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Yorodumi- PDB-2qna: Crystal structure of human Importin-beta (127-876) in complex wit... -
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-Basic information
Entry | Database: PDB / ID: 2qna | ||||||
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Title | Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of Snurportin1 (1-65) | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / Nuclear transport / import of spliceosomal subunits / protein-protein interaction / HEAT-repeat protein / Host-virus interaction / Nucleus / Protein transport / RNA-binding | ||||||
Function / homology | Function and homology information RNA import into nucleus / Inhibition of nitric oxide production / mitotic chromosome movement towards spindle pole / endoplasmic reticulum tubular network / establishment of mitotic spindle localization / astral microtubule organization / RNA cap binding / snRNA import into nucleus / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of cholesterol biosynthesis by SREBP (SREBF) ...RNA import into nucleus / Inhibition of nitric oxide production / mitotic chromosome movement towards spindle pole / endoplasmic reticulum tubular network / establishment of mitotic spindle localization / astral microtubule organization / RNA cap binding / snRNA import into nucleus / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of cholesterol biosynthesis by SREBP (SREBF) / ribosomal protein import into nucleus / importin-alpha family protein binding / NS1 Mediated Effects on Host Pathways / Initiation of Nuclear Envelope (NE) Reformation / NLS-dependent protein nuclear import complex / Apoptosis induced DNA fragmentation / Nuclear import of Rev protein / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / mitotic metaphase chromosome alignment / mitotic spindle assembly / nuclear pore / Assembly of the ORC complex at the origin of replication / Hsp90 protein binding / ISG15 antiviral mechanism / small GTPase binding / cytoplasmic stress granule / protein import into nucleus / specific granule lumen / SARS-CoV-1 activates/modulates innate immune responses / Interferon alpha/beta signaling / nuclear envelope / snRNP Assembly / nuclear membrane / ficolin-1-rich granule lumen / protein domain specific binding / Neutrophil degranulation / enzyme binding / RNA binding / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.84 Å | ||||||
Authors | Wohlwend, D. / Strasser, A. / Dickmanns, A. / Ficner, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structural basis for RanGTP independent entry of spliceosomal U snRNPs into the nucleus. Authors: Wohlwend, D. / Strasser, A. / Dickmanns, A. / Ficner, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qna.cif.gz | 160 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qna.ent.gz | 123.7 KB | Display | PDB format |
PDBx/mmJSON format | 2qna.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qn/2qna ftp://data.pdbj.org/pub/pdb/validation_reports/qn/2qna | HTTPS FTP |
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-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: 84567.398 Da / Num. of mol.: 1 / Fragment: residues 127-876 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: KPNB1, NTF97 / Plasmid: pGEX-6P-1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q14974 | ||
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#2: Protein | Mass: 7677.634 Da / Num. of mol.: 1 / Fragment: residues 1-66 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SNUPN, RNUT1, SPN1 / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta2 (DE3) / References: UniProt: O95149 | ||
#3: Chemical | #4: 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: 2.91 Å3/Da / Density % sol: 57.66 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, sitting drop / pH: 5.55 Details: sodium citrate, Ammonium SO4, Ethanol, NaCl, Tris, pH 5.55, VAPOR DIFFUSION, SITTING DROP, temperature 283K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.91841 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Jun 13, 2007 |
Radiation | Monochromator: Si-111 crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91841 Å / Relative weight: 1 |
Reflection | Resolution: 2.84→3104.26 Å / Num. obs: 25868 / % possible obs: 100 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4.82 % / Rmerge(I) obs: 0.192 / Net I/σ(I): 9.18 |
Reflection shell | Resolution: 2.84→2.92 Å / Redundancy: 4.92 % / Rmerge(I) obs: 0.626 / Mean I/σ(I) obs: 2.55 / % possible all: 100 |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.84→15 Å / Cor.coef. Fo:Fc: 0.889 / Cor.coef. Fo:Fc free: 0.821 / SU B: 34.556 / SU ML: 0.312 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 30.298 / ESU R Free: 0.408 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.16 Å2
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Refinement step | Cycle: LAST / Resolution: 2.84→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.84→2.911 Å / Total num. of bins used: 20
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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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