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- PDB-1n3k: Solution structure of phosphoprotein enriched in astrocytes 15 kD... -

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Basic information

Entry
Database: PDB / ID: 1n3k
TitleSolution structure of phosphoprotein enriched in astrocytes 15 kDa (PEA-15)
ComponentsAstrocytic phosphoprotein PEA-15
KeywordsAPOPTOSIS / 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 / carbohydrate transport / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / MAPK cascade / apoptotic process / nucleoplasm / cytosol
Similarity search - Function
Astrocytic phosphoprotein PEA-15, death effector domain / Death effector domain / Death effector domain / Death effector domain (DED) profile. / Death effector domain / Death Domain, Fas / Death Domain, Fas / Death-like domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Astrocytic phosphoprotein PEA-15
Similarity search - Component
Biological speciesCricetulus griseus (Chinese hamster)
MethodSOLUTION NMR / simulated annealing
AuthorsHill, J.M. / Vaidyanathan, H. / Ramos, J.W. / Ginsberg, M.H. / Werner, M.H.
CitationJournal: 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
DepositionOct 28, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 14, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Astrocytic phosphoprotein PEA-15


Theoretical massNumber of molelcules
Total (without water)15,0611
Polymers15,0611
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 50structures with the least restraint violations,structures with the lowest energy
Representative

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Components

#1: Protein Astrocytic phosphoprotein PEA-15 / PHOSPHOPROTEIN ENRICHED IN ASTROCYTES 15 kDa


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

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: VARIOUS DOUBLE AND TRIPLE RESONANCE EXPERIMENTS

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Sample preparation

DetailsContents: 1mM protein U-15N,13C
Solvent system: 10mM sodium phosphate buffer, 1mM DTT, 50uM NaN3
Sample conditionsIonic strength: 10mM phosphate buffer / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX5001
Bruker DMXBrukerDMX6002

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.843Brungerstructure solution
X-PLOR3.843Brungerrefinement
RefinementMethod: 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 ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 50 / Conformers submitted total number: 20

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