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Open data
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Basic information
| Entry | Database: PDB / ID: 4kf7 | ||||||
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| Title | Nup188(aa1-1160) from Myceliophthora thermophila | ||||||
Components | Nup188 | ||||||
Keywords | STRUCTURAL PROTEIN / Nucleoporin | ||||||
| Function / homology | Function and homology informationnuclear pore inner ring / structural constituent of nuclear pore / RNA export from nucleus / mRNA transport / protein import into nucleus Similarity search - Function | ||||||
| Biological species | Myceliophthora thermophila (fungus) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.65 Å | ||||||
Authors | Schwartz, T.U. / Andersen, K.R. | ||||||
Citation | Journal: Elife / Year: 2013Title: Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors. Authors: Andersen, K.R. / Onischenko, E. / Tang, J.H. / Kumar, P. / Chen, J.Z. / Ulrich, A. / Liphardt, J.T. / Weis, K. / Schwartz, T.U. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 4kf7.cif.gz | 442.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4kf7.ent.gz | 364.7 KB | Display | PDB format |
| PDBx/mmJSON format | 4kf7.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4kf7_validation.pdf.gz | 433.6 KB | Display | wwPDB validaton report |
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| Full document | 4kf7_full_validation.pdf.gz | 448.5 KB | Display | |
| Data in XML | 4kf7_validation.xml.gz | 38.7 KB | Display | |
| Data in CIF | 4kf7_validation.cif.gz | 53.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kf/4kf7 ftp://data.pdbj.org/pub/pdb/validation_reports/kf/4kf7 | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 128246.492 Da / Num. of mol.: 1 / Fragment: N-terminal domain (UNP residues 1-1160) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Myceliophthora thermophila (fungus) / Gene: MYCTH_2303581 / Production host: ![]() |
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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: 2.83 Å3/Da / Density % sol: 56.49 % |
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| Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 0.1 M MES, 4.5-7.0% w/v PEG4000, 150 mM ammonium sulfate, 1 mM DTT, 1.0-2.5% tert-butanol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å |
| Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 3, 2012 |
| Radiation | Monochromator: double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
| Reflection | Resolution: 2.65→66.8 Å / Num. all: 41673 / Num. obs: 41673 / % possible obs: 100 % / Observed criterion σ(F): 1.8 / Observed criterion σ(I): 1.8 / Redundancy: 4.1 % / Rmerge(I) obs: 0.031 / Net I/σ(I): 31.3 |
| Reflection shell | Resolution: 2.65→2.72 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.772 / Mean I/σ(I) obs: 1.8 / % possible all: 99.9 |
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Processing
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| Refinement | Method to determine structure: SAD / Resolution: 2.65→66.759 Å / SU ML: 0.34 / σ(F): 1.8 / Phase error: 24.77 / Stereochemistry target values: ML
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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: 2.65→66.759 Å
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| Refine LS restraints |
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| LS refinement shell |
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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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Myceliophthora thermophila (fungus)
X-RAY DIFFRACTION
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