data_16588 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Assignment of the C-terminal Domain of yeast Aha-1 ; _BMRB_accession_number 16588 _BMRB_flat_file_name bmr16588.str _Entry_type original _Submission_date 2009-10-27 _Accession_date 2009-10-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hagn Franz . . 2 Retzlaff Marco . . 3 Mitschke Lars . . 4 Hessling Martin . . 5 Gugel Frederik . . 6 Richter Klaus . . 7 Buchner Johannes . . 8 Kessler Horst . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 122 "13C chemical shifts" 385 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-03-01 update BMRB 'completed entry citation' 2009-11-24 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 20159554 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Retzlaff Marco . . 2 Hagn Franz . . 3 Mitschke Lars . . 4 Hessling Martin . . 5 Gugel Frederik . . 6 Kessler Horst . . 7 Richter Klaus . . 8 Buchner Johannes . . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_name_full 'Molecular cell' _Journal_volume 37 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 344 _Page_last 354 _Year 2010 _Details . loop_ _Keyword ATPase 'Heat shock proteins' NMR structure stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Aha1 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Aha1 C-terminal domain' $Aha1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Aha1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Aha1 _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'Activator of Hsp90 ATPase' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 198 _Mol_residue_sequence ; GSHMPESQVKSNYTRGNQKS SFTEIKDSASKPKKNALPSS TSTSAPVSSTNKVPQNGSGN STSIYLEPTFNVPSSELYET FLDKQRILAWTRSAQFFNSG PKLETKEKFELFGGNVISEL VSCEKDKKLVFHWKLKDWSA PFNSTIEMTFHESQEFHETK LQVKWTGIPVGEEDRVRANF EEYYVRSIKLTFGFGAVL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 153 GLY 2 154 SER 3 155 HIS 4 156 MET 5 157 PRO 6 158 GLU 7 159 SER 8 160 GLN 9 161 VAL 10 162 LYS 11 163 SER 12 164 ASN 13 165 TYR 14 166 THR 15 167 ARG 16 168 GLY 17 169 ASN 18 170 GLN 19 171 LYS 20 172 SER 21 173 SER 22 174 PHE 23 175 THR 24 176 GLU 25 177 ILE 26 178 LYS 27 179 ASP 28 180 SER 29 181 ALA 30 182 SER 31 183 LYS 32 184 PRO 33 185 LYS 34 186 LYS 35 187 ASN 36 188 ALA 37 189 LEU 38 190 PRO 39 191 SER 40 192 SER 41 193 THR 42 194 SER 43 195 THR 44 196 SER 45 197 ALA 46 198 PRO 47 199 VAL 48 200 SER 49 201 SER 50 202 THR 51 203 ASN 52 204 LYS 53 205 VAL 54 206 PRO 55 207 GLN 56 208 ASN 57 209 GLY 58 210 SER 59 211 GLY 60 212 ASN 61 213 SER 62 214 THR 63 215 SER 64 216 ILE 65 217 TYR 66 218 LEU 67 219 GLU 68 220 PRO 69 221 THR 70 222 PHE 71 223 ASN 72 224 VAL 73 225 PRO 74 226 SER 75 227 SER 76 228 GLU 77 229 LEU 78 230 TYR 79 231 GLU 80 232 THR 81 233 PHE 82 234 LEU 83 235 ASP 84 236 LYS 85 237 GLN 86 238 ARG 87 239 ILE 88 240 LEU 89 241 ALA 90 242 TRP 91 243 THR 92 244 ARG 93 245 SER 94 246 ALA 95 247 GLN 96 248 PHE 97 249 PHE 98 250 ASN 99 251 SER 100 252 GLY 101 253 PRO 102 254 LYS 103 255 LEU 104 256 GLU 105 257 THR 106 258 LYS 107 259 GLU 108 260 LYS 109 261 PHE 110 262 GLU 111 263 LEU 112 264 PHE 113 265 GLY 114 266 GLY 115 267 ASN 116 268 VAL 117 269 ILE 118 270 SER 119 271 GLU 120 272 LEU 121 273 VAL 122 274 SER 123 275 CYS 124 276 GLU 125 277 LYS 126 278 ASP 127 279 LYS 128 280 LYS 129 281 LEU 130 282 VAL 131 283 PHE 132 284 HIS 133 285 TRP 134 286 LYS 135 287 LEU 136 288 LYS 137 289 ASP 138 290 TRP 139 291 SER 140 292 ALA 141 293 PRO 142 294 PHE 143 295 ASN 144 296 SER 145 297 THR 146 298 ILE 147 299 GLU 148 300 MET 149 301 THR 150 302 PHE 151 303 HIS 152 304 GLU 153 305 SER 154 306 GLN 155 307 GLU 156 308 PHE 157 309 HIS 158 310 GLU 159 311 THR 160 312 LYS 161 313 LEU 162 314 GLN 163 315 VAL 164 316 LYS 165 317 TRP 166 318 THR 167 319 GLY 168 320 ILE 169 321 PRO 170 322 VAL 171 323 GLY 172 324 GLU 173 325 GLU 174 326 ASP 175 327 ARG 176 328 VAL 177 329 ARG 178 330 ALA 179 331 ASN 180 332 PHE 181 333 GLU 182 334 GLU 183 335 TYR 184 336 TYR 185 337 VAL 186 338 ARG 187 339 SER 188 340 ILE 189 341 LYS 190 342 LEU 191 343 THR 192 344 PHE 193 345 GLY 194 346 PHE 195 347 GLY 196 348 ALA 197 349 VAL 198 350 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value DBJ GAA22442 "K7_Aha1p [Saccharomyces cerevisiae Kyokai no. 7]" 98.99 350 97.96 98.47 6.34e-134 EMBL CAA92357 "unknown [Saccharomyces cerevisiae]" 98.99 350 98.98 99.49 3.27e-136 EMBL CAA92365 "unknown [Saccharomyces cerevisiae]" 98.99 350 98.98 99.49 3.27e-136 EMBL CAY78716 "Aha1p [Saccharomyces cerevisiae EC1118]" 98.99 350 97.96 98.47 6.41e-134 GB AAA73862 "unknown, partial [Saccharomyces cerevisiae]" 98.99 222 98.98 99.49 7.37e-138 GB AAS56020 "YDR214W [Saccharomyces cerevisiae]" 98.99 350 98.98 99.49 3.27e-136 GB AHY75197 "Aha1p [Saccharomyces cerevisiae YJM993]" 98.99 350 97.96 98.98 1.00e-134 GB AJP37925 "Aha1p [Saccharomyces cerevisiae YJM1078]" 98.99 350 98.47 98.98 3.97e-135 GB AJU58047 "Aha1p [Saccharomyces cerevisiae YJM189]" 98.99 350 97.45 98.98 7.23e-134 REF NP_010500 "Aha1p [Saccharomyces cerevisiae S288c]" 98.99 350 98.98 99.49 3.27e-136 SP Q12449 "RecName: Full=Hsp90 co-chaperone AHA1; AltName: Full=Activator of Hsp90 ATPase protein 1" 98.99 350 98.98 99.49 3.27e-136 TPG DAA12058 "TPA: Aha1p [Saccharomyces cerevisiae S288c]" 98.99 350 98.98 99.49 3.27e-136 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Aha1 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name _Details $Aha1 'recombinant technology' . Escherichia coli BL21 DE3 pET28a 'N-terminal His6-tag, cleavable with Thrombin' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1.2mM Aha1 C-terminal domain in 20mM K-phospate 50mM KCl pH7.5' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Aha1 1.2 mM '[U-100% 13C; U-100% 15N]' 'potassium phosphate' 20 mM 'natural abundance' KCl 50 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_PASTA _Saveframe_category software _Name PASTA _Version 2 loop_ _Vendor _Address _Electronic_address 'Gemmecker and Kessler' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'NMR Assignment' save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; 20mM K-phosphate pH7.5 50mM KCl ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 7.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'Aha1 C-terminal domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 212 60 ASN C C 174.55 0.05 1 2 212 60 ASN CA C 52.87 0.05 1 3 212 60 ASN CB C 38.48 0.05 1 4 213 61 SER H H 8.10 0.02 1 5 213 61 SER C C 172.99 0.05 1 6 213 61 SER CA C 57.03 0.05 1 7 213 61 SER CB C 65.77 0.05 1 8 213 61 SER N N 114.52 0.05 1 9 214 62 THR H H 9.44 0.02 1 10 214 62 THR C C 171.88 0.05 1 11 214 62 THR CA C 59.30 0.05 1 12 214 62 THR CB C 70.06 0.05 1 13 214 62 THR N N 116.90 0.05 1 14 215 63 SER H H 8.01 0.02 1 15 215 63 SER C C 173.53 0.05 1 16 215 63 SER CA C 55.68 0.05 1 17 215 63 SER CB C 66.67 0.05 1 18 215 63 SER N N 114.51 0.05 1 19 216 64 ILE H H 8.99 0.02 1 20 216 64 ILE C C 173.18 0.05 1 21 216 64 ILE CA C 59.84 0.05 1 22 216 64 ILE CB C 42.22 0.05 1 23 216 64 ILE N N 115.15 0.05 1 24 217 65 TYR H H 8.17 0.02 1 25 217 65 TYR C C 175.04 0.05 1 26 217 65 TYR CA C 56.22 0.05 1 27 217 65 TYR CB C 40.98 0.05 1 28 217 65 TYR N N 121.37 0.05 1 29 218 66 LEU H H 8.43 0.02 1 30 218 66 LEU C C 176.00 0.05 1 31 218 66 LEU CA C 53.55 0.05 1 32 218 66 LEU CB C 45.05 0.05 1 33 218 66 LEU N N 124.76 0.05 1 34 225 73 PRO CA C 62.07 0.05 1 35 225 73 PRO CB C 31.97 0.05 1 36 226 74 SER H H 8.85 0.02 1 37 226 74 SER C C 176.50 0.05 1 38 226 74 SER CA C 62.52 0.05 1 39 226 74 SER CB C 64.40 0.05 1 40 226 74 SER N N 119.97 0.05 1 41 227 75 SER H H 8.42 0.02 1 42 227 75 SER C C 177.01 0.05 1 43 227 75 SER CA C 60.41 0.05 1 44 227 75 SER CB C 61.92 0.05 1 45 227 75 SER N N 115.22 0.05 1 46 228 76 GLU H H 6.64 0.02 1 47 228 76 GLU C C 179.48 0.05 1 48 228 76 GLU CA C 57.48 0.05 1 49 228 76 GLU CB C 29.27 0.05 1 50 228 76 GLU N N 119.93 0.05 1 51 229 77 LEU H H 7.38 0.02 1 52 229 77 LEU C C 177.01 0.05 1 53 229 77 LEU CA C 57.11 0.05 1 54 229 77 LEU CB C 40.54 0.05 1 55 229 77 LEU N N 122.13 0.05 1 56 230 78 TYR H H 8.75 0.02 1 57 230 78 TYR C C 177.06 0.05 1 58 230 78 TYR CA C 62.26 0.05 1 59 230 78 TYR CB C 38.18 0.05 1 60 230 78 TYR N N 120.30 0.05 1 61 231 79 GLU H H 7.46 0.02 1 62 231 79 GLU C C 179.14 0.05 1 63 231 79 GLU CA C 58.25 0.05 1 64 231 79 GLU CB C 29.14 0.05 1 65 231 79 GLU N N 114.62 0.05 1 66 232 80 THR H H 7.48 0.02 1 67 232 80 THR C C 172.89 0.05 1 68 232 80 THR CA C 66.65 0.05 1 69 232 80 THR CB C 67.61 0.05 1 70 232 80 THR N N 116.38 0.05 1 71 233 81 PHE H H 7.11 0.02 1 72 233 81 PHE C C 175.18 0.05 1 73 233 81 PHE CA C 59.78 0.05 1 74 233 81 PHE CB C 41.05 0.05 1 75 233 81 PHE N N 114.26 0.05 1 76 234 82 LEU H H 7.01 0.02 1 77 234 82 LEU C C 176.28 0.05 1 78 234 82 LEU CA C 55.27 0.05 1 79 234 82 LEU CB C 45.84 0.05 1 80 234 82 LEU N N 115.98 0.05 1 81 235 83 ASP H H 8.25 0.02 1 82 235 83 ASP C C 176.18 0.05 1 83 235 83 ASP CA C 54.74 0.05 1 84 235 83 ASP CB C 42.23 0.05 1 85 235 83 ASP N N 119.45 0.05 1 86 236 84 LYS H H 7.91 0.02 1 87 236 84 LYS C C 177.82 0.05 1 88 236 84 LYS CA C 60.61 0.05 1 89 236 84 LYS CB C 31.27 0.05 1 90 236 84 LYS N N 126.15 0.05 1 91 237 85 GLN H H 8.08 0.02 1 92 237 85 GLN C C 180.07 0.05 1 93 237 85 GLN CA C 58.85 0.05 1 94 237 85 GLN CB C 27.06 0.05 1 95 237 85 GLN N N 118.49 0.05 1 96 238 86 ARG H H 8.39 0.02 1 97 238 86 ARG C C 177.84 0.05 1 98 238 86 ARG CA C 60.31 0.05 1 99 238 86 ARG CB C 29.34 0.05 1 100 238 86 ARG N N 120.88 0.05 1 101 239 87 ILE H H 8.65 0.02 1 102 239 87 ILE C C 180.38 0.05 1 103 239 87 ILE CA C 64.18 0.05 1 104 239 87 ILE CB C 37.90 0.05 1 105 239 87 ILE N N 118.68 0.05 1 106 240 88 LEU H H 8.31 0.02 1 107 240 88 LEU C C 178.70 0.05 1 108 240 88 LEU CA C 57.99 0.05 1 109 240 88 LEU CB C 41.02 0.05 1 110 240 88 LEU N N 122.20 0.05 1 111 241 89 ALA H H 7.43 0.02 1 112 241 89 ALA C C 178.98 0.05 1 113 241 89 ALA CA C 54.86 0.05 1 114 241 89 ALA CB C 17.52 0.05 1 115 241 89 ALA N N 121.42 0.05 1 116 242 90 TRP H H 7.97 0.02 1 117 242 90 TRP C C 178.85 0.05 1 118 242 90 TRP CA C 57.58 0.05 1 119 242 90 TRP CB C 28.90 0.05 1 120 242 90 TRP N N 110.82 0.05 1 121 243 91 THR H H 7.82 0.02 1 122 243 91 THR C C 175.13 0.05 1 123 243 91 THR CA C 63.77 0.05 1 124 243 91 THR CB C 69.59 0.05 1 125 243 91 THR N N 114.02 0.05 1 126 244 92 ARG H H 7.42 0.02 1 127 244 92 ARG C C 175.82 0.05 1 128 244 92 ARG CA C 57.85 0.05 1 129 244 92 ARG CB C 27.21 0.05 1 130 244 92 ARG N N 115.22 0.05 1 131 245 93 SER H H 7.48 0.02 1 132 245 93 SER C C 171.00 0.05 1 133 245 93 SER CA C 57.84 0.05 1 134 245 93 SER CB C 61.48 0.05 1 135 245 93 SER N N 112.19 0.05 1 136 246 94 ALA H H 7.73 0.02 1 137 246 94 ALA C C 174.32 0.05 1 138 246 94 ALA CA C 51.11 0.05 1 139 246 94 ALA CB C 22.49 0.05 1 140 246 94 ALA N N 127.99 0.05 1 141 247 95 GLN H H 8.48 0.02 1 142 247 95 GLN C C 172.57 0.05 1 143 247 95 GLN CA C 54.05 0.05 1 144 247 95 GLN CB C 30.64 0.05 1 145 247 95 GLN N N 121.35 0.05 1 146 248 96 PHE H H 8.33 0.02 1 147 248 96 PHE C C 176.12 0.05 1 148 248 96 PHE CA C 55.39 0.05 1 149 248 96 PHE CB C 40.97 0.05 1 150 248 96 PHE N N 122.02 0.05 1 151 249 97 PHE H H 9.72 0.02 1 152 249 97 PHE C C 175.41 0.05 1 153 249 97 PHE CA C 58.68 0.05 1 154 249 97 PHE CB C 39.62 0.05 1 155 249 97 PHE N N 119.89 0.05 1 156 250 98 ASN H H 8.03 0.02 1 157 250 98 ASN C C 177.41 0.05 1 158 250 98 ASN CA C 51.78 0.05 1 159 250 98 ASN CB C 39.47 0.05 1 160 250 98 ASN N N 117.81 0.05 1 161 251 99 SER C C 174.80 0.05 1 162 251 99 SER CA C 58.88 0.05 1 163 251 99 SER CB C 63.80 0.05 1 164 252 100 GLY H H 8.00 0.02 1 165 252 100 GLY C C 173.24 0.05 1 166 252 100 GLY CA C 44.28 0.05 1 167 252 100 GLY N N 111.34 0.05 1 168 253 101 PRO CA C 64.27 0.05 1 169 253 101 PRO CB C 31.52 0.05 1 170 254 102 LYS H H 7.58 0.02 1 171 254 102 LYS C C 175.72 0.05 1 172 254 102 LYS CA C 52.63 0.05 1 173 254 102 LYS CB C 34.50 0.05 1 174 254 102 LYS N N 117.18 0.05 1 175 255 103 LEU H H 8.35 0.02 1 176 255 103 LEU C C 175.46 0.05 1 177 255 103 LEU CA C 55.34 0.05 1 178 255 103 LEU CB C 43.11 0.05 1 179 255 103 LEU N N 122.02 0.05 1 180 256 104 GLU H H 8.07 0.02 1 181 256 104 GLU C C 176.81 0.05 1 182 256 104 GLU CA C 53.11 0.05 1 183 256 104 GLU CB C 31.84 0.05 1 184 256 104 GLU N N 120.05 0.05 1 185 257 105 THR H H 8.45 0.02 1 186 257 105 THR C C 175.92 0.05 1 187 257 105 THR CA C 64.47 0.05 1 188 257 105 THR CB C 68.19 0.05 1 189 257 105 THR N N 114.29 0.05 1 190 258 106 LYS H H 9.05 0.02 1 191 258 106 LYS C C 175.39 0.05 1 192 258 106 LYS CA C 58.02 0.05 1 193 258 106 LYS CB C 28.95 0.05 1 194 258 106 LYS N N 116.33 0.05 1 195 259 107 GLU H H 8.19 0.02 1 196 259 107 GLU C C 175.68 0.05 1 197 259 107 GLU CA C 56.56 0.05 1 198 259 107 GLU CB C 30.47 0.05 1 199 259 107 GLU N N 121.94 0.05 1 200 260 108 LYS H H 8.45 0.02 1 201 260 108 LYS C C 175.82 0.05 1 202 260 108 LYS CA C 55.43 0.05 1 203 260 108 LYS CB C 33.30 0.05 1 204 260 108 LYS N N 127.63 0.05 1 205 261 109 PHE H H 8.95 0.02 1 206 261 109 PHE C C 172.00 0.05 1 207 261 109 PHE CA C 55.98 0.05 1 208 261 109 PHE CB C 41.03 0.05 1 209 261 109 PHE N N 117.23 0.05 1 210 262 110 GLU H H 8.44 0.02 1 211 262 110 GLU C C 175.65 0.05 1 212 262 110 GLU CA C 53.24 0.05 1 213 262 110 GLU CB C 33.31 0.05 1 214 262 110 GLU N N 117.00 0.05 1 215 263 111 LEU H H 8.80 0.02 1 216 263 111 LEU C C 177.17 0.05 1 217 263 111 LEU CA C 52.03 0.05 1 218 263 111 LEU CB C 45.87 0.05 1 219 263 111 LEU N N 120.83 0.05 1 220 264 112 PHE H H 7.72 0.02 1 221 264 112 PHE C C 177.88 0.05 1 222 264 112 PHE CA C 56.16 0.05 1 223 264 112 PHE CB C 34.55 0.05 1 224 264 112 PHE N N 114.93 0.05 1 225 265 113 GLY H H 8.18 0.02 1 226 265 113 GLY C C 175.48 0.05 1 227 265 113 GLY CA C 45.97 0.05 1 228 265 113 GLY N N 110.34 0.05 1 229 266 114 GLY H H 7.41 0.02 1 230 266 114 GLY C C 173.16 0.05 1 231 266 114 GLY CA C 44.15 0.05 1 232 266 114 GLY N N 105.40 0.05 1 233 267 115 ASN H H 7.28 0.02 1 234 267 115 ASN C C 174.44 0.05 1 235 267 115 ASN CA C 55.37 0.05 1 236 267 115 ASN CB C 39.50 0.05 1 237 267 115 ASN N N 116.55 0.05 1 238 268 116 VAL H H 7.66 0.02 1 239 268 116 VAL C C 173.97 0.05 1 240 268 116 VAL CA C 60.09 0.05 1 241 268 116 VAL CB C 33.89 0.05 1 242 268 116 VAL N N 115.64 0.05 1 243 269 117 ILE H H 8.09 0.02 1 244 269 117 ILE C C 175.81 0.05 1 245 269 117 ILE CA C 60.38 0.05 1 246 269 117 ILE CB C 39.08 0.05 1 247 269 117 ILE N N 126.36 0.05 1 248 270 118 SER H H 8.62 0.02 1 249 270 118 SER C C 170.56 0.05 1 250 270 118 SER CA C 54.52 0.05 1 251 270 118 SER CB C 66.17 0.05 1 252 270 118 SER N N 123.68 0.05 1 253 271 119 GLU H H 7.68 0.02 1 254 271 119 GLU C C 176.14 0.05 1 255 271 119 GLU CA C 54.66 0.05 1 256 271 119 GLU CB C 34.11 0.05 1 257 271 119 GLU N N 119.61 0.05 1 258 272 120 LEU H H 8.98 0.02 1 259 272 120 LEU C C 175.02 0.05 1 260 272 120 LEU CA C 55.04 0.05 1 261 272 120 LEU CB C 40.54 0.05 1 262 272 120 LEU N N 128.03 0.05 1 263 273 121 VAL H H 9.22 0.02 1 264 273 121 VAL C C 176.00 0.05 1 265 273 121 VAL CA C 63.69 0.05 1 266 273 121 VAL CB C 32.18 0.05 1 267 273 121 VAL N N 129.88 0.05 1 268 274 122 SER H H 7.40 0.02 1 269 274 122 SER C C 171.19 0.05 1 270 274 122 SER CA C 57.06 0.05 1 271 274 122 SER CB C 64.38 0.05 1 272 274 122 SER N N 109.89 0.05 1 273 275 123 CYS H H 8.47 0.02 1 274 275 123 CYS C C 172.56 0.05 1 275 275 123 CYS CA C 55.16 0.05 1 276 275 123 CYS CB C 31.44 0.05 1 277 275 123 CYS N N 114.93 0.05 1 278 276 124 GLU H H 8.88 0.02 1 279 276 124 GLU C C 175.01 0.05 1 280 276 124 GLU CA C 55.44 0.05 1 281 276 124 GLU CB C 31.54 0.05 1 282 276 124 GLU N N 123.10 0.05 1 283 277 125 LYS H H 8.35 0.02 1 284 277 125 LYS C C 174.60 0.05 1 285 277 125 LYS CA C 58.28 0.05 1 286 277 125 LYS CB C 31.78 0.05 1 287 277 125 LYS N N 127.86 0.05 1 288 278 126 ASP C C 173.20 0.05 1 289 278 126 ASP CA C 57.73 0.05 1 290 278 126 ASP CB C 38.70 0.05 1 291 279 127 LYS H H 7.92 0.02 1 292 279 127 LYS C C 176.70 0.05 1 293 279 127 LYS CA C 57.58 0.05 1 294 279 127 LYS CB C 35.83 0.05 1 295 279 127 LYS N N 115.86 0.05 1 296 280 128 LYS H H 8.62 0.02 1 297 280 128 LYS C C 174.77 0.05 1 298 280 128 LYS CA C 55.55 0.05 1 299 280 128 LYS CB C 35.98 0.05 1 300 280 128 LYS N N 120.57 0.05 1 301 281 129 LEU H H 9.10 0.02 1 302 281 129 LEU C C 174.65 0.05 1 303 281 129 LEU CA C 53.87 0.05 1 304 281 129 LEU CB C 47.15 0.05 1 305 281 129 LEU N N 125.08 0.05 1 306 282 130 VAL H H 7.93 0.02 1 307 282 130 VAL C C 175.13 0.05 1 308 282 130 VAL CA C 60.38 0.05 1 309 282 130 VAL CB C 33.09 0.05 1 310 282 130 VAL N N 119.86 0.05 1 311 283 131 PHE H H 9.25 0.02 1 312 283 131 PHE C C 177.43 0.05 1 313 283 131 PHE CA C 55.91 0.05 1 314 283 131 PHE CB C 42.79 0.05 1 315 283 131 PHE N N 123.21 0.05 1 316 284 132 HIS H H 9.14 0.02 1 317 284 132 HIS C C 176.43 0.05 1 318 284 132 HIS CA C 54.80 0.05 1 319 284 132 HIS CB C 30.72 0.05 1 320 284 132 HIS N N 118.58 0.05 1 321 285 133 TRP H H 9.26 0.02 1 322 285 133 TRP C C 175.12 0.05 1 323 285 133 TRP CA C 59.58 0.05 1 324 285 133 TRP CB C 34.91 0.05 1 325 285 133 TRP N N 126.43 0.05 1 326 286 134 LYS H H 8.71 0.02 1 327 286 134 LYS C C 172.68 0.05 1 328 286 134 LYS CA C 55.24 0.05 1 329 286 134 LYS CB C 35.11 0.05 1 330 286 134 LYS N N 129.88 0.05 1 331 287 135 LEU C C 179.40 0.05 1 332 287 135 LEU CA C 52.54 0.05 1 333 287 135 LEU CB C 41.09 0.05 1 334 288 136 LYS H H 8.32 0.02 1 335 288 136 LYS C C 176.00 0.05 1 336 288 136 LYS CA C 58.70 0.05 1 337 288 136 LYS CB C 31.31 0.05 1 338 288 136 LYS N N 122.15 0.05 1 339 289 137 ASP H H 7.85 0.02 1 340 289 137 ASP C C 176.86 0.05 1 341 289 137 ASP CA C 53.35 0.05 1 342 289 137 ASP CB C 40.06 0.05 1 343 289 137 ASP N N 112.02 0.05 1 344 290 138 TRP H H 7.58 0.02 1 345 290 138 TRP C C 177.26 0.05 1 346 290 138 TRP CA C 55.05 0.05 1 347 290 138 TRP CB C 29.23 0.05 1 348 290 138 TRP N N 120.40 0.05 1 349 291 139 SER H H 9.05 0.02 1 350 291 139 SER C C 174.45 0.05 1 351 291 139 SER CA C 57.91 0.05 1 352 291 139 SER CB C 64.01 0.05 1 353 291 139 SER N N 119.71 0.05 1 354 292 140 ALA H H 8.66 0.02 1 355 292 140 ALA C C 176.73 0.05 1 356 292 140 ALA CA C 51.21 0.05 1 357 292 140 ALA CB C 16.48 0.05 1 358 292 140 ALA N N 126.68 0.05 1 359 293 141 PRO CA C 64.40 0.05 1 360 293 141 PRO CB C 30.75 0.05 1 361 294 142 PHE H H 7.57 0.02 1 362 294 142 PHE C C 177.40 0.05 1 363 294 142 PHE CA C 57.33 0.05 1 364 294 142 PHE CB C 39.98 0.05 1 365 294 142 PHE N N 115.79 0.05 1 366 295 143 ASN H H 8.79 0.02 1 367 295 143 ASN C C 174.79 0.05 1 368 295 143 ASN CA C 54.47 0.05 1 369 295 143 ASN CB C 37.77 0.05 1 370 295 143 ASN N N 120.40 0.05 1 371 296 144 SER H H 8.92 0.02 1 372 296 144 SER C C 173.28 0.05 1 373 296 144 SER CA C 59.40 0.05 1 374 296 144 SER CB C 67.10 0.05 1 375 296 144 SER N N 123.66 0.05 1 376 297 145 THR H H 9.23 0.02 1 377 297 145 THR C C 172.10 0.05 1 378 297 145 THR CA C 62.67 0.05 1 379 297 145 THR CB C 70.58 0.05 1 380 297 145 THR N N 116.80 0.05 1 381 298 146 ILE H H 9.42 0.02 1 382 298 146 ILE C C 174.06 0.05 1 383 298 146 ILE CA C 59.86 0.05 1 384 298 146 ILE CB C 39.45 0.05 1 385 298 146 ILE N N 126.05 0.05 1 386 299 147 GLU H H 8.91 0.02 1 387 299 147 GLU C C 175.03 0.05 1 388 299 147 GLU CA C 54.52 0.05 1 389 299 147 GLU CB C 31.05 0.05 1 390 299 147 GLU N N 127.11 0.05 1 391 300 148 MET H H 9.53 0.02 1 392 300 148 MET C C 174.87 0.05 1 393 300 148 MET CA C 53.82 0.05 1 394 300 148 MET CB C 34.36 0.05 1 395 300 148 MET N N 126.02 0.05 1 396 301 149 THR H H 9.03 0.02 1 397 301 149 THR C C 173.13 0.05 1 398 301 149 THR CA C 60.52 0.05 1 399 301 149 THR CB C 70.04 0.05 1 400 301 149 THR N N 116.63 0.05 1 401 302 150 PHE H H 9.02 0.02 1 402 302 150 PHE C C 175.21 0.05 1 403 302 150 PHE CA C 55.96 0.05 1 404 302 150 PHE CB C 43.86 0.05 1 405 302 150 PHE N N 119.29 0.05 1 406 303 151 HIS H H 8.76 0.02 1 407 303 151 HIS C C 173.13 0.05 1 408 303 151 HIS CA C 52.78 0.05 1 409 303 151 HIS CB C 37.05 0.05 1 410 303 151 HIS N N 125.20 0.05 1 411 304 152 GLU H H 7.28 0.02 1 412 304 152 GLU C C 171.57 0.05 1 413 304 152 GLU CA C 57.98 0.05 1 414 304 152 GLU CB C 32.98 0.05 1 415 304 152 GLU N N 117.19 0.05 1 416 306 154 GLN C C 177.19 0.05 1 417 306 154 GLN CA C 57.62 0.05 1 418 306 154 GLN CB C 27.76 0.05 1 419 307 155 GLU H H 8.39 0.02 1 420 307 155 GLU C C 176.53 0.05 1 421 307 155 GLU CA C 57.70 0.05 1 422 307 155 GLU CB C 28.98 0.05 1 423 307 155 GLU N N 118.58 0.05 1 424 308 156 PHE H H 7.49 0.02 1 425 308 156 PHE C C 174.91 0.05 1 426 308 156 PHE CA C 56.54 0.05 1 427 308 156 PHE CB C 38.89 0.05 1 428 308 156 PHE N N 114.68 0.05 1 429 309 157 HIS H H 7.83 0.02 1 430 309 157 HIS C C 173.39 0.05 1 431 309 157 HIS CA C 55.98 0.05 1 432 309 157 HIS CB C 26.92 0.05 1 433 309 157 HIS N N 117.35 0.05 1 434 310 158 GLU H H 7.51 0.02 1 435 310 158 GLU C C 175.23 0.05 1 436 310 158 GLU CA C 54.52 0.05 1 437 310 158 GLU CB C 32.93 0.05 1 438 310 158 GLU N N 116.30 0.05 1 439 311 159 THR H H 9.20 0.02 1 440 311 159 THR C C 173.33 0.05 1 441 311 159 THR CA C 62.72 0.05 1 442 311 159 THR CB C 70.44 0.05 1 443 311 159 THR N N 120.12 0.05 1 444 312 160 LYS H H 9.00 0.02 1 445 312 160 LYS C C 173.87 0.05 1 446 312 160 LYS CA C 54.76 0.05 1 447 312 160 LYS CB C 33.37 0.05 1 448 312 160 LYS N N 128.47 0.05 1 449 313 161 LEU H H 8.62 0.02 1 450 313 161 LEU C C 174.44 0.05 1 451 313 161 LEU CA C 51.77 0.05 1 452 313 161 LEU CB C 43.69 0.05 1 453 313 161 LEU N N 129.04 0.05 1 454 314 162 GLN H H 8.63 0.02 1 455 314 162 GLN C C 175.75 0.05 1 456 314 162 GLN CA C 55.47 0.05 1 457 314 162 GLN CB C 28.07 0.05 1 458 314 162 GLN N N 122.30 0.05 1 459 315 163 VAL H H 8.93 0.02 1 460 315 163 VAL C C 173.78 0.05 1 461 315 163 VAL CA C 61.23 0.05 1 462 315 163 VAL CB C 32.17 0.05 1 463 315 163 VAL N N 126.69 0.05 1 464 316 164 LYS H H 8.69 0.02 1 465 316 164 LYS C C 174.37 0.05 1 466 316 164 LYS CA C 55.19 0.05 1 467 316 164 LYS CB C 33.69 0.05 1 468 316 164 LYS N N 127.44 0.05 1 469 317 165 TRP H H 8.77 0.02 1 470 317 165 TRP C C 175.33 0.05 1 471 317 165 TRP CA C 54.19 0.05 1 472 317 165 TRP CB C 32.11 0.05 1 473 317 165 TRP N N 134.92 0.05 1 474 318 166 THR H H 9.54 0.02 1 475 318 166 THR C C 175.31 0.05 1 476 318 166 THR CA C 59.64 0.05 1 477 318 166 THR CB C 71.59 0.05 1 478 318 166 THR N N 114.87 0.05 1 479 319 167 GLY H H 8.74 0.02 1 480 319 167 GLY C C 174.11 0.05 1 481 319 167 GLY CA C 46.09 0.05 1 482 319 167 GLY N N 108.63 0.05 1 483 320 168 ILE H H 7.93 0.02 1 484 320 168 ILE C C 174.64 0.05 1 485 320 168 ILE CA C 58.52 0.05 1 486 320 168 ILE CB C 39.57 0.05 1 487 320 168 ILE N N 120.48 0.05 1 488 321 169 PRO CA C 62.28 0.05 1 489 321 169 PRO CB C 29.56 0.05 1 490 322 170 VAL H H 7.52 0.02 1 491 322 170 VAL C C 177.00 0.05 1 492 322 170 VAL CA C 64.72 0.05 1 493 322 170 VAL CB C 30.59 0.05 1 494 322 170 VAL N N 122.23 0.05 1 495 323 171 GLY H H 9.09 0.02 1 496 323 171 GLY C C 175.99 0.05 1 497 323 171 GLY CA C 44.56 0.05 1 498 323 171 GLY N N 117.08 0.05 1 499 324 172 GLU H H 7.81 0.02 1 500 324 172 GLU C C 176.58 0.05 1 501 324 172 GLU CA C 55.36 0.05 1 502 324 172 GLU CB C 30.08 0.05 1 503 324 172 GLU N N 118.17 0.05 1 504 325 173 GLU C C 177.60 0.05 1 505 325 173 GLU CA C 61.07 0.05 1 506 325 173 GLU CB C 27.24 0.05 1 507 326 174 ASP H H 8.24 0.02 1 508 326 174 ASP C C 178.62 0.05 1 509 326 174 ASP CA C 57.11 0.05 1 510 326 174 ASP CB C 39.23 0.05 1 511 326 174 ASP N N 119.15 0.05 1 512 327 175 ARG H H 7.95 0.02 1 513 327 175 ARG C C 179.82 0.05 1 514 327 175 ARG CA C 58.95 0.05 1 515 327 175 ARG CB C 29.59 0.05 1 516 327 175 ARG N N 123.52 0.05 1 517 328 176 VAL H H 8.32 0.02 1 518 328 176 VAL C C 177.16 0.05 1 519 328 176 VAL CA C 65.92 0.05 1 520 328 176 VAL CB C 29.38 0.05 1 521 328 176 VAL N N 117.60 0.05 1 522 329 177 ARG H H 7.75 0.02 1 523 329 177 ARG C C 178.18 0.05 1 524 329 177 ARG CA C 60.05 0.05 1 525 329 177 ARG CB C 29.52 0.05 1 526 329 177 ARG N N 120.05 0.05 1 527 330 178 ALA H H 7.94 0.02 1 528 330 178 ALA C C 180.97 0.05 1 529 330 178 ALA CA C 54.69 0.05 1 530 330 178 ALA CB C 17.54 0.05 1 531 330 178 ALA N N 119.23 0.05 1 532 331 179 ASN H H 8.03 0.02 1 533 331 179 ASN C C 175.81 0.05 1 534 331 179 ASN CA C 56.81 0.05 1 535 331 179 ASN CB C 39.38 0.05 1 536 331 179 ASN N N 117.74 0.05 1 537 332 180 PHE H H 8.79 0.02 1 538 332 180 PHE C C 178.87 0.05 1 539 332 180 PHE CA C 61.41 0.05 1 540 332 180 PHE CB C 39.83 0.05 1 541 332 180 PHE N N 120.26 0.05 1 542 333 181 GLU H H 8.94 0.02 1 543 333 181 GLU C C 177.93 0.05 1 544 333 181 GLU CA C 59.58 0.05 1 545 333 181 GLU CB C 28.71 0.05 1 546 333 181 GLU N N 118.49 0.05 1 547 334 182 GLU H H 7.96 0.02 1 548 334 182 GLU C C 177.73 0.05 1 549 334 182 GLU CA C 58.54 0.05 1 550 334 182 GLU CB C 29.52 0.05 1 551 334 182 GLU N N 117.14 0.05 1 552 335 183 TYR H H 8.43 0.02 1 553 335 183 TYR C C 175.81 0.05 1 554 335 183 TYR CA C 59.61 0.05 1 555 335 183 TYR CB C 37.44 0.05 1 556 335 183 TYR N N 114.75 0.05 1 557 336 184 TYR H H 7.67 0.02 1 558 336 184 TYR C C 175.03 0.05 1 559 336 184 TYR CA C 57.94 0.05 1 560 336 184 TYR CB C 36.83 0.05 1 561 336 184 TYR N N 115.58 0.05 1 562 337 185 VAL H H 7.55 0.02 1 563 337 185 VAL C C 177.43 0.05 1 564 337 185 VAL CA C 67.12 0.05 1 565 337 185 VAL CB C 30.79 0.05 1 566 337 185 VAL N N 115.21 0.05 1 567 338 186 ARG H H 8.31 0.02 1 568 338 186 ARG C C 178.51 0.05 1 569 338 186 ARG CA C 60.10 0.05 1 570 338 186 ARG CB C 28.88 0.05 1 571 338 186 ARG N N 116.85 0.05 1 572 339 187 SER H H 6.63 0.02 1 573 339 187 SER C C 178.50 0.05 1 574 339 187 SER CA C 60.72 0.05 1 575 339 187 SER CB C 63.35 0.05 1 576 339 187 SER N N 108.90 0.05 1 577 340 188 ILE H H 8.15 0.02 1 578 340 188 ILE C C 177.80 0.05 1 579 340 188 ILE CA C 67.08 0.05 1 580 340 188 ILE CB C 37.05 0.05 1 581 340 188 ILE N N 123.33 0.05 1 582 341 189 LYS H H 7.97 0.02 1 583 341 189 LYS C C 179.56 0.05 1 584 341 189 LYS CA C 62.03 0.05 1 585 341 189 LYS CB C 31.73 0.05 1 586 341 189 LYS N N 117.24 0.05 1 587 342 190 LEU H H 8.38 0.02 1 588 342 190 LEU C C 179.63 0.05 1 589 342 190 LEU CA C 56.93 0.05 1 590 342 190 LEU CB C 41.83 0.05 1 591 342 190 LEU N N 117.31 0.05 1 592 343 191 THR H H 8.40 0.02 1 593 343 191 THR C C 175.25 0.05 1 594 343 191 THR CA C 66.41 0.05 1 595 343 191 THR CB C 68.48 0.05 1 596 343 191 THR N N 115.28 0.05 1 597 344 192 PHE H H 7.02 0.02 1 598 344 192 PHE C C 175.47 0.05 1 599 344 192 PHE CA C 56.89 0.05 1 600 344 192 PHE CB C 38.16 0.05 1 601 344 192 PHE N N 114.22 0.05 1 602 345 193 GLY H H 7.49 0.02 1 603 345 193 GLY C C 175.92 0.05 1 604 345 193 GLY CA C 46.44 0.05 1 605 345 193 GLY N N 108.88 0.05 1 606 346 194 PHE H H 7.70 0.02 1 607 346 194 PHE C C 175.45 0.05 1 608 346 194 PHE CA C 53.35 0.05 1 609 346 194 PHE CB C 38.15 0.05 1 610 346 194 PHE N N 117.38 0.05 1 611 347 195 GLY H H 7.96 0.02 1 612 347 195 GLY C C 172.15 0.05 1 613 347 195 GLY CA C 44.69 0.05 1 614 347 195 GLY N N 109.43 0.05 1 615 348 196 ALA H H 8.19 0.02 1 616 348 196 ALA C C 177.80 0.05 1 617 348 196 ALA CA C 51.94 0.05 1 618 348 196 ALA CB C 19.02 0.05 1 619 348 196 ALA N N 123.22 0.05 1 620 349 197 VAL H H 8.26 0.02 1 621 349 197 VAL C C 174.73 0.05 1 622 349 197 VAL CA C 61.39 0.05 1 623 349 197 VAL CB C 32.56 0.05 1 624 349 197 VAL N N 119.33 0.05 1 625 350 198 LEU H H 7.82 0.02 1 626 350 198 LEU C C 182.33 0.05 1 627 350 198 LEU CA C 56.23 0.05 1 628 350 198 LEU CB C 42.63 0.05 1 629 350 198 LEU N N 131.02 0.05 1 stop_ save_