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- PDB-1q6b: Solution Structure of the C-terminal Domain of Thermosynechococcu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1q6b | ||||||
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Title | Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Ensemble of 25 Structures | ||||||
![]() | Circadian clock protein KaiA homolog![]() | ||||||
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Function / homology | ![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Vakonakis, I. / Sun, J. / Golden, S.S. / Holzenburg, A. / LiWang, A.C. | ||||||
![]() | ![]() Title: NMR structure of the KaiC-interacting C-terminal domain of KaiA, a circadian clock protein: implications for KaiA-KaiC interaction Authors: Vakonakis, I. / Sun, J. / Wu, T. / Holzenburg, A. / Golden, S.S. / LiWang, A.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.7 MB | Display | ![]() |
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PDB format | ![]() | 1.5 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1q6aC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | ![]() Mass: 12601.585 Da / Num. of mol.: 2 / Fragment: C-terminal domain (ThKaiA180C) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Strain: BP-1 / Gene: KaiA / Plasmid: pET-32a / Species (production host): Escherichia coli / Production host: ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This is the oxidized form of the protein. A disulfide bond connects residue C96 of each monomeric unit. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 20 mM NaCl, 20 mM NaPi / pH: 7.0 / Pressure: ambient / Temperature: 323 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: Distance geometry, Simulating annealing, Radius-of-gyration, Carbon chemical shift, conformational database potential refinement Software ordinal: 1 Details: The structure is based on 2207 restraints per monomeric unit of which 1740 are NOE restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 25 |