3610 0.5295 0.6316 -0.0478 -0.0900 0.0312 1 ILE B CA 2076 C C . ILE B 1 ? 0.3556 0.4960 0.5953 -0.0488 -0.0840 0.0257 1 ILE B C 2077 O O . ILE B 1 ? 0.3554 0.4845 0.5667 -0.0409 -0.0725 0.0289 1 ILE B O 2078 C CB . ILE B 1 ? 0.3493 0.5354 0.6542 -0.0550 -0.0774 0.0451 1 ILE B CB 2079 N N . GLN B 2 ? 0.3570 0.4864 0.6053 -0.0582 -0.0930 0.0167 2 GLN B N 2080 C CA . GLN B 2 ? 0.3582 0.4630 0.5822 -0.0590 -0.0879 0.0106 2 GLN B CA 2081 C C . GLN B 2 ? 0.3366 0.4369 0.5683 -0.0635 -0.0707 0.0236 2 GLN B C 2082 O O . GLN B 2 ? 0.3325 0.4470 0.5966 -0.0708 -0.0673 0.0348 2 GLN B O 2083 C CB . GLN B 2 ? 0.3795 0.4737 0.6123 -0.0653 -0.1050 -0.0057 2 GLN B CB 2084 C CG . GLN B 2 ? 0.4038 0.5028 0.6185 -0.0574 -0.1219 -0.0215 2 GLN B CG 2085 C CD . GLN B 2 ? 0.4307 0.5175 0.6448 -0.0592 -0.1386 -0.0429 2 GLN B CD 2086 O OE1 . GLN B 2 ? 0.4345 0.5131 0.6812 -0.0699 -0.1458 -0.0468 2 GLN B OE1 2087 N NE2 . GLN B 2 ? 0.4513 0.5379 0.6292 -0.0477 -0.1453 -0.0568 2 GLN B NE2 2088 N N . LYS B 3 ? 0.3210 0.4047 0.5231 -0.0586 -0.0600 0.0231 3 LYS B N 2089 C CA . LYS B 3 ? 0.3061 0.3850 0.5105 -0.0612 -0.0454 0.0333 3 LYS B CA 2090 C C . LYS B 3 ? 0.2977 0.3538 0.4859 -0.0627 -0.0460 0.0250 3 LYS B C 2091 O O . LYS B 3 ? 0.2933 0.3392 0.4544 -0.0566 -0.0484 0.0146 3 LYS B O 2092 C CB . LYS B 3 ? 0.3061 0.3906 0.4933 -0.0516 -0.0314 0.0407 3 LYS B CB 2093 C CG . LYS B 3 ? 0.3137 0.4228 0.5192 -0.0477 -0.0296 0.0485 3 LYS B CG 2094 C CD . LYS B 3 ? 0.3221 0.4344 0.5114 -0.0359 -0.0180 0.0519 3 LYS B CD 2095 C CE . LYS B 3 ? 0.3302 0.4710 0.5421 -0.0309 -0.0138 0.0596 3 LYS B CE 2096 N NZ . LYS B 3 ? 0.3375 0.4813 0.5355 -0.0171 -0.0042 0.0594 3 LYS B NZ 2097 N N . THR B 4 ? 0.2853 0.3358 0.4917 -0.0703 -0.0434 0.0313 4 THR B N 2098 C CA . THR B 4 ? 0.2858 0.3149 0.4849 -0.0720 -0.0462 0.0233 4 THR B CA 2099 C C . THR B 4 ? 0.2694 0.2905 0.4408 -0.0652 -0.0326 0.0259 4 THR B C 2100 O O . THR B 4 ? 0.2559 0.2859 0.4274 -0.0636 -0.0207 0.0386 4 THR B O 2101 C CB . THR B 4 ? 0.2916 0.3168 0.5262 -0.0831 -0.0506 0.0318 4 THR B CB 2102 O OG1 . THR B 4 ? 0.2996 0.3315 0.5638 -0.0904 -0.0657 0.0274 4 THR B OG1 2103 C CG2 . THR B 4 ? 0.3043 0.3059 0.5348 -0.0835 -0.0553 0.0229 4 THR B CG2 2104 N N . PRO B 5 ? 0.2718 0.2787 0.4207 -0.0605 -0.0347 0.0130 5 PRO B N 2105 C CA . PRO B 5 ? 0.2642 0.2651 0.3915 -0.0550 -0.0228 0.0155 5 PRO B CA 2106 C C . PRO B 5 ? 0.2668 0.2619 0.4046 -0.0581 -0.0174 0.0243 5 PRO B C 2107 O O . PRO B 5 ? 0.2675 0.2542 0.4248 -0.0638 -0.0247 0.0240 5 PRO B O 2108 C CB . PRO B 5 ? 0.2719 0.2637 0.3786 -0.0501 -0.0267 0.0008 5 PRO B CB 2109 C CG . PRO B 5 ? 0.2906 0.2797 0.4091 -0.0525 -0.0415 -0.0114 5 PRO B CG 2110 C CD . PRO B 5 ? 0.2863 0.2865 0.4275 -0.0583 -0.0473 -0.0046 5 PRO B CD 2111 N N . GLN B 6 ? 0.2607 0.2600 0.3864 -0.0537 -0.0061 0.0318 6 GLN B N 2112 C CA . GLN B 6 ? 0.2697 0.2648 0.3968 -0.0535 -0.0005 0.0393 6 GLN B CA 2113 C C . GLN B 6 ? 0.2570 0.2411 0.3638 -0.0480 0.0012 0.0293 6 GLN B C 2114 O O . GLN B 6 ? 0.2478 0.2328 0.3386 -0.0441 0.0030 0.0223 6 GLN B O 2115 C CB . GLN B 6 ? 0.2782 0.2902 0.4058 -0.0505 0.0094 0.0528 6 GLN B CB 2116 C CG . GLN B 6 ? 0.2966 0.3260 0.4465 -0.0552 0.0093 0.0638 6 GLN B CG 2117 C CD . GLN B 6 ? 0.3243 0.3497 0.5034 -0.0658 0.0017 0.0712 6 GLN B CD 2118 O OE1 . GLN B 6 ? 0.3507 0.3785 0.5487 -0.0720 -0.0069 0.0686 6 GLN B OE1 2119 N NE2 . GLN B 6 ? 0.3391 0.3576 0.5243 -0.0679 0.0034 0.0807 6 GLN B NE2 2120 N N . ILE B 7 ? 0.2589 0.2334 0.3694 -0.0482 0.0003 0.0299 7 ILE B N 2121 C CA . ILE B 7 ? 0.2564 0.2223 0.3530 -0.0433 0.0008 0.0195 7 ILE B CA 2122 C C . ILE B 7 ? 0.2535 0.2192 0.3484 -0.0402 0.0057 0.0271 7 ILE B C 2123 O O . ILE B 7 ? 0.2575 0.2208 0.3660 -0.0425 0.0040 0.0374 7 ILE B O 2124 C CB . ILE B 7 ? 0.2700 0.2237 0.3735 -0.0436 -0.0085 0.0073 7 ILE B CB 2125 C CG1 . ILE B 7 ? 0.2774 0.2336 0.3811 -0.0452 -0.0155 -0.0020 7 ILE B CG1 2126 C CG2 . ILE B 7 ? 0.2688 0.2189 0.3591 -0.0371 -0.0062 -0.0029 7 ILE B CG2 2127 C CD1 . ILE B 7 ? 0.2977 0.2428 0.4112 -0.0445 -0.0276 -0.0166 7 ILE B CD1 2128 N N . GLN B 8 ? 0.2435 0.2120 0.3231 -0.0351 0.0106 0.0225 8 GLN B N 2129 C CA . GLN B 8 ? 0.2425 0.2121 0.3185 -0.0307 0.0132 0.0264 8 GLN B CA 2130 C C . GLN B 8 ? 0.2325 0.1979 0.3018 -0.0273 0.0128 0.0149 8 GLN B C 2131 O O . GLN B 8 ? 0.2178 0.1858 0.2797 -0.0273 0.0149 0.0078 8 GLN B O 2132 C CB . GLN B 8 ? 0.2488 0.2309 0.3164 -0.0270 0.0188 0.0320 8 GLN B CB 2133 C CG . GLN B 8 ? 0.2583 0.2507 0.3338 -0.0290 0.0211 0.0447 8 GLN B CG 2134 C CD . GLN B 8 ? 0.2643 0.2717 0.3301 -0.0228 0.0266 0.0459 8 GLN B CD 2135 O OE1 . GLN B 8 ? 0.2720 0.2820 0.3362 -0.0226 0.0272 0.0409 8 GLN B OE1 2136 N NE2 . GLN B 8 ? 0.2679 0.2860 0.3268 -0.0161 0.0295 0.0514 8 GLN B NE2 2137 N N . VAL B 9 ? 0.2313 0.1917 0.3056 -0.0243 0.0100 0.0149 9 VAL B N 2138 C CA . VAL B 9 ? 0.2296 0.1888 0.3021 -0.0203 0.0094 0.0042 9 VAL B CA 2139 C C . VAL B 9 ? 0.2273 0.1913 0.2980 -0.0154 0.0098 0.0077 9 VAL B C 2140 O O . VAL B 9 ? 0.2348 0.1968 0.3097 -0.0134 0.0073 0.0174 9 VAL B O 2141 C CB . VAL B 9 ? 0.2400 0.1887 0.3228 -0.0188 0.0031 -0.0028 9 VAL B CB 2142 C CG1 . VAL B 9 ? 0.2428 0.1953 0.3246 -0.0127 0.0037 -0.0146 9 VAL B CG1 2143 C CG2 . VAL B 9 ? 0.2443 0.1894 0.3286 -0.0226 0.0001 -0.0082 9 VAL B CG2 2144 N N . TYR B 10 ? 0.2184 0.1898 0.2846 -0.0137 0.0122 0.0009 10 TYR B N 2145 C CA . TYR B 10 ? 0.2167 0.1950 0.2812 -0.0089 0.0107 0.0016 10 TYR B CA 2146 C C . TYR B 10 ? 0.2090 0.1937 0.2780 -0.0084 0.0113 -0.0080 10 TYR B C 2147 O O . TYR B 10 ? 0.2043 0.1908 0.2743 -0.0126 0.0152 -0.0121 10 TYR B O 2148 C CB . TYR B 10 ? 0.2200 0.2046 0.2757 -0.0081 0.0121 0.0059 10 TYR B CB 2149 C CG . TYR B 10 ? 0.2146 0.1992 0.2677 -0.0126 0.0153 0.0023 10 TYR B CG 2150 C CD1 . TYR B 10 ? 0.2150 0.1956 0.2678 -0.0169 0.0176 0.0063 10 TYR B CD1 2151 C CD2 . TYR B 10 ? 0.2145 0.2025 0.2680 -0.0122 0.0145 -0.0044 10 TYR B CD2 2152 C CE1 . TYR B 10 ? 0.2112 0.1920 0.2619 -0.0198 0.0197 0.0045 10 TYR B CE1 2153 C CE2 . TYR B 10 ? 0.2109 0.1965 0.2645 -0.0159 0.0164 -0.0055 10 TYR B CE2 2154 C CZ . TYR B 10 ? 0.2111 0.1935 0.2621 -0.0191 0.0193 -0.0005 10 TYR B CZ 2155 O OH . TYR B 10 ? 0.2130 0.1931 0.2642 -0.0216 0.0203 -0.0002 10 TYR B OH 2156 N N . SER B 11 ? 0.2061 0.1966 0.2792 -0.0033 0.0074 -0.0103 11 SER B N 2157 C CA . SER B 11 ? 0.2023 0.2023 0.2851 -0.0036 0.0075 -0.0185 11 SER B CA 2158 C C . SER B 11 ? 0.1970 0.2025 0.2806 -0.0059 0.0056 -0.0215 11 SER B C 2159 O O . SER B 11 ? 0.2012 0.2063 0.2759 -0.0024 0.0019 -0.0201 11 SER B O 2160 C CB . SER B 11 ? 0.2065 0.2115 0.2982 0.0034 0.0026 -0.0212 11 SER B CB 2161 O OG . SER B 11 ? 0.2140 0.2214 0.3005 0.0090 -0.0038 -0.0177 11 SER B OG 2162 N N . ARG B 12 ? 0.1898 0.2017 0.2857 -0.0111 0.0078 -0.0255 12 ARG B N 2163 C CA . ARG B 12 ? 0.1907 0.2051 0.2949 -0.0146 0.0038 -0.0295 12 ARG B CA 2164 C C . ARG B 12 ? 0.1974 0.2194 0.3076 -0.0087 -0.0058 -0.0368 12 ARG B C 2165 O O . ARG B 12 ? 0.2040 0.2249 0.3121 -0.0065 -0.0130 -0.0425 12 ARG B O 2166 C CB . ARG B 12 ? 0.1879 0.2085 0.3091 -0.0232 0.0088 -0.0279 12 ARG B CB 2167 C CG . ARG B 12 ? 0.1908 0.2131 0.3306 -0.0284 0.0026 -0.0317 12 ARG B CG 2168 C CD . ARG B 12 ? 0.1951 0.2038 0.3269 -0.0288 -0.0010 -0.0326 12 ARG B CD 2169 N NE . ARG B 12 ? 0.2019 0.2082 0.3547 -0.0332 -0.0097 -0.0385 12 ARG B NE 2170 C CZ . ARG B 12 ? 0.2086 0.2176 0.3685 -0.0283 -0.0218 -0.0511 12 ARG B CZ 2171 N NH1 . ARG B 12 ? 0.2101 0.2264 0.3558 -0.0185 -0.0256 -0.0567 12 ARG B NH1 2172 N NH2 . ARG B 12 ? 0.2207 0.2252 0.4040 -0.0333 -0.0316 -0.0580 12 ARG B NH2 2173 N N . HIS B 13 ? 0.1981 0.2287 0.3160 -0.0048 -0.0072 -0.0380 13 HIS B N 2174 C CA . HIS B 13 ? 0.2063 0.2468 0.3313 0.0014 -0.0174 -0.0447 13 HIS B CA 2175 C C . HIS B 13 ? 0.2113 0.2512 0.3244 0.0114 -0.0197 -0.0399 13 HIS B C 2176 O O . HIS B 13 ? 0.2052 0.2371 0.3127 0.0116 -0.0135 -0.0332 13 HIS B O 2177 C CB . HIS B 13 ? 0.2043 0.2593 0.3564 -0.0028 -0.0178 -0.0492 13 HIS B CB 2178 C CG . HIS B 13 ? 0.2043 0.2605 0.3737 -0.0143 -0.0149 -0.0493 13 HIS B CG 2179 N ND1 . HIS B 13 ? 0.2129 0.2661 0.3915 -0.0175 -0.0244 -0.0561 13 HIS B ND1 2180 C CD2 . HIS B 13 ? 0.2008 0.2618 0.3815 -0.0228 -0.0043 -0.0425 13 HIS B CD2 2181 C CE1 . HIS B 13 ? 0.2122 0.2649 0.4098 -0.0288 -0.0201 -0.0518 13 HIS B CE1 2182 N NE2 . HIS B 13 ? 0.2054 0.2646 0.4034 -0.0323 -0.0071 -0.0420 13 HIS B NE2 2183 N N . PRO B 14 ? 0.2243 0.2727 0.3354 0.0200 -0.0301 -0.0434 14 PRO B N 2184 C CA . PRO B 14 ? 0.2351 0.2832 0.3381 0.0297 -0.0331 -0.0357 14 PRO B CA 2185 C C . PRO B 14 ? 0.2380 0.2859 0.3567 0.0301 -0.0296 -0.0351 14 PRO B C 2186 O O . PRO B 14 ? 0.2303 0.2899 0.3687 0.0278 -0.0298 -0.0431 14 PRO B O 2187 C CB . PRO B 14 ? 0.2461 0.3086 0.3485 0.0391 -0.0460 -0.0416 14 PRO B CB 2188 C CG . PRO B 14 ? 0.2459 0.3131 0.3515 0.0350 -0.0508 -0.0538 14 PRO B CG 2189 C CD . PRO B 14 ? 0.2315 0.2898 0.3489 0.0219 -0.0410 -0.0547 14 PRO B CD 2190 N N . PRO B 15 ? 0.2482 0.2839 0.3606 0.0334 -0.0269 -0.0261 15 PRO B N 2191 C CA . PRO B 15 ? 0.2529 0.2870 0.3798 0.0360 -0.0248 -0.0291 15 PRO B CA 2192 C C . PRO B 15 ? 0.2665 0.3117 0.4067 0.0463 -0.0337 -0.0321 15 PRO B C 2193 O O . PRO B 15 ? 0.2732 0.3185 0.4060 0.0541 -0.0423 -0.0249 15 PRO B O 2194 C CB . PRO B 15 ? 0.2596 0.2742 0.3782 0.0366 -0.0229 -0.0196 15 PRO B CB 2195 C CG . PRO B 15 ? 0.2659 0.2768 0.3680 0.0372 -0.0255 -0.0072 15 PRO B CG 2196 C CD . PRO B 15 ? 0.2577 0.2813 0.3524 0.0342 -0.0256 -0.0133 15 PRO B CD 2197 N N . GLU B 16 ? 0.2693 0.3272 0.4290 0.0470 -0.0311 -0.0418 16 GLU B N 2198 C CA . GLU B 16 ? 0.2871 0.3581 0.4644 0.0576 -0.0388 -0.0462 16 GLU B CA 2199 C C . GLU B 16 ? 0.2851 0.3588 0.4767 0.0615 -0.0324 -0.0535 16 GLU B C 2200 O O . GLU B 16 ? 0.2680 0.3520 0.4650 0.0546 -0.0220 -0.0592 16 GLU B O 2201 C CB . GLU B 16 ? 0.2927 0.3872 0.4855 0.0552 -0.0431 -0.0539 16 GLU B CB 2202 C CG . GLU B 16 ? 0.3105 0.4055 0.4902 0.0531 -0.0513 -0.0525 16 GLU B CG 2203 C CD . GLU B 16 ? 0.3216 0.4389 0.5226 0.0507 -0.0590 -0.0630 16 GLU B CD 2204 O OE1 . GLU B 16 ? 0.3438 0.4613 0.5388 0.0454 -0.0638 -0.0668 16 GLU B OE1 2205 O OE2 . GLU B 16 ? 0.3227 0.4577 0.5486 0.0543 -0.0609 -0.0683 16 GLU B OE2 2206 N N . ASN B 17 ? 0.3015 0.3671 0.4995 0.0738 -0.0388 -0.0531 17 ASN B N 2207 C CA . ASN B 17 ? 0.3068 0.3736 0.5168 0.0804 -0.0340 -0.0634 17 ASN B CA 2208 C C . ASN B 17 ? 0.2958 0.3954 0.5264 0.0817 -0.0278 -0.0743 17 ASN B C 2209 O O . ASN B 17 ? 0.2903 0.4086 0.5344 0.0828 -0.0332 -0.0746 17 ASN B O 2210 C CB . ASN B 17 ? 0.3309 0.3807 0.5485 0.0946 -0.0444 -0.0623 17 ASN B CB 2211 C CG . ASN B 17 ? 0.3426 0.3599 0.5460 0.0914 -0.0479 -0.0508 17 ASN B CG 2212 O OD1 . ASN B 17 ? 0.3345 0.3427 0.5239 0.0804 -0.0407 -0.0487 17 ASN B OD1 2213 N ND2 . ASN B 17 ? 0.3648 0.3657 0.5746 0.1009 -0.0595 -0.0415 17 ASN B ND2 2214 N N . GLY B 18 ? 0.2937 0.4029 0.5265 0.0810 -0.0164 -0.0826 18 GLY B N 2215 C CA . GLY B 18 ? 0.2871 0.4323 0.5397 0.0811 -0.0070 -0.0898 18 GLY B CA 2216 C C . GLY B 18 ? 0.2729 0.4347 0.5290 0.0648 0.0000 -0.0831 18 GLY B C 2217 O O . GLY B 18 ? 0.2668 0.4604 0.5433 0.0627 0.0085 -0.0852 18 GLY B O 2218 N N . LYS B 19 ? 0.2698 0.4117 0.5090 0.0536 -0.0033 -0.0745 19 LYS B N 2219 C CA . LYS B 19 ? 0.2617 0.4141 0.5068 0.0387 0.0004 -0.0693 19 LYS B CA 2220 C C . LYS B 19 ? 0.2521 0.3933 0.4791 0.0282 0.0108 -0.0636 19 LYS B C 2221 O O . LYS B 19 ? 0.2497 0.3649 0.4534 0.0282 0.0086 -0.0609 19 LYS B O 2222 C CB . LYS B 19 ? 0.2687 0.4117 0.5115 0.0359 -0.0129 -0.0669 19 LYS B CB 2223 C CG . LYS B 19 ? 0.2841 0.4409 0.5445 0.0465 -0.0250 -0.0719 19 LYS B CG 2224 C CD . LYS B 19 ? 0.2882 0.4799 0.5839 0.0443 -0.0215 -0.0767 19 LYS B CD 2225 C CE . LYS B 19 ? 0.2997 0.5070 0.6155 0.0521 -0.0363 -0.0819 19 LYS B CE 2226 N NZ . LYS B 19 ? 0.3000 0.5430 0.6547 0.0458 -0.0333 -0.0851 19 LYS B NZ 2227 N N . PRO B 20 ? 0.2420 0.4046 0.4814 0.0194 0.0221 -0.0599 20 PRO B N 2228 C CA . PRO B 20 ? 0.2336 0.3880 0.4573 0.0096 0.0312 -0.0524 20 PRO B CA 2229 C C . PRO B 20 ? 0.2232 0.3509 0.4320 0.0012 0.0239 -0.0474 20 PRO B C 2230 O O . PRO B 20 ? 0.2223 0.3480 0.4412 -0.0023 0.0146 -0.0480 20 PRO B O 2231 C CB . PRO B 20 ? 0.2350 0.4197 0.4830 0.0003 0.0415 -0.0451 20 PRO B CB 2232 C CG . PRO B 20 ? 0.2393 0.4536 0.5105 0.0096 0.0434 -0.0517 20 PRO B CG 2233 C CD . PRO B 20 ? 0.2424 0.4415 0.5123 0.0199 0.0283 -0.0611 20 PRO B CD 2234 N N . ASN B 21 ? 0.2141 0.3237 0.3995 -0.0004 0.0276 -0.0442 21 ASN B N 2235 C CA . ASN B 21 ? 0.2061 0.2916 0.3749 -0.0054 0.0218 -0.0403 21 ASN B CA 2236 C C . ASN B 21 ? 0.2044 0.2841 0.3586 -0.0108 0.0305 -0.0345 21 ASN B C 2237 O O . ASN B 21 ? 0.2013 0.2973 0.3577 -0.0103 0.0401 -0.0333 21 ASN B O 2238 C CB . ASN B 21 ? 0.2086 0.2762 0.3631 0.0037 0.0134 -0.0432 21 ASN B CB 2239 C CG . ASN B 21 ? 0.2078 0.2598 0.3501 0.0015 0.0058 -0.0397 21 ASN B CG 2240 O OD1 . ASN B 21 ? 0.2061 0.2520 0.3425 -0.0057 0.0077 -0.0364 21 ASN B OD1 2241 N ND2 . ASN B 21 ? 0.2099 0.2570 0.3480 0.0096 -0.0026 -0.0400 21 ASN B ND2 2242 N N . ILE B 22 ? 0.1991 0.2590 0.3383 -0.0145 0.0271 -0.0308 22 ILE B N 2243 C CA . ILE B 22 ? 0.2015 0.2538 0.3257 -0.0184 0.0328 -0.0256 22 ILE B CA 2244 C C . ILE B 22 ? 0.2019 0.2340 0.3083 -0.0148 0.0277 -0.0265 22 ILE B C 2245 O O . ILE B 22 ? 0.1978 0.2202 0.3016 -0.0137 0.0209 -0.0261 22 ILE B O 2246 C CB . ILE B 22 ? 0.2003 0.2515 0.3306 -0.0285 0.0342 -0.0175 22 ILE B CB 2247 C CG1 . ILE B 22 ? 0.2047 0.2780 0.3573 -0.0342 0.0407 -0.0122 22 ILE B CG1 2248 C CG2 . ILE B 22 ? 0.2000 0.2413 0.3133 -0.0311 0.0378 -0.0115 22 ILE B CG2 2249 C CD1 . ILE B 22 ? 0.2105 0.2806 0.3802 -0.0449 0.0381 -0.0046 22 ILE B CD1 2250 N N . LEU B 23 ? 0.2071 0.2359 0.3024 -0.0127 0.0308 -0.0277 23 LEU B N 2251 C CA . LEU B 23 ? 0.2132 0.2246 0.2971 -0.0110 0.0260 -0.0275 23 LEU B CA 2252 C C . LEU B 23 ? 0.2121 0.2187 0.2857 -0.0168 0.0285 -0.0219 23 LEU B C 2253 O O . LEU B 23 ? 0.2203 0.2359 0.2900 -0.0182 0.0338 -0.0214 23 LEU B O 2254 C CB . LEU B 23 ? 0.2243 0.2335 0.3076 -0.0037 0.0240 -0.0358 23 LEU B CB 2255 C CG . LEU B 23 ? 0.2294 0.2193 0.3093 -0.0030 0.0168 -0.0345 23 LEU B CG 2256 C CD1 . LEU B 23 ? 0.2296 0.2120 0.3142 -0.0021 0.0118 -0.0275 23 LEU B CD1 2257 C CD2 . LEU B 23 ? 0.2434 0.2287 0.3268 0.0041 0.0125 -0.0457 23 LEU B CD2 2258 N N . ASN B 24 ? 0.2094 0.2048 0.2786 -0.0190 0.0248 -0.0171 24 ASN B N 2259 C CA . ASN B 24 ? 0.2104 0.2010 0.2720 -0.0233 0.0258 -0.0118 24 ASN B CA 2260 C C . ASN B 24 ? 0.2148 0.1970 0.2714 -0.0226 0.0226 -0.0115 24 ASN B C 2261 O O . ASN B 24 ? 0.2148 0.1908 0.2751 -0.0203 0.0186 -0.0109 24 ASN B O 2262 C CB . ASN B 24 ? 0.2086 0.1960 0.2712 -0.0245 0.0237 -0.0082 24 ASN B CB 2263 C CG . ASN B 24 ? 0.2119 0.2051 0.2843 -0.0267 0.0241 -0.0096 24 ASN B CG 2264 O OD1 . ASN B 24 ? 0.2166 0.2167 0.2945 -0.0304 0.0284 -0.0075 24 ASN B OD1 2265 N ND2 . ASN B 24 ? 0.2133 0.2056 0.2891 -0.0242 0.0191 -0.0126 24 ASN B ND2 2266 N N . CYS B 25 ? 0.2196 0.2023 0.2701 -0.0249 0.0235 -0.0105 25 CYS B N 2267 C CA . CYS B 25 ? 0.2253 0.2015 0.2748 -0.0259 0.0191 -0.0099 25 CYS B CA 2268 C C . CYS B 25 ? 0.2209 0.1984 0.2663 -0.0291 0.0202 -0.0033 25 CYS B C 2269 O O . CYS B 25 ? 0.2288 0.2114 0.2681 -0.0298 0.0224 -0.0025 25 CYS B O 2270 C CB . CYS B 25 ? 0.2399 0.2175 0.2866 -0.0233 0.0161 -0.0191 25 CYS B CB 2271 S SG . CYS B 25 ? 0.2532 0.2227 0.3044 -0.0262 0.0078 -0.0194 25 CYS B SG 2272 N N . TYR B 26 ? 0.2146 0.1894 0.2636 -0.0298 0.0191 0.0023 26 TYR B N 2273 C CA . TYR B 26 ? 0.2124 0.1895 0.2596 -0.0306 0.0200 0.0075 26 TYR B CA 2274 C C . TYR B 26 ? 0.2145 0.1923 0.2660 -0.0326 0.0165 0.0100 26 TYR B C 2275 O O . TYR B 26 ? 0.2172 0.1940 0.2767 -0.0336 0.0148 0.0132 26 TYR B O 2276 C CB . TYR B 26 ? 0.2103 0.1892 0.2588 -0.0276 0.0215 0.0100 26 TYR B CB 2277 C CG . TYR B 26 ? 0.2159 0.1971 0.2638 -0.0257 0.0218 0.0122 26 TYR B CG 2278 C CD1 . TYR B 26 ? 0.2209 0.1993 0.2679 -0.0270 0.0214 0.0125 26 TYR B CD1 2279 C CD2 . TYR B 26 ? 0.2192 0.2071 0.2680 -0.0213 0.0227 0.0147 26 TYR B CD2 2280 C CE1 . TYR B 26 ? 0.2270 0.2051 0.2760 -0.0239 0.0202 0.0140 26 TYR B CE1 2281 C CE2 . TYR B 26 ? 0.2237 0.2147 0.2731 -0.0171 0.0224 0.0142 26 TYR B CE2 2282 C CZ . TYR B 26 ? 0.2256 0.2097 0.2762 -0.0185 0.0204 0.0132 26 TYR B CZ 2283 O OH . TYR B 26 ? 0.2450 0.2294 0.2987 -0.0134 0.0186 0.0124 26 TYR B OH 2284 N N . VAL B 27 ? 0.2134 0.1938 0.2616 -0.0335 0.0147 0.0100 27 VAL B N 2285 C CA . VAL B 27 ? 0.2208 0.2037 0.2753 -0.0357 0.0093 0.0105 27 VAL B CA 2286 C C . VAL B 27 ? 0.2195 0.2087 0.2759 -0.0347 0.0099 0.0167 27 VAL B C 2287 O O . VAL B 27 ? 0.2158 0.2053 0.2648 -0.0324 0.0112 0.0179 27 VAL B O 2288 C CB . VAL B 27 ? 0.2296 0.2129 0.2780 -0.0354 0.0040 0.0023 27 VAL B CB 2289 C CG1 . VAL B 27 ? 0.2362 0.2211 0.2950 -0.0381 -0.0047 0.0000 27 VAL B CG1 2290 C CG2 . VAL B 27 ? 0.2360 0.2147 0.2821 -0.0336 0.0042 -0.0058 27 VAL B CG2 2291 N N . THR B 28 ? 0.2177 0.2129 0.2864 -0.0362 0.0090 0.0218 28 THR B N 2292 C CA . THR B 28 ? 0.2194 0.2242 0.2924 -0.0331 0.0110 0.0272 28 THR B CA 2293 C C . THR B 28 ? 0.2247 0.2397 0.3134 -0.0365 0.0065 0.0312 28 THR B C 2294 O O . THR B 28 ? 0.2269 0.2399 0.3260 -0.0424 0.0014 0.0303 28 THR B O 2295 C CB . THR B 28 ? 0.2161 0.2261 0.2898 -0.0289 0.0175 0.0309 28 THR B CB 2296 O OG1 . THR B 28 ? 0.2204 0.2337 0.3030 -0.0325 0.0187 0.0365 28 THR B OG1 2297 C CG2 . THR B 28 ? 0.2157 0.2167 0.2777 -0.0254 0.0198 0.0256 28 THR B CG2 2298 N N . GLN B 29 ? 0.2289 0.2550 0.3223 -0.0324 0.0074 0.0349 29 GLN B N 2299 C CA . GLN B 29 ? 0.2373 0.2794 0.3503 -0.0348 0.0052 0.0407 29 GLN B CA 2300 C C . GLN B 29 ? 0.2382 0.2799 0.3593 -0.0403 -0.0056 0.0368 29 GLN B C 2301 O O . GLN B 29 ? 0.2410 0.2923 0.3841 -0.0463 -0.0097 0.0407 29 GLN B O 2302 C CB . GLN B 29 ? 0.2467 0.2990 0.3741 -0.0381 0.0109 0.0500 29 GLN B CB 2303 C CG . GLN B 29 ? 0.2593 0.3219 0.3793 -0.0294 0.0210 0.0537 29 GLN B CG 2304 C CD . GLN B 29 ? 0.2712 0.3527 0.3972 -0.0212 0.0237 0.0550 29 GLN B CD 2305 O OE1 . GLN B 29 ? 0.2818 0.3771 0.4258 -0.0241 0.0207 0.0595 29 GLN B OE1 2306 N NE2 . GLN B 29 ? 0.2886 0.3714 0.4017 -0.0102 0.0283 0.0498 29 GLN B NE2 2307 N N . PHE B 30 ? 0.2374 0.2704 0.3422 -0.0380 -0.0107 0.0296 30 PHE B N 2308 C CA . PHE B 30 ? 0.2412 0.2757 0.3489 -0.0408 -0.0224 0.0230 30 PHE B CA 2309 C C . PHE B 30 ? 0.2455 0.2884 0.3477 -0.0352 -0.0277 0.0239 30 PHE B C 2310 O O . PHE B 30 ? 0.2412 0.2830 0.3336 -0.0289 -0.0223 0.0290 30 PHE B O 2311 C CB . PHE B 30 ? 0.2472 0.2692 0.3404 -0.0416 -0.0259 0.0128 30 PHE B CB 2312 C CG . PHE B 30 ? 0.2472 0.2632 0.3159 -0.0361 -0.0198 0.0123 30 PHE B CG 2313 C CD1 . PHE B 30 ? 0.2395 0.2472 0.3025 -0.0357 -0.0103 0.0146 30 PHE B CD1 2314 C CD2 . PHE B 30 ? 0.2567 0.2771 0.3093 -0.0314 -0.0242 0.0107 30 PHE B CD2 2315 C CE1 . PHE B 30 ? 0.2445 0.2481 0.2907 -0.0324 -0.0052 0.0154 30 PHE B CE1 2316 C CE2 . PHE B 30 ? 0.2620 0.2791 0.2959 -0.0277 -0.0177 0.0141 30 PHE B CE2 2317 C CZ . PHE B 30 ? 0.2555 0.2639 0.2884 -0.0290 -0.0082 0.0165 30 PHE B CZ 2318 N N . HIS B 31 ? 0.2538 0.3048 0.3654 -0.0373 -0.0398 0.0189 31 HIS B N 2319 C CA . HIS B 31 ? 0.2647 0.3258 0.3712 -0.0315 -0.0482 0.0191 31 HIS B CA 2320 C C . HIS B 31 ? 0.2763 0.3428 0.3893 -0.0346 -0.0638 0.0076 31 HIS B C 2321 O O . HIS B 31 ? 0.2666 0.3355 0.4054 -0.0426 -0.0688 0.0046 31 HIS B O 2322 C CB . HIS B 31 ? 0.2599 0.3356 0.3861 -0.0290 -0.0467 0.0277 31 HIS B CB 2323 C CG . HIS B 31 ? 0.2737 0.3594 0.3961 -0.0219 -0.0564 0.0289 31 HIS B CG 2324 N ND1 . HIS B 31 ? 0.2801 0.3619 0.3881 -0.0130 -0.0530 0.0360 31 HIS B ND1 2325 C CD2 . HIS B 31 ? 0.2879 0.3868 0.4195 -0.0222 -0.0710 0.0239 31 HIS B CD2 2326 C CE1 . HIS B 31 ? 0.2912 0.3834 0.3982 -0.0075 -0.0641 0.0374 31 HIS B CE1 2327 N NE2 . HIS B 31 ? 0.2986 0.4027 0.4188 -0.0126 -0.0754 0.0293 31 HIS B NE2 2328 N N . PRO B 32 ? 0.2937 0.3639 0.3859 -0.0283 -0.0727 0.0015 32 PRO B N 2329 C CA . PRO B 32 ? 0.2992 0.3692 0.3645 -0.0195 -0.0679 0.0095 32 PRO B CA 2330 C C . PRO B 32 ? 0.2986 0.3557 0.3422 -0.0187 -0.0562 0.0107 32 PRO B C 2331 O O . PRO B 32 ? 0.2955 0.3441 0.3427 -0.0236 -0.0528 0.0033 32 PRO B O 2332 C CB . PRO B 32 ? 0.3209 0.4041 0.3732 -0.0134 -0.0832 0.0022 32 PRO B CB 2333 C CG . PRO B 32 ? 0.3287 0.4123 0.3924 -0.0183 -0.0947 -0.0156 32 PRO B CG 2334 C CD . PRO B 32 ? 0.3099 0.3872 0.4067 -0.0289 -0.0903 -0.0133 32 PRO B CD 2335 N N . PRO B 33 ? 0.3075 0.3634 0.3321 -0.0130 -0.0502 0.0215 33 PRO B N 2336 C CA . PRO B 33 ? 0.3068 0.3521 0.3182 -0.0140 -0.0381 0.0246 33 PRO B CA 2337 C C . PRO B 33 ? 0.3212 0.3704 0.3130 -0.0122 -0.0384 0.0148 33 PRO B C 2338 O O . PRO B 33 ? 0.3282 0.3708 0.3145 -0.0139 -0.0284 0.0156 33 PRO B O 2339 C CB . PRO B 33 ? 0.3118 0.3550 0.3153 -0.0097 -0.0333 0.0410 33 PRO B CB 2340 C CG . PRO B 33 ? 0.3242 0.3796 0.3250 -0.0037 -0.0443 0.0453 33 PRO B CG 2341 C CD . PRO B 33 ? 0.3177 0.3807 0.3365 -0.0061 -0.0542 0.0332 33 PRO B CD 2342 N N A HIS B 34 ? 0.3388 0.4006 0.3207 -0.0075 -0.0502 0.0045 34 HIS B N 2343 N N B HIS B 34 ? 0.3352 0.3966 0.3179 -0.0078 -0.0502 0.0041 34 HIS B N 2344 C CA A HIS B 34 ? 0.3538 0.4226 0.3163 -0.0027 -0.0518 -0.0088 34 HIS B CA 2345 C CA B HIS B 34 ? 0.3485 0.4172 0.3113 -0.0028 -0.0517 -0.0085 34 HIS B CA 2346 C C A HIS B 34 ? 0.3411 0.3974 0.3186 -0.0081 -0.0515 -0.0232 34 HIS B C 2347 C C B HIS B 34 ? 0.3396 0.3966 0.3164 -0.0077 -0.0522 -0.0241 34 HIS B C 2348 O O A HIS B 34 ? 0.3349 0.3847 0.3358 -0.0138 -0.0597 -0.0301 34 HIS B O 2349 O O B HIS B 34 ? 0.3363 0.3875 0.3353 -0.0128 -0.0616 -0.0326 34 HIS B O 2350 C CB A HIS B 34 ? 0.3798 0.4654 0.3297 0.0050 -0.0677 -0.0210 34 HIS B CB 2351 C CB B HIS B 34 ? 0.3705 0.4566 0.3200 0.0051 -0.0668 -0.0177 34 HIS B CB 2352 C CG A HIS B 34 ? 0.4007 0.4949 0.3319 0.0123 -0.0712 -0.0401 34 HIS B CG 2353 C CG B HIS B 34 ? 0.3748 0.4699 0.3183 0.0089 -0.0690 -0.0005 34 HIS B CG 2354 N ND1 A HIS B 34 ? 0.4194 0.5305 0.3197 0.0218 -0.0635 -0.0355 34 HIS B ND1 2355 N ND1 B HIS B 34 ? 0.3857 0.4884 0.3074 0.0144 -0.0603 0.0177 34 HIS B ND1 2356 C CD2 A HIS B 34 ? 0.4073 0.4962 0.3481 0.0124 -0.0814 -0.0638 34 HIS B CD2 2357 C CD2 B HIS B 34 ? 0.3703 0.4674 0.3307 0.0079 -0.0784 0.0035 34 HIS B CD2 2358 C CE1 A HIS B 34 ? 0.4354 0.5536 0.3246 0.0291 -0.0683 -0.0577 34 HIS B CE1 2359 C CE1 B HIS B 34 ? 0.3901 0.4969 0.3141 0.0173 -0.0655 0.0317 34 HIS B CE1 2360 N NE2 A HIS B 34 ? 0.4295 0.5321 0.3436 0.0237 -0.0803 -0.0762 34 HIS B NE2 2361 N NE2 B HIS B 34 ? 0.3811 0.4855 0.3279 0.0141 -0.0765 0.0223 34 HIS B NE2 2362 N N . ILE B 35 ? 0.3385 0.3927 0.3054 -0.0063 -0.0420 -0.0259 35 ILE B N 2363 C CA . ILE B 35 ? 0.3298 0.3703 0.3114 -0.0106 -0.0407 -0.0367 35 ILE B CA 2364 C C . ILE B 35 ? 0.3445 0.3912 0.3085 -0.0037 -0.0342 -0.0450 35 ILE B C 2365 O O . ILE B 35 ? 0.3460 0.4064 0.2902 0.0010 -0.0251 -0.0353 35 ILE B O 2366 C CB . ILE B 35 ? 0.3034 0.3299 0.3035 -0.0191 -0.0310 -0.0232 35 ILE B CB 2367 C CG1 . ILE B 35 ? 0.2936 0.3065 0.3129 -0.0240 -0.0326 -0.0313 35 ILE B CG1 2368 C CG2 . ILE B 35 ? 0.2974 0.3246 0.2864 -0.0183 -0.0169 -0.0095 35 ILE B CG2 2369 C CD1 . ILE B 35 ? 0.2777 0.2825 0.3164 -0.0312 -0.0276 -0.0190 35 ILE B CD1 2370 N N . GLU B 36 ? 0.3525 0.3906 0.3262 -0.0029 -0.0392 -0.0619 36 GLU B N 2371 C CA . GLU B 36 ? 0.3675 0.4114 0.3293 0.0042 -0.0323 -0.0708 36 GLU B CA 2372 C C . GLU B 36 ? 0.3488 0.3748 0.3305 -0.0018 -0.0271 -0.0692 36 GLU B C 2373 O O . GLU B 36 ? 0.3383 0.3479 0.3415 -0.0070 -0.0359 -0.0747 36 GLU B O 2374 C CB . GLU B 36 ? 0.4045 0.4569 0.3565 0.0155 -0.0449 -0.0966 36 GLU B CB 2375 C CG . GLU B 36 ? 0.4273 0.4942 0.3626 0.0265 -0.0358 -0.1053 36 GLU B CG 2376 C CD . GLU B 36 ? 0.4659 0.5419 0.3912 0.0407 -0.0488 -0.1351 36 GLU B CD 2377 O OE1 . GLU B 36 ? 0.4929 0.5728 0.4133 0.0446 -0.0643 -0.1478 36 GLU B OE1 2378 O OE2 . GLU B 36 ? 0.4835 0.5640 0.4064 0.0493 -0.0442 -0.1475 36 GLU B OE2 2379 N N . ILE B 37 ? 0.3402 0.3710 0.3162 -0.0011 -0.0132 -0.0604 37 ILE B N 2380 C CA . ILE B 37 ? 0.3291 0.3462 0.3213 -0.0054 -0.0082 -0.0581 37 ILE B CA 2381 C C . ILE B 37 ? 0.3428 0.3703 0.3279 0.0033 -0.0027 -0.0686 37 ILE B C 2382 O O . ILE B 37 ? 0.3429 0.3909 0.3119 0.0081 0.0067 -0.0639 37 ILE B O 2383 C CB . ILE B 37 ? 0.3101 0.3233 0.3075 -0.0133 0.0018 -0.0379 37 ILE B CB 2384 C CG1 . ILE B 37 ? 0.3035 0.3097 0.3086 -0.0195 -0.0031 -0.0292 37 ILE B CG1 2385 C CG2 . ILE B 37 ? 0.2987 0.3010 0.3101 -0.0160 0.0059 -0.0366 37 ILE B CG2 2386 C CD1 . ILE B 37 ? 0.2926 0.2974 0.2994 -0.0240 0.0049 -0.0126 37 ILE B CD1 2387 N N . GLN B 38 ? 0.3484 0.3633 0.3471 0.0060 -0.0089 -0.0819 38 GLN B N 2388 C CA . GLN B 38 ? 0.3631 0.3871 0.3593 0.0159 -0.0049 -0.0941 38 GLN B CA 2389 C C . GLN B 38 ? 0.3416 0.3510 0.3566 0.0114 -0.0020 -0.0879 38 GLN B C 2390 O O . GLN B 38 ? 0.3330 0.3223 0.3637 0.0039 -0.0082 -0.0823 38 GLN B O 2391 C CB . GLN B 38 ? 0.3966 0.4173 0.3940 0.0267 -0.0187 -0.1200 38 GLN B CB 2392 C CG . GLN B 38 ? 0.4295 0.4662 0.4069 0.0342 -0.0254 -0.1317 38 GLN B CG 2393 C CD . GLN B 38 ? 0.4666 0.4916 0.4524 0.0420 -0.0448 -0.1591 38 GLN B CD 2394 O OE1 . GLN B 38 ? 0.4830 0.4864 0.4916 0.0419 -0.0531 -0.1686 38 GLN B OE1 2395 N NE2 . GLN B 38 ? 0.4956 0.5346 0.4643 0.0494 -0.0538 -0.1722 38 GLN B NE2 2396 N N . MET B 39 ? 0.3318 0.3540 0.3457 0.0164 0.0074 -0.0878 39 MET B N 2397 C CA . MET B 39 ? 0.3206 0.3315 0.3517 0.0154 0.0079 -0.0857 39 MET B CA 2398 C C . MET B 39 ? 0.3325 0.3483 0.3671 0.0289 0.0040 -0.1059 39 MET B C 2399 O O . MET B 39 ? 0.3450 0.3842 0.3659 0.0388 0.0089 -0.1161 39 MET B O 2400 C CB . MET B 39 ? 0.3021 0.3231 0.3347 0.0094 0.0200 -0.0694 39 MET B CB 2401 C CG . MET B 39 ? 0.2897 0.3030 0.3206 -0.0017 0.0215 -0.0528 39 MET B CG 2402 S SD . MET B 39 ? 0.2764 0.2949 0.3150 -0.0085 0.0307 -0.0376 39 MET B SD 2403 C CE . MET B 39 ? 0.2677 0.2690 0.3209 -0.0081 0.0241 -0.0390 39 MET B CE 2404 N N . LEU B 40 ? 0.3332 0.3277 0.3861 0.0303 -0.0053 -0.1112 40 LEU B N 2405 C CA . LEU B 40 ? 0.3546 0.3459 0.4156 0.0441 -0.0138 -0.1331 40 LEU B CA 2406 C C . LEU B 40 ? 0.3455 0.3347 0.4218 0.0484 -0.0115 -0.1309 40 LEU B C 2407 O O . LEU B 40 ? 0.3238 0.3005 0.4100 0.0395 -0.0108 -0.1142 40 LEU B O 2408 C CB . LEU B 40 ? 0.3739 0.3374 0.4490 0.0431 -0.0317 -0.1432 40 LEU B CB 2409 C CG . LEU B 40 ? 0.3816 0.3438 0.4476 0.0370 -0.0376 -0.1446 40 LEU B CG 2410 C CD1 . LEU B 40 ? 0.4030 0.3375 0.4914 0.0351 -0.0571 -0.1551 40 LEU B CD1 2411 C CD2 . LEU B 40 ? 0.3967 0.3863 0.4377 0.0481 -0.0338 -0.1598 40 LEU B CD2 2412 N N . LYS B 41 ? 0.3608 0.3651 0.4380 0.0637 -0.0105 -0.1487 41 LYS B N 2413 C CA . LYS B 41 ? 0.3628 0.3654 0.4574 0.0716 -0.0114 -0.1516 41 LYS B CA 2414 C C . LYS B 41 ? 0.3911 0.3779 0.4982 0.0865 -0.0267 -0.1763 41 LYS B C 2415 O O . LYS B 41 ? 0.4060 0.4090 0.5026 0.0998 -0.0274 -0.1981 41 LYS B O 2416 C CB . LYS B 41 ? 0.3601 0.3996 0.4492 0.0780 0.0039 -0.1514 41 LYS B CB 2417 C CG . LYS B 41 ? 0.3672 0.4104 0.4755 0.0882 0.0027 -0.1565 41 LYS B CG 2418 C CD . LYS B 41 ? 0.3622 0.4440 0.4706 0.0902 0.0188 -0.1509 41 LYS B CD 2419 C CE . LYS B 41 ? 0.3723 0.4602 0.5021 0.1021 0.0162 -0.1582 41 LYS B CE 2420 N NZ . LYS B 41 ? 0.3735 0.5055 0.5076 0.1074 0.0315 -0.1576 41 LYS B NZ 2421 N N . ASN B 42 ? 0.3993 0.3551 0.5288 0.0851 -0.0394 -0.1729 42 ASN B N 2422 C CA . ASN B 42 ? 0.4319 0.3642 0.5799 0.0976 -0.0577 -0.1951 42 ASN B CA 2423 C C . ASN B 42 ? 0.4530 0.3807 0.5929 0.1002 -0.0675 -0.2150 42 ASN B C 2424 O O . ASN B 42 ? 0.4792 0.4084 0.6216 0.1175 -0.0772 -0.2443 42 ASN B O 2425 C CB . ASN B 42 ? 0.4464 0.3939 0.6019 0.1181 -0.0571 -0.2142 42 ASN B CB 2426 C CG . ASN B 42 ? 0.4291 0.3834 0.5945 0.1163 -0.0493 -0.1960 42 ASN B CG 2427 O OD1 . ASN B 42 ? 0.4210 0.3533 0.5976 0.1050 -0.0537 -0.1746 42 ASN B OD1 2428 N ND2 . ASN B 42 ? 0.4264 0.4144 0.5882 0.1281 -0.0380 -0.2040 42 ASN B ND2 2429 N N . GLY B 43 ? 0.4418 0.3660 0.5719 0.0842 -0.0656 -0.2004 43 GLY B N 2430 C CA . GLY B 43 ? 0.4630 0.3853 0.5848 0.0845 -0.0752 -0.2163 43 GLY B CA 2431 C C . GLY B 43 ? 0.4710 0.4297 0.5610 0.0938 -0.0653 -0.2295 43 GLY B C 2432 O O . GLY B 43 ? 0.4811 0.4408 0.5614 0.0946 -0.0739 -0.2420 43 GLY B O 2433 N N . LYS B 44 ? 0.4637 0.4542 0.5388 0.1007 -0.0476 -0.2254 44 LYS B N 2434 C CA . LYS B 44 ? 0.4773 0.5074 0.5235 0.1116 -0.0362 -0.2354 44 LYS B CA 2435 C C . LYS B 44 ? 0.4556 0.5037 0.4855 0.0964 -0.0191 -0.2064 44 LYS B C 2436 O O . LYS B 44 ? 0.4315 0.4749 0.4716 0.0849 -0.0104 -0.1843 44 LYS B O 2437 C CB . LYS B 44 ? 0.4866 0.5444 0.5322 0.1304 -0.0274 -0.2493 44 LYS B CB 2438 N N . LYS B 45 ? 0.4706 0.5390 0.4759 0.0975 -0.0155 -0.2073 45 LYS B N 2439 C CA . LYS B 45 ? 0.4584 0.5412 0.4497 0.0836 -0.0013 -0.1797 45 LYS B CA 2440 C C . LYS B 45 ? 0.4459 0.5550 0.4374 0.0827 0.0179 -0.1634 45 LYS B C 2441 O O . LYS B 45 ? 0.4544 0.5933 0.4398 0.0974 0.0257 -0.1746 45 LYS B O 2442 C CB . LYS B 45 ? 0.4830 0.5877 0.4465 0.0890 -0.0014 -0.1846 45 LYS B CB 2443 C CG . LYS B 45 ? 0.4975 0.5770 0.4632 0.0838 -0.0198 -0.1930 45 LYS B CG 2444 C CD . LYS B 45 ? 0.5347 0.6376 0.4734 0.0972 -0.0258 -0.2109 45 LYS B CD 2445 C CE . LYS B 45 ? 0.5365 0.6247 0.4737 0.0866 -0.0378 -0.2057 45 LYS B CE 2446 N NZ . LYS B 45 ? 0.5717 0.6836 0.4818 0.1008 -0.0462 -0.2245 45 LYS B NZ 2447 N N . ILE B 46 ? 0.4226 0.5218 0.4239 0.0661 0.0247 -0.1384 46 ILE B N 2448 C CA . ILE B 46 ? 0.4142 0.5372 0.4197 0.0620 0.0413 -0.1209 46 ILE B CA 2449 C C . ILE B 46 ? 0.4281 0.5795 0.4130 0.0599 0.0530 -0.1070 46 ILE B C 2450 O O . ILE B 46 ? 0.4196 0.5591 0.3959 0.0504 0.0499 -0.0958 46 ILE B O 2451 C CB . ILE B 46 ? 0.3888 0.4896 0.4126 0.0463 0.0413 -0.1023 46 ILE B CB 2452 C CG1 . ILE B 46 ? 0.3848 0.4613 0.4275 0.0499 0.0303 -0.1129 46 ILE B CG1 2453 C CG2 . ILE B 46 ? 0.3768 0.5014 0.4081 0.0402 0.0561 -0.0846 46 ILE B CG2 2454 C CD1 . ILE B 46 ? 0.3651 0.4208 0.4220 0.0373 0.0282 -0.0968 46 ILE B CD1 2455 N N . PRO B 47 ? 0.4576 0.6486 0.4358 0.0692 0.0668 -0.1060 47 PRO B N 2456 C CA . PRO B 47 ? 0.4798 0.7003 0.4359 0.0695 0.0773 -0.0919 47 PRO B CA 2457 C C . PRO B 47 ? 0.4753 0.6934 0.4378 0.0510 0.0857 -0.0598 47 PRO B C 2458 O O . PRO B 47 ? 0.4988 0.7199 0.4442 0.0479 0.0858 -0.0484 47 PRO B O 2459 C CB . PRO B 47 ? 0.4951 0.7623 0.4461 0.0851 0.0913 -0.0978 47 PRO B CB 2460 C CG . PRO B 47 ? 0.4801 0.7424 0.4590 0.0852 0.0924 -0.1032 47 PRO B CG 2461 C CD . PRO B 47 ? 0.4643 0.6780 0.4556 0.0802 0.0741 -0.1153 47 PRO B CD 2462 N N . LYS B 48 ? 0.4614 0.6735 0.4491 0.0398 0.0908 -0.0466 48 LYS B N 2463 C CA . LYS B 48 ? 0.4602 0.6771 0.4577 0.0244 0.0998 -0.0174 48 LYS B CA 2464 C C . LYS B 48 ? 0.4440 0.6221 0.4512 0.0096 0.0900 -0.0083 48 LYS B C 2465 O O . LYS B 48 ? 0.4540 0.6273 0.4812 -0.0024 0.0934 0.0078 48 LYS B O 2466 C CB . LYS B 48 ? 0.4543 0.6955 0.4767 0.0210 0.1117 -0.0074 48 LYS B CB 2467 N N . VAL B 49 ? 0.4289 0.5818 0.4237 0.0111 0.0778 -0.0190 49 VAL B N 2468 C CA . VAL B 49 ? 0.4032 0.5227 0.4073 0.0000 0.0689 -0.0136 49 VAL B CA 2469 C C . VAL B 49 ? 0.3974 0.5163 0.4005 -0.0096 0.0725 0.0086 49 VAL B C 2470 O O . VAL B 49 ? 0.4106 0.5434 0.3963 -0.0064 0.0750 0.0155 49 VAL B O 2471 C CB . VAL B 49 ? 0.3987 0.4955 0.3943 0.0039 0.0555 -0.0296 49 VAL B CB 2472 C CG1 . VAL B 49 ? 0.3833 0.4525 0.3876 -0.0063 0.0487 -0.0218 49 VAL B CG1 2473 C CG2 . VAL B 49 ? 0.3991 0.4914 0.4017 0.0126 0.0504 -0.0495 49 VAL B CG2 2474 N N . GLU B 50 ? 0.3756 0.4792 0.3980 -0.0203 0.0716 0.0189 50 GLU B N 2475 C CA . GLU B 50 ? 0.3754 0.4729 0.4030 -0.0293 0.0726 0.0386 50 GLU B CA 2476 C C . GLU B 50 ? 0.3593 0.4294 0.3825 -0.0312 0.0618 0.0345 50 GLU B C 2477 O O . GLU B 50 ? 0.3348 0.3884 0.3628 -0.0306 0.0552 0.0221 50 GLU B O 2478 C CB . GLU B 50 ? 0.3751 0.4719 0.4299 -0.0390 0.0760 0.0494 50 GLU B CB 2479 C CG . GLU B 50 ? 0.3975 0.5260 0.4630 -0.0402 0.0885 0.0609 50 GLU B CG 2480 C CD . GLU B 50 ? 0.4269 0.5738 0.4861 -0.0427 0.0968 0.0843 50 GLU B CD 2481 O OE1 . GLU B 50 ? 0.4536 0.6347 0.5109 -0.0393 0.1091 0.0930 50 GLU B OE1 2482 O OE2 . GLU B 50 ? 0.4400 0.5696 0.4962 -0.0471 0.0916 0.0954 50 GLU B OE2 2483 N N . MET B 51 ? 0.3610 0.4290 0.3756 -0.0325 0.0604 0.0461 51 MET B N 2484 C CA . MET B 51 ? 0.3577 0.4047 0.3696 -0.0334 0.0509 0.0438 51 MET B CA 2485 C C . MET B 51 ? 0.3420 0.3775 0.3677 -0.0401 0.0499 0.0595 51 MET B C 2486 O O . MET B 51 ? 0.3496 0.3952 0.3780 -0.0430 0.0552 0.0767 51 MET B O 2487 C CB . MET B 51 ? 0.3854 0.4400 0.3764 -0.0272 0.0472 0.0426 51 MET B CB 2488 C CG . MET B 51 ? 0.4091 0.4765 0.3855 -0.0188 0.0461 0.0257 51 MET B CG 2489 S SD . MET B 51 ? 0.4149 0.4610 0.3988 -0.0182 0.0355 0.0060 51 MET B SD 2490 C CE . MET B 51 ? 0.4293 0.4905 0.4019 -0.0076 0.0345 -0.0134 51 MET B CE 2491 N N . SER B 52 ? 0.3217 0.3372 0.3565 -0.0417 0.0430 0.0540 52 SER B N 2492 C CA . SER B 52 ? 0.3195 0.3215 0.3658 -0.0449 0.0389 0.0647 52 SER B CA 2493 C C . SER B 52 ? 0.3246 0.3292 0.3580 -0.0415 0.0364 0.0740 52 SER B C 2494 O O . SER B 52 ? 0.3230 0.3387 0.3384 -0.0367 0.0360 0.0688 52 SER B O 2495 C CB . SER B 52 ? 0.3085 0.2933 0.3633 -0.0436 0.0321 0.0531 52 SER B CB 2496 O OG . SER B 52 ? 0.3004 0.2841 0.3431 -0.0387 0.0284 0.0452 52 SER B OG 2497 N N . ASP B 53 ? 0.3299 0.3234 0.3741 -0.0433 0.0327 0.0863 53 ASP B N 2498 C CA . ASP B 53 ? 0.3405 0.3343 0.3750 -0.0389 0.0281 0.0951 53 ASP B CA 2499 C C . ASP B 53 ? 0.3315 0.3192 0.3612 -0.0338 0.0213 0.0800 53 ASP B C 2500 O O . ASP B 53 ? 0.3281 0.3055 0.3679 -0.0339 0.0194 0.0689 53 ASP B O 2501 C CB . ASP B 53 ? 0.3523 0.3321 0.4044 -0.0413 0.0243 0.1115 53 ASP B CB 2502 C CG . ASP B 53 ? 0.3682 0.3553 0.4296 -0.0480 0.0309 0.1317 53 ASP B CG 2503 O OD1 . ASP B 53 ? 0.3764 0.3864 0.4209 -0.0471 0.0385 0.1402 53 ASP B OD1 2504 O OD2 . ASP B 53 ? 0.3721 0.3438 0.4593 -0.0539 0.0282 0.1392 53 ASP B OD2 2505 N N . MET B 54 ? 0.3366 0.3339 0.3515 -0.0291 0.0177 0.0800 54 MET B N 2506 C CA . MET B 54 ? 0.3300 0.3246 0.3455 -0.0253 0.0109 0.0694 54 MET B CA 2507 C C . MET B 54 ? 0.3151 0.2956 0.3469 -0.0234 0.0067 0.0727 54 MET B C 2508 O O . MET B 54 ? 0.3214 0.2954 0.3593 -0.0229 0.0050 0.0863 54 MET B O 2509 C CB . MET B 54 ? 0.3577 0.3659 0.3582 -0.0207 0.0055 0.0716 54 MET B CB 2510 C CG . MET B 54 ? 0.3652 0.3748 0.3700 -0.0178 -0.0025 0.0623 54 MET B CG 2511 S SD . MET B 54 ? 0.3757 0.3863 0.3841 -0.0211 -0.0023 0.0439 54 MET B SD 2512 C CE . MET B 54 ? 0.3822 0.4065 0.3706 -0.0190 -0.0038 0.0367 54 MET B CE 2513 N N . SER B 55 ? 0.2900 0.2667 0.3297 -0.0215 0.0050 0.0609 55 SER B N 2514 C CA . SER B 55 ? 0.2872 0.2549 0.3406 -0.0162 0.0007 0.0604 55 SER B CA 2515 C C . SER B 55 ? 0.2718 0.2490 0.3277 -0.0120 -0.0013 0.0516 55 SER B C 2516 O O . SER B 55 ? 0.2569 0.2443 0.3065 -0.0150 -0.0004 0.0472 55 SER B O 2517 C CB . SER B 55 ? 0.2879 0.2426 0.3530 -0.0171 0.0021 0.0556 55 SER B CB 2518 O OG . SER B 55 ? 0.2954 0.2398 0.3741 -0.0102 -0.0035 0.0538 55 SER B OG 2519 N N . PHE B 56 ? 0.2686 0.2435 0.3359 -0.0048 -0.0045 0.0494 56 PHE B N 2520 C CA . PHE B 56 ? 0.2592 0.2476 0.3322 -0.0007 -0.0043 0.0428 56 PHE B CA 2521 C C . PHE B 56 ? 0.2678 0.2552 0.3506 0.0076 -0.0032 0.0348 56 PHE B C 2522 O O . PHE B 56 ? 0.2736 0.2465 0.3615 0.0118 -0.0060 0.0329 56 PHE B O 2523 C CB . PHE B 56 ? 0.2560 0.2561 0.3318 0.0020 -0.0102 0.0480 56 PHE B CB 2524 C CG . PHE B 56 ? 0.2651 0.2589 0.3480 0.0101 -0.0166 0.0544 56 PHE B CG 2525 C CD1 . PHE B 56 ? 0.2657 0.2622 0.3628 0.0204 -0.0183 0.0493 56 PHE B CD1 2526 C CD2 . PHE B 56 ? 0.2776 0.2651 0.3530 0.0089 -0.0211 0.0663 56 PHE B CD2 2527 C CE1 . PHE B 56 ? 0.2812 0.2699 0.3874 0.0293 -0.0258 0.0546 56 PHE B CE1 2528 C CE2 . PHE B 56 ? 0.2907 0.2711 0.3743 0.0165 -0.0280 0.0749 56 PHE B CE2 2529 C CZ . PHE B 56 ? 0.2931 0.2721 0.3935 0.0267 -0.0311 0.0685 56 PHE B CZ 2530 N N . SER B 57 ? 0.2673 0.2714 0.3536 0.0102 0.0006 0.0301 57 SER B N 2531 C CA . SER B 57 ? 0.2784 0.2892 0.3693 0.0196 0.0037 0.0214 57 SER B CA 2532 C C . SER B 57 ? 0.2863 0.3092 0.3892 0.0314 0.0010 0.0199 57 SER B C 2533 O O . SER B 57 ? 0.2845 0.3108 0.3930 0.0309 -0.0034 0.0267 57 SER B O 2534 C CB . SER B 57 ? 0.2752 0.3018 0.3628 0.0162 0.0113 0.0208 57 SER B CB 2535 O OG . SER B 57 ? 0.2864 0.3018 0.3645 0.0071 0.0129 0.0211 57 SER B OG 2536 N N . LYS B 58 ? 0.2963 0.3282 0.4024 0.0434 0.0035 0.0100 58 LYS B N 2537 C CA . LYS B 58 ? 0.3102 0.3583 0.4285 0.0579 0.0022 0.0058 58 LYS B CA 2538 C C . LYS B 58 ? 0.2918 0.3661 0.4197 0.0547 0.0055 0.0154 58 LYS B C 2539 O O . LYS B 58 ? 0.2956 0.3780 0.4360 0.0620 0.0009 0.0169 58 LYS B O 2540 C CB . LYS B 58 ? 0.3296 0.3904 0.4456 0.0721 0.0065 -0.0080 58 LYS B CB 2541 C CG . LYS B 58 ? 0.3536 0.4280 0.4812 0.0916 0.0041 -0.0179 58 LYS B CG 2542 C CD . LYS B 58 ? 0.3778 0.4542 0.4987 0.1070 0.0040 -0.0370 58 LYS B CD 2543 C CE . LYS B 58 ? 0.4012 0.5026 0.5311 0.1296 0.0048 -0.0492 58 LYS B CE 2544 N NZ . LYS B 58 ? 0.4247 0.5351 0.5433 0.1458 0.0056 -0.0694 58 LYS B NZ 2545 N N . ASP B 59 ? 0.2723 0.3583 0.3973 0.0433 0.0119 0.0223 59 ASP B N 2546 C CA . ASP B 59 ? 0.2591 0.3681 0.3983 0.0371 0.0132 0.0319 59 ASP B CA 2547 C C . ASP B 59 ? 0.2483 0.3456 0.3886 0.0264 0.0041 0.0377 59 ASP B C 2548 O O . ASP B 59 ? 0.2340 0.3475 0.3873 0.0194 0.0024 0.0436 59 ASP B O 2549 C CB . ASP B 59 ? 0.2548 0.3811 0.3958 0.0296 0.0226 0.0381 59 ASP B CB 2550 C CG . ASP B 59 ? 0.2544 0.3605 0.3847 0.0149 0.0211 0.0410 59 ASP B CG 2551 O OD1 . ASP B 59 ? 0.2491 0.3318 0.3696 0.0100 0.0142 0.0382 59 ASP B OD1 2552 O OD2 . ASP B 59 ? 0.2543 0.3703 0.3868 0.0091 0.0274 0.0470 59 ASP B OD2 2553 N N . TRP B 60 ? 0.2452 0.3168 0.3728 0.0255 -0.0020 0.0363 60 TRP B N 2554 C CA . TRP B 60 ? 0.2439 0.3063 0.3669 0.0191 -0.0106 0.0416 60 TRP B CA 2555 C C . TRP B 60 ? 0.2378 0.2940 0.3502 0.0060 -0.0107 0.0428 60 TRP B C 2556 O O . TRP B 60 ? 0.2439 0.2928 0.3470 0.0026 -0.0172 0.0453 60 TRP B O 2557 C CB . TRP B 60 ? 0.2438 0.3243 0.3820 0.0232 -0.0178 0.0453 60 TRP B CB 2558 C CG . TRP B 60 ? 0.2490 0.3349 0.3984 0.0380 -0.0193 0.0435 60 TRP B CG 2559 C CD1 . TRP B 60 ? 0.2454 0.3550 0.4112 0.0470 -0.0142 0.0402 60 TRP B CD1 2560 C CD2 . TRP B 60 ? 0.2614 0.3292 0.4081 0.0467 -0.0269 0.0453 60 TRP B CD2 2561 N NE1 . TRP B 60 ? 0.2571 0.3642 0.4303 0.0624 -0.0187 0.0365 60 TRP B NE1 2562 C CE2 . TRP B 60 ? 0.2665 0.3457 0.4294 0.0620 -0.0273 0.0401 60 TRP B CE2 2563 C CE3 . TRP B 60 ? 0.2703 0.3150 0.4040 0.0434 -0.0329 0.0522 60 TRP B CE3 2564 C CZ2 . TRP B 60 ? 0.2832 0.3468 0.4516 0.0742 -0.0357 0.0404 60 TRP B CZ2 2565 C CZ3 . TRP B 60 ? 0.2870 0.3172 0.4264 0.0540 -0.0403 0.0561 60 TRP B CZ3 2566 C CH2 . TRP B 60 ? 0.2928 0.3303 0.4503 0.0691 -0.0425 0.0495 60 TRP B CH2 2567 N N . SER B 61 ? 0.2304 0.2902 0.3435 0.0002 -0.0039 0.0409 61 SER B N 2568 C CA . SER B 61 ? 0.2294 0.2819 0.3354 -0.0103 -0.0047 0.0401 61 SER B CA 2569 C C . SER B 61 ? 0.2311 0.2633 0.3182 -0.0114 -0.0032 0.0378 61 SER B C 2570 O O . SER B 61 ? 0.2332 0.2566 0.3164 -0.0065 0.0005 0.0365 61 SER B O 2571 C CB . SER B 61 ? 0.2237 0.2855 0.3394 -0.0156 0.0014 0.0415 61 SER B CB 2572 O OG . SER B 61 ? 0.2260 0.2838 0.3339 -0.0113 0.0096 0.0401 61 SER B OG 2573 N N . PHE B 62 ? 0.2302 0.2570 0.3080 -0.0174 -0.0069 0.0365 62 PHE B N 2574 C CA . PHE B 62 ? 0.2358 0.2492 0.2976 -0.0186 -0.0048 0.0361 62 PHE B CA 2575 C C . PHE B 62 ? 0.2345 0.2412 0.2933 -0.0226 0.0013 0.0319 62 PHE B C 2576 O O . PHE B 62 ? 0.2244 0.2354 0.2907 -0.0259 0.0024 0.0295 62 PHE B O 2577 C CB . PHE B 62 ? 0.2438 0.2598 0.2943 -0.0203 -0.0110 0.0358 62 PHE B CB 2578 C CG . PHE B 62 ? 0.2521 0.2740 0.3013 -0.0151 -0.0177 0.0422 62 PHE B CG 2579 C CD1 . PHE B 62 ? 0.2599 0.2748 0.3006 -0.0115 -0.0167 0.0513 62 PHE B CD1 2580 C CD2 . PHE B 62 ? 0.2508 0.2858 0.3100 -0.0140 -0.0260 0.0404 62 PHE B CD2 2581 C CE1 . PHE B 62 ? 0.2724 0.2921 0.3121 -0.0058 -0.0237 0.0595 62 PHE B CE1 2582 C CE2 . PHE B 62 ? 0.2623 0.3039 0.3204 -0.0080 -0.0334 0.0465 62 PHE B CE2 2583 C CZ . PHE B 62 ? 0.2742 0.3077 0.3211 -0.0033 -0.0323 0.0566 62 PHE B CZ 2584 N N . TYR B 63 ? 0.2387 0.2354 0.2892 -0.0224 0.0048 0.0324 63 TYR B N 2585 C CA . TYR B 63 ? 0.2400 0.2313 0.2872 -0.0255 0.0094 0.0282 63 TYR B CA 2586 C C . TYR B 63 ? 0.2468 0.2332 0.2849 -0.0273 0.0115 0.0300 63 TYR B C 2587 O O . TYR B 63 ? 0.2505 0.2349 0.2866 -0.0261 0.0107 0.0373 63 TYR B O 2588 C CB . TYR B 63 ? 0.2413 0.2305 0.2942 -0.0224 0.0131 0.0260 63 TYR B CB 2589 C CG . TYR B 63 ? 0.2551 0.2370 0.3107 -0.0178 0.0124 0.0265 63 TYR B CG 2590 C CD1 . TYR B 63 ? 0.2654 0.2376 0.3205 -0.0200 0.0133 0.0260 63 TYR B CD1 2591 C CD2 . TYR B 63 ? 0.2663 0.2513 0.3288 -0.0111 0.0099 0.0270 63 TYR B CD2 2592 C CE1 . TYR B 63 ? 0.2832 0.2458 0.3463 -0.0167 0.0102 0.0260 63 TYR B CE1 2593 C CE2 . TYR B 63 ? 0.2811 0.2561 0.3492 -0.0058 0.0069 0.0255 63 TYR B CE2 2594 C CZ . TYR B 63 ? 0.2902 0.2525 0.3595 -0.0092 0.0064 0.0250 63 TYR B CZ 2595 O OH . TYR B 63 ? 0.3219 0.2714 0.4020 -0.0048 0.0012 0.0232 63 TYR B OH 2596 N N . ILE B 64 ? 0.2460 0.2318 0.2809 -0.0298 0.0144 0.0251 64 ILE B N 2597 C CA . ILE B 64 ? 0.2495 0.2360 0.2783 -0.0313 0.0181 0.0268 64 ILE B CA 2598 C C . ILE B 64 ? 0.2408 0.2256 0.2725 -0.0325 0.0213 0.0200 64 ILE B C 2599 O O . ILE B 64 ? 0.2272 0.2108 0.2617 -0.0323 0.0195 0.0144 64 ILE B O 2600 C CB . ILE B 64 ? 0.2664 0.2627 0.2829 -0.0301 0.0164 0.0274 64 ILE B CB 2601 C CG1 . ILE B 64 ? 0.2789 0.2823 0.2885 -0.0305 0.0224 0.0335 64 ILE B CG1 2602 C CG2 . ILE B 64 ? 0.2675 0.2664 0.2821 -0.0295 0.0123 0.0159 64 ILE B CG2 2603 C CD1 . ILE B 64 ? 0.2967 0.3134 0.2910 -0.0271 0.0213 0.0387 64 ILE B CD1 2604 N N . LEU B 65 ? 0.2413 0.2263 0.2755 -0.0341 0.0254 0.0223 65 LEU B N 2605 C CA . LEU B 65 ? 0.2377 0.2235 0.2758 -0.0345 0.0279 0.0162 65 LEU B CA 2606 C C . LEU B 65 ? 0.2427 0.2396 0.2756 -0.0343 0.0322 0.0155 65 LEU B C 2607 O O . LEU B 65 ? 0.2492 0.2533 0.2814 -0.0361 0.0362 0.0242 65 LEU B O 2608 C CB . LEU B 65 ? 0.2375 0.2184 0.2868 -0.0361 0.0282 0.0174 65 LEU B CB 2609 C CG . LEU B 65 ? 0.2317 0.2150 0.2873 -0.0360 0.0292 0.0113 65 LEU B CG 2610 C CD1 . LEU B 65 ? 0.2272 0.2081 0.2795 -0.0322 0.0266 0.0051 65 LEU B CD1 2611 C CD2 . LEU B 65 ? 0.2338 0.2130 0.3027 -0.0380 0.0270 0.0114 65 LEU B CD2 2612 N N . ALA B 66 ? 0.2402 0.2396 0.2707 -0.0314 0.0315 0.0061 66 ALA B N 2613 C CA . ALA B 66 ? 0.2466 0.2591 0.2739 -0.0286 0.0361 0.0021 66 ALA B CA 2614 C C . ALA B 66 ? 0.2396 0.2518 0.2789 -0.0289 0.0379 -0.0010 66 ALA B C 2615 O O . ALA B 66 ? 0.2314 0.2329 0.2763 -0.0288 0.0336 -0.0040 66 ALA B O 2616 C CB . ALA B 66 ? 0.2532 0.2678 0.2721 -0.0229 0.0317 -0.0095 66 ALA B CB 2617 N N . HIS B 67 ? 0.2474 0.2746 0.2911 -0.0285 0.0443 0.0005 67 HIS B N 2618 C CA . HIS B 67 ? 0.2421 0.2725 0.2989 -0.0275 0.0450 -0.0043 67 HIS B CA 2619 C C . HIS B 67 ? 0.2521 0.3046 0.3109 -0.0234 0.0522 -0.0069 67 HIS B C 2620 O O . HIS B 67 ? 0.2600 0.3286 0.3123 -0.0234 0.0591 -0.0001 67 HIS B O 2621 C CB . HIS B 67 ? 0.2396 0.2650 0.3111 -0.0337 0.0437 0.0018 67 HIS B CB 2622 C CG . HIS B 67 ? 0.2465 0.2838 0.3287 -0.0399 0.0497 0.0131 67 HIS B CG 2623 N ND1 . HIS B 67 ? 0.2549 0.2892 0.3339 -0.0442 0.0510 0.0247 67 HIS B ND1 2624 C CD2 . HIS B 67 ? 0.2535 0.3071 0.3528 -0.0428 0.0547 0.0168 67 HIS B CD2 2625 C CE1 . HIS B 67 ? 0.2620 0.3085 0.3559 -0.0502 0.0566 0.0367 67 HIS B CE1 2626 N NE2 . HIS B 67 ? 0.2610 0.3205 0.3684 -0.0500 0.0593 0.0322 67 HIS B NE2 2627 N N . THR B 68 ? 0.2512 0.3071 0.3192 -0.0187 0.0510 -0.0158 68 THR B N 2628 C CA . THR B 68 ? 0.2622 0.3422 0.3350 -0.0127 0.0581 -0.0201 68 THR B CA 2629 C C . THR B 68 ? 0.2600 0.3444 0.3524 -0.0120 0.0567 -0.0235 68 THR B C 2630 O O . THR B 68 ? 0.2505 0.3173 0.3471 -0.0123 0.0483 -0.0268 68 THR B O 2631 C CB . THR B 68 ? 0.2747 0.3572 0.3338 -0.0013 0.0560 -0.0347 68 THR B CB 2632 O OG1 . THR B 68 ? 0.2862 0.3977 0.3473 0.0065 0.0646 -0.0393 68 THR B OG1 2633 C CG2 . THR B 68 ? 0.2725 0.3334 0.3364 0.0032 0.0452 -0.0461 68 THR B CG2 2634 N N . GLU B 69 ? 0.2731 0.3842 0.3780 -0.0107 0.0651 -0.0215 69 GLU B N 2635 C CA . GLU B 69 ? 0.2807 0.4014 0.4060 -0.0077 0.0634 -0.0268 69 GLU B CA 2636 C C . GLU B 69 ? 0.2848 0.3992 0.4042 0.0053 0.0577 -0.0428 69 GLU B C 2637 O O . GLU B 69 ? 0.3016 0.4200 0.4070 0.0137 0.0598 -0.0511 69 GLU B O 2638 C CB . GLU B 69 ? 0.2968 0.4526 0.4396 -0.0092 0.0751 -0.0198 69 GLU B CB 2639 C CG . GLU B 69 ? 0.3092 0.4690 0.4659 -0.0239 0.0790 -0.0017 69 GLU B CG 2640 C CD . GLU B 69 ? 0.3291 0.5266 0.5063 -0.0274 0.0920 0.0102 69 GLU B CD 2641 O OE1 . GLU B 69 ? 0.3522 0.5774 0.5214 -0.0173 0.1023 0.0071 69 GLU B OE1 2642 O OE2 . GLU B 69 ? 0.3371 0.5379 0.5404 -0.0401 0.0917 0.0228 69 GLU B OE2 2643 N N . PHE B 70 ? 0.2743 0.3772 0.4044 0.0078 0.0489 -0.0473 70 PHE B N 2644 C CA . PHE B 70 ? 0.2798 0.3757 0.4105 0.0204 0.0423 -0.0602 70 PHE B CA 2645 C C . PHE B 70 ? 0.2808 0.3801 0.4304 0.0237 0.0363 -0.0617 70 PHE B C 2646 O O . PHE B 70 ? 0.2640 0.3624 0.4218 0.0158 0.0333 -0.0544 70 PHE B O 2647 C CB . PHE B 70 ? 0.2816 0.3474 0.3974 0.0215 0.0335 -0.0627 70 PHE B CB 2648 C CG . PHE B 70 ? 0.2735 0.3179 0.3909 0.0175 0.0244 -0.0558 70 PHE B CG 2649 C CD1 . PHE B 70 ? 0.2599 0.3038 0.3776 0.0081 0.0248 -0.0460 70 PHE B CD1 2650 C CD2 . PHE B 70 ? 0.2787 0.3037 0.3973 0.0239 0.0149 -0.0587 70 PHE B CD2 2651 C CE1 . PHE B 70 ? 0.2559 0.2848 0.3712 0.0071 0.0170 -0.0409 70 PHE B CE1 2652 C CE2 . PHE B 70 ? 0.2738 0.2839 0.3917 0.0211 0.0080 -0.0493 70 PHE B CE2 2653 C CZ . PHE B 70 ? 0.2665 0.2806 0.3807 0.0136 0.0096 -0.0411 70 PHE B CZ 2654 N N . THR B 71 ? 0.2943 0.3982 0.4512 0.0368 0.0332 -0.0730 71 THR B N 2655 C CA . THR B 71 ? 0.2978 0.4061 0.4728 0.0432 0.0261 -0.0757 71 THR B CA 2656 C C . THR B 71 ? 0.3099 0.3914 0.4804 0.0527 0.0146 -0.0809 71 THR B C 2657 O O . THR B 71 ? 0.3295 0.4106 0.5019 0.0644 0.0134 -0.0930 71 THR B O 2658 C CB . THR B 71 ? 0.3027 0.4459 0.4967 0.0516 0.0335 -0.0832 71 THR B CB 2659 O OG1 . THR B 71 ? 0.2939 0.4621 0.4958 0.0403 0.0446 -0.0738 71 THR B OG1 2660 C CG2 . THR B 71 ? 0.3071 0.4554 0.5216 0.0597 0.0245 -0.0868 71 THR B CG2 2661 N N . PRO B 72 ? 0.3046 0.3644 0.4701 0.0482 0.0058 -0.0714 72 PRO B N 2662 C CA . PRO B 72 ? 0.3170 0.3514 0.4816 0.0556 -0.0047 -0.0715 72 PRO B CA 2663 C C . PRO B 72 ? 0.3280 0.3675 0.5108 0.0700 -0.0120 -0.0786 72 PRO B C 2664 O O . PRO B 72 ? 0.3193 0.3814 0.5148 0.0726 -0.0109 -0.0800 72 PRO B O 2665 C CB . PRO B 72 ? 0.3127 0.3323 0.4680 0.0480 -0.0099 -0.0565 72 PRO B CB 2666 C CG . PRO B 72 ? 0.3007 0.3394 0.4574 0.0413 -0.0062 -0.0537 72 PRO B CG 2667 C CD . PRO B 72 ? 0.2938 0.3526 0.4553 0.0376 0.0046 -0.0605 72 PRO B CD 2668 N N . THR B 73 ? 0.3464 0.3648 0.5335 0.0791 -0.0204 -0.0834 73 THR B N 2669 C CA . THR B 73 ? 0.3655 0.3816 0.5712 0.0944 -0.0300 -0.0893 73 THR B CA 2670 C C . THR B 73 ? 0.3858 0.3677 0.5934 0.0957 -0.0429 -0.0781 73 THR B C 2671 O O . THR B 73 ? 0.3821 0.3465 0.5776 0.0847 -0.0427 -0.0670 73 THR B O 2672 C CB . THR B 73 ? 0.3812 0.4072 0.5964 0.1079 -0.0280 -0.1108 73 THR B CB 2673 O OG1 . THR B 73 ? 0.3933 0.3969 0.6001 0.1069 -0.0308 -0.1175 73 THR B OG1 2674 C CG2 . THR B 73 ? 0.3678 0.4326 0.5821 0.1066 -0.0131 -0.1183 73 THR B CG2 2675 N N . GLU B 74 ? 0.4079 0.3813 0.6331 0.1093 -0.0540 -0.0793 74 GLU B N 2676 C CA . GLU B 74 ? 0.4327 0.3726 0.6650 0.1110 -0.0669 -0.0663 74 GLU B CA 2677 C C . GLU B 74 ? 0.4373 0.3521 0.6733 0.1094 -0.0706 -0.0752 74 GLU B C 2678 O O . GLU B 74 ? 0.4469 0.3354 0.6854 0.1023 -0.0774 -0.0599 74 GLU B O 2679 C CB . GLU B 74 ? 0.4652 0.4000 0.7188 0.1274 -0.0794 -0.0661 74 GLU B CB 2680 C CG . GLU B 74 ? 0.4718 0.4257 0.7226 0.1290 -0.0807 -0.0528 74 GLU B CG 2681 C CD . GLU B 74 ? 0.4967 0.4576 0.7695 0.1474 -0.0907 -0.0592 74 GLU B CD 2682 O OE1 . GLU B 74 ? 0.5028 0.4938 0.7777 0.1506 -0.0882 -0.0625 74 GLU B OE1 2683 O OE2 . GLU B 74 ? 0.5310 0.4674 0.8219 0.1588 -0.1022 -0.0614 74 GLU B OE2 2684 N N . THR B 75 ? 0.4313 0.3567 0.6685 0.1163 -0.0665 -0.0997 75 THR B N 2685 C CA . THR B 75 ? 0.4473 0.3497 0.6920 0.1205 -0.0745 -0.1154 75 THR B CA 2686 C C . THR B 75 ? 0.4337 0.3427 0.6597 0.1108 -0.0658 -0.1245 75 THR B C 2687 O O . THR B 75 ? 0.4548 0.3421 0.6862 0.1111 -0.0746 -0.1347 75 THR B O 2688 C CB . THR B 75 ? 0.4670 0.3742 0.7293 0.1421 -0.0809 -0.1414 75 THR B CB 2689 O OG1 . THR B 75 ? 0.4509 0.3995 0.7036 0.1478 -0.0664 -0.1548 75 THR B OG1 2690 C CG2 . THR B 75 ? 0.4817 0.3745 0.7671 0.1534 -0.0939 -0.1327 75 THR B CG2 2691 N N . ASP B 76 ? 0.4001 0.3379 0.6066 0.1027 -0.0504 -0.1214 76 ASP B N 2692 C CA . ASP B 76 ? 0.3913 0.3362 0.5798 0.0949 -0.0428 -0.1283 76 ASP B CA 2693 C C . ASP B 76 ? 0.3790 0.3034 0.5602 0.0778 -0.0447 -0.1090 76 ASP B C 2694 O O . ASP B 76 ? 0.3671 0.2875 0.5479 0.0699 -0.0439 -0.0881 76 ASP B O 2695 C CB . ASP B 76 ? 0.3756 0.3583 0.5494 0.0927 -0.0260 -0.1301 76 ASP B CB 2696 C CG . ASP B 76 ? 0.3879 0.3975 0.5689 0.1099 -0.0218 -0.1501 76 ASP B CG 2697 O OD1 . ASP B 76 ? 0.4096 0.4158 0.5931 0.1232 -0.0275 -0.1716 76 ASP B OD1 2698 O OD2 . ASP B 76 ? 0.3862 0.4230 0.5717 0.1107 -0.0129 -0.1453 76 ASP B OD2 2699 N N . THR B 77 ? 0.3804 0.2935 0.5572 0.0738 -0.0482 -0.1171 77 THR B N 2700 C CA . THR B 77 ? 0.3685 0.2687 0.5392 0.0578 -0.0483 -0.1005 77 THR B CA 2701 C C . THR B 77 ? 0.3477 0.2697 0.4956 0.0511 -0.0360 -0.1030 77 THR B C 2702 O O . THR B 77 ? 0.3569 0.2959 0.4960 0.0593 -0.0322 -0.1214 77 THR B O 2703 C CB . THR B 77 ? 0.3911 0.2621 0.5781 0.0562 -0.0633 -0.1060 77 THR B CB 2704 O OG1 . THR B 77 ? 0.4113 0.2870 0.5947 0.0660 -0.0674 -0.1340 77 THR B OG1 2705 C CG2 . THR B 77 ? 0.4113 0.2566 0.6250 0.0614 -0.0767 -0.0992 77 THR B CG2 2706 N N . TYR B 78 ? 0.3221 0.2450 0.4605 0.0376 -0.0301 -0.0841 78 TYR B N 2707 C CA . TYR B 78 ? 0.3020 0.2415 0.4212 0.0303 -0.0200 -0.0829 78 TYR B CA 2708 C C . TYR B 78 ? 0.2999 0.2253 0.4184 0.0189 -0.0238 -0.0724 78 TYR B C 2709 O O . TYR B 78 ? 0.2961 0.2066 0.4257 0.0134 -0.0285 -0.0576 78 TYR B O 2710 C CB . TYR B 78 ? 0.2797 0.2385 0.3903 0.0263 -0.0084 -0.0717 78 TYR B CB 2711 C CG . TYR B 78 ? 0.2776 0.2565 0.3914 0.0360 -0.0033 -0.0817 78 TYR B CG 2712 C CD1 . TYR B 78 ? 0.2761 0.2782 0.3802 0.0390 0.0056 -0.0906 78 TYR B CD1 2713 C CD2 . TYR B 78 ? 0.2791 0.2564 0.4069 0.0432 -0.0076 -0.0812 78 TYR B CD2 2714 C CE1 . TYR B 78 ? 0.2773 0.3032 0.3873 0.0479 0.0118 -0.0983 78 TYR B CE1 2715 C CE2 . TYR B 78 ? 0.2793 0.2785 0.4137 0.0525 -0.0030 -0.0908 78 TYR B CE2 2716 C CZ . TYR B 78 ? 0.2790 0.3033 0.4053 0.0545 0.0073 -0.0991 78 TYR B CZ 2717 O OH . TYR B 78 ? 0.2830 0.3340 0.4181 0.0636 0.0135 -0.1069 78 TYR B OH 2718 N N . ALA B 79 ? 0.2980 0.2312 0.4042 0.0161 -0.0215 -0.0790 79 ALA B N 2719 C CA . ALA B 79 ? 0.3000 0.2235 0.4074 0.0062 -0.0256 -0.0715 79 ALA B CA 2720 C C . ALA B 79 ? 0.2952 0.2355 0.3831 0.0023 -0.0176 -0.0708 79 ALA B C 2721 O O . ALA B 79 ? 0.2929 0.2515 0.3670 0.0077 -0.0100 -0.0777 79 ALA B O 2722 C CB . ALA B 79 ? 0.3212 0.2269 0.4443 0.0089 -0.0407 -0.0854 79 ALA B CB 2723 N N . CYS B 80 ? 0.2952 0.2307 0.3843 -0.0069 -0.0194 -0.0605 80 CYS B N 2724 C CA . CYS B 80 ? 0.2941 0.2421 0.3680 -0.0102 -0.0151 -0.0595 80 CYS B CA 2725 C C . CYS B 80 ? 0.3082 0.2478 0.3904 -0.0135 -0.0267 -0.0653 80 CYS B C 2726 O O . CYS B 80 ? 0.3063 0.2330 0.4072 -0.0206 -0.0326 -0.0561 80 CYS B O 2727 C CB . CYS B 80 ? 0.2767 0.2302 0.3455 -0.0173 -0.0061 -0.0416 80 CYS B CB 2728 S SG . CYS B 80 ? 0.2790 0.2472 0.3299 -0.0195 -0.0007 -0.0390 80 CYS B SG 2729 N N . ARG B 81 ? 0.3242 0.2736 0.3937 -0.0083 -0.0300 -0.0795 81 ARG B N 2730 C CA . ARG B 81 ? 0.3487 0.2917 0.4265 -0.0095 -0.0442 -0.0904 81 ARG B CA 2731 C C . ARG B 81 ? 0.3393 0.2976 0.4009 -0.0116 -0.0419 -0.0866 81 ARG B C 2732 O O . ARG B 81 ? 0.3316 0.3073 0.3702 -0.0056 -0.0338 -0.0881 81 ARG B O 2733 C CB . ARG B 81 ? 0.3870 0.3281 0.4644 0.0023 -0.0550 -0.1165 81 ARG B CB 2734 C CG . ARG B 81 ? 0.4223 0.3532 0.5143 0.0010 -0.0738 -0.1312 81 ARG B CG 2735 C CD . ARG B 81 ? 0.4657 0.3871 0.5656 0.0132 -0.0878 -0.1589 81 ARG B CD 2736 N NE . ARG B 81 ? 0.5001 0.4447 0.5709 0.0281 -0.0871 -0.1797 81 ARG B NE 2737 C CZ . ARG B 81 ? 0.5406 0.4911 0.6049 0.0351 -0.1017 -0.2016 81 ARG B CZ 2738 N NH1 . ARG B 81 ? 0.5626 0.4956 0.6519 0.0273 -0.1204 -0.2078 81 ARG B NH1 2739 N NH2 . ARG B 81 ? 0.5673 0.5444 0.6005 0.0506 -0.0981 -0.2179 81 ARG B NH2 2740 N N . VAL B 82 ? 0.3346 0.2875 0.4104 -0.0200 -0.0494 -0.0804 82 VAL B N 2741 C CA . VAL B 82 ? 0.3308 0.2971 0.3955 -0.0226 -0.0478 -0.0736 82 VAL B CA 2742 C C . VAL B 82 ? 0.3456 0.3117 0.4199 -0.0230 -0.0649 -0.0871 82 VAL B C 2743 O O . VAL B 82 ? 0.3487 0.3007 0.4512 -0.0293 -0.0763 -0.0897 82 VAL B O 2744 C CB . VAL B 82 ? 0.3110 0.2767 0.3851 -0.0319 -0.0394 -0.0513 82 VAL B CB 2745 C CG1 . VAL B 82 ? 0.3115 0.2889 0.3809 -0.0341 -0.0408 -0.0452 82 VAL B CG1 2746 C CG2 . VAL B 82 ? 0.2977 0.2658 0.3599 -0.0303 -0.0247 -0.0410 82 VAL B CG2 2747 N N . LYS B 83 ? 0.3557 0.3383 0.4080 -0.0163 -0.0672 -0.0944 83 LYS B N 2748 C CA . LYS B 83 ? 0.3727 0.3596 0.4309 -0.0156 -0.0843 -0.1075 83 LYS B CA 2749 C C . LYS B 83 ? 0.3584 0.3586 0.4100 -0.0194 -0.0805 -0.0916 83 LYS B C 2750 O O . LYS B 83 ? 0.3480 0.3602 0.3757 -0.0153 -0.0682 -0.0807 83 LYS B O 2751 C CB . LYS B 83 ? 0.4034 0.4025 0.4378 -0.0011 -0.0926 -0.1317 83 LYS B CB 2752 C CG . LYS B 83 ? 0.4220 0.4121 0.4576 0.0071 -0.0946 -0.1501 83 LYS B CG 2753 C CD . LYS B 83 ? 0.4566 0.4645 0.4667 0.0240 -0.1033 -0.1761 83 LYS B CD 2754 C CE . LYS B 83 ? 0.4741 0.4791 0.4809 0.0359 -0.1020 -0.1946 83 LYS B CE 2755 N NZ . LYS B 83 ? 0.5066 0.5360 0.4836 0.0551 -0.1079 -0.2197 83 LYS B NZ 2756 N N . HIS B 84 ? 0.3569 0.3555 0.4326 -0.0270 -0.0921 -0.0903 84 HIS B N 2757 C CA . HIS B 84 ? 0.3477 0.3587 0.4238 -0.0305 -0.0896 -0.0751 84 HIS B CA 2758 C C . HIS B 84 ? 0.3588 0.3728 0.4605 -0.0353 -0.1089 -0.0843 84 HIS B C 2759 O O . HIS B 84 ? 0.3666 0.3678 0.4962 -0.0410 -0.1205 -0.0943 84 HIS B O 2760 C CB . HIS B 84 ? 0.3240 0.3300 0.4125 -0.0385 -0.0744 -0.0527 84 HIS B CB 2761 C CG . HIS B 84 ? 0.3173 0.3359 0.4052 -0.0395 -0.0698 -0.0377 84 HIS B CG 2762 N ND1 . HIS B 84 ? 0.3122 0.3361 0.4283 -0.0468 -0.0740 -0.0296 84 HIS B ND1 2763 C CD2 . HIS B 84 ? 0.3144 0.3416 0.3797 -0.0335 -0.0618 -0.0289 84 HIS B CD2 2764 C CE1 . HIS B 84 ? 0.3052 0.3409 0.4147 -0.0438 -0.0690 -0.0187 84 HIS B CE1 2765 N NE2 . HIS B 84 ? 0.3061 0.3418 0.3853 -0.0359 -0.0623 -0.0178 84 HIS B NE2 2766 N N . ALA B 85 ? 0.3619 0.3925 0.4573 -0.0329 -0.1138 -0.0808 85 ALA B N 2767 C CA . ALA B 85 ? 0.3800 0.4177 0.4995 -0.0364 -0.1343 -0.0914 85 ALA B CA 2768 C C . ALA B 85 ? 0.3674 0.3993 0.5334 -0.0512 -0.1368 -0.0805 85 ALA B C 2769 O O . ALA B 85 ? 0.3783 0.4106 0.5746 -0.0571 -0.1554 -0.0913 85 ALA B O 2770 C CB . ALA B 85 ? 0.3858 0.4444 0.4882 -0.0296 -0.1382 -0.0871 85 ALA B CB 2771 N N . SER B 86 ? 0.3474 0.3767 0.5196 -0.0568 -0.1184 -0.0586 86 SER B N 2772 C CA . SER B 86 ? 0.3410 0.3692 0.5544 -0.0698 -0.1163 -0.0438 86 SER B CA 2773 C C . SER B 86 ? 0.3544 0.3633 0.5960 -0.0781 -0.1244 -0.0495 86 SER B C 2774 O O . SER B 86 ? 0.3510 0.3608 0.6320 -0.0902 -0.1261 -0.0365 86 SER B O 2775 C CB . SER B 86 ? 0.3164 0.3482 0.5223 -0.0702 -0.0941 -0.0215 86 SER B CB 2776 O OG . SER B 86 ? 0.3129 0.3292 0.4977 -0.0665 -0.0835 -0.0221 86 SER B OG 2777 N N . MET B 87 ? 0.3719 0.3645 0.5948 -0.0713 -0.1283 -0.0667 87 MET B N 2778 C CA . MET B 87 ? 0.3891 0.3598 0.6377 -0.0767 -0.1368 -0.0733 87 MET B CA 2779 C C . MET B 87 ? 0.4153 0.3774 0.6622 -0.0697 -0.1590 -0.1049 87 MET B C 2780 O O . MET B 87 ? 0.4242 0.3931 0.6324 -0.0559 -0.1587 -0.1211 87 MET B O 2781 C CB . MET B 87 ? 0.3847 0.3433 0.6135 -0.0724 -0.1201 -0.0657 87 MET B CB 2782 C CG . MET B 87 ? 0.3652 0.3351 0.5809 -0.0736 -0.0980 -0.0408 87 MET B CG 2783 S SD . MET B 87 ? 0.3641 0.3208 0.5622 -0.0693 -0.0820 -0.0333 87 MET B SD 2784 C CE . MET B 87 ? 0.3624 0.3234 0.5143 -0.0547 -0.0771 -0.0502 87 MET B CE 2785 N N . ALA B 88 ? 0.4318 0.3800 0.7217 -0.0787 -0.1786 -0.1138 88 ALA B N 2786 C CA . ALA B 88 ? 0.4622 0.3987 0.7547 -0.0708 -0.2025 -0.1481 88 ALA B CA 2787 C C . ALA B 88 ? 0.4688 0.3885 0.7384 -0.0591 -0.1977 -0.1613 88 ALA B C 2788 O O . ALA B 88 ? 0.4922 0.4138 0.7364 -0.0440 -0.2077 -0.1902 88 ALA B O 2789 C CB . ALA B 88 ? 0.4819 0.4039 0.8333 -0.0847 -0.2263 -0.1536 88 ALA B CB 2790 N N . GLU B 89 ? 0.4492 0.3560 0.7268 -0.0647 -0.1821 -0.1402 89 GLU B N 2791 C CA . GLU B 89 ? 0.4560 0.3478 0.7170 -0.0541 -0.1771 -0.1500 89 GLU B CA 2792 C C . GLU B 89 ? 0.4273 0.3320 0.6498 -0.0487 -0.1502 -0.1321 89 GLU B C 2793 O O . GLU B 89 ? 0.3977 0.3124 0.6209 -0.0573 -0.1353 -0.1056 89 GLU B O 2794 C CB . GLU B 89 ? 0.4661 0.3300 0.7710 -0.0638 -0.1843 -0.1416 89 GLU B CB 2795 C CG . GLU B 89 ? 0.5005 0.3445 0.8468 -0.0671 -0.2143 -0.1650 89 GLU B CG 2796 C CD . GLU B 89 ? 0.5307 0.3661 0.8583 -0.0480 -0.2299 -0.2057 89 GLU B CD 2797 O OE1 . GLU B 89 ? 0.5276 0.3711 0.8137 -0.0329 -0.2156 -0.2126 89 GLU B OE1 2798 O OE2 . GLU B 89 ? 0.5595 0.3813 0.9156 -0.0475 -0.2571 -0.2319 89 GLU B OE2 2799 N N . PRO B 90 ? 0.4366 0.3423 0.6278 -0.0341 -0.1447 -0.1474 90 PRO B N 2800 C CA . PRO B 90 ? 0.4145 0.3293 0.5777 -0.0307 -0.1210 -0.1301 90 PRO B CA 2801 C C . PRO B 90 ? 0.4003 0.3003 0.5859 -0.0401 -0.1125 -0.1072 90 PRO B C 2802 O O . PRO B 90 ? 0.4148 0.2936 0.6314 -0.0437 -0.1241 -0.1102 90 PRO B O 2803 C CB . PRO B 90 ? 0.4311 0.3490 0.5681 -0.0139 -0.1205 -0.1530 90 PRO B CB 2804 C CG . PRO B 90 ? 0.4626 0.3841 0.5982 -0.0056 -0.1408 -0.1823 90 PRO B CG 2805 C CD . PRO B 90 ? 0.4695 0.3727 0.6491 -0.0188 -0.1595 -0.1819 90 PRO B CD 2806 N N . LYS B 91 ? 0.3758 0.2871 0.5467 -0.0434 -0.0935 -0.0846 91 LYS B N 2807 C CA . LYS B 91 ? 0.3681 0.2716 0.5529 -0.0499 -0.0836 -0.0620 91 LYS B CA 2808 C C . LYS B 91 ? 0.3584 0.2615 0.5209 -0.0405 -0.0723 -0.0639 91 LYS B C 2809 O O . LYS B 91 ? 0.3401 0.2581 0.4731 -0.0338 -0.0621 -0.0675 91 LYS B O 2810 C CB . LYS B 91 ? 0.3580 0.2767 0.5420 -0.0580 -0.0712 -0.0380 91 LYS B CB 2811 C CG . LYS B 91 ? 0.3600 0.2756 0.5575 -0.0636 -0.0616 -0.0141 91 LYS B CG 2812 C CD . LYS B 91 ? 0.3594 0.2890 0.5735 -0.0733 -0.0565 0.0074 91 LYS B CD 2813 C CE . LYS B 91 ? 0.3431 0.2918 0.5306 -0.0691 -0.0410 0.0155 91 LYS B CE 2814 N NZ . LYS B 91 ? 0.3422 0.3079 0.5452 -0.0756 -0.0344 0.0359 91 LYS B NZ 2815 N N . THR B 92 ? 0.3593 0.2460 0.5390 -0.0403 -0.0749 -0.0601 92 THR B N 2816 C CA . THR B 92 ? 0.3531 0.2392 0.5177 -0.0312 -0.0664 -0.0620 92 THR B CA 2817 C C . THR B 92 ? 0.3413 0.2246 0.5146 -0.0366 -0.0577 -0.0369 92 THR B C 2818 O O . THR B 92 ? 0.3465 0.2175 0.5473 -0.0441 -0.0641 -0.0233 92 THR B O 2819 C CB . THR B 92 ? 0.3769 0.2471 0.5522 -0.0215 -0.0796 -0.0844 92 THR B CB 2820 O OG1 . THR B 92 ? 0.3903 0.2667 0.5550 -0.0146 -0.0885 -0.1096 92 THR B OG1 2821 C CG2 . THR B 92 ? 0.3740 0.2479 0.5353 -0.0110 -0.0706 -0.0874 92 THR B CG2 2822 N N . VAL B 93 ? 0.3232 0.2196 0.4741 -0.0328 -0.0438 -0.0301 93 VAL B N 2823 C CA . VAL B 93 ? 0.3200 0.2167 0.4734 -0.0341 -0.0364 -0.0105 93 VAL B CA 2824 C C . VAL B 93 ? 0.3222 0.2181 0.4659 -0.0238 -0.0340 -0.0196 93 VAL B C 2825 O O . VAL B 93 ? 0.3145 0.2220 0.4393 -0.0182 -0.0282 -0.0317 93 VAL B O 2826 C CB . VAL B 93 ? 0.3007 0.2152 0.4395 -0.0381 -0.0241 0.0040 93 VAL B CB 2827 C CG1 . VAL B 93 ? 0.2969 0.2168 0.4297 -0.0354 -0.0162 0.0187 93 VAL B CG1 2828 C CG2 . VAL B 93 ? 0.3025 0.2197 0.4573 -0.0475 -0.0268 0.0154 93 VAL B CG2 2829 N N . TYR B 94 ? 0.3356 0.2189 0.4945 -0.0213 -0.0388 -0.0127 94 TYR B N 2830 C CA . TYR B 94 ? 0.3419 0.2261 0.4949 -0.0109 -0.0374 -0.0205 94 TYR B CA 2831 C C . TYR B 94 ? 0.3261 0.2248 0.4650 -0.0104 -0.0267 -0.0062 94 TYR B C 2832 O O . TYR B 94 ? 0.3163 0.2185 0.4558 -0.0161 -0.0233 0.0128 94 TYR B O 2833 C CB . TYR B 94 ? 0.3695 0.2328 0.5465 -0.0062 -0.0495 -0.0208 94 TYR B CB 2834 C CG . TYR B 94 ? 0.3939 0.2430 0.5837 -0.0014 -0.0622 -0.0444 94 TYR B CG 2835 C CD1 . TYR B 94 ? 0.4072 0.2435 0.6146 -0.0094 -0.0724 -0.0458 94 TYR B CD1 2836 C CD2 . TYR B 94 ? 0.4072 0.2587 0.5922 0.0121 -0.0644 -0.0669 94 TYR B CD2 2837 C CE1 . TYR B 94 ? 0.4328 0.2561 0.6518 -0.0035 -0.0867 -0.0711 94 TYR B CE1 2838 C CE2 . TYR B 94 ? 0.4301 0.2712 0.6244 0.0195 -0.0767 -0.0920 94 TYR B CE2 2839 C CZ . TYR B 94 ? 0.4432 0.2692 0.6537 0.0118 -0.0887 -0.0951 94 TYR B CZ 2840 O OH . TYR B 94 ? 0.4723 0.2878 0.6922 0.0205 -0.1034 -0.1233 94 TYR B OH 2841 N N . TRP B 95 ? 0.3198 0.2293 0.4470 -0.0031 -0.0219 -0.0165 95 TRP B N 2842 C CA . TRP B 95 ? 0.3193 0.2406 0.4376 -0.0009 -0.0158 -0.0070 95 TRP B CA 2843 C C . TRP B 95 ? 0.3412 0.2525 0.4727 0.0035 -0.0225 0.0041 95 TRP B C 2844 O O . TRP B 95 ? 0.3540 0.2523 0.5000 0.0095 -0.0307 -0.0035 95 TRP B O 2845 C CB . TRP B 95 ? 0.3094 0.2451 0.4194 0.0048 -0.0107 -0.0206 95 TRP B CB 2846 C CG . TRP B 95 ? 0.3014 0.2483 0.4071 0.0075 -0.0078 -0.0142 95 TRP B CG 2847 C CD1 . TRP B 95 ? 0.2939 0.2489 0.3896 0.0038 -0.0039 -0.0041 95 TRP B CD1 2848 C CD2 . TRP B 95 ? 0.3060 0.2592 0.4184 0.0160 -0.0102 -0.0197 95 TRP B CD2 2849 N NE1 . TRP B 95 ? 0.2919 0.2568 0.3868 0.0091 -0.0048 -0.0041 95 TRP B NE1 2850 C CE2 . TRP B 95 ? 0.2985 0.2632 0.4044 0.0159 -0.0085 -0.0127 95 TRP B CE2 2851 C CE3 . TRP B 95 ? 0.3160 0.2677 0.4401 0.0249 -0.0143 -0.0316 95 TRP B CE3 2852 C CZ2 . TRP B 95 ? 0.3017 0.2765 0.4137 0.0232 -0.0115 -0.0160 95 TRP B CZ2 2853 C CZ3 . TRP B 95 ? 0.3203 0.2831 0.4509 0.0326 -0.0159 -0.0339 95 TRP B CZ3 2854 C CH2 . TRP B 95 ? 0.3088 0.2830 0.4338 0.0310 -0.0148 -0.0256 95 TRP B CH2 2855 N N . ASP B 96 ? 0.3518 0.2698 0.4777 0.0019 -0.0195 0.0222 96 ASP B N 2856 C CA . ASP B 96 ? 0.3881 0.3019 0.5216 0.0073 -0.0247 0.0367 96 ASP B CA 2857 C C . ASP B 96 ? 0.4001 0.3336 0.5162 0.0121 -0.0198 0.0405 96 ASP B C 2858 O O . ASP B 96 ? 0.3994 0.3450 0.5025 0.0090 -0.0140 0.0497 96 ASP B O 2859 C CB . ASP B 96 ? 0.4028 0.3084 0.5478 0.0006 -0.0266 0.0591 96 ASP B CB 2860 C CG . ASP B 96 ? 0.4250 0.3245 0.5806 0.0060 -0.0327 0.0785 96 ASP B CG 2861 O OD1 . ASP B 96 ? 0.4289 0.3337 0.5787 0.0158 -0.0352 0.0754 96 ASP B OD1 2862 O OD2 . ASP B 96 ? 0.4469 0.3370 0.6190 -0.0001 -0.0356 0.0985 96 ASP B OD2 2863 N N . ARG B 97 ? 0.4181 0.3559 0.5354 0.0207 -0.0233 0.0319 97 ARG B N 2864 C CA . ARG B 97 ? 0.4313 0.3879 0.5354 0.0257 -0.0218 0.0320 97 ARG B CA 2865 C C . ARG B 97 ? 0.4519 0.4156 0.5466 0.0288 -0.0228 0.0531 97 ARG B C 2866 O O . ARG B 97 ? 0.4540 0.4349 0.5326 0.0315 -0.0205 0.0530 97 ARG B O 2867 C CB . ARG B 97 ? 0.4387 0.4003 0.5513 0.0347 -0.0271 0.0204 97 ARG B CB 2868 C CG . ARG B 97 ? 0.4644 0.4215 0.5852 0.0444 -0.0362 0.0322 97 ARG B CG 2869 C CD . ARG B 97 ? 0.4734 0.4394 0.6038 0.0537 -0.0411 0.0184 97 ARG B CD 2870 N NE . ARG B 97 ? 0.4740 0.4326 0.6191 0.0546 -0.0404 0.0018 97 ARG B NE 2871 C CZ . ARG B 97 ? 0.4721 0.4437 0.6268 0.0608 -0.0403 -0.0141 97 ARG B CZ 2872 N NH1 . ARG B 97 ? 0.4641 0.4556 0.6192 0.0651 -0.0423 -0.0163 97 ARG B NH1 2873 N NH2 . ARG B 97 ? 0.4744 0.4420 0.6394 0.0633 -0.0385 -0.0289 97 ARG B NH2 2874 N N . ASP B 98 ? 0.4733 0.4247 0.5793 0.0289 -0.0268 0.0712 98 ASP B N 2875 C CA . ASP B 98 ? 0.4918 0.4529 0.5897 0.0320 -0.0264 0.0962 98 ASP B CA 2876 C C . ASP B 98 ? 0.4943 0.4681 0.5797 0.0253 -0.0168 0.1052 98 ASP B C 2877 O O . ASP B 98 ? 0.5105 0.5039 0.5802 0.0306 -0.0136 0.1199 98 ASP B O 2878 C CB . ASP B 98 ? 0.5141 0.4570 0.6331 0.0323 -0.0335 0.1165 98 ASP B CB 2879 C CG . ASP B 98 ? 0.5293 0.4605 0.6616 0.0418 -0.0440 0.1079 98 ASP B CG 2880 O OD1 . ASP B 98 ? 0.5217 0.4678 0.6427 0.0511 -0.0463 0.0989 98 ASP B OD1 2881 O OD2 . ASP B 98 ? 0.5483 0.4556 0.7046 0.0404 -0.0511 0.1086 98 ASP B OD2 2882 N N . MET B 99 ? 0.4849 0.4502 0.5769 0.0155 -0.0126 0.0961 99 MET B N 2883 C CA . MET B 99 ? 0.4898 0.4664 0.5750 0.0092 -0.0042 0.1041 99 MET B CA 2884 C C . MET B 99 ? 0.4787 0.4681 0.5457 0.0108 0.0005 0.0851 99 MET B C 2885 O O . MET B 99 ? 0.5032 0.5006 0.5651 0.0067 0.0069 0.0856 99 MET B O 2886 C CB . MET B 99 ? 0.4864 0.4465 0.5921 -0.0021 -0.0046 0.1057 99 MET B CB 2887 N N . ASP C 4 ? 0.8946 0.8941 0.6701 0.0006 -0.2134 0.1577 0 ASP C N 2888 C CA . ASP C 4 ? 0.8952 0.8882 0.6778 -0.0046 -0.2156 0.1918 0 ASP C CA 2889 C C . ASP C 4 ? 0.8768 0.8505 0.6677 -0.0046 -0.1995 0.1937 0 ASP C C 2890 O O . ASP C 4 ? 0.8723 0.8238 0.6887 -0.0046 -0.2015 0.2107 0 ASP C O 2891 C CB . ASP C 4 ? 0.9243 0.9557 0.6775 -0.0125 -0.2237 0.2153 0 ASP C CB 2892 N N . PHE C 5 ? 0.8636 0.8456 0.6367 -0.0041 -0.1849 0.1746 1 PHE C N 2893 C CA . PHE C 5 ? 0.8515 0.8265 0.6250 -0.0065 -0.1714 0.1808 1 PHE C CA 2894 C C . PHE C 5 ? 0.8711 0.8646 0.6380 -0.0151 -0.1757 0.2154 1 PHE C C 2895 O O . PHE C 5 ? 0.8666 0.8435 0.6536 -0.0172 -0.1734 0.2322 1 PHE C O 2896 C CB . PHE C 5 ? 0.8231 0.7597 0.6267 -0.0008 -0.1662 0.1755 1 PHE C CB 2897 C CG . PHE C 5 ? 0.8037 0.7285 0.6101 0.0057 -0.1552 0.1462 1 PHE C CG 2898 C CD1 . PHE C 5 ? 0.7966 0.7253 0.5927 0.0049 -0.1417 0.1347 1 PHE C CD1 2899 C CD2 . PHE C 5 ? 0.7898 0.7001 0.6136 0.0126 -0.1583 0.1326 1 PHE C CD2 2900 C CE1 . PHE C 5 ? 0.7796 0.6981 0.5829 0.0105 -0.1328 0.1109 1 PHE C CE1 2901 C CE2 . PHE C 5 ? 0.7769 0.6783 0.6082 0.0181 -0.1484 0.1105 1 PHE C CE2 2902 C CZ . PHE C 5 ? 0.7670 0.6722 0.5883 0.0170 -0.1363 0.1000 1 PHE C CZ 2903 N N . HIS C 6 ? 0.8959 0.9265 0.6359 -0.0199 -0.1823 0.2257 2 HIS C N 2904 C CA . HIS C 6 ? 0.9189 0.9735 0.6541 -0.0284 -0.1897 0.2651 2 HIS C CA 2905 C C . HIS C 6 ? 0.9183 0.9789 0.6568 -0.0342 -0.1776 0.2844 2 HIS C C 2906 O O . HIS C 6 ? 0.9230 0.9784 0.6860 -0.0397 -0.1844 0.3184 2 HIS C O 2907 C CB . HIS C 6 ? 0.9508 1.0524 0.6478 -0.0312 -0.1965 0.2676 2 HIS C CB 2908 C CG . HIS C 6 ? 0.9815 1.1163 0.6689 -0.0403 -0.2029 0.3110 2 HIS C CG 2909 N ND1 . HIS C 6 ? 0.9991 1.1694 0.6633 -0.0458 -0.1901 0.3248 2 HIS C ND1 2910 C CD2 . HIS C 6 ? 1.0007 1.1408 0.7020 -0.0450 -0.2208 0.3462 2 HIS C CD2 2911 C CE1 . HIS C 6 ? 1.0288 1.2263 0.6922 -0.0538 -0.1993 0.3688 2 HIS C CE1 2912 N NE2 . HIS C 6 ? 1.0299 1.2091 0.7162 -0.0536 -0.2188 0.3828 2 HIS C NE2 2913 N N . HIS C 7 ? 0.9050 0.9774 0.6240 -0.0332 -0.1609 0.2633 3 HIS C N 2914 C CA . HIS C 7 ? 0.9051 0.9885 0.6260 -0.0388 -0.1484 0.2801 3 HIS C CA 2915 C C . HIS C 7 ? 0.8803 0.9214 0.6405 -0.0374 -0.1460 0.2827 3 HIS C C 2916 O O . HIS C 7 ? 0.8848 0.9262 0.6665 -0.0435 -0.1470 0.3126 3 HIS C O 2917 C CB . HIS C 7 ? 0.9069 1.0173 0.5979 -0.0374 -0.1313 0.2542 3 HIS C CB 2918 C CG . HIS C 7 ? 0.9374 1.0973 0.5882 -0.0384 -0.1327 0.2502 3 HIS C CG 2919 N ND1 . HIS C 7 ? 0.9392 1.1043 0.5736 -0.0319 -0.1382 0.2170 3 HIS C ND1 2920 C CD2 . HIS C 7 ? 0.9705 1.1798 0.5951 -0.0446 -0.1298 0.2748 3 HIS C CD2 2921 C CE1 . HIS C 7 ? 0.9728 1.1878 0.5710 -0.0334 -0.1399 0.2180 3 HIS C CE1 2922 N NE2 . HIS C 7 ? 0.9942 1.2386 0.5831 -0.0410 -0.1340 0.2536 3 HIS C NE2 2923 N N . ILE C 8 ? 0.8513 0.8589 0.6223 -0.0293 -0.1435 0.2519 4 ILE C N 2924 C CA . ILE C 8 ? 0.8266 0.7955 0.6313 -0.0258 -0.1425 0.2486 4 ILE C CA 2925 C C . ILE C 8 ? 0.8363 0.7872 0.6755 -0.0272 -0.1578 0.2744 4 ILE C C 2926 O O . ILE C 8 ? 0.8238 0.7584 0.6930 -0.0288 -0.1593 0.2869 4 ILE C O 2927 C CB . ILE C 8 ? 0.7996 0.7418 0.6068 -0.0161 -0.1382 0.2137 4 ILE C CB 2928 C CG1 . ILE C 8 ? 0.7901 0.7441 0.5769 -0.0148 -0.1231 0.1893 4 ILE C CG1 2929 C CG2 . ILE C 8 ? 0.7838 0.6893 0.6237 -0.0108 -0.1410 0.2112 4 ILE C CG2 2930 C CD1 . ILE C 8 ? 0.7814 0.7272 0.5790 -0.0164 -0.1131 0.1901 4 ILE C CD1 2931 N N . ARG C 9 ? 0.8522 0.8062 0.6911 -0.0264 -0.1704 0.2809 5 ARG C N 2932 C CA . ARG C 9 ? 0.8645 0.8050 0.7394 -0.0281 -0.1868 0.3064 5 ARG C CA 2933 C C . ARG C 9 ? 0.8909 0.8535 0.7776 -0.0387 -0.1915 0.3473 5 ARG C C 2934 O O . ARG C 9 ? 0.8984 0.8428 0.8288 -0.0404 -0.2004 0.3664 5 ARG C O 2935 C CB . ARG C 9 ? 0.8694 0.8115 0.7416 -0.0252 -0.1994 0.3047 5 ARG C CB 2936 C CG . ARG C 9 ? 0.8487 0.7670 0.7215 -0.0147 -0.1955 0.2691 5 ARG C CG 2937 C CD . ARG C 9 ? 0.8546 0.7744 0.7308 -0.0121 -0.2085 0.2687 5 ARG C CD 2938 N NE . ARG C 9 ? 0.8788 0.8336 0.7203 -0.0170 -0.2123 0.2735 5 ARG C NE 2939 N N . GLU C 10 ? 0.9143 0.9178 0.7650 -0.0452 -0.1854 0.3600 6 GLU C N 2940 C CA . GLU C 10 ? 0.9383 0.9707 0.7958 -0.0557 -0.1853 0.4006 6 GLU C CA 2941 C C . GLU C 10 ? 0.9348 0.9557 0.8140 -0.0575 -0.1739 0.4017 6 GLU C C 2942 O O . GLU C 10 ? 0.9409 0.9648 0.8553 -0.0645 -0.1795 0.4365 6 GLU C O 2943 C CB . GLU C 10 ? 0.9632 1.0481 0.7705 -0.0604 -0.1788 0.4089 6 GLU C CB 2944 N N . LYS C 11 ? 0.9225 0.9311 0.7846 -0.0515 -0.1594 0.3653 7 LYS C N 2945 C CA . LYS C 11 ? 0.9236 0.9163 0.8077 -0.0517 -0.1501 0.3605 7 LYS C CA 2946 C C . LYS C 11 ? 0.9200 0.8724 0.8572 -0.0487 -0.1632 0.3643 7 LYS C C 2947 O O . LYS C 11 ? 0.9340 0.8845 0.9090 -0.0544 -0.1676 0.3900 7 LYS C O 2948 C CB . LYS C 11 ? 0.9069 0.8911 0.7649 -0.0447 -0.1349 0.3187 7 LYS C CB 2949 C CG . LYS C 11 ? 0.8975 0.8660 0.7750 -0.0443 -0.1256 0.3101 7 LYS C CG 2950 C CD . LYS C 11 ? 0.8807 0.8046 0.7928 -0.0369 -0.1334 0.2939 7 LYS C CD 2951 C CE . LYS C 11 ? 0.8697 0.7715 0.7668 -0.0263 -0.1328 0.2586 7 LYS C CE 2952 N NZ . LYS C 11 ? 0.8651 0.7319 0.7957 -0.0193 -0.1430 0.2498 7 LYS C NZ 2953 N N . GLY C 12 ? 0.9088 0.8311 0.8512 -0.0393 -0.1693 0.3377 8 GLY C N 2954 C CA . GLY C 12 ? 0.9019 0.7874 0.8914 -0.0335 -0.1812 0.3323 8 GLY C CA 2955 C C . GLY C 12 ? 0.9214 0.8056 0.9579 -0.0392 -0.1992 0.3680 8 GLY C C 2956 O O . GLY C 12 ? 0.9315 0.7924 1.0170 -0.0374 -0.2085 0.3703 8 GLY C O 2957 N N . ASN C 13 ? 0.9341 0.8442 0.9588 -0.0457 -0.2056 0.3954 9 ASN C N 2958 C CA . ASN C 13 ? 0.9476 0.8626 1.0180 -0.0530 -0.2233 0.4368 9 ASN C CA 2959 C C . ASN C 13 ? 0.9575 0.8910 1.0535 -0.0637 -0.2219 0.4733 9 ASN C C 2960 O O . ASN C 13 ? 0.9732 0.8961 1.1294 -0.0676 -0.2372 0.5003 9 ASN C O 2961 C CB . ASN C 13 ? 0.9657 0.9073 1.0124 -0.0571 -0.2312 0.4575 9 ASN C CB 2962 N N . HIS C 14 ? 0.9532 0.9155 1.0088 -0.0682 -0.2038 0.4746 10 HIS C N 2963 C CA . HIS C 14 ? 0.9590 0.9436 1.0366 -0.0783 -0.1989 0.5094 10 HIS C CA 2964 C C . HIS C 14 ? 0.9362 0.8901 1.0526 -0.0751 -0.1966 0.4924 10 HIS C C 2965 O O . HIS C 14 ? 0.9403 0.8929 1.1112 -0.0816 -0.2044 0.5225 10 HIS C O 2966 C CB . HIS C 14 ? 0.9708 1.0029 0.9902 -0.0835 -0.1793 0.5158 10 HIS C CB 2967 N N . TRP C 15 ? 0.9049 0.8358 0.9958 -0.0651 -0.1873 0.4456 11 TRP C N 2968 C CA . TRP C 15 ? 0.8881 0.7902 1.0079 -0.0604 -0.1857 0.4232 11 TRP C CA 2969 C C . TRP C 15 ? 0.8720 0.7311 1.0283 -0.0495 -0.2011 0.3962 11 TRP C C 2970 O O . TRP C 15 ? 0.8634 0.6987 1.0257 -0.0418 -0.1987 0.3647 11 TRP C O 2971 C CB . TRP C 15 ? 0.8724 0.7816 0.9428 -0.0568 -0.1651 0.3919 11 TRP C CB 2972 C CG . TRP C 15 ? 0.8875 0.8395 0.9329 -0.0665 -0.1496 0.4158 11 TRP C CG 2973 C CD1 . TRP C 15 ? 0.9021 0.8918 0.8988 -0.0699 -0.1401 0.4234 11 TRP C CD1 2974 C CD2 . TRP C 15 ? 0.8912 0.8562 0.9617 -0.0736 -0.1422 0.4352 11 TRP C CD2 2975 N NE1 . TRP C 15 ? 0.9175 0.9452 0.9040 -0.0779 -0.1257 0.4450 11 TRP C NE1 2976 C CE2 . TRP C 15 ? 0.9091 0.9223 0.9415 -0.0807 -0.1260 0.4542 11 TRP C CE2 2977 C CE3 . TRP C 15 ? 0.8829 0.8249 1.0060 -0.0741 -0.1480 0.4371 11 TRP C CE3 2978 C CZ2 . TRP C 15 ? 0.9143 0.9546 0.9597 -0.0886 -0.1134 0.4769 11 TRP C CZ2 2979 C CZ3 . TRP C 15 ? 0.8904 0.8564 1.0293 -0.0825 -0.1372 0.4602 11 TRP C CZ3 2980 C CH2 . TRP C 15 ? 0.9045 0.9198 1.0048 -0.0897 -0.1190 0.4809 11 TRP C CH2 2981 N N . LYS C 16 ? 0.8696 0.7216 1.0493 -0.0485 -0.2166 0.4078 12 LYS C N 2982 C CA . LYS C 16 ? 0.8569 0.6738 1.0878 -0.0397 -0.2341 0.3911 12 LYS C CA 2983 C C . LYS C 16 ? 0.8589 0.6674 1.1624 -0.0452 -0.2485 0.4158 12 LYS C C 2984 O O . LYS C 16 ? 0.8483 0.6294 1.1895 -0.0376 -0.2565 0.3910 12 LYS C O 2985 C CB . LYS C 16 ? 0.8612 0.6761 1.0997 -0.0376 -0.2464 0.3985 12 LYS C CB 2986 N N . ASN C 17 ? 0.8703 0.7051 1.1943 -0.0584 -0.2522 0.4650 13 ASN C N 2987 C CA . ASN C 17 ? 0.8778 0.7094 1.2791 -0.0659 -0.2670 0.4981 13 ASN C CA 2988 C C . ASN C 17 ? 0.8669 0.6899 1.2864 -0.0659 -0.2609 0.4859 13 ASN C C 2989 O O . ASN C 17 ? 0.8679 0.6690 1.3589 -0.0647 -0.2775 0.4866 13 ASN C O 2990 C CB . ASN C 17 ? 0.8977 0.7680 1.3071 -0.0810 -0.2679 0.5581 13 ASN C CB 2991 N N . PHE C 18 ? 0.8567 0.6966 1.2164 -0.0669 -0.2387 0.4736 14 PHE C N 2992 C CA . PHE C 18 ? 0.8497 0.6813 1.2237 -0.0664 -0.2325 0.4596 14 PHE C CA 2993 C C . PHE C 18 ? 0.8309 0.6226 1.2200 -0.0521 -0.2417 0.4094 14 PHE C C 2994 O O . PHE C 18 ? 0.8263 0.5997 1.2718 -0.0507 -0.2538 0.4043 14 PHE C O 2995 C CB . PHE C 18 ? 0.8459 0.7053 1.1541 -0.0698 -0.2067 0.4551 14 PHE C CB 2996 C CG . PHE C 18 ? 0.8370 0.6848 1.1566 -0.0677 -0.2005 0.4348 14 PHE C CG 2997 C CD1 . PHE C 18 ? 0.8453 0.6910 1.2320 -0.0744 -0.2094 0.4594 14 PHE C CD1 2998 C CD2 . PHE C 18 ? 0.8211 0.6597 1.0905 -0.0590 -0.1876 0.3925 14 PHE C CD2 2999 C CE1 . PHE C 18 ? 0.8364 0.6709 1.2370 -0.0723 -0.2057 0.4402 14 PHE C CE1 3000 C CE2 . PHE C 18 ? 0.8127 0.6409 1.0947 -0.0571 -0.1838 0.3750 14 PHE C CE2 3001 C CZ . PHE C 18 ? 0.8172 0.6429 1.1638 -0.0636 -0.1930 0.3977 14 PHE C CZ 3002 N N . LEU C 19 ? 0.8180 0.5991 1.1579 -0.0413 -0.2364 0.3733 15 LEU C N 3003 C CA . LEU C 19 ? 0.8049 0.5549 1.1498 -0.0267 -0.2430 0.3260 15 LEU C CA 3004 C C . LEU C 19 ? 0.8157 0.5424 1.2252 -0.0203 -0.2671 0.3208 15 LEU C C 3005 O O . LEU C 19 ? 0.8124 0.5154 1.2459 -0.0086 -0.2772 0.2854 15 LEU C O 3006 C CB . LEU C 19 ? 0.7874 0.5376 1.0628 -0.0176 -0.2287 0.2937 15 LEU C CB 3007 C CG . LEU C 19 ? 0.7784 0.5477 0.9910 -0.0207 -0.2060 0.2876 15 LEU C CG 3008 C CD1 . LEU C 19 ? 0.7632 0.5263 0.9258 -0.0099 -0.1973 0.2535 15 LEU C CD1 3009 C CD2 . LEU C 19 ? 0.7716 0.5377 0.9938 -0.0219 -0.2012 0.2793 15 LEU C CD2 3010 C C1 . NAG D . ? 0.6893 0.9216 0.4205 -0.0085 0.0271 -0.0388 301 NAG A C1 3011 C C2 . NAG D . ? 0.7147 0.9967 0.4335 -0.0028 0.0349 -0.0763 301 NAG A C2 3012 C C3 . NAG D . ? 0.7505 1.0735 0.4253 -0.0026 0.0302 -0.0705 301 NAG A C3 3013 C C4 . NAG D . ? 0.7677 1.1071 0.4187 -0.0112 0.0357 -0.0220 301 NAG A C4 3014 C C5 . NAG D . ? 0.7383 1.0206 0.4105 -0.0164 0.0254 0.0108 301 NAG A C5 3015 C C6 . NAG D . ? 0.7505 1.0417 0.4115 -0.0252 0.0270 0.0605 301 NAG A C6 3016 C C7 . NAG D . ? 0.6940 0.9655 0.4709 0.0091 0.0348 -0.1491 301 NAG A C7 3017 C C8 . NAG D . ? 0.6800 0.9314 0.4908 0.0161 0.0225 -0.1851 301 NAG A C8 3018 N N2 . NAG D . ? 0.6993 0.9638 0.4457 0.0046 0.0268 -0.1165 301 NAG A N2 3019 O O3 . NAG D . ? 0.7752 1.1509 0.4358 0.0036 0.0383 -0.1079 301 NAG A O3 3020 O O4 . NAG D . ? 0.8061 1.1852 0.4159 -0.0113 0.0296 -0.0134 301 NAG A O4 3021 O O5 . NAG D . ? 0.7072 0.9566 0.4166 -0.0158 0.0310 0.0014 301 NAG A O5 3022 O O6 . NAG D . ? 0.7597 1.0790 0.4274 -0.0291 0.0456 0.0718 301 NAG A O6 3023 O O7 . NAG D . ? 0.7002 0.9934 0.4831 0.0075 0.0507 -0.1494 301 NAG A O7 3024 C C1 . NAG E . ? 0.8456 1.2872 0.4272 -0.0137 0.0462 -0.0014 302 NAG A C1 3025 C C2 . NAG E . ? 0.8808 1.3576 0.4199 -0.0162 0.0371 0.0240 302 NAG A C2 3026 C C3 . NAG E . ? 0.9258 1.4815 0.4263 -0.0161 0.0533 0.0287 302 NAG A C3 3027 C C4 . NAG E . ? 0.9355 1.5262 0.4363 -0.0066 0.0669 -0.0254 302 NAG A C4 3028 C C5 . NAG E . ? 0.8990 1.4484 0.4486 -0.0070 0.0772 -0.0370 302 NAG A C5 3029 C C6 . NAG E . ? 0.9073 1.4910 0.4680 0.0012 0.0935 -0.0860 302 NAG A C6 3030 C C7 . NAG E . ? 0.8615 1.2644 0.4164 -0.0265 0.0093 0.0886 302 NAG A C7 3031 C C8 . NAG E . ? 0.8509 1.2251 0.4235 -0.0355 0.0040 0.1400 302 NAG A C8 3032 N N2 . NAG E . ? 0.8714 1.3146 0.4211 -0.0254 0.0293 0.0757 302 NAG A N2 3033 O O3 . NAG E . ? 0.9603 1.5521 0.4184 -0.0158 0.0411 0.0400 302 NAG A O3 3034 O O4 . NAG E . ? 0.9804 1.6490 0.4439 -0.0061 0.0845 -0.0190 302 NAG A O4 3035 O O5 . NAG E . ? 0.8603 1.3407 0.4409 -0.0061 0.0591 -0.0463 302 NAG A O5 3036 O O6 . NAG E . ? 0.9430 1.5821 0.4694 0.0102 0.0918 -0.1240 302 NAG A O6 3037 O O7 . NAG E . ? 0.8622 1.2523 0.4125 -0.0205 -0.0043 0.0609 302 NAG A O7 3038 C C1 . NAG F . ? 0.6263 0.3245 0.7848 0.1291 -0.2167 -0.0242 303 NAG A C1 3039 C C2 . NAG F . ? 0.6387 0.3282 0.8503 0.1305 -0.2307 -0.0211 303 NAG A C2 3040 C C3 . NAG F . ? 0.6394 0.3399 0.8366 0.1371 -0.2195 -0.0234 303 NAG A C3 3041 C C4 . NAG F . ? 0.6480 0.3653 0.8098 0.1536 -0.2051 -0.0528 303 NAG A C4 3042 C C5 . NAG F . ? 0.6456 0.3700 0.7598 0.1509 -0.1942 -0.0527 303 NAG A C5 3043 C C6 . NAG F . ? 0.6617 0.4061 0.7437 0.1676 -0.1818 -0.0792 303 NAG A C6 3044 C C7 . NAG F . ? 0.6389 0.3066 0.9243 0.1079 -0.2576 0.0209 303 NAG A C7 3045 C C8 . NAG F . ? 0.6376 0.3024 0.9459 0.0900 -0.2643 0.0631 303 NAG A C8 3046 N N2 . NAG F . ? 0.6326 0.3125 0.8724 0.1135 -0.2406 0.0139 303 NAG A N2 3047 O O3 . NAG F . ? 0.6448 0.3370 0.8975 0.1406 -0.2343 -0.0253 303 NAG A O3 3048 O O4 . NAG F . ? 0.6491 0.3788 0.7917 0.1558 -0.1907 -0.0457 303 NAG A O4 3049 O O5 . NAG F . ? 0.6403 0.3517 0.7745 0.1461 -0.2082 -0.0548 303 NAG A O5 3050 O O6 . NAG F . ? 0.6726 0.4234 0.7150 0.1646 -0.1740 -0.0770 303 NAG A O6 3051 O O7 . NAG F . ? 0.6474 0.3084 0.9565 0.1166 -0.2679 -0.0041 303 NAG A O7 3052 C C1 . NAG G . ? 0.6693 0.4043 0.8427 0.1701 -0.1935 -0.0663 304 NAG A C1 3053 C C2 . NAG G . ? 0.6668 0.4217 0.8106 0.1770 -0.1737 -0.0668 304 NAG A C2 3054 C C3 . NAG G . ? 0.6837 0.4469 0.8625 0.1927 -0.1752 -0.0894 304 NAG A C3 3055 C C4 . NAG G . ? 0.6902 0.4344 0.9262 0.1864 -0.1941 -0.0788 304 NAG A C4 3056 C C5 . NAG G . ? 0.6947 0.4186 0.9582 0.1780 -0.2140 -0.0750 304 NAG A C5 3057 C C6 . NAG G . ? 0.6991 0.4053 1.0233 0.1695 -0.2342 -0.0569 304 NAG A C6 3058 C C7 . NAG G . ? 0.6528 0.4390 0.7128 0.1800 -0.1405 -0.0613 304 NAG A C7 3059 C C8 . NAG G . ? 0.6542 0.4591 0.6729 0.1872 -0.1276 -0.0706 304 NAG A C8 3060 N N2 . NAG G . ? 0.6641 0.4366 0.7605 0.1834 -0.1583 -0.0767 304 NAG A N2 3061 O O3 . NAG G . ? 0.6775 0.4604 0.8340 0.1979 -0.1561 -0.0851 304 NAG A O3 3062 O O4 . NAG G . ? 0.7155 0.4667 0.9914 0.2028 -0.1974 -0.1057 304 NAG A O4 3063 O O5 . NAG G . ? 0.6773 0.3980 0.9003 0.1635 -0.2086 -0.0521 304 NAG A O5 3064 O O6 . NAG G . ? 0.6886 0.3935 0.9969 0.1537 -0.2304 -0.0193 304 NAG A O6 3065 O O7 . NAG G . ? 0.6393 0.4240 0.7014 0.1717 -0.1361 -0.0403 304 NAG A O7 3066 C C1 . BMA H . ? 0.7194 0.4791 1.0042 0.2042 -0.1887 -0.0956 305 BMA A C1 3067 C C2 . BMA H . ? 0.7368 0.4912 1.0883 0.2143 -0.2034 -0.1143 305 BMA A C2 3068 C C3 . BMA H . ? 0.7378 0.5014 1.1038 0.2166 -0.1950 -0.1049 305 BMA A C3 3069 C C4 . BMA H . ? 0.7338 0.5261 1.0547 0.2275 -0.1684 -0.1148 305 BMA A C4 3070 C C5 . BMA H . ? 0.7169 0.5123 0.9753 0.2169 -0.1564 -0.0956 305 BMA A C5 3071 C C6 . BMA H . ? 0.7152 0.5413 0.9346 0.2282 -0.1310 -0.1038 305 BMA A C6 3072 O O2 . BMA H . ? 0.7547 0.5221 1.1157 0.2343 -0.2028 -0.1576 305 BMA A O2 3073 O O3 . BMA H . ? 0.7607 0.5221 1.1912 0.2284 -0.2071 -0.1268 305 BMA A O3 3074 O O4 . BMA H . ? 0.7290 0.5288 1.0679 0.2280 -0.1613 -0.1024 305 BMA A O4 3075 O O5 . BMA H . ? 0.7218 0.5078 0.9675 0.2151 -0.1654 -0.1057 305 BMA A O5 3076 O O6 . BMA H . ? 0.6993 0.5278 0.8671 0.2186 -0.1216 -0.0867 305 BMA A O6 3077 C C1 . MAN I . ? 0.6977 0.5562 0.8337 0.2279 -0.0984 -0.0879 306 MAN A C1 3078 C C2 . MAN I . ? 0.6823 0.5400 0.7752 0.2147 -0.0903 -0.0632 306 MAN A C2 3079 C C3 . MAN I . ? 0.6887 0.5416 0.7540 0.2138 -0.0956 -0.0733 306 MAN A C3 3080 C C4 . MAN I . ? 0.7110 0.5880 0.7679 0.2340 -0.0897 -0.1056 306 MAN A C4 3081 C C5 . MAN I . ? 0.7256 0.6021 0.8277 0.2466 -0.0989 -0.1317 306 MAN A C5 3082 C C6 . MAN I . ? 0.7512 0.6564 0.8439 0.2685 -0.0931 -0.1688 306 MAN A C6 3083 O O2 . MAN I . ? 0.6775 0.5634 0.7508 0.2210 -0.0687 -0.0557 306 MAN A O2 3084 O O3 . MAN I . ? 0.6751 0.5308 0.7028 0.2036 -0.0864 -0.0527 306 MAN A O3 3085 O O4 . MAN I . ? 0.7194 0.5900 0.7547 0.2329 -0.0980 -0.1158 306 MAN A O4 3086 O O5 . MAN I . ? 0.7173 0.6000 0.8425 0.2468 -0.0907 -0.1193 306 MAN A O5 3087 O O6 . MAN I . ? 0.7661 0.6793 0.9019 0.2826 -0.0957 -0.1933 306 MAN A O6 3088 C C1 . FUC J . ? 0.6723 0.4355 0.6752 0.1591 -0.1552 -0.0582 307 FUC A C1 3089 C C2 . FUC J . ? 0.6770 0.4514 0.6439 0.1618 -0.1480 -0.0638 307 FUC A C2 3090 C C3 . FUC J . ? 0.6790 0.4373 0.6517 0.1502 -0.1580 -0.0562 307 FUC A C3 3091 C C4 . FUC J . ? 0.6659 0.4121 0.6459 0.1320 -0.1572 -0.0270 307 FUC A C4 3092 C C5 . FUC J . ? 0.6639 0.4040 0.6719 0.1300 -0.1621 -0.0187 307 FUC A C5 3093 C C6 . FUC J . ? 0.6539 0.3902 0.6578 0.1133 -0.1587 0.0106 307 FUC A C6 3094 O O2 . FUC J . ? 0.6985 0.4882 0.6605 0.1800 -0.1496 -0.0933 307 FUC A O2 3095 O O3 . FUC J . ? 0.6781 0.4465 0.6188 0.1514 -0.1515 -0.0585 307 FUC A O3 3096 O O4 . FUC J . ? 0.6546 0.4108 0.6022 0.1254 -0.1417 -0.0114 307 FUC A O4 3097 O O5 . FUC J . ? 0.6622 0.4157 0.6633 0.1418 -0.1532 -0.0289 307 FUC A O5 3098 C C1 . MAN K . ? 0.7675 0.5088 1.2457 0.2153 -0.2257 -0.0988 308 MAN A C1 3099 C C2 . MAN K . ? 0.7827 0.5266 1.3281 0.2296 -0.2337 -0.1221 308 MAN A C2 3100 C C3 . MAN K . ? 0.8036 0.5400 1.3990 0.2412 -0.2510 -0.1569 308 MAN A C3 3101 C C4 . MAN K . ? 0.8031 0.5149 1.4141 0.2260 -0.2724 -0.1373 308 MAN A C4 3102 C C5 . MAN K . ? 0.7886 0.5005 1.3253 0.2117 -0.2605 -0.1118 308 MAN A C5 3103 C C6 . MAN K . ? 0.7883 0.4784 1.3426 0.1946 -0.2800 -0.0850 308 MAN A C6 3104 O O2 . MAN K . ? 0.7832 0.5130 1.3699 0.2172 -0.2480 -0.0903 308 MAN A O2 3105 O O3 . MAN K . ? 0.8132 0.5470 1.4841 0.2507 -0.2636 -0.1720 308 MAN A O3 3106 O O4 . MAN K . ? 0.8194 0.5286 1.4673 0.2396 -0.2849 -0.1768 308 MAN A O4 3107 O O5 . MAN K . ? 0.7723 0.4913 1.2687 0.2016 -0.2461 -0.0812 308 MAN A O5 3108 O O6 . MAN K . ? 0.7784 0.4721 1.2655 0.1866 -0.2675 -0.0752 308 MAN A O6 3109 C C1 . NAG L . ? 0.7608 1.0844 0.6348 0.0601 -0.0786 -0.4027 309 NAG A C1 3110 C C2 . NAG L . ? 0.7899 1.1521 0.6915 0.0708 -0.0851 -0.4654 309 NAG A C2 3111 C C3 . NAG L . ? 0.7962 1.1849 0.7062 0.0731 -0.0649 -0.4857 309 NAG A C3 3112 C C4 . NAG L . ? 0.7573 1.0993 0.7124 0.0676 -0.0556 -0.4617 309 NAG A C4 3113 C C5 . NAG L . ? 0.7348 1.0395 0.6578 0.0573 -0.0515 -0.4004 309 NAG A C5 3114 C C6 . NAG L . ? 0.6991 0.9580 0.6635 0.0524 -0.0445 -0.3761 309 NAG A C6 3115 C C7 . NAG L . ? 0.8422 1.2478 0.7061 0.0795 -0.1179 -0.5006 309 NAG A C7 3116 C C8 . NAG L . ? 0.8885 1.3511 0.6968 0.0849 -0.1262 -0.5221 309 NAG A C8 3117 N N2 . NAG L . ? 0.8326 1.2425 0.6877 0.0759 -0.0948 -0.4866 309 NAG A N2 3118 O O3 . NAG L . ? 0.8187 1.2397 0.7651 0.0843 -0.0725 -0.5483 309 NAG A O3 3119 O O4 . NAG L . ? 0.7650 1.1326 0.7249 0.0689 -0.0361 -0.4762 309 NAG A O4 3120 O O5 . NAG L . ? 0.7275 1.0111 0.6440 0.0564 -0.0695 -0.3863 309 NAG A O5 3121 O O6 . NAG L . ? 0.6819 0.9134 0.7162 0.0563 -0.0575 -0.3973 309 NAG A O6 3122 O O7 . NAG L . ? 0.8175 1.1785 0.7313 0.0786 -0.1318 -0.4950 309 NAG A O7 3123 C C1 . CIT M . ? 0.8534 0.6992 0.7735 -0.0084 -0.0715 0.1251 310 CIT A C1 3124 O O1 . CIT M . ? 0.8538 0.6818 0.7972 -0.0070 -0.0815 0.1294 310 CIT A O1 3125 O O2 . CIT M . ? 0.8531 0.7134 0.7685 -0.0105 -0.0603 0.1164 310 CIT A O2 3126 C C2 . CIT M . ? 0.8507 0.7012 0.7530 -0.0072 -0.0746 0.1298 310 CIT A C2 3127 C C3 . CIT M . ? 0.8380 0.6918 0.7181 -0.0020 -0.0700 0.1118 310 CIT A C3 3128 O O7 . CIT M . ? 0.8330 0.6898 0.7132 -0.0004 -0.0617 0.0951 310 CIT A O7 3129 C C4 . CIT M . ? 0.8345 0.7125 0.6951 -0.0062 -0.0660 0.1174 310 CIT A C4 3130 C C5 . CIT M . ? 0.8376 0.7467 0.6871 -0.0118 -0.0536 0.1147 310 CIT A C5 3131 O O3 . CIT M . ? 0.8177 0.7311 0.6741 -0.0120 -0.0453 0.1028 310 CIT A O3 3132 O O4 . CIT M . ? 0.8479 0.7806 0.6812 -0.0157 -0.0524 0.1239 310 CIT A O4 3133 C C6 . CIT M . ? 0.8400 0.6722 0.7203 0.0065 -0.0793 0.1051 310 CIT A C6 3134 O O5 . CIT M . ? 0.8302 0.6514 0.7105 0.0132 -0.0787 0.0905 310 CIT A O5 3135 O O6 . CIT M . ? 0.8513 0.6797 0.7326 0.0069 -0.0870 0.1153 310 CIT A O6 3137 C C1 . PLM O . ? 0.8463 0.6894 0.7832 -0.0110 -0.1401 0.2238 101 PLM C C1 3138 O O2 . PLM O . ? 0.8583 0.6780 0.8235 -0.0050 -0.1502 0.2185 101 PLM C O2 3139 C C2 . PLM O . ? 0.8267 0.6710 0.7404 -0.0079 -0.1259 0.1996 101 PLM C C2 3140 C C3 . PLM O . ? 0.8019 0.6280 0.7080 0.0030 -0.1250 0.1725 101 PLM C C3 3141 C C4 . PLM O . ? 0.7855 0.6133 0.6735 0.0060 -0.1125 0.1513 101 PLM C C4 3142 C C5 . PLM O . ? 0.7680 0.5737 0.6652 0.0158 -0.1135 0.1322 101 PLM C C5 3143 C C6 . PLM O . ? 0.7674 0.5592 0.6908 0.0162 -0.1208 0.1356 101 PLM C C6 3144 C C7 . PLM O . ? 0.7527 0.5345 0.6748 0.0223 -0.1172 0.1167 101 PLM C C7 3145 C C8 . PLM O . ? 0.7512 0.5149 0.7007 0.0280 -0.1293 0.1116 101 PLM C C8 3146 C C9 . PLM O . ? 0.7422 0.5012 0.6948 0.0294 -0.1277 0.1008 101 PLM C C9 3147 C CA . PLM O . ? 0.7428 0.4848 0.7205 0.0375 -0.1417 0.0891 101 PLM C CA 3148 C CB . PLM O . ? 0.7418 0.4803 0.7360 0.0342 -0.1445 0.0881 101 PLM C CB 3149 C CC . PLM O . ? 0.7482 0.4852 0.7788 0.0250 -0.1525 0.1082 101 PLM C CC 3150 C CD . PLM O . ? 0.7458 0.4850 0.7908 0.0188 -0.1506 0.1121 101 PLM C CD 3151 C CE . PLM O . ? 0.7424 0.5029 0.7731 0.0071 -0.1346 0.1311 101 PLM C CE 3152 C CF . PLM O . ? 0.7354 0.5009 0.7785 0.0018 -0.1295 0.1327 101 PLM C CF 3153 C CG . PLM O . ? 0.7280 0.5134 0.7417 -0.0025 -0.1109 0.1319 101 PLM C CG 3154 C C1 . OCA P . ? 0.8524 0.7123 0.6947 0.0110 -0.1200 0.1399 102 OCA C C1 3155 C C2 . OCA P . ? 0.8202 0.6712 0.6621 0.0178 -0.1110 0.1177 102 OCA C C2 3156 C C3 . OCA P . ? 0.8024 0.6466 0.6518 0.0248 -0.1137 0.1090 102 OCA C C3 3157 C C4 . OCA P . ? 0.7944 0.6546 0.6350 0.0239 -0.1116 0.0970 102 OCA C C4 3158 C C5 . OCA P . ? 0.7743 0.6261 0.6294 0.0315 -0.1093 0.0850 102 OCA C C5 3159 C C6 . OCA P . ? 0.7695 0.6361 0.6234 0.0301 -0.1066 0.0696 102 OCA C C6 3160 C C7 . OCA P . ? 0.7551 0.6164 0.6308 0.0365 -0.1058 0.0614 102 OCA C C7 3161 C C8 . OCA P . ? 0.7517 0.6265 0.6349 0.0352 -0.1049 0.0445 102 OCA C C8 3162 O O1 . OCA P . ? 0.8613 0.7128 0.7171 0.0089 -0.1229 0.1526 102 OCA C O1 3163 O O2 . OCA P . ? 0.8765 0.7528 0.7084 0.0079 -0.1253 0.1456 102 OCA C O2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 SER 1 1 ? ? ? A . n A 1 2 GLU 2 2 ? ? ? A . n A 1 3 ALA 3 3 ? ? ? A . n A 1 4 GLN 4 4 ? ? ? A . n A 1 5 GLN 5 5 ? ? ? A . n A 1 6 LYS 6 6 6 LYS LYS A . n A 1 7 ASN 7 7 7 ASN ASN A . n A 1 8 TYR 8 8 8 TYR TYR A . n A 1 9 THR 9 9 9 THR THR A . n A 1 10 PHE 10 10 10 PHE PHE A . n A 1 11 ARG 11 11 11 ARG ARG A . n A 1 12 CYS 12 12 12 CYS CYS A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 GLN 14 14 14 GLN GLN A . n A 1 15 MET 15 15 15 MET MET A . n A 1 16 SER 16 16 16 SER SER A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 PHE 18 18 18 PHE PHE A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 ASN 20 20 20 ASN ASN A . n A 1 21 ARG 21 21 21 ARG ARG A . n A 1 22 SER 22 22 22 SER SER A . n A 1 23 TRP 23 23 23 TRP TRP A . n A 1 24 SER 24 24 24 SER SER A . n A 1 25 ARG 25 25 25 ARG ARG A . n A 1 26 THR 26 26 26 THR THR A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 SER 28 28 28 SER SER A . n A 1 29 VAL 29 29 29 VAL VAL A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 TRP 31 31 31 TRP TRP A . n A 1 32 LEU 32 32 32 LEU LEU A . n A 1 33 GLY 33 33 33 GLY GLY A . n A 1 34 ASP 34 34 34 ASP ASP A . n A 1 35 LEU 35 35 35 LEU LEU A . n A 1 36 GLN 36 36 36 GLN GLN A . n A 1 37 THR 37 37 37 THR THR A . n A 1 38 HIS 38 38 38 HIS HIS A . n A 1 39 ARG 39 39 39 ARG ARG A . n A 1 40 TRP 40 40 40 TRP TRP A . n A 1 41 SER 41 41 41 SER SER A . n A 1 42 ASN 42 42 42 ASN ASN A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 SER 44 44 44 SER SER A . n A 1 45 ALA 45 45 45 ALA ALA A . n A 1 46 THR 46 46 46 THR THR A . n A 1 47 ILE 47 47 47 ILE ILE A . n A 1 48 SER 48 48 48 SER SER A . n A 1 49 PHE 49 49 49 PHE PHE A . n A 1 50 THR 50 50 50 THR THR A . n A 1 51 LYS 51 51 51 LYS LYS A . n A 1 52 PRO 52 52 52 PRO PRO A . n A 1 53 TRP 53 53 53 TRP TRP A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 GLN 55 55 55 GLN GLN A . n A 1 56 GLY 56 56 56 GLY GLY A . n A 1 57 LYS 57 57 57 LYS LYS A . n A 1 58 LEU 58 58 58 LEU LEU A . n A 1 59 SER 59 59 59 SER SER A . n A 1 60 ASN 60 60 60 ASN ASN A . n A 1 61 GLN 61 61 61 GLN GLN A . n A 1 62 GLN 62 62 62 GLN GLN A . n A 1 63 TRP 63 63 63 TRP TRP A . n A 1 64 GLU 64 64 64 GLU GLU A . n A 1 65 LYS 65 65 65 LYS LYS A . n A 1 66 LEU 66 66 66 LEU LEU A . n A 1 67 GLN 67 67 67 GLN GLN A . n A 1 68 HIS 68 68 68 HIS HIS A . n A 1 69 MET 69 69 69 MET MET A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 GLN 71 71 71 GLN GLN A . n A 1 72 VAL 72 72 72 VAL VAL A . n A 1 73 TYR 73 73 73 TYR TYR A . n A 1 74 ARG 74 74 74 ARG ARG A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 SER 76 76 76 SER SER A . n A 1 77 PHE 77 77 77 PHE PHE A . n A 1 78 THR 78 78 78 THR THR A . n A 1 79 ARG 79 79 79 ARG ARG A . n A 1 80 ASP 80 80 80 ASP ASP A . n A 1 81 ILE 81 81 81 ILE ILE A . n A 1 82 GLN 82 82 82 GLN GLN A . n A 1 83 GLU 83 83 83 GLU GLU A . n A 1 84 LEU 84 84 84 LEU LEU A . n A 1 85 VAL 85 85 85 VAL VAL A . n A 1 86 LYS 86 86 86 LYS LYS A . n A 1 87 MET 87 87 87 MET MET A . n A 1 88 MET 88 88 88 MET MET A . n A 1 89 SER 89 89 ? ? ? A . n A 1 90 PRO 90 90 ? ? ? A . n A 1 91 LYS 91 91 ? ? ? A . n A 1 92 GLU 92 92 ? ? ? A . n A 1 93 ASP 93 93 93 ASP ASP A . n A 1 94 TYR 94 94 94 TYR TYR A . n A 1 95 PRO 95 95 95 PRO PRO A . n A 1 96 ILE 96 96 96 ILE ILE A . n A 1 97 GLU 97 97 97 GLU GLU A . n A 1 98 ILE 98 98 98 ILE ILE A . n A 1 99 GLN 99 99 99 GLN GLN A . n A 1 100 LEU 100 100 100 LEU LEU A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 ALA 102 102 102 ALA ALA A . n A 1 103 GLY 103 103 103 GLY GLY A . n A 1 104 CYS 104 104 104 CYS CYS A . n A 1 105 GLU 105 105 105 GLU GLU A . n A 1 106 MET 106 106 106 MET MET A . n A 1 107 TYR 107 107 107 TYR TYR A . n A 1 108 PRO 108 108 ? ? ? A . n A 1 109 GLY 109 109 ? ? ? A . n A 1 110 ASN 110 110 ? ? ? A . n A 1 111 ALA 111 111 111 ALA ALA A . n A 1 112 SER 112 112 112 SER SER A . n A 1 113 GLU 113 113 113 GLU GLU A . n A 1 114 SER 114 114 114 SER SER A . n A 1 115 PHE 115 115 115 PHE PHE A . n A 1 116 LEU 116 116 116 LEU LEU A . n A 1 117 HIS 117 117 117 HIS HIS A . n A 1 118 VAL 118 118 118 VAL VAL A . n A 1 119 ALA 119 119 119 ALA ALA A . n A 1 120 PHE 120 120 120 PHE PHE A . n A 1 121 GLN 121 121 121 GLN GLN A . n A 1 122 GLY 122 122 122 GLY GLY A . n A 1 123 LYS 123 123 123 LYS LYS A . n A 1 124 TYR 124 124 124 TYR TYR A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 VAL 126 126 126 VAL VAL A . n A 1 127 ARG 127 127 127 ARG ARG A . n A 1 128 PHE 128 128 128 PHE PHE A . n A 1 129 TRP 129 129 129 TRP TRP A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 THR 131 131 131 THR THR A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 TRP 133 133 133 TRP TRP A . n A 1 134 GLN 134 134 134 GLN GLN A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 VAL 136 136 136 VAL VAL A . n A 1 137 PRO 137 137 137 PRO PRO A . n A 1 138 GLY 138 138 138 GLY GLY A . n A 1 139 ALA 139 139 139 ALA ALA A . n A 1 140 PRO 140 140 140 PRO PRO A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 TRP 142 142 142 TRP TRP A . n A 1 143 LEU 143 143 143 LEU LEU A . n A 1 144 ASP 144 144 144 ASP ASP A . n A 1 145 LEU 145 145 145 LEU LEU A . n A 1 146 PRO 146 146 146 PRO PRO A . n A 1 147 ILE 147 147 147 ILE ILE A . n A 1 148 LYS 148 148 148 LYS LYS A . n A 1 149 VAL 149 149 149 VAL VAL A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ASN 151 151 151 ASN ASN A . n A 1 152 ALA 152 152 152 ALA ALA A . n A 1 153 ASP 153 153 153 ASP ASP A . n A 1 154 GLN 154 154 154 GLN GLN A . n A 1 155 GLY 155 155 155 GLY GLY A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 SER 157 157 157 SER SER A . n A 1 158 ALA 158 158 158 ALA ALA A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 VAL 160 160 160 VAL VAL A . n A 1 161 GLN 161 161 161 GLN GLN A . n A 1 162 MET 162 162 162 MET MET A . n A 1 163 LEU 163 163 163 LEU LEU A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASP 166 166 166 ASP ASP A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 CYS 168 168 168 CYS CYS A . n A 1 169 PRO 169 169 169 PRO PRO A . n A 1 170 LEU 170 170 170 LEU LEU A . n A 1 171 PHE 171 171 171 PHE PHE A . n A 1 172 VAL 172 172 172 VAL VAL A . n A 1 173 ARG 173 173 173 ARG ARG A . n A 1 174 GLY 174 174 174 GLY GLY A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 LEU 176 176 176 LEU LEU A . n A 1 177 GLU 177 177 177 GLU GLU A . n A 1 178 ALA 178 178 178 ALA ALA A . n A 1 179 GLY 179 179 179 GLY GLY A . n A 1 180 LYS 180 180 180 LYS LYS A . n A 1 181 SER 181 181 181 SER SER A . n A 1 182 ASP 182 182 182 ASP ASP A . n A 1 183 LEU 183 183 183 LEU LEU A . n A 1 184 GLU 184 184 184 GLU GLU A . n A 1 185 LYS 185 185 185 LYS LYS A . n A 1 186 GLN 186 186 186 GLN GLN A . n A 1 187 GLU 187 187 187 GLU GLU A . n A 1 188 LYS 188 188 188 LYS LYS A . n A 1 189 PRO 189 189 189 PRO PRO A . n A 1 190 VAL 190 190 190 VAL VAL A . n A 1 191 ALA 191 191 191 ALA ALA A . n A 1 192 TRP 192 192 192 TRP TRP A . n A 1 193 LEU 193 193 193 LEU LEU A . n A 1 194 SER 194 194 194 SER SER A . n A 1 195 SER 195 195 195 SER SER A . n A 1 196 VAL 196 196 196 VAL ALA A . n A 1 197 PRO 197 197 ? ? ? A . n A 1 198 SER 198 198 ? ? ? A . n A 1 199 SER 199 199 ? ? ? A . n A 1 200 ALA 200 200 ? ? ? A . n A 1 201 ASP 201 201 201 ASP ASP A . n A 1 202 GLY 202 202 202 GLY GLY A . n A 1 203 HIS 203 203 203 HIS HIS A . n A 1 204 ARG 204 204 204 ARG ARG A . n A 1 205 GLN 205 205 205 GLN GLN A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 VAL 207 207 207 VAL VAL A . n A 1 208 CYS 208 208 208 CYS CYS A . n A 1 209 HIS 209 209 209 HIS HIS A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 SER 211 211 211 SER SER A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 PHE 213 213 213 PHE PHE A . n A 1 214 TYR 214 214 214 TYR TYR A . n A 1 215 PRO 215 215 215 PRO PRO A . n A 1 216 LYS 216 216 216 LYS LYS A . n A 1 217 PRO 217 217 217 PRO PRO A . n A 1 218 VAL 218 218 218 VAL VAL A . n A 1 219 TRP 219 219 219 TRP TRP A . n A 1 220 VAL 220 220 220 VAL VAL A . n A 1 221 MET 221 221 221 MET MET A . n A 1 222 TRP 222 222 222 TRP TRP A . n A 1 223 MET 223 223 223 MET MET A . n A 1 224 ARG 224 224 224 ARG ARG A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 ASP 226 226 226 ASP ASP A . n A 1 227 GLN 227 227 227 GLN GLN A . n A 1 228 GLU 228 228 228 GLU GLU A . n A 1 229 GLN 229 229 229 GLN GLN A . n A 1 230 GLN 230 230 230 GLN GLN A . n A 1 231 GLY 231 231 231 GLY GLY A . n A 1 232 THR 232 232 232 THR THR A . n A 1 233 HIS 233 233 233 HIS HIS A . n A 1 234 ARG 234 234 234 ARG ARG A . n A 1 235 GLY 235 235 235 GLY GLY A . n A 1 236 ASP 236 236 236 ASP ASP A . n A 1 237 PHE 237 237 237 PHE PHE A . n A 1 238 LEU 238 238 238 LEU LEU A . n A 1 239 PRO 239 239 239 PRO PRO A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 ALA 241 241 241 ALA ALA A . n A 1 242 ASP 242 242 242 ASP ASP A . n A 1 243 GLU 243 243 243 GLU GLU A . n A 1 244 THR 244 244 244 THR THR A . n A 1 245 TRP 245 245 245 TRP TRP A . n A 1 246 TYR 246 246 246 TYR TYR A . n A 1 247 LEU 247 247 247 LEU LEU A . n A 1 248 GLN 248 248 248 GLN GLN A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 THR 250 250 250 THR THR A . n A 1 251 LEU 251 251 251 LEU LEU A . n A 1 252 ASP 252 252 252 ASP ASP A . n A 1 253 VAL 253 253 253 VAL VAL A . n A 1 254 GLU 254 254 254 GLU GLU A . n A 1 255 ALA 255 255 255 ALA ALA A . n A 1 256 GLY 256 256 256 GLY GLY A . n A 1 257 GLU 257 257 257 GLU GLU A . n A 1 258 GLU 258 258 258 GLU GLU A . n A 1 259 ALA 259 259 259 ALA ALA A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 LEU 261 261 261 LEU LEU A . n A 1 262 ALA 262 262 262 ALA ALA A . n A 1 263 CYS 263 263 263 CYS CYS A . n A 1 264 ARG 264 264 264 ARG ARG A . n A 1 265 VAL 265 265 265 VAL VAL A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 HIS 267 267 267 HIS HIS A . n A 1 268 SER 268 268 268 SER SER A . n A 1 269 SER 269 269 269 SER SER A . n A 1 270 LEU 270 270 270 LEU LEU A . n A 1 271 GLY 271 271 271 GLY GLY A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 GLN 273 273 273 GLN GLN A . n A 1 274 ASP 274 274 274 ASP ASP A . n A 1 275 ILE 275 275 275 ILE ILE A . n A 1 276 ILE 276 276 276 ILE ILE A . n A 1 277 LEU 277 277 277 LEU LEU A . n A 1 278 TYR 278 278 278 TYR TYR A . n A 1 279 TRP 279 279 279 TRP TRP A . n A 1 280 HIS 280 280 ? ? ? A . n A 1 281 HIS 281 281 ? ? ? A . n A 1 282 HIS 282 282 ? ? ? A . n A 1 283 HIS 283 283 ? ? ? A . n A 1 284 HIS 284 284 ? ? ? A . n A 1 285 HIS 285 285 ? ? ? A . n B 2 1 ILE 1 1 1 ILE ILE B . n B 2 2 GLN 2 2 2 GLN GLN B . n B 2 3 LYS 3 3 3 LYS LYS B . n B 2 4 THR 4 4 4 THR THR B . n B 2 5 PRO 5 5 5 PRO PRO B . n B 2 6 GLN 6 6 6 GLN GLN B . n B 2 7 ILE 7 7 7 ILE ILE B . n B 2 8 GLN 8 8 8 GLN GLN B . n B 2 9 VAL 9 9 9 VAL VAL B . n B 2 10 TYR 10 10 10 TYR TYR B . n B 2 11 SER 11 11 11 SER SER B . n B 2 12 ARG 12 12 12 ARG ARG B . n B 2 13 HIS 13 13 13 HIS HIS B . n B 2 14 PRO 14 14 14 PRO PRO B . n B 2 15 PRO 15 15 15 PRO PRO B . n B 2 16 GLU 16 16 16 GLU GLU B . n B 2 17 ASN 17 17 17 ASN ASN B . n B 2 18 GLY 18 18 18 GLY GLY B . n B 2 19 LYS 19 19 19 LYS LYS B . n B 2 20 PRO 20 20 20 PRO PRO B . n B 2 21 ASN 21 21 21 ASN ASN B . n B 2 22 ILE 22 22 22 ILE ILE B . n B 2 23 LEU 23 23 23 LEU LEU B . n B 2 24 ASN 24 24 24 ASN ASN B . n B 2 25 CYS 25 25 25 CYS CYS B . n B 2 26 TYR 26 26 26 TYR TYR B . n B 2 27 VAL 27 27 27 VAL VAL B . n B 2 28 THR 28 28 28 THR THR B . n B 2 29 GLN 29 29 29 GLN GLN B . n B 2 30 PHE 30 30 30 PHE PHE B . n B 2 31 HIS 31 31 31 HIS HIS B . n B 2 32 PRO 32 32 32 PRO PRO B . n B 2 33 PRO 33 33 33 PRO PRO B . n B 2 34 HIS 34 34 34 HIS HIS B . n B 2 35 ILE 35 35 35 ILE ILE B . n B 2 36 GLU 36 36 36 GLU GLU B . n B 2 37 ILE 37 37 37 ILE ILE B . n B 2 38 GLN 38 38 38 GLN GLN B . n B 2 39 MET 39 39 39 MET MET B . n B 2 40 LEU 40 40 40 LEU LEU B . n B 2 41 LYS 41 41 41 LYS LYS B . n B 2 42 ASN 42 42 42 ASN ASN B . n B 2 43 GLY 43 43 43 GLY GLY B . n B 2 44 LYS 44 44 44 LYS LYS B . n B 2 45 LYS 45 45 45 LYS LYS B . n B 2 46 ILE 46 46 46 ILE ILE B . n B 2 47 PRO 47 47 47 PRO PRO B . n B 2 48 LYS 48 48 48 LYS LYS B . n B 2 49 VAL 49 49 49 VAL VAL B . n B 2 50 GLU 50 50 50 GLU GLU B . n B 2 51 MET 51 51 51 MET MET B . n B 2 52 SER 52 52 52 SER SER B . n B 2 53 ASP 53 53 53 ASP ASP B . n B 2 54 MET 54 54 54 MET MET B . n B 2 55 SER 55 55 55 SER SER B . n B 2 56 PHE 56 56 56 PHE PHE B . n B 2 57 SER 57 57 57 SER SER B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 ASP 59 59 59 ASP ASP B . n B 2 60 TRP 60 60 60 TRP TRP B . n B 2 61 SER 61 61 61 SER SER B . n B 2 62 PHE 62 62 62 PHE PHE B . n B 2 63 TYR 63 63 63 TYR TYR B . n B 2 64 ILE 64 64 64 ILE ILE B . n B 2 65 LEU 65 65 65 LEU LEU B . n B 2 66 ALA 66 66 66 ALA ALA B . n B 2 67 HIS 67 67 67 HIS HIS B . n B 2 68 THR 68 68 68 THR THR B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 THR 71 71 71 THR THR B . n B 2 72 PRO 72 72 72 PRO PRO B . n B 2 73 THR 73 73 73 THR THR B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 THR 75 75 75 THR THR B . n B 2 76 ASP 76 76 76 ASP ASP B . n B 2 77 THR 77 77 77 THR THR B . n B 2 78 TYR 78 78 78 TYR TYR B . n B 2 79 ALA 79 79 79 ALA ALA B . n B 2 80 CYS 80 80 80 CYS CYS B . n B 2 81 ARG 81 81 81 ARG ARG B . n B 2 82 VAL 82 82 82 VAL VAL B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 HIS 84 84 84 HIS HIS B . n B 2 85 ALA 85 85 85 ALA ALA B . n B 2 86 SER 86 86 86 SER SER B . n B 2 87 MET 87 87 87 MET MET B . n B 2 88 ALA 88 88 88 ALA ALA B . n B 2 89 GLU 89 89 89 GLU GLU B . n B 2 90 PRO 90 90 90 PRO PRO B . n B 2 91 LYS 91 91 91 LYS LYS B . n B 2 92 THR 92 92 92 THR THR B . n B 2 93 VAL 93 93 93 VAL VAL B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 TRP 95 95 95 TRP TRP B . n B 2 96 ASP 96 96 96 ASP ASP B . n B 2 97 ARG 97 97 97 ARG ARG B . n B 2 98 ASP 98 98 98 ASP ASP B . n B 2 99 MET 99 99 99 MET MET B . n C 3 1 TYR 1 -3 ? ? ? C . n C 3 2 GLU 2 -2 ? ? ? C . n C 3 3 HIS 3 -1 ? ? ? C . n C 3 4 ASP 4 0 0 ASP ASP C . n C 3 5 PHE 5 1 1 PHE PHE C . n C 3 6 HIS 6 2 2 HIS HIS C . n C 3 7 HIS 7 3 3 HIS HIS C . n C 3 8 ILE 8 4 4 ILE ILE C . n C 3 9 ARG 9 5 5 ARG ARG C . n C 3 10 GLU 10 6 6 GLU GLU C . n C 3 11 LYS 11 7 7 LYS LYS C . n C 3 12 GLY 12 8 8 GLY GLY C . n C 3 13 ASN 13 9 9 ASN ASN C . n C 3 14 HIS 14 10 10 HIS HIS C . n C 3 15 TRP 15 11 11 TRP TRP C . n C 3 16 LYS 16 12 12 LYS LYS C . n C 3 17 ASN 17 13 13 ASN ASN C . n C 3 18 PHE 18 14 14 PHE PHE C . n C 3 19 LEU 19 15 15 LEU LEU C . n C 3 20 ALA 20 16 ? ? ? C . n C 3 21 VAL 21 17 ? ? ? C . n C 3 22 MET 22 18 ? ? ? C . 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 D 4 NAG 1 301 521 NAG NAG A . E 4 NAG 2 302 522 NAG NAG A . F 4 NAG 1 303 511 NAG NAG A . G 4 NAG 2 304 512 NAG NAG A . H 5 BMA 3 305 513 BMA BMA A . I 6 MAN 4 306 514 MAN MAN A . J 7 FUC 5 307 515 FUC FUC A . K 6 MAN 6 308 516 MAN MAN A . L 4 NAG 1 309 501 NAG NAG A . M 8 CIT 1 310 1 CIT CIT A . N 9 NA 1 311 1 NA NA A . O 10 PLM 1 101 100 PLM PLM C . P 11 OCA 1 102 1 OCA OCA C . Q 12 HOH 1 401 77 HOH HOH A . Q 12 HOH 2 402 94 HOH HOH A . Q 12 HOH 3 403 195 HOH HOH A . Q 12 HOH 4 404 86 HOH HOH A . Q 12 HOH 5 405 27 HOH HOH A . Q 12 HOH 6 406 55 HOH HOH A . Q 12 HOH 7 407 118 HOH HOH A . Q 12 HOH 8 408 58 HOH HOH A . Q 12 HOH 9 409 190 HOH HOH A . Q 12 HOH 10 410 160 HOH HOH A . Q 12 HOH 11 411 13 HOH HOH A . Q 12 HOH 12 412 22 HOH HOH A . Q 12 HOH 13 413 79 HOH HOH A . Q 12 HOH 14 414 90 HOH HOH A . Q 12 HOH 15 415 106 HOH HOH A . Q 12 HOH 16 416 156 HOH HOH A . Q 12 HOH 17 417 176 HOH HOH A . Q 12 HOH 18 418 115 HOH HOH A . Q 12 HOH 19 419 28 HOH HOH A . Q 12 HOH 20 420 83 HOH HOH A . Q 12 HOH 21 421 135 HOH HOH A . Q 12 HOH 22 422 84 HOH HOH A . Q 12 HOH 23 423 159 HOH HOH A . Q 12 HOH 24 424 66 HOH HOH A . Q 12 HOH 25 425 46 HOH HOH A . Q 12 HOH 26 426 31 HOH HOH A . Q 12 HOH 27 427 69 HOH HOH A . Q 12 HOH 28 428 81 HOH HOH A . Q 12 HOH 29 429 2 HOH HOH A . Q 12 HOH 30 430 89 HOH HOH A . Q 12 HOH 31 431 48 HOH HOH A . Q 12 HOH 32 432 14 HOH HOH A . Q 12 HOH 33 433 142 HOH HOH A . Q 12 HOH 34 434 107 HOH HOH A . Q 12 HOH 35 435 4 HOH HOH A . Q 12 HOH 36 436 21 HOH HOH A . Q 12 HOH 37 437 204 HOH HOH A . Q 12 HOH 38 438 20 HOH HOH A . Q 12 HOH 39 439 30 HOH HOH A . Q 12 HOH 40 440 44 HOH HOH A . Q 12 HOH 41 441 182 HOH HOH A . Q 12 HOH 42 442 62 HOH HOH A . Q 12 HOH 43 443 110 HOH HOH A . Q 12 HOH 44 444 8 HOH HOH A . Q 12 HOH 45 445 140 HOH HOH A . Q 12 HOH 46 446 88 HOH HOH A . Q 12 HOH 47 447 15 HOH HOH A . Q 12 HOH 48 448 112 HOH HOH A . Q 12 HOH 49 449 60 HOH HOH A . Q 12 HOH 50 450 163 HOH HOH A . Q 12 HOH 51 451 114 HOH HOH A . Q 12 HOH 52 452 144 HOH HOH A . Q 12 HOH 53 453 56 HOH HOH A . Q 12 HOH 54 454 70 HOH HOH A . Q 12 HOH 55 455 211 HOH HOH A . Q 12 HOH 56 456 141 HOH HOH A . Q 12 HOH 57 457 139 HOH HOH A . Q 12 HOH 58 458 108 HOH HOH A . Q 12 HOH 59 459 197 HOH HOH A . Q 12 HOH 60 460 19 HOH HOH A . Q 12 HOH 61 461 120 HOH HOH A . Q 12 HOH 62 462 82 HOH HOH A . Q 12 HOH 63 463 162 HOH HOH A . Q 12 HOH 64 464 111 HOH HOH A . Q 12 HOH 65 465 16 HOH HOH A . Q 12 HOH 66 466 51 HOH HOH A . Q 12 HOH 67 467 198 HOH HOH A . Q 12 HOH 68 468 104 HOH HOH A . Q 12 HOH 69 469 10 HOH HOH A . Q 12 HOH 70 470 188 HOH HOH A . Q 12 HOH 71 471 167 HOH HOH A . Q 12 HOH 72 472 5 HOH HOH A . Q 12 HOH 73 473 133 HOH HOH A . Q 12 HOH 74 474 199 HOH HOH A . Q 12 HOH 75 475 200 HOH HOH A . Q 12 HOH 76 476 18 HOH HOH A . Q 12 HOH 77 477 186 HOH HOH A . Q 12 HOH 78 478 23 HOH HOH A . Q 12 HOH 79 479 75 HOH HOH A . Q 12 HOH 80 480 131 HOH HOH A . Q 12 HOH 81 481 193 HOH HOH A . Q 12 HOH 82 482 3 HOH HOH A . Q 12 HOH 83 483 149 HOH HOH A . Q 12 HOH 84 484 34 HOH HOH A . Q 12 HOH 85 485 155 HOH HOH A . Q 12 HOH 86 486 100 HOH HOH A . Q 12 HOH 87 487 129 HOH HOH A . Q 12 HOH 88 488 113 HOH HOH A . Q 12 HOH 89 489 12 HOH HOH A . Q 12 HOH 90 490 61 HOH HOH A . Q 12 HOH 91 491 11 HOH HOH A . Q 12 HOH 92 492 35 HOH HOH A . Q 12 HOH 93 493 1 HOH HOH A . Q 12 HOH 94 494 121 HOH HOH A . Q 12 HOH 95 495 192 HOH HOH A . Q 12 HOH 96 496 189 HOH HOH A . Q 12 HOH 97 497 95 HOH HOH A . Q 12 HOH 98 498 134 HOH HOH A . Q 12 HOH 99 499 54 HOH HOH A . Q 12 HOH 100 500 39 HOH HOH A . Q 12 HOH 101 501 212 HOH HOH A . Q 12 HOH 102 502 147 HOH HOH A . Q 12 HOH 103 503 208 HOH HOH A . Q 12 HOH 104 504 76 HOH HOH A . Q 12 HOH 105 505 209 HOH HOH A . Q 12 HOH 106 506 203 HOH HOH A . Q 12 HOH 107 507 105 HOH HOH A . Q 12 HOH 108 508 130 HOH HOH A . Q 12 HOH 109 509 161 HOH HOH A . Q 12 HOH 110 510 145 HOH HOH A . Q 12 HOH 111 511 191 HOH HOH A . Q 12 HOH 112 512 37 HOH HOH A . Q 12 HOH 113 513 206 HOH HOH A . Q 12 HOH 114 514 17 HOH HOH A . Q 12 HOH 115 515 205 HOH HOH A . Q 12 HOH 116 516 97 HOH HOH A . Q 12 HOH 117 517 29 HOH HOH A . Q 12 HOH 118 518 53 HOH HOH A . Q 12 HOH 119 519 214 HOH HOH A . Q 12 HOH 120 520 42 HOH HOH A . Q 12 HOH 121 521 9 HOH HOH A . Q 12 HOH 122 522 24 HOH HOH A . Q 12 HOH 123 523 36 HOH HOH A . Q 12 HOH 124 524 26 HOH HOH A . Q 12 HOH 125 525 128 HOH HOH A . Q 12 HOH 126 526 213 HOH HOH A . Q 12 HOH 127 527 38 HOH HOH A . Q 12 HOH 128 528 183 HOH HOH A . Q 12 HOH 129 529 25 HOH HOH A . R 12 HOH 1 101 172 HOH HOH B . R 12 HOH 2 102 98 HOH HOH B . R 12 HOH 3 103 71 HOH HOH B . R 12 HOH 4 104 96 HOH HOH B . R 12 HOH 5 105 138 HOH HOH B . R 12 HOH 6 106 93 HOH HOH B . R 12 HOH 7 107 184 HOH HOH B . R 12 HOH 8 108 32 HOH HOH B . R 12 HOH 9 109 47 HOH HOH B . R 12 HOH 10 110 101 HOH HOH B . R 12 HOH 11 111 68 HOH HOH B . R 12 HOH 12 112 194 HOH HOH B . R 12 HOH 13 113 166 HOH HOH B . R 12 HOH 14 114 175 HOH HOH B . R 12 HOH 15 115 173 HOH HOH B . R 12 HOH 16 116 103 HOH HOH B . R 12 HOH 17 117 99 HOH HOH B . R 12 HOH 18 118 119 HOH HOH B . R 12 HOH 19 119 49 HOH HOH B . R 12 HOH 20 120 136 HOH HOH B . R 12 HOH 21 121 102 HOH HOH B . R 12 HOH 22 122 123 HOH HOH B . R 12 HOH 23 123 87 HOH HOH B . R 12 HOH 24 124 78 HOH HOH B . R 12 HOH 25 125 207 HOH HOH B . R 12 HOH 26 126 196 HOH HOH B . R 12 HOH 27 127 45 HOH HOH B . R 12 HOH 28 128 169 HOH HOH B . R 12 HOH 29 129 92 HOH HOH B . R 12 HOH 30 130 170 HOH HOH B . R 12 HOH 31 131 168 HOH HOH B . R 12 HOH 32 132 125 HOH HOH B . R 12 HOH 33 133 177 HOH HOH B . R 12 HOH 34 134 180 HOH HOH B . R 12 HOH 35 135 72 HOH HOH B . R 12 HOH 36 136 64 HOH HOH B . R 12 HOH 37 137 152 HOH HOH B . R 12 HOH 38 138 124 HOH HOH B . R 12 HOH 39 139 157 HOH HOH B . R 12 HOH 40 140 143 HOH HOH B . R 12 HOH 41 141 91 HOH HOH B . R 12 HOH 42 142 43 HOH HOH B . R 12 HOH 43 143 73 HOH HOH B . R 12 HOH 44 144 153 HOH HOH B . R 12 HOH 45 145 126 HOH HOH B . R 12 HOH 46 146 109 HOH HOH B . R 12 HOH 47 147 67 HOH HOH B . R 12 HOH 48 148 50 HOH HOH B . R 12 HOH 49 149 201 HOH HOH B . R 12 HOH 50 150 41 HOH HOH B . R 12 HOH 51 151 40 HOH HOH B . R 12 HOH 52 152 179 HOH HOH B . R 12 HOH 53 153 57 HOH HOH B . R 12 HOH 54 154 151 HOH HOH B . R 12 HOH 55 155 63 HOH HOH B . R 12 HOH 56 156 137 HOH HOH B . R 12 HOH 57 157 116 HOH HOH B . R 12 HOH 58 158 158 HOH HOH B . R 12 HOH 59 159 132 HOH HOH B . R 12 HOH 60 160 178 HOH HOH B . R 12 HOH 61 161 174 HOH HOH B . R 12 HOH 62 162 150 HOH HOH B . R 12 HOH 63 163 210 HOH HOH B . R 12 HOH 64 164 33 HOH HOH B . R 12 HOH 65 165 187 HOH HOH B . R 12 HOH 66 166 6 HOH HOH B . R 12 HOH 67 167 171 HOH HOH B . R 12 HOH 68 168 146 HOH HOH B . R 12 HOH 69 169 164 HOH HOH B . R 12 HOH 70 170 185 HOH HOH B . R 12 HOH 71 171 85 HOH HOH B . R 12 HOH 72 172 165 HOH HOH B . R 12 HOH 73 173 7 HOH HOH B . R 12 HOH 74 174 181 HOH HOH B . S 12 HOH 1 201 202 HOH HOH C . # _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 trimeric _pdbx_struct_assembly.oligomeric_count 3 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S # 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)' 8380 ? 1 MORE -7 ? 1 'SSA (A^2)' 18520 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_struct_conn_angle.id 1 _pdbx_struct_conn_angle.ptnr1_label_atom_id O _pdbx_struct_conn_angle.ptnr1_label_alt_id ? _pdbx_struct_conn_angle.ptnr1_label_asym_id A _pdbx_struct_conn_angle.ptnr1_label_comp_id THR _pdbx_struct_conn_angle.ptnr1_label_seq_id 26 _pdbx_struct_conn_angle.ptnr1_auth_atom_id ? _pdbx_struct_conn_angle.ptnr1_auth_asym_id A _pdbx_struct_conn_angle.ptnr1_auth_comp_id THR _pdbx_struct_conn_angle.ptnr1_auth_seq_id 26 _pdbx_struct_conn_angle.ptnr1_PDB_ins_code ? _pdbx_struct_conn_angle.ptnr1_symmetry 1_555 _pdbx_struct_conn_angle.ptnr2_label_atom_id NA _pdbx_struct_conn_angle.ptnr2_label_alt_id ? _pdbx_struct_conn_angle.ptnr2_label_asym_id N _pdbx_struct_conn_angle.ptnr2_label_comp_id NA _pdbx_struct_conn_angle.ptnr2_label_seq_id . _pdbx_struct_conn_angle.ptnr2_auth_atom_id ? _pdbx_struct_conn_angle.ptnr2_auth_asym_id A _pdbx_struct_conn_angle.ptnr2_auth_comp_id NA _pdbx_struct_conn_angle.ptnr2_auth_seq_id 311 _pdbx_struct_conn_angle.ptnr2_PDB_ins_code ? _pdbx_struct_conn_angle.ptnr2_symmetry 1_555 _pdbx_struct_conn_angle.ptnr3_label_atom_id O _pdbx_struct_conn_angle.ptnr3_label_alt_id ? _pdbx_struct_conn_angle.ptnr3_label_asym_id A _pdbx_struct_conn_angle.ptnr3_label_comp_id TRP _pdbx_struct_conn_angle.ptnr3_label_seq_id 40 _pdbx_struct_conn_angle.ptnr3_auth_atom_id ? _pdbx_struct_conn_angle.ptnr3_auth_asym_id A _pdbx_struct_conn_angle.ptnr3_auth_comp_id TRP _pdbx_struct_conn_angle.ptnr3_auth_seq_id 40 _pdbx_struct_conn_angle.ptnr3_PDB_ins_code ? _pdbx_struct_conn_angle.ptnr3_symmetry 1_555 _pdbx_struct_conn_angle.value 98.3 _pdbx_struct_conn_angle.value_esd ? # 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 2016-03-30 2 'Structure model' 1 1 2016-04-06 3 'Structure model' 1 2 2016-06-01 4 'Structure model' 1 3 2017-09-20 # _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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 3 'Structure model' 'Database references' 3 4 'Structure model' 'Author supporting evidence' 4 4 'Structure model' 'Database references' 5 4 'Structure model' 'Derived calculations' # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' citation 2 4 'Structure model' pdbx_audit_support 3 4 'Structure model' pdbx_struct_oper_list # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 4 'Structure model' '_citation.journal_id_CSD' 2 4 'Structure model' '_pdbx_audit_support.funding_organization' 3 4 'Structure model' '_pdbx_struct_oper_list.symmetry_operation' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] 'X-RAY DIFFRACTION' 1 ? refined 28.2544 1.9566 33.0568 0.3445 0.1619 0.2193 0.0154 -0.0948 0.1105 4.9663 2.0683 0.2657 -0.4219 0.9577 -0.2106 0.2473 -0.0999 -0.1473 -0.5630 -0.5027 0.1121 0.1730 0.1804 -0.0566 'X-RAY DIFFRACTION' 2 ? refined 9.9827 21.8624 5.8703 0.0113 0.0423 0.0991 0.0150 -0.0048 0.0195 2.5746 1.9352 4.6751 0.5752 -0.2791 -1.6905 0.0649 -0.0665 0.0016 0.2857 0.1056 0.0083 -0.1092 0.0673 0.1338 'X-RAY DIFFRACTION' 3 ? refined 13.2529 26.9112 26.6570 0.0752 0.0485 0.1229 -0.0244 0.0109 -0.0210 4.1227 1.8923 1.8288 -1.1064 1.0514 -0.1714 -0.1267 -0.0239 0.1506 -0.3109 0.3305 -0.0384 0.1752 -0.1633 -0.0893 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 6 A 180 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 2 1 A 301 A 309 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 3 1 C 0 C 15 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 4 1 C 101 C 101 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 5 1 C 102 C 102 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 6 1 A 310 A 310 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 7 2 A 181 A 279 ? ? ? ? ? ? 'X-RAY DIFFRACTION' 8 3 B 1 B 99 ? ? ? ? ? ? # loop_ _software.citation_id _software.classification _software.compiler_name _software.compiler_version _software.contact_author _software.contact_author_email _software.date _software.description _software.dependencies _software.hardware _software.language _software.location _software.mods _software.name _software.os _software.os_version _software.type _software.version _software.pdbx_ordinal ? refinement ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0131 1 ? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot ? ? ? . 2 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASP A 166 ? ? -107.84 -61.28 2 1 LYS B 48 ? ? -99.45 37.68 3 1 TRP B 60 ? ? 81.66 -10.31 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A LYS 6 ? CG ? A LYS 6 CG 2 1 Y 1 A LYS 6 ? CD ? A LYS 6 CD 3 1 Y 1 A LYS 6 ? CE ? A LYS 6 CE 4 1 Y 1 A LYS 6 ? NZ ? A LYS 6 NZ 5 1 Y 1 A ASN 7 ? CG ? A ASN 7 CG 6 1 Y 1 A ASN 7 ? OD1 ? A ASN 7 OD1 7 1 Y 1 A ASN 7 ? ND2 ? A ASN 7 ND2 8 1 Y 1 A ARG 21 ? CG ? A ARG 21 CG 9 1 Y 1 A ARG 21 ? CD ? A ARG 21 CD 10 1 Y 1 A ARG 21 ? NE ? A ARG 21 NE 11 1 Y 1 A ARG 21 ? CZ ? A ARG 21 CZ 12 1 Y 1 A ARG 21 ? NH1 ? A ARG 21 NH1 13 1 Y 1 A ARG 21 ? NH2 ? A ARG 21 NH2 14 1 Y 1 A SER 22 ? OG ? A SER 22 OG 15 1 Y 1 A GLN 61 ? CG ? A GLN 61 CG 16 1 Y 1 A GLN 61 ? CD ? A GLN 61 CD 17 1 Y 1 A GLN 61 ? OE1 ? A GLN 61 OE1 18 1 Y 1 A GLN 61 ? NE2 ? A GLN 61 NE2 19 1 Y 1 A GLU 64 ? CG ? A GLU 64 CG 20 1 Y 1 A GLU 64 ? CD ? A GLU 64 CD 21 1 Y 1 A GLU 64 ? OE1 ? A GLU 64 OE1 22 1 Y 1 A GLU 64 ? OE2 ? A GLU 64 OE2 23 1 Y 1 A VAL 75 ? CG1 ? A VAL 75 CG1 24 1 Y 1 A VAL 75 ? CG2 ? A VAL 75 CG2 25 1 Y 1 A ARG 79 ? CG ? A ARG 79 CG 26 1 Y 1 A ARG 79 ? CD ? A ARG 79 CD 27 1 Y 1 A ARG 79 ? NE ? A ARG 79 NE 28 1 Y 1 A ARG 79 ? CZ ? A ARG 79 CZ 29 1 Y 1 A ARG 79 ? NH1 ? A ARG 79 NH1 30 1 Y 1 A ARG 79 ? NH2 ? A ARG 79 NH2 31 1 Y 1 A LYS 86 ? CG ? A LYS 86 CG 32 1 Y 1 A LYS 86 ? CD ? A LYS 86 CD 33 1 Y 1 A LYS 86 ? CE ? A LYS 86 CE 34 1 Y 1 A LYS 86 ? NZ ? A LYS 86 NZ 35 1 Y 1 A MET 87 ? CG ? A MET 87 CG 36 1 Y 1 A MET 87 ? SD ? A MET 87 SD 37 1 Y 1 A MET 87 ? CE ? A MET 87 CE 38 1 Y 1 A ASP 93 ? CG ? A ASP 93 CG 39 1 Y 1 A ASP 93 ? OD1 ? A ASP 93 OD1 40 1 Y 1 A ASP 93 ? OD2 ? A ASP 93 OD2 41 1 Y 1 A TYR 107 ? CG ? A TYR 107 CG 42 1 Y 1 A TYR 107 ? CD1 ? A TYR 107 CD1 43 1 Y 1 A TYR 107 ? CD2 ? A TYR 107 CD2 44 1 Y 1 A TYR 107 ? CE1 ? A TYR 107 CE1 45 1 Y 1 A TYR 107 ? CE2 ? A TYR 107 CE2 46 1 Y 1 A TYR 107 ? CZ ? A TYR 107 CZ 47 1 Y 1 A TYR 107 ? OH ? A TYR 107 OH 48 1 Y 1 A GLU 113 ? CG ? A GLU 113 CG 49 1 Y 1 A GLU 113 ? CD ? A GLU 113 CD 50 1 Y 1 A GLU 113 ? OE1 ? A GLU 113 OE1 51 1 Y 1 A GLU 113 ? OE2 ? A GLU 113 OE2 52 1 Y 1 A LEU 145 ? CG ? A LEU 145 CG 53 1 Y 1 A LEU 145 ? CD1 ? A LEU 145 CD1 54 1 Y 1 A LEU 145 ? CD2 ? A LEU 145 CD2 55 1 Y 1 A VAL 196 ? CG1 ? A VAL 196 CG1 56 1 Y 1 A VAL 196 ? CG2 ? A VAL 196 CG2 57 1 Y 1 A ASP 201 ? CG ? A ASP 201 CG 58 1 Y 1 A ASP 201 ? OD1 ? A ASP 201 OD1 59 1 Y 1 A ASP 201 ? OD2 ? A ASP 201 OD2 60 1 Y 1 A GLU 254 ? CG ? A GLU 254 CG 61 1 Y 1 A GLU 254 ? CD ? A GLU 254 CD 62 1 Y 1 A GLU 254 ? OE1 ? A GLU 254 OE1 63 1 Y 1 A GLU 254 ? OE2 ? A GLU 254 OE2 64 1 Y 1 A GLU 257 ? CG ? A GLU 257 CG 65 1 Y 1 A GLU 257 ? CD ? A GLU 257 CD 66 1 Y 1 A GLU 257 ? OE1 ? A GLU 257 OE1 67 1 Y 1 A GLU 257 ? OE2 ? A GLU 257 OE2 68 1 Y 1 A GLN 273 ? CG ? A GLN 273 CG 69 1 Y 1 A GLN 273 ? CD ? A GLN 273 CD 70 1 Y 1 A GLN 273 ? OE1 ? A GLN 273 OE1 71 1 Y 1 A GLN 273 ? NE2 ? A GLN 273 NE2 72 1 Y 1 B ILE 1 ? CG1 ? B ILE 1 CG1 73 1 Y 1 B ILE 1 ? CG2 ? B ILE 1 CG2 74 1 Y 1 B ILE 1 ? CD1 ? B ILE 1 CD1 75 1 Y 1 B LYS 44 ? CG ? B LYS 44 CG 76 1 Y 1 B LYS 44 ? CD ? B LYS 44 CD 77 1 Y 1 B LYS 44 ? CE ? B LYS 44 CE 78 1 Y 1 B LYS 44 ? NZ ? B LYS 44 NZ 79 1 Y 1 B LYS 48 ? CG ? B LYS 48 CG 80 1 Y 1 B LYS 48 ? CD ? B LYS 48 CD 81 1 Y 1 B LYS 48 ? CE ? B LYS 48 CE 82 1 Y 1 B LYS 48 ? NZ ? B LYS 48 NZ 83 1 Y 1 B MET 99 ? CG ? B MET 99 CG 84 1 Y 1 B MET 99 ? SD ? B MET 99 SD 85 1 Y 1 B MET 99 ? CE ? B MET 99 CE 86 1 Y 1 C ASP 0 ? CG ? C ASP 4 CG 87 1 Y 1 C ASP 0 ? OD1 ? C ASP 4 OD1 88 1 Y 1 C ASP 0 ? OD2 ? C ASP 4 OD2 89 1 Y 1 C ARG 5 ? CZ ? C ARG 9 CZ 90 1 Y 1 C ARG 5 ? NH1 ? C ARG 9 NH1 91 1 Y 1 C ARG 5 ? NH2 ? C ARG 9 NH2 92 1 Y 1 C GLU 6 ? CG ? C GLU 10 CG 93 1 Y 1 C GLU 6 ? CD ? C GLU 10 CD 94 1 Y 1 C GLU 6 ? OE1 ? C GLU 10 OE1 95 1 Y 1 C GLU 6 ? OE2 ? C GLU 10 OE2 96 1 Y 1 C ASN 9 ? CG ? C ASN 13 CG 97 1 Y 1 C ASN 9 ? OD1 ? C ASN 13 OD1 98 1 Y 1 C ASN 9 ? ND2 ? C ASN 13 ND2 99 1 Y 1 C HIS 10 ? CG ? C HIS 14 CG 100 1 Y 1 C HIS 10 ? ND1 ? C HIS 14 ND1 101 1 Y 1 C HIS 10 ? CD2 ? C HIS 14 CD2 102 1 Y 1 C HIS 10 ? CE1 ? C HIS 14 CE1 103 1 Y 1 C HIS 10 ? NE2 ? C HIS 14 NE2 104 1 Y 1 C LYS 12 ? CG ? C LYS 16 CG 105 1 Y 1 C LYS 12 ? CD ? C LYS 16 CD 106 1 Y 1 C LYS 12 ? CE ? C LYS 16 CE 107 1 Y 1 C LYS 12 ? NZ ? C LYS 16 NZ 108 1 Y 1 C ASN 13 ? CG ? C ASN 17 CG 109 1 Y 1 C ASN 13 ? OD1 ? C ASN 17 OD1 110 1 Y 1 C ASN 13 ? ND2 ? C ASN 17 ND2 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A SER 1 ? A SER 1 2 1 Y 1 A GLU 2 ? A GLU 2 3 1 Y 1 A ALA 3 ? A ALA 3 4 1 Y 1 A GLN 4 ? A GLN 4 5 1 Y 1 A GLN 5 ? A GLN 5 6 1 Y 1 A SER 89 ? A SER 89 7 1 Y 1 A PRO 90 ? A PRO 90 8 1 Y 1 A LYS 91 ? A LYS 91 9 1 Y 1 A GLU 92 ? A GLU 92 10 1 Y 1 A PRO 108 ? A PRO 108 11 1 Y 1 A GLY 109 ? A GLY 109 12 1 Y 1 A ASN 110 ? A ASN 110 13 1 Y 1 A PRO 197 ? A PRO 197 14 1 Y 1 A SER 198 ? A SER 198 15 1 Y 1 A SER 199 ? A SER 199 16 1 Y 1 A ALA 200 ? A ALA 200 17 1 Y 1 A HIS 280 ? A HIS 280 18 1 Y 1 A HIS 281 ? A HIS 281 19 1 Y 1 A HIS 282 ? A HIS 282 20 1 Y 1 A HIS 283 ? A HIS 283 21 1 Y 1 A HIS 284 ? A HIS 284 22 1 Y 1 A HIS 285 ? A HIS 285 23 1 Y 1 C TYR -3 ? C TYR 1 24 1 Y 1 C GLU -2 ? C GLU 2 25 1 Y 1 C HIS -1 ? C HIS 3 26 1 Y 1 C ALA 16 ? C ALA 20 27 1 Y 1 C VAL 17 ? C VAL 21 28 1 Y 1 C MET 18 ? C MET 22 # _pdbx_audit_support.funding_organization 'National Institutes of Health/National Institute Of Allergy and Infectious Diseases' _pdbx_audit_support.country 'United States' _pdbx_audit_support.grant_number 5R21AI107318-02 _pdbx_audit_support.ordinal 1 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 N-ACETYL-D-GLUCOSAMINE NAG 5 BETA-D-MANNOSE BMA 6 ALPHA-D-MANNOSE MAN 7 ALPHA-L-FUCOSE FUC 8 'CITRIC ACID' CIT 9 'SODIUM ION' NA 10 'PALMITIC ACID' PLM 11 'OCTANOIC ACID (CAPRYLIC ACID)' OCA 12 water HOH #