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- PDB-1ezt: HIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR -

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Basic information

Entry
Database: PDB / ID: 1ezt
TitleHIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR
ComponentsREGULATOR OF G-PROTEIN SIGNALING 4
KeywordsSIGNALING 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
Regulator of G-protein signaling 4
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / distance geometry simulated annealing
AuthorsMoy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Mason, K. / Semus, S. / Powers, R.
Citation
Journal: Biochemistry / Year: 2000
Title: NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha.
Authors: Moy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Mason, K. / Semus, S. / Powers, R.
#1: Journal: J.Biomol.NMR / Year: 1999
Title: 1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of RGS4
Authors: Moy, F.J. / Chanda, P.K. / Cockett, M.I. / Edris, W. / Jones, P.G. / Powers, R.
History
DepositionMay 11, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 15, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: REGULATOR OF G-PROTEIN SIGNALING 4


Theoretical massNumber of molelcules
Total (without water)19,1461
Polymers19,1461
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)1 / -
Representative

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Components

#1: Protein REGULATOR OF G-PROTEIN SIGNALING 4 / RGS4


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

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1123D 13C-separated NOESY
1233D 15N-separated NOESY
133HNHA

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Sample preparation

Details
Solution-IDContentsSolvent system
11 mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.090% H2O/10% D2O
21 mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0100% D2O
31 mM RGS4 U-15N; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.090% H2O/10% D2O
Sample conditionsIonic 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 spectrometerType: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.84Brungerstructure solution
NMRPipe1.7Delaglioprocessing
PIPP4.2.8Garrettdata analysis
XwinNMR2Brukercollection
X-PLOR3.84Brungerrefinement
RefinementMethod: 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 ensembleConformers submitted total number: 1

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