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Yorodumi- PDB-1q6a: Solution Structure of the C-terminal Domain of Thermosynechococcu... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1q6a | ||||||
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Title | Solution Structure of the C-terminal Domain of Thermosynechococcus elongatus KaiA (ThKaiA180C); Averaged Minimized Structure | ||||||
Components | Circadian clock protein KaiA homolog | ||||||
Keywords | CIRCADIAN CLOCK PROTEIN / All alpha-helix protein / Homodimer | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Thermosynechococcus elongatus (bacteria) | ||||||
Method | SOLUTION NMR / Distance geometry, Simulated Annealing, Radius-of-gyration, Carbon chemical shift, conformational database potential refinement | ||||||
Model type details | minimized average | ||||||
Authors | Vakonakis, I. / Sun, J. / Holzenburg, A. / Golden, S.S. / LiWang, A.C. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1q6a.cif.gz | 84.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1q6a.ent.gz | 70.8 KB | Display | PDB format |
PDBx/mmJSON format | 1q6a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1q6a_validation.pdf.gz | 340.8 KB | Display | wwPDB validaton report |
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Full document | 1q6a_full_validation.pdf.gz | 360.1 KB | Display | |
Data in XML | 1q6a_validation.xml.gz | 8.3 KB | Display | |
Data in CIF | 1q6a_validation.cif.gz | 10.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q6/1q6a ftp://data.pdbj.org/pub/pdb/validation_reports/q6/1q6a | HTTPS FTP |
-Related structure data
Related structure data | 1q6bC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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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.) Thermosynechococcus elongatus (bacteria) Strain: BP-1 / Gene: KaiA / Plasmid: pET-32a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q8RR35, UniProt: Q79V62*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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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. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 20 mM NaCl, 20 mM NaPi / pH: 7 / Pressure: ambient / Temperature: 323 K | |||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-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, Simulated Annealing, Radius-of-gyration, Carbon chemical shift, conformational database potential refinement Software ordinal: 1 Details: The structure is based on 2207 restraints of which 1740 are NOE restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |