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- PDB-1m2f: Solution structure of the N-terminal domain of Synechococcus elon... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1m2f | ||||||
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Title | Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Family of 25 structures | ||||||
![]() | KaiA | ||||||
![]() | CIRCADIAN CLOCK PROTEIN / ALPHA-BETA-ALPHA SANDWICH | ||||||
Function / homology | ![]() detection of redox state / negative regulation of protein dephosphorylation / entrainment of circadian clock / positive regulation of circadian rhythm / circadian rhythm / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / Distance geometry, Simulated annealing regularization, Simulated annealing refinement | ||||||
![]() | Williams, S.B. / Vakonakis, I. / Golden, S.S. / LiWang, A.C. | ||||||
![]() | ![]() Title: Structure and Function from the Circadian Clock Protein KaiA of Synechococcus elongatus: A potential Clock Input Mechanism Authors: Williams, S.B. / Vakonakis, I. / 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 | ![]() | 1009 KB | Display | ![]() |
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PDB format | ![]() | 845.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 362 KB | Display | ![]() |
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Full document | ![]() | 620.1 KB | Display | |
Data in XML | ![]() | 104.7 KB | Display | |
Data in CIF | ![]() | 137.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1m2eC C: citing same article ( |
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Similar 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: 15077.117 Da / Num. of mol.: 1 / Fragment: N-terminal domain (Residues 1-135) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: Submission corresponds to family of 25-low-energy-structures. The 1H, 15N and 13C chemical shifts of KaiA135N are deposited at the BMRB database (http://www.bmrb.wisc.edu) under the accession number 5031. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 0.17 / pH: 7.0 / Pressure: ambient / Temperature: 298 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: Distance geometry, Simulated annealing regularization, Simulated annealing refinement Software ordinal: 1 Details: The structures are based on 2034 restraints: 1816 are NOE-derived distance constraints, 187 dihedral angle restraints, 31 distance restraints from hydrogen bonds | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 25 |