+Open data
-Basic information
Entry | Database: PDB / ID: 1oun | ||||||
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Title | CRYSTAL STRUCTURE OF NUCLEAR TRANSPORT FACTOR 2 (NTF2) | ||||||
Components | NUCLEAR TRANSPORT FACTOR 2 | ||||||
Keywords | TRANSPORT / NUCLEAR TRANSPORT PROTEIN | ||||||
Function / homology | Function and homology information negative regulation of vascular endothelial growth factor production / protein localization to nuclear pore / nuclear pore central transport channel / structural constituent of nuclear pore / nuclear outer membrane / nuclear inner membrane / nuclear import signal receptor activity / mRNA transport / protein export from nucleus / small GTPase binding ...negative regulation of vascular endothelial growth factor production / protein localization to nuclear pore / nuclear pore central transport channel / structural constituent of nuclear pore / nuclear outer membrane / nuclear inner membrane / nuclear import signal receptor activity / mRNA transport / protein export from nucleus / small GTPase binding / positive regulation of protein import into nucleus / protein import into nucleus / nuclear membrane / nucleoplasm / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SINGLE ISOMORPHOUS REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Bullock, T.L. / Stewart, M.J. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1996 Title: The 1.6 angstroms resolution crystal structure of nuclear transport factor 2 (NTF2). Authors: Bullock, T.L. / Clarkson, W.D. / Kent, H.M. / Stewart, M. #1: Journal: Structure / Year: 1994 Title: Crystal Structure of Scytalone Dehydratase--A Disease Determinant of the Rice Pathogen, Magnaporthe Grisea Authors: Lundqvist, T. / Rice, J. / Hodge, C.N. / Basarab, G.S. / Pierce, J. / Lindqvist, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1oun.cif.gz | 61.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1oun.ent.gz | 46 KB | Display | PDB format |
PDBx/mmJSON format | 1oun.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1oun_validation.pdf.gz | 374 KB | Display | wwPDB validaton report |
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Full document | 1oun_full_validation.pdf.gz | 383.8 KB | Display | |
Data in XML | 1oun_validation.xml.gz | 7.1 KB | Display | |
Data in CIF | 1oun_validation.cif.gz | 10.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ou/1oun ftp://data.pdbj.org/pub/pdb/validation_reports/ou/1oun | 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: 14491.425 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: LIVER / Plasmid: PET VECTOR / Production host: Escherichia coli (E. coli) / Strain (production host): PET / References: UniProt: P61972 #2: 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: 2.48 Å3/Da / Density % sol: 47 % | ||||||||||||||||||||
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Crystal grow | pH: 4.5 / Details: pH 4.5 | ||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion / PH range low: 5.5 / PH range high: 4.5 | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: ELLIOTT GX-13 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→100 Å / Num. obs: 12825 / % possible obs: 96.9 % / Observed criterion σ(I): 0 / Redundancy: 5.8 % / Rmerge(I) obs: 0.059 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.175 / Mean I/σ(I) obs: 4.1 / % possible all: 94.7 |
Reflection | *PLUS Redundancy: 5.4 % / Num. measured all: 90240 |
Reflection shell | *PLUS % possible obs: 94.7 % |
-Processing
Software |
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Refinement | Method to determine structure: SINGLE ISOMORPHOUS REPLACEMENT Resolution: 2.3→100 Å / σ(F): 0 Details: TNT LIBRARY RMS CO-ORDINATE SHIFT IN FINAL CYCLE (A) : 0.01
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Refinement step | Cycle: LAST / Resolution: 2.3→100 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.158 | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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