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

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Entry
Database: PDB / ID: 1ezy
TitleHIGH-RESOLUTION SOLUTION STRUCTURE OF FREE RGS4 BY NMR
ComponentsREGULATOR OF G-PROTEIN SIGNALING 4
KeywordsSIGNALING PROTEIN INHIBITOR / 4-helix bundle / free RGS4 NMR Structure
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 / regulation of actin filament organization / regulation of potassium ion transmembrane transport / G alpha (q) signalling events / G alpha (i) signalling events / negative regulation of G protein-coupled receptor signaling pathway ...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 / regulation of actin filament organization / regulation of potassium ion transmembrane transport / G alpha (q) signalling events / G alpha (i) signalling events / negative regulation of G protein-coupled receptor signaling pathway / 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 domain / RGS domain profile. / Regulator of G protein signalling domain ...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 domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 / 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 12, 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
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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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
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 100structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function
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 DOMAIN OF RGS
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
2123D 13C-separated NOESY
3233D 13C-separated NOESY
333HNHA

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Sample preparation

Details
Solution-IDContentsSolvent system
11mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.090% H2O/10% D2O
21mM RGS4 U-15N,13C; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.0100% D2O
31mM RGS4 U-15N; 50mM phosphate buffer, 2 mM NaN3, 50 mM deuterated DTT, pH 6.090% H2O/10% D2O
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
XwinNMR2Brukercollection
PIPP4.8.2Garrettdata analysis
X-PLOR3.84Brungerrefinement
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
Details: the structures are based on a total of 2871 restraints, 3167 are NOE-derived distance constraints, 431 dihedral angle restraints,78 distance restraints from 39 backbone hydrogen bond, 132 ...Details: the structures are based on a total of 2871 restraints, 3167 are NOE-derived distance constraints, 431 dihedral angle restraints,78 distance restraints from 39 backbone hydrogen bond, 132 3JHNa restraints, 136 Ca and 134 Cb chemical shift restraints and the use of a conformational database target function.
NMR ensembleConformer selection criteria: structures with acceptable covalent geometry,structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function
Conformers calculated total number: 100 / Conformers submitted total number: 30

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