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Yorodumi- PDB-1n3k: Solution structure of phosphoprotein enriched in astrocytes 15 kD... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1n3k | ||||||
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Title | Solution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15) | ||||||
Components | Astrocytic phosphoprotein PEA-15 | ||||||
Keywords | APOPTOSIS / DEATH EFFECTOR DOMAIN / SIX HELIX BUNDLE | ||||||
Function / homology | Function and homology information positive regulation of extrinsic apoptotic signaling pathway via death domain receptors / : / negative regulation of glucose import / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / MAPK cascade / apoptotic process / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Cricetulus griseus (Chinese hamster) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Hill, J.M. / Vaidyanathan, H. / Ramos, J.W. / Ginsberg, M.H. / Werner, M.H. | ||||||
Citation | Journal: Embo J. / Year: 2002 Title: Recognition of ERK MAP Kinase by PEA-15 Reveals a Common Docking Site Within the Death Domain and Death Effector Domain Authors: Hill, J.M. / Vaidyanathan, H. / Ramos, J.W. / Ginsberg, M.H. / Werner, M.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1n3k.cif.gz | 843.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1n3k.ent.gz | 722 KB | Display | PDB format |
PDBx/mmJSON format | 1n3k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1n3k_validation.pdf.gz | 347.7 KB | Display | wwPDB validaton report |
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Full document | 1n3k_full_validation.pdf.gz | 485.7 KB | Display | |
Data in XML | 1n3k_validation.xml.gz | 59.7 KB | Display | |
Data in CIF | 1n3k_validation.cif.gz | 77.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n3/1n3k ftp://data.pdbj.org/pub/pdb/validation_reports/n3/1n3k | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 15061.084 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Cricetulus griseus (Chinese hamster) / Gene: PEA15 / Plasmid: pQE-9 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9Z297 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: VARIOUS DOUBLE AND TRIPLE RESONANCE EXPERIMENTS |
-Sample preparation
Details | Contents: 1mM protein U-15N,13C Solvent system: 10mM sodium phosphate buffer, 1mM DTT, 50uM NaN3 |
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Sample conditions | Ionic strength: 10mM phosphate buffer / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 2937 NMR-derived restraints, including 2522 NOEs, 308 dihedral angle restraints (121 phi, 95 psi, 84 chi1 and 8 chi2) and 107 3J(NH-Ha) coupling constants | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |