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Open data
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Basic information
| Entry | Database: PDB / ID: 4c0p | ||||||
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| Title | Unliganded Transportin 3 | ||||||
Components | TRANSPORTIN-3 | ||||||
Keywords | TRANSPORT PROTEIN / NUCLEAR IMPORT / HEAT REPEAT / TNPO3 | ||||||
| Function / homology | Function and homology informationannulate lamellae / nuclear import signal receptor activity / small GTPase binding / protein import into nucleus / nuclear envelope / nucleoplasm / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
| Biological species | HOMO SAPIENS (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å | ||||||
Authors | Maertens, G.N. / Cook, N.J. / Hare, S. / Cherepanov, P. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2014Title: Structural Basis for Nuclear Import of Splicing Factors by Human Transportin 3. Authors: Maertens, G.N. / Cook, N.J. / Wang, W. / Hare, S. / Gupta, S.S. / Oztop, I. / Lee, K. / Pye, V.E. / Cosnefroy, O. / Snijders, A.P. / Kewalramani, V.N. / Fassati, A. / Engelman, A. / Cherepanov, P. | ||||||
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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 | 4c0p.cif.gz | 689.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb4c0p.ent.gz | 567.6 KB | Display | PDB format |
| PDBx/mmJSON format | 4c0p.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4c0p_validation.pdf.gz | 481.5 KB | Display | wwPDB validaton report |
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| Full document | 4c0p_full_validation.pdf.gz | 525.1 KB | Display | |
| Data in XML | 4c0p_validation.xml.gz | 113.1 KB | Display | |
| Data in CIF | 4c0p_validation.cif.gz | 150.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c0/4c0p ftp://data.pdbj.org/pub/pdb/validation_reports/c0/4c0p | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 4c0oC ![]() 4c0qC ![]() 2x19S ![]() 2xwuS C: citing same article ( S: Starting model for refinement |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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| 3 | ![]()
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| 4 | ![]()
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| Unit cell |
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| Noncrystallographic symmetry (NCS) | NCS oper:
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Components
| #1: Protein | Mass: 104281.148 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Details: C511A MUTATION ENGINEERED TO IMPROVE CRYSTAL PACKING Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PETSUMO-TNPO3(C511A) / Production host: ![]() #2: Chemical | ChemComp-DTT / Sequence details | C511A MUTATION ENGINEERED | |
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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: 2.88 Å3/Da / Density % sol: 57.3 % / Description: NONE |
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| Crystal grow | pH: 8.2 Details: 20% (W/V) PEG3350, 0.2 M NABR, 10 MM DTT, 2 MM EDTA, 0.1 M BIS-TRIS PROPANE, PH8.2 |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9394 |
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 15, 2012 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9394 Å / Relative weight: 1 |
| Reflection | Resolution: 2.95→40 Å / Num. obs: 96311 / % possible obs: 98.6 % / Redundancy: 3.7 % / Biso Wilson estimate: 78.3 Å2 / Rmerge(I) obs: 0.14 / Net I/σ(I): 8.1 |
| Reflection shell | Resolution: 2.95→3.11 Å / Redundancy: 3.9 % / Rmerge(I) obs: 1.13 / Mean I/σ(I) obs: 1.4 / % possible all: 98.7 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRIES 2X19, 2XWU Resolution: 2.95→38.17 Å / SU ML: 0.44 / σ(F): 1.96 / Phase error: 30.95 / 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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 90.8 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 2.95→38.17 Å
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| LS refinement shell |
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HOMO SAPIENS (human)
X-RAY DIFFRACTION
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