1Q6B | pdb_00001q6b

Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Ensemble of 25 Structures


SOLUTION NMR
NMR Experiment
ExperimentTypeSample ContentsSolventIonic StrengthpHPressureTemperature (K)Spectrometer
13D_15N-separated_NOESY1.3 mM ThKaiA180C U-15N, 20 mM NaCl, 20 mM phosphate buffer, 95% H2O, 5% D2O95% H2O/5% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
24D_13C-separated_NOESY1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer100% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
33D 13C-edited, 12C filtered NOESY1.0 mM ThKaiA180C U-15N,U-13C, 1.0 mM ThKaiA180C NA-N,Na-C, 20 mM NaCl, 20 mM phosphate buffer100% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
4HACAHB1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer100% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
5HNHB1.3 mM ThKaiA180C U-15N, 20 mM NaCl, 20 mM phosphate buffer, 95% H2O, 5% D2O95% H2O/5% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
6BRCTCO/CN1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer100% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
7CBCA(CO)NH1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer, 95% H2O, 5% D2O95% H2O/5% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
8CBCANH1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer, 95% H2O, 5% D2O95% H2O/5% D2O20 mM NaCl, 20 mM NaPi7.0ambient323
NMR Spectrometer Information
SpectrometerManufacturerModelField Strength
1VarianINOVA600
2VarianINOVA500
NMR Refinement
MethodDetailsSoftware
Distance geometry, Simulating annealing, Radius-of-gyration, Carbon chemical shift and conformational database potential refinementThe structure is based on 2207 restraints per monomeric unit of which 1740 are NOE restraints.NMRPipe
NMR Ensemble Information
Conformer Selection Criteriastructures with the least restraint violations
Conformers Calculated Total Number50
Conformers Submitted Total Number25
Representative Model13 (closest to the average)
Additional NMR Experimental Information
DetailsThis is the oxidized form of the protein. A disulfide bond connects residue C96 of each monomeric unit.
Computation: NMR Software
#ClassificationVersionSoftware NameAuthor
1processingNMRPipe2.1 Rev 2002.044.17.08Delaglio
2data analysisPIPP4.2.6Garrett
3structure solutionXPLOR-NIH2.9.1Clore
4collectionVNMR6.1 Rev. CVarian Assoc.
5refinementXPLOR-NIH2.9.1Clore