data_3DBX # _entry.id 3DBX # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3DBX RCSB RCSB047845 WWPDB D_1000047845 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3DBX _pdbx_database_status.recvd_initial_deposition_date 2008-06-02 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Zajonc, D.M.' 1 'Wilson, I.A.' 2 # _citation.id primary _citation.title 'The crystal structure of avian CD1 reveals a smaller, more primordial antigen-binding pocket compared to mammalian CD1' _citation.journal_abbrev Proc.Natl.Acad.Sci.Usa _citation.journal_volume 105 _citation.page_first 17925 _citation.page_last 17930 _citation.year 2008 _citation.journal_id_ASTM PNASA6 _citation.country US _citation.journal_id_ISSN 0027-8424 _citation.journal_id_CSD 0040 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 19004781 _citation.pdbx_database_id_DOI 10.1073/pnas.0809814105 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zajonc, D.M.' 1 primary 'Striegl, H.' 2 primary 'Dascher, C.C.' 3 primary 'Wilson, I.A.' 4 # _cell.entry_id 3DBX _cell.length_a 92.154 _cell.length_b 92.154 _cell.length_c 96.693 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3DBX _symmetry.space_group_name_H-M 'P 41 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 92 _symmetry.space_group_name_Hall ? # 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 'CD1-2 antigen' 32792.660 1 ? ? 'ectodomain of chicken CD1-2, UNP residues 20-302' ? 2 polymer man Beta-2-microglobulin 11748.160 1 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 4 non-polymer syn 'PALMITIC ACID' 256.424 1 ? ? ? ? 5 water nat water 18.015 149 ? ? ? ? # _entity_name_com.entity_id 2 _entity_name_com.name 'Beta-2-microglobulin form pI 5.3' # 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 ;ETSCPPPEESQFFQLFYTLLLGNVSSTELTGMALLADVPIMVLDPHTWNLNICRPWVQEITAETEVKKILSFSMVGIRNT IRFMHEMTAKAGLDYPRVFQIHTGCKLYTNGTRWSFVNIGEGGRDLVTYELSRERWVPQRSTLLAKVMSNTLTDLRAVSG FLEHIFSSSFPNYILMLHEEGRTDLERRVPPMAVVFARTAGQVQLLLVCRVTSFYPRPIAVTWLRDGREVPPSPALSTGT VLPNADLTYQLRSTLLVSPQDGHGYACRVQHCSLGDRSLLVPWHHHHHH ; ;ETSCPPPEESQFFQLFYTLLLGNVSSTELTGMALLADVPIMVLDPHTWNLNICRPWVQEITAETEVKKILSFSMVGIRNT IRFMHEMTAKAGLDYPRVFQIHTGCKLYTNGTRWSFVNIGEGGRDLVTYELSRERWVPQRSTLLAKVMSNTLTDLRAVSG FLEHIFSSSFPNYILMLHEEGRTDLERRVPPMAVVFARTAGQVQLLLVCRVTSFYPRPIAVTWLRDGREVPPSPALSTGT VLPNADLTYQLRSTLLVSPQDGHGYACRVQHCSLGDRSLLVPWHHHHHH ; A ? 2 'polypeptide(L)' no no ;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDM ; ;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDM ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLU n 1 2 THR n 1 3 SER n 1 4 CYS n 1 5 PRO n 1 6 PRO n 1 7 PRO n 1 8 GLU n 1 9 GLU n 1 10 SER n 1 11 GLN n 1 12 PHE n 1 13 PHE n 1 14 GLN n 1 15 LEU n 1 16 PHE n 1 17 TYR n 1 18 THR n 1 19 LEU n 1 20 LEU n 1 21 LEU n 1 22 GLY n 1 23 ASN n 1 24 VAL n 1 25 SER n 1 26 SER n 1 27 THR n 1 28 GLU n 1 29 LEU n 1 30 THR n 1 31 GLY n 1 32 MET n 1 33 ALA n 1 34 LEU n 1 35 LEU n 1 36 ALA n 1 37 ASP n 1 38 VAL n 1 39 PRO n 1 40 ILE n 1 41 MET n 1 42 VAL n 1 43 LEU n 1 44 ASP n 1 45 PRO n 1 46 HIS n 1 47 THR n 1 48 TRP n 1 49 ASN n 1 50 LEU n 1 51 ASN n 1 52 ILE n 1 53 CYS n 1 54 ARG n 1 55 PRO n 1 56 TRP n 1 57 VAL n 1 58 GLN n 1 59 GLU n 1 60 ILE n 1 61 THR n 1 62 ALA n 1 63 GLU n 1 64 THR n 1 65 GLU n 1 66 VAL n 1 67 LYS n 1 68 LYS n 1 69 ILE n 1 70 LEU n 1 71 SER n 1 72 PHE n 1 73 SER n 1 74 MET n 1 75 VAL n 1 76 GLY n 1 77 ILE n 1 78 ARG n 1 79 ASN n 1 80 THR n 1 81 ILE n 1 82 ARG n 1 83 PHE n 1 84 MET n 1 85 HIS n 1 86 GLU n 1 87 MET n 1 88 THR n 1 89 ALA n 1 90 LYS n 1 91 ALA n 1 92 GLY n 1 93 LEU n 1 94 ASP n 1 95 TYR n 1 96 PRO n 1 97 ARG n 1 98 VAL n 1 99 PHE n 1 100 GLN n 1 101 ILE n 1 102 HIS n 1 103 THR n 1 104 GLY n 1 105 CYS n 1 106 LYS n 1 107 LEU n 1 108 TYR n 1 109 THR n 1 110 ASN n 1 111 GLY n 1 112 THR n 1 113 ARG n 1 114 TRP n 1 115 SER n 1 116 PHE n 1 117 VAL n 1 118 ASN n 1 119 ILE n 1 120 GLY n 1 121 GLU n 1 122 GLY n 1 123 GLY n 1 124 ARG n 1 125 ASP n 1 126 LEU n 1 127 VAL n 1 128 THR n 1 129 TYR n 1 130 GLU n 1 131 LEU n 1 132 SER n 1 133 ARG n 1 134 GLU n 1 135 ARG n 1 136 TRP n 1 137 VAL n 1 138 PRO n 1 139 GLN n 1 140 ARG n 1 141 SER n 1 142 THR n 1 143 LEU n 1 144 LEU n 1 145 ALA n 1 146 LYS n 1 147 VAL n 1 148 MET n 1 149 SER n 1 150 ASN n 1 151 THR n 1 152 LEU n 1 153 THR n 1 154 ASP n 1 155 LEU n 1 156 ARG n 1 157 ALA n 1 158 VAL n 1 159 SER n 1 160 GLY n 1 161 PHE n 1 162 LEU n 1 163 GLU n 1 164 HIS n 1 165 ILE n 1 166 PHE n 1 167 SER n 1 168 SER n 1 169 SER n 1 170 PHE n 1 171 PRO n 1 172 ASN n 1 173 TYR n 1 174 ILE n 1 175 LEU n 1 176 MET n 1 177 LEU n 1 178 HIS n 1 179 GLU n 1 180 GLU n 1 181 GLY n 1 182 ARG n 1 183 THR n 1 184 ASP n 1 185 LEU n 1 186 GLU n 1 187 ARG n 1 188 ARG n 1 189 VAL n 1 190 PRO n 1 191 PRO n 1 192 MET n 1 193 ALA n 1 194 VAL n 1 195 VAL n 1 196 PHE n 1 197 ALA n 1 198 ARG n 1 199 THR n 1 200 ALA n 1 201 GLY n 1 202 GLN n 1 203 VAL n 1 204 GLN n 1 205 LEU n 1 206 LEU n 1 207 LEU n 1 208 VAL n 1 209 CYS n 1 210 ARG n 1 211 VAL n 1 212 THR n 1 213 SER n 1 214 PHE n 1 215 TYR n 1 216 PRO n 1 217 ARG n 1 218 PRO n 1 219 ILE n 1 220 ALA n 1 221 VAL n 1 222 THR n 1 223 TRP n 1 224 LEU n 1 225 ARG n 1 226 ASP n 1 227 GLY n 1 228 ARG n 1 229 GLU n 1 230 VAL n 1 231 PRO n 1 232 PRO n 1 233 SER n 1 234 PRO n 1 235 ALA n 1 236 LEU n 1 237 SER n 1 238 THR n 1 239 GLY n 1 240 THR n 1 241 VAL n 1 242 LEU n 1 243 PRO n 1 244 ASN n 1 245 ALA n 1 246 ASP n 1 247 LEU n 1 248 THR n 1 249 TYR n 1 250 GLN n 1 251 LEU n 1 252 ARG n 1 253 SER n 1 254 THR n 1 255 LEU n 1 256 LEU n 1 257 VAL n 1 258 SER n 1 259 PRO n 1 260 GLN n 1 261 ASP n 1 262 GLY n 1 263 HIS n 1 264 GLY n 1 265 TYR n 1 266 ALA n 1 267 CYS n 1 268 ARG n 1 269 VAL n 1 270 GLN n 1 271 HIS n 1 272 CYS n 1 273 SER n 1 274 LEU n 1 275 GLY n 1 276 ASP n 1 277 ARG n 1 278 SER n 1 279 LEU n 1 280 LEU n 1 281 VAL n 1 282 PRO n 1 283 TRP n 1 284 HIS n 1 285 HIS n 1 286 HIS n 1 287 HIS n 1 288 HIS n 1 289 HIS n 2 1 ILE n 2 2 GLN n 2 3 ARG n 2 4 THR n 2 5 PRO n 2 6 LYS 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 ALA n 2 16 GLU n 2 17 ASN n 2 18 GLY n 2 19 LYS n 2 20 SER n 2 21 ASN n 2 22 PHE n 2 23 LEU n 2 24 ASN n 2 25 CYS n 2 26 TYR n 2 27 VAL n 2 28 SER n 2 29 GLY n 2 30 PHE n 2 31 HIS n 2 32 PRO n 2 33 SER n 2 34 ASP n 2 35 ILE n 2 36 GLU n 2 37 VAL n 2 38 ASP n 2 39 LEU n 2 40 LEU n 2 41 LYS n 2 42 ASN n 2 43 GLY n 2 44 GLU n 2 45 ARG n 2 46 ILE n 2 47 GLU n 2 48 LYS n 2 49 VAL n 2 50 GLU n 2 51 HIS n 2 52 SER n 2 53 ASP n 2 54 LEU 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 LEU n 2 65 LEU n 2 66 TYR n 2 67 TYR 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 LYS n 2 76 ASP n 2 77 GLU n 2 78 TYR n 2 79 ALA n 2 80 CYS n 2 81 ARG n 2 82 VAL n 2 83 ASN n 2 84 HIS n 2 85 VAL n 2 86 THR n 2 87 LEU n 2 88 SER n 2 89 GLN n 2 90 PRO n 2 91 LYS n 2 92 ILE n 2 93 VAL n 2 94 LYS n 2 95 TRP n 2 96 ASP n 2 97 ARG n 2 98 ASP n 2 99 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 ? ? ? chicken ? CD1-2 ? ? ? ? ? ? 'Gallus gallus' 9031 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? SF9 ? ? ? ? ? ? ? 'baculovirus shuttle vector' ? ? ? pBACpHp10 ? ? 2 1 sample ? ? ? human ? 'B2M, CDABP0092, HDCMA22P' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? SF9 ? ? ? ? ? ? ? 'baculovirus shuttle vector' ? ? ? pBACpHp10 ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP Q5GL29_CHICK Q5GL29 1 ;ETSCPPPEESQFFQLFYTLLLGNVSSTELTGMALLADVPIMVLDPHTWNLNICRPWVQEITAETEVKKILSFSMVGIRNT IRFMHEMTAKAGLDYPRVFQIHTGCKLYTNGTRWSFVNIGEGGRDLVTYELSRERWVPQRSTLLAKVMSNTLTDLRAVSG FLEHIFSSSFPNYILMLHEEGRTDLERRVPPMAVVFARTAGQVQLLLVCRVTSFYPRPIAVTWLRDGREVPPSPALSTGT VLPNADLTYQLRSTLLVSPQDGHGYACRVQHCSLGDRSLLVPW ; 20 ? 2 UNP B2MG_HUMAN P61769 2 ;IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYAC RVNHVTLSQPKIVKWDRDM ; 21 ? # 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 3DBX A 1 ? 283 ? Q5GL29 20 ? 302 ? 1 283 2 2 3DBX B 1 ? 99 ? P61769 21 ? 119 ? 1 99 # 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 3DBX HIS A 284 ? UNP Q5GL29 ? ? 'EXPRESSION TAG' 284 1 1 3DBX HIS A 285 ? UNP Q5GL29 ? ? 'EXPRESSION TAG' 285 2 1 3DBX HIS A 286 ? UNP Q5GL29 ? ? 'EXPRESSION TAG' 286 3 1 3DBX HIS A 287 ? UNP Q5GL29 ? ? 'EXPRESSION TAG' 287 4 1 3DBX HIS A 288 ? UNP Q5GL29 ? ? 'EXPRESSION TAG' 288 5 1 3DBX HIS A 289 ? UNP Q5GL29 ? ? 'EXPRESSION TAG' 289 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 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.entry_id 3DBX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.30 _exptl_crystal.density_percent_sol 46.63 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 277 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pdbx_details '20% PEG4000, 0.1M sodium citrate, 10% isopropanol, pH5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 315' _diffrn_detector.pdbx_collection_date 2005-10-21 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'double crystal, Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.97 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ALS BEAMLINE 8.2.1' _diffrn_source.pdbx_synchrotron_site ALS _diffrn_source.pdbx_synchrotron_beamline 8.2.1 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.97 # _reflns.entry_id 3DBX _reflns.observed_criterion_sigma_F 0 _reflns.observed_criterion_sigma_I 0 _reflns.d_resolution_high 2.0 _reflns.d_resolution_low 30 _reflns.number_all 26874 _reflns.number_obs 26874 _reflns.percent_possible_obs 93.2 _reflns.pdbx_Rmerge_I_obs 0.082 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 23.0 _reflns.B_iso_Wilson_estimate 33.9 _reflns.pdbx_redundancy 4.1 _reflns.R_free_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.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.0 _reflns_shell.d_res_low 2.07 _reflns_shell.percent_possible_all 95.6 _reflns_shell.Rmerge_I_obs 0.649 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.0 _reflns_shell.pdbx_redundancy 4.0 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 2680 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3DBX _refine.ls_number_reflns_obs 25747 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 27.91 _refine.ls_d_res_high 2.00 _refine.ls_percent_reflns_obs 93.28 _refine.ls_R_factor_obs 0.21779 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.21578 _refine.ls_R_factor_R_free 0.26614 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.1 _refine.ls_number_reflns_R_free 1096 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.954 _refine.correlation_coeff_Fo_to_Fc_free 0.927 _refine.B_iso_mean 45.698 _refine.aniso_B[1][1] 0.02 _refine.aniso_B[2][2] 0.02 _refine.aniso_B[3][3] -0.05 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _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_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ENTRY 1MHE' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.224 _refine.pdbx_overall_ESU_R_Free 0.195 _refine.overall_SU_ML 0.155 _refine.overall_SU_B 11.245 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2997 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 60 _refine_hist.number_atoms_solvent 149 _refine_hist.number_atoms_total 3206 _refine_hist.d_res_high 2.00 _refine_hist.d_res_low 27.91 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.015 0.022 ? 3150 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.576 1.967 ? 4294 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.514 5.000 ? 378 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.021 22.754 ? 138 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 15.208 15.000 ? 488 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 23.961 15.000 ? 24 'X-RAY DIFFRACTION' ? r_chiral_restr 0.113 0.200 ? 488 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.020 ? 2369 'X-RAY DIFFRACTION' ? r_nbd_refined 0.201 0.200 ? 1210 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.306 0.200 ? 2095 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.138 0.200 ? 160 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.219 0.200 ? 43 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.200 0.200 ? 6 'X-RAY DIFFRACTION' ? r_mcbond_it 0.950 1.500 ? 1960 'X-RAY DIFFRACTION' ? r_mcangle_it 1.393 2.000 ? 3080 'X-RAY DIFFRACTION' ? r_scbond_it 2.021 3.000 ? 1371 'X-RAY DIFFRACTION' ? r_scangle_it 2.971 4.500 ? 1214 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.999 _refine_ls_shell.d_res_low 2.051 _refine_ls_shell.number_reflns_R_work 1886 _refine_ls_shell.R_factor_R_work 0.25 _refine_ls_shell.percent_reflns_obs 95.46 _refine_ls_shell.R_factor_R_free 0.27 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 92 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3DBX _struct.title 'Structure of chicken CD1-2 with bound fatty acid' _struct.pdbx_descriptor 'CD1-2 antigen, Beta-2-microglobulin' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3DBX _struct_keywords.pdbx_keywords 'IMMUNE SYSTEM' _struct_keywords.text ;CD1, evolution, antigen-presentation, MHC-fold, hydrophobic binding groove, Immunoglobulin domain, Membrane, Transmembrane, Disease mutation, Glycation, Glycoprotein, Immune response, MHC I, Pyrrolidone carboxylic acid, Secreted, IMMUNE SYSTEM ; # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 4 ? G N N 5 ? H N N 5 ? # _struct_biol.id 1 _struct_biol.details ? # 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 1 GLU A 65 ? PHE A 72 ? GLU A 65 PHE A 72 1 ? 8 HELX_P HELX_P2 2 GLY A 76 ? LYS A 90 ? GLY A 76 LYS A 90 1 ? 15 HELX_P HELX_P3 3 THR A 142 ? LEU A 155 ? THR A 142 LEU A 155 1 ? 14 HELX_P HELX_P4 4 LEU A 155 ? SER A 168 ? LEU A 155 SER A 168 1 ? 14 HELX_P HELX_P5 5 SER A 168 ? GLY A 181 ? SER A 168 GLY A 181 1 ? 14 HELX_P HELX_P6 6 GLY A 181 ? GLU A 186 ? GLY A 181 GLU A 186 1 ? 6 HELX_P HELX_P7 7 HIS A 271 ? GLY A 275 ? HIS A 271 GLY A 275 5 ? 5 # _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 209 SG ? ? ? 1_555 A CYS 267 SG ? ? A CYS 209 A CYS 267 1_555 ? ? ? ? ? ? ? 1.984 ? disulf2 disulf ? ? B CYS 25 SG ? ? ? 1_555 B CYS 80 SG ? ? B CYS 25 B CYS 80 1_555 ? ? ? ? ? ? ? 2.019 ? covale1 covale ? ? A ASN 23 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 23 A NAG 500 1_555 ? ? ? ? ? ? ? 1.452 ? covale2 covale ? ? A ASN 51 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 51 A NAG 511 1_555 ? ? ? ? ? ? ? 1.465 ? covale3 covale ? ? A ASN 110 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 110 A NAG 521 1_555 ? ? ? ? ? ? ? 1.451 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 THR 61 A . ? THR 61 A ALA 62 A ? ALA 62 A 1 -6.98 2 TYR 95 A . ? TYR 95 A PRO 96 A ? PRO 96 A 1 -3.58 3 TYR 215 A . ? TYR 215 A PRO 216 A ? PRO 216 A 1 3.47 4 HIS 31 B . ? HIS 31 B PRO 32 B ? PRO 32 B 1 0.73 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 4 ? C ? 4 ? D ? 4 ? E ? 4 ? F ? 4 ? G ? 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 A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 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 A 1 LEU A 50 ? ILE A 52 ? LEU A 50 ILE A 52 A 2 VAL A 38 ? LEU A 43 ? VAL A 38 LEU A 43 A 3 THR A 27 ? LEU A 35 ? THR A 27 LEU A 35 A 4 PHE A 12 ? LEU A 21 ? PHE A 12 LEU A 21 A 5 ARG A 97 ? LEU A 107 ? ARG A 97 LEU A 107 A 6 ARG A 113 ? GLU A 121 ? ARG A 113 GLU A 121 A 7 ARG A 124 ? GLU A 130 ? ARG A 124 GLU A 130 A 8 ARG A 135 ? PRO A 138 ? ARG A 135 PRO A 138 B 1 MET A 192 ? ALA A 200 ? MET A 192 ALA A 200 B 2 GLN A 204 ? PHE A 214 ? GLN A 204 PHE A 214 B 3 TYR A 249 ? VAL A 257 ? TYR A 249 VAL A 257 B 4 LEU A 236 ? THR A 238 ? LEU A 236 THR A 238 C 1 MET A 192 ? ALA A 200 ? MET A 192 ALA A 200 C 2 GLN A 204 ? PHE A 214 ? GLN A 204 PHE A 214 C 3 TYR A 249 ? VAL A 257 ? TYR A 249 VAL A 257 C 4 LEU A 242 ? PRO A 243 ? LEU A 242 PRO A 243 D 1 ARG A 228 ? GLU A 229 ? ARG A 228 GLU A 229 D 2 ALA A 220 ? ARG A 225 ? ALA A 220 ARG A 225 D 3 TYR A 265 ? GLN A 270 ? TYR A 265 GLN A 270 D 4 LEU A 279 ? PRO A 282 ? LEU A 279 PRO A 282 E 1 LYS B 6 ? SER B 11 ? LYS B 6 SER B 11 E 2 ASN B 21 ? PHE B 30 ? ASN B 21 PHE B 30 E 3 PHE B 62 ? PHE B 70 ? PHE B 62 PHE B 70 E 4 GLU B 50 ? HIS B 51 ? GLU B 50 HIS B 51 F 1 LYS B 6 ? SER B 11 ? LYS B 6 SER B 11 F 2 ASN B 21 ? PHE B 30 ? ASN B 21 PHE B 30 F 3 PHE B 62 ? PHE B 70 ? PHE B 62 PHE B 70 F 4 SER B 55 ? PHE B 56 ? SER B 55 PHE B 56 G 1 GLU B 44 ? ARG B 45 ? GLU B 44 ARG B 45 G 2 GLU B 36 ? LYS B 41 ? GLU B 36 LYS B 41 G 3 TYR B 78 ? ASN B 83 ? TYR B 78 ASN B 83 G 4 LYS B 91 ? LYS B 94 ? LYS B 91 LYS 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 A 1 2 O ASN A 51 ? O ASN A 51 N VAL A 42 ? N VAL A 42 A 2 3 O ILE A 40 ? O ILE A 40 N ALA A 33 ? N ALA A 33 A 3 4 O LEU A 34 ? O LEU A 34 N GLN A 14 ? N GLN A 14 A 4 5 N PHE A 13 ? N PHE A 13 O CYS A 105 ? O CYS A 105 A 5 6 N HIS A 102 ? N HIS A 102 O ASN A 118 ? O ASN A 118 A 6 7 N ILE A 119 ? N ILE A 119 O VAL A 127 ? O VAL A 127 A 7 8 N THR A 128 ? N THR A 128 O VAL A 137 ? O VAL A 137 B 1 2 N ARG A 198 ? N ARG A 198 O LEU A 206 ? O LEU A 206 B 2 3 N LEU A 205 ? N LEU A 205 O VAL A 257 ? O VAL A 257 B 3 4 O THR A 254 ? O THR A 254 N SER A 237 ? N SER A 237 C 1 2 N ARG A 198 ? N ARG A 198 O LEU A 206 ? O LEU A 206 C 2 3 N LEU A 205 ? N LEU A 205 O VAL A 257 ? O VAL A 257 C 3 4 O GLN A 250 ? O GLN A 250 N LEU A 242 ? N LEU A 242 D 1 2 O ARG A 228 ? O ARG A 228 N ARG A 225 ? N ARG A 225 D 2 3 N THR A 222 ? N THR A 222 O ARG A 268 ? O ARG A 268 D 3 4 N CYS A 267 ? N CYS A 267 O VAL A 281 ? O VAL A 281 E 1 2 N TYR B 10 ? N TYR B 10 O ASN B 24 ? O ASN B 24 E 2 3 N CYS B 25 ? N CYS B 25 O TYR B 66 ? O TYR B 66 E 3 4 O TYR B 67 ? O TYR B 67 N GLU B 50 ? N GLU B 50 F 1 2 N TYR B 10 ? N TYR B 10 O ASN B 24 ? O ASN B 24 F 2 3 N CYS B 25 ? N CYS B 25 O TYR B 66 ? O TYR B 66 F 3 4 O TYR B 63 ? O TYR B 63 N SER B 55 ? N SER B 55 G 1 2 O GLU B 44 ? O GLU B 44 N LYS B 41 ? N LYS B 41 G 2 3 N LEU B 40 ? N LEU B 40 O ALA B 79 ? O ALA B 79 G 3 4 N CYS B 80 ? N CYS B 80 O VAL B 93 ? O VAL B 93 # 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 ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG A 500' AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 511' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 521' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE PLM A 522' # 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 2 ASN A 23 ? ASN A 23 . ? 1_555 ? 2 AC1 2 SER A 25 ? SER A 25 . ? 1_555 ? 3 AC2 3 ASP A 44 ? ASP A 44 . ? 1_555 ? 4 AC2 3 ASN A 51 ? ASN A 51 . ? 1_555 ? 5 AC2 3 ASP B 53 ? ASP B 53 . ? 1_555 ? 6 AC3 3 TYR A 108 ? TYR A 108 . ? 1_555 ? 7 AC3 3 ASN A 110 ? ASN A 110 . ? 1_555 ? 8 AC3 3 THR A 112 ? THR A 112 . ? 1_555 ? 9 AC4 4 MET A 74 ? MET A 74 . ? 1_555 ? 10 AC4 4 ASN A 79 ? ASN A 79 . ? 1_555 ? 11 AC4 4 ARG A 82 ? ARG A 82 . ? 1_555 ? 12 AC4 4 PHE A 83 ? PHE A 83 . ? 1_555 ? # _database_PDB_matrix.entry_id 3DBX _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 3DBX _atom_sites.fract_transf_matrix[1][1] 0.010851 _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] 0.010851 _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] 0.010342 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PRO A 1 7 ? 18.745 33.350 44.534 1.00 85.90 ? 7 PRO A N 1 ATOM 2 C CA . PRO A 1 7 ? 17.419 33.202 43.922 1.00 88.15 ? 7 PRO A CA 1 ATOM 3 C C . PRO A 1 7 ? 17.264 33.966 42.583 1.00 85.78 ? 7 PRO A C 1 ATOM 4 O O . PRO A 1 7 ? 17.779 33.522 41.549 1.00 85.49 ? 7 PRO A O 1 ATOM 5 C CB . PRO A 1 7 ? 16.461 33.757 45.002 1.00 89.37 ? 7 PRO A CB 1 ATOM 6 C CG . PRO A 1 7 ? 17.337 34.215 46.169 1.00 87.58 ? 7 PRO A CG 1 ATOM 7 C CD . PRO A 1 7 ? 18.739 34.320 45.643 1.00 84.67 ? 7 PRO A CD 1 ATOM 8 N N . GLU A 1 8 ? 16.565 35.102 42.620 1.00 84.22 ? 8 GLU A N 1 ATOM 9 C CA . GLU A 1 8 ? 16.247 35.896 41.427 1.00 82.33 ? 8 GLU A CA 1 ATOM 10 C C . GLU A 1 8 ? 16.659 37.366 41.592 1.00 77.79 ? 8 GLU A C 1 ATOM 11 O O . GLU A 1 8 ? 16.237 38.228 40.808 1.00 76.71 ? 8 GLU A O 1 ATOM 12 C CB . GLU A 1 8 ? 14.751 35.795 41.096 1.00 85.99 ? 8 GLU A CB 1 ATOM 13 C CG . GLU A 1 8 ? 13.847 36.200 42.253 1.00 87.92 ? 8 GLU A CG 1 ATOM 14 C CD . GLU A 1 8 ? 12.373 36.231 41.889 1.00 92.13 ? 8 GLU A CD 1 ATOM 15 O OE1 . GLU A 1 8 ? 11.832 35.209 41.399 1.00 96.88 ? 8 GLU A OE1 1 ATOM 16 O OE2 . GLU A 1 8 ? 11.745 37.286 42.123 1.00 93.11 ? 8 GLU A OE2 1 ATOM 17 N N . GLU A 1 9 ? 17.459 37.640 42.628 1.00 74.90 ? 9 GLU A N 1 ATOM 18 C CA . GLU A 1 9 ? 18.201 38.892 42.735 1.00 70.65 ? 9 GLU A CA 1 ATOM 19 C C . GLU A 1 9 ? 19.228 38.887 41.617 1.00 67.33 ? 9 GLU A C 1 ATOM 20 O O . GLU A 1 9 ? 19.649 39.937 41.133 1.00 64.92 ? 9 GLU A O 1 ATOM 21 C CB . GLU A 1 9 ? 18.918 39.009 44.093 1.00 70.39 ? 9 GLU A CB 1 ATOM 22 C CG . GLU A 1 9 ? 18.035 39.522 45.264 1.00 72.86 ? 9 GLU A CG 1 ATOM 23 C CD . GLU A 1 9 ? 18.812 39.812 46.576 1.00 72.05 ? 9 GLU A CD 1 ATOM 24 O OE1 . GLU A 1 9 ? 20.016 40.160 46.532 1.00 72.63 ? 9 GLU A OE1 1 ATOM 25 O OE2 . GLU A 1 9 ? 18.198 39.715 47.663 1.00 75.16 ? 9 GLU A OE2 1 ATOM 26 N N . SER A 1 10 ? 19.611 37.682 41.199 1.00 66.96 ? 10 SER A N 1 ATOM 27 C CA . SER A 1 10 ? 20.651 37.505 40.194 1.00 64.03 ? 10 SER A CA 1 ATOM 28 C C . SER A 1 10 ? 20.192 37.839 38.777 1.00 62.32 ? 10 SER A C 1 ATOM 29 O O . SER A 1 10 ? 21.024 38.001 37.886 1.00 61.60 ? 10 SER A O 1 ATOM 30 C CB . SER A 1 10 ? 21.238 36.099 40.257 1.00 66.43 ? 10 SER A CB 1 ATOM 31 O OG . SER A 1 10 ? 22.604 36.145 39.884 1.00 67.28 ? 10 SER A OG 1 ATOM 32 N N . GLN A 1 11 ? 18.877 37.933 38.576 1.00 61.05 ? 11 GLN A N 1 ATOM 33 C CA . GLN A 1 11 ? 18.305 38.355 37.296 1.00 59.11 ? 11 GLN A CA 1 ATOM 34 C C . GLN A 1 11 ? 17.592 39.712 37.397 1.00 56.01 ? 11 GLN A C 1 ATOM 35 O O . GLN A 1 11 ? 16.534 39.931 36.787 1.00 57.37 ? 11 GLN A O 1 ATOM 36 C CB . GLN A 1 11 ? 17.393 37.253 36.740 1.00 63.70 ? 11 GLN A CB 1 ATOM 37 C CG . GLN A 1 11 ? 18.177 35.988 36.440 1.00 65.21 ? 11 GLN A CG 1 ATOM 38 C CD . GLN A 1 11 ? 17.312 34.819 36.072 1.00 71.41 ? 11 GLN A CD 1 ATOM 39 O OE1 . GLN A 1 11 ? 16.503 34.345 36.873 1.00 74.44 ? 11 GLN A OE1 1 ATOM 40 N NE2 . GLN A 1 11 ? 17.491 34.326 34.854 1.00 72.72 ? 11 GLN A NE2 1 ATOM 41 N N . PHE A 1 12 ? 18.191 40.607 38.186 1.00 50.57 ? 12 PHE A N 1 ATOM 42 C CA . PHE A 1 12 ? 17.695 41.962 38.388 1.00 47.50 ? 12 PHE A CA 1 ATOM 43 C C . PHE A 1 12 ? 18.770 42.932 37.916 1.00 43.87 ? 12 PHE A C 1 ATOM 44 O O . PHE A 1 12 ? 19.816 43.120 38.573 1.00 41.82 ? 12 PHE A O 1 ATOM 45 C CB . PHE A 1 12 ? 17.335 42.198 39.870 1.00 47.27 ? 12 PHE A CB 1 ATOM 46 C CG . PHE A 1 12 ? 16.608 43.523 40.160 1.00 46.88 ? 12 PHE A CG 1 ATOM 47 C CD1 . PHE A 1 12 ? 15.979 44.255 39.161 1.00 47.80 ? 12 PHE A CD1 1 ATOM 48 C CD2 . PHE A 1 12 ? 16.522 44.001 41.468 1.00 46.44 ? 12 PHE A CD2 1 ATOM 49 C CE1 . PHE A 1 12 ? 15.300 45.457 39.450 1.00 45.96 ? 12 PHE A CE1 1 ATOM 50 C CE2 . PHE A 1 12 ? 15.840 45.182 41.759 1.00 47.02 ? 12 PHE A CE2 1 ATOM 51 C CZ . PHE A 1 12 ? 15.232 45.909 40.740 1.00 46.58 ? 12 PHE A CZ 1 ATOM 52 N N . PHE A 1 13 ? 18.499 43.535 36.768 1.00 43.04 ? 13 PHE A N 1 ATOM 53 C CA . PHE A 1 13 ? 19.380 44.511 36.137 1.00 40.71 ? 13 PHE A CA 1 ATOM 54 C C . PHE A 1 13 ? 18.898 45.932 36.431 1.00 38.74 ? 13 PHE A C 1 ATOM 55 O O . PHE A 1 13 ? 17.737 46.238 36.212 1.00 39.75 ? 13 PHE A O 1 ATOM 56 C CB . PHE A 1 13 ? 19.380 44.278 34.629 1.00 42.89 ? 13 PHE A CB 1 ATOM 57 C CG . PHE A 1 13 ? 20.339 45.142 33.892 1.00 43.80 ? 13 PHE A CG 1 ATOM 58 C CD1 . PHE A 1 13 ? 21.721 44.979 34.065 1.00 44.34 ? 13 PHE A CD1 1 ATOM 59 C CD2 . PHE A 1 13 ? 19.884 46.121 33.029 1.00 46.46 ? 13 PHE A CD2 1 ATOM 60 C CE1 . PHE A 1 13 ? 22.632 45.780 33.376 1.00 43.04 ? 13 PHE A CE1 1 ATOM 61 C CE2 . PHE A 1 13 ? 20.791 46.937 32.343 1.00 46.42 ? 13 PHE A CE2 1 ATOM 62 C CZ . PHE A 1 13 ? 22.164 46.750 32.512 1.00 44.12 ? 13 PHE A CZ 1 ATOM 63 N N . GLN A 1 14 ? 19.795 46.778 36.936 1.00 35.82 ? 14 GLN A N 1 ATOM 64 C CA . GLN A 1 14 ? 19.479 48.156 37.293 1.00 34.80 ? 14 GLN A CA 1 ATOM 65 C C . GLN A 1 14 ? 20.512 49.132 36.765 1.00 34.00 ? 14 GLN A C 1 ATOM 66 O O . GLN A 1 14 ? 21.691 48.813 36.692 1.00 32.91 ? 14 GLN A O 1 ATOM 67 C CB . GLN A 1 14 ? 19.409 48.315 38.809 1.00 33.71 ? 14 GLN A CB 1 ATOM 68 C CG . GLN A 1 14 ? 18.262 47.581 39.469 1.00 36.85 ? 14 GLN A CG 1 ATOM 69 C CD . GLN A 1 14 ? 18.175 47.916 40.951 1.00 38.33 ? 14 GLN A CD 1 ATOM 70 O OE1 . GLN A 1 14 ? 17.493 48.854 41.341 1.00 36.45 ? 14 GLN A OE1 1 ATOM 71 N NE2 . GLN A 1 14 ? 18.883 47.154 41.774 1.00 38.61 ? 14 GLN A NE2 1 ATOM 72 N N . LEU A 1 15 ? 20.041 50.341 36.448 1.00 34.18 ? 15 LEU A N 1 ATOM 73 C CA . LEU A 1 15 ? 20.848 51.430 35.968 1.00 33.58 ? 15 LEU A CA 1 ATOM 74 C C . LEU A 1 15 ? 20.545 52.651 36.843 1.00 33.71 ? 15 LEU A C 1 ATOM 75 O O . LEU A 1 15 ? 19.382 52.990 37.093 1.00 34.79 ? 15 LEU A O 1 ATOM 76 C CB . LEU A 1 15 ? 20.489 51.752 34.514 1.00 35.44 ? 15 LEU A CB 1 ATOM 77 C CG . LEU A 1 15 ? 20.784 50.767 33.391 1.00 38.30 ? 15 LEU A CG 1 ATOM 78 C CD1 . LEU A 1 15 ? 20.050 51.187 32.093 1.00 44.31 ? 15 LEU A CD1 1 ATOM 79 C CD2 . LEU A 1 15 ? 22.271 50.677 33.131 1.00 38.97 ? 15 LEU A CD2 1 ATOM 80 N N . PHE A 1 16 ? 21.598 53.315 37.289 1.00 33.35 ? 16 PHE A N 1 ATOM 81 C CA . PHE A 1 16 ? 21.504 54.517 38.115 1.00 33.41 ? 16 PHE A CA 1 ATOM 82 C C . PHE A 1 16 ? 22.330 55.629 37.442 1.00 34.32 ? 16 PHE A C 1 ATOM 83 O O . PHE A 1 16 ? 23.526 55.470 37.288 1.00 34.71 ? 16 PHE A O 1 ATOM 84 C CB . PHE A 1 16 ? 22.159 54.214 39.479 1.00 32.63 ? 16 PHE A CB 1 ATOM 85 C CG . PHE A 1 16 ? 21.457 53.158 40.272 1.00 31.62 ? 16 PHE A CG 1 ATOM 86 C CD1 . PHE A 1 16 ? 20.513 53.506 41.215 1.00 34.44 ? 16 PHE A CD1 1 ATOM 87 C CD2 . PHE A 1 16 ? 21.734 51.815 40.071 1.00 34.65 ? 16 PHE A CD2 1 ATOM 88 C CE1 . PHE A 1 16 ? 19.839 52.514 41.955 1.00 37.16 ? 16 PHE A CE1 1 ATOM 89 C CE2 . PHE A 1 16 ? 21.068 50.819 40.795 1.00 34.42 ? 16 PHE A CE2 1 ATOM 90 C CZ . PHE A 1 16 ? 20.132 51.166 41.731 1.00 35.10 ? 16 PHE A CZ 1 ATOM 91 N N . TYR A 1 17 ? 21.724 56.750 37.084 1.00 34.75 ? 17 TYR A N 1 ATOM 92 C CA . TYR A 1 17 ? 22.445 57.841 36.414 1.00 36.32 ? 17 TYR A CA 1 ATOM 93 C C . TYR A 1 17 ? 22.181 59.151 37.128 1.00 36.03 ? 17 TYR A C 1 ATOM 94 O O . TYR A 1 17 ? 21.047 59.415 37.476 1.00 34.89 ? 17 TYR A O 1 ATOM 95 C CB . TYR A 1 17 ? 21.979 57.999 34.967 1.00 38.91 ? 17 TYR A CB 1 ATOM 96 C CG . TYR A 1 17 ? 22.638 57.051 34.011 1.00 41.10 ? 17 TYR A CG 1 ATOM 97 C CD1 . TYR A 1 17 ? 23.712 57.451 33.235 1.00 42.11 ? 17 TYR A CD1 1 ATOM 98 C CD2 . TYR A 1 17 ? 22.213 55.735 33.907 1.00 44.21 ? 17 TYR A CD2 1 ATOM 99 C CE1 . TYR A 1 17 ? 24.346 56.558 32.344 1.00 44.90 ? 17 TYR A CE1 1 ATOM 100 C CE2 . TYR A 1 17 ? 22.846 54.828 33.019 1.00 43.21 ? 17 TYR A CE2 1 ATOM 101 C CZ . TYR A 1 17 ? 23.907 55.253 32.256 1.00 44.05 ? 17 TYR A CZ 1 ATOM 102 O OH . TYR A 1 17 ? 24.518 54.371 31.374 1.00 47.54 ? 17 TYR A OH 1 ATOM 103 N N . THR A 1 18 ? 23.234 59.950 37.308 1.00 36.69 ? 18 THR A N 1 ATOM 104 C CA . THR A 1 18 ? 23.169 61.295 37.917 1.00 38.60 ? 18 THR A CA 1 ATOM 105 C C . THR A 1 18 ? 23.787 62.295 36.936 1.00 40.80 ? 18 THR A C 1 ATOM 106 O O . THR A 1 18 ? 24.929 62.122 36.456 1.00 41.80 ? 18 THR A O 1 ATOM 107 C CB . THR A 1 18 ? 23.912 61.346 39.243 1.00 37.94 ? 18 THR A CB 1 ATOM 108 O OG1 . THR A 1 18 ? 23.336 60.388 40.139 1.00 38.36 ? 18 THR A OG1 1 ATOM 109 C CG2 . THR A 1 18 ? 23.844 62.723 39.878 1.00 38.97 ? 18 THR A CG2 1 ATOM 110 N N . LEU A 1 19 ? 22.989 63.292 36.592 1.00 41.34 ? 19 LEU A N 1 ATOM 111 C CA . LEU A 1 19 ? 23.383 64.335 35.676 1.00 43.35 ? 19 LEU A CA 1 ATOM 112 C C . LEU A 1 19 ? 23.371 65.618 36.500 1.00 44.24 ? 19 LEU A C 1 ATOM 113 O O . LEU A 1 19 ? 22.312 66.106 36.840 1.00 44.47 ? 19 LEU A O 1 ATOM 114 C CB . LEU A 1 19 ? 22.379 64.425 34.517 1.00 45.38 ? 19 LEU A CB 1 ATOM 115 C CG . LEU A 1 19 ? 22.490 63.393 33.388 1.00 44.51 ? 19 LEU A CG 1 ATOM 116 C CD1 . LEU A 1 19 ? 22.325 61.967 33.931 1.00 45.22 ? 19 LEU A CD1 1 ATOM 117 C CD2 . LEU A 1 19 ? 21.505 63.637 32.292 1.00 45.16 ? 19 LEU A CD2 1 ATOM 118 N N . LEU A 1 20 ? 24.556 66.087 36.880 1.00 45.23 ? 20 LEU A N 1 ATOM 119 C CA . LEU A 1 20 ? 24.722 67.323 37.632 1.00 47.69 ? 20 LEU A CA 1 ATOM 120 C C . LEU A 1 20 ? 25.058 68.426 36.658 1.00 51.00 ? 20 LEU A C 1 ATOM 121 O O . LEU A 1 20 ? 26.166 68.496 36.092 1.00 52.92 ? 20 LEU A O 1 ATOM 122 C CB . LEU A 1 20 ? 25.799 67.206 38.715 1.00 47.38 ? 20 LEU A CB 1 ATOM 123 C CG . LEU A 1 20 ? 26.278 68.504 39.403 1.00 51.84 ? 20 LEU A CG 1 ATOM 124 C CD1 . LEU A 1 20 ? 25.143 69.474 39.861 1.00 50.33 ? 20 LEU A CD1 1 ATOM 125 C CD2 . LEU A 1 20 ? 27.194 68.147 40.576 1.00 52.00 ? 20 LEU A CD2 1 ATOM 126 N N . LEU A 1 21 ? 24.073 69.289 36.466 1.00 51.88 ? 21 LEU A N 1 ATOM 127 C CA . LEU A 1 21 ? 24.144 70.345 35.505 1.00 55.15 ? 21 LEU A CA 1 ATOM 128 C C . LEU A 1 21 ? 24.596 71.620 36.233 1.00 57.45 ? 21 LEU A C 1 ATOM 129 O O . LEU A 1 21 ? 23.780 72.405 36.706 1.00 57.21 ? 21 LEU A O 1 ATOM 130 C CB . LEU A 1 21 ? 22.770 70.497 34.841 1.00 55.73 ? 21 LEU A CB 1 ATOM 131 C CG . LEU A 1 21 ? 22.383 69.626 33.634 1.00 56.40 ? 21 LEU A CG 1 ATOM 132 C CD1 . LEU A 1 21 ? 22.807 68.182 33.742 1.00 53.50 ? 21 LEU A CD1 1 ATOM 133 C CD2 . LEU A 1 21 ? 20.888 69.756 33.300 1.00 56.42 ? 21 LEU A CD2 1 ATOM 134 N N . GLY A 1 22 ? 25.918 71.785 36.308 1.00 59.41 ? 22 GLY A N 1 ATOM 135 C CA . GLY A 1 22 ? 26.579 72.914 36.972 1.00 63.10 ? 22 GLY A CA 1 ATOM 136 C C . GLY A 1 22 ? 26.196 74.282 36.472 1.00 67.14 ? 22 GLY A C 1 ATOM 137 O O . GLY A 1 22 ? 25.506 75.015 37.166 1.00 68.42 ? 22 GLY A O 1 ATOM 138 N N . ASN A 1 23 ? 26.682 74.640 35.284 1.00 70.25 ? 23 ASN A N 1 ATOM 139 C CA . ASN A 1 23 ? 26.249 75.840 34.552 1.00 73.94 ? 23 ASN A CA 1 ATOM 140 C C . ASN A 1 23 ? 25.845 75.447 33.127 1.00 74.20 ? 23 ASN A C 1 ATOM 141 O O . ASN A 1 23 ? 25.725 74.258 32.813 1.00 71.14 ? 23 ASN A O 1 ATOM 142 C CB . ASN A 1 23 ? 27.333 76.940 34.544 1.00 79.06 ? 23 ASN A CB 1 ATOM 143 C CG . ASN A 1 23 ? 28.718 76.419 34.169 1.00 81.02 ? 23 ASN A CG 1 ATOM 144 O OD1 . ASN A 1 23 ? 28.844 75.389 33.509 1.00 80.22 ? 23 ASN A OD1 1 ATOM 145 N ND2 . ASN A 1 23 ? 29.764 77.144 34.586 1.00 85.95 ? 23 ASN A ND2 1 ATOM 146 N N . VAL A 1 24 ? 25.638 76.429 32.264 1.00 78.26 ? 24 VAL A N 1 ATOM 147 C CA . VAL A 1 24 ? 25.222 76.137 30.891 1.00 79.55 ? 24 VAL A CA 1 ATOM 148 C C . VAL A 1 24 ? 26.216 75.199 30.138 1.00 78.95 ? 24 VAL A C 1 ATOM 149 O O . VAL A 1 24 ? 25.804 74.235 29.492 1.00 76.93 ? 24 VAL A O 1 ATOM 150 C CB . VAL A 1 24 ? 24.865 77.435 30.133 1.00 84.64 ? 24 VAL A CB 1 ATOM 151 C CG1 . VAL A 1 24 ? 26.079 78.341 29.988 1.00 89.73 ? 24 VAL A CG1 1 ATOM 152 C CG2 . VAL A 1 24 ? 24.223 77.122 28.794 1.00 86.97 ? 24 VAL A CG2 1 ATOM 153 N N . SER A 1 25 ? 27.512 75.463 30.297 1.00 80.86 ? 25 SER A N 1 ATOM 154 C CA . SER A 1 25 ? 28.584 74.690 29.666 1.00 81.31 ? 25 SER A CA 1 ATOM 155 C C . SER A 1 25 ? 29.105 73.493 30.470 1.00 77.10 ? 25 SER A C 1 ATOM 156 O O . SER A 1 25 ? 30.101 72.868 30.078 1.00 77.85 ? 25 SER A O 1 ATOM 157 C CB . SER A 1 25 ? 29.755 75.616 29.292 1.00 87.31 ? 25 SER A CB 1 ATOM 158 O OG . SER A 1 25 ? 29.919 76.680 30.221 1.00 88.39 ? 25 SER A OG 1 ATOM 159 N N . SER A 1 26 ? 28.440 73.149 31.571 1.00 72.66 ? 26 SER A N 1 ATOM 160 C CA . SER A 1 26 ? 28.970 72.104 32.441 1.00 69.38 ? 26 SER A CA 1 ATOM 161 C C . SER A 1 26 ? 27.985 70.977 32.812 1.00 64.83 ? 26 SER A C 1 ATOM 162 O O . SER A 1 26 ? 26.900 71.215 33.359 1.00 63.18 ? 26 SER A O 1 ATOM 163 C CB . SER A 1 26 ? 29.628 72.711 33.694 1.00 70.16 ? 26 SER A CB 1 ATOM 164 O OG . SER A 1 26 ? 30.273 71.718 34.481 1.00 68.34 ? 26 SER A OG 1 ATOM 165 N N . THR A 1 27 ? 28.384 69.751 32.488 1.00 62.82 ? 27 THR A N 1 ATOM 166 C CA . THR A 1 27 ? 27.716 68.564 32.978 1.00 58.85 ? 27 THR A CA 1 ATOM 167 C C . THR A 1 27 ? 28.764 67.696 33.641 1.00 57.72 ? 27 THR A C 1 ATOM 168 O O . THR A 1 27 ? 29.857 67.493 33.096 1.00 60.17 ? 27 THR A O 1 ATOM 169 C CB . THR A 1 27 ? 27.041 67.736 31.848 1.00 58.05 ? 27 THR A CB 1 ATOM 170 O OG1 . THR A 1 27 ? 26.359 68.604 30.939 1.00 61.14 ? 27 THR A OG1 1 ATOM 171 C CG2 . THR A 1 27 ? 26.043 66.754 32.437 1.00 53.73 ? 27 THR A CG2 1 ATOM 172 N N . GLU A 1 28 ? 28.420 67.174 34.812 1.00 54.72 ? 28 GLU A N 1 ATOM 173 C CA . GLU A 1 28 ? 29.214 66.161 35.451 1.00 53.09 ? 28 GLU A CA 1 ATOM 174 C C . GLU A 1 28 ? 28.350 64.909 35.500 1.00 49.59 ? 28 GLU A C 1 ATOM 175 O O . GLU A 1 28 ? 27.192 64.936 35.922 1.00 48.28 ? 28 GLU A O 1 ATOM 176 C CB . GLU A 1 28 ? 29.640 66.613 36.850 1.00 53.31 ? 28 GLU A CB 1 ATOM 177 N N . LEU A 1 29 ? 28.890 63.793 35.055 1.00 48.99 ? 29 LEU A N 1 ATOM 178 C CA . LEU A 1 29 ? 28.063 62.587 35.055 1.00 45.63 ? 29 LEU A CA 1 ATOM 179 C C . LEU A 1 29 ? 28.595 61.505 35.961 1.00 43.69 ? 29 LEU A C 1 ATOM 180 O O . LEU A 1 29 ? 29.800 61.335 36.103 1.00 44.47 ? 29 LEU A O 1 ATOM 181 C CB . LEU A 1 29 ? 27.919 62.015 33.646 1.00 46.78 ? 29 LEU A CB 1 ATOM 182 C CG . LEU A 1 29 ? 27.252 62.793 32.504 1.00 50.35 ? 29 LEU A CG 1 ATOM 183 C CD1 . LEU A 1 29 ? 27.477 62.004 31.225 1.00 53.46 ? 29 LEU A CD1 1 ATOM 184 C CD2 . LEU A 1 29 ? 25.769 62.958 32.746 1.00 49.80 ? 29 LEU A CD2 1 ATOM 185 N N . THR A 1 30 ? 27.674 60.755 36.549 1.00 41.11 ? 30 THR A N 1 ATOM 186 C CA . THR A 1 30 ? 27.997 59.452 37.123 1.00 40.16 ? 30 THR A CA 1 ATOM 187 C C . THR A 1 30 ? 26.919 58.484 36.678 1.00 37.36 ? 30 THR A C 1 ATOM 188 O O . THR A 1 30 ? 25.783 58.884 36.411 1.00 36.47 ? 30 THR A O 1 ATOM 189 C CB . THR A 1 30 ? 28.035 59.485 38.684 1.00 40.19 ? 30 THR A CB 1 ATOM 190 O OG1 . THR A 1 30 ? 26.755 59.890 39.178 1.00 43.13 ? 30 THR A OG1 1 ATOM 191 C CG2 . THR A 1 30 ? 29.082 60.469 39.175 1.00 42.30 ? 30 THR A CG2 1 ATOM 192 N N . GLY A 1 31 ? 27.279 57.217 36.569 1.00 35.75 ? 31 GLY A N 1 ATOM 193 C CA . GLY A 1 31 ? 26.286 56.196 36.271 1.00 34.30 ? 31 GLY A CA 1 ATOM 194 C C . GLY A 1 31 ? 26.853 54.810 36.483 1.00 34.64 ? 31 GLY A C 1 ATOM 195 O O . GLY A 1 31 ? 28.065 54.563 36.310 1.00 33.41 ? 31 GLY A O 1 ATOM 196 N N . MET A 1 32 ? 25.969 53.911 36.876 1.00 34.32 ? 32 MET A N 1 ATOM 197 C CA . MET A 1 32 ? 26.343 52.514 37.150 1.00 37.62 ? 32 MET A CA 1 ATOM 198 C C . MET A 1 32 ? 25.291 51.565 36.649 1.00 34.62 ? 32 MET A C 1 ATOM 199 O O . MET A 1 32 ? 24.118 51.871 36.726 1.00 34.38 ? 32 MET A O 1 ATOM 200 C CB . MET A 1 32 ? 26.464 52.305 38.647 1.00 37.05 ? 32 MET A CB 1 ATOM 201 C CG . MET A 1 32 ? 27.118 50.965 38.980 1.00 40.79 ? 32 MET A CG 1 ATOM 202 S SD . MET A 1 32 ? 27.257 50.828 40.734 1.00 44.93 ? 32 MET A SD 1 ATOM 203 C CE . MET A 1 32 ? 28.184 52.296 41.127 1.00 42.40 ? 32 MET A CE 1 ATOM 204 N N . ALA A 1 33 ? 25.718 50.415 36.134 1.00 35.30 ? 33 ALA A N 1 ATOM 205 C CA . ALA A 1 33 ? 24.820 49.313 35.846 1.00 33.70 ? 33 ALA A CA 1 ATOM 206 C C . ALA A 1 33 ? 25.139 48.153 36.782 1.00 33.63 ? 33 ALA A C 1 ATOM 207 O O . ALA A 1 33 ? 26.314 47.794 36.944 1.00 33.96 ? 33 ALA A O 1 ATOM 208 C CB . ALA A 1 33 ? 24.972 48.870 34.392 1.00 34.92 ? 33 ALA A CB 1 ATOM 209 N N . LEU A 1 34 ? 24.095 47.531 37.334 1.00 31.87 ? 34 LEU A N 1 ATOM 210 C CA . LEU A 1 34 ? 24.238 46.440 38.327 1.00 31.63 ? 34 LEU A CA 1 ATOM 211 C C . LEU A 1 34 ? 23.435 45.231 37.901 1.00 32.05 ? 34 LEU A C 1 ATOM 212 O O . LEU A 1 34 ? 22.341 45.390 37.404 1.00 32.15 ? 34 LEU A O 1 ATOM 213 C CB . LEU A 1 34 ? 23.681 46.884 39.705 1.00 30.70 ? 34 LEU A CB 1 ATOM 214 C CG . LEU A 1 34 ? 24.313 47.990 40.542 1.00 32.65 ? 34 LEU A CG 1 ATOM 215 C CD1 . LEU A 1 34 ? 23.398 48.220 41.727 1.00 36.93 ? 34 LEU A CD1 1 ATOM 216 C CD2 . LEU A 1 34 ? 25.610 47.535 41.101 1.00 32.26 ? 34 LEU A CD2 1 ATOM 217 N N . LEU A 1 35 ? 23.990 44.038 38.106 1.00 32.16 ? 35 LEU A N 1 ATOM 218 C CA . LEU A 1 35 ? 23.223 42.809 38.110 1.00 33.38 ? 35 LEU A CA 1 ATOM 219 C C . LEU A 1 35 ? 23.352 42.283 39.538 1.00 33.07 ? 35 LEU A C 1 ATOM 220 O O . LEU A 1 35 ? 24.475 42.122 40.005 1.00 33.71 ? 35 LEU A O 1 ATOM 221 C CB . LEU A 1 35 ? 23.766 41.791 37.081 1.00 34.17 ? 35 LEU A CB 1 ATOM 222 C CG . LEU A 1 35 ? 22.942 40.516 36.868 1.00 38.66 ? 35 LEU A CG 1 ATOM 223 C CD1 . LEU A 1 35 ? 21.600 40.822 36.247 1.00 37.34 ? 35 LEU A CD1 1 ATOM 224 C CD2 . LEU A 1 35 ? 23.694 39.457 36.029 1.00 39.51 ? 35 LEU A CD2 1 ATOM 225 N N . ALA A 1 36 ? 22.227 42.012 40.217 1.00 33.16 ? 36 ALA A N 1 ATOM 226 C CA . ALA A 1 36 ? 22.195 41.859 41.684 1.00 33.08 ? 36 ALA A CA 1 ATOM 227 C C . ALA A 1 36 ? 22.911 43.059 42.349 1.00 31.84 ? 36 ALA A C 1 ATOM 228 O O . ALA A 1 36 ? 22.549 44.202 42.072 1.00 32.45 ? 36 ALA A O 1 ATOM 229 C CB . ALA A 1 36 ? 22.804 40.504 42.127 1.00 34.18 ? 36 ALA A CB 1 ATOM 230 N N . ASP A 1 37 ? 23.929 42.819 43.168 1.00 31.03 ? 37 ASP A N 1 ATOM 231 C CA . ASP A 1 37 ? 24.755 43.926 43.728 1.00 30.24 ? 37 ASP A CA 1 ATOM 232 C C . ASP A 1 37 ? 26.121 44.022 43.072 1.00 29.14 ? 37 ASP A C 1 ATOM 233 O O . ASP A 1 37 ? 27.020 44.673 43.587 1.00 29.51 ? 37 ASP A O 1 ATOM 234 C CB . ASP A 1 37 ? 24.925 43.784 45.265 1.00 31.85 ? 37 ASP A CB 1 ATOM 235 C CG . ASP A 1 37 ? 25.403 42.417 45.698 1.00 35.78 ? 37 ASP A CG 1 ATOM 236 O OD1 . ASP A 1 37 ? 25.597 41.530 44.840 1.00 36.93 ? 37 ASP A OD1 1 ATOM 237 O OD2 . ASP A 1 37 ? 25.594 42.226 46.923 1.00 37.90 ? 37 ASP A OD2 1 ATOM 238 N N . VAL A 1 38 ? 26.283 43.378 41.925 1.00 28.97 ? 38 VAL A N 1 ATOM 239 C CA . VAL A 1 38 ? 27.576 43.339 41.256 1.00 30.91 ? 38 VAL A CA 1 ATOM 240 C C . VAL A 1 38 ? 27.545 44.440 40.211 1.00 31.34 ? 38 VAL A C 1 ATOM 241 O O . VAL A 1 38 ? 26.686 44.393 39.325 1.00 30.83 ? 38 VAL A O 1 ATOM 242 C CB . VAL A 1 38 ? 27.752 42.000 40.505 1.00 30.98 ? 38 VAL A CB 1 ATOM 243 C CG1 . VAL A 1 38 ? 29.090 41.988 39.730 1.00 33.20 ? 38 VAL A CG1 1 ATOM 244 C CG2 . VAL A 1 38 ? 27.648 40.820 41.494 1.00 34.04 ? 38 VAL A CG2 1 ATOM 245 N N . PRO A 1 39 ? 28.447 45.432 40.333 1.00 33.05 ? 39 PRO A N 1 ATOM 246 C CA . PRO A 1 39 ? 28.651 46.474 39.325 1.00 33.59 ? 39 PRO A CA 1 ATOM 247 C C . PRO A 1 39 ? 29.161 45.840 38.034 1.00 35.20 ? 39 PRO A C 1 ATOM 248 O O . PRO A 1 39 ? 30.157 45.120 38.057 1.00 37.74 ? 39 PRO A O 1 ATOM 249 C CB . PRO A 1 39 ? 29.738 47.330 39.951 1.00 34.80 ? 39 PRO A CB 1 ATOM 250 C CG . PRO A 1 39 ? 29.588 47.088 41.453 1.00 34.54 ? 39 PRO A CG 1 ATOM 251 C CD . PRO A 1 39 ? 29.347 45.624 41.491 1.00 33.56 ? 39 PRO A CD 1 ATOM 252 N N . ILE A 1 40 ? 28.450 46.060 36.931 1.00 35.31 ? 40 ILE A N 1 ATOM 253 C CA . ILE A 1 40 ? 28.769 45.450 35.622 1.00 37.83 ? 40 ILE A CA 1 ATOM 254 C C . ILE A 1 40 ? 29.522 46.470 34.765 1.00 39.08 ? 40 ILE A C 1 ATOM 255 O O . ILE A 1 40 ? 30.493 46.130 34.074 1.00 40.76 ? 40 ILE A O 1 ATOM 256 C CB . ILE A 1 40 ? 27.448 44.963 34.894 1.00 36.91 ? 40 ILE A CB 1 ATOM 257 C CG1 . ILE A 1 40 ? 26.856 43.768 35.615 1.00 39.11 ? 40 ILE A CG1 1 ATOM 258 C CG2 . ILE A 1 40 ? 27.697 44.555 33.480 1.00 41.85 ? 40 ILE A CG2 1 ATOM 259 C CD1 . ILE A 1 40 ? 27.889 42.798 36.102 1.00 39.27 ? 40 ILE A CD1 1 ATOM 260 N N . MET A 1 41 ? 29.049 47.717 34.831 1.00 38.14 ? 41 MET A N 1 ATOM 261 C CA . MET A 1 41 ? 29.551 48.817 34.017 1.00 40.72 ? 41 MET A CA 1 ATOM 262 C C . MET A 1 41 ? 29.492 50.073 34.857 1.00 38.43 ? 41 MET A C 1 ATOM 263 O O . MET A 1 41 ? 28.572 50.244 35.657 1.00 35.92 ? 41 MET A O 1 ATOM 264 C CB . MET A 1 41 ? 28.685 49.016 32.768 1.00 41.13 ? 41 MET A CB 1 ATOM 265 C CG . MET A 1 41 ? 28.955 48.025 31.674 1.00 45.69 ? 41 MET A CG 1 ATOM 266 S SD . MET A 1 41 ? 28.031 48.284 30.143 1.00 50.97 ? 41 MET A SD 1 ATOM 267 C CE . MET A 1 41 ? 26.338 48.093 30.713 1.00 46.89 ? 41 MET A CE 1 ATOM 268 N N . VAL A 1 42 ? 30.475 50.936 34.699 1.00 39.39 ? 42 VAL A N 1 ATOM 269 C CA . VAL A 1 42 ? 30.434 52.222 35.376 1.00 39.40 ? 42 VAL A CA 1 ATOM 270 C C . VAL A 1 42 ? 30.772 53.299 34.351 1.00 41.42 ? 42 VAL A C 1 ATOM 271 O O . VAL A 1 42 ? 31.683 53.141 33.541 1.00 43.61 ? 42 VAL A O 1 ATOM 272 C CB . VAL A 1 42 ? 31.373 52.220 36.627 1.00 39.76 ? 42 VAL A CB 1 ATOM 273 C CG1 . VAL A 1 42 ? 31.857 53.602 37.022 1.00 42.48 ? 42 VAL A CG1 1 ATOM 274 C CG2 . VAL A 1 42 ? 30.639 51.590 37.814 1.00 39.83 ? 42 VAL A CG2 1 ATOM 275 N N . LEU A 1 43 ? 30.018 54.385 34.359 1.00 41.13 ? 43 LEU A N 1 ATOM 276 C CA . LEU A 1 43 ? 30.276 55.440 33.410 1.00 44.53 ? 43 LEU A CA 1 ATOM 277 C C . LEU A 1 43 ? 31.531 56.192 33.871 1.00 47.28 ? 43 LEU A C 1 ATOM 278 O O . LEU A 1 43 ? 31.637 56.537 35.051 1.00 46.87 ? 43 LEU A O 1 ATOM 279 C CB . LEU A 1 43 ? 29.048 56.356 33.321 1.00 43.23 ? 43 LEU A CB 1 ATOM 280 C CG . LEU A 1 43 ? 29.093 57.510 32.311 1.00 46.12 ? 43 LEU A CG 1 ATOM 281 C CD1 . LEU A 1 43 ? 28.879 56.962 30.937 1.00 46.88 ? 43 LEU A CD1 1 ATOM 282 C CD2 . LEU A 1 43 ? 28.050 58.603 32.610 1.00 45.45 ? 43 LEU A CD2 1 ATOM 283 N N . ASP A 1 44 ? 32.493 56.425 32.980 1.00 51.80 ? 44 ASP A N 1 ATOM 284 C CA . ASP A 1 44 ? 33.648 57.238 33.378 1.00 55.87 ? 44 ASP A CA 1 ATOM 285 C C . ASP A 1 44 ? 33.291 58.713 33.252 1.00 57.48 ? 44 ASP A C 1 ATOM 286 O O . ASP A 1 44 ? 32.933 59.157 32.163 1.00 59.51 ? 44 ASP A O 1 ATOM 287 C CB . ASP A 1 44 ? 34.921 56.927 32.580 1.00 60.01 ? 44 ASP A CB 1 ATOM 288 C CG . ASP A 1 44 ? 36.115 57.755 33.060 1.00 65.33 ? 44 ASP A CG 1 ATOM 289 O OD1 . ASP A 1 44 ? 36.599 57.518 34.186 1.00 67.48 ? 44 ASP A OD1 1 ATOM 290 O OD2 . ASP A 1 44 ? 36.561 58.667 32.330 1.00 70.79 ? 44 ASP A OD2 1 ATOM 291 N N . PRO A 1 45 ? 33.363 59.471 34.371 1.00 57.33 ? 45 PRO A N 1 ATOM 292 C CA . PRO A 1 45 ? 32.934 60.868 34.396 1.00 58.40 ? 45 PRO A CA 1 ATOM 293 C C . PRO A 1 45 ? 33.692 61.770 33.435 1.00 62.93 ? 45 PRO A C 1 ATOM 294 O O . PRO A 1 45 ? 33.145 62.772 32.974 1.00 63.70 ? 45 PRO A O 1 ATOM 295 C CB . PRO A 1 45 ? 33.216 61.286 35.843 1.00 57.89 ? 45 PRO A CB 1 ATOM 296 C CG . PRO A 1 45 ? 33.121 59.983 36.602 1.00 56.16 ? 45 PRO A CG 1 ATOM 297 C CD . PRO A 1 45 ? 33.824 59.037 35.702 1.00 55.92 ? 45 PRO A CD 1 ATOM 298 N N . HIS A 1 46 ? 34.935 61.401 33.138 1.00 65.87 ? 46 HIS A N 1 ATOM 299 C CA . HIS A 1 46 ? 35.825 62.233 32.351 1.00 70.98 ? 46 HIS A CA 1 ATOM 300 C C . HIS A 1 46 ? 35.639 62.025 30.854 1.00 72.15 ? 46 HIS A C 1 ATOM 301 O O . HIS A 1 46 ? 35.764 62.969 30.092 1.00 75.50 ? 46 HIS A O 1 ATOM 302 C CB . HIS A 1 46 ? 37.285 61.985 32.758 1.00 74.69 ? 46 HIS A CB 1 ATOM 303 C CG . HIS A 1 46 ? 37.543 62.168 34.225 1.00 75.53 ? 46 HIS A CG 1 ATOM 304 N ND1 . HIS A 1 46 ? 37.908 63.383 34.774 1.00 80.25 ? 46 HIS A ND1 1 ATOM 305 C CD2 . HIS A 1 46 ? 37.487 61.291 35.257 1.00 73.53 ? 46 HIS A CD2 1 ATOM 306 C CE1 . HIS A 1 46 ? 38.064 63.244 36.080 1.00 79.14 ? 46 HIS A CE1 1 ATOM 307 N NE2 . HIS A 1 46 ? 37.813 61.985 36.399 1.00 75.28 ? 46 HIS A NE2 1 ATOM 308 N N . THR A 1 47 ? 35.320 60.794 30.453 1.00 69.52 ? 47 THR A N 1 ATOM 309 C CA . THR A 1 47 ? 35.269 60.395 29.043 1.00 70.89 ? 47 THR A CA 1 ATOM 310 C C . THR A 1 47 ? 33.859 60.061 28.544 1.00 67.75 ? 47 THR A C 1 ATOM 311 O O . THR A 1 47 ? 33.615 60.039 27.338 1.00 69.42 ? 47 THR A O 1 ATOM 312 C CB . THR A 1 47 ? 36.140 59.144 28.802 1.00 72.44 ? 47 THR A CB 1 ATOM 313 O OG1 . THR A 1 47 ? 35.620 58.040 29.556 1.00 67.90 ? 47 THR A OG1 1 ATOM 314 C CG2 . THR A 1 47 ? 37.601 59.394 29.197 1.00 76.49 ? 47 THR A CG2 1 ATOM 315 N N . TRP A 1 48 ? 32.956 59.786 29.488 1.00 63.01 ? 48 TRP A N 1 ATOM 316 C CA . TRP A 1 48 ? 31.571 59.310 29.253 1.00 60.26 ? 48 TRP A CA 1 ATOM 317 C C . TRP A 1 48 ? 31.458 57.969 28.541 1.00 60.03 ? 48 TRP A C 1 ATOM 318 O O . TRP A 1 48 ? 30.397 57.623 28.002 1.00 58.99 ? 48 TRP A O 1 ATOM 319 C CB . TRP A 1 48 ? 30.689 60.329 28.532 1.00 61.57 ? 48 TRP A CB 1 ATOM 320 C CG . TRP A 1 48 ? 30.509 61.651 29.207 1.00 61.43 ? 48 TRP A CG 1 ATOM 321 C CD1 . TRP A 1 48 ? 30.928 62.019 30.456 1.00 59.83 ? 48 TRP A CD1 1 ATOM 322 C CD2 . TRP A 1 48 ? 29.825 62.776 28.663 1.00 62.57 ? 48 TRP A CD2 1 ATOM 323 N NE1 . TRP A 1 48 ? 30.561 63.320 30.709 1.00 61.20 ? 48 TRP A NE1 1 ATOM 324 C CE2 . TRP A 1 48 ? 29.882 63.806 29.623 1.00 62.95 ? 48 TRP A CE2 1 ATOM 325 C CE3 . TRP A 1 48 ? 29.171 63.016 27.447 1.00 64.64 ? 48 TRP A CE3 1 ATOM 326 C CZ2 . TRP A 1 48 ? 29.309 65.059 29.407 1.00 64.63 ? 48 TRP A CZ2 1 ATOM 327 C CZ3 . TRP A 1 48 ? 28.607 64.262 27.228 1.00 67.02 ? 48 TRP A CZ3 1 ATOM 328 C CH2 . TRP A 1 48 ? 28.680 65.268 28.203 1.00 66.74 ? 48 TRP A CH2 1 ATOM 329 N N . ASN A 1 49 ? 32.546 57.213 28.531 1.00 61.76 ? 49 ASN A N 1 ATOM 330 C CA . ASN A 1 49 ? 32.480 55.857 28.029 1.00 61.99 ? 49 ASN A CA 1 ATOM 331 C C . ASN A 1 49 ? 32.090 54.914 29.182 1.00 57.83 ? 49 ASN A C 1 ATOM 332 O O . ASN A 1 49 ? 32.279 55.251 30.360 1.00 55.91 ? 49 ASN A O 1 ATOM 333 C CB . ASN A 1 49 ? 33.788 55.465 27.319 1.00 66.31 ? 49 ASN A CB 1 ATOM 334 C CG . ASN A 1 49 ? 34.083 56.352 26.075 1.00 72.49 ? 49 ASN A CG 1 ATOM 335 O OD1 . ASN A 1 49 ? 33.249 56.486 25.163 1.00 73.41 ? 49 ASN A OD1 1 ATOM 336 N ND2 . ASN A 1 49 ? 35.282 56.948 26.042 1.00 76.92 ? 49 ASN A ND2 1 ATOM 337 N N . LEU A 1 50 ? 31.511 53.767 28.838 1.00 56.59 ? 50 LEU A N 1 ATOM 338 C CA . LEU A 1 50 ? 31.134 52.764 29.825 1.00 53.68 ? 50 LEU A CA 1 ATOM 339 C C . LEU A 1 50 ? 32.309 51.842 30.112 1.00 54.23 ? 50 LEU A C 1 ATOM 340 O O . LEU A 1 50 ? 32.694 51.045 29.259 1.00 56.55 ? 50 LEU A O 1 ATOM 341 C CB . LEU A 1 50 ? 29.906 51.974 29.348 1.00 52.73 ? 50 LEU A CB 1 ATOM 342 C CG . LEU A 1 50 ? 28.619 52.743 29.663 1.00 51.86 ? 50 LEU A CG 1 ATOM 343 C CD1 . LEU A 1 50 ? 27.514 52.454 28.676 1.00 54.92 ? 50 LEU A CD1 1 ATOM 344 C CD2 . LEU A 1 50 ? 28.146 52.482 31.080 1.00 47.56 ? 50 LEU A CD2 1 ATOM 345 N N . ASN A 1 51 ? 32.910 52.002 31.291 1.00 52.22 ? 51 ASN A N 1 ATOM 346 C CA . ASN A 1 51 ? 33.924 51.072 31.782 1.00 52.87 ? 51 ASN A CA 1 ATOM 347 C C . ASN A 1 51 ? 33.237 49.752 32.133 1.00 50.35 ? 51 ASN A C 1 ATOM 348 O O . ASN A 1 51 ? 32.183 49.753 32.752 1.00 46.57 ? 51 ASN A O 1 ATOM 349 C CB . ASN A 1 51 ? 34.640 51.624 33.028 1.00 52.30 ? 51 ASN A CB 1 ATOM 350 C CG . ASN A 1 51 ? 35.787 52.569 32.697 1.00 57.87 ? 51 ASN A CG 1 ATOM 351 O OD1 . ASN A 1 51 ? 35.790 53.220 31.642 1.00 58.08 ? 51 ASN A OD1 1 ATOM 352 N ND2 . ASN A 1 51 ? 36.778 52.652 33.636 1.00 61.44 ? 51 ASN A ND2 1 ATOM 353 N N . ILE A 1 52 ? 33.823 48.640 31.704 1.00 52.11 ? 52 ILE A N 1 ATOM 354 C CA . ILE A 1 52 ? 33.395 47.306 32.129 1.00 51.26 ? 52 ILE A CA 1 ATOM 355 C C . ILE A 1 52 ? 34.191 46.826 33.364 1.00 51.11 ? 52 ILE A C 1 ATOM 356 O O . ILE A 1 52 ? 35.430 46.826 33.346 1.00 53.98 ? 52 ILE A O 1 ATOM 357 C CB . ILE A 1 52 ? 33.501 46.321 30.970 1.00 54.14 ? 52 ILE A CB 1 ATOM 358 C CG1 . ILE A 1 52 ? 32.267 46.465 30.086 1.00 54.05 ? 52 ILE A CG1 1 ATOM 359 C CG2 . ILE A 1 52 ? 33.570 44.909 31.482 1.00 53.35 ? 52 ILE A CG2 1 ATOM 360 C CD1 . ILE A 1 52 ? 32.600 46.691 28.647 1.00 58.42 ? 52 ILE A CD1 1 ATOM 361 N N . CYS A 1 53 ? 33.471 46.399 34.409 1.00 48.57 ? 53 CYS A N 1 ATOM 362 C CA . CYS A 1 53 ? 34.038 46.197 35.738 1.00 48.57 ? 53 CYS A CA 1 ATOM 363 C C . CYS A 1 53 ? 34.523 44.784 36.012 1.00 50.32 ? 53 CYS A C 1 ATOM 364 O O . CYS A 1 53 ? 35.267 44.560 36.971 1.00 51.15 ? 53 CYS A O 1 ATOM 365 C CB . CYS A 1 53 ? 33.015 46.542 36.812 1.00 46.30 ? 53 CYS A CB 1 ATOM 366 S SG . CYS A 1 53 ? 32.306 48.199 36.740 1.00 47.57 ? 53 CYS A SG 1 ATOM 367 N N . ARG A 1 54 ? 34.075 43.827 35.209 1.00 50.66 ? 54 ARG A N 1 ATOM 368 C CA . ARG A 1 54 ? 34.391 42.416 35.463 1.00 52.29 ? 54 ARG A CA 1 ATOM 369 C C . ARG A 1 54 ? 34.968 41.766 34.225 1.00 54.80 ? 54 ARG A C 1 ATOM 370 O O . ARG A 1 54 ? 34.518 42.079 33.129 1.00 54.27 ? 54 ARG A O 1 ATOM 371 C CB . ARG A 1 54 ? 33.142 41.650 35.936 1.00 50.18 ? 54 ARG A CB 1 ATOM 372 C CG . ARG A 1 54 ? 32.536 42.196 37.215 1.00 49.01 ? 54 ARG A CG 1 ATOM 373 C CD . ARG A 1 54 ? 33.379 41.802 38.403 1.00 53.76 ? 54 ARG A CD 1 ATOM 374 N NE . ARG A 1 54 ? 32.801 42.299 39.642 1.00 55.41 ? 54 ARG A NE 1 ATOM 375 C CZ . ARG A 1 54 ? 33.479 42.961 40.574 1.00 58.26 ? 54 ARG A CZ 1 ATOM 376 N NH1 . ARG A 1 54 ? 34.785 43.183 40.417 1.00 62.51 ? 54 ARG A NH1 1 ATOM 377 N NH2 . ARG A 1 54 ? 32.860 43.385 41.673 1.00 56.15 ? 54 ARG A NH2 1 ATOM 378 N N . PRO A 1 55 ? 35.965 40.852 34.400 1.00 57.88 ? 55 PRO A N 1 ATOM 379 C CA . PRO A 1 55 ? 36.605 40.194 33.258 1.00 61.33 ? 55 PRO A CA 1 ATOM 380 C C . PRO A 1 55 ? 35.664 39.283 32.457 1.00 61.61 ? 55 PRO A C 1 ATOM 381 O O . PRO A 1 55 ? 35.922 39.048 31.271 1.00 64.53 ? 55 PRO A O 1 ATOM 382 C CB . PRO A 1 55 ? 37.756 39.391 33.900 1.00 64.04 ? 55 PRO A CB 1 ATOM 383 C CG . PRO A 1 55 ? 37.957 40.003 35.254 1.00 62.36 ? 55 PRO A CG 1 ATOM 384 C CD . PRO A 1 55 ? 36.570 40.410 35.674 1.00 58.50 ? 55 PRO A CD 1 ATOM 385 N N . TRP A 1 56 ? 34.594 38.792 33.091 1.00 59.44 ? 56 TRP A N 1 ATOM 386 C CA . TRP A 1 56 ? 33.547 37.987 32.420 1.00 59.53 ? 56 TRP A CA 1 ATOM 387 C C . TRP A 1 56 ? 32.468 38.821 31.682 1.00 59.56 ? 56 TRP A C 1 ATOM 388 O O . TRP A 1 56 ? 31.630 38.254 30.983 1.00 61.00 ? 56 TRP A O 1 ATOM 389 C CB . TRP A 1 56 ? 32.879 37.006 33.419 1.00 56.98 ? 56 TRP A CB 1 ATOM 390 C CG . TRP A 1 56 ? 32.199 37.677 34.622 1.00 51.09 ? 56 TRP A CG 1 ATOM 391 C CD1 . TRP A 1 56 ? 32.733 37.863 35.860 1.00 48.02 ? 56 TRP A CD1 1 ATOM 392 C CD2 . TRP A 1 56 ? 30.880 38.238 34.672 1.00 47.67 ? 56 TRP A CD2 1 ATOM 393 N NE1 . TRP A 1 56 ? 31.839 38.518 36.678 1.00 45.78 ? 56 TRP A NE1 1 ATOM 394 C CE2 . TRP A 1 56 ? 30.699 38.769 35.968 1.00 43.54 ? 56 TRP A CE2 1 ATOM 395 C CE3 . TRP A 1 56 ? 29.841 38.352 33.747 1.00 46.87 ? 56 TRP A CE3 1 ATOM 396 C CZ2 . TRP A 1 56 ? 29.522 39.388 36.361 1.00 43.14 ? 56 TRP A CZ2 1 ATOM 397 C CZ3 . TRP A 1 56 ? 28.683 38.979 34.133 1.00 44.88 ? 56 TRP A CZ3 1 ATOM 398 C CH2 . TRP A 1 56 ? 28.526 39.482 35.429 1.00 43.38 ? 56 TRP A CH2 1 ATOM 399 N N . VAL A 1 57 ? 32.483 40.151 31.844 1.00 59.79 ? 57 VAL A N 1 ATOM 400 C CA . VAL A 1 57 ? 31.463 41.047 31.257 1.00 60.33 ? 57 VAL A CA 1 ATOM 401 C C . VAL A 1 57 ? 31.679 41.501 29.775 1.00 64.61 ? 57 VAL A C 1 ATOM 402 O O . VAL A 1 57 ? 30.701 41.793 29.060 1.00 64.75 ? 57 VAL A O 1 ATOM 403 C CB . VAL A 1 57 ? 31.249 42.311 32.166 1.00 57.63 ? 57 VAL A CB 1 ATOM 404 C CG1 . VAL A 1 57 ? 30.508 43.428 31.433 1.00 56.92 ? 57 VAL A CG1 1 ATOM 405 C CG2 . VAL A 1 57 ? 30.493 41.964 33.440 1.00 55.53 ? 57 VAL A CG2 1 ATOM 406 N N . GLN A 1 58 ? 32.938 41.533 29.320 1.00 68.75 ? 58 GLN A N 1 ATOM 407 C CA . GLN A 1 58 ? 33.348 42.306 28.124 1.00 72.97 ? 58 GLN A CA 1 ATOM 408 C C . GLN A 1 58 ? 32.857 41.796 26.757 1.00 76.76 ? 58 GLN A C 1 ATOM 409 O O . GLN A 1 58 ? 32.059 42.468 26.087 1.00 76.57 ? 58 GLN A O 1 ATOM 410 C CB . GLN A 1 58 ? 34.884 42.471 28.103 1.00 75.83 ? 58 GLN A CB 1 ATOM 411 C CG . GLN A 1 58 ? 35.396 43.750 27.437 1.00 78.17 ? 58 GLN A CG 1 ATOM 412 C CD . GLN A 1 58 ? 35.414 43.668 25.921 1.00 83.10 ? 58 GLN A CD 1 ATOM 413 O OE1 . GLN A 1 58 ? 36.110 42.832 25.328 1.00 86.13 ? 58 GLN A OE1 1 ATOM 414 N NE2 . GLN A 1 58 ? 34.650 44.546 25.282 1.00 83.75 ? 58 GLN A NE2 1 ATOM 415 N N . GLU A 1 59 ? 33.365 40.629 26.347 1.00 80.84 ? 59 GLU A N 1 ATOM 416 C CA . GLU A 1 59 ? 33.121 40.073 25.008 1.00 85.72 ? 59 GLU A CA 1 ATOM 417 C C . GLU A 1 59 ? 31.771 39.352 24.910 1.00 85.62 ? 59 GLU A C 1 ATOM 418 O O . GLU A 1 59 ? 31.633 38.353 24.194 1.00 88.78 ? 59 GLU A O 1 ATOM 419 C CB . GLU A 1 59 ? 34.263 39.123 24.606 1.00 89.86 ? 59 GLU A CB 1 ATOM 420 N N . ILE A 1 60 ? 30.782 39.861 25.642 1.00 82.82 ? 60 ILE A N 1 ATOM 421 C CA . ILE A 1 60 ? 29.452 39.262 25.659 1.00 83.04 ? 60 ILE A CA 1 ATOM 422 C C . ILE A 1 60 ? 28.438 40.245 25.068 1.00 82.88 ? 60 ILE A C 1 ATOM 423 O O . ILE A 1 60 ? 27.797 39.934 24.061 1.00 86.00 ? 60 ILE A O 1 ATOM 424 C CB . ILE A 1 60 ? 29.064 38.732 27.069 1.00 80.34 ? 60 ILE A CB 1 ATOM 425 C CG1 . ILE A 1 60 ? 30.075 37.668 27.532 1.00 81.67 ? 60 ILE A CG1 1 ATOM 426 C CG2 . ILE A 1 60 ? 27.658 38.111 27.063 1.00 80.75 ? 60 ILE A CG2 1 ATOM 427 C CD1 . ILE A 1 60 ? 31.431 38.210 27.991 1.00 80.72 ? 60 ILE A CD1 1 ATOM 428 N N . THR A 1 61 ? 28.315 41.434 25.653 1.00 79.84 ? 61 THR A N 1 ATOM 429 C CA . THR A 1 61 ? 27.569 42.497 24.983 1.00 80.34 ? 61 THR A CA 1 ATOM 430 C C . THR A 1 61 ? 28.259 43.861 25.099 1.00 79.40 ? 61 THR A C 1 ATOM 431 O O . THR A 1 61 ? 28.218 44.464 26.185 1.00 76.15 ? 61 THR A O 1 ATOM 432 C CB . THR A 1 61 ? 26.101 42.566 25.463 1.00 78.55 ? 61 THR A CB 1 ATOM 433 O OG1 . THR A 1 61 ? 25.376 41.443 24.943 1.00 80.90 ? 61 THR A OG1 1 ATOM 434 C CG2 . THR A 1 61 ? 25.434 43.844 24.984 1.00 78.39 ? 61 THR A CG2 1 ATOM 435 N N . ALA A 1 62 ? 28.905 44.370 24.035 1.00 82.34 ? 62 ALA A N 1 ATOM 436 C CA . ALA A 1 62 ? 29.193 43.728 22.713 1.00 87.14 ? 62 ALA A CA 1 ATOM 437 C C . ALA A 1 62 ? 28.030 43.365 21.773 1.00 89.40 ? 62 ALA A C 1 ATOM 438 O O . ALA A 1 62 ? 27.568 44.198 20.994 1.00 91.16 ? 62 ALA A O 1 ATOM 439 C CB . ALA A 1 62 ? 30.217 42.556 22.833 1.00 88.79 ? 62 ALA A CB 1 ATOM 440 N N . GLU A 1 63 ? 27.589 42.108 21.861 1.00 89.60 ? 63 GLU A N 1 ATOM 441 C CA . GLU A 1 63 ? 26.676 41.468 20.909 1.00 92.90 ? 63 GLU A CA 1 ATOM 442 C C . GLU A 1 63 ? 25.263 42.055 20.862 1.00 91.92 ? 63 GLU A C 1 ATOM 443 O O . GLU A 1 63 ? 24.650 42.129 19.790 1.00 95.57 ? 63 GLU A O 1 ATOM 444 C CB . GLU A 1 63 ? 26.601 39.973 21.222 1.00 93.47 ? 63 GLU A CB 1 ATOM 445 C CG . GLU A 1 63 ? 26.166 39.102 20.074 1.00 99.12 ? 63 GLU A CG 1 ATOM 446 C CD . GLU A 1 63 ? 26.780 37.722 20.154 1.00 101.99 ? 63 GLU A CD 1 ATOM 447 O OE1 . GLU A 1 63 ? 27.141 37.300 21.276 1.00 99.50 ? 63 GLU A OE1 1 ATOM 448 O OE2 . GLU A 1 63 ? 26.910 37.063 19.097 1.00 106.91 ? 63 GLU A OE2 1 ATOM 449 N N . THR A 1 64 ? 24.740 42.440 22.023 1.00 87.12 ? 64 THR A N 1 ATOM 450 C CA . THR A 1 64 ? 23.408 43.037 22.104 1.00 86.30 ? 64 THR A CA 1 ATOM 451 C C . THR A 1 64 ? 23.485 44.563 22.008 1.00 84.83 ? 64 THR A C 1 ATOM 452 O O . THR A 1 64 ? 22.455 45.242 21.956 1.00 85.03 ? 64 THR A O 1 ATOM 453 C CB . THR A 1 64 ? 22.686 42.596 23.393 1.00 83.21 ? 64 THR A CB 1 ATOM 454 N N . GLU A 1 65 ? 24.714 45.082 21.970 1.00 83.79 ? 65 GLU A N 1 ATOM 455 C CA . GLU A 1 65 ? 25.004 46.528 21.938 1.00 82.31 ? 65 GLU A CA 1 ATOM 456 C C . GLU A 1 65 ? 24.202 47.344 22.956 1.00 77.88 ? 65 GLU A C 1 ATOM 457 O O . GLU A 1 65 ? 23.689 48.423 22.646 1.00 78.63 ? 65 GLU A O 1 ATOM 458 C CB . GLU A 1 65 ? 24.840 47.089 20.505 1.00 87.25 ? 65 GLU A CB 1 ATOM 459 N N . VAL A 1 66 ? 24.094 46.813 24.173 1.00 73.43 ? 66 VAL A N 1 ATOM 460 C CA . VAL A 1 66 ? 23.529 47.545 25.301 1.00 68.79 ? 66 VAL A CA 1 ATOM 461 C C . VAL A 1 66 ? 24.370 48.813 25.546 1.00 67.13 ? 66 VAL A C 1 ATOM 462 O O . VAL A 1 66 ? 23.851 49.870 25.911 1.00 65.00 ? 66 VAL A O 1 ATOM 463 C CB . VAL A 1 66 ? 23.468 46.666 26.566 1.00 65.84 ? 66 VAL A CB 1 ATOM 464 C CG1 . VAL A 1 66 ? 23.154 47.507 27.820 1.00 62.23 ? 66 VAL A CG1 1 ATOM 465 C CG2 . VAL A 1 66 ? 22.432 45.569 26.395 1.00 66.93 ? 66 VAL A CG2 1 ATOM 466 N N . LYS A 1 67 ? 25.669 48.686 25.295 1.00 67.49 ? 67 LYS A N 1 ATOM 467 C CA . LYS A 1 67 ? 26.631 49.763 25.450 1.00 66.80 ? 67 LYS A CA 1 ATOM 468 C C . LYS A 1 67 ? 26.384 50.857 24.411 1.00 68.64 ? 67 LYS A C 1 ATOM 469 O O . LYS A 1 67 ? 26.657 52.023 24.670 1.00 68.22 ? 67 LYS A O 1 ATOM 470 C CB . LYS A 1 67 ? 28.046 49.184 25.353 1.00 68.17 ? 67 LYS A CB 1 ATOM 471 C CG . LYS A 1 67 ? 29.160 50.078 25.865 1.00 68.70 ? 67 LYS A CG 1 ATOM 472 C CD . LYS A 1 67 ? 30.482 49.316 25.924 1.00 70.35 ? 67 LYS A CD 1 ATOM 473 C CE . LYS A 1 67 ? 31.640 50.248 26.279 1.00 73.38 ? 67 LYS A CE 1 ATOM 474 N NZ . LYS A 1 67 ? 32.849 49.503 26.750 1.00 74.89 ? 67 LYS A NZ 1 ATOM 475 N N . LYS A 1 68 ? 25.851 50.482 23.244 1.00 71.09 ? 68 LYS A N 1 ATOM 476 C CA . LYS A 1 68 ? 25.455 51.460 22.219 1.00 73.45 ? 68 LYS A CA 1 ATOM 477 C C . LYS A 1 68 ? 24.123 52.150 22.559 1.00 71.60 ? 68 LYS A C 1 ATOM 478 O O . LYS A 1 68 ? 23.975 53.358 22.348 1.00 72.48 ? 68 LYS A O 1 ATOM 479 C CB . LYS A 1 68 ? 25.399 50.811 20.829 1.00 78.40 ? 68 LYS A CB 1 ATOM 480 N N . ILE A 1 69 ? 23.174 51.371 23.091 1.00 68.91 ? 69 ILE A N 1 ATOM 481 C CA . ILE A 1 69 ? 21.865 51.853 23.554 1.00 67.29 ? 69 ILE A CA 1 ATOM 482 C C . ILE A 1 69 ? 22.013 52.943 24.615 1.00 63.96 ? 69 ILE A C 1 ATOM 483 O O . ILE A 1 69 ? 21.329 53.978 24.577 1.00 64.63 ? 69 ILE A O 1 ATOM 484 C CB . ILE A 1 69 ? 21.029 50.681 24.161 1.00 65.93 ? 69 ILE A CB 1 ATOM 485 C CG1 . ILE A 1 69 ? 20.398 49.826 23.061 1.00 70.56 ? 69 ILE A CG1 1 ATOM 486 C CG2 . ILE A 1 69 ? 19.960 51.191 25.156 1.00 63.46 ? 69 ILE A CG2 1 ATOM 487 C CD1 . ILE A 1 69 ? 19.874 48.476 23.545 1.00 69.74 ? 69 ILE A CD1 1 ATOM 488 N N . LEU A 1 70 ? 22.906 52.692 25.569 1.00 60.33 ? 70 LEU A N 1 ATOM 489 C CA . LEU A 1 70 ? 23.073 53.541 26.728 1.00 57.07 ? 70 LEU A CA 1 ATOM 490 C C . LEU A 1 70 ? 23.782 54.858 26.412 1.00 58.36 ? 70 LEU A C 1 ATOM 491 O O . LEU A 1 70 ? 23.591 55.858 27.116 1.00 56.62 ? 70 LEU A O 1 ATOM 492 C CB . LEU A 1 70 ? 23.813 52.770 27.828 1.00 53.76 ? 70 LEU A CB 1 ATOM 493 C CG . LEU A 1 70 ? 23.098 51.530 28.411 1.00 53.00 ? 70 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 70 ? 23.948 50.777 29.452 1.00 49.00 ? 70 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 70 ? 21.742 51.890 28.991 1.00 50.96 ? 70 LEU A CD2 1 ATOM 496 N N . SER A 1 71 ? 24.570 54.856 25.341 1.00 61.41 ? 71 SER A N 1 ATOM 497 C CA . SER A 1 71 ? 25.442 55.978 24.999 1.00 63.65 ? 71 SER A CA 1 ATOM 498 C C . SER A 1 71 ? 24.978 56.812 23.805 1.00 67.96 ? 71 SER A C 1 ATOM 499 O O . SER A 1 71 ? 24.849 58.028 23.909 1.00 68.76 ? 71 SER A O 1 ATOM 500 C CB . SER A 1 71 ? 26.847 55.452 24.730 1.00 64.58 ? 71 SER A CB 1 ATOM 501 O OG . SER A 1 71 ? 27.100 54.318 25.544 1.00 61.95 ? 71 SER A OG 1 ATOM 502 N N . PHE A 1 72 ? 24.726 56.167 22.672 1.00 71.69 ? 72 PHE A N 1 ATOM 503 C CA . PHE A 1 72 ? 24.554 56.908 21.422 1.00 77.07 ? 72 PHE A CA 1 ATOM 504 C C . PHE A 1 72 ? 23.111 56.995 20.944 1.00 78.88 ? 72 PHE A C 1 ATOM 505 O O . PHE A 1 72 ? 22.815 57.766 20.029 1.00 83.46 ? 72 PHE A O 1 ATOM 506 C CB . PHE A 1 72 ? 25.426 56.330 20.295 1.00 81.11 ? 72 PHE A CB 1 ATOM 507 C CG . PHE A 1 72 ? 26.772 55.816 20.746 1.00 80.61 ? 72 PHE A CG 1 ATOM 508 C CD1 . PHE A 1 72 ? 27.721 56.675 21.300 1.00 79.43 ? 72 PHE A CD1 1 ATOM 509 C CD2 . PHE A 1 72 ? 27.101 54.459 20.583 1.00 82.06 ? 72 PHE A CD2 1 ATOM 510 C CE1 . PHE A 1 72 ? 28.965 56.189 21.717 1.00 79.15 ? 72 PHE A CE1 1 ATOM 511 C CE2 . PHE A 1 72 ? 28.345 53.961 20.986 1.00 80.69 ? 72 PHE A CE2 1 ATOM 512 C CZ . PHE A 1 72 ? 29.278 54.828 21.555 1.00 79.83 ? 72 PHE A CZ 1 ATOM 513 N N . SER A 1 73 ? 22.216 56.217 21.557 1.00 76.24 ? 73 SER A N 1 ATOM 514 C CA . SER A 1 73 ? 20.856 56.067 21.031 1.00 77.85 ? 73 SER A CA 1 ATOM 515 C C . SER A 1 73 ? 19.913 57.185 21.472 1.00 77.43 ? 73 SER A C 1 ATOM 516 O O . SER A 1 73 ? 20.286 58.073 22.246 1.00 74.68 ? 73 SER A O 1 ATOM 517 C CB . SER A 1 73 ? 20.271 54.695 21.391 1.00 76.39 ? 73 SER A CB 1 ATOM 518 O OG . SER A 1 73 ? 19.864 54.638 22.753 1.00 71.24 ? 73 SER A OG 1 ATOM 519 N N . MET A 1 74 ? 18.693 57.117 20.952 1.00 79.95 ? 74 MET A N 1 ATOM 520 C CA . MET A 1 74 ? 17.602 58.029 21.267 1.00 80.95 ? 74 MET A CA 1 ATOM 521 C C . MET A 1 74 ? 17.411 58.310 22.761 1.00 76.09 ? 74 MET A C 1 ATOM 522 O O . MET A 1 74 ? 17.054 59.421 23.145 1.00 76.49 ? 74 MET A O 1 ATOM 523 C CB . MET A 1 74 ? 16.323 57.433 20.706 1.00 84.41 ? 74 MET A CB 1 ATOM 524 C CG . MET A 1 74 ? 15.084 58.246 20.937 1.00 86.53 ? 74 MET A CG 1 ATOM 525 S SD . MET A 1 74 ? 13.729 57.447 20.061 1.00 92.19 ? 74 MET A SD 1 ATOM 526 C CE . MET A 1 74 ? 13.954 58.050 18.367 1.00 97.59 ? 74 MET A CE 1 ATOM 527 N N . VAL A 1 75 ? 17.614 57.289 23.590 1.00 72.02 ? 75 VAL A N 1 ATOM 528 C CA . VAL A 1 75 ? 17.457 57.420 25.038 1.00 67.21 ? 75 VAL A CA 1 ATOM 529 C C . VAL A 1 75 ? 18.822 57.357 25.735 1.00 63.10 ? 75 VAL A C 1 ATOM 530 O O . VAL A 1 75 ? 18.896 57.254 26.952 1.00 60.39 ? 75 VAL A O 1 ATOM 531 C CB . VAL A 1 75 ? 16.486 56.352 25.614 1.00 66.39 ? 75 VAL A CB 1 ATOM 532 C CG1 . VAL A 1 75 ? 15.140 56.405 24.895 1.00 70.07 ? 75 VAL A CG1 1 ATOM 533 C CG2 . VAL A 1 75 ? 17.083 54.954 25.513 1.00 65.52 ? 75 VAL A CG2 1 ATOM 534 N N . GLY A 1 76 ? 19.889 57.454 24.943 1.00 63.86 ? 76 GLY A N 1 ATOM 535 C CA . GLY A 1 76 ? 21.262 57.365 25.424 1.00 61.08 ? 76 GLY A CA 1 ATOM 536 C C . GLY A 1 76 ? 21.676 58.618 26.167 1.00 59.70 ? 76 GLY A C 1 ATOM 537 O O . GLY A 1 76 ? 20.953 59.613 26.158 1.00 60.70 ? 76 GLY A O 1 ATOM 538 N N . ILE A 1 77 ? 22.842 58.565 26.809 1.00 57.64 ? 77 ILE A N 1 ATOM 539 C CA . ILE A 1 77 ? 23.277 59.629 27.726 1.00 56.20 ? 77 ILE A CA 1 ATOM 540 C C . ILE A 1 77 ? 23.483 60.959 27.000 1.00 59.82 ? 77 ILE A C 1 ATOM 541 O O . ILE A 1 77 ? 23.037 62.010 27.466 1.00 60.05 ? 77 ILE A O 1 ATOM 542 C CB . ILE A 1 77 ? 24.502 59.168 28.601 1.00 54.29 ? 77 ILE A CB 1 ATOM 543 C CG1 . ILE A 1 77 ? 24.687 60.062 29.839 1.00 51.65 ? 77 ILE A CG1 1 ATOM 544 C CG2 . ILE A 1 77 ? 25.788 58.995 27.753 1.00 56.16 ? 77 ILE A CG2 1 ATOM 545 C CD1 . ILE A 1 77 ? 23.410 60.351 30.616 1.00 48.72 ? 77 ILE A CD1 1 ATOM 546 N N . ARG A 1 78 ? 24.080 60.897 25.817 1.00 63.10 ? 78 ARG A N 1 ATOM 547 C CA . ARG A 1 78 ? 24.315 62.082 25.005 1.00 67.45 ? 78 ARG A CA 1 ATOM 548 C C . ARG A 1 78 ? 23.024 62.859 24.662 1.00 69.13 ? 78 ARG A C 1 ATOM 549 O O . ARG A 1 78 ? 23.001 64.097 24.731 1.00 71.30 ? 78 ARG A O 1 ATOM 550 C CB . ARG A 1 78 ? 25.136 61.705 23.754 1.00 71.46 ? 78 ARG A CB 1 ATOM 551 C CG . ARG A 1 78 ? 26.618 61.511 24.092 1.00 73.34 ? 78 ARG A CG 1 ATOM 552 C CD . ARG A 1 78 ? 27.325 60.526 23.174 1.00 81.64 ? 78 ARG A CD 1 ATOM 553 N NE . ARG A 1 78 ? 28.728 60.336 23.564 1.00 85.33 ? 78 ARG A NE 1 ATOM 554 C CZ . ARG A 1 78 ? 29.164 59.460 24.476 1.00 83.63 ? 78 ARG A CZ 1 ATOM 555 N NH1 . ARG A 1 78 ? 28.322 58.649 25.118 1.00 79.81 ? 78 ARG A NH1 1 ATOM 556 N NH2 . ARG A 1 78 ? 30.464 59.384 24.742 1.00 85.94 ? 78 ARG A NH2 1 ATOM 557 N N . ASN A 1 79 ? 21.954 62.144 24.311 1.00 68.73 ? 79 ASN A N 1 ATOM 558 C CA . ASN A 1 79 ? 20.644 62.779 24.122 1.00 69.83 ? 79 ASN A CA 1 ATOM 559 C C . ASN A 1 79 ? 20.002 63.183 25.438 1.00 66.48 ? 79 ASN A C 1 ATOM 560 O O . ASN A 1 79 ? 19.456 64.279 25.546 1.00 67.93 ? 79 ASN A O 1 ATOM 561 C CB . ASN A 1 79 ? 19.691 61.889 23.325 1.00 71.71 ? 79 ASN A CB 1 ATOM 562 C CG . ASN A 1 79 ? 19.830 62.071 21.808 1.00 76.84 ? 79 ASN A CG 1 ATOM 563 O OD1 . ASN A 1 79 ? 19.974 63.187 21.301 1.00 79.33 ? 79 ASN A OD1 1 ATOM 564 N ND2 . ASN A 1 79 ? 19.765 60.965 21.083 1.00 77.96 ? 79 ASN A ND2 1 ATOM 565 N N . THR A 1 80 ? 20.069 62.300 26.436 1.00 62.41 ? 80 THR A N 1 ATOM 566 C CA . THR A 1 80 ? 19.533 62.596 27.785 1.00 59.68 ? 80 THR A CA 1 ATOM 567 C C . THR A 1 80 ? 20.096 63.884 28.423 1.00 59.32 ? 80 THR A C 1 ATOM 568 O O . THR A 1 80 ? 19.342 64.684 28.963 1.00 59.10 ? 80 THR A O 1 ATOM 569 C CB . THR A 1 80 ? 19.727 61.409 28.767 1.00 55.90 ? 80 THR A CB 1 ATOM 570 O OG1 . THR A 1 80 ? 19.247 60.208 28.161 1.00 56.98 ? 80 THR A OG1 1 ATOM 571 C CG2 . THR A 1 80 ? 18.959 61.654 30.054 1.00 54.56 ? 80 THR A CG2 1 ATOM 572 N N . ILE A 1 81 ? 21.416 64.059 28.373 1.00 59.59 ? 81 ILE A N 1 ATOM 573 C CA . ILE A 1 81 ? 22.060 65.281 28.848 1.00 60.92 ? 81 ILE A CA 1 ATOM 574 C C . ILE A 1 81 ? 21.449 66.507 28.174 1.00 64.80 ? 81 ILE A C 1 ATOM 575 O O . ILE A 1 81 ? 21.057 67.447 28.850 1.00 65.47 ? 81 ILE A O 1 ATOM 576 C CB . ILE A 1 81 ? 23.579 65.257 28.594 1.00 61.86 ? 81 ILE A CB 1 ATOM 577 C CG1 . ILE A 1 81 ? 24.255 64.257 29.513 1.00 58.07 ? 81 ILE A CG1 1 ATOM 578 C CG2 . ILE A 1 81 ? 24.202 66.669 28.754 1.00 64.95 ? 81 ILE A CG2 1 ATOM 579 C CD1 . ILE A 1 81 ? 25.465 63.658 28.890 1.00 60.61 ? 81 ILE A CD1 1 ATOM 580 N N . ARG A 1 82 ? 21.352 66.492 26.847 1.00 67.81 ? 82 ARG A N 1 ATOM 581 C CA . ARG A 1 82 ? 20.753 67.605 26.127 1.00 72.05 ? 82 ARG A CA 1 ATOM 582 C C . ARG A 1 82 ? 19.257 67.754 26.411 1.00 71.75 ? 82 ARG A C 1 ATOM 583 O O . ARG A 1 82 ? 18.766 68.865 26.519 1.00 73.87 ? 82 ARG A O 1 ATOM 584 C CB . ARG A 1 82 ? 21.024 67.512 24.623 1.00 76.01 ? 82 ARG A CB 1 ATOM 585 C CG . ARG A 1 82 ? 20.700 68.803 23.873 1.00 82.64 ? 82 ARG A CG 1 ATOM 586 C CD . ARG A 1 82 ? 21.396 68.894 22.507 1.00 88.03 ? 82 ARG A CD 1 ATOM 587 N NE . ARG A 1 82 ? 21.415 67.594 21.840 1.00 89.52 ? 82 ARG A NE 1 ATOM 588 C CZ . ARG A 1 82 ? 20.399 67.106 21.133 1.00 92.43 ? 82 ARG A CZ 1 ATOM 589 N NH1 . ARG A 1 82 ? 19.277 67.821 20.996 1.00 94.33 ? 82 ARG A NH1 1 ATOM 590 N NH2 . ARG A 1 82 ? 20.508 65.905 20.564 1.00 92.43 ? 82 ARG A NH2 1 ATOM 591 N N . PHE A 1 83 ? 18.541 66.647 26.559 1.00 69.81 ? 83 PHE A N 1 ATOM 592 C CA . PHE A 1 83 ? 17.142 66.708 26.968 1.00 69.90 ? 83 PHE A CA 1 ATOM 593 C C . PHE A 1 83 ? 16.973 67.350 28.350 1.00 68.13 ? 83 PHE A C 1 ATOM 594 O O . PHE A 1 83 ? 16.002 68.074 28.576 1.00 69.76 ? 83 PHE A O 1 ATOM 595 C CB . PHE A 1 83 ? 16.518 65.316 26.986 1.00 68.45 ? 83 PHE A CB 1 ATOM 596 C CG . PHE A 1 83 ? 15.053 65.319 27.326 1.00 69.59 ? 83 PHE A CG 1 ATOM 597 C CD1 . PHE A 1 83 ? 14.111 65.787 26.407 1.00 74.19 ? 83 PHE A CD1 1 ATOM 598 C CD2 . PHE A 1 83 ? 14.614 64.862 28.569 1.00 66.73 ? 83 PHE A CD2 1 ATOM 599 C CE1 . PHE A 1 83 ? 12.755 65.794 26.720 1.00 76.37 ? 83 PHE A CE1 1 ATOM 600 C CE2 . PHE A 1 83 ? 13.259 64.872 28.895 1.00 67.85 ? 83 PHE A CE2 1 ATOM 601 C CZ . PHE A 1 83 ? 12.330 65.334 27.972 1.00 72.97 ? 83 PHE A CZ 1 ATOM 602 N N . MET A 1 84 ? 17.903 67.079 29.269 1.00 64.64 ? 84 MET A N 1 ATOM 603 C CA . MET A 1 84 ? 17.817 67.663 30.620 1.00 63.55 ? 84 MET A CA 1 ATOM 604 C C . MET A 1 84 ? 18.169 69.153 30.640 1.00 66.00 ? 84 MET A C 1 ATOM 605 O O . MET A 1 84 ? 17.464 69.940 31.273 1.00 67.40 ? 84 MET A O 1 ATOM 606 C CB . MET A 1 84 ? 18.640 66.875 31.628 1.00 59.48 ? 84 MET A CB 1 ATOM 607 C CG . MET A 1 84 ? 18.165 65.416 31.874 1.00 58.60 ? 84 MET A CG 1 ATOM 608 S SD . MET A 1 84 ? 16.397 65.205 32.226 1.00 59.91 ? 84 MET A SD 1 ATOM 609 C CE . MET A 1 84 ? 16.288 63.416 32.272 1.00 57.86 ? 84 MET A CE 1 ATOM 610 N N . HIS A 1 85 ? 19.230 69.544 29.932 1.00 67.80 ? 85 HIS A N 1 ATOM 611 C CA . HIS A 1 85 ? 19.542 70.972 29.724 1.00 71.10 ? 85 HIS A CA 1 ATOM 612 C C . HIS A 1 85 ? 18.377 71.733 29.098 1.00 75.38 ? 85 HIS A C 1 ATOM 613 O O . HIS A 1 85 ? 18.143 72.888 29.438 1.00 77.37 ? 85 HIS A O 1 ATOM 614 C CB . HIS A 1 85 ? 20.797 71.164 28.862 1.00 72.86 ? 85 HIS A CB 1 ATOM 615 C CG . HIS A 1 85 ? 22.084 71.093 29.626 1.00 70.33 ? 85 HIS A CG 1 ATOM 616 N ND1 . HIS A 1 85 ? 22.569 72.147 30.371 1.00 70.74 ? 85 HIS A ND1 1 ATOM 617 C CD2 . HIS A 1 85 ? 22.991 70.096 29.754 1.00 67.03 ? 85 HIS A CD2 1 ATOM 618 C CE1 . HIS A 1 85 ? 23.717 71.802 30.928 1.00 68.25 ? 85 HIS A CE1 1 ATOM 619 N NE2 . HIS A 1 85 ? 23.995 70.561 30.568 1.00 67.59 ? 85 HIS A NE2 1 ATOM 620 N N . GLU A 1 86 ? 17.658 71.081 28.186 1.00 77.28 ? 86 GLU A N 1 ATOM 621 C CA . GLU A 1 86 ? 16.527 71.684 27.480 1.00 82.13 ? 86 GLU A CA 1 ATOM 622 C C . GLU A 1 86 ? 15.299 71.921 28.355 1.00 81.95 ? 86 GLU A C 1 ATOM 623 O O . GLU A 1 86 ? 14.609 72.929 28.199 1.00 85.33 ? 86 GLU A O 1 ATOM 624 C CB . GLU A 1 86 ? 16.096 70.816 26.294 1.00 84.26 ? 86 GLU A CB 1 ATOM 625 C CG . GLU A 1 86 ? 17.192 70.393 25.319 1.00 87.18 ? 86 GLU A CG 1 ATOM 626 C CD . GLU A 1 86 ? 18.122 71.521 24.907 1.00 92.49 ? 86 GLU A CD 1 ATOM 627 O OE1 . GLU A 1 86 ? 17.686 72.404 24.129 1.00 98.30 ? 86 GLU A OE1 1 ATOM 628 O OE2 . GLU A 1 86 ? 19.297 71.502 25.350 1.00 90.65 ? 86 GLU A OE2 1 ATOM 629 N N . MET A 1 87 ? 15.004 70.971 29.236 1.00 78.40 ? 87 MET A N 1 ATOM 630 C CA . MET A 1 87 ? 13.829 71.062 30.108 1.00 79.06 ? 87 MET A CA 1 ATOM 631 C C . MET A 1 87 ? 14.030 72.105 31.210 1.00 78.85 ? 87 MET A C 1 ATOM 632 O O . MET A 1 87 ? 13.082 72.778 31.624 1.00 80.95 ? 87 MET A O 1 ATOM 633 C CB . MET A 1 87 ? 13.490 69.692 30.717 1.00 75.87 ? 87 MET A CB 1 ATOM 634 C CG . MET A 1 87 ? 13.065 68.615 29.707 1.00 77.80 ? 87 MET A CG 1 ATOM 635 S SD . MET A 1 87 ? 11.513 68.925 28.825 1.00 86.25 ? 87 MET A SD 1 ATOM 636 C CE . MET A 1 87 ? 12.070 69.744 27.326 1.00 88.93 ? 87 MET A CE 1 ATOM 637 N N . THR A 1 88 ? 15.273 72.215 31.682 1.00 76.69 ? 88 THR A N 1 ATOM 638 C CA . THR A 1 88 ? 15.679 73.270 32.601 1.00 77.02 ? 88 THR A CA 1 ATOM 639 C C . THR A 1 88 ? 15.439 74.617 31.937 1.00 81.64 ? 88 THR A C 1 ATOM 640 O O . THR A 1 88 ? 14.849 75.510 32.527 1.00 83.99 ? 88 THR A O 1 ATOM 641 C CB . THR A 1 88 ? 17.166 73.126 33.000 1.00 74.67 ? 88 THR A CB 1 ATOM 642 O OG1 . THR A 1 88 ? 17.411 71.793 33.453 1.00 70.85 ? 88 THR A OG1 1 ATOM 643 C CG2 . THR A 1 88 ? 17.519 74.072 34.122 1.00 74.85 ? 88 THR A CG2 1 ATOM 644 N N . ALA A 1 89 ? 15.873 74.730 30.686 1.00 83.91 ? 89 ALA A N 1 ATOM 645 C CA . ALA A 1 89 ? 15.683 75.918 29.868 1.00 88.44 ? 89 ALA A CA 1 ATOM 646 C C . ALA A 1 89 ? 14.207 76.233 29.584 1.00 91.76 ? 89 ALA A C 1 ATOM 647 O O . ALA A 1 89 ? 13.761 77.376 29.767 1.00 95.15 ? 89 ALA A O 1 ATOM 648 C CB . ALA A 1 89 ? 16.465 75.772 28.558 1.00 90.26 ? 89 ALA A CB 1 ATOM 649 N N . LYS A 1 90 ? 13.456 75.225 29.137 1.00 90.85 ? 90 LYS A N 1 ATOM 650 C CA . LYS A 1 90 ? 12.046 75.402 28.769 1.00 94.25 ? 90 LYS A CA 1 ATOM 651 C C . LYS A 1 90 ? 11.116 75.483 29.987 1.00 93.16 ? 90 LYS A C 1 ATOM 652 O O . LYS A 1 90 ? 9.893 75.512 29.855 1.00 96.26 ? 90 LYS A O 1 ATOM 653 C CB . LYS A 1 90 ? 11.591 74.301 27.799 1.00 94.74 ? 90 LYS A CB 1 ATOM 654 N N . ALA A 1 91 ? 11.711 75.522 31.171 1.00 89.45 ? 91 ALA A N 1 ATOM 655 C CA . ALA A 1 91 ? 10.964 75.658 32.415 1.00 88.71 ? 91 ALA A CA 1 ATOM 656 C C . ALA A 1 91 ? 11.385 76.935 33.130 1.00 89.69 ? 91 ALA A C 1 ATOM 657 O O . ALA A 1 91 ? 10.811 77.296 34.174 1.00 90.29 ? 91 ALA A O 1 ATOM 658 C CB . ALA A 1 91 ? 11.179 74.446 33.301 1.00 83.66 ? 91 ALA A CB 1 ATOM 659 N N . GLY A 1 92 ? 12.388 77.608 32.545 1.00 90.59 ? 92 GLY A N 1 ATOM 660 C CA . GLY A 1 92 ? 12.879 78.897 33.033 1.00 92.45 ? 92 GLY A CA 1 ATOM 661 C C . GLY A 1 92 ? 13.680 78.758 34.311 1.00 88.87 ? 92 GLY A C 1 ATOM 662 O O . GLY A 1 92 ? 13.901 79.746 35.024 1.00 90.54 ? 92 GLY A O 1 ATOM 663 N N . LEU A 1 93 ? 14.107 77.527 34.596 1.00 84.10 ? 93 LEU A N 1 ATOM 664 C CA . LEU A 1 93 ? 14.802 77.190 35.842 1.00 81.01 ? 93 LEU A CA 1 ATOM 665 C C . LEU A 1 93 ? 16.284 77.537 35.756 1.00 80.52 ? 93 LEU A C 1 ATOM 666 O O . LEU A 1 93 ? 16.847 77.642 34.669 1.00 82.40 ? 93 LEU A O 1 ATOM 667 C CB . LEU A 1 93 ? 14.622 75.704 36.199 1.00 76.72 ? 93 LEU A CB 1 ATOM 668 C CG . LEU A 1 93 ? 13.198 75.166 36.408 1.00 78.06 ? 93 LEU A CG 1 ATOM 669 C CD1 . LEU A 1 93 ? 13.225 73.705 36.802 1.00 75.62 ? 93 LEU A CD1 1 ATOM 670 C CD2 . LEU A 1 93 ? 12.398 75.974 37.434 1.00 82.16 ? 93 LEU A CD2 1 ATOM 671 N N . ASP A 1 94 ? 16.911 77.711 36.910 1.00 78.95 ? 94 ASP A N 1 ATOM 672 C CA . ASP A 1 94 ? 18.307 78.133 36.975 1.00 78.58 ? 94 ASP A CA 1 ATOM 673 C C . ASP A 1 94 ? 19.226 77.008 37.463 1.00 73.22 ? 94 ASP A C 1 ATOM 674 O O . ASP A 1 94 ? 18.824 76.213 38.302 1.00 70.80 ? 94 ASP A O 1 ATOM 675 C CB . ASP A 1 94 ? 18.430 79.347 37.894 1.00 81.46 ? 94 ASP A CB 1 ATOM 676 C CG . ASP A 1 94 ? 17.670 79.168 39.209 1.00 81.32 ? 94 ASP A CG 1 ATOM 677 O OD1 . ASP A 1 94 ? 18.179 78.479 40.114 1.00 79.92 ? 94 ASP A OD1 1 ATOM 678 O OD2 . ASP A 1 94 ? 16.562 79.731 39.343 1.00 84.92 ? 94 ASP A OD2 1 ATOM 679 N N . TYR A 1 95 ? 20.456 76.979 36.945 1.00 72.00 ? 95 TYR A N 1 ATOM 680 C CA . TYR A 1 95 ? 21.540 76.096 37.415 1.00 68.24 ? 95 TYR A CA 1 ATOM 681 C C . TYR A 1 95 ? 22.043 76.463 38.840 1.00 67.56 ? 95 TYR A C 1 ATOM 682 O O . TYR A 1 95 ? 21.924 77.615 39.246 1.00 71.12 ? 95 TYR A O 1 ATOM 683 C CB . TYR A 1 95 ? 22.713 76.140 36.419 1.00 69.99 ? 95 TYR A CB 1 ATOM 684 C CG . TYR A 1 95 ? 22.380 75.701 34.987 1.00 70.26 ? 95 TYR A CG 1 ATOM 685 C CD1 . TYR A 1 95 ? 22.637 74.401 34.551 1.00 67.99 ? 95 TYR A CD1 1 ATOM 686 C CD2 . TYR A 1 95 ? 21.812 76.588 34.084 1.00 74.58 ? 95 TYR A CD2 1 ATOM 687 C CE1 . TYR A 1 95 ? 22.340 74.003 33.234 1.00 67.79 ? 95 TYR A CE1 1 ATOM 688 C CE2 . TYR A 1 95 ? 21.504 76.202 32.772 1.00 75.60 ? 95 TYR A CE2 1 ATOM 689 C CZ . TYR A 1 95 ? 21.769 74.906 32.360 1.00 72.09 ? 95 TYR A CZ 1 ATOM 690 O OH . TYR A 1 95 ? 21.465 74.544 31.062 1.00 73.28 ? 95 TYR A OH 1 ATOM 691 N N . PRO A 1 96 ? 22.613 75.493 39.599 1.00 63.95 ? 96 PRO A N 1 ATOM 692 C CA . PRO A 1 96 ? 22.772 74.058 39.284 1.00 59.59 ? 96 PRO A CA 1 ATOM 693 C C . PRO A 1 96 ? 21.450 73.325 39.377 1.00 57.02 ? 96 PRO A C 1 ATOM 694 O O . PRO A 1 96 ? 20.542 73.739 40.103 1.00 57.21 ? 96 PRO A O 1 ATOM 695 C CB . PRO A 1 96 ? 23.742 73.539 40.375 1.00 58.38 ? 96 PRO A CB 1 ATOM 696 C CG . PRO A 1 96 ? 24.251 74.802 41.108 1.00 62.23 ? 96 PRO A CG 1 ATOM 697 C CD . PRO A 1 96 ? 23.177 75.820 40.921 1.00 64.15 ? 96 PRO A CD 1 ATOM 698 N N . ARG A 1 97 ? 21.340 72.264 38.601 1.00 54.42 ? 97 ARG A N 1 ATOM 699 C CA . ARG A 1 97 ? 20.228 71.341 38.673 1.00 52.69 ? 97 ARG A CA 1 ATOM 700 C C . ARG A 1 97 ? 20.835 69.937 38.740 1.00 49.39 ? 97 ARG A C 1 ATOM 701 O O . ARG A 1 97 ? 21.801 69.654 38.040 1.00 49.85 ? 97 ARG A O 1 ATOM 702 C CB . ARG A 1 97 ? 19.350 71.468 37.426 1.00 53.48 ? 97 ARG A CB 1 ATOM 703 C CG . ARG A 1 97 ? 18.393 72.624 37.454 1.00 57.72 ? 97 ARG A CG 1 ATOM 704 C CD . ARG A 1 97 ? 17.284 72.416 38.456 1.00 58.34 ? 97 ARG A CD 1 ATOM 705 N NE . ARG A 1 97 ? 16.697 73.699 38.822 1.00 62.14 ? 97 ARG A NE 1 ATOM 706 C CZ . ARG A 1 97 ? 15.795 73.868 39.777 1.00 61.49 ? 97 ARG A CZ 1 ATOM 707 N NH1 . ARG A 1 97 ? 15.362 72.839 40.491 1.00 59.54 ? 97 ARG A NH1 1 ATOM 708 N NH2 . ARG A 1 97 ? 15.356 75.073 40.043 1.00 65.56 ? 97 ARG A NH2 1 ATOM 709 N N . VAL A 1 98 ? 20.312 69.078 39.606 1.00 47.37 ? 98 VAL A N 1 ATOM 710 C CA . VAL A 1 98 ? 20.723 67.677 39.601 1.00 44.66 ? 98 VAL A CA 1 ATOM 711 C C . VAL A 1 98 ? 19.562 66.793 39.158 1.00 43.00 ? 98 VAL A C 1 ATOM 712 O O . VAL A 1 98 ? 18.511 66.745 39.816 1.00 41.84 ? 98 VAL A O 1 ATOM 713 C CB . VAL A 1 98 ? 21.212 67.164 40.982 1.00 43.78 ? 98 VAL A CB 1 ATOM 714 C CG1 . VAL A 1 98 ? 21.862 65.781 40.836 1.00 42.12 ? 98 VAL A CG1 1 ATOM 715 C CG2 . VAL A 1 98 ? 22.181 68.120 41.622 1.00 47.91 ? 98 VAL A CG2 1 ATOM 716 N N . PHE A 1 99 ? 19.772 66.056 38.068 1.00 41.81 ? 99 PHE A N 1 ATOM 717 C CA . PHE A 1 99 ? 18.782 65.077 37.607 1.00 40.98 ? 99 PHE A CA 1 ATOM 718 C C . PHE A 1 99 ? 19.279 63.672 37.877 1.00 38.66 ? 99 PHE A C 1 ATOM 719 O O . PHE A 1 99 ? 20.477 63.438 37.837 1.00 39.00 ? 99 PHE A O 1 ATOM 720 C CB . PHE A 1 99 ? 18.472 65.252 36.112 1.00 41.96 ? 99 PHE A CB 1 ATOM 721 C CG . PHE A 1 99 ? 17.712 66.528 35.787 1.00 44.59 ? 99 PHE A CG 1 ATOM 722 C CD1 . PHE A 1 99 ? 16.323 66.518 35.686 1.00 43.68 ? 99 PHE A CD1 1 ATOM 723 C CD2 . PHE A 1 99 ? 18.391 67.723 35.577 1.00 44.72 ? 99 PHE A CD2 1 ATOM 724 C CE1 . PHE A 1 99 ? 15.617 67.685 35.398 1.00 49.92 ? 99 PHE A CE1 1 ATOM 725 C CE2 . PHE A 1 99 ? 17.704 68.884 35.272 1.00 50.25 ? 99 PHE A CE2 1 ATOM 726 C CZ . PHE A 1 99 ? 16.309 68.867 35.178 1.00 51.12 ? 99 PHE A CZ 1 ATOM 727 N N . GLN A 1 100 ? 18.360 62.739 38.132 1.00 37.90 ? 100 GLN A N 1 ATOM 728 C CA . GLN A 1 100 ? 18.709 61.330 38.400 1.00 35.09 ? 100 GLN A CA 1 ATOM 729 C C . GLN A 1 100 ? 17.750 60.390 37.669 1.00 35.77 ? 100 GLN A C 1 ATOM 730 O O . GLN A 1 100 ? 16.562 60.706 37.499 1.00 36.28 ? 100 GLN A O 1 ATOM 731 C CB . GLN A 1 100 ? 18.711 61.044 39.901 1.00 35.19 ? 100 GLN A CB 1 ATOM 732 C CG . GLN A 1 100 ? 19.853 61.731 40.684 1.00 35.59 ? 100 GLN A CG 1 ATOM 733 C CD . GLN A 1 100 ? 19.600 61.840 42.159 1.00 36.55 ? 100 GLN A CD 1 ATOM 734 O OE1 . GLN A 1 100 ? 19.001 62.791 42.598 1.00 37.97 ? 100 GLN A OE1 1 ATOM 735 N NE2 . GLN A 1 100 ? 20.083 60.876 42.934 1.00 35.26 ? 100 GLN A NE2 1 ATOM 736 N N A ILE A 1 101 ? 18.272 59.245 37.218 0.50 34.28 ? 101 ILE A N 1 ATOM 737 N N B ILE A 1 101 ? 18.279 59.273 37.176 0.50 34.08 ? 101 ILE A N 1 ATOM 738 C CA A ILE A 1 101 ? 17.491 58.275 36.437 0.50 35.64 ? 101 ILE A CA 1 ATOM 739 C CA B ILE A 1 101 ? 17.453 58.284 36.489 0.50 35.04 ? 101 ILE A CA 1 ATOM 740 C C A ILE A 1 101 ? 17.713 56.872 36.982 0.50 34.42 ? 101 ILE A C 1 ATOM 741 C C B ILE A 1 101 ? 17.712 56.946 37.138 0.50 34.03 ? 101 ILE A C 1 ATOM 742 O O A ILE A 1 101 ? 18.844 56.392 37.021 0.50 33.20 ? 101 ILE A O 1 ATOM 743 O O B ILE A 1 101 ? 18.860 56.600 37.420 0.50 32.39 ? 101 ILE A O 1 ATOM 744 C CB A ILE A 1 101 ? 17.862 58.292 34.909 0.50 36.61 ? 101 ILE A CB 1 ATOM 745 C CB B ILE A 1 101 ? 17.739 58.195 34.952 0.50 36.08 ? 101 ILE A CB 1 ATOM 746 C CG1 A ILE A 1 101 ? 17.603 59.664 34.278 0.50 39.51 ? 101 ILE A CG1 1 ATOM 747 C CG1 B ILE A 1 101 ? 17.767 59.587 34.311 0.50 38.07 ? 101 ILE A CG1 1 ATOM 748 C CG2 A ILE A 1 101 ? 17.061 57.234 34.132 0.50 37.58 ? 101 ILE A CG2 1 ATOM 749 C CG2 B ILE A 1 101 ? 16.675 57.312 34.253 0.50 36.83 ? 101 ILE A CG2 1 ATOM 750 C CD1 A ILE A 1 101 ? 18.830 60.555 34.192 0.50 40.36 ? 101 ILE A CD1 1 ATOM 751 C CD1 B ILE A 1 101 ? 18.104 59.594 32.824 0.50 39.04 ? 101 ILE A CD1 1 ATOM 752 N N . HIS A 1 102 ? 16.638 56.219 37.409 1.00 35.56 ? 102 HIS A N 1 ATOM 753 C CA . HIS A 1 102 ? 16.730 54.868 37.940 1.00 34.66 ? 102 HIS A CA 1 ATOM 754 C C . HIS A 1 102 ? 15.859 53.976 37.076 1.00 37.11 ? 102 HIS A C 1 ATOM 755 O O . HIS A 1 102 ? 14.666 54.196 36.962 1.00 38.31 ? 102 HIS A O 1 ATOM 756 C CB . HIS A 1 102 ? 16.297 54.837 39.408 1.00 35.56 ? 102 HIS A CB 1 ATOM 757 C CG . HIS A 1 102 ? 16.372 53.478 40.032 1.00 34.57 ? 102 HIS A CG 1 ATOM 758 N ND1 . HIS A 1 102 ? 15.634 53.134 41.141 1.00 33.83 ? 102 HIS A ND1 1 ATOM 759 C CD2 . HIS A 1 102 ? 17.106 52.380 39.709 1.00 36.72 ? 102 HIS A CD2 1 ATOM 760 C CE1 . HIS A 1 102 ? 15.904 51.881 41.477 1.00 38.22 ? 102 HIS A CE1 1 ATOM 761 N NE2 . HIS A 1 102 ? 16.783 51.394 40.615 1.00 35.12 ? 102 HIS A NE2 1 ATOM 762 N N . THR A 1 103 ? 16.498 52.981 36.460 1.00 37.18 ? 103 THR A N 1 ATOM 763 C CA . THR A 1 103 ? 15.852 52.018 35.600 1.00 40.21 ? 103 THR A CA 1 ATOM 764 C C . THR A 1 103 ? 16.101 50.600 36.145 1.00 39.74 ? 103 THR A C 1 ATOM 765 O O . THR A 1 103 ? 17.148 50.338 36.748 1.00 37.86 ? 103 THR A O 1 ATOM 766 C CB . THR A 1 103 ? 16.452 52.124 34.177 1.00 41.25 ? 103 THR A CB 1 ATOM 767 O OG1 . THR A 1 103 ? 16.309 53.467 33.693 1.00 43.99 ? 103 THR A OG1 1 ATOM 768 C CG2 . THR A 1 103 ? 15.770 51.190 33.226 1.00 45.38 ? 103 THR A CG2 1 ATOM 769 N N . GLY A 1 104 ? 15.159 49.684 35.909 1.00 41.83 ? 104 GLY A N 1 ATOM 770 C CA . GLY A 1 104 ? 15.334 48.284 36.288 1.00 41.90 ? 104 GLY A CA 1 ATOM 771 C C . GLY A 1 104 ? 14.594 47.301 35.405 1.00 45.50 ? 104 GLY A C 1 ATOM 772 O O . GLY A 1 104 ? 13.591 47.646 34.791 1.00 47.03 ? 104 GLY A O 1 ATOM 773 N N . CYS A 1 105 ? 15.110 46.072 35.366 1.00 46.32 ? 105 CYS A N 1 ATOM 774 C CA . CYS A 1 105 ? 14.491 44.936 34.678 1.00 50.46 ? 105 CYS A CA 1 ATOM 775 C C . CYS A 1 105 ? 14.755 43.690 35.529 1.00 51.60 ? 105 CYS A C 1 ATOM 776 O O . CYS A 1 105 ? 15.921 43.304 35.732 1.00 50.04 ? 105 CYS A O 1 ATOM 777 C CB . CYS A 1 105 ? 15.104 44.755 33.277 1.00 50.53 ? 105 CYS A CB 1 ATOM 778 S SG . CYS A 1 105 ? 14.371 43.462 32.238 1.00 54.45 ? 105 CYS A SG 1 ATOM 779 N N . LYS A 1 106 ? 13.688 43.091 36.045 1.00 55.48 ? 106 LYS A N 1 ATOM 780 C CA . LYS A 1 106 ? 13.767 41.840 36.798 1.00 58.19 ? 106 LYS A CA 1 ATOM 781 C C . LYS A 1 106 ? 13.129 40.727 35.982 1.00 62.79 ? 106 LYS A C 1 ATOM 782 O O . LYS A 1 106 ? 12.071 40.935 35.387 1.00 66.11 ? 106 LYS A O 1 ATOM 783 C CB . LYS A 1 106 ? 13.020 41.979 38.126 1.00 59.15 ? 106 LYS A CB 1 ATOM 784 C CG . LYS A 1 106 ? 13.383 40.949 39.199 1.00 60.16 ? 106 LYS A CG 1 ATOM 785 C CD . LYS A 1 106 ? 12.886 41.407 40.575 1.00 61.17 ? 106 LYS A CD 1 ATOM 786 C CE . LYS A 1 106 ? 13.966 41.232 41.660 1.00 62.64 ? 106 LYS A CE 1 ATOM 787 N NZ . LYS A 1 106 ? 13.748 42.100 42.874 1.00 62.29 ? 106 LYS A NZ 1 ATOM 788 N N . LEU A 1 107 ? 13.773 39.554 35.948 1.00 64.60 ? 107 LEU A N 1 ATOM 789 C CA . LEU A 1 107 ? 13.173 38.338 35.351 1.00 69.91 ? 107 LEU A CA 1 ATOM 790 C C . LEU A 1 107 ? 12.824 37.283 36.400 1.00 72.58 ? 107 LEU A C 1 ATOM 791 O O . LEU A 1 107 ? 13.718 36.658 36.993 1.00 70.97 ? 107 LEU A O 1 ATOM 792 C CB . LEU A 1 107 ? 14.095 37.702 34.298 1.00 70.16 ? 107 LEU A CB 1 ATOM 793 C CG . LEU A 1 107 ? 14.786 38.490 33.176 1.00 68.83 ? 107 LEU A CG 1 ATOM 794 C CD1 . LEU A 1 107 ? 15.155 37.512 32.067 1.00 71.01 ? 107 LEU A CD1 1 ATOM 795 C CD2 . LEU A 1 107 ? 13.912 39.599 32.604 1.00 70.24 ? 107 LEU A CD2 1 ATOM 796 N N . TYR A 1 108 ? 11.525 37.087 36.617 1.00 77.24 ? 108 TYR A N 1 ATOM 797 C CA . TYR A 1 108 ? 11.033 36.008 37.480 1.00 81.23 ? 108 TYR A CA 1 ATOM 798 C C . TYR A 1 108 ? 11.062 34.709 36.692 1.00 84.90 ? 108 TYR A C 1 ATOM 799 O O . TYR A 1 108 ? 10.813 34.708 35.484 1.00 87.02 ? 108 TYR A O 1 ATOM 800 C CB . TYR A 1 108 ? 9.606 36.293 37.980 1.00 85.07 ? 108 TYR A CB 1 ATOM 801 C CG . TYR A 1 108 ? 9.457 37.643 38.652 1.00 82.85 ? 108 TYR A CG 1 ATOM 802 C CD1 . TYR A 1 108 ? 9.799 37.819 39.992 1.00 80.76 ? 108 TYR A CD1 1 ATOM 803 C CD2 . TYR A 1 108 ? 8.991 38.748 37.943 1.00 82.65 ? 108 TYR A CD2 1 ATOM 804 C CE1 . TYR A 1 108 ? 9.676 39.056 40.609 1.00 78.83 ? 108 TYR A CE1 1 ATOM 805 C CE2 . TYR A 1 108 ? 8.860 39.989 38.552 1.00 80.57 ? 108 TYR A CE2 1 ATOM 806 C CZ . TYR A 1 108 ? 9.205 40.137 39.885 1.00 78.54 ? 108 TYR A CZ 1 ATOM 807 O OH . TYR A 1 108 ? 9.076 41.366 40.491 1.00 76.25 ? 108 TYR A OH 1 ATOM 808 N N . THR A 1 109 ? 11.366 33.604 37.363 1.00 86.14 ? 109 THR A N 1 ATOM 809 C CA . THR A 1 109 ? 11.441 32.319 36.665 1.00 89.75 ? 109 THR A CA 1 ATOM 810 C C . THR A 1 109 ? 10.058 31.672 36.445 1.00 95.84 ? 109 THR A C 1 ATOM 811 O O . THR A 1 109 ? 9.950 30.450 36.349 1.00 99.89 ? 109 THR A O 1 ATOM 812 C CB . THR A 1 109 ? 12.472 31.345 37.313 1.00 88.91 ? 109 THR A CB 1 ATOM 813 O OG1 . THR A 1 109 ? 12.243 31.246 38.725 1.00 90.02 ? 109 THR A OG1 1 ATOM 814 C CG2 . THR A 1 109 ? 13.904 31.836 37.064 1.00 84.13 ? 109 THR A CG2 1 ATOM 815 N N . ASN A 1 110 ? 9.015 32.501 36.357 1.00 96.93 ? 110 ASN A N 1 ATOM 816 C CA . ASN A 1 110 ? 7.686 32.046 35.911 1.00 103.35 ? 110 ASN A CA 1 ATOM 817 C C . ASN A 1 110 ? 7.218 32.735 34.619 1.00 104.33 ? 110 ASN A C 1 ATOM 818 O O . ASN A 1 110 ? 6.097 32.517 34.161 1.00 109.57 ? 110 ASN A O 1 ATOM 819 C CB . ASN A 1 110 ? 6.638 32.154 37.036 1.00 106.37 ? 110 ASN A CB 1 ATOM 820 C CG . ASN A 1 110 ? 6.041 33.560 37.187 1.00 104.82 ? 110 ASN A CG 1 ATOM 821 O OD1 . ASN A 1 110 ? 6.568 34.551 36.666 1.00 99.74 ? 110 ASN A OD1 1 ATOM 822 N ND2 . ASN A 1 110 ? 4.917 33.633 37.919 1.00 109.27 ? 110 ASN A ND2 1 ATOM 823 N N . GLY A 1 111 ? 8.087 33.578 34.053 1.00 99.17 ? 111 GLY A N 1 ATOM 824 C CA . GLY A 1 111 ? 7.834 34.224 32.762 1.00 100.02 ? 111 GLY A CA 1 ATOM 825 C C . GLY A 1 111 ? 7.729 35.737 32.823 1.00 96.57 ? 111 GLY A C 1 ATOM 826 O O . GLY A 1 111 ? 8.320 36.450 31.999 1.00 93.58 ? 111 GLY A O 1 ATOM 827 N N . THR A 1 112 ? 6.974 36.225 33.804 1.00 97.04 ? 112 THR A N 1 ATOM 828 C CA . THR A 1 112 ? 6.727 37.663 33.980 1.00 94.47 ? 112 THR A CA 1 ATOM 829 C C . THR A 1 112 ? 7.991 38.513 34.213 1.00 86.65 ? 112 THR A C 1 ATOM 830 O O . THR A 1 112 ? 9.003 38.023 34.727 1.00 83.83 ? 112 THR A O 1 ATOM 831 C CB . THR A 1 112 ? 5.708 37.912 35.123 1.00 97.07 ? 112 THR A CB 1 ATOM 832 O OG1 . THR A 1 112 ? 6.140 37.228 36.305 1.00 96.71 ? 112 THR A OG1 1 ATOM 833 C CG2 . THR A 1 112 ? 4.326 37.404 34.737 1.00 105.10 ? 112 THR A CG2 1 ATOM 834 N N . ARG A 1 113 ? 7.923 39.784 33.810 1.00 83.78 ? 113 ARG A N 1 ATOM 835 C CA . ARG A 1 113 ? 9.007 40.751 34.017 1.00 77.05 ? 113 ARG A CA 1 ATOM 836 C C . ARG A 1 113 ? 8.507 41.960 34.793 1.00 75.20 ? 113 ARG A C 1 ATOM 837 O O . ARG A 1 113 ? 7.366 42.385 34.607 1.00 79.04 ? 113 ARG A O 1 ATOM 838 C CB . ARG A 1 113 ? 9.547 41.282 32.682 1.00 76.17 ? 113 ARG A CB 1 ATOM 839 C CG . ARG A 1 113 ? 10.229 40.286 31.753 1.00 76.95 ? 113 ARG A CG 1 ATOM 840 C CD . ARG A 1 113 ? 10.351 40.894 30.346 1.00 77.28 ? 113 ARG A CD 1 ATOM 841 N NE . ARG A 1 113 ? 9.145 40.693 29.539 1.00 81.28 ? 113 ARG A NE 1 ATOM 842 C CZ . ARG A 1 113 ? 8.983 39.679 28.697 1.00 84.91 ? 113 ARG A CZ 1 ATOM 843 N NH1 . ARG A 1 113 ? 9.949 38.781 28.549 1.00 82.53 ? 113 ARG A NH1 1 ATOM 844 N NH2 . ARG A 1 113 ? 7.857 39.554 28.005 1.00 91.93 ? 113 ARG A NH2 1 ATOM 845 N N . TRP A 1 114 ? 9.365 42.527 35.637 1.00 69.52 ? 114 TRP A N 1 ATOM 846 C CA . TRP A 1 114 ? 9.106 43.845 36.197 1.00 67.23 ? 114 TRP A CA 1 ATOM 847 C C . TRP A 1 114 ? 10.112 44.831 35.602 1.00 62.47 ? 114 TRP A C 1 ATOM 848 O O . TRP A 1 114 ? 11.319 44.623 35.712 1.00 58.38 ? 114 TRP A O 1 ATOM 849 C CB . TRP A 1 114 ? 9.186 43.832 37.729 1.00 66.53 ? 114 TRP A CB 1 ATOM 850 C CG . TRP A 1 114 ? 8.846 45.167 38.394 1.00 66.41 ? 114 TRP A CG 1 ATOM 851 C CD1 . TRP A 1 114 ? 7.815 46.019 38.065 1.00 69.32 ? 114 TRP A CD1 1 ATOM 852 C CD2 . TRP A 1 114 ? 9.519 45.774 39.514 1.00 64.13 ? 114 TRP A CD2 1 ATOM 853 N NE1 . TRP A 1 114 ? 7.825 47.119 38.894 1.00 67.91 ? 114 TRP A NE1 1 ATOM 854 C CE2 . TRP A 1 114 ? 8.850 46.993 39.796 1.00 64.35 ? 114 TRP A CE2 1 ATOM 855 C CE3 . TRP A 1 114 ? 10.625 45.411 40.302 1.00 61.37 ? 114 TRP A CE3 1 ATOM 856 C CZ2 . TRP A 1 114 ? 9.253 47.851 40.831 1.00 62.34 ? 114 TRP A CZ2 1 ATOM 857 C CZ3 . TRP A 1 114 ? 11.020 46.267 41.337 1.00 58.44 ? 114 TRP A CZ3 1 ATOM 858 C CH2 . TRP A 1 114 ? 10.336 47.471 41.587 1.00 58.44 ? 114 TRP A CH2 1 ATOM 859 N N . SER A 1 115 ? 9.605 45.882 34.960 1.00 62.43 ? 115 SER A N 1 ATOM 860 C CA . SER A 1 115 ? 10.449 46.905 34.341 1.00 59.22 ? 115 SER A CA 1 ATOM 861 C C . SER A 1 115 ? 9.970 48.287 34.754 1.00 57.64 ? 115 SER A C 1 ATOM 862 O O . SER A 1 115 ? 8.775 48.506 34.898 1.00 60.58 ? 115 SER A O 1 ATOM 863 C CB . SER A 1 115 ? 10.421 46.781 32.816 1.00 61.97 ? 115 SER A CB 1 ATOM 864 O OG . SER A 1 115 ? 11.148 45.639 32.358 1.00 64.39 ? 115 SER A OG 1 ATOM 865 N N . PHE A 1 116 ? 10.899 49.218 34.950 1.00 52.75 ? 116 PHE A N 1 ATOM 866 C CA . PHE A 1 116 ? 10.542 50.582 35.356 1.00 51.72 ? 116 PHE A CA 1 ATOM 867 C C . PHE A 1 116 ? 11.560 51.624 34.897 1.00 48.99 ? 116 PHE A C 1 ATOM 868 O O . PHE A 1 116 ? 12.737 51.309 34.704 1.00 46.29 ? 116 PHE A O 1 ATOM 869 C CB . PHE A 1 116 ? 10.328 50.670 36.878 1.00 50.35 ? 116 PHE A CB 1 ATOM 870 C CG . PHE A 1 116 ? 11.570 50.368 37.698 1.00 46.95 ? 116 PHE A CG 1 ATOM 871 C CD1 . PHE A 1 116 ? 11.791 49.093 38.204 1.00 44.85 ? 116 PHE A CD1 1 ATOM 872 C CD2 . PHE A 1 116 ? 12.508 51.376 37.978 1.00 43.60 ? 116 PHE A CD2 1 ATOM 873 C CE1 . PHE A 1 116 ? 12.921 48.825 38.968 1.00 42.59 ? 116 PHE A CE1 1 ATOM 874 C CE2 . PHE A 1 116 ? 13.629 51.106 38.720 1.00 41.49 ? 116 PHE A CE2 1 ATOM 875 C CZ . PHE A 1 116 ? 13.838 49.816 39.212 1.00 39.50 ? 116 PHE A CZ 1 ATOM 876 N N . VAL A 1 117 ? 11.089 52.853 34.707 1.00 49.89 ? 117 VAL A N 1 ATOM 877 C CA . VAL A 1 117 ? 11.957 54.013 34.516 1.00 48.51 ? 117 VAL A CA 1 ATOM 878 C C . VAL A 1 117 ? 11.467 55.164 35.382 1.00 48.59 ? 117 VAL A C 1 ATOM 879 O O . VAL A 1 117 ? 10.331 55.642 35.217 1.00 51.83 ? 117 VAL A O 1 ATOM 880 C CB . VAL A 1 117 ? 12.016 54.528 33.078 1.00 50.72 ? 117 VAL A CB 1 ATOM 881 C CG1 . VAL A 1 117 ? 13.030 55.679 33.000 1.00 49.81 ? 117 VAL A CG1 1 ATOM 882 C CG2 . VAL A 1 117 ? 12.399 53.429 32.112 1.00 51.63 ? 117 VAL A CG2 1 ATOM 883 N N . ASN A 1 118 ? 12.337 55.611 36.290 1.00 45.60 ? 118 ASN A N 1 ATOM 884 C CA . ASN A 1 118 ? 12.049 56.745 37.166 1.00 45.96 ? 118 ASN A CA 1 ATOM 885 C C . ASN A 1 118 ? 13.028 57.906 36.994 1.00 44.53 ? 118 ASN A C 1 ATOM 886 O O . ASN A 1 118 ? 14.233 57.703 37.019 1.00 41.54 ? 118 ASN A O 1 ATOM 887 C CB . ASN A 1 118 ? 12.102 56.277 38.622 1.00 45.45 ? 118 ASN A CB 1 ATOM 888 C CG . ASN A 1 118 ? 11.028 55.273 38.954 1.00 47.15 ? 118 ASN A CG 1 ATOM 889 O OD1 . ASN A 1 118 ? 9.980 55.245 38.335 1.00 53.81 ? 118 ASN A OD1 1 ATOM 890 N ND2 . ASN A 1 118 ? 11.288 54.441 39.930 1.00 47.10 ? 118 ASN A ND2 1 ATOM 891 N N . ILE A 1 119 ? 12.504 59.123 36.857 1.00 46.60 ? 119 ILE A N 1 ATOM 892 C CA . ILE A 1 119 ? 13.336 60.337 36.827 1.00 45.17 ? 119 ILE A CA 1 ATOM 893 C C . ILE A 1 119 ? 13.084 61.210 38.063 1.00 45.85 ? 119 ILE A C 1 ATOM 894 O O . ILE A 1 119 ? 11.944 61.457 38.416 1.00 48.32 ? 119 ILE A O 1 ATOM 895 C CB . ILE A 1 119 ? 13.111 61.177 35.520 1.00 47.30 ? 119 ILE A CB 1 ATOM 896 C CG1 . ILE A 1 119 ? 13.303 60.289 34.275 1.00 47.99 ? 119 ILE A CG1 1 ATOM 897 C CG2 . ILE A 1 119 ? 14.065 62.335 35.467 1.00 44.93 ? 119 ILE A CG2 1 ATOM 898 C CD1 . ILE A 1 119 ? 13.047 60.970 32.921 1.00 51.34 ? 119 ILE A CD1 1 ATOM 899 N N . GLY A 1 120 ? 14.158 61.674 38.703 1.00 43.50 ? 120 GLY A N 1 ATOM 900 C CA . GLY A 1 120 ? 14.070 62.654 39.776 1.00 44.45 ? 120 GLY A CA 1 ATOM 901 C C . GLY A 1 120 ? 14.791 63.960 39.467 1.00 45.23 ? 120 GLY A C 1 ATOM 902 O O . GLY A 1 120 ? 15.704 64.011 38.622 1.00 43.95 ? 120 GLY A O 1 ATOM 903 N N . GLU A 1 121 ? 14.380 65.018 40.158 1.00 47.13 ? 121 GLU A N 1 ATOM 904 C CA . GLU A 1 121 ? 15.090 66.284 40.129 1.00 48.47 ? 121 GLU A CA 1 ATOM 905 C C . GLU A 1 121 ? 15.200 66.797 41.551 1.00 48.96 ? 121 GLU A C 1 ATOM 906 O O . GLU A 1 121 ? 14.243 66.715 42.336 1.00 49.79 ? 121 GLU A O 1 ATOM 907 C CB . GLU A 1 121 ? 14.361 67.299 39.239 1.00 51.95 ? 121 GLU A CB 1 ATOM 908 C CG . GLU A 1 121 ? 15.058 68.659 39.084 1.00 55.76 ? 121 GLU A CG 1 ATOM 909 C CD . GLU A 1 121 ? 14.836 69.580 40.277 1.00 62.86 ? 121 GLU A CD 1 ATOM 910 O OE1 . GLU A 1 121 ? 13.740 69.546 40.878 1.00 66.20 ? 121 GLU A OE1 1 ATOM 911 O OE2 . GLU A 1 121 ? 15.772 70.323 40.641 1.00 66.08 ? 121 GLU A OE2 1 ATOM 912 N N . GLY A 1 122 ? 16.372 67.335 41.880 1.00 48.73 ? 122 GLY A N 1 ATOM 913 C CA . GLY A 1 122 ? 16.638 67.810 43.235 1.00 49.05 ? 122 GLY A CA 1 ATOM 914 C C . GLY A 1 122 ? 16.386 66.774 44.312 1.00 47.65 ? 122 GLY A C 1 ATOM 915 O O . GLY A 1 122 ? 16.039 67.129 45.428 1.00 50.37 ? 122 GLY A O 1 ATOM 916 N N . GLY A 1 123 ? 16.543 65.495 43.987 1.00 45.48 ? 123 GLY A N 1 ATOM 917 C CA . GLY A 1 123 ? 16.452 64.432 44.993 1.00 44.05 ? 123 GLY A CA 1 ATOM 918 C C . GLY A 1 123 ? 15.044 64.035 45.399 1.00 45.55 ? 123 GLY A C 1 ATOM 919 O O . GLY A 1 123 ? 14.847 63.437 46.436 1.00 45.83 ? 123 GLY A O 1 ATOM 920 N N . ARG A 1 124 ? 14.056 64.394 44.584 1.00 46.51 ? 124 ARG A N 1 ATOM 921 C CA . ARG A 1 124 ? 12.675 63.978 44.786 1.00 48.92 ? 124 ARG A CA 1 ATOM 922 C C . ARG A 1 124 ? 12.181 63.455 43.444 1.00 48.43 ? 124 ARG A C 1 ATOM 923 O O . ARG A 1 124 ? 12.729 63.831 42.414 1.00 46.87 ? 124 ARG A O 1 ATOM 924 C CB . ARG A 1 124 ? 11.808 65.191 45.191 1.00 52.36 ? 124 ARG A CB 1 ATOM 925 C CG . ARG A 1 124 ? 12.256 65.885 46.474 1.00 53.99 ? 124 ARG A CG 1 ATOM 926 C CD . ARG A 1 124 ? 11.404 67.116 46.815 1.00 58.92 ? 124 ARG A CD 1 ATOM 927 N NE . ARG A 1 124 ? 11.456 68.157 45.783 1.00 64.69 ? 124 ARG A NE 1 ATOM 928 C CZ . ARG A 1 124 ? 10.388 68.726 45.218 1.00 69.67 ? 124 ARG A CZ 1 ATOM 929 N NH1 . ARG A 1 124 ? 9.155 68.348 45.555 1.00 73.37 ? 124 ARG A NH1 1 ATOM 930 N NH2 . ARG A 1 124 ? 10.550 69.682 44.308 1.00 70.38 ? 124 ARG A NH2 1 ATOM 931 N N . ASP A 1 125 ? 11.131 62.633 43.445 1.00 49.92 ? 125 ASP A N 1 ATOM 932 C CA . ASP A 1 125 ? 10.541 62.134 42.193 1.00 50.92 ? 125 ASP A CA 1 ATOM 933 C C . ASP A 1 125 ? 10.101 63.285 41.307 1.00 52.74 ? 125 ASP A C 1 ATOM 934 O O . ASP A 1 125 ? 9.690 64.339 41.808 1.00 54.01 ? 125 ASP A O 1 ATOM 935 C CB . ASP A 1 125 ? 9.339 61.224 42.455 1.00 53.89 ? 125 ASP A CB 1 ATOM 936 C CG . ASP A 1 125 ? 9.637 60.116 43.446 1.00 54.21 ? 125 ASP A CG 1 ATOM 937 O OD1 . ASP A 1 125 ? 10.835 59.855 43.727 1.00 50.81 ? 125 ASP A OD1 1 ATOM 938 O OD2 . ASP A 1 125 ? 8.664 59.511 43.961 1.00 57.17 ? 125 ASP A OD2 1 ATOM 939 N N . LEU A 1 126 ? 10.200 63.075 39.992 1.00 52.51 ? 126 LEU A N 1 ATOM 940 C CA . LEU A 1 126 ? 9.814 64.093 39.007 1.00 54.59 ? 126 LEU A CA 1 ATOM 941 C C . LEU A 1 126 ? 8.816 63.563 37.969 1.00 57.83 ? 126 LEU A C 1 ATOM 942 O O . LEU A 1 126 ? 7.748 64.141 37.823 1.00 61.76 ? 126 LEU A O 1 ATOM 943 C CB . LEU A 1 126 ? 11.043 64.721 38.326 1.00 52.46 ? 126 LEU A CB 1 ATOM 944 C CG . LEU A 1 126 ? 10.787 65.781 37.238 1.00 55.57 ? 126 LEU A CG 1 ATOM 945 C CD1 . LEU A 1 126 ? 10.113 67.004 37.818 1.00 57.67 ? 126 LEU A CD1 1 ATOM 946 C CD2 . LEU A 1 126 ? 12.076 66.164 36.507 1.00 53.75 ? 126 LEU A CD2 1 ATOM 947 N N . VAL A 1 127 ? 9.174 62.493 37.246 1.00 57.12 ? 127 VAL A N 1 ATOM 948 C CA . VAL A 1 127 ? 8.248 61.781 36.323 1.00 60.58 ? 127 VAL A CA 1 ATOM 949 C C . VAL A 1 127 ? 8.504 60.261 36.298 1.00 59.23 ? 127 VAL A C 1 ATOM 950 O O . VAL A 1 127 ? 9.631 59.807 36.531 1.00 55.08 ? 127 VAL A O 1 ATOM 951 C CB . VAL A 1 127 ? 8.268 62.335 34.848 1.00 62.54 ? 127 VAL A CB 1 ATOM 952 C CG1 . VAL A 1 127 ? 7.726 63.750 34.778 1.00 66.24 ? 127 VAL A CG1 1 ATOM 953 C CG2 . VAL A 1 127 ? 9.662 62.267 34.227 1.00 59.33 ? 127 VAL A CG2 1 ATOM 954 N N . THR A 1 128 ? 7.467 59.469 36.026 1.00 62.51 ? 128 THR A N 1 ATOM 955 C CA . THR A 1 128 ? 7.670 58.018 35.884 1.00 62.49 ? 128 THR A CA 1 ATOM 956 C C . THR A 1 128 ? 7.116 57.457 34.567 1.00 65.74 ? 128 THR A C 1 ATOM 957 O O . THR A 1 128 ? 6.175 58.004 34.015 1.00 68.90 ? 128 THR A O 1 ATOM 958 C CB . THR A 1 128 ? 7.138 57.216 37.109 1.00 63.35 ? 128 THR A CB 1 ATOM 959 O OG1 . THR A 1 128 ? 7.620 55.865 37.041 1.00 62.92 ? 128 THR A OG1 1 ATOM 960 C CG2 . THR A 1 128 ? 5.626 57.207 37.162 1.00 67.92 ? 128 THR A CG2 1 ATOM 961 N N . TYR A 1 129 ? 7.714 56.376 34.069 1.00 64.57 ? 129 TYR A N 1 ATOM 962 C CA . TYR A 1 129 ? 7.250 55.766 32.822 1.00 68.31 ? 129 TYR A CA 1 ATOM 963 C C . TYR A 1 129 ? 6.369 54.539 33.047 1.00 71.48 ? 129 TYR A C 1 ATOM 964 O O . TYR A 1 129 ? 6.805 53.532 33.599 1.00 68.54 ? 129 TYR A O 1 ATOM 965 C CB . TYR A 1 129 ? 8.414 55.464 31.865 1.00 66.09 ? 129 TYR A CB 1 ATOM 966 C CG . TYR A 1 129 ? 7.994 54.787 30.572 1.00 70.74 ? 129 TYR A CG 1 ATOM 967 C CD1 . TYR A 1 129 ? 7.196 55.455 29.636 1.00 75.23 ? 129 TYR A CD1 1 ATOM 968 C CD2 . TYR A 1 129 ? 8.380 53.471 30.286 1.00 71.12 ? 129 TYR A CD2 1 ATOM 969 C CE1 . TYR A 1 129 ? 6.803 54.838 28.448 1.00 79.74 ? 129 TYR A CE1 1 ATOM 970 C CE2 . TYR A 1 129 ? 7.980 52.840 29.085 1.00 74.93 ? 129 TYR A CE2 1 ATOM 971 C CZ . TYR A 1 129 ? 7.195 53.536 28.179 1.00 78.95 ? 129 TYR A CZ 1 ATOM 972 O OH . TYR A 1 129 ? 6.790 52.944 27.000 1.00 84.28 ? 129 TYR A OH 1 ATOM 973 N N . GLU A 1 130 ? 5.119 54.650 32.598 1.00 77.56 ? 130 GLU A N 1 ATOM 974 C CA . GLU A 1 130 ? 4.127 53.584 32.692 1.00 82.73 ? 130 GLU A CA 1 ATOM 975 C C . GLU A 1 130 ? 4.135 52.739 31.405 1.00 85.67 ? 130 GLU A C 1 ATOM 976 O O . GLU A 1 130 ? 3.601 53.153 30.379 1.00 89.17 ? 130 GLU A O 1 ATOM 977 C CB . GLU A 1 130 ? 2.749 54.212 32.923 1.00 88.20 ? 130 GLU A CB 1 ATOM 978 C CG . GLU A 1 130 ? 1.734 53.336 33.631 1.00 93.17 ? 130 GLU A CG 1 ATOM 979 C CD . GLU A 1 130 ? 0.686 54.166 34.350 1.00 98.18 ? 130 GLU A CD 1 ATOM 980 O OE1 . GLU A 1 130 ? -0.459 54.273 33.842 1.00 105.07 ? 130 GLU A OE1 1 ATOM 981 O OE2 . GLU A 1 130 ? 1.018 54.735 35.412 1.00 95.31 ? 130 GLU A OE2 1 ATOM 982 N N . LEU A 1 131 ? 4.760 51.563 31.471 1.00 84.34 ? 131 LEU A N 1 ATOM 983 C CA . LEU A 1 131 ? 4.963 50.720 30.294 1.00 86.70 ? 131 LEU A CA 1 ATOM 984 C C . LEU A 1 131 ? 3.650 50.293 29.655 1.00 93.79 ? 131 LEU A C 1 ATOM 985 O O . LEU A 1 131 ? 3.475 50.451 28.448 1.00 97.13 ? 131 LEU A O 1 ATOM 986 C CB . LEU A 1 131 ? 5.813 49.489 30.641 1.00 83.99 ? 131 LEU A CB 1 ATOM 987 C CG . LEU A 1 131 ? 6.653 48.828 29.526 1.00 84.37 ? 131 LEU A CG 1 ATOM 988 C CD1 . LEU A 1 131 ? 7.607 47.815 30.134 1.00 80.81 ? 131 LEU A CD1 1 ATOM 989 C CD2 . LEU A 1 131 ? 5.827 48.179 28.392 1.00 89.78 ? 131 LEU A CD2 1 ATOM 990 N N . SER A 1 132 ? 2.733 49.764 30.468 1.00 96.62 ? 132 SER A N 1 ATOM 991 C CA . SER A 1 132 ? 1.454 49.228 29.986 1.00 103.51 ? 132 SER A CA 1 ATOM 992 C C . SER A 1 132 ? 0.572 50.297 29.340 1.00 107.98 ? 132 SER A C 1 ATOM 993 O O . SER A 1 132 ? -0.059 50.047 28.313 1.00 113.31 ? 132 SER A O 1 ATOM 994 C CB . SER A 1 132 ? 0.696 48.533 31.122 1.00 105.85 ? 132 SER A CB 1 ATOM 995 O OG . SER A 1 132 ? 1.549 47.639 31.820 1.00 102.01 ? 132 SER A OG 1 ATOM 996 N N . ARG A 1 133 ? 0.551 51.484 29.943 1.00 105.58 ? 133 ARG A N 1 ATOM 997 C CA . ARG A 1 133 ? -0.250 52.610 29.462 1.00 109.42 ? 133 ARG A CA 1 ATOM 998 C C . ARG A 1 133 ? 0.440 53.441 28.367 1.00 107.83 ? 133 ARG A C 1 ATOM 999 O O . ARG A 1 133 ? -0.114 54.441 27.909 1.00 110.99 ? 133 ARG A O 1 ATOM 1000 C CB . ARG A 1 133 ? -0.645 53.508 30.640 1.00 108.46 ? 133 ARG A CB 1 ATOM 1001 N N . GLU A 1 134 ? 1.646 53.032 27.963 1.00 103.16 ? 134 GLU A N 1 ATOM 1002 C CA . GLU A 1 134 ? 2.427 53.731 26.926 1.00 101.84 ? 134 GLU A CA 1 ATOM 1003 C C . GLU A 1 134 ? 2.514 55.243 27.216 1.00 100.01 ? 134 GLU A C 1 ATOM 1004 O O . GLU A 1 134 ? 2.288 56.079 26.331 1.00 103.17 ? 134 GLU A O 1 ATOM 1005 C CB . GLU A 1 134 ? 1.840 53.442 25.527 1.00 108.41 ? 134 GLU A CB 1 ATOM 1006 C CG . GLU A 1 134 ? 2.766 53.786 24.364 1.00 108.03 ? 134 GLU A CG 1 ATOM 1007 C CD . GLU A 1 134 ? 2.320 53.204 23.031 1.00 114.47 ? 134 GLU A CD 1 ATOM 1008 O OE1 . GLU A 1 134 ? 1.178 53.467 22.582 1.00 121.87 ? 134 GLU A OE1 1 ATOM 1009 O OE2 . GLU A 1 134 ? 3.140 52.493 22.413 1.00 115.19 ? 134 GLU A OE2 1 ATOM 1010 N N . ARG A 1 135 ? 2.844 55.575 28.467 1.00 95.16 ? 135 ARG A N 1 ATOM 1011 C CA . ARG A 1 135 ? 2.706 56.938 28.992 1.00 94.28 ? 135 ARG A CA 1 ATOM 1012 C C . ARG A 1 135 ? 3.729 57.272 30.078 1.00 87.58 ? 135 ARG A C 1 ATOM 1013 O O . ARG A 1 135 ? 4.047 56.433 30.921 1.00 84.45 ? 135 ARG A O 1 ATOM 1014 C CB . ARG A 1 135 ? 1.293 57.118 29.560 1.00 99.53 ? 135 ARG A CB 1 ATOM 1015 C CG . ARG A 1 135 ? 0.938 58.524 30.032 1.00 100.32 ? 135 ARG A CG 1 ATOM 1016 C CD . ARG A 1 135 ? -0.485 58.580 30.589 1.00 105.96 ? 135 ARG A CD 1 ATOM 1017 N NE . ARG A 1 135 ? -0.651 57.857 31.856 1.00 103.97 ? 135 ARG A NE 1 ATOM 1018 C CZ . ARG A 1 135 ? -1.772 57.233 32.224 1.00 108.73 ? 135 ARG A CZ 1 ATOM 1019 N NH1 . ARG A 1 135 ? -2.830 57.221 31.418 1.00 114.55 ? 135 ARG A NH1 1 ATOM 1020 N NH2 . ARG A 1 135 ? -1.833 56.606 33.393 1.00 106.55 ? 135 ARG A NH2 1 ATOM 1021 N N . TRP A 1 136 ? 4.226 58.508 30.051 1.00 85.71 ? 136 TRP A N 1 ATOM 1022 C CA . TRP A 1 136 ? 5.011 59.079 31.155 1.00 80.38 ? 136 TRP A CA 1 ATOM 1023 C C . TRP A 1 136 ? 4.093 59.857 32.103 1.00 82.62 ? 136 TRP A C 1 ATOM 1024 O O . TRP A 1 136 ? 3.286 60.684 31.650 1.00 87.19 ? 136 TRP A O 1 ATOM 1025 C CB . TRP A 1 136 ? 6.085 60.010 30.606 1.00 77.77 ? 136 TRP A CB 1 ATOM 1026 C CG . TRP A 1 136 ? 7.214 59.295 29.956 1.00 75.45 ? 136 TRP A CG 1 ATOM 1027 C CD1 . TRP A 1 136 ? 7.252 58.812 28.683 1.00 77.59 ? 136 TRP A CD1 1 ATOM 1028 C CD2 . TRP A 1 136 ? 8.485 58.984 30.544 1.00 69.34 ? 136 TRP A CD2 1 ATOM 1029 N NE1 . TRP A 1 136 ? 8.467 58.215 28.442 1.00 73.77 ? 136 TRP A NE1 1 ATOM 1030 C CE2 . TRP A 1 136 ? 9.242 58.307 29.565 1.00 68.93 ? 136 TRP A CE2 1 ATOM 1031 C CE3 . TRP A 1 136 ? 9.056 59.211 31.805 1.00 65.92 ? 136 TRP A CE3 1 ATOM 1032 C CZ2 . TRP A 1 136 ? 10.544 57.850 29.804 1.00 64.37 ? 136 TRP A CZ2 1 ATOM 1033 C CZ3 . TRP A 1 136 ? 10.352 58.757 32.043 1.00 61.48 ? 136 TRP A CZ3 1 ATOM 1034 C CH2 . TRP A 1 136 ? 11.078 58.086 31.044 1.00 61.15 ? 136 TRP A CH2 1 ATOM 1035 N N . VAL A 1 137 ? 4.210 59.587 33.403 1.00 79.79 ? 137 VAL A N 1 ATOM 1036 C CA . VAL A 1 137 ? 3.300 60.135 34.423 1.00 82.33 ? 137 VAL A CA 1 ATOM 1037 C C . VAL A 1 137 ? 4.019 61.096 35.383 1.00 78.90 ? 137 VAL A C 1 ATOM 1038 O O . VAL A 1 137 ? 5.088 60.756 35.918 1.00 73.65 ? 137 VAL A O 1 ATOM 1039 C CB . VAL A 1 137 ? 2.618 59.013 35.261 1.00 83.77 ? 137 VAL A CB 1 ATOM 1040 C CG1 . VAL A 1 137 ? 1.266 59.469 35.762 1.00 89.23 ? 137 VAL A CG1 1 ATOM 1041 C CG2 . VAL A 1 137 ? 2.464 57.727 34.453 1.00 85.43 ? 137 VAL A CG2 1 ATOM 1042 N N . PRO A 1 138 ? 3.437 62.296 35.612 1.00 81.79 ? 138 PRO A N 1 ATOM 1043 C CA . PRO A 1 138 ? 4.010 63.280 36.542 1.00 79.58 ? 138 PRO A CA 1 ATOM 1044 C C . PRO A 1 138 ? 3.959 62.818 38.001 1.00 78.70 ? 138 PRO A C 1 ATOM 1045 O O . PRO A 1 138 ? 2.946 62.265 38.438 1.00 81.89 ? 138 PRO A O 1 ATOM 1046 C CB . PRO A 1 138 ? 3.110 64.510 36.354 1.00 84.63 ? 138 PRO A CB 1 ATOM 1047 C CG . PRO A 1 138 ? 2.378 64.275 35.093 1.00 87.90 ? 138 PRO A CG 1 ATOM 1048 C CD . PRO A 1 138 ? 2.199 62.807 34.996 1.00 87.64 ? 138 PRO A CD 1 ATOM 1049 N N . GLN A 1 139 ? 5.052 63.049 38.734 1.00 74.89 ? 139 GLN A N 1 ATOM 1050 C CA . GLN A 1 139 ? 5.175 62.646 40.137 1.00 74.09 ? 139 GLN A CA 1 ATOM 1051 C C . GLN A 1 139 ? 5.003 63.818 41.111 1.00 75.63 ? 139 GLN A C 1 ATOM 1052 O O . GLN A 1 139 ? 4.693 63.612 42.289 1.00 76.87 ? 139 GLN A O 1 ATOM 1053 C CB . GLN A 1 139 ? 6.523 61.976 40.384 1.00 69.02 ? 139 GLN A CB 1 ATOM 1054 C CG . GLN A 1 139 ? 6.807 60.698 39.569 1.00 68.76 ? 139 GLN A CG 1 ATOM 1055 C CD . GLN A 1 139 ? 6.204 59.443 40.182 1.00 70.26 ? 139 GLN A CD 1 ATOM 1056 O OE1 . GLN A 1 139 ? 5.010 59.398 40.501 1.00 76.09 ? 139 GLN A OE1 1 ATOM 1057 N NE2 . GLN A 1 139 ? 7.025 58.416 40.346 1.00 64.96 ? 139 GLN A NE2 1 ATOM 1058 N N . ARG A 1 140 ? 5.232 65.037 40.626 1.00 75.92 ? 140 ARG A N 1 ATOM 1059 C CA . ARG A 1 140 ? 4.965 66.247 41.397 1.00 77.79 ? 140 ARG A CA 1 ATOM 1060 C C . ARG A 1 140 ? 4.006 67.105 40.580 1.00 83.28 ? 140 ARG A C 1 ATOM 1061 O O . ARG A 1 140 ? 3.711 66.760 39.430 1.00 84.40 ? 140 ARG A O 1 ATOM 1062 C CB . ARG A 1 140 ? 6.262 66.986 41.772 1.00 74.13 ? 140 ARG A CB 1 ATOM 1063 C CG . ARG A 1 140 ? 7.059 67.550 40.614 1.00 71.79 ? 140 ARG A CG 1 ATOM 1064 C CD . ARG A 1 140 ? 8.331 68.234 41.070 1.00 68.73 ? 140 ARG A CD 1 ATOM 1065 N NE . ARG A 1 140 ? 9.381 67.272 41.414 1.00 62.37 ? 140 ARG A NE 1 ATOM 1066 C CZ . ARG A 1 140 ? 10.683 67.543 41.403 1.00 59.74 ? 140 ARG A CZ 1 ATOM 1067 N NH1 . ARG A 1 140 ? 11.111 68.743 41.040 1.00 60.75 ? 140 ARG A NH1 1 ATOM 1068 N NH2 . ARG A 1 140 ? 11.565 66.603 41.734 1.00 54.65 ? 140 ARG A NH2 1 ATOM 1069 N N . SER A 1 141 ? 3.505 68.200 41.155 1.00 87.09 ? 141 SER A N 1 ATOM 1070 C CA . SER A 1 141 ? 2.455 68.980 40.480 1.00 93.12 ? 141 SER A CA 1 ATOM 1071 C C . SER A 1 141 ? 2.866 70.347 39.900 1.00 94.07 ? 141 SER A C 1 ATOM 1072 O O . SER A 1 141 ? 2.022 71.234 39.760 1.00 99.04 ? 141 SER A O 1 ATOM 1073 C CB . SER A 1 141 ? 1.191 69.092 41.358 1.00 98.44 ? 141 SER A CB 1 ATOM 1074 O OG . SER A 1 141 ? 1.422 69.836 42.542 1.00 98.99 ? 141 SER A OG 1 ATOM 1075 N N . THR A 1 142 ? 4.138 70.499 39.524 1.00 90.14 ? 142 THR A N 1 ATOM 1076 C CA . THR A 1 142 ? 4.632 71.760 38.925 1.00 91.10 ? 142 THR A CA 1 ATOM 1077 C C . THR A 1 142 ? 4.942 71.701 37.401 1.00 91.03 ? 142 THR A C 1 ATOM 1078 O O . THR A 1 142 ? 4.701 70.676 36.752 1.00 90.63 ? 142 THR A O 1 ATOM 1079 C CB . THR A 1 142 ? 5.828 72.347 39.727 1.00 88.11 ? 142 THR A CB 1 ATOM 1080 O OG1 . THR A 1 142 ? 6.082 73.693 39.298 1.00 90.88 ? 142 THR A OG1 1 ATOM 1081 C CG2 . THR A 1 142 ? 7.095 71.484 39.571 1.00 82.38 ? 142 THR A CG2 1 ATOM 1082 N N . LEU A 1 143 ? 5.460 72.810 36.854 1.00 91.87 ? 143 LEU A N 1 ATOM 1083 C CA . LEU A 1 143 ? 5.717 72.976 35.410 1.00 92.70 ? 143 LEU A CA 1 ATOM 1084 C C . LEU A 1 143 ? 6.770 72.018 34.853 1.00 88.25 ? 143 LEU A C 1 ATOM 1085 O O . LEU A 1 143 ? 6.540 71.397 33.811 1.00 89.31 ? 143 LEU A O 1 ATOM 1086 C CB . LEU A 1 143 ? 6.143 74.414 35.095 1.00 94.94 ? 143 LEU A CB 1 ATOM 1087 C CG . LEU A 1 143 ? 6.617 74.761 33.676 1.00 96.43 ? 143 LEU A CG 1 ATOM 1088 C CD1 . LEU A 1 143 ? 5.440 75.050 32.730 1.00 102.40 ? 143 LEU A CD1 1 ATOM 1089 C CD2 . LEU A 1 143 ? 7.554 75.959 33.728 1.00 97.12 ? 143 LEU A CD2 1 ATOM 1090 N N . LEU A 1 144 ? 7.920 71.908 35.527 1.00 83.34 ? 144 LEU A N 1 ATOM 1091 C CA . LEU A 1 144 ? 8.996 71.049 35.037 1.00 78.75 ? 144 LEU A CA 1 ATOM 1092 C C . LEU A 1 144 ? 8.491 69.619 34.896 1.00 77.85 ? 144 LEU A C 1 ATOM 1093 O O . LEU A 1 144 ? 8.846 68.924 33.938 1.00 77.13 ? 144 LEU A O 1 ATOM 1094 C CB . LEU A 1 144 ? 10.230 71.110 35.943 1.00 74.84 ? 144 LEU A CB 1 ATOM 1095 C CG . LEU A 1 144 ? 11.392 70.144 35.661 1.00 70.25 ? 144 LEU A CG 1 ATOM 1096 C CD1 . LEU A 1 144 ? 12.215 70.577 34.457 1.00 69.62 ? 144 LEU A CD1 1 ATOM 1097 C CD2 . LEU A 1 144 ? 12.281 70.013 36.884 1.00 66.89 ? 144 LEU A CD2 1 ATOM 1098 N N . ALA A 1 145 ? 7.652 69.196 35.842 1.00 78.08 ? 145 ALA A N 1 ATOM 1099 C CA . ALA A 1 145 ? 7.024 67.878 35.792 1.00 78.03 ? 145 ALA A CA 1 ATOM 1100 C C . ALA A 1 145 ? 6.034 67.746 34.639 1.00 82.02 ? 145 ALA A C 1 ATOM 1101 O O . ALA A 1 145 ? 5.961 66.703 34.010 1.00 81.38 ? 145 ALA A O 1 ATOM 1102 C CB . ALA A 1 145 ? 6.345 67.557 37.108 1.00 78.14 ? 145 ALA A CB 1 ATOM 1103 N N . LYS A 1 146 ? 5.271 68.807 34.379 1.00 87.16 ? 146 LYS A N 1 ATOM 1104 C CA . LYS A 1 146 ? 4.258 68.815 33.319 1.00 92.30 ? 146 LYS A CA 1 ATOM 1105 C C . LYS A 1 146 ? 4.904 68.831 31.930 1.00 92.38 ? 146 LYS A C 1 ATOM 1106 O O . LYS A 1 146 ? 4.436 68.150 31.018 1.00 94.82 ? 146 LYS A O 1 ATOM 1107 C CB . LYS A 1 146 ? 3.312 70.017 33.499 1.00 97.53 ? 146 LYS A CB 1 ATOM 1108 C CG . LYS A 1 146 ? 2.209 70.154 32.455 1.00 103.76 ? 146 LYS A CG 1 ATOM 1109 C CD . LYS A 1 146 ? 1.411 71.442 32.658 1.00 108.74 ? 146 LYS A CD 1 ATOM 1110 C CE . LYS A 1 146 ? 0.488 71.734 31.473 1.00 115.33 ? 146 LYS A CE 1 ATOM 1111 N NZ . LYS A 1 146 ? -0.178 73.060 31.588 1.00 120.31 ? 146 LYS A NZ 1 ATOM 1112 N N . VAL A 1 147 ? 5.981 69.609 31.789 1.00 90.26 ? 147 VAL A N 1 ATOM 1113 C CA . VAL A 1 147 ? 6.700 69.774 30.526 1.00 90.59 ? 147 VAL A CA 1 ATOM 1114 C C . VAL A 1 147 ? 7.446 68.486 30.130 1.00 87.27 ? 147 VAL A C 1 ATOM 1115 O O . VAL A 1 147 ? 7.302 68.007 29.002 1.00 89.79 ? 147 VAL A O 1 ATOM 1116 C CB . VAL A 1 147 ? 7.679 70.985 30.591 1.00 89.81 ? 147 VAL A CB 1 ATOM 1117 C CG1 . VAL A 1 147 ? 8.640 70.979 29.415 1.00 90.14 ? 147 VAL A CG1 1 ATOM 1118 C CG2 . VAL A 1 147 ? 6.910 72.311 30.642 1.00 93.52 ? 147 VAL A CG2 1 ATOM 1119 N N . MET A 1 148 ? 8.221 67.926 31.059 1.00 81.69 ? 148 MET A N 1 ATOM 1120 C CA . MET A 1 148 ? 8.990 66.715 30.800 1.00 78.30 ? 148 MET A CA 1 ATOM 1121 C C . MET A 1 148 ? 8.107 65.510 30.486 1.00 80.13 ? 148 MET A C 1 ATOM 1122 O O . MET A 1 148 ? 8.482 64.672 29.577 1.00 80.20 ? 148 MET A O 1 ATOM 1123 C CB . MET A 1 148 ? 9.893 66.391 31.993 1.00 72.97 ? 148 MET A CB 1 ATOM 1124 C CG . MET A 1 148 ? 10.754 65.156 31.774 1.00 69.26 ? 148 MET A CG 1 ATOM 1125 S SD . MET A 1 148 ? 12.089 65.061 32.970 1.00 64.44 ? 148 MET A SD 1 ATOM 1126 C CE . MET A 1 148 ? 13.033 66.520 32.489 1.00 66.10 ? 148 MET A CE 1 ATOM 1127 N N . SER A 1 149 ? 6.951 65.414 31.252 1.00 82.74 ? 149 SER A N 1 ATOM 1128 C CA . SER A 1 149 ? 6.015 64.302 31.087 1.00 85.70 ? 149 SER A CA 1 ATOM 1129 C C . SER A 1 149 ? 5.299 64.359 29.731 1.00 91.30 ? 149 SER A C 1 ATOM 1130 O O . SER A 1 149 ? 5.050 63.316 29.120 1.00 92.80 ? 149 SER A O 1 ATOM 1131 C CB . SER A 1 149 ? 4.985 64.312 32.220 1.00 87.54 ? 149 SER A CB 1 ATOM 1132 O OG . SER A 1 149 ? 4.162 63.157 32.189 1.00 90.94 ? 149 SER A OG 1 ATOM 1133 N N . ASN A 1 150 ? 4.984 65.574 29.271 1.00 94.83 ? 150 ASN A N 1 ATOM 1134 C CA . ASN A 1 150 ? 4.243 65.781 28.015 1.00 101.10 ? 150 ASN A CA 1 ATOM 1135 C C . ASN A 1 150 ? 5.097 65.563 26.762 1.00 101.14 ? 150 ASN A C 1 ATOM 1136 O O . ASN A 1 150 ? 4.607 64.911 25.724 1.00 105.43 ? 150 ASN A O 1 ATOM 1137 C CB . ASN A 1 150 ? 3.611 67.183 27.981 1.00 105.34 ? 150 ASN A CB 1 ATOM 1138 C CG . ASN A 1 150 ? 2.343 67.274 28.814 1.00 108.56 ? 150 ASN A CG 1 ATOM 1139 O OD1 . ASN A 1 150 ? 1.746 66.136 29.216 1.00 109.76 ? 150 ASN A OD1 1 ATOM 1140 N ND2 . ASN A 1 150 ? 1.916 68.638 29.099 1.00 111.70 ? 150 ASN A ND2 1 ATOM 1141 N N . THR A 1 151 ? 6.368 66.145 26.867 1.00 97.39 ? 151 THR A N 1 ATOM 1142 C CA . THR A 1 151 ? 7.349 65.974 25.790 1.00 96.97 ? 151 THR A CA 1 ATOM 1143 C C . THR A 1 151 ? 7.692 64.497 25.595 1.00 94.67 ? 151 THR A C 1 ATOM 1144 O O . THR A 1 151 ? 7.781 64.017 24.465 1.00 97.25 ? 151 THR A O 1 ATOM 1145 C CB . THR A 1 151 ? 8.650 66.775 26.088 1.00 93.42 ? 151 THR A CB 1 ATOM 1146 O OG1 . THR A 1 151 ? 8.318 68.128 26.462 1.00 96.03 ? 151 THR A OG1 1 ATOM 1147 C CG2 . THR A 1 151 ? 9.565 66.814 24.870 1.00 94.47 ? 151 THR A CG2 1 ATOM 1148 N N . LEU A 1 152 ? 7.881 63.779 26.700 1.00 90.32 ? 152 LEU A N 1 ATOM 1149 C CA . LEU A 1 152 ? 8.242 62.365 26.626 1.00 88.05 ? 152 LEU A CA 1 ATOM 1150 C C . LEU A 1 152 ? 7.120 61.473 26.064 1.00 92.35 ? 152 LEU A C 1 ATOM 1151 O O . LEU A 1 152 ? 7.384 60.607 25.216 1.00 92.95 ? 152 LEU A O 1 ATOM 1152 C CB . LEU A 1 152 ? 8.753 61.855 27.979 1.00 82.48 ? 152 LEU A CB 1 ATOM 1153 C CG . LEU A 1 152 ? 10.167 62.303 28.382 1.00 77.83 ? 152 LEU A CG 1 ATOM 1154 C CD1 . LEU A 1 152 ? 10.430 62.009 29.853 1.00 73.37 ? 152 LEU A CD1 1 ATOM 1155 C CD2 . LEU A 1 152 ? 11.233 61.658 27.491 1.00 75.79 ? 152 LEU A CD2 1 ATOM 1156 N N . THR A 1 153 ? 5.882 61.698 26.529 1.00 95.80 ? 153 THR A N 1 ATOM 1157 C CA . THR A 1 153 ? 4.738 60.907 26.074 1.00 101.22 ? 153 THR A CA 1 ATOM 1158 C C . THR A 1 153 ? 4.460 61.170 24.597 1.00 107.16 ? 153 THR A C 1 ATOM 1159 O O . THR A 1 153 ? 4.158 60.236 23.852 1.00 110.04 ? 153 THR A O 1 ATOM 1160 C CB . THR A 1 153 ? 3.462 61.177 26.915 1.00 104.14 ? 153 THR A CB 1 ATOM 1161 O OG1 . THR A 1 153 ? 3.782 61.114 28.307 1.00 98.77 ? 153 THR A OG1 1 ATOM 1162 C CG2 . THR A 1 153 ? 2.378 60.146 26.620 1.00 108.58 ? 153 THR A CG2 1 ATOM 1163 N N . ASP A 1 154 ? 4.581 62.436 24.184 1.00 109.64 ? 154 ASP A N 1 ATOM 1164 C CA . ASP A 1 154 ? 4.389 62.831 22.775 1.00 116.02 ? 154 ASP A CA 1 ATOM 1165 C C . ASP A 1 154 ? 5.411 62.182 21.857 1.00 115.21 ? 154 ASP A C 1 ATOM 1166 O O . ASP A 1 154 ? 5.101 61.857 20.708 1.00 120.58 ? 154 ASP A O 1 ATOM 1167 C CB . ASP A 1 154 ? 4.432 64.361 22.591 1.00 118.03 ? 154 ASP A CB 1 ATOM 1168 C CG . ASP A 1 154 ? 3.093 65.070 22.964 1.00 123.13 ? 154 ASP A CG 1 ATOM 1169 O OD1 . ASP A 1 154 ? 1.806 64.114 23.017 1.00 127.80 ? 154 ASP A OD1 1 ATOM 1170 O OD2 . ASP A 1 154 ? 3.153 66.478 23.448 1.00 124.25 ? 154 ASP A OD2 1 ATOM 1171 N N . LEU A 1 155 ? 6.628 61.999 22.369 1.00 109.54 ? 155 LEU A N 1 ATOM 1172 C CA . LEU A 1 155 ? 7.674 61.289 21.641 1.00 108.35 ? 155 LEU A CA 1 ATOM 1173 C C . LEU A 1 155 ? 7.334 59.796 21.557 1.00 108.60 ? 155 LEU A C 1 ATOM 1174 O O . LEU A 1 155 ? 7.805 58.985 22.355 1.00 103.81 ? 155 LEU A O 1 ATOM 1175 C CB . LEU A 1 155 ? 9.043 61.547 22.287 1.00 102.23 ? 155 LEU A CB 1 ATOM 1176 C CG . LEU A 1 155 ? 9.907 62.683 21.705 1.00 103.69 ? 155 LEU A CG 1 ATOM 1177 C CD1 . LEU A 1 155 ? 9.149 64.018 21.476 1.00 108.38 ? 155 LEU A CD1 1 ATOM 1178 C CD2 . LEU A 1 155 ? 11.149 62.900 22.567 1.00 97.30 ? 155 LEU A CD2 1 ATOM 1179 N N . ARG A 1 156 ? 6.494 59.452 20.580 1.00 114.74 ? 156 ARG A N 1 ATOM 1180 C CA . ARG A 1 156 ? 5.959 58.095 20.448 1.00 116.51 ? 156 ARG A CA 1 ATOM 1181 C C . ARG A 1 156 ? 7.034 57.073 20.072 1.00 113.62 ? 156 ARG A C 1 ATOM 1182 O O . ARG A 1 156 ? 6.940 55.888 20.440 1.00 112.15 ? 156 ARG A O 1 ATOM 1183 C CB . ARG A 1 156 ? 4.800 58.071 19.445 1.00 124.75 ? 156 ARG A CB 1 ATOM 1184 C CG . ARG A 1 156 ? 3.503 58.712 19.970 1.00 128.61 ? 156 ARG A CG 1 ATOM 1185 C CD . ARG A 1 156 ? 2.660 57.731 20.805 1.00 129.62 ? 156 ARG A CD 1 ATOM 1186 N NE . ARG A 1 156 ? 2.119 56.633 19.991 1.00 135.56 ? 156 ARG A NE 1 ATOM 1187 C CZ . ARG A 1 156 ? 0.968 56.678 19.317 1.00 144.30 ? 156 ARG A CZ 1 ATOM 1188 N NH1 . ARG A 1 156 ? 0.207 57.773 19.340 1.00 148.54 ? 156 ARG A NH1 1 ATOM 1189 N NH2 . ARG A 1 156 ? 0.575 55.622 18.609 1.00 149.23 ? 156 ARG A NH2 1 ATOM 1190 N N . ALA A 1 157 ? 8.052 57.549 19.350 1.00 113.02 ? 157 ALA A N 1 ATOM 1191 C CA . ALA A 1 157 ? 9.217 56.740 19.001 1.00 110.43 ? 157 ALA A CA 1 ATOM 1192 C C . ALA A 1 157 ? 10.020 56.315 20.241 1.00 103.12 ? 157 ALA A C 1 ATOM 1193 O O . ALA A 1 157 ? 10.541 55.194 20.292 1.00 101.66 ? 157 ALA A O 1 ATOM 1194 C CB . ALA A 1 157 ? 10.102 57.490 18.007 1.00 112.23 ? 157 ALA A CB 1 ATOM 1195 N N . VAL A 1 158 ? 10.114 57.201 21.236 1.00 99.09 ? 158 VAL A N 1 ATOM 1196 C CA . VAL A 1 158 ? 10.807 56.893 22.498 1.00 92.21 ? 158 VAL A CA 1 ATOM 1197 C C . VAL A 1 158 ? 10.062 55.797 23.249 1.00 91.09 ? 158 VAL A C 1 ATOM 1198 O O . VAL A 1 158 ? 10.671 54.866 23.770 1.00 87.61 ? 158 VAL A O 1 ATOM 1199 C CB . VAL A 1 158 ? 10.960 58.150 23.410 1.00 89.62 ? 158 VAL A CB 1 ATOM 1200 C CG1 . VAL A 1 158 ? 11.352 57.762 24.832 1.00 83.23 ? 158 VAL A CG1 1 ATOM 1201 C CG2 . VAL A 1 158 ? 11.971 59.136 22.825 1.00 89.67 ? 158 VAL A CG2 1 ATOM 1202 N N . SER A 1 159 ? 8.740 55.922 23.285 1.00 94.45 ? 159 SER A N 1 ATOM 1203 C CA . SER A 1 159 ? 7.863 54.948 23.918 1.00 94.89 ? 159 SER A CA 1 ATOM 1204 C C . SER A 1 159 ? 8.035 53.563 23.285 1.00 96.01 ? 159 SER A C 1 ATOM 1205 O O . SER A 1 159 ? 8.163 52.556 23.990 1.00 93.38 ? 159 SER A O 1 ATOM 1206 C CB . SER A 1 159 ? 6.411 55.420 23.798 1.00 100.42 ? 159 SER A CB 1 ATOM 1207 O OG . SER A 1 159 ? 5.649 55.048 24.931 1.00 100.49 ? 159 SER A OG 1 ATOM 1208 N N . GLY A 1 160 ? 8.043 53.530 21.953 1.00 99.83 ? 160 GLY A N 1 ATOM 1209 C CA . GLY A 1 160 ? 8.329 52.314 21.199 1.00 101.33 ? 160 GLY A CA 1 ATOM 1210 C C . GLY A 1 160 ? 9.721 51.769 21.471 1.00 95.98 ? 160 GLY A C 1 ATOM 1211 O O . GLY A 1 160 ? 9.890 50.563 21.655 1.00 95.28 ? 160 GLY A O 1 ATOM 1212 N N . PHE A 1 161 ? 10.716 52.655 21.506 1.00 92.51 ? 161 PHE A N 1 ATOM 1213 C CA . PHE A 1 161 ? 12.100 52.247 21.748 1.00 88.05 ? 161 PHE A CA 1 ATOM 1214 C C . PHE A 1 161 ? 12.278 51.610 23.133 1.00 82.61 ? 161 PHE A C 1 ATOM 1215 O O . PHE A 1 161 ? 12.990 50.608 23.282 1.00 80.99 ? 161 PHE A O 1 ATOM 1216 C CB . PHE A 1 161 ? 13.067 53.427 21.559 1.00 86.78 ? 161 PHE A CB 1 ATOM 1217 C CG . PHE A 1 161 ? 14.514 53.015 21.477 1.00 85.03 ? 161 PHE A CG 1 ATOM 1218 C CD1 . PHE A 1 161 ? 15.018 52.419 20.325 1.00 90.49 ? 161 PHE A CD1 1 ATOM 1219 C CD2 . PHE A 1 161 ? 15.368 53.207 22.552 1.00 81.61 ? 161 PHE A CD2 1 ATOM 1220 C CE1 . PHE A 1 161 ? 16.357 52.024 20.251 1.00 88.74 ? 161 PHE A CE1 1 ATOM 1221 C CE2 . PHE A 1 161 ? 16.705 52.816 22.485 1.00 80.08 ? 161 PHE A CE2 1 ATOM 1222 C CZ . PHE A 1 161 ? 17.197 52.230 21.335 1.00 81.80 ? 161 PHE A CZ 1 ATOM 1223 N N . LEU A 1 162 ? 11.615 52.182 24.136 1.00 80.02 ? 162 LEU A N 1 ATOM 1224 C CA . LEU A 1 162 ? 11.676 51.661 25.503 1.00 75.21 ? 162 LEU A CA 1 ATOM 1225 C C . LEU A 1 162 ? 11.022 50.301 25.629 1.00 76.83 ? 162 LEU A C 1 ATOM 1226 O O . LEU A 1 162 ? 11.522 49.447 26.359 1.00 73.78 ? 162 LEU A O 1 ATOM 1227 C CB . LEU A 1 162 ? 11.037 52.632 26.498 1.00 73.82 ? 162 LEU A CB 1 ATOM 1228 C CG . LEU A 1 162 ? 11.888 53.831 26.909 1.00 69.99 ? 162 LEU A CG 1 ATOM 1229 C CD1 . LEU A 1 162 ? 11.088 54.757 27.795 1.00 70.23 ? 162 LEU A CD1 1 ATOM 1230 C CD2 . LEU A 1 162 ? 13.157 53.374 27.612 1.00 65.48 ? 162 LEU A CD2 1 ATOM 1231 N N . GLU A 1 163 ? 9.906 50.106 24.924 1.00 81.67 ? 163 GLU A N 1 ATOM 1232 C CA . GLU A 1 163 ? 9.229 48.811 24.889 1.00 84.40 ? 163 GLU A CA 1 ATOM 1233 C C . GLU A 1 163 ? 10.183 47.690 24.453 1.00 83.33 ? 163 GLU A C 1 ATOM 1234 O O . GLU A 1 163 ? 10.325 46.653 25.190 1.00 81.73 ? 163 GLU A O 1 ATOM 1235 C CB . GLU A 1 163 ? 8.007 48.858 23.965 1.00 91.17 ? 163 GLU A CB 1 ATOM 1236 N N . HIS A 1 164 ? 10.839 47.910 23.274 1.00 84.31 ? 164 HIS A N 1 ATOM 1237 C CA . HIS A 1 164 ? 11.827 46.954 22.771 1.00 83.59 ? 164 HIS A CA 1 ATOM 1238 C C . HIS A 1 164 ? 12.955 46.684 23.768 1.00 77.96 ? 164 HIS A C 1 ATOM 1239 O O . HIS A 1 164 ? 13.375 45.536 23.946 1.00 77.33 ? 164 HIS A O 1 ATOM 1240 C CB . HIS A 1 164 ? 12.440 47.437 21.463 1.00 85.79 ? 164 HIS A CB 1 ATOM 1241 C CG . HIS A 1 164 ? 13.415 46.464 20.879 1.00 86.83 ? 164 HIS A CG 1 ATOM 1242 N ND1 . HIS A 1 164 ? 14.783 46.637 20.969 1.00 83.53 ? 164 HIS A ND1 1 ATOM 1243 C CD2 . HIS A 1 164 ? 13.219 45.285 20.234 1.00 90.37 ? 164 HIS A CD2 1 ATOM 1244 C CE1 . HIS A 1 164 ? 15.388 45.619 20.382 1.00 84.15 ? 164 HIS A CE1 1 ATOM 1245 N NE2 . HIS A 1 164 ? 14.462 44.782 19.933 1.00 89.41 ? 164 HIS A NE2 1 ATOM 1246 N N . ILE A 1 165 ? 13.436 47.754 24.399 1.00 73.67 ? 165 ILE A N 1 ATOM 1247 C CA . ILE A 1 165 ? 14.530 47.688 25.358 1.00 69.00 ? 165 ILE A CA 1 ATOM 1248 C C . ILE A 1 165 ? 14.204 46.711 26.480 1.00 66.88 ? 165 ILE A C 1 ATOM 1249 O O . ILE A 1 165 ? 14.985 45.805 26.768 1.00 65.06 ? 165 ILE A O 1 ATOM 1250 C CB . ILE A 1 165 ? 14.818 49.087 25.932 1.00 65.83 ? 165 ILE A CB 1 ATOM 1251 C CG1 . ILE A 1 165 ? 15.668 49.921 24.966 1.00 67.60 ? 165 ILE A CG1 1 ATOM 1252 C CG2 . ILE A 1 165 ? 15.515 49.003 27.244 1.00 62.19 ? 165 ILE A CG2 1 ATOM 1253 C CD1 . ILE A 1 165 ? 16.192 51.233 25.632 1.00 64.43 ? 165 ILE A CD1 1 ATOM 1254 N N . PHE A 1 166 ? 13.034 46.889 27.087 1.00 67.82 ? 166 PHE A N 1 ATOM 1255 C CA . PHE A 1 166 ? 12.632 46.116 28.261 1.00 66.62 ? 166 PHE A CA 1 ATOM 1256 C C . PHE A 1 166 ? 12.078 44.736 27.939 1.00 69.91 ? 166 PHE A C 1 ATOM 1257 O O . PHE A 1 166 ? 12.072 43.863 28.804 1.00 68.75 ? 166 PHE A O 1 ATOM 1258 C CB . PHE A 1 166 ? 11.624 46.901 29.115 1.00 66.78 ? 166 PHE A CB 1 ATOM 1259 C CG . PHE A 1 166 ? 12.208 48.119 29.764 1.00 62.77 ? 166 PHE A CG 1 ATOM 1260 C CD1 . PHE A 1 166 ? 13.223 48.002 30.711 1.00 59.28 ? 166 PHE A CD1 1 ATOM 1261 C CD2 . PHE A 1 166 ? 11.744 49.382 29.431 1.00 63.63 ? 166 PHE A CD2 1 ATOM 1262 C CE1 . PHE A 1 166 ? 13.778 49.119 31.303 1.00 56.88 ? 166 PHE A CE1 1 ATOM 1263 C CE2 . PHE A 1 166 ? 12.282 50.508 30.008 1.00 59.42 ? 166 PHE A CE2 1 ATOM 1264 C CZ . PHE A 1 166 ? 13.308 50.385 30.947 1.00 57.79 ? 166 PHE A CZ 1 ATOM 1265 N N . SER A 1 167 ? 11.607 44.544 26.707 1.00 74.97 ? 167 SER A N 1 ATOM 1266 C CA . SER A 1 167 ? 11.044 43.250 26.269 1.00 79.38 ? 167 SER A CA 1 ATOM 1267 C C . SER A 1 167 ? 12.070 42.322 25.630 1.00 79.48 ? 167 SER A C 1 ATOM 1268 O O . SER A 1 167 ? 11.908 41.091 25.651 1.00 82.18 ? 167 SER A O 1 ATOM 1269 C CB . SER A 1 167 ? 9.903 43.451 25.261 1.00 85.14 ? 167 SER A CB 1 ATOM 1270 O OG . SER A 1 167 ? 8.959 44.371 25.754 1.00 86.79 ? 167 SER A OG 1 ATOM 1271 N N . SER A 1 168 ? 13.092 42.908 25.015 1.00 77.43 ? 168 SER A N 1 ATOM 1272 C CA . SER A 1 168 ? 14.018 42.136 24.209 1.00 78.76 ? 168 SER A CA 1 ATOM 1273 C C . SER A 1 168 ? 15.455 42.347 24.634 1.00 73.96 ? 168 SER A C 1 ATOM 1274 O O . SER A 1 168 ? 16.147 41.386 24.964 1.00 73.41 ? 168 SER A O 1 ATOM 1275 C CB . SER A 1 168 ? 13.847 42.481 22.728 1.00 83.50 ? 168 SER A CB 1 ATOM 1276 O OG . SER A 1 168 ? 14.945 42.003 21.969 1.00 85.45 ? 168 SER A OG 1 ATOM 1277 N N . SER A 1 169 ? 15.891 43.604 24.644 1.00 71.05 ? 169 SER A N 1 ATOM 1278 C CA . SER A 1 169 ? 17.302 43.921 24.799 1.00 67.41 ? 169 SER A CA 1 ATOM 1279 C C . SER A 1 169 ? 17.833 43.570 26.180 1.00 62.83 ? 169 SER A C 1 ATOM 1280 O O . SER A 1 169 ? 18.808 42.817 26.294 1.00 61.90 ? 169 SER A O 1 ATOM 1281 C CB . SER A 1 169 ? 17.573 45.385 24.436 1.00 66.93 ? 169 SER A CB 1 ATOM 1282 O OG . SER A 1 169 ? 17.319 45.599 23.046 1.00 71.53 ? 169 SER A OG 1 ATOM 1283 N N . PHE A 1 170 ? 17.180 44.083 27.224 1.00 59.98 ? 170 PHE A N 1 ATOM 1284 C CA . PHE A 1 170 ? 17.642 43.842 28.599 1.00 55.79 ? 170 PHE A CA 1 ATOM 1285 C C . PHE A 1 170 ? 17.479 42.385 29.079 1.00 56.14 ? 170 PHE A C 1 ATOM 1286 O O . PHE A 1 170 ? 18.399 41.872 29.716 1.00 53.56 ? 170 PHE A O 1 ATOM 1287 C CB . PHE A 1 170 ? 17.036 44.834 29.613 1.00 53.41 ? 170 PHE A CB 1 ATOM 1288 C CG . PHE A 1 170 ? 17.489 46.258 29.441 1.00 51.87 ? 170 PHE A CG 1 ATOM 1289 C CD1 . PHE A 1 170 ? 18.511 46.596 28.551 1.00 53.31 ? 170 PHE A CD1 1 ATOM 1290 C CD2 . PHE A 1 170 ? 16.906 47.265 30.204 1.00 50.81 ? 170 PHE A CD2 1 ATOM 1291 C CE1 . PHE A 1 170 ? 18.943 47.924 28.403 1.00 53.42 ? 170 PHE A CE1 1 ATOM 1292 C CE2 . PHE A 1 170 ? 17.324 48.607 30.077 1.00 51.82 ? 170 PHE A CE2 1 ATOM 1293 C CZ . PHE A 1 170 ? 18.355 48.935 29.177 1.00 51.41 ? 170 PHE A CZ 1 ATOM 1294 N N . PRO A 1 171 ? 16.315 41.725 28.805 1.00 59.11 ? 171 PRO A N 1 ATOM 1295 C CA . PRO A 1 171 ? 16.157 40.291 29.093 1.00 60.64 ? 171 PRO A CA 1 ATOM 1296 C C . PRO A 1 171 ? 17.210 39.340 28.491 1.00 61.94 ? 171 PRO A C 1 ATOM 1297 O O . PRO A 1 171 ? 17.710 38.465 29.213 1.00 61.21 ? 171 PRO A O 1 ATOM 1298 C CB . PRO A 1 171 ? 14.758 39.975 28.541 1.00 65.44 ? 171 PRO A CB 1 ATOM 1299 C CG . PRO A 1 171 ? 14.040 41.231 28.666 1.00 64.45 ? 171 PRO A CG 1 ATOM 1300 C CD . PRO A 1 171 ? 15.047 42.291 28.315 1.00 61.86 ? 171 PRO A CD 1 ATOM 1301 N N . ASN A 1 172 ? 17.510 39.467 27.194 1.00 64.07 ? 172 ASN A N 1 ATOM 1302 C CA . ASN A 1 172 ? 18.619 38.727 26.570 1.00 65.10 ? 172 ASN A CA 1 ATOM 1303 C C . ASN A 1 172 ? 19.985 38.966 27.243 1.00 61.06 ? 172 ASN A C 1 ATOM 1304 O O . ASN A 1 172 ? 20.763 38.032 27.421 1.00 60.99 ? 172 ASN A O 1 ATOM 1305 C CB . ASN A 1 172 ? 18.712 39.029 25.068 1.00 68.63 ? 172 ASN A CB 1 ATOM 1306 C CG . ASN A 1 172 ? 17.703 38.233 24.244 1.00 76.08 ? 172 ASN A CG 1 ATOM 1307 O OD1 . ASN A 1 172 ? 16.505 38.213 24.550 1.00 79.46 ? 172 ASN A OD1 1 ATOM 1308 N ND2 . ASN A 1 172 ? 18.186 37.568 23.189 1.00 80.59 ? 172 ASN A ND2 1 ATOM 1309 N N . TYR A 1 173 ? 20.248 40.218 27.615 1.00 58.13 ? 173 TYR A N 1 ATOM 1310 C CA . TYR A 1 173 ? 21.485 40.630 28.282 1.00 55.39 ? 173 TYR A CA 1 ATOM 1311 C C . TYR A 1 173 ? 21.663 39.981 29.667 1.00 52.88 ? 173 TYR A C 1 ATOM 1312 O O . TYR A 1 173 ? 22.727 39.427 29.966 1.00 52.21 ? 173 TYR A O 1 ATOM 1313 C CB . TYR A 1 173 ? 21.505 42.161 28.381 1.00 53.96 ? 173 TYR A CB 1 ATOM 1314 C CG . TYR A 1 173 ? 22.805 42.803 28.816 1.00 52.06 ? 173 TYR A CG 1 ATOM 1315 C CD1 . TYR A 1 173 ? 24.044 42.376 28.328 1.00 54.94 ? 173 TYR A CD1 1 ATOM 1316 C CD2 . TYR A 1 173 ? 22.785 43.879 29.683 1.00 49.50 ? 173 TYR A CD2 1 ATOM 1317 C CE1 . TYR A 1 173 ? 25.247 43.012 28.741 1.00 53.86 ? 173 TYR A CE1 1 ATOM 1318 C CE2 . TYR A 1 173 ? 23.954 44.505 30.086 1.00 50.61 ? 173 TYR A CE2 1 ATOM 1319 C CZ . TYR A 1 173 ? 25.177 44.072 29.613 1.00 50.92 ? 173 TYR A CZ 1 ATOM 1320 O OH . TYR A 1 173 ? 26.313 44.739 30.050 1.00 51.31 ? 173 TYR A OH 1 ATOM 1321 N N . ILE A 1 174 ? 20.616 40.032 30.490 1.00 52.25 ? 174 ILE A N 1 ATOM 1322 C CA . ILE A 1 174 ? 20.604 39.398 31.817 1.00 50.91 ? 174 ILE A CA 1 ATOM 1323 C C . ILE A 1 174 ? 20.957 37.904 31.702 1.00 53.76 ? 174 ILE A C 1 ATOM 1324 O O . ILE A 1 174 ? 21.799 37.386 32.451 1.00 52.65 ? 174 ILE A O 1 ATOM 1325 C CB . ILE A 1 174 ? 19.210 39.544 32.487 1.00 51.36 ? 174 ILE A CB 1 ATOM 1326 C CG1 . ILE A 1 174 ? 18.935 41.007 32.861 1.00 48.71 ? 174 ILE A CG1 1 ATOM 1327 C CG2 . ILE A 1 174 ? 19.112 38.678 33.727 1.00 50.74 ? 174 ILE A CG2 1 ATOM 1328 C CD1 . ILE A 1 174 ? 17.465 41.305 33.232 1.00 50.07 ? 174 ILE A CD1 1 ATOM 1329 N N . LEU A 1 175 ? 20.308 37.243 30.742 1.00 57.16 ? 175 LEU A N 1 ATOM 1330 C CA . LEU A 1 175 ? 20.452 35.824 30.488 1.00 60.31 ? 175 LEU A CA 1 ATOM 1331 C C . LEU A 1 175 ? 21.887 35.441 30.148 1.00 60.57 ? 175 LEU A C 1 ATOM 1332 O O . LEU A 1 175 ? 22.432 34.483 30.705 1.00 60.46 ? 175 LEU A O 1 ATOM 1333 C CB . LEU A 1 175 ? 19.513 35.411 29.357 1.00 64.42 ? 175 LEU A CB 1 ATOM 1334 C CG . LEU A 1 175 ? 18.255 34.638 29.748 1.00 67.07 ? 175 LEU A CG 1 ATOM 1335 C CD1 . LEU A 1 175 ? 17.451 35.385 30.801 1.00 62.83 ? 175 LEU A CD1 1 ATOM 1336 C CD2 . LEU A 1 175 ? 17.409 34.349 28.514 1.00 72.07 ? 175 LEU A CD2 1 ATOM 1337 N N . MET A 1 176 ? 22.491 36.199 29.240 1.00 60.86 ? 176 MET A N 1 ATOM 1338 C CA . MET A 1 176 ? 23.882 35.989 28.861 1.00 62.34 ? 176 MET A CA 1 ATOM 1339 C C . MET A 1 176 ? 24.844 36.293 30.028 1.00 58.90 ? 176 MET A C 1 ATOM 1340 O O . MET A 1 176 ? 25.818 35.561 30.237 1.00 59.38 ? 176 MET A O 1 ATOM 1341 C CB . MET A 1 176 ? 24.219 36.770 27.582 1.00 63.37 ? 176 MET A CB 1 ATOM 1342 C CG . MET A 1 176 ? 23.373 36.311 26.362 1.00 69.38 ? 176 MET A CG 1 ATOM 1343 S SD . MET A 1 176 ? 23.729 37.013 24.720 1.00 73.20 ? 176 MET A SD 1 ATOM 1344 C CE . MET A 1 176 ? 24.899 35.823 24.051 1.00 77.67 ? 176 MET A CE 1 ATOM 1345 N N . LEU A 1 177 ? 24.539 37.328 30.813 1.00 55.69 ? 177 LEU A N 1 ATOM 1346 C CA . LEU A 1 177 ? 25.394 37.719 31.939 1.00 53.32 ? 177 LEU A CA 1 ATOM 1347 C C . LEU A 1 177 ? 25.308 36.689 33.052 1.00 53.71 ? 177 LEU A C 1 ATOM 1348 O O . LEU A 1 177 ? 26.303 36.375 33.705 1.00 53.78 ? 177 LEU A O 1 ATOM 1349 C CB . LEU A 1 177 ? 24.998 39.087 32.493 1.00 50.04 ? 177 LEU A CB 1 ATOM 1350 C CG . LEU A 1 177 ? 25.273 40.375 31.697 1.00 50.06 ? 177 LEU A CG 1 ATOM 1351 C CD1 . LEU A 1 177 ? 24.660 41.547 32.437 1.00 46.31 ? 177 LEU A CD1 1 ATOM 1352 C CD2 . LEU A 1 177 ? 26.761 40.607 31.431 1.00 51.18 ? 177 LEU A CD2 1 ATOM 1353 N N . HIS A 1 178 ? 24.097 36.185 33.268 1.00 54.28 ? 178 HIS A N 1 ATOM 1354 C CA . HIS A 1 178 ? 23.832 35.175 34.268 1.00 55.31 ? 178 HIS A CA 1 ATOM 1355 C C . HIS A 1 178 ? 24.657 33.906 33.993 1.00 57.62 ? 178 HIS A C 1 ATOM 1356 O O . HIS A 1 178 ? 25.222 33.331 34.911 1.00 58.35 ? 178 HIS A O 1 ATOM 1357 C CB . HIS A 1 178 ? 22.331 34.866 34.270 1.00 57.31 ? 178 HIS A CB 1 ATOM 1358 C CG . HIS A 1 178 ? 21.875 34.064 35.443 1.00 60.13 ? 178 HIS A CG 1 ATOM 1359 N ND1 . HIS A 1 178 ? 21.564 32.723 35.351 1.00 67.64 ? 178 HIS A ND1 1 ATOM 1360 C CD2 . HIS A 1 178 ? 21.674 34.411 36.736 1.00 60.86 ? 178 HIS A CD2 1 ATOM 1361 C CE1 . HIS A 1 178 ? 21.190 32.276 36.540 1.00 69.42 ? 178 HIS A CE1 1 ATOM 1362 N NE2 . HIS A 1 178 ? 21.243 33.283 37.398 1.00 64.49 ? 178 HIS A NE2 1 ATOM 1363 N N . GLU A 1 179 ? 24.727 33.494 32.728 1.00 59.03 ? 179 GLU A N 1 ATOM 1364 C CA . GLU A 1 179 ? 25.486 32.323 32.278 1.00 61.27 ? 179 GLU A CA 1 ATOM 1365 C C . GLU A 1 179 ? 27.029 32.445 32.414 1.00 59.54 ? 179 GLU A C 1 ATOM 1366 O O . GLU A 1 179 ? 27.728 31.442 32.610 1.00 61.52 ? 179 GLU A O 1 ATOM 1367 C CB . GLU A 1 179 ? 25.050 31.988 30.833 1.00 64.22 ? 179 GLU A CB 1 ATOM 1368 C CG . GLU A 1 179 ? 26.065 31.279 29.938 1.00 67.61 ? 179 GLU A CG 1 ATOM 1369 C CD . GLU A 1 179 ? 25.449 30.747 28.641 1.00 73.27 ? 179 GLU A CD 1 ATOM 1370 O OE1 . GLU A 1 179 ? 24.269 30.325 28.659 1.00 77.78 ? 179 GLU A OE1 1 ATOM 1371 O OE2 . GLU A 1 179 ? 26.148 30.722 27.600 1.00 77.40 ? 179 GLU A OE2 1 ATOM 1372 N N . GLU A 1 180 ? 27.534 33.674 32.327 1.00 56.09 ? 180 GLU A N 1 ATOM 1373 C CA . GLU A 1 180 ? 28.969 33.996 32.284 1.00 54.91 ? 180 GLU A CA 1 ATOM 1374 C C . GLU A 1 180 ? 29.508 34.457 33.642 1.00 51.11 ? 180 GLU A C 1 ATOM 1375 O O . GLU A 1 180 ? 30.718 34.426 33.899 1.00 51.17 ? 180 GLU A O 1 ATOM 1376 C CB . GLU A 1 180 ? 29.175 35.189 31.333 1.00 54.60 ? 180 GLU A CB 1 ATOM 1377 C CG . GLU A 1 180 ? 28.959 34.889 29.886 1.00 60.64 ? 180 GLU A CG 1 ATOM 1378 C CD . GLU A 1 180 ? 30.029 33.989 29.338 1.00 67.77 ? 180 GLU A CD 1 ATOM 1379 O OE1 . GLU A 1 180 ? 31.223 34.271 29.596 1.00 70.32 ? 180 GLU A OE1 1 ATOM 1380 O OE2 . GLU A 1 180 ? 29.680 33.005 28.656 1.00 71.40 ? 180 GLU A OE2 1 ATOM 1381 N N . GLY A 1 181 ? 28.610 34.942 34.488 1.00 46.29 ? 181 GLY A N 1 ATOM 1382 C CA . GLY A 1 181 ? 29.050 35.662 35.667 1.00 42.55 ? 181 GLY A CA 1 ATOM 1383 C C . GLY A 1 181 ? 28.873 34.969 36.991 1.00 41.01 ? 181 GLY A C 1 ATOM 1384 O O . GLY A 1 181 ? 28.814 35.646 38.023 1.00 37.96 ? 181 GLY A O 1 ATOM 1385 N N . ARG A 1 182 ? 28.793 33.641 36.980 1.00 41.69 ? 182 ARG A N 1 ATOM 1386 C CA . ARG A 1 182 ? 28.514 32.924 38.227 1.00 43.12 ? 182 ARG A CA 1 ATOM 1387 C C . ARG A 1 182 ? 29.594 33.053 39.294 1.00 43.02 ? 182 ARG A C 1 ATOM 1388 O O . ARG A 1 182 ? 29.295 32.987 40.481 1.00 42.68 ? 182 ARG A O 1 ATOM 1389 C CB . ARG A 1 182 ? 28.152 31.471 37.990 1.00 45.27 ? 182 ARG A CB 1 ATOM 1390 C CG . ARG A 1 182 ? 26.799 31.319 37.334 1.00 47.44 ? 182 ARG A CG 1 ATOM 1391 C CD . ARG A 1 182 ? 26.270 29.885 37.430 1.00 48.81 ? 182 ARG A CD 1 ATOM 1392 N NE . ARG A 1 182 ? 26.779 29.048 36.380 1.00 53.52 ? 182 ARG A NE 1 ATOM 1393 C CZ . ARG A 1 182 ? 26.790 27.722 36.403 1.00 55.47 ? 182 ARG A CZ 1 ATOM 1394 N NH1 . ARG A 1 182 ? 26.341 27.044 37.461 1.00 56.61 ? 182 ARG A NH1 1 ATOM 1395 N NH2 . ARG A 1 182 ? 27.283 27.083 35.360 1.00 57.82 ? 182 ARG A NH2 1 ATOM 1396 N N . THR A 1 183 ? 30.831 33.277 38.859 1.00 44.43 ? 183 THR A N 1 ATOM 1397 C CA . THR A 1 183 ? 31.967 33.492 39.758 1.00 45.42 ? 183 THR A CA 1 ATOM 1398 C C . THR A 1 183 ? 31.707 34.603 40.803 1.00 44.20 ? 183 THR A C 1 ATOM 1399 O O . THR A 1 183 ? 32.157 34.521 41.940 1.00 43.85 ? 183 THR A O 1 ATOM 1400 C CB . THR A 1 183 ? 33.291 33.696 38.964 1.00 46.11 ? 183 THR A CB 1 ATOM 1401 O OG1 . THR A 1 183 ? 34.392 33.691 39.869 1.00 44.76 ? 183 THR A OG1 1 ATOM 1402 C CG2 . THR A 1 183 ? 33.290 35.003 38.185 1.00 42.71 ? 183 THR A CG2 1 ATOM 1403 N N . ASP A 1 184 ? 30.965 35.625 40.394 1.00 32.39 ? 184 ASP A N 1 ATOM 1404 C CA . ASP A 1 184 ? 30.471 36.688 41.290 1.00 33.99 ? 184 ASP A CA 1 ATOM 1405 C C . ASP A 1 184 ? 29.025 36.481 41.770 1.00 33.98 ? 184 ASP A C 1 ATOM 1406 O O . ASP A 1 184 ? 28.709 36.650 42.964 1.00 31.93 ? 184 ASP A O 1 ATOM 1407 C CB . ASP A 1 184 ? 30.604 38.029 40.572 1.00 36.90 ? 184 ASP A CB 1 ATOM 1408 C CG . ASP A 1 184 ? 31.894 38.723 40.903 1.00 40.01 ? 184 ASP A CG 1 ATOM 1409 O OD1 . ASP A 1 184 ? 32.060 39.109 42.091 1.00 47.71 ? 184 ASP A OD1 1 ATOM 1410 O OD2 . ASP A 1 184 ? 32.723 38.879 40.003 1.00 44.70 ? 184 ASP A OD2 1 ATOM 1411 N N . LEU A 1 185 ? 28.143 36.120 40.840 1.00 36.62 ? 185 LEU A N 1 ATOM 1412 C CA . LEU A 1 185 ? 26.722 35.939 41.174 1.00 37.77 ? 185 LEU A CA 1 ATOM 1413 C C . LEU A 1 185 ? 26.405 34.721 42.056 1.00 38.75 ? 185 LEU A C 1 ATOM 1414 O O . LEU A 1 185 ? 25.413 34.756 42.808 1.00 38.92 ? 185 LEU A O 1 ATOM 1415 C CB . LEU A 1 185 ? 25.870 35.918 39.905 1.00 40.23 ? 185 LEU A CB 1 ATOM 1416 C CG . LEU A 1 185 ? 26.103 37.095 38.943 1.00 41.59 ? 185 LEU A CG 1 ATOM 1417 C CD1 . LEU A 1 185 ? 25.525 36.796 37.569 1.00 42.74 ? 185 LEU A CD1 1 ATOM 1418 C CD2 . LEU A 1 185 ? 25.520 38.387 39.523 1.00 41.87 ? 185 LEU A CD2 1 ATOM 1419 N N . GLU A 1 186 ? 27.205 33.641 41.985 1.00 37.71 ? 186 GLU A N 1 ATOM 1420 C CA . GLU A 1 186 ? 26.986 32.514 42.909 1.00 37.89 ? 186 GLU A CA 1 ATOM 1421 C C . GLU A 1 186 ? 28.028 32.328 44.026 1.00 35.37 ? 186 GLU A C 1 ATOM 1422 O O . GLU A 1 186 ? 28.104 31.260 44.614 1.00 36.21 ? 186 GLU A O 1 ATOM 1423 C CB . GLU A 1 186 ? 26.765 31.193 42.152 1.00 40.38 ? 186 GLU A CB 1 ATOM 1424 C CG . GLU A 1 186 ? 25.551 31.211 41.239 1.00 42.23 ? 186 GLU A CG 1 ATOM 1425 C CD . GLU A 1 186 ? 25.399 29.942 40.421 1.00 48.38 ? 186 GLU A CD 1 ATOM 1426 O OE1 . GLU A 1 186 ? 26.111 28.918 40.673 1.00 52.13 ? 186 GLU A OE1 1 ATOM 1427 O OE2 . GLU A 1 186 ? 24.527 29.968 39.513 1.00 57.37 ? 186 GLU A OE2 1 ATOM 1428 N N . ARG A 1 187 ? 28.813 33.361 44.307 1.00 33.35 ? 187 ARG A N 1 ATOM 1429 C CA . ARG A 1 187 ? 29.795 33.338 45.366 1.00 31.90 ? 187 ARG A CA 1 ATOM 1430 C C . ARG A 1 187 ? 28.997 33.303 46.672 1.00 30.65 ? 187 ARG A C 1 ATOM 1431 O O . ARG A 1 187 ? 27.918 33.908 46.761 1.00 28.42 ? 187 ARG A O 1 ATOM 1432 C CB . ARG A 1 187 ? 30.693 34.593 45.303 1.00 32.27 ? 187 ARG A CB 1 ATOM 1433 C CG . ARG A 1 187 ? 31.732 34.703 46.457 1.00 30.74 ? 187 ARG A CG 1 ATOM 1434 C CD . ARG A 1 187 ? 32.691 35.929 46.290 1.00 33.34 ? 187 ARG A CD 1 ATOM 1435 N NE . ARG A 1 187 ? 31.907 37.150 46.067 1.00 33.67 ? 187 ARG A NE 1 ATOM 1436 C CZ . ARG A 1 187 ? 31.765 38.155 46.937 1.00 30.96 ? 187 ARG A CZ 1 ATOM 1437 N NH1 . ARG A 1 187 ? 32.398 38.166 48.095 1.00 31.71 ? 187 ARG A NH1 1 ATOM 1438 N NH2 . ARG A 1 187 ? 31.021 39.186 46.592 1.00 32.05 ? 187 ARG A NH2 1 ATOM 1439 N N . ARG A 1 188 ? 29.504 32.557 47.654 1.00 29.81 ? 188 ARG A N 1 ATOM 1440 C CA . ARG A 1 188 ? 28.880 32.450 48.991 1.00 29.94 ? 188 ARG A CA 1 ATOM 1441 C C . ARG A 1 188 ? 30.011 32.512 49.989 1.00 28.11 ? 188 ARG A C 1 ATOM 1442 O O . ARG A 1 188 ? 30.956 31.710 49.909 1.00 28.93 ? 188 ARG A O 1 ATOM 1443 C CB . ARG A 1 188 ? 28.094 31.119 49.128 1.00 32.25 ? 188 ARG A CB 1 ATOM 1444 C CG . ARG A 1 188 ? 27.039 30.976 48.025 1.00 36.29 ? 188 ARG A CG 1 ATOM 1445 C CD . ARG A 1 188 ? 26.227 29.712 48.058 1.00 41.27 ? 188 ARG A CD 1 ATOM 1446 N NE . ARG A 1 188 ? 26.983 28.548 47.564 1.00 54.09 ? 188 ARG A NE 1 ATOM 1447 C CZ . ARG A 1 188 ? 26.526 27.635 46.702 1.00 58.27 ? 188 ARG A CZ 1 ATOM 1448 N NH1 . ARG A 1 188 ? 25.296 27.739 46.183 1.00 61.91 ? 188 ARG A NH1 1 ATOM 1449 N NH2 . ARG A 1 188 ? 27.311 26.619 46.347 1.00 57.77 ? 188 ARG A NH2 1 ATOM 1450 N N . VAL A 1 189 ? 29.938 33.476 50.912 1.00 25.57 ? 189 VAL A N 1 ATOM 1451 C CA . VAL A 1 189 ? 30.927 33.603 51.982 1.00 24.44 ? 189 VAL A CA 1 ATOM 1452 C C . VAL A 1 189 ? 30.155 33.686 53.304 1.00 23.35 ? 189 VAL A C 1 ATOM 1453 O O . VAL A 1 189 ? 29.363 34.608 53.480 1.00 22.20 ? 189 VAL A O 1 ATOM 1454 C CB . VAL A 1 189 ? 31.724 34.927 51.857 1.00 24.59 ? 189 VAL A CB 1 ATOM 1455 C CG1 . VAL A 1 189 ? 32.682 34.999 52.968 1.00 25.19 ? 189 VAL A CG1 1 ATOM 1456 C CG2 . VAL A 1 189 ? 32.483 34.984 50.503 1.00 25.15 ? 189 VAL A CG2 1 ATOM 1457 N N . PRO A 1 190 ? 30.280 32.664 54.183 1.00 23.24 ? 190 PRO A N 1 ATOM 1458 C CA . PRO A 1 190 ? 29.500 32.707 55.443 1.00 22.33 ? 190 PRO A CA 1 ATOM 1459 C C . PRO A 1 190 ? 29.921 33.818 56.421 1.00 22.85 ? 190 PRO A C 1 ATOM 1460 O O . PRO A 1 190 ? 31.103 34.220 56.420 1.00 21.55 ? 190 PRO A O 1 ATOM 1461 C CB . PRO A 1 190 ? 29.695 31.307 56.045 1.00 24.28 ? 190 PRO A CB 1 ATOM 1462 C CG . PRO A 1 190 ? 30.093 30.439 54.871 1.00 24.24 ? 190 PRO A CG 1 ATOM 1463 C CD . PRO A 1 190 ? 30.962 31.387 54.007 1.00 24.40 ? 190 PRO A CD 1 ATOM 1464 N N . PRO A 1 191 ? 28.970 34.290 57.269 1.00 22.06 ? 191 PRO A N 1 ATOM 1465 C CA . PRO A 1 191 ? 29.253 35.332 58.225 1.00 22.74 ? 191 PRO A CA 1 ATOM 1466 C C . PRO A 1 191 ? 30.061 34.798 59.379 1.00 25.63 ? 191 PRO A C 1 ATOM 1467 O O . PRO A 1 191 ? 30.071 33.573 59.604 1.00 25.06 ? 191 PRO A O 1 ATOM 1468 C CB . PRO A 1 191 ? 27.837 35.743 58.709 1.00 22.30 ? 191 PRO A CB 1 ATOM 1469 C CG . PRO A 1 191 ? 27.067 34.484 58.631 1.00 23.07 ? 191 PRO A CG 1 ATOM 1470 C CD . PRO A 1 191 ? 27.552 33.854 57.349 1.00 24.01 ? 191 PRO A CD 1 ATOM 1471 N N . MET A 1 192 ? 30.743 35.693 60.096 1.00 25.84 ? 192 MET A N 1 ATOM 1472 C CA . MET A 1 192 ? 31.297 35.336 61.400 1.00 31.22 ? 192 MET A CA 1 ATOM 1473 C C . MET A 1 192 ? 30.679 36.328 62.355 1.00 28.94 ? 192 MET A C 1 ATOM 1474 O O . MET A 1 192 ? 30.303 37.391 61.917 1.00 27.61 ? 192 MET A O 1 ATOM 1475 C CB . MET A 1 192 ? 32.826 35.369 61.458 1.00 32.35 ? 192 MET A CB 1 ATOM 1476 C CG . MET A 1 192 ? 33.522 36.632 61.114 1.00 36.11 ? 192 MET A CG 1 ATOM 1477 S SD . MET A 1 192 ? 35.245 36.639 61.781 1.00 47.11 ? 192 MET A SD 1 ATOM 1478 C CE . MET A 1 192 ? 34.912 36.971 63.524 1.00 47.02 ? 192 MET A CE 1 ATOM 1479 N N . ALA A 1 193 ? 30.526 35.977 63.633 1.00 29.20 ? 193 ALA A N 1 ATOM 1480 C CA . ALA A 1 193 ? 29.825 36.881 64.568 1.00 28.16 ? 193 ALA A CA 1 ATOM 1481 C C . ALA A 1 193 ? 30.500 36.912 65.938 1.00 28.93 ? 193 ALA A C 1 ATOM 1482 O O . ALA A 1 193 ? 31.163 35.960 66.354 1.00 30.68 ? 193 ALA A O 1 ATOM 1483 C CB . ALA A 1 193 ? 28.345 36.516 64.694 1.00 27.07 ? 193 ALA A CB 1 ATOM 1484 N N . VAL A 1 194 ? 30.370 38.046 66.606 1.00 28.72 ? 194 VAL A N 1 ATOM 1485 C CA . VAL A 1 194 ? 30.950 38.231 67.928 1.00 28.85 ? 194 VAL A CA 1 ATOM 1486 C C . VAL A 1 194 ? 29.871 38.889 68.778 1.00 27.40 ? 194 VAL A C 1 ATOM 1487 O O . VAL A 1 194 ? 29.080 39.695 68.260 1.00 25.43 ? 194 VAL A O 1 ATOM 1488 C CB . VAL A 1 194 ? 32.280 39.054 67.915 1.00 30.01 ? 194 VAL A CB 1 ATOM 1489 C CG1 . VAL A 1 194 ? 33.428 38.290 67.192 1.00 32.63 ? 194 VAL A CG1 1 ATOM 1490 C CG2 . VAL A 1 194 ? 32.118 40.479 67.324 1.00 29.78 ? 194 VAL A CG2 1 ATOM 1491 N N . VAL A 1 195 ? 29.826 38.514 70.059 1.00 27.49 ? 195 VAL A N 1 ATOM 1492 C CA . VAL A 1 195 ? 28.866 39.082 71.025 1.00 27.10 ? 195 VAL A CA 1 ATOM 1493 C C . VAL A 1 195 ? 29.645 39.714 72.192 1.00 28.59 ? 195 VAL A C 1 ATOM 1494 O O . VAL A 1 195 ? 30.577 39.091 72.742 1.00 30.45 ? 195 VAL A O 1 ATOM 1495 C CB . VAL A 1 195 ? 27.891 38.004 71.553 1.00 28.07 ? 195 VAL A CB 1 ATOM 1496 C CG1 . VAL A 1 195 ? 27.028 38.559 72.663 1.00 27.81 ? 195 VAL A CG1 1 ATOM 1497 C CG2 . VAL A 1 195 ? 26.975 37.511 70.440 1.00 26.87 ? 195 VAL A CG2 1 ATOM 1498 N N . PHE A 1 196 ? 29.311 40.954 72.545 1.00 27.77 ? 196 PHE A N 1 ATOM 1499 C CA . PHE A 1 196 ? 29.889 41.584 73.740 1.00 29.95 ? 196 PHE A CA 1 ATOM 1500 C C . PHE A 1 196 ? 28.856 42.502 74.406 1.00 30.04 ? 196 PHE A C 1 ATOM 1501 O O . PHE A 1 196 ? 27.804 42.759 73.831 1.00 29.61 ? 196 PHE A O 1 ATOM 1502 C CB . PHE A 1 196 ? 31.176 42.350 73.399 1.00 31.09 ? 196 PHE A CB 1 ATOM 1503 C CG . PHE A 1 196 ? 31.035 43.273 72.212 1.00 30.60 ? 196 PHE A CG 1 ATOM 1504 C CD1 . PHE A 1 196 ? 31.181 42.776 70.905 1.00 32.15 ? 196 PHE A CD1 1 ATOM 1505 C CD2 . PHE A 1 196 ? 30.710 44.598 72.392 1.00 28.86 ? 196 PHE A CD2 1 ATOM 1506 C CE1 . PHE A 1 196 ? 31.029 43.618 69.805 1.00 33.51 ? 196 PHE A CE1 1 ATOM 1507 C CE2 . PHE A 1 196 ? 30.555 45.464 71.292 1.00 31.40 ? 196 PHE A CE2 1 ATOM 1508 C CZ . PHE A 1 196 ? 30.732 44.980 70.004 1.00 30.75 ? 196 PHE A CZ 1 ATOM 1509 N N . ALA A 1 197 ? 29.153 42.963 75.620 1.00 31.39 ? 197 ALA A N 1 ATOM 1510 C CA . ALA A 1 197 ? 28.230 43.817 76.379 1.00 31.39 ? 197 ALA A CA 1 ATOM 1511 C C . ALA A 1 197 ? 28.829 45.169 76.667 1.00 32.08 ? 197 ALA A C 1 ATOM 1512 O O . ALA A 1 197 ? 30.040 45.283 76.943 1.00 33.23 ? 197 ALA A O 1 ATOM 1513 C CB . ALA A 1 197 ? 27.818 43.146 77.674 1.00 32.94 ? 197 ALA A CB 1 ATOM 1514 N N . ARG A 1 198 ? 27.994 46.208 76.598 1.00 31.91 ? 198 ARG A N 1 ATOM 1515 C CA . ARG A 1 198 ? 28.466 47.571 76.851 1.00 33.46 ? 198 ARG A CA 1 ATOM 1516 C C . ARG A 1 198 ? 27.475 48.319 77.746 1.00 35.53 ? 198 ARG A C 1 ATOM 1517 O O . ARG A 1 198 ? 26.351 47.854 77.942 1.00 34.63 ? 198 ARG A O 1 ATOM 1518 C CB . ARG A 1 198 ? 28.699 48.305 75.517 1.00 33.31 ? 198 ARG A CB 1 ATOM 1519 C CG . ARG A 1 198 ? 29.679 47.591 74.538 1.00 32.75 ? 198 ARG A CG 1 ATOM 1520 C CD . ARG A 1 198 ? 31.091 47.739 75.109 1.00 34.74 ? 198 ARG A CD 1 ATOM 1521 N NE . ARG A 1 198 ? 32.189 47.262 74.279 1.00 34.08 ? 198 ARG A NE 1 ATOM 1522 C CZ . ARG A 1 198 ? 33.007 46.266 74.603 1.00 35.30 ? 198 ARG A CZ 1 ATOM 1523 N NH1 . ARG A 1 198 ? 32.814 45.567 75.719 1.00 32.32 ? 198 ARG A NH1 1 ATOM 1524 N NH2 . ARG A 1 198 ? 33.998 45.949 73.784 1.00 33.26 ? 198 ARG A NH2 1 ATOM 1525 N N . THR A 1 199 ? 27.896 49.444 78.330 1.00 39.05 ? 199 THR A N 1 ATOM 1526 C CA . THR A 1 199 ? 27.006 50.224 79.171 1.00 42.68 ? 199 THR A CA 1 ATOM 1527 C C . THR A 1 199 ? 25.844 50.789 78.350 1.00 43.75 ? 199 THR A C 1 ATOM 1528 O O . THR A 1 199 ? 25.981 51.030 77.149 1.00 42.82 ? 199 THR A O 1 ATOM 1529 C CB . THR A 1 199 ? 27.724 51.404 79.894 1.00 46.58 ? 199 THR A CB 1 ATOM 1530 O OG1 . THR A 1 199 ? 28.292 52.306 78.931 1.00 49.27 ? 199 THR A OG1 1 ATOM 1531 C CG2 . THR A 1 199 ? 28.815 50.899 80.778 1.00 49.02 ? 199 THR A CG2 1 ATOM 1532 N N . ALA A 1 200 ? 24.701 50.967 79.006 1.00 46.02 ? 200 ALA A N 1 ATOM 1533 C CA . ALA A 1 200 ? 23.561 51.687 78.446 1.00 48.76 ? 200 ALA A CA 1 ATOM 1534 C C . ALA A 1 200 ? 22.833 52.462 79.560 1.00 52.94 ? 200 ALA A C 1 ATOM 1535 O O . ALA A 1 200 ? 23.058 52.213 80.755 1.00 53.39 ? 200 ALA A O 1 ATOM 1536 C CB . ALA A 1 200 ? 22.618 50.730 77.781 1.00 46.62 ? 200 ALA A CB 1 ATOM 1537 N N . GLY A 1 201 ? 21.959 53.387 79.168 1.00 56.91 ? 201 GLY A N 1 ATOM 1538 C CA . GLY A 1 201 ? 21.214 54.206 80.133 1.00 62.61 ? 201 GLY A CA 1 ATOM 1539 C C . GLY A 1 201 ? 20.161 53.426 80.898 1.00 64.40 ? 201 GLY A C 1 ATOM 1540 O O . GLY A 1 201 ? 19.848 52.286 80.549 1.00 62.96 ? 201 GLY A O 1 ATOM 1541 N N . GLN A 1 202 ? 19.612 54.045 81.943 1.00 69.13 ? 202 GLN A N 1 ATOM 1542 C CA . GLN A 1 202 ? 18.506 53.472 82.736 1.00 71.86 ? 202 GLN A CA 1 ATOM 1543 C C . GLN A 1 202 ? 18.885 52.146 83.435 1.00 69.27 ? 202 GLN A C 1 ATOM 1544 O O . GLN A 1 202 ? 18.029 51.265 83.650 1.00 69.60 ? 202 GLN A O 1 ATOM 1545 C CB . GLN A 1 202 ? 17.242 53.324 81.866 1.00 73.34 ? 202 GLN A CB 1 ATOM 1546 C CG . GLN A 1 202 ? 16.868 54.606 81.097 1.00 77.49 ? 202 GLN A CG 1 ATOM 1547 C CD . GLN A 1 202 ? 15.583 54.475 80.288 1.00 80.19 ? 202 GLN A CD 1 ATOM 1548 O OE1 . GLN A 1 202 ? 15.600 54.032 79.135 1.00 80.37 ? 202 GLN A OE1 1 ATOM 1549 N NE2 . GLN A 1 202 ? 14.462 54.878 80.886 1.00 86.12 ? 202 GLN A NE2 1 ATOM 1550 N N . VAL A 1 203 ? 20.175 52.042 83.786 1.00 67.09 ? 203 VAL A N 1 ATOM 1551 C CA . VAL A 1 203 ? 20.788 50.874 84.462 1.00 64.56 ? 203 VAL A CA 1 ATOM 1552 C C . VAL A 1 203 ? 20.636 49.571 83.648 1.00 61.25 ? 203 VAL A C 1 ATOM 1553 O O . VAL A 1 203 ? 20.426 48.476 84.178 1.00 61.50 ? 203 VAL A O 1 ATOM 1554 C CB . VAL A 1 203 ? 20.351 50.766 85.964 1.00 67.52 ? 203 VAL A CB 1 ATOM 1555 C CG1 . VAL A 1 203 ? 21.177 49.724 86.717 1.00 66.43 ? 203 VAL A CG1 1 ATOM 1556 C CG2 . VAL A 1 203 ? 20.505 52.138 86.655 1.00 70.42 ? 203 VAL A CG2 1 ATOM 1557 N N . GLN A 1 204 ? 20.757 49.709 82.340 1.00 58.21 ? 204 GLN A N 1 ATOM 1558 C CA . GLN A 1 204 ? 20.681 48.562 81.463 1.00 54.61 ? 204 GLN A CA 1 ATOM 1559 C C . GLN A 1 204 ? 22.030 48.264 80.821 1.00 50.52 ? 204 GLN A C 1 ATOM 1560 O O . GLN A 1 204 ? 22.947 49.081 80.873 1.00 51.10 ? 204 GLN A O 1 ATOM 1561 C CB . GLN A 1 204 ? 19.623 48.786 80.392 1.00 55.32 ? 204 GLN A CB 1 ATOM 1562 C CG . GLN A 1 204 ? 18.222 48.398 80.815 1.00 58.47 ? 204 GLN A CG 1 ATOM 1563 C CD . GLN A 1 204 ? 17.218 48.758 79.749 1.00 62.20 ? 204 GLN A CD 1 ATOM 1564 O OE1 . GLN A 1 204 ? 17.274 49.853 79.184 1.00 63.56 ? 204 GLN A OE1 1 ATOM 1565 N NE2 . GLN A 1 204 ? 16.304 47.836 79.449 1.00 63.39 ? 204 GLN A NE2 1 ATOM 1566 N N . LEU A 1 205 ? 22.140 47.077 80.244 1.00 46.59 ? 205 LEU A N 1 ATOM 1567 C CA . LEU A 1 205 ? 23.317 46.649 79.520 1.00 42.88 ? 205 LEU A CA 1 ATOM 1568 C C . LEU A 1 205 ? 22.923 46.625 78.071 1.00 39.48 ? 205 LEU A C 1 ATOM 1569 O O . LEU A 1 205 ? 21.783 46.305 77.758 1.00 40.03 ? 205 LEU A O 1 ATOM 1570 C CB . LEU A 1 205 ? 23.669 45.210 79.908 1.00 43.27 ? 205 LEU A CB 1 ATOM 1571 C CG . LEU A 1 205 ? 24.550 44.858 81.092 1.00 45.00 ? 205 LEU A CG 1 ATOM 1572 C CD1 . LEU A 1 205 ? 24.303 43.441 81.420 1.00 46.72 ? 205 LEU A CD1 1 ATOM 1573 C CD2 . LEU A 1 205 ? 25.965 44.985 80.620 1.00 45.68 ? 205 LEU A CD2 1 ATOM 1574 N N . LEU A 1 206 ? 23.852 46.956 77.184 1.00 36.70 ? 206 LEU A N 1 ATOM 1575 C CA . LEU A 1 206 ? 23.609 46.798 75.767 1.00 34.32 ? 206 LEU A CA 1 ATOM 1576 C C . LEU A 1 206 ? 24.349 45.554 75.295 1.00 31.67 ? 206 LEU A C 1 ATOM 1577 O O . LEU A 1 206 ? 25.575 45.499 75.375 1.00 30.54 ? 206 LEU A O 1 ATOM 1578 C CB . LEU A 1 206 ? 24.061 48.030 74.992 1.00 34.66 ? 206 LEU A CB 1 ATOM 1579 C CG . LEU A 1 206 ? 23.764 48.045 73.479 1.00 34.88 ? 206 LEU A CG 1 ATOM 1580 C CD1 . LEU A 1 206 ? 22.265 48.214 73.303 1.00 36.82 ? 206 LEU A CD1 1 ATOM 1581 C CD2 . LEU A 1 206 ? 24.496 49.210 72.799 1.00 35.76 ? 206 LEU A CD2 1 ATOM 1582 N N . LEU A 1 207 ? 23.615 44.535 74.839 1.00 29.63 ? 207 LEU A N 1 ATOM 1583 C CA . LEU A 1 207 ? 24.289 43.396 74.234 1.00 26.61 ? 207 LEU A CA 1 ATOM 1584 C C . LEU A 1 207 ? 24.397 43.682 72.754 1.00 26.63 ? 207 LEU A C 1 ATOM 1585 O O . LEU A 1 207 ? 23.425 44.140 72.170 1.00 25.64 ? 207 LEU A O 1 ATOM 1586 C CB . LEU A 1 207 ? 23.529 42.088 74.461 1.00 28.22 ? 207 LEU A CB 1 ATOM 1587 C CG . LEU A 1 207 ? 23.184 41.799 75.928 1.00 30.96 ? 207 LEU A CG 1 ATOM 1588 C CD1 . LEU A 1 207 ? 22.502 40.461 76.030 1.00 32.17 ? 207 LEU A CD1 1 ATOM 1589 C CD2 . LEU A 1 207 ? 24.418 41.852 76.822 1.00 31.66 ? 207 LEU A CD2 1 ATOM 1590 N N . VAL A 1 208 ? 25.571 43.413 72.168 1.00 24.27 ? 208 VAL A N 1 ATOM 1591 C CA . VAL A 1 208 ? 25.855 43.714 70.755 1.00 24.05 ? 208 VAL A CA 1 ATOM 1592 C C . VAL A 1 208 ? 26.252 42.435 70.068 1.00 25.08 ? 208 VAL A C 1 ATOM 1593 O O . VAL A 1 208 ? 27.089 41.705 70.581 1.00 24.53 ? 208 VAL A O 1 ATOM 1594 C CB . VAL A 1 208 ? 27.032 44.716 70.589 1.00 24.04 ? 208 VAL A CB 1 ATOM 1595 C CG1 . VAL A 1 208 ? 27.316 45.016 69.125 1.00 23.06 ? 208 VAL A CG1 1 ATOM 1596 C CG2 . VAL A 1 208 ? 26.760 46.044 71.340 1.00 24.39 ? 208 VAL A CG2 1 ATOM 1597 N N . CYS A 1 209 ? 25.623 42.141 68.932 1.00 25.87 ? 209 CYS A N 1 ATOM 1598 C CA . CYS A 1 209 ? 26.065 41.038 68.090 1.00 24.88 ? 209 CYS A CA 1 ATOM 1599 C C . CYS A 1 209 ? 26.586 41.693 66.790 1.00 25.09 ? 209 CYS A C 1 ATOM 1600 O O . CYS A 1 209 ? 25.809 42.327 66.088 1.00 24.08 ? 209 CYS A O 1 ATOM 1601 C CB . CYS A 1 209 ? 24.863 40.192 67.763 1.00 25.75 ? 209 CYS A CB 1 ATOM 1602 S SG . CYS A 1 209 ? 25.227 38.764 66.738 1.00 29.63 ? 209 CYS A SG 1 ATOM 1603 N N . ARG A 1 210 ? 27.883 41.580 66.504 1.00 24.70 ? 210 ARG A N 1 ATOM 1604 C CA . ARG A 1 210 ? 28.432 42.181 65.308 1.00 24.26 ? 210 ARG A CA 1 ATOM 1605 C C . ARG A 1 210 ? 28.681 41.046 64.317 1.00 23.58 ? 210 ARG A C 1 ATOM 1606 O O . ARG A 1 210 ? 29.408 40.111 64.630 1.00 23.74 ? 210 ARG A O 1 ATOM 1607 C CB . ARG A 1 210 ? 29.723 42.922 65.642 1.00 26.76 ? 210 ARG A CB 1 ATOM 1608 C CG . ARG A 1 210 ? 30.421 43.548 64.417 1.00 28.11 ? 210 ARG A CG 1 ATOM 1609 C CD . ARG A 1 210 ? 31.794 44.086 64.830 1.00 34.79 ? 210 ARG A CD 1 ATOM 1610 N NE . ARG A 1 210 ? 32.611 44.400 63.661 1.00 37.25 ? 210 ARG A NE 1 ATOM 1611 C CZ . ARG A 1 210 ? 33.856 44.842 63.705 1.00 38.83 ? 210 ARG A CZ 1 ATOM 1612 N NH1 . ARG A 1 210 ? 34.445 45.069 64.876 1.00 40.91 ? 210 ARG A NH1 1 ATOM 1613 N NH2 . ARG A 1 210 ? 34.491 45.095 62.577 1.00 41.73 ? 210 ARG A NH2 1 ATOM 1614 N N . VAL A 1 211 ? 28.050 41.118 63.144 1.00 21.58 ? 211 VAL A N 1 ATOM 1615 C CA . VAL A 1 211 ? 28.124 40.026 62.154 1.00 21.49 ? 211 VAL A CA 1 ATOM 1616 C C . VAL A 1 211 ? 28.861 40.577 60.953 1.00 21.86 ? 211 VAL A C 1 ATOM 1617 O O . VAL A 1 211 ? 28.499 41.631 60.474 1.00 20.89 ? 211 VAL A O 1 ATOM 1618 C CB . VAL A 1 211 ? 26.717 39.614 61.708 1.00 22.07 ? 211 VAL A CB 1 ATOM 1619 C CG1 . VAL A 1 211 ? 26.813 38.383 60.790 1.00 22.64 ? 211 VAL A CG1 1 ATOM 1620 C CG2 . VAL A 1 211 ? 25.831 39.247 62.976 1.00 19.52 ? 211 VAL A CG2 1 ATOM 1621 N N . THR A 1 212 ? 29.917 39.890 60.513 1.00 22.44 ? 212 THR A N 1 ATOM 1622 C CA . THR A 1 212 ? 30.813 40.442 59.494 1.00 24.68 ? 212 THR A CA 1 ATOM 1623 C C . THR A 1 212 ? 31.057 39.420 58.359 1.00 25.38 ? 212 THR A C 1 ATOM 1624 O O . THR A 1 212 ? 30.671 38.249 58.477 1.00 25.62 ? 212 THR A O 1 ATOM 1625 C CB . THR A 1 212 ? 32.171 40.905 60.173 1.00 28.56 ? 212 THR A CB 1 ATOM 1626 O OG1 . THR A 1 212 ? 32.815 39.764 60.757 1.00 30.35 ? 212 THR A OG1 1 ATOM 1627 C CG2 . THR A 1 212 ? 31.903 41.876 61.325 1.00 28.05 ? 212 THR A CG2 1 ATOM 1628 N N . SER A 1 213 ? 31.614 39.875 57.243 1.00 25.73 ? 213 SER A N 1 ATOM 1629 C CA . SER A 1 213 ? 32.266 39.004 56.238 1.00 27.50 ? 213 SER A CA 1 ATOM 1630 C C . SER A 1 213 ? 31.374 38.257 55.296 1.00 26.50 ? 213 SER A C 1 ATOM 1631 O O . SER A 1 213 ? 31.882 37.422 54.520 1.00 28.05 ? 213 SER A O 1 ATOM 1632 C CB . SER A 1 213 ? 33.260 38.018 56.884 1.00 29.42 ? 213 SER A CB 1 ATOM 1633 O OG . SER A 1 213 ? 34.336 38.740 57.464 1.00 35.51 ? 213 SER A OG 1 ATOM 1634 N N . PHE A 1 214 ? 30.069 38.549 55.299 1.00 23.80 ? 214 PHE A N 1 ATOM 1635 C CA . PHE A 1 214 ? 29.144 37.657 54.597 1.00 23.42 ? 214 PHE A CA 1 ATOM 1636 C C . PHE A 1 214 ? 28.694 38.089 53.202 1.00 24.79 ? 214 PHE A C 1 ATOM 1637 O O . PHE A 1 214 ? 28.563 39.270 52.900 1.00 24.01 ? 214 PHE A O 1 ATOM 1638 C CB . PHE A 1 214 ? 27.914 37.352 55.455 1.00 22.26 ? 214 PHE A CB 1 ATOM 1639 C CG . PHE A 1 214 ? 27.119 38.575 55.844 1.00 21.76 ? 214 PHE A CG 1 ATOM 1640 C CD1 . PHE A 1 214 ? 27.404 39.244 57.012 1.00 23.62 ? 214 PHE A CD1 1 ATOM 1641 C CD2 . PHE A 1 214 ? 26.046 38.993 55.068 1.00 22.23 ? 214 PHE A CD2 1 ATOM 1642 C CE1 . PHE A 1 214 ? 26.619 40.365 57.415 1.00 22.90 ? 214 PHE A CE1 1 ATOM 1643 C CE2 . PHE A 1 214 ? 25.295 40.099 55.411 1.00 24.04 ? 214 PHE A CE2 1 ATOM 1644 C CZ . PHE A 1 214 ? 25.593 40.806 56.588 1.00 22.91 ? 214 PHE A CZ 1 ATOM 1645 N N . TYR A 1 215 ? 28.439 37.102 52.356 1.00 23.92 ? 215 TYR A N 1 ATOM 1646 C CA . TYR A 1 215 ? 27.884 37.405 51.043 1.00 25.17 ? 215 TYR A CA 1 ATOM 1647 C C . TYR A 1 215 ? 27.060 36.178 50.643 1.00 25.23 ? 215 TYR A C 1 ATOM 1648 O O . TYR A 1 215 ? 27.511 35.058 50.838 1.00 24.62 ? 215 TYR A O 1 ATOM 1649 C CB . TYR A 1 215 ? 29.017 37.692 50.021 1.00 25.71 ? 215 TYR A CB 1 ATOM 1650 C CG . TYR A 1 215 ? 28.449 38.082 48.668 1.00 26.66 ? 215 TYR A CG 1 ATOM 1651 C CD1 . TYR A 1 215 ? 28.276 37.141 47.664 1.00 26.68 ? 215 TYR A CD1 1 ATOM 1652 C CD2 . TYR A 1 215 ? 28.022 39.387 48.432 1.00 27.56 ? 215 TYR A CD2 1 ATOM 1653 C CE1 . TYR A 1 215 ? 27.706 37.490 46.433 1.00 31.58 ? 215 TYR A CE1 1 ATOM 1654 C CE2 . TYR A 1 215 ? 27.455 39.754 47.202 1.00 28.70 ? 215 TYR A CE2 1 ATOM 1655 C CZ . TYR A 1 215 ? 27.302 38.803 46.212 1.00 30.63 ? 215 TYR A CZ 1 ATOM 1656 O OH . TYR A 1 215 ? 26.749 39.186 45.003 1.00 34.03 ? 215 TYR A OH 1 ATOM 1657 N N . PRO A 1 216 ? 25.870 36.366 50.049 1.00 26.24 ? 216 PRO A N 1 ATOM 1658 C CA . PRO A 1 216 ? 25.181 37.580 49.622 1.00 27.31 ? 216 PRO A CA 1 ATOM 1659 C C . PRO A 1 216 ? 24.586 38.413 50.781 1.00 27.45 ? 216 PRO A C 1 ATOM 1660 O O . PRO A 1 216 ? 24.718 38.043 51.942 1.00 25.85 ? 216 PRO A O 1 ATOM 1661 C CB . PRO A 1 216 ? 24.104 37.048 48.656 1.00 29.51 ? 216 PRO A CB 1 ATOM 1662 C CG . PRO A 1 216 ? 23.850 35.627 49.092 1.00 29.63 ? 216 PRO A CG 1 ATOM 1663 C CD . PRO A 1 216 ? 25.175 35.135 49.620 1.00 27.54 ? 216 PRO A CD 1 ATOM 1664 N N . ARG A 1 217 ? 23.933 39.517 50.440 1.00 28.12 ? 217 ARG A N 1 ATOM 1665 C CA . ARG A 1 217 ? 23.466 40.505 51.405 1.00 29.86 ? 217 ARG A CA 1 ATOM 1666 C C . ARG A 1 217 ? 22.359 40.069 52.368 1.00 30.04 ? 217 ARG A C 1 ATOM 1667 O O . ARG A 1 217 ? 22.351 40.536 53.526 1.00 30.11 ? 217 ARG A O 1 ATOM 1668 C CB . ARG A 1 217 ? 22.969 41.741 50.634 1.00 31.90 ? 217 ARG A CB 1 ATOM 1669 C CG . ARG A 1 217 ? 22.794 43.037 51.488 1.00 33.77 ? 217 ARG A CG 1 ATOM 1670 C CD . ARG A 1 217 ? 22.218 44.132 50.592 1.00 39.39 ? 217 ARG A CD 1 ATOM 1671 N NE . ARG A 1 217 ? 22.321 45.479 51.177 1.00 51.37 ? 217 ARG A NE 1 ATOM 1672 C CZ . ARG A 1 217 ? 21.414 46.040 51.981 1.00 56.47 ? 217 ARG A CZ 1 ATOM 1673 N NH1 . ARG A 1 217 ? 20.338 45.355 52.364 1.00 58.94 ? 217 ARG A NH1 1 ATOM 1674 N NH2 . ARG A 1 217 ? 21.596 47.284 52.435 1.00 58.61 ? 217 ARG A NH2 1 ATOM 1675 N N . PRO A 1 218 ? 21.325 39.325 51.878 1.00 31.69 ? 218 PRO A N 1 ATOM 1676 C CA . PRO A 1 218 ? 20.219 38.998 52.796 1.00 32.65 ? 218 PRO A CA 1 ATOM 1677 C C . PRO A 1 218 ? 20.696 38.178 53.987 1.00 31.50 ? 218 PRO A C 1 ATOM 1678 O O . PRO A 1 218 ? 21.553 37.311 53.829 1.00 29.50 ? 218 PRO A O 1 ATOM 1679 C CB . PRO A 1 218 ? 19.297 38.151 51.922 1.00 35.96 ? 218 PRO A CB 1 ATOM 1680 C CG . PRO A 1 218 ? 19.569 38.652 50.530 1.00 35.74 ? 218 PRO A CG 1 ATOM 1681 C CD . PRO A 1 218 ? 21.034 38.843 50.512 1.00 32.76 ? 218 PRO A CD 1 ATOM 1682 N N . ILE A 1 219 ? 20.178 38.482 55.173 1.00 32.23 ? 219 ILE A N 1 ATOM 1683 C CA . ILE A 1 219 ? 20.593 37.789 56.412 1.00 31.23 ? 219 ILE A CA 1 ATOM 1684 C C . ILE A 1 219 ? 19.546 38.080 57.479 1.00 33.95 ? 219 ILE A C 1 ATOM 1685 O O . ILE A 1 219 ? 18.816 39.096 57.392 1.00 33.98 ? 219 ILE A O 1 ATOM 1686 C CB . ILE A 1 219 ? 22.016 38.281 56.872 1.00 29.38 ? 219 ILE A CB 1 ATOM 1687 C CG1 . ILE A 1 219 ? 22.666 37.321 57.893 1.00 27.19 ? 219 ILE A CG1 1 ATOM 1688 C CG2 . ILE A 1 219 ? 21.970 39.728 57.376 1.00 28.99 ? 219 ILE A CG2 1 ATOM 1689 C CD1 . ILE A 1 219 ? 24.089 37.732 58.234 1.00 27.05 ? 219 ILE A CD1 1 ATOM 1690 N N . ALA A 1 220 ? 19.414 37.181 58.456 1.00 33.68 ? 220 ALA A N 1 ATOM 1691 C CA . ALA A 1 220 ? 18.543 37.485 59.567 1.00 36.24 ? 220 ALA A CA 1 ATOM 1692 C C . ALA A 1 220 ? 19.269 37.163 60.864 1.00 35.47 ? 220 ALA A C 1 ATOM 1693 O O . ALA A 1 220 ? 19.790 36.063 61.040 1.00 36.51 ? 220 ALA A O 1 ATOM 1694 C CB . ALA A 1 220 ? 17.243 36.760 59.479 1.00 39.72 ? 220 ALA A CB 1 ATOM 1695 N N . VAL A 1 221 ? 19.295 38.146 61.749 1.00 34.95 ? 221 VAL A N 1 ATOM 1696 C CA . VAL A 1 221 ? 20.004 38.064 63.021 1.00 33.51 ? 221 VAL A CA 1 ATOM 1697 C C . VAL A 1 221 ? 18.961 38.268 64.108 1.00 37.27 ? 221 VAL A C 1 ATOM 1698 O O . VAL A 1 221 ? 18.262 39.304 64.115 1.00 38.42 ? 221 VAL A O 1 ATOM 1699 C CB . VAL A 1 221 ? 21.038 39.166 63.134 1.00 30.98 ? 221 VAL A CB 1 ATOM 1700 C CG1 . VAL A 1 221 ? 21.737 39.086 64.496 1.00 29.51 ? 221 VAL A CG1 1 ATOM 1701 C CG2 . VAL A 1 221 ? 22.059 39.078 61.974 1.00 29.75 ? 221 VAL A CG2 1 ATOM 1702 N N . THR A 1 222 ? 18.816 37.275 64.992 1.00 37.97 ? 222 THR A N 1 ATOM 1703 C CA . THR A 1 222 ? 17.860 37.375 66.078 1.00 41.30 ? 222 THR A CA 1 ATOM 1704 C C . THR A 1 222 ? 18.558 37.128 67.421 1.00 39.74 ? 222 THR A C 1 ATOM 1705 O O . THR A 1 222 ? 19.648 36.556 67.475 1.00 37.35 ? 222 THR A O 1 ATOM 1706 C CB . THR A 1 222 ? 16.637 36.434 65.897 1.00 45.74 ? 222 THR A CB 1 ATOM 1707 O OG1 . THR A 1 222 ? 17.076 35.074 65.817 1.00 48.66 ? 222 THR A OG1 1 ATOM 1708 C CG2 . THR A 1 222 ? 15.857 36.777 64.587 1.00 48.60 ? 222 THR A CG2 1 ATOM 1709 N N . TRP A 1 223 ? 17.926 37.610 68.486 1.00 40.19 ? 223 TRP A N 1 ATOM 1710 C CA . TRP A 1 223 ? 18.398 37.377 69.831 1.00 38.70 ? 223 TRP A CA 1 ATOM 1711 C C . TRP A 1 223 ? 17.565 36.301 70.419 1.00 41.49 ? 223 TRP A C 1 ATOM 1712 O O . TRP A 1 223 ? 16.374 36.241 70.158 1.00 44.42 ? 223 TRP A O 1 ATOM 1713 C CB . TRP A 1 223 ? 18.277 38.654 70.640 1.00 38.40 ? 223 TRP A CB 1 ATOM 1714 C CG . TRP A 1 223 ? 19.389 39.606 70.285 1.00 35.23 ? 223 TRP A CG 1 ATOM 1715 C CD1 . TRP A 1 223 ? 19.352 40.627 69.356 1.00 34.66 ? 223 TRP A CD1 1 ATOM 1716 C CD2 . TRP A 1 223 ? 20.705 39.601 70.831 1.00 32.41 ? 223 TRP A CD2 1 ATOM 1717 N NE1 . TRP A 1 223 ? 20.578 41.244 69.303 1.00 32.52 ? 223 TRP A NE1 1 ATOM 1718 C CE2 . TRP A 1 223 ? 21.420 40.641 70.206 1.00 31.39 ? 223 TRP A CE2 1 ATOM 1719 C CE3 . TRP A 1 223 ? 21.354 38.812 71.798 1.00 33.90 ? 223 TRP A CE3 1 ATOM 1720 C CZ2 . TRP A 1 223 ? 22.747 40.905 70.505 1.00 29.12 ? 223 TRP A CZ2 1 ATOM 1721 C CZ3 . TRP A 1 223 ? 22.680 39.088 72.094 1.00 33.04 ? 223 TRP A CZ3 1 ATOM 1722 C CH2 . TRP A 1 223 ? 23.359 40.099 71.445 1.00 28.91 ? 223 TRP A CH2 1 ATOM 1723 N N . LEU A 1 224 ? 18.188 35.432 71.202 1.00 41.34 ? 224 LEU A N 1 ATOM 1724 C CA . LEU A 1 224 ? 17.448 34.413 71.943 1.00 45.12 ? 224 LEU A CA 1 ATOM 1725 C C . LEU A 1 224 ? 17.611 34.681 73.442 1.00 45.83 ? 224 LEU A C 1 ATOM 1726 O O . LEU A 1 224 ? 18.720 34.990 73.899 1.00 41.88 ? 224 LEU A O 1 ATOM 1727 C CB . LEU A 1 224 ? 17.931 33.005 71.587 1.00 45.90 ? 224 LEU A CB 1 ATOM 1728 C CG . LEU A 1 224 ? 17.945 32.550 70.116 1.00 45.97 ? 224 LEU A CG 1 ATOM 1729 C CD1 . LEU A 1 224 ? 18.921 31.396 69.968 1.00 46.81 ? 224 LEU A CD1 1 ATOM 1730 C CD2 . LEU A 1 224 ? 16.591 32.142 69.659 1.00 47.59 ? 224 LEU A CD2 1 ATOM 1731 N N . ARG A 1 225 ? 16.493 34.632 74.167 1.00 49.52 ? 225 ARG A N 1 ATOM 1732 C CA . ARG A 1 225 ? 16.471 34.772 75.630 1.00 53.46 ? 225 ARG A CA 1 ATOM 1733 C C . ARG A 1 225 ? 16.032 33.403 76.160 1.00 58.62 ? 225 ARG A C 1 ATOM 1734 O O . ARG A 1 225 ? 14.923 32.937 75.863 1.00 62.08 ? 225 ARG A O 1 ATOM 1735 C CB . ARG A 1 225 ? 15.508 35.891 76.061 1.00 54.58 ? 225 ARG A CB 1 ATOM 1736 C CG . ARG A 1 225 ? 15.255 35.993 77.556 1.00 58.54 ? 225 ARG A CG 1 ATOM 1737 C CD . ARG A 1 225 ? 14.130 36.988 77.898 1.00 62.00 ? 225 ARG A CD 1 ATOM 1738 N NE . ARG A 1 225 ? 14.400 38.356 77.426 1.00 64.57 ? 225 ARG A NE 1 ATOM 1739 C CZ . ARG A 1 225 ? 13.612 39.046 76.594 1.00 65.98 ? 225 ARG A CZ 1 ATOM 1740 N NH1 . ARG A 1 225 ? 12.480 38.514 76.135 1.00 69.88 ? 225 ARG A NH1 1 ATOM 1741 N NH2 . ARG A 1 225 ? 13.952 40.280 76.225 1.00 63.00 ? 225 ARG A NH2 1 ATOM 1742 N N . ASP A 1 226 ? 16.941 32.750 76.884 1.00 59.54 ? 226 ASP A N 1 ATOM 1743 C CA . ASP A 1 226 ? 16.844 31.320 77.227 1.00 64.87 ? 226 ASP A CA 1 ATOM 1744 C C . ASP A 1 226 ? 16.603 30.336 76.070 1.00 66.67 ? 226 ASP A C 1 ATOM 1745 O O . ASP A 1 226 ? 16.245 29.188 76.297 1.00 71.97 ? 226 ASP A O 1 ATOM 1746 C CB . ASP A 1 226 ? 15.893 31.128 78.401 1.00 69.90 ? 226 ASP A CB 1 ATOM 1747 C CG . ASP A 1 226 ? 16.414 31.828 79.642 1.00 70.27 ? 226 ASP A CG 1 ATOM 1748 O OD1 . ASP A 1 226 ? 17.682 31.800 79.802 1.00 68.75 ? 226 ASP A OD1 1 ATOM 1749 O OD2 . ASP A 1 226 ? 15.606 32.432 80.417 1.00 74.79 ? 226 ASP A OD2 1 ATOM 1750 N N . GLY A 1 227 ? 16.863 30.782 74.844 1.00 63.08 ? 227 GLY A N 1 ATOM 1751 C CA . GLY A 1 227 ? 16.780 29.934 73.652 1.00 64.49 ? 227 GLY A CA 1 ATOM 1752 C C . GLY A 1 227 ? 15.518 30.149 72.831 1.00 66.52 ? 227 GLY A C 1 ATOM 1753 O O . GLY A 1 227 ? 15.336 29.520 71.776 1.00 67.41 ? 227 GLY A O 1 ATOM 1754 N N . ARG A 1 228 ? 14.643 31.022 73.334 1.00 67.31 ? 228 ARG A N 1 ATOM 1755 C CA . ARG A 1 228 ? 13.454 31.478 72.616 1.00 68.61 ? 228 ARG A CA 1 ATOM 1756 C C . ARG A 1 228 ? 13.685 32.861 71.992 1.00 63.62 ? 228 ARG A C 1 ATOM 1757 O O . ARG A 1 228 ? 14.271 33.734 72.626 1.00 59.36 ? 228 ARG A O 1 ATOM 1758 C CB . ARG A 1 228 ? 12.258 31.530 73.575 1.00 73.97 ? 228 ARG A CB 1 ATOM 1759 N N . GLU A 1 229 ? 13.199 33.070 70.772 1.00 63.52 ? 229 GLU A N 1 ATOM 1760 C CA . GLU A 1 229 ? 13.369 34.358 70.096 1.00 61.82 ? 229 GLU A CA 1 ATOM 1761 C C . GLU A 1 229 ? 12.773 35.551 70.845 1.00 61.96 ? 229 GLU A C 1 ATOM 1762 O O . GLU A 1 229 ? 11.619 35.528 71.245 1.00 67.50 ? 229 GLU A O 1 ATOM 1763 C CB . GLU A 1 229 ? 12.829 34.317 68.653 1.00 62.65 ? 229 GLU A CB 1 ATOM 1764 C CG . GLU A 1 229 ? 13.079 35.609 67.869 1.00 60.89 ? 229 GLU A CG 1 ATOM 1765 C CD . GLU A 1 229 ? 12.525 35.595 66.441 1.00 63.75 ? 229 GLU A CD 1 ATOM 1766 O OE1 . GLU A 1 229 ? 11.927 34.578 66.014 1.00 71.21 ? 229 GLU A OE1 1 ATOM 1767 O OE2 . GLU A 1 229 ? 12.698 36.613 65.732 1.00 66.45 ? 229 GLU A OE2 1 ATOM 1768 N N . VAL A 1 230 ? 13.581 36.594 71.023 1.00 57.94 ? 230 VAL A N 1 ATOM 1769 C CA . VAL A 1 230 ? 13.113 37.854 71.575 1.00 58.62 ? 230 VAL A CA 1 ATOM 1770 C C . VAL A 1 230 ? 12.284 38.546 70.498 1.00 60.80 ? 230 VAL A C 1 ATOM 1771 O O . VAL A 1 230 ? 12.809 38.857 69.426 1.00 58.20 ? 230 VAL A O 1 ATOM 1772 C CB . VAL A 1 230 ? 14.286 38.791 72.010 1.00 53.94 ? 230 VAL A CB 1 ATOM 1773 C CG1 . VAL A 1 230 ? 13.758 40.112 72.548 1.00 55.08 ? 230 VAL A CG1 1 ATOM 1774 C CG2 . VAL A 1 230 ? 15.155 38.121 73.044 1.00 51.36 ? 230 VAL A CG2 1 ATOM 1775 N N . PRO A 1 231 ? 10.991 38.802 70.784 1.00 66.52 ? 231 PRO A N 1 ATOM 1776 C CA . PRO A 1 231 ? 10.153 39.522 69.834 1.00 69.45 ? 231 PRO A CA 1 ATOM 1777 C C . PRO A 1 231 ? 10.613 40.976 69.726 1.00 67.32 ? 231 PRO A C 1 ATOM 1778 O O . PRO A 1 231 ? 11.350 41.435 70.602 1.00 64.74 ? 231 PRO A O 1 ATOM 1779 C CB . PRO A 1 231 ? 8.759 39.436 70.472 1.00 76.05 ? 231 PRO A CB 1 ATOM 1780 C CG . PRO A 1 231 ? 9.042 39.331 71.930 1.00 76.10 ? 231 PRO A CG 1 ATOM 1781 C CD . PRO A 1 231 ? 10.243 38.447 72.006 1.00 70.73 ? 231 PRO A CD 1 ATOM 1782 N N . PRO A 1 232 ? 10.154 41.714 68.693 1.00 69.28 ? 232 PRO A N 1 ATOM 1783 C CA . PRO A 1 232 ? 10.678 43.066 68.568 1.00 67.46 ? 232 PRO A CA 1 ATOM 1784 C C . PRO A 1 232 ? 9.972 44.005 69.549 1.00 71.66 ? 232 PRO A C 1 ATOM 1785 O O . PRO A 1 232 ? 8.761 43.923 69.741 1.00 76.97 ? 232 PRO A O 1 ATOM 1786 C CB . PRO A 1 232 ? 10.360 43.452 67.114 1.00 69.23 ? 232 PRO A CB 1 ATOM 1787 C CG . PRO A 1 232 ? 9.528 42.299 66.526 1.00 72.27 ? 232 PRO A CG 1 ATOM 1788 C CD . PRO A 1 232 ? 9.118 41.432 67.677 1.00 73.84 ? 232 PRO A CD 1 ATOM 1789 N N . SER A 1 233 ? 10.768 44.864 70.176 1.00 69.15 ? 233 SER A N 1 ATOM 1790 C CA . SER A 1 233 ? 10.320 45.887 71.095 1.00 71.77 ? 233 SER A CA 1 ATOM 1791 C C . SER A 1 233 ? 11.352 47.022 71.012 1.00 68.30 ? 233 SER A C 1 ATOM 1792 O O . SER A 1 233 ? 12.370 46.873 70.315 1.00 64.73 ? 233 SER A O 1 ATOM 1793 C CB . SER A 1 233 ? 10.243 45.298 72.504 1.00 72.68 ? 233 SER A CB 1 ATOM 1794 O OG . SER A 1 233 ? 11.493 44.769 72.902 1.00 67.72 ? 233 SER A OG 1 ATOM 1795 N N . PRO A 1 234 ? 11.102 48.159 71.696 1.00 71.17 ? 234 PRO A N 1 ATOM 1796 C CA . PRO A 1 234 ? 12.121 49.203 71.829 1.00 68.43 ? 234 PRO A CA 1 ATOM 1797 C C . PRO A 1 234 ? 13.474 48.680 72.359 1.00 62.21 ? 234 PRO A C 1 ATOM 1798 O O . PRO A 1 234 ? 14.498 49.289 72.093 1.00 60.34 ? 234 PRO A O 1 ATOM 1799 C CB . PRO A 1 234 ? 11.499 50.167 72.842 1.00 72.94 ? 234 PRO A CB 1 ATOM 1800 C CG . PRO A 1 234 ? 10.044 49.995 72.684 1.00 79.13 ? 234 PRO A CG 1 ATOM 1801 C CD . PRO A 1 234 ? 9.847 48.542 72.377 1.00 77.13 ? 234 PRO A CD 1 ATOM 1802 N N . ALA A 1 235 ? 13.465 47.558 73.075 1.00 59.70 ? 235 ALA A N 1 ATOM 1803 C CA . ALA A 1 235 ? 14.670 46.951 73.611 1.00 54.90 ? 235 ALA A CA 1 ATOM 1804 C C . ALA A 1 235 ? 15.607 46.418 72.526 1.00 50.67 ? 235 ALA A C 1 ATOM 1805 O O . ALA A 1 235 ? 16.802 46.322 72.746 1.00 46.83 ? 235 ALA A O 1 ATOM 1806 C CB . ALA A 1 235 ? 14.312 45.834 74.571 1.00 54.59 ? 235 ALA A CB 1 ATOM 1807 N N . LEU A 1 236 ? 15.055 46.079 71.363 1.00 52.10 ? 236 LEU A N 1 ATOM 1808 C CA . LEU A 1 236 ? 15.796 45.362 70.319 1.00 49.45 ? 236 LEU A CA 1 ATOM 1809 C C . LEU A 1 236 ? 15.992 46.260 69.098 1.00 50.43 ? 236 LEU A C 1 ATOM 1810 O O . LEU A 1 236 ? 15.035 46.800 68.551 1.00 53.85 ? 236 LEU A O 1 ATOM 1811 C CB . LEU A 1 236 ? 15.023 44.090 69.919 1.00 50.43 ? 236 LEU A CB 1 ATOM 1812 C CG . LEU A 1 236 ? 15.714 42.828 69.379 1.00 47.33 ? 236 LEU A CG 1 ATOM 1813 C CD1 . LEU A 1 236 ? 14.650 42.002 68.706 1.00 52.96 ? 236 LEU A CD1 1 ATOM 1814 C CD2 . LEU A 1 236 ? 16.766 43.133 68.405 1.00 43.26 ? 236 LEU A CD2 1 ATOM 1815 N N . SER A 1 237 ? 17.231 46.425 68.667 1.00 48.13 ? 237 SER A N 1 ATOM 1816 C CA . SER A 1 237 ? 17.502 47.173 67.455 1.00 49.83 ? 237 SER A CA 1 ATOM 1817 C C . SER A 1 237 ? 18.405 46.347 66.544 1.00 47.21 ? 237 SER A C 1 ATOM 1818 O O . SER A 1 237 ? 19.469 45.904 66.942 1.00 43.21 ? 237 SER A O 1 ATOM 1819 C CB . SER A 1 237 ? 18.151 48.523 67.792 1.00 51.38 ? 237 SER A CB 1 ATOM 1820 O OG . SER A 1 237 ? 18.699 49.153 66.630 1.00 53.14 ? 237 SER A OG 1 ATOM 1821 N N . THR A 1 238 ? 17.957 46.100 65.324 1.00 49.19 ? 238 THR A N 1 ATOM 1822 C CA . THR A 1 238 ? 18.873 45.511 64.366 1.00 48.68 ? 238 THR A CA 1 ATOM 1823 C C . THR A 1 238 ? 19.247 46.596 63.382 1.00 49.48 ? 238 THR A C 1 ATOM 1824 O O . THR A 1 238 ? 18.376 47.320 62.879 1.00 54.24 ? 238 THR A O 1 ATOM 1825 C CB . THR A 1 238 ? 18.339 44.236 63.713 1.00 48.60 ? 238 THR A CB 1 ATOM 1826 O OG1 . THR A 1 238 ? 19.241 43.838 62.657 1.00 48.56 ? 238 THR A OG1 1 ATOM 1827 C CG2 . THR A 1 238 ? 16.893 44.429 63.193 1.00 54.00 ? 238 THR A CG2 1 ATOM 1828 N N . GLY A 1 239 ? 20.548 46.774 63.194 1.00 47.16 ? 239 GLY A N 1 ATOM 1829 C CA . GLY A 1 239 ? 21.049 47.858 62.371 1.00 47.67 ? 239 GLY A CA 1 ATOM 1830 C C . GLY A 1 239 ? 20.858 47.575 60.894 1.00 47.50 ? 239 GLY A C 1 ATOM 1831 O O . GLY A 1 239 ? 20.269 46.557 60.487 1.00 47.11 ? 239 GLY A O 1 ATOM 1832 N N . THR A 1 240 ? 21.375 48.496 60.093 1.00 47.77 ? 240 THR A N 1 ATOM 1833 C CA . THR A 1 240 ? 21.305 48.404 58.658 1.00 47.53 ? 240 THR A CA 1 ATOM 1834 C C . THR A 1 240 ? 22.568 47.665 58.240 1.00 42.08 ? 240 THR A C 1 ATOM 1835 O O . THR A 1 240 ? 23.562 47.661 58.973 1.00 39.55 ? 240 THR A O 1 ATOM 1836 C CB . THR A 1 240 ? 21.224 49.812 58.034 1.00 50.91 ? 240 THR A CB 1 ATOM 1837 O OG1 . THR A 1 240 ? 20.091 50.503 58.573 1.00 59.59 ? 240 THR A OG1 1 ATOM 1838 C CG2 . THR A 1 240 ? 21.046 49.753 56.541 1.00 54.67 ? 240 THR A CG2 1 ATOM 1839 N N . VAL A 1 241 ? 22.500 46.999 57.098 1.00 40.28 ? 241 VAL A N 1 ATOM 1840 C CA . VAL A 1 241 ? 23.626 46.257 56.574 1.00 36.29 ? 241 VAL A CA 1 ATOM 1841 C C . VAL A 1 241 ? 24.600 47.267 55.958 1.00 36.09 ? 241 VAL A C 1 ATOM 1842 O O . VAL A 1 241 ? 24.165 48.235 55.334 1.00 39.05 ? 241 VAL A O 1 ATOM 1843 C CB . VAL A 1 241 ? 23.146 45.223 55.539 1.00 37.43 ? 241 VAL A CB 1 ATOM 1844 C CG1 . VAL A 1 241 ? 24.290 44.477 54.971 1.00 33.27 ? 241 VAL A CG1 1 ATOM 1845 C CG2 . VAL A 1 241 ? 22.180 44.199 56.208 1.00 38.06 ? 241 VAL A CG2 1 ATOM 1846 N N . LEU A 1 242 ? 25.905 47.065 56.161 1.00 31.74 ? 242 LEU A N 1 ATOM 1847 C CA . LEU A 1 242 ? 26.928 48.028 55.710 1.00 31.93 ? 242 LEU A CA 1 ATOM 1848 C C . LEU A 1 242 ? 27.841 47.318 54.754 1.00 28.96 ? 242 LEU A C 1 ATOM 1849 O O . LEU A 1 242 ? 28.128 46.154 54.978 1.00 25.82 ? 242 LEU A O 1 ATOM 1850 C CB . LEU A 1 242 ? 27.773 48.517 56.899 1.00 32.46 ? 242 LEU A CB 1 ATOM 1851 C CG . LEU A 1 242 ? 27.129 49.115 58.156 1.00 33.92 ? 242 LEU A CG 1 ATOM 1852 C CD1 . LEU A 1 242 ? 28.081 48.977 59.333 1.00 35.68 ? 242 LEU A CD1 1 ATOM 1853 C CD2 . LEU A 1 242 ? 26.724 50.542 57.964 1.00 37.46 ? 242 LEU A CD2 1 ATOM 1854 N N . PRO A 1 243 ? 28.314 48.008 53.703 1.00 30.65 ? 243 PRO A N 1 ATOM 1855 C CA . PRO A 1 243 ? 29.217 47.345 52.762 1.00 30.18 ? 243 PRO A CA 1 ATOM 1856 C C . PRO A 1 243 ? 30.697 47.401 53.180 1.00 33.03 ? 243 PRO A C 1 ATOM 1857 O O . PRO A 1 243 ? 31.167 48.387 53.766 1.00 34.10 ? 243 PRO A O 1 ATOM 1858 C CB . PRO A 1 243 ? 29.044 48.176 51.480 1.00 32.74 ? 243 PRO A CB 1 ATOM 1859 C CG . PRO A 1 243 ? 28.731 49.552 51.937 1.00 33.41 ? 243 PRO A CG 1 ATOM 1860 C CD . PRO A 1 243 ? 28.020 49.402 53.292 1.00 33.31 ? 243 PRO A CD 1 ATOM 1861 N N . ASN A 1 244 ? 31.413 46.338 52.831 1.00 34.47 ? 244 ASN A N 1 ATOM 1862 C CA . ASN A 1 244 ? 32.882 46.284 52.807 1.00 36.98 ? 244 ASN A CA 1 ATOM 1863 C C . ASN A 1 244 ? 33.395 46.508 51.374 1.00 39.28 ? 244 ASN A C 1 ATOM 1864 O O . ASN A 1 244 ? 32.649 46.318 50.425 1.00 39.81 ? 244 ASN A O 1 ATOM 1865 C CB . ASN A 1 244 ? 33.293 44.897 53.322 1.00 35.40 ? 244 ASN A CB 1 ATOM 1866 C CG . ASN A 1 244 ? 32.830 44.641 54.757 1.00 34.52 ? 244 ASN A CG 1 ATOM 1867 O OD1 . ASN A 1 244 ? 32.882 45.527 55.594 1.00 40.16 ? 244 ASN A OD1 1 ATOM 1868 N ND2 . ASN A 1 244 ? 32.410 43.409 55.048 1.00 34.42 ? 244 ASN A ND2 1 ATOM 1869 N N . ALA A 1 245 ? 34.648 46.946 51.195 1.00 43.57 ? 245 ALA A N 1 ATOM 1870 C CA . ALA A 1 245 ? 35.197 47.162 49.858 1.00 46.56 ? 245 ALA A CA 1 ATOM 1871 C C . ALA A 1 245 ? 35.260 45.896 48.995 1.00 45.89 ? 245 ALA A C 1 ATOM 1872 O O . ALA A 1 245 ? 35.310 45.980 47.754 1.00 48.35 ? 245 ALA A O 1 ATOM 1873 C CB . ALA A 1 245 ? 36.587 47.808 49.941 1.00 51.49 ? 245 ALA A CB 1 ATOM 1874 N N . ASP A 1 246 ? 35.230 44.731 49.632 1.00 42.80 ? 246 ASP A N 1 ATOM 1875 C CA . ASP A 1 246 ? 35.443 43.457 48.910 1.00 43.15 ? 246 ASP A CA 1 ATOM 1876 C C . ASP A 1 246 ? 34.145 42.752 48.512 1.00 39.32 ? 246 ASP A C 1 ATOM 1877 O O . ASP A 1 246 ? 34.117 41.536 48.355 1.00 37.85 ? 246 ASP A O 1 ATOM 1878 C CB . ASP A 1 246 ? 36.343 42.517 49.742 1.00 42.94 ? 246 ASP A CB 1 ATOM 1879 C CG . ASP A 1 246 ? 35.722 42.093 51.084 1.00 43.93 ? 246 ASP A CG 1 ATOM 1880 O OD1 . ASP A 1 246 ? 34.683 42.640 51.536 1.00 43.83 ? 246 ASP A OD1 1 ATOM 1881 O OD2 . ASP A 1 246 ? 36.276 41.154 51.705 1.00 47.46 ? 246 ASP A OD2 1 ATOM 1882 N N . LEU A 1 247 ? 33.067 43.519 48.376 1.00 38.12 ? 247 LEU A N 1 ATOM 1883 C CA . LEU A 1 247 ? 31.731 42.973 48.177 1.00 35.64 ? 247 LEU A CA 1 ATOM 1884 C C . LEU A 1 247 ? 31.409 41.889 49.211 1.00 32.32 ? 247 LEU A C 1 ATOM 1885 O O . LEU A 1 247 ? 31.038 40.779 48.844 1.00 31.90 ? 247 LEU A O 1 ATOM 1886 C CB . LEU A 1 247 ? 31.554 42.414 46.743 1.00 37.19 ? 247 LEU A CB 1 ATOM 1887 C CG . LEU A 1 247 ? 30.129 42.278 46.200 1.00 37.19 ? 247 LEU A CG 1 ATOM 1888 C CD1 . LEU A 1 247 ? 29.318 43.548 46.449 1.00 40.58 ? 247 LEU A CD1 1 ATOM 1889 C CD2 . LEU A 1 247 ? 30.136 41.963 44.722 1.00 38.96 ? 247 LEU A CD2 1 ATOM 1890 N N . THR A 1 248 ? 31.587 42.206 50.494 1.00 30.01 ? 248 THR A N 1 ATOM 1891 C CA . THR A 1 248 ? 30.960 41.457 51.586 1.00 26.87 ? 248 THR A CA 1 ATOM 1892 C C . THR A 1 248 ? 30.190 42.491 52.451 1.00 26.52 ? 248 THR A C 1 ATOM 1893 O O . THR A 1 248 ? 30.256 43.686 52.196 1.00 28.80 ? 248 THR A O 1 ATOM 1894 C CB . THR A 1 248 ? 31.943 40.704 52.457 1.00 26.59 ? 248 THR A CB 1 ATOM 1895 O OG1 . THR A 1 248 ? 32.871 41.623 53.001 1.00 29.38 ? 248 THR A OG1 1 ATOM 1896 C CG2 . THR A 1 248 ? 32.700 39.583 51.695 1.00 27.34 ? 248 THR A CG2 1 ATOM 1897 N N . TYR A 1 249 ? 29.455 42.046 53.461 1.00 24.55 ? 249 TYR A N 1 ATOM 1898 C CA . TYR A 1 249 ? 28.620 42.971 54.237 1.00 25.05 ? 249 TYR A CA 1 ATOM 1899 C C . TYR A 1 249 ? 28.821 42.750 55.738 1.00 24.35 ? 249 TYR A C 1 ATOM 1900 O O . TYR A 1 249 ? 29.400 41.763 56.127 1.00 23.37 ? 249 TYR A O 1 ATOM 1901 C CB . TYR A 1 249 ? 27.137 42.786 53.869 1.00 25.10 ? 249 TYR A CB 1 ATOM 1902 C CG . TYR A 1 249 ? 26.816 43.161 52.427 1.00 26.88 ? 249 TYR A CG 1 ATOM 1903 C CD1 . TYR A 1 249 ? 26.511 44.481 52.085 1.00 25.65 ? 249 TYR A CD1 1 ATOM 1904 C CD2 . TYR A 1 249 ? 26.843 42.194 51.417 1.00 25.47 ? 249 TYR A CD2 1 ATOM 1905 C CE1 . TYR A 1 249 ? 26.218 44.825 50.785 1.00 31.30 ? 249 TYR A CE1 1 ATOM 1906 C CE2 . TYR A 1 249 ? 26.559 42.535 50.085 1.00 28.42 ? 249 TYR A CE2 1 ATOM 1907 C CZ . TYR A 1 249 ? 26.259 43.850 49.787 1.00 29.92 ? 249 TYR A CZ 1 ATOM 1908 O OH . TYR A 1 249 ? 25.953 44.233 48.513 1.00 34.51 ? 249 TYR A OH 1 ATOM 1909 N N . GLN A 1 250 ? 28.326 43.690 56.555 1.00 25.77 ? 250 GLN A N 1 ATOM 1910 C CA . GLN A 1 250 ? 28.443 43.679 57.996 1.00 25.73 ? 250 GLN A CA 1 ATOM 1911 C C . GLN A 1 250 ? 27.139 44.263 58.586 1.00 26.72 ? 250 GLN A C 1 ATOM 1912 O O . GLN A 1 250 ? 26.545 45.128 57.999 1.00 26.08 ? 250 GLN A O 1 ATOM 1913 C CB . GLN A 1 250 ? 29.496 44.710 58.375 1.00 28.82 ? 250 GLN A CB 1 ATOM 1914 C CG . GLN A 1 250 ? 30.699 44.116 58.899 1.00 31.87 ? 250 GLN A CG 1 ATOM 1915 C CD . GLN A 1 250 ? 31.696 45.140 59.323 1.00 32.45 ? 250 GLN A CD 1 ATOM 1916 O OE1 . GLN A 1 250 ? 32.608 45.499 58.564 1.00 35.73 ? 250 GLN A OE1 1 ATOM 1917 N NE2 . GLN A 1 250 ? 31.567 45.588 60.550 1.00 34.07 ? 250 GLN A NE2 1 ATOM 1918 N N . LEU A 1 251 ? 26.760 43.844 59.780 1.00 26.46 ? 251 LEU A N 1 ATOM 1919 C CA . LEU A 1 251 ? 25.503 44.281 60.412 1.00 28.11 ? 251 LEU A CA 1 ATOM 1920 C C . LEU A 1 251 ? 25.798 44.200 61.907 1.00 28.56 ? 251 LEU A C 1 ATOM 1921 O O . LEU A 1 251 ? 26.596 43.348 62.340 1.00 27.16 ? 251 LEU A O 1 ATOM 1922 C CB . LEU A 1 251 ? 24.375 43.251 60.078 1.00 29.23 ? 251 LEU A CB 1 ATOM 1923 C CG . LEU A 1 251 ? 22.926 43.464 60.501 1.00 31.86 ? 251 LEU A CG 1 ATOM 1924 C CD1 . LEU A 1 251 ? 22.077 42.530 59.656 1.00 38.26 ? 251 LEU A CD1 1 ATOM 1925 C CD2 . LEU A 1 251 ? 22.750 43.071 61.932 1.00 37.97 ? 251 LEU A CD2 1 ATOM 1926 N N . ARG A 1 252 ? 25.149 45.059 62.685 1.00 30.19 ? 252 ARG A N 1 ATOM 1927 C CA . ARG A 1 252 ? 25.204 45.017 64.143 1.00 31.45 ? 252 ARG A CA 1 ATOM 1928 C C . ARG A 1 252 ? 23.749 44.909 64.631 1.00 31.07 ? 252 ARG A C 1 ATOM 1929 O O . ARG A 1 252 ? 22.898 45.695 64.178 1.00 31.33 ? 252 ARG A O 1 ATOM 1930 C CB . ARG A 1 252 ? 25.772 46.356 64.610 1.00 33.35 ? 252 ARG A CB 1 ATOM 1931 C CG . ARG A 1 252 ? 26.973 46.339 65.564 1.00 36.48 ? 252 ARG A CG 1 ATOM 1932 C CD . ARG A 1 252 ? 27.467 47.833 65.765 1.00 39.08 ? 252 ARG A CD 1 ATOM 1933 N NE . ARG A 1 252 ? 27.546 48.237 67.181 1.00 48.56 ? 252 ARG A NE 1 ATOM 1934 C CZ . ARG A 1 252 ? 26.582 48.872 67.862 1.00 50.62 ? 252 ARG A CZ 1 ATOM 1935 N NH1 . ARG A 1 252 ? 25.422 49.182 67.281 1.00 52.94 ? 252 ARG A NH1 1 ATOM 1936 N NH2 . ARG A 1 252 ? 26.781 49.201 69.133 1.00 50.55 ? 252 ARG A NH2 1 ATOM 1937 N N . SER A 1 253 ? 23.454 43.959 65.528 1.00 28.88 ? 253 SER A N 1 ATOM 1938 C CA . SER A 1 253 ? 22.140 43.910 66.183 1.00 30.84 ? 253 SER A CA 1 ATOM 1939 C C . SER A 1 253 ? 22.349 44.147 67.671 1.00 30.68 ? 253 SER A C 1 ATOM 1940 O O . SER A 1 253 ? 23.368 43.737 68.189 1.00 29.87 ? 253 SER A O 1 ATOM 1941 C CB . SER A 1 253 ? 21.460 42.558 65.969 1.00 30.90 ? 253 SER A CB 1 ATOM 1942 O OG . SER A 1 253 ? 20.171 42.580 66.598 1.00 37.34 ? 253 SER A OG 1 ATOM 1943 N N . THR A 1 254 ? 21.425 44.839 68.348 1.00 31.79 ? 254 THR A N 1 ATOM 1944 C CA . THR A 1 254 ? 21.623 45.094 69.771 1.00 31.27 ? 254 THR A CA 1 ATOM 1945 C C . THR A 1 254 ? 20.358 44.846 70.543 1.00 32.90 ? 254 THR A C 1 ATOM 1946 O O . THR A 1 254 ? 19.246 45.036 69.997 1.00 34.60 ? 254 THR A O 1 ATOM 1947 C CB . THR A 1 254 ? 22.103 46.553 70.093 1.00 32.52 ? 254 THR A CB 1 ATOM 1948 O OG1 . THR A 1 254 ? 21.069 47.493 69.815 1.00 36.12 ? 254 THR A OG1 1 ATOM 1949 C CG2 . THR A 1 254 ? 23.384 46.946 69.334 1.00 29.14 ? 254 THR A CG2 1 ATOM 1950 N N . LEU A 1 255 ? 20.527 44.450 71.810 1.00 31.70 ? 255 LEU A N 1 ATOM 1951 C CA . LEU A 1 255 ? 19.416 44.183 72.719 1.00 32.67 ? 255 LEU A CA 1 ATOM 1952 C C . LEU A 1 255 ? 19.716 44.831 74.064 1.00 33.56 ? 255 LEU A C 1 ATOM 1953 O O . LEU A 1 255 ? 20.745 44.523 74.677 1.00 31.95 ? 255 LEU A O 1 ATOM 1954 C CB . LEU A 1 255 ? 19.224 42.679 72.923 1.00 31.57 ? 255 LEU A CB 1 ATOM 1955 C CG . LEU A 1 255 ? 18.057 42.220 73.821 1.00 36.83 ? 255 LEU A CG 1 ATOM 1956 C CD1 . LEU A 1 255 ? 16.726 42.621 73.211 1.00 38.42 ? 255 LEU A CD1 1 ATOM 1957 C CD2 . LEU A 1 255 ? 18.097 40.725 74.099 1.00 37.37 ? 255 LEU A CD2 1 ATOM 1958 N N . LEU A 1 256 ? 18.837 45.715 74.530 1.00 35.96 ? 256 LEU A N 1 ATOM 1959 C CA . LEU A 1 256 ? 18.933 46.189 75.919 1.00 38.52 ? 256 LEU A CA 1 ATOM 1960 C C . LEU A 1 256 ? 18.425 45.151 76.925 1.00 40.45 ? 256 LEU A C 1 ATOM 1961 O O . LEU A 1 256 ? 17.342 44.597 76.759 1.00 42.61 ? 256 LEU A O 1 ATOM 1962 C CB . LEU A 1 256 ? 18.213 47.518 76.112 1.00 41.58 ? 256 LEU A CB 1 ATOM 1963 C CG . LEU A 1 256 ? 18.860 48.692 75.367 1.00 43.25 ? 256 LEU A CG 1 ATOM 1964 C CD1 . LEU A 1 256 ? 17.815 49.751 74.979 1.00 49.14 ? 256 LEU A CD1 1 ATOM 1965 C CD2 . LEU A 1 256 ? 19.938 49.331 76.230 1.00 43.57 ? 256 LEU A CD2 1 ATOM 1966 N N . VAL A 1 257 ? 19.229 44.872 77.952 1.00 39.93 ? 257 VAL A N 1 ATOM 1967 C CA . VAL A 1 257 ? 18.841 43.949 79.008 1.00 42.83 ? 257 VAL A CA 1 ATOM 1968 C C . VAL A 1 257 ? 19.140 44.563 80.381 1.00 45.55 ? 257 VAL A C 1 ATOM 1969 O O . VAL A 1 257 ? 19.942 45.489 80.489 1.00 43.97 ? 257 VAL A O 1 ATOM 1970 C CB . VAL A 1 257 ? 19.550 42.581 78.848 1.00 41.04 ? 257 VAL A CB 1 ATOM 1971 C CG1 . VAL A 1 257 ? 19.239 41.963 77.475 1.00 36.88 ? 257 VAL A CG1 1 ATOM 1972 C CG2 . VAL A 1 257 ? 21.075 42.725 79.024 1.00 39.45 ? 257 VAL A CG2 1 ATOM 1973 N N . SER A 1 258 ? 18.488 44.054 81.420 1.00 50.68 ? 258 SER A N 1 ATOM 1974 C CA . SER A 1 258 ? 18.824 44.407 82.797 1.00 54.35 ? 258 SER A CA 1 ATOM 1975 C C . SER A 1 258 ? 19.996 43.531 83.263 1.00 54.59 ? 258 SER A C 1 ATOM 1976 O O . SER A 1 258 ? 20.051 42.357 82.931 1.00 54.51 ? 258 SER A O 1 ATOM 1977 C CB . SER A 1 258 ? 17.616 44.179 83.711 1.00 58.88 ? 258 SER A CB 1 ATOM 1978 O OG . SER A 1 258 ? 16.837 45.353 83.844 1.00 62.24 ? 258 SER A OG 1 ATOM 1979 N N . PRO A 1 259 ? 20.953 44.100 84.011 1.00 56.21 ? 259 PRO A N 1 ATOM 1980 C CA . PRO A 1 259 ? 22.016 43.256 84.566 1.00 56.91 ? 259 PRO A CA 1 ATOM 1981 C C . PRO A 1 259 ? 21.501 42.244 85.604 1.00 61.03 ? 259 PRO A C 1 ATOM 1982 O O . PRO A 1 259 ? 20.532 42.515 86.332 1.00 62.97 ? 259 PRO A O 1 ATOM 1983 C CB . PRO A 1 259 ? 22.952 44.266 85.235 1.00 57.27 ? 259 PRO A CB 1 ATOM 1984 C CG . PRO A 1 259 ? 22.089 45.448 85.524 1.00 58.84 ? 259 PRO A CG 1 ATOM 1985 C CD . PRO A 1 259 ? 21.130 45.517 84.376 1.00 57.09 ? 259 PRO A CD 1 ATOM 1986 N N . GLN A 1 260 ? 22.160 41.085 85.644 1.00 62.02 ? 260 GLN A N 1 ATOM 1987 C CA . GLN A 1 260 ? 21.832 39.988 86.564 1.00 66.32 ? 260 GLN A CA 1 ATOM 1988 C C . GLN A 1 260 ? 20.348 39.577 86.548 1.00 68.44 ? 260 GLN A C 1 ATOM 1989 O O . GLN A 1 260 ? 19.769 39.264 87.600 1.00 72.11 ? 260 GLN A O 1 ATOM 1990 C CB . GLN A 1 260 ? 22.277 40.329 87.995 1.00 69.07 ? 260 GLN A CB 1 ATOM 1991 C CG . GLN A 1 260 ? 23.782 40.479 88.184 1.00 69.84 ? 260 GLN A CG 1 ATOM 1992 C CD . GLN A 1 260 ? 24.114 41.143 89.507 1.00 73.56 ? 260 GLN A CD 1 ATOM 1993 O OE1 . GLN A 1 260 ? 23.645 42.254 89.793 1.00 76.34 ? 260 GLN A OE1 1 ATOM 1994 N NE2 . GLN A 1 260 ? 24.920 40.467 90.331 1.00 77.32 ? 260 GLN A NE2 1 ATOM 1995 N N . ASP A 1 261 ? 19.740 39.559 85.363 1.00 66.52 ? 261 ASP A N 1 ATOM 1996 C CA . ASP A 1 261 ? 18.305 39.268 85.275 1.00 68.73 ? 261 ASP A CA 1 ATOM 1997 C C . ASP A 1 261 ? 17.948 37.777 85.351 1.00 70.89 ? 261 ASP A C 1 ATOM 1998 O O . ASP A 1 261 ? 16.781 37.421 85.557 1.00 75.20 ? 261 ASP A O 1 ATOM 1999 C CB . ASP A 1 261 ? 17.643 39.984 84.084 1.00 67.09 ? 261 ASP A CB 1 ATOM 2000 C CG . ASP A 1 261 ? 18.131 39.491 82.730 1.00 63.58 ? 261 ASP A CG 1 ATOM 2001 O OD1 . ASP A 1 261 ? 18.972 38.564 82.672 1.00 63.14 ? 261 ASP A OD1 1 ATOM 2002 O OD2 . ASP A 1 261 ? 17.643 40.039 81.713 1.00 60.37 ? 261 ASP A OD2 1 ATOM 2003 N N . GLY A 1 262 ? 18.953 36.915 85.216 1.00 68.95 ? 262 GLY A N 1 ATOM 2004 C CA . GLY A 1 262 ? 18.747 35.465 85.337 1.00 71.14 ? 262 GLY A CA 1 ATOM 2005 C C . GLY A 1 262 ? 18.346 34.775 84.042 1.00 69.74 ? 262 GLY A C 1 ATOM 2006 O O . GLY A 1 262 ? 17.874 33.628 84.065 1.00 73.83 ? 262 GLY A O 1 ATOM 2007 N N . HIS A 1 263 ? 18.525 35.482 82.922 1.00 64.28 ? 263 HIS A N 1 ATOM 2008 C CA . HIS A 1 263 ? 18.322 34.939 81.593 1.00 61.65 ? 263 HIS A CA 1 ATOM 2009 C C . HIS A 1 263 ? 19.681 34.736 80.933 1.00 57.27 ? 263 HIS A C 1 ATOM 2010 O O . HIS A 1 263 ? 20.633 35.470 81.209 1.00 54.85 ? 263 HIS A O 1 ATOM 2011 C CB . HIS A 1 263 ? 17.472 35.892 80.733 1.00 60.19 ? 263 HIS A CB 1 ATOM 2012 C CG . HIS A 1 263 ? 16.106 36.167 81.290 1.00 64.78 ? 263 HIS A CG 1 ATOM 2013 N ND1 . HIS A 1 263 ? 15.635 37.445 81.514 1.00 65.29 ? 263 HIS A ND1 1 ATOM 2014 C CD2 . HIS A 1 263 ? 15.113 35.328 81.675 1.00 70.68 ? 263 HIS A CD2 1 ATOM 2015 C CE1 . HIS A 1 263 ? 14.415 37.381 82.017 1.00 71.48 ? 263 HIS A CE1 1 ATOM 2016 N NE2 . HIS A 1 263 ? 14.075 36.107 82.125 1.00 73.46 ? 263 HIS A NE2 1 ATOM 2017 N N . GLY A 1 264 ? 19.783 33.720 80.087 1.00 55.79 ? 264 GLY A N 1 ATOM 2018 C CA . GLY A 1 264 ? 20.963 33.539 79.266 1.00 51.92 ? 264 GLY A CA 1 ATOM 2019 C C . GLY A 1 264 ? 20.630 34.102 77.900 1.00 48.00 ? 264 GLY A C 1 ATOM 2020 O O . GLY A 1 264 ? 19.518 33.903 77.415 1.00 49.03 ? 264 GLY A O 1 ATOM 2021 N N . TYR A 1 265 ? 21.578 34.812 77.289 1.00 43.37 ? 265 TYR A N 1 ATOM 2022 C CA . TYR A 1 265 ? 21.393 35.389 75.961 1.00 40.62 ? 265 TYR A CA 1 ATOM 2023 C C . TYR A 1 265 ? 22.363 34.814 74.885 1.00 38.91 ? 265 TYR A C 1 ATOM 2024 O O . TYR A 1 265 ? 23.479 34.369 75.191 1.00 38.10 ? 265 TYR A O 1 ATOM 2025 C CB . TYR A 1 265 ? 21.474 36.935 76.022 1.00 37.33 ? 265 TYR A CB 1 ATOM 2026 C CG . TYR A 1 265 ? 20.332 37.542 76.832 1.00 39.76 ? 265 TYR A CG 1 ATOM 2027 C CD1 . TYR A 1 265 ? 20.474 37.808 78.191 1.00 38.78 ? 265 TYR A CD1 1 ATOM 2028 C CD2 . TYR A 1 265 ? 19.112 37.830 76.235 1.00 38.27 ? 265 TYR A CD2 1 ATOM 2029 C CE1 . TYR A 1 265 ? 19.431 38.360 78.924 1.00 42.37 ? 265 TYR A CE1 1 ATOM 2030 C CE2 . TYR A 1 265 ? 18.077 38.373 76.956 1.00 41.40 ? 265 TYR A CE2 1 ATOM 2031 C CZ . TYR A 1 265 ? 18.238 38.646 78.284 1.00 42.57 ? 265 TYR A CZ 1 ATOM 2032 O OH . TYR A 1 265 ? 17.184 39.173 78.977 1.00 49.40 ? 265 TYR A OH 1 ATOM 2033 N N . ALA A 1 266 ? 21.890 34.803 73.635 1.00 37.79 ? 266 ALA A N 1 ATOM 2034 C CA . ALA A 1 266 ? 22.685 34.422 72.471 1.00 36.21 ? 266 ALA A CA 1 ATOM 2035 C C . ALA A 1 266 ? 22.127 35.101 71.230 1.00 35.31 ? 266 ALA A C 1 ATOM 2036 O O . ALA A 1 266 ? 20.901 35.284 71.130 1.00 34.70 ? 266 ALA A O 1 ATOM 2037 C CB . ALA A 1 266 ? 22.654 32.906 72.263 1.00 39.97 ? 266 ALA A CB 1 ATOM 2038 N N . CYS A 1 267 ? 23.043 35.465 70.314 1.00 33.91 ? 267 CYS A N 1 ATOM 2039 C CA . CYS A 1 267 ? 22.744 35.950 68.967 1.00 31.86 ? 267 CYS A CA 1 ATOM 2040 C C . CYS A 1 267 ? 22.681 34.754 67.997 1.00 32.07 ? 267 CYS A C 1 ATOM 2041 O O . CYS A 1 267 ? 23.595 33.944 67.999 1.00 31.17 ? 267 CYS A O 1 ATOM 2042 C CB . CYS A 1 267 ? 23.900 36.882 68.540 1.00 30.14 ? 267 CYS A CB 1 ATOM 2043 S SG . CYS A 1 267 ? 23.584 37.684 67.007 1.00 36.90 ? 267 CYS A SG 1 ATOM 2044 N N . ARG A 1 268 ? 21.613 34.639 67.206 1.00 30.99 ? 268 ARG A N 1 ATOM 2045 C CA . ARG A 1 268 ? 21.507 33.616 66.189 1.00 33.55 ? 268 ARG A CA 1 ATOM 2046 C C . ARG A 1 268 ? 21.448 34.271 64.799 1.00 31.71 ? 268 ARG A C 1 ATOM 2047 O O . ARG A 1 268 ? 20.717 35.259 64.588 1.00 32.00 ? 268 ARG A O 1 ATOM 2048 C CB . ARG A 1 268 ? 20.289 32.706 66.439 1.00 36.35 ? 268 ARG A CB 1 ATOM 2049 C CG . ARG A 1 268 ? 20.170 31.557 65.395 1.00 41.21 ? 268 ARG A CG 1 ATOM 2050 C CD . ARG A 1 268 ? 19.340 30.389 65.842 1.00 46.13 ? 268 ARG A CD 1 ATOM 2051 N NE . ARG A 1 268 ? 17.907 30.681 65.837 1.00 55.75 ? 268 ARG A NE 1 ATOM 2052 C CZ . ARG A 1 268 ? 17.000 30.045 66.572 1.00 58.83 ? 268 ARG A CZ 1 ATOM 2053 N NH1 . ARG A 1 268 ? 17.330 29.037 67.376 1.00 62.93 ? 268 ARG A NH1 1 ATOM 2054 N NH2 . ARG A 1 268 ? 15.741 30.425 66.502 1.00 65.42 ? 268 ARG A NH2 1 ATOM 2055 N N . VAL A 1 269 ? 22.249 33.737 63.879 1.00 31.01 ? 269 VAL A N 1 ATOM 2056 C CA . VAL A 1 269 ? 22.408 34.299 62.525 1.00 29.24 ? 269 VAL A CA 1 ATOM 2057 C C . VAL A 1 269 ? 21.997 33.259 61.510 1.00 30.83 ? 269 VAL A C 1 ATOM 2058 O O . VAL A 1 269 ? 22.511 32.130 61.494 1.00 32.53 ? 269 VAL A O 1 ATOM 2059 C CB . VAL A 1 269 ? 23.857 34.749 62.225 1.00 27.72 ? 269 VAL A CB 1 ATOM 2060 C CG1 . VAL A 1 269 ? 23.900 35.549 60.957 1.00 26.34 ? 269 VAL A CG1 1 ATOM 2061 C CG2 . VAL A 1 269 ? 24.417 35.613 63.344 1.00 25.91 ? 269 VAL A CG2 1 ATOM 2062 N N . GLN A 1 270 ? 21.048 33.633 60.670 1.00 31.41 ? 270 GLN A N 1 ATOM 2063 C CA . GLN A 1 270 ? 20.564 32.755 59.612 1.00 34.36 ? 270 GLN A CA 1 ATOM 2064 C C . GLN A 1 270 ? 21.055 33.429 58.312 1.00 31.94 ? 270 GLN A C 1 ATOM 2065 O O . GLN A 1 270 ? 20.929 34.651 58.134 1.00 30.55 ? 270 GLN A O 1 ATOM 2066 C CB . GLN A 1 270 ? 19.036 32.651 59.714 1.00 37.27 ? 270 GLN A CB 1 ATOM 2067 C CG . GLN A 1 270 ? 18.289 32.012 58.494 1.00 43.22 ? 270 GLN A CG 1 ATOM 2068 C CD . GLN A 1 270 ? 16.753 32.116 58.613 1.00 48.34 ? 270 GLN A CD 1 ATOM 2069 O OE1 . GLN A 1 270 ? 16.216 33.068 59.218 1.00 56.47 ? 270 GLN A OE1 1 ATOM 2070 N NE2 . GLN A 1 270 ? 16.048 31.124 58.074 1.00 54.07 ? 270 GLN A NE2 1 ATOM 2071 N N . HIS A 1 271 ? 21.721 32.648 57.462 1.00 31.87 ? 271 HIS A N 1 ATOM 2072 C CA . HIS A 1 271 ? 22.274 33.128 56.201 1.00 29.34 ? 271 HIS A CA 1 ATOM 2073 C C . HIS A 1 271 ? 22.264 31.960 55.242 1.00 31.90 ? 271 HIS A C 1 ATOM 2074 O O . HIS A 1 271 ? 22.505 30.829 55.642 1.00 32.14 ? 271 HIS A O 1 ATOM 2075 C CB . HIS A 1 271 ? 23.700 33.664 56.397 1.00 26.75 ? 271 HIS A CB 1 ATOM 2076 C CG . HIS A 1 271 ? 24.238 34.365 55.172 1.00 25.60 ? 271 HIS A CG 1 ATOM 2077 N ND1 . HIS A 1 271 ? 25.084 33.753 54.277 1.00 24.93 ? 271 HIS A ND1 1 ATOM 2078 C CD2 . HIS A 1 271 ? 23.995 35.599 54.674 1.00 26.58 ? 271 HIS A CD2 1 ATOM 2079 C CE1 . HIS A 1 271 ? 25.369 34.596 53.295 1.00 28.18 ? 271 HIS A CE1 1 ATOM 2080 N NE2 . HIS A 1 271 ? 24.732 35.732 53.523 1.00 27.61 ? 271 HIS A NE2 1 ATOM 2081 N N . CYS A 1 272 ? 21.943 32.214 53.979 1.00 34.10 ? 272 CYS A N 1 ATOM 2082 C CA . CYS A 1 272 ? 21.781 31.128 53.020 1.00 37.52 ? 272 CYS A CA 1 ATOM 2083 C C . CYS A 1 272 ? 23.083 30.315 52.802 1.00 36.54 ? 272 CYS A C 1 ATOM 2084 O O . CYS A 1 272 ? 23.017 29.139 52.480 1.00 38.16 ? 272 CYS A O 1 ATOM 2085 C CB . CYS A 1 272 ? 21.222 31.657 51.692 1.00 39.62 ? 272 CYS A CB 1 ATOM 2086 S SG . CYS A 1 272 ? 22.369 32.722 50.782 1.00 42.85 ? 272 CYS A SG 1 ATOM 2087 N N . SER A 1 273 ? 24.252 30.931 53.021 1.00 32.83 ? 273 SER A N 1 ATOM 2088 C CA . SER A 1 273 ? 25.530 30.208 52.864 1.00 33.28 ? 273 SER A CA 1 ATOM 2089 C C . SER A 1 273 ? 25.767 29.142 53.945 1.00 35.23 ? 273 SER A C 1 ATOM 2090 O O . SER A 1 273 ? 26.640 28.277 53.818 1.00 35.61 ? 273 SER A O 1 ATOM 2091 C CB . SER A 1 273 ? 26.667 31.204 52.893 1.00 30.29 ? 273 SER A CB 1 ATOM 2092 O OG . SER A 1 273 ? 26.818 31.710 54.224 1.00 28.40 ? 273 SER A OG 1 ATOM 2093 N N . LEU A 1 274 ? 24.965 29.206 55.007 1.00 35.51 ? 274 LEU A N 1 ATOM 2094 C CA . LEU A 1 274 ? 25.093 28.301 56.136 1.00 36.52 ? 274 LEU A CA 1 ATOM 2095 C C . LEU A 1 274 ? 24.218 27.072 56.001 1.00 41.03 ? 274 LEU A C 1 ATOM 2096 O O . LEU A 1 274 ? 24.384 26.101 56.742 1.00 43.43 ? 274 LEU A O 1 ATOM 2097 C CB . LEU A 1 274 ? 24.779 29.063 57.439 1.00 35.29 ? 274 LEU A CB 1 ATOM 2098 C CG . LEU A 1 274 ? 25.650 30.266 57.811 1.00 30.62 ? 274 LEU A CG 1 ATOM 2099 C CD1 . LEU A 1 274 ? 24.979 31.116 58.916 1.00 29.04 ? 274 LEU A CD1 1 ATOM 2100 C CD2 . LEU A 1 274 ? 26.969 29.790 58.298 1.00 34.51 ? 274 LEU A CD2 1 ATOM 2101 N N . GLY A 1 275 ? 23.298 27.094 55.044 1.00 41.90 ? 275 GLY A N 1 ATOM 2102 C CA . GLY A 1 275 ? 22.333 26.022 54.891 1.00 46.21 ? 275 GLY A CA 1 ATOM 2103 C C . GLY A 1 275 ? 21.421 25.940 56.095 1.00 49.39 ? 275 GLY A C 1 ATOM 2104 O O . GLY A 1 275 ? 20.975 26.965 56.618 1.00 48.21 ? 275 GLY A O 1 ATOM 2105 N N . ASP A 1 276 ? 21.198 24.724 56.577 1.00 54.89 ? 276 ASP A N 1 ATOM 2106 C CA . ASP A 1 276 ? 20.276 24.475 57.679 1.00 59.04 ? 276 ASP A CA 1 ATOM 2107 C C . ASP A 1 276 ? 20.852 24.787 59.043 1.00 57.68 ? 276 ASP A C 1 ATOM 2108 O O . ASP A 1 276 ? 20.103 24.867 60.020 1.00 60.18 ? 276 ASP A O 1 ATOM 2109 C CB . ASP A 1 276 ? 19.791 23.028 57.656 1.00 65.50 ? 276 ASP A CB 1 ATOM 2110 C CG . ASP A 1 276 ? 18.691 22.800 56.644 1.00 70.82 ? 276 ASP A CG 1 ATOM 2111 O OD1 . ASP A 1 276 ? 18.245 23.780 55.997 1.00 72.89 ? 276 ASP A OD1 1 ATOM 2112 O OD2 . ASP A 1 276 ? 18.268 21.646 56.500 1.00 76.78 ? 276 ASP A OD2 1 ATOM 2113 N N . ARG A 1 277 ? 22.167 24.971 59.113 1.00 54.82 ? 277 ARG A N 1 ATOM 2114 C CA . ARG A 1 277 ? 22.822 25.303 60.369 1.00 53.14 ? 277 ARG A CA 1 ATOM 2115 C C . ARG A 1 277 ? 22.890 26.807 60.580 1.00 48.39 ? 277 ARG A C 1 ATOM 2116 O O . ARG A 1 277 ? 23.241 27.544 59.677 1.00 46.06 ? 277 ARG A O 1 ATOM 2117 C CB . ARG A 1 277 ? 24.233 24.709 60.431 1.00 54.17 ? 277 ARG A CB 1 ATOM 2118 C CG . ARG A 1 277 ? 24.291 23.261 60.927 1.00 62.42 ? 277 ARG A CG 1 ATOM 2119 C CD . ARG A 1 277 ? 25.609 22.993 61.680 1.00 67.01 ? 277 ARG A CD 1 ATOM 2120 N NE . ARG A 1 277 ? 25.548 23.343 63.103 1.00 67.64 ? 277 ARG A NE 1 ATOM 2121 C CZ . ARG A 1 277 ? 26.430 24.104 63.753 1.00 68.26 ? 277 ARG A CZ 1 ATOM 2122 N NH1 . ARG A 1 277 ? 27.482 24.644 63.126 1.00 67.76 ? 277 ARG A NH1 1 ATOM 2123 N NH2 . ARG A 1 277 ? 26.263 24.338 65.046 1.00 67.64 ? 277 ARG A NH2 1 ATOM 2124 N N . SER A 1 278 ? 22.515 27.265 61.762 1.00 46.55 ? 278 SER A N 1 ATOM 2125 C CA . SER A 1 278 ? 22.663 28.677 62.106 1.00 42.73 ? 278 SER A CA 1 ATOM 2126 C C . SER A 1 278 ? 24.044 28.868 62.678 1.00 40.36 ? 278 SER A C 1 ATOM 2127 O O . SER A 1 278 ? 24.719 27.910 63.080 1.00 40.62 ? 278 SER A O 1 ATOM 2128 C CB . SER A 1 278 ? 21.677 29.057 63.220 1.00 43.85 ? 278 SER A CB 1 ATOM 2129 O OG . SER A 1 278 ? 20.393 28.557 62.927 1.00 50.26 ? 278 SER A OG 1 ATOM 2130 N N . LEU A 1 279 ? 24.426 30.127 62.756 1.00 37.02 ? 279 LEU A N 1 ATOM 2131 C CA . LEU A 1 279 ? 25.523 30.550 63.568 1.00 37.51 ? 279 LEU A CA 1 ATOM 2132 C C . LEU A 1 279 ? 24.900 30.978 64.893 1.00 38.65 ? 279 LEU A C 1 ATOM 2133 O O . LEU A 1 279 ? 24.046 31.885 64.903 1.00 38.52 ? 279 LEU A O 1 ATOM 2134 C CB . LEU A 1 279 ? 26.164 31.753 62.877 1.00 34.19 ? 279 LEU A CB 1 ATOM 2135 C CG . LEU A 1 279 ? 27.305 32.540 63.473 1.00 36.61 ? 279 LEU A CG 1 ATOM 2136 C CD1 . LEU A 1 279 ? 28.493 31.645 63.836 1.00 42.04 ? 279 LEU A CD1 1 ATOM 2137 C CD2 . LEU A 1 279 ? 27.672 33.590 62.436 1.00 33.30 ? 279 LEU A CD2 1 ATOM 2138 N N . LEU A 1 280 ? 25.332 30.365 66.000 1.00 39.57 ? 280 LEU A N 1 ATOM 2139 C CA . LEU A 1 280 ? 24.799 30.671 67.311 1.00 40.30 ? 280 LEU A CA 1 ATOM 2140 C C . LEU A 1 280 ? 25.935 31.109 68.262 1.00 39.96 ? 280 LEU A C 1 ATOM 2141 O O . LEU A 1 280 ? 26.870 30.324 68.534 1.00 41.73 ? 280 LEU A O 1 ATOM 2142 C CB . LEU A 1 280 ? 24.043 29.471 67.887 1.00 44.29 ? 280 LEU A CB 1 ATOM 2143 C CG . LEU A 1 280 ? 23.479 29.692 69.291 1.00 47.46 ? 280 LEU A CG 1 ATOM 2144 C CD1 . LEU A 1 280 ? 22.210 30.538 69.239 1.00 47.75 ? 280 LEU A CD1 1 ATOM 2145 C CD2 . LEU A 1 280 ? 23.229 28.374 69.987 1.00 52.55 ? 280 LEU A CD2 1 ATOM 2146 N N . VAL A 1 281 ? 25.824 32.335 68.778 1.00 36.47 ? 281 VAL A N 1 ATOM 2147 C CA . VAL A 1 281 ? 26.888 32.979 69.557 1.00 36.18 ? 281 VAL A CA 1 ATOM 2148 C C . VAL A 1 281 ? 26.381 33.455 70.928 1.00 36.18 ? 281 VAL A C 1 ATOM 2149 O O . VAL A 1 281 ? 25.662 34.446 71.006 1.00 33.40 ? 281 VAL A O 1 ATOM 2150 C CB . VAL A 1 281 ? 27.554 34.152 68.766 1.00 33.67 ? 281 VAL A CB 1 ATOM 2151 C CG1 . VAL A 1 281 ? 28.801 34.601 69.459 1.00 34.14 ? 281 VAL A CG1 1 ATOM 2152 C CG2 . VAL A 1 281 ? 27.924 33.705 67.343 1.00 33.34 ? 281 VAL A CG2 1 ATOM 2153 N N . PRO A 1 282 ? 26.740 32.729 72.010 1.00 39.15 ? 282 PRO A N 1 ATOM 2154 C CA . PRO A 1 282 ? 26.292 33.033 73.371 1.00 40.11 ? 282 PRO A CA 1 ATOM 2155 C C . PRO A 1 282 ? 26.899 34.321 73.888 1.00 38.34 ? 282 PRO A C 1 ATOM 2156 O O . PRO A 1 282 ? 27.991 34.703 73.441 1.00 37.76 ? 282 PRO A O 1 ATOM 2157 C CB . PRO A 1 282 ? 26.833 31.847 74.201 1.00 44.38 ? 282 PRO A CB 1 ATOM 2158 C CG . PRO A 1 282 ? 27.169 30.791 73.206 1.00 46.08 ? 282 PRO A CG 1 ATOM 2159 C CD . PRO A 1 282 ? 27.617 31.546 71.993 1.00 42.45 ? 282 PRO A CD 1 ATOM 2160 N N . TRP A 1 283 ? 26.183 35.014 74.769 1.00 38.24 ? 283 TRP A N 1 ATOM 2161 C CA . TRP A 1 283 ? 26.805 36.072 75.550 1.00 38.51 ? 283 TRP A CA 1 ATOM 2162 C C . TRP A 1 283 ? 27.389 35.472 76.817 1.00 42.50 ? 283 TRP A C 1 ATOM 2163 O O . TRP A 1 283 ? 26.660 34.969 77.666 1.00 44.62 ? 283 TRP A O 1 ATOM 2164 C CB . TRP A 1 283 ? 25.825 37.167 75.922 1.00 37.18 ? 283 TRP A CB 1 ATOM 2165 C CG . TRP A 1 283 ? 26.418 38.146 76.916 1.00 35.56 ? 283 TRP A CG 1 ATOM 2166 C CD1 . TRP A 1 283 ? 27.676 38.679 76.888 1.00 36.40 ? 283 TRP A CD1 1 ATOM 2167 C CD2 . TRP A 1 283 ? 25.766 38.722 78.054 1.00 37.24 ? 283 TRP A CD2 1 ATOM 2168 N NE1 . TRP A 1 283 ? 27.857 39.527 77.947 1.00 35.02 ? 283 TRP A NE1 1 ATOM 2169 C CE2 . TRP A 1 283 ? 26.702 39.578 78.681 1.00 34.20 ? 283 TRP A CE2 1 ATOM 2170 C CE3 . TRP A 1 283 ? 24.489 38.590 78.610 1.00 38.55 ? 283 TRP A CE3 1 ATOM 2171 C CZ2 . TRP A 1 283 ? 26.398 40.315 79.818 1.00 36.20 ? 283 TRP A CZ2 1 ATOM 2172 C CZ3 . TRP A 1 283 ? 24.175 39.324 79.745 1.00 40.02 ? 283 TRP A CZ3 1 ATOM 2173 C CH2 . TRP A 1 283 ? 25.142 40.181 80.346 1.00 40.21 ? 283 TRP A CH2 1 ATOM 2174 N N . HIS A 1 284 ? 28.703 35.535 76.934 1.00 44.70 ? 284 HIS A N 1 ATOM 2175 C CA . HIS A 1 284 ? 29.386 35.062 78.134 1.00 50.94 ? 284 HIS A CA 1 ATOM 2176 C C . HIS A 1 284 ? 29.929 36.256 78.914 1.00 52.14 ? 284 HIS A C 1 ATOM 2177 O O . HIS A 1 284 ? 30.432 37.204 78.305 1.00 50.93 ? 284 HIS A O 1 ATOM 2178 C CB . HIS A 1 284 ? 30.532 34.135 77.745 1.00 52.98 ? 284 HIS A CB 1 ATOM 2179 C CG . HIS A 1 284 ? 30.086 32.771 77.315 1.00 56.56 ? 284 HIS A CG 1 ATOM 2180 N ND1 . HIS A 1 284 ? 30.331 32.270 76.055 1.00 55.96 ? 284 HIS A ND1 1 ATOM 2181 C CD2 . HIS A 1 284 ? 29.430 31.794 77.989 1.00 61.07 ? 284 HIS A CD2 1 ATOM 2182 C CE1 . HIS A 1 284 ? 29.837 31.048 75.967 1.00 59.36 ? 284 HIS A CE1 1 ATOM 2183 N NE2 . HIS A 1 284 ? 29.275 30.739 77.122 1.00 62.60 ? 284 HIS A NE2 1 ATOM 2184 N N . HIS A 1 285 ? 29.815 36.230 80.240 1.00 53.18 ? 285 HIS A N 1 ATOM 2185 C CA . HIS A 1 285 ? 30.350 37.320 81.077 1.00 55.05 ? 285 HIS A CA 1 ATOM 2186 C C . HIS A 1 285 ? 31.803 36.999 81.399 1.00 55.50 ? 285 HIS A C 1 ATOM 2187 O O . HIS A 1 285 ? 32.079 36.209 82.309 1.00 56.44 ? 285 HIS A O 1 ATOM 2188 C CB . HIS A 1 285 ? 29.574 37.506 82.398 1.00 55.66 ? 285 HIS A CB 1 ATOM 2189 C CG . HIS A 1 285 ? 28.078 37.505 82.263 1.00 57.23 ? 285 HIS A CG 1 ATOM 2190 N ND1 . HIS A 1 285 ? 27.404 36.796 81.288 1.00 59.47 ? 285 HIS A ND1 1 ATOM 2191 C CD2 . HIS A 1 285 ? 27.122 38.073 83.037 1.00 58.88 ? 285 HIS A CD2 1 ATOM 2192 C CE1 . HIS A 1 285 ? 26.102 36.946 81.451 1.00 58.05 ? 285 HIS A CE1 1 ATOM 2193 N NE2 . HIS A 1 285 ? 25.903 37.718 82.506 1.00 60.43 ? 285 HIS A NE2 1 ATOM 2194 N N . ILE B 2 1 ? 15.541 68.641 47.822 1.00 62.48 ? 1 ILE B N 1 ATOM 2195 C CA . ILE B 2 1 ? 15.802 68.840 49.276 1.00 61.36 ? 1 ILE B CA 1 ATOM 2196 C C . ILE B 2 1 ? 17.237 68.501 49.594 1.00 57.43 ? 1 ILE B C 1 ATOM 2197 O O . ILE B 2 1 ? 17.824 67.620 48.963 1.00 55.62 ? 1 ILE B O 1 ATOM 2198 C CB . ILE B 2 1 ? 14.847 67.993 50.182 1.00 61.69 ? 1 ILE B CB 1 ATOM 2199 C CG1 . ILE B 2 1 ? 14.844 66.511 49.779 1.00 60.43 ? 1 ILE B CG1 1 ATOM 2200 C CG2 . ILE B 2 1 ? 13.411 68.546 50.139 1.00 65.96 ? 1 ILE B CG2 1 ATOM 2201 C CD1 . ILE B 2 1 ? 14.232 65.585 50.846 1.00 59.88 ? 1 ILE B CD1 1 ATOM 2202 N N . GLN B 2 2 ? 17.799 69.194 50.576 1.00 56.11 ? 2 GLN B N 1 ATOM 2203 C CA . GLN B 2 2 ? 19.111 68.860 51.110 1.00 51.78 ? 2 GLN B CA 1 ATOM 2204 C C . GLN B 2 2 ? 18.952 67.815 52.198 1.00 48.60 ? 2 GLN B C 1 ATOM 2205 O O . GLN B 2 2 ? 17.996 67.846 52.988 1.00 49.57 ? 2 GLN B O 1 ATOM 2206 C CB . GLN B 2 2 ? 19.768 70.102 51.720 1.00 54.63 ? 2 GLN B CB 1 ATOM 2207 C CG . GLN B 2 2 ? 19.676 71.362 50.854 1.00 59.71 ? 2 GLN B CG 1 ATOM 2208 C CD . GLN B 2 2 ? 19.062 72.561 51.579 1.00 66.20 ? 2 GLN B CD 1 ATOM 2209 O OE1 . GLN B 2 2 ? 19.198 72.726 52.803 1.00 67.66 ? 2 GLN B OE1 1 ATOM 2210 N NE2 . GLN B 2 2 ? 18.379 73.403 50.819 1.00 71.86 ? 2 GLN B NE2 1 ATOM 2211 N N . ARG B 2 3 ? 19.907 66.893 52.237 1.00 43.45 ? 3 ARG B N 1 ATOM 2212 C CA . ARG B 2 3 ? 19.969 65.850 53.236 1.00 40.44 ? 3 ARG B CA 1 ATOM 2213 C C . ARG B 2 3 ? 21.407 65.788 53.673 1.00 37.65 ? 3 ARG B C 1 ATOM 2214 O O . ARG B 2 3 ? 22.308 65.717 52.840 1.00 33.79 ? 3 ARG B O 1 ATOM 2215 C CB . ARG B 2 3 ? 19.596 64.496 52.644 1.00 38.67 ? 3 ARG B CB 1 ATOM 2216 C CG . ARG B 2 3 ? 18.148 64.345 52.185 1.00 42.82 ? 3 ARG B CG 1 ATOM 2217 C CD . ARG B 2 3 ? 18.011 62.929 51.579 1.00 44.00 ? 3 ARG B CD 1 ATOM 2218 N NE . ARG B 2 3 ? 16.657 62.610 51.126 1.00 47.96 ? 3 ARG B NE 1 ATOM 2219 C CZ . ARG B 2 3 ? 15.670 62.239 51.944 1.00 53.10 ? 3 ARG B CZ 1 ATOM 2220 N NH1 . ARG B 2 3 ? 15.890 62.165 53.260 1.00 53.67 ? 3 ARG B NH1 1 ATOM 2221 N NH2 . ARG B 2 3 ? 14.459 61.959 51.460 1.00 54.09 ? 3 ARG B NH2 1 ATOM 2222 N N . THR B 2 4 ? 21.611 65.800 54.980 1.00 38.45 ? 4 THR B N 1 ATOM 2223 C CA . THR B 2 4 ? 22.941 65.713 55.572 1.00 38.31 ? 4 THR B CA 1 ATOM 2224 C C . THR B 2 4 ? 23.414 64.252 55.623 1.00 36.02 ? 4 THR B C 1 ATOM 2225 O O . THR B 2 4 ? 22.588 63.340 55.810 1.00 36.86 ? 4 THR B O 1 ATOM 2226 C CB . THR B 2 4 ? 22.955 66.441 56.969 1.00 40.56 ? 4 THR B CB 1 ATOM 2227 O OG1 . THR B 2 4 ? 24.291 66.843 57.285 1.00 40.74 ? 4 THR B OG1 1 ATOM 2228 C CG2 . THR B 2 4 ? 22.386 65.570 58.072 1.00 41.30 ? 4 THR B CG2 1 ATOM 2229 N N . PRO B 2 5 ? 24.722 64.000 55.407 1.00 35.03 ? 5 PRO B N 1 ATOM 2230 C CA . PRO B 2 5 ? 25.203 62.609 55.426 1.00 32.79 ? 5 PRO B CA 1 ATOM 2231 C C . PRO B 2 5 ? 25.127 61.919 56.810 1.00 32.58 ? 5 PRO B C 1 ATOM 2232 O O . PRO B 2 5 ? 25.395 62.556 57.833 1.00 31.75 ? 5 PRO B O 1 ATOM 2233 C CB . PRO B 2 5 ? 26.669 62.733 54.991 1.00 31.34 ? 5 PRO B CB 1 ATOM 2234 C CG . PRO B 2 5 ? 27.037 64.149 55.281 1.00 33.52 ? 5 PRO B CG 1 ATOM 2235 C CD . PRO B 2 5 ? 25.814 64.952 55.109 1.00 35.21 ? 5 PRO B CD 1 ATOM 2236 N N . LYS B 2 6 ? 24.709 60.647 56.809 1.00 31.37 ? 6 LYS B N 1 ATOM 2237 C CA . LYS B 2 6 ? 24.991 59.728 57.892 1.00 31.39 ? 6 LYS B CA 1 ATOM 2238 C C . LYS B 2 6 ? 26.419 59.253 57.682 1.00 29.17 ? 6 LYS B C 1 ATOM 2239 O O . LYS B 2 6 ? 26.838 59.019 56.552 1.00 27.72 ? 6 LYS B O 1 ATOM 2240 C CB . LYS B 2 6 ? 24.026 58.547 57.825 1.00 33.23 ? 6 LYS B CB 1 ATOM 2241 C CG . LYS B 2 6 ? 24.127 57.564 58.984 1.00 34.81 ? 6 LYS B CG 1 ATOM 2242 C CD . LYS B 2 6 ? 22.994 56.528 58.848 1.00 39.04 ? 6 LYS B CD 1 ATOM 2243 C CE . LYS B 2 6 ? 22.811 55.777 60.151 1.00 44.69 ? 6 LYS B CE 1 ATOM 2244 N NZ . LYS B 2 6 ? 21.819 54.669 59.995 1.00 52.95 ? 6 LYS B NZ 1 ATOM 2245 N N . ILE B 2 7 ? 27.188 59.110 58.753 1.00 28.61 ? 7 ILE B N 1 ATOM 2246 C CA . ILE B 2 7 ? 28.612 58.787 58.648 1.00 26.96 ? 7 ILE B CA 1 ATOM 2247 C C . ILE B 2 7 ? 28.847 57.630 59.620 1.00 27.87 ? 7 ILE B C 1 ATOM 2248 O O . ILE B 2 7 ? 28.592 57.781 60.817 1.00 28.48 ? 7 ILE B O 1 ATOM 2249 C CB . ILE B 2 7 ? 29.470 59.990 59.102 1.00 27.90 ? 7 ILE B CB 1 ATOM 2250 C CG1 . ILE B 2 7 ? 29.172 61.245 58.235 1.00 27.21 ? 7 ILE B CG1 1 ATOM 2251 C CG2 . ILE B 2 7 ? 30.943 59.682 59.003 1.00 23.93 ? 7 ILE B CG2 1 ATOM 2252 C CD1 . ILE B 2 7 ? 29.500 62.514 58.933 1.00 29.92 ? 7 ILE B CD1 1 ATOM 2253 N N . GLN B 2 8 ? 29.281 56.484 59.114 1.00 25.61 ? 8 GLN B N 1 ATOM 2254 C CA . GLN B 2 8 ? 29.497 55.293 59.939 1.00 26.21 ? 8 GLN B CA 1 ATOM 2255 C C . GLN B 2 8 ? 30.918 54.856 59.705 1.00 25.58 ? 8 GLN B C 1 ATOM 2256 O O . GLN B 2 8 ? 31.315 54.719 58.543 1.00 25.28 ? 8 GLN B O 1 ATOM 2257 C CB . GLN B 2 8 ? 28.519 54.197 59.534 1.00 27.86 ? 8 GLN B CB 1 ATOM 2258 C CG . GLN B 2 8 ? 27.069 54.554 59.954 1.00 29.27 ? 8 GLN B CG 1 ATOM 2259 C CD . GLN B 2 8 ? 25.992 53.653 59.409 1.00 33.06 ? 8 GLN B CD 1 ATOM 2260 O OE1 . GLN B 2 8 ? 25.472 52.790 60.131 1.00 38.44 ? 8 GLN B OE1 1 ATOM 2261 N NE2 . GLN B 2 8 ? 25.582 53.894 58.156 1.00 31.77 ? 8 GLN B NE2 1 ATOM 2262 N N . VAL B 2 9 ? 31.685 54.654 60.788 1.00 23.85 ? 9 VAL B N 1 ATOM 2263 C CA . VAL B 2 9 ? 33.093 54.286 60.700 1.00 22.33 ? 9 VAL B CA 1 ATOM 2264 C C . VAL B 2 9 ? 33.265 52.934 61.371 1.00 23.65 ? 9 VAL B C 1 ATOM 2265 O O . VAL B 2 9 ? 32.778 52.732 62.494 1.00 25.15 ? 9 VAL B O 1 ATOM 2266 C CB . VAL B 2 9 ? 33.974 55.383 61.406 1.00 23.76 ? 9 VAL B CB 1 ATOM 2267 C CG1 . VAL B 2 9 ? 35.457 55.080 61.239 1.00 22.29 ? 9 VAL B CG1 1 ATOM 2268 C CG2 . VAL B 2 9 ? 33.716 56.682 60.738 1.00 20.75 ? 9 VAL B CG2 1 ATOM 2269 N N . TYR B 2 10 ? 33.891 51.991 60.666 1.00 23.36 ? 10 TYR B N 1 ATOM 2270 C CA . TYR B 2 10 ? 33.982 50.613 61.130 1.00 23.00 ? 10 TYR B CA 1 ATOM 2271 C C . TYR B 2 10 ? 35.151 49.940 60.472 1.00 23.81 ? 10 TYR B C 1 ATOM 2272 O O . TYR B 2 10 ? 35.653 50.407 59.445 1.00 24.11 ? 10 TYR B O 1 ATOM 2273 C CB . TYR B 2 10 ? 32.676 49.838 60.844 1.00 25.96 ? 10 TYR B CB 1 ATOM 2274 C CG . TYR B 2 10 ? 32.112 49.923 59.429 1.00 23.78 ? 10 TYR B CG 1 ATOM 2275 C CD1 . TYR B 2 10 ? 31.455 51.050 59.004 1.00 23.21 ? 10 TYR B CD1 1 ATOM 2276 C CD2 . TYR B 2 10 ? 32.213 48.842 58.534 1.00 27.15 ? 10 TYR B CD2 1 ATOM 2277 C CE1 . TYR B 2 10 ? 30.953 51.166 57.716 1.00 22.57 ? 10 TYR B CE1 1 ATOM 2278 C CE2 . TYR B 2 10 ? 31.678 48.917 57.239 1.00 22.35 ? 10 TYR B CE2 1 ATOM 2279 C CZ . TYR B 2 10 ? 31.052 50.069 56.830 1.00 25.66 ? 10 TYR B CZ 1 ATOM 2280 O OH . TYR B 2 10 ? 30.517 50.162 55.558 1.00 23.58 ? 10 TYR B OH 1 ATOM 2281 N N . SER B 2 11 ? 35.615 48.839 61.055 1.00 26.07 ? 11 SER B N 1 ATOM 2282 C CA . SER B 2 11 ? 36.693 48.085 60.460 1.00 25.61 ? 11 SER B CA 1 ATOM 2283 C C . SER B 2 11 ? 36.085 46.900 59.717 1.00 27.40 ? 11 SER B C 1 ATOM 2284 O O . SER B 2 11 ? 34.912 46.528 59.933 1.00 28.71 ? 11 SER B O 1 ATOM 2285 C CB . SER B 2 11 ? 37.674 47.614 61.537 1.00 28.09 ? 11 SER B CB 1 ATOM 2286 O OG . SER B 2 11 ? 36.964 46.985 62.578 1.00 31.32 ? 11 SER B OG 1 ATOM 2287 N N . ARG B 2 12 ? 36.858 46.320 58.814 1.00 28.20 ? 12 ARG B N 1 ATOM 2288 C CA . ARG B 2 12 ? 36.409 45.109 58.073 1.00 31.23 ? 12 ARG B CA 1 ATOM 2289 C C . ARG B 2 12 ? 36.210 43.891 58.992 1.00 35.22 ? 12 ARG B C 1 ATOM 2290 O O . ARG B 2 12 ? 35.177 43.175 58.919 1.00 37.16 ? 12 ARG B O 1 ATOM 2291 C CB . ARG B 2 12 ? 37.429 44.821 56.944 1.00 31.36 ? 12 ARG B CB 1 ATOM 2292 C CG . ARG B 2 12 ? 37.267 43.494 56.165 1.00 37.99 ? 12 ARG B CG 1 ATOM 2293 C CD . ARG B 2 12 ? 36.051 43.519 55.269 1.00 37.88 ? 12 ARG B CD 1 ATOM 2294 N NE . ARG B 2 12 ? 35.880 42.255 54.536 1.00 43.48 ? 12 ARG B NE 1 ATOM 2295 C CZ . ARG B 2 12 ? 35.537 41.095 55.089 1.00 44.87 ? 12 ARG B CZ 1 ATOM 2296 N NH1 . ARG B 2 12 ? 35.338 40.997 56.400 1.00 47.49 ? 12 ARG B NH1 1 ATOM 2297 N NH2 . ARG B 2 12 ? 35.401 40.020 54.332 1.00 47.45 ? 12 ARG B NH2 1 ATOM 2298 N N . HIS B 2 13 ? 37.216 43.629 59.834 1.00 37.33 ? 13 HIS B N 1 ATOM 2299 C CA . HIS B 2 13 ? 37.197 42.521 60.799 1.00 41.46 ? 13 HIS B CA 1 ATOM 2300 C C . HIS B 2 13 ? 37.288 43.142 62.187 1.00 40.51 ? 13 HIS B C 1 ATOM 2301 O O . HIS B 2 13 ? 37.843 44.232 62.316 1.00 38.03 ? 13 HIS B O 1 ATOM 2302 C CB . HIS B 2 13 ? 38.428 41.616 60.595 1.00 44.16 ? 13 HIS B CB 1 ATOM 2303 C CG . HIS B 2 13 ? 38.591 41.124 59.193 1.00 47.12 ? 13 HIS B CG 1 ATOM 2304 N ND1 . HIS B 2 13 ? 37.872 40.057 58.689 1.00 53.31 ? 13 HIS B ND1 1 ATOM 2305 C CD2 . HIS B 2 13 ? 39.397 41.542 58.188 1.00 47.28 ? 13 HIS B CD2 1 ATOM 2306 C CE1 . HIS B 2 13 ? 38.215 39.850 57.429 1.00 52.58 ? 13 HIS B CE1 1 ATOM 2307 N NE2 . HIS B 2 13 ? 39.147 40.727 57.103 1.00 50.16 ? 13 HIS B NE2 1 ATOM 2308 N N . PRO B 2 14 ? 36.767 42.453 63.224 1.00 43.30 ? 14 PRO B N 1 ATOM 2309 C CA . PRO B 2 14 ? 37.023 42.875 64.600 1.00 43.92 ? 14 PRO B CA 1 ATOM 2310 C C . PRO B 2 14 ? 38.520 43.045 64.807 1.00 43.90 ? 14 PRO B C 1 ATOM 2311 O O . PRO B 2 14 ? 39.298 42.146 64.457 1.00 46.49 ? 14 PRO B O 1 ATOM 2312 C CB . PRO B 2 14 ? 36.538 41.682 65.432 1.00 48.42 ? 14 PRO B CB 1 ATOM 2313 C CG . PRO B 2 14 ? 35.443 41.075 64.604 1.00 49.09 ? 14 PRO B CG 1 ATOM 2314 C CD . PRO B 2 14 ? 35.942 41.225 63.173 1.00 47.35 ? 14 PRO B CD 1 ATOM 2315 N N . ALA B 2 15 ? 38.882 44.174 65.412 1.00 41.83 ? 15 ALA B N 1 ATOM 2316 C CA . ALA B 2 15 ? 40.239 44.679 65.507 1.00 39.69 ? 15 ALA B CA 1 ATOM 2317 C C . ALA B 2 15 ? 41.105 43.974 66.522 1.00 41.93 ? 15 ALA B C 1 ATOM 2318 O O . ALA B 2 15 ? 40.635 43.518 67.559 1.00 43.27 ? 15 ALA B O 1 ATOM 2319 C CB . ALA B 2 15 ? 40.195 46.175 65.829 1.00 38.08 ? 15 ALA B CB 1 ATOM 2320 N N . GLU B 2 16 ? 42.390 43.900 66.194 1.00 41.47 ? 16 GLU B N 1 ATOM 2321 C CA . GLU B 2 16 ? 43.402 43.293 67.032 1.00 42.70 ? 16 GLU B CA 1 ATOM 2322 C C . GLU B 2 16 ? 44.658 44.096 66.734 1.00 41.60 ? 16 GLU B C 1 ATOM 2323 O O . GLU B 2 16 ? 45.065 44.189 65.570 1.00 39.88 ? 16 GLU B O 1 ATOM 2324 C CB . GLU B 2 16 ? 43.625 41.827 66.663 1.00 46.87 ? 16 GLU B CB 1 ATOM 2325 N N . ASN B 2 17 ? 45.261 44.674 67.774 1.00 41.22 ? 17 ASN B N 1 ATOM 2326 C CA . ASN B 2 17 ? 46.465 45.481 67.625 1.00 40.68 ? 17 ASN B CA 1 ATOM 2327 C C . ASN B 2 17 ? 47.545 44.720 66.892 1.00 42.58 ? 17 ASN B C 1 ATOM 2328 O O . ASN B 2 17 ? 47.800 43.566 67.191 1.00 44.47 ? 17 ASN B O 1 ATOM 2329 C CB . ASN B 2 17 ? 46.960 45.976 68.990 1.00 41.58 ? 17 ASN B CB 1 ATOM 2330 C CG . ASN B 2 17 ? 46.101 47.112 69.530 1.00 40.16 ? 17 ASN B CG 1 ATOM 2331 O OD1 . ASN B 2 17 ? 45.568 47.910 68.762 1.00 37.38 ? 17 ASN B OD1 1 ATOM 2332 N ND2 . ASN B 2 17 ? 45.947 47.171 70.842 1.00 43.33 ? 17 ASN B ND2 1 ATOM 2333 N N . GLY B 2 18 ? 48.143 45.349 65.891 1.00 42.14 ? 18 GLY B N 1 ATOM 2334 C CA . GLY B 2 18 ? 49.222 44.688 65.156 1.00 44.95 ? 18 GLY B CA 1 ATOM 2335 C C . GLY B 2 18 ? 48.831 43.791 63.985 1.00 46.12 ? 18 GLY B C 1 ATOM 2336 O O . GLY B 2 18 ? 49.695 43.236 63.318 1.00 48.23 ? 18 GLY B O 1 ATOM 2337 N N . LYS B 2 19 ? 47.538 43.647 63.708 1.00 45.36 ? 19 LYS B N 1 ATOM 2338 C CA . LYS B 2 19 ? 47.115 42.792 62.596 1.00 45.45 ? 19 LYS B CA 1 ATOM 2339 C C . LYS B 2 19 ? 46.410 43.671 61.586 1.00 43.15 ? 19 LYS B C 1 ATOM 2340 O O . LYS B 2 19 ? 45.605 44.556 61.966 1.00 39.59 ? 19 LYS B O 1 ATOM 2341 C CB . LYS B 2 19 ? 46.224 41.650 63.078 1.00 47.99 ? 19 LYS B CB 1 ATOM 2342 N N . SER B 2 20 ? 46.729 43.475 60.304 1.00 43.27 ? 20 SER B N 1 ATOM 2343 C CA . SER B 2 20 ? 46.170 44.360 59.277 1.00 41.57 ? 20 SER B CA 1 ATOM 2344 C C . SER B 2 20 ? 44.689 44.136 59.051 1.00 39.12 ? 20 SER B C 1 ATOM 2345 O O . SER B 2 20 ? 44.161 43.020 59.180 1.00 38.84 ? 20 SER B O 1 ATOM 2346 C CB . SER B 2 20 ? 46.931 44.266 57.963 1.00 44.59 ? 20 SER B CB 1 ATOM 2347 O OG . SER B 2 20 ? 46.747 42.995 57.394 1.00 50.44 ? 20 SER B OG 1 ATOM 2348 N N . ASN B 2 21 ? 44.022 45.231 58.687 1.00 35.76 ? 21 ASN B N 1 ATOM 2349 C CA . ASN B 2 21 ? 42.588 45.279 58.654 1.00 34.57 ? 21 ASN B CA 1 ATOM 2350 C C . ASN B 2 21 ? 42.256 46.340 57.580 1.00 33.40 ? 21 ASN B C 1 ATOM 2351 O O . ASN B 2 21 ? 43.154 46.824 56.882 1.00 33.01 ? 21 ASN B O 1 ATOM 2352 C CB . ASN B 2 21 ? 42.126 45.737 60.048 1.00 32.61 ? 21 ASN B CB 1 ATOM 2353 C CG . ASN B 2 21 ? 40.725 45.265 60.417 1.00 34.07 ? 21 ASN B CG 1 ATOM 2354 O OD1 . ASN B 2 21 ? 39.847 45.165 59.571 1.00 30.86 ? 21 ASN B OD1 1 ATOM 2355 N ND2 . ASN B 2 21 ? 40.509 45.012 61.721 1.00 32.31 ? 21 ASN B ND2 1 ATOM 2356 N N . PHE B 2 22 ? 40.978 46.681 57.455 1.00 30.96 ? 22 PHE B N 1 ATOM 2357 C CA . PHE B 2 22 ? 40.560 47.806 56.647 1.00 29.51 ? 22 PHE B CA 1 ATOM 2358 C C . PHE B 2 22 ? 39.710 48.716 57.476 1.00 26.73 ? 22 PHE B C 1 ATOM 2359 O O . PHE B 2 22 ? 38.855 48.248 58.202 1.00 25.61 ? 22 PHE B O 1 ATOM 2360 C CB . PHE B 2 22 ? 39.766 47.334 55.431 1.00 30.07 ? 22 PHE B CB 1 ATOM 2361 C CG . PHE B 2 22 ? 40.641 46.796 54.352 1.00 35.33 ? 22 PHE B CG 1 ATOM 2362 C CD1 . PHE B 2 22 ? 41.017 47.603 53.288 1.00 38.20 ? 22 PHE B CD1 1 ATOM 2363 C CD2 . PHE B 2 22 ? 41.126 45.505 54.428 1.00 39.30 ? 22 PHE B CD2 1 ATOM 2364 C CE1 . PHE B 2 22 ? 41.873 47.115 52.313 1.00 42.74 ? 22 PHE B CE1 1 ATOM 2365 C CE2 . PHE B 2 22 ? 41.963 44.999 53.449 1.00 45.62 ? 22 PHE B CE2 1 ATOM 2366 C CZ . PHE B 2 22 ? 42.337 45.808 52.388 1.00 44.76 ? 22 PHE B CZ 1 ATOM 2367 N N . LEU B 2 23 ? 39.977 50.011 57.376 1.00 25.70 ? 23 LEU B N 1 ATOM 2368 C CA . LEU B 2 23 ? 39.147 51.026 57.971 1.00 25.09 ? 23 LEU B CA 1 ATOM 2369 C C . LEU B 2 23 ? 38.192 51.554 56.915 1.00 24.94 ? 23 LEU B C 1 ATOM 2370 O O . LEU B 2 23 ? 38.608 51.891 55.785 1.00 26.06 ? 23 LEU B O 1 ATOM 2371 C CB . LEU B 2 23 ? 40.034 52.169 58.487 1.00 23.67 ? 23 LEU B CB 1 ATOM 2372 C CG . LEU B 2 23 ? 39.363 53.363 59.112 1.00 25.87 ? 23 LEU B CG 1 ATOM 2373 C CD1 . LEU B 2 23 ? 38.638 52.997 60.389 1.00 29.04 ? 23 LEU B CD1 1 ATOM 2374 C CD2 . LEU B 2 23 ? 40.410 54.453 59.371 1.00 26.52 ? 23 LEU B CD2 1 ATOM 2375 N N . ASN B 2 24 ? 36.920 51.663 57.287 1.00 24.77 ? 24 ASN B N 1 ATOM 2376 C CA . ASN B 2 24 ? 35.858 52.015 56.358 1.00 25.07 ? 24 ASN B CA 1 ATOM 2377 C C . ASN B 2 24 ? 35.153 53.274 56.866 1.00 23.81 ? 24 ASN B C 1 ATOM 2378 O O . ASN B 2 24 ? 34.825 53.377 58.049 1.00 24.81 ? 24 ASN B O 1 ATOM 2379 C CB . ASN B 2 24 ? 34.770 50.908 56.339 1.00 24.44 ? 24 ASN B CB 1 ATOM 2380 C CG . ASN B 2 24 ? 35.199 49.627 55.674 1.00 26.78 ? 24 ASN B CG 1 ATOM 2381 O OD1 . ASN B 2 24 ? 35.802 49.614 54.615 1.00 28.89 ? 24 ASN B OD1 1 ATOM 2382 N ND2 . ASN B 2 24 ? 34.774 48.508 56.248 1.00 30.19 ? 24 ASN B ND2 1 ATOM 2383 N N . CYS B 2 25 ? 34.874 54.205 55.968 1.00 24.38 ? 25 CYS B N 1 ATOM 2384 C CA . CYS B 2 25 ? 33.923 55.259 56.270 1.00 23.98 ? 25 CYS B CA 1 ATOM 2385 C C . CYS B 2 25 ? 32.791 55.275 55.234 1.00 24.41 ? 25 CYS B C 1 ATOM 2386 O O . CYS B 2 25 ? 32.988 55.621 54.074 1.00 23.76 ? 25 CYS B O 1 ATOM 2387 C CB . CYS B 2 25 ? 34.625 56.610 56.324 1.00 23.80 ? 25 CYS B CB 1 ATOM 2388 S SG . CYS B 2 25 ? 33.531 57.983 56.860 1.00 27.13 ? 25 CYS B SG 1 ATOM 2389 N N . TYR B 2 26 ? 31.601 54.906 55.685 1.00 23.37 ? 26 TYR B N 1 ATOM 2390 C CA . TYR B 2 26 ? 30.468 54.862 54.851 1.00 23.46 ? 26 TYR B CA 1 ATOM 2391 C C . TYR B 2 26 ? 29.593 56.087 55.062 1.00 24.17 ? 26 TYR B C 1 ATOM 2392 O O . TYR B 2 26 ? 29.040 56.294 56.159 1.00 23.36 ? 26 TYR B O 1 ATOM 2393 C CB . TYR B 2 26 ? 29.731 53.564 55.154 1.00 24.87 ? 26 TYR B CB 1 ATOM 2394 C CG . TYR B 2 26 ? 28.526 53.352 54.357 1.00 27.10 ? 26 TYR B CG 1 ATOM 2395 C CD1 . TYR B 2 26 ? 28.606 53.267 52.973 1.00 25.94 ? 26 TYR B CD1 1 ATOM 2396 C CD2 . TYR B 2 26 ? 27.305 53.150 54.968 1.00 24.36 ? 26 TYR B CD2 1 ATOM 2397 C CE1 . TYR B 2 26 ? 27.486 53.017 52.220 1.00 30.93 ? 26 TYR B CE1 1 ATOM 2398 C CE2 . TYR B 2 26 ? 26.179 52.899 54.214 1.00 29.27 ? 26 TYR B CE2 1 ATOM 2399 C CZ . TYR B 2 26 ? 26.276 52.836 52.847 1.00 30.92 ? 26 TYR B CZ 1 ATOM 2400 O OH . TYR B 2 26 ? 25.155 52.576 52.081 1.00 33.91 ? 26 TYR B OH 1 ATOM 2401 N N . VAL B 2 27 ? 29.484 56.908 54.007 1.00 24.16 ? 27 VAL B N 1 ATOM 2402 C CA . VAL B 2 27 ? 28.682 58.138 54.072 1.00 26.64 ? 27 VAL B CA 1 ATOM 2403 C C . VAL B 2 27 ? 27.468 57.953 53.189 1.00 26.92 ? 27 VAL B C 1 ATOM 2404 O O . VAL B 2 27 ? 27.593 57.500 52.069 1.00 27.29 ? 27 VAL B O 1 ATOM 2405 C CB . VAL B 2 27 ? 29.495 59.425 53.718 1.00 26.82 ? 27 VAL B CB 1 ATOM 2406 C CG1 . VAL B 2 27 ? 30.752 59.505 54.580 1.00 30.28 ? 27 VAL B CG1 1 ATOM 2407 C CG2 . VAL B 2 27 ? 29.959 59.400 52.288 1.00 29.95 ? 27 VAL B CG2 1 ATOM 2408 N N . SER B 2 28 ? 26.279 58.212 53.729 1.00 27.23 ? 28 SER B N 1 ATOM 2409 C CA . SER B 2 28 ? 25.058 57.852 53.035 1.00 28.10 ? 28 SER B CA 1 ATOM 2410 C C . SER B 2 28 ? 23.948 58.825 53.332 1.00 29.31 ? 28 SER B C 1 ATOM 2411 O O . SER B 2 28 ? 24.074 59.680 54.219 1.00 30.83 ? 28 SER B O 1 ATOM 2412 C CB . SER B 2 28 ? 24.668 56.409 53.343 1.00 27.79 ? 28 SER B CB 1 ATOM 2413 O OG . SER B 2 28 ? 24.297 56.194 54.693 1.00 29.40 ? 28 SER B OG 1 ATOM 2414 N N . GLY B 2 29 ? 22.867 58.742 52.570 1.00 30.96 ? 29 GLY B N 1 ATOM 2415 C CA . GLY B 2 29 ? 21.701 59.565 52.842 1.00 30.66 ? 29 GLY B CA 1 ATOM 2416 C C . GLY B 2 29 ? 21.874 61.041 52.560 1.00 31.65 ? 29 GLY B C 1 ATOM 2417 O O . GLY B 2 29 ? 21.110 61.847 53.048 1.00 32.11 ? 29 GLY B O 1 ATOM 2418 N N . PHE B 2 30 ? 22.883 61.419 51.786 1.00 30.81 ? 30 PHE B N 1 ATOM 2419 C CA . PHE B 2 30 ? 23.124 62.848 51.515 1.00 30.75 ? 30 PHE B CA 1 ATOM 2420 C C . PHE B 2 30 ? 22.654 63.324 50.128 1.00 32.63 ? 30 PHE B C 1 ATOM 2421 O O . PHE B 2 30 ? 22.530 62.530 49.170 1.00 31.17 ? 30 PHE B O 1 ATOM 2422 C CB . PHE B 2 30 ? 24.601 63.206 51.780 1.00 31.08 ? 30 PHE B CB 1 ATOM 2423 C CG . PHE B 2 30 ? 25.593 62.451 50.909 1.00 28.65 ? 30 PHE B CG 1 ATOM 2424 C CD1 . PHE B 2 30 ? 26.069 61.198 51.287 1.00 28.42 ? 30 PHE B CD1 1 ATOM 2425 C CD2 . PHE B 2 30 ? 26.054 63.014 49.725 1.00 28.88 ? 30 PHE B CD2 1 ATOM 2426 C CE1 . PHE B 2 30 ? 26.983 60.508 50.493 1.00 27.41 ? 30 PHE B CE1 1 ATOM 2427 C CE2 . PHE B 2 30 ? 26.989 62.358 48.928 1.00 28.13 ? 30 PHE B CE2 1 ATOM 2428 C CZ . PHE B 2 30 ? 27.444 61.092 49.297 1.00 27.85 ? 30 PHE B CZ 1 ATOM 2429 N N . HIS B 2 31 ? 22.315 64.611 50.056 1.00 34.11 ? 31 HIS B N 1 ATOM 2430 C CA . HIS B 2 31 ? 21.961 65.269 48.803 1.00 35.81 ? 31 HIS B CA 1 ATOM 2431 C C . HIS B 2 31 ? 22.253 66.736 49.052 1.00 37.88 ? 31 HIS B C 1 ATOM 2432 O O . HIS B 2 31 ? 21.930 67.234 50.129 1.00 38.80 ? 31 HIS B O 1 ATOM 2433 C CB . HIS B 2 31 ? 20.488 65.076 48.486 1.00 38.42 ? 31 HIS B CB 1 ATOM 2434 C CG . HIS B 2 31 ? 20.200 64.887 47.024 1.00 37.96 ? 31 HIS B CG 1 ATOM 2435 N ND1 . HIS B 2 31 ? 20.321 65.908 46.102 1.00 40.88 ? 31 HIS B ND1 1 ATOM 2436 C CD2 . HIS B 2 31 ? 19.791 63.804 46.338 1.00 35.19 ? 31 HIS B CD2 1 ATOM 2437 C CE1 . HIS B 2 31 ? 20.004 65.456 44.904 1.00 41.90 ? 31 HIS B CE1 1 ATOM 2438 N NE2 . HIS B 2 31 ? 19.679 64.178 45.020 1.00 41.54 ? 31 HIS B NE2 1 ATOM 2439 N N . PRO B 2 32 ? 22.918 67.427 48.107 1.00 39.06 ? 32 PRO B N 1 ATOM 2440 C CA . PRO B 2 32 ? 23.419 66.981 46.810 1.00 39.17 ? 32 PRO B CA 1 ATOM 2441 C C . PRO B 2 32 ? 24.667 66.093 46.923 1.00 37.22 ? 32 PRO B C 1 ATOM 2442 O O . PRO B 2 32 ? 25.060 65.744 48.029 1.00 34.25 ? 32 PRO B O 1 ATOM 2443 C CB . PRO B 2 32 ? 23.736 68.285 46.073 1.00 42.71 ? 32 PRO B CB 1 ATOM 2444 C CG . PRO B 2 32 ? 23.482 69.410 47.047 1.00 44.64 ? 32 PRO B CG 1 ATOM 2445 C CD . PRO B 2 32 ? 23.262 68.836 48.388 1.00 41.64 ? 32 PRO B CD 1 ATOM 2446 N N . SER B 2 33 ? 25.270 65.724 45.788 1.00 37.84 ? 33 SER B N 1 ATOM 2447 C CA . SER B 2 33 ? 26.308 64.683 45.748 1.00 37.11 ? 33 SER B CA 1 ATOM 2448 C C . SER B 2 33 ? 27.710 65.149 46.055 1.00 37.65 ? 33 SER B C 1 ATOM 2449 O O . SER B 2 33 ? 28.545 64.317 46.346 1.00 37.32 ? 33 SER B O 1 ATOM 2450 C CB . SER B 2 33 ? 26.355 64.005 44.382 1.00 38.17 ? 33 SER B CB 1 ATOM 2451 O OG . SER B 2 33 ? 26.411 64.997 43.371 1.00 42.44 ? 33 SER B OG 1 ATOM 2452 N N . ASP B 2 34 ? 28.009 66.437 45.932 1.00 40.11 ? 34 ASP B N 1 ATOM 2453 C CA . ASP B 2 34 ? 29.372 66.878 46.225 1.00 42.02 ? 34 ASP B CA 1 ATOM 2454 C C . ASP B 2 34 ? 29.688 66.606 47.695 1.00 39.01 ? 34 ASP B C 1 ATOM 2455 O O . ASP B 2 34 ? 28.942 66.963 48.585 1.00 38.17 ? 34 ASP B O 1 ATOM 2456 C CB . ASP B 2 34 ? 29.618 68.346 45.865 1.00 45.64 ? 34 ASP B CB 1 ATOM 2457 C CG . ASP B 2 34 ? 29.901 68.553 44.367 1.00 53.12 ? 34 ASP B CG 1 ATOM 2458 O OD1 . ASP B 2 34 ? 30.421 67.617 43.683 1.00 56.47 ? 34 ASP B OD1 1 ATOM 2459 O OD2 . ASP B 2 34 ? 29.608 69.667 43.860 1.00 59.65 ? 34 ASP B OD2 1 ATOM 2460 N N . ILE B 2 35 ? 30.800 65.944 47.938 1.00 38.39 ? 35 ILE B N 1 ATOM 2461 C CA . ILE B 2 35 ? 31.151 65.596 49.295 1.00 36.21 ? 35 ILE B CA 1 ATOM 2462 C C . ILE B 2 35 ? 32.663 65.439 49.373 1.00 37.85 ? 35 ILE B C 1 ATOM 2463 O O . ILE B 2 35 ? 33.298 65.116 48.379 1.00 39.09 ? 35 ILE B O 1 ATOM 2464 C CB . ILE B 2 35 ? 30.374 64.341 49.773 1.00 34.41 ? 35 ILE B CB 1 ATOM 2465 C CG1 . ILE B 2 35 ? 30.404 64.225 51.304 1.00 31.66 ? 35 ILE B CG1 1 ATOM 2466 C CG2 . ILE B 2 35 ? 30.885 63.015 49.066 1.00 33.19 ? 35 ILE B CG2 1 ATOM 2467 C CD1 . ILE B 2 35 ? 29.313 63.383 51.885 1.00 31.42 ? 35 ILE B CD1 1 ATOM 2468 N N . GLU B 2 36 ? 33.246 65.749 50.525 1.00 36.96 ? 36 GLU B N 1 ATOM 2469 C CA . GLU B 2 36 ? 34.656 65.505 50.726 1.00 37.19 ? 36 GLU B CA 1 ATOM 2470 C C . GLU B 2 36 ? 34.821 64.641 51.974 1.00 34.21 ? 36 GLU B C 1 ATOM 2471 O O . GLU B 2 36 ? 34.267 64.962 53.016 1.00 33.24 ? 36 GLU B O 1 ATOM 2472 C CB . GLU B 2 36 ? 35.375 66.834 50.885 1.00 41.13 ? 36 GLU B CB 1 ATOM 2473 C CG . GLU B 2 36 ? 36.893 66.703 50.855 1.00 46.07 ? 36 GLU B CG 1 ATOM 2474 C CD . GLU B 2 36 ? 37.598 68.052 50.944 1.00 55.95 ? 36 GLU B CD 1 ATOM 2475 O OE1 . GLU B 2 36 ? 36.894 69.102 50.952 1.00 60.70 ? 36 GLU B OE1 1 ATOM 2476 O OE2 . GLU B 2 36 ? 38.857 68.058 51.022 1.00 57.44 ? 36 GLU B OE2 1 ATOM 2477 N N . VAL B 2 37 ? 35.553 63.530 51.855 1.00 31.96 ? 37 VAL B N 1 ATOM 2478 C CA . VAL B 2 37 ? 35.748 62.596 52.959 1.00 30.35 ? 37 VAL B CA 1 ATOM 2479 C C . VAL B 2 37 ? 37.242 62.316 53.081 1.00 30.99 ? 37 VAL B C 1 ATOM 2480 O O . VAL B 2 37 ? 37.893 62.031 52.058 1.00 30.61 ? 37 VAL B O 1 ATOM 2481 C CB . VAL B 2 37 ? 34.945 61.301 52.727 1.00 28.65 ? 37 VAL B CB 1 ATOM 2482 C CG1 . VAL B 2 37 ? 35.133 60.317 53.862 1.00 27.53 ? 37 VAL B CG1 1 ATOM 2483 C CG2 . VAL B 2 37 ? 33.465 61.650 52.545 1.00 29.97 ? 37 VAL B CG2 1 ATOM 2484 N N . ASP B 2 38 ? 37.799 62.515 54.288 1.00 30.13 ? 38 ASP B N 1 ATOM 2485 C CA . ASP B 2 38 ? 39.192 62.098 54.554 1.00 31.68 ? 38 ASP B CA 1 ATOM 2486 C C . ASP B 2 38 ? 39.192 61.108 55.696 1.00 29.07 ? 38 ASP B C 1 ATOM 2487 O O . ASP B 2 38 ? 38.363 61.220 56.572 1.00 28.43 ? 38 ASP B O 1 ATOM 2488 C CB . ASP B 2 38 ? 40.094 63.272 54.918 1.00 33.91 ? 38 ASP B CB 1 ATOM 2489 C CG . ASP B 2 38 ? 40.140 64.327 53.842 1.00 41.34 ? 38 ASP B CG 1 ATOM 2490 O OD1 . ASP B 2 38 ? 40.173 63.962 52.645 1.00 44.88 ? 38 ASP B OD1 1 ATOM 2491 O OD2 . ASP B 2 38 ? 40.177 65.532 54.189 1.00 49.06 ? 38 ASP B OD2 1 ATOM 2492 N N . LEU B 2 39 ? 40.122 60.154 55.689 1.00 27.79 ? 39 LEU B N 1 ATOM 2493 C CA . LEU B 2 39 ? 40.331 59.280 56.854 1.00 25.83 ? 39 LEU B CA 1 ATOM 2494 C C . LEU B 2 39 ? 41.573 59.808 57.524 1.00 25.98 ? 39 LEU B C 1 ATOM 2495 O O . LEU B 2 39 ? 42.528 60.174 56.853 1.00 27.11 ? 39 LEU B O 1 ATOM 2496 C CB . LEU B 2 39 ? 40.549 57.842 56.411 1.00 25.18 ? 39 LEU B CB 1 ATOM 2497 C CG . LEU B 2 39 ? 39.418 57.270 55.529 1.00 28.35 ? 39 LEU B CG 1 ATOM 2498 C CD1 . LEU B 2 39 ? 39.690 55.806 55.238 1.00 28.18 ? 39 LEU B CD1 1 ATOM 2499 C CD2 . LEU B 2 39 ? 38.043 57.401 56.185 1.00 30.19 ? 39 LEU B CD2 1 ATOM 2500 N N . LEU B 2 40 ? 41.557 59.838 58.851 1.00 25.79 ? 40 LEU B N 1 ATOM 2501 C CA . LEU B 2 40 ? 42.614 60.515 59.665 1.00 26.62 ? 40 LEU B CA 1 ATOM 2502 C C . LEU B 2 40 ? 43.275 59.511 60.586 1.00 26.17 ? 40 LEU B C 1 ATOM 2503 O O . LEU B 2 40 ? 42.642 58.572 61.075 1.00 26.14 ? 40 LEU B O 1 ATOM 2504 C CB . LEU B 2 40 ? 41.997 61.657 60.489 1.00 27.97 ? 40 LEU B CB 1 ATOM 2505 C CG . LEU B 2 40 ? 41.124 62.728 59.782 1.00 27.81 ? 40 LEU B CG 1 ATOM 2506 C CD1 . LEU B 2 40 ? 40.514 63.718 60.798 1.00 33.15 ? 40 LEU B CD1 1 ATOM 2507 C CD2 . LEU B 2 40 ? 41.956 63.520 58.710 1.00 28.92 ? 40 LEU B CD2 1 ATOM 2508 N N . LYS B 2 41 ? 44.555 59.692 60.827 1.00 26.95 ? 41 LYS B N 1 ATOM 2509 C CA . LYS B 2 41 ? 45.271 58.881 61.792 1.00 26.93 ? 41 LYS B CA 1 ATOM 2510 C C . LYS B 2 41 ? 45.917 59.918 62.704 1.00 29.73 ? 41 LYS B C 1 ATOM 2511 O O . LYS B 2 41 ? 46.732 60.744 62.229 1.00 30.56 ? 41 LYS B O 1 ATOM 2512 C CB . LYS B 2 41 ? 46.399 58.121 61.106 1.00 27.54 ? 41 LYS B CB 1 ATOM 2513 C CG . LYS B 2 41 ? 47.221 57.231 62.065 1.00 26.01 ? 41 LYS B CG 1 ATOM 2514 C CD . LYS B 2 41 ? 48.331 56.541 61.341 1.00 27.88 ? 41 LYS B CD 1 ATOM 2515 C CE . LYS B 2 41 ? 49.201 55.761 62.325 1.00 32.57 ? 41 LYS B CE 1 ATOM 2516 N NZ . LYS B 2 41 ? 50.294 55.067 61.625 1.00 39.12 ? 41 LYS B NZ 1 ATOM 2517 N N . ASN B 2 42 ? 45.570 59.881 63.996 1.00 28.84 ? 42 ASN B N 1 ATOM 2518 C CA . ASN B 2 42 ? 46.130 60.813 64.946 1.00 32.09 ? 42 ASN B CA 1 ATOM 2519 C C . ASN B 2 42 ? 46.003 62.210 64.402 1.00 34.23 ? 42 ASN B C 1 ATOM 2520 O O . ASN B 2 42 ? 46.949 62.996 64.457 1.00 37.11 ? 42 ASN B O 1 ATOM 2521 C CB . ASN B 2 42 ? 47.594 60.502 65.210 1.00 32.77 ? 42 ASN B CB 1 ATOM 2522 C CG . ASN B 2 42 ? 47.808 59.123 65.810 1.00 32.51 ? 42 ASN B CG 1 ATOM 2523 O OD1 . ASN B 2 42 ? 46.956 58.597 66.525 1.00 30.61 ? 42 ASN B OD1 1 ATOM 2524 N ND2 . ASN B 2 42 ? 48.955 58.553 65.548 1.00 31.49 ? 42 ASN B ND2 1 ATOM 2525 N N . GLY B 2 43 ? 44.841 62.481 63.832 1.00 33.51 ? 43 GLY B N 1 ATOM 2526 C CA . GLY B 2 43 ? 44.488 63.836 63.377 1.00 37.59 ? 43 GLY B CA 1 ATOM 2527 C C . GLY B 2 43 ? 44.894 64.247 61.974 1.00 38.61 ? 43 GLY B C 1 ATOM 2528 O O . GLY B 2 43 ? 44.456 65.297 61.501 1.00 39.76 ? 43 GLY B O 1 ATOM 2529 N N . GLU B 2 44 ? 45.755 63.446 61.328 1.00 37.97 ? 44 GLU B N 1 ATOM 2530 C CA . GLU B 2 44 ? 46.282 63.784 60.003 1.00 39.57 ? 44 GLU B CA 1 ATOM 2531 C C . GLU B 2 44 ? 45.706 62.909 58.899 1.00 36.82 ? 44 GLU B C 1 ATOM 2532 O O . GLU B 2 44 ? 45.591 61.715 59.059 1.00 35.35 ? 44 GLU B O 1 ATOM 2533 C CB . GLU B 2 44 ? 47.788 63.715 60.012 1.00 42.30 ? 44 GLU B CB 1 ATOM 2534 C CG . GLU B 2 44 ? 48.356 64.612 61.113 1.00 46.77 ? 44 GLU B CG 1 ATOM 2535 C CD . GLU B 2 44 ? 49.800 64.910 60.962 1.00 52.94 ? 44 GLU B CD 1 ATOM 2536 O OE1 . GLU B 2 44 ? 50.605 64.234 61.644 1.00 55.64 ? 44 GLU B OE1 1 ATOM 2537 O OE2 . GLU B 2 44 ? 50.125 65.845 60.192 1.00 57.58 ? 44 GLU B OE2 1 ATOM 2538 N N . ARG B 2 45 ? 45.335 63.541 57.800 1.00 37.50 ? 45 ARG B N 1 ATOM 2539 C CA . ARG B 2 45 ? 44.838 62.887 56.594 1.00 36.20 ? 45 ARG B CA 1 ATOM 2540 C C . ARG B 2 45 ? 45.686 61.682 56.173 1.00 36.18 ? 45 ARG B C 1 ATOM 2541 O O . ARG B 2 45 ? 46.886 61.769 56.071 1.00 38.46 ? 45 ARG B O 1 ATOM 2542 C CB . ARG B 2 45 ? 44.796 63.929 55.470 1.00 38.87 ? 45 ARG B CB 1 ATOM 2543 C CG . ARG B 2 45 ? 44.052 63.506 54.246 1.00 41.25 ? 45 ARG B CG 1 ATOM 2544 C CD . ARG B 2 45 ? 43.983 64.643 53.267 1.00 48.22 ? 45 ARG B CD 1 ATOM 2545 N NE . ARG B 2 45 ? 43.767 64.060 51.958 1.00 54.96 ? 45 ARG B NE 1 ATOM 2546 C CZ . ARG B 2 45 ? 44.749 63.704 51.134 1.00 60.70 ? 45 ARG B CZ 1 ATOM 2547 N NH1 . ARG B 2 45 ? 46.023 63.914 51.471 1.00 63.74 ? 45 ARG B NH1 1 ATOM 2548 N NH2 . ARG B 2 45 ? 44.454 63.159 49.961 1.00 62.97 ? 45 ARG B NH2 1 ATOM 2549 N N . ILE B 2 46 ? 45.058 60.541 55.955 1.00 34.95 ? 46 ILE B N 1 ATOM 2550 C CA . ILE B 2 46 ? 45.780 59.388 55.398 1.00 36.02 ? 46 ILE B CA 1 ATOM 2551 C C . ILE B 2 46 ? 45.843 59.575 53.860 1.00 38.92 ? 46 ILE B C 1 ATOM 2552 O O . ILE B 2 46 ? 44.854 59.962 53.231 1.00 38.26 ? 46 ILE B O 1 ATOM 2553 C CB . ILE B 2 46 ? 45.079 58.025 55.826 1.00 33.61 ? 46 ILE B CB 1 ATOM 2554 C CG1 . ILE B 2 46 ? 45.045 57.869 57.349 1.00 30.97 ? 46 ILE B CG1 1 ATOM 2555 C CG2 . ILE B 2 46 ? 45.752 56.800 55.140 1.00 34.37 ? 46 ILE B CG2 1 ATOM 2556 C CD1 . ILE B 2 46 ? 44.198 56.663 57.874 1.00 28.45 ? 46 ILE B CD1 1 ATOM 2557 N N . GLU B 2 47 ? 47.005 59.305 53.270 1.00 43.38 ? 47 GLU B N 1 ATOM 2558 C CA . GLU B 2 47 ? 47.250 59.523 51.836 1.00 47.80 ? 47 GLU B CA 1 ATOM 2559 C C . GLU B 2 47 ? 46.603 58.521 50.881 1.00 46.82 ? 47 GLU B C 1 ATOM 2560 O O . GLU B 2 47 ? 46.040 58.910 49.848 1.00 48.27 ? 47 GLU B O 1 ATOM 2561 C CB . GLU B 2 47 ? 48.747 59.573 51.559 1.00 52.44 ? 47 GLU B CB 1 ATOM 2562 C CG . GLU B 2 47 ? 49.457 60.815 52.114 1.00 59.55 ? 47 GLU B CG 1 ATOM 2563 C CD . GLU B 2 47 ? 48.818 62.111 51.627 1.00 65.68 ? 47 GLU B CD 1 ATOM 2564 O OE1 . GLU B 2 47 ? 49.062 62.488 50.451 1.00 70.20 ? 47 GLU B OE1 1 ATOM 2565 O OE2 . GLU B 2 47 ? 48.075 62.741 52.425 1.00 64.68 ? 47 GLU B OE2 1 ATOM 2566 N N . LYS B 2 48 ? 46.680 57.238 51.210 1.00 45.52 ? 48 LYS B N 1 ATOM 2567 C CA . LYS B 2 48 ? 46.214 56.216 50.280 1.00 46.22 ? 48 LYS B CA 1 ATOM 2568 C C . LYS B 2 48 ? 44.840 55.759 50.734 1.00 42.84 ? 48 LYS B C 1 ATOM 2569 O O . LYS B 2 48 ? 44.695 54.879 51.618 1.00 43.35 ? 48 LYS B O 1 ATOM 2570 C CB . LYS B 2 48 ? 47.212 55.061 50.166 1.00 48.55 ? 48 LYS B CB 1 ATOM 2571 N N . VAL B 2 49 ? 43.820 56.421 50.199 1.00 40.11 ? 49 VAL B N 1 ATOM 2572 C CA . VAL B 2 49 ? 42.449 56.111 50.588 1.00 35.54 ? 49 VAL B CA 1 ATOM 2573 C C . VAL B 2 49 ? 41.640 55.896 49.317 1.00 35.80 ? 49 VAL B C 1 ATOM 2574 O O . VAL B 2 49 ? 41.665 56.728 48.417 1.00 36.62 ? 49 VAL B O 1 ATOM 2575 C CB . VAL B 2 49 ? 41.831 57.230 51.454 1.00 33.62 ? 49 VAL B CB 1 ATOM 2576 C CG1 . VAL B 2 49 ? 40.343 56.934 51.731 1.00 32.55 ? 49 VAL B CG1 1 ATOM 2577 C CG2 . VAL B 2 49 ? 42.610 57.354 52.787 1.00 30.80 ? 49 VAL B CG2 1 ATOM 2578 N N . GLU B 2 50 ? 40.939 54.770 49.231 1.00 33.82 ? 50 GLU B N 1 ATOM 2579 C CA . GLU B 2 50 ? 40.177 54.467 48.028 1.00 34.00 ? 50 GLU B CA 1 ATOM 2580 C C . GLU B 2 50 ? 38.712 54.768 48.295 1.00 30.82 ? 50 GLU B C 1 ATOM 2581 O O . GLU B 2 50 ? 38.301 54.987 49.437 1.00 28.54 ? 50 GLU B O 1 ATOM 2582 C CB . GLU B 2 50 ? 40.402 52.994 47.629 1.00 36.58 ? 50 GLU B CB 1 ATOM 2583 C CG . GLU B 2 50 ? 41.819 52.639 47.130 1.00 44.12 ? 50 GLU B CG 1 ATOM 2584 C CD . GLU B 2 50 ? 42.071 53.092 45.691 1.00 55.04 ? 50 GLU B CD 1 ATOM 2585 O OE1 . GLU B 2 50 ? 41.123 53.618 45.043 1.00 58.17 ? 50 GLU B OE1 1 ATOM 2586 O OE2 . GLU B 2 50 ? 43.213 52.923 45.184 1.00 61.65 ? 50 GLU B OE2 1 ATOM 2587 N N . HIS B 2 51 ? 37.898 54.795 47.262 1.00 30.38 ? 51 HIS B N 1 ATOM 2588 C CA . HIS B 2 51 ? 36.475 54.913 47.507 1.00 29.65 ? 51 HIS B CA 1 ATOM 2589 C C . HIS B 2 51 ? 35.677 54.251 46.402 1.00 31.50 ? 51 HIS B C 1 ATOM 2590 O O . HIS B 2 51 ? 36.210 53.966 45.338 1.00 32.78 ? 51 HIS B O 1 ATOM 2591 C CB . HIS B 2 51 ? 36.065 56.372 47.726 1.00 28.75 ? 51 HIS B CB 1 ATOM 2592 C CG . HIS B 2 51 ? 36.297 57.263 46.547 1.00 34.50 ? 51 HIS B CG 1 ATOM 2593 N ND1 . HIS B 2 51 ? 35.404 57.367 45.504 1.00 38.77 ? 51 HIS B ND1 1 ATOM 2594 C CD2 . HIS B 2 51 ? 37.320 58.097 46.252 1.00 36.94 ? 51 HIS B CD2 1 ATOM 2595 C CE1 . HIS B 2 51 ? 35.874 58.217 44.610 1.00 41.89 ? 51 HIS B CE1 1 ATOM 2596 N NE2 . HIS B 2 51 ? 37.033 58.676 45.043 1.00 41.95 ? 51 HIS B NE2 1 ATOM 2597 N N . SER B 2 52 ? 34.401 53.993 46.665 1.00 31.39 ? 52 SER B N 1 ATOM 2598 C CA . SER B 2 52 ? 33.566 53.290 45.702 1.00 34.69 ? 52 SER B CA 1 ATOM 2599 C C . SER B 2 52 ? 33.051 54.315 44.698 1.00 36.43 ? 52 SER B C 1 ATOM 2600 O O . SER B 2 52 ? 33.288 55.516 44.840 1.00 35.99 ? 52 SER B O 1 ATOM 2601 C CB . SER B 2 52 ? 32.402 52.612 46.431 1.00 33.96 ? 52 SER B CB 1 ATOM 2602 O OG . SER B 2 52 ? 31.598 53.582 47.104 1.00 30.57 ? 52 SER B OG 1 ATOM 2603 N N . ASP B 2 53 ? 32.360 53.848 43.676 1.00 38.82 ? 53 ASP B N 1 ATOM 2604 C CA . ASP B 2 53 ? 31.707 54.769 42.744 1.00 41.86 ? 53 ASP B CA 1 ATOM 2605 C C . ASP B 2 53 ? 30.449 55.377 43.352 1.00 39.79 ? 53 ASP B C 1 ATOM 2606 O O . ASP B 2 53 ? 29.658 54.658 43.931 1.00 40.33 ? 53 ASP B O 1 ATOM 2607 C CB . ASP B 2 53 ? 31.413 54.025 41.435 1.00 44.73 ? 53 ASP B CB 1 ATOM 2608 C CG . ASP B 2 53 ? 32.696 53.646 40.702 1.00 51.28 ? 53 ASP B CG 1 ATOM 2609 O OD1 . ASP B 2 53 ? 33.453 54.575 40.323 1.00 55.11 ? 53 ASP B OD1 1 ATOM 2610 O OD2 . ASP B 2 53 ? 32.976 52.431 40.540 1.00 56.82 ? 53 ASP B OD2 1 ATOM 2611 N N . LEU B 2 54 ? 30.272 56.689 43.256 1.00 40.16 ? 54 LEU B N 1 ATOM 2612 C CA . LEU B 2 54 ? 29.055 57.336 43.800 1.00 38.81 ? 54 LEU B CA 1 ATOM 2613 C C . LEU B 2 54 ? 27.834 56.652 43.216 1.00 39.04 ? 54 LEU B C 1 ATOM 2614 O O . LEU B 2 54 ? 27.744 56.496 42.016 1.00 41.96 ? 54 LEU B O 1 ATOM 2615 C CB . LEU B 2 54 ? 28.985 58.820 43.431 1.00 40.05 ? 54 LEU B CB 1 ATOM 2616 C CG . LEU B 2 54 ? 27.780 59.670 43.873 1.00 39.75 ? 54 LEU B CG 1 ATOM 2617 C CD1 . LEU B 2 54 ? 27.919 60.120 45.330 1.00 36.12 ? 54 LEU B CD1 1 ATOM 2618 C CD2 . LEU B 2 54 ? 27.644 60.882 42.955 1.00 41.88 ? 54 LEU B CD2 1 ATOM 2619 N N . SER B 2 55 ? 26.910 56.204 44.053 1.00 37.16 ? 55 SER B N 1 ATOM 2620 C CA . SER B 2 55 ? 25.595 55.862 43.514 1.00 37.16 ? 55 SER B CA 1 ATOM 2621 C C . SER B 2 55 ? 24.516 56.378 44.438 1.00 34.61 ? 55 SER B C 1 ATOM 2622 O O . SER B 2 55 ? 24.796 57.222 45.264 1.00 32.66 ? 55 SER B O 1 ATOM 2623 C CB . SER B 2 55 ? 25.422 54.376 43.196 1.00 37.90 ? 55 SER B CB 1 ATOM 2624 O OG . SER B 2 55 ? 24.475 54.265 42.136 1.00 41.00 ? 55 SER B OG 1 ATOM 2625 N N . PHE B 2 56 ? 23.294 55.901 44.278 1.00 33.89 ? 56 PHE B N 1 ATOM 2626 C CA . PHE B 2 56 ? 22.212 56.432 45.083 1.00 34.53 ? 56 PHE B CA 1 ATOM 2627 C C . PHE B 2 56 ? 21.156 55.373 45.356 1.00 36.34 ? 56 PHE B C 1 ATOM 2628 O O . PHE B 2 56 ? 21.070 54.360 44.637 1.00 37.67 ? 56 PHE B O 1 ATOM 2629 C CB . PHE B 2 56 ? 21.635 57.737 44.469 1.00 32.60 ? 56 PHE B CB 1 ATOM 2630 C CG . PHE B 2 56 ? 21.023 57.573 43.079 1.00 35.43 ? 56 PHE B CG 1 ATOM 2631 C CD1 . PHE B 2 56 ? 19.717 57.128 42.922 1.00 33.59 ? 56 PHE B CD1 1 ATOM 2632 C CD2 . PHE B 2 56 ? 21.743 57.910 41.932 1.00 32.71 ? 56 PHE B CD2 1 ATOM 2633 C CE1 . PHE B 2 56 ? 19.133 57.010 41.665 1.00 36.35 ? 56 PHE B CE1 1 ATOM 2634 C CE2 . PHE B 2 56 ? 21.185 57.777 40.685 1.00 35.93 ? 56 PHE B CE2 1 ATOM 2635 C CZ . PHE B 2 56 ? 19.870 57.333 40.540 1.00 37.90 ? 56 PHE B CZ 1 ATOM 2636 N N . SER B 2 57 ? 20.385 55.615 46.412 1.00 37.00 ? 57 SER B N 1 ATOM 2637 C CA . SER B 2 57 ? 19.360 54.695 46.863 1.00 39.29 ? 57 SER B CA 1 ATOM 2638 C C . SER B 2 57 ? 17.998 55.059 46.289 1.00 42.10 ? 57 SER B C 1 ATOM 2639 O O . SER B 2 57 ? 17.828 56.087 45.604 1.00 42.30 ? 57 SER B O 1 ATOM 2640 C CB . SER B 2 57 ? 19.281 54.724 48.385 1.00 39.11 ? 57 SER B CB 1 ATOM 2641 O OG . SER B 2 57 ? 20.546 54.517 49.007 1.00 39.56 ? 57 SER B OG 1 ATOM 2642 N N . LYS B 2 58 ? 17.011 54.216 46.602 1.00 44.40 ? 58 LYS B N 1 ATOM 2643 C CA . LYS B 2 58 ? 15.637 54.395 46.141 1.00 46.99 ? 58 LYS B CA 1 ATOM 2644 C C . LYS B 2 58 ? 15.059 55.775 46.495 1.00 46.89 ? 58 LYS B C 1 ATOM 2645 O O . LYS B 2 58 ? 14.224 56.294 45.757 1.00 49.68 ? 58 LYS B O 1 ATOM 2646 C CB . LYS B 2 58 ? 14.736 53.266 46.682 1.00 49.51 ? 58 LYS B CB 1 ATOM 2647 N N . ASP B 2 59 ? 15.488 56.377 47.601 1.00 44.44 ? 59 ASP B N 1 ATOM 2648 C CA . ASP B 2 59 ? 14.966 57.697 47.960 1.00 44.97 ? 59 ASP B CA 1 ATOM 2649 C C . ASP B 2 59 ? 15.762 58.844 47.294 1.00 42.82 ? 59 ASP B C 1 ATOM 2650 O O . ASP B 2 59 ? 15.585 60.016 47.641 1.00 42.59 ? 59 ASP B O 1 ATOM 2651 C CB . ASP B 2 59 ? 14.827 57.871 49.491 1.00 44.94 ? 59 ASP B CB 1 ATOM 2652 C CG . ASP B 2 59 ? 16.164 57.944 50.220 1.00 45.34 ? 59 ASP B CG 1 ATOM 2653 O OD1 . ASP B 2 59 ? 16.151 58.397 51.382 1.00 47.97 ? 59 ASP B OD1 1 ATOM 2654 O OD2 . ASP B 2 59 ? 17.227 57.561 49.666 1.00 43.71 ? 59 ASP B OD2 1 ATOM 2655 N N . TRP B 2 60 ? 16.609 58.481 46.316 1.00 39.84 ? 60 TRP B N 1 ATOM 2656 C CA . TRP B 2 60 ? 17.446 59.428 45.546 1.00 37.63 ? 60 TRP B CA 1 ATOM 2657 C C . TRP B 2 60 ? 18.668 59.928 46.269 1.00 35.94 ? 60 TRP B C 1 ATOM 2658 O O . TRP B 2 60 ? 19.473 60.665 45.677 1.00 35.26 ? 60 TRP B O 1 ATOM 2659 C CB . TRP B 2 60 ? 16.655 60.632 44.999 1.00 39.00 ? 60 TRP B CB 1 ATOM 2660 C CG . TRP B 2 60 ? 15.460 60.243 44.165 1.00 40.09 ? 60 TRP B CG 1 ATOM 2661 C CD1 . TRP B 2 60 ? 14.157 60.351 44.523 1.00 41.50 ? 60 TRP B CD1 1 ATOM 2662 C CD2 . TRP B 2 60 ? 15.468 59.687 42.843 1.00 41.60 ? 60 TRP B CD2 1 ATOM 2663 N NE1 . TRP B 2 60 ? 13.351 59.899 43.523 1.00 43.10 ? 60 TRP B NE1 1 ATOM 2664 C CE2 . TRP B 2 60 ? 14.126 59.488 42.472 1.00 43.43 ? 60 TRP B CE2 1 ATOM 2665 C CE3 . TRP B 2 60 ? 16.479 59.331 41.940 1.00 41.29 ? 60 TRP B CE3 1 ATOM 2666 C CZ2 . TRP B 2 60 ? 13.761 58.957 41.240 1.00 45.84 ? 60 TRP B CZ2 1 ATOM 2667 C CZ3 . TRP B 2 60 ? 16.120 58.809 40.719 1.00 41.67 ? 60 TRP B CZ3 1 ATOM 2668 C CH2 . TRP B 2 60 ? 14.773 58.624 40.377 1.00 45.81 ? 60 TRP B CH2 1 ATOM 2669 N N . SER B 2 61 ? 18.846 59.530 47.526 1.00 34.52 ? 61 SER B N 1 ATOM 2670 C CA . SER B 2 61 ? 19.952 60.059 48.298 1.00 33.68 ? 61 SER B CA 1 ATOM 2671 C C . SER B 2 61 ? 21.219 59.278 47.997 1.00 31.64 ? 61 SER B C 1 ATOM 2672 O O . SER B 2 61 ? 21.154 58.076 47.713 1.00 31.29 ? 61 SER B O 1 ATOM 2673 C CB . SER B 2 61 ? 19.646 60.059 49.801 1.00 33.56 ? 61 SER B CB 1 ATOM 2674 O OG . SER B 2 61 ? 19.555 58.725 50.275 1.00 34.30 ? 61 SER B OG 1 ATOM 2675 N N . PHE B 2 62 ? 22.372 59.952 48.079 1.00 30.39 ? 62 PHE B N 1 ATOM 2676 C CA . PHE B 2 62 ? 23.639 59.348 47.604 1.00 29.65 ? 62 PHE B CA 1 ATOM 2677 C C . PHE B 2 62 ? 24.345 58.563 48.694 1.00 28.97 ? 62 PHE B C 1 ATOM 2678 O O . PHE B 2 62 ? 24.116 58.812 49.871 1.00 26.76 ? 62 PHE B O 1 ATOM 2679 C CB . PHE B 2 62 ? 24.586 60.448 47.082 1.00 30.19 ? 62 PHE B CB 1 ATOM 2680 C CG . PHE B 2 62 ? 24.071 61.159 45.864 1.00 32.70 ? 62 PHE B CG 1 ATOM 2681 C CD1 . PHE B 2 62 ? 24.138 60.550 44.599 1.00 35.09 ? 62 PHE B CD1 1 ATOM 2682 C CD2 . PHE B 2 62 ? 23.523 62.432 45.972 1.00 34.62 ? 62 PHE B CD2 1 ATOM 2683 C CE1 . PHE B 2 62 ? 23.636 61.192 43.455 1.00 35.60 ? 62 PHE B CE1 1 ATOM 2684 C CE2 . PHE B 2 62 ? 23.027 63.087 44.838 1.00 36.36 ? 62 PHE B CE2 1 ATOM 2685 C CZ . PHE B 2 62 ? 23.087 62.456 43.566 1.00 36.58 ? 62 PHE B CZ 1 ATOM 2686 N N . TYR B 2 63 ? 25.214 57.622 48.293 1.00 29.60 ? 63 TYR B N 1 ATOM 2687 C CA . TYR B 2 63 ? 26.080 56.952 49.240 1.00 28.49 ? 63 TYR B CA 1 ATOM 2688 C C . TYR B 2 63 ? 27.431 56.680 48.606 1.00 29.05 ? 63 TYR B C 1 ATOM 2689 O O . TYR B 2 63 ? 27.507 56.476 47.389 1.00 29.08 ? 63 TYR B O 1 ATOM 2690 C CB . TYR B 2 63 ? 25.444 55.655 49.765 1.00 29.31 ? 63 TYR B CB 1 ATOM 2691 C CG . TYR B 2 63 ? 25.160 54.597 48.734 1.00 32.77 ? 63 TYR B CG 1 ATOM 2692 C CD1 . TYR B 2 63 ? 26.148 53.694 48.352 1.00 35.83 ? 63 TYR B CD1 1 ATOM 2693 C CD2 . TYR B 2 63 ? 23.903 54.474 48.154 1.00 33.11 ? 63 TYR B CD2 1 ATOM 2694 C CE1 . TYR B 2 63 ? 25.898 52.692 47.387 1.00 36.50 ? 63 TYR B CE1 1 ATOM 2695 C CE2 . TYR B 2 63 ? 23.635 53.452 47.183 1.00 37.37 ? 63 TYR B CE2 1 ATOM 2696 C CZ . TYR B 2 63 ? 24.650 52.586 46.815 1.00 37.14 ? 63 TYR B CZ 1 ATOM 2697 O OH . TYR B 2 63 ? 24.448 51.588 45.887 1.00 41.06 ? 63 TYR B OH 1 ATOM 2698 N N . LEU B 2 64 ? 28.463 56.621 49.451 1.00 27.88 ? 64 LEU B N 1 ATOM 2699 C CA . LEU B 2 64 ? 29.865 56.359 49.072 1.00 28.71 ? 64 LEU B CA 1 ATOM 2700 C C . LEU B 2 64 ? 30.555 55.611 50.210 1.00 26.39 ? 64 LEU B C 1 ATOM 2701 O O . LEU B 2 64 ? 30.283 55.883 51.362 1.00 25.96 ? 64 LEU B O 1 ATOM 2702 C CB . LEU B 2 64 ? 30.610 57.714 48.898 1.00 30.24 ? 64 LEU B CB 1 ATOM 2703 C CG . LEU B 2 64 ? 30.599 58.311 47.499 1.00 37.02 ? 64 LEU B CG 1 ATOM 2704 C CD1 . LEU B 2 64 ? 30.952 59.784 47.512 1.00 39.65 ? 64 LEU B CD1 1 ATOM 2705 C CD2 . LEU B 2 64 ? 31.657 57.580 46.718 1.00 38.36 ? 64 LEU B CD2 1 ATOM 2706 N N . LEU B 2 65 ? 31.435 54.674 49.883 1.00 25.56 ? 65 LEU B N 1 ATOM 2707 C CA . LEU B 2 65 ? 32.283 54.006 50.863 1.00 24.05 ? 65 LEU B CA 1 ATOM 2708 C C . LEU B 2 65 ? 33.726 54.462 50.619 1.00 24.60 ? 65 LEU B C 1 ATOM 2709 O O . LEU B 2 65 ? 34.252 54.280 49.524 1.00 23.84 ? 65 LEU B O 1 ATOM 2710 C CB . LEU B 2 65 ? 32.211 52.479 50.681 1.00 24.14 ? 65 LEU B CB 1 ATOM 2711 C CG . LEU B 2 65 ? 33.130 51.669 51.623 1.00 24.39 ? 65 LEU B CG 1 ATOM 2712 C CD1 . LEU B 2 65 ? 32.632 51.898 53.051 1.00 24.42 ? 65 LEU B CD1 1 ATOM 2713 C CD2 . LEU B 2 65 ? 33.164 50.177 51.257 1.00 26.48 ? 65 LEU B CD2 1 ATOM 2714 N N . TYR B 2 66 ? 34.353 55.035 51.633 1.00 23.61 ? 66 TYR B N 1 ATOM 2715 C CA . TYR B 2 66 ? 35.787 55.290 51.601 1.00 25.17 ? 66 TYR B CA 1 ATOM 2716 C C . TYR B 2 66 ? 36.510 54.249 52.468 1.00 25.33 ? 66 TYR B C 1 ATOM 2717 O O . TYR B 2 66 ? 36.020 53.870 53.529 1.00 23.41 ? 66 TYR B O 1 ATOM 2718 C CB . TYR B 2 66 ? 36.055 56.674 52.167 1.00 26.31 ? 66 TYR B CB 1 ATOM 2719 C CG . TYR B 2 66 ? 35.747 57.786 51.192 1.00 27.53 ? 66 TYR B CG 1 ATOM 2720 C CD1 . TYR B 2 66 ? 36.760 58.448 50.525 1.00 28.09 ? 66 TYR B CD1 1 ATOM 2721 C CD2 . TYR B 2 66 ? 34.440 58.134 50.915 1.00 29.90 ? 66 TYR B CD2 1 ATOM 2722 C CE1 . TYR B 2 66 ? 36.465 59.462 49.604 1.00 33.97 ? 66 TYR B CE1 1 ATOM 2723 C CE2 . TYR B 2 66 ? 34.135 59.146 50.018 1.00 30.34 ? 66 TYR B CE2 1 ATOM 2724 C CZ . TYR B 2 66 ? 35.146 59.801 49.378 1.00 31.78 ? 66 TYR B CZ 1 ATOM 2725 O OH . TYR B 2 66 ? 34.828 60.821 48.498 1.00 39.12 ? 66 TYR B OH 1 ATOM 2726 N N . TYR B 2 67 ? 37.695 53.839 52.059 1.00 26.13 ? 67 TYR B N 1 ATOM 2727 C CA . TYR B 2 67 ? 38.380 52.807 52.797 1.00 26.32 ? 67 TYR B CA 1 ATOM 2728 C C . TYR B 2 67 ? 39.880 52.800 52.600 1.00 28.02 ? 67 TYR B C 1 ATOM 2729 O O . TYR B 2 67 ? 40.405 53.333 51.603 1.00 26.99 ? 67 TYR B O 1 ATOM 2730 C CB . TYR B 2 67 ? 37.823 51.420 52.404 1.00 27.63 ? 67 TYR B CB 1 ATOM 2731 C CG . TYR B 2 67 ? 37.947 51.081 50.934 1.00 29.68 ? 67 TYR B CG 1 ATOM 2732 C CD1 . TYR B 2 67 ? 36.980 51.506 50.024 1.00 28.73 ? 67 TYR B CD1 1 ATOM 2733 C CD2 . TYR B 2 67 ? 39.013 50.315 50.458 1.00 31.91 ? 67 TYR B CD2 1 ATOM 2734 C CE1 . TYR B 2 67 ? 37.082 51.198 48.679 1.00 31.06 ? 67 TYR B CE1 1 ATOM 2735 C CE2 . TYR B 2 67 ? 39.120 49.991 49.091 1.00 35.59 ? 67 TYR B CE2 1 ATOM 2736 C CZ . TYR B 2 67 ? 38.131 50.438 48.224 1.00 34.21 ? 67 TYR B CZ 1 ATOM 2737 O OH . TYR B 2 67 ? 38.181 50.108 46.897 1.00 38.29 ? 67 TYR B OH 1 ATOM 2738 N N . THR B 2 68 ? 40.573 52.146 53.546 1.00 28.12 ? 68 THR B N 1 ATOM 2739 C CA . THR B 2 68 ? 42.027 52.112 53.554 1.00 29.83 ? 68 THR B CA 1 ATOM 2740 C C . THR B 2 68 ? 42.477 50.910 54.392 1.00 31.69 ? 68 THR B C 1 ATOM 2741 O O . THR B 2 68 ? 41.855 50.561 55.405 1.00 30.20 ? 68 THR B O 1 ATOM 2742 C CB . THR B 2 68 ? 42.649 53.447 54.090 1.00 29.86 ? 68 THR B CB 1 ATOM 2743 O OG1 . THR B 2 68 ? 44.017 53.499 53.694 1.00 35.82 ? 68 THR B OG1 1 ATOM 2744 C CG2 . THR B 2 68 ? 42.602 53.534 55.604 1.00 28.70 ? 68 THR B CG2 1 ATOM 2745 N N . GLU B 2 69 ? 43.535 50.257 53.938 1.00 34.86 ? 69 GLU B N 1 ATOM 2746 C CA . GLU B 2 69 ? 44.193 49.205 54.694 1.00 38.12 ? 69 GLU B CA 1 ATOM 2747 C C . GLU B 2 69 ? 44.886 49.869 55.868 1.00 37.90 ? 69 GLU B C 1 ATOM 2748 O O . GLU B 2 69 ? 45.520 50.910 55.707 1.00 38.47 ? 69 GLU B O 1 ATOM 2749 C CB . GLU B 2 69 ? 45.204 48.496 53.781 1.00 41.62 ? 69 GLU B CB 1 ATOM 2750 C CG . GLU B 2 69 ? 46.081 47.458 54.473 1.00 49.41 ? 69 GLU B CG 1 ATOM 2751 C CD . GLU B 2 69 ? 46.645 46.418 53.514 1.00 59.83 ? 69 GLU B CD 1 ATOM 2752 O OE1 . GLU B 2 69 ? 46.171 46.334 52.345 1.00 64.67 ? 69 GLU B OE1 1 ATOM 2753 O OE2 . GLU B 2 69 ? 47.553 45.654 53.938 1.00 67.60 ? 69 GLU B OE2 1 ATOM 2754 N N . PHE B 2 70 ? 44.732 49.318 57.068 1.00 37.31 ? 70 PHE B N 1 ATOM 2755 C CA . PHE B 2 70 ? 45.457 49.852 58.210 1.00 36.25 ? 70 PHE B CA 1 ATOM 2756 C C . PHE B 2 70 ? 45.819 48.748 59.189 1.00 38.39 ? 70 PHE B C 1 ATOM 2757 O O . PHE B 2 70 ? 45.269 47.650 59.117 1.00 40.04 ? 70 PHE B O 1 ATOM 2758 C CB . PHE B 2 70 ? 44.703 51.011 58.892 1.00 34.04 ? 70 PHE B CB 1 ATOM 2759 C CG . PHE B 2 70 ? 43.561 50.575 59.781 1.00 31.26 ? 70 PHE B CG 1 ATOM 2760 C CD1 . PHE B 2 70 ? 42.674 49.591 59.371 1.00 31.45 ? 70 PHE B CD1 1 ATOM 2761 C CD2 . PHE B 2 70 ? 43.373 51.162 61.019 1.00 31.59 ? 70 PHE B CD2 1 ATOM 2762 C CE1 . PHE B 2 70 ? 41.627 49.198 60.200 1.00 32.59 ? 70 PHE B CE1 1 ATOM 2763 C CE2 . PHE B 2 70 ? 42.324 50.771 61.848 1.00 29.70 ? 70 PHE B CE2 1 ATOM 2764 C CZ . PHE B 2 70 ? 41.463 49.802 61.447 1.00 31.53 ? 70 PHE B CZ 1 ATOM 2765 N N . THR B 2 71 ? 46.787 49.044 60.055 1.00 40.51 ? 71 THR B N 1 ATOM 2766 C CA . THR B 2 71 ? 47.164 48.190 61.167 1.00 41.75 ? 71 THR B CA 1 ATOM 2767 C C . THR B 2 71 ? 46.918 48.999 62.448 1.00 41.38 ? 71 THR B C 1 ATOM 2768 O O . THR B 2 71 ? 47.642 49.953 62.740 1.00 41.88 ? 71 THR B O 1 ATOM 2769 C CB . THR B 2 71 ? 48.602 47.685 61.018 1.00 44.70 ? 71 THR B CB 1 ATOM 2770 O OG1 . THR B 2 71 ? 48.682 46.827 59.872 1.00 46.07 ? 71 THR B OG1 1 ATOM 2771 C CG2 . THR B 2 71 ? 49.050 46.872 62.251 1.00 46.27 ? 71 THR B CG2 1 ATOM 2772 N N . PRO B 2 72 ? 45.846 48.651 63.190 1.00 40.39 ? 72 PRO B N 1 ATOM 2773 C CA . PRO B 2 72 ? 45.549 49.307 64.451 1.00 39.95 ? 72 PRO B CA 1 ATOM 2774 C C . PRO B 2 72 ? 46.670 49.103 65.474 1.00 42.44 ? 72 PRO B C 1 ATOM 2775 O O . PRO B 2 72 ? 47.327 48.072 65.470 1.00 44.94 ? 72 PRO B O 1 ATOM 2776 C CB . PRO B 2 72 ? 44.266 48.618 64.939 1.00 39.75 ? 72 PRO B CB 1 ATOM 2777 C CG . PRO B 2 72 ? 43.850 47.666 63.903 1.00 39.26 ? 72 PRO B CG 1 ATOM 2778 C CD . PRO B 2 72 ? 44.878 47.599 62.840 1.00 40.54 ? 72 PRO B CD 1 ATOM 2779 N N . THR B 2 73 ? 46.867 50.090 66.345 1.00 43.12 ? 73 THR B N 1 ATOM 2780 C CA . THR B 2 73 ? 47.873 50.045 67.416 1.00 45.29 ? 73 THR B CA 1 ATOM 2781 C C . THR B 2 73 ? 47.226 50.702 68.626 1.00 44.69 ? 73 THR B C 1 ATOM 2782 O O . THR B 2 73 ? 46.279 51.499 68.464 1.00 43.01 ? 73 THR B O 1 ATOM 2783 C CB . THR B 2 73 ? 49.145 50.788 66.978 1.00 46.22 ? 73 THR B CB 1 ATOM 2784 O OG1 . THR B 2 73 ? 49.868 49.954 66.072 1.00 48.54 ? 73 THR B OG1 1 ATOM 2785 C CG2 . THR B 2 73 ? 50.060 51.145 68.147 1.00 50.50 ? 73 THR B CG2 1 ATOM 2786 N N . GLU B 2 74 ? 47.703 50.370 69.829 1.00 45.47 ? 74 GLU B N 1 ATOM 2787 C CA . GLU B 2 74 ? 47.125 50.913 71.069 1.00 46.16 ? 74 GLU B CA 1 ATOM 2788 C C . GLU B 2 74 ? 47.191 52.427 71.129 1.00 44.81 ? 74 GLU B C 1 ATOM 2789 O O . GLU B 2 74 ? 46.314 53.059 71.696 1.00 45.70 ? 74 GLU B O 1 ATOM 2790 C CB . GLU B 2 74 ? 47.797 50.329 72.327 1.00 48.64 ? 74 GLU B CB 1 ATOM 2791 C CG . GLU B 2 74 ? 47.585 48.841 72.460 1.00 51.52 ? 74 GLU B CG 1 ATOM 2792 C CD . GLU B 2 74 ? 48.157 48.241 73.733 1.00 54.95 ? 74 GLU B CD 1 ATOM 2793 O OE1 . GLU B 2 74 ? 47.712 48.620 74.832 1.00 57.88 ? 74 GLU B OE1 1 ATOM 2794 O OE2 . GLU B 2 74 ? 49.032 47.348 73.632 1.00 60.78 ? 74 GLU B OE2 1 ATOM 2795 N N . LYS B 2 75 ? 48.229 52.998 70.530 1.00 43.43 ? 75 LYS B N 1 ATOM 2796 C CA . LYS B 2 75 ? 48.514 54.409 70.667 1.00 43.19 ? 75 LYS B CA 1 ATOM 2797 C C . LYS B 2 75 ? 47.830 55.302 69.624 1.00 40.13 ? 75 LYS B C 1 ATOM 2798 O O . LYS B 2 75 ? 47.788 56.522 69.791 1.00 40.88 ? 75 LYS B O 1 ATOM 2799 C CB . LYS B 2 75 ? 50.027 54.605 70.601 1.00 45.88 ? 75 LYS B CB 1 ATOM 2800 C CG . LYS B 2 75 ? 50.775 54.176 71.867 1.00 50.72 ? 75 LYS B CG 1 ATOM 2801 C CD . LYS B 2 75 ? 52.238 53.806 71.586 1.00 57.48 ? 75 LYS B CD 1 ATOM 2802 C CE . LYS B 2 75 ? 52.929 54.694 70.529 1.00 58.51 ? 75 LYS B CE 1 ATOM 2803 N NZ . LYS B 2 75 ? 54.435 54.613 70.699 1.00 64.37 ? 75 LYS B NZ 1 ATOM 2804 N N . ASP B 2 76 ? 47.302 54.706 68.559 1.00 36.60 ? 76 ASP B N 1 ATOM 2805 C CA . ASP B 2 76 ? 46.827 55.472 67.416 1.00 34.83 ? 76 ASP B CA 1 ATOM 2806 C C . ASP B 2 76 ? 45.336 55.636 67.415 1.00 32.84 ? 76 ASP B C 1 ATOM 2807 O O . ASP B 2 76 ? 44.629 54.664 67.706 1.00 32.03 ? 76 ASP B O 1 ATOM 2808 C CB . ASP B 2 76 ? 47.205 54.781 66.119 1.00 34.34 ? 76 ASP B CB 1 ATOM 2809 C CG . ASP B 2 76 ? 48.685 54.680 65.947 1.00 37.71 ? 76 ASP B CG 1 ATOM 2810 O OD1 . ASP B 2 76 ? 49.415 55.668 66.227 1.00 41.40 ? 76 ASP B OD1 1 ATOM 2811 O OD2 . ASP B 2 76 ? 49.123 53.587 65.597 1.00 41.80 ? 76 ASP B OD2 1 ATOM 2812 N N . GLU B 2 77 ? 44.874 56.843 67.048 1.00 30.50 ? 77 GLU B N 1 ATOM 2813 C CA . GLU B 2 77 ? 43.449 57.156 66.926 1.00 29.34 ? 77 GLU B CA 1 ATOM 2814 C C . GLU B 2 77 ? 43.089 57.282 65.446 1.00 27.71 ? 77 GLU B C 1 ATOM 2815 O O . GLU B 2 77 ? 43.832 57.895 64.708 1.00 26.91 ? 77 GLU B O 1 ATOM 2816 C CB . GLU B 2 77 ? 43.120 58.471 67.661 1.00 30.50 ? 77 GLU B CB 1 ATOM 2817 C CG . GLU B 2 77 ? 41.793 59.064 67.250 1.00 34.14 ? 77 GLU B CG 1 ATOM 2818 C CD . GLU B 2 77 ? 41.677 60.539 67.555 1.00 39.29 ? 77 GLU B CD 1 ATOM 2819 O OE1 . GLU B 2 77 ? 42.282 61.349 66.813 1.00 42.09 ? 77 GLU B OE1 1 ATOM 2820 O OE2 . GLU B 2 77 ? 40.980 60.879 68.531 1.00 40.34 ? 77 GLU B OE2 1 ATOM 2821 N N . TYR B 2 78 ? 41.943 56.726 65.012 1.00 26.27 ? 78 TYR B N 1 ATOM 2822 C CA . TYR B 2 78 ? 41.523 56.849 63.601 1.00 25.49 ? 78 TYR B CA 1 ATOM 2823 C C . TYR B 2 78 ? 40.173 57.537 63.591 1.00 25.66 ? 78 TYR B C 1 ATOM 2824 O O . TYR B 2 78 ? 39.445 57.515 64.616 1.00 26.92 ? 78 TYR B O 1 ATOM 2825 C CB . TYR B 2 78 ? 41.457 55.458 62.937 1.00 24.98 ? 78 TYR B CB 1 ATOM 2826 C CG . TYR B 2 78 ? 42.817 54.852 62.735 1.00 25.36 ? 78 TYR B CG 1 ATOM 2827 C CD1 . TYR B 2 78 ? 43.540 55.107 61.579 1.00 23.52 ? 78 TYR B CD1 1 ATOM 2828 C CD2 . TYR B 2 78 ? 43.425 54.093 63.737 1.00 28.77 ? 78 TYR B CD2 1 ATOM 2829 C CE1 . TYR B 2 78 ? 44.819 54.593 61.403 1.00 30.61 ? 78 TYR B CE1 1 ATOM 2830 C CE2 . TYR B 2 78 ? 44.730 53.590 63.582 1.00 28.62 ? 78 TYR B CE2 1 ATOM 2831 C CZ . TYR B 2 78 ? 45.394 53.830 62.395 1.00 29.10 ? 78 TYR B CZ 1 ATOM 2832 O OH . TYR B 2 78 ? 46.654 53.316 62.213 1.00 34.45 ? 78 TYR B OH 1 ATOM 2833 N N . ALA B 2 79 ? 39.837 58.200 62.480 1.00 24.54 ? 79 ALA B N 1 ATOM 2834 C CA . ALA B 2 79 ? 38.615 58.996 62.384 1.00 24.94 ? 79 ALA B CA 1 ATOM 2835 C C . ALA B 2 79 ? 38.299 59.248 60.914 1.00 25.60 ? 79 ALA B C 1 ATOM 2836 O O . ALA B 2 79 ? 39.174 59.103 60.068 1.00 25.04 ? 79 ALA B O 1 ATOM 2837 C CB . ALA B 2 79 ? 38.818 60.356 63.059 1.00 26.44 ? 79 ALA B CB 1 ATOM 2838 N N . CYS B 2 80 ? 37.082 59.704 60.650 1.00 26.33 ? 80 CYS B N 1 ATOM 2839 C CA . CYS B 2 80 ? 36.617 60.043 59.308 1.00 26.23 ? 80 CYS B CA 1 ATOM 2840 C C . CYS B 2 80 ? 36.156 61.495 59.377 1.00 27.08 ? 80 CYS B C 1 ATOM 2841 O O . CYS B 2 80 ? 35.448 61.858 60.304 1.00 27.97 ? 80 CYS B O 1 ATOM 2842 C CB . CYS B 2 80 ? 35.434 59.139 58.909 1.00 25.67 ? 80 CYS B CB 1 ATOM 2843 S SG . CYS B 2 80 ? 34.855 59.461 57.231 1.00 29.98 ? 80 CYS B SG 1 ATOM 2844 N N . ARG B 2 81 ? 36.580 62.321 58.425 1.00 26.74 ? 81 ARG B N 1 ATOM 2845 C CA . ARG B 2 81 ? 36.203 63.742 58.394 1.00 28.41 ? 81 ARG B CA 1 ATOM 2846 C C . ARG B 2 81 ? 35.432 63.979 57.116 1.00 28.61 ? 81 ARG B C 1 ATOM 2847 O O . ARG B 2 81 ? 35.916 63.619 56.021 1.00 26.24 ? 81 ARG B O 1 ATOM 2848 C CB . ARG B 2 81 ? 37.446 64.608 58.419 1.00 30.54 ? 81 ARG B CB 1 ATOM 2849 C CG . ARG B 2 81 ? 37.187 66.082 58.445 1.00 33.96 ? 81 ARG B CG 1 ATOM 2850 C CD . ARG B 2 81 ? 38.270 66.723 57.631 1.00 38.68 ? 81 ARG B CD 1 ATOM 2851 N NE . ARG B 2 81 ? 39.445 66.973 58.409 1.00 44.99 ? 81 ARG B NE 1 ATOM 2852 C CZ . ARG B 2 81 ? 40.696 66.961 57.937 1.00 48.97 ? 81 ARG B CZ 1 ATOM 2853 N NH1 . ARG B 2 81 ? 40.959 66.669 56.664 1.00 48.18 ? 81 ARG B NH1 1 ATOM 2854 N NH2 . ARG B 2 81 ? 41.689 67.238 58.760 1.00 49.91 ? 81 ARG B NH2 1 ATOM 2855 N N . VAL B 2 82 ? 34.228 64.561 57.260 1.00 28.86 ? 82 VAL B N 1 ATOM 2856 C CA . VAL B 2 82 ? 33.294 64.738 56.146 1.00 28.47 ? 82 VAL B CA 1 ATOM 2857 C C . VAL B 2 82 ? 32.925 66.195 55.992 1.00 31.60 ? 82 VAL B C 1 ATOM 2858 O O . VAL B 2 82 ? 32.567 66.882 56.980 1.00 33.53 ? 82 VAL B O 1 ATOM 2859 C CB . VAL B 2 82 ? 32.024 63.818 56.310 1.00 27.29 ? 82 VAL B CB 1 ATOM 2860 C CG1 . VAL B 2 82 ? 31.085 63.939 55.111 1.00 27.23 ? 82 VAL B CG1 1 ATOM 2861 C CG2 . VAL B 2 82 ? 32.438 62.342 56.429 1.00 24.98 ? 82 VAL B CG2 1 ATOM 2862 N N . ASN B 2 83 ? 33.039 66.717 54.778 1.00 32.82 ? 83 ASN B N 1 ATOM 2863 C CA . ASN B 2 83 ? 32.428 68.038 54.513 1.00 35.15 ? 83 ASN B CA 1 ATOM 2864 C C . ASN B 2 83 ? 31.346 67.981 53.433 1.00 34.43 ? 83 ASN B C 1 ATOM 2865 O O . ASN B 2 83 ? 31.475 67.272 52.429 1.00 33.23 ? 83 ASN B O 1 ATOM 2866 C CB . ASN B 2 83 ? 33.452 69.127 54.240 1.00 38.55 ? 83 ASN B CB 1 ATOM 2867 C CG . ASN B 2 83 ? 32.977 70.530 54.749 1.00 45.53 ? 83 ASN B CG 1 ATOM 2868 O OD1 . ASN B 2 83 ? 31.799 70.733 55.089 1.00 45.62 ? 83 ASN B OD1 1 ATOM 2869 N ND2 . ASN B 2 83 ? 33.897 71.478 54.786 1.00 50.02 ? 83 ASN B ND2 1 ATOM 2870 N N . HIS B 2 84 ? 30.277 68.742 53.659 1.00 35.40 ? 84 HIS B N 1 ATOM 2871 C CA . HIS B 2 84 ? 29.095 68.718 52.811 1.00 34.01 ? 84 HIS B CA 1 ATOM 2872 C C . HIS B 2 84 ? 28.374 70.065 53.006 1.00 37.29 ? 84 HIS B C 1 ATOM 2873 O O . HIS B 2 84 ? 28.501 70.717 54.037 1.00 38.80 ? 84 HIS B O 1 ATOM 2874 C CB . HIS B 2 84 ? 28.208 67.503 53.176 1.00 31.82 ? 84 HIS B CB 1 ATOM 2875 C CG . HIS B 2 84 ? 27.056 67.287 52.236 1.00 34.00 ? 84 HIS B CG 1 ATOM 2876 N ND1 . HIS B 2 84 ? 25.778 67.749 52.496 1.00 33.31 ? 84 HIS B ND1 1 ATOM 2877 C CD2 . HIS B 2 84 ? 27.005 66.718 51.010 1.00 32.24 ? 84 HIS B CD2 1 ATOM 2878 C CE1 . HIS B 2 84 ? 24.984 67.420 51.493 1.00 32.52 ? 84 HIS B CE1 1 ATOM 2879 N NE2 . HIS B 2 84 ? 25.706 66.816 50.570 1.00 33.49 ? 84 HIS B NE2 1 ATOM 2880 N N . VAL B 2 85 ? 27.677 70.519 51.983 1.00 37.88 ? 85 VAL B N 1 ATOM 2881 C CA . VAL B 2 85 ? 27.067 71.851 52.009 1.00 41.95 ? 85 VAL B CA 1 ATOM 2882 C C . VAL B 2 85 ? 26.073 72.013 53.182 1.00 42.82 ? 85 VAL B C 1 ATOM 2883 O O . VAL B 2 85 ? 25.811 73.138 53.657 1.00 47.14 ? 85 VAL B O 1 ATOM 2884 C CB . VAL B 2 85 ? 26.446 72.136 50.611 1.00 42.69 ? 85 VAL B CB 1 ATOM 2885 C CG1 . VAL B 2 85 ? 25.148 71.334 50.391 1.00 40.18 ? 85 VAL B CG1 1 ATOM 2886 C CG2 . VAL B 2 85 ? 26.289 73.581 50.368 1.00 48.09 ? 85 VAL B CG2 1 ATOM 2887 N N . THR B 2 86 ? 25.526 70.897 53.667 1.00 40.07 ? 86 THR B N 1 ATOM 2888 C CA . THR B 2 86 ? 24.634 70.939 54.839 1.00 42.23 ? 86 THR B CA 1 ATOM 2889 C C . THR B 2 86 ? 25.351 71.116 56.200 1.00 44.34 ? 86 THR B C 1 ATOM 2890 O O . THR B 2 86 ? 24.692 71.278 57.228 1.00 44.96 ? 86 THR B O 1 ATOM 2891 C CB . THR B 2 86 ? 23.740 69.705 54.927 1.00 38.98 ? 86 THR B CB 1 ATOM 2892 O OG1 . THR B 2 86 ? 24.557 68.519 54.918 1.00 34.86 ? 86 THR B OG1 1 ATOM 2893 C CG2 . THR B 2 86 ? 22.759 69.682 53.780 1.00 38.03 ? 86 THR B CG2 1 ATOM 2894 N N . LEU B 2 87 ? 26.682 71.029 56.203 1.00 44.57 ? 87 LEU B N 1 ATOM 2895 C CA . LEU B 2 87 ? 27.461 71.121 57.448 1.00 47.15 ? 87 LEU B CA 1 ATOM 2896 C C . LEU B 2 87 ? 28.123 72.508 57.478 1.00 52.27 ? 87 LEU B C 1 ATOM 2897 O O . LEU B 2 87 ? 28.601 72.999 56.447 1.00 54.01 ? 87 LEU B O 1 ATOM 2898 C CB . LEU B 2 87 ? 28.484 69.966 57.535 1.00 42.90 ? 87 LEU B CB 1 ATOM 2899 C CG . LEU B 2 87 ? 28.007 68.497 57.555 1.00 40.50 ? 87 LEU B CG 1 ATOM 2900 C CD1 . LEU B 2 87 ? 29.165 67.488 57.371 1.00 36.59 ? 87 LEU B CD1 1 ATOM 2901 C CD2 . LEU B 2 87 ? 27.278 68.189 58.847 1.00 43.01 ? 87 LEU B CD2 1 ATOM 2902 N N . SER B 2 88 ? 28.109 73.167 58.632 1.00 56.25 ? 88 SER B N 1 ATOM 2903 C CA . SER B 2 88 ? 28.786 74.446 58.765 1.00 61.71 ? 88 SER B CA 1 ATOM 2904 C C . SER B 2 88 ? 30.295 74.268 58.907 1.00 61.08 ? 88 SER B C 1 ATOM 2905 O O . SER B 2 88 ? 31.090 75.152 58.531 1.00 64.28 ? 88 SER B O 1 ATOM 2906 C CB . SER B 2 88 ? 28.253 75.201 59.990 1.00 66.43 ? 88 SER B CB 1 ATOM 2907 O OG . SER B 2 88 ? 28.627 74.494 61.178 1.00 67.85 ? 88 SER B OG 1 ATOM 2908 N N . GLN B 2 89 ? 30.674 73.144 59.509 1.00 57.26 ? 89 GLN B N 1 ATOM 2909 C CA . GLN B 2 89 ? 32.056 72.765 59.654 1.00 55.86 ? 89 GLN B CA 1 ATOM 2910 C C . GLN B 2 89 ? 32.187 71.278 59.381 1.00 50.16 ? 89 GLN B C 1 ATOM 2911 O O . GLN B 2 89 ? 31.216 70.536 59.518 1.00 47.90 ? 89 GLN B O 1 ATOM 2912 C CB . GLN B 2 89 ? 32.558 73.119 61.056 1.00 58.42 ? 89 GLN B CB 1 ATOM 2913 C CG . GLN B 2 89 ? 32.088 72.230 62.220 1.00 57.21 ? 89 GLN B CG 1 ATOM 2914 C CD . GLN B 2 89 ? 32.515 72.839 63.569 1.00 62.07 ? 89 GLN B CD 1 ATOM 2915 O OE1 . GLN B 2 89 ? 32.912 72.138 64.513 1.00 63.93 ? 89 GLN B OE1 1 ATOM 2916 N NE2 . GLN B 2 89 ? 32.474 74.147 63.637 1.00 68.12 ? 89 GLN B NE2 1 ATOM 2917 N N . PRO B 2 90 ? 33.395 70.823 59.031 1.00 48.34 ? 90 PRO B N 1 ATOM 2918 C CA . PRO B 2 90 ? 33.541 69.393 58.816 1.00 43.03 ? 90 PRO B CA 1 ATOM 2919 C C . PRO B 2 90 ? 33.113 68.631 60.074 1.00 41.44 ? 90 PRO B C 1 ATOM 2920 O O . PRO B 2 90 ? 33.339 69.098 61.204 1.00 42.78 ? 90 PRO B O 1 ATOM 2921 C CB . PRO B 2 90 ? 35.036 69.239 58.555 1.00 43.55 ? 90 PRO B CB 1 ATOM 2922 C CG . PRO B 2 90 ? 35.479 70.627 58.075 1.00 47.26 ? 90 PRO B CG 1 ATOM 2923 C CD . PRO B 2 90 ? 34.666 71.557 58.870 1.00 50.58 ? 90 PRO B CD 1 ATOM 2924 N N . LYS B 2 91 ? 32.419 67.525 59.863 1.00 38.21 ? 91 LYS B N 1 ATOM 2925 C CA . LYS B 2 91 ? 32.035 66.580 60.909 1.00 38.21 ? 91 LYS B CA 1 ATOM 2926 C C . LYS B 2 91 ? 33.107 65.517 61.044 1.00 34.15 ? 91 LYS B C 1 ATOM 2927 O O . LYS B 2 91 ? 33.444 64.861 60.056 1.00 31.37 ? 91 LYS B O 1 ATOM 2928 C CB . LYS B 2 91 ? 30.746 65.836 60.521 1.00 37.33 ? 91 LYS B CB 1 ATOM 2929 C CG . LYS B 2 91 ? 29.694 65.754 61.647 1.00 41.53 ? 91 LYS B CG 1 ATOM 2930 C CD . LYS B 2 91 ? 28.458 64.948 61.197 1.00 39.24 ? 91 LYS B CD 1 ATOM 2931 C CE . LYS B 2 91 ? 27.222 65.316 62.044 1.00 47.25 ? 91 LYS B CE 1 ATOM 2932 N NZ . LYS B 2 91 ? 25.914 65.165 61.299 1.00 45.03 ? 91 LYS B NZ 1 ATOM 2933 N N . ILE B 2 92 ? 33.614 65.324 62.257 1.00 34.31 ? 92 ILE B N 1 ATOM 2934 C CA . ILE B 2 92 ? 34.623 64.278 62.524 1.00 32.91 ? 92 ILE B CA 1 ATOM 2935 C C . ILE B 2 92 ? 33.964 63.168 63.334 1.00 32.60 ? 92 ILE B C 1 ATOM 2936 O O . ILE B 2 92 ? 33.316 63.445 64.351 1.00 35.67 ? 92 ILE B O 1 ATOM 2937 C CB . ILE B 2 92 ? 35.841 64.808 63.316 1.00 35.06 ? 92 ILE B CB 1 ATOM 2938 C CG1 . ILE B 2 92 ? 36.595 65.871 62.522 1.00 35.46 ? 92 ILE B CG1 1 ATOM 2939 C CG2 . ILE B 2 92 ? 36.817 63.657 63.596 1.00 31.93 ? 92 ILE B CG2 1 ATOM 2940 C CD1 . ILE B 2 92 ? 37.540 66.686 63.343 1.00 42.50 ? 92 ILE B CD1 1 ATOM 2941 N N . VAL B 2 93 ? 34.099 61.937 62.868 1.00 30.09 ? 93 VAL B N 1 ATOM 2942 C CA . VAL B 2 93 ? 33.599 60.755 63.569 1.00 29.61 ? 93 VAL B CA 1 ATOM 2943 C C . VAL B 2 93 ? 34.785 59.843 63.869 1.00 27.37 ? 93 VAL B C 1 ATOM 2944 O O . VAL B 2 93 ? 35.407 59.296 62.962 1.00 25.40 ? 93 VAL B O 1 ATOM 2945 C CB . VAL B 2 93 ? 32.518 60.012 62.701 1.00 28.82 ? 93 VAL B CB 1 ATOM 2946 C CG1 . VAL B 2 93 ? 32.008 58.718 63.393 1.00 31.25 ? 93 VAL B CG1 1 ATOM 2947 C CG2 . VAL B 2 93 ? 31.313 60.950 62.413 1.00 30.11 ? 93 VAL B CG2 1 ATOM 2948 N N . LYS B 2 94 ? 35.090 59.665 65.144 1.00 28.91 ? 94 LYS B N 1 ATOM 2949 C CA . LYS B 2 94 ? 36.222 58.831 65.556 1.00 29.69 ? 94 LYS B CA 1 ATOM 2950 C C . LYS B 2 94 ? 35.887 57.350 65.400 1.00 28.19 ? 94 LYS B C 1 ATOM 2951 O O . LYS B 2 94 ? 34.745 56.982 65.555 1.00 28.96 ? 94 LYS B O 1 ATOM 2952 C CB . LYS B 2 94 ? 36.583 59.112 67.010 1.00 31.52 ? 94 LYS B CB 1 ATOM 2953 C CG . LYS B 2 94 ? 36.967 60.570 67.265 1.00 35.27 ? 94 LYS B CG 1 ATOM 2954 C CD . LYS B 2 94 ? 37.400 60.806 68.707 1.00 37.89 ? 94 LYS B CD 1 ATOM 2955 C CE . LYS B 2 94 ? 36.908 62.198 69.181 1.00 46.42 ? 94 LYS B CE 1 ATOM 2956 N NZ . LYS B 2 94 ? 37.459 62.608 70.537 1.00 50.62 ? 94 LYS B NZ 1 ATOM 2957 N N . TRP B 2 95 ? 36.857 56.494 65.100 1.00 25.89 ? 95 TRP B N 1 ATOM 2958 C CA . TRP B 2 95 ? 36.539 55.069 64.988 1.00 25.83 ? 95 TRP B CA 1 ATOM 2959 C C . TRP B 2 95 ? 36.389 54.493 66.409 1.00 28.40 ? 95 TRP B C 1 ATOM 2960 O O . TRP B 2 95 ? 37.284 54.655 67.228 1.00 28.74 ? 95 TRP B O 1 ATOM 2961 C CB . TRP B 2 95 ? 37.632 54.340 64.200 1.00 24.54 ? 95 TRP B CB 1 ATOM 2962 C CG . TRP B 2 95 ? 37.625 52.821 64.212 1.00 25.16 ? 95 TRP B CG 1 ATOM 2963 C CD1 . TRP B 2 95 ? 36.566 51.965 63.864 1.00 23.88 ? 95 TRP B CD1 1 ATOM 2964 C CD2 . TRP B 2 95 ? 38.722 51.971 64.564 1.00 24.16 ? 95 TRP B CD2 1 ATOM 2965 N NE1 . TRP B 2 95 ? 36.968 50.659 64.000 1.00 24.95 ? 95 TRP B NE1 1 ATOM 2966 C CE2 . TRP B 2 95 ? 38.275 50.625 64.432 1.00 23.99 ? 95 TRP B CE2 1 ATOM 2967 C CE3 . TRP B 2 95 ? 40.029 52.214 65.012 1.00 25.69 ? 95 TRP B CE3 1 ATOM 2968 C CZ2 . TRP B 2 95 ? 39.100 49.543 64.681 1.00 26.46 ? 95 TRP B CZ2 1 ATOM 2969 C CZ3 . TRP B 2 95 ? 40.846 51.138 65.287 1.00 28.19 ? 95 TRP B CZ3 1 ATOM 2970 C CH2 . TRP B 2 95 ? 40.372 49.802 65.133 1.00 27.82 ? 95 TRP B CH2 1 ATOM 2971 N N . ASP B 2 96 ? 35.233 53.879 66.690 1.00 30.24 ? 96 ASP B N 1 ATOM 2972 C CA . ASP B 2 96 ? 35.008 53.094 67.894 1.00 34.60 ? 96 ASP B CA 1 ATOM 2973 C C . ASP B 2 96 ? 35.439 51.667 67.561 1.00 36.59 ? 96 ASP B C 1 ATOM 2974 O O . ASP B 2 96 ? 34.824 51.024 66.687 1.00 35.84 ? 96 ASP B O 1 ATOM 2975 C CB . ASP B 2 96 ? 33.519 53.083 68.204 1.00 36.30 ? 96 ASP B CB 1 ATOM 2976 C CG . ASP B 2 96 ? 33.187 52.396 69.523 1.00 41.31 ? 96 ASP B CG 1 ATOM 2977 O OD1 . ASP B 2 96 ? 34.030 51.612 70.054 1.00 43.03 ? 96 ASP B OD1 1 ATOM 2978 O OD2 . ASP B 2 96 ? 32.062 52.625 70.021 1.00 42.31 ? 96 ASP B OD2 1 ATOM 2979 N N . ARG B 2 97 ? 36.470 51.172 68.243 1.00 38.74 ? 97 ARG B N 1 ATOM 2980 C CA . ARG B 2 97 ? 37.040 49.841 67.964 1.00 42.16 ? 97 ARG B CA 1 ATOM 2981 C C . ARG B 2 97 ? 36.045 48.685 68.067 1.00 45.50 ? 97 ARG B C 1 ATOM 2982 O O . ARG B 2 97 ? 36.328 47.575 67.571 1.00 46.21 ? 97 ARG B O 1 ATOM 2983 C CB . ARG B 2 97 ? 38.201 49.549 68.909 1.00 43.79 ? 97 ARG B CB 1 ATOM 2984 C CG . ARG B 2 97 ? 39.278 50.604 68.875 1.00 45.18 ? 97 ARG B CG 1 ATOM 2985 C CD . ARG B 2 97 ? 40.609 50.021 69.336 1.00 49.06 ? 97 ARG B CD 1 ATOM 2986 N NE . ARG B 2 97 ? 41.699 50.851 68.842 1.00 49.91 ? 97 ARG B NE 1 ATOM 2987 C CZ . ARG B 2 97 ? 42.924 50.410 68.572 1.00 49.41 ? 97 ARG B CZ 1 ATOM 2988 N NH1 . ARG B 2 97 ? 43.230 49.125 68.732 1.00 48.44 ? 97 ARG B NH1 1 ATOM 2989 N NH2 . ARG B 2 97 ? 43.826 51.264 68.107 1.00 48.33 ? 97 ARG B NH2 1 ATOM 2990 N N . ASP B 2 98 ? 34.904 48.935 68.733 1.00 47.75 ? 98 ASP B N 1 ATOM 2991 C CA . ASP B 2 98 ? 33.783 47.987 68.823 1.00 50.72 ? 98 ASP B CA 1 ATOM 2992 C C . ASP B 2 98 ? 33.091 47.833 67.469 1.00 50.16 ? 98 ASP B C 1 ATOM 2993 O O . ASP B 2 98 ? 32.218 46.976 67.304 1.00 51.82 ? 98 ASP B O 1 ATOM 2994 C CB . ASP B 2 98 ? 32.742 48.497 69.823 1.00 52.30 ? 98 ASP B CB 1 ATOM 2995 C CG . ASP B 2 98 ? 33.204 48.402 71.258 1.00 55.19 ? 98 ASP B CG 1 ATOM 2996 O OD1 . ASP B 2 98 ? 34.307 47.872 71.523 1.00 54.39 ? 98 ASP B OD1 1 ATOM 2997 O OD2 . ASP B 2 98 ? 32.443 48.871 72.133 1.00 57.66 ? 98 ASP B OD2 1 ATOM 2998 N N . MET B 2 99 ? 33.467 48.700 66.522 1.00 48.22 ? 99 MET B N 1 ATOM 2999 C CA . MET B 2 99 ? 32.802 48.834 65.221 1.00 47.75 ? 99 MET B CA 1 ATOM 3000 C C . MET B 2 99 ? 33.745 48.453 64.062 1.00 46.08 ? 99 MET B C 1 ATOM 3001 O O . MET B 2 99 ? 34.972 48.590 64.178 1.00 44.45 ? 99 MET B O 1 ATOM 3002 C CB . MET B 2 99 ? 32.317 50.273 65.014 1.00 47.11 ? 99 MET B CB 1 ATOM 3003 C CG . MET B 2 99 ? 30.841 50.547 65.350 1.00 51.57 ? 99 MET B CG 1 ATOM 3004 S SD . MET B 2 99 ? 30.634 50.900 67.105 1.00 62.03 ? 99 MET B SD 1 ATOM 3005 C CE . MET B 2 99 ? 28.930 51.505 67.178 1.00 59.71 ? 99 MET B CE 1 HETATM 3006 C C1 . NAG C 3 . ? 31.044 76.494 34.365 1.00 88.57 ? 500 NAG A C1 1 HETATM 3007 C C2 . NAG C 3 . ? 31.858 77.771 34.101 1.00 95.79 ? 500 NAG A C2 1 HETATM 3008 C C3 . NAG C 3 . ? 33.331 77.390 33.978 1.00 98.66 ? 500 NAG A C3 1 HETATM 3009 C C4 . NAG C 3 . ? 33.771 76.710 35.266 1.00 96.86 ? 500 NAG A C4 1 HETATM 3010 C C5 . NAG C 3 . ? 32.945 75.437 35.516 1.00 89.92 ? 500 NAG A C5 1 HETATM 3011 C C6 . NAG C 3 . ? 33.402 74.802 36.838 1.00 87.99 ? 500 NAG A C6 1 HETATM 3012 C C7 . NAG C 3 . ? 30.799 79.678 32.954 1.00 103.44 ? 500 NAG A C7 1 HETATM 3013 C C8 . NAG C 3 . ? 31.676 80.898 33.061 1.00 109.23 ? 500 NAG A C8 1 HETATM 3014 N N2 . NAG C 3 . ? 31.407 78.484 32.909 1.00 99.39 ? 500 NAG A N2 1 HETATM 3015 O O3 . NAG C 3 . ? 34.164 78.494 33.740 1.00 103.77 ? 500 NAG A O3 1 HETATM 3016 O O4 . NAG C 3 . ? 35.160 76.447 35.182 1.00 102.21 ? 500 NAG A O4 1 HETATM 3017 O O5 . NAG C 3 . ? 31.539 75.723 35.480 1.00 86.78 ? 500 NAG A O5 1 HETATM 3018 O O6 . NAG C 3 . ? 32.361 74.215 37.588 1.00 83.84 ? 500 NAG A O6 1 HETATM 3019 O O7 . NAG C 3 . ? 29.572 79.815 32.907 1.00 102.08 ? 500 NAG A O7 1 HETATM 3020 C C1 . NAG D 3 . ? 37.792 53.708 33.589 1.00 67.19 ? 511 NAG A C1 1 HETATM 3021 C C2 . NAG D 3 . ? 38.091 54.239 35.015 1.00 66.90 ? 511 NAG A C2 1 HETATM 3022 C C3 . NAG D 3 . ? 39.301 55.185 35.038 1.00 72.69 ? 511 NAG A C3 1 HETATM 3023 C C4 . NAG D 3 . ? 40.532 54.529 34.399 1.00 76.27 ? 511 NAG A C4 1 HETATM 3024 C C5 . NAG D 3 . ? 40.175 53.972 33.010 1.00 76.88 ? 511 NAG A C5 1 HETATM 3025 C C6 . NAG D 3 . ? 41.297 53.071 32.496 1.00 81.67 ? 511 NAG A C6 1 HETATM 3026 C C7 . NAG D 3 . ? 35.896 54.372 36.197 1.00 61.49 ? 511 NAG A C7 1 HETATM 3027 C C8 . NAG D 3 . ? 35.117 55.240 37.146 1.00 58.73 ? 511 NAG A C8 1 HETATM 3028 N N2 . NAG D 3 . ? 36.971 54.944 35.623 1.00 65.25 ? 511 NAG A N2 1 HETATM 3029 O O3 . NAG D 3 . ? 39.569 55.595 36.369 1.00 71.74 ? 511 NAG A O3 1 HETATM 3030 O O4 . NAG D 3 . ? 41.628 55.434 34.341 1.00 81.50 ? 511 NAG A O4 1 HETATM 3031 O O5 . NAG D 3 . ? 38.985 53.186 33.007 1.00 70.85 ? 511 NAG A O5 1 HETATM 3032 O O6 . NAG D 3 . ? 41.288 53.004 31.085 1.00 85.28 ? 511 NAG A O6 1 HETATM 3033 O O7 . NAG D 3 . ? 35.532 53.215 35.984 1.00 58.72 ? 511 NAG A O7 1 HETATM 3034 C C1 . NAG E 3 . ? 4.481 34.964 38.300 1.00 106.60 ? 521 NAG A C1 1 HETATM 3035 C C2 . NAG E 3 . ? 3.157 34.839 39.063 1.00 112.08 ? 521 NAG A C2 1 HETATM 3036 C C3 . NAG E 3 . ? 2.621 36.237 39.368 1.00 110.77 ? 521 NAG A C3 1 HETATM 3037 C C4 . NAG E 3 . ? 3.662 37.053 40.145 1.00 103.76 ? 521 NAG A C4 1 HETATM 3038 C C5 . NAG E 3 . ? 5.039 36.981 39.474 1.00 97.34 ? 521 NAG A C5 1 HETATM 3039 C C6 . NAG E 3 . ? 6.107 37.592 40.373 1.00 90.60 ? 521 NAG A C6 1 HETATM 3040 C C7 . NAG E 3 . ? 1.885 32.781 38.702 1.00 125.84 ? 521 NAG A C7 1 HETATM 3041 C C8 . NAG E 3 . ? 0.438 32.467 38.961 1.00 134.53 ? 521 NAG A C8 1 HETATM 3042 N N2 . NAG E 3 . ? 2.181 34.034 38.345 1.00 120.51 ? 521 NAG A N2 1 HETATM 3043 O O3 . NAG E 3 . ? 1.435 36.135 40.121 1.00 116.86 ? 521 NAG A O3 1 HETATM 3044 O O4 . NAG E 3 . ? 3.254 38.404 40.275 1.00 102.68 ? 521 NAG A O4 1 HETATM 3045 O O5 . NAG E 3 . ? 5.399 35.645 39.145 1.00 99.28 ? 521 NAG A O5 1 HETATM 3046 O O6 . NAG E 3 . ? 6.598 36.631 41.281 1.00 90.53 ? 521 NAG A O6 1 HETATM 3047 O O7 . NAG E 3 . ? 2.733 31.896 38.820 1.00 124.51 ? 521 NAG A O7 1 HETATM 3048 C C1 . PLM F 4 . ? 16.328 66.355 22.677 1.00 68.45 ? 522 PLM A C1 1 HETATM 3049 O O1 . PLM F 4 . ? 17.556 66.519 22.893 1.00 69.12 ? 522 PLM A O1 1 HETATM 3050 O O2 . PLM F 4 . ? 15.580 67.359 22.712 1.00 68.55 ? 522 PLM A O2 1 HETATM 3051 C C2 . PLM F 4 . ? 15.746 64.984 22.379 1.00 68.29 ? 522 PLM A C2 1 HETATM 3052 C C3 . PLM F 4 . ? 16.643 63.870 22.925 1.00 68.56 ? 522 PLM A C3 1 HETATM 3053 C C4 . PLM F 4 . ? 15.993 62.493 22.808 1.00 68.16 ? 522 PLM A C4 1 HETATM 3054 C C5 . PLM F 4 . ? 15.198 62.117 24.061 1.00 68.15 ? 522 PLM A C5 1 HETATM 3055 C C6 . PLM F 4 . ? 16.053 61.493 25.167 1.00 67.41 ? 522 PLM A C6 1 HETATM 3056 C C7 . PLM F 4 . ? 15.553 61.871 26.560 1.00 66.76 ? 522 PLM A C7 1 HETATM 3057 C C8 . PLM F 4 . ? 14.832 60.717 27.234 1.00 65.86 ? 522 PLM A C8 1 HETATM 3058 C C9 . PLM F 4 . ? 15.123 60.688 28.732 1.00 65.75 ? 522 PLM A C9 1 HETATM 3059 C CA . PLM F 4 . ? 14.451 59.464 29.346 1.00 65.12 ? 522 PLM A CA 1 HETATM 3060 C CB . PLM F 4 . ? 15.297 58.814 30.433 1.00 64.64 ? 522 PLM A CB 1 HETATM 3061 C CC . PLM F 4 . ? 16.141 57.659 29.906 1.00 63.52 ? 522 PLM A CC 1 HETATM 3062 C CD . PLM F 4 . ? 15.468 56.310 30.121 1.00 63.09 ? 522 PLM A CD 1 HETATM 3063 C CE . PLM F 4 . ? 16.099 55.294 29.193 1.00 63.06 ? 522 PLM A CE 1 HETATM 3064 C CF . PLM F 4 . ? 16.483 54.019 29.933 1.00 63.32 ? 522 PLM A CF 1 HETATM 3065 C CG . PLM F 4 . ? 17.737 53.402 29.324 1.00 62.30 ? 522 PLM A CG 1 HETATM 3066 O O . HOH G 5 . ? 21.178 29.626 58.273 1.00 30.58 ? 523 HOH A O 1 HETATM 3067 O O . HOH G 5 . ? 22.401 59.611 23.014 1.00 49.59 ? 524 HOH A O 1 HETATM 3068 O O . HOH G 5 . ? 20.813 34.636 53.196 1.00 35.53 ? 525 HOH A O 1 HETATM 3069 O O . HOH G 5 . ? 31.707 36.537 70.804 1.00 34.52 ? 526 HOH A O 1 HETATM 3070 O O . HOH G 5 . ? 24.640 47.697 61.263 1.00 31.36 ? 527 HOH A O 1 HETATM 3071 O O . HOH G 5 . ? 32.637 42.303 57.700 1.00 45.34 ? 528 HOH A O 1 HETATM 3072 O O . HOH G 5 . ? 30.206 57.007 37.126 1.00 35.87 ? 529 HOH A O 1 HETATM 3073 O O . HOH G 5 . ? 31.509 41.705 76.842 1.00 38.60 ? 530 HOH A O 1 HETATM 3074 O O . HOH G 5 . ? 31.716 33.353 35.887 1.00 44.89 ? 531 HOH A O 1 HETATM 3075 O O . HOH G 5 . ? 23.992 40.414 47.719 1.00 31.68 ? 532 HOH A O 1 HETATM 3076 O O . HOH G 5 . ? 33.689 44.258 67.613 1.00 45.95 ? 533 HOH A O 1 HETATM 3077 O O . HOH G 5 . ? 25.373 49.734 82.318 1.00 35.59 ? 534 HOH A O 1 HETATM 3078 O O . HOH G 5 . ? 25.125 58.308 40.348 1.00 54.32 ? 535 HOH A O 1 HETATM 3079 O O . HOH G 5 . ? 28.469 28.089 51.729 1.00 39.78 ? 536 HOH A O 1 HETATM 3080 O O . HOH G 5 . ? 15.312 38.702 67.967 1.00 45.38 ? 537 HOH A O 1 HETATM 3081 O O . HOH G 5 . ? 18.939 48.095 71.332 1.00 39.81 ? 538 HOH A O 1 HETATM 3082 O O . HOH G 5 . ? 27.998 46.510 45.350 1.00 41.28 ? 539 HOH A O 1 HETATM 3083 O O . HOH G 5 . ? 17.939 34.641 55.785 1.00 56.63 ? 540 HOH A O 1 HETATM 3084 O O . HOH G 5 . ? 18.513 70.160 41.366 1.00 44.04 ? 541 HOH A O 1 HETATM 3085 O O . HOH G 5 . ? 20.280 44.849 40.738 1.00 41.58 ? 542 HOH A O 1 HETATM 3086 O O . HOH G 5 . ? 31.278 33.220 64.108 1.00 31.06 ? 543 HOH A O 1 HETATM 3087 O O . HOH G 5 . ? 12.559 45.756 67.623 1.00 39.64 ? 544 HOH A O 1 HETATM 3088 O O . HOH G 5 . ? 30.145 38.591 44.190 1.00 37.45 ? 545 HOH A O 1 HETATM 3089 O O . HOH G 5 . ? 39.640 54.203 28.933 1.00 61.07 ? 546 HOH A O 1 HETATM 3090 O O . HOH G 5 . ? 31.392 64.247 33.950 1.00 50.29 ? 547 HOH A O 1 HETATM 3091 O O . HOH G 5 . ? 29.779 45.524 49.801 1.00 38.76 ? 548 HOH A O 1 HETATM 3092 O O . HOH G 5 . ? 35.089 41.915 30.823 1.00 60.81 ? 549 HOH A O 1 HETATM 3093 O O . HOH G 5 . ? 24.290 40.317 84.195 1.00 59.40 ? 550 HOH A O 1 HETATM 3094 O O . HOH G 5 . ? 21.757 48.110 65.769 1.00 46.70 ? 551 HOH A O 1 HETATM 3095 O O . HOH G 5 . ? 30.814 46.901 62.875 1.00 43.55 ? 552 HOH A O 1 HETATM 3096 O O . HOH G 5 . ? 17.984 34.610 62.965 1.00 43.61 ? 553 HOH A O 1 HETATM 3097 O O . HOH G 5 . ? 24.473 49.947 62.327 1.00 59.68 ? 554 HOH A O 1 HETATM 3098 O O . HOH G 5 . ? 28.204 46.602 48.051 1.00 43.29 ? 555 HOH A O 1 HETATM 3099 O O . HOH G 5 . ? 32.265 39.785 63.678 1.00 41.93 ? 556 HOH A O 1 HETATM 3100 O O . HOH G 5 . ? 17.977 40.603 60.898 1.00 42.23 ? 557 HOH A O 1 HETATM 3101 O O . HOH G 5 . ? 12.215 39.209 66.339 1.00 61.07 ? 558 HOH A O 1 HETATM 3102 O O . HOH G 5 . ? 18.846 42.181 58.304 1.00 67.99 ? 559 HOH A O 1 HETATM 3103 O O . HOH G 5 . ? 13.578 54.725 42.061 1.00 50.44 ? 560 HOH A O 1 HETATM 3104 O O . HOH G 5 . ? 13.249 62.524 48.403 1.00 53.03 ? 561 HOH A O 1 HETATM 3105 O O . HOH G 5 . ? 32.292 45.367 43.424 1.00 72.87 ? 562 HOH A O 1 HETATM 3106 O O . HOH G 5 . ? 32.094 34.636 68.370 1.00 36.32 ? 563 HOH A O 1 HETATM 3107 O O . HOH G 5 . ? 22.217 50.419 69.729 1.00 53.31 ? 564 HOH A O 1 HETATM 3108 O O . HOH G 5 . ? 30.505 37.087 74.706 1.00 47.58 ? 565 HOH A O 1 HETATM 3109 O O . HOH G 5 . ? 13.629 70.582 43.199 1.00 61.34 ? 566 HOH A O 1 HETATM 3110 O O . HOH G 5 . ? 38.865 42.965 52.388 1.00 51.16 ? 567 HOH A O 1 HETATM 3111 O O . HOH G 5 . ? 35.258 38.469 38.893 1.00 58.65 ? 568 HOH A O 1 HETATM 3112 O O . HOH G 5 . ? 23.558 32.119 76.759 1.00 47.91 ? 569 HOH A O 1 HETATM 3113 O O . HOH G 5 . ? 33.708 47.447 40.871 1.00 55.90 ? 570 HOH A O 1 HETATM 3114 O O . HOH G 5 . ? 24.604 29.498 76.405 1.00 63.22 ? 571 HOH A O 1 HETATM 3115 O O . HOH G 5 . ? 20.609 48.497 44.857 1.00 67.30 ? 572 HOH A O 1 HETATM 3116 O O . HOH G 5 . ? 35.647 39.623 47.256 1.00 41.33 ? 573 HOH A O 1 HETATM 3117 O O . HOH G 5 . ? 30.460 34.385 72.542 1.00 46.97 ? 574 HOH A O 1 HETATM 3118 O O . HOH G 5 . ? 16.239 42.431 80.884 1.00 43.16 ? 575 HOH A O 1 HETATM 3119 O O . HOH G 5 . ? 34.335 40.903 44.484 1.00 56.40 ? 576 HOH A O 1 HETATM 3120 O O . HOH G 5 . ? 20.359 42.134 54.269 1.00 35.76 ? 577 HOH A O 1 HETATM 3121 O O . HOH G 5 . ? 19.651 31.939 74.824 1.00 40.88 ? 578 HOH A O 1 HETATM 3122 O O . HOH G 5 . ? 10.217 71.223 39.918 1.00 62.24 ? 579 HOH A O 1 HETATM 3123 O O . HOH G 5 . ? 25.610 56.014 29.309 1.00 47.46 ? 580 HOH A O 1 HETATM 3124 O O . HOH G 5 . ? 21.096 30.976 77.015 1.00 43.68 ? 581 HOH A O 1 HETATM 3125 O O . HOH G 5 . ? 10.984 35.409 74.314 1.00 69.88 ? 582 HOH A O 1 HETATM 3126 O O . HOH G 5 . ? 27.238 62.867 39.099 1.00 61.44 ? 583 HOH A O 1 HETATM 3127 O O . HOH G 5 . ? 20.735 45.897 44.491 1.00 68.03 ? 584 HOH A O 1 HETATM 3128 O O . HOH G 5 . ? 14.847 82.640 35.011 1.00 80.24 ? 585 HOH A O 1 HETATM 3129 O O . HOH G 5 . ? 15.329 42.735 76.893 1.00 48.10 ? 586 HOH A O 1 HETATM 3130 O O . HOH G 5 . ? 21.271 40.178 82.234 1.00 55.01 ? 587 HOH A O 1 HETATM 3131 O O . HOH G 5 . ? -1.262 54.724 23.990 1.00 46.78 ? 588 HOH A O 1 HETATM 3132 O O . HOH G 5 . ? 16.284 33.485 61.660 1.00 49.44 ? 589 HOH A O 1 HETATM 3133 O O . HOH G 5 . ? 24.076 35.102 78.614 1.00 42.06 ? 590 HOH A O 1 HETATM 3134 O O . HOH G 5 . ? 4.095 40.906 40.901 1.00 71.26 ? 591 HOH A O 1 HETATM 3135 O O . HOH G 5 . ? 30.985 31.792 61.569 1.00 41.98 ? 592 HOH A O 1 HETATM 3136 O O . HOH G 5 . ? 6.372 37.973 43.656 1.00 77.37 ? 593 HOH A O 1 HETATM 3137 O O . HOH G 5 . ? 33.674 36.604 43.044 1.00 44.75 ? 594 HOH A O 1 HETATM 3138 O O . HOH G 5 . ? 27.420 28.250 65.789 1.00 37.62 ? 595 HOH A O 1 HETATM 3139 O O . HOH G 5 . ? 10.524 59.882 39.721 1.00 44.25 ? 596 HOH A O 1 HETATM 3140 O O . HOH G 5 . ? 35.088 38.653 45.008 1.00 55.20 ? 597 HOH A O 1 HETATM 3141 O O . HOH G 5 . ? 19.267 29.316 56.042 1.00 50.13 ? 598 HOH A O 1 HETATM 3142 O O . HOH G 5 . ? 35.806 50.945 27.940 1.00 60.21 ? 599 HOH A O 1 HETATM 3143 O O . HOH G 5 . ? 32.570 74.881 31.010 1.00 67.64 ? 600 HOH A O 1 HETATM 3144 O O . HOH G 5 . ? 7.380 33.974 40.045 1.00 66.16 ? 601 HOH A O 1 HETATM 3145 O O . HOH G 5 . ? 21.111 29.919 73.164 1.00 43.54 ? 602 HOH A O 1 HETATM 3146 O O . HOH H 5 . ? 33.018 53.785 64.959 1.00 33.84 ? 100 HOH B O 1 HETATM 3147 O O . HOH H 5 . ? 26.366 55.960 56.749 1.00 25.07 ? 101 HOH B O 1 HETATM 3148 O O . HOH H 5 . ? 43.105 44.241 63.215 1.00 27.26 ? 102 HOH B O 1 HETATM 3149 O O . HOH H 5 . ? 28.687 55.158 39.727 1.00 54.78 ? 103 HOH B O 1 HETATM 3150 O O . HOH H 5 . ? 27.979 69.412 49.253 1.00 41.73 ? 104 HOH B O 1 HETATM 3151 O O . HOH H 5 . ? 42.047 60.569 53.546 1.00 31.26 ? 105 HOH B O 1 HETATM 3152 O O . HOH H 5 . ? 47.354 45.542 72.677 0.50 33.84 ? 106 HOH B O 1 HETATM 3153 O O . HOH H 5 . ? 42.661 60.631 64.161 1.00 34.31 ? 107 HOH B O 1 HETATM 3154 O O . HOH H 5 . ? 21.510 56.677 50.654 1.00 34.06 ? 108 HOH B O 1 HETATM 3155 O O . HOH H 5 . ? 49.612 48.258 69.934 1.00 64.00 ? 109 HOH B O 1 HETATM 3156 O O . HOH H 5 . ? 36.381 47.176 53.494 1.00 40.11 ? 110 HOH B O 1 HETATM 3157 O O . HOH H 5 . ? 40.221 55.399 66.991 1.00 32.51 ? 111 HOH B O 1 HETATM 3158 O O . HOH H 5 . ? 37.309 66.175 54.669 1.00 44.20 ? 112 HOH B O 1 HETATM 3159 O O . HOH H 5 . ? 37.862 45.365 52.394 1.00 47.12 ? 113 HOH B O 1 HETATM 3160 O O . HOH H 5 . ? 39.539 55.365 44.710 1.00 46.99 ? 114 HOH B O 1 HETATM 3161 O O . HOH H 5 . ? 44.690 44.192 55.253 1.00 57.00 ? 115 HOH B O 1 HETATM 3162 O O . HOH H 5 . ? 35.562 70.083 62.647 1.00 36.29 ? 116 HOH B O 1 HETATM 3163 O O . HOH H 5 . ? 30.354 54.885 63.342 1.00 38.47 ? 117 HOH B O 1 HETATM 3164 O O . HOH H 5 . ? 49.284 60.482 61.251 1.00 43.99 ? 118 HOH B O 1 HETATM 3165 O O . HOH H 5 . ? 33.101 60.282 67.189 1.00 37.32 ? 119 HOH B O 1 HETATM 3166 O O . HOH H 5 . ? 24.249 66.566 43.279 1.00 46.05 ? 120 HOH B O 1 HETATM 3167 O O . HOH H 5 . ? 49.930 58.167 69.040 1.00 47.71 ? 121 HOH B O 1 HETATM 3168 O O . HOH H 5 . ? 48.876 41.561 59.762 1.00 47.83 ? 122 HOH B O 1 HETATM 3169 O O . HOH H 5 . ? 40.365 60.853 51.215 1.00 42.91 ? 123 HOH B O 1 HETATM 3170 O O . HOH H 5 . ? 46.370 66.598 57.658 1.00 50.08 ? 124 HOH B O 1 HETATM 3171 O O . HOH H 5 . ? 41.886 41.584 63.112 1.00 41.59 ? 125 HOH B O 1 HETATM 3172 O O . HOH H 5 . ? 36.840 63.194 49.130 1.00 42.06 ? 126 HOH B O 1 HETATM 3173 O O . HOH H 5 . ? 32.731 67.299 64.607 1.00 43.66 ? 127 HOH B O 1 HETATM 3174 O O . HOH H 5 . ? 28.998 53.770 46.351 1.00 50.88 ? 128 HOH B O 1 HETATM 3175 O O . HOH H 5 . ? 26.547 69.538 44.500 1.00 53.79 ? 129 HOH B O 1 HETATM 3176 O O . HOH H 5 . ? 25.218 55.926 39.938 1.00 42.52 ? 130 HOH B O 1 HETATM 3177 O O . HOH H 5 . ? 16.728 70.579 46.418 1.00 76.08 ? 131 HOH B O 1 HETATM 3178 O O . HOH H 5 . ? 24.192 62.361 60.496 1.00 50.93 ? 132 HOH B O 1 HETATM 3179 O O . HOH H 5 . ? 31.187 70.175 49.584 1.00 59.16 ? 133 HOH B O 1 HETATM 3180 O O . HOH H 5 . ? 38.771 57.045 69.463 1.00 46.45 ? 134 HOH B O 1 HETATM 3181 O O . HOH H 5 . ? 32.563 57.683 67.279 1.00 47.69 ? 135 HOH B O 1 HETATM 3182 O O . HOH H 5 . ? 37.100 74.497 59.172 1.00 56.38 ? 136 HOH B O 1 HETATM 3183 O O . HOH H 5 . ? 29.334 64.901 42.861 1.00 57.76 ? 137 HOH B O 1 HETATM 3184 O O . HOH H 5 . ? 44.253 57.559 46.148 1.00 52.28 ? 138 HOH B O 1 HETATM 3185 O O . HOH H 5 . ? 47.765 52.792 60.143 1.00 43.72 ? 139 HOH B O 1 HETATM 3186 O O . HOH H 5 . ? 32.785 58.368 42.668 1.00 57.59 ? 140 HOH B O 1 HETATM 3187 O O . HOH H 5 . ? 49.340 58.697 54.722 1.00 54.60 ? 141 HOH B O 1 HETATM 3188 O O . HOH H 5 . ? 44.192 49.071 72.502 0.50 25.99 ? 142 HOH B O 1 HETATM 3189 O O . HOH H 5 . ? 30.786 62.107 66.140 1.00 52.54 ? 143 HOH B O 1 HETATM 3190 O O . HOH H 5 . ? 19.872 68.407 46.655 1.00 46.09 ? 144 HOH B O 1 HETATM 3191 O O . HOH H 5 . ? 29.655 69.625 61.420 1.00 47.71 ? 145 HOH B O 1 HETATM 3192 O O . HOH H 5 . ? 39.462 41.190 54.294 1.00 59.66 ? 146 HOH B O 1 HETATM 3193 O O . HOH H 5 . ? 49.697 62.910 63.833 1.00 36.06 ? 147 HOH B O 1 HETATM 3194 O O . HOH H 5 . ? 35.684 65.545 46.980 1.00 60.15 ? 148 HOH B O 1 HETATM 3195 O O . HOH H 5 . ? 34.740 63.821 67.019 1.00 49.69 ? 149 HOH B O 1 HETATM 3196 O O . HOH H 5 . ? 18.668 60.722 54.291 1.00 48.66 ? 150 HOH B O 1 HETATM 3197 O O . HOH H 5 . ? 51.210 61.833 65.759 1.00 39.94 ? 151 HOH B O 1 HETATM 3198 O O . HOH H 5 . ? 48.739 57.564 57.576 1.00 56.58 ? 152 HOH B O 1 HETATM 3199 O O . HOH H 5 . ? 18.937 65.252 56.662 1.00 47.09 ? 153 HOH B O 1 HETATM 3200 O O . HOH H 5 . ? 23.202 52.759 57.138 1.00 45.14 ? 154 HOH B O 1 HETATM 3201 O O . HOH H 5 . ? 26.763 50.013 44.258 1.00 61.97 ? 155 HOH B O 1 HETATM 3202 O O . HOH H 5 . ? 25.804 60.144 61.401 1.00 39.18 ? 156 HOH B O 1 HETATM 3203 O O . HOH H 5 . ? 32.640 76.351 61.806 1.00 63.58 ? 157 HOH B O 1 HETATM 3204 O O . HOH H 5 . ? 50.147 43.927 69.851 1.00 62.96 ? 158 HOH B O 1 HETATM 3205 O O . HOH H 5 . ? 48.259 47.446 57.264 1.00 72.11 ? 159 HOH B O 1 HETATM 3206 O O . HOH H 5 . ? 21.484 56.622 55.485 1.00 40.41 ? 160 HOH B O 1 HETATM 3207 O O . HOH H 5 . ? 52.285 65.189 50.099 1.00 64.95 ? 161 HOH B O 1 HETATM 3208 O O . HOH H 5 . ? 20.241 56.309 53.033 1.00 51.92 ? 162 HOH B O 1 HETATM 3209 O O . HOH H 5 . ? 42.023 41.711 59.776 1.00 49.54 ? 163 HOH B O 1 HETATM 3210 O O . HOH H 5 . ? 37.002 46.231 65.608 1.00 38.49 ? 164 HOH B O 1 HETATM 3211 O O . HOH H 5 . ? 30.924 63.532 45.196 1.00 47.48 ? 165 HOH B O 1 HETATM 3212 O O . HOH H 5 . ? 48.639 50.782 59.214 1.00 59.85 ? 166 HOH B O 1 HETATM 3213 O O . HOH H 5 . ? 22.340 52.709 62.202 1.00 60.17 ? 167 HOH B O 1 HETATM 3214 O O . HOH H 5 . ? 31.524 49.395 47.727 1.00 46.46 ? 168 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . PRO A 7 ? 1.1585 0.8283 1.2770 -0.2008 0.1479 0.0539 7 PRO A N 2 C CA . PRO A 7 ? 1.1527 0.8606 1.3359 -0.2404 0.1505 0.0422 7 PRO A CA 3 C C . PRO A 7 ? 1.0936 0.8592 1.3063 -0.2432 0.1174 0.0112 7 PRO A C 4 O O . PRO A 7 ? 1.1030 0.8422 1.3030 -0.2440 0.0961 -0.0115 7 PRO A O 5 C CB . PRO A 7 ? 1.1487 0.8937 1.3533 -0.2455 0.1810 0.0665 7 PRO A CB 6 C CG . PRO A 7 ? 1.1590 0.8750 1.2935 -0.2063 0.1914 0.0896 7 PRO A CG 7 C CD . PRO A 7 ? 1.1423 0.8372 1.2378 -0.1781 0.1602 0.0748 7 PRO A CD 8 N N . GLU A 8 ? 1.0397 0.8767 1.2836 -0.2413 0.1149 0.0111 8 GLU A N 9 C CA . GLU A 8 ? 0.9902 0.8798 1.2581 -0.2424 0.0840 -0.0149 8 GLU A CA 10 C C . GLU A 8 ? 0.9266 0.8580 1.1710 -0.2104 0.0776 -0.0112 8 GLU A C 11 O O . GLU A 8 ? 0.8916 0.8697 1.1533 -0.2079 0.0567 -0.0265 8 GLU A O 12 C CB . GLU A 8 ? 0.9945 0.9336 1.3390 -0.2759 0.0800 -0.0236 8 GLU A CB 13 C CG . GLU A 8 ? 0.9913 0.9729 1.3764 -0.2801 0.1128 0.0011 8 GLU A CG 14 C CD . GLU A 8 ? 0.9916 1.0387 1.4704 -0.3104 0.1080 -0.0089 8 GLU A CD 15 O OE1 . GLU A 8 ? 1.0409 1.0740 1.5662 -0.3467 0.1002 -0.0216 8 GLU A OE1 16 O OE2 . GLU A 8 ? 0.9715 1.0845 1.4816 -0.2975 0.1112 -0.0047 8 GLU A OE2 17 N N . GLU A 9 ? 0.9115 0.8206 1.1138 -0.1857 0.0933 0.0088 9 GLU A N 18 C CA . GLU A 9 ? 0.8613 0.7909 1.0320 -0.1554 0.0830 0.0092 9 GLU A CA 19 C C . GLU A 9 ? 0.8322 0.7444 0.9816 -0.1463 0.0617 -0.0107 9 GLU A C 20 O O . GLU A 9 ? 0.7979 0.7338 0.9348 -0.1308 0.0489 -0.0188 9 GLU A O 21 C CB . GLU A 9 ? 0.8825 0.7816 1.0102 -0.1321 0.0980 0.0318 9 GLU A CB 22 C CG . GLU A 9 ? 0.9070 0.8258 1.0356 -0.1286 0.1218 0.0523 9 GLU A CG 23 C CD . GLU A 9 ? 0.9296 0.8109 0.9973 -0.0995 0.1291 0.0714 9 GLU A CD 24 O OE1 . GLU A 9 ? 0.9523 0.8177 0.9897 -0.0783 0.1074 0.0654 9 GLU A OE1 25 O OE2 . GLU A 9 ? 0.9793 0.8469 1.0297 -0.0972 0.1567 0.0921 9 GLU A OE2 26 N N . SER A 10 ? 0.8452 0.7108 0.9883 -0.1562 0.0614 -0.0181 10 SER A N 27 C CA . SER A 10 ? 0.8244 0.6649 0.9437 -0.1448 0.0491 -0.0359 10 SER A CA 28 C C . SER A 10 ? 0.7952 0.6543 0.9184 -0.1545 0.0304 -0.0603 10 SER A C 29 O O . SER A 10 ? 0.8006 0.6438 0.8962 -0.1411 0.0244 -0.0742 10 SER A O 30 C CB . SER A 10 ? 0.8807 0.6581 0.9854 -0.1467 0.0565 -0.0360 10 SER A CB 31 O OG . SER A 10 ? 0.9058 0.6639 0.9867 -0.1213 0.0539 -0.0428 10 SER A OG 32 N N . GLN A 11 ? 0.7570 0.6485 0.9142 -0.1760 0.0216 -0.0654 11 GLN A N 33 C CA . GLN A 11 ? 0.7256 0.6368 0.8835 -0.1819 -0.0038 -0.0884 11 GLN A CA 34 C C . GLN A 11 ? 0.6600 0.6321 0.8360 -0.1737 -0.0121 -0.0837 11 GLN A C 35 O O . GLN A 11 ? 0.6574 0.6615 0.8610 -0.1851 -0.0333 -0.0965 11 GLN A O 36 C CB . GLN A 11 ? 0.7800 0.6746 0.9657 -0.2128 -0.0181 -0.1052 11 GLN A CB 37 C CG . GLN A 11 ? 0.8335 0.6564 0.9877 -0.2162 -0.0124 -0.1138 11 GLN A CG 38 C CD . GLN A 11 ? 0.9117 0.7078 1.0938 -0.2501 -0.0249 -0.1292 11 GLN A CD 39 O OE1 . GLN A 11 ? 0.9286 0.7379 1.1621 -0.2747 -0.0133 -0.1164 11 GLN A OE1 40 N NE2 . GLN A 11 ? 0.9549 0.7076 1.1007 -0.2521 -0.0469 -0.1573 11 GLN A NE2 41 N N . PHE A 12 ? 0.5917 0.5771 0.7525 -0.1523 0.0020 -0.0665 12 PHE A N 42 C CA . PHE A 12 ? 0.5351 0.5670 0.7025 -0.1391 -0.0025 -0.0607 12 PHE A CA 43 C C . PHE A 12 ? 0.5089 0.5279 0.6301 -0.1162 -0.0058 -0.0631 12 PHE A C 44 O O . PHE A 12 ? 0.4942 0.4967 0.5980 -0.1033 0.0075 -0.0522 12 PHE A O 45 C CB . PHE A 12 ? 0.5184 0.5711 0.7065 -0.1356 0.0194 -0.0378 12 PHE A CB 46 C CG . PHE A 12 ? 0.4938 0.5941 0.6933 -0.1214 0.0173 -0.0325 12 PHE A CG 47 C CD1 . PHE A 12 ? 0.4928 0.6230 0.7005 -0.1176 -0.0061 -0.0469 12 PHE A CD1 48 C CD2 . PHE A 12 ? 0.4866 0.5953 0.6825 -0.1090 0.0382 -0.0132 12 PHE A CD2 49 C CE1 . PHE A 12 ? 0.4527 0.6229 0.6706 -0.1007 -0.0079 -0.0417 12 PHE A CE1 50 C CE2 . PHE A 12 ? 0.4789 0.6256 0.6823 -0.0932 0.0387 -0.0093 12 PHE A CE2 51 C CZ . PHE A 12 ? 0.4577 0.6366 0.6754 -0.0889 0.0157 -0.0234 12 PHE A CZ 52 N N . PHE A 13 ? 0.5027 0.5275 0.6053 -0.1117 -0.0246 -0.0776 13 PHE A N 53 C CA . PHE A 13 ? 0.4936 0.5024 0.5508 -0.0930 -0.0247 -0.0798 13 PHE A CA 54 C C . PHE A 13 ? 0.4585 0.4991 0.5143 -0.0786 -0.0298 -0.0715 13 PHE A C 55 O O . PHE A 13 ? 0.4549 0.5258 0.5294 -0.0794 -0.0463 -0.0757 13 PHE A O 56 C CB . PHE A 13 ? 0.5436 0.5233 0.5627 -0.0936 -0.0400 -0.0998 13 PHE A CB 57 C CG . PHE A 13 ? 0.5812 0.5344 0.5486 -0.0763 -0.0316 -0.1004 13 PHE A CG 58 C CD1 . PHE A 13 ? 0.5989 0.5282 0.5578 -0.0707 -0.0068 -0.0950 13 PHE A CD1 59 C CD2 . PHE A 13 ? 0.6282 0.5793 0.5580 -0.0649 -0.0470 -0.1054 13 PHE A CD2 60 C CE1 . PHE A 13 ? 0.6024 0.5095 0.5234 -0.0580 0.0075 -0.0944 13 PHE A CE1 61 C CE2 . PHE A 13 ? 0.6559 0.5745 0.5335 -0.0505 -0.0327 -0.1030 13 PHE A CE2 62 C CZ . PHE A 13 ? 0.6338 0.5320 0.5108 -0.0493 -0.0029 -0.0974 13 PHE A CZ 63 N N . GLN A 14 ? 0.4301 0.4629 0.4678 -0.0651 -0.0174 -0.0608 14 GLN A N 64 C CA . GLN A 14 ? 0.4142 0.4650 0.4431 -0.0501 -0.0206 -0.0530 14 GLN A CA 65 C C . GLN A 14 ? 0.4266 0.4495 0.4158 -0.0391 -0.0157 -0.0525 14 GLN A C 66 O O . GLN A 14 ? 0.4220 0.4222 0.4063 -0.0419 -0.0027 -0.0525 14 GLN A O 67 C CB . GLN A 14 ? 0.3881 0.4549 0.4379 -0.0461 -0.0093 -0.0385 14 GLN A CB 68 C CG . GLN A 14 ? 0.4047 0.5007 0.4947 -0.0557 -0.0055 -0.0342 14 GLN A CG 69 C CD . GLN A 14 ? 0.4207 0.5229 0.5126 -0.0460 0.0099 -0.0184 14 GLN A CD 70 O OE1 . GLN A 14 ? 0.3899 0.5133 0.4818 -0.0322 0.0106 -0.0141 14 GLN A OE1 71 N NE2 . GLN A 14 ? 0.4343 0.5122 0.5207 -0.0496 0.0216 -0.0101 14 GLN A NE2 72 N N . LEU A 15 ? 0.4357 0.4612 0.4016 -0.0260 -0.0245 -0.0511 15 LEU A N 73 C CA . LEU A 15 ? 0.4513 0.4464 0.3781 -0.0169 -0.0179 -0.0482 15 LEU A CA 74 C C . LEU A 15 ? 0.4506 0.4547 0.3755 -0.0039 -0.0207 -0.0389 15 LEU A C 75 O O . LEU A 15 ? 0.4534 0.4825 0.3860 0.0063 -0.0326 -0.0381 15 LEU A O 76 C CB . LEU A 15 ? 0.4987 0.4696 0.3781 -0.0099 -0.0280 -0.0561 15 LEU A CB 77 C CG . LEU A 15 ? 0.5512 0.4964 0.4075 -0.0173 -0.0265 -0.0681 15 LEU A CG 78 C CD1 . LEU A 15 ? 0.6544 0.5754 0.4536 -0.0047 -0.0471 -0.0765 15 LEU A CD1 79 C CD2 . LEU A 15 ? 0.5747 0.4877 0.4182 -0.0216 0.0024 -0.0655 15 LEU A CD2 80 N N . PHE A 16 ? 0.4555 0.4387 0.3731 -0.0037 -0.0101 -0.0334 16 PHE A N 81 C CA . PHE A 16 ? 0.4616 0.4394 0.3683 0.0080 -0.0133 -0.0269 16 PHE A CA 82 C C . PHE A 16 ? 0.4980 0.4349 0.3710 0.0088 -0.0064 -0.0251 16 PHE A C 83 O O . PHE A 16 ? 0.5039 0.4263 0.3887 -0.0038 0.0065 -0.0254 16 PHE A O 84 C CB . PHE A 16 ? 0.4414 0.4249 0.3735 0.0038 -0.0104 -0.0235 16 PHE A CB 85 C CG . PHE A 16 ? 0.4106 0.4226 0.3682 0.0028 -0.0104 -0.0213 16 PHE A CG 86 C CD1 . PHE A 16 ? 0.4421 0.4688 0.3975 0.0157 -0.0116 -0.0162 16 PHE A CD1 87 C CD2 . PHE A 16 ? 0.4386 0.4578 0.4201 -0.0105 -0.0055 -0.0237 16 PHE A CD2 88 C CE1 . PHE A 16 ? 0.4610 0.5109 0.4402 0.0128 -0.0042 -0.0115 16 PHE A CE1 89 C CE2 . PHE A 16 ? 0.4223 0.4602 0.4255 -0.0140 -0.0021 -0.0197 16 PHE A CE2 90 C CZ . PHE A 16 ? 0.4257 0.4793 0.4288 -0.0037 0.0002 -0.0127 16 PHE A CZ 91 N N . TYR A 17 ? 0.5225 0.4401 0.3576 0.0237 -0.0130 -0.0223 17 TYR A N 92 C CA . TYR A 17 ? 0.5714 0.4404 0.3682 0.0233 -0.0030 -0.0180 17 TYR A CA 93 C C . TYR A 17 ? 0.5817 0.4297 0.3577 0.0367 -0.0106 -0.0138 17 TYR A C 94 O O . TYR A 17 ? 0.5644 0.4287 0.3324 0.0561 -0.0242 -0.0139 17 TYR A O 95 C CB . TYR A 17 ? 0.6298 0.4725 0.3761 0.0324 -0.0036 -0.0179 17 TYR A CB 96 C CG . TYR A 17 ? 0.6614 0.4956 0.4046 0.0193 0.0117 -0.0220 17 TYR A CG 97 C CD1 . TYR A 17 ? 0.6980 0.4877 0.4142 0.0109 0.0382 -0.0170 17 TYR A CD1 98 C CD2 . TYR A 17 ? 0.6814 0.5488 0.4498 0.0147 0.0032 -0.0309 17 TYR A CD2 99 C CE1 . TYR A 17 ? 0.7393 0.5179 0.4487 0.0023 0.0580 -0.0212 17 TYR A CE1 100 C CE2 . TYR A 17 ? 0.6770 0.5288 0.4358 0.0052 0.0182 -0.0367 17 TYR A CE2 101 C CZ . TYR A 17 ? 0.7125 0.5208 0.4404 0.0010 0.0463 -0.0319 17 TYR A CZ 102 O OH . TYR A 17 ? 0.7676 0.5575 0.4812 -0.0043 0.0659 -0.0379 17 TYR A OH 103 N N . THR A 18 ? 0.6036 0.4154 0.3751 0.0259 -0.0009 -0.0112 18 THR A N 104 C CA . THR A 18 ? 0.6489 0.4243 0.3933 0.0357 -0.0078 -0.0089 18 THR A CA 105 C C . THR A 18 ? 0.7095 0.4254 0.4151 0.0290 0.0077 -0.0021 18 THR A C 106 O O . THR A 18 ? 0.7194 0.4234 0.4455 0.0059 0.0280 -0.0004 18 THR A O 107 C CB . THR A 18 ? 0.6278 0.4082 0.4056 0.0254 -0.0147 -0.0141 18 THR A CB 108 O OG1 . THR A 18 ? 0.6098 0.4357 0.4120 0.0331 -0.0242 -0.0173 18 THR A OG1 109 C CG2 . THR A 18 ? 0.6677 0.4020 0.4108 0.0355 -0.0244 -0.0149 18 THR A CG2 110 N N . LEU A 19 ? 0.7475 0.4259 0.3972 0.0510 0.0009 0.0029 19 LEU A N 111 C CA . LEU A 19 ? 0.8137 0.4230 0.4106 0.0495 0.0159 0.0124 19 LEU A CA 112 C C . LEU A 19 ? 0.8463 0.4121 0.4226 0.0565 0.0070 0.0125 19 LEU A C 113 O O . LEU A 19 ? 0.8606 0.4225 0.4065 0.0860 -0.0105 0.0116 19 LEU A O 114 C CB . LEU A 19 ? 0.8662 0.4568 0.4014 0.0755 0.0101 0.0182 19 LEU A CB 115 C CG . LEU A 19 ? 0.8530 0.4569 0.3811 0.0692 0.0202 0.0180 19 LEU A CG 116 C CD1 . LEU A 19 ? 0.8142 0.4947 0.4092 0.0601 0.0108 0.0066 19 LEU A CD1 117 C CD2 . LEU A 19 ? 0.8949 0.4695 0.3515 0.0979 0.0059 0.0218 19 LEU A CD2 118 N N . LEU A 20 ? 0.8597 0.3977 0.4609 0.0293 0.0176 0.0114 20 LEU A N 119 C CA . LEU A 20 ? 0.9153 0.4006 0.4961 0.0302 0.0081 0.0088 20 LEU A CA 120 C C . LEU A 20 ? 1.0020 0.4059 0.5299 0.0244 0.0286 0.0215 20 LEU A C 121 O O . LEU A 20 ? 1.0259 0.4084 0.5766 -0.0071 0.0551 0.0274 20 LEU A O 122 C CB . LEU A 20 ? 0.8856 0.3864 0.5283 0.0028 -0.0002 -0.0029 20 LEU A CB 123 C CG . LEU A 20 ? 0.9691 0.4047 0.5959 -0.0063 -0.0109 -0.0088 20 LEU A CG 124 C CD1 . LEU A 20 ? 0.9901 0.3788 0.5435 0.0304 -0.0277 -0.0101 20 LEU A CD1 125 C CD2 . LEU A 20 ? 0.9402 0.4047 0.6307 -0.0278 -0.0310 -0.0245 20 LEU A CD2 126 N N . LEU A 21 ? 1.0522 0.4095 0.5096 0.0569 0.0185 0.0269 21 LEU A N 127 C CA . LEU A 21 ? 1.1460 0.4160 0.5335 0.0608 0.0357 0.0417 21 LEU A CA 128 C C . LEU A 21 ? 1.2033 0.4031 0.5765 0.0508 0.0319 0.0387 21 LEU A C 129 O O . LEU A 21 ? 1.2281 0.3922 0.5535 0.0818 0.0125 0.0358 21 LEU A O 130 C CB . LEU A 21 ? 1.1800 0.4392 0.4981 0.1068 0.0213 0.0486 21 LEU A CB 131 C CG . LEU A 21 ? 1.1866 0.4718 0.4845 0.1168 0.0266 0.0552 21 LEU A CG 132 C CD1 . LEU A 21 ? 1.0975 0.4659 0.4692 0.0935 0.0316 0.0462 21 LEU A CD1 133 C CD2 . LEU A 21 ? 1.2006 0.4929 0.4502 0.1656 -0.0026 0.0557 21 LEU A CD2 134 N N . GLY A 22 ? 1.2180 0.4004 0.6388 0.0068 0.0504 0.0379 22 GLY A N 135 C CA . GLY A 22 ? 1.2860 0.4024 0.7091 -0.0144 0.0460 0.0321 22 GLY A CA 136 C C . GLY A 22 ? 1.4036 0.4110 0.7364 0.0015 0.0539 0.0449 22 GLY A C 137 O O . GLY A 22 ? 1.4472 0.4168 0.7355 0.0291 0.0291 0.0372 22 GLY A O 138 N N . ASN A 23 ? 1.4724 0.4226 0.7742 -0.0151 0.0911 0.0649 23 ASN A N 139 C CA . ASN A 23 ? 1.5911 0.4286 0.7898 0.0050 0.1037 0.0830 23 ASN A CA 140 C C . ASN A 23 ? 1.6194 0.4447 0.7552 0.0253 0.1279 0.1041 23 ASN A C 141 O O . ASN A 23 ? 1.5420 0.4491 0.7120 0.0284 0.1283 0.1010 23 ASN A O 142 C CB . ASN A 23 ? 1.6847 0.4303 0.8888 -0.0382 0.1285 0.0890 23 ASN A CB 143 C CG . ASN A 23 ? 1.6681 0.4481 0.9620 -0.0938 0.1664 0.0928 23 ASN A CG 144 O OD1 . ASN A 23 ? 1.6293 0.4714 0.9473 -0.0946 0.1862 0.0989 23 ASN A OD1 145 N ND2 . ASN A 23 ? 1.7267 0.4651 1.0738 -0.1401 0.1765 0.0880 23 ASN A ND2 146 N N . VAL A 24 ? 1.7399 0.4563 0.7772 0.0402 0.1462 0.1249 24 VAL A N 147 C CA . VAL A 24 ? 1.7923 0.4810 0.7494 0.0648 0.1647 0.1448 24 VAL A CA 148 C C . VAL A 24 ? 1.7569 0.4835 0.7592 0.0278 0.2076 0.1516 24 VAL A C 149 O O . VAL A 24 ? 1.7207 0.4950 0.7075 0.0468 0.2048 0.1518 24 VAL A O 150 C CB . VAL A 24 ? 1.9451 0.4948 0.7760 0.0900 0.1766 0.1678 24 VAL A CB 151 C CG1 . VAL A 24 ? 2.0398 0.4968 0.8728 0.0409 0.2229 0.1820 24 VAL A CG1 152 C CG2 . VAL A 24 ? 2.0178 0.5372 0.7496 0.1276 0.1819 0.1855 24 VAL A CG2 153 N N . SER A 25 ? 1.7651 0.4753 0.8318 -0.0247 0.2447 0.1545 25 SER A N 154 C CA . SER A 25 ? 1.7406 0.4853 0.8634 -0.0616 0.2923 0.1609 25 SER A CA 155 C C . SER A 25 ? 1.6006 0.4738 0.8549 -0.0848 0.2781 0.1378 25 SER A C 156 O O . SER A 25 ? 1.5772 0.4854 0.8955 -0.1166 0.3174 0.1407 25 SER A O 157 C CB . SER A 25 ? 1.8419 0.5015 0.9738 -0.1073 0.3475 0.1788 25 SER A CB 158 O OG . SER A 25 ? 1.8621 0.4783 1.0180 -0.1247 0.3275 0.1710 25 SER A OG 159 N N . SER A 26 ? 1.5093 0.4502 0.8013 -0.0666 0.2251 0.1161 26 SER A N 160 C CA . SER A 26 ? 1.3924 0.4419 0.8017 -0.0878 0.2096 0.0955 26 SER A CA 161 C C . SER A 26 ? 1.3039 0.4396 0.7199 -0.0543 0.1715 0.0816 26 SER A C 162 O O . SER A 26 ? 1.2949 0.4328 0.6729 -0.0206 0.1338 0.0748 26 SER A O 163 C CB . SER A 26 ? 1.3764 0.4291 0.8602 -0.1173 0.1890 0.0798 26 SER A CB 164 O OG . SER A 26 ? 1.2840 0.4342 0.8783 -0.1379 0.1744 0.0615 26 SER A OG 165 N N . THR A 27 ? 1.2385 0.4427 0.7057 -0.0644 0.1855 0.0781 27 THR A N 166 C CA . THR A 27 ? 1.1486 0.4399 0.6474 -0.0450 0.1536 0.0634 27 THR A CA 167 C C . THR A 27 ? 1.0727 0.4374 0.6831 -0.0764 0.1575 0.0509 27 THR A C 168 O O . THR A 27 ? 1.0892 0.4543 0.7426 -0.1045 0.1957 0.0565 27 THR A O 169 C CB . THR A 27 ? 1.1544 0.4547 0.5966 -0.0205 0.1606 0.0694 27 THR A CB 170 O OG1 . THR A 27 ? 1.2578 0.4747 0.5905 0.0056 0.1649 0.0846 27 THR A OG1 171 C CG2 . THR A 27 ? 1.0663 0.4440 0.5313 0.0028 0.1207 0.0546 27 THR A CG2 172 N N . GLU A 28 ? 0.9995 0.4248 0.6550 -0.0687 0.1195 0.0348 28 GLU A N 173 C CA . GLU A 28 ? 0.9231 0.4211 0.6729 -0.0882 0.1148 0.0227 28 GLU A CA 174 C C . GLU A 28 ? 0.8608 0.4178 0.6056 -0.0644 0.0978 0.0172 28 GLU A C 175 O O . GLU A 28 ? 0.8551 0.4188 0.5607 -0.0373 0.0705 0.0140 28 GLU A O 176 C CB . GLU A 28 ? 0.9059 0.4133 0.7064 -0.1007 0.0835 0.0086 28 GLU A CB 177 N N . LEU A 29 ? 0.8249 0.4244 0.6122 -0.0741 0.1158 0.0157 29 LEU A N 178 C CA . LEU A 29 ? 0.7682 0.4159 0.5495 -0.0546 0.1000 0.0101 29 LEU A CA 179 C C . LEU A 29 ? 0.6961 0.4077 0.5564 -0.0641 0.0872 -0.0010 29 LEU A C 180 O O . LEU A 29 ? 0.6788 0.4062 0.6047 -0.0858 0.1008 -0.0037 29 LEU A O 181 C CB . LEU A 29 ? 0.8021 0.4353 0.5400 -0.0483 0.1264 0.0166 29 LEU A CB 182 C CG . LEU A 29 ? 0.9023 0.4685 0.5421 -0.0309 0.1370 0.0284 29 LEU A CG 183 C CD1 . LEU A 29 ? 0.9568 0.5106 0.5639 -0.0292 0.1655 0.0314 29 LEU A CD1 184 C CD2 . LEU A 29 ? 0.9094 0.4805 0.5024 -0.0005 0.0989 0.0255 29 LEU A CD2 185 N N . THR A 30 ? 0.6529 0.4007 0.5085 -0.0466 0.0619 -0.0068 30 THR A N 186 C CA . THR A 30 ? 0.6044 0.4053 0.5163 -0.0504 0.0543 -0.0143 30 THR A CA 187 C C . THR A 30 ? 0.5716 0.3929 0.4550 -0.0347 0.0498 -0.0150 30 THR A C 188 O O . THR A 30 ? 0.5814 0.3898 0.4146 -0.0180 0.0396 -0.0125 30 THR A O 189 C CB . THR A 30 ? 0.5882 0.4091 0.5296 -0.0479 0.0237 -0.0214 30 THR A CB 190 O OG1 . THR A 30 ? 0.6446 0.4574 0.5367 -0.0267 0.0057 -0.0204 30 THR A OG1 191 C CG2 . THR A 30 ? 0.6122 0.4109 0.5843 -0.0649 0.0193 -0.0247 30 THR A CG2 192 N N . GLY A 31 ? 0.5290 0.3813 0.4479 -0.0399 0.0561 -0.0194 31 GLY A N 193 C CA . GLY A 31 ? 0.5100 0.3819 0.4113 -0.0294 0.0481 -0.0226 31 GLY A CA 194 C C . GLY A 31 ? 0.4891 0.3901 0.4368 -0.0364 0.0525 -0.0280 31 GLY A C 195 O O . GLY A 31 ? 0.4604 0.3631 0.4459 -0.0466 0.0703 -0.0292 31 GLY A O 196 N N . MET A 32 ? 0.4770 0.4008 0.4260 -0.0304 0.0376 -0.0309 32 MET A N 197 C CA . MET A 32 ? 0.5002 0.4440 0.4853 -0.0347 0.0395 -0.0351 32 MET A CA 198 C C . MET A 32 ? 0.4665 0.4159 0.4331 -0.0326 0.0340 -0.0397 32 MET A C 199 O O . MET A 32 ? 0.4673 0.4245 0.4144 -0.0267 0.0200 -0.0388 32 MET A O 200 C CB . MET A 32 ? 0.4764 0.4390 0.4921 -0.0325 0.0231 -0.0326 32 MET A CB 201 C CG . MET A 32 ? 0.5079 0.4819 0.5599 -0.0347 0.0252 -0.0351 32 MET A CG 202 S SD . MET A 32 ? 0.5523 0.5345 0.6203 -0.0273 0.0033 -0.0305 32 MET A SD 203 C CE . MET A 32 ? 0.5186 0.4934 0.5989 -0.0292 -0.0062 -0.0322 32 MET A CE 204 N N . ALA A 33 ? 0.4728 0.4185 0.4501 -0.0371 0.0444 -0.0459 33 ALA A N 205 C CA . ALA A 33 ? 0.4538 0.4029 0.4237 -0.0392 0.0358 -0.0525 33 ALA A CA 206 C C . ALA A 33 ? 0.4362 0.3969 0.4448 -0.0429 0.0348 -0.0513 33 ALA A C 207 O O . ALA A 33 ? 0.4336 0.3899 0.4667 -0.0417 0.0461 -0.0514 33 ALA A O 208 C CB . ALA A 33 ? 0.4912 0.4106 0.4251 -0.0393 0.0470 -0.0626 33 ALA A CB 209 N N . LEU A 34 ? 0.4071 0.3810 0.4229 -0.0467 0.0229 -0.0500 34 LEU A N 210 C CA . LEU A 34 ? 0.3948 0.3704 0.4367 -0.0493 0.0231 -0.0453 34 LEU A CA 211 C C . LEU A 34 ? 0.4022 0.3704 0.4453 -0.0604 0.0211 -0.0522 34 LEU A C 212 O O . LEU A 34 ? 0.4021 0.3813 0.4382 -0.0663 0.0115 -0.0573 34 LEU A O 213 C CB . LEU A 34 ? 0.3752 0.3676 0.4235 -0.0449 0.0159 -0.0331 34 LEU A CB 214 C CG . LEU A 34 ? 0.4004 0.3949 0.4454 -0.0341 0.0111 -0.0266 34 LEU A CG 215 C CD1 . LEU A 34 ? 0.4545 0.4577 0.4907 -0.0283 0.0071 -0.0167 34 LEU A CD1 216 C CD2 . LEU A 34 ? 0.3928 0.3765 0.4564 -0.0295 0.0099 -0.0253 34 LEU A CD2 217 N N . LEU A 35 ? 0.4065 0.3546 0.4608 -0.0625 0.0276 -0.0531 35 LEU A N 218 C CA . LEU A 35 ? 0.4239 0.3596 0.4848 -0.0756 0.0257 -0.0564 35 LEU A CA 219 C C . LEU A 35 ? 0.4165 0.3479 0.4922 -0.0731 0.0302 -0.0405 35 LEU A C 220 O O . LEU A 35 ? 0.4284 0.3463 0.5061 -0.0601 0.0332 -0.0360 35 LEU A O 221 C CB . LEU A 35 ? 0.4505 0.3498 0.4981 -0.0777 0.0311 -0.0713 35 LEU A CB 222 C CG . LEU A 35 ? 0.5139 0.3907 0.5644 -0.0950 0.0258 -0.0793 35 LEU A CG 223 C CD1 . LEU A 35 ? 0.4903 0.3869 0.5413 -0.1095 0.0085 -0.0889 35 LEU A CD1 224 C CD2 . LEU A 35 ? 0.5474 0.3764 0.5776 -0.0916 0.0331 -0.0940 35 LEU A CD2 225 N N . ALA A 36 ? 0.4108 0.3522 0.4969 -0.0839 0.0311 -0.0318 36 ALA A N 226 C CA . ALA A 36 ? 0.4124 0.3476 0.4969 -0.0776 0.0386 -0.0128 36 ALA A CA 227 C C . ALA A 36 ? 0.3975 0.3442 0.4679 -0.0576 0.0325 -0.0065 36 ALA A C 228 O O . ALA A 36 ? 0.3971 0.3702 0.4655 -0.0551 0.0276 -0.0099 36 ALA A O 229 C CB . ALA A 36 ? 0.4429 0.3338 0.5221 -0.0766 0.0452 -0.0071 36 ALA A CB 230 N N . ASP A 37 ? 0.3981 0.3223 0.4586 -0.0428 0.0292 0.0008 37 ASP A N 231 C CA . ASP A 37 ? 0.3881 0.3204 0.4405 -0.0259 0.0166 0.0023 37 ASP A CA 232 C C . ASP A 37 ? 0.3666 0.3001 0.4403 -0.0197 0.0100 -0.0085 37 ASP A C 233 O O . ASP A 37 ? 0.3679 0.3054 0.4479 -0.0078 -0.0031 -0.0085 37 ASP A O 234 C CB . ASP A 37 ? 0.4259 0.3337 0.4504 -0.0102 0.0111 0.0173 37 ASP A CB 235 C CG . ASP A 37 ? 0.4902 0.3607 0.5086 -0.0047 0.0126 0.0246 37 ASP A CG 236 O OD1 . ASP A 37 ? 0.5003 0.3636 0.5393 -0.0135 0.0192 0.0173 37 ASP A OD1 237 O OD2 . ASP A 37 ? 0.5383 0.3789 0.5230 0.0114 0.0065 0.0377 37 ASP A OD2 238 N N . VAL A 38 ? 0.3613 0.2909 0.4483 -0.0279 0.0196 -0.0189 38 VAL A N 239 C CA . VAL A 38 ? 0.3778 0.3081 0.4886 -0.0206 0.0222 -0.0283 38 VAL A CA 240 C C . VAL A 38 ? 0.3774 0.3262 0.4872 -0.0274 0.0288 -0.0368 38 VAL A C 241 O O . VAL A 38 ? 0.3786 0.3245 0.4685 -0.0377 0.0349 -0.0426 38 VAL A O 242 C CB . VAL A 38 ? 0.3863 0.2912 0.4995 -0.0224 0.0341 -0.0359 38 VAL A CB 243 C CG1 . VAL A 38 ? 0.4041 0.3126 0.5450 -0.0119 0.0444 -0.0460 38 VAL A CG1 244 C CG2 . VAL A 38 ? 0.4377 0.3124 0.5434 -0.0167 0.0298 -0.0254 38 VAL A CG2 245 N N . PRO A 39 ? 0.3874 0.3514 0.5171 -0.0221 0.0256 -0.0373 39 PRO A N 246 C CA . PRO A 39 ? 0.3923 0.3642 0.5199 -0.0279 0.0371 -0.0430 39 PRO A CA 247 C C . PRO A 39 ? 0.4160 0.3754 0.5461 -0.0286 0.0599 -0.0524 39 PRO A C 248 O O . PRO A 39 ? 0.4373 0.3961 0.6005 -0.0206 0.0676 -0.0554 39 PRO A O 249 C CB . PRO A 39 ? 0.3906 0.3776 0.5540 -0.0237 0.0286 -0.0414 39 PRO A CB 250 C CG . PRO A 39 ? 0.3889 0.3742 0.5493 -0.0145 0.0035 -0.0342 39 PRO A CG 251 C CD . PRO A 39 ? 0.3835 0.3536 0.5380 -0.0104 0.0082 -0.0326 39 PRO A CD 252 N N . ILE A 40 ? 0.4351 0.3809 0.5257 -0.0348 0.0694 -0.0578 40 ILE A N 253 C CA . ILE A 40 ? 0.4817 0.4028 0.5528 -0.0332 0.0913 -0.0683 40 ILE A CA 254 C C . ILE A 40 ? 0.5003 0.4178 0.5668 -0.0324 0.1150 -0.0684 40 ILE A C 255 O O . ILE A 40 ? 0.5208 0.4282 0.5997 -0.0267 0.1426 -0.0732 40 ILE A O 256 C CB . ILE A 40 ? 0.4942 0.3935 0.5146 -0.0396 0.0817 -0.0764 40 ILE A CB 257 C CG1 . ILE A 40 ? 0.5187 0.4155 0.5518 -0.0442 0.0673 -0.0766 40 ILE A CG1 258 C CG2 . ILE A 40 ? 0.5822 0.4455 0.5623 -0.0357 0.1005 -0.0892 40 ILE A CG2 259 C CD1 . ILE A 40 ? 0.5129 0.4013 0.5778 -0.0354 0.0762 -0.0758 40 ILE A CD1 260 N N . MET A 41 ? 0.4929 0.4156 0.5407 -0.0372 0.1071 -0.0620 41 MET A N 261 C CA . MET A 41 ? 0.5356 0.4447 0.5668 -0.0389 0.1298 -0.0591 41 MET A CA 262 C C . MET A 41 ? 0.4957 0.4212 0.5434 -0.0439 0.1148 -0.0502 41 MET A C 263 O O . MET A 41 ? 0.4634 0.3997 0.5015 -0.0430 0.0876 -0.0475 41 MET A O 264 C CB . MET A 41 ? 0.5793 0.4513 0.5322 -0.0361 0.1343 -0.0631 41 MET A CB 265 C CG . MET A 41 ? 0.6585 0.4985 0.5791 -0.0299 0.1556 -0.0739 41 MET A CG 266 S SD . MET A 41 ? 0.7792 0.5642 0.5931 -0.0226 0.1554 -0.0810 41 MET A SD 267 C CE . MET A 41 ? 0.7225 0.5293 0.5298 -0.0268 0.1034 -0.0855 41 MET A CE 268 N N . VAL A 42 ? 0.4989 0.4243 0.5733 -0.0495 0.1342 -0.0461 42 VAL A N 269 C CA . VAL A 42 ? 0.4953 0.4245 0.5772 -0.0556 0.1200 -0.0396 42 VAL A CA 270 C C . VAL A 42 ? 0.5411 0.4383 0.5943 -0.0619 0.1496 -0.0339 42 VAL A C 271 O O . VAL A 42 ? 0.5661 0.4551 0.6357 -0.0656 0.1858 -0.0337 42 VAL A O 272 C CB . VAL A 42 ? 0.4637 0.4256 0.6215 -0.0594 0.1034 -0.0409 42 VAL A CB 273 C CG1 . VAL A 42 ? 0.4923 0.4507 0.6708 -0.0704 0.0988 -0.0376 42 VAL A CG1 274 C CG2 . VAL A 42 ? 0.4617 0.4374 0.6143 -0.0506 0.0689 -0.0416 42 VAL A CG2 275 N N . LEU A 43 ? 0.5608 0.4353 0.5667 -0.0612 0.1377 -0.0283 43 LEU A N 276 C CA . LEU A 43 ? 0.6307 0.4634 0.5979 -0.0659 0.1658 -0.0202 43 LEU A CA 277 C C . LEU A 43 ? 0.6390 0.4815 0.6761 -0.0840 0.1802 -0.0170 43 LEU A C 278 O O . LEU A 43 ? 0.6122 0.4774 0.6913 -0.0888 0.1507 -0.0200 43 LEU A O 279 C CB . LEU A 43 ? 0.6483 0.4508 0.5432 -0.0557 0.1448 -0.0153 43 LEU A CB 280 C CG . LEU A 43 ? 0.7256 0.4695 0.5574 -0.0556 0.1696 -0.0046 43 LEU A CG 281 C CD1 . LEU A 43 ? 0.7687 0.4785 0.5339 -0.0450 0.1916 -0.0046 43 LEU A CD1 282 C CD2 . LEU A 43 ? 0.7423 0.4618 0.5228 -0.0441 0.1425 0.0004 43 LEU A CD2 283 N N . ASP A 44 ? 0.6969 0.5221 0.7490 -0.0943 0.2251 -0.0118 44 ASP A N 284 C CA . ASP A 44 ? 0.7189 0.5556 0.8482 -0.1160 0.2388 -0.0091 44 ASP A CA 285 C C . ASP A 44 ? 0.7728 0.5591 0.8520 -0.1240 0.2396 0.0007 44 ASP A C 286 O O . ASP A 44 ? 0.8428 0.5752 0.8430 -0.1189 0.2682 0.0112 44 ASP A O 287 C CB . ASP A 44 ? 0.7491 0.5954 0.9356 -0.1266 0.2924 -0.0066 44 ASP A CB 288 C CG . ASP A 44 ? 0.7754 0.6439 1.0628 -0.1530 0.3030 -0.0054 44 ASP A CG 289 O OD1 . ASP A 44 ? 0.7572 0.6766 1.1302 -0.1580 0.2671 -0.0161 44 ASP A OD1 290 O OD2 . ASP A 44 ? 0.8594 0.6908 1.1393 -0.1694 0.3453 0.0060 44 ASP A OD2 291 N N . PRO A 45 ? 0.7558 0.5512 0.8711 -0.1338 0.2060 -0.0031 45 PRO A N 292 C CA . PRO A 45 ? 0.8047 0.5465 0.8679 -0.1386 0.2004 0.0043 45 PRO A CA 293 C C . PRO A 45 ? 0.8788 0.5735 0.9390 -0.1588 0.2504 0.0173 45 PRO A C 294 O O . PRO A 45 ? 0.9360 0.5666 0.9176 -0.1555 0.2579 0.0282 45 PRO A O 295 C CB . PRO A 45 ? 0.7706 0.5366 0.8925 -0.1479 0.1574 -0.0068 45 PRO A CB 296 C CG . PRO A 45 ? 0.7167 0.5411 0.8760 -0.1344 0.1291 -0.0177 45 PRO A CG 297 C CD . PRO A 45 ? 0.6930 0.5418 0.8900 -0.1375 0.1678 -0.0157 45 PRO A CD 298 N N . HIS A 46 ? 0.8772 0.6023 1.0233 -0.1780 0.2865 0.0171 46 HIS A N 299 C CA . HIS A 46 ? 0.9474 0.6357 1.1139 -0.2028 0.3408 0.0301 46 HIS A CA 300 C C . HIS A 46 ? 1.0083 0.6459 1.0871 -0.1904 0.3962 0.0451 46 HIS A C 301 O O . HIS A 46 ? 1.0900 0.6607 1.1179 -0.2004 0.4355 0.0615 46 HIS A O 302 C CB . HIS A 46 ? 0.9241 0.6752 1.2385 -0.2298 0.3561 0.0224 46 HIS A CB 303 C CG . HIS A 46 ? 0.8928 0.6884 1.2884 -0.2401 0.2961 0.0056 46 HIS A CG 304 N ND1 . HIS A 46 ? 0.9493 0.7206 1.3791 -0.2666 0.2811 0.0037 46 HIS A ND1 305 C CD2 . HIS A 46 ? 0.8336 0.6873 1.2731 -0.2263 0.2463 -0.0104 46 HIS A CD2 306 C CE1 . HIS A 46 ? 0.9017 0.7149 1.3903 -0.2672 0.2218 -0.0146 46 HIS A CE1 307 N NE2 . HIS A 46 ? 0.8349 0.6976 1.3279 -0.2419 0.2009 -0.0221 46 HIS A NE2 308 N N . THR A 47 ? 0.9757 0.6371 1.0287 -0.1677 0.3974 0.0391 47 THR A N 309 C CA . THR A 47 ? 1.0356 0.6507 1.0070 -0.1535 0.4485 0.0490 47 THR A CA 310 C C . THR A 47 ? 1.0527 0.6276 0.8941 -0.1215 0.4195 0.0477 47 THR A C 311 O O . THR A 47 ? 1.1275 0.6406 0.8694 -0.1069 0.4526 0.0567 47 THR A O 312 C CB . THR A 47 ? 1.0134 0.6812 1.0577 -0.1514 0.4788 0.0405 47 THR A CB 313 O OG1 . THR A 47 ? 0.9309 0.6522 0.9967 -0.1349 0.4272 0.0234 47 THR A OG1 314 C CG2 . THR A 47 ? 1.0001 0.7177 1.1887 -0.1812 0.5099 0.0408 47 THR A CG2 315 N N . TRP A 48 ? 0.9793 0.5899 0.8249 -0.1104 0.3576 0.0358 48 TRP A N 316 C CA . TRP A 48 ? 0.9790 0.5758 0.7347 -0.0825 0.3199 0.0301 48 TRP A CA 317 C C . TRP A 48 ? 0.9822 0.5871 0.7115 -0.0675 0.3297 0.0210 48 TRP A C 318 O O . TRP A 48 ? 1.0059 0.5851 0.6502 -0.0463 0.3068 0.0167 48 TRP A O 319 C CB . TRP A 48 ? 1.0600 0.5805 0.6990 -0.0674 0.3168 0.0424 48 TRP A CB 320 C CG . TRP A 48 ? 1.0641 0.5637 0.7063 -0.0753 0.2993 0.0498 48 TRP A CG 321 C CD1 . TRP A 48 ? 1.0001 0.5414 0.7317 -0.0938 0.2787 0.0441 48 TRP A CD1 322 C CD2 . TRP A 48 ? 1.1371 0.5607 0.6794 -0.0614 0.2975 0.0632 48 TRP A CD2 323 N NE1 . TRP A 48 ? 1.0464 0.5396 0.7393 -0.0939 0.2666 0.0521 48 TRP A NE1 324 C CE2 . TRP A 48 ? 1.1307 0.5519 0.7095 -0.0736 0.2789 0.0648 48 TRP A CE2 325 C CE3 . TRP A 48 ? 1.2289 0.5796 0.6474 -0.0370 0.3072 0.0733 48 TRP A CE3 326 C CZ2 . TRP A 48 ? 1.2026 0.5513 0.7017 -0.0622 0.2729 0.0770 48 TRP A CZ2 327 C CZ3 . TRP A 48 ? 1.3089 0.5894 0.6480 -0.0244 0.2993 0.0867 48 TRP A CZ3 328 C CH2 . TRP A 48 ? 1.2915 0.5714 0.6729 -0.0370 0.2839 0.0888 48 TRP A CH2 329 N N . ASN A 49 ? 0.9676 0.6072 0.7719 -0.0774 0.3616 0.0165 49 ASN A N 330 C CA . ASN A 49 ? 0.9730 0.6218 0.7606 -0.0626 0.3671 0.0049 49 ASN A CA 331 C C . ASN A 49 ? 0.8767 0.5911 0.7293 -0.0607 0.3173 -0.0096 49 ASN A C 332 O O . ASN A 49 ? 0.8129 0.5709 0.7403 -0.0724 0.2915 -0.0101 49 ASN A O 333 C CB . ASN A 49 ? 1.0169 0.6619 0.8408 -0.0677 0.4318 0.0077 49 ASN A CB 334 C CG . ASN A 49 ? 1.1495 0.7159 0.8890 -0.0676 0.4890 0.0249 49 ASN A CG 335 O OD1 . ASN A 49 ? 1.2268 0.7247 0.8379 -0.0485 0.4862 0.0280 49 ASN A OD1 336 N ND2 . ASN A 49 ? 1.1784 0.7529 0.9913 -0.0887 0.5406 0.0363 49 ASN A ND2 337 N N . LEU A 50 ? 0.8740 0.5868 0.6894 -0.0458 0.3033 -0.0213 50 LEU A N 338 C CA . LEU A 50 ? 0.8026 0.5666 0.6705 -0.0442 0.2634 -0.0330 50 LEU A CA 339 C C . LEU A 50 ? 0.7692 0.5696 0.7216 -0.0469 0.2858 -0.0387 50 LEU A C 340 O O . LEU A 50 ? 0.8131 0.5925 0.7431 -0.0375 0.3164 -0.0446 50 LEU A O 341 C CB . LEU A 50 ? 0.8219 0.5651 0.6166 -0.0302 0.2350 -0.0435 50 LEU A CB 342 C CG . LEU A 50 ? 0.8252 0.5654 0.5797 -0.0268 0.1940 -0.0403 50 LEU A CG 343 C CD1 . LEU A 50 ? 0.9074 0.6085 0.5707 -0.0122 0.1753 -0.0481 50 LEU A CD1 344 C CD2 . LEU A 50 ? 0.7309 0.5259 0.5504 -0.0322 0.1563 -0.0427 50 LEU A CD2 345 N N . ASN A 51 ? 0.6959 0.5467 0.7417 -0.0572 0.2702 -0.0376 51 ASN A N 346 C CA . ASN A 51 ? 0.6603 0.5537 0.7949 -0.0555 0.2776 -0.0441 51 ASN A CA 347 C C . ASN A 51 ? 0.6321 0.5313 0.7497 -0.0429 0.2480 -0.0541 51 ASN A C 348 O O . ASN A 51 ? 0.5930 0.4942 0.6821 -0.0431 0.2089 -0.0543 51 ASN A O 349 C CB . ASN A 51 ? 0.6049 0.5464 0.8360 -0.0677 0.2561 -0.0421 51 ASN A CB 350 C CG . ASN A 51 ? 0.6533 0.6020 0.9434 -0.0836 0.2939 -0.0357 51 ASN A CG 351 O OD1 . ASN A 51 ? 0.6871 0.5940 0.9257 -0.0884 0.3338 -0.0275 51 ASN A OD1 352 N ND2 . ASN A 51 ? 0.6444 0.6448 1.0451 -0.0922 0.2796 -0.0394 51 ASN A ND2 353 N N . ILE A 52 ? 0.6492 0.5474 0.7834 -0.0319 0.2703 -0.0619 52 ILE A N 354 C CA . ILE A 52 ? 0.6381 0.5393 0.7702 -0.0216 0.2454 -0.0710 52 ILE A CA 355 C C . ILE A 52 ? 0.5888 0.5376 0.8154 -0.0182 0.2268 -0.0710 52 ILE A C 356 O O . ILE A 52 ? 0.5919 0.5674 0.8918 -0.0148 0.2508 -0.0714 52 ILE A O 357 C CB . ILE A 52 ? 0.7043 0.5650 0.7877 -0.0081 0.2758 -0.0814 52 ILE A CB 358 C CG1 . ILE A 52 ? 0.7556 0.5662 0.7318 -0.0086 0.2660 -0.0854 52 ILE A CG1 359 C CG2 . ILE A 52 ? 0.6834 0.5501 0.7933 0.0027 0.2601 -0.0903 52 ILE A CG2 360 C CD1 . ILE A 52 ? 0.8506 0.6103 0.7587 -0.0002 0.3107 -0.0875 52 ILE A CD1 361 N N . CYS A 53 ? 0.5548 0.5123 0.7783 -0.0177 0.1850 -0.0704 53 CYS A N 362 C CA . CYS A 53 ? 0.5199 0.5132 0.8123 -0.0134 0.1573 -0.0679 53 CYS A CA 363 C C . CYS A 53 ? 0.5324 0.5260 0.8536 0.0039 0.1552 -0.0732 53 CYS A C 364 O O . CYS A 53 ? 0.5127 0.5343 0.8963 0.0131 0.1355 -0.0720 53 CYS A O 365 C CB . CYS A 53 ? 0.5004 0.4947 0.7642 -0.0190 0.1172 -0.0618 53 CYS A CB 366 S SG . CYS A 53 ? 0.5302 0.5204 0.7567 -0.0340 0.1112 -0.0555 53 CYS A SG 367 N N . ARG A 54 ? 0.5655 0.5226 0.8367 0.0100 0.1709 -0.0800 54 ARG A N 368 C CA . ARG A 54 ? 0.5859 0.5299 0.8712 0.0272 0.1678 -0.0851 54 ARG A CA 369 C C . ARG A 54 ? 0.6294 0.5485 0.9043 0.0397 0.2091 -0.0959 54 ARG A C 370 O O . ARG A 54 ? 0.6524 0.5421 0.8673 0.0330 0.2312 -0.1006 54 ARG A O 371 C CB . ARG A 54 ? 0.5881 0.5007 0.8180 0.0222 0.1406 -0.0838 54 ARG A CB 372 C CG . ARG A 54 ? 0.5659 0.4974 0.7988 0.0138 0.1058 -0.0722 54 ARG A CG 373 C CD . ARG A 54 ? 0.6031 0.5517 0.8879 0.0299 0.0855 -0.0667 54 ARG A CD 374 N NE . ARG A 54 ? 0.6259 0.5816 0.8980 0.0252 0.0539 -0.0560 54 ARG A NE 375 C CZ . ARG A 54 ? 0.6401 0.6224 0.9513 0.0316 0.0315 -0.0521 54 ARG A CZ 376 N NH1 . ARG A 54 ? 0.6604 0.6735 1.0413 0.0405 0.0357 -0.0581 54 ARG A NH1 377 N NH2 . ARG A 54 ? 0.6245 0.6020 0.9068 0.0298 0.0049 -0.0434 54 ARG A NH2 378 N N . PRO A 55 ? 0.6483 0.5747 0.9763 0.0617 0.2190 -0.1003 55 PRO A N 379 C CA . PRO A 55 ? 0.7031 0.6042 1.0231 0.0789 0.2632 -0.1115 55 PRO A CA 380 C C . PRO A 55 ? 0.7621 0.5940 0.9848 0.0796 0.2669 -0.1227 55 PRO A C 381 O O . PRO A 55 ? 0.8240 0.6211 1.0068 0.0895 0.3053 -0.1332 55 PRO A O 382 C CB . PRO A 55 ? 0.7000 0.6283 1.1049 0.1052 0.2616 -0.1128 55 PRO A CB 383 C CG . PRO A 55 ? 0.6409 0.6194 1.1089 0.0990 0.2198 -0.1020 55 PRO A CG 384 C CD . PRO A 55 ? 0.6242 0.5797 1.0187 0.0758 0.1887 -0.0953 55 PRO A CD 385 N N . TRP A 56 ? 0.7545 0.5646 0.9394 0.0687 0.2287 -0.1210 56 TRP A N 386 C CA . TRP A 56 ? 0.8046 0.5522 0.9050 0.0621 0.2229 -0.1330 56 TRP A CA 387 C C . TRP A 56 ? 0.8317 0.5660 0.8653 0.0412 0.2168 -0.1357 56 TRP A C 388 O O . TRP A 56 ? 0.8891 0.5738 0.8547 0.0354 0.2092 -0.1488 56 TRP A O 389 C CB . TRP A 56 ? 0.7793 0.5080 0.8777 0.0575 0.1885 -0.1293 56 TRP A CB 390 C CG . TRP A 56 ? 0.6852 0.4515 0.8045 0.0399 0.1553 -0.1128 56 TRP A CG 391 C CD1 . TRP A 56 ? 0.6164 0.4180 0.7902 0.0480 0.1388 -0.0990 56 TRP A CD1 392 C CD2 . TRP A 56 ? 0.6532 0.4223 0.7358 0.0152 0.1353 -0.1097 56 TRP A CD2 393 N NE1 . TRP A 56 ? 0.5847 0.4052 0.7496 0.0302 0.1136 -0.0873 56 TRP A NE1 394 C CE2 . TRP A 56 ? 0.5779 0.3833 0.6931 0.0102 0.1132 -0.0932 56 TRP A CE2 395 C CE3 . TRP A 56 ? 0.6702 0.4147 0.6958 -0.0005 0.1319 -0.1204 56 TRP A CE3 396 C CZ2 . TRP A 56 ? 0.5746 0.3939 0.6707 -0.0091 0.0945 -0.0862 56 TRP A CZ2 397 C CZ3 . TRP A 56 ? 0.6413 0.4064 0.6575 -0.0201 0.1087 -0.1138 56 TRP A CZ3 398 C CH2 . TRP A 56 ? 0.5974 0.4004 0.6503 -0.0240 0.0933 -0.0964 56 TRP A CH2 399 N N . VAL A 57 ? 0.8147 0.5897 0.8673 0.0310 0.2164 -0.1245 57 VAL A N 400 C CA . VAL A 57 ? 0.8451 0.6097 0.8375 0.0152 0.2064 -0.1246 57 VAL A CA 401 C C . VAL A 57 ? 0.9337 0.6601 0.8611 0.0222 0.2406 -0.1325 57 VAL A C 402 O O . VAL A 57 ? 0.9709 0.6654 0.8240 0.0154 0.2267 -0.1387 57 VAL A O 403 C CB . VAL A 57 ? 0.7812 0.5964 0.8120 0.0023 0.1874 -0.1083 57 VAL A CB 404 C CG1 . VAL A 57 ? 0.7947 0.5992 0.7687 -0.0069 0.1860 -0.1068 57 VAL A CG1 405 C CG2 . VAL A 57 ? 0.7406 0.5750 0.7942 -0.0065 0.1500 -0.1014 57 VAL A CG2 406 N N . GLN A 58 ? 0.9768 0.7047 0.9308 0.0374 0.2852 -0.1322 58 GLN A N 407 C CA . GLN A 58 ? 1.0555 0.7563 0.9606 0.0431 0.3279 -0.1317 58 GLN A CA 408 C C . GLN A 58 ? 1.1683 0.7904 0.9577 0.0541 0.3405 -0.1482 58 GLN A C 409 O O . GLN A 58 ? 1.2032 0.7933 0.9129 0.0486 0.3297 -0.1487 58 GLN A O 410 C CB . GLN A 58 ? 1.0551 0.7877 1.0386 0.0549 0.3777 -0.1255 58 GLN A CB 411 C CG . GLN A 58 ? 1.0865 0.8204 1.0630 0.0495 0.4195 -0.1138 58 GLN A CG 412 C CD . GLN A 58 ? 1.2091 0.8694 1.0790 0.0641 0.4647 -0.1210 58 GLN A CD 413 O OE1 . GLN A 58 ? 1.2586 0.8932 1.1210 0.0849 0.5040 -0.1310 58 GLN A OE1 414 N NE2 . GLN A 58 ? 1.2605 0.8810 1.0405 0.0565 0.4593 -0.1159 58 GLN A NE2 415 N N . GLU A 59 ? 1.2358 0.8230 1.0127 0.0726 0.3619 -0.1626 59 GLU A N 416 C CA . GLU A 59 ? 1.3641 0.8670 1.0261 0.0880 0.3796 -0.1813 59 GLU A CA 417 C C . GLU A 59 ? 1.3988 0.8598 0.9947 0.0778 0.3245 -0.1987 59 GLU A C 418 O O . GLU A 59 ? 1.4840 0.8780 1.0112 0.0902 0.3258 -0.2199 59 GLU A O 419 C CB . GLU A 59 ? 1.4202 0.8987 1.0956 0.1151 0.4283 -0.1912 59 GLU A CB 420 N N . ILE A 60 ? 1.3417 0.8423 0.9629 0.0549 0.2769 -0.1905 60 ILE A N 421 C CA . ILE A 60 ? 1.3653 0.8419 0.9481 0.0403 0.2239 -0.2052 60 ILE A CA 422 C C . ILE A 60 ? 1.3884 0.8548 0.9059 0.0326 0.1967 -0.2054 60 ILE A C 423 O O . ILE A 60 ? 1.4796 0.8838 0.9040 0.0376 0.1785 -0.2250 60 ILE A O 424 C CB . ILE A 60 ? 1.2843 0.8117 0.9564 0.0225 0.1915 -0.1975 60 ILE A CB 425 C CG1 . ILE A 60 ? 1.2867 0.8091 1.0072 0.0365 0.2154 -0.1988 60 ILE A CG1 426 C CG2 . ILE A 60 ? 1.3060 0.8120 0.9500 0.0031 0.1418 -0.2121 60 ILE A CG2 427 C CD1 . ILE A 60 ? 1.2340 0.8052 1.0277 0.0508 0.2539 -0.1820 60 ILE A CD1 428 N N . THR A 61 ? 1.3174 0.8387 0.8777 0.0234 0.1919 -0.1850 61 THR A N 429 C CA . THR A 61 ? 1.3518 0.8567 0.8440 0.0239 0.1751 -0.1826 61 THR A CA 430 C C . THR A 61 ? 1.3249 0.8558 0.8360 0.0268 0.2084 -0.1595 61 THR A C 431 O O . THR A 61 ? 1.2367 0.8299 0.8270 0.0141 0.1971 -0.1438 61 THR A O 432 C CB . THR A 61 ? 1.3141 0.8485 0.8217 0.0066 0.1148 -0.1867 61 THR A CB 433 O OG1 . THR A 61 ? 1.3722 0.8639 0.8378 0.0032 0.0834 -0.2119 61 THR A OG1 434 C CG2 . THR A 61 ? 1.3304 0.8615 0.7866 0.0111 0.0975 -0.1795 61 THR A CG2 435 N N . ALA A 62 ? 1.4033 0.8832 0.8420 0.0427 0.2511 -0.1567 62 ALA A N 436 C CA . ALA A 62 ? 1.5272 0.9231 0.8605 0.0634 0.2778 -0.1736 62 ALA A CA 437 C C . ALA A 62 ? 1.6164 0.9458 0.8346 0.0706 0.2328 -0.1957 62 ALA A C 438 O O . ALA A 62 ? 1.6826 0.9703 0.8108 0.0802 0.2246 -0.1928 62 ALA A O 439 C CB . ALA A 62 ? 1.5344 0.9278 0.9115 0.0722 0.3143 -0.1826 62 ALA A CB 440 N N . GLU A 63 ? 1.6217 0.9384 0.8444 0.0662 0.2021 -0.2181 63 GLU A N 441 C CA . GLU A 63 ? 1.7220 0.9674 0.8404 0.0729 0.1606 -0.2461 63 GLU A CA 442 C C . GLU A 63 ? 1.7118 0.9715 0.8093 0.0630 0.0948 -0.2501 63 GLU A C 443 O O . GLU A 63 ? 1.8181 1.0106 0.8024 0.0770 0.0665 -0.2670 63 GLU A O 444 C CB . GLU A 63 ? 1.7211 0.9569 0.8733 0.0646 0.1443 -0.2675 63 GLU A CB 445 C CG . GLU A 63 ? 1.8639 1.0040 0.8984 0.0768 0.1215 -0.3004 63 GLU A CG 446 C CD . GLU A 63 ? 1.9071 1.0132 0.9549 0.0810 0.1423 -0.3169 63 GLU A CD 447 O OE1 . GLU A 63 ? 1.8172 0.9842 0.9790 0.0675 0.1517 -0.3049 63 GLU A OE1 448 O OE2 . GLU A 63 ? 2.0375 1.0499 0.9748 0.1007 0.1488 -0.3419 63 GLU A OE2 449 N N . THR A 64 ? 1.5867 0.9320 0.7914 0.0418 0.0691 -0.2359 64 THR A N 450 C CA . THR A 64 ? 1.5665 0.9399 0.7727 0.0340 0.0105 -0.2378 64 THR A CA 451 C C . THR A 64 ? 1.5524 0.9364 0.7343 0.0456 0.0239 -0.2144 64 THR A C 452 O O . THR A 64 ? 1.5531 0.9537 0.7240 0.0470 -0.0206 -0.2139 64 THR A O 453 C CB . THR A 64 ? 1.4591 0.9138 0.7886 0.0065 -0.0222 -0.2358 64 THR A CB 454 N N . GLU A 65 ? 1.5446 0.9173 0.7216 0.0541 0.0856 -0.1955 65 GLU A N 455 C CA . GLU A 65 ? 1.5303 0.9065 0.6906 0.0615 0.1094 -0.1707 65 GLU A CA 456 C C . GLU A 65 ? 1.4240 0.8731 0.6618 0.0489 0.0733 -0.1575 65 GLU A C 457 O O . GLU A 65 ? 1.4539 0.8892 0.6444 0.0596 0.0577 -0.1479 65 GLU A O 458 C CB . GLU A 65 ? 1.6741 0.9573 0.6836 0.0874 0.1125 -0.1738 65 GLU A CB 459 N N . VAL A 66 ? 1.3062 0.8269 0.6567 0.0289 0.0616 -0.1566 66 VAL A N 460 C CA . VAL A 66 ? 1.1977 0.7882 0.6278 0.0180 0.0398 -0.1423 66 VAL A CA 461 C C . VAL A 66 ? 1.1735 0.7671 0.6100 0.0218 0.0782 -0.1184 66 VAL A C 462 O O . VAL A 66 ? 1.1374 0.7511 0.5810 0.0240 0.0619 -0.1065 66 VAL A O 463 C CB . VAL A 66 ? 1.1039 0.7568 0.6409 -0.0019 0.0316 -0.1435 66 VAL A CB 464 C CG1 . VAL A 66 ? 1.0117 0.7292 0.6237 -0.0097 0.0226 -0.1256 66 VAL A CG1 465 C CG2 . VAL A 66 ? 1.1171 0.7695 0.6563 -0.0106 -0.0105 -0.1652 66 VAL A CG2 466 N N . LYS A 67 ? 1.1864 0.7569 0.6212 0.0228 0.1301 -0.1128 67 LYS A N 467 C CA . LYS A 67 ? 1.1723 0.7429 0.6230 0.0215 0.1724 -0.0921 67 LYS A CA 468 C C . LYS A 67 ? 1.2522 0.7587 0.5972 0.0370 0.1800 -0.0833 67 LYS A C 469 O O . LYS A 67 ? 1.2432 0.7513 0.5974 0.0342 0.1955 -0.0651 67 LYS A O 470 C CB . LYS A 67 ? 1.1793 0.7461 0.6649 0.0193 0.2261 -0.0912 67 LYS A CB 471 C CG . LYS A 67 ? 1.1555 0.7484 0.7063 0.0096 0.2664 -0.0722 67 LYS A CG 472 C CD . LYS A 67 ? 1.1507 0.7590 0.7633 0.0082 0.3115 -0.0746 67 LYS A CD 473 C CE . LYS A 67 ? 1.1572 0.7908 0.8399 -0.0032 0.3526 -0.0575 67 LYS A CE 474 N NZ . LYS A 67 ? 1.1281 0.8059 0.9113 -0.0059 0.3809 -0.0607 67 LYS A NZ 475 N N . LYS A 68 ? 1.3398 0.7829 0.5783 0.0543 0.1662 -0.0967 68 LYS A N 476 C CA . LYS A 68 ? 1.4331 0.8049 0.5528 0.0744 0.1640 -0.0890 68 LYS A CA 477 C C . LYS A 68 ? 1.4015 0.7983 0.5206 0.0802 0.1033 -0.0884 68 LYS A C 478 O O . LYS A 68 ? 1.4385 0.8053 0.5103 0.0911 0.1061 -0.0719 68 LYS A O 479 C CB . LYS A 68 ? 1.5667 0.8526 0.5597 0.0952 0.1682 -0.1049 68 LYS A CB 480 N N . ILE A 69 ? 1.3307 0.7814 0.5062 0.0731 0.0519 -0.1058 69 ILE A N 481 C CA . ILE A 69 ? 1.2868 0.7801 0.4897 0.0774 -0.0046 -0.1076 69 ILE A CA 482 C C . ILE A 69 ? 1.2074 0.7455 0.4773 0.0708 0.0075 -0.0863 69 ILE A C 483 O O . ILE A 69 ? 1.2278 0.7588 0.4689 0.0861 -0.0154 -0.0778 69 ILE A O 484 C CB . ILE A 69 ? 1.2219 0.7781 0.5052 0.0622 -0.0470 -0.1278 69 ILE A CB 485 C CG1 . ILE A 69 ? 1.3204 0.8306 0.5298 0.0717 -0.0838 -0.1534 69 ILE A CG1 486 C CG2 . ILE A 69 ? 1.1395 0.7692 0.5025 0.0590 -0.0848 -0.1232 69 ILE A CG2 487 C CD1 . ILE A 69 ? 1.2690 0.8253 0.5554 0.0505 -0.1121 -0.1741 69 ILE A CD1 488 N N . LEU A 70 ? 1.1184 0.6989 0.4751 0.0503 0.0405 -0.0792 70 LEU A N 489 C CA . LEU A 70 ? 1.0386 0.6637 0.4661 0.0414 0.0468 -0.0637 70 LEU A CA 490 C C . LEU A 70 ? 1.0863 0.6630 0.4680 0.0466 0.0811 -0.0443 70 LEU A C 491 O O . LEU A 70 ? 1.0504 0.6432 0.4575 0.0468 0.0742 -0.0328 70 LEU A O 492 C CB . LEU A 70 ? 0.9449 0.6249 0.4730 0.0200 0.0643 -0.0646 70 LEU A CB 493 C CG . LEU A 70 ? 0.9001 0.6290 0.4846 0.0112 0.0337 -0.0794 70 LEU A CG 494 C CD1 . LEU A 70 ? 0.8084 0.5767 0.4768 -0.0054 0.0534 -0.0777 70 LEU A CD1 495 C CD2 . LEU A 70 ? 0.8520 0.6223 0.4621 0.0158 -0.0085 -0.0803 70 LEU A CD2 496 N N . SER A 71 ? 1.1703 0.6823 0.4806 0.0513 0.1198 -0.0407 71 SER A N 497 C CA . SER A 71 ? 1.2276 0.6891 0.5016 0.0503 0.1653 -0.0205 71 SER A CA 498 C C . SER A 71 ? 1.3556 0.7296 0.4969 0.0750 0.1639 -0.0118 71 SER A C 499 O O . SER A 71 ? 1.3832 0.7301 0.4993 0.0803 0.1653 0.0042 71 SER A O 500 C CB . SER A 71 ? 1.2340 0.6860 0.5337 0.0364 0.2240 -0.0182 71 SER A CB 501 O OG . SER A 71 ? 1.1459 0.6660 0.5421 0.0227 0.2155 -0.0315 71 SER A OG 502 N N . PHE A 72 ? 1.4512 0.7730 0.4997 0.0922 0.1594 -0.0227 72 PHE A N 503 C CA . PHE A 72 ? 1.6011 0.8218 0.5053 0.1179 0.1687 -0.0123 72 PHE A CA 504 C C . PHE A 72 ? 1.6550 0.8567 0.4853 0.1465 0.0995 -0.0239 72 PHE A C 505 O O . PHE A 72 ? 1.7819 0.8995 0.4896 0.1728 0.0957 -0.0138 72 PHE A O 506 C CB . PHE A 72 ? 1.7040 0.8534 0.5246 0.1234 0.2210 -0.0134 72 PHE A CB 507 C CG . PHE A 72 ? 1.6531 0.8412 0.5686 0.0972 0.2815 -0.0104 72 PHE A CG 508 C CD1 . PHE A 72 ? 1.6103 0.8140 0.5937 0.0764 0.3286 0.0106 72 PHE A CD1 509 C CD2 . PHE A 72 ? 1.6581 0.8643 0.5955 0.0947 0.2893 -0.0299 72 PHE A CD2 510 C CE1 . PHE A 72 ? 1.5591 0.8063 0.6419 0.0539 0.3790 0.0115 72 PHE A CE1 511 C CE2 . PHE A 72 ? 1.5975 0.8418 0.6264 0.0756 0.3428 -0.0278 72 PHE A CE2 512 C CZ . PHE A 72 ? 1.5527 0.8218 0.6585 0.0556 0.3865 -0.0072 72 PHE A CZ 513 N N . SER A 73 ? 1.5708 0.8491 0.4769 0.1421 0.0450 -0.0445 73 SER A N 514 C CA . SER A 73 ? 1.6115 0.8823 0.4643 0.1669 -0.0242 -0.0610 73 SER A CA 515 C C . SER A 73 ? 1.5949 0.8869 0.4602 0.1840 -0.0632 -0.0513 73 SER A C 516 O O . SER A 73 ? 1.5386 0.8479 0.4509 0.1754 -0.0375 -0.0325 73 SER A O 517 C CB . SER A 73 ? 1.5441 0.8837 0.4746 0.1528 -0.0637 -0.0883 73 SER A CB 518 O OG . SER A 73 ? 1.4003 0.8396 0.4669 0.1338 -0.0798 -0.0879 73 SER A OG 519 N N . MET A 74 ? 1.6421 0.9304 0.4650 0.2096 -0.1278 -0.0661 74 MET A N 520 C CA . MET A 74 ? 1.6414 0.9557 0.4785 0.2329 -0.1751 -0.0618 74 MET A CA 521 C C . MET A 74 ? 1.5012 0.9119 0.4779 0.2146 -0.1715 -0.0558 74 MET A C 522 O O . MET A 74 ? 1.5064 0.9161 0.4837 0.2314 -0.1782 -0.0417 74 MET A O 523 C CB . MET A 74 ? 1.6832 1.0170 0.5071 0.2529 -0.2506 -0.0876 74 MET A CB 524 C CG . MET A 74 ? 1.6903 1.0598 0.5377 0.2819 -0.3064 -0.0872 74 MET A CG 525 S SD . MET A 74 ? 1.7633 1.1481 0.5912 0.3036 -0.3974 -0.1210 74 MET A SD 526 C CE . MET A 74 ? 1.9577 1.1865 0.5637 0.3477 -0.4087 -0.1152 74 MET A CE 527 N N . VAL A 75 ? 1.3880 0.8747 0.4738 0.1831 -0.1621 -0.0668 75 VAL A N 528 C CA . VAL A 75 ? 1.2574 0.8298 0.4663 0.1662 -0.1568 -0.0620 75 VAL A CA 529 C C . VAL A 75 ? 1.1911 0.7652 0.4414 0.1371 -0.0975 -0.0497 75 VAL A C 530 O O . VAL A 75 ? 1.1037 0.7415 0.4494 0.1201 -0.0896 -0.0476 75 VAL A O 531 C CB . VAL A 75 ? 1.1831 0.8458 0.4933 0.1544 -0.1959 -0.0823 75 VAL A CB 532 C CG1 . VAL A 75 ? 1.2364 0.9054 0.5204 0.1819 -0.2596 -0.0972 75 VAL A CG1 533 C CG2 . VAL A 75 ? 1.1617 0.8315 0.4963 0.1266 -0.1796 -0.0958 75 VAL A CG2 534 N N . GLY A 76 ? 1.2495 0.7512 0.4256 0.1338 -0.0561 -0.0415 76 GLY A N 535 C CA . GLY A 76 ? 1.2001 0.7024 0.4181 0.1074 -0.0002 -0.0315 76 GLY A CA 536 C C . GLY A 76 ? 1.1765 0.6744 0.4176 0.1035 0.0209 -0.0125 76 GLY A C 537 O O . GLY A 76 ? 1.2077 0.6860 0.4127 0.1247 -0.0020 -0.0052 76 GLY A O 538 N N . ILE A 77 ? 1.1244 0.6388 0.4269 0.0776 0.0617 -0.0060 77 ILE A N 539 C CA . ILE A 77 ? 1.0909 0.6103 0.4343 0.0680 0.0759 0.0073 77 ILE A CA 540 C C . ILE A 77 ? 1.1952 0.6285 0.4493 0.0801 0.0960 0.0253 77 ILE A C 541 O O . ILE A 77 ? 1.2048 0.6257 0.4509 0.0907 0.0808 0.0331 77 ILE A O 542 C CB . ILE A 77 ? 1.0208 0.5827 0.4594 0.0371 0.1071 0.0067 77 ILE A CB 543 C CG1 . ILE A 77 ? 0.9613 0.5449 0.4563 0.0277 0.1024 0.0127 77 ILE A CG1 544 C CG2 . ILE A 77 ? 1.0657 0.5847 0.4835 0.0237 0.1601 0.0132 77 ILE A CG2 545 C CD1 . ILE A 77 ? 0.9096 0.5269 0.4147 0.0459 0.0588 0.0081 77 ILE A CD1 546 N N . ARG A 78 ? 1.2847 0.6512 0.4617 0.0820 0.1303 0.0321 78 ARG A N 547 C CA . ARG A 78 ? 1.4046 0.6756 0.4826 0.0935 0.1564 0.0521 78 ARG A CA 548 C C . ARG A 78 ? 1.4662 0.6988 0.4615 0.1304 0.1100 0.0551 78 ARG A C 549 O O . ARG A 78 ? 1.5242 0.7043 0.4805 0.1385 0.1164 0.0713 78 ARG A O 550 C CB . ARG A 78 ? 1.5029 0.7072 0.5049 0.0920 0.2057 0.0584 78 ARG A CB 551 C CG . ARG A 78 ? 1.4924 0.7176 0.5767 0.0566 0.2654 0.0641 78 ARG A CG 552 C CD . ARG A 78 ? 1.6142 0.8190 0.6688 0.0548 0.3067 0.0597 78 ARG A CD 553 N NE . ARG A 78 ? 1.6172 0.8552 0.7699 0.0231 0.3619 0.0641 78 ARG A NE 554 C CZ . ARG A 78 ? 1.5255 0.8521 0.8002 0.0048 0.3543 0.0498 78 ARG A CZ 555 N NH1 . ARG A 78 ? 1.4442 0.8321 0.7563 0.0119 0.2994 0.0314 78 ARG A NH1 556 N NH2 . ARG A 78 ? 1.5166 0.8698 0.8790 -0.0205 0.4029 0.0543 78 ARG A NH2 557 N N . ASN A 79 ? 1.4595 0.7184 0.4334 0.1529 0.0615 0.0389 79 ASN A N 558 C CA . ASN A 79 ? 1.4955 0.7402 0.4175 0.1898 0.0086 0.0380 79 ASN A CA 559 C C . ASN A 79 ? 1.3973 0.7150 0.4135 0.1903 -0.0195 0.0344 79 ASN A C 560 O O . ASN A 79 ? 1.4384 0.7240 0.4185 0.2144 -0.0359 0.0441 79 ASN A O 561 C CB . ASN A 79 ? 1.5299 0.7844 0.4103 0.2124 -0.0392 0.0192 79 ASN A CB 562 C CG . ASN A 79 ? 1.6829 0.8266 0.4101 0.2364 -0.0306 0.0263 79 ASN A CG 563 O OD1 . ASN A 79 ? 1.7756 0.8311 0.4077 0.2550 -0.0141 0.0470 79 ASN A OD1 564 N ND2 . ASN A 79 ? 1.7089 0.8491 0.4040 0.2375 -0.0423 0.0089 79 ASN A ND2 565 N N . THR A 80 ? 1.2776 0.6867 0.4070 0.1664 -0.0231 0.0211 80 THR A N 566 C CA . THR A 80 ? 1.1912 0.6682 0.4082 0.1659 -0.0425 0.0177 80 THR A CA 567 C C . THR A 80 ? 1.2012 0.6384 0.4142 0.1616 -0.0185 0.0331 80 THR A C 568 O O . THR A 80 ? 1.1964 0.6378 0.4111 0.1835 -0.0412 0.0350 80 THR A O 569 C CB . THR A 80 ? 1.0768 0.6431 0.4040 0.1382 -0.0406 0.0044 80 THR A CB 570 O OG1 . THR A 80 ? 1.0800 0.6748 0.4103 0.1387 -0.0616 -0.0106 80 THR A OG1 571 C CG2 . THR A 80 ? 1.0146 0.6444 0.4139 0.1449 -0.0624 0.0007 80 THR A CG2 572 N N . ILE A 81 ? 1.2168 0.6170 0.4302 0.1332 0.0271 0.0426 81 ILE A N 573 C CA . ILE A 81 ? 1.2516 0.6036 0.4593 0.1236 0.0505 0.0560 81 ILE A CA 574 C C . ILE A 81 ? 1.3636 0.6305 0.4679 0.1564 0.0404 0.0698 81 ILE A C 575 O O . ILE A 81 ? 1.3759 0.6300 0.4816 0.1694 0.0266 0.0729 81 ILE A O 576 C CB . ILE A 81 ? 1.2694 0.5897 0.4913 0.0876 0.1033 0.0647 81 ILE A CB 577 C CG1 . ILE A 81 ? 1.1567 0.5596 0.4902 0.0579 0.1094 0.0517 81 ILE A CG1 578 C CG2 . ILE A 81 ? 1.3414 0.5886 0.5376 0.0775 0.1286 0.0806 81 ILE A CG2 579 C CD1 . ILE A 81 ? 1.1870 0.5805 0.5356 0.0328 0.1542 0.0548 81 ILE A CD1 580 N N . ARG A 82 ? 1.4556 0.6583 0.4626 0.1733 0.0462 0.0778 82 ARG A N 581 C CA . ARG A 82 ? 1.5762 0.6893 0.4720 0.2095 0.0336 0.0922 82 ARG A CA 582 C C . ARG A 82 ? 1.5578 0.7113 0.4570 0.2510 -0.0261 0.0819 82 ARG A C 583 O O . ARG A 82 ? 1.6158 0.7212 0.4699 0.2784 -0.0396 0.0913 82 ARG A O 584 C CB . ARG A 82 ? 1.6949 0.7209 0.4721 0.2207 0.0539 0.1037 82 ARG A CB 585 C CG . ARG A 82 ? 1.8612 0.7697 0.5090 0.2543 0.0532 0.1248 82 ARG A CG 586 C CD . ARG A 82 ? 2.0071 0.8066 0.5312 0.2550 0.0972 0.1432 82 ARG A CD 587 N NE . ARG A 82 ? 2.0179 0.8499 0.5336 0.2536 0.0930 0.1285 82 ARG A NE 588 C CZ . ARG A 82 ? 2.0766 0.9073 0.5281 0.2907 0.0408 0.1161 82 ARG A CZ 589 N NH1 . ARG A 82 ? 2.1276 0.9326 0.5238 0.3346 -0.0119 0.1178 82 ARG A NH1 590 N NH2 . ARG A 82 ? 2.0710 0.9250 0.5158 0.2852 0.0390 0.1006 82 ARG A NH2 591 N N . PHE A 83 ? 1.4836 0.7261 0.4427 0.2552 -0.0601 0.0626 83 PHE A N 592 C CA . PHE A 83 ? 1.4540 0.7550 0.4467 0.2895 -0.1126 0.0513 83 PHE A CA 593 C C . PHE A 83 ? 1.3952 0.7343 0.4590 0.2886 -0.1109 0.0511 83 PHE A C 594 O O . PHE A 83 ? 1.4190 0.7588 0.4727 0.3260 -0.1402 0.0513 83 PHE A O 595 C CB . PHE A 83 ? 1.3806 0.7759 0.4441 0.2837 -0.1425 0.0302 83 PHE A CB 596 C CG . PHE A 83 ? 1.3564 0.8199 0.4678 0.3169 -0.1942 0.0182 83 PHE A CG 597 C CD1 . PHE A 83 ? 1.4504 0.8785 0.4901 0.3615 -0.2377 0.0181 83 PHE A CD1 598 C CD2 . PHE A 83 ? 1.2480 0.8104 0.4769 0.3054 -0.1985 0.0077 83 PHE A CD2 599 C CE1 . PHE A 83 ? 1.4335 0.9345 0.5335 0.3931 -0.2859 0.0061 83 PHE A CE1 600 C CE2 . PHE A 83 ? 1.2208 0.8519 0.5053 0.3354 -0.2392 -0.0023 83 PHE A CE2 601 C CZ . PHE A 83 ? 1.3128 0.9189 0.5410 0.3786 -0.2834 -0.0039 83 PHE A CZ 602 N N . MET A 84 ? 1.3183 0.6868 0.4508 0.2495 -0.0787 0.0494 84 MET A N 603 C CA . MET A 84 ? 1.2772 0.6721 0.4655 0.2486 -0.0776 0.0473 84 MET A CA 604 C C . MET A 84 ? 1.3633 0.6613 0.4830 0.2590 -0.0630 0.0621 84 MET A C 605 O O . MET A 84 ? 1.3830 0.6769 0.5009 0.2873 -0.0805 0.0610 84 MET A O 606 C CB . MET A 84 ? 1.1758 0.6303 0.4537 0.2077 -0.0565 0.0390 84 MET A CB 607 C CG . MET A 84 ? 1.1072 0.6589 0.4607 0.1990 -0.0717 0.0243 84 MET A CG 608 S SD . MET A 84 ? 1.0850 0.7122 0.4792 0.2373 -0.1145 0.0137 84 MET A SD 609 C CE . MET A 84 ? 1.0030 0.7184 0.4770 0.2102 -0.1194 -0.0005 84 MET A CE 610 N N . HIS A 85 ? 1.4320 0.6489 0.4951 0.2370 -0.0289 0.0760 85 HIS A N 611 C CA . HIS A 85 ? 1.5362 0.6444 0.5208 0.2459 -0.0130 0.0928 85 HIS A CA 612 C C . HIS A 85 ? 1.6361 0.6938 0.5341 0.3009 -0.0453 0.0998 85 HIS A C 613 O O . HIS A 85 ? 1.6942 0.6919 0.5535 0.3217 -0.0491 0.1068 85 HIS A O 614 C CB . HIS A 85 ? 1.6013 0.6301 0.5369 0.2137 0.0342 0.1091 85 HIS A CB 615 C CG . HIS A 85 ? 1.5376 0.5830 0.5514 0.1628 0.0685 0.1065 85 HIS A CG 616 N ND1 . HIS A 85 ? 1.5557 0.5536 0.5786 0.1481 0.0787 0.1097 85 HIS A ND1 617 C CD2 . HIS A 85 ? 1.4517 0.5549 0.5401 0.1246 0.0912 0.0995 85 HIS A CD2 618 C CE1 . HIS A 85 ? 1.4862 0.5164 0.5907 0.1020 0.1028 0.1039 85 HIS A CE1 619 N NE2 . HIS A 85 ? 1.4418 0.5376 0.5885 0.0885 0.1117 0.0985 85 HIS A NE2 620 N N . GLU A 86 ? 1.6633 0.7424 0.5304 0.3256 -0.0716 0.0967 86 GLU A N 621 C CA . GLU A 86 ? 1.7654 0.8028 0.5523 0.3816 -0.1106 0.1017 86 GLU A CA 622 C C . GLU A 86 ? 1.7201 0.8269 0.5667 0.4186 -0.1505 0.0890 86 GLU A C 623 O O . GLU A 86 ? 1.8006 0.8534 0.5880 0.4637 -0.1715 0.0964 86 GLU A O 624 C CB . GLU A 86 ? 1.8032 0.8510 0.5474 0.3965 -0.1353 0.0971 86 GLU A CB 625 C CG . GLU A 86 ? 1.8825 0.8675 0.5626 0.3663 -0.0951 0.1074 86 GLU A CG 626 C CD . GLU A 86 ? 2.0238 0.8802 0.6101 0.3571 -0.0480 0.1332 86 GLU A CD 627 O OE1 . GLU A 86 ? 2.1693 0.9274 0.6382 0.3969 -0.0607 0.1489 86 GLU A OE1 628 O OE2 . GLU A 86 ? 1.9862 0.8393 0.6188 0.3097 0.0011 0.1379 86 GLU A OE2 629 N N . MET A 87 ? 1.5978 0.8217 0.5592 0.4021 -0.1588 0.0709 87 MET A N 630 C CA . MET A 87 ? 1.5574 0.8587 0.5877 0.4349 -0.1886 0.0589 87 MET A CA 631 C C . MET A 87 ? 1.5655 0.8319 0.5987 0.4396 -0.1701 0.0622 87 MET A C 632 O O . MET A 87 ? 1.5889 0.8624 0.6245 0.4837 -0.1906 0.0597 87 MET A O 633 C CB . MET A 87 ? 1.4355 0.8644 0.5830 0.4126 -0.1959 0.0409 87 MET A CB 634 C CG . MET A 87 ? 1.4435 0.9147 0.5977 0.4120 -0.2235 0.0323 87 MET A CG 635 S SD . MET A 87 ? 1.5559 1.0392 0.6820 0.4749 -0.2857 0.0272 87 MET A SD 636 C CE . MET A 87 ? 1.6959 1.0296 0.6533 0.4939 -0.2864 0.0461 87 MET A CE 637 N N . THR A 88 ? 1.5495 0.7790 0.5854 0.3947 -0.1328 0.0661 88 THR A N 638 C CA . THR A 88 ? 1.5774 0.7501 0.5990 0.3927 -0.1161 0.0684 88 THR A CA 639 C C . THR A 88 ? 1.7105 0.7671 0.6244 0.4297 -0.1217 0.0838 88 THR A C 640 O O . THR A 88 ? 1.7550 0.7845 0.6519 0.4650 -0.1325 0.0820 88 THR A O 641 C CB . THR A 88 ? 1.5486 0.6968 0.5919 0.3341 -0.0801 0.0696 88 THR A CB 642 O OG1 . THR A 88 ? 1.4366 0.6857 0.5698 0.3032 -0.0768 0.0573 88 THR A OG1 643 C CG2 . THR A 88 ? 1.5659 0.6692 0.6088 0.3297 -0.0716 0.0656 88 THR A CG2 644 N N . ALA A 89 ? 1.7897 0.7735 0.6248 0.4245 -0.1129 0.0994 89 ALA A N 645 C CA . ALA A 89 ? 1.9277 0.7885 0.6442 0.4598 -0.1165 0.1180 89 ALA A CA 646 C C . ALA A 89 ? 1.9729 0.8500 0.6637 0.5289 -0.1638 0.1153 89 ALA A C 647 O O . ALA A 89 ? 2.0572 0.8644 0.6937 0.5687 -0.1730 0.1217 89 ALA A O 648 C CB . ALA A 89 ? 2.0029 0.7880 0.6387 0.4387 -0.0925 0.1358 89 ALA A CB 649 N N . LYS A 90 ? 1.9166 0.8852 0.6500 0.5434 -0.1954 0.1047 90 LYS A N 650 C CA . LYS A 90 ? 1.9524 0.9511 0.6777 0.6075 -0.2462 0.1000 90 LYS A CA 651 C C . LYS A 90 ? 1.8747 0.9663 0.6986 0.6340 -0.2610 0.0840 90 LYS A C 652 O O . LYS A 90 ? 1.8870 1.0320 0.7385 0.6850 -0.3016 0.0767 90 LYS A O 653 C CB . LYS A 90 ? 1.9348 0.9936 0.6714 0.6110 -0.2788 0.0922 90 LYS A CB 654 N N . ALA A 91 ? 1.8043 0.9136 0.6809 0.6003 -0.2276 0.0784 91 ALA A N 655 C CA . ALA A 91 ? 1.7452 0.9257 0.6998 0.6238 -0.2309 0.0648 91 ALA A CA 656 C C . ALA A 91 ? 1.8103 0.8907 0.7068 0.6324 -0.2092 0.0701 91 ALA A C 657 O O . ALA A 91 ? 1.7952 0.9057 0.7299 0.6592 -0.2081 0.0599 91 ALA A O 658 C CB . ALA A 91 ? 1.6058 0.9003 0.6727 0.5802 -0.2147 0.0502 91 ALA A CB 659 N N . GLY A 92 ? 1.8940 0.8514 0.6966 0.6093 -0.1901 0.0859 92 GLY A N 660 C CA . GLY A 92 ? 1.9794 0.8195 0.7138 0.6128 -0.1714 0.0921 92 GLY A CA 661 C C . GLY A 92 ? 1.9087 0.7686 0.6992 0.5672 -0.1452 0.0791 92 GLY A C 662 O O . GLY A 92 ? 1.9682 0.7508 0.7213 0.5740 -0.1362 0.0765 92 GLY A O 663 N N . LEU A 93 ? 1.7875 0.7454 0.6627 0.5229 -0.1362 0.0700 93 LEU A N 664 C CA . LEU A 93 ? 1.7166 0.7093 0.6522 0.4827 -0.1181 0.0559 93 LEU A CA 665 C C . LEU A 93 ? 1.7475 0.6573 0.6545 0.4267 -0.0930 0.0621 93 LEU A C 666 O O . LEU A 93 ? 1.8051 0.6590 0.6669 0.4081 -0.0813 0.0780 93 LEU A O 667 C CB . LEU A 93 ? 1.5832 0.7117 0.6203 0.4614 -0.1197 0.0448 93 LEU A CB 668 C CG . LEU A 93 ? 1.5464 0.7781 0.6413 0.5059 -0.1402 0.0367 93 LEU A CG 669 C CD1 . LEU A 93 ? 1.4445 0.7931 0.6355 0.4736 -0.1353 0.0274 93 LEU A CD1 670 C CD2 . LEU A 93 ? 1.6028 0.8259 0.6929 0.5527 -0.1420 0.0285 93 LEU A CD2 671 N N . ASP A 94 ? 1.7213 0.6228 0.6556 0.4006 -0.0844 0.0490 94 ASP A N 672 C CA . ASP A 94 ? 1.7455 0.5723 0.6680 0.3469 -0.0648 0.0512 94 ASP A CA 673 C C . ASP A 94 ? 1.6210 0.5291 0.6318 0.2936 -0.0558 0.0411 94 ASP A C 674 O O . ASP A 94 ? 1.5416 0.5388 0.6097 0.3003 -0.0659 0.0274 94 ASP A O 675 C CB . ASP A 94 ? 1.8275 0.5625 0.7050 0.3570 -0.0689 0.0417 94 ASP A CB 676 C CG . ASP A 94 ? 1.7971 0.5894 0.7034 0.3890 -0.0841 0.0214 94 ASP A CG 677 O OD1 . ASP A 94 ? 1.7408 0.5901 0.7059 0.3589 -0.0841 0.0069 94 ASP A OD1 678 O OD2 . ASP A 94 ? 1.8608 0.6378 0.7280 0.4471 -0.0946 0.0206 94 ASP A OD2 679 N N . TYR A 95 ? 1.6140 0.4871 0.6345 0.2429 -0.0347 0.0489 95 TYR A N 680 C CA . TYR A 95 ? 1.5182 0.4522 0.6226 0.1904 -0.0260 0.0392 95 TYR A CA 681 C C . TYR A 95 ? 1.5054 0.4257 0.6359 0.1742 -0.0398 0.0188 95 TYR A C 682 O O . TYR A 95 ? 1.5981 0.4311 0.6732 0.1887 -0.0472 0.0148 95 TYR A O 683 C CB . TYR A 95 ? 1.5533 0.4451 0.6611 0.1444 0.0046 0.0540 95 TYR A CB 684 C CG . TYR A 95 ? 1.5677 0.4633 0.6385 0.1572 0.0201 0.0732 95 TYR A CG 685 C CD1 . TYR A 95 ? 1.4923 0.4729 0.6179 0.1392 0.0291 0.0727 95 TYR A CD1 686 C CD2 . TYR A 95 ? 1.6845 0.4912 0.6578 0.1900 0.0233 0.0906 95 TYR A CD2 687 C CE1 . TYR A 95 ? 1.5071 0.4814 0.5873 0.1526 0.0404 0.0876 95 TYR A CE1 688 C CE2 . TYR A 95 ? 1.7155 0.5159 0.6409 0.2054 0.0326 0.1069 95 TYR A CE2 689 C CZ . TYR A 95 ? 1.6255 0.5099 0.6039 0.1860 0.0406 0.1041 95 TYR A CZ 690 O OH . TYR A 95 ? 1.6656 0.5336 0.5850 0.2030 0.0470 0.1177 95 TYR A OH 691 N N . PRO A 96 ? 1.4079 0.4064 0.6155 0.1461 -0.0456 0.0052 96 PRO A N 692 C CA . PRO A 96 ? 1.2959 0.3967 0.5715 0.1298 -0.0386 0.0073 96 PRO A CA 693 C C . PRO A 96 ? 1.2381 0.4130 0.5154 0.1722 -0.0491 0.0066 96 PRO A C 694 O O . PRO A 96 ? 1.2517 0.4212 0.5007 0.2103 -0.0627 -0.0005 96 PRO A O 695 C CB . PRO A 96 ? 1.2454 0.3837 0.5890 0.0948 -0.0491 -0.0099 96 PRO A CB 696 C CG . PRO A 96 ? 1.3356 0.3820 0.6469 0.0851 -0.0619 -0.0212 96 PRO A CG 697 C CD . PRO A 96 ? 1.4116 0.3898 0.6359 0.1306 -0.0639 -0.0153 96 PRO A CD 698 N N . ARG A 97 ? 1.1719 0.4126 0.4831 0.1655 -0.0408 0.0138 97 ARG A N 699 C CA . ARG A 97 ? 1.1137 0.4384 0.4497 0.1939 -0.0507 0.0115 97 ARG A CA 700 C C . ARG A 97 ? 1.0219 0.4244 0.4302 0.1608 -0.0444 0.0076 97 ARG A C 701 O O . ARG A 97 ? 1.0257 0.4186 0.4496 0.1280 -0.0290 0.0130 97 ARG A O 702 C CB . ARG A 97 ? 1.1406 0.4570 0.4345 0.2235 -0.0529 0.0237 97 ARG A CB 703 C CG . ARG A 97 ? 1.2332 0.4955 0.4645 0.2704 -0.0651 0.0265 97 ARG A CG 704 C CD . ARG A 97 ? 1.2108 0.5345 0.4712 0.3059 -0.0784 0.0156 97 ARG A CD 705 N NE . ARG A 97 ? 1.3013 0.5573 0.5026 0.3464 -0.0853 0.0149 97 ARG A NE 706 C CZ . ARG A 97 ? 1.2806 0.5647 0.4909 0.3831 -0.0907 0.0057 97 ARG A CZ 707 N NH1 . ARG A 97 ? 1.2026 0.5808 0.4789 0.3824 -0.0880 -0.0019 97 ARG A NH1 708 N NH2 . ARG A 97 ? 1.3761 0.5883 0.5266 0.4207 -0.0951 0.0047 97 ARG A NH2 709 N N . VAL A 98 ? 0.9583 0.4323 0.4092 0.1697 -0.0528 -0.0010 98 VAL A N 710 C CA . VAL A 98 ? 0.8795 0.4244 0.3930 0.1442 -0.0479 -0.0033 98 VAL A CA 711 C C . VAL A 98 ? 0.8295 0.4413 0.3628 0.1648 -0.0520 -0.0013 98 VAL A C 712 O O . VAL A 98 ? 0.8010 0.4468 0.3419 0.1928 -0.0593 -0.0047 98 VAL A O 713 C CB . VAL A 98 ? 0.8463 0.4190 0.3980 0.1310 -0.0536 -0.0141 98 VAL A CB 714 C CG1 . VAL A 98 ? 0.7857 0.4167 0.3978 0.1025 -0.0474 -0.0147 98 VAL A CG1 715 C CG2 . VAL A 98 ? 0.9263 0.4342 0.4599 0.1157 -0.0597 -0.0210 98 VAL A CG2 716 N N . PHE A 99 ? 0.8039 0.4352 0.3494 0.1497 -0.0463 0.0031 99 PHE A N 717 C CA . PHE A 99 ? 0.7631 0.4587 0.3354 0.1619 -0.0548 0.0017 99 PHE A CA 718 C C . PHE A 99 ? 0.6957 0.4464 0.3269 0.1337 -0.0479 -0.0031 99 PHE A C 719 O O . PHE A 99 ? 0.7017 0.4357 0.3443 0.1055 -0.0357 -0.0029 99 PHE A O 720 C CB . PHE A 99 ? 0.7992 0.4678 0.3272 0.1726 -0.0599 0.0078 99 PHE A CB 721 C CG . PHE A 99 ? 0.8694 0.4879 0.3369 0.2096 -0.0721 0.0133 99 PHE A CG 722 C CD1 . PHE A 99 ? 0.8415 0.5007 0.3175 0.2458 -0.0943 0.0104 99 PHE A CD1 723 C CD2 . PHE A 99 ? 0.9202 0.4511 0.3278 0.2082 -0.0616 0.0215 99 PHE A CD2 724 C CE1 . PHE A 99 ? 0.9536 0.5673 0.3758 0.2852 -0.1078 0.0153 99 PHE A CE1 725 C CE2 . PHE A 99 ? 1.0291 0.5052 0.3748 0.2446 -0.0728 0.0276 99 PHE A CE2 726 C CZ . PHE A 99 ? 1.0246 0.5421 0.3755 0.2859 -0.0972 0.0244 99 PHE A CZ 727 N N . GLN A 100 ? 0.6504 0.4663 0.3231 0.1413 -0.0549 -0.0070 100 GLN A N 728 C CA . GLN A 100 ? 0.5814 0.4452 0.3067 0.1167 -0.0487 -0.0108 100 GLN A CA 729 C C . GLN A 100 ? 0.5648 0.4776 0.3169 0.1202 -0.0587 -0.0143 100 GLN A C 730 O O . GLN A 100 ? 0.5630 0.4983 0.3171 0.1450 -0.0725 -0.0152 100 GLN A O 731 C CB . GLN A 100 ? 0.5653 0.4524 0.3192 0.1162 -0.0439 -0.0124 100 GLN A CB 732 C CG . GLN A 100 ? 0.5928 0.4327 0.3267 0.1066 -0.0410 -0.0134 100 GLN A CG 733 C CD . GLN A 100 ? 0.6043 0.4478 0.3365 0.1193 -0.0418 -0.0157 100 GLN A CD 734 O OE1 . GLN A 100 ? 0.6409 0.4616 0.3403 0.1441 -0.0443 -0.0163 100 GLN A OE1 735 N NE2 . GLN A 100 ? 0.5717 0.4364 0.3314 0.1051 -0.0392 -0.0169 100 GLN A NE2 736 N N A ILE A 101 ? 0.5330 0.4613 0.3082 0.0962 -0.0538 -0.0176 101 ILE A N 737 N N B ILE A 101 ? 0.5317 0.4583 0.3050 0.0965 -0.0540 -0.0175 101 ILE A N 738 C CA A ILE A 101 ? 0.5304 0.4958 0.3279 0.0943 -0.0666 -0.0241 101 ILE A CA 739 C CA B ILE A 101 ? 0.5218 0.4889 0.3208 0.0949 -0.0667 -0.0240 101 ILE A CA 740 C C A ILE A 101 ? 0.4847 0.4880 0.3352 0.0710 -0.0578 -0.0275 101 ILE A C 741 C C B ILE A 101 ? 0.4791 0.4829 0.3308 0.0721 -0.0568 -0.0268 101 ILE A C 742 O O A ILE A 101 ? 0.4754 0.4598 0.3262 0.0519 -0.0443 -0.0272 101 ILE A O 743 O O B ILE A 101 ? 0.4640 0.4492 0.3174 0.0544 -0.0425 -0.0252 101 ILE A O 744 C CB A ILE A 101 ? 0.5734 0.4973 0.3203 0.0923 -0.0717 -0.0264 101 ILE A CB 745 C CB B ILE A 101 ? 0.5623 0.4933 0.3154 0.0925 -0.0734 -0.0272 101 ILE A CB 746 C CG1 A ILE A 101 ? 0.6478 0.5229 0.3304 0.1177 -0.0804 -0.0205 101 ILE A CG1 747 C CG1 B ILE A 101 ? 0.6294 0.5031 0.3138 0.1138 -0.0772 -0.0204 101 ILE A CG1 748 C CG2 A ILE A 101 ? 0.5683 0.5253 0.3342 0.0898 -0.0916 -0.0372 101 ILE A CG2 749 C CG2 B ILE A 101 ? 0.5514 0.5214 0.3266 0.0954 -0.0975 -0.0377 101 ILE A CG2 750 C CD1 A ILE A 101 ? 0.6953 0.5052 0.3330 0.1095 -0.0578 -0.0114 101 ILE A CD1 751 C CD1 B ILE A 101 ? 0.6799 0.5031 0.3003 0.1148 -0.0787 -0.0205 101 ILE A CD1 752 N N . HIS A 102 ? 0.4655 0.5214 0.3643 0.0731 -0.0641 -0.0303 102 HIS A N 753 C CA . HIS A 102 ? 0.4287 0.5139 0.3745 0.0512 -0.0544 -0.0318 102 HIS A CA 754 C C . HIS A 102 ? 0.4390 0.5558 0.4151 0.0434 -0.0716 -0.0418 102 HIS A C 755 O O . HIS A 102 ? 0.4324 0.5868 0.4364 0.0563 -0.0866 -0.0450 102 HIS A O 756 C CB . HIS A 102 ? 0.4208 0.5330 0.3972 0.0565 -0.0399 -0.0242 102 HIS A CB 757 C CG . HIS A 102 ? 0.3884 0.5207 0.4044 0.0357 -0.0270 -0.0222 102 HIS A CG 758 N ND1 . HIS A 102 ? 0.3579 0.5204 0.4070 0.0383 -0.0113 -0.0150 102 HIS A ND1 759 C CD2 . HIS A 102 ? 0.4174 0.5373 0.4404 0.0139 -0.0244 -0.0255 102 HIS A CD2 760 C CE1 . HIS A 102 ? 0.4053 0.5696 0.4773 0.0174 -0.0005 -0.0125 102 HIS A CE1 761 N NE2 . HIS A 102 ? 0.3789 0.5185 0.4371 0.0031 -0.0102 -0.0197 102 HIS A NE2 762 N N . THR A 103 ? 0.4470 0.5468 0.4190 0.0233 -0.0707 -0.0483 103 THR A N 763 C CA . THR A 103 ? 0.4729 0.5894 0.4654 0.0120 -0.0895 -0.0613 103 THR A CA 764 C C . THR A 103 ? 0.4495 0.5769 0.4838 -0.0136 -0.0756 -0.0623 103 THR A C 765 O O . THR A 103 ? 0.4363 0.5408 0.4614 -0.0205 -0.0544 -0.0549 103 THR A O 766 C CB . THR A 103 ? 0.5245 0.5906 0.4522 0.0147 -0.1004 -0.0700 103 THR A CB 767 O OG1 . THR A 103 ? 0.5834 0.6265 0.4614 0.0392 -0.1100 -0.0658 103 THR A OG1 768 C CG2 . THR A 103 ? 0.5717 0.6450 0.5074 0.0058 -0.1267 -0.0870 103 THR A CG2 769 N N . GLY A 104 ? 0.4496 0.6090 0.5307 -0.0274 -0.0897 -0.0719 104 GLY A N 770 C CA . GLY A 104 ? 0.4393 0.5984 0.5545 -0.0530 -0.0777 -0.0734 104 GLY A CA 771 C C . GLY A 104 ? 0.4727 0.6411 0.6149 -0.0708 -0.1025 -0.0915 104 GLY A C 772 O O . GLY A 104 ? 0.4761 0.6739 0.6369 -0.0645 -0.1313 -0.1020 104 GLY A O 773 N N . CYS A 105 ? 0.4917 0.6324 0.6360 -0.0917 -0.0938 -0.0962 105 CYS A N 774 C CA . CYS A 105 ? 0.5354 0.6750 0.7069 -0.1142 -0.1154 -0.1147 105 CYS A CA 775 C C . CYS A 105 ? 0.5425 0.6706 0.7476 -0.1379 -0.0900 -0.1073 105 CYS A C 776 O O . CYS A 105 ? 0.5503 0.6340 0.7171 -0.1357 -0.0700 -0.1015 105 CYS A O 777 C CB . CYS A 105 ? 0.5785 0.6627 0.6787 -0.1090 -0.1350 -0.1335 105 CYS A CB 778 S SG . CYS A 105 ? 0.6294 0.6969 0.7426 -0.1330 -0.1720 -0.1629 105 CYS A SG 779 N N . LYS A 106 ? 0.5540 0.7215 0.8326 -0.1590 -0.0894 -0.1061 106 LYS A N 780 C CA . LYS A 106 ? 0.5840 0.7336 0.8935 -0.1841 -0.0654 -0.0982 106 LYS A CA 781 C C . LYS A 106 ? 0.6345 0.7747 0.9767 -0.2135 -0.0908 -0.1206 106 LYS A C 782 O O . LYS A 106 ? 0.6474 0.8300 1.0344 -0.2205 -0.1219 -0.1360 106 LYS A O 783 C CB . LYS A 106 ? 0.5612 0.7564 0.9299 -0.1889 -0.0362 -0.0766 106 LYS A CB 784 C CG . LYS A 106 ? 0.5836 0.7452 0.9569 -0.2045 -0.0002 -0.0584 106 LYS A CG 785 C CD . LYS A 106 ? 0.5768 0.7708 0.9766 -0.1969 0.0350 -0.0332 106 LYS A CD 786 C CE . LYS A 106 ? 0.6325 0.7744 0.9731 -0.1828 0.0640 -0.0118 106 LYS A CE 787 N NZ . LYS A 106 ? 0.6248 0.7863 0.9557 -0.1613 0.0908 0.0093 106 LYS A NZ 788 N N . LEU A 107 ? 0.6838 0.7666 1.0043 -0.2291 -0.0808 -0.1239 107 LEU A N 789 C CA . LEU A 107 ? 0.7467 0.8096 1.1000 -0.2619 -0.1014 -0.1448 107 LEU A CA 790 C C . LEU A 107 ? 0.7640 0.8209 1.1728 -0.2915 -0.0704 -0.1289 107 LEU A C 791 O O . LEU A 107 ? 0.7739 0.7774 1.1452 -0.2888 -0.0421 -0.1148 107 LEU A O 792 C CB . LEU A 107 ? 0.8004 0.7876 1.0779 -0.2574 -0.1168 -0.1657 107 LEU A CB 793 C CG . LEU A 107 ? 0.8190 0.7813 1.0150 -0.2273 -0.1362 -0.1798 107 LEU A CG 794 C CD1 . LEU A 107 ? 0.8883 0.7789 1.0309 -0.2342 -0.1557 -0.2071 107 LEU A CD1 795 C CD2 . LEU A 107 ? 0.8157 0.8297 1.0234 -0.2157 -0.1691 -0.1882 107 LEU A CD2 796 N N . TYR A 108 ? 0.7749 0.8854 1.2744 -0.3188 -0.0752 -0.1308 108 TYR A N 797 C CA . TYR A 108 ? 0.8087 0.9101 1.3677 -0.3537 -0.0444 -0.1169 108 TYR A CA 798 C C . TYR A 108 ? 0.8766 0.9175 1.4319 -0.3841 -0.0673 -0.1411 108 TYR A C 799 O O . TYR A 108 ? 0.9063 0.9453 1.4549 -0.3878 -0.1147 -0.1728 108 TYR A O 800 C CB . TYR A 108 ? 0.7915 0.9786 1.4621 -0.3737 -0.0361 -0.1101 108 TYR A CB 801 C CG . TYR A 108 ? 0.7427 0.9893 1.4158 -0.3404 -0.0173 -0.0906 108 TYR A CG 802 C CD1 . TYR A 108 ? 0.7269 0.9632 1.3784 -0.3274 0.0345 -0.0577 108 TYR A CD1 803 C CD2 . TYR A 108 ? 0.7166 1.0205 1.4034 -0.3191 -0.0533 -0.1058 108 TYR A CD2 804 C CE1 . TYR A 108 ? 0.6896 0.9710 1.3345 -0.2955 0.0505 -0.0424 108 TYR A CE1 805 C CE2 . TYR A 108 ? 0.6757 1.0258 1.3599 -0.2869 -0.0361 -0.0890 108 TYR A CE2 806 C CZ . TYR A 108 ? 0.6606 0.9991 1.3244 -0.2760 0.0161 -0.0583 108 TYR A CZ 807 O OH . TYR A 108 ? 0.6225 0.9984 1.2763 -0.2432 0.0320 -0.0441 108 TYR A OH 808 N N . THR A 109 ? 0.9128 0.8960 1.4640 -0.4039 -0.0354 -0.1270 109 THR A N 809 C CA . THR A 109 ? 0.9853 0.8983 1.5263 -0.4322 -0.0548 -0.1500 109 THR A CA 810 C C . THR A 109 ? 1.0157 0.9618 1.6638 -0.4826 -0.0729 -0.1659 109 THR A C 811 O O . THR A 109 ? 1.0830 0.9690 1.7434 -0.5167 -0.0724 -0.1747 109 THR A O 812 C CB . THR A 109 ? 1.0257 0.8473 1.5050 -0.4280 -0.0191 -0.1318 109 THR A CB 813 O OG1 . THR A 109 ? 1.0261 0.8583 1.5361 -0.4347 0.0303 -0.0947 109 THR A OG1 814 C CG2 . THR A 109 ? 1.0103 0.7958 1.3905 -0.3809 -0.0191 -0.1307 109 THR A CG2 815 N N . ASN A 110 ? 0.9707 1.0123 1.6999 -0.4868 -0.0899 -0.1704 110 ASN A N 816 C CA . ASN A 110 ? 0.9981 1.0872 1.8415 -0.5317 -0.1213 -0.1932 110 ASN A CA 817 C C . ASN A 110 ? 0.9939 1.1267 1.8436 -0.5195 -0.1907 -0.2299 110 ASN A C 818 O O . ASN A 110 ? 1.0103 1.1939 1.9591 -0.5513 -0.2286 -0.2529 110 ASN A O 819 C CB . ASN A 110 ? 0.9702 1.1374 1.9339 -0.5562 -0.0773 -0.1661 110 ASN A CB 820 C CG . ASN A 110 ? 0.8998 1.1725 1.9104 -0.5270 -0.0816 -0.1596 110 ASN A CG 821 O OD1 . ASN A 110 ? 0.8572 1.1369 1.7955 -0.4841 -0.1078 -0.1669 110 ASN A OD1 822 N ND2 . ASN A 110 ? 0.8879 1.2406 2.0231 -0.5508 -0.0517 -0.1447 110 ASN A ND2 823 N N . GLY A 111 ? 0.9707 1.0824 1.7150 -0.4727 -0.2071 -0.2344 111 GLY A N 824 C CA . GLY A 111 ? 0.9853 1.1138 1.7012 -0.4536 -0.2714 -0.2672 111 GLY A CA 825 C C . GLY A 111 ? 0.9213 1.1185 1.6295 -0.4121 -0.2742 -0.2551 111 GLY A C 826 O O . GLY A 111 ? 0.9241 1.0938 1.5378 -0.3759 -0.2999 -0.2659 111 GLY A O 827 N N . THR A 112 ? 0.8672 1.1482 1.6715 -0.4168 -0.2443 -0.2318 112 THR A N 828 C CA . THR A 112 ? 0.8101 1.1597 1.6196 -0.3782 -0.2445 -0.2196 112 THR A CA 829 C C . THR A 112 ? 0.7651 1.0712 1.4558 -0.3340 -0.2166 -0.1995 112 THR A C 830 O O . THR A 112 ? 0.7704 1.0139 1.4008 -0.3337 -0.1787 -0.1837 112 THR A O 831 C CB . THR A 112 ? 0.7707 1.2119 1.7058 -0.3914 -0.2063 -0.1966 112 THR A CB 832 O OG1 . THR A 112 ? 0.7783 1.1847 1.7116 -0.4088 -0.1415 -0.1671 112 THR A OG1 833 C CG2 . THR A 112 ? 0.8034 1.3130 1.8768 -0.4297 -0.2428 -0.2197 112 THR A CG2 834 N N . ARG A 113 ? 0.7281 1.0664 1.3887 -0.2967 -0.2381 -0.2010 113 ARG A N 835 C CA . ARG A 113 ? 0.6864 0.9926 1.2485 -0.2570 -0.2141 -0.1827 113 ARG A CA 836 C C . ARG A 113 ? 0.6269 1.0020 1.2282 -0.2321 -0.1950 -0.1623 113 ARG A C 837 O O . ARG A 113 ? 0.6262 1.0719 1.3052 -0.2305 -0.2208 -0.1710 113 ARG A O 838 C CB . ARG A 113 ? 0.7240 0.9834 1.1867 -0.2301 -0.2558 -0.2032 113 ARG A CB 839 C CG . ARG A 113 ? 0.7850 0.9615 1.1773 -0.2424 -0.2739 -0.2253 113 ARG A CG 840 C CD . ARG A 113 ? 0.8296 0.9715 1.1350 -0.2153 -0.3212 -0.2481 113 ARG A CD 841 N NE . ARG A 113 ? 0.8535 1.0267 1.2081 -0.2272 -0.3831 -0.2773 113 ARG A NE 842 C CZ . ARG A 113 ? 0.9204 1.0472 1.2587 -0.2487 -0.4206 -0.3077 113 ARG A CZ 843 N NH1 . ARG A 113 ? 0.9396 0.9851 1.2110 -0.2583 -0.3979 -0.3114 113 ARG A NH1 844 N NH2 . ARG A 113 ? 0.9809 1.1411 1.3709 -0.2593 -0.4833 -0.3359 113 ARG A NH2 845 N N . TRP A 114 ? 0.5802 0.9335 1.1278 -0.2107 -0.1530 -0.1372 114 TRP A N 846 C CA . TRP A 114 ? 0.5350 0.9326 1.0870 -0.1788 -0.1399 -0.1214 114 TRP A CA 847 C C . TRP A 114 ? 0.5263 0.8759 0.9712 -0.1449 -0.1515 -0.1220 114 TRP A C 848 O O . TRP A 114 ? 0.5179 0.8074 0.8928 -0.1427 -0.1319 -0.1151 114 TRP A O 849 C CB . TRP A 114 ? 0.5141 0.9239 1.0897 -0.1801 -0.0831 -0.0924 114 TRP A CB 850 C CG . TRP A 114 ? 0.4976 0.9490 1.0767 -0.1462 -0.0671 -0.0775 114 TRP A CG 851 C CD1 . TRP A 114 ? 0.4957 1.0115 1.1268 -0.1279 -0.0900 -0.0852 114 TRP A CD1 852 C CD2 . TRP A 114 ? 0.4939 0.9211 1.0214 -0.1250 -0.0271 -0.0542 114 TRP A CD2 853 N NE1 . TRP A 114 ? 0.4801 1.0091 1.0911 -0.0959 -0.0632 -0.0677 114 TRP A NE1 854 C CE2 . TRP A 114 ? 0.4750 0.9491 1.0211 -0.0948 -0.0255 -0.0494 114 TRP A CE2 855 C CE3 . TRP A 114 ? 0.4993 0.8674 0.9651 -0.1262 0.0035 -0.0385 114 TRP A CE3 856 C CZ2 . TRP A 114 ? 0.4707 0.9284 0.9696 -0.0679 0.0065 -0.0308 114 TRP A CZ2 857 C CZ3 . TRP A 114 ? 0.4805 0.8368 0.9031 -0.0998 0.0310 -0.0202 114 TRP A CZ3 858 C CH2 . TRP A 114 ? 0.4620 0.8600 0.8984 -0.0720 0.0327 -0.0172 114 TRP A CH2 859 N N . SER A 115 ? 0.5199 0.8958 0.9564 -0.1185 -0.1831 -0.1301 115 SER A N 860 C CA . SER A 115 ? 0.5287 0.8566 0.8648 -0.0870 -0.1925 -0.1292 115 SER A CA 861 C C . SER A 115 ? 0.4938 0.8594 0.8370 -0.0544 -0.1899 -0.1175 115 SER A C 862 O O . SER A 115 ? 0.4827 0.9150 0.9040 -0.0499 -0.2041 -0.1210 115 SER A O 863 C CB . SER A 115 ? 0.5923 0.8853 0.8771 -0.0831 -0.2410 -0.1539 115 SER A CB 864 O OG . SER A 115 ? 0.6538 0.8906 0.9023 -0.1059 -0.2390 -0.1648 115 SER A OG 865 N N . PHE A 116 ? 0.4713 0.7946 0.7382 -0.0316 -0.1715 -0.1044 116 PHE A N 866 C CA . PHE A 116 ? 0.4534 0.7977 0.7139 0.0013 -0.1678 -0.0936 116 PHE A CA 867 C C . PHE A 116 ? 0.4742 0.7538 0.6333 0.0244 -0.1672 -0.0881 116 PHE A C 868 O O . PHE A 116 ? 0.4765 0.7016 0.5806 0.0134 -0.1527 -0.0863 116 PHE A O 869 C CB . PHE A 116 ? 0.4087 0.7872 0.7173 0.0009 -0.1259 -0.0752 116 PHE A CB 870 C CG . PHE A 116 ? 0.3972 0.7265 0.6601 -0.0096 -0.0899 -0.0615 116 PHE A CG 871 C CD1 . PHE A 116 ? 0.3616 0.6877 0.6546 -0.0391 -0.0701 -0.0584 116 PHE A CD1 872 C CD2 . PHE A 116 ? 0.3933 0.6780 0.5853 0.0107 -0.0785 -0.0520 116 PHE A CD2 873 C CE1 . PHE A 116 ? 0.3619 0.6433 0.6130 -0.0438 -0.0426 -0.0462 116 PHE A CE1 874 C CE2 . PHE A 116 ? 0.3906 0.6361 0.5498 0.0022 -0.0530 -0.0420 116 PHE A CE2 875 C CZ . PHE A 116 ? 0.3560 0.6009 0.5439 -0.0231 -0.0366 -0.0391 116 PHE A CZ 876 N N . VAL A 117 ? 0.4902 0.7759 0.6295 0.0566 -0.1818 -0.0855 117 VAL A N 877 C CA . VAL A 117 ? 0.5222 0.7473 0.5735 0.0786 -0.1737 -0.0762 117 VAL A CA 878 C C . VAL A 117 ? 0.5121 0.7584 0.5756 0.1065 -0.1624 -0.0647 117 VAL A C 879 O O . VAL A 117 ? 0.5268 0.8160 0.6264 0.1295 -0.1848 -0.0690 117 VAL A O 880 C CB . VAL A 117 ? 0.5906 0.7690 0.5676 0.0964 -0.2068 -0.0849 117 VAL A CB 881 C CG1 . VAL A 117 ? 0.6309 0.7407 0.5211 0.1125 -0.1876 -0.0716 117 VAL A CG1 882 C CG2 . VAL A 117 ? 0.6192 0.7699 0.5727 0.0743 -0.2206 -0.0993 117 VAL A CG2 883 N N . ASN A 118 ? 0.4950 0.7096 0.5280 0.1063 -0.1302 -0.0518 118 ASN A N 884 C CA . ASN A 118 ? 0.5009 0.7178 0.5274 0.1335 -0.1169 -0.0421 118 ASN A CA 885 C C . ASN A 118 ? 0.5360 0.6793 0.4768 0.1470 -0.1123 -0.0355 118 ASN A C 886 O O . ASN A 118 ? 0.5239 0.6240 0.4305 0.1273 -0.0979 -0.0326 118 ASN A O 887 C CB . ASN A 118 ? 0.4731 0.7143 0.5395 0.1223 -0.0830 -0.0336 118 ASN A CB 888 C CG . ASN A 118 ? 0.4406 0.7537 0.5971 0.1097 -0.0785 -0.0364 118 ASN A CG 889 O OD1 . ASN A 118 ? 0.4930 0.8535 0.6982 0.1180 -0.1021 -0.0450 118 ASN A OD1 890 N ND2 . ASN A 118 ? 0.4297 0.7496 0.6103 0.0893 -0.0492 -0.0290 118 ASN A ND2 891 N N . ILE A 119 ? 0.5763 0.7059 0.4884 0.1807 -0.1236 -0.0331 119 ILE A N 892 C CA . ILE A 119 ? 0.6089 0.6643 0.4429 0.1934 -0.1165 -0.0257 119 ILE A CA 893 C C . ILE A 119 ? 0.6184 0.6716 0.4522 0.2152 -0.1003 -0.0201 119 ILE A C 894 O O . ILE A 119 ? 0.6222 0.7203 0.4935 0.2411 -0.1044 -0.0213 119 ILE A O 895 C CB . ILE A 119 ? 0.6714 0.6827 0.4432 0.2174 -0.1428 -0.0262 119 ILE A CB 896 C CG1 . ILE A 119 ? 0.6862 0.6921 0.4452 0.1997 -0.1599 -0.0337 119 ILE A CG1 897 C CG2 . ILE A 119 ? 0.6955 0.6229 0.3886 0.2230 -0.1298 -0.0169 119 ILE A CG2 898 C CD1 . ILE A 119 ? 0.7698 0.7258 0.4550 0.2252 -0.1880 -0.0342 119 ILE A CD1 899 N N . GLY A 120 ? 0.6200 0.6201 0.4126 0.2054 -0.0827 -0.0154 120 GLY A N 900 C CA . GLY A 120 ? 0.6482 0.6235 0.4172 0.2276 -0.0714 -0.0125 120 GLY A CA 901 C C . GLY A 120 ? 0.7110 0.6025 0.4050 0.2368 -0.0752 -0.0095 120 GLY A C 902 O O . GLY A 120 ? 0.7196 0.5684 0.3817 0.2167 -0.0773 -0.0074 120 GLY A O 903 N N . GLU A 121 ? 0.7537 0.6181 0.4189 0.2673 -0.0726 -0.0090 121 GLU A N 904 C CA . GLU A 121 ? 0.8232 0.6002 0.4181 0.2734 -0.0737 -0.0070 121 GLU A CA 905 C C . GLU A 121 ? 0.8431 0.5962 0.4211 0.2844 -0.0626 -0.0111 121 GLU A C 906 O O . GLU A 121 ? 0.8329 0.6258 0.4332 0.3107 -0.0548 -0.0130 121 GLU A O 907 C CB . GLU A 121 ? 0.8925 0.6366 0.4449 0.3094 -0.0891 -0.0032 121 GLU A CB 908 C CG . GLU A 121 ? 1.0013 0.6427 0.4746 0.3151 -0.0887 0.0009 121 GLU A CG 909 C CD . GLU A 121 ? 1.1119 0.7180 0.5585 0.3405 -0.0830 -0.0038 121 GLU A CD 910 O OE1 . GLU A 121 ? 1.1296 0.7831 0.6026 0.3741 -0.0816 -0.0073 121 GLU A OE1 911 O OE2 . GLU A 121 ? 1.1931 0.7234 0.5944 0.3260 -0.0788 -0.0052 121 GLU A OE2 912 N N . GLY A 122 ? 0.8756 0.5618 0.4143 0.2644 -0.0616 -0.0131 122 GLY A N 913 C CA . GLY A 122 ? 0.9004 0.5513 0.4120 0.2719 -0.0575 -0.0202 122 GLY A CA 914 C C . GLY A 122 ? 0.8516 0.5585 0.4006 0.2694 -0.0463 -0.0227 122 GLY A C 915 O O . GLY A 122 ? 0.9009 0.5905 0.4224 0.2927 -0.0392 -0.0273 122 GLY A O 916 N N . GLY A 123 ? 0.7859 0.5523 0.3899 0.2432 -0.0426 -0.0192 123 GLY A N 917 C CA . GLY A 123 ? 0.7437 0.5522 0.3778 0.2362 -0.0302 -0.0190 123 GLY A CA 918 C C . GLY A 123 ? 0.7319 0.6000 0.3987 0.2629 -0.0124 -0.0151 123 GLY A C 919 O O . GLY A 123 ? 0.7277 0.6129 0.4008 0.2656 0.0047 -0.0133 123 GLY A O 920 N N . ARG A 124 ? 0.7271 0.6251 0.4150 0.2842 -0.0160 -0.0134 124 ARG A N 921 C CA . ARG A 124 ? 0.7154 0.6852 0.4581 0.3067 -0.0006 -0.0104 124 ARG A CA 922 C C . ARG A 124 ? 0.6730 0.6965 0.4707 0.2967 -0.0177 -0.0099 124 ARG A C 923 O O . ARG A 124 ? 0.6747 0.6628 0.4434 0.2880 -0.0388 -0.0112 124 ARG A O 924 C CB . ARG A 124 ? 0.7754 0.7259 0.4881 0.3554 0.0057 -0.0123 124 ARG A CB 925 C CG . ARG A 124 ? 0.8433 0.7246 0.4836 0.3712 0.0187 -0.0161 124 ARG A CG 926 C CD . ARG A 124 ? 0.9268 0.7807 0.5310 0.4229 0.0260 -0.0195 124 ARG A CD 927 N NE . ARG A 124 ? 1.0240 0.8358 0.5981 0.4365 0.0003 -0.0214 124 ARG A NE 928 C CZ . ARG A 124 ? 1.0716 0.9095 0.6659 0.4751 -0.0043 -0.0202 124 ARG A CZ 929 N NH1 . ARG A 124 ? 1.0697 0.9879 0.7302 0.5020 0.0156 -0.0184 124 ARG A NH1 930 N NH2 . ARG A 124 ? 1.1135 0.8965 0.6641 0.4877 -0.0283 -0.0202 124 ARG A NH2 931 N N . ASP A 125 ? 0.6395 0.7436 0.5135 0.2987 -0.0087 -0.0085 125 ASP A N 932 C CA . ASP A 125 ? 0.6167 0.7732 0.5450 0.2916 -0.0318 -0.0117 125 ASP A CA 933 C C . ASP A 125 ? 0.6576 0.7912 0.5550 0.3255 -0.0577 -0.0144 125 ASP A C 934 O O . ASP A 125 ? 0.6912 0.8014 0.5595 0.3629 -0.0511 -0.0136 125 ASP A O 935 C CB . ASP A 125 ? 0.5906 0.8402 0.6166 0.2911 -0.0187 -0.0114 125 ASP A CB 936 C CG . ASP A 125 ? 0.5812 0.8466 0.6318 0.2623 0.0127 -0.0055 125 ASP A CG 937 O OD1 . ASP A 125 ? 0.5733 0.7848 0.5723 0.2392 0.0152 -0.0036 125 ASP A OD1 938 O OD2 . ASP A 125 ? 0.5724 0.9036 0.6962 0.2639 0.0359 -0.0021 125 ASP A OD2 939 N N . LEU A 126 ? 0.6559 0.7884 0.5509 0.3150 -0.0870 -0.0176 126 LEU A N 940 C CA . LEU A 126 ? 0.7061 0.8077 0.5603 0.3479 -0.1158 -0.0187 126 LEU A CA 941 C C . LEU A 126 ? 0.7065 0.8724 0.6185 0.3555 -0.1484 -0.0257 126 LEU A C 942 O O . LEU A 126 ? 0.7361 0.9350 0.6756 0.3951 -0.1646 -0.0281 126 LEU A O 943 C CB . LEU A 126 ? 0.7428 0.7477 0.5028 0.3358 -0.1227 -0.0146 126 LEU A CB 944 C CG . LEU A 126 ? 0.8211 0.7726 0.5177 0.3683 -0.1496 -0.0122 126 LEU A CG 945 C CD1 . LEU A 126 ? 0.8614 0.7927 0.5371 0.4153 -0.1477 -0.0103 126 LEU A CD1 946 C CD2 . LEU A 126 ? 0.8571 0.7162 0.4690 0.3462 -0.1473 -0.0059 126 LEU A CD2 947 N N . VAL A 127 ? 0.6869 0.8675 0.6160 0.3200 -0.1608 -0.0304 127 VAL A N 948 C CA . VAL A 127 ? 0.6892 0.9331 0.6795 0.3202 -0.1959 -0.0411 127 VAL A CA 949 C C . VAL A 127 ? 0.6409 0.9241 0.6854 0.2731 -0.1899 -0.0470 127 VAL A C 950 O O . VAL A 127 ? 0.6145 0.8557 0.6227 0.2420 -0.1678 -0.0427 127 VAL A O 951 C CB . VAL A 127 ? 0.7560 0.9471 0.6732 0.3405 -0.2387 -0.0446 127 VAL A CB 952 C CG1 . VAL A 127 ? 0.8265 0.9877 0.7025 0.3926 -0.2519 -0.0396 127 VAL A CG1 953 C CG2 . VAL A 127 ? 0.7759 0.8788 0.5995 0.3136 -0.2300 -0.0397 127 VAL A CG2 954 N N . THR A 128 ? 0.6253 0.9885 0.7612 0.2679 -0.2107 -0.0576 128 THR A N 955 C CA . THR A 128 ? 0.6004 0.9911 0.7828 0.2230 -0.2091 -0.0648 128 THR A CA 956 C C . THR A 128 ? 0.6283 1.0395 0.8301 0.2186 -0.2604 -0.0820 128 THR A C 957 O O . THR A 128 ? 0.6510 1.0924 0.8747 0.2505 -0.2977 -0.0895 128 THR A O 958 C CB . THR A 128 ? 0.5541 1.0162 0.8365 0.2033 -0.1729 -0.0606 128 THR A CB 959 O OG1 . THR A 128 ? 0.5415 1.0042 0.8450 0.1583 -0.1658 -0.0644 128 THR A OG1 960 C CG2 . THR A 128 ? 0.5437 1.1003 0.9366 0.2212 -0.1874 -0.0676 128 THR A CG2 961 N N . TYR A 129 ? 0.6247 1.0149 0.8139 0.1819 -0.2648 -0.0896 129 TYR A N 962 C CA . TYR A 129 ? 0.6671 1.0654 0.8630 0.1760 -0.3157 -0.1090 129 TYR A CA 963 C C . TYR A 129 ? 0.6384 1.1201 0.9573 0.1456 -0.3250 -0.1220 129 TYR A C 964 O O . TYR A 129 ? 0.5903 1.0752 0.9385 0.1080 -0.2944 -0.1196 129 TYR A O 965 C CB . TYR A 129 ? 0.7052 1.0137 0.7922 0.1617 -0.3209 -0.1123 129 TYR A CB 966 C CG . TYR A 129 ? 0.7700 1.0724 0.8454 0.1569 -0.3739 -0.1345 129 TYR A CG 967 C CD1 . TYR A 129 ? 0.8359 1.1371 0.8856 0.1931 -0.4279 -0.1446 129 TYR A CD1 968 C CD2 . TYR A 129 ? 0.7751 1.0673 0.8599 0.1186 -0.3735 -0.1468 129 TYR A CD2 969 C CE1 . TYR A 129 ? 0.9036 1.1926 0.9334 0.1910 -0.4832 -0.1675 129 TYR A CE1 970 C CE2 . TYR A 129 ? 0.8344 1.1125 0.8999 0.1149 -0.4262 -0.1706 129 TYR A CE2 971 C CZ . TYR A 129 ? 0.8956 1.1720 0.9321 0.1510 -0.4821 -0.1813 129 TYR A CZ 972 O OH . TYR A 129 ? 0.9791 1.2357 0.9876 0.1503 -0.5404 -0.2069 129 TYR A OH 973 N N . GLU A 130 ? 0.6690 1.2163 1.0618 0.1631 -0.3694 -0.1360 130 GLU A N 974 C CA . GLU A 130 ? 0.6613 1.2954 1.1866 0.1345 -0.3858 -0.1510 130 GLU A CA 975 C C . GLU A 130 ? 0.7162 1.3228 1.2161 0.1150 -0.4413 -0.1758 130 GLU A C 976 O O . GLU A 130 ? 0.7691 1.3730 1.2462 0.1421 -0.5013 -0.1916 130 GLU A O 977 C CB . GLU A 130 ? 0.6632 1.3916 1.2962 0.1658 -0.4056 -0.1544 130 GLU A CB 978 C CG . GLU A 130 ? 0.6355 1.4707 1.4337 0.1363 -0.3901 -0.1591 130 GLU A CG 979 C CD . GLU A 130 ? 0.6385 1.5592 1.5327 0.1720 -0.3747 -0.1512 130 GLU A CD 980 O OE1 . GLU A 130 ? 0.6664 1.6661 1.6597 0.1884 -0.4229 -0.1679 130 GLU A OE1 981 O OE2 . GLU A 130 ? 0.6155 1.5222 1.4837 0.1863 -0.3163 -0.1296 130 GLU A OE2 982 N N . LEU A 131 ? 0.7101 1.2889 1.2054 0.0711 -0.4223 -0.1796 131 LEU A N 983 C CA . LEU A 131 ? 0.7708 1.3034 1.2200 0.0523 -0.4676 -0.2033 131 LEU A CA 984 C C . LEU A 131 ? 0.8045 1.4067 1.3523 0.0480 -0.5331 -0.2305 131 LEU A C 985 O O . LEU A 131 ? 0.8798 1.4460 1.3647 0.0672 -0.5950 -0.2506 131 LEU A O 986 C CB . LEU A 131 ? 0.7520 1.2470 1.1921 0.0069 -0.4299 -0.2017 131 LEU A CB 987 C CG . LEU A 131 ? 0.8230 1.2270 1.1555 -0.0044 -0.4524 -0.2182 131 LEU A CG 988 C CD1 . LEU A 131 ? 0.7925 1.1609 1.1171 -0.0406 -0.4021 -0.2097 131 LEU A CD1 989 C CD2 . LEU A 131 ? 0.8818 1.2937 1.2356 -0.0127 -0.5246 -0.2520 131 LEU A CD2 990 N N . SER A 132 ? 0.7566 1.4562 1.4582 0.0232 -0.5193 -0.2312 132 SER A N 991 C CA . SER A 132 ? 0.7751 1.5557 1.6022 0.0098 -0.5784 -0.2582 132 SER A CA 992 C C . SER A 132 ? 0.8134 1.6349 1.6545 0.0602 -0.6388 -0.2687 132 SER A C 993 O O . SER A 132 ? 0.8713 1.7044 1.7296 0.0637 -0.7152 -0.2977 132 SER A O 994 C CB . SER A 132 ? 0.7156 1.5942 1.7118 -0.0276 -0.5363 -0.2511 132 SER A CB 995 O OG . SER A 132 ? 0.6911 1.5231 1.6619 -0.0677 -0.4767 -0.2368 132 SER A OG 996 N N . ARG A 133 ? 0.7826 1.6193 1.6098 0.1012 -0.6071 -0.2459 133 ARG A N 997 C CA . ARG A 133 ? 0.8166 1.6881 1.6530 0.1562 -0.6569 -0.2513 133 ARG A CA 998 C C . ARG A 133 ? 0.8940 1.6539 1.5490 0.1978 -0.6947 -0.2522 133 ARG A C 999 O O . ARG A 133 ? 0.9376 1.7058 1.5738 0.2487 -0.7369 -0.2542 133 ARG A O 1000 C CB . ARG A 133 ? 0.7607 1.6951 1.6653 0.1838 -0.6031 -0.2271 133 ARG A CB 1001 N N . GLU A 134 ? 0.9143 1.5684 1.4367 0.1778 -0.6762 -0.2492 134 GLU A N 1002 C CA . GLU A 134 ? 0.9967 1.5340 1.3387 0.2116 -0.6991 -0.2471 134 GLU A CA 1003 C C . GLU A 134 ? 0.9997 1.5158 1.2843 0.2631 -0.6797 -0.2235 134 GLU A C 1004 O O . GLU A 134 ? 1.0827 1.5542 1.2833 0.3089 -0.7279 -0.2270 134 GLU A O 1005 C CB . GLU A 134 ? 1.0985 1.6154 1.4051 0.2256 -0.7901 -0.2787 134 GLU A CB 1006 C CG . GLU A 134 ? 1.2068 1.5856 1.3124 0.2490 -0.8073 -0.2787 134 GLU A CG 1007 C CD . GLU A 134 ? 1.3161 1.6601 1.3731 0.2539 -0.8927 -0.3130 134 GLU A CD 1008 O OE1 . GLU A 134 ? 1.3713 1.7711 1.4881 0.2816 -0.9671 -0.3319 134 GLU A OE1 1009 O OE2 . GLU A 134 ? 1.3891 1.6453 1.3422 0.2326 -0.8868 -0.3219 134 GLU A OE2 1010 N N . ARG A 135 ? 0.9171 1.4578 1.2407 0.2561 -0.6100 -0.1997 135 ARG A N 1011 C CA . ARG A 135 ? 0.9124 1.4531 1.2169 0.3016 -0.5892 -0.1799 135 ARG A CA 1012 C C . ARG A 135 ? 0.8543 1.3556 1.1177 0.2888 -0.5104 -0.1540 135 ARG A C 1013 O O . ARG A 135 ? 0.7854 1.3158 1.1076 0.2476 -0.4660 -0.1497 135 ARG A O 1014 C CB . ARG A 135 ? 0.8842 1.5497 1.3479 0.3202 -0.6056 -0.1860 135 ARG A CB 1015 C CG . ARG A 135 ? 0.8953 1.5674 1.3491 0.3750 -0.5926 -0.1698 135 ARG A CG 1016 C CD . ARG A 135 ? 0.8645 1.6702 1.4913 0.3928 -0.6045 -0.1774 135 ARG A CD 1017 N NE . ARG A 135 ? 0.7729 1.6557 1.5217 0.3535 -0.5411 -0.1700 135 ARG A NE 1018 C CZ . ARG A 135 ? 0.7343 1.7398 1.6570 0.3387 -0.5467 -0.1813 135 ARG A CZ 1019 N NH1 . ARG A 135 ? 0.7573 1.8311 1.7641 0.3589 -0.6190 -0.2037 135 ARG A NH1 1020 N NH2 . ARG A 135 ? 0.6589 1.7174 1.6724 0.3035 -0.4804 -0.1703 135 ARG A NH2 1021 N N . TRP A 136 ? 0.8882 1.3193 1.0489 0.3251 -0.4967 -0.1373 136 TRP A N 1022 C CA . TRP A 136 ? 0.8407 1.2413 0.9722 0.3221 -0.4312 -0.1149 136 TRP A CA 1023 C C . TRP A 136 ? 0.8191 1.2880 1.0320 0.3555 -0.4170 -0.1079 136 TRP A C 1024 O O . TRP A 136 ? 0.8719 1.3543 1.0865 0.4021 -0.4557 -0.1115 136 TRP A O 1025 C CB . TRP A 136 ? 0.8988 1.1798 0.8765 0.3396 -0.4221 -0.1016 136 TRP A CB 1026 C CG . TRP A 136 ? 0.9195 1.1300 0.8174 0.3050 -0.4126 -0.1035 136 TRP A CG 1027 C CD1 . TRP A 136 ? 0.9791 1.1505 0.8185 0.3032 -0.4540 -0.1175 136 TRP A CD1 1028 C CD2 . TRP A 136 ? 0.8665 1.0354 0.7327 0.2704 -0.3584 -0.0918 136 TRP A CD2 1029 N NE1 . TRP A 136 ? 0.9736 1.0819 0.7476 0.2701 -0.4230 -0.1146 136 TRP A NE1 1030 C CE2 . TRP A 136 ? 0.9045 1.0145 0.7000 0.2494 -0.3657 -0.0989 136 TRP A CE2 1031 C CE3 . TRP A 136 ? 0.8139 0.9879 0.7029 0.2575 -0.3068 -0.0774 136 TRP A CE3 1032 C CZ2 . TRP A 136 ? 0.8739 0.9386 0.6333 0.2166 -0.3212 -0.0913 136 TRP A CZ2 1033 C CZ3 . TRP A 136 ? 0.7857 0.9134 0.6367 0.2240 -0.2692 -0.0707 136 TRP A CZ3 1034 C CH2 . TRP A 136 ? 0.8176 0.8955 0.6105 0.2042 -0.2758 -0.0774 136 TRP A CH2 1035 N N . VAL A 137 ? 0.7497 1.2574 1.0245 0.3352 -0.3618 -0.0979 137 VAL A N 1036 C CA . VAL A 137 ? 0.7291 1.3081 1.0908 0.3633 -0.3383 -0.0920 137 VAL A CA 1037 C C . VAL A 137 ? 0.7318 1.2481 1.0181 0.3800 -0.2887 -0.0736 137 VAL A C 1038 O O . VAL A 137 ? 0.6981 1.1649 0.9352 0.3476 -0.2511 -0.0650 137 VAL A O 1039 C CB . VAL A 137 ? 0.6650 1.3471 1.1708 0.3296 -0.3111 -0.0957 137 VAL A CB 1040 C CG1 . VAL A 137 ? 0.6628 1.4422 1.2852 0.3653 -0.3098 -0.0975 137 VAL A CG1 1041 C CG2 . VAL A 137 ? 0.6593 1.3716 1.2153 0.2885 -0.3470 -0.1131 137 VAL A CG2 1042 N N . PRO A 138 ? 0.7712 1.2875 1.0488 0.4320 -0.2913 -0.0692 138 PRO A N 1043 C CA . PRO A 138 ? 0.7880 1.2414 0.9942 0.4513 -0.2488 -0.0549 138 PRO A CA 1044 C C . PRO A 138 ? 0.7418 1.2390 1.0095 0.4334 -0.1913 -0.0484 138 PRO A C 1045 O O . PRO A 138 ? 0.7098 1.3051 1.0964 0.4334 -0.1805 -0.0522 138 PRO A O 1046 C CB . PRO A 138 ? 0.8507 1.3098 1.0550 0.5150 -0.2716 -0.0554 138 PRO A CB 1047 C CG . PRO A 138 ? 0.8676 1.3653 1.1068 0.5283 -0.3342 -0.0684 138 PRO A CG 1048 C CD . PRO A 138 ? 0.8079 1.3803 1.1418 0.4782 -0.3384 -0.0789 138 PRO A CD 1049 N N . GLN A 139 ? 0.7458 1.1681 0.9318 0.4183 -0.1553 -0.0385 139 GLN A N 1050 C CA . GLN A 139 ? 0.7201 1.1607 0.9342 0.4033 -0.1022 -0.0312 139 GLN A CA 1051 C C . GLN A 139 ? 0.7649 1.1719 0.9368 0.4468 -0.0734 -0.0253 139 GLN A C 1052 O O . GLN A 139 ? 0.7597 1.1956 0.9654 0.4500 -0.0296 -0.0203 139 GLN A O 1053 C CB . GLN A 139 ? 0.6948 1.0769 0.8507 0.3567 -0.0857 -0.0267 139 GLN A CB 1054 C CG . GLN A 139 ? 0.6720 1.0781 0.8626 0.3117 -0.1058 -0.0327 139 GLN A CG 1055 C CD . GLN A 139 ? 0.6297 1.1158 0.9241 0.2836 -0.0818 -0.0327 139 GLN A CD 1056 O OE1 . GLN A 139 ? 0.6467 1.2114 1.0329 0.3005 -0.0736 -0.0340 139 GLN A OE1 1057 N NE2 . GLN A 139 ? 0.5729 1.0386 0.8569 0.2410 -0.0687 -0.0304 139 GLN A NE2 1058 N N . ARG A 140 ? 0.8196 1.1562 0.9086 0.4806 -0.0958 -0.0254 140 ARG A N 1059 C CA . ARG A 140 ? 0.8709 1.1689 0.9160 0.5281 -0.0757 -0.0225 140 ARG A CA 1060 C C . ARG A 140 ? 0.9290 1.2453 0.9898 0.5798 -0.1111 -0.0267 140 ARG A C 1061 O O . ARG A 140 ? 0.9228 1.2702 1.0140 0.5747 -0.1536 -0.0317 140 ARG A O 1062 C CB . ARG A 140 ? 0.9060 1.0843 0.8263 0.5198 -0.0659 -0.0185 140 ARG A CB 1063 C CG . ARG A 140 ? 0.9310 1.0282 0.7684 0.5131 -0.1013 -0.0175 140 ARG A CG 1064 C CD . ARG A 140 ? 0.9628 0.9510 0.6975 0.4991 -0.0882 -0.0143 140 ARG A CD 1065 N NE . ARG A 140 ? 0.8829 0.8673 0.6197 0.4455 -0.0739 -0.0135 140 ARG A NE 1066 C CZ . ARG A 140 ? 0.8993 0.8033 0.5673 0.4178 -0.0733 -0.0119 140 ARG A CZ 1067 N NH1 . ARG A 140 ? 0.9677 0.7835 0.5568 0.4338 -0.0839 -0.0101 140 ARG A NH1 1068 N NH2 . ARG A 140 ? 0.8276 0.7391 0.5099 0.3737 -0.0623 -0.0119 140 ARG A NH2 1069 N N . SER A 141 ? 0.9928 1.2867 1.0296 0.6322 -0.0966 -0.0257 141 SER A N 1070 C CA . SER A 141 ? 1.0501 1.3724 1.1156 0.6889 -0.1295 -0.0296 141 SER A CA 1071 C C . SER A 141 ? 1.1417 1.3483 1.0842 0.7258 -0.1558 -0.0266 141 SER A C 1072 O O . SER A 141 ? 1.2012 1.4122 1.1495 0.7851 -0.1698 -0.0282 141 SER A O 1073 C CB . SER A 141 ? 1.0531 1.4669 1.2202 0.7310 -0.0978 -0.0320 141 SER A CB 1074 O OG . SER A 141 ? 1.1025 1.4548 1.2038 0.7556 -0.0521 -0.0284 141 SER A OG 1075 N N . THR A 142 ? 1.1611 1.2659 0.9981 0.6914 -0.1620 -0.0216 142 THR A N 1076 C CA . THR A 142 ? 1.2541 1.2378 0.9697 0.7181 -0.1827 -0.0163 142 THR A CA 1077 C C . THR A 142 ? 1.2816 1.2273 0.9499 0.7079 -0.2280 -0.0128 142 THR A C 1078 O O . THR A 142 ? 1.2314 1.2488 0.9633 0.6834 -0.2497 -0.0175 142 THR A O 1079 C CB . THR A 142 ? 1.2855 1.1600 0.9025 0.6969 -0.1513 -0.0125 142 THR A CB 1080 O OG1 . THR A 142 ? 1.3941 1.1539 0.9049 0.7302 -0.1661 -0.0075 142 THR A OG1 1081 C CG2 . THR A 142 ? 1.2263 1.0792 0.8244 0.6280 -0.1444 -0.0101 142 THR A CG2 1082 N N . LEU A 143 ? 1.3710 1.1972 0.9224 0.7278 -0.2404 -0.0047 143 LEU A N 1083 C CA . LEU A 143 ? 1.4248 1.1919 0.9055 0.7292 -0.2789 0.0016 143 LEU A CA 1084 C C . LEU A 143 ? 1.3784 1.1330 0.8417 0.6651 -0.2747 0.0036 143 LEU A C 1085 O O . LEU A 143 ? 1.3792 1.1615 0.8524 0.6595 -0.3074 0.0011 143 LEU A O 1086 C CB . LEU A 143 ? 1.5432 1.1701 0.8942 0.7606 -0.2814 0.0131 143 LEU A CB 1087 C CG . LEU A 143 ? 1.6288 1.1604 0.8745 0.7611 -0.3093 0.0248 143 LEU A CG 1088 C CD1 . LEU A 143 ? 1.6971 1.2505 0.9430 0.8223 -0.3620 0.0238 143 LEU A CD1 1089 C CD2 . LEU A 143 ? 1.7284 1.1110 0.8508 0.7599 -0.2870 0.0381 143 LEU A CD2 1090 N N . LEU A 144 ? 1.3401 1.0506 0.7758 0.6197 -0.2371 0.0068 144 LEU A N 1091 C CA . LEU A 144 ? 1.2918 0.9877 0.7128 0.5617 -0.2289 0.0089 144 LEU A CA 1092 C C . LEU A 144 ? 1.2083 1.0193 0.7304 0.5390 -0.2404 -0.0013 144 LEU A C 1093 O O . LEU A 144 ? 1.2048 1.0129 0.7128 0.5138 -0.2558 -0.0020 144 LEU A O 1094 C CB . LEU A 144 ? 1.2656 0.9139 0.6639 0.5196 -0.1898 0.0113 144 LEU A CB 1095 C CG . LEU A 144 ? 1.2062 0.8535 0.6093 0.4596 -0.1754 0.0122 144 LEU A CG 1096 C CD1 . LEU A 144 ? 1.2606 0.8126 0.5722 0.4480 -0.1788 0.0232 144 LEU A CD1 1097 C CD2 . LEU A 144 ? 1.1607 0.8006 0.5803 0.4259 -0.1436 0.0096 144 LEU A CD2 1098 N N . ALA A 145 ? 1.1466 1.0530 0.7671 0.5487 -0.2306 -0.0091 145 ALA A N 1099 C CA . ALA A 145 ? 1.0724 1.0913 0.8010 0.5281 -0.2400 -0.0189 145 ALA A CA 1100 C C . ALA A 145 ? 1.1001 1.1606 0.8556 0.5566 -0.2911 -0.0258 145 ALA A C 1101 O O . ALA A 145 ? 1.0637 1.1693 0.8593 0.5290 -0.3113 -0.0338 145 ALA A O 1102 C CB . ALA A 145 ? 1.0141 1.1170 0.8377 0.5333 -0.2102 -0.0227 145 ALA A CB 1103 N N . LYS A 146 ? 1.1795 1.2213 0.9108 0.6140 -0.3148 -0.0241 146 LYS A N 1104 C CA . LYS A 146 ? 1.2242 1.3037 0.9792 0.6507 -0.3714 -0.0318 146 LYS A CA 1105 C C . LYS A 146 ? 1.2919 1.2822 0.9358 0.6424 -0.4034 -0.0281 146 LYS A C 1106 O O . LYS A 146 ? 1.3015 1.3307 0.9703 0.6412 -0.4474 -0.0389 146 LYS A O 1107 C CB . LYS A 146 ? 1.2912 1.3686 1.0461 0.7205 -0.3863 -0.0298 146 LYS A CB 1108 C CG . LYS A 146 ? 1.3481 1.4647 1.1296 0.7681 -0.4514 -0.0383 146 LYS A CG 1109 C CD . LYS A 146 ? 1.4213 1.5206 1.1897 0.8414 -0.4629 -0.0344 146 LYS A CD 1110 C CE . LYS A 146 ? 1.5022 1.6130 1.2667 0.8945 -0.5359 -0.0408 146 LYS A CE 1111 N NZ . LYS A 146 ? 1.5874 1.6628 1.3209 0.9704 -0.5485 -0.0351 146 LYS A NZ 1112 N N . VAL A 147 ? 1.3471 1.2149 0.8677 0.6360 -0.3796 -0.0135 147 VAL A N 1113 C CA . VAL A 147 ? 1.4260 1.1912 0.8248 0.6299 -0.3964 -0.0055 147 VAL A CA 1114 C C . VAL A 147 ? 1.3739 1.1569 0.7850 0.5720 -0.3873 -0.0115 147 VAL A C 1115 O O . VAL A 147 ? 1.4214 1.1930 0.7974 0.5738 -0.4237 -0.0173 147 VAL A O 1116 C CB . VAL A 147 ? 1.5019 1.1324 0.7782 0.6339 -0.3640 0.0134 147 VAL A CB 1117 C CG1 . VAL A 147 ? 1.5799 1.1066 0.7385 0.6134 -0.3625 0.0242 147 VAL A CG1 1118 C CG2 . VAL A 147 ? 1.5768 1.1643 0.8122 0.6993 -0.3829 0.0196 147 VAL A CG2 1119 N N . MET A 148 ? 1.2801 1.0872 0.7364 0.5245 -0.3415 -0.0110 148 MET A N 1120 C CA . MET A 148 ? 1.2274 1.0492 0.6984 0.4716 -0.3282 -0.0162 148 MET A CA 1121 C C . MET A 148 ? 1.1864 1.1084 0.7498 0.4638 -0.3631 -0.0343 148 MET A C 1122 O O . MET A 148 ? 1.2028 1.1082 0.7363 0.4396 -0.3776 -0.0411 148 MET A O 1123 C CB . MET A 148 ? 1.1429 0.9769 0.6529 0.4293 -0.2770 -0.0127 148 MET A CB 1124 C CG . MET A 148 ? 1.0867 0.9324 0.6123 0.3778 -0.2611 -0.0172 148 MET A CG 1125 S SD . MET A 148 ? 1.0285 0.8545 0.5655 0.3350 -0.2066 -0.0099 148 MET A SD 1126 C CE . MET A 148 ? 1.1339 0.8293 0.5483 0.3461 -0.1911 0.0063 148 MET A CE 1127 N N . SER A 149 ? 1.1477 1.1713 0.8248 0.4831 -0.3734 -0.0426 149 SER A N 1128 C CA . SER A 149 ? 1.1130 1.2425 0.9008 0.4727 -0.4047 -0.0603 149 SER A CA 1129 C C . SER A 149 ? 1.1978 1.3185 0.9529 0.5044 -0.4712 -0.0713 149 SER A C 1130 O O . SER A 149 ? 1.1914 1.3509 0.9835 0.4822 -0.5021 -0.0872 149 SER A O 1131 C CB . SER A 149 ? 1.0585 1.2932 0.9745 0.4876 -0.3923 -0.0638 149 SER A CB 1132 O OG . SER A 149 ? 1.0252 1.3662 1.0638 0.4672 -0.4131 -0.0798 149 SER A OG 1133 N N . ASN A 150 ? 1.2870 1.3497 0.9666 0.5572 -0.4952 -0.0635 150 ASN A N 1134 C CA . ASN A 150 ? 1.3863 1.4322 1.0228 0.5981 -0.5644 -0.0728 150 ASN A CA 1135 C C . ASN A 150 ? 1.4695 1.4072 0.9663 0.5851 -0.5784 -0.0708 150 ASN A C 1136 O O . ASN A 150 ? 1.5231 1.4720 1.0107 0.5906 -0.6366 -0.0885 150 ASN A O 1137 C CB . ASN A 150 ? 1.4645 1.4773 1.0608 0.6646 -0.5847 -0.0632 150 ASN A CB 1138 C CG . ASN A 150 ? 1.4134 1.5515 1.1600 0.6932 -0.5954 -0.0727 150 ASN A CG 1139 O OD1 . ASN A 150 ? 1.3381 1.6006 1.2318 0.6618 -0.5999 -0.0894 150 ASN A OD1 1140 N ND2 . ASN A 150 ? 1.4759 1.5794 1.1887 0.7534 -0.5956 -0.0614 150 ASN A ND2 1141 N N . THR A 151 ? 1.4940 1.3245 0.8817 0.5692 -0.5247 -0.0499 151 THR A N 1142 C CA . THR A 151 ? 1.5694 1.2916 0.8234 0.5530 -0.5190 -0.0439 151 THR A CA 1143 C C . THR A 151 ? 1.5102 1.2765 0.8104 0.5032 -0.5165 -0.0603 151 THR A C 1144 O O . THR A 151 ? 1.5834 1.3031 0.8087 0.5043 -0.5472 -0.0692 151 THR A O 1145 C CB . THR A 151 ? 1.5889 1.2085 0.7521 0.5367 -0.4553 -0.0197 151 THR A CB 1146 O OG1 . THR A 151 ? 1.6451 1.2261 0.7775 0.5792 -0.4537 -0.0058 151 THR A OG1 1147 C CG2 . THR A 151 ? 1.6915 1.1903 0.7078 0.5302 -0.4461 -0.0098 151 THR A CG2 1148 N N . LEU A 152 ? 1.3895 1.2378 0.8046 0.4621 -0.4800 -0.0643 152 LEU A N 1149 C CA . LEU A 152 ? 1.3325 1.2188 0.7944 0.4143 -0.4732 -0.0786 152 LEU A CA 1150 C C . LEU A 152 ? 1.3394 1.2990 0.8704 0.4188 -0.5365 -0.1043 152 LEU A C 1151 O O . LEU A 152 ? 1.3704 1.3016 0.8596 0.4000 -0.5559 -0.1178 152 LEU A O 1152 C CB . LEU A 152 ? 1.2108 1.1553 0.7677 0.3723 -0.4183 -0.0740 152 LEU A CB 1153 C CG . LEU A 152 ? 1.1992 1.0682 0.6897 0.3508 -0.3586 -0.0550 152 LEU A CG 1154 C CD1 . LEU A 152 ? 1.0905 1.0211 0.6760 0.3227 -0.3165 -0.0513 152 LEU A CD1 1155 C CD2 . LEU A 152 ? 1.2228 1.0232 0.6338 0.3233 -0.3435 -0.0558 152 LEU A CD2 1156 N N . THR A 153 ? 1.3167 1.3688 0.9547 0.4440 -0.5684 -0.1120 153 THR A N 1157 C CA . THR A 153 ? 1.3278 1.4627 1.0554 0.4468 -0.6316 -0.1379 153 THR A CA 1158 C C . THR A 153 ? 1.4652 1.5277 1.0786 0.4837 -0.6989 -0.1483 153 THR A C 1159 O O . THR A 153 ? 1.4948 1.5700 1.1163 0.4695 -0.7451 -0.1714 153 THR A O 1160 C CB . THR A 153 ? 1.2740 1.5300 1.1526 0.4688 -0.6463 -0.1426 153 THR A CB 1161 O OG1 . THR A 153 ? 1.1657 1.4670 1.1201 0.4425 -0.5784 -0.1291 153 THR A OG1 1162 C CG2 . THR A 153 ? 1.2540 1.6126 1.2590 0.4554 -0.7021 -0.1705 153 THR A CG2 1163 N N . ASP A 154 ? 1.5628 1.5409 1.0620 0.5312 -0.7042 -0.1313 154 ASP A N 1164 C CA . ASP A 154 ? 1.7197 1.6067 1.0816 0.5736 -0.7645 -0.1362 154 ASP A CA 1165 C C . ASP A 154 ? 1.7861 1.5723 1.0190 0.5465 -0.7517 -0.1384 154 ASP A C 1166 O O . ASP A 154 ? 1.8952 1.6364 1.0499 0.5650 -0.8111 -0.1552 154 ASP A O 1167 C CB . ASP A 154 ? 1.8104 1.6107 1.0634 0.6286 -0.7615 -0.1124 154 ASP A CB 1168 C CG . ASP A 154 ? 1.8150 1.6987 1.1646 0.6805 -0.8079 -0.1173 154 ASP A CG 1169 O OD1 . ASP A 154 ? 1.7682 1.7989 1.2887 0.6758 -0.8714 -0.1494 154 ASP A OD1 1170 O OD2 . ASP A 154 ? 1.8607 1.6958 1.1644 0.7213 -0.7792 -0.0927 154 ASP A OD2 1171 N N . LEU A 155 ? 1.7341 1.4840 0.9441 0.5051 -0.6750 -0.1225 155 LEU A N 1172 C CA . LEU A 155 ? 1.7804 1.4475 0.8890 0.4755 -0.6502 -0.1243 155 LEU A CA 1173 C C . LEU A 155 ? 1.7304 1.4691 0.9267 0.4389 -0.6788 -0.1541 155 LEU A C 1174 O O . LEU A 155 ? 1.6227 1.4143 0.9074 0.3917 -0.6347 -0.1557 155 LEU A O 1175 C CB . LEU A 155 ? 1.7272 1.3486 0.8084 0.4430 -0.5621 -0.0997 155 LEU A CB 1176 C CG . LEU A 155 ? 1.8433 1.3305 0.7658 0.4659 -0.5271 -0.0728 155 LEU A CG 1177 C CD1 . LEU A 155 ? 1.9334 1.3836 0.8009 0.5238 -0.5628 -0.0608 155 LEU A CD1 1178 C CD2 . LEU A 155 ? 1.7612 1.2332 0.7024 0.4281 -0.4450 -0.0523 155 LEU A CD2 1179 N N . ARG A 156 ? 1.8188 1.5537 0.9873 0.4625 -0.7569 -0.1783 156 ARG A N 1180 C CA . ARG A 156 ? 1.7874 1.5922 1.0472 0.4308 -0.7983 -0.2108 156 ARG A CA 1181 C C . ARG A 156 ? 1.7948 1.5355 0.9868 0.3904 -0.7606 -0.2169 156 ARG A C 1182 O O . ARG A 156 ? 1.7217 1.5258 1.0138 0.3477 -0.7602 -0.2357 156 ARG A O 1183 C CB . ARG A 156 ? 1.8968 1.7062 1.1370 0.4694 -0.8996 -0.2375 156 ARG A CB 1184 C CG . ARG A 156 ? 1.8659 1.7838 1.2371 0.5014 -0.9453 -0.2405 156 ARG A CG 1185 C CD . ARG A 156 ? 1.7567 1.8264 1.3420 0.4615 -0.9593 -0.2620 156 ARG A CD 1186 N NE . ARG A 156 ? 1.8202 1.9044 1.4259 0.4451 -1.0317 -0.2993 156 ARG A NE 1187 C CZ . ARG A 156 ? 1.9062 2.0293 1.5473 0.4772 -1.1273 -0.3253 156 ARG A CZ 1188 N NH1 . ARG A 156 ? 1.9427 2.0970 1.6041 0.5318 -1.1621 -0.3170 156 ARG A NH1 1189 N NH2 . ARG A 156 ? 1.9616 2.0903 1.6180 0.4562 -1.1919 -0.3613 156 ARG A NH2 1190 N N . ALA A 157 ? 1.8859 1.4988 0.9095 0.4050 -0.7255 -0.1999 157 ALA A N 1191 C CA . ALA A 157 ? 1.9007 1.4446 0.8507 0.3728 -0.6764 -0.2011 157 ALA A CA 1192 C C . ALA A 157 ? 1.7518 1.3552 0.8110 0.3248 -0.6003 -0.1876 157 ALA A C 1193 O O . ALA A 157 ? 1.7242 1.3317 0.8068 0.2885 -0.5786 -0.1999 157 ALA A O 1194 C CB . ALA A 157 ? 2.0379 1.4355 0.7907 0.4021 -0.6472 -0.1816 157 ALA A CB 1195 N N . VAL A 158 ? 1.6669 1.3109 0.7871 0.3273 -0.5628 -0.1635 158 VAL A N 1196 C CA . VAL A 158 ? 1.5270 1.2277 0.7490 0.2869 -0.4979 -0.1509 158 VAL A CA 1197 C C . VAL A 158 ? 1.4237 1.2372 0.7999 0.2556 -0.5187 -0.1707 158 VAL A C 1198 O O . VAL A 158 ? 1.3557 1.1901 0.7828 0.2165 -0.4817 -0.1731 158 VAL A O 1199 C CB . VAL A 158 ? 1.4815 1.1954 0.7282 0.3005 -0.4617 -0.1238 158 VAL A CB 1200 C CG1 . VAL A 158 ? 1.3345 1.1244 0.7035 0.2629 -0.4128 -0.1164 158 VAL A CG1 1201 C CG2 . VAL A 158 ? 1.5683 1.1656 0.6732 0.3177 -0.4225 -0.1005 158 VAL A CG2 1202 N N . SER A 159 ? 1.4177 1.3019 0.8691 0.2741 -0.5774 -0.1842 159 SER A N 1203 C CA . SER A 159 ? 1.3353 1.3295 0.9407 0.2457 -0.6006 -0.2031 159 SER A CA 1204 C C . SER A 159 ? 1.3603 1.3333 0.9542 0.2141 -0.6202 -0.2286 159 SER A C 1205 O O . SER A 159 ? 1.2794 1.3021 0.9664 0.1724 -0.5948 -0.2338 159 SER A O 1206 C CB . SER A 159 ? 1.3579 1.4229 1.0348 0.2777 -0.6668 -0.2152 159 SER A CB 1207 O OG . SER A 159 ? 1.2612 1.4474 1.1094 0.2560 -0.6578 -0.2172 159 SER A OG 1208 N N . GLY A 160 ? 1.4779 1.3678 0.9474 0.2364 -0.6652 -0.2443 160 GLY A N 1209 C CA . GLY A 160 ? 1.5280 1.3707 0.9513 0.2131 -0.6831 -0.2696 160 GLY A CA 1210 C C . GLY A 160 ? 1.4916 1.2825 0.8727 0.1838 -0.6077 -0.2570 160 GLY A C 1211 O O . GLY A 160 ? 1.4607 1.2674 0.8920 0.1476 -0.6003 -0.2725 160 GLY A O 1212 N N . PHE A 161 ? 1.4969 1.2265 0.7914 0.1994 -0.5523 -0.2292 161 PHE A N 1213 C CA . PHE A 161 ? 1.4667 1.1513 0.7275 0.1753 -0.4801 -0.2162 161 PHE A CA 1214 C C . PHE A 161 ? 1.3210 1.0926 0.7251 0.1358 -0.4414 -0.2097 161 PHE A C 1215 O O . PHE A 161 ? 1.3010 1.0597 0.7164 0.1076 -0.4107 -0.2152 161 PHE A O 1216 C CB . PHE A 161 ? 1.5097 1.1204 0.6672 0.1977 -0.4298 -0.1870 161 PHE A CB 1217 C CG . PHE A 161 ? 1.5239 1.0763 0.6305 0.1787 -0.3620 -0.1774 161 PHE A CG 1218 C CD1 . PHE A 161 ? 1.6617 1.1247 0.6518 0.1847 -0.3602 -0.1911 161 PHE A CD1 1219 C CD2 . PHE A 161 ? 1.4459 1.0328 0.6219 0.1569 -0.3015 -0.1563 161 PHE A CD2 1220 C CE1 . PHE A 161 ? 1.6676 1.0831 0.6209 0.1698 -0.2936 -0.1825 161 PHE A CE1 1221 C CE2 . PHE A 161 ? 1.4519 0.9946 0.5961 0.1408 -0.2417 -0.1487 161 PHE A CE2 1222 C CZ . PHE A 161 ? 1.5367 0.9970 0.5742 0.1476 -0.2353 -0.1611 161 PHE A CZ 1223 N N . LEU A 162 ? 1.2264 1.0809 0.7332 0.1373 -0.4430 -0.1980 162 LEU A N 1224 C CA . LEU A 162 ? 1.0971 1.0298 0.7307 0.1047 -0.4075 -0.1899 162 LEU A CA 1225 C C . LEU A 162 ? 1.0713 1.0540 0.7937 0.0732 -0.4343 -0.2131 162 LEU A C 1226 O O . LEU A 162 ? 1.0091 1.0089 0.7853 0.0416 -0.3977 -0.2099 162 LEU A O 1227 C CB . LEU A 162 ? 1.0306 1.0328 0.7414 0.1188 -0.4026 -0.1732 162 LEU A CB 1228 C CG . LEU A 162 ? 1.0132 0.9767 0.6692 0.1358 -0.3574 -0.1463 162 LEU A CG 1229 C CD1 . LEU A 162 ? 0.9726 0.9987 0.6972 0.1546 -0.3610 -0.1349 162 LEU A CD1 1230 C CD2 . LEU A 162 ? 0.9590 0.9063 0.6228 0.1071 -0.2981 -0.1342 162 LEU A CD2 1231 N N . GLU A 163 ? 1.1203 1.1238 0.8590 0.0819 -0.5003 -0.2367 163 GLU A N 1232 C CA . GLU A 163 ? 1.1140 1.1576 0.9353 0.0493 -0.5334 -0.2627 163 GLU A CA 1233 C C . GLU A 163 ? 1.1460 1.1165 0.9036 0.0255 -0.5123 -0.2740 163 GLU A C 1234 O O . GLU A 163 ? 1.0891 1.0893 0.9269 -0.0117 -0.4866 -0.2755 163 GLU A O 1235 C CB . GLU A 163 ? 1.1914 1.2528 1.0197 0.0664 -0.6167 -0.2901 163 GLU A CB 1236 N N . HIS A 164 ? 1.2414 1.1116 0.8505 0.0495 -0.5196 -0.2805 164 HIS A N 1237 C CA . HIS A 164 ? 1.2838 1.0753 0.8171 0.0351 -0.4940 -0.2907 164 HIS A CA 1238 C C . HIS A 164 ? 1.1983 0.9966 0.7670 0.0148 -0.4185 -0.2675 164 HIS A C 1239 O O . HIS A 164 ? 1.1877 0.9721 0.7782 -0.0115 -0.4009 -0.2770 164 HIS A O 1240 C CB . HIS A 164 ? 1.4049 1.0867 0.7679 0.0693 -0.4979 -0.2943 164 HIS A CB 1241 C CG . HIS A 164 ? 1.4730 1.0717 0.7543 0.0596 -0.4698 -0.3066 164 HIS A CG 1242 N ND1 . HIS A 164 ? 1.4664 1.0164 0.6909 0.0635 -0.3979 -0.2856 164 HIS A ND1 1243 C CD2 . HIS A 164 ? 1.5407 1.0982 0.7946 0.0461 -0.5030 -0.3388 164 HIS A CD2 1244 C CE1 . HIS A 164 ? 1.5168 1.0002 0.6803 0.0565 -0.3854 -0.3035 164 HIS A CE1 1245 N NE2 . HIS A 164 ? 1.5804 1.0622 0.7547 0.0460 -0.4485 -0.3362 164 HIS A NE2 1246 N N . ILE A 165 ? 1.1374 0.9526 0.7090 0.0287 -0.3782 -0.2383 165 ILE A N 1247 C CA . ILE A 165 ? 1.0657 0.8880 0.6680 0.0143 -0.3130 -0.2159 165 ILE A CA 1248 C C . ILE A 165 ? 0.9761 0.8649 0.7003 -0.0195 -0.3044 -0.2169 165 ILE A C 1249 O O . ILE A 165 ? 0.9577 0.8252 0.6890 -0.0382 -0.2729 -0.2170 165 ILE A O 1250 C CB . ILE A 165 ? 1.0206 0.8598 0.6209 0.0334 -0.2853 -0.1882 165 ILE A CB 1251 C CG1 . ILE A 165 ? 1.1141 0.8680 0.5865 0.0596 -0.2660 -0.1796 165 ILE A CG1 1252 C CG2 . ILE A 165 ? 0.9379 0.8150 0.6100 0.0152 -0.2360 -0.1685 165 ILE A CG2 1253 C CD1 . ILE A 165 ? 1.0710 0.8320 0.5451 0.0714 -0.2293 -0.1511 165 ILE A CD1 1254 N N . PHE A 166 ? 0.9307 0.8970 0.7490 -0.0253 -0.3312 -0.2170 166 PHE A N 1255 C CA . PHE A 166 ? 0.8548 0.8860 0.7904 -0.0560 -0.3160 -0.2125 166 PHE A CA 1256 C C . PHE A 166 ? 0.8828 0.9138 0.8598 -0.0859 -0.3449 -0.2377 166 PHE A C 1257 O O . PHE A 166 ? 0.8352 0.8915 0.8855 -0.1148 -0.3214 -0.2329 166 PHE A O 1258 C CB . PHE A 166 ? 0.7992 0.9146 0.8234 -0.0493 -0.3223 -0.2000 166 PHE A CB 1259 C CG . PHE A 166 ? 0.7569 0.8730 0.7552 -0.0264 -0.2863 -0.1739 166 PHE A CG 1260 C CD1 . PHE A 166 ? 0.7154 0.8204 0.7168 -0.0361 -0.2352 -0.1549 166 PHE A CD1 1261 C CD2 . PHE A 166 ? 0.7749 0.8984 0.7443 0.0059 -0.3072 -0.1694 166 PHE A CD2 1262 C CE1 . PHE A 166 ? 0.6940 0.7954 0.6718 -0.0174 -0.2071 -0.1340 166 PHE A CE1 1263 C CE2 . PHE A 166 ? 0.7334 0.8487 0.6755 0.0253 -0.2756 -0.1472 166 PHE A CE2 1264 C CZ . PHE A 166 ? 0.7147 0.8191 0.6619 0.0121 -0.2261 -0.1303 166 PHE A CZ 1265 N N . SER A 167 ? 0.9755 0.9719 0.9010 -0.0788 -0.3973 -0.2648 167 SER A N 1266 C CA . SER A 167 ? 1.0237 1.0107 0.9817 -0.1080 -0.4341 -0.2942 167 SER A CA 1267 C C . SER A 167 ? 1.0870 0.9799 0.9532 -0.1138 -0.4182 -0.3072 167 SER A C 1268 O O . SER A 167 ? 1.1143 0.9928 1.0154 -0.1440 -0.4270 -0.3246 167 SER A O 1269 C CB . SER A 167 ? 1.0943 1.0924 1.0481 -0.0974 -0.5103 -0.3223 167 SER A CB 1270 O OG . SER A 167 ? 1.0589 1.1436 1.0952 -0.0851 -0.5264 -0.3114 167 SER A OG 1271 N N . SER A 168 ? 1.1225 0.9482 0.8714 -0.0844 -0.3945 -0.2996 168 SER A N 1272 C CA . SER A 168 ? 1.2036 0.9355 0.8533 -0.0817 -0.3809 -0.3145 168 SER A CA 1273 C C . SER A 168 ? 1.1643 0.8677 0.7782 -0.0717 -0.3114 -0.2895 168 SER A C 1274 O O . SER A 168 ? 1.1613 0.8406 0.7873 -0.0868 -0.2805 -0.2903 168 SER A O 1275 C CB . SER A 168 ? 1.3295 0.9896 0.8533 -0.0534 -0.4243 -0.3368 168 SER A CB 1276 O OG . SER A 168 ? 1.4248 0.9878 0.8341 -0.0414 -0.3943 -0.3445 168 SER A OG 1277 N N . SER A 169 ? 1.1390 0.8459 0.7146 -0.0464 -0.2887 -0.2677 169 SER A N 1278 C CA . SER A 169 ? 1.1186 0.7915 0.6512 -0.0346 -0.2278 -0.2475 169 SER A CA 1279 C C . SER A 169 ? 1.0121 0.7350 0.6400 -0.0540 -0.1875 -0.2279 169 SER A C 1280 O O . SER A 169 ? 1.0138 0.7045 0.6335 -0.0586 -0.1530 -0.2275 169 SER A O 1281 C CB . SER A 169 ? 1.1380 0.7973 0.6077 -0.0063 -0.2160 -0.2297 169 SER A CB 1282 O OG . SER A 169 ? 1.2584 0.8474 0.6120 0.0165 -0.2463 -0.2468 169 SER A OG 1283 N N . PHE A 170 ? 0.9225 0.7200 0.6363 -0.0623 -0.1929 -0.2125 170 PHE A N 1284 C CA . PHE A 170 ? 0.8296 0.6686 0.6216 -0.0767 -0.1571 -0.1924 170 PHE A CA 1285 C C . PHE A 170 ? 0.8156 0.6559 0.6616 -0.1037 -0.1571 -0.2016 170 PHE A C 1286 O O . PHE A 170 ? 0.7822 0.6105 0.6422 -0.1076 -0.1220 -0.1908 170 PHE A O 1287 C CB . PHE A 170 ? 0.7554 0.6635 0.6103 -0.0741 -0.1574 -0.1727 170 PHE A CB 1288 C CG . PHE A 170 ? 0.7547 0.6545 0.5617 -0.0492 -0.1449 -0.1580 170 PHE A CG 1289 C CD1 . PHE A 170 ? 0.8220 0.6598 0.5438 -0.0338 -0.1250 -0.1581 170 PHE A CD1 1290 C CD2 . PHE A 170 ? 0.7109 0.6613 0.5584 -0.0414 -0.1485 -0.1432 170 PHE A CD2 1291 C CE1 . PHE A 170 ? 0.8420 0.6663 0.5214 -0.0145 -0.1097 -0.1427 170 PHE A CE1 1292 C CE2 . PHE A 170 ? 0.7441 0.6791 0.5456 -0.0195 -0.1371 -0.1296 170 PHE A CE2 1293 C CZ . PHE A 170 ? 0.7879 0.6589 0.5066 -0.0080 -0.1176 -0.1287 170 PHE A CZ 1294 N N . PRO A 171 ? 0.8372 0.6913 0.7174 -0.1224 -0.1973 -0.2211 171 PRO A N 1295 C CA . PRO A 171 ? 0.8477 0.6871 0.7691 -0.1506 -0.1981 -0.2321 171 PRO A CA 1296 C C . PRO A 171 ? 0.9136 0.6723 0.7677 -0.1472 -0.1802 -0.2448 171 PRO A C 1297 O O . PRO A 171 ? 0.8978 0.6447 0.7831 -0.1596 -0.1537 -0.2371 171 PRO A O 1298 C CB . PRO A 171 ? 0.8900 0.7506 0.8460 -0.1681 -0.2523 -0.2563 171 PRO A CB 1299 C CG . PRO A 171 ? 0.8483 0.7702 0.8302 -0.1530 -0.2692 -0.2466 171 PRO A CG 1300 C CD . PRO A 171 ? 0.8551 0.7447 0.7507 -0.1196 -0.2453 -0.2331 171 PRO A CD 1301 N N . ASN A 172 ? 0.9919 0.6911 0.7512 -0.1286 -0.1941 -0.2640 172 ASN A N 1302 C CA . ASN A 172 ? 1.0558 0.6760 0.7416 -0.1175 -0.1685 -0.2746 172 ASN A CA 1303 C C . ASN A 172 ? 1.0013 0.6247 0.6941 -0.1030 -0.1120 -0.2496 172 ASN A C 1304 O O . ASN A 172 ? 1.0125 0.6004 0.7043 -0.1036 -0.0867 -0.2515 172 ASN A O 1305 C CB . ASN A 172 ? 1.1615 0.7148 0.7313 -0.0943 -0.1870 -0.2961 172 ASN A CB 1306 C CG . ASN A 172 ? 1.2767 0.7932 0.8209 -0.1084 -0.2439 -0.3312 172 ASN A CG 1307 O OD1 . ASN A 172 ? 1.2779 0.8474 0.8939 -0.1300 -0.2863 -0.3376 172 ASN A OD1 1308 N ND2 . ASN A 172 ? 1.3979 0.8227 0.8415 -0.0957 -0.2450 -0.3556 172 ASN A ND2 1309 N N . TYR A 173 ? 0.9468 0.6122 0.6499 -0.0895 -0.0958 -0.2275 173 TYR A N 1310 C CA . TYR A 173 ? 0.9019 0.5802 0.6226 -0.0774 -0.0496 -0.2047 173 TYR A CA 1311 C C . TYR A 173 ? 0.8314 0.5441 0.6339 -0.0922 -0.0359 -0.1898 173 TYR A C 1312 O O . TYR A 173 ? 0.8277 0.5201 0.6359 -0.0850 -0.0063 -0.1848 173 TYR A O 1313 C CB . TYR A 173 ? 0.8740 0.5870 0.5894 -0.0644 -0.0446 -0.1870 173 TYR A CB 1314 C CG . TYR A 173 ? 0.8440 0.5649 0.5692 -0.0518 -0.0015 -0.1672 173 TYR A CG 1315 C CD1 . TYR A 173 ? 0.9045 0.5834 0.5998 -0.0399 0.0345 -0.1703 173 TYR A CD1 1316 C CD2 . TYR A 173 ? 0.7813 0.5515 0.5479 -0.0512 0.0024 -0.1469 173 TYR A CD2 1317 C CE1 . TYR A 173 ? 0.8762 0.5721 0.5980 -0.0307 0.0723 -0.1528 173 TYR A CE1 1318 C CE2 . TYR A 173 ? 0.7875 0.5658 0.5697 -0.0429 0.0359 -0.1312 173 TYR A CE2 1319 C CZ . TYR A 173 ? 0.8079 0.5531 0.5738 -0.0341 0.0698 -0.1342 173 TYR A CZ 1320 O OH . TYR A 173 ? 0.7959 0.5591 0.5946 -0.0286 0.1002 -0.1193 173 TYR A OH 1321 N N . ILE A 174 ? 0.7867 0.5486 0.6498 -0.1104 -0.0564 -0.1828 174 ILE A N 1322 C CA . ILE A 174 ? 0.7396 0.5259 0.6688 -0.1246 -0.0440 -0.1673 174 ILE A CA 1323 C C . ILE A 174 ? 0.7961 0.5283 0.7183 -0.1336 -0.0378 -0.1792 174 ILE A C 1324 O O . ILE A 174 ? 0.7804 0.5008 0.7193 -0.1279 -0.0133 -0.1666 174 ILE A O 1325 C CB . ILE A 174 ? 0.7075 0.5469 0.6970 -0.1449 -0.0654 -0.1620 174 ILE A CB 1326 C CG1 . ILE A 174 ? 0.6527 0.5445 0.6537 -0.1319 -0.0663 -0.1468 174 ILE A CG1 1327 C CG2 . ILE A 174 ? 0.6795 0.5259 0.7225 -0.1615 -0.0493 -0.1473 174 ILE A CG2 1328 C CD1 . ILE A 174 ? 0.6327 0.5802 0.6896 -0.1457 -0.0888 -0.1457 174 ILE A CD1 1329 N N . LEU A 175 ? 0.8608 0.5562 0.7546 -0.1454 -0.0636 -0.2046 175 LEU A N 1330 C CA . LEU A 175 ? 0.9257 0.5600 0.8056 -0.1562 -0.0641 -0.2209 175 LEU A CA 1331 C C . LEU A 175 ? 0.9627 0.5446 0.7943 -0.1304 -0.0321 -0.2226 175 LEU A C 1332 O O . LEU A 175 ? 0.9657 0.5186 0.8129 -0.1305 -0.0146 -0.2178 175 LEU A O 1333 C CB . LEU A 175 ? 0.9997 0.6012 0.8466 -0.1706 -0.1046 -0.2523 175 LEU A CB 1334 C CG . LEU A 175 ? 1.0067 0.6233 0.9182 -0.2082 -0.1326 -0.2602 175 LEU A CG 1335 C CD1 . LEU A 175 ? 0.8967 0.5997 0.8908 -0.2208 -0.1320 -0.2365 175 LEU A CD1 1336 C CD2 . LEU A 175 ? 1.0923 0.6772 0.9690 -0.2196 -0.1810 -0.2956 175 LEU A CD2 1337 N N . MET A 176 ? 0.9896 0.5588 0.7639 -0.1069 -0.0223 -0.2283 176 MET A N 1338 C CA . MET A 176 ? 1.0339 0.5637 0.7712 -0.0802 0.0148 -0.2290 176 MET A CA 1339 C C . MET A 176 ? 0.9556 0.5291 0.7531 -0.0695 0.0445 -0.2019 176 MET A C 1340 O O . MET A 176 ? 0.9681 0.5153 0.7726 -0.0551 0.0683 -0.2006 176 MET A O 1341 C CB . MET A 176 ? 1.0821 0.5847 0.7411 -0.0595 0.0230 -0.2397 176 MET A CB 1342 C CG . MET A 176 ? 1.2038 0.6462 0.7861 -0.0645 -0.0114 -0.2708 176 MET A CG 1343 S SD . MET A 176 ? 1.3144 0.6954 0.7717 -0.0355 -0.0022 -0.2862 176 MET A SD 1344 C CE . MET A 176 ? 1.4204 0.7140 0.8166 -0.0131 0.0377 -0.3039 176 MET A CE 1345 N N . LEU A 177 ? 0.8794 0.5166 0.7201 -0.0751 0.0392 -0.1819 177 LEU A N 1346 C CA . LEU A 177 ? 0.8188 0.4958 0.7114 -0.0652 0.0591 -0.1586 177 LEU A CA 1347 C C . LEU A 177 ? 0.8123 0.4835 0.7450 -0.0737 0.0564 -0.1494 177 LEU A C 1348 O O . LEU A 177 ? 0.8056 0.4754 0.7623 -0.0581 0.0729 -0.1388 177 LEU A O 1349 C CB . LEU A 177 ? 0.7494 0.4852 0.6668 -0.0688 0.0512 -0.1422 177 LEU A CB 1350 C CG . LEU A 177 ? 0.7573 0.5030 0.6419 -0.0575 0.0592 -0.1422 177 LEU A CG 1351 C CD1 . LEU A 177 ? 0.6834 0.4808 0.5954 -0.0633 0.0457 -0.1266 177 LEU A CD1 1352 C CD2 . LEU A 177 ? 0.7742 0.5112 0.6591 -0.0381 0.0942 -0.1386 177 LEU A CD2 1353 N N . HIS A 178 ? 0.8177 0.4853 0.7595 -0.0983 0.0349 -0.1528 178 HIS A N 1354 C CA . HIS A 178 ? 0.8258 0.4778 0.7978 -0.1107 0.0350 -0.1426 178 HIS A CA 1355 C C . HIS A 178 ? 0.8849 0.4704 0.8341 -0.0987 0.0478 -0.1526 178 HIS A C 1356 O O . HIS A 178 ? 0.8922 0.4644 0.8603 -0.0892 0.0588 -0.1377 178 HIS A O 1357 C CB . HIS A 178 ? 0.8432 0.5017 0.8327 -0.1432 0.0127 -0.1487 178 HIS A CB 1358 C CG . HIS A 178 ? 0.8693 0.5202 0.8952 -0.1606 0.0185 -0.1318 178 HIS A CG 1359 N ND1 . HIS A 178 ? 0.9846 0.5778 1.0074 -0.1788 0.0166 -0.1409 178 HIS A ND1 1360 C CD2 . HIS A 178 ? 0.8563 0.5415 0.9146 -0.1619 0.0286 -0.1056 178 HIS A CD2 1361 C CE1 . HIS A 178 ? 0.9971 0.5897 1.0509 -0.1918 0.0281 -0.1188 178 HIS A CE1 1362 N NE2 . HIS A 178 ? 0.9101 0.5578 0.9825 -0.1805 0.0359 -0.0971 178 HIS A NE2 1363 N N . GLU A 179 ? 0.9338 0.4731 0.8360 -0.0957 0.0455 -0.1781 179 GLU A N 1364 C CA . GLU A 179 ? 0.9964 0.4649 0.8668 -0.0805 0.0591 -0.1921 179 GLU A CA 1365 C C . GLU A 179 ? 0.9706 0.4431 0.8485 -0.0437 0.0893 -0.1838 179 GLU A C 1366 O O . GLU A 179 ? 1.0111 0.4388 0.8874 -0.0271 0.1019 -0.1852 179 GLU A O 1367 C CB . GLU A 179 ? 1.0725 0.4879 0.8795 -0.0859 0.0462 -0.2241 179 GLU A CB 1368 C CG . GLU A 179 ? 1.1570 0.5033 0.9087 -0.0577 0.0685 -0.2431 179 GLU A CG 1369 C CD . GLU A 179 ? 1.2765 0.5534 0.9540 -0.0661 0.0486 -0.2771 179 GLU A CD 1370 O OE1 . GLU A 179 ? 1.3355 0.6003 1.0195 -0.0989 0.0141 -0.2877 179 GLU A OE1 1371 O OE2 . GLU A 179 ? 1.3657 0.5972 0.9779 -0.0397 0.0676 -0.2942 179 GLU A OE2 1372 N N . GLU A 180 ? 0.9043 0.4309 0.7960 -0.0316 0.0998 -0.1752 180 GLU A N 1373 C CA . GLU A 180 ? 0.8773 0.4204 0.7885 -0.0004 0.1288 -0.1699 180 GLU A CA 1374 C C . GLU A 180 ? 0.7894 0.3872 0.7653 0.0067 0.1268 -0.1451 180 GLU A C 1375 O O . GLU A 180 ? 0.7739 0.3855 0.7847 0.0321 0.1436 -0.1400 180 GLU A O 1376 C CB . GLU A 180 ? 0.8731 0.4403 0.7609 0.0044 0.1425 -0.1748 180 GLU A CB 1377 C CG . GLU A 180 ? 0.9951 0.5034 0.8057 0.0081 0.1495 -0.1993 180 GLU A CG 1378 C CD . GLU A 180 ? 1.1084 0.5666 0.9000 0.0361 0.1813 -0.2118 180 GLU A CD 1379 O OE1 . GLU A 180 ? 1.1143 0.6046 0.9528 0.0583 0.2111 -0.2012 180 GLU A OE1 1380 O OE2 . GLU A 180 ? 1.1973 0.5847 0.9309 0.0363 0.1757 -0.2333 180 GLU A OE2 1381 N N . GLY A 181 ? 0.7120 0.3424 0.7044 -0.0142 0.1055 -0.1309 181 GLY A N 1382 C CA . GLY A 181 ? 0.6326 0.3133 0.6709 -0.0070 0.1008 -0.1099 181 GLY A CA 1383 C C . GLY A 181 ? 0.6121 0.2803 0.6657 -0.0071 0.0885 -0.0932 181 GLY A C 1384 O O . GLY A 181 ? 0.5544 0.2585 0.6292 -0.0071 0.0780 -0.0762 181 GLY A O 1385 N N . ARG A 182 ? 0.6462 0.2560 0.6816 -0.0058 0.0905 -0.0976 182 ARG A N 1386 C CA . ARG A 182 ? 0.6722 0.2565 0.7096 -0.0074 0.0820 -0.0791 182 ARG A CA 1387 C C . ARG A 182 ? 0.6571 0.2570 0.7204 0.0226 0.0772 -0.0626 182 ARG A C 1388 O O . ARG A 182 ? 0.6562 0.2505 0.7148 0.0222 0.0670 -0.0429 182 ARG A O 1389 C CB . ARG A 182 ? 0.7340 0.2430 0.7430 -0.0150 0.0856 -0.0863 182 ARG A CB 1390 C CG . ARG A 182 ? 0.7717 0.2677 0.7630 -0.0522 0.0797 -0.0989 182 ARG A CG 1391 C CD . ARG A 182 ? 0.8214 0.2409 0.7922 -0.0681 0.0801 -0.1015 182 ARG A CD 1392 N NE . ARG A 182 ? 0.9109 0.2717 0.8510 -0.0563 0.0855 -0.1256 182 ARG A NE 1393 C CZ . ARG A 182 ? 0.9703 0.2505 0.8867 -0.0570 0.0888 -0.1301 182 ARG A CZ 1394 N NH1 . ARG A 182 ? 0.9948 0.2410 0.9151 -0.0700 0.0892 -0.1091 182 ARG A NH1 1395 N NH2 . ARG A 182 ? 1.0291 0.2561 0.9117 -0.0425 0.0945 -0.1552 182 ARG A NH2 1396 N N . THR A 183 ? 0.6589 0.2792 0.7499 0.0490 0.0845 -0.0711 183 THR A N 1397 C CA . THR A 183 ? 0.6499 0.2960 0.7798 0.0790 0.0739 -0.0600 183 THR A CA 1398 C C . THR A 183 ? 0.6158 0.3072 0.7565 0.0720 0.0542 -0.0442 183 THR A C 1399 O O . THR A 183 ? 0.6102 0.2988 0.7571 0.0909 0.0353 -0.0304 183 THR A O 1400 C CB . THR A 183 ? 0.6338 0.3090 0.8092 0.1038 0.0895 -0.0741 183 THR A CB 1401 O OG1 . THR A 183 ? 0.5932 0.2913 0.8163 0.1342 0.0734 -0.0654 183 THR A OG1 1402 C CG2 . THR A 183 ? 0.5671 0.2960 0.7597 0.0886 0.1014 -0.0819 183 THR A CG2 1403 N N . ASP A 184 ? 0.4867 0.3828 0.3612 -0.0439 0.0997 -0.0710 184 ASP A N 1404 C CA . ASP A 184 ? 0.5067 0.3977 0.3871 -0.0410 0.0901 -0.0533 184 ASP A CA 1405 C C . ASP A 184 ? 0.5018 0.4024 0.3869 -0.0302 0.0634 -0.0462 184 ASP A C 1406 O O . ASP A 184 ? 0.4613 0.3739 0.3780 -0.0259 0.0540 -0.0405 184 ASP A O 1407 C CB . ASP A 184 ? 0.5746 0.4291 0.3985 -0.0477 0.1025 -0.0409 184 ASP A CB 1408 C CG . ASP A 184 ? 0.6120 0.4647 0.4435 -0.0684 0.1285 -0.0445 184 ASP A CG 1409 O OD1 . ASP A 184 ? 0.6950 0.5578 0.5600 -0.0695 0.1255 -0.0411 184 ASP A OD1 1410 O OD2 . ASP A 184 ? 0.6828 0.5294 0.4863 -0.0872 0.1526 -0.0531 184 ASP A OD2 1411 N N . LEU A 185 ? 0.5443 0.4488 0.3983 -0.0282 0.0519 -0.0495 185 LEU A N 1412 C CA . LEU A 185 ? 0.5462 0.4826 0.4062 -0.0224 0.0276 -0.0490 185 LEU A CA 1413 C C . LEU A 185 ? 0.5400 0.4951 0.4370 -0.0374 0.0217 -0.0609 185 LEU A C 1414 O O . LEU A 185 ? 0.5252 0.5135 0.4402 -0.0385 0.0072 -0.0601 185 LEU A O 1415 C CB . LEU A 185 ? 0.5880 0.5374 0.4032 -0.0177 0.0153 -0.0531 185 LEU A CB 1416 C CG . LEU A 185 ? 0.6376 0.5497 0.3930 -0.0008 0.0202 -0.0393 185 LEU A CG 1417 C CD1 . LEU A 185 ? 0.6653 0.5862 0.3722 0.0019 0.0100 -0.0467 185 LEU A CD1 1418 C CD2 . LEU A 185 ? 0.6491 0.5532 0.3887 0.0271 0.0082 -0.0220 185 LEU A CD2 1419 N N . GLU A 186 ? 0.5342 0.4642 0.4343 -0.0477 0.0336 -0.0730 186 GLU A N 1420 C CA . GLU A 186 ? 0.5351 0.4550 0.4493 -0.0602 0.0298 -0.0816 186 GLU A CA 1421 C C . GLU A 186 ? 0.5013 0.3997 0.4429 -0.0491 0.0375 -0.0785 186 GLU A C 1422 O O . GLU A 186 ? 0.5252 0.3919 0.4588 -0.0536 0.0368 -0.0858 186 GLU A O 1423 C CB . GLU A 186 ? 0.5879 0.4807 0.4655 -0.0785 0.0318 -0.1002 186 GLU A CB 1424 C CG . GLU A 186 ? 0.6075 0.5363 0.4609 -0.0956 0.0198 -0.1078 186 GLU A CG 1425 C CD . GLU A 186 ? 0.7109 0.6072 0.5203 -0.1197 0.0241 -0.1289 186 GLU A CD 1426 O OE1 . GLU A 186 ? 0.7861 0.6186 0.5759 -0.1220 0.0359 -0.1375 186 GLU A OE1 1427 O OE2 . GLU A 186 ? 0.8197 0.7528 0.6072 -0.1341 0.0142 -0.1383 186 GLU A OE2 1428 N N . ARG A 187 ? 0.4637 0.3752 0.4284 -0.0358 0.0444 -0.0689 187 ARG A N 1429 C CA . ARG A 187 ? 0.4355 0.3461 0.4305 -0.0247 0.0490 -0.0682 187 ARG A CA 1430 C C . ARG A 187 ? 0.4144 0.3264 0.4237 -0.0295 0.0356 -0.0599 187 ARG A C 1431 O O . ARG A 187 ? 0.3797 0.3118 0.3884 -0.0371 0.0269 -0.0524 187 ARG A O 1432 C CB . ARG A 187 ? 0.4278 0.3594 0.4390 -0.0219 0.0614 -0.0630 187 ARG A CB 1433 C CG . ARG A 187 ? 0.3897 0.3403 0.4381 -0.0135 0.0645 -0.0658 187 ARG A CG 1434 C CD . ARG A 187 ? 0.4111 0.3866 0.4693 -0.0242 0.0818 -0.0667 187 ARG A CD 1435 N NE . ARG A 187 ? 0.4328 0.3844 0.4620 -0.0361 0.0818 -0.0504 187 ARG A NE 1436 C CZ . ARG A 187 ? 0.3997 0.3449 0.4319 -0.0411 0.0799 -0.0402 187 ARG A CZ 1437 N NH1 . ARG A 187 ? 0.3892 0.3585 0.4573 -0.0420 0.0788 -0.0448 187 ARG A NH1 1438 N NH2 . ARG A 187 ? 0.4389 0.3492 0.4297 -0.0421 0.0792 -0.0266 187 ARG A NH2 1439 N N . ARG A 188 ? 0.4083 0.2999 0.4245 -0.0218 0.0335 -0.0628 188 ARG A N 1440 C CA . ARG A 188 ? 0.4097 0.2954 0.4323 -0.0285 0.0236 -0.0553 188 ARG A CA 1441 C C . ARG A 188 ? 0.3796 0.2648 0.4236 -0.0080 0.0234 -0.0540 188 ARG A C 1442 O O . ARG A 188 ? 0.3999 0.2651 0.4342 0.0125 0.0255 -0.0637 188 ARG A O 1443 C CB . ARG A 188 ? 0.4676 0.3085 0.4493 -0.0472 0.0199 -0.0622 188 ARG A CB 1444 C CG . ARG A 188 ? 0.5200 0.3768 0.4822 -0.0712 0.0196 -0.0698 188 ARG A CG 1445 C CD . ARG A 188 ? 0.6124 0.4279 0.5277 -0.1033 0.0198 -0.0812 188 ARG A CD 1446 N NE . ARG A 188 ? 0.8158 0.5560 0.6833 -0.0954 0.0270 -0.0916 188 ARG A NE 1447 C CZ . ARG A 188 ? 0.8976 0.6009 0.7154 -0.1200 0.0315 -0.1066 188 ARG A CZ 1448 N NH1 . ARG A 188 ? 0.9289 0.6789 0.7445 -0.1579 0.0283 -0.1148 188 ARG A NH1 1449 N NH2 . ARG A 188 ? 0.9347 0.5579 0.7024 -0.1041 0.0387 -0.1162 188 ARG A NH2 1450 N N . VAL A 189 ? 0.3299 0.2409 0.4005 -0.0096 0.0200 -0.0443 189 VAL A N 1451 C CA . VAL A 189 ? 0.3053 0.2263 0.3970 0.0063 0.0171 -0.0446 189 VAL A CA 1452 C C . VAL A 189 ? 0.2960 0.2060 0.3853 -0.0024 0.0077 -0.0345 189 VAL A C 1453 O O . VAL A 189 ? 0.2713 0.2013 0.3709 -0.0154 0.0080 -0.0272 189 VAL A O 1454 C CB . VAL A 189 ? 0.2820 0.2475 0.4048 0.0042 0.0262 -0.0454 189 VAL A CB 1455 C CG1 . VAL A 189 ? 0.2738 0.2632 0.4200 0.0165 0.0213 -0.0499 189 VAL A CG1 1456 C CG2 . VAL A 189 ? 0.2838 0.2659 0.4059 0.0050 0.0404 -0.0566 189 VAL A CG2 1457 N N . PRO A 190 ? 0.3160 0.1864 0.3808 0.0063 -0.0001 -0.0345 190 PRO A N 1458 C CA . PRO A 190 ? 0.3123 0.1691 0.3670 -0.0076 -0.0060 -0.0254 190 PRO A CA 1459 C C . PRO A 190 ? 0.2949 0.1897 0.3837 -0.0019 -0.0093 -0.0204 190 PRO A C 1460 O O . PRO A 190 ? 0.2606 0.1842 0.3741 0.0154 -0.0097 -0.0261 190 PRO A O 1461 C CB . PRO A 190 ? 0.3789 0.1639 0.3797 0.0019 -0.0120 -0.0261 190 PRO A CB 1462 C CG . PRO A 190 ? 0.3975 0.1508 0.3726 0.0138 -0.0078 -0.0362 190 PRO A CG 1463 C CD . PRO A 190 ? 0.3578 0.1812 0.3879 0.0290 -0.0028 -0.0427 190 PRO A CD 1464 N N . PRO A 191 ? 0.2831 0.1832 0.3717 -0.0188 -0.0103 -0.0133 191 PRO A N 1465 C CA . PRO A 191 ? 0.2756 0.2016 0.3869 -0.0161 -0.0123 -0.0097 191 PRO A CA 1466 C C . PRO A 191 ? 0.3219 0.2301 0.4216 -0.0016 -0.0226 -0.0093 191 PRO A C 1467 O O . PRO A 191 ? 0.3440 0.2037 0.4045 0.0057 -0.0282 -0.0082 191 PRO A O 1468 C CB . PRO A 191 ? 0.2687 0.2036 0.3750 -0.0347 -0.0098 -0.0052 191 PRO A CB 1469 C CG . PRO A 191 ? 0.2995 0.2048 0.3724 -0.0516 -0.0093 -0.0069 191 PRO A CG 1470 C CD . PRO A 191 ? 0.3190 0.2085 0.3847 -0.0444 -0.0078 -0.0122 191 PRO A CD 1471 N N . MET A 192 ? 0.3060 0.2461 0.4298 0.0031 -0.0255 -0.0109 192 MET A N 1472 C CA . MET A 192 ? 0.3818 0.3126 0.4918 0.0164 -0.0384 -0.0100 192 MET A CA 1473 C C . MET A 192 ? 0.3475 0.2890 0.4630 -0.0017 -0.0357 -0.0053 192 MET A C 1474 O O . MET A 192 ? 0.3174 0.2795 0.4522 -0.0145 -0.0254 -0.0062 192 MET A O 1475 C CB . MET A 192 ? 0.3740 0.3476 0.5074 0.0412 -0.0472 -0.0224 192 MET A CB 1476 C CG . MET A 192 ? 0.3867 0.4220 0.5631 0.0271 -0.0380 -0.0334 192 MET A CG 1477 S SD . MET A 192 ? 0.4915 0.6024 0.6963 0.0494 -0.0521 -0.0539 192 MET A SD 1478 C CE . MET A 192 ? 0.5023 0.5972 0.6871 0.0444 -0.0655 -0.0459 192 MET A CE 1479 N N . ALA A 193 ? 0.3675 0.2859 0.4562 -0.0006 -0.0443 -0.0002 193 ALA A N 1480 C CA . ALA A 193 ? 0.3513 0.2781 0.4407 -0.0180 -0.0396 0.0027 193 ALA A CA 1481 C C . ALA A 193 ? 0.3659 0.2919 0.4413 -0.0096 -0.0524 0.0022 193 ALA A C 1482 O O . ALA A 193 ? 0.4044 0.3082 0.4531 0.0112 -0.0670 0.0037 193 ALA A O 1483 C CB . ALA A 193 ? 0.3524 0.2579 0.4182 -0.0380 -0.0304 0.0082 193 ALA A CB 1484 N N . VAL A 194 ? 0.3523 0.2994 0.4396 -0.0219 -0.0482 -0.0009 194 VAL A N 1485 C CA . VAL A 194 ? 0.3567 0.3091 0.4305 -0.0184 -0.0600 -0.0034 194 VAL A CA 1486 C C . VAL A 194 ? 0.3481 0.2873 0.4056 -0.0372 -0.0496 -0.0002 194 VAL A C 1487 O O . VAL A 194 ? 0.3160 0.2627 0.3876 -0.0469 -0.0347 -0.0019 194 VAL A O 1488 C CB . VAL A 194 ? 0.3427 0.3483 0.4494 -0.0166 -0.0656 -0.0185 194 VAL A CB 1489 C CG1 . VAL A 194 ? 0.3587 0.3966 0.4845 0.0076 -0.0769 -0.0266 194 VAL A CG1 1490 C CG2 . VAL A 194 ? 0.3286 0.3469 0.4559 -0.0403 -0.0469 -0.0256 194 VAL A CG2 1491 N N . VAL A 195 ? 0.3681 0.2866 0.3899 -0.0375 -0.0581 0.0036 195 VAL A N 1492 C CA . VAL A 195 ? 0.3722 0.2829 0.3748 -0.0548 -0.0475 0.0040 195 VAL A CA 1493 C C . VAL A 195 ? 0.3908 0.3120 0.3837 -0.0541 -0.0581 -0.0027 195 VAL A C 1494 O O . VAL A 195 ? 0.4211 0.3401 0.3959 -0.0391 -0.0780 -0.0018 195 VAL A O 1495 C CB . VAL A 195 ? 0.4135 0.2842 0.3689 -0.0672 -0.0424 0.0135 195 VAL A CB 1496 C CG1 . VAL A 195 ? 0.4157 0.2897 0.3513 -0.0849 -0.0308 0.0104 195 VAL A CG1 1497 C CG2 . VAL A 195 ? 0.3943 0.2665 0.3601 -0.0778 -0.0292 0.0147 195 VAL A CG2 1498 N N . PHE A 196 ? 0.3743 0.3066 0.3743 -0.0664 -0.0466 -0.0111 196 PHE A N 1499 C CA . PHE A 196 ? 0.4058 0.3437 0.3884 -0.0727 -0.0541 -0.0197 196 PHE A CA 1500 C C . PHE A 196 ? 0.4180 0.3415 0.3819 -0.0846 -0.0365 -0.0243 196 PHE A C 1501 O O . PHE A 196 ? 0.4106 0.3318 0.3827 -0.0828 -0.0200 -0.0232 196 PHE A O 1502 C CB . PHE A 196 ? 0.3995 0.3723 0.4097 -0.0771 -0.0607 -0.0343 196 PHE A CB 1503 C CG . PHE A 196 ? 0.3862 0.3571 0.4196 -0.0861 -0.0427 -0.0395 196 PHE A CG 1504 C CD1 . PHE A 196 ? 0.3933 0.3744 0.4539 -0.0770 -0.0412 -0.0348 196 PHE A CD1 1505 C CD2 . PHE A 196 ? 0.3782 0.3245 0.3938 -0.1008 -0.0268 -0.0484 196 PHE A CD2 1506 C CE1 . PHE A 196 ? 0.4115 0.3809 0.4809 -0.0843 -0.0248 -0.0378 196 PHE A CE1 1507 C CE2 . PHE A 196 ? 0.4179 0.3410 0.4343 -0.1050 -0.0103 -0.0510 196 PHE A CE2 1508 C CZ . PHE A 196 ? 0.3963 0.3324 0.4395 -0.0977 -0.0097 -0.0451 196 PHE A CZ 1509 N N . ALA A 197 ? 0.4454 0.3647 0.3825 -0.0928 -0.0411 -0.0315 197 ALA A N 1510 C CA . ALA A 197 ? 0.4587 0.3627 0.3714 -0.1005 -0.0243 -0.0386 197 ALA A CA 1511 C C . ALA A 197 ? 0.4729 0.3688 0.3772 -0.1109 -0.0207 -0.0549 197 ALA A C 1512 O O . ALA A 197 ? 0.4811 0.3938 0.3877 -0.1217 -0.0357 -0.0629 197 ALA A O 1513 C CB . ALA A 197 ? 0.4964 0.3880 0.3671 -0.1067 -0.0273 -0.0335 197 ALA A CB 1514 N N . ARG A 198 ? 0.4839 0.3549 0.3734 -0.1073 -0.0007 -0.0627 198 ARG A N 1515 C CA . ARG A 198 ? 0.5241 0.3617 0.3855 -0.1199 0.0072 -0.0791 198 ARG A CA 1516 C C . ARG A 198 ? 0.5741 0.3816 0.3941 -0.1119 0.0232 -0.0883 198 ARG A C 1517 O O . ARG A 198 ? 0.5552 0.3813 0.3792 -0.0953 0.0307 -0.0833 198 ARG A O 1518 C CB . ARG A 198 ? 0.5286 0.3402 0.3969 -0.1184 0.0171 -0.0811 198 ARG A CB 1519 C CG . ARG A 198 ? 0.4947 0.3434 0.4063 -0.1263 0.0047 -0.0750 198 ARG A CG 1520 C CD . ARG A 198 ? 0.5104 0.3868 0.4227 -0.1562 -0.0077 -0.0896 198 ARG A CD 1521 N NE . ARG A 198 ? 0.4726 0.3974 0.4248 -0.1649 -0.0178 -0.0921 198 ARG A NE 1522 C CZ . ARG A 198 ? 0.4575 0.4449 0.4387 -0.1587 -0.0410 -0.0926 198 ARG A CZ 1523 N NH1 . ARG A 198 ? 0.4217 0.4176 0.3885 -0.1443 -0.0573 -0.0865 198 ARG A NH1 1524 N NH2 . ARG A 198 ? 0.4024 0.4408 0.4205 -0.1629 -0.0475 -0.0996 198 ARG A NH2 1525 N N . THR A 199 ? 0.6471 0.4123 0.4244 -0.1268 0.0298 -0.1048 199 THR A N 1526 C CA . THR A 199 ? 0.7202 0.4502 0.4513 -0.1147 0.0460 -0.1165 199 THR A CA 1527 C C . THR A 199 ? 0.7440 0.4500 0.4682 -0.0757 0.0636 -0.1166 199 THR A C 1528 O O . THR A 199 ? 0.7356 0.4219 0.4693 -0.0658 0.0650 -0.1110 199 THR A O 1529 C CB . THR A 199 ? 0.8077 0.4807 0.4814 -0.1408 0.0514 -0.1367 199 THR A CB 1530 O OG1 . THR A 199 ? 0.8673 0.4849 0.5199 -0.1521 0.0599 -0.1427 199 THR A OG1 1531 C CG2 . THR A 199 ? 0.8233 0.5359 0.5034 -0.1747 0.0312 -0.1409 199 THR A CG2 1532 N N . ALA A 200 ? 0.7756 0.4908 0.4821 -0.0511 0.0761 -0.1245 200 ALA A N 1533 C CA . ALA A 200 ? 0.8212 0.5205 0.5111 -0.0035 0.0915 -0.1318 200 ALA A CA 1534 C C . ALA A 200 ? 0.8982 0.5757 0.5375 0.0159 0.1073 -0.1518 200 ALA A C 1535 O O . ALA A 200 ? 0.9040 0.5934 0.5311 -0.0114 0.1069 -0.1572 200 ALA A O 1536 C CB . ALA A 200 ? 0.7474 0.5291 0.4947 0.0169 0.0899 -0.1229 200 ALA A CB 1537 N N . GLY A 201 ? 0.9710 0.6157 0.5756 0.0679 0.1203 -0.1635 201 GLY A N 1538 C CA . GLY A 201 ? 1.0688 0.6899 0.6201 0.0979 0.1368 -0.1859 201 GLY A CA 1539 C C . GLY A 201 ? 1.0407 0.7726 0.6336 0.1045 0.1443 -0.1942 201 GLY A C 1540 O O . GLY A 201 ? 0.9708 0.7926 0.6289 0.0899 0.1382 -0.1829 201 GLY A O 1541 N N . GLN A 202 ? 1.1190 0.8404 0.6672 0.1225 0.1601 -0.2161 202 GLN A N 1542 C CA . GLN A 202 ? 1.1083 0.9367 0.6854 0.1288 0.1740 -0.2306 202 GLN A CA 1543 C C . GLN A 202 ? 1.0456 0.9291 0.6573 0.0633 0.1683 -0.2161 202 GLN A C 1544 O O . GLN A 202 ? 1.0040 0.9862 0.6543 0.0529 0.1778 -0.2196 202 GLN A O 1545 C CB . GLN A 202 ? 1.0792 1.0042 0.7033 0.1820 0.1793 -0.2399 202 GLN A CB 1546 C CG . GLN A 202 ? 1.1690 1.0291 0.7460 0.2593 0.1805 -0.2516 202 GLN A CG 1547 C CD . GLN A 202 ? 1.1497 1.1235 0.7736 0.3205 0.1818 -0.2649 202 GLN A CD 1548 O OE1 . GLN A 202 ? 1.1283 1.1314 0.7939 0.3247 0.1679 -0.2498 202 GLN A OE1 1549 N NE2 . GLN A 202 ? 1.2030 1.2494 0.8199 0.3700 0.1982 -0.2962 202 GLN A NE2 1550 N N . VAL A 203 ? 1.0478 0.8643 0.6370 0.0198 0.1531 -0.2021 203 VAL A N 1551 C CA . VAL A 203 ? 1.0038 0.8442 0.6051 -0.0340 0.1413 -0.1860 203 VAL A CA 1552 C C . VAL A 203 ? 0.9215 0.8235 0.5821 -0.0485 0.1322 -0.1656 203 VAL A C 1553 O O . VAL A 203 ? 0.9105 0.8508 0.5754 -0.0799 0.1335 -0.1574 203 VAL A O 1554 C CB . VAL A 203 ? 1.0491 0.9063 0.6100 -0.0522 0.1560 -0.1997 203 VAL A CB 1555 C CG1 . VAL A 203 ? 1.0421 0.8926 0.5895 -0.1019 0.1394 -0.1815 203 VAL A CG1 1556 C CG2 . VAL A 203 ? 1.1308 0.9172 0.6277 -0.0346 0.1656 -0.2223 203 VAL A CG2 1557 N N . GLN A 204 ? 0.8727 0.7714 0.5675 -0.0270 0.1242 -0.1578 204 GLN A N 1558 C CA . GLN A 204 ? 0.7944 0.7407 0.5400 -0.0397 0.1153 -0.1403 204 GLN A CA 1559 C C . GLN A 204 ? 0.7539 0.6547 0.5110 -0.0572 0.0920 -0.1206 204 GLN A C 1560 O O . GLN A 204 ? 0.7891 0.6313 0.5211 -0.0586 0.0848 -0.1233 204 GLN A O 1561 C CB . GLN A 204 ? 0.7729 0.7738 0.5551 0.0000 0.1242 -0.1488 204 GLN A CB 1562 C CG . GLN A 204 ? 0.7750 0.8726 0.5739 0.0036 0.1448 -0.1669 204 GLN A CG 1563 C CD . GLN A 204 ? 0.7876 0.9523 0.6232 0.0518 0.1494 -0.1803 204 GLN A CD 1564 O OE1 . GLN A 204 ? 0.8260 0.9455 0.6437 0.1022 0.1453 -0.1855 204 GLN A OE1 1565 N NE2 . GLN A 204 ? 0.7536 1.0223 0.6326 0.0355 0.1577 -0.1869 204 GLN A NE2 1566 N N . LEU A 205 ? 0.6829 0.6136 0.4738 -0.0734 0.0823 -0.1039 205 LEU A N 1567 C CA . LEU A 205 ? 0.6382 0.5434 0.4475 -0.0836 0.0614 -0.0876 205 LEU A CA 1568 C C . LEU A 205 ? 0.5744 0.5014 0.4242 -0.0627 0.0627 -0.0837 205 LEU A C 1569 O O . LEU A 205 ? 0.5578 0.5361 0.4271 -0.0527 0.0744 -0.0884 205 LEU A O 1570 C CB . LEU A 205 ? 0.6423 0.5544 0.4473 -0.1104 0.0493 -0.0714 205 LEU A CB 1571 C CG . LEU A 205 ? 0.6881 0.5703 0.4513 -0.1296 0.0345 -0.0666 205 LEU A CG 1572 C CD1 . LEU A 205 ? 0.7185 0.5978 0.4589 -0.1472 0.0317 -0.0518 205 LEU A CD1 1573 C CD2 . LEU A 205 ? 0.6965 0.5637 0.4754 -0.1269 0.0113 -0.0621 205 LEU A CD2 1574 N N . LEU A 206 ? 0.5457 0.4414 0.4071 -0.0588 0.0515 -0.0774 206 LEU A N 1575 C CA . LEU A 206 ? 0.4992 0.4107 0.3943 -0.0421 0.0504 -0.0710 206 LEU A CA 1576 C C . LEU A 206 ? 0.4529 0.3759 0.3745 -0.0621 0.0351 -0.0552 206 LEU A C 1577 O O . LEU A 206 ? 0.4468 0.3473 0.3661 -0.0750 0.0218 -0.0511 206 LEU A O 1578 C CB . LEU A 206 ? 0.5265 0.3858 0.4045 -0.0242 0.0525 -0.0753 206 LEU A CB 1579 C CG . LEU A 206 ? 0.5198 0.3855 0.4201 -0.0016 0.0520 -0.0689 206 LEU A CG 1580 C CD1 . LEU A 206 ? 0.5277 0.4382 0.4331 0.0351 0.0617 -0.0781 206 LEU A CD1 1581 C CD2 . LEU A 206 ? 0.5682 0.3584 0.4320 0.0041 0.0550 -0.0706 206 LEU A CD2 1582 N N . LEU A 207 ? 0.4073 0.3682 0.3504 -0.0653 0.0372 -0.0493 207 LEU A N 1583 C CA . LEU A 207 ? 0.3654 0.3220 0.3236 -0.0776 0.0238 -0.0352 207 LEU A CA 1584 C C . LEU A 207 ? 0.3538 0.3156 0.3423 -0.0610 0.0224 -0.0333 207 LEU A C 1585 O O . LEU A 207 ? 0.3293 0.3166 0.3285 -0.0431 0.0322 -0.0400 207 LEU A O 1586 C CB . LEU A 207 ? 0.3827 0.3574 0.3321 -0.0979 0.0287 -0.0302 207 LEU A CB 1587 C CG . LEU A 207 ? 0.4344 0.4004 0.3415 -0.1183 0.0356 -0.0324 207 LEU A CG 1588 C CD1 . LEU A 207 ? 0.4573 0.4243 0.3409 -0.1479 0.0439 -0.0272 207 LEU A CD1 1589 C CD2 . LEU A 207 ? 0.4681 0.3898 0.3452 -0.1192 0.0184 -0.0261 207 LEU A CD2 1590 N N . VAL A 208 ? 0.3262 0.2698 0.3261 -0.0642 0.0097 -0.0261 208 VAL A N 1591 C CA . VAL A 208 ? 0.3167 0.2585 0.3386 -0.0527 0.0095 -0.0242 208 VAL A CA 1592 C C . VAL A 208 ? 0.3205 0.2717 0.3606 -0.0583 0.0000 -0.0149 208 VAL A C 1593 O O . VAL A 208 ? 0.3187 0.2612 0.3520 -0.0654 -0.0120 -0.0108 208 VAL A O 1594 C CB . VAL A 208 ? 0.3288 0.2414 0.3431 -0.0568 0.0080 -0.0293 208 VAL A CB 1595 C CG1 . VAL A 208 ? 0.3157 0.2189 0.3417 -0.0502 0.0113 -0.0270 208 VAL A CG1 1596 C CG2 . VAL A 208 ? 0.3560 0.2362 0.3346 -0.0541 0.0186 -0.0400 208 VAL A CG2 1597 N N . CYS A 209 ? 0.3196 0.2869 0.3766 -0.0513 0.0040 -0.0129 209 CYS A N 1598 C CA . CYS A 209 ? 0.3033 0.2696 0.3724 -0.0550 -0.0033 -0.0061 209 CYS A CA 1599 C C . CYS A 209 ? 0.3009 0.2651 0.3874 -0.0437 -0.0021 -0.0070 209 CYS A C 1600 O O . CYS A 209 ? 0.2852 0.2568 0.3728 -0.0316 0.0052 -0.0092 209 CYS A O 1601 C CB . CYS A 209 ? 0.3076 0.2950 0.3759 -0.0638 0.0028 -0.0062 209 CYS A CB 1602 S SG . CYS A 209 ? 0.3626 0.3330 0.4300 -0.0712 -0.0033 0.0002 209 CYS A SG 1603 N N . ARG A 210 ? 0.2953 0.2526 0.3906 -0.0461 -0.0088 -0.0070 210 ARG A N 1604 C CA . ARG A 210 ? 0.2879 0.2415 0.3925 -0.0437 -0.0036 -0.0093 210 ARG A CA 1605 C C . ARG A 210 ? 0.2702 0.2347 0.3909 -0.0399 -0.0084 -0.0058 210 ARG A C 1606 O O . ARG A 210 ? 0.2691 0.2388 0.3942 -0.0383 -0.0186 -0.0058 210 ARG A O 1607 C CB . ARG A 210 ? 0.3202 0.2724 0.4242 -0.0568 -0.0033 -0.0180 210 ARG A CB 1608 C CG . ARG A 210 ? 0.3392 0.2847 0.4443 -0.0654 0.0070 -0.0226 210 ARG A CG 1609 C CD . ARG A 210 ? 0.4163 0.3803 0.5253 -0.0896 0.0086 -0.0371 210 ARG A CD 1610 N NE . ARG A 210 ? 0.4437 0.4149 0.5569 -0.1057 0.0202 -0.0444 210 ARG A NE 1611 C CZ . ARG A 210 ? 0.4504 0.4540 0.5711 -0.1349 0.0263 -0.0620 210 ARG A CZ 1612 N NH1 . ARG A 210 ? 0.4653 0.4983 0.5908 -0.1493 0.0189 -0.0745 210 ARG A NH1 1613 N NH2 . ARG A 210 ? 0.4847 0.4955 0.6052 -0.1537 0.0409 -0.0694 210 ARG A NH2 1614 N N . VAL A 211 ? 0.2444 0.2087 0.3667 -0.0340 -0.0025 -0.0036 211 VAL A N 1615 C CA . VAL A 211 ? 0.2384 0.2085 0.3696 -0.0321 -0.0055 -0.0017 211 VAL A CA 1616 C C . VAL A 211 ? 0.2420 0.2100 0.3785 -0.0307 0.0010 -0.0044 211 VAL A C 1617 O O . VAL A 211 ? 0.2395 0.1930 0.3610 -0.0280 0.0090 -0.0035 211 VAL A O 1618 C CB . VAL A 211 ? 0.2435 0.2252 0.3699 -0.0318 -0.0035 -0.0003 211 VAL A CB 1619 C CG1 . VAL A 211 ? 0.2521 0.2298 0.3783 -0.0360 -0.0060 -0.0004 211 VAL A CG1 1620 C CG2 . VAL A 211 ? 0.2118 0.2019 0.3280 -0.0421 -0.0038 -0.0009 211 VAL A CG2 1621 N N . THR A 212 ? 0.2413 0.2198 0.3914 -0.0306 -0.0017 -0.0088 212 THR A N 1622 C CA . THR A 212 ? 0.2657 0.2510 0.4210 -0.0367 0.0081 -0.0151 212 THR A CA 1623 C C . THR A 212 ? 0.2694 0.2626 0.4323 -0.0287 0.0077 -0.0172 212 THR A C 1624 O O . THR A 212 ? 0.2758 0.2620 0.4358 -0.0190 -0.0012 -0.0146 212 THR A O 1625 C CB . THR A 212 ? 0.3007 0.3139 0.4705 -0.0489 0.0090 -0.0273 212 THR A CB 1626 O OG1 . THR A 212 ? 0.3076 0.3499 0.4957 -0.0332 -0.0060 -0.0323 212 THR A OG1 1627 C CG2 . THR A 212 ? 0.3047 0.3018 0.4592 -0.0595 0.0097 -0.0267 212 THR A CG2 1628 N N . SER A 213 ? 0.2728 0.2703 0.4345 -0.0359 0.0197 -0.0222 213 SER A N 1629 C CA . SER A 213 ? 0.2860 0.3009 0.4581 -0.0292 0.0220 -0.0300 213 SER A CA 1630 C C . SER A 213 ? 0.2856 0.2789 0.4425 -0.0212 0.0202 -0.0242 213 SER A C 1631 O O . SER A 213 ? 0.3019 0.3021 0.4617 -0.0137 0.0218 -0.0317 213 SER A O 1632 C CB . SER A 213 ? 0.2920 0.3393 0.4864 -0.0129 0.0111 -0.0406 213 SER A CB 1633 O OG . SER A 213 ? 0.3475 0.4391 0.5627 -0.0237 0.0142 -0.0531 213 SER A OG 1634 N N . PHE A 214 ? 0.2631 0.2378 0.4032 -0.0221 0.0172 -0.0144 214 PHE A N 1635 C CA . PHE A 214 ? 0.2643 0.2329 0.3928 -0.0196 0.0127 -0.0133 214 PHE A CA 1636 C C . PHE A 214 ? 0.2887 0.2542 0.3991 -0.0188 0.0181 -0.0122 214 PHE A C 1637 O O . PHE A 214 ? 0.2877 0.2428 0.3816 -0.0161 0.0234 -0.0072 214 PHE A O 1638 C CB . PHE A 214 ? 0.2501 0.2212 0.3744 -0.0236 0.0046 -0.0095 214 PHE A CB 1639 C CG . PHE A 214 ? 0.2410 0.2229 0.3628 -0.0190 0.0048 -0.0048 214 PHE A CG 1640 C CD1 . PHE A 214 ? 0.2645 0.2419 0.3912 -0.0187 0.0052 -0.0025 214 PHE A CD1 1641 C CD2 . PHE A 214 ? 0.2457 0.2436 0.3555 -0.0105 0.0030 -0.0047 214 PHE A CD2 1642 C CE1 . PHE A 214 ? 0.2587 0.2372 0.3743 -0.0090 0.0061 0.0001 214 PHE A CE1 1643 C CE2 . PHE A 214 ? 0.2693 0.2748 0.3694 0.0056 0.0015 -0.0022 214 PHE A CE2 1644 C CZ . PHE A 214 ? 0.2598 0.2500 0.3606 0.0068 0.0043 0.0004 214 PHE A CZ 1645 N N . TYR A 215 ? 0.2805 0.2453 0.3832 -0.0202 0.0164 -0.0171 215 TYR A N 1646 C CA . TYR A 215 ? 0.3032 0.2689 0.3844 -0.0182 0.0182 -0.0167 215 TYR A CA 1647 C C . TYR A 215 ? 0.3040 0.2771 0.3776 -0.0268 0.0113 -0.0239 215 TYR A C 1648 O O . TYR A 215 ? 0.3031 0.2573 0.3751 -0.0328 0.0122 -0.0300 215 TYR A O 1649 C CB . TYR A 215 ? 0.3174 0.2707 0.3887 -0.0193 0.0318 -0.0200 215 TYR A CB 1650 C CG . TYR A 215 ? 0.3440 0.2882 0.3809 -0.0159 0.0331 -0.0174 215 TYR A CG 1651 C CD1 . TYR A 215 ? 0.3466 0.2942 0.3728 -0.0188 0.0321 -0.0252 215 TYR A CD1 1652 C CD2 . TYR A 215 ? 0.3729 0.2969 0.3773 -0.0065 0.0338 -0.0072 215 TYR A CD2 1653 C CE1 . TYR A 215 ? 0.4221 0.3651 0.4127 -0.0141 0.0304 -0.0233 215 TYR A CE1 1654 C CE2 . TYR A 215 ? 0.4065 0.3165 0.3676 0.0043 0.0314 -0.0036 215 TYR A CE2 1655 C CZ . TYR A 215 ? 0.4267 0.3523 0.3847 -0.0004 0.0289 -0.0117 215 TYR A CZ 1656 O OH . TYR A 215 ? 0.4891 0.4037 0.4004 0.0117 0.0244 -0.0085 215 TYR A OH 1657 N N . PRO A 216 ? 0.3122 0.3110 0.3737 -0.0269 0.0043 -0.0254 216 PRO A N 1658 C CA . PRO A 216 ? 0.3244 0.3407 0.3726 -0.0079 -0.0008 -0.0195 216 PRO A CA 1659 C C . PRO A 216 ? 0.3167 0.3500 0.3764 0.0041 -0.0057 -0.0147 216 PRO A C 1660 O O . PRO A 216 ? 0.2888 0.3236 0.3696 -0.0076 -0.0044 -0.0154 216 PRO A O 1661 C CB . PRO A 216 ? 0.3437 0.3984 0.3793 -0.0113 -0.0106 -0.0295 216 PRO A CB 1662 C CG . PRO A 216 ? 0.3389 0.4016 0.3853 -0.0423 -0.0099 -0.0414 216 PRO A CG 1663 C CD . PRO A 216 ? 0.3290 0.3376 0.3797 -0.0463 0.0005 -0.0371 216 PRO A CD 1664 N N . ARG A 217 ? 0.3304 0.3705 0.3675 0.0314 -0.0118 -0.0103 217 ARG A N 1665 C CA . ARG A 217 ? 0.3517 0.3953 0.3876 0.0521 -0.0147 -0.0062 217 ARG A CA 1666 C C . ARG A 217 ? 0.3210 0.4318 0.3887 0.0480 -0.0223 -0.0169 217 ARG A C 1667 O O . ARG A 217 ? 0.3203 0.4265 0.3972 0.0518 -0.0194 -0.0148 217 ARG A O 1668 C CB . ARG A 217 ? 0.4010 0.4237 0.3872 0.0926 -0.0212 0.0000 217 ARG A CB 1669 C CG . ARG A 217 ? 0.4453 0.4328 0.4051 0.1214 -0.0201 0.0064 217 ARG A CG 1670 C CD . ARG A 217 ? 0.5508 0.5033 0.4424 0.1703 -0.0291 0.0126 217 ARG A CD 1671 N NE . ARG A 217 ? 0.7462 0.6223 0.5834 0.1982 -0.0237 0.0211 217 ARG A NE 1672 C CZ . ARG A 217 ? 0.8028 0.7050 0.6379 0.2360 -0.0327 0.0154 217 ARG A CZ 1673 N NH1 . ARG A 217 ? 0.7757 0.7940 0.6697 0.2447 -0.0461 -0.0005 217 ARG A NH1 1674 N NH2 . ARG A 217 ? 0.8819 0.6931 0.6521 0.2613 -0.0257 0.0229 217 ARG A NH2 1675 N N . PRO A 218 ? 0.3150 0.4947 0.3946 0.0400 -0.0312 -0.0309 218 PRO A N 1676 C CA . PRO A 218 ? 0.2925 0.5480 0.3999 0.0294 -0.0344 -0.0453 218 PRO A CA 1677 C C . PRO A 218 ? 0.2816 0.5106 0.4046 -0.0091 -0.0232 -0.0442 218 PRO A C 1678 O O . PRO A 218 ? 0.2758 0.4533 0.3917 -0.0336 -0.0171 -0.0399 218 PRO A O 1679 C CB . PRO A 218 ? 0.3082 0.6367 0.4216 0.0110 -0.0420 -0.0636 218 PRO A CB 1680 C CG . PRO A 218 ? 0.3239 0.6272 0.4069 0.0409 -0.0503 -0.0566 218 PRO A CG 1681 C CD . PRO A 218 ? 0.3260 0.5269 0.3916 0.0378 -0.0380 -0.0377 218 PRO A CD 1682 N N . ILE A 219 ? 0.2761 0.5353 0.4132 -0.0087 -0.0208 -0.0481 219 ILE A N 1683 C CA . ILE A 219 ? 0.2730 0.5002 0.4135 -0.0417 -0.0112 -0.0454 219 ILE A CA 1684 C C . ILE A 219 ? 0.2807 0.5732 0.4361 -0.0443 -0.0085 -0.0571 219 ILE A C 1685 O O . ILE A 219 ? 0.2600 0.6068 0.4241 -0.0067 -0.0146 -0.0636 219 ILE A O 1686 C CB . ILE A 219 ? 0.2794 0.4252 0.4116 -0.0288 -0.0080 -0.0279 219 ILE A CB 1687 C CG1 . ILE A 219 ? 0.2679 0.3710 0.3941 -0.0573 -0.0029 -0.0241 219 ILE A CG1 1688 C CG2 . ILE A 219 ? 0.2763 0.4190 0.4061 0.0047 -0.0087 -0.0232 219 ILE A CG2 1689 C CD1 . ILE A 219 ? 0.2851 0.3329 0.4097 -0.0439 -0.0028 -0.0126 219 ILE A CD1 1690 N N . ALA A 220 ? 0.2807 0.5675 0.4314 -0.0860 0.0011 -0.0613 220 ALA A N 1691 C CA . ALA A 220 ? 0.2898 0.6351 0.4521 -0.0920 0.0075 -0.0726 220 ALA A CA 1692 C C . ALA A 220 ? 0.3103 0.5846 0.4528 -0.1119 0.0155 -0.0606 220 ALA A C 1693 O O . ALA A 220 ? 0.3536 0.5658 0.4678 -0.1453 0.0198 -0.0547 220 ALA A O 1694 C CB . ALA A 220 ? 0.2989 0.7395 0.4708 -0.1308 0.0139 -0.0977 220 ALA A CB 1695 N N . VAL A 221 ? 0.3000 0.5785 0.4493 -0.0866 0.0163 -0.0578 221 VAL A N 1696 C CA . VAL A 221 ? 0.3084 0.5261 0.4386 -0.0976 0.0209 -0.0470 221 VAL A CA 1697 C C . VAL A 221 ? 0.3343 0.6135 0.4682 -0.1105 0.0317 -0.0615 221 VAL A C 1698 O O . VAL A 221 ? 0.3208 0.6633 0.4757 -0.0766 0.0310 -0.0726 221 VAL A O 1699 C CB . VAL A 221 ? 0.2930 0.4604 0.4239 -0.0603 0.0141 -0.0338 221 VAL A CB 1700 C CG1 . VAL A 221 ? 0.2966 0.4154 0.4091 -0.0720 0.0162 -0.0261 221 VAL A CG1 1701 C CG2 . VAL A 221 ? 0.2926 0.4146 0.4230 -0.0491 0.0067 -0.0235 221 VAL A CG2 1702 N N . THR A 222 ? 0.3597 0.6179 0.4653 -0.1572 0.0428 -0.0629 222 THR A N 1703 C CA . THR A 222 ? 0.3831 0.6994 0.4869 -0.1785 0.0574 -0.0781 222 THR A CA 1704 C C . THR A 222 ? 0.4041 0.6395 0.4665 -0.1941 0.0615 -0.0642 222 THR A C 1705 O O . THR A 222 ? 0.4154 0.5573 0.4464 -0.1964 0.0531 -0.0456 222 THR A O 1706 C CB . THR A 222 ? 0.4147 0.8075 0.5158 -0.2331 0.0728 -0.1012 222 THR A CB 1707 O OG1 . THR A 222 ? 0.4984 0.8033 0.5472 -0.2821 0.0779 -0.0919 222 THR A OG1 1708 C CG2 . THR A 222 ? 0.4013 0.8975 0.5478 -0.2116 0.0649 -0.1194 222 THR A CG2 1709 N N . TRP A 223 ? 0.3953 0.6741 0.4575 -0.1987 0.0731 -0.0751 223 TRP A N 1710 C CA . TRP A 223 ? 0.4134 0.6263 0.4309 -0.2170 0.0783 -0.0649 223 TRP A CA 1711 C C . TRP A 223 ? 0.4590 0.6822 0.4352 -0.2804 0.0995 -0.0757 223 TRP A C 1712 O O . TRP A 223 ? 0.4541 0.7787 0.4548 -0.3045 0.1144 -0.1000 223 TRP A O 1713 C CB . TRP A 223 ? 0.3933 0.6377 0.4279 -0.1829 0.0797 -0.0710 223 TRP A CB 1714 C CG . TRP A 223 ? 0.3655 0.5592 0.4137 -0.1344 0.0614 -0.0569 223 TRP A CG 1715 C CD1 . TRP A 223 ? 0.3387 0.5589 0.4193 -0.0903 0.0537 -0.0605 223 TRP A CD1 1716 C CD2 . TRP A 223 ? 0.3670 0.4754 0.3891 -0.1294 0.0496 -0.0391 223 TRP A CD2 1717 N NE1 . TRP A 223 ? 0.3378 0.4877 0.4103 -0.0680 0.0420 -0.0463 223 TRP A NE1 1718 C CE2 . TRP A 223 ? 0.3517 0.4451 0.3959 -0.0912 0.0386 -0.0352 223 TRP A CE2 1719 C CE3 . TRP A 223 ? 0.4228 0.4667 0.3986 -0.1528 0.0467 -0.0274 223 TRP A CE3 1720 C CZ2 . TRP A 223 ? 0.3465 0.3811 0.3788 -0.0831 0.0266 -0.0240 223 TRP A CZ2 1721 C CZ3 . TRP A 223 ? 0.4333 0.4223 0.3997 -0.1332 0.0300 -0.0153 223 TRP A CZ3 1722 C CH2 . TRP A 223 ? 0.3686 0.3619 0.3680 -0.1027 0.0210 -0.0155 223 TRP A CH2 1723 N N . LEU A 224 ? 0.5150 0.6336 0.4219 -0.3086 0.1012 -0.0593 224 LEU A N 1724 C CA . LEU A 224 ? 0.5907 0.6909 0.4329 -0.3766 0.1255 -0.0673 224 LEU A CA 1725 C C . LEU A 224 ? 0.6257 0.6897 0.4259 -0.3807 0.1320 -0.0614 224 LEU A C 1726 O O . LEU A 224 ? 0.6053 0.5962 0.3899 -0.3424 0.1123 -0.0413 224 LEU A O 1727 C CB . LEU A 224 ? 0.6653 0.6474 0.4313 -0.4103 0.1246 -0.0529 224 LEU A CB 1728 C CG . LEU A 224 ? 0.6555 0.6460 0.4453 -0.4096 0.1177 -0.0565 224 LEU A CG 1729 C CD1 . LEU A 224 ? 0.7444 0.5832 0.4508 -0.4129 0.1084 -0.0349 224 LEU A CD1 1730 C CD2 . LEU A 224 ? 0.6416 0.7248 0.4418 -0.4689 0.1409 -0.0851 224 LEU A CD2 1731 N N . ARG A 225 ? 0.6544 0.7849 0.4421 -0.4266 0.1595 -0.0825 225 ARG A N 1732 C CA . ARG A 225 ? 0.7317 0.8309 0.4688 -0.4422 0.1715 -0.0801 225 ARG A CA 1733 C C . ARG A 225 ? 0.8558 0.8810 0.4904 -0.5232 0.1969 -0.0797 225 ARG A C 1734 O O . ARG A 225 ? 0.8740 0.9740 0.5108 -0.5823 0.2238 -0.1047 225 ARG A O 1735 C CB . ARG A 225 ? 0.6791 0.9165 0.4782 -0.4287 0.1866 -0.1082 225 ARG A CB 1736 C CG . ARG A 225 ? 0.7514 0.9749 0.4981 -0.4550 0.2059 -0.1124 225 ARG A CG 1737 C CD . ARG A 225 ? 0.7243 1.0998 0.5317 -0.4436 0.2256 -0.1471 225 ARG A CD 1738 N NE . ARG A 225 ? 0.7164 1.1397 0.5975 -0.3615 0.2040 -0.1500 225 ARG A NE 1739 C CZ . ARG A 225 ? 0.6676 1.2162 0.6231 -0.3259 0.2039 -0.1744 225 ARG A CZ 1740 N NH1 . ARG A 225 ? 0.6696 1.3345 0.6513 -0.3658 0.2230 -0.2021 225 ARG A NH1 1741 N NH2 . ARG A 225 ? 0.6139 1.1698 0.6102 -0.2506 0.1846 -0.1729 225 ARG A NH2 1742 N N . ASP A 226 ? 0.9495 0.8245 0.4882 -0.5248 0.1873 -0.0523 226 ASP A N 1743 C CA . ASP A 226 ? 1.1027 0.8487 0.5132 -0.5904 0.2049 -0.0426 226 ASP A CA 1744 C C . ASP A 226 ? 1.1431 0.8577 0.5324 -0.6265 0.2110 -0.0468 226 ASP A C 1745 O O . ASP A 226 ? 1.2796 0.8973 0.5577 -0.6958 0.2342 -0.0463 226 ASP A O 1746 C CB . ASP A 226 ? 1.1818 0.9442 0.5299 -0.6595 0.2418 -0.0578 226 ASP A CB 1747 C CG . ASP A 226 ? 1.2005 0.9381 0.5315 -0.6230 0.2317 -0.0458 226 ASP A CG 1748 O OD1 . ASP A 226 ? 1.2269 0.8584 0.5267 -0.5668 0.1978 -0.0170 226 ASP A OD1 1749 O OD2 . ASP A 226 ? 1.2191 1.0509 0.5718 -0.6460 0.2556 -0.0673 226 ASP A OD2 1750 N N . GLY A 227 ? 1.0440 0.8250 0.5277 -0.5801 0.1904 -0.0499 227 GLY A N 1751 C CA . GLY A 227 ? 1.0767 0.8271 0.5464 -0.6036 0.1912 -0.0532 227 GLY A CA 1752 C C . GLY A 227 ? 1.0232 0.9337 0.5703 -0.6436 0.2106 -0.0885 227 GLY A C 1753 O O . GLY A 227 ? 1.0372 0.9429 0.5811 -0.6674 0.2120 -0.0962 227 GLY A O 1754 N N . ARG A 228 ? 0.9632 1.0186 0.5758 -0.6488 0.2249 -0.1122 228 ARG A N 1755 C CA . ARG A 228 ? 0.8868 1.1289 0.5910 -0.6651 0.2371 -0.1495 228 ARG A CA 1756 C C . ARG A 228 ? 0.7509 1.0955 0.5708 -0.5721 0.2088 -0.1503 228 ARG A C 1757 O O . ARG A 228 ? 0.6980 1.0221 0.5353 -0.5165 0.1952 -0.1358 228 ARG A O 1758 C CB . ARG A 228 ? 0.9223 1.2695 0.6186 -0.7280 0.2736 -0.1809 228 ARG A CB 1759 N N . GLU A 229 ? 0.6918 1.1411 0.5805 -0.5581 0.2009 -0.1685 229 GLU A N 1760 C CA . GLU A 229 ? 0.6134 1.1429 0.5927 -0.4706 0.1752 -0.1686 229 GLU A CA 1761 C C . GLU A 229 ? 0.5621 1.2016 0.5907 -0.4320 0.1803 -0.1863 229 GLU A C 1762 O O . GLU A 229 ? 0.5848 1.3494 0.6304 -0.4689 0.2036 -0.2195 229 GLU A O 1763 C CB . GLU A 229 ? 0.5737 1.1999 0.6068 -0.4641 0.1662 -0.1872 229 GLU A CB 1764 C CG . GLU A 229 ? 0.5099 1.1893 0.6145 -0.3713 0.1386 -0.1830 229 GLU A CG 1765 C CD . GLU A 229 ? 0.4990 1.2740 0.6492 -0.3597 0.1272 -0.2008 229 GLU A CD 1766 O OE1 . GLU A 229 ? 0.5862 1.3987 0.7207 -0.4270 0.1403 -0.2196 229 GLU A OE1 1767 O OE2 . GLU A 229 ? 0.5087 1.3143 0.7019 -0.2845 0.1051 -0.1963 229 GLU A OE2 1768 N N . VAL A 230 ? 0.5205 1.1128 0.5682 -0.3589 0.1598 -0.1666 230 VAL A N 1769 C CA . VAL A 230 ? 0.4873 1.1648 0.5753 -0.3080 0.1611 -0.1823 230 VAL A CA 1770 C C . VAL A 230 ? 0.4459 1.2611 0.6030 -0.2609 0.1514 -0.2070 230 VAL A C 1771 O O . VAL A 230 ? 0.4182 1.2000 0.5933 -0.2171 0.1285 -0.1927 230 VAL A O 1772 C CB . VAL A 230 ? 0.4675 1.0385 0.5434 -0.2483 0.1423 -0.1549 230 VAL A CB 1773 C CG1 . VAL A 230 ? 0.4480 1.0924 0.5523 -0.1948 0.1454 -0.1732 230 VAL A CG1 1774 C CG2 . VAL A 230 ? 0.4998 0.9440 0.5078 -0.2855 0.1460 -0.1314 230 VAL A CG2 1775 N N . PRO A 231 ? 0.4534 1.4281 0.6461 -0.2665 0.1683 -0.2457 231 PRO A N 1776 C CA . PRO A 231 ? 0.4219 1.5399 0.6769 -0.2085 0.1555 -0.2724 231 PRO A CA 1777 C C . PRO A 231 ? 0.4068 1.4816 0.6697 -0.1071 0.1338 -0.2594 231 PRO A C 1778 O O . PRO A 231 ? 0.4208 1.3895 0.6494 -0.0939 0.1356 -0.2396 231 PRO A O 1779 C CB . PRO A 231 ? 0.4352 1.7342 0.7201 -0.2404 0.1820 -0.3193 231 PRO A CB 1780 C CG . PRO A 231 ? 0.4759 1.7016 0.7140 -0.2771 0.2045 -0.3107 231 PRO A CG 1781 C CD . PRO A 231 ? 0.4923 1.5287 0.6663 -0.3242 0.2004 -0.2689 231 PRO A CD 1782 N N . PRO A 232 ? 0.3939 1.5463 0.6919 -0.0367 0.1141 -0.2720 232 PRO A N 1783 C CA . PRO A 232 ? 0.4030 1.4770 0.6834 0.0542 0.0958 -0.2562 232 PRO A CA 1784 C C . PRO A 232 ? 0.4320 1.5757 0.7148 0.1013 0.1070 -0.2815 232 PRO A C 1785 O O . PRO A 232 ? 0.4298 1.7433 0.7516 0.1018 0.1184 -0.3212 232 PRO A O 1786 C CB . PRO A 232 ? 0.4015 1.5264 0.7025 0.1129 0.0714 -0.2611 232 PRO A CB 1787 C CG . PRO A 232 ? 0.3804 1.6427 0.7228 0.0520 0.0768 -0.2863 232 PRO A CG 1788 C CD . PRO A 232 ? 0.3830 1.6947 0.7279 -0.0335 0.1077 -0.3032 232 PRO A CD 1789 N N . SER A 233 ? 0.4580 1.4719 0.6973 0.1366 0.1049 -0.2609 233 SER A N 1790 C CA . SER A 233 ? 0.4881 1.5260 0.7126 0.1894 0.1140 -0.2800 233 SER A CA 1791 C C . SER A 233 ? 0.5203 1.3874 0.6872 0.2469 0.0996 -0.2520 233 SER A C 1792 O O . SER A 233 ? 0.5196 1.2723 0.6675 0.2331 0.0860 -0.2207 233 SER A O 1793 C CB . SER A 233 ? 0.4979 1.5484 0.7154 0.1196 0.1414 -0.2874 233 SER A CB 1794 O OG . SER A 233 ? 0.4990 1.3962 0.6779 0.0646 0.1410 -0.2509 233 SER A OG 1795 N N . PRO A 234 ? 0.5743 1.4219 0.7078 0.3085 0.1045 -0.2654 234 PRO A N 1796 C CA . PRO A 234 ? 0.6217 1.2924 0.6858 0.3443 0.0975 -0.2416 234 PRO A CA 1797 C C . PRO A 234 ? 0.5926 1.1356 0.6357 0.2690 0.1010 -0.2101 234 PRO A C 1798 O O . PRO A 234 ? 0.6300 1.0356 0.6270 0.2800 0.0920 -0.1877 234 PRO A O 1799 C CB . PRO A 234 ? 0.6822 1.3728 0.7165 0.3973 0.1107 -0.2680 234 PRO A CB 1800 C CG . PRO A 234 ? 0.6767 1.5643 0.7654 0.4324 0.1144 -0.3072 234 PRO A CG 1801 C CD . PRO A 234 ? 0.5950 1.5865 0.7491 0.3470 0.1188 -0.3072 234 PRO A CD 1802 N N . ALA A 235 ? 0.5357 1.1259 0.6067 0.1941 0.1138 -0.2104 235 ALA A N 1803 C CA . ALA A 235 ? 0.5171 1.0021 0.5669 0.1308 0.1138 -0.1832 235 ALA A CA 1804 C C . ALA A 235 ? 0.4832 0.9022 0.5398 0.1106 0.0966 -0.1559 235 ALA A C 1805 O O . ALA A 235 ? 0.4768 0.7935 0.5090 0.0845 0.0905 -0.1338 235 ALA A O 1806 C CB . ALA A 235 ? 0.4893 1.0337 0.5513 0.0619 0.1315 -0.1904 235 ALA A CB 1807 N N . LEU A 236 ? 0.4671 0.9547 0.5577 0.1240 0.0886 -0.1606 236 LEU A N 1808 C CA . LEU A 236 ? 0.4445 0.8885 0.5459 0.0981 0.0755 -0.1387 236 LEU A CA 1809 C C . LEU A 236 ? 0.4752 0.8778 0.5631 0.1567 0.0601 -0.1319 236 LEU A C 1810 O O . LEU A 236 ? 0.4925 0.9657 0.5879 0.2102 0.0557 -0.1494 236 LEU A O 1811 C CB . LEU A 236 ? 0.4089 0.9571 0.5503 0.0536 0.0803 -0.1499 236 LEU A CB 1812 C CG . LEU A 236 ? 0.3833 0.8877 0.5273 -0.0021 0.0756 -0.1307 236 LEU A CG 1813 C CD1 . LEU A 236 ? 0.4049 1.0247 0.5826 -0.0272 0.0800 -0.1507 236 LEU A CD1 1814 C CD2 . LEU A 236 ? 0.3646 0.7800 0.4990 0.0209 0.0586 -0.1082 236 LEU A CD2 1815 N N . SER A 237 ? 0.4918 0.7824 0.5546 0.1479 0.0519 -0.1080 237 SER A N 1816 C CA . SER A 237 ? 0.5393 0.7763 0.5777 0.1915 0.0405 -0.0991 237 SER A CA 1817 C C . SER A 237 ? 0.5125 0.7150 0.5662 0.1537 0.0328 -0.0798 237 SER A C 1818 O O . SER A 237 ? 0.4812 0.6276 0.5331 0.1118 0.0342 -0.0663 237 SER A O 1819 C CB . SER A 237 ? 0.6198 0.7389 0.5934 0.2221 0.0433 -0.0935 237 SER A CB 1820 O OG . SER A 237 ? 0.6834 0.7189 0.6167 0.2465 0.0358 -0.0800 237 SER A OG 1821 N N . THR A 238 ? 0.5183 0.7633 0.5874 0.1713 0.0236 -0.0809 238 THR A N 1822 C CA . THR A 238 ? 0.5257 0.7246 0.5991 0.1442 0.0173 -0.0634 238 THR A CA 1823 C C . THR A 238 ? 0.5775 0.6990 0.6035 0.1871 0.0115 -0.0542 238 THR A C 1824 O O . THR A 238 ? 0.6376 0.7815 0.6416 0.2431 0.0052 -0.0629 238 THR A O 1825 C CB . THR A 238 ? 0.4829 0.7650 0.5985 0.1154 0.0135 -0.0690 238 THR A CB 1826 O OG1 . THR A 238 ? 0.5017 0.7303 0.6131 0.1011 0.0073 -0.0533 238 THR A OG1 1827 C CG2 . THR A 238 ? 0.5081 0.9019 0.6417 0.1537 0.0079 -0.0907 238 THR A CG2 1828 N N . GLY A 239 ? 0.5871 0.6153 0.5893 0.1627 0.0145 -0.0384 239 GLY A N 1829 C CA . GLY A 239 ? 0.6461 0.5786 0.5866 0.1897 0.0151 -0.0293 239 GLY A CA 1830 C C . GLY A 239 ? 0.6393 0.5861 0.5792 0.2047 0.0060 -0.0237 239 GLY A C 1831 O O . GLY A 239 ? 0.5874 0.6250 0.5776 0.1957 -0.0017 -0.0293 239 GLY A O 1832 N N . THR A 240 ? 0.6979 0.5463 0.5708 0.2229 0.0086 -0.0135 240 THR A N 1833 C CA . THR A 240 ? 0.7040 0.5442 0.5578 0.2390 0.0011 -0.0063 240 THR A CA 1834 C C . THR A 240 ? 0.6327 0.4538 0.5124 0.1806 0.0087 0.0026 240 THR A C 1835 O O . THR A 240 ? 0.6088 0.3975 0.4963 0.1408 0.0194 0.0039 240 THR A O 1836 C CB . THR A 240 ? 0.8198 0.5458 0.5688 0.2889 0.0023 0.0009 240 THR A CB 1837 O OG1 . THR A 240 ? 0.9319 0.6769 0.6554 0.3520 -0.0054 -0.0104 240 THR A OG1 1838 C CG2 . THR A 240 ? 0.8810 0.5968 0.5996 0.3119 -0.0074 0.0088 240 THR A CG2 1839 N N . VAL A 241 ? 0.5939 0.4470 0.4896 0.1780 0.0019 0.0057 241 VAL A N 1840 C CA . VAL A 241 ? 0.5390 0.3821 0.4579 0.1318 0.0088 0.0112 241 VAL A CA 1841 C C . VAL A 241 ? 0.5962 0.3313 0.4436 0.1236 0.0227 0.0202 241 VAL A C 1842 O O . VAL A 241 ? 0.6803 0.3499 0.4534 0.1607 0.0219 0.0259 241 VAL A O 1843 C CB . VAL A 241 ? 0.5206 0.4295 0.4721 0.1322 -0.0017 0.0090 241 VAL A CB 1844 C CG1 . VAL A 241 ? 0.4664 0.3618 0.4360 0.0925 0.0060 0.0125 241 VAL A CG1 1845 C CG2 . VAL A 241 ? 0.4743 0.4852 0.4868 0.1260 -0.0106 -0.0034 241 VAL A CG2 1846 N N . LEU A 242 ? 0.5424 0.2586 0.4051 0.0757 0.0359 0.0197 242 LEU A N 1847 C CA . LEU A 242 ? 0.5987 0.2206 0.3939 0.0513 0.0550 0.0232 242 LEU A CA 1848 C C . LEU A 242 ? 0.5451 0.1903 0.3649 0.0186 0.0622 0.0223 242 LEU A C 1849 O O . LEU A 242 ? 0.4543 0.1783 0.3485 0.0041 0.0556 0.0165 242 LEU A O 1850 C CB . LEU A 242 ? 0.6137 0.2115 0.4081 0.0162 0.0671 0.0156 242 LEU A CB 1851 C CG . LEU A 242 ? 0.6424 0.2239 0.4225 0.0371 0.0631 0.0123 242 LEU A CG 1852 C CD1 . LEU A 242 ? 0.6445 0.2503 0.4608 -0.0063 0.0690 0.0020 242 LEU A CD1 1853 C CD2 . LEU A 242 ? 0.7625 0.2261 0.4348 0.0649 0.0717 0.0168 242 LEU A CD2 1854 N N . PRO A 243 ? 0.6151 0.1852 0.3643 0.0076 0.0772 0.0274 243 PRO A N 1855 C CA . PRO A 243 ? 0.5917 0.1908 0.3641 -0.0245 0.0872 0.0235 243 PRO A CA 1856 C C . PRO A 243 ? 0.6156 0.2295 0.4098 -0.0806 0.1072 0.0098 243 PRO A C 1857 O O . PRO A 243 ? 0.6632 0.2206 0.4119 -0.1067 0.1220 0.0056 243 PRO A O 1858 C CB . PRO A 243 ? 0.6886 0.1936 0.3616 -0.0142 0.0971 0.0343 243 PRO A CB 1859 C CG . PRO A 243 ? 0.7648 0.1602 0.3445 -0.0004 0.1039 0.0407 243 PRO A CG 1860 C CD . PRO A 243 ? 0.7288 0.1751 0.3620 0.0262 0.0868 0.0366 243 PRO A CD 1861 N N . ASN A 244 ? 0.5859 0.2784 0.4453 -0.0975 0.1075 0.0002 244 ASN A N 1862 C CA . ASN A 244 ? 0.5976 0.3276 0.4798 -0.1458 0.1270 -0.0175 244 ASN A CA 1863 C C . ASN A 244 ? 0.6529 0.3517 0.4879 -0.1688 0.1486 -0.0190 244 ASN A C 1864 O O . ASN A 244 ? 0.6793 0.3482 0.4851 -0.1409 0.1419 -0.0062 244 ASN A O 1865 C CB . ASN A 244 ? 0.5101 0.3470 0.4879 -0.1363 0.1113 -0.0286 244 ASN A CB 1866 C CG . ASN A 244 ? 0.4791 0.3397 0.4929 -0.1180 0.0919 -0.0266 244 ASN A CG 1867 O OD1 . ASN A 244 ? 0.5691 0.3984 0.5584 -0.1319 0.0964 -0.0280 244 ASN A OD1 1868 N ND2 . ASN A 244 ? 0.4450 0.3540 0.5089 -0.0908 0.0723 -0.0244 244 ASN A ND2 1869 N N . ALA A 245 ? 0.7079 0.4168 0.5307 -0.2228 0.1756 -0.0364 245 ALA A N 1870 C CA . ALA A 245 ? 0.7710 0.4531 0.5450 -0.2526 0.2009 -0.0402 245 ALA A CA 1871 C C . ALA A 245 ? 0.7184 0.4756 0.5497 -0.2296 0.1925 -0.0441 245 ALA A C 1872 O O . ALA A 245 ? 0.7776 0.4994 0.5599 -0.2383 0.2072 -0.0409 245 ALA A O 1873 C CB . ALA A 245 ? 0.8317 0.5336 0.5911 -0.3248 0.2347 -0.0650 245 ALA A CB 1874 N N . ASP A 246 ? 0.6191 0.4663 0.5408 -0.1998 0.1695 -0.0506 246 ASP A N 1875 C CA . ASP A 246 ? 0.5850 0.4983 0.5561 -0.1799 0.1635 -0.0588 246 ASP A CA 1876 C C . ASP A 246 ? 0.5466 0.4337 0.5136 -0.1347 0.1396 -0.0407 246 ASP A C 1877 O O . ASP A 246 ? 0.4967 0.4324 0.5092 -0.1127 0.1274 -0.0468 246 ASP A O 1878 C CB . ASP A 246 ? 0.5183 0.5378 0.5756 -0.1735 0.1548 -0.0804 246 ASP A CB 1879 C CG . ASP A 246 ? 0.5159 0.5439 0.6092 -0.1427 0.1266 -0.0716 246 ASP A CG 1880 O OD1 . ASP A 246 ? 0.5460 0.5121 0.6074 -0.1327 0.1167 -0.0528 246 ASP A OD1 1881 O OD2 . ASP A 246 ? 0.5186 0.6164 0.6685 -0.1242 0.1138 -0.0846 246 ASP A OD2 1882 N N . LEU A 247 ? 0.5765 0.3875 0.4841 -0.1201 0.1328 -0.0210 247 LEU A N 1883 C CA . LEU A 247 ? 0.5470 0.3520 0.4553 -0.0798 0.1082 -0.0080 247 LEU A CA 1884 C C . LEU A 247 ? 0.4610 0.3264 0.4408 -0.0619 0.0874 -0.0124 247 LEU A C 1885 O O . LEU A 247 ? 0.4378 0.3323 0.4420 -0.0479 0.0763 -0.0153 247 LEU A O 1886 C CB . LEU A 247 ? 0.5744 0.3778 0.4610 -0.0732 0.1099 -0.0080 247 LEU A CB 1887 C CG . LEU A 247 ? 0.5896 0.3755 0.4480 -0.0387 0.0884 0.0043 247 LEU A CG 1888 C CD1 . LEU A 247 ? 0.6744 0.3967 0.4707 -0.0182 0.0823 0.0197 247 LEU A CD1 1889 C CD2 . LEU A 247 ? 0.6281 0.4025 0.4496 -0.0393 0.0939 0.0031 247 LEU A CD2 1890 N N . THR A 248 ? 0.4209 0.2958 0.4236 -0.0664 0.0840 -0.0136 248 THR A N 1891 C CA . THR A 248 ? 0.3565 0.2629 0.4016 -0.0481 0.0639 -0.0121 248 THR A CA 1892 C C . THR A 248 ? 0.3716 0.2440 0.3918 -0.0401 0.0590 -0.0024 248 THR A C 1893 O O . THR A 248 ? 0.4362 0.2541 0.4039 -0.0465 0.0707 0.0024 248 THR A O 1894 C CB . THR A 248 ? 0.3201 0.2749 0.4155 -0.0543 0.0615 -0.0245 248 THR A CB 1895 O OG1 . THR A 248 ? 0.3544 0.3134 0.4487 -0.0776 0.0740 -0.0319 248 THR A OG1 1896 C CG2 . THR A 248 ? 0.3105 0.2998 0.4285 -0.0504 0.0644 -0.0370 248 THR A CG2 1897 N N . TYR A 249 ? 0.3297 0.2255 0.3774 -0.0265 0.0439 -0.0005 249 TYR A N 1898 C CA . TYR A 249 ? 0.3522 0.2231 0.3767 -0.0129 0.0396 0.0060 249 TYR A CA 1899 C C . TYR A 249 ? 0.3244 0.2187 0.3821 -0.0200 0.0344 0.0020 249 TYR A C 1900 O O . TYR A 249 ? 0.2883 0.2167 0.3829 -0.0284 0.0299 -0.0035 249 TYR A O 1901 C CB . TYR A 249 ? 0.3503 0.2368 0.3666 0.0157 0.0259 0.0104 249 TYR A CB 1902 C CG . TYR A 249 ? 0.3965 0.2565 0.3685 0.0303 0.0271 0.0152 249 TYR A CG 1903 C CD1 . TYR A 249 ? 0.4243 0.2212 0.3292 0.0514 0.0307 0.0231 249 TYR A CD1 1904 C CD2 . TYR A 249 ? 0.3650 0.2521 0.3507 0.0247 0.0245 0.0116 249 TYR A CD2 1905 C CE1 . TYR A 249 ? 0.5247 0.2882 0.3765 0.0690 0.0298 0.0291 249 TYR A CE1 1906 C CE2 . TYR A 249 ? 0.4258 0.2885 0.3657 0.0382 0.0245 0.0159 249 TYR A CE2 1907 C CZ . TYR A 249 ? 0.4876 0.2891 0.3603 0.0609 0.0265 0.0254 249 TYR A CZ 1908 O OH . TYR A 249 ? 0.5769 0.3438 0.3905 0.0794 0.0245 0.0315 249 TYR A OH 1909 N N . GLN A 250 ? 0.3585 0.2273 0.3934 -0.0121 0.0345 0.0048 250 GLN A N 1910 C CA . GLN A 250 ? 0.3466 0.2295 0.4013 -0.0188 0.0306 0.0012 250 GLN A CA 1911 C C . GLN A 250 ? 0.3685 0.2431 0.4036 0.0062 0.0256 0.0043 250 GLN A C 1912 O O . GLN A 250 ? 0.3865 0.2253 0.3791 0.0282 0.0281 0.0079 250 GLN A O 1913 C CB . GLN A 250 ? 0.4059 0.2532 0.4361 -0.0423 0.0438 -0.0042 250 GLN A CB 1914 C CG . GLN A 250 ? 0.4168 0.3076 0.4865 -0.0649 0.0427 -0.0143 250 GLN A CG 1915 C CD . GLN A 250 ? 0.4374 0.3096 0.4857 -0.0964 0.0562 -0.0250 250 GLN A CD 1916 O OE1 . GLN A 250 ? 0.4840 0.3533 0.5204 -0.1228 0.0713 -0.0333 250 GLN A OE1 1917 N NE2 . GLN A 250 ? 0.4631 0.3268 0.5047 -0.0997 0.0526 -0.0276 250 GLN A NE2 1918 N N . LEU A 251 ? 0.3472 0.2519 0.4064 0.0049 0.0193 0.0014 251 LEU A N 1919 C CA . LEU A 251 ? 0.3676 0.2840 0.4163 0.0280 0.0163 -0.0003 251 LEU A CA 1920 C C . LEU A 251 ? 0.3677 0.2896 0.4279 0.0125 0.0163 -0.0039 251 LEU A C 1921 O O . LEU A 251 ? 0.3371 0.2732 0.4217 -0.0092 0.0126 -0.0040 251 LEU A O 1922 C CB . LEU A 251 ? 0.3513 0.3313 0.4282 0.0350 0.0080 -0.0032 251 LEU A CB 1923 C CG . LEU A 251 ? 0.3674 0.3965 0.4466 0.0576 0.0048 -0.0114 251 LEU A CG 1924 C CD1 . LEU A 251 ? 0.4202 0.5120 0.5214 0.0554 -0.0014 -0.0173 251 LEU A CD1 1925 C CD2 . LEU A 251 ? 0.4322 0.4834 0.5271 0.0393 0.0075 -0.0161 251 LEU A CD2 1926 N N . ARG A 252 ? 0.4001 0.3096 0.4375 0.0285 0.0194 -0.0078 252 ARG A N 1927 C CA . ARG A 252 ? 0.4116 0.3291 0.4543 0.0164 0.0197 -0.0122 252 ARG A CA 1928 C C . ARG A 252 ? 0.3890 0.3537 0.4379 0.0363 0.0193 -0.0187 252 ARG A C 1929 O O . ARG A 252 ? 0.3989 0.3643 0.4272 0.0711 0.0207 -0.0228 252 ARG A O 1930 C CB . ARG A 252 ? 0.4713 0.3254 0.4702 0.0155 0.0282 -0.0157 252 ARG A CB 1931 C CG . ARG A 252 ? 0.5127 0.3575 0.5158 -0.0176 0.0283 -0.0199 252 ARG A CG 1932 C CD . ARG A 252 ? 0.5898 0.3600 0.5350 -0.0257 0.0410 -0.0265 252 ARG A CD 1933 N NE . ARG A 252 ? 0.7178 0.4791 0.6480 -0.0360 0.0421 -0.0351 252 ARG A NE 1934 C CZ . ARG A 252 ? 0.7619 0.5006 0.6606 -0.0114 0.0467 -0.0394 252 ARG A CZ 1935 N NH1 . ARG A 252 ? 0.7991 0.5314 0.6812 0.0306 0.0486 -0.0371 252 ARG A NH1 1936 N NH2 . ARG A 252 ? 0.7695 0.4987 0.6525 -0.0254 0.0484 -0.0482 252 ARG A NH2 1937 N N . SER A 253 ? 0.3405 0.3453 0.4115 0.0161 0.0179 -0.0211 253 SER A N 1938 C CA . SER A 253 ? 0.3455 0.4047 0.4216 0.0248 0.0224 -0.0319 253 SER A CA 1939 C C . SER A 253 ? 0.3540 0.3966 0.4149 0.0124 0.0272 -0.0350 253 SER A C 1940 O O . SER A 253 ? 0.3558 0.3660 0.4131 -0.0111 0.0229 -0.0278 253 SER A O 1941 C CB . SER A 253 ? 0.3184 0.4359 0.4197 0.0009 0.0220 -0.0349 253 SER A CB 1942 O OG . SER A 253 ? 0.3748 0.5609 0.4830 0.0030 0.0300 -0.0504 253 SER A OG 1943 N N . THR A 254 ? 0.3636 0.4309 0.4133 0.0325 0.0348 -0.0472 254 THR A N 1944 C CA . THR A 254 ? 0.3699 0.4184 0.3999 0.0197 0.0403 -0.0512 254 THR A CA 1945 C C . THR A 254 ? 0.3649 0.4828 0.4022 0.0192 0.0507 -0.0659 254 THR A C 1946 O O . THR A 254 ? 0.3592 0.5425 0.4128 0.0455 0.0542 -0.0787 254 THR A O 1947 C CB . THR A 254 ? 0.4218 0.4027 0.4111 0.0417 0.0438 -0.0547 254 THR A CB 1948 O OG1 . THR A 254 ? 0.4699 0.4618 0.4408 0.0882 0.0496 -0.0663 254 THR A OG1 1949 C CG2 . THR A 254 ? 0.4057 0.3203 0.3811 0.0329 0.0386 -0.0447 254 THR A CG2 1950 N N . LEU A 255 ? 0.3571 0.4674 0.3800 -0.0096 0.0557 -0.0663 255 LEU A N 1951 C CA . LEU A 255 ? 0.3485 0.5220 0.3709 -0.0209 0.0701 -0.0817 255 LEU A CA 1952 C C . LEU A 255 ? 0.3840 0.5196 0.3717 -0.0219 0.0758 -0.0858 255 LEU A C 1953 O O . LEU A 255 ? 0.3898 0.4680 0.3559 -0.0459 0.0680 -0.0733 255 LEU A O 1954 C CB . LEU A 255 ? 0.3268 0.5219 0.3510 -0.0705 0.0739 -0.0768 255 LEU A CB 1955 C CG . LEU A 255 ? 0.3727 0.6363 0.3902 -0.0994 0.0942 -0.0944 255 LEU A CG 1956 C CD1 . LEU A 255 ? 0.3429 0.7181 0.3988 -0.0755 0.1035 -0.1191 255 LEU A CD1 1957 C CD2 . LEU A 255 ? 0.3954 0.6380 0.3864 -0.1571 0.0996 -0.0855 255 LEU A CD2 1958 N N . LEU A 256 ? 0.4052 0.5760 0.3852 0.0074 0.0880 -0.1052 256 LEU A N 1959 C CA . LEU A 256 ? 0.4583 0.6029 0.4023 0.0008 0.0970 -0.1128 256 LEU A CA 1960 C C . LEU A 256 ? 0.4701 0.6585 0.4082 -0.0444 0.1096 -0.1168 256 LEU A C 1961 O O . LEU A 256 ? 0.4610 0.7353 0.4226 -0.0557 0.1225 -0.1301 256 LEU A O 1962 C CB . LEU A 256 ? 0.4995 0.6546 0.4260 0.0524 0.1070 -0.1338 256 LEU A CB 1963 C CG . LEU A 256 ? 0.5584 0.6279 0.4568 0.0919 0.0978 -0.1285 256 LEU A CG 1964 C CD1 . LEU A 256 ? 0.6305 0.7229 0.5137 0.1598 0.1043 -0.1482 256 LEU A CD1 1965 C CD2 . LEU A 256 ? 0.6104 0.5846 0.4603 0.0739 0.0970 -0.1248 256 LEU A CD2 1966 N N . VAL A 257 ? 0.4958 0.6248 0.3966 -0.0735 0.1059 -0.1063 257 VAL A N 1967 C CA . VAL A 257 ? 0.5369 0.6811 0.4094 -0.1172 0.1185 -0.1073 257 VAL A CA 1968 C C . VAL A 257 ? 0.5992 0.7054 0.4260 -0.1192 0.1229 -0.1130 257 VAL A C 1969 O O . VAL A 257 ? 0.6006 0.6543 0.4155 -0.0965 0.1116 -0.1117 257 VAL A O 1970 C CB . VAL A 257 ? 0.5360 0.6326 0.3909 -0.1547 0.1060 -0.0840 257 VAL A CB 1971 C CG1 . VAL A 257 ? 0.4587 0.5887 0.3537 -0.1556 0.1031 -0.0806 257 VAL A CG1 1972 C CG2 . VAL A 257 ? 0.5495 0.5649 0.3845 -0.1459 0.0810 -0.0661 257 VAL A CG2 1973 N N . SER A 258 ? 0.6661 0.7975 0.4619 -0.1516 0.1414 -0.1212 258 SER A N 1974 C CA . SER A 258 ? 0.7444 0.8337 0.4868 -0.1616 0.1448 -0.1241 258 SER A CA 1975 C C . SER A 258 ? 0.7894 0.7977 0.4869 -0.1894 0.1235 -0.0983 258 SER A C 1976 O O . SER A 258 ? 0.7965 0.7903 0.4843 -0.2149 0.1197 -0.0829 258 SER A O 1977 C CB . SER A 258 ? 0.7879 0.9400 0.5092 -0.1873 0.1759 -0.1445 258 SER A CB 1978 O OG . SER A 258 ? 0.8047 1.0146 0.5456 -0.1477 0.1917 -0.1728 258 SER A OG 1979 N N . PRO A 259 ? 0.8387 0.7933 0.5039 -0.1817 0.1083 -0.0953 259 PRO A N 1980 C CA . PRO A 259 ? 0.8841 0.7761 0.5022 -0.1999 0.0854 -0.0743 259 PRO A CA 1981 C C . PRO A 259 ? 0.9666 0.8371 0.5152 -0.2378 0.0989 -0.0682 259 PRO A C 1982 O O . PRO A 259 ? 0.9867 0.8900 0.5159 -0.2540 0.1264 -0.0851 259 PRO A O 1983 C CB . PRO A 259 ? 0.9043 0.7668 0.5047 -0.1861 0.0702 -0.0814 259 PRO A CB 1984 C CG . PRO A 259 ? 0.9125 0.8039 0.5191 -0.1730 0.0949 -0.1063 259 PRO A CG 1985 C CD . PRO A 259 ? 0.8537 0.7993 0.5162 -0.1554 0.1103 -0.1127 259 PRO A CD 1986 N N . GLN A 260 ? 1.0137 0.8245 0.5181 -0.2500 0.0804 -0.0450 260 GLN A N 1987 C CA . GLN A 260 ? 1.1165 0.8735 0.5300 -0.2872 0.0905 -0.0336 260 GLN A CA 1988 C C . GLN A 260 ? 1.1305 0.9318 0.5383 -0.3296 0.1314 -0.0467 260 GLN A C 1989 O O . GLN A 260 ? 1.2056 0.9903 0.5439 -0.3664 0.1537 -0.0509 260 GLN A O 1990 C CB . GLN A 260 ? 1.1864 0.9057 0.5321 -0.2891 0.0831 -0.0344 260 GLN A CB 1991 C CG . GLN A 260 ? 1.2126 0.8935 0.5475 -0.2563 0.0407 -0.0231 260 GLN A CG 1992 C CD . GLN A 260 ? 1.2799 0.9490 0.5660 -0.2575 0.0352 -0.0325 260 GLN A CD 1993 O OE1 . GLN A 260 ? 1.2913 1.0035 0.6058 -0.2587 0.0537 -0.0551 260 GLN A OE1 1994 N NE2 . GLN A 260 ? 1.3757 0.9821 0.5801 -0.2532 0.0085 -0.0163 260 GLN A NE2 1995 N N . ASP A 261 ? 1.0621 0.9255 0.5400 -0.3278 0.1417 -0.0551 261 ASP A N 1996 C CA . ASP A 261 ? 1.0627 0.9992 0.5497 -0.3682 0.1801 -0.0752 261 ASP A CA 1997 C C . ASP A 261 ? 1.1350 1.0136 0.5448 -0.4276 0.1954 -0.0629 261 ASP A C 1998 O O . ASP A 261 ? 1.1761 1.1097 0.5717 -0.4787 0.2319 -0.0818 261 ASP A O 1999 C CB . ASP A 261 ? 0.9715 1.0158 0.5616 -0.3400 0.1863 -0.0957 261 ASP A CB 2000 C CG . ASP A 261 ? 0.9203 0.9465 0.5489 -0.3261 0.1657 -0.0804 261 ASP A CG 2001 O OD1 . ASP A 261 ? 0.9624 0.8955 0.5413 -0.3361 0.1474 -0.0554 261 ASP A OD1 2002 O OD2 . ASP A 261 ? 0.8279 0.9338 0.5322 -0.3008 0.1676 -0.0948 261 ASP A OD2 2003 N N . GLY A 262 ? 1.1671 0.9332 0.5194 -0.4217 0.1689 -0.0337 262 GLY A N 2004 C CA . GLY A 262 ? 1.2602 0.9321 0.5105 -0.4741 0.1815 -0.0185 262 GLY A CA 2005 C C . GLY A 262 ? 1.2260 0.9149 0.5089 -0.4934 0.1885 -0.0205 262 GLY A C 2006 O O . GLY A 262 ? 1.3275 0.9511 0.5264 -0.5515 0.2096 -0.0160 262 GLY A O 2007 N N . HIS A 263 ? 1.0927 0.8619 0.4877 -0.4486 0.1724 -0.0280 263 HIS A N 2008 C CA . HIS A 263 ? 1.0406 0.8275 0.4743 -0.4556 0.1719 -0.0290 263 HIS A CA 2009 C C . HIS A 263 ? 1.0089 0.7193 0.4477 -0.4033 0.1326 -0.0046 263 HIS A C 2010 O O . HIS A 263 ? 0.9720 0.6763 0.4357 -0.3535 0.1062 0.0029 263 HIS A O 2011 C CB . HIS A 263 ? 0.9318 0.8710 0.4842 -0.4397 0.1826 -0.0571 263 HIS A CB 2012 C CG . HIS A 263 ? 0.9506 0.9964 0.5143 -0.4812 0.2202 -0.0880 263 HIS A CG 2013 N ND1 . HIS A 263 ? 0.8976 1.0517 0.5312 -0.4445 0.2256 -0.1109 263 HIS A ND1 2014 C CD2 . HIS A 263 ? 1.0377 1.1008 0.5472 -0.5571 0.2560 -0.1028 263 HIS A CD2 2015 C CE1 . HIS A 263 ? 0.9464 1.1928 0.5768 -0.4896 0.2615 -0.1396 263 HIS A CE1 2016 N NE2 . HIS A 263 ? 1.0115 1.2102 0.5695 -0.5635 0.2819 -0.1361 263 HIS A NE2 2017 N N . GLY A 264 ? 1.0183 0.6726 0.4289 -0.4177 0.1301 0.0048 264 GLY A N 2018 C CA . GLY A 264 ? 0.9790 0.5849 0.4088 -0.3663 0.0963 0.0219 264 GLY A CA 2019 C C . GLY A 264 ? 0.8588 0.5665 0.3985 -0.3510 0.0968 0.0073 264 GLY A C 2020 O O . GLY A 264 ? 0.8446 0.6135 0.4048 -0.3918 0.1218 -0.0099 264 GLY A O 2021 N N . TYR A 265 ? 0.7705 0.5008 0.3767 -0.2950 0.0701 0.0121 265 TYR A N 2022 C CA . TYR A 265 ? 0.6783 0.4885 0.3765 -0.2748 0.0680 0.0015 265 TYR A CA 2023 C C . TYR A 265 ? 0.6708 0.4324 0.3752 -0.2474 0.0463 0.0145 265 TYR A C 2024 O O . TYR A 265 ? 0.6996 0.3863 0.3615 -0.2220 0.0249 0.0300 265 TYR A O 2025 C CB . TYR A 265 ? 0.5860 0.4741 0.3582 -0.2381 0.0631 -0.0096 265 TYR A CB 2026 C CG . TYR A 265 ? 0.5934 0.5472 0.3702 -0.2585 0.0875 -0.0284 265 TYR A CG 2027 C CD1 . TYR A 265 ? 0.6048 0.5316 0.3369 -0.2643 0.0905 -0.0274 265 TYR A CD1 2028 C CD2 . TYR A 265 ? 0.5262 0.5770 0.3510 -0.2691 0.1067 -0.0497 265 TYR A CD2 2029 C CE1 . TYR A 265 ? 0.6276 0.6189 0.3634 -0.2810 0.1148 -0.0473 265 TYR A CE1 2030 C CE2 . TYR A 265 ? 0.5384 0.6637 0.3710 -0.2814 0.1290 -0.0711 265 TYR A CE2 2031 C CZ . TYR A 265 ? 0.5782 0.6722 0.3671 -0.2875 0.1343 -0.0700 265 TYR A CZ 2032 O OH . TYR A 265 ? 0.6354 0.8093 0.4323 -0.2985 0.1588 -0.0942 265 TYR A OH 2033 N N . ALA A 266 ? 0.6231 0.4345 0.3781 -0.2509 0.0521 0.0056 266 ALA A N 2034 C CA . ALA A 266 ? 0.6061 0.3904 0.3792 -0.2249 0.0355 0.0133 266 ALA A CA 2035 C C . ALA A 266 ? 0.5386 0.4119 0.3911 -0.2168 0.0403 0.0000 266 ALA A C 2036 O O . ALA A 266 ? 0.5009 0.4442 0.3735 -0.2435 0.0589 -0.0161 266 ALA A O 2037 C CB . ALA A 266 ? 0.7121 0.4028 0.4039 -0.2531 0.0398 0.0214 266 ALA A CB 2038 N N . CYS A 267 ? 0.5069 0.3815 0.3999 -0.1790 0.0234 0.0050 267 CYS A N 2039 C CA . CYS A 267 ? 0.4422 0.3753 0.3933 -0.1661 0.0241 -0.0031 267 CYS A CA 2040 C C . CYS A 267 ? 0.4641 0.3627 0.3917 -0.1840 0.0252 -0.0018 267 CYS A C 2041 O O . CYS A 267 ? 0.4917 0.3139 0.3788 -0.1748 0.0148 0.0094 267 CYS A O 2042 C CB . CYS A 267 ? 0.4067 0.3420 0.3966 -0.1245 0.0085 0.0019 267 CYS A CB 2043 S SG . CYS A 267 ? 0.4558 0.4463 0.4999 -0.1053 0.0098 -0.0054 267 CYS A SG 2044 N N . ARG A 268 ? 0.4244 0.3803 0.3728 -0.2066 0.0369 -0.0153 268 ARG A N 2045 C CA . ARG A 268 ? 0.4732 0.4013 0.4005 -0.2265 0.0388 -0.0175 268 ARG A CA 2046 C C . ARG A 268 ? 0.4086 0.3999 0.3963 -0.2002 0.0321 -0.0239 268 ARG A C 2047 O O . ARG A 268 ? 0.3679 0.4454 0.4025 -0.1874 0.0341 -0.0346 268 ARG A O 2048 C CB . ARG A 268 ? 0.5203 0.4565 0.4043 -0.2892 0.0598 -0.0314 268 ARG A CB 2049 C CG . ARG A 268 ? 0.6086 0.5012 0.4559 -0.3185 0.0639 -0.0360 268 ARG A CG 2050 C CD . ARG A 268 ? 0.7122 0.5599 0.4805 -0.3905 0.0864 -0.0459 268 ARG A CD 2051 N NE . ARG A 268 ? 0.7795 0.7539 0.5850 -0.4355 0.1048 -0.0726 268 ARG A NE 2052 C CZ . ARG A 268 ? 0.8355 0.8117 0.5879 -0.5054 0.1302 -0.0870 268 ARG A CZ 2053 N NH1 . ARG A 268 ? 0.9704 0.8062 0.6143 -0.5416 0.1413 -0.0741 268 ARG A NH1 2054 N NH2 . ARG A 268 ? 0.8539 0.9753 0.6566 -0.5388 0.1451 -0.1162 268 ARG A NH2 2055 N N . VAL A 269 ? 0.4189 0.3618 0.3976 -0.1869 0.0235 -0.0173 269 VAL A N 2056 C CA . VAL A 269 ? 0.3678 0.3519 0.3914 -0.1611 0.0168 -0.0204 269 VAL A CA 2057 C C . VAL A 269 ? 0.3995 0.3717 0.4002 -0.1882 0.0213 -0.0287 269 VAL A C 2058 O O . VAL A 269 ? 0.4666 0.3548 0.4144 -0.2011 0.0221 -0.0241 269 VAL A O 2059 C CB . VAL A 269 ? 0.3552 0.3041 0.3939 -0.1206 0.0046 -0.0088 269 VAL A CB 2060 C CG1 . VAL A 269 ? 0.3110 0.3018 0.3880 -0.0990 0.0019 -0.0118 269 VAL A CG1 2061 C CG2 . VAL A 269 ? 0.3292 0.2772 0.3781 -0.1026 0.0003 -0.0024 269 VAL A CG2 2062 N N . GLN A 270 ? 0.3688 0.4224 0.4022 -0.1945 0.0234 -0.0426 270 GLN A N 2063 C CA . GLN A 270 ? 0.4105 0.4687 0.4263 -0.2236 0.0271 -0.0546 270 GLN A CA 2064 C C . GLN A 270 ? 0.3610 0.4408 0.4117 -0.1827 0.0156 -0.0513 270 GLN A C 2065 O O . GLN A 270 ? 0.3121 0.4467 0.4021 -0.1480 0.0091 -0.0497 270 GLN A O 2066 C CB . GLN A 270 ? 0.4123 0.5658 0.4379 -0.2659 0.0378 -0.0777 270 GLN A CB 2067 C CG . GLN A 270 ? 0.4737 0.6731 0.4953 -0.2981 0.0399 -0.0977 270 GLN A CG 2068 C CD . GLN A 270 ? 0.4854 0.8183 0.5328 -0.3353 0.0484 -0.1268 270 GLN A CD 2069 O OE1 . GLN A 270 ? 0.5461 0.9641 0.6355 -0.3112 0.0469 -0.1322 270 GLN A OE1 2070 N NE2 . GLN A 270 ? 0.5602 0.9148 0.5794 -0.3952 0.0585 -0.1486 270 GLN A NE2 2071 N N . HIS A 271 ? 0.3885 0.4091 0.4133 -0.1842 0.0141 -0.0491 271 HIS A N 2072 C CA . HIS A 271 ? 0.3463 0.3759 0.3926 -0.1524 0.0067 -0.0464 271 HIS A CA 2073 C C . HIS A 271 ? 0.4036 0.3952 0.4132 -0.1767 0.0101 -0.0555 271 HIS A C 2074 O O . HIS A 271 ? 0.4492 0.3643 0.4078 -0.2005 0.0164 -0.0560 271 HIS A O 2075 C CB . HIS A 271 ? 0.3250 0.3094 0.3819 -0.1143 0.0021 -0.0311 271 HIS A CB 2076 C CG . HIS A 271 ? 0.2993 0.2979 0.3756 -0.0872 -0.0011 -0.0291 271 HIS A CG 2077 N ND1 . HIS A 271 ? 0.3086 0.2683 0.3702 -0.0813 0.0003 -0.0302 271 HIS A ND1 2078 C CD2 . HIS A 271 ? 0.2908 0.3306 0.3885 -0.0654 -0.0040 -0.0268 271 HIS A CD2 2079 C CE1 . HIS A 271 ? 0.3376 0.3188 0.4143 -0.0624 0.0000 -0.0284 271 HIS A CE1 2080 N NE2 . HIS A 271 ? 0.3115 0.3329 0.4046 -0.0521 -0.0030 -0.0250 271 HIS A NE2 2081 N N . CYS A 272 ? 0.4119 0.4479 0.4359 -0.1706 0.0059 -0.0634 272 CYS A N 2082 C CA . CYS A 272 ? 0.4773 0.4844 0.4639 -0.1990 0.0098 -0.0759 272 CYS A CA 2083 C C . CYS A 272 ? 0.5129 0.4147 0.4606 -0.1845 0.0129 -0.0685 272 CYS A C 2084 O O . CYS A 272 ? 0.5723 0.4122 0.4655 -0.2124 0.0196 -0.0780 272 CYS A O 2085 C CB . CYS A 272 ? 0.4720 0.5526 0.4807 -0.1894 0.0021 -0.0856 272 CYS A CB 2086 S SG . CYS A 272 ? 0.5112 0.5767 0.5404 -0.1330 -0.0044 -0.0694 272 CYS A SG 2087 N N . SER A 273 ? 0.4643 0.3477 0.4354 -0.1416 0.0089 -0.0544 273 SER A N 2088 C CA . SER A 273 ? 0.5054 0.3115 0.4475 -0.1186 0.0102 -0.0516 273 SER A CA 2089 C C . SER A 273 ? 0.5779 0.2972 0.4634 -0.1263 0.0120 -0.0488 273 SER A C 2090 O O . SER A 273 ? 0.6229 0.2657 0.4646 -0.1052 0.0119 -0.0499 273 SER A O 2091 C CB . SER A 273 ? 0.4439 0.2762 0.4307 -0.0776 0.0065 -0.0425 273 SER A CB 2092 O OG . SER A 273 ? 0.4118 0.2515 0.4156 -0.0705 0.0025 -0.0330 273 SER A OG 2093 N N . LEU A 274 ? 0.5808 0.3089 0.4595 -0.1538 0.0138 -0.0459 274 LEU A N 2094 C CA . LEU A 274 ? 0.6453 0.2837 0.4585 -0.1645 0.0163 -0.0408 274 LEU A CA 2095 C C . LEU A 274 ? 0.7523 0.3216 0.4850 -0.2194 0.0292 -0.0523 274 LEU A C 2096 O O . LEU A 274 ? 0.8477 0.3063 0.4959 -0.2301 0.0337 -0.0481 274 LEU A O 2097 C CB . LEU A 274 ? 0.6067 0.2860 0.4482 -0.1678 0.0143 -0.0318 274 LEU A CB 2098 C CG . LEU A 274 ? 0.5083 0.2406 0.4144 -0.1225 0.0036 -0.0217 274 LEU A CG 2099 C CD1 . LEU A 274 ? 0.4619 0.2458 0.3957 -0.1353 0.0046 -0.0176 274 LEU A CD1 2100 C CD2 . LEU A 274 ? 0.5883 0.2563 0.4666 -0.0832 -0.0054 -0.0146 274 LEU A CD2 2101 N N . GLY A 275 ? 0.7385 0.3666 0.4871 -0.2556 0.0351 -0.0679 275 GLY A N 2102 C CA . GLY A 275 ? 0.8323 0.4147 0.5087 -0.3223 0.0499 -0.0845 275 GLY A CA 2103 C C . GLY A 275 ? 0.8761 0.4693 0.5311 -0.3718 0.0608 -0.0867 275 GLY A C 2104 O O . GLY A 275 ? 0.8021 0.5013 0.5282 -0.3649 0.0568 -0.0846 275 GLY A O 2105 N N . ASP A 276 ? 1.0225 0.4940 0.5692 -0.4198 0.0762 -0.0908 276 ASP A N 2106 C CA . ASP A 276 ? 1.0894 0.5579 0.5960 -0.4820 0.0928 -0.0961 276 ASP A CA 2107 C C . ASP A 276 ? 1.0898 0.5146 0.5870 -0.4482 0.0874 -0.0738 276 ASP A C 2108 O O . ASP A 276 ? 1.1178 0.5668 0.6018 -0.4921 0.1002 -0.0771 276 ASP A O 2109 C CB . ASP A 276 ? 1.2597 0.5959 0.6330 -0.5574 0.1157 -0.1099 276 ASP A CB 2110 C CG . ASP A 276 ? 1.2937 0.7164 0.6806 -0.6256 0.1276 -0.1415 276 ASP A CG 2111 O OD1 . ASP A 276 ? 1.2255 0.8175 0.7264 -0.6084 0.1158 -0.1518 276 ASP A OD1 2112 O OD2 . ASP A 276 ? 1.4410 0.7592 0.7171 -0.6962 0.1484 -0.1571 276 ASP A OD2 2113 N N . ARG A 277 ? 1.0689 0.4403 0.5739 -0.3723 0.0689 -0.0542 277 ARG A N 2114 C CA . ARG A 277 ? 1.0603 0.3993 0.5596 -0.3342 0.0595 -0.0346 277 ARG A CA 2115 C C . ARG A 277 ? 0.9111 0.3943 0.5331 -0.2991 0.0474 -0.0303 277 ARG A C 2116 O O . ARG A 277 ? 0.8300 0.3906 0.5296 -0.2640 0.0372 -0.0324 277 ARG A O 2117 C CB . ARG A 277 ? 1.1329 0.3512 0.5743 -0.2683 0.0441 -0.0199 277 ARG A CB 2118 C CG . ARG A 277 ? 1.3529 0.3826 0.6361 -0.2892 0.0538 -0.0156 277 ARG A CG 2119 C CD . ARG A 277 ? 1.4594 0.3948 0.6919 -0.2109 0.0329 0.0031 277 ARG A CD 2120 N NE . ARG A 277 ? 1.4729 0.4054 0.6918 -0.2121 0.0293 0.0169 277 ARG A NE 2121 C CZ . ARG A 277 ? 1.4416 0.4317 0.7203 -0.1506 0.0072 0.0279 277 ARG A CZ 2122 N NH1 . ARG A 277 ? 1.3827 0.4471 0.7448 -0.0847 -0.0121 0.0256 277 ARG A NH1 2123 N NH2 . ARG A 277 ? 1.4464 0.4242 0.6994 -0.1600 0.0061 0.0389 277 ARG A NH2 2124 N N . SER A 278 ? 0.8762 0.3870 0.5054 -0.3121 0.0509 -0.0252 278 SER A N 2125 C CA . SER A 278 ? 0.7582 0.3803 0.4851 -0.2757 0.0402 -0.0205 278 SER A CA 2126 C C . SER A 278 ? 0.7463 0.3175 0.4696 -0.2161 0.0222 -0.0032 278 SER A C 2127 O O . SER A 278 ? 0.8156 0.2712 0.4565 -0.2020 0.0176 0.0058 278 SER A O 2128 C CB . SER A 278 ? 0.7547 0.4267 0.4846 -0.3146 0.0529 -0.0252 278 SER A CB 2129 O OG . SER A 278 ? 0.8304 0.5388 0.5405 -0.3816 0.0728 -0.0454 278 SER A OG 2130 N N . LEU A 279 ? 0.6477 0.3054 0.4536 -0.1814 0.0121 -0.0003 279 LEU A N 2131 C CA . LEU A 279 ? 0.6560 0.2993 0.4701 -0.1380 -0.0028 0.0110 279 LEU A CA 2132 C C . LEU A 279 ? 0.6676 0.3275 0.4735 -0.1604 0.0030 0.0139 279 LEU A C 2133 O O . LEU A 279 ? 0.6193 0.3658 0.4784 -0.1771 0.0114 0.0060 279 LEU A O 2134 C CB . LEU A 279 ? 0.5571 0.2841 0.4578 -0.1029 -0.0113 0.0087 279 LEU A CB 2135 C CG . LEU A 279 ? 0.5691 0.3194 0.5026 -0.0650 -0.0248 0.0135 279 LEU A CG 2136 C CD1 . LEU A 279 ? 0.6750 0.3601 0.5623 -0.0301 -0.0396 0.0179 279 LEU A CD1 2137 C CD2 . LEU A 279 ? 0.4813 0.3008 0.4830 -0.0500 -0.0243 0.0077 279 LEU A CD2 2138 N N . LEU A 280 ? 0.7302 0.3077 0.4657 -0.1552 -0.0022 0.0243 280 LEU A N 2139 C CA . LEU A 280 ? 0.7448 0.3266 0.4598 -0.1779 0.0044 0.0273 280 LEU A CA 2140 C C . LEU A 280 ? 0.7442 0.3142 0.4599 -0.1326 -0.0159 0.0375 280 LEU A C 2141 O O . LEU A 280 ? 0.8138 0.3025 0.4693 -0.1001 -0.0316 0.0465 280 LEU A O 2142 C CB . LEU A 280 ? 0.8630 0.3487 0.4713 -0.2288 0.0213 0.0290 280 LEU A CB 2143 C CG . LEU A 280 ? 0.9151 0.3983 0.4897 -0.2578 0.0316 0.0315 280 LEU A CG 2144 C CD1 . LEU A 280 ? 0.8540 0.4613 0.4989 -0.2967 0.0512 0.0138 280 LEU A CD1 2145 C CD2 . LEU A 280 ? 1.0718 0.4154 0.5094 -0.2963 0.0437 0.0394 280 LEU A CD2 2146 N N . VAL A 281 ? 0.6530 0.3030 0.4296 -0.1289 -0.0162 0.0339 281 VAL A N 2147 C CA . VAL A 281 ? 0.6393 0.3031 0.4324 -0.0920 -0.0348 0.0381 281 VAL A CA 2148 C C . VAL A 281 ? 0.6442 0.3139 0.4166 -0.1115 -0.0289 0.0394 281 VAL A C 2149 O O . VAL A 281 ? 0.5699 0.3081 0.3911 -0.1273 -0.0165 0.0307 281 VAL A O 2150 C CB . VAL A 281 ? 0.5496 0.2971 0.4325 -0.0663 -0.0414 0.0299 281 VAL A CB 2151 C CG1 . VAL A 281 ? 0.5472 0.3096 0.4403 -0.0345 -0.0608 0.0297 281 VAL A CG1 2152 C CG2 . VAL A 281 ? 0.5388 0.2863 0.4416 -0.0528 -0.0428 0.0269 281 VAL A CG2 2153 N N . PRO A 282 ? 0.7350 0.3266 0.4258 -0.1066 -0.0380 0.0499 282 PRO A N 2154 C CA . PRO A 282 ? 0.7616 0.3455 0.4167 -0.1271 -0.0317 0.0520 282 PRO A CA 2155 C C . PRO A 282 ? 0.6956 0.3506 0.4106 -0.1038 -0.0435 0.0458 282 PRO A C 2156 O O . PRO A 282 ? 0.6626 0.3501 0.4219 -0.0681 -0.0622 0.0428 282 PRO A O 2157 C CB . PRO A 282 ? 0.8933 0.3589 0.4341 -0.1138 -0.0453 0.0673 282 PRO A CB 2158 C CG . PRO A 282 ? 0.9478 0.3488 0.4544 -0.0983 -0.0502 0.0715 282 PRO A CG 2159 C CD . PRO A 282 ? 0.8328 0.3304 0.4495 -0.0751 -0.0558 0.0604 282 PRO A CD 2160 N N . TRP A 283 ? 0.6845 0.3677 0.4007 -0.1276 -0.0300 0.0407 283 TRP A N 2161 C CA . TRP A 283 ? 0.6665 0.3883 0.4085 -0.1101 -0.0414 0.0354 283 TRP A CA 2162 C C . TRP A 283 ? 0.7649 0.4234 0.4265 -0.1002 -0.0581 0.0456 283 TRP A C 2163 O O . TRP A 283 ? 0.8319 0.4399 0.4236 -0.1279 -0.0452 0.0515 283 TRP A O 2164 C CB . TRP A 283 ? 0.6204 0.3972 0.3950 -0.1320 -0.0203 0.0231 283 TRP A CB 2165 C CG . TRP A 283 ? 0.5930 0.3873 0.3707 -0.1208 -0.0298 0.0172 283 TRP A CG 2166 C CD1 . TRP A 283 ? 0.5890 0.4015 0.3925 -0.0960 -0.0512 0.0136 283 TRP A CD1 2167 C CD2 . TRP A 283 ? 0.6200 0.4216 0.3735 -0.1385 -0.0165 0.0103 283 TRP A CD2 2168 N NE1 . TRP A 283 ? 0.5712 0.3957 0.3637 -0.1001 -0.0530 0.0053 283 TRP A NE1 2169 C CE2 . TRP A 283 ? 0.5752 0.3887 0.3357 -0.1231 -0.0322 0.0041 283 TRP A CE2 2170 C CE3 . TRP A 283 ? 0.6442 0.4502 0.3701 -0.1688 0.0088 0.0057 283 TRP A CE3 2171 C CZ2 . TRP A 283 ? 0.6067 0.4249 0.3439 -0.1339 -0.0243 -0.0048 283 TRP A CZ2 2172 C CZ3 . TRP A 283 ? 0.6653 0.4833 0.3720 -0.1768 0.0178 -0.0036 283 TRP A CZ3 2173 C CH2 . TRP A 283 ? 0.6669 0.4843 0.3766 -0.1577 0.0005 -0.0078 283 TRP A CH2 2174 N N . HIS A 284 ? 0.7876 0.4544 0.4565 -0.0612 -0.0866 0.0457 284 HIS A N 2175 C CA . HIS A 284 ? 0.9076 0.5262 0.5018 -0.0401 -0.1093 0.0536 284 HIS A CA 2176 C C . HIS A 284 ? 0.8882 0.5735 0.5193 -0.0365 -0.1195 0.0405 284 HIS A C 2177 O O . HIS A 284 ? 0.8212 0.5817 0.5320 -0.0320 -0.1212 0.0259 284 HIS A O 2178 C CB . HIS A 284 ? 0.9527 0.5401 0.5201 0.0099 -0.1387 0.0595 284 HIS A CB 2179 C CG . HIS A 284 ? 1.0589 0.5418 0.5481 0.0090 -0.1318 0.0746 284 HIS A CG 2180 N ND1 . HIS A 284 ? 1.0432 0.5236 0.5594 0.0259 -0.1323 0.0732 284 HIS A ND1 2181 C CD2 . HIS A 284 ? 1.1934 0.5605 0.5666 -0.0112 -0.1222 0.0901 284 HIS A CD2 2182 C CE1 . HIS A 284 ? 1.1566 0.5218 0.5768 0.0168 -0.1239 0.0865 284 HIS A CE1 2183 N NE2 . HIS A 284 ? 1.2523 0.5442 0.5820 -0.0087 -0.1164 0.0971 284 HIS A NE2 2194 N N . ILE B 1 ? 0.8027 0.7559 0.8152 0.3243 -0.2433 -0.1093 1 ILE B N 2195 C CA . ILE B 1 ? 0.7794 0.7443 0.8077 0.3332 -0.2341 -0.1310 1 ILE B CA 2196 C C . ILE B 1 ? 0.7488 0.6693 0.7639 0.2971 -0.2152 -0.1163 1 ILE B C 2197 O O . ILE B 1 ? 0.7298 0.6480 0.7356 0.2624 -0.1985 -0.0957 1 ILE B O 2198 C CB . ILE B 1 ? 0.7358 0.8082 0.8000 0.3385 -0.2162 -0.1516 1 ILE B CB 2199 C CG1 . ILE B 1 ? 0.7008 0.8184 0.7766 0.2967 -0.1938 -0.1352 1 ILE B CG1 2200 C CG2 . ILE B 1 ? 0.7648 0.8929 0.8486 0.3833 -0.2363 -0.1725 1 ILE B CG2 2201 C CD1 . ILE B 1 ? 0.6495 0.8634 0.7624 0.2881 -0.1729 -0.1447 1 ILE B CD1 2202 N N . GLN B 2 ? 0.7430 0.6309 0.7580 0.3081 -0.2201 -0.1301 2 GLN B N 2203 C CA . GLN B 2 ? 0.6997 0.5589 0.7088 0.2768 -0.2026 -0.1212 2 GLN B CA 2204 C C . GLN B 2 ? 0.6273 0.5628 0.6564 0.2679 -0.1759 -0.1350 2 GLN B C 2205 O O . GLN B 2 ? 0.6123 0.6117 0.6594 0.2953 -0.1759 -0.1585 2 GLN B O 2206 C CB . GLN B 2 ? 0.7613 0.5508 0.7637 0.2927 -0.2251 -0.1320 2 GLN B CB 2207 C CG . GLN B 2 ? 0.8562 0.5681 0.8446 0.3101 -0.2608 -0.1204 2 GLN B CG 2208 C CD . GLN B 2 ? 0.9445 0.6315 0.9395 0.3594 -0.2947 -0.1549 2 GLN B CD 2209 O OE1 . GLN B 2 ? 0.9552 0.6566 0.9591 0.3756 -0.2951 -0.1863 2 GLN B OE1 2210 N NE2 . GLN B 2 ? 1.0304 0.6808 1.0191 0.3868 -0.3257 -0.1511 2 GLN B NE2 2211 N N . ARG B 3 ? 0.5643 0.4965 0.5902 0.2305 -0.1534 -0.1183 3 ARG B N 2212 C CA . ARG B 3 ? 0.5009 0.4926 0.5429 0.2159 -0.1293 -0.1231 3 ARG B CA 2213 C C . ARG B 3 ? 0.4839 0.4314 0.5150 0.1939 -0.1205 -0.1154 3 ARG B C 2214 O O . ARG B 3 ? 0.4560 0.3550 0.4731 0.1712 -0.1192 -0.0953 3 ARG B O 2215 C CB . ARG B 3 ? 0.4605 0.4951 0.5138 0.1893 -0.1138 -0.1078 3 ARG B CB 2216 C CG . ARG B 3 ? 0.4885 0.5788 0.5597 0.2042 -0.1221 -0.1134 3 ARG B CG 2217 C CD . ARG B 3 ? 0.4906 0.6078 0.5735 0.1709 -0.1112 -0.0983 3 ARG B CD 2218 N NE . ARG B 3 ? 0.5132 0.6892 0.6197 0.1775 -0.1202 -0.1020 3 ARG B NE 2219 C CZ . ARG B 3 ? 0.5390 0.7984 0.6801 0.1814 -0.1141 -0.1075 3 ARG B CZ 2220 N NH1 . ARG B 3 ? 0.5319 0.8251 0.6823 0.1824 -0.0983 -0.1101 3 ARG B NH1 2221 N NH2 . ARG B 3 ? 0.5237 0.8404 0.6910 0.1847 -0.1240 -0.1093 3 ARG B NH2 2222 N N . THR B 4 ? 0.4835 0.4567 0.5209 0.2019 -0.1141 -0.1313 4 THR B N 2223 C CA . THR B 4 ? 0.4946 0.4360 0.5251 0.1833 -0.1070 -0.1273 4 THR B CA 2224 C C . THR B 4 ? 0.4536 0.4252 0.4899 0.1503 -0.0817 -0.1086 4 THR B C 2225 O O . THR B 4 ? 0.4393 0.4710 0.4902 0.1464 -0.0698 -0.1056 4 THR B O 2226 C CB . THR B 4 ? 0.5187 0.4731 0.5494 0.2116 -0.1162 -0.1567 4 THR B CB 2227 O OG1 . THR B 4 ? 0.5421 0.4410 0.5648 0.1980 -0.1225 -0.1557 4 THR B OG1 2228 C CG2 . THR B 4 ? 0.4948 0.5381 0.5364 0.2166 -0.0959 -0.1637 4 THR B CG2 2229 N N . PRO B 5 ? 0.4572 0.3883 0.4855 0.1260 -0.0755 -0.0946 5 PRO B N 2230 C CA . PRO B 5 ? 0.4199 0.3729 0.4533 0.0996 -0.0557 -0.0797 5 PRO B CA 2231 C C . PRO B 5 ? 0.3967 0.4005 0.4409 0.0991 -0.0434 -0.0842 5 PRO B C 2232 O O . PRO B 5 ? 0.3858 0.3942 0.4264 0.1140 -0.0475 -0.0989 5 PRO B O 2233 C CB . PRO B 5 ? 0.4213 0.3251 0.4444 0.0814 -0.0542 -0.0677 5 PRO B CB 2234 C CG . PRO B 5 ? 0.4637 0.3277 0.4820 0.0943 -0.0721 -0.0772 5 PRO B CG 2235 C CD . PRO B 5 ? 0.4847 0.3508 0.5024 0.1208 -0.0881 -0.0902 5 PRO B CD 2236 N N . LYS B 6 ? 0.3645 0.4059 0.4214 0.0826 -0.0314 -0.0711 6 LYS B N 2237 C CA . LYS B 6 ? 0.3504 0.4270 0.4152 0.0712 -0.0187 -0.0626 6 LYS B CA 2238 C C . LYS B 6 ? 0.3399 0.3721 0.3964 0.0533 -0.0148 -0.0535 6 LYS B C 2239 O O . LYS B 6 ? 0.3351 0.3314 0.3867 0.0428 -0.0167 -0.0478 6 LYS B O 2240 C CB . LYS B 6 ? 0.3512 0.4742 0.4372 0.0556 -0.0127 -0.0469 6 LYS B CB 2241 C CG . LYS B 6 ? 0.3536 0.5187 0.4504 0.0418 -0.0014 -0.0302 6 LYS B CG 2242 C CD . LYS B 6 ? 0.3822 0.5942 0.5071 0.0230 -0.0001 -0.0111 6 LYS B CD 2243 C CE . LYS B 6 ? 0.4297 0.7009 0.5675 0.0116 0.0109 0.0110 6 LYS B CE 2244 N NZ . LYS B 6 ? 0.5099 0.8207 0.6813 -0.0156 0.0092 0.0368 6 LYS B NZ 2245 N N . ILE B 7 ? 0.3309 0.3714 0.3848 0.0522 -0.0096 -0.0532 7 ILE B N 2246 C CA . ILE B 7 ? 0.3237 0.3285 0.3721 0.0393 -0.0073 -0.0473 7 ILE B CA 2247 C C . ILE B 7 ? 0.3232 0.3575 0.3781 0.0293 0.0012 -0.0339 7 ILE B C 2248 O O . ILE B 7 ? 0.3184 0.3919 0.3719 0.0388 0.0038 -0.0363 7 ILE B O 2249 C CB . ILE B 7 ? 0.3466 0.3274 0.3861 0.0498 -0.0155 -0.0617 7 ILE B CB 2250 C CG1 . ILE B 7 ? 0.3511 0.2972 0.3854 0.0595 -0.0287 -0.0708 7 ILE B CG1 2251 C CG2 . ILE B 7 ? 0.3047 0.2604 0.3442 0.0355 -0.0129 -0.0544 7 ILE B CG2 2252 C CD1 . ILE B 7 ? 0.3929 0.3205 0.4233 0.0747 -0.0443 -0.0895 7 ILE B CD1 2253 N N . GLN B 8 ? 0.2984 0.3157 0.3590 0.0129 0.0037 -0.0202 8 GLN B N 2254 C CA . GLN B 8 ? 0.2975 0.3325 0.3659 0.0019 0.0074 -0.0028 8 GLN B CA 2255 C C . GLN B 8 ? 0.3026 0.3026 0.3668 -0.0020 0.0064 -0.0023 8 GLN B C 2256 O O . GLN B 8 ? 0.3098 0.2785 0.3723 -0.0043 0.0040 -0.0072 8 GLN B O 2257 C CB . GLN B 8 ? 0.3095 0.3543 0.3947 -0.0133 0.0047 0.0128 8 GLN B CB 2258 C CG . GLN B 8 ? 0.3058 0.4051 0.4014 -0.0103 0.0075 0.0160 8 GLN B CG 2259 C CD . GLN B 8 ? 0.3416 0.4542 0.4604 -0.0283 0.0018 0.0305 8 GLN B CD 2260 O OE1 . GLN B 8 ? 0.3916 0.5401 0.5288 -0.0448 0.0031 0.0552 8 GLN B OE1 2261 N NE2 . GLN B 8 ? 0.3330 0.4217 0.4524 -0.0263 -0.0060 0.0173 8 GLN B NE2 2262 N N . VAL B 9 ? 0.2775 0.2894 0.3391 -0.0002 0.0080 0.0028 9 VAL B N 2263 C CA . VAL B 9 ? 0.2665 0.2547 0.3272 -0.0008 0.0064 0.0022 9 VAL B CA 2264 C C . VAL B 9 ? 0.2797 0.2723 0.3467 -0.0075 0.0037 0.0219 9 VAL B C 2265 O O . VAL B 9 ? 0.2878 0.3139 0.3540 -0.0089 0.0055 0.0360 9 VAL B O 2266 C CB . VAL B 9 ? 0.2845 0.2800 0.3382 0.0084 0.0054 -0.0109 9 VAL B CB 2267 C CG1 . VAL B 9 ? 0.2695 0.2499 0.3277 0.0071 0.0039 -0.0115 9 VAL B CG1 2268 C CG2 . VAL B 9 ? 0.2521 0.2338 0.3024 0.0126 0.0029 -0.0259 9 VAL B CG2 2269 N N . TYR B 10 ? 0.2847 0.2456 0.3573 -0.0100 -0.0019 0.0238 10 TYR B N 2270 C CA . TYR B 10 ? 0.2807 0.2312 0.3619 -0.0163 -0.0107 0.0433 10 TYR B CA 2271 C C . TYR B 10 ? 0.3014 0.2188 0.3846 -0.0074 -0.0182 0.0339 10 TYR B C 2272 O O . TYR B 10 ? 0.3097 0.2177 0.3888 0.0005 -0.0145 0.0147 10 TYR B O 2273 C CB . TYR B 10 ? 0.3154 0.2613 0.4095 -0.0320 -0.0175 0.0585 10 TYR B CB 2274 C CG . TYR B 10 ? 0.2944 0.2181 0.3912 -0.0331 -0.0214 0.0421 10 TYR B CG 2275 C CD1 . TYR B 10 ? 0.2828 0.2257 0.3734 -0.0299 -0.0128 0.0299 10 TYR B CD1 2276 C CD2 . TYR B 10 ? 0.3483 0.2306 0.4528 -0.0349 -0.0372 0.0374 10 TYR B CD2 2277 C CE1 . TYR B 10 ? 0.2806 0.2067 0.3703 -0.0291 -0.0172 0.0163 10 TYR B CE1 2278 C CE2 . TYR B 10 ? 0.2931 0.1599 0.3962 -0.0333 -0.0426 0.0199 10 TYR B CE2 2279 C CZ . TYR B 10 ? 0.3296 0.2204 0.4248 -0.0313 -0.0316 0.0113 10 TYR B CZ 2280 O OH . TYR B 10 ? 0.3087 0.1875 0.3997 -0.0284 -0.0379 -0.0042 10 TYR B OH 2281 N N . SER B 11 ? 0.3328 0.2360 0.4218 -0.0068 -0.0292 0.0486 11 SER B N 2282 C CA . SER B 11 ? 0.3358 0.2093 0.4281 0.0075 -0.0394 0.0369 11 SER B CA 2283 C C . SER B 11 ? 0.3697 0.2001 0.4713 0.0033 -0.0576 0.0381 11 SER B C 2284 O O . SER B 11 ? 0.3850 0.2105 0.4955 -0.0158 -0.0638 0.0566 11 SER B O 2285 C CB . SER B 11 ? 0.3650 0.2440 0.4583 0.0158 -0.0455 0.0489 11 SER B CB 2286 O OG . SER B 11 ? 0.4044 0.2852 0.5003 0.0020 -0.0527 0.0801 11 SER B OG 2287 N N . ARG B 12 ? 0.3889 0.1921 0.4905 0.0219 -0.0678 0.0168 12 ARG B N 2288 C CA . ARG B 12 ? 0.4412 0.1944 0.5512 0.0233 -0.0926 0.0102 12 ARG B CA 2289 C C . ARG B 12 ? 0.4985 0.2161 0.6237 0.0126 -0.1161 0.0385 12 ARG B C 2290 O O . ARG B 12 ? 0.5283 0.2157 0.6681 -0.0076 -0.1343 0.0535 12 ARG B O 2291 C CB . ARG B 12 ? 0.4493 0.1907 0.5516 0.0542 -0.0982 -0.0247 12 ARG B CB 2292 C CG . ARG B 12 ? 0.5503 0.2349 0.6583 0.0673 -0.1302 -0.0427 12 ARG B CG 2293 C CD . ARG B 12 ? 0.5539 0.2242 0.6613 0.0539 -0.1372 -0.0517 12 ARG B CD 2294 N NE . ARG B 12 ? 0.6424 0.2536 0.7562 0.0665 -0.1735 -0.0733 12 ARG B NE 2295 C CZ . ARG B 12 ? 0.6716 0.2268 0.8065 0.0544 -0.2055 -0.0564 12 ARG B CZ 2296 N NH1 . ARG B 12 ? 0.6989 0.2572 0.8483 0.0294 -0.2027 -0.0137 12 ARG B NH1 2297 N NH2 . ARG B 12 ? 0.7221 0.2178 0.8632 0.0679 -0.2430 -0.0818 12 ARG B NH2 2298 N N . HIS B 13 ? 0.5244 0.2453 0.6486 0.0248 -0.1183 0.0480 13 HIS B N 2299 C CA . HIS B 13 ? 0.5837 0.2721 0.7195 0.0167 -0.1411 0.0804 13 HIS B CA 2300 C C . HIS B 13 ? 0.5573 0.2962 0.6855 0.0065 -0.1232 0.1098 13 HIS B C 2301 O O . HIS B 13 ? 0.5149 0.2992 0.6308 0.0165 -0.1008 0.0942 13 HIS B O 2302 C CB . HIS B 13 ? 0.6302 0.2794 0.7681 0.0483 -0.1636 0.0633 13 HIS B CB 2303 C CG . HIS B 13 ? 0.6801 0.2914 0.8188 0.0705 -0.1797 0.0231 13 HIS B CG 2304 N ND1 . HIS B 13 ? 0.7758 0.3221 0.9275 0.0636 -0.2128 0.0217 13 HIS B ND1 2305 C CD2 . HIS B 13 ? 0.6783 0.3120 0.8060 0.1003 -0.1690 -0.0174 13 HIS B CD2 2306 C CE1 . HIS B 13 ? 0.7746 0.3036 0.9195 0.0923 -0.2224 -0.0231 13 HIS B CE1 2307 N NE2 . HIS B 13 ? 0.7303 0.3159 0.8597 0.1155 -0.1944 -0.0457 13 HIS B NE2 2308 N N . PRO B 14 ? 0.5922 0.3250 0.7279 -0.0133 -0.1349 0.1529 14 PRO B N 2309 C CA . PRO B 14 ? 0.5876 0.3702 0.7110 -0.0157 -0.1219 0.1795 14 PRO B CA 2310 C C . PRO B 14 ? 0.5886 0.3771 0.7024 0.0145 -0.1221 0.1591 14 PRO B C 2311 O O . PRO B 14 ? 0.6343 0.3765 0.7557 0.0333 -0.1443 0.1504 14 PRO B O 2312 C CB . PRO B 14 ? 0.6493 0.4063 0.7843 -0.0360 -0.1442 0.2302 14 PRO B CB 2313 C CG . PRO B 14 ? 0.6639 0.3803 0.8211 -0.0593 -0.1593 0.2354 14 PRO B CG 2314 C CD . PRO B 14 ? 0.6541 0.3346 0.8106 -0.0354 -0.1633 0.1811 14 PRO B CD 2315 N N . ALA B 15 ? 0.5479 0.3942 0.6472 0.0198 -0.1005 0.1513 15 ALA B N 2316 C CA . ALA B 15 ? 0.5154 0.3828 0.6098 0.0440 -0.0965 0.1268 15 ALA B CA 2317 C C . ALA B 15 ? 0.5449 0.4113 0.6368 0.0576 -0.1130 0.1469 15 ALA B C 2318 O O . ALA B 15 ? 0.5621 0.4351 0.6467 0.0459 -0.1196 0.1851 15 ALA B O 2319 C CB . ALA B 15 ? 0.4801 0.4037 0.5631 0.0408 -0.0733 0.1117 15 ALA B CB 2320 N N . GLU B 16 ? 0.5375 0.4021 0.6359 0.0833 -0.1194 0.1221 16 GLU B N 2321 C CA . GLU B 16 ? 0.5526 0.4192 0.6508 0.1028 -0.1368 0.1341 16 GLU B CA 2322 C C . GLU B 16 ? 0.5223 0.4306 0.6276 0.1230 -0.1273 0.0987 16 GLU B C 2323 O O . GLU B 16 ? 0.4983 0.4008 0.6161 0.1341 -0.1229 0.0689 16 GLU B O 2324 C CB . GLU B 16 ? 0.6236 0.4236 0.7336 0.1174 -0.1668 0.1420 16 GLU B CB 2325 N N . ASN B 17 ? 0.5042 0.4597 0.6024 0.1269 -0.1250 0.1028 17 ASN B N 2326 C CA . ASN B 17 ? 0.4777 0.4791 0.5887 0.1404 -0.1189 0.0735 17 ASN B CA 2327 C C . ASN B 17 ? 0.4986 0.4891 0.6301 0.1686 -0.1313 0.0557 17 ASN B C 2328 O O . ASN B 17 ? 0.5335 0.4908 0.6654 0.1866 -0.1536 0.0696 17 ASN B O 2329 C CB . ASN B 17 ? 0.4773 0.5248 0.5778 0.1430 -0.1235 0.0820 17 ASN B CB 2330 C CG . ASN B 17 ? 0.4560 0.5314 0.5384 0.1220 -0.1084 0.0825 17 ASN B CG 2331 O OD1 . ASN B 17 ? 0.4202 0.4935 0.5065 0.1078 -0.0926 0.0660 17 ASN B OD1 2332 N ND2 . ASN B 17 ? 0.4943 0.5971 0.5550 0.1233 -0.1148 0.1007 17 ASN B ND2 2333 N N . GLY B 18 ? 0.4777 0.4971 0.6263 0.1733 -0.1177 0.0261 18 GLY B N 2334 C CA . GLY B 18 ? 0.5042 0.5310 0.6728 0.2050 -0.1267 0.0054 18 GLY B CA 2335 C C . GLY B 18 ? 0.5353 0.5133 0.7038 0.2195 -0.1329 -0.0074 18 GLY B C 2336 O O . GLY B 18 ? 0.5539 0.5421 0.7364 0.2516 -0.1408 -0.0299 18 GLY B O 2337 N N . LYS B 19 ? 0.5468 0.4763 0.7002 0.1984 -0.1310 0.0038 19 LYS B N 2338 C CA . LYS B 19 ? 0.5648 0.4442 0.7179 0.2116 -0.1417 -0.0117 19 LYS B CA 2339 C C . LYS B 19 ? 0.5331 0.4263 0.6803 0.1920 -0.1178 -0.0249 19 LYS B C 2340 O O . LYS B 19 ? 0.4875 0.3910 0.6258 0.1606 -0.1019 -0.0092 19 LYS B O 2341 C CB . LYS B 19 ? 0.6246 0.4282 0.7705 0.2045 -0.1684 0.0145 19 LYS B CB 2342 N N . SER B 20 ? 0.5316 0.4305 0.6820 0.2136 -0.1156 -0.0549 20 SER B N 2343 C CA . SER B 20 ? 0.5058 0.4250 0.6486 0.1975 -0.0927 -0.0661 20 SER B CA 2344 C C . SER B 20 ? 0.4979 0.3613 0.6273 0.1752 -0.0983 -0.0562 20 SER B C 2345 O O . SER B 20 ? 0.5148 0.3174 0.6437 0.1795 -0.1238 -0.0508 20 SER B O 2346 C CB . SER B 20 ? 0.5310 0.4861 0.6771 0.2278 -0.0863 -0.0987 20 SER B CB 2347 O OG . SER B 20 ? 0.6244 0.5269 0.7652 0.2566 -0.1120 -0.1187 20 SER B OG 2348 N N . ASN B 21 ? 0.4505 0.3358 0.5724 0.1504 -0.0763 -0.0530 21 ASN B N 2349 C CA . ASN B 21 ? 0.4506 0.2997 0.5633 0.1251 -0.0777 -0.0400 21 ASN B CA 2350 C C . ASN B 21 ? 0.4290 0.3070 0.5331 0.1166 -0.0562 -0.0529 21 ASN B C 2351 O O . ASN B 21 ? 0.4094 0.3299 0.5151 0.1303 -0.0434 -0.0684 21 ASN B O 2352 C CB . ASN B 21 ? 0.4235 0.2801 0.5356 0.1004 -0.0734 -0.0098 21 ASN B CB 2353 C CG . ASN B 21 ? 0.4554 0.2744 0.5647 0.0780 -0.0830 0.0125 21 ASN B CG 2354 O OD1 . ASN B 21 ? 0.4226 0.2201 0.5300 0.0702 -0.0847 0.0053 21 ASN B OD1 2355 N ND2 . ASN B 21 ? 0.4329 0.2525 0.5424 0.0666 -0.0888 0.0421 21 ASN B ND2 2356 N N . PHE B 22 ? 0.4069 0.2662 0.5034 0.0942 -0.0533 -0.0437 22 PHE B N 2357 C CA . PHE B 22 ? 0.3834 0.2671 0.4709 0.0835 -0.0348 -0.0494 22 PHE B CA 2358 C C . PHE B 22 ? 0.3464 0.2365 0.4326 0.0579 -0.0260 -0.0301 22 PHE B C 2359 O O . PHE B 22 ? 0.3387 0.2076 0.4268 0.0462 -0.0350 -0.0147 22 PHE B O 2360 C CB . PHE B 22 ? 0.4025 0.2601 0.4800 0.0888 -0.0430 -0.0649 22 PHE B CB 2361 C CG . PHE B 22 ? 0.4673 0.3356 0.5394 0.1197 -0.0467 -0.0919 22 PHE B CG 2362 C CD1 . PHE B 22 ? 0.4928 0.4052 0.5536 0.1266 -0.0284 -0.1024 22 PHE B CD1 2363 C CD2 . PHE B 22 ? 0.5256 0.3641 0.6036 0.1438 -0.0693 -0.1056 22 PHE B CD2 2364 C CE1 . PHE B 22 ? 0.5437 0.4823 0.5978 0.1589 -0.0292 -0.1275 22 PHE B CE1 2365 C CE2 . PHE B 22 ? 0.6020 0.4576 0.6739 0.1796 -0.0739 -0.1360 22 PHE B CE2 2366 C CZ . PHE B 22 ? 0.5766 0.4884 0.6356 0.1880 -0.0519 -0.1476 22 PHE B CZ 2367 N N . LEU B 23 ? 0.3234 0.2454 0.4077 0.0503 -0.0100 -0.0304 23 LEU B N 2368 C CA . LEU B 23 ? 0.3150 0.2426 0.3957 0.0323 -0.0037 -0.0200 23 LEU B CA 2369 C C . LEU B 23 ? 0.3190 0.2387 0.3900 0.0263 0.0009 -0.0248 23 LEU B C 2370 O O . LEU B 23 ? 0.3316 0.2611 0.3975 0.0321 0.0073 -0.0335 23 LEU B O 2371 C CB . LEU B 23 ? 0.2850 0.2425 0.3717 0.0282 0.0039 -0.0197 23 LEU B CB 2372 C CG . LEU B 23 ? 0.3128 0.2748 0.3955 0.0157 0.0062 -0.0162 23 LEU B CG 2373 C CD1 . LEU B 23 ? 0.3545 0.3164 0.4326 0.0142 0.0006 -0.0074 23 LEU B CD1 2374 C CD2 . LEU B 23 ? 0.3103 0.2938 0.4034 0.0110 0.0076 -0.0196 23 LEU B CD2 2375 N N . ASN B 24 ? 0.3208 0.2309 0.3893 0.0156 -0.0017 -0.0173 24 ASN B N 2376 C CA . ASN B 24 ? 0.3298 0.2320 0.3909 0.0113 -0.0011 -0.0214 24 ASN B CA 2377 C C . ASN B 24 ? 0.3101 0.2258 0.3687 0.0035 0.0045 -0.0170 24 ASN B C 2378 O O . ASN B 24 ? 0.3174 0.2453 0.3798 -0.0001 0.0039 -0.0097 24 ASN B O 2379 C CB . ASN B 24 ? 0.3266 0.2086 0.3932 0.0058 -0.0137 -0.0170 24 ASN B CB 2380 C CG . ASN B 24 ? 0.3645 0.2200 0.4331 0.0161 -0.0271 -0.0270 24 ASN B CG 2381 O OD1 . ASN B 24 ? 0.3944 0.2500 0.4534 0.0306 -0.0259 -0.0439 24 ASN B OD1 2382 N ND2 . ASN B 24 ? 0.4110 0.2438 0.4921 0.0091 -0.0426 -0.0162 24 ASN B ND2 2383 N N . CYS B 25 ? 0.3204 0.2351 0.3709 0.0035 0.0080 -0.0218 25 CYS B N 2384 C CA . CYS B 25 ? 0.3147 0.2338 0.3626 0.0007 0.0076 -0.0212 25 CYS B CA 2385 C C . CYS B 25 ? 0.3245 0.2367 0.3662 0.0014 0.0041 -0.0238 25 CYS B C 2386 O O . CYS B 25 ? 0.3222 0.2272 0.3535 0.0042 0.0051 -0.0262 25 CYS B O 2387 C CB . CYS B 25 ? 0.3130 0.2318 0.3593 0.0001 0.0091 -0.0226 25 CYS B CB 2388 S SG . CYS B 25 ? 0.3570 0.2736 0.4002 0.0043 0.0020 -0.0284 25 CYS B SG 2389 N N . TYR B 26 ? 0.3057 0.2275 0.3547 -0.0016 -0.0001 -0.0212 26 TYR B N 2390 C CA . TYR B 26 ? 0.3073 0.2287 0.3554 -0.0017 -0.0058 -0.0240 26 TYR B CA 2391 C C . TYR B 26 ? 0.3123 0.2474 0.3587 0.0044 -0.0063 -0.0265 26 TYR B C 2392 O O . TYR B 26 ? 0.2909 0.2511 0.3457 0.0061 -0.0048 -0.0248 26 TYR B O 2393 C CB . TYR B 26 ? 0.3179 0.2447 0.3822 -0.0117 -0.0131 -0.0175 26 TYR B CB 2394 C CG . TYR B 26 ? 0.3431 0.2735 0.4131 -0.0149 -0.0225 -0.0207 26 TYR B CG 2395 C CD1 . TYR B 26 ? 0.3394 0.2502 0.3960 -0.0085 -0.0292 -0.0329 26 TYR B CD1 2396 C CD2 . TYR B 26 ? 0.2917 0.2522 0.3816 -0.0243 -0.0255 -0.0112 26 TYR B CD2 2397 C CE1 . TYR B 26 ? 0.3994 0.3144 0.4615 -0.0109 -0.0414 -0.0381 26 TYR B CE1 2398 C CE2 . TYR B 26 ? 0.3477 0.3161 0.4482 -0.0292 -0.0367 -0.0142 26 TYR B CE2 2399 C CZ . TYR B 26 ? 0.3821 0.3244 0.4684 -0.0223 -0.0460 -0.0289 26 TYR B CZ 2400 O OH . TYR B 26 ? 0.4136 0.3647 0.5103 -0.0263 -0.0603 -0.0343 26 TYR B OH 2401 N N . VAL B 27 ? 0.3209 0.2422 0.3547 0.0105 -0.0093 -0.0305 27 VAL B N 2402 C CA . VAL B 27 ? 0.3520 0.2770 0.3831 0.0206 -0.0146 -0.0345 27 VAL B CA 2403 C C . VAL B 27 ? 0.3526 0.2862 0.3842 0.0239 -0.0221 -0.0367 27 VAL B C 2404 O O . VAL B 27 ? 0.3643 0.2861 0.3863 0.0216 -0.0248 -0.0364 27 VAL B O 2405 C CB . VAL B 27 ? 0.3673 0.2654 0.3865 0.0242 -0.0172 -0.0327 27 VAL B CB 2406 C CG1 . VAL B 27 ? 0.4109 0.3047 0.4348 0.0181 -0.0121 -0.0314 27 VAL B CG1 2407 C CG2 . VAL B 27 ? 0.4166 0.3000 0.4212 0.0207 -0.0162 -0.0246 27 VAL B CG2 2408 N N . SER B 28 ? 0.3429 0.3051 0.3867 0.0308 -0.0261 -0.0406 28 SER B N 2409 C CA . SER B 28 ? 0.3448 0.3258 0.3970 0.0313 -0.0343 -0.0423 28 SER B CA 2410 C C . SER B 28 ? 0.3491 0.3569 0.4076 0.0488 -0.0404 -0.0494 28 SER B C 2411 O O . SER B 28 ? 0.3673 0.3800 0.4241 0.0620 -0.0388 -0.0555 28 SER B O 2412 C CB . SER B 28 ? 0.3264 0.3292 0.4002 0.0136 -0.0342 -0.0360 28 SER B CB 2413 O OG . SER B 28 ? 0.3275 0.3696 0.4200 0.0092 -0.0272 -0.0285 28 SER B OG 2414 N N . GLY B 29 ? 0.3619 0.3872 0.4272 0.0527 -0.0502 -0.0520 29 GLY B N 2415 C CA . GLY B 29 ? 0.3429 0.4035 0.4186 0.0729 -0.0572 -0.0605 29 GLY B CA 2416 C C . GLY B 29 ? 0.3736 0.3998 0.4290 0.0967 -0.0670 -0.0683 29 GLY B C 2417 O O . GLY B 29 ? 0.3694 0.4191 0.4317 0.1198 -0.0740 -0.0798 29 GLY B O 2418 N N . PHE B 30 ? 0.3888 0.3611 0.4207 0.0920 -0.0691 -0.0610 30 PHE B N 2419 C CA . PHE B 30 ? 0.4074 0.3382 0.4229 0.1092 -0.0820 -0.0618 30 PHE B CA 2420 C C . PHE B 30 ? 0.4429 0.3543 0.4424 0.1177 -0.0965 -0.0543 30 PHE B C 2421 O O . PHE B 30 ? 0.4235 0.3445 0.4162 0.1074 -0.0944 -0.0482 30 PHE B O 2422 C CB . PHE B 30 ? 0.4292 0.3177 0.4338 0.0969 -0.0767 -0.0535 30 PHE B CB 2423 C CG . PHE B 30 ? 0.4071 0.2819 0.3994 0.0752 -0.0657 -0.0377 30 PHE B CG 2424 C CD1 . PHE B 30 ? 0.3948 0.2897 0.3953 0.0598 -0.0511 -0.0384 30 PHE B CD1 2425 C CD2 . PHE B 30 ? 0.4268 0.2717 0.3987 0.0727 -0.0712 -0.0216 30 PHE B CD2 2426 C CE1 . PHE B 30 ? 0.3889 0.2747 0.3777 0.0469 -0.0430 -0.0295 30 PHE B CE1 2427 C CE2 . PHE B 30 ? 0.4218 0.2667 0.3804 0.0579 -0.0597 -0.0092 30 PHE B CE2 2428 C CZ . PHE B 30 ? 0.4084 0.2742 0.3755 0.0474 -0.0461 -0.0165 30 PHE B CZ 2429 N N . HIS B 31 ? 0.4727 0.3577 0.4658 0.1395 -0.1144 -0.0569 31 HIS B N 2430 C CA . HIS B 31 ? 0.5090 0.3680 0.4835 0.1497 -0.1313 -0.0450 31 HIS B CA 2431 C C . HIS B 31 ? 0.5554 0.3603 0.5235 0.1650 -0.1506 -0.0425 31 HIS B C 2432 O O . HIS B 31 ? 0.5608 0.3700 0.5435 0.1836 -0.1577 -0.0636 31 HIS B O 2433 C CB . HIS B 31 ? 0.5236 0.4269 0.5093 0.1687 -0.1416 -0.0572 31 HIS B CB 2434 C CG . HIS B 31 ? 0.5255 0.4255 0.4913 0.1674 -0.1501 -0.0443 31 HIS B CG 2435 N ND1 . HIS B 31 ? 0.5856 0.4421 0.5257 0.1786 -0.1674 -0.0269 31 HIS B ND1 2436 C CD2 . HIS B 31 ? 0.4785 0.4133 0.4453 0.1571 -0.1466 -0.0465 31 HIS B CD2 2437 C CE1 . HIS B 31 ? 0.5994 0.4708 0.5218 0.1772 -0.1715 -0.0188 31 HIS B CE1 2438 N NE2 . HIS B 31 ? 0.5741 0.4916 0.5127 0.1650 -0.1602 -0.0337 31 HIS B NE2 2439 N N . PRO B 32 ? 0.5942 0.3489 0.5412 0.1567 -0.1604 -0.0163 32 PRO B N 2440 C CA . PRO B 32 ? 0.6033 0.3578 0.5272 0.1384 -0.1519 0.0100 32 PRO B CA 2441 C C . PRO B 32 ? 0.5750 0.3413 0.4979 0.1099 -0.1266 0.0178 32 PRO B C 2442 O O . PRO B 32 ? 0.5284 0.3032 0.4697 0.1033 -0.1161 0.0034 32 PRO B O 2443 C CB . PRO B 32 ? 0.6730 0.3707 0.5790 0.1408 -0.1732 0.0388 32 PRO B CB 2444 C CG . PRO B 32 ? 0.7059 0.3616 0.6286 0.1596 -0.1965 0.0238 32 PRO B CG 2445 C CD . PRO B 32 ? 0.6481 0.3401 0.5941 0.1664 -0.1842 -0.0110 32 PRO B CD 2446 N N . SER B 33 ? 0.5884 0.3608 0.4886 0.0966 -0.1176 0.0395 33 SER B N 2447 C CA . SER B 33 ? 0.5719 0.3680 0.4703 0.0770 -0.0942 0.0411 33 SER B CA 2448 C C . SER B 33 ? 0.5843 0.3597 0.4867 0.0572 -0.0859 0.0605 33 SER B C 2449 O O . SER B 33 ? 0.5710 0.3678 0.4794 0.0448 -0.0678 0.0559 33 SER B O 2450 C CB . SER B 33 ? 0.5855 0.4086 0.4561 0.0773 -0.0884 0.0497 33 SER B CB 2451 O OG . SER B 33 ? 0.6539 0.4591 0.4996 0.0802 -0.0994 0.0797 33 SER B OG 2452 N N . ASP B 34 ? 0.6295 0.3640 0.5304 0.0530 -0.1010 0.0839 34 ASP B N 2453 C CA . ASP B 34 ? 0.6555 0.3740 0.5670 0.0289 -0.0954 0.1046 34 ASP B CA 2454 C C . ASP B 34 ? 0.6091 0.3259 0.5473 0.0267 -0.0914 0.0776 34 ASP B C 2455 O O . ASP B 34 ? 0.6002 0.3000 0.5503 0.0430 -0.1053 0.0540 34 ASP B O 2456 C CB . ASP B 34 ? 0.7188 0.3858 0.6294 0.0203 -0.1182 0.1379 34 ASP B CB 2457 C CG . ASP B 34 ? 0.8181 0.4992 0.7009 0.0108 -0.1145 0.1802 34 ASP B CG 2458 O OD1 . ASP B 34 ? 0.8478 0.5832 0.7146 0.0050 -0.0898 0.1859 34 ASP B OD1 2459 O OD2 . ASP B 34 ? 0.9175 0.5561 0.7926 0.0112 -0.1381 0.2083 34 ASP B OD2 2460 N N . ILE B 35 ? 0.5902 0.3318 0.5365 0.0093 -0.0722 0.0805 35 ILE B N 2461 C CA . ILE B 35 ? 0.5541 0.2993 0.5223 0.0077 -0.0680 0.0571 35 ILE B CA 2462 C C . ILE B 35 ? 0.5666 0.3255 0.5460 -0.0158 -0.0551 0.0732 35 ILE B C 2463 O O . ILE B 35 ? 0.5771 0.3627 0.5456 -0.0260 -0.0413 0.0949 35 ILE B O 2464 C CB . ILE B 35 ? 0.5197 0.2994 0.4885 0.0218 -0.0566 0.0290 35 ILE B CB 2465 C CG1 . ILE B 35 ? 0.4776 0.2596 0.4657 0.0257 -0.0576 0.0064 35 ILE B CG1 2466 C CG2 . ILE B 35 ? 0.4949 0.3122 0.4539 0.0154 -0.0361 0.0317 35 ILE B CG2 2467 C CD1 . ILE B 35 ? 0.4633 0.2752 0.4554 0.0399 -0.0533 -0.0150 35 ILE B CD1 2468 N N . GLU B 36 ? 0.5526 0.2979 0.5537 -0.0226 -0.0612 0.0627 36 GLU B N 2469 C CA . GLU B 36 ? 0.5432 0.3098 0.5602 -0.0435 -0.0497 0.0741 36 GLU B CA 2470 C C . GLU B 36 ? 0.4951 0.2813 0.5233 -0.0361 -0.0421 0.0456 36 GLU B C 2471 O O . GLU B 36 ? 0.4873 0.2548 0.5209 -0.0242 -0.0552 0.0235 36 GLU B O 2472 C CB . GLU B 36 ? 0.5990 0.3282 0.6354 -0.0643 -0.0699 0.0944 36 GLU B CB 2473 C CG . GLU B 36 ? 0.6441 0.4048 0.7017 -0.0910 -0.0584 0.1147 36 GLU B CG 2474 C CD . GLU B 36 ? 0.7733 0.4957 0.8567 -0.1184 -0.0825 0.1399 36 GLU B CD 2475 O OE1 . GLU B 36 ? 0.8541 0.5168 0.9353 -0.1143 -0.1103 0.1416 36 GLU B OE1 2476 O OE2 . GLU B 36 ? 0.7741 0.5256 0.8827 -0.1437 -0.0763 0.1575 36 GLU B OE2 2477 N N . VAL B 37 ? 0.4528 0.2793 0.4822 -0.0398 -0.0219 0.0459 37 VAL B N 2478 C CA . VAL B 37 ? 0.4233 0.2683 0.4615 -0.0330 -0.0152 0.0244 37 VAL B CA 2479 C C . VAL B 37 ? 0.4168 0.2889 0.4719 -0.0473 -0.0059 0.0338 37 VAL B C 2480 O O . VAL B 37 ? 0.4038 0.3036 0.4556 -0.0536 0.0070 0.0507 37 VAL B O 2481 C CB . VAL B 37 ? 0.4001 0.2640 0.4243 -0.0183 -0.0045 0.0119 37 VAL B CB 2482 C CG1 . VAL B 37 ? 0.3776 0.2572 0.4111 -0.0136 0.0003 -0.0030 37 VAL B CG1 2483 C CG2 . VAL B 37 ? 0.4264 0.2730 0.4393 -0.0059 -0.0143 0.0047 37 VAL B CG2 2484 N N . ASP B 38 ? 0.4009 0.2701 0.4739 -0.0512 -0.0139 0.0232 38 ASP B N 2485 C CA . ASP B 38 ? 0.4030 0.3054 0.4954 -0.0617 -0.0060 0.0283 38 ASP B CA 2486 C C . ASP B 38 ? 0.3654 0.2808 0.4583 -0.0480 -0.0035 0.0076 38 ASP B C 2487 O O . ASP B 38 ? 0.3655 0.2634 0.4513 -0.0375 -0.0126 -0.0079 38 ASP B O 2488 C CB . ASP B 38 ? 0.4260 0.3177 0.5446 -0.0835 -0.0216 0.0390 38 ASP B CB 2489 C CG . ASP B 38 ? 0.5248 0.3997 0.6464 -0.1021 -0.0276 0.0675 38 ASP B CG 2490 O OD1 . ASP B 38 ? 0.5650 0.4664 0.6738 -0.1030 -0.0106 0.0863 38 ASP B OD1 2491 O OD2 . ASP B 38 ? 0.6310 0.4658 0.7674 -0.1157 -0.0515 0.0718 38 ASP B OD2 2492 N N . LEU B 39 ? 0.3351 0.2848 0.4359 -0.0462 0.0080 0.0087 39 LEU B N 2493 C CA . LEU B 39 ? 0.3056 0.2662 0.4097 -0.0354 0.0069 -0.0054 39 LEU B CA 2494 C C . LEU B 39 ? 0.2936 0.2712 0.4225 -0.0469 -0.0008 -0.0041 39 LEU B C 2495 O O . LEU B 39 ? 0.2943 0.2945 0.4411 -0.0611 0.0032 0.0102 39 LEU B O 2496 C CB . LEU B 39 ? 0.2926 0.2735 0.3906 -0.0224 0.0191 -0.0070 39 LEU B CB 2497 C CG . LEU B 39 ? 0.3449 0.3103 0.4220 -0.0134 0.0237 -0.0089 39 LEU B CG 2498 C CD1 . LEU B 39 ? 0.3403 0.3165 0.4139 0.0013 0.0281 -0.0157 39 LEU B CD1 2499 C CD2 . LEU B 39 ? 0.3799 0.3204 0.4468 -0.0106 0.0161 -0.0151 39 LEU B CD2 2500 N N . LEU B 40 ? 0.2919 0.2655 0.4226 -0.0411 -0.0124 -0.0181 40 LEU B N 2501 C CA . LEU B 40 ? 0.2908 0.2754 0.4452 -0.0519 -0.0271 -0.0223 40 LEU B CA 2502 C C . LEU B 40 ? 0.2741 0.2885 0.4319 -0.0399 -0.0258 -0.0294 40 LEU B C 2503 O O . LEU B 40 ? 0.2805 0.2938 0.4189 -0.0232 -0.0209 -0.0340 40 LEU B O 2504 C CB . LEU B 40 ? 0.3205 0.2714 0.4706 -0.0515 -0.0490 -0.0380 40 LEU B CB 2505 C CG . LEU B 40 ? 0.3345 0.2443 0.4779 -0.0571 -0.0571 -0.0347 40 LEU B CG 2506 C CD1 . LEU B 40 ? 0.4146 0.2931 0.5517 -0.0464 -0.0826 -0.0594 40 LEU B CD1 2507 C CD2 . LEU B 40 ? 0.3416 0.2475 0.5095 -0.0848 -0.0596 -0.0102 40 LEU B CD2 2508 N N . LYS B 41 ? 0.2653 0.3083 0.4503 -0.0495 -0.0317 -0.0274 41 LYS B N 2509 C CA . LYS B 41 ? 0.2538 0.3255 0.4439 -0.0371 -0.0354 -0.0346 41 LYS B CA 2510 C C . LYS B 41 ? 0.2816 0.3565 0.4917 -0.0487 -0.0585 -0.0455 41 LYS B C 2511 O O . LYS B 41 ? 0.2779 0.3633 0.5198 -0.0717 -0.0653 -0.0374 41 LYS B O 2512 C CB . LYS B 41 ? 0.2403 0.3548 0.4512 -0.0358 -0.0231 -0.0244 41 LYS B CB 2513 C CG . LYS B 41 ? 0.2085 0.3530 0.4267 -0.0196 -0.0294 -0.0310 41 LYS B CG 2514 C CD . LYS B 41 ? 0.2091 0.4004 0.4499 -0.0132 -0.0187 -0.0247 41 LYS B CD 2515 C CE . LYS B 41 ? 0.2554 0.4757 0.5063 0.0043 -0.0291 -0.0314 41 LYS B CE 2516 N NZ . LYS B 41 ? 0.3135 0.5852 0.5879 0.0166 -0.0199 -0.0291 41 LYS B NZ 2517 N N . ASN B 42 ? 0.2778 0.3474 0.4706 -0.0339 -0.0721 -0.0628 42 ASN B N 2518 C CA . ASN B 42 ? 0.3134 0.3848 0.5209 -0.0399 -0.0987 -0.0801 42 ASN B CA 2519 C C . ASN B 42 ? 0.3467 0.3829 0.5711 -0.0616 -0.1135 -0.0816 42 ASN B C 2520 O O . ASN B 42 ? 0.3699 0.4111 0.6290 -0.0829 -0.1327 -0.0821 42 ASN B O 2521 C CB . ASN B 42 ? 0.2964 0.4126 0.5361 -0.0464 -0.1046 -0.0769 42 ASN B CB 2522 C CG . ASN B 42 ? 0.2884 0.4344 0.5125 -0.0224 -0.0955 -0.0747 42 ASN B CG 2523 O OD1 . ASN B 42 ? 0.2794 0.4148 0.4690 -0.0029 -0.0937 -0.0792 42 ASN B OD1 2524 N ND2 . ASN B 42 ? 0.2529 0.4394 0.5043 -0.0236 -0.0913 -0.0661 42 ASN B ND2 2525 N N . GLY B 43 ? 0.3567 0.3572 0.5593 -0.0577 -0.1061 -0.0794 43 GLY B N 2526 C CA . GLY B 43 ? 0.4204 0.3753 0.6324 -0.0732 -0.1242 -0.0813 43 GLY B CA 2527 C C . GLY B 43 ? 0.4270 0.3766 0.6633 -0.1015 -0.1156 -0.0511 43 GLY B C 2528 O O . GLY B 43 ? 0.4550 0.3606 0.6952 -0.1135 -0.1302 -0.0468 43 GLY B O 2529 N N . GLU B 44 ? 0.3977 0.3950 0.6502 -0.1101 -0.0938 -0.0301 44 GLU B N 2530 C CA . GLU B 44 ? 0.4052 0.4173 0.6808 -0.1362 -0.0826 0.0015 44 GLU B CA 2531 C C . GLU B 44 ? 0.3746 0.3998 0.6245 -0.1233 -0.0522 0.0153 44 GLU B C 2532 O O . GLU B 44 ? 0.3545 0.4018 0.5870 -0.1007 -0.0365 0.0065 44 GLU B O 2533 C CB . GLU B 44 ? 0.4066 0.4753 0.7252 -0.1559 -0.0831 0.0143 44 GLU B CB 2534 C CG . GLU B 44 ? 0.4590 0.5123 0.8056 -0.1702 -0.1186 -0.0021 44 GLU B CG 2535 C CD . GLU B 44 ? 0.5020 0.6072 0.9023 -0.2008 -0.1252 0.0165 44 GLU B CD 2536 O OE1 . GLU B 44 ? 0.5156 0.6691 0.9293 -0.1906 -0.1249 0.0050 44 GLU B OE1 2537 O OE2 . GLU B 44 ? 0.5526 0.6517 0.9837 -0.2362 -0.1328 0.0447 44 GLU B OE2 2538 N N . ARG B 45 ? 0.3899 0.3974 0.6375 -0.1378 -0.0482 0.0367 45 ARG B N 2539 C CA . ARG B 45 ? 0.3767 0.3984 0.6005 -0.1279 -0.0230 0.0503 45 ARG B CA 2540 C C . ARG B 45 ? 0.3531 0.4397 0.5820 -0.1168 0.0003 0.0538 45 ARG B C 2541 O O . ARG B 45 ? 0.3547 0.4910 0.6157 -0.1313 0.0031 0.0665 45 ARG B O 2542 C CB . ARG B 45 ? 0.4120 0.4218 0.6433 -0.1529 -0.0250 0.0815 45 ARG B CB 2543 C CG . ARG B 45 ? 0.4510 0.4651 0.6511 -0.1410 -0.0053 0.0929 45 ARG B CG 2544 C CD . ARG B 45 ? 0.5427 0.5412 0.7482 -0.1662 -0.0113 0.1272 45 ARG B CD 2545 N NE . ARG B 45 ? 0.6244 0.6594 0.8047 -0.1561 0.0131 0.1428 45 ARG B NE 2546 C CZ . ARG B 45 ? 0.6692 0.7772 0.8601 -0.1633 0.0339 0.1649 45 ARG B CZ 2547 N NH1 . ARG B 45 ? 0.6787 0.8327 0.9105 -0.1846 0.0338 0.1781 45 ARG B NH1 2548 N NH2 . ARG B 45 ? 0.6968 0.8378 0.8580 -0.1477 0.0539 0.1727 45 ARG B NH2 2549 N N . ILE B 46 ? 0.3473 0.4340 0.5469 -0.0899 0.0143 0.0408 46 ILE B N 2550 C CA . ILE B 46 ? 0.3423 0.4831 0.5432 -0.0735 0.0327 0.0402 46 ILE B CA 2551 C C . ILE B 46 ? 0.3713 0.5426 0.5649 -0.0787 0.0495 0.0613 46 ILE B C 2552 O O . ILE B 46 ? 0.3824 0.5193 0.5522 -0.0804 0.0496 0.0673 46 ILE B O 2553 C CB . ILE B 46 ? 0.3276 0.4475 0.5020 -0.0427 0.0346 0.0171 46 ILE B CB 2554 C CG1 . ILE B 46 ? 0.2993 0.3994 0.4780 -0.0384 0.0195 0.0030 46 ILE B CG1 2555 C CG2 . ILE B 46 ? 0.3227 0.4875 0.4957 -0.0198 0.0482 0.0114 46 ILE B CG2 2556 C CD1 . ILE B 46 ? 0.2843 0.3583 0.4385 -0.0155 0.0184 -0.0105 46 ILE B CD1 2557 N N . GLU B 47 ? 0.3972 0.6402 0.6107 -0.0791 0.0636 0.0726 47 GLU B N 2558 C CA . GLU B 47 ? 0.4388 0.7310 0.6465 -0.0839 0.0816 0.0962 47 GLU B CA 2559 C C . GLU B 47 ? 0.4381 0.7350 0.6057 -0.0511 0.0945 0.0807 47 GLU B C 2560 O O . GLU B 47 ? 0.4645 0.7603 0.6091 -0.0544 0.1012 0.0957 47 GLU B O 2561 C CB . GLU B 47 ? 0.4544 0.8384 0.6997 -0.0938 0.0938 0.1138 47 GLU B CB 2562 C CG . GLU B 47 ? 0.5272 0.9170 0.8182 -0.1367 0.0800 0.1400 47 GLU B CG 2563 C CD . GLU B 47 ? 0.6216 0.9654 0.9085 -0.1690 0.0706 0.1704 47 GLU B CD 2564 O OE1 . GLU B 47 ? 0.6630 1.0549 0.9494 -0.1826 0.0859 0.2045 47 GLU B OE1 2565 O OE2 . GLU B 47 ? 0.6374 0.8997 0.9204 -0.1781 0.0470 0.1601 47 GLU B OE2 2566 N N . LYS B 48 ? 0.4236 0.7231 0.5828 -0.0190 0.0946 0.0508 48 LYS B N 2567 C CA . LYS B 48 ? 0.4416 0.7471 0.5672 0.0138 0.1018 0.0316 48 LYS B CA 2568 C C . LYS B 48 ? 0.4343 0.6582 0.5352 0.0221 0.0869 0.0125 48 LYS B C 2569 O O . LYS B 48 ? 0.4504 0.6432 0.5535 0.0363 0.0759 -0.0076 48 LYS B O 2570 C CB . LYS B 48 ? 0.4497 0.8117 0.5833 0.0467 0.1079 0.0106 48 LYS B CB 2571 N N . VAL B 49 ? 0.4176 0.6087 0.4979 0.0106 0.0854 0.0230 49 VAL B N 2572 C CA . VAL B 49 ? 0.3882 0.5125 0.4497 0.0152 0.0721 0.0083 49 VAL B CA 2573 C C . VAL B 49 ? 0.4027 0.5250 0.4324 0.0281 0.0746 0.0040 49 VAL B C 2574 O O . VAL B 49 ? 0.4086 0.5541 0.4286 0.0183 0.0826 0.0247 49 VAL B O 2575 C CB . VAL B 49 ? 0.3754 0.4558 0.4463 -0.0095 0.0617 0.0206 49 VAL B CB 2576 C CG1 . VAL B 49 ? 0.3856 0.4135 0.4378 -0.0029 0.0509 0.0074 49 VAL B CG1 2577 C CG2 . VAL B 49 ? 0.3294 0.4122 0.4285 -0.0183 0.0555 0.0189 49 VAL B CG2 2578 N N . GLU B 50 ? 0.3921 0.4870 0.4061 0.0493 0.0654 -0.0213 50 GLU B N 2579 C CA . GLU B 50 ? 0.4048 0.4984 0.3886 0.0642 0.0635 -0.0312 50 GLU B CA 2580 C C . GLU B 50 ? 0.3850 0.4245 0.3616 0.0528 0.0508 -0.0305 50 GLU B C 2581 O O . GLU B 50 ? 0.3614 0.3681 0.3547 0.0388 0.0440 -0.0269 50 GLU B O 2582 C CB . GLU B 50 ? 0.4387 0.5386 0.4125 0.0970 0.0564 -0.0635 50 GLU B CB 2583 C CG . GLU B 50 ? 0.5107 0.6784 0.4874 0.1184 0.0694 -0.0699 50 GLU B CG 2584 C CD . GLU B 50 ? 0.6368 0.8665 0.5878 0.1284 0.0845 -0.0621 50 GLU B CD 2585 O OE1 . GLU B 50 ? 0.6899 0.9023 0.6181 0.1203 0.0822 -0.0532 50 GLU B OE1 2586 O OE2 . GLU B 50 ? 0.6957 0.9985 0.6484 0.1461 0.0989 -0.0637 50 GLU B OE2 2587 N N . HIS B 51 ? 0.3888 0.4253 0.3403 0.0605 0.0470 -0.0345 51 HIS B N 2588 C CA . HIS B 51 ? 0.3951 0.3877 0.3436 0.0533 0.0333 -0.0376 51 HIS B CA 2589 C C . HIS B 51 ? 0.4278 0.4178 0.3513 0.0709 0.0229 -0.0565 51 HIS B C 2590 O O . HIS B 51 ? 0.4396 0.4644 0.3416 0.0893 0.0279 -0.0646 51 HIS B O 2591 C CB . HIS B 51 ? 0.3864 0.3677 0.3383 0.0333 0.0352 -0.0127 51 HIS B CB 2592 C CG . HIS B 51 ? 0.4571 0.4647 0.3890 0.0316 0.0428 0.0080 51 HIS B CG 2593 N ND1 . HIS B 51 ? 0.5205 0.5269 0.4257 0.0408 0.0365 0.0070 51 HIS B ND1 2594 C CD2 . HIS B 51 ? 0.4760 0.5153 0.4122 0.0196 0.0549 0.0344 51 HIS B CD2 2595 C CE1 . HIS B 51 ? 0.5553 0.5911 0.4451 0.0362 0.0455 0.0333 51 HIS B CE1 2596 N NE2 . HIS B 51 ? 0.5425 0.5989 0.4526 0.0213 0.0570 0.0521 51 HIS B NE2 2597 N N . SER B 52 ? 0.4367 0.3919 0.3641 0.0663 0.0074 -0.0647 52 SER B N 2598 C CA . SER B 52 ? 0.4866 0.4356 0.3957 0.0809 -0.0082 -0.0858 52 SER B CA 2599 C C . SER B 52 ? 0.5115 0.4772 0.3956 0.0817 -0.0054 -0.0723 52 SER B C 2600 O O . SER B 52 ? 0.5031 0.4764 0.3880 0.0689 0.0062 -0.0454 52 SER B O 2601 C CB . SER B 52 ? 0.4825 0.3944 0.4133 0.0707 -0.0269 -0.0952 52 SER B CB 2602 O OG . SER B 52 ? 0.4376 0.3429 0.3811 0.0530 -0.0240 -0.0760 52 SER B OG 2603 N N . ASP B 53 ? 0.5482 0.5168 0.4102 0.0969 -0.0193 -0.0906 53 ASP B N 2604 C CA . ASP B 53 ? 0.5905 0.5726 0.4275 0.0990 -0.0206 -0.0771 53 ASP B CA 2605 C C . ASP B 53 ? 0.5677 0.5212 0.4232 0.0834 -0.0310 -0.0674 53 ASP B C 2606 O O . ASP B 53 ? 0.5740 0.5066 0.4518 0.0783 -0.0450 -0.0831 53 ASP B O 2607 C CB . ASP B 53 ? 0.6316 0.6319 0.4359 0.1244 -0.0343 -0.1039 53 ASP B CB 2608 C CG . ASP B 53 ? 0.7080 0.7529 0.4874 0.1464 -0.0210 -0.1123 53 ASP B CG 2609 O OD1 . ASP B 53 ? 0.7483 0.8326 0.5133 0.1431 0.0002 -0.0823 53 ASP B OD1 2610 O OD2 . ASP B 53 ? 0.7796 0.8222 0.5569 0.1669 -0.0327 -0.1477 53 ASP B OD2 2611 N N . LEU B 54 ? 0.5741 0.5286 0.4232 0.0762 -0.0255 -0.0407 54 LEU B N 2612 C CA . LEU B 54 ? 0.5587 0.4915 0.4244 0.0685 -0.0369 -0.0353 54 LEU B CA 2613 C C . LEU B 54 ? 0.5623 0.4970 0.4242 0.0779 -0.0569 -0.0568 54 LEU B C 2614 O O . LEU B 54 ? 0.6038 0.5549 0.4355 0.0925 -0.0635 -0.0635 54 LEU B O 2615 C CB . LEU B 54 ? 0.5803 0.5092 0.4321 0.0666 -0.0356 -0.0066 54 LEU B CB 2616 C CG . LEU B 54 ? 0.5790 0.4874 0.4439 0.0665 -0.0495 -0.0024 54 LEU B CG 2617 C CD1 . LEU B 54 ? 0.5291 0.4182 0.4250 0.0556 -0.0455 -0.0003 54 LEU B CD1 2618 C CD2 . LEU B 54 ? 0.6162 0.5197 0.4554 0.0721 -0.0557 0.0233 54 LEU B CD2 2619 N N . SER B 55 ? 0.5315 0.4557 0.4247 0.0693 -0.0672 -0.0674 55 SER B N 2620 C CA . SER B 55 ? 0.5282 0.4591 0.4246 0.0741 -0.0885 -0.0818 55 SER B CA 2621 C C . SER B 55 ? 0.4845 0.4182 0.4124 0.0655 -0.0928 -0.0749 55 SER B C 2622 O O . SER B 55 ? 0.4590 0.3867 0.3951 0.0618 -0.0808 -0.0600 55 SER B O 2623 C CB . SER B 55 ? 0.5364 0.4639 0.4397 0.0748 -0.1049 -0.1090 55 SER B CB 2624 O OG . SER B 55 ? 0.5763 0.5156 0.4658 0.0857 -0.1263 -0.1231 55 SER B OG 2625 N N . PHE B 56 ? 0.4648 0.4122 0.4108 0.0641 -0.1113 -0.0871 56 PHE B N 2626 C CA . PHE B 56 ? 0.4567 0.4223 0.4330 0.0601 -0.1144 -0.0810 56 PHE B CA 2627 C C . PHE B 56 ? 0.4599 0.4469 0.4740 0.0460 -0.1304 -0.0921 56 PHE B C 2628 O O . PHE B 56 ? 0.4795 0.4596 0.4920 0.0424 -0.1469 -0.1077 56 PHE B O 2629 C CB . PHE B 56 ? 0.4366 0.4078 0.3941 0.0785 -0.1207 -0.0731 56 PHE B CB 2630 C CG . PHE B 56 ? 0.4763 0.4578 0.4119 0.0908 -0.1405 -0.0829 56 PHE B CG 2631 C CD1 . PHE B 56 ? 0.4352 0.4448 0.3963 0.0899 -0.1607 -0.0961 56 PHE B CD1 2632 C CD2 . PHE B 56 ? 0.4609 0.4315 0.3506 0.1036 -0.1392 -0.0771 56 PHE B CD2 2633 C CE1 . PHE B 56 ? 0.4732 0.4941 0.4139 0.1028 -0.1820 -0.1074 56 PHE B CE1 2634 C CE2 . PHE B 56 ? 0.5050 0.4902 0.3700 0.1179 -0.1579 -0.0867 56 PHE B CE2 2635 C CZ . PHE B 56 ? 0.5143 0.5218 0.4039 0.1185 -0.1809 -0.1038 56 PHE B CZ 2636 N N . SER B 57 ? 0.4472 0.4626 0.4959 0.0384 -0.1266 -0.0839 57 SER B N 2637 C CA . SER B 57 ? 0.4508 0.4983 0.5440 0.0191 -0.1388 -0.0854 57 SER B CA 2638 C C . SER B 57 ? 0.4685 0.5548 0.5763 0.0273 -0.1567 -0.0915 57 SER B C 2639 O O . SER B 57 ? 0.4805 0.5655 0.5614 0.0508 -0.1598 -0.0942 57 SER B O 2640 C CB . SER B 57 ? 0.4295 0.5034 0.5529 0.0070 -0.1221 -0.0699 57 SER B CB 2641 O OG . SER B 57 ? 0.4507 0.4922 0.5604 0.0021 -0.1059 -0.0635 57 SER B OG 2642 N N . LYS B 58 ? 0.4699 0.5932 0.6238 0.0062 -0.1701 -0.0907 58 LYS B N 2643 C CA . LYS B 58 ? 0.4781 0.6501 0.6572 0.0097 -0.1893 -0.0964 58 LYS B CA 2644 C C . LYS B 58 ? 0.4648 0.6747 0.6421 0.0359 -0.1794 -0.0922 58 LYS B C 2645 O O . LYS B 58 ? 0.4927 0.7260 0.6689 0.0533 -0.1956 -0.1006 58 LYS B O 2646 C CB . LYS B 58 ? 0.4757 0.6901 0.7154 -0.0244 -0.2023 -0.0886 58 LYS B CB 2647 N N . ASP B 59 ? 0.4327 0.6472 0.6088 0.0420 -0.1565 -0.0820 59 ASP B N 2648 C CA . ASP B 59 ? 0.4305 0.6741 0.6039 0.0720 -0.1519 -0.0839 59 ASP B CA 2649 C C . ASP B 59 ? 0.4406 0.6240 0.5624 0.0987 -0.1520 -0.0869 59 ASP B C 2650 O O . ASP B 59 ? 0.4393 0.6252 0.5536 0.1249 -0.1508 -0.0887 59 ASP B O 2651 C CB . ASP B 59 ? 0.4060 0.6960 0.6056 0.0710 -0.1323 -0.0759 59 ASP B CB 2652 C CG . ASP B 59 ? 0.4352 0.6777 0.6099 0.0667 -0.1129 -0.0698 59 ASP B CG 2653 O OD1 . ASP B 59 ? 0.4554 0.7289 0.6384 0.0762 -0.0989 -0.0681 59 ASP B OD1 2654 O OD2 . ASP B 59 ? 0.4441 0.6251 0.5914 0.0562 -0.1121 -0.0684 59 ASP B OD2 2655 N N . TRP B 60 ? 0.4312 0.5635 0.5192 0.0922 -0.1557 -0.0869 60 TRP B N 2656 C CA . TRP B 60 ? 0.4365 0.5172 0.4762 0.1103 -0.1553 -0.0819 60 TRP B CA 2657 C C . TRP B 60 ? 0.4332 0.4757 0.4569 0.1083 -0.1359 -0.0721 60 TRP B C 2658 O O . TRP B 60 ? 0.4499 0.4512 0.4386 0.1166 -0.1348 -0.0625 60 TRP B O 2659 C CB . TRP B 60 ? 0.4555 0.5424 0.4841 0.1398 -0.1715 -0.0820 60 TRP B CB 2660 C CG . TRP B 60 ? 0.4514 0.5783 0.4934 0.1450 -0.1937 -0.0921 60 TRP B CG 2661 C CD1 . TRP B 60 ? 0.4369 0.6224 0.5176 0.1540 -0.2044 -0.1001 60 TRP B CD1 2662 C CD2 . TRP B 60 ? 0.4818 0.5996 0.4994 0.1429 -0.2092 -0.0973 60 TRP B CD2 2663 N NE1 . TRP B 60 ? 0.4470 0.6580 0.5327 0.1548 -0.2268 -0.1087 60 TRP B NE1 2664 C CE2 . TRP B 60 ? 0.4791 0.6469 0.5242 0.1491 -0.2313 -0.1087 60 TRP B CE2 2665 C CE3 . TRP B 60 ? 0.5046 0.5843 0.4798 0.1388 -0.2068 -0.0951 60 TRP B CE3 2666 C CZ2 . TRP B 60 ? 0.5126 0.6866 0.5426 0.1507 -0.2540 -0.1198 60 TRP B CZ2 2667 C CZ3 . TRP B 60 ? 0.5123 0.6018 0.4691 0.1438 -0.2274 -0.1070 60 TRP B CZ3 2668 C CH2 . TRP B 60 ? 0.5415 0.6743 0.5248 0.1494 -0.2520 -0.1201 60 TRP B CH2 2669 N N . SER B 61 ? 0.4012 0.4599 0.4505 0.0956 -0.1216 -0.0719 61 SER B N 2670 C CA . SER B 61 ? 0.4053 0.4323 0.4421 0.0953 -0.1063 -0.0655 61 SER B CA 2671 C C . SER B 61 ? 0.3961 0.3905 0.4158 0.0770 -0.0959 -0.0599 61 SER B C 2672 O O . SER B 61 ? 0.3856 0.3888 0.4146 0.0621 -0.0983 -0.0643 61 SER B O 2673 C CB . SER B 61 ? 0.3821 0.4453 0.4477 0.0948 -0.0959 -0.0685 61 SER B CB 2674 O OG . SER B 61 ? 0.3738 0.4651 0.4643 0.0701 -0.0888 -0.0647 61 SER B OG 2675 N N . PHE B 62 ? 0.3995 0.3575 0.3976 0.0785 -0.0869 -0.0513 62 PHE B N 2676 C CA . PHE B 62 ? 0.4042 0.3388 0.3835 0.0663 -0.0772 -0.0460 62 PHE B CA 2677 C C . PHE B 62 ? 0.3892 0.3259 0.3858 0.0514 -0.0638 -0.0470 62 PHE B C 2678 O O . PHE B 62 ? 0.3504 0.3004 0.3658 0.0511 -0.0593 -0.0475 62 PHE B O 2679 C CB . PHE B 62 ? 0.4308 0.3338 0.3825 0.0713 -0.0743 -0.0306 62 PHE B CB 2680 C CG . PHE B 62 ? 0.4725 0.3695 0.4005 0.0848 -0.0879 -0.0228 62 PHE B CG 2681 C CD1 . PHE B 62 ? 0.5074 0.4143 0.4114 0.0867 -0.0909 -0.0233 62 PHE B CD1 2682 C CD2 . PHE B 62 ? 0.5023 0.3836 0.4297 0.0989 -0.1004 -0.0163 62 PHE B CD2 2683 C CE1 . PHE B 62 ? 0.5227 0.4291 0.4007 0.1007 -0.1045 -0.0141 62 PHE B CE1 2684 C CE2 . PHE B 62 ? 0.5344 0.4082 0.4388 0.1125 -0.1156 -0.0056 62 PHE B CE2 2685 C CZ . PHE B 62 ? 0.5409 0.4299 0.4193 0.1124 -0.1166 -0.0026 62 PHE B CZ 2686 N N . TYR B 63 ? 0.4035 0.3298 0.3915 0.0426 -0.0587 -0.0484 63 TYR B N 2687 C CA . TYR B 63 ? 0.3868 0.3089 0.3869 0.0313 -0.0476 -0.0470 63 TYR B CA 2688 C C . TYR B 63 ? 0.4060 0.3123 0.3855 0.0317 -0.0399 -0.0457 63 TYR B C 2689 O O . TYR B 63 ? 0.4136 0.3194 0.3719 0.0393 -0.0449 -0.0504 63 TYR B O 2690 C CB . TYR B 63 ? 0.3834 0.3200 0.4102 0.0190 -0.0537 -0.0519 63 TYR B CB 2691 C CG . TYR B 63 ? 0.4304 0.3602 0.4546 0.0171 -0.0685 -0.0635 63 TYR B CG 2692 C CD1 . TYR B 63 ? 0.4798 0.3882 0.4934 0.0175 -0.0693 -0.0715 63 TYR B CD1 2693 C CD2 . TYR B 63 ? 0.4260 0.3723 0.4597 0.0173 -0.0847 -0.0701 63 TYR B CD2 2694 C CE1 . TYR B 63 ? 0.4932 0.3911 0.5024 0.0205 -0.0881 -0.0891 63 TYR B CE1 2695 C CE2 . TYR B 63 ? 0.4838 0.4205 0.5156 0.0161 -0.1041 -0.0857 63 TYR B CE2 2696 C CZ . TYR B 63 ? 0.4944 0.4043 0.5124 0.0188 -0.1062 -0.0965 63 TYR B CZ 2697 O OH . TYR B 63 ? 0.5500 0.4462 0.5637 0.0224 -0.1291 -0.1180 63 TYR B OH 2698 N N . LEU B 64 ? 0.3907 0.2917 0.3768 0.0257 -0.0285 -0.0408 64 LEU B N 2699 C CA . LEU B 64 ? 0.4067 0.3037 0.3803 0.0265 -0.0190 -0.0389 64 LEU B CA 2700 C C . LEU B 64 ? 0.3717 0.2673 0.3636 0.0195 -0.0136 -0.0402 64 LEU B C 2701 O O . LEU B 64 ? 0.3603 0.2584 0.3678 0.0136 -0.0121 -0.0358 64 LEU B O 2702 C CB . LEU B 64 ? 0.4307 0.3248 0.3935 0.0255 -0.0112 -0.0229 64 LEU B CB 2703 C CG . LEU B 64 ? 0.5239 0.4221 0.4606 0.0320 -0.0127 -0.0135 64 LEU B CG 2704 C CD1 . LEU B 64 ? 0.5622 0.4480 0.4962 0.0259 -0.0122 0.0082 64 LEU B CD1 2705 C CD2 . LEU B 64 ? 0.5391 0.4573 0.4612 0.0368 -0.0034 -0.0161 64 LEU B CD2 2706 N N . LEU B 65 ? 0.3628 0.2575 0.3508 0.0238 -0.0119 -0.0474 65 LEU B N 2707 C CA . LEU B 65 ? 0.3396 0.2319 0.3424 0.0205 -0.0080 -0.0469 65 LEU B CA 2708 C C . LEU B 65 ? 0.3444 0.2504 0.3396 0.0248 0.0047 -0.0425 65 LEU B C 2709 O O . LEU B 65 ? 0.3359 0.2547 0.3151 0.0357 0.0076 -0.0480 65 LEU B O 2710 C CB . LEU B 65 ? 0.3436 0.2217 0.3518 0.0250 -0.0209 -0.0604 65 LEU B CB 2711 C CG . LEU B 65 ? 0.3446 0.2156 0.3666 0.0248 -0.0206 -0.0588 65 LEU B CG 2712 C CD1 . LEU B 65 ? 0.3379 0.2122 0.3778 0.0096 -0.0184 -0.0424 65 LEU B CD1 2713 C CD2 . LEU B 65 ? 0.3780 0.2243 0.4039 0.0333 -0.0391 -0.0742 65 LEU B CD2 2714 N N . TYR B 66 ? 0.3264 0.2364 0.3341 0.0169 0.0113 -0.0329 66 TYR B N 2715 C CA . TYR B 66 ? 0.3391 0.2676 0.3496 0.0174 0.0212 -0.0278 66 TYR B CA 2716 C C . TYR B 66 ? 0.3360 0.2659 0.3604 0.0219 0.0198 -0.0342 66 TYR B C 2717 O O . TYR B 66 ? 0.3128 0.2294 0.3472 0.0172 0.0136 -0.0333 66 TYR B O 2718 C CB . TYR B 66 ? 0.3509 0.2794 0.3694 0.0047 0.0238 -0.0142 66 TYR B CB 2719 C CG . TYR B 66 ? 0.3714 0.2974 0.3773 0.0004 0.0240 -0.0022 66 TYR B CG 2720 C CD1 . TYR B 66 ? 0.3720 0.3180 0.3774 -0.0069 0.0316 0.0141 66 TYR B CD1 2721 C CD2 . TYR B 66 ? 0.4108 0.3188 0.4066 0.0034 0.0156 -0.0043 66 TYR B CD2 2722 C CE1 . TYR B 66 ? 0.4519 0.3938 0.4448 -0.0127 0.0300 0.0319 66 TYR B CE1 2723 C CE2 . TYR B 66 ? 0.4227 0.3247 0.4055 0.0015 0.0127 0.0089 66 TYR B CE2 2724 C CZ . TYR B 66 ? 0.4373 0.3529 0.4175 -0.0073 0.0194 0.0284 66 TYR B CZ 2725 O OH . TYR B 66 ? 0.5376 0.4445 0.5043 -0.0112 0.0146 0.0479 66 TYR B OH 2726 N N . TYR B 67 ? 0.3386 0.2903 0.3638 0.0318 0.0256 -0.0383 67 TYR B N 2727 C CA . TYR B 67 ? 0.3373 0.2878 0.3749 0.0405 0.0209 -0.0453 67 TYR B CA 2728 C C . TYR B 67 ? 0.3437 0.3320 0.3890 0.0498 0.0300 -0.0464 67 TYR B C 2729 O O . TYR B 67 ? 0.3216 0.3436 0.3602 0.0522 0.0411 -0.0430 67 TYR B O 2730 C CB . TYR B 67 ? 0.3645 0.2890 0.3962 0.0543 0.0065 -0.0613 67 TYR B CB 2731 C CG . TYR B 67 ? 0.3926 0.3292 0.4058 0.0730 0.0061 -0.0781 67 TYR B CG 2732 C CD1 . TYR B 67 ? 0.3876 0.3202 0.3839 0.0701 0.0048 -0.0795 67 TYR B CD1 2733 C CD2 . TYR B 67 ? 0.4149 0.3715 0.4259 0.0976 0.0054 -0.0949 67 TYR B CD2 2734 C CE1 . TYR B 67 ? 0.4188 0.3679 0.3932 0.0900 0.0034 -0.0963 67 TYR B CE1 2735 C CE2 . TYR B 67 ? 0.4622 0.4387 0.4515 0.1205 0.0047 -0.1146 67 TYR B CE2 2736 C CZ . TYR B 67 ? 0.4527 0.4246 0.4224 0.1156 0.0036 -0.1146 67 TYR B CZ 2737 O OH . TYR B 67 ? 0.5056 0.4999 0.4495 0.1401 0.0011 -0.1352 67 TYR B OH 2738 N N . THR B 68 ? 0.3398 0.3286 0.4002 0.0557 0.0250 -0.0490 68 THR B N 2739 C CA . THR B 68 ? 0.3427 0.3740 0.4168 0.0652 0.0320 -0.0503 68 THR B CA 2740 C C . THR B 68 ? 0.3675 0.3850 0.4515 0.0814 0.0191 -0.0593 68 THR B C 2741 O O . THR B 68 ? 0.3597 0.3423 0.4455 0.0738 0.0083 -0.0531 68 THR B O 2742 C CB . THR B 68 ? 0.3286 0.3866 0.4195 0.0432 0.0404 -0.0330 68 THR B CB 2743 O OG1 . THR B 68 ? 0.3804 0.4939 0.4868 0.0500 0.0498 -0.0318 68 THR B OG1 2744 C CG2 . THR B 68 ? 0.3162 0.3556 0.4187 0.0343 0.0309 -0.0293 68 THR B CG2 2745 N N . GLU B 69 ? 0.3956 0.4439 0.4851 0.1057 0.0197 -0.0726 69 GLU B N 2746 C CA . GLU B 69 ? 0.4357 0.4755 0.5371 0.1249 0.0058 -0.0804 69 GLU B CA 2747 C C . GLU B 69 ? 0.4185 0.4819 0.5394 0.1098 0.0093 -0.0649 69 GLU B C 2748 O O . GLU B 69 ? 0.4067 0.5155 0.5395 0.0967 0.0230 -0.0570 69 GLU B O 2749 C CB . GLU B 69 ? 0.4668 0.5452 0.5695 0.1601 0.0063 -0.1027 69 GLU B CB 2750 C CG . GLU B 69 ? 0.5614 0.6374 0.6788 0.1864 -0.0096 -0.1130 69 GLU B CG 2751 C CD . GLU B 69 ? 0.6906 0.7805 0.8022 0.2306 -0.0188 -0.1446 69 GLU B CD 2752 O OE1 . GLU B 69 ? 0.7583 0.8491 0.8497 0.2413 -0.0161 -0.1608 69 GLU B OE1 2753 O OE2 . GLU B 69 ? 0.7811 0.8807 0.9067 0.2585 -0.0313 -0.1559 69 GLU B OE2 2754 N N . PHE B 70 ? 0.4200 0.4531 0.5446 0.1093 -0.0049 -0.0585 70 PHE B N 2755 C CA . PHE B 70 ? 0.3928 0.4516 0.5331 0.1002 -0.0052 -0.0482 70 PHE B CA 2756 C C . PHE B 70 ? 0.4246 0.4654 0.5689 0.1174 -0.0233 -0.0465 70 PHE B C 2757 O O . PHE B 70 ? 0.4634 0.4593 0.5985 0.1292 -0.0372 -0.0480 70 PHE B O 2758 C CB . PHE B 70 ? 0.3694 0.4192 0.5049 0.0716 -0.0009 -0.0351 70 PHE B CB 2759 C CG . PHE B 70 ? 0.3529 0.3612 0.4738 0.0655 -0.0106 -0.0253 70 PHE B CG 2760 C CD1 . PHE B 70 ? 0.3718 0.3410 0.4820 0.0707 -0.0177 -0.0249 70 PHE B CD1 2761 C CD2 . PHE B 70 ? 0.3556 0.3699 0.4748 0.0542 -0.0137 -0.0163 70 PHE B CD2 2762 C CE1 . PHE B 70 ? 0.3980 0.3397 0.5004 0.0604 -0.0256 -0.0095 70 PHE B CE1 2763 C CE2 . PHE B 70 ? 0.3435 0.3355 0.4493 0.0491 -0.0196 -0.0038 70 PHE B CE2 2764 C CZ . PHE B 70 ? 0.3800 0.3387 0.4794 0.0500 -0.0243 0.0026 70 PHE B CZ 2765 N N . THR B 71 ? 0.4344 0.5101 0.5946 0.1185 -0.0257 -0.0427 71 THR B N 2766 C CA . THR B 71 ? 0.4533 0.5170 0.6158 0.1326 -0.0436 -0.0361 71 THR B CA 2767 C C . THR B 71 ? 0.4474 0.5189 0.6059 0.1119 -0.0445 -0.0218 71 THR B C 2768 O O . THR B 71 ? 0.4348 0.5484 0.6080 0.1031 -0.0402 -0.0255 71 THR B O 2769 C CB . THR B 71 ? 0.4699 0.5749 0.6536 0.1609 -0.0492 -0.0489 71 THR B CB 2770 O OG1 . THR B 71 ? 0.4917 0.5858 0.6731 0.1869 -0.0514 -0.0667 71 THR B OG1 2771 C CG2 . THR B 71 ? 0.4929 0.5862 0.6788 0.1766 -0.0705 -0.0396 71 THR B CG2 2772 N N . PRO B 72 ? 0.4536 0.4880 0.5929 0.1033 -0.0512 -0.0059 72 PRO B N 2773 C CA . PRO B 72 ? 0.4466 0.4948 0.5763 0.0905 -0.0530 0.0050 72 PRO B CA 2774 C C . PRO B 72 ? 0.4655 0.5437 0.6033 0.1043 -0.0660 0.0069 72 PRO B C 2775 O O . PRO B 72 ? 0.4968 0.5688 0.6420 0.1248 -0.0777 0.0090 72 PRO B O 2776 C CB . PRO B 72 ? 0.4627 0.4751 0.5727 0.0836 -0.0575 0.0261 72 PRO B CB 2777 C CG . PRO B 72 ? 0.4693 0.4407 0.5818 0.0885 -0.0609 0.0252 72 PRO B CG 2778 C CD . PRO B 72 ? 0.4765 0.4598 0.6043 0.1056 -0.0587 0.0025 72 PRO B CD 2779 N N . THR B 73 ? 0.4644 0.5734 0.6005 0.0954 -0.0671 0.0036 73 THR B N 2780 C CA . THR B 73 ? 0.4787 0.6216 0.6206 0.1071 -0.0818 0.0035 73 THR B CA 2781 C C . THR B 73 ? 0.4755 0.6290 0.5935 0.0993 -0.0858 0.0078 73 THR B C 2782 O O . THR B 73 ? 0.4611 0.6051 0.5679 0.0847 -0.0761 0.0029 73 THR B O 2783 C CB . THR B 73 ? 0.4652 0.6510 0.6401 0.1057 -0.0814 -0.0154 73 THR B CB 2784 O OG1 . THR B 73 ? 0.4863 0.6776 0.6803 0.1229 -0.0795 -0.0189 73 THR B OG1 2785 C CG2 . THR B 73 ? 0.5031 0.7297 0.6861 0.1111 -0.0982 -0.0205 73 THR B CG2 2786 N N . GLU B 74 ? 0.4810 0.6575 0.5892 0.1123 -0.1009 0.0156 74 GLU B N 2787 C CA . GLU B 74 ? 0.4923 0.6896 0.5719 0.1113 -0.1059 0.0181 74 GLU B CA 2788 C C . GLU B 74 ? 0.4670 0.6830 0.5526 0.1007 -0.1067 -0.0109 74 GLU B C 2789 O O . GLU B 74 ? 0.4845 0.7059 0.5461 0.0987 -0.1053 -0.0163 74 GLU B O 2790 C CB . GLU B 74 ? 0.5184 0.7446 0.5853 0.1298 -0.1243 0.0303 74 GLU B CB 2791 C CG . GLU B 74 ? 0.5670 0.7669 0.6238 0.1396 -0.1288 0.0649 74 GLU B CG 2792 C CD . GLU B 74 ? 0.6072 0.8336 0.6469 0.1582 -0.1482 0.0836 74 GLU B CD 2793 O OE1 . GLU B 74 ? 0.6435 0.9031 0.6525 0.1597 -0.1505 0.0906 74 GLU B OE1 2794 O OE2 . GLU B 74 ? 0.6795 0.8955 0.7344 0.1745 -0.1622 0.0916 74 GLU B OE2 2795 N N . LYS B 75 ? 0.4344 0.6617 0.5540 0.0943 -0.1106 -0.0290 75 LYS B N 2796 C CA . LYS B 75 ? 0.4224 0.6635 0.5551 0.0819 -0.1197 -0.0544 75 LYS B CA 2797 C C . LYS B 75 ? 0.3909 0.6021 0.5316 0.0622 -0.1073 -0.0620 75 LYS B C 2798 O O . LYS B 75 ? 0.3993 0.6082 0.5457 0.0518 -0.1180 -0.0817 75 LYS B O 2799 C CB . LYS B 75 ? 0.4319 0.7074 0.6039 0.0800 -0.1330 -0.0645 75 LYS B CB 2800 C CG . LYS B 75 ? 0.4836 0.7953 0.6482 0.0994 -0.1537 -0.0658 75 LYS B CG 2801 C CD . LYS B 75 ? 0.5429 0.8917 0.7492 0.1039 -0.1618 -0.0669 75 LYS B CD 2802 C CE . LYS B 75 ? 0.5347 0.8988 0.7894 0.0792 -0.1573 -0.0776 75 LYS B CE 2803 N NZ . LYS B 75 ? 0.5752 0.9976 0.8731 0.0831 -0.1724 -0.0834 75 LYS B NZ 2804 N N . ASP B 76 ? 0.3548 0.5403 0.4956 0.0584 -0.0884 -0.0477 76 ASP B N 2805 C CA . ASP B 76 ? 0.3370 0.4985 0.4878 0.0407 -0.0770 -0.0519 76 ASP B CA 2806 C C . ASP B 76 ? 0.3308 0.4642 0.4526 0.0404 -0.0687 -0.0497 76 ASP B C 2807 O O . ASP B 76 ? 0.3295 0.4572 0.4302 0.0500 -0.0623 -0.0345 76 ASP B O 2808 C CB . ASP B 76 ? 0.3259 0.4842 0.4946 0.0392 -0.0622 -0.0414 76 ASP B CB 2809 C CG . ASP B 76 ? 0.3440 0.5421 0.5467 0.0406 -0.0673 -0.0441 76 ASP B CG 2810 O OD1 . ASP B 76 ? 0.3749 0.5968 0.6014 0.0269 -0.0789 -0.0536 76 ASP B OD1 2811 O OD2 . ASP B 76 ? 0.3914 0.5983 0.5987 0.0567 -0.0628 -0.0376 76 ASP B OD2 2812 N N . GLU B 77 ? 0.3060 0.4224 0.4305 0.0285 -0.0705 -0.0626 77 GLU B N 2813 C CA . GLU B 77 ? 0.3065 0.4004 0.4078 0.0298 -0.0634 -0.0638 77 GLU B CA 2814 C C . GLU B 77 ? 0.2914 0.3585 0.4029 0.0167 -0.0497 -0.0562 77 GLU B C 2815 O O . GLU B 77 ? 0.2743 0.3387 0.4093 0.0030 -0.0516 -0.0576 77 GLU B O 2816 C CB . GLU B 77 ? 0.3248 0.4163 0.4178 0.0331 -0.0807 -0.0885 77 GLU B CB 2817 C CG . GLU B 77 ? 0.3837 0.4515 0.4620 0.0345 -0.0754 -0.0939 77 GLU B CG 2818 C CD . GLU B 77 ? 0.4543 0.5043 0.5342 0.0365 -0.0971 -0.1218 77 GLU B CD 2819 O OE1 . GLU B 77 ? 0.4901 0.5131 0.5959 0.0181 -0.1068 -0.1241 77 GLU B OE1 2820 O OE2 . GLU B 77 ? 0.4709 0.5355 0.5266 0.0571 -0.1060 -0.1407 77 GLU B OE2 2821 N N . TYR B 78 ? 0.2838 0.3358 0.3787 0.0197 -0.0371 -0.0463 78 TYR B N 2822 C CA . TYR B 78 ? 0.2799 0.3086 0.3801 0.0100 -0.0261 -0.0409 78 TYR B CA 2823 C C . TYR B 78 ? 0.2926 0.3053 0.3769 0.0114 -0.0260 -0.0470 78 TYR B C 2824 O O . TYR B 78 ? 0.3095 0.3361 0.3773 0.0223 -0.0294 -0.0515 78 TYR B O 2825 C CB . TYR B 78 ? 0.2753 0.2998 0.3741 0.0142 -0.0152 -0.0270 78 TYR B CB 2826 C CG . TYR B 78 ? 0.2684 0.3102 0.3848 0.0181 -0.0159 -0.0250 78 TYR B CG 2827 C CD1 . TYR B 78 ? 0.2369 0.2868 0.3698 0.0123 -0.0091 -0.0257 78 TYR B CD1 2828 C CD2 . TYR B 78 ? 0.3060 0.3641 0.4230 0.0292 -0.0238 -0.0217 78 TYR B CD2 2829 C CE1 . TYR B 78 ? 0.3107 0.3898 0.4626 0.0192 -0.0088 -0.0257 78 TYR B CE1 2830 C CE2 . TYR B 78 ? 0.2906 0.3701 0.4267 0.0366 -0.0265 -0.0225 78 TYR B CE2 2831 C CZ . TYR B 78 ? 0.2863 0.3784 0.4408 0.0324 -0.0181 -0.0258 78 TYR B CZ 2832 O OH . TYR B 78 ? 0.3363 0.4612 0.5115 0.0432 -0.0193 -0.0278 78 TYR B OH 2833 N N . ALA B 79 ? 0.2846 0.2748 0.3731 0.0026 -0.0230 -0.0469 79 ALA B N 2834 C CA . ALA B 79 ? 0.2992 0.2730 0.3756 0.0065 -0.0262 -0.0549 79 ALA B CA 2835 C C . ALA B 79 ? 0.3141 0.2651 0.3933 -0.0028 -0.0195 -0.0463 79 ALA B C 2836 O O . ALA B 79 ? 0.3029 0.2546 0.3939 -0.0131 -0.0141 -0.0366 79 ALA B O 2837 C CB . ALA B 79 ? 0.3203 0.2846 0.3997 0.0090 -0.0457 -0.0742 79 ALA B CB 2838 N N . CYS B 80 ? 0.3315 0.2692 0.3997 0.0029 -0.0208 -0.0505 80 CYS B N 2839 C CA . CYS B 80 ? 0.3379 0.2546 0.4042 -0.0029 -0.0173 -0.0427 80 CYS B CA 2840 C C . CYS B 80 ? 0.3576 0.2485 0.4229 0.0004 -0.0337 -0.0533 80 CYS B C 2841 O O . CYS B 80 ? 0.3697 0.2656 0.4276 0.0159 -0.0424 -0.0701 80 CYS B O 2842 C CB . CYS B 80 ? 0.3320 0.2557 0.3876 0.0034 -0.0078 -0.0385 80 CYS B CB 2843 S SG . CYS B 80 ? 0.3955 0.2986 0.4448 -0.0005 -0.0053 -0.0308 80 CYS B SG 2844 N N . ARG B 81 ? 0.3593 0.2248 0.4319 -0.0125 -0.0396 -0.0430 81 ARG B N 2845 C CA . ARG B 81 ? 0.3924 0.2205 0.4664 -0.0105 -0.0610 -0.0503 81 ARG B CA 2846 C C . ARG B 81 ? 0.4042 0.2145 0.4684 -0.0110 -0.0580 -0.0364 81 ARG B C 2847 O O . ARG B 81 ? 0.3714 0.1892 0.4361 -0.0250 -0.0453 -0.0148 81 ARG B O 2848 C CB . ARG B 81 ? 0.4186 0.2278 0.5140 -0.0305 -0.0762 -0.0434 81 ARG B CB 2849 C CG . ARG B 81 ? 0.4767 0.2356 0.5778 -0.0308 -0.1056 -0.0504 81 ARG B CG 2850 C CD . ARG B 81 ? 0.5344 0.2766 0.6586 -0.0625 -0.1123 -0.0219 81 ARG B CD 2851 N NE . ARG B 81 ? 0.6039 0.3523 0.7533 -0.0775 -0.1253 -0.0272 81 ARG B NE 2852 C CZ . ARG B 81 ? 0.6384 0.4082 0.8141 -0.1070 -0.1199 -0.0013 81 ARG B CZ 2853 N NH1 . ARG B 81 ? 0.6208 0.4128 0.7972 -0.1224 -0.0990 0.0320 81 ARG B NH1 2854 N NH2 . ARG B 81 ? 0.6393 0.4159 0.8410 -0.1193 -0.1360 -0.0100 81 ARG B NH2 2855 N N . VAL B 82 ? 0.4163 0.2099 0.4704 0.0076 -0.0699 -0.0503 82 VAL B N 2856 C CA . VAL B 82 ? 0.4192 0.2003 0.4622 0.0124 -0.0692 -0.0403 82 VAL B CA 2857 C C . VAL B 82 ? 0.4747 0.2075 0.5184 0.0193 -0.0962 -0.0440 82 VAL B C 2858 O O . VAL B 82 ? 0.5033 0.2219 0.5490 0.0378 -0.1156 -0.0699 82 VAL B O 2859 C CB . VAL B 82 ? 0.3962 0.2116 0.4290 0.0299 -0.0571 -0.0509 82 VAL B CB 2860 C CG1 . VAL B 82 ? 0.4016 0.2086 0.4243 0.0348 -0.0581 -0.0418 82 VAL B CG1 2861 C CG2 . VAL B 82 ? 0.3546 0.2054 0.3889 0.0207 -0.0360 -0.0444 82 VAL B CG2 2862 N N . ASN B 83 ? 0.4998 0.2060 0.5411 0.0066 -0.1006 -0.0188 83 ASN B N 2863 C CA . ASN B 83 ? 0.5472 0.2014 0.5869 0.0170 -0.1295 -0.0198 83 ASN B CA 2864 C C . ASN B 83 ? 0.5437 0.1987 0.5659 0.0290 -0.1267 -0.0092 83 ASN B C 2865 O O . ASN B 83 ? 0.5234 0.2034 0.5358 0.0172 -0.1071 0.0123 83 ASN B O 2866 C CB . ASN B 83 ? 0.6010 0.2069 0.6569 -0.0078 -0.1510 0.0021 83 ASN B CB 2867 C CG . ASN B 83 ? 0.7092 0.2497 0.7709 0.0091 -0.1926 -0.0169 83 ASN B CG 2868 O OD1 . ASN B 83 ? 0.7160 0.2518 0.7657 0.0435 -0.2031 -0.0444 83 ASN B OD1 2869 N ND2 . ASN B 83 ? 0.7752 0.2676 0.8577 -0.0144 -0.2180 -0.0025 83 ASN B ND2 2870 N N . HIS B 84 ? 0.5656 0.1958 0.5836 0.0560 -0.1488 -0.0280 84 HIS B N 2871 C CA . HIS B 84 ? 0.5507 0.1869 0.5545 0.0734 -0.1500 -0.0243 84 HIS B CA 2872 C C . HIS B 84 ? 0.6092 0.1937 0.6139 0.0997 -0.1862 -0.0391 84 HIS B C 2873 O O . HIS B 84 ? 0.6331 0.1937 0.6474 0.1131 -0.2063 -0.0649 84 HIS B O 2874 C CB . HIS B 84 ? 0.5025 0.2028 0.5036 0.0877 -0.1277 -0.0435 84 HIS B CB 2875 C CG . HIS B 84 ? 0.5282 0.2449 0.5187 0.1009 -0.1273 -0.0390 84 HIS B CG 2876 N ND1 . HIS B 84 ? 0.5162 0.2412 0.5084 0.1323 -0.1425 -0.0600 84 HIS B ND1 2877 C CD2 . HIS B 84 ? 0.5061 0.2348 0.4841 0.0892 -0.1163 -0.0176 84 HIS B CD2 2878 C CE1 . HIS B 84 ? 0.5031 0.2456 0.4871 0.1366 -0.1404 -0.0504 84 HIS B CE1 2879 N NE2 . HIS B 84 ? 0.5190 0.2610 0.4924 0.1111 -0.1258 -0.0254 84 HIS B NE2 2880 N N . VAL B 85 ? 0.6274 0.1910 0.6209 0.1086 -0.1982 -0.0233 85 VAL B N 2881 C CA . VAL B 85 ? 0.6987 0.2025 0.6928 0.1343 -0.2374 -0.0329 85 VAL B CA 2882 C C . VAL B 85 ? 0.7007 0.2264 0.6999 0.1775 -0.2488 -0.0827 85 VAL B C 2883 O O . VAL B 85 ? 0.7711 0.2455 0.7746 0.2039 -0.2850 -0.1050 85 VAL B O 2884 C CB . VAL B 85 ? 0.7187 0.2067 0.6966 0.1373 -0.2452 -0.0033 85 VAL B CB 2885 C CG1 . VAL B 85 ? 0.6686 0.2196 0.6384 0.1627 -0.2300 -0.0211 85 VAL B CG1 2886 C CG2 . VAL B 85 ? 0.8139 0.2205 0.7929 0.1497 -0.2885 0.0051 85 VAL B CG2 2887 N N . THR B 86 ? 0.6396 0.2435 0.6393 0.1856 -0.2196 -0.1000 86 THR B N 2888 C CA . THR B 86 ? 0.6511 0.2975 0.6561 0.2245 -0.2240 -0.1430 86 THR B CA 2889 C C . THR B 86 ? 0.6763 0.3215 0.6870 0.2283 -0.2287 -0.1696 86 THR B C 2890 O O . THR B 86 ? 0.6715 0.3538 0.6828 0.2645 -0.2347 -0.2071 86 THR B O 2891 C CB . THR B 86 ? 0.5789 0.3156 0.5866 0.2287 -0.1932 -0.1468 86 THR B CB 2892 O OG1 . THR B 86 ? 0.5171 0.2817 0.5260 0.1917 -0.1623 -0.1266 86 THR B OG1 2893 C CG2 . THR B 86 ? 0.5654 0.3103 0.5694 0.2372 -0.1969 -0.1337 86 THR B CG2 2894 N N . LEU B 87 ? 0.6885 0.3020 0.7030 0.1926 -0.2245 -0.1505 87 LEU B N 2895 C CA . LEU B 87 ? 0.7190 0.3337 0.7390 0.1929 -0.2295 -0.1740 87 LEU B CA 2896 C C . LEU B 87 ? 0.8115 0.3352 0.8392 0.1917 -0.2727 -0.1794 87 LEU B C 2897 O O . LEU B 87 ? 0.8509 0.3177 0.8834 0.1652 -0.2844 -0.1443 87 LEU B O 2898 C CB . LEU B 87 ? 0.6518 0.3028 0.6755 0.1550 -0.1964 -0.1514 87 LEU B CB 2899 C CG . LEU B 87 ? 0.5964 0.3262 0.6163 0.1499 -0.1581 -0.1431 87 LEU B CG 2900 C CD1 . LEU B 87 ? 0.5408 0.2847 0.5647 0.1127 -0.1332 -0.1175 87 LEU B CD1 2901 C CD2 . LEU B 87 ? 0.6084 0.4001 0.6259 0.1800 -0.1524 -0.1749 87 LEU B CD2 2902 N N . SER B 88 ? 0.8662 0.3761 0.8951 0.2211 -0.2993 -0.2224 88 SER B N 2903 C CA . SER B 88 ? 0.9622 0.3799 1.0026 0.2181 -0.3462 -0.2314 88 SER B CA 2904 C C . SER B 88 ? 0.9545 0.3555 1.0109 0.1712 -0.3421 -0.2094 88 SER B C 2905 O O . SER B 88 ? 1.0146 0.3388 1.0888 0.1450 -0.3737 -0.1910 88 SER B O 2906 C CB . SER B 88 ? 1.0263 0.4366 1.0610 0.2713 -0.3803 -0.2931 88 SER B CB 2907 O OG . SER B 88 ? 1.0237 0.5015 1.0528 0.2762 -0.3601 -0.3177 88 SER B OG 2908 N N . GLN B 89 ? 0.8826 0.3575 0.9354 0.1615 -0.3060 -0.2114 89 GLN B N 2909 C CA . GLN B 89 ? 0.8587 0.3368 0.9267 0.1206 -0.2961 -0.1911 89 GLN B CA 2910 C C . GLN B 89 ? 0.7632 0.3180 0.8246 0.1022 -0.2455 -0.1659 89 GLN B C 2911 O O . GLN B 89 ? 0.7214 0.3312 0.7672 0.1245 -0.2223 -0.1750 89 GLN B O 2912 C CB . GLN B 89 ? 0.8906 0.3670 0.9622 0.1366 -0.3198 -0.2340 89 GLN B CB 2913 C CG . GLN B 89 ? 0.8535 0.4150 0.9051 0.1676 -0.2954 -0.2658 89 GLN B CG 2914 C CD . GLN B 89 ? 0.9188 0.4706 0.9690 0.1909 -0.3283 -0.3137 89 GLN B CD 2915 O OE1 . GLN B 89 ? 0.9255 0.5360 0.9676 0.1941 -0.3121 -0.3260 89 GLN B OE1 2916 N NE2 . GLN B 89 ? 1.0188 0.4928 1.0767 0.2067 -0.3779 -0.3401 89 GLN B NE2 2917 N N . PRO B 90 ? 0.7334 0.2944 0.8090 0.0621 -0.2305 -0.1351 90 PRO B N 2918 C CA . PRO B 90 ? 0.6461 0.2736 0.7152 0.0498 -0.1876 -0.1166 90 PRO B CA 2919 C C . PRO B 90 ? 0.6109 0.2960 0.6677 0.0756 -0.1744 -0.1469 90 PRO B C 2920 O O . PRO B 90 ? 0.6288 0.3108 0.6860 0.0917 -0.1945 -0.1781 90 PRO B O 2921 C CB . PRO B 90 ? 0.6465 0.2720 0.7363 0.0108 -0.1824 -0.0900 90 PRO B CB 2922 C CG . PRO B 90 ? 0.7111 0.2651 0.8194 -0.0071 -0.2182 -0.0768 90 PRO B CG 2923 C CD . PRO B 90 ? 0.7691 0.2823 0.8705 0.0278 -0.2533 -0.1174 90 PRO B CD 2924 N N . LYS B 91 ? 0.5565 0.2931 0.6020 0.0807 -0.1441 -0.1378 91 LYS B N 2925 C CA . LYS B 91 ? 0.5386 0.3387 0.5746 0.0966 -0.1259 -0.1522 91 LYS B CA 2926 C C . LYS B 91 ? 0.4766 0.3022 0.5188 0.0715 -0.1054 -0.1329 91 LYS B C 2927 O O . LYS B 91 ? 0.4401 0.2650 0.4870 0.0498 -0.0884 -0.1058 91 LYS B O 2928 C CB . LYS B 91 ? 0.5164 0.3578 0.5440 0.1079 -0.1058 -0.1453 91 LYS B CB 2929 C CG . LYS B 91 ? 0.5543 0.4515 0.5722 0.1413 -0.1044 -0.1713 91 LYS B CG 2930 C CD . LYS B 91 ? 0.5094 0.4541 0.5276 0.1448 -0.0845 -0.1584 91 LYS B CD 2931 C CE . LYS B 91 ? 0.5946 0.5935 0.6071 0.1829 -0.0889 -0.1851 91 LYS B CE 2932 N NZ . LYS B 91 ? 0.5555 0.5808 0.5745 0.1913 -0.0831 -0.1787 91 LYS B NZ 2933 N N . ILE B 92 ? 0.4707 0.3220 0.5111 0.0786 -0.1082 -0.1488 92 ILE B N 2934 C CA . ILE B 92 ? 0.4420 0.3204 0.4880 0.0600 -0.0914 -0.1325 92 ILE B CA 2935 C C . ILE B 92 ? 0.4232 0.3599 0.4556 0.0733 -0.0724 -0.1315 92 ILE B C 2936 O O . ILE B 92 ? 0.4563 0.4232 0.4757 0.0985 -0.0787 -0.1532 92 ILE B O 2937 C CB . ILE B 92 ? 0.4696 0.3368 0.5257 0.0546 -0.1108 -0.1461 92 ILE B CB 2938 C CG1 . ILE B 92 ? 0.4861 0.2980 0.5632 0.0332 -0.1312 -0.1393 92 ILE B CG1 2939 C CG2 . ILE B 92 ? 0.4167 0.3180 0.4786 0.0400 -0.0935 -0.1293 92 ILE B CG2 2940 C CD1 . ILE B 92 ? 0.5770 0.3698 0.6682 0.0298 -0.1604 -0.1593 92 ILE B CD1 2941 N N . VAL B 93 ? 0.3846 0.3383 0.4203 0.0574 -0.0512 -0.1061 93 VAL B N 2942 C CA . VAL B 93 ? 0.3647 0.3673 0.3929 0.0620 -0.0353 -0.0956 93 VAL B CA 2943 C C . VAL B 93 ? 0.3325 0.3413 0.3661 0.0486 -0.0295 -0.0814 93 VAL B C 2944 O O . VAL B 93 ? 0.3107 0.2996 0.3548 0.0324 -0.0228 -0.0662 93 VAL B O 2945 C CB . VAL B 93 ? 0.3513 0.3620 0.3819 0.0559 -0.0212 -0.0783 93 VAL B CB 2946 C CG1 . VAL B 93 ? 0.3667 0.4245 0.3961 0.0532 -0.0076 -0.0600 93 VAL B CG1 2947 C CG2 . VAL B 93 ? 0.3690 0.3794 0.3959 0.0727 -0.0284 -0.0935 93 VAL B CG2 2948 N N . LYS B 94 ? 0.3442 0.3853 0.3690 0.0590 -0.0329 -0.0875 94 LYS B N 2949 C CA . LYS B 94 ? 0.3498 0.3993 0.3791 0.0506 -0.0308 -0.0750 94 LYS B CA 2950 C C . LYS B 94 ? 0.3258 0.3895 0.3557 0.0422 -0.0157 -0.0467 94 LYS B C 2951 O O . LYS B 94 ? 0.3300 0.4165 0.3539 0.0449 -0.0081 -0.0374 94 LYS B O 2952 C CB . LYS B 94 ? 0.3664 0.4489 0.3823 0.0668 -0.0418 -0.0901 94 LYS B CB 2953 C CG . LYS B 94 ? 0.4204 0.4822 0.4377 0.0761 -0.0644 -0.1230 94 LYS B CG 2954 C CD . LYS B 94 ? 0.4473 0.5433 0.4492 0.0948 -0.0789 -0.1429 94 LYS B CD 2955 C CE . LYS B 94 ? 0.5615 0.6496 0.5528 0.1181 -0.1016 -0.1827 94 LYS B CE 2956 N NZ . LYS B 94 ? 0.6106 0.7267 0.5860 0.1392 -0.1227 -0.2115 94 LYS B NZ 2957 N N . TRP B 95 ? 0.2975 0.3488 0.3374 0.0325 -0.0138 -0.0333 95 TRP B N 2958 C CA . TRP B 95 ? 0.2953 0.3492 0.3371 0.0260 -0.0062 -0.0083 95 TRP B CA 2959 C C . TRP B 95 ? 0.3188 0.4123 0.3481 0.0328 -0.0072 0.0060 95 TRP B C 2960 O O . TRP B 95 ? 0.3202 0.4278 0.3441 0.0409 -0.0146 0.0000 95 TRP B O 2961 C CB . TRP B 95 ? 0.2833 0.3107 0.3384 0.0201 -0.0071 -0.0029 95 TRP B CB 2962 C CG . TRP B 95 ? 0.2927 0.3119 0.3514 0.0174 -0.0079 0.0187 95 TRP B CG 2963 C CD1 . TRP B 95 ? 0.2793 0.2878 0.3401 0.0090 -0.0065 0.0351 95 TRP B CD1 2964 C CD2 . TRP B 95 ? 0.2793 0.2953 0.3431 0.0229 -0.0149 0.0263 95 TRP B CD2 2965 N NE1 . TRP B 95 ? 0.2965 0.2881 0.3632 0.0080 -0.0145 0.0524 95 TRP B NE1 2966 C CE2 . TRP B 95 ? 0.2828 0.2787 0.3500 0.0188 -0.0194 0.0471 95 TRP B CE2 2967 C CE3 . TRP B 95 ? 0.2929 0.3219 0.3613 0.0312 -0.0205 0.0176 95 TRP B CE3 2968 C CZ2 . TRP B 95 ? 0.3170 0.2986 0.3896 0.0259 -0.0304 0.0580 95 TRP B CZ2 2969 C CZ3 . TRP B 95 ? 0.3242 0.3487 0.3980 0.0390 -0.0287 0.0284 95 TRP B CZ3 2970 C CH2 . TRP B 95 ? 0.3281 0.3263 0.4026 0.0379 -0.0341 0.0485 95 TRP B CH2 2971 N N . ASP B 96 ? 0.3355 0.4523 0.3612 0.0286 -0.0004 0.0263 96 ASP B N 2972 C CA . ASP B 96 ? 0.3806 0.5383 0.3960 0.0297 0.0007 0.0524 96 ASP B CA 2973 C C . ASP B 96 ? 0.4124 0.5373 0.4406 0.0161 -0.0040 0.0802 96 ASP B C 2974 O O . ASP B 96 ? 0.4070 0.5050 0.4499 0.0021 -0.0034 0.0917 96 ASP B O 2975 C CB . ASP B 96 ? 0.3879 0.5908 0.4005 0.0270 0.0104 0.0662 96 ASP B CB 2976 C CG . ASP B 96 ? 0.4359 0.6976 0.4361 0.0272 0.0141 0.0984 96 ASP B CG 2977 O OD1 . ASP B 96 ? 0.4618 0.7151 0.4579 0.0248 0.0072 0.1182 96 ASP B OD1 2978 O OD2 . ASP B 96 ? 0.4305 0.7520 0.4252 0.0306 0.0238 0.1062 96 ASP B OD2 2979 N N . ARG B 97 ? 0.4410 0.5664 0.4643 0.0223 -0.0121 0.0888 97 ARG B N 2980 C CA . ARG B 97 ? 0.4931 0.5805 0.5284 0.0158 -0.0219 0.1108 97 ARG B CA 2981 C C . ARG B 97 ? 0.5343 0.6173 0.5772 -0.0020 -0.0243 0.1498 97 ARG B C 2982 O O . ARG B 97 ? 0.5544 0.5900 0.6116 -0.0086 -0.0372 0.1641 97 ARG B O 2983 C CB . ARG B 97 ? 0.5126 0.6120 0.5392 0.0288 -0.0319 0.1165 97 ARG B CB 2984 C CG . ARG B 97 ? 0.5282 0.6343 0.5541 0.0423 -0.0338 0.0812 97 ARG B CG 2985 C CD . ARG B 97 ? 0.5772 0.6806 0.6061 0.0538 -0.0470 0.0853 97 ARG B CD 2986 N NE . ARG B 97 ? 0.5842 0.6855 0.6266 0.0600 -0.0494 0.0533 97 ARG B NE 2987 C CZ . ARG B 97 ? 0.5755 0.6680 0.6339 0.0685 -0.0580 0.0485 97 ARG B CZ 2988 N NH1 . ARG B 97 ? 0.5683 0.6434 0.6287 0.0758 -0.0678 0.0701 97 ARG B NH1 2989 N NH2 . ARG B 97 ? 0.5532 0.6549 0.6282 0.0693 -0.0582 0.0232 97 ARG B NH2 2990 N N . ASP B 98 ? 0.5480 0.6827 0.5835 -0.0091 -0.0141 0.1669 98 ASP B N 2991 C CA . ASP B 98 ? 0.5780 0.7219 0.6271 -0.0324 -0.0148 0.2078 98 ASP B CA 2992 C C . ASP B 98 ? 0.5770 0.6799 0.6489 -0.0465 -0.0168 0.1971 98 ASP B C 2993 O O . ASP B 98 ? 0.5934 0.6907 0.6846 -0.0696 -0.0227 0.2275 98 ASP B O 2994 C CB . ASP B 98 ? 0.5739 0.8029 0.6104 -0.0328 0.0004 0.2238 98 ASP B CB 2995 C CG . ASP B 98 ? 0.6018 0.8820 0.6132 -0.0212 0.0010 0.2444 98 ASP B CG 2996 O OD1 . ASP B 98 ? 0.6045 0.8514 0.6105 -0.0153 -0.0120 0.2505 98 ASP B OD1 2997 O OD2 . ASP B 98 ? 0.6114 0.9720 0.6072 -0.0151 0.0143 0.2533 98 ASP B OD2 2998 N N . MET B 99 ? 0.5613 0.6395 0.6313 -0.0339 -0.0132 0.1557 99 MET B N 2999 C CA . MET B 99 ? 0.5601 0.6098 0.6442 -0.0417 -0.0133 0.1394 99 MET B CA 3000 C C . MET B 99 ? 0.5584 0.5445 0.6481 -0.0352 -0.0241 0.1180 99 MET B C 3001 O O . MET B 99 ? 0.5441 0.5188 0.6260 -0.0202 -0.0259 0.1048 99 MET B O 3002 C CB . MET B 99 ? 0.5448 0.6259 0.6193 -0.0304 0.0000 0.1111 99 MET B CB 3003 C CG . MET B 99 ? 0.5811 0.7172 0.6610 -0.0379 0.0089 0.1235 99 MET B CG 3004 S SD . MET B 99 ? 0.6924 0.9113 0.7533 -0.0269 0.0194 0.1396 99 MET B SD 3005 C CE . MET B 99 ? 0.6361 0.9274 0.7052 -0.0269 0.0319 0.1406 99 MET B CE 3006 C C1 . NAG C . ? 1.7038 0.5008 1.1606 -0.1897 0.2082 0.0878 500 NAG A C1 3007 C C2 . NAG C . ? 1.8312 0.5228 1.2855 -0.2308 0.2397 0.0992 500 NAG A C2 3008 C C3 . NAG C . ? 1.8063 0.5491 1.3933 -0.2903 0.2749 0.0979 500 NAG A C3 3009 C C4 . NAG C . ? 1.7102 0.5563 1.4138 -0.3046 0.2252 0.0655 500 NAG A C4 3010 C C5 . NAG C . ? 1.5951 0.5356 1.2861 -0.2603 0.1960 0.0566 500 NAG A C5 3011 C C6 . NAG C . ? 1.5066 0.5359 1.3006 -0.2723 0.1467 0.0264 500 NAG A C6 3012 C C7 . NAG C . ? 2.0748 0.5461 1.3092 -0.1912 0.2677 0.1366 500 NAG A C7 3013 C C8 . NAG C . ? 2.1758 0.5468 1.4275 -0.2395 0.2902 0.1414 500 NAG A C8 3014 N N2 . NAG C . ? 1.9531 0.5367 1.2865 -0.2119 0.2791 0.1297 500 NAG A N2 3015 O O3 . NAG C . ? 1.8939 0.5493 1.4997 -0.3360 0.3083 0.1081 500 NAG A O3 3016 O O4 . NAG C . ? 1.7173 0.6119 1.5545 -0.3586 0.2536 0.0627 500 NAG A O4 3017 O O5 . NAG C . ? 1.6110 0.5077 1.1787 -0.2069 0.1736 0.0613 500 NAG A O5 3018 O O6 . NAG C . ? 1.4544 0.5259 1.2050 -0.2273 0.1018 0.0133 500 NAG A O6 3019 O O7 . NAG C . ? 2.0986 0.5455 1.2344 -0.1352 0.2399 0.1387 500 NAG A O7 3020 C C1 . NAG D . ? 0.6875 0.7025 1.1627 -0.1142 0.3037 -0.0346 511 NAG A C1 3021 C C2 . NAG D . ? 0.6473 0.6993 1.1954 -0.1254 0.2507 -0.0405 511 NAG A C2 3022 C C3 . NAG D . ? 0.6777 0.7545 1.3295 -0.1517 0.2709 -0.0397 511 NAG A C3 3023 C C4 . NAG D . ? 0.6768 0.7956 1.4255 -0.1507 0.3199 -0.0414 511 NAG A C4 3024 C C5 . NAG D . ? 0.7275 0.8036 1.3900 -0.1360 0.3780 -0.0336 511 NAG A C5 3025 C C6 . NAG D . ? 0.7452 0.8628 1.4953 -0.1254 0.4237 -0.0377 511 NAG A C6 3026 C C7 . NAG D . ? 0.6390 0.6506 1.0466 -0.1089 0.1727 -0.0410 511 NAG A C7 3027 C C8 . NAG D . ? 0.6234 0.6175 0.9907 -0.1110 0.1301 -0.0408 511 NAG A C8 3028 N N2 . NAG D . ? 0.6629 0.6825 1.1338 -0.1263 0.2101 -0.0384 511 NAG A N2 3029 O O3 . NAG D . ? 0.6355 0.7418 1.3484 -0.1600 0.2138 -0.0491 511 NAG A O3 3030 O O4 . NAG D . ? 0.6988 0.8440 1.5539 -0.1790 0.3446 -0.0397 511 NAG A O4 3031 O O5 . NAG D . ? 0.6974 0.7420 1.2526 -0.1132 0.3508 -0.0363 511 NAG A O5 3032 O O6 . NAG D . ? 0.8292 0.8998 1.5113 -0.1200 0.4934 -0.0286 511 NAG A O6 3033 O O7 . NAG D . ? 0.6111 0.6262 0.9936 -0.0922 0.1744 -0.0435 511 NAG A O7 3034 C C1 . NAG E . ? 0.8139 1.2557 1.9808 -0.5159 -0.0416 -0.1318 521 NAG A C1 3035 C C2 . NAG E . ? 0.8028 1.3327 2.1231 -0.5478 -0.0041 -0.1176 521 NAG A C2 3036 C C3 . NAG E . ? 0.7415 1.3669 2.1004 -0.5080 0.0026 -0.1083 521 NAG A C3 3037 C C4 . NAG E . ? 0.7104 1.2913 1.9406 -0.4582 0.0418 -0.0796 521 NAG A C4 3038 C C5 . NAG E . ? 0.7091 1.1950 1.7945 -0.4368 0.0090 -0.0912 521 NAG A C5 3039 C C6 . NAG E . ? 0.6774 1.1155 1.6497 -0.3964 0.0504 -0.0620 521 NAG A C6 3040 C C7 . NAG E . ? 0.9177 1.4465 2.4171 -0.6523 -0.0158 -0.1418 521 NAG A C7 3041 C C8 . NAG E . ? 0.9328 1.5579 2.6207 -0.6998 -0.0021 -0.1436 521 NAG A C8 3042 N N2 . NAG E . ? 0.8578 1.4221 2.2990 -0.5987 -0.0443 -0.1472 521 NAG A N2 3043 O O3 . NAG E . ? 0.7430 1.4518 2.2452 -0.5337 0.0458 -0.0933 521 NAG A O3 3044 O O4 . NAG E . ? 0.6657 1.3214 1.9143 -0.4175 0.0393 -0.0759 521 NAG A O4 3045 O O5 . NAG E . ? 0.7643 1.1754 1.8324 -0.4739 0.0016 -0.1014 521 NAG A O5 3046 O O6 . NAG E . ? 0.7110 1.0798 1.6491 -0.4141 0.0994 -0.0378 521 NAG A O6 3047 O O7 . NAG E . ? 0.9661 1.3882 2.3764 -0.6637 0.0000 -0.1354 521 NAG A O7 # 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 GLU 1 1 ? ? ? A . n A 1 2 THR 2 2 ? ? ? A . n A 1 3 SER 3 3 ? ? ? A . n A 1 4 CYS 4 4 ? ? ? A . n A 1 5 PRO 5 5 ? ? ? A . n A 1 6 PRO 6 6 ? ? ? A . n A 1 7 PRO 7 7 7 PRO PRO A . n A 1 8 GLU 8 8 8 GLU GLU A . n A 1 9 GLU 9 9 9 GLU GLU A . n A 1 10 SER 10 10 10 SER SER A . n A 1 11 GLN 11 11 11 GLN GLN A . n A 1 12 PHE 12 12 12 PHE PHE A . n A 1 13 PHE 13 13 13 PHE PHE A . n A 1 14 GLN 14 14 14 GLN GLN A . n A 1 15 LEU 15 15 15 LEU LEU A . n A 1 16 PHE 16 16 16 PHE PHE A . n A 1 17 TYR 17 17 17 TYR TYR A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 LEU 20 20 20 LEU LEU A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 GLY 22 22 22 GLY GLY A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 SER 25 25 25 SER SER A . n A 1 26 SER 26 26 26 SER SER A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 GLU 28 28 28 GLU GLU A . n A 1 29 LEU 29 29 29 LEU LEU A . n A 1 30 THR 30 30 30 THR THR A . n A 1 31 GLY 31 31 31 GLY GLY A . n A 1 32 MET 32 32 32 MET MET A . n A 1 33 ALA 33 33 33 ALA ALA A . n A 1 34 LEU 34 34 34 LEU LEU A . n A 1 35 LEU 35 35 35 LEU LEU A . n A 1 36 ALA 36 36 36 ALA ALA A . n A 1 37 ASP 37 37 37 ASP ASP A . n A 1 38 VAL 38 38 38 VAL VAL A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 ILE 40 40 40 ILE ILE A . n A 1 41 MET 41 41 41 MET MET A . n A 1 42 VAL 42 42 42 VAL VAL A . n A 1 43 LEU 43 43 43 LEU LEU A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 PRO 45 45 45 PRO PRO A . n A 1 46 HIS 46 46 46 HIS HIS A . n A 1 47 THR 47 47 47 THR THR A . n A 1 48 TRP 48 48 48 TRP TRP A . n A 1 49 ASN 49 49 49 ASN ASN A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ASN 51 51 51 ASN ASN A . n A 1 52 ILE 52 52 52 ILE ILE A . n A 1 53 CYS 53 53 53 CYS CYS A . n A 1 54 ARG 54 54 54 ARG ARG A . n A 1 55 PRO 55 55 55 PRO PRO A . n A 1 56 TRP 56 56 56 TRP TRP A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 GLN 58 58 58 GLN GLN A . n A 1 59 GLU 59 59 59 GLU GLU A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 ALA 62 62 62 ALA ALA A . n A 1 63 GLU 63 63 63 GLU GLU A . n A 1 64 THR 64 64 64 THR THR A . n A 1 65 GLU 65 65 65 GLU GLU A . n A 1 66 VAL 66 66 66 VAL VAL A . n A 1 67 LYS 67 67 67 LYS LYS A . n A 1 68 LYS 68 68 68 LYS LYS A . n A 1 69 ILE 69 69 69 ILE ILE A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 SER 71 71 71 SER SER A . n A 1 72 PHE 72 72 72 PHE PHE A . n A 1 73 SER 73 73 73 SER SER A . n A 1 74 MET 74 74 74 MET MET A . n A 1 75 VAL 75 75 75 VAL VAL A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 ILE 77 77 77 ILE ILE A . n A 1 78 ARG 78 78 78 ARG ARG A . n A 1 79 ASN 79 79 79 ASN ASN A . n A 1 80 THR 80 80 80 THR THR A . n A 1 81 ILE 81 81 81 ILE ILE A . n A 1 82 ARG 82 82 82 ARG ARG A . n A 1 83 PHE 83 83 83 PHE PHE A . n A 1 84 MET 84 84 84 MET MET A . n A 1 85 HIS 85 85 85 HIS HIS A . n A 1 86 GLU 86 86 86 GLU GLU A . n A 1 87 MET 87 87 87 MET MET A . n A 1 88 THR 88 88 88 THR THR A . n A 1 89 ALA 89 89 89 ALA ALA A . n A 1 90 LYS 90 90 90 LYS LYS A . n A 1 91 ALA 91 91 91 ALA ALA A . n A 1 92 GLY 92 92 92 GLY GLY A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 TYR 95 95 95 TYR TYR A . n A 1 96 PRO 96 96 96 PRO PRO A . n A 1 97 ARG 97 97 97 ARG ARG A . n A 1 98 VAL 98 98 98 VAL VAL A . n A 1 99 PHE 99 99 99 PHE PHE A . n A 1 100 GLN 100 100 100 GLN GLN A . n A 1 101 ILE 101 101 101 ILE ILE A . n A 1 102 HIS 102 102 102 HIS HIS A . n A 1 103 THR 103 103 103 THR THR A . n A 1 104 GLY 104 104 104 GLY GLY A . n A 1 105 CYS 105 105 105 CYS CYS A . n A 1 106 LYS 106 106 106 LYS LYS A . n A 1 107 LEU 107 107 107 LEU LEU A . n A 1 108 TYR 108 108 108 TYR TYR A . n A 1 109 THR 109 109 109 THR THR A . n A 1 110 ASN 110 110 110 ASN ASN A . n A 1 111 GLY 111 111 111 GLY GLY A . n A 1 112 THR 112 112 112 THR THR A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 TRP 114 114 114 TRP TRP A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 PHE 116 116 116 PHE PHE A . n A 1 117 VAL 117 117 117 VAL VAL A . n A 1 118 ASN 118 118 118 ASN ASN A . n A 1 119 ILE 119 119 119 ILE ILE A . n A 1 120 GLY 120 120 120 GLY GLY A . n A 1 121 GLU 121 121 121 GLU GLU A . n A 1 122 GLY 122 122 122 GLY GLY A . n A 1 123 GLY 123 123 123 GLY GLY A . n A 1 124 ARG 124 124 124 ARG ARG A . n A 1 125 ASP 125 125 125 ASP ASP A . n A 1 126 LEU 126 126 126 LEU LEU A . n A 1 127 VAL 127 127 127 VAL VAL A . n A 1 128 THR 128 128 128 THR THR A . n A 1 129 TYR 129 129 129 TYR TYR A . n A 1 130 GLU 130 130 130 GLU GLU A . n A 1 131 LEU 131 131 131 LEU LEU A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 ARG 133 133 133 ARG ARG A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 ARG 135 135 135 ARG ARG A . n A 1 136 TRP 136 136 136 TRP TRP A . n A 1 137 VAL 137 137 137 VAL VAL A . n A 1 138 PRO 138 138 138 PRO PRO A . n A 1 139 GLN 139 139 139 GLN GLN A . n A 1 140 ARG 140 140 140 ARG ARG A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 THR 142 142 142 THR THR A . n A 1 143 LEU 143 143 143 LEU LEU A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 ALA 145 145 145 ALA ALA A . n A 1 146 LYS 146 146 146 LYS LYS A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 MET 148 148 148 MET MET A . n A 1 149 SER 149 149 149 SER SER A . n A 1 150 ASN 150 150 150 ASN ASN A . n A 1 151 THR 151 151 151 THR THR A . n A 1 152 LEU 152 152 152 LEU LEU A . n A 1 153 THR 153 153 153 THR THR A . n A 1 154 ASP 154 154 154 ASP ASP A . n A 1 155 LEU 155 155 155 LEU LEU A . n A 1 156 ARG 156 156 156 ARG ARG A . n A 1 157 ALA 157 157 157 ALA ALA A . n A 1 158 VAL 158 158 158 VAL VAL A . n A 1 159 SER 159 159 159 SER SER A . n A 1 160 GLY 160 160 160 GLY GLY A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 LEU 162 162 162 LEU LEU A . n A 1 163 GLU 163 163 163 GLU GLU A . n A 1 164 HIS 164 164 164 HIS HIS A . n A 1 165 ILE 165 165 165 ILE ILE A . n A 1 166 PHE 166 166 166 PHE PHE A . n A 1 167 SER 167 167 167 SER SER A . n A 1 168 SER 168 168 168 SER SER A . n A 1 169 SER 169 169 169 SER SER A . n A 1 170 PHE 170 170 170 PHE PHE A . n A 1 171 PRO 171 171 171 PRO PRO A . n A 1 172 ASN 172 172 172 ASN ASN A . n A 1 173 TYR 173 173 173 TYR TYR A . n A 1 174 ILE 174 174 174 ILE ILE A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 MET 176 176 176 MET MET A . n A 1 177 LEU 177 177 177 LEU LEU A . n A 1 178 HIS 178 178 178 HIS HIS A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 GLU 180 180 180 GLU GLU A . n A 1 181 GLY 181 181 181 GLY GLY A . n A 1 182 ARG 182 182 182 ARG ARG A . n A 1 183 THR 183 183 183 THR THR A . n A 1 184 ASP 184 184 184 ASP ASP A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 ARG 187 187 187 ARG ARG A . n A 1 188 ARG 188 188 188 ARG ARG A . n A 1 189 VAL 189 189 189 VAL VAL A . n A 1 190 PRO 190 190 190 PRO PRO A . n A 1 191 PRO 191 191 191 PRO PRO A . n A 1 192 MET 192 192 192 MET MET A . n A 1 193 ALA 193 193 193 ALA ALA A . n A 1 194 VAL 194 194 194 VAL VAL A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 PHE 196 196 196 PHE PHE A . n A 1 197 ALA 197 197 197 ALA ALA A . n A 1 198 ARG 198 198 198 ARG ARG A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 ALA 200 200 200 ALA ALA A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 GLN 202 202 202 GLN GLN A . n A 1 203 VAL 203 203 203 VAL VAL A . n A 1 204 GLN 204 204 204 GLN GLN A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 CYS 209 209 209 CYS CYS A . n A 1 210 ARG 210 210 210 ARG ARG A . n A 1 211 VAL 211 211 211 VAL VAL A . n A 1 212 THR 212 212 212 THR THR A . n A 1 213 SER 213 213 213 SER SER A . n A 1 214 PHE 214 214 214 PHE PHE A . n A 1 215 TYR 215 215 215 TYR TYR A . n A 1 216 PRO 216 216 216 PRO PRO A . n A 1 217 ARG 217 217 217 ARG ARG A . n A 1 218 PRO 218 218 218 PRO PRO A . n A 1 219 ILE 219 219 219 ILE ILE A . n A 1 220 ALA 220 220 220 ALA ALA A . n A 1 221 VAL 221 221 221 VAL VAL A . n A 1 222 THR 222 222 222 THR THR A . n A 1 223 TRP 223 223 223 TRP TRP A . n A 1 224 LEU 224 224 224 LEU LEU A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 ASP 226 226 226 ASP ASP A . n A 1 227 GLY 227 227 227 GLY GLY A . n A 1 228 ARG 228 228 228 ARG ARG A . n A 1 229 GLU 229 229 229 GLU GLU A . n A 1 230 VAL 230 230 230 VAL VAL A . n A 1 231 PRO 231 231 231 PRO PRO A . n A 1 232 PRO 232 232 232 PRO PRO A . n A 1 233 SER 233 233 233 SER SER A . n A 1 234 PRO 234 234 234 PRO PRO A . n A 1 235 ALA 235 235 235 ALA ALA A . n A 1 236 LEU 236 236 236 LEU LEU A . n A 1 237 SER 237 237 237 SER SER A . n A 1 238 THR 238 238 238 THR THR A . n A 1 239 GLY 239 239 239 GLY GLY A . n A 1 240 THR 240 240 240 THR THR A . n A 1 241 VAL 241 241 241 VAL VAL A . n A 1 242 LEU 242 242 242 LEU LEU A . n A 1 243 PRO 243 243 243 PRO PRO A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 ALA 245 245 245 ALA ALA A . n A 1 246 ASP 246 246 246 ASP ASP A . n A 1 247 LEU 247 247 247 LEU LEU A . n A 1 248 THR 248 248 248 THR THR A . n A 1 249 TYR 249 249 249 TYR TYR A . n A 1 250 GLN 250 250 250 GLN GLN A . n A 1 251 LEU 251 251 251 LEU LEU A . n A 1 252 ARG 252 252 252 ARG ARG A . n A 1 253 SER 253 253 253 SER SER A . n A 1 254 THR 254 254 254 THR THR A . n A 1 255 LEU 255 255 255 LEU LEU A . n A 1 256 LEU 256 256 256 LEU LEU A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 SER 258 258 258 SER SER A . n A 1 259 PRO 259 259 259 PRO PRO A . n A 1 260 GLN 260 260 260 GLN GLN A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 GLY 262 262 262 GLY GLY A . n A 1 263 HIS 263 263 263 HIS HIS A . n A 1 264 GLY 264 264 264 GLY GLY A . n A 1 265 TYR 265 265 265 TYR TYR A . n A 1 266 ALA 266 266 266 ALA ALA A . n A 1 267 CYS 267 267 267 CYS CYS A . n A 1 268 ARG 268 268 268 ARG ARG A . n A 1 269 VAL 269 269 269 VAL VAL A . n A 1 270 GLN 270 270 270 GLN GLN A . n A 1 271 HIS 271 271 271 HIS HIS A . n A 1 272 CYS 272 272 272 CYS CYS A . n A 1 273 SER 273 273 273 SER SER A . n A 1 274 LEU 274 274 274 LEU LEU A . n A 1 275 GLY 275 275 275 GLY GLY A . n A 1 276 ASP 276 276 276 ASP ASP A . n A 1 277 ARG 277 277 277 ARG ARG A . n A 1 278 SER 278 278 278 SER SER A . n A 1 279 LEU 279 279 279 LEU LEU A . n A 1 280 LEU 280 280 280 LEU LEU A . n A 1 281 VAL 281 281 281 VAL VAL A . n A 1 282 PRO 282 282 282 PRO PRO A . n A 1 283 TRP 283 283 283 TRP TRP A . n A 1 284 HIS 284 284 284 HIS HIS A . n A 1 285 HIS 285 285 285 HIS HIS A . n A 1 286 HIS 286 286 ? ? ? A . n A 1 287 HIS 287 287 ? ? ? A . n A 1 288 HIS 288 288 ? ? ? A . n A 1 289 HIS 289 289 ? ? ? 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 ARG 3 3 3 ARG ARG 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 LYS 6 6 6 LYS LYS 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 ALA 15 15 15 ALA ALA 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 SER 20 20 20 SER SER B . n B 2 21 ASN 21 21 21 ASN ASN B . n B 2 22 PHE 22 22 22 PHE PHE 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 SER 28 28 28 SER SER B . n B 2 29 GLY 29 29 29 GLY GLY 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 SER 33 33 33 SER SER B . n B 2 34 ASP 34 34 34 ASP ASP 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 VAL 37 37 37 VAL VAL B . n B 2 38 ASP 38 38 38 ASP ASP B . n B 2 39 LEU 39 39 39 LEU LEU 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 GLU 44 44 44 GLU GLU B . n B 2 45 ARG 45 45 45 ARG ARG B . n B 2 46 ILE 46 46 46 ILE ILE B . n B 2 47 GLU 47 47 47 GLU GLU 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 HIS 51 51 51 HIS HIS 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 LEU 54 54 54 LEU LEU 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 LEU 64 64 64 LEU LEU B . n B 2 65 LEU 65 65 65 LEU LEU B . n B 2 66 TYR 66 66 66 TYR TYR B . n B 2 67 TYR 67 67 67 TYR TYR 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 LYS 75 75 75 LYS LYS B . n B 2 76 ASP 76 76 76 ASP ASP B . n B 2 77 GLU 77 77 77 GLU GLU 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 ASN 83 83 83 ASN ASN B . n B 2 84 HIS 84 84 84 HIS HIS B . n B 2 85 VAL 85 85 85 VAL VAL B . n B 2 86 THR 86 86 86 THR THR B . n B 2 87 LEU 87 87 87 LEU LEU B . n B 2 88 SER 88 88 88 SER SER B . n B 2 89 GLN 89 89 89 GLN GLN 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 ILE 92 92 92 ILE ILE B . n B 2 93 VAL 93 93 93 VAL VAL B . n B 2 94 LYS 94 94 94 LYS LYS 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 # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 500 500 NAG NAG A . D 3 NAG 1 511 511 NAG NAG A . E 3 NAG 1 521 521 NAG NAG A . F 4 PLM 1 522 1 PLM PLM A . G 5 HOH 1 523 2 HOH HOH A . G 5 HOH 2 524 5 HOH HOH A . G 5 HOH 3 525 8 HOH HOH A . G 5 HOH 4 526 12 HOH HOH A . G 5 HOH 5 527 14 HOH HOH A . G 5 HOH 6 528 17 HOH HOH A . G 5 HOH 7 529 23 HOH HOH A . G 5 HOH 8 530 24 HOH HOH A . G 5 HOH 9 531 25 HOH HOH A . G 5 HOH 10 532 29 HOH HOH A . G 5 HOH 11 533 30 HOH HOH A . G 5 HOH 12 534 31 HOH HOH A . G 5 HOH 13 535 32 HOH HOH A . G 5 HOH 14 536 33 HOH HOH A . G 5 HOH 15 537 34 HOH HOH A . G 5 HOH 16 538 36 HOH HOH A . G 5 HOH 17 539 41 HOH HOH A . G 5 HOH 18 540 43 HOH HOH A . G 5 HOH 19 541 45 HOH HOH A . G 5 HOH 20 542 47 HOH HOH A . G 5 HOH 21 543 49 HOH HOH A . G 5 HOH 22 544 51 HOH HOH A . G 5 HOH 23 545 53 HOH HOH A . G 5 HOH 24 546 57 HOH HOH A . G 5 HOH 25 547 62 HOH HOH A . G 5 HOH 26 548 66 HOH HOH A . G 5 HOH 27 549 77 HOH HOH A . G 5 HOH 28 550 78 HOH HOH A . G 5 HOH 29 551 83 HOH HOH A . G 5 HOH 30 552 84 HOH HOH A . G 5 HOH 31 553 94 HOH HOH A . G 5 HOH 32 554 97 HOH HOH A . G 5 HOH 33 555 99 HOH HOH A . G 5 HOH 34 556 100 HOH HOH A . G 5 HOH 35 557 104 HOH HOH A . G 5 HOH 36 558 111 HOH HOH A . G 5 HOH 37 559 112 HOH HOH A . G 5 HOH 38 560 113 HOH HOH A . G 5 HOH 39 561 114 HOH HOH A . G 5 HOH 40 562 115 HOH HOH A . G 5 HOH 41 563 123 HOH HOH A . G 5 HOH 42 564 124 HOH HOH A . G 5 HOH 43 565 126 HOH HOH A . G 5 HOH 44 566 127 HOH HOH A . G 5 HOH 45 567 129 HOH HOH A . G 5 HOH 46 568 132 HOH HOH A . G 5 HOH 47 569 134 HOH HOH A . G 5 HOH 48 570 140 HOH HOH A . G 5 HOH 49 571 147 HOH HOH A . G 5 HOH 50 572 148 HOH HOH A . G 5 HOH 51 573 157 HOH HOH A . G 5 HOH 52 574 158 HOH HOH A . G 5 HOH 53 575 160 HOH HOH A . G 5 HOH 54 576 167 HOH HOH A . G 5 HOH 55 577 175 HOH HOH A . G 5 HOH 56 578 176 HOH HOH A . G 5 HOH 57 579 177 HOH HOH A . G 5 HOH 58 580 185 HOH HOH A . G 5 HOH 59 581 193 HOH HOH A . G 5 HOH 60 582 196 HOH HOH A . G 5 HOH 61 583 199 HOH HOH A . G 5 HOH 62 584 200 HOH HOH A . G 5 HOH 63 585 201 HOH HOH A . G 5 HOH 64 586 203 HOH HOH A . G 5 HOH 65 587 222 HOH HOH A . G 5 HOH 66 588 223 HOH HOH A . G 5 HOH 67 589 225 HOH HOH A . G 5 HOH 68 590 229 HOH HOH A . G 5 HOH 69 591 235 HOH HOH A . G 5 HOH 70 592 236 HOH HOH A . G 5 HOH 71 593 239 HOH HOH A . G 5 HOH 72 594 244 HOH HOH A . G 5 HOH 73 595 250 HOH HOH A . G 5 HOH 74 596 253 HOH HOH A . G 5 HOH 75 597 268 HOH HOH A . G 5 HOH 76 598 288 HOH HOH A . G 5 HOH 77 599 289 HOH HOH A . G 5 HOH 78 600 294 HOH HOH A . G 5 HOH 79 601 299 HOH HOH A . G 5 HOH 80 602 302 HOH HOH A . H 5 HOH 1 100 1 HOH HOH B . H 5 HOH 2 101 4 HOH HOH B . H 5 HOH 3 102 6 HOH HOH B . H 5 HOH 4 103 7 HOH HOH B . H 5 HOH 5 104 9 HOH HOH B . H 5 HOH 6 105 10 HOH HOH B . H 5 HOH 7 106 13 HOH HOH B . H 5 HOH 8 107 15 HOH HOH B . H 5 HOH 9 108 18 HOH HOH B . H 5 HOH 10 109 19 HOH HOH B . H 5 HOH 11 110 21 HOH HOH B . H 5 HOH 12 111 27 HOH HOH B . H 5 HOH 13 112 37 HOH HOH B . H 5 HOH 14 113 38 HOH HOH B . H 5 HOH 15 114 39 HOH HOH B . H 5 HOH 16 115 40 HOH HOH B . H 5 HOH 17 116 46 HOH HOH B . H 5 HOH 18 117 50 HOH HOH B . H 5 HOH 19 118 52 HOH HOH B . H 5 HOH 20 119 60 HOH HOH B . H 5 HOH 21 120 63 HOH HOH B . H 5 HOH 22 121 65 HOH HOH B . H 5 HOH 23 122 67 HOH HOH B . H 5 HOH 24 123 73 HOH HOH B . H 5 HOH 25 124 74 HOH HOH B . H 5 HOH 26 125 79 HOH HOH B . H 5 HOH 27 126 85 HOH HOH B . H 5 HOH 28 127 86 HOH HOH B . H 5 HOH 29 128 90 HOH HOH B . H 5 HOH 30 129 92 HOH HOH B . H 5 HOH 31 130 93 HOH HOH B . H 5 HOH 32 131 95 HOH HOH B . H 5 HOH 33 132 102 HOH HOH B . H 5 HOH 34 133 103 HOH HOH B . H 5 HOH 35 134 116 HOH HOH B . H 5 HOH 36 135 118 HOH HOH B . H 5 HOH 37 136 119 HOH HOH B . H 5 HOH 38 137 120 HOH HOH B . H 5 HOH 39 138 122 HOH HOH B . H 5 HOH 40 139 125 HOH HOH B . H 5 HOH 41 140 128 HOH HOH B . H 5 HOH 42 141 130 HOH HOH B . H 5 HOH 43 142 131 HOH HOH B . H 5 HOH 44 143 136 HOH HOH B . H 5 HOH 45 144 137 HOH HOH B . H 5 HOH 46 145 138 HOH HOH B . H 5 HOH 47 146 139 HOH HOH B . H 5 HOH 48 147 141 HOH HOH B . H 5 HOH 49 148 151 HOH HOH B . H 5 HOH 50 149 156 HOH HOH B . H 5 HOH 51 150 161 HOH HOH B . H 5 HOH 52 151 168 HOH HOH B . H 5 HOH 53 152 171 HOH HOH B . H 5 HOH 54 153 172 HOH HOH B . H 5 HOH 55 154 173 HOH HOH B . H 5 HOH 56 155 179 HOH HOH B . H 5 HOH 57 156 187 HOH HOH B . H 5 HOH 58 157 188 HOH HOH B . H 5 HOH 59 158 198 HOH HOH B . H 5 HOH 60 159 209 HOH HOH B . H 5 HOH 61 160 212 HOH HOH B . H 5 HOH 62 161 213 HOH HOH B . H 5 HOH 63 162 231 HOH HOH B . H 5 HOH 64 163 232 HOH HOH B . H 5 HOH 65 164 242 HOH HOH B . H 5 HOH 66 165 256 HOH HOH B . H 5 HOH 67 166 271 HOH HOH B . H 5 HOH 68 167 272 HOH HOH B . H 5 HOH 69 168 300 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 23 A ASN 23 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 51 A ASN 51 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 110 A ASN 110 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H # 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)' 3960 ? 1 MORE -2.5 ? 1 'SSA (A^2)' 19010 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2008-11-25 2 'Structure model' 1 1 2011-07-13 # _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' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' # loop_ _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] _pdbx_refine_tls.pdbx_refine_id 1 ? refined 18.5508 54.4005 32.5367 0.0947 0.0254 -0.1450 0.0409 -0.0752 -0.0566 2.6669 8.2790 4.8542 -1.8318 -0.1351 0.4468 0.1121 0.4154 -0.2782 -1.2645 -0.1788 0.3953 -0.4877 -0.7518 0.0667 'X-RAY DIFFRACTION' 2 ? refined 23.6257 39.4460 65.3062 -0.2598 -0.2235 -0.1624 -0.0622 0.0077 -0.0106 2.0048 3.4239 12.5015 0.2378 -0.9049 3.0484 0.1590 -0.1136 -0.0068 0.3324 -0.2693 0.0867 0.2529 -0.9914 0.1103 'X-RAY DIFFRACTION' 3 ? refined 34.3015 57.3507 56.2204 -0.2433 -0.3289 -0.1996 0.0003 0.0069 -0.0238 6.6947 2.5797 5.5496 -1.5154 3.2104 -0.3006 -0.0731 -0.0668 0.1217 -0.1414 -0.0183 -0.0942 -0.1610 0.0212 0.0914 'X-RAY DIFFRACTION' # loop_ _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.selection_details 1 1 A 7 A 7 A 183 A 183 ? 'X-RAY DIFFRACTION' ? 2 1 A 500 C 1 A 521 E 1 ? 'X-RAY DIFFRACTION' ? 3 2 A 184 A 184 A 284 A 284 ? 'X-RAY DIFFRACTION' ? 4 3 B 1 B 1 B 99 B 99 ? 'X-RAY DIFFRACTION' ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.2.0019 ? 1 HKL-2000 'data collection' . ? 2 DENZO 'data reduction' . ? 3 SCALEPACK 'data scaling' . ? 4 MOLREP phasing . ? 5 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_value _pdbx_validate_rmsd_bond.bond_target_value _pdbx_validate_rmsd_bond.bond_deviation _pdbx_validate_rmsd_bond.bond_standard_deviation _pdbx_validate_rmsd_bond.linker_flag 1 1 CG A ASP 154 ? ? OD1 A ASP 154 ? ? 1.604 1.249 0.355 0.023 N 2 1 CG A ASP 154 ? ? OD2 A ASP 154 ? ? 1.490 1.249 0.241 0.023 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 23 ? ? -127.72 -169.24 2 1 ALA A 36 ? ? 49.87 -123.30 3 1 GLU A 59 ? ? -81.59 33.84 4 1 ALA A 62 ? ? 65.51 -95.00 5 1 LEU A 126 ? ? -126.73 -57.21 6 1 SER A 168 ? ? -126.12 -55.90 7 1 ASP A 226 ? ? 51.91 17.88 8 1 TRP B 60 ? ? 77.31 -2.96 # 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 GLU 28 ? CG ? A GLU 28 CG 2 1 Y 1 A GLU 28 ? CD ? A GLU 28 CD 3 1 Y 1 A GLU 28 ? OE1 ? A GLU 28 OE1 4 1 Y 1 A GLU 28 ? OE2 ? A GLU 28 OE2 5 1 Y 1 A GLU 59 ? CG ? A GLU 59 CG 6 1 Y 1 A GLU 59 ? CD ? A GLU 59 CD 7 1 Y 1 A GLU 59 ? OE1 ? A GLU 59 OE1 8 1 Y 1 A GLU 59 ? OE2 ? A GLU 59 OE2 9 1 Y 1 A THR 64 ? OG1 ? A THR 64 OG1 10 1 Y 1 A THR 64 ? CG2 ? A THR 64 CG2 11 1 Y 1 A GLU 65 ? CG ? A GLU 65 CG 12 1 Y 1 A GLU 65 ? CD ? A GLU 65 CD 13 1 Y 1 A GLU 65 ? OE1 ? A GLU 65 OE1 14 1 Y 1 A GLU 65 ? OE2 ? A GLU 65 OE2 15 1 Y 1 A LYS 68 ? CG ? A LYS 68 CG 16 1 Y 1 A LYS 68 ? CD ? A LYS 68 CD 17 1 Y 1 A LYS 68 ? CE ? A LYS 68 CE 18 1 Y 1 A LYS 68 ? NZ ? A LYS 68 NZ 19 1 Y 1 A LYS 90 ? CG ? A LYS 90 CG 20 1 Y 1 A LYS 90 ? CD ? A LYS 90 CD 21 1 Y 1 A LYS 90 ? CE ? A LYS 90 CE 22 1 Y 1 A LYS 90 ? NZ ? A LYS 90 NZ 23 1 Y 1 A ARG 133 ? CG ? A ARG 133 CG 24 1 Y 1 A ARG 133 ? CD ? A ARG 133 CD 25 1 Y 1 A ARG 133 ? NE ? A ARG 133 NE 26 1 Y 1 A ARG 133 ? CZ ? A ARG 133 CZ 27 1 Y 1 A ARG 133 ? NH1 ? A ARG 133 NH1 28 1 Y 1 A ARG 133 ? NH2 ? A ARG 133 NH2 29 1 Y 1 A GLU 163 ? CG ? A GLU 163 CG 30 1 Y 1 A GLU 163 ? CD ? A GLU 163 CD 31 1 Y 1 A GLU 163 ? OE1 ? A GLU 163 OE1 32 1 Y 1 A GLU 163 ? OE2 ? A GLU 163 OE2 33 1 Y 1 A ARG 228 ? CG ? A ARG 228 CG 34 1 Y 1 A ARG 228 ? CD ? A ARG 228 CD 35 1 Y 1 A ARG 228 ? NE ? A ARG 228 NE 36 1 Y 1 A ARG 228 ? CZ ? A ARG 228 CZ 37 1 Y 1 A ARG 228 ? NH1 ? A ARG 228 NH1 38 1 Y 1 A ARG 228 ? NH2 ? A ARG 228 NH2 39 1 Y 1 B GLU 16 ? CG ? B GLU 16 CG 40 1 Y 1 B GLU 16 ? CD ? B GLU 16 CD 41 1 Y 1 B GLU 16 ? OE1 ? B GLU 16 OE1 42 1 Y 1 B GLU 16 ? OE2 ? B GLU 16 OE2 43 1 Y 1 B LYS 19 ? CG ? B LYS 19 CG 44 1 Y 1 B LYS 19 ? CD ? B LYS 19 CD 45 1 Y 1 B LYS 19 ? CE ? B LYS 19 CE 46 1 Y 1 B LYS 19 ? NZ ? B LYS 19 NZ 47 1 Y 1 B LYS 48 ? CG ? B LYS 48 CG 48 1 Y 1 B LYS 48 ? CD ? B LYS 48 CD 49 1 Y 1 B LYS 48 ? CE ? B LYS 48 CE 50 1 Y 1 B LYS 48 ? NZ ? B LYS 48 NZ 51 1 Y 1 B LYS 58 ? CG ? B LYS 58 CG 52 1 Y 1 B LYS 58 ? CD ? B LYS 58 CD 53 1 Y 1 B LYS 58 ? CE ? B LYS 58 CE 54 1 Y 1 B LYS 58 ? NZ ? B LYS 58 NZ # 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 GLU 1 ? A GLU 1 2 1 Y 1 A THR 2 ? A THR 2 3 1 Y 1 A SER 3 ? A SER 3 4 1 Y 1 A CYS 4 ? A CYS 4 5 1 Y 1 A PRO 5 ? A PRO 5 6 1 Y 1 A PRO 6 ? A PRO 6 7 1 Y 1 A HIS 286 ? A HIS 286 8 1 Y 1 A HIS 287 ? A HIS 287 9 1 Y 1 A HIS 288 ? A HIS 288 10 1 Y 1 A HIS 289 ? A HIS 289 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'PALMITIC ACID' PLM 5 water HOH #