+Open data
-Basic information
Entry | Database: PDB / ID: 1tvj | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of chick cofilin | ||||||
Components | CofilinADF/Cofilin family | ||||||
Keywords | ACTIN-BINDING PROTEIN / cofilin / ADF / actin binding protein / actin depolymerizing factor | ||||||
Function / homology | Function and homology information actin filament fragmentation / actin filament severing / nuclear matrix / actin filament binding / actin cytoskeleton / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, simulated annealing | ||||||
Authors | Gorbatyuk, V.Y. / Nosworthy, N.J. / Robson, S.A. / Maciejewski, M.W. / dos Remedios, C.G. / King, G.F. | ||||||
Citation | Journal: To be Published Title: NMR Study of the Molecular Basis for Phosphoinositide Regulation of the Cofilin-Actin Interactions. Authors: Gorbatyuk, V.Y. / Nosworthy, N.J. / Robson, S.A. / Maciejewski, M.W. / dos Remedios, C.G. / King, G.F. #1: Journal: J.BIOMOL.NMR / Year: 2002 Title: Letter to the editor: backbone and side-chain 1H, 15N, and 13C assignments for chick cofilin Authors: Bains, N.P.S. / Gorbatyuk, V.Y. / Nosworthy, N.J. / Robson, S.A. / Maciejewski, M.W. / dos Remedios, C.G. / King, G.F. | ||||||
History |
| ||||||
Remark 700 | SHEET SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1tvj.cif.gz | 1 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1tvj.ent.gz | 893.9 KB | Display | PDB format |
PDBx/mmJSON format | 1tvj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tv/1tvj ftp://data.pdbj.org/pub/pdb/validation_reports/tv/1tvj | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 18690.598 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Production host: Escherichia coli (E. coli) / References: UniProt: P21566 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details |
| ||||||
---|---|---|---|---|---|---|---|
Sample conditions | Ionic strength: 0.06 / pH: 6.8 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: Structures with lowest energy, best covalent geometry, and least restraint violations Conformers calculated total number: 50 / Conformers submitted total number: 20 |