+Open data
-Basic information
Entry | Database: PDB / ID: 1jhs | ||||||
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Title | Protein Mog1 E65A mutant | ||||||
Components | MOG1 PROTEIN | ||||||
Keywords | GENE REGULATION / NUCLEAR-PROTEIN IMPORT / GSP1 | ||||||
Function / homology | Function and homology information regulation of membrane depolarization / sodium channel regulator activity / mRNA transport / guanyl-nucleotide exchange factor activity / small GTPase binding / protein import into nucleus / transmembrane transporter binding / nucleus Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Baker, R.P. / Harreman, M.T. / Ecclestone, J.F. / Corbett, A.H. / Stewart, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: Interaction between Ran and Mog1 is required for efficient nuclear protein import Authors: Baker, R.P. / Harreman, M.T. / Ecclestone, J.F. / Corbett, A.H. / Stewart, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jhs.cif.gz | 52.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jhs.ent.gz | 37.1 KB | Display | PDB format |
PDBx/mmJSON format | 1jhs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jhs_validation.pdf.gz | 357.5 KB | Display | wwPDB validaton report |
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Full document | 1jhs_full_validation.pdf.gz | 359.8 KB | Display | |
Data in XML | 1jhs_validation.xml.gz | 5.2 KB | Display | |
Data in CIF | 1jhs_validation.cif.gz | 8.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jh/1jhs ftp://data.pdbj.org/pub/pdb/validation_reports/jh/1jhs | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 21015.564 Da / Num. of mol.: 1 / Mutation: E65A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: Mog1 / Production host: Escherichia coli (E. coli) / Strain (production host): pET / References: UniProt: P47123 |
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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: 2.63 Å3/Da / Density % sol: 53.27 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / Details: PEG, VAPOR DIFFUSION, HANGING DROP at 291K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 291 K / pH: 5.6 / Method: vapor diffusion, hanging drop / Details: Baker, R.P., (2000) Acta Crystallogr., D56, 229. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.933 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 24, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→31.2 Å / Num. all: 18211 / Num. obs: 18191 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Biso Wilson estimate: 20 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 6.4 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.076 / Mean I/σ(I) obs: 8.9 / % possible all: 99.9 |
Reflection | *PLUS Num. measured all: 62794 |
Reflection shell | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 2 Å / % possible obs: 99.9 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Mog1 native Resolution: 1.9→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 18.2 Å2
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Refine analyze | Luzzati coordinate error obs: 0.22 Å / Luzzati sigma a obs: 0.06 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→20 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 31.2 Å / % reflection Rfree: 5 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |