data_5376 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; C-terminal peptide of alpha-subunit of transducin ; _BMRB_accession_number 5376 _BMRB_flat_file_name bmr5376.str _Entry_type original _Submission_date 2002-05-15 _Accession_date 2002-05-15 _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 Koenig Bernd W. . 2 Kontaxis Georg . . 3 Mitchell Drake C. . 4 Louis John M. . 5 Litman Burton J. . 6 Bax Ad . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 69 "13C chemical shifts" 36 "15N chemical shifts" 10 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-06 original author . stop_ _Original_release_date 2003-01-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Orientation of a G Protein Fragment in the Receptor Bound State from Residual Dipolar Couplings ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22206956 _PubMed_ID 12217702 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Koenig Bernd W. . 2 Kontaxis Georg . . 3 Mitchell Drake C. . 4 Louis John M. . 5 Litman Burton J. . 6 Bax Ad . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 322 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 441 _Page_last 461 _Year 2002 _Details . loop_ _Keyword NMR 'membrane protein' rhodopsin transducin 'transferred dipolar couplings' stop_ save_ ################################## # Molecular system description # ################################## save_Gt_alpha340-350 _Saveframe_category molecular_system _Mol_system_name 'complex of transducin peptide and rhodopsin' _Abbreviation_common Gt-alpha(340-350) _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S2 peptide' $S2 rhodopsin $rhodopsin stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'signal transduction in the visual system' stop_ _Database_query_date . _Details 'peptide analog of C-terminal binding region of alpha subunit of transducin' save_ ######################## # Monomeric polymers # ######################## save_S2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Gt-alpha(340-350) _Name_variant Gt-alpha(340-350)K341R,C347S _Abbreviation_common S2 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 11 _Mol_residue_sequence IRENLKDSGLF loop_ _Residue_seq_code _Residue_label 1 ILE 2 ARG 3 GLU 4 ASN 5 LEU 6 LYS 7 ASP 8 SER 9 GLY 10 LEU 11 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 PDB 1F88 "Crystal Structure Of Bovine Rhodopsin" 100.00 348 100.00 100.00 0.00e+00 PDB 1GZM "Structure Of Bovine Rhodopsin In A Trigonal Crystal Form" 100.00 349 100.00 100.00 0.00e+00 PDB 1HZX "Crystal Structure Of Bovine Rhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 1JFP "Structure Of Bovine Rhodopsin (Dark Adapted)" 100.00 348 100.00 100.00 0.00e+00 PDB 1L9H "Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution" 100.00 349 100.00 100.00 0.00e+00 PDB 1LN6 "Structure Of Bovine Rhodopsin (Metarhodopsin Ii)" 100.00 348 100.00 100.00 0.00e+00 PDB 1U19 "Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution" 100.00 349 100.00 100.00 0.00e+00 PDB 2G87 "Crystallographic Model Of Bathorhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 2HPY "Crystallographic Model Of Lumirhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 2I35 "Crystal Structure Of Rhombohedral Crystal Form Of Ground-State Rhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 2I36 "Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 2I37 "Crystal Structure Of A Photoactivated Rhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 2J4Y "Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells" 100.00 349 99.43 99.43 0.00e+00 PDB 2PED "Crystallographic Model Of 9-Cis-Rhodopsin" 100.00 349 100.00 100.00 0.00e+00 PDB 2X72 "Crystal Structure Of The Constitutively Active E113q,N2c, D282c Rhodopsin Mutant With Bound Galphact Peptide" 100.00 349 99.14 99.43 0.00e+00 PDB 3C9L "Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form" 100.00 348 100.00 100.00 0.00e+00 PDB 3C9M "Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form" 100.00 348 99.43 99.43 0.00e+00 PDB 3CAP "Crystal Structure Of Native Opsin: The G Protein-Coupled Receptor Rhodopsin In Its Ligand-Free State" 100.00 348 100.00 100.00 0.00e+00 PDB 3DQB "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With A C-terminal Peptide Derived From The Galpha S" 100.00 348 100.00 100.00 0.00e+00 PDB 3OAX "Crystal Structure Of Bovine Rhodopsin With Beta-Ionone" 100.00 349 100.00 100.00 0.00e+00 PDB 3PQR "Crystal Structure Of Metarhodopsin Ii In Complex With A C-Terminal Peptide Derived From The Galpha Subunit Of Transducin" 100.00 348 100.00 100.00 0.00e+00 PDB 3PXO "Crystal Structure Of Metarhodopsin Ii" 100.00 348 100.00 100.00 0.00e+00 PDB 4A4M "Crystal Structure Of The Light-Activated Constitutively Active N2c,M257y,D282c Rhodopsin Mutant In Complex With A Peptide Resem" 100.00 349 99.14 99.14 0.00e+00 PDB 4BEY "Night Blindness Causing G90d Rhodopsin In Complex With Gact2 Peptide" 100.00 349 99.14 99.14 0.00e+00 PDB 4BEZ "Night Blindness Causing G90d Rhodopsin In The Active Conformation" 100.00 349 99.14 99.14 0.00e+00 PDB 4J4Q "Crystal Structure Of Active Conformation Of Gpcr Opsin Stabilized By Octylglucoside" 100.00 348 100.00 100.00 0.00e+00 PDB 4PXF "Crystal Structure Of The Active G-protein-coupled Receptor Opsin In Complex With The Finger-loop Peptide Derived From The Full-" 100.00 348 100.00 100.00 0.00e+00 DBJ BAB83621 "rhodopsin [synthetic construct]" 100.00 348 100.00 100.00 0.00e+00 GB AAA30674 "rhodopsin [Bos taurus]" 100.00 348 100.00 100.00 0.00e+00 GB AAA30675 "rhodopsin, partial [Bos taurus]" 98.56 343 99.71 99.71 0.00e+00 GB ELR51227 "Rhodopsin, partial [Bos mutus]" 100.00 351 99.43 99.71 0.00e+00 PRF 0811197A rhodopsin 100.00 347 99.71 99.71 0.00e+00 PRF 0901188A rhodopsin 100.00 348 100.00 100.00 0.00e+00 PRF 0901212A rhodopsin 100.00 348 100.00 100.00 0.00e+00 PRF 1001148A rhodopsin 100.00 348 100.00 100.00 0.00e+00 REF NP_001014890 "rhodopsin [Bos taurus]" 100.00 348 100.00 100.00 0.00e+00 REF XP_004018583 "PREDICTED: rhodopsin [Ovis aries]" 100.00 348 97.41 98.56 0.00e+00 REF XP_005902896 "PREDICTED: rhodopsin [Bos mutus]" 100.00 348 99.43 99.71 0.00e+00 REF XP_006078962 "PREDICTED: rhodopsin [Bubalus bubalis]" 100.00 348 98.85 99.14 0.00e+00 REF XP_010860750 "PREDICTED: rhodopsin [Bison bison bison]" 100.00 348 99.43 100.00 0.00e+00 SP P02699 "RecName: Full=Rhodopsin [Bos taurus]" 100.00 348 100.00 100.00 0.00e+00 TPG DAA16827 "TPA: rhodopsin [Bos taurus]" 100.00 348 100.00 100.00 0.00e+00 stop_ save_ save_rhodopsin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common rhodopsin _Name_variant rhodopsin _Molecular_mass . _Mol_thiol_state 'not reported' _Details . _Residue_count 348 _Mol_residue_sequence ; MNGTEGPNFYVPFSNKTGVV RSPFEAPQYYLAEPWQFSML AAYMFLLIMLGFPINFLTLY VTVQHKKLRTPLNYILLNLA VADLFMVFGGFTTTLYTSLH GYFVFGPTGCNLEGFFATLG GEIALWSLVVLAIERYVVVC KPMSNFRFGENHAIMGVAFT WVMALACAAPPLVGWSRYIP EGMQCSCGIDYYTPHEETNN ESFVIYMFVVHFIIPLIVIF FCYGQLVFTVKEAAAQQQES ATTQKAEKEVTRMVIIMVIA FLICWLPYAGVAFYIFTHQG SDFGPIFMTIPAFFAKTSAV YNPVIYIMMNKQFRNCMVTT LCCGKNPLGDDEASTTVSKT ETSQVAPA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASN 3 GLY 4 THR 5 GLU 6 GLY 7 PRO 8 ASN 9 PHE 10 TYR 11 VAL 12 PRO 13 PHE 14 SER 15 ASN 16 LYS 17 THR 18 GLY 19 VAL 20 VAL 21 ARG 22 SER 23 PRO 24 PHE 25 GLU 26 ALA 27 PRO 28 GLN 29 TYR 30 TYR 31 LEU 32 ALA 33 GLU 34 PRO 35 TRP 36 GLN 37 PHE 38 SER 39 MET 40 LEU 41 ALA 42 ALA 43 TYR 44 MET 45 PHE 46 LEU 47 LEU 48 ILE 49 MET 50 LEU 51 GLY 52 PHE 53 PRO 54 ILE 55 ASN 56 PHE 57 LEU 58 THR 59 LEU 60 TYR 61 VAL 62 THR 63 VAL 64 GLN 65 HIS 66 LYS 67 LYS 68 LEU 69 ARG 70 THR 71 PRO 72 LEU 73 ASN 74 TYR 75 ILE 76 LEU 77 LEU 78 ASN 79 LEU 80 ALA 81 VAL 82 ALA 83 ASP 84 LEU 85 PHE 86 MET 87 VAL 88 PHE 89 GLY 90 GLY 91 PHE 92 THR 93 THR 94 THR 95 LEU 96 TYR 97 THR 98 SER 99 LEU 100 HIS 101 GLY 102 TYR 103 PHE 104 VAL 105 PHE 106 GLY 107 PRO 108 THR 109 GLY 110 CYS 111 ASN 112 LEU 113 GLU 114 GLY 115 PHE 116 PHE 117 ALA 118 THR 119 LEU 120 GLY 121 GLY 122 GLU 123 ILE 124 ALA 125 LEU 126 TRP 127 SER 128 LEU 129 VAL 130 VAL 131 LEU 132 ALA 133 ILE 134 GLU 135 ARG 136 TYR 137 VAL 138 VAL 139 VAL 140 CYS 141 LYS 142 PRO 143 MET 144 SER 145 ASN 146 PHE 147 ARG 148 PHE 149 GLY 150 GLU 151 ASN 152 HIS 153 ALA 154 ILE 155 MET 156 GLY 157 VAL 158 ALA 159 PHE 160 THR 161 TRP 162 VAL 163 MET 164 ALA 165 LEU 166 ALA 167 CYS 168 ALA 169 ALA 170 PRO 171 PRO 172 LEU 173 VAL 174 GLY 175 TRP 176 SER 177 ARG 178 TYR 179 ILE 180 PRO 181 GLU 182 GLY 183 MET 184 GLN 185 CYS 186 SER 187 CYS 188 GLY 189 ILE 190 ASP 191 TYR 192 TYR 193 THR 194 PRO 195 HIS 196 GLU 197 GLU 198 THR 199 ASN 200 ASN 201 GLU 202 SER 203 PHE 204 VAL 205 ILE 206 TYR 207 MET 208 PHE 209 VAL 210 VAL 211 HIS 212 PHE 213 ILE 214 ILE 215 PRO 216 LEU 217 ILE 218 VAL 219 ILE 220 PHE 221 PHE 222 CYS 223 TYR 224 GLY 225 GLN 226 LEU 227 VAL 228 PHE 229 THR 230 VAL 231 LYS 232 GLU 233 ALA 234 ALA 235 ALA 236 GLN 237 GLN 238 GLN 239 GLU 240 SER 241 ALA 242 THR 243 THR 244 GLN 245 LYS 246 ALA 247 GLU 248 LYS 249 GLU 250 VAL 251 THR 252 ARG 253 MET 254 VAL 255 ILE 256 ILE 257 MET 258 VAL 259 ILE 260 ALA 261 PHE 262 LEU 263 ILE 264 CYS 265 TRP 266 LEU 267 PRO 268 TYR 269 ALA 270 GLY 271 VAL 272 ALA 273 PHE 274 TYR 275 ILE 276 PHE 277 THR 278 HIS 279 GLN 280 GLY 281 SER 282 ASP 283 PHE 284 GLY 285 PRO 286 ILE 287 PHE 288 MET 289 THR 290 ILE 291 PRO 292 ALA 293 PHE 294 PHE 295 ALA 296 LYS 297 THR 298 SER 299 ALA 300 VAL 301 TYR 302 ASN 303 PRO 304 VAL 305 ILE 306 TYR 307 ILE 308 MET 309 MET 310 ASN 311 LYS 312 GLN 313 PHE 314 ARG 315 ASN 316 CYS 317 MET 318 VAL 319 THR 320 THR 321 LEU 322 CYS 323 CYS 324 GLY 325 LYS 326 ASN 327 PRO 328 LEU 329 GLY 330 ASP 331 ASP 332 GLU 333 ALA 334 SER 335 THR 336 THR 337 VAL 338 SER 339 LYS 340 THR 341 GLU 342 THR 343 SER 344 GLN 345 VAL 346 ALA 347 PRO 348 ALA stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 REF NP_001014890 'rhodopsin [Bos taurus]' 100.00 348 100.00 100.00 0.00e+00 SWISS-PROT P02699 Rhodopsin 100.00 348 100.00 100.00 0.00e+00 PRF 0901212A rhodopsin 100.00 348 100.00 100.00 0.00e+00 PRF 1001148A rhodopsin 100.00 348 100.00 100.00 0.00e+00 PRF 0811197A rhodopsin 100.00 347 99.71 99.71 0.00e+00 PRF 0901188A rhodopsin 100.00 348 100.00 100.00 0.00e+00 GenBank AAA30674 rhodopsin 100.00 348 100.00 100.00 0.00e+00 GenBank AAA30675 rhodopsin 98.56 343 99.71 99.71 0.00e+00 PDB 3CAP 'Crystal Structure Of Native Opsin: The G Protein-Coupled Receptor Rhodopsin In Its Ligand-Free State' 100.00 348 100.00 100.00 0.00e+00 DBJ BAB83621 'rhodopsin [synthetic construct]' 100.00 348 100.00 100.00 0.00e+00 PDB 3C9L 'Structure Of Ground-State Bovine Rhodospin In A Hexagonal Crystal Form' 100.00 348 100.00 100.00 0.00e+00 PDB 3C9M 'Structure Of A Mutant Bovine Rhodopsin In Hexagonal Crystal Form' 100.00 348 99.43 99.43 0.00e+00 PDB 2J4Y 'Crystal Structure Of A Rhodopsin Stabilizing Mutant Expressed In Mammalian Cells' 99.43 348 99.42 99.42 0.00e+00 PDB 2PED 'Crystallographic Model Of 9-Cis-Rhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 2I36 'Crystal Structure Of Trigonal Crystal Form Of Ground-State Rhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 2I37 'Crystal Structure Of A Photoactivated Rhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 2HPY 'Crystallographic Model Of Lumirhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 2I35 'Crystal Structure Of Rhombohedral Crystal Form Of Ground- State Rhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 1U19 'Crystal Structure Of Bovine Rhodopsin At 2.2 Angstroms Resolution' 100.00 348 100.00 100.00 0.00e+00 PDB 2G87 'Crystallographic Model Of Bathorhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 1L9H 'Crystal Structure Of Bovine Rhodopsin At 2.6 Angstroms Resolution' 100.00 348 100.00 100.00 0.00e+00 PDB 1LN6 'Structure Of Bovine Rhodopsin (Metarhodopsin Ii)' 100.00 348 100.00 100.00 0.00e+00 PDB 1HZX 'Crystal Structure Of Bovine Rhodopsin' 100.00 348 100.00 100.00 0.00e+00 PDB 1JFP 'Structure Of Bovine Rhodopsin (Dark Adapted)' 100.00 348 100.00 100.00 0.00e+00 PDB 1F88 'Crystal Structure Of Bovine Rhodopsin' 99.71 348 100.00 100.00 0.00e+00 PDB 1GZM 'Structure Of Bovine Rhodopsin In A Trigonal Crystal Form' 100.00 348 100.00 100.00 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue $S2 cow 9913 Eukaryota Metazoa Bos taurus eye retina stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $S2 'recombinant technology' 'E. coli' Escherichia coli . plasmid GEV-S2 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type emulsion _Details ; sample contains individual, intact rhodopsin rich disk membranes isolated from the rod outer segment of bovine retina; S2 peptide is in fast exchange between a free form in solution and a rhodopsin bound form ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $S2 2.6 mM '[U-15N; U-13C]' $rhodopsin 0.063 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $S2 2.6 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'raw spectral data processing' 'peak picking' stop_ _Details 'Delaglio, F. et al. (1995) J. Biomol. NMR 6(3), 277-293' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label . save_ save_2D_1H-1H_TOCSY_(15N_separated)_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY (15N separated)' _Sample_label . save_ save_2D_1H-15N_HSQC_(w/o_1H_decoupling)_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC (w/o 1H decoupling)' _Sample_label . save_ save_2D_1H-13C_CT-HSQC_(w/o_1H_decoupling)_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C CT-HSQC (w/o 1H decoupling)' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY (15N separated)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC (w/o 1H decoupling)' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C CT-HSQC (w/o 1H decoupling)' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details ; sample was studied in dark adapted state and after photo activation of rhodopsin by illuminating the sample for 60s with a focussed microscope light, chemical shifts of S2 are identical in both states, TrNOEs and TrDCs are difference values between the dark and light-activated states ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.2 na temperature 283 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_S2_shift_set _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY (15N separated)' '2D 1H-15N HSQC (w/o 1H decoupling)' '2D 1H-13C CT-HSQC (w/o 1H decoupling)' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'S2 peptide' _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 . 1 ILE HA H 3.86 . 1 2 . 1 ILE HB H 1.95 . 1 3 . 1 ILE HG12 H 1.47 . 2 4 . 1 ILE HG13 H 1.21 . 2 5 . 1 ILE HG2 H 0.99 . 1 6 . 1 ILE HD1 H 0.92 . 1 7 . 1 ILE CA C 60.5 . 1 8 . 1 ILE CB C 39.3 . 1 9 . 1 ILE CG1 C 26.7 . 1 10 . 1 ILE CG2 C 16.9 . 1 11 . 1 ILE CD1 C 13.3 . 1 12 . 2 ARG HA H 4.32 . 1 13 . 2 ARG HB2 H 1.86 . 2 14 . 2 ARG HB3 H 1.79 . 2 15 . 2 ARG HG2 H 1.63 . 1 16 . 2 ARG HG3 H 1.63 . 1 17 . 2 ARG HD2 H 3.20 . 1 18 . 2 ARG HD3 H 3.20 . 1 19 . 2 ARG CA C 56.4 . 1 20 . 2 ARG CB C 30.4 . 1 21 . 2 ARG CG C 27.2 . 1 22 . 2 ARG CD C 43.3 . 1 23 . 3 GLU H H 8.76 . 1 24 . 3 GLU HA H 4.23 . 1 25 . 3 GLU HB2 H 2.00 . 2 26 . 3 GLU HB3 H 1.92 . 2 27 . 3 GLU HG2 H 2.26 . 1 28 . 3 GLU HG3 H 2.26 . 1 29 . 3 GLU CA C 56.9 . 1 30 . 3 GLU CB C 30.4 . 1 31 . 3 GLU CG C 36.3 . 1 32 . 3 GLU N N 123.4 . 1 33 . 4 ASN H H 8.65 . 1 34 . 4 ASN HA H 4.67 . 1 35 . 4 ASN HB2 H 2.85 . 2 36 . 4 ASN HB3 H 2.75 . 2 37 . 4 ASN HD21 H 7.68 . 2 38 . 4 ASN HD22 H 6.97 . 2 39 . 4 ASN CA C 53.1 . 1 40 . 4 ASN CB C 38.6 . 1 41 . 4 ASN N N 119.7 . 1 42 . 4 ASN ND2 N 113.2 . 1 43 . 5 LEU H H 8.35 . 1 44 . 5 LEU HA H 4.31 . 1 45 . 5 LEU HB2 H 1.65 . 2 46 . 5 LEU HB3 H 1.59 . 2 47 . 5 LEU HG H 1.60 . 1 48 . 5 LEU HD1 H 0.92 . 1 49 . 5 LEU HD2 H 0.86 . 1 50 . 5 LEU CA C 55.4 . 1 51 . 5 LEU CB C 42.2 . 1 52 . 5 LEU CG C 27.0 . 1 53 . 5 LEU CD1 C 25.0 . 1 54 . 5 LEU CD2 C 23.2 . 1 55 . 5 LEU N N 122.9 . 1 56 . 6 LYS H H 8.36 . 1 57 . 6 LYS HA H 4.27 . 1 58 . 6 LYS HB2 H 1.82 . 2 59 . 6 LYS HB3 H 1.78 . 2 60 . 6 LYS HG2 H 1.43 . 2 61 . 6 LYS HG3 H 1.39 . 2 62 . 6 LYS HD2 H 1.66 . 1 63 . 6 LYS HD3 H 1.66 . 1 64 . 6 LYS HE2 H 2.97 . 1 65 . 6 LYS HE3 H 2.97 . 1 66 . 6 LYS CA C 56.7 . 1 67 . 6 LYS CB C 32.9 . 1 68 . 6 LYS CG C 24.7 . 1 69 . 6 LYS CD C 29.1 . 1 70 . 6 LYS CE C 42.1 . 1 71 . 6 LYS N N 121.8 . 1 72 . 7 ASP H H 8.36 . 1 73 . 7 ASP HA H 4.61 . 1 74 . 7 ASP HB2 H 2.75 . 2 75 . 7 ASP HB3 H 2.66 . 2 76 . 7 ASP CA C 54.5 . 1 77 . 7 ASP CB C 41.1 . 1 78 . 7 ASP N N 121.4 . 1 79 . 8 SER H H 8.31 . 1 80 . 8 SER HA H 4.37 . 1 81 . 8 SER HB2 H 3.93 . 2 82 . 8 SER HB3 H 3.89 . 2 83 . 8 SER CA C 58.9 . 1 84 . 8 SER CB C 63.8 . 1 85 . 8 SER N N 116.3 . 1 86 . 9 GLY H H 8.53 . 1 87 . 9 GLY HA2 H 3.93 . 1 88 . 9 GLY HA3 H 3.93 . 1 89 . 9 GLY CA C 45.4 . 1 90 . 9 GLY N N 110.8 . 1 91 . 10 LEU H H 7.94 . 1 92 . 10 LEU HA H 4.30 . 1 93 . 10 LEU HB2 H 1.50 . 2 94 . 10 LEU HB3 H 1.44 . 2 95 . 10 LEU HG H 1.50 . 1 96 . 10 LEU HD1 H 0.88 . 1 97 . 10 LEU HD2 H 0.81 . 1 98 . 10 LEU CA C 55.0 . 1 99 . 10 LEU CB C 42.4 . 1 100 . 10 LEU CG C 26.8 . 1 101 . 10 LEU CD1 C 25.0 . 1 102 . 10 LEU CD2 C 23.1 . 1 103 . 10 LEU N N 121.4 . 1 104 . 11 PHE H H 7.71 . 1 105 . 11 PHE HA H 4.43 . 1 106 . 11 PHE HB2 H 3.17 . 2 107 . 11 PHE HB3 H 2.94 . 2 108 . 11 PHE HD1 H 7.22 . 1 109 . 11 PHE HD2 H 7.22 . 1 110 . 11 PHE HE1 H 7.33 . 1 111 . 11 PHE HE2 H 7.33 . 1 112 . 11 PHE HZ H 7.27 . 1 113 . 11 PHE CA C 58.9 . 1 114 . 11 PHE CB C 40.4 . 1 115 . 11 PHE N N 124.9 . 1 stop_ save_