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- PDB-5hb6: Crystal structure of Chaetomium thermophilum Nup145N APD T994A mu... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5hb6 | ||||||||||||||||||||||||||||||
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Title | Crystal structure of Chaetomium thermophilum Nup145N APD T994A mutant fused to Nup145C N | ||||||||||||||||||||||||||||||
![]() | Nucleoporin NUP145 | ||||||||||||||||||||||||||||||
![]() | TRANSPORT PROTEIN / Nucleocytoplasmic transport / Protein transport | ||||||||||||||||||||||||||||||
Function / homology | ![]() telomere tethering at nuclear periphery / nuclear pore cytoplasmic filaments / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / structural constituent of nuclear pore / RNA export from nucleus / nuclear localization sequence binding / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / mRNA transport / protein import into nucleus / nuclear membrane ...telomere tethering at nuclear periphery / nuclear pore cytoplasmic filaments / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / structural constituent of nuclear pore / RNA export from nucleus / nuclear localization sequence binding / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / mRNA transport / protein import into nucleus / nuclear membrane / hydrolase activity / RNA binding Similarity search - Function | ||||||||||||||||||||||||||||||
Biological species | ![]() | ||||||||||||||||||||||||||||||
Method | ![]() ![]() | ||||||||||||||||||||||||||||||
![]() | Lin, D.H. / Stuwe, T. / Hoelz, A. | ||||||||||||||||||||||||||||||
Funding support | ![]() ![]() ![]()
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![]() | ![]() Title: Architecture of the symmetric core of the nuclear pore. Authors: Lin, D.H. / Stuwe, T. / Schilbach, S. / Rundlet, E.J. / Perriches, T. / Mobbs, G. / Fan, Y. / Thierbach, K. / Huber, F.M. / Collins, L.N. / Davenport, A.M. / Jeon, Y.E. / Hoelz, A. | ||||||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 184.9 KB | Display | ![]() |
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PDB format | ![]() | 150.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.3 KB | Display | ![]() |
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Full document | ![]() | 449.4 KB | Display | |
Data in XML | ![]() | 18 KB | Display | |
Data in CIF | ![]() | 27.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5haxC ![]() 5hayC ![]() 5hazC ![]() 5hb0C ![]() 5hb1C ![]() 5hb2C ![]() 5hb3C ![]() 5hb4C ![]() 5hb5C ![]() 5hb7C ![]() 5hb8C C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 16035.193 Da / Num. of mol.: 2 / Mutation: T994A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: DSM 1495 / CBS 144.50 / IMI 039719 / Gene: NUP145, CTHT_0042590 / Production host: ![]() ![]() References: UniProt: G0SAK3, Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.51 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, hanging drop Details: 0.1 M TRIS (pH 8.8), 32 % (w/v) PEG 4000, 0.2 M lithium sulfate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 17, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.3→30 Å / Num. obs: 66722 / % possible obs: 94.7 % / Redundancy: 6.9 % / Net I/σ(I): 17.2 |
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Processing
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Refinement | Resolution: 1.3→25.926 Å / SU ML: 0.12 / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 18.74 / 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: 1.3→25.926 Å
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Refine LS restraints |
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LS refinement shell |
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