+Open data
-Basic information
Entry | Database: PDB / ID: 4igu | ||||||
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Title | Crystal structure of the RGS domain of CG5036 | ||||||
Components | CG5036 | ||||||
Keywords | SIGNALING PROTEIN / REGULATOR OF G-PROTEIN SIGNALING / GTPASE-ACTIVATING PROTEINS (GAP) / REGULATOR OF GZ-SELECTIVE PROTEIN SIGNALING 2 | ||||||
Function / homology | Function and homology information G alpha (z) signalling events / G alpha (q) signalling events / G alpha (i) signalling events / GDP-dissociation inhibitor activity / G-protein alpha-subunit binding / GTPase activator activity / positive regulation of GTPase activity Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Gabdulkhakov, A. / Tishchenko, S. | ||||||
Citation | Journal: Mol.Cell / Year: 2014 Title: Double suppression of the G alpha protein activity by RGS proteins Authors: Lin, C. / Koval, A. / Tishchenko, S. / Gabdulkhakov, A. / Tin, U. / Solis, G.P. / Katanaev, V.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4igu.cif.gz | 75.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4igu.ent.gz | 55.6 KB | Display | PDB format |
PDBx/mmJSON format | 4igu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ig/4igu ftp://data.pdbj.org/pub/pdb/validation_reports/ig/4igu | HTTPS FTP |
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-Related structure data
Related structure data | 1zv4S S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 17547.889 Da / Num. of mol.: 2 / Fragment: RGC domain, UNP residues 130-257 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: CG5036, Dmel_CG5036, EG:52C10.2 / Plasmid: pQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15(pREP4) / References: UniProt: Q8T017 #2: Chemical | ChemComp-CL / #3: Chemical | #4: Chemical | ChemComp-EDO / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.99 % Description: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS. |
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Crystal grow | Temperature: 297 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 30% Jeffamine ED-2001, 0.1M HEPES , pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 297.0K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER AXS MICROSTAR / Wavelength: 1.54178 Å |
Detector | Type: Bruker Platinum 135 / Detector: CCD / Date: Nov 14, 2012 |
Radiation | Monochromator: Montel 200 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. all: 45976 / Num. obs: 45971 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 |
Reflection shell | Resolution: 1.9→1.95 Å / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1ZV4 Resolution: 1.9→27.046 Å / SU ML: 0.21 / σ(F): 1.3 / Phase error: 21.72 / Stereochemistry target values: ML Details: SF FILE CONTAINS FRIEDEL PAIRS UNDER I/F_MINUS AND I/F_PLUS COLUMNS.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→27.046 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 17
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