+Open data
-Basic information
Entry | Database: PDB / ID: 1zv4 | ||||||
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Title | Structure of the Regulator of G-Protein Signaling 17 (RGSZ2) | ||||||
Components | Regulator of G-protein signaling 17 | ||||||
Keywords | SIGNALING PROTEIN / Human RGSZ2 / Human RGS17(Z2) / regulator of G-protein signaling / mu-opioid receptor interacting protein / GTPase-activating proteins (GAP) / Regulator of Gz-selective protein signaling 2 / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | Function and homology information negative regulation of signal transduction / response to amphetamine / GTPase activator activity / G alpha (z) signalling events / G alpha (i) signalling events / G alpha (q) signalling events / neuron projection / G protein-coupled receptor signaling pathway / GTPase activity / synapse ...negative regulation of signal transduction / response to amphetamine / GTPase activator activity / G alpha (z) signalling events / G alpha (i) signalling events / G alpha (q) signalling events / neuron projection / G protein-coupled receptor signaling pathway / GTPase activity / synapse / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Schoch, G.A. / Jansson, A. / Elkins, J.M. / Haroniti, A. / Niesen, F.H. / Bunkoczi, G. / Lee, W.H. / Turnbull, A.P. / Yang, X. / Sundstrom, M. ...Schoch, G.A. / Jansson, A. / Elkins, J.M. / Haroniti, A. / Niesen, F.H. / Bunkoczi, G. / Lee, W.H. / Turnbull, A.P. / Yang, X. / Sundstrom, M. / Arrowsmith, C. / Edwards, A. / Marsden, B. / Gileadi, O. / Ball, L. / von Delft, F. / Doyle, D.A. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2008 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zv4.cif.gz | 40.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zv4.ent.gz | 27.4 KB | Display | PDB format |
PDBx/mmJSON format | 1zv4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zv/1zv4 ftp://data.pdbj.org/pub/pdb/validation_reports/zv/1zv4 | HTTPS FTP |
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-Related structure data
Related structure data | 2a72C 2af0C 2bt2C 2bv1C 2es0C 2gtpC 2i59C 2ihbC 2ihdC 2ik8C 2jm5C 2jnuC 2odeC 2owiC 1cmzS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 18727.100 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RGS17 / Plasmid: pLIC-SGC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3 / References: UniProt: Q9UGC6 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 49.5 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: mPEG2K, Na succinate, Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.987 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: May 23, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→52.56 Å / Num. all: 7748 / Num. obs: 7589 / % possible obs: 98.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.9 % / Biso Wilson estimate: 71.3 Å2 / Rmerge(I) obs: 0.072 / Net I/σ(I): 23 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 9 % / Rmerge(I) obs: 0.421 / Mean I/σ(I) obs: 4.2 / Num. unique all: 1082 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1CMZ Resolution: 2.4→35.7 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.925 / SU B: 17.958 / SU ML: 0.195 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.338 / ESU R Free: 0.248 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 68.449 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→35.7 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.462 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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