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Open data
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Basic information
Entry | Database: PDB / ID: 9glc | |||||||||||||||||||||||||||
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Title | NONO/SFPQ filament: local refinement central units (strand 1) | |||||||||||||||||||||||||||
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![]() | NUCLEAR PROTEIN / filament / RNA binding / DNA binding / gene regulation | |||||||||||||||||||||||||||
Function / homology | ![]() dendritic transport of messenger ribonucleoprotein complex / positive regulation of sister chromatid cohesion / negative regulation of circadian rhythm / alternative mRNA splicing, via spliceosome / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / paraspeckles / chromosome organization / activation of innate immune response / double-strand break repair via homologous recombination ...dendritic transport of messenger ribonucleoprotein complex / positive regulation of sister chromatid cohesion / negative regulation of circadian rhythm / alternative mRNA splicing, via spliceosome / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / paraspeckles / chromosome organization / activation of innate immune response / double-strand break repair via homologous recombination / regulation of circadian rhythm / RNA polymerase II transcription regulator complex / histone deacetylase binding / nuclear matrix / fibrillar center / transcription cis-regulatory region binding / nuclear speck / chromatin remodeling / innate immune response / negative regulation of DNA-templated transcription / dendrite / chromatin binding / chromatin / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / RNA binding / identical protein binding Similarity search - Function | |||||||||||||||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||||||||
![]() | Rasmussen, T. / Bottcher, B. | |||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: A filamentous scaffold for gene regulation Authors: Rasmussen, T. / Kuspert, J. / Schonemann, L. / Geiger, D. / Bottcher, B. | |||||||||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 424.5 KB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.2 MB | Display | |
Data in XML | ![]() | 68.5 KB | Display | |
Data in CIF | ![]() | 103.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 51438MC ![]() 9gldC ![]() 9gniC C: citing same article ( M: map data used to model this data |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
#1: Protein | Mass: 75880.156 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein | Mass: 54519.828 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() Has protein modification | N | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: NONO/SFPQ filament / Type: COMPLEX / Details: filaments formed by concentrating to 1 mg/ml / Entity ID: all / Source: NATURAL | ||||||||||||||||||||||||||||||
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
Source (natural) | Organism: ![]() ![]() | ||||||||||||||||||||||||||||||
Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R0.6/1 | ||||||||||||||||||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 90 % / Chamber temperature: 277 K / Details: blot time 5 sec, blot force +20 |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: TFS KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 130000 X / Nominal defocus max: 1400 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm / Alignment procedure: ZEMLIN TABLEAU |
Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
Image recording | Average exposure time: 6.2 sec. / Electron dose: 70 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 17059 |
EM imaging optics | Energyfilter name: TFS Selectris / Energyfilter slit width: 5 eV |
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Processing
EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 4144650 / Details: blob picker | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 2974535 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL Details: first rigid fitting with Chimera, then further refinemnt with Coot, C-terminal some de-novo residues | ||||||||||||||||||||||||
Atomic model building | 3D fitting-ID: 1 / Accession code: 6WMZ / Initial refinement model-ID: 1 / PDB-ID: 6WMZ / Source name: PDB / Type: experimental model
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Refine LS restraints |
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