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- PDB-1sv1: NMR structure of the ThKaiA180C-CIIABD complex (25-structure ensemble) -
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Open data
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Basic information
Entry | Database: PDB / ID: 1sv1 | ||||||
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Title | NMR structure of the ThKaiA180C-CIIABD complex (25-structure ensemble) | ||||||
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![]() | CIRCADIAN CLOCK PROTEIN / X-class Four Helix Bundle / Protein-peptide complex | ||||||
Function / homology | ![]() protein serine/threonine/tyrosine kinase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / regulation of circadian rhythm / circadian rhythm / kinase activity / protein autophosphorylation / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / regulation of DNA-templated transcription ...protein serine/threonine/tyrosine kinase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / regulation of circadian rhythm / circadian rhythm / kinase activity / protein autophosphorylation / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / regulation of DNA-templated transcription / magnesium ion binding / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / Distance geometry, Simulated annealing | ||||||
![]() | Vakonakis, I. / LiWang, A.C. | ||||||
![]() | ![]() Title: Structure of the C-terminal domain of the clock protein KaiA in complex with a KaiC-derived peptide: implications for KaiC regulation. Authors: Vakonakis, I. / 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 | ![]() | 2.2 MB | Display | ![]() |
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PDB format | ![]() | 1.9 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 373.9 KB | Display | ![]() |
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Full document | ![]() | 1018.4 KB | Display | |
Data in XML | ![]() | 194.4 KB | Display | |
Data in CIF | ![]() | 253.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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 residues 180-283 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: BP-1 / Gene: KaiA / Plasmid: pET32a+ / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Protein/peptide | Mass: 3623.117 Da / Num. of mol.: 2 / Fragment: C-terminal residues 488-518 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: BP-1 / Gene: KaiC / Plasmid: pET32a+ / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Assignments of ThKaiA180C and CIIABD were performed through CBCA(CO)NH, CBCANH, HBHA(CO)NH and HC(C)H-COSY experiments. |
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Sample preparation
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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, Simulated annealing / Software ordinal: 1 Details: The structure is based on 2420 total restraints: 1858 are NOE derived, 58 are from hydrogen bonds, 244 are dihedral angles and 260 are 13C chemical shifts. | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: lowest energy structures that satisfy all experimental restraints Conformers calculated total number: 50 / Conformers submitted total number: 25 |