+Open data
-Basic information
Entry | Database: PDB / ID: 6p6a | ||||||
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Title | Structure of Mouse Importin alpha - NIT2 NLS peptide complex | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / nuclear import / importin alpha / transcription factor | ||||||
Function / homology | Function and homology information Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / nitrate assimilation / cytoplasmic stress granule ...Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / nitrate assimilation / cytoplasmic stress granule / protein import into nucleus / host cell / DNA-binding transcription factor binding / postsynaptic density / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / glutamatergic synapse / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Neurospora crassa (fungus) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.151 Å | ||||||
Authors | Bernardes, N.E. / Fukuda, C.A. / Silva, T.D. / Oliveira, H.C. / Fontes, M.R.M. | ||||||
Funding support | Brazil, 1items
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Citation | Journal: Sci Rep / Year: 2020 Title: Comparative study of the interactions between fungal transcription factor nuclear localization sequences with mammalian and fungal importin-alpha. Authors: Bernardes, N.E. / Fukuda, C.A. / da Silva, T.D. / de Oliveira, H.C. / de Barros, A.C. / Dreyer, T.R. / Bertolini, M.C. / Fontes, M.R.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6p6a.cif.gz | 188.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6p6a.ent.gz | 147.3 KB | Display | PDB format |
PDBx/mmJSON format | 6p6a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6p6a_validation.pdf.gz | 435.7 KB | Display | wwPDB validaton report |
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Full document | 6p6a_full_validation.pdf.gz | 439.9 KB | Display | |
Data in XML | 6p6a_validation.xml.gz | 19.7 KB | Display | |
Data in CIF | 6p6a_validation.cif.gz | 29.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p6/6p6a ftp://data.pdbj.org/pub/pdb/validation_reports/p6/6p6a | HTTPS FTP |
-Related structure data
Related structure data | 6p6eC 5u5pS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 49886.633 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kpna2, Rch1 Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria) References: UniProt: P52293 | ||
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#2: Protein/peptide | Mass: 1576.805 Da / Num. of mol.: 2 / Source method: obtained synthetically Source: (synth.) Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (fungus) References: UniProt: P19212 #3: 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: 3.32 Å3/Da / Density % sol: 66.51 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: Sodium Citrate, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: LNLS / Beamline: W01B-MX2 / Wavelength: 1.425 Å |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 16, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.425 Å / Relative weight: 1 |
Reflection | Resolution: 2.151→36.57 Å / Num. obs: 38952 / % possible obs: 99.82 % / Redundancy: 12.7 % / Biso Wilson estimate: 33.73 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.1158 / Rpim(I) all: 0.03352 / Rrim(I) all: 0.1206 / Net I/σ(I): 2.28 |
Reflection shell | Resolution: 2.151→2.228 Å / Redundancy: 11.6 % / Rmerge(I) obs: 1.056 / Mean I/σ(I) obs: 0.819 / Num. unique obs: 3788 / CC1/2: 0.819 / Rpim(I) all: 0.3214 / % possible all: 99.11 |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 5U5P Resolution: 2.151→36.568 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.18
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 125.28 Å2 / Biso mean: 44.1196 Å2 / Biso min: 18.63 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.151→36.568 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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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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