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Open data
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Basic information
Entry | Database: PDB / ID: 2owi | |||||||||
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Title | Solution structure of the RGS domain from human RGS18 | |||||||||
![]() | Regulator of G-protein signaling 18 | |||||||||
![]() | SIGNALING PROTEIN / STRUCTURAL GENOMICS / STRUCTURAL GENOMICS CONSORTIUM / SGC | |||||||||
Function / homology | ![]() regulation of G protein-coupled receptor signaling pathway / negative regulation of signal transduction / GTPase activator activity / G alpha (i) signalling events / G alpha (q) signalling events / G protein-coupled receptor signaling pathway / GTPase activity / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, MOLECULAR DYNAMICS | |||||||||
![]() | Higman, V.A. / Leidert, M. / Bray, J. / Elkins, J. / Soundararajan, M. / Doyle, D.A. / Gileadi, C. / Phillips, C. / Schoch, G. / Yang, X. ...Higman, V.A. / Leidert, M. / Bray, J. / Elkins, J. / Soundararajan, M. / Doyle, D.A. / Gileadi, C. / Phillips, C. / Schoch, G. / Yang, X. / Brockmann, C. / Schmieder, P. / Diehl, A. / Sundstrom, M. / Arrowsmith, C. / Weigelt, J. / Edwards, A. / Oschkinat, H. / Ball, L.J. / Structural Genomics Consortium (SGC) | |||||||||
![]() | ![]() Title: Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits. Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / ...Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / Doyle, D.A. / Siderovski, D.P. #1: ![]() Title: NMR Assignment of Human Rgs18 Authors: Higman, V.A. / Leidert, M. / Diehl, A. / Elkins, J. / Soundararajan, M. / Oschkinat, H. / Ball, L.J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 842.4 KB | Display | ![]() |
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PDB format | ![]() | 703.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 346 KB | Display | ![]() |
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Full document | ![]() | 471.2 KB | Display | |
Data in XML | ![]() | 38.6 KB | Display | |
Data in CIF | ![]() | 65.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zv4C ![]() 2a72C ![]() 2af0C ![]() 2bt2C ![]() 2bv1C ![]() 2es0C ![]() 2gtpC ![]() 2i59C ![]() 2ihbC ![]() 2ihdC ![]() 2ik8C ![]() 2jm5C ![]() 2jnuC ![]() 2odeC C: citing same article ( |
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Similar structure data | |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 17786.023 Da / Num. of mol.: 1 / Fragment: RGS DOMAIN, RESIDUES 75-223 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: BL21 (DE3) STRAIN ENRICHED WITH GENES THAT ENCODE RARE TRNAS Gene: RGS18, RGS13 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample conditions | pH: 6.0 / Pressure: AMBIENT / Temperature: 297 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
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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, MOLECULAR DYNAMICS / Software ordinal: 1 Details: NOE ASSIGNMENT WITH CYANA, REFINEMENT BY SIMULATED ANNEALING IN XPLOR-NIH USING NOE RESTRAINTS AND H-BOND RESTRAINTS FROM H/D EXCHANGE DATA. WATER REFINEMENT IN CNS. THE C-TERMINAL TAIL HAS ...Details: NOE ASSIGNMENT WITH CYANA, REFINEMENT BY SIMULATED ANNEALING IN XPLOR-NIH USING NOE RESTRAINTS AND H-BOND RESTRAINTS FROM H/D EXCHANGE DATA. WATER REFINEMENT IN CNS. THE C-TERMINAL TAIL HAS BEEN TRUNCATED PAST RESIDUE 134 BECAUSE OF FLEXIBILITY AND LACK OF STRUCTURE IN THIS REGION. THIS IS INDICATED (A) BY A LACK OF NOE RESTRAINTS PAST RESIDUE 132 AND (B) BY 15N T1, T2 AND HETERONCULEAR NOE EXPERIMENTS RESIDUE 131 ONWARDS. | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |