- PDB-1m2e: Solution structure of the N-terminal domain of Synechococcus elon... -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1m2e
Title
Solution structure of the N-terminal domain of Synechococcus elongatus KaiA (KaiA135N); Average minimized structure.
Components
KaiA
Keywords
CIRCADIAN CLOCK PROTEIN / ALPHA-BETA-ALPHA SANDWICH
Function / homology
Function and homology information
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
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.) Synechococcus elongatus (bacteria) / Gene: kaiA / Plasmid: pET32a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q79PF6
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
HNHA
1
2
2
4D 13C/15N-separated NOESY
1
3
3
4D 13C-separated NOESY
1
4
1
HNHB
1
5
3
HAHB
1
6
3
BRCTCO/BRCTCN
NMR details
Text: Submission corresponds to the average minimized structure based on a 25-low-energy-structures family. The 1H, 15N and 13C chemical shifts of KaiA135N are deposited at the BMRB database (http: ...Text: Submission corresponds to the average minimized structure based on a 25-low-energy-structures family. 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.
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 are dihedral angle restraints and 31 are distance restraints from hydrogen bonds
NMR ensemble
Conformers submitted total number: 1
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