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Open data
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Basic information
Entry | Database: PDB / ID: 2af0 | ||||||
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Title | Structure of the Regulator of G-Protein Signaling Domain of RGS2 | ||||||
![]() | Regulator of G-protein signaling 2 | ||||||
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Function / homology | ![]() negative regulation of adenylate cyclase-inhibiting adrenergic receptor signaling pathway involved in heart process / negative regulation of phospholipase activity / negative regulation of glycine import across plasma membrane / adenylate cyclase inhibitor activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Papagrigoriou, E. / Johannson, C. / Phillips, C. / Smee, C. / Elkins, J.M. / Weigelt, J. / Arrowsmith, C. / Edwards, A. / Sundstrom, M. / Von Delft, F. ...Papagrigoriou, E. / Johannson, C. / Phillips, C. / Smee, C. / Elkins, J.M. / Weigelt, J. / Arrowsmith, C. / Edwards, A. / Sundstrom, M. / Von Delft, F. / Doyle, D.A. / 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 36.9 KB | Display | ![]() |
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PDB format | ![]() | 28 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 282.6 KB | Display | ![]() |
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Full document | ![]() | 283.6 KB | Display | |
Data in XML | ![]() | 7.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zv4C ![]() 2a72C ![]() 2bt2C ![]() 2bv1C ![]() 2es0C ![]() 2gtpC ![]() 2i59C ![]() 2ihbC ![]() 2ihdC ![]() 2ik8C ![]() 2jm5C ![]() 2jnuC ![]() 2odeC ![]() 2owiC 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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Unit cell |
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Components
#1: Protein | Mass: 16994.148 Da / Num. of mol.: 1 / Fragment: residues 71-203 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 37.9 % |
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: (NH4)2SO4, NaCl, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 10, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.3→36.9 Å / Num. all: 7531 / Num. obs: 7422 / % possible obs: 98.6 % |
Reflection shell | Resolution: 2.3→2.38 Å / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.407 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→33.69 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.359 Å / Total num. of bins used: 20
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