- PDB-1ezt: HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1ezt
Title
HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR
Components
REGULATOR OF G-PROTEIN SIGNALING 4
Keywords
SIGNALING PROTEIN INHIBITOR / 4-helix-bundle / free form of protein
Function / homology
Function and homology information
negative regulation of glycine import across plasma membrane / negative regulation of dopamine receptor signaling pathway / negative regulation of potassium ion transmembrane transport / dorsal root ganglion development / negative regulation of cell growth involved in cardiac muscle cell development / negative regulation of G protein-coupled receptor signaling pathway / regulation of actin filament organization / regulation of potassium ion transmembrane transport / G alpha (q) signalling events / G alpha (i) signalling events ...negative regulation of glycine import across plasma membrane / negative regulation of dopamine receptor signaling pathway / negative regulation of potassium ion transmembrane transport / dorsal root ganglion development / negative regulation of cell growth involved in cardiac muscle cell development / negative regulation of G protein-coupled receptor signaling pathway / regulation of actin filament organization / regulation of potassium ion transmembrane transport / G alpha (q) signalling events / G alpha (i) signalling events / positive regulation of heart rate / regulation of calcium ion transport / positive regulation of excitatory postsynaptic potential / G-protein alpha-subunit binding / response to amphetamine / GTPase activator activity / response to cocaine / response to ethanol / protein kinase binding / protein-containing complex / nucleus / cytoplasm Similarity search - Function
Regulator of G-protein signalling 4, RGS domain / Regulator of G-protein Signalling 4; domain 1 - #10 / Regulator of G-protein Signalling 4; domain 1 / RGS, subdomain 1/3 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS, subdomain 2 / RGS domain / RGS domain profile. ...Regulator of G-protein signalling 4, RGS domain / Regulator of G-protein Signalling 4; domain 1 - #10 / Regulator of G-protein Signalling 4; domain 1 / RGS, subdomain 1/3 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS, subdomain 2 / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS domain superfamily / Orthogonal Bundle / Mainly Alpha Similarity search - Domain/homology
Mass: 19145.711 Da / Num. of mol.: 1 / Fragment: CORE RGS DOMAIN Source method: isolated from a genetically manipulated source Details: SIX RESIDUE HISTIDINE TAG AT C-TERMINUS / Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Plasmid: PRGS4 / Production host: Escherichia coli (E. coli) / References: UniProt: P49799
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
2
3D 13C-separated NOESY
1
2
3
3D 15N-separated NOESY
1
3
3
HNHA
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Sample preparation
Details
Solution-ID
Contents
Solvent system
1
1 mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0
90% H2O/10% D2O
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1 mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0
100% D2O
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1 mM RGS4 U-15N; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0
90% H2O/10% D2O
Sample conditions
Ionic strength: 50 mM K / pH: 6.0 / Pressure: ambient / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR
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NMR measurement
NMR spectrometer
Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz
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Processing
NMR software
Name
Version
Developer
Classification
X-PLOR
3.84
Brunger
structuresolution
NMRPipe
1.7
Delaglio
processing
PIPP
4.2.8
Garrett
dataanalysis
XwinNMR
2
Bruker
collection
X-PLOR
3.84
Brunger
refinement
Refinement
Method: distance geometry simulated annealing / Software ordinal: 1 Details: The structure is based on a total of 2871 restraints, 1960 approximate interproton distance restraints, 78 distance restraints for 39 backbone hydrogen bonds, 431 torsion angle restraints, ...Details: The structure is based on a total of 2871 restraints, 1960 approximate interproton distance restraints, 78 distance restraints for 39 backbone hydrogen bonds, 431 torsion angle restraints, 132 3JHNa restraints, 136 Ca and 134 Cb chemical shift restraints. Structure also refined with conformational database target function.
NMR ensemble
Conformers submitted total number: 1
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