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- PDB-1udm: Solution structure of Coactosin-like protein (Cofilin family) fro... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1udm | ||||||
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Title | Solution structure of Coactosin-like protein (Cofilin family) from Mus Musculus | ||||||
![]() | Coactosin-like protein | ||||||
![]() | PROTEIN BINDING / Actin binding protein / cytoskeletal / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | ![]() site of polarized growth / regulation of actin filament polymerization / cortical actin cytoskeleton / defense response to fungus / Neutrophil degranulation / actin filament / actin filament binding / actin binding / enzyme binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Goroncy, A.K. / Kigawa, T. / Koshiba, S. / Kobayashi, N. / Tochio, N. / Inoue, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: NMR solution structures of actin depolymerizing factor homology domains. Authors: Goroncy, A.K. / Koshiba, S. / Tochio, N. / Tomizawa, T. / Sato, M. / Inoue, M. / Watanabe, S. / Hayashizaki, Y. / Tanaka, A. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 884.9 KB | Display | ![]() |
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PDB format | ![]() | 740.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 342.5 KB | Display | ![]() |
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Full document | ![]() | 519.6 KB | Display | |
Data in XML | ![]() | 72.7 KB | Display | |
Data in CIF | ![]() | 89.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1v6fC ![]() 1wfsC ![]() 1x67C ![]() 2d8bC C: citing same article ( |
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Similar structure data | |
Other databases |
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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: 16538.457 Da / Num. of mol.: 1 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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Sample preparation
Details | Contents: 0.67mM COFILIN-ADF domain, 20mM phosphate buffer, 100mM NaCl, 0.02% NaN3 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest target function | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |