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Yorodumi- PDB-4z2x: Crystal structure of a RNA binding domain of a U2 small nuclear r... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4z2x | ||||||
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Title | Crystal structure of a RNA binding domain of a U2 small nuclear ribonucleoprotein auxiliary factor 2 (U2AF) from mouse at 2.15 A resolution | ||||||
Components | Splicing factor U2AF 65 kDa subunit | ||||||
Keywords | RNA BINDING PROTEIN / Canonical RNA binding protein / RNA Splicing / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-BIOLOGY / Partnership for T-Cell Biology / TCELL | ||||||
Function / homology | Function and homology information mRNA 3'-end processing / RNA Polymerase II Transcription Termination / Transport of Mature mRNA derived from an Intron-Containing Transcript / Protein hydroxylation / mRNA Splicing - Major Pathway / U2AF complex / poly-pyrimidine tract binding / pre-mRNA 3'-splice site binding / Prp19 complex / C2H2 zinc finger domain binding ...mRNA 3'-end processing / RNA Polymerase II Transcription Termination / Transport of Mature mRNA derived from an Intron-Containing Transcript / Protein hydroxylation / mRNA Splicing - Major Pathway / U2AF complex / poly-pyrimidine tract binding / pre-mRNA 3'-splice site binding / Prp19 complex / C2H2 zinc finger domain binding / commitment complex / U2-type prespliceosome / molecular function inhibitor activity / negative regulation of mRNA splicing, via spliceosome / negative regulation of protein ubiquitination / positive regulation of RNA splicing / RNA splicing / spliceosomal complex / mRNA splicing, via spliceosome / nuclear speck / enzyme binding / nucleus Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.15 Å | ||||||
Authors | Joint Center for Structural Genomics (JCSG) / Partnership for T-Cell Biology (TCELL) | ||||||
Citation | Journal: To be published Title: Crystal structure of a RNA binding domain of a U2 small nuclear ribonucleoprotein auxiliary factor 2 (U2AF) from mouse at 2.15 A resolution Authors: Joint Center for Structural Genomics (JCSG) / Partnership for T-Cell Biology (TCELL) | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4z2x.cif.gz | 99.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4z2x.ent.gz | 75 KB | Display | PDB format |
PDBx/mmJSON format | 4z2x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z2/4z2x ftp://data.pdbj.org/pub/pdb/validation_reports/z2/4z2x | HTTPS FTP |
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-Related structure data
Related structure data | 3v4mS S: Starting model for refinement |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 12033.667 Da / Num. of mol.: 2 / Fragment: RNA binding domain (UNP residues 371-475) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: U2af2, U2af65 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): BL21Gold(DE3) / References: UniProt: P26369 #2: Water | ChemComp-HOH / | Sequence details | THE CRYSTALLIZATION CONTAINED TWO DIFFERENT CONSTRUCTS OF UNIPROTKB P26369. THE TAGS WERE REMOVED ...THE CRYSTALLIZ | |
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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: 2.1 Å3/Da / Density % sol: 41.46 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: 0.2M sodium thiocyanate, 20% polyethylene glycol 3350 |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.97879 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 2, 2013 Details: Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: single crystal Si(111) bent / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97879 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.15→37.9 Å / Num. obs: 11422 / % possible obs: 98.2 % / Observed criterion σ(I): -3 / Redundancy: 3.782 % / Biso Wilson estimate: 35.62 Å2 / Rmerge F obs: 0.998 / Rmerge(I) obs: 0.098 / Rrim(I) all: 0.113 / Net I/σ(I): 12.09 / Num. measured all: 43198 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3v4m Resolution: 2.15→37.9 Å / Cor.coef. Fo:Fc: 0.9378 / Cor.coef. Fo:Fc free: 0.9046 / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0 Details: 1. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 2. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS)
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Displacement parameters | Biso max: 139.08 Å2 / Biso mean: 46.7017 Å2 / Biso min: 22.07 Å2
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Refine analyze | Luzzati coordinate error obs: 0.336 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→37.9 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.35 Å / Total num. of bins used: 6
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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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