Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Averaged Minimized Structure
NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: Implications for KaiA-KaiC interaction
AMARMSPADKRKLLDELRSIYRTIVLEYFNTDAKVNERIDEFVSKAFFADISVSQVLEIHVELMDTFSKQLKLEGRSEDI LLDYRLTLIDVIAHLCEMYRRSIPREV
1H, 13C and 15N backbone and sidechain chemical shifts for the oxidized form of this protein
1H, 13C and 15N backbone and sidechain chemical shifts for the reduced form of this protein
This is the oxidized form of the protein. A disulfide bond connects residue C96 of each monomeric unit.
The structure is based on 2207 restraints of which 1740 are NOE restraints.
Distance geometry, Simulated Annealing, Radius-of-gyration, Carbon chemical shift and conformational database potential refinement
1.3 mM ThKaiA180C U-15N, 20 mM NaCl, 20 mM phosphate buffer, 95% H2O, 5% D2O
1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer, 95% H2O, 5% D2O
1.3 mM ThKaiA180C U-15N,U-13C, 20 mM NaCl, 20 mM phosphate buffer, 100% D2O
1 mM ThKaiA180C U-15N,U-13C, 1 mM ThKaiA180C NA-N,NA-C, 20 mM NaCl, 20 mM phosphate buffer, 100% D2O
All alpha-helix protein, Homodimer, Circadian Clock Protein
RMSPADKRKLLDELRSIYRTIVLEYFNTDAKVNERIDEFVSKAFFADISVSQVLEIHVELMDTFSKQLKLEGRSEDILLD YRLTLIDVIAHLCEMYRRSIPREV