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Yorodumi- PDB-1suy: NMR structure of the ThKaiA180C-CIIABD complex (average minimized... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1suy | ||||||
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Title | NMR structure of the ThKaiA180C-CIIABD complex (average minimized structure) | ||||||
Components |
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Keywords | CIRCADIAN CLOCK PROTEIN / X-class Four Helix Bundle / Protein-peptide complex | ||||||
Function / homology | Function and homology information 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 | Thermosynechococcus elongatus (bacteria) | ||||||
Method | SOLUTION NMR / Distance geometry, Simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Vakonakis, I. / LiWang, A.C. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2004 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1suy.cif.gz | 108.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1suy.ent.gz | 90.7 KB | Display | PDB format |
PDBx/mmJSON format | 1suy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1suy_validation.pdf.gz | 344.9 KB | Display | wwPDB validaton report |
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Full document | 1suy_full_validation.pdf.gz | 393.5 KB | Display | |
Data in XML | 1suy_validation.xml.gz | 14 KB | Display | |
Data in CIF | 1suy_validation.cif.gz | 18.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/su/1suy ftp://data.pdbj.org/pub/pdb/validation_reports/su/1suy | HTTPS FTP |
-Related structure data
-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 residues 180-283 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermosynechococcus elongatus (bacteria) Strain: BP-1 / Gene: KaiA / Plasmid: pET32a+ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q79V62 #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.) Thermosynechococcus elongatus (bacteria) Strain: BP-1 / Gene: KaiC / Plasmid: pET32a+ / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q8RR33, UniProt: Q79V60*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: Assignments of ThKaiA180C and CIIABD were performed through CBCA(CO)NH, CBCANH, HBHA(CO)NH and HC(C)H-COSY experiments |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 20 mM NaCl, 20 mM NaPi / pH: 7 / 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 a total of 2420 restraints: 1858 are NOE-derived, 58 are from hydrogen bonds, 244 are dihedral angles and 260 are 13C chemical shifts. | ||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |