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Yorodumi- PDB-2eel: Solution structure of the CIDE-N domain of human cell death activ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2eel | ||||||
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Title | Solution structure of the CIDE-N domain of human cell death activator CIDE-A | ||||||
Components | Cell death activator CIDE-A | ||||||
Keywords | APOPTOSIS / CIDE-N domain / Cell death activator CIDE-A / Cell death-inducing DFFA-like effector A / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information Lipid particle organization / lipid droplet fusion / positive regulation of sequestering of triglyceride / response to stilbenoid / regulation of apoptotic DNA fragmentation / lipid transfer activity / lipid storage / phosphatidic acid binding / negative regulation of execution phase of apoptosis / mitochondrial envelope ...Lipid particle organization / lipid droplet fusion / positive regulation of sequestering of triglyceride / response to stilbenoid / regulation of apoptotic DNA fragmentation / lipid transfer activity / lipid storage / phosphatidic acid binding / negative regulation of execution phase of apoptosis / mitochondrial envelope / negative regulation of cold-induced thermogenesis / cellular response to cold / negative regulation of cytokine production / temperature homeostasis / negative regulation of tumor necrosis factor production / negative regulation of lipid catabolic process / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / lipid droplet / negative regulation of transforming growth factor beta receptor signaling pathway / lipid metabolic process / regulation of apoptotic process / apoptotic process / protein homodimerization activity / mitochondrion / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Qin, X.R. / Nagashima, T. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be published Title: Solution structure of the CIDE-N domain of human cell death activator CIDE-A Authors: Qin, X.R. / Nagashima, T. / Hayashi, F. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eel.cif.gz | 520.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eel.ent.gz | 436.8 KB | Display | PDB format |
PDBx/mmJSON format | 2eel.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2eel_validation.pdf.gz | 343.4 KB | Display | wwPDB validaton report |
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Full document | 2eel_full_validation.pdf.gz | 486.3 KB | Display | |
Data in XML | 2eel_validation.xml.gz | 31.5 KB | Display | |
Data in CIF | 2eel_validation.cif.gz | 49.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ee/2eel ftp://data.pdbj.org/pub/pdb/validation_reports/ee/2eel | HTTPS FTP |
-Related structure data
Similar structure data | |
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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: 9733.857 Da / Num. of mol.: 1 / Fragment: CIDE-N domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: cell free protein synthesis / Gene: CIDEA / Plasmid: P050613-03 / References: UniProt: O60543 |
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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: 1.10mM 13C,15N-labeled protein; 20mM d-Tris-HCl(pH7.0); 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: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / 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 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 |