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Yorodumi- PDB-1g1i: CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1g1i | ||||||
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Title | CRYSTAL STRUCTURE OF THE OLIGOMERIZATION DOMAIN FROM ROTAVIRUS NSP4 | ||||||
Components | NON-STRUCTURAL GLYCOPROTEIN NSP4 | ||||||
Keywords | METAL BINDING PROTEIN / NS28 / parallel coiled-coil / homo-tetramer / metal binding site | ||||||
Function / homology | Function and homology information host caveola / host cell rough endoplasmic reticulum membrane / : / protein complex oligomerization / monoatomic ion channel activity / toxin activity / induction by virus of host autophagy / extracellular region / membrane / metal ion binding Similarity search - Function | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2 Å | ||||||
Authors | Bowman, G.D. / Nodelman, I.M. / Schutt, C.E. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: Crystal structure of the oligomerization domain of NSP4 from rotavirus reveals a core metal-binding site. Authors: Bowman, G.D. / Nodelman, I.M. / Levy, O. / Lin, S.L. / Tian, P. / Zamb, T.J. / Udem, S.A. / Venkataraghavan, B. / Schutt, C.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g1i.cif.gz | 27.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g1i.ent.gz | 20.9 KB | Display | PDB format |
PDBx/mmJSON format | 1g1i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g1/1g1i ftp://data.pdbj.org/pub/pdb/validation_reports/g1/1g1i | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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Details | The biological assembly is a tetramer which can be generated from chains A and B by constructing symmetry mates across the two-fold. |
-Components
#1: Protein/peptide | Mass: 5404.255 Da / Num. of mol.: 2 / Fragment: OLIGOMERIZATION DOMAIN / Source method: obtained synthetically Details: This sequence is derived from NSP4 from Simian 11 rotavirus (strain SA11). References: UniProt: O92323, UniProt: P04512*PLUS #2: Chemical | ChemComp-CA / | #3: 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: 1.77 Å3/Da / Density % sol: 30.5 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG400, magnesium sulfate, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 | ||||||||||||||||||||||||||||||
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: NSLS / Beamline: X12C / Wavelength: 0.9785,0.9788,0.95 | ||||||||||||
Detector | Type: BRANDEIS - B4 / Detector: CCD / Date: Apr 27, 1999 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2→14 Å / Num. all: 109286 / Num. obs: 10000 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.2 % / Biso Wilson estimate: 16.3 Å2 / Rmerge(I) obs: 0.045 / Net I/σ(I): 11.7 | ||||||||||||
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.235 / % possible all: 99.6 | ||||||||||||
Reflection | *PLUS Num. measured all: 109286 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2→14.07 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 934198.13 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: Four water molecules have been modelled above the metal and hydrating water molecules. It is also possible that the four water molecules (two per ASU) are instead a small molecule lying ...Details: Four water molecules have been modelled above the metal and hydrating water molecules. It is also possible that the four water molecules (two per ASU) are instead a small molecule lying across the two-fold crystallographic axis. There are two residues whose side chains have alternative rotomer conformations and have been modelled as such: B106 and B112.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 60.16 Å2 / ksol: 0.373 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→14.07 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.07 Å / Rfactor Rfree error: 0.033 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 8.5 % | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 27.9 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.307 / % reflection Rfree: 9.4 % / Rfactor Rwork: 0.296 |