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Yorodumi- PDB-2e9i: Solution structure of the N-terminal extended 20th Filamin domain... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2e9i | ||||||
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Title | Solution structure of the N-terminal extended 20th Filamin domain from human Filamin-B | ||||||
Components | Filamin-B | ||||||
Keywords | STRUCTURAL PROTEIN / beta-sandwich / immunoglobulin-like fold / filamin / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information epithelial cell morphogenesis / keratinocyte development / brush border / phagocytic vesicle / stress fiber / skeletal muscle tissue development / cellular response to type II interferon / ISG15 antiviral mechanism / Z disc / actin filament binding ...epithelial cell morphogenesis / keratinocyte development / brush border / phagocytic vesicle / stress fiber / skeletal muscle tissue development / cellular response to type II interferon / ISG15 antiviral mechanism / Z disc / actin filament binding / actin cytoskeleton / actin binding / cell cortex / actin cytoskeleton organization / cadherin binding / focal adhesion / signal transduction / RNA binding / extracellular exosome / identical protein binding / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, restrained molecular dynamics | ||||||
Authors | Tomizawa, T. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the N-terminal extended 20th Filamin domain from human Filamin-B Authors: Tomizawa, T. / Koshiba, S. / Watanabe, S. / Harada, T. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2e9i.cif.gz | 600.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2e9i.ent.gz | 502.4 KB | Display | PDB format |
PDBx/mmJSON format | 2e9i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2e9i_validation.pdf.gz | 341.3 KB | Display | wwPDB validaton report |
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Full document | 2e9i_full_validation.pdf.gz | 487.1 KB | Display | |
Data in XML | 2e9i_validation.xml.gz | 33.8 KB | Display | |
Data in CIF | 2e9i_validation.cif.gz | 53.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e9/2e9i ftp://data.pdbj.org/pub/pdb/validation_reports/e9/2e9i | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11068.437 Da / Num. of mol.: 1 / Fragment: filamin domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: FLNB / Plasmid: P060515-02 / References: UniProt: O75369 |
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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: 1.53mM filamin domain U-15N, 13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE II / Manufacturer: Bruker / Model: AVANCE II / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, restrained molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |