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Yorodumi- PDB-2f3j: The solution structure of the REF2-I mRNA export factor (residues... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2f3j | ||||||
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Title | The solution structure of the REF2-I mRNA export factor (residues 1-155). | ||||||
Components | RNA and export factor binding protein 2 | ||||||
Keywords | TRANSPORT PROTEIN / RRM domain / RBD domain. | ||||||
Function / homology | Function and homology information mRNA transport / mRNA export from nucleus / RNA splicing / spliceosomal complex / mRNA processing / single-stranded DNA binding / mRNA binding / RNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / ARIA protocol (Nilges et al., 1997, J. Mol. Biol. 269, 408-422) used for structure calculation. | ||||||
Authors | Golovanov, A.P. / Hautbergue, G.M. / Wilson, S.A. / Lian, L.Y. | ||||||
Citation | Journal: Rna / Year: 2006 Title: The solution structure of REF2-I reveals interdomain interactions and regions involved in binding mRNA export factors and RNA. Authors: Golovanov, A.P. / Hautbergue, G.M. / Tintaru, A.M. / Lian, L.Y. / Wilson, S.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2f3j.cif.gz | 758 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2f3j.ent.gz | 642.6 KB | Display | PDB format |
PDBx/mmJSON format | 2f3j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2f3j_validation.pdf.gz | 350.6 KB | Display | wwPDB validaton report |
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Full document | 2f3j_full_validation.pdf.gz | 497.2 KB | Display | |
Data in XML | 2f3j_validation.xml.gz | 48.4 KB | Display | |
Data in CIF | 2f3j_validation.cif.gz | 63.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f3/2f3j ftp://data.pdbj.org/pub/pdb/validation_reports/f3/2f3j | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19630.188 Da / Num. of mol.: 1 / Fragment: RRM Domain (Residues 1 - 155) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Refbp2, Ref2 / Plasmid: PET24B / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-RP / References: UniProt: Q9JJW6 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The protein construct contains 14-residue N-terminal T7 tag (MASMTGGQQMGRDP), and C-terminal tag (LEHHHHHH). The T7 tag is unstructured and is omitted in the coordinate file, where residue ...Text: The protein construct contains 14-residue N-terminal T7 tag (MASMTGGQQMGRDP), and C-terminal tag (LEHHHHHH). The T7 tag is unstructured and is omitted in the coordinate file, where residue numbering starts from residue 1 of REF2-I. Last three residues (LEH) in the coordinate file originate from the beginning of C-terminal tag. The N-terminal domain (1-74) of REF2-I is flexible and is largely unstructured, apart from the region 8-18 which forms a transient helix. |
-Sample preparation
Details |
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Sample conditions |
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-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: ARIA protocol (Nilges et al., 1997, J. Mol. Biol. 269, 408-422) used for structure calculation. Software ordinal: 1 Details: Residual dipolar couplings were measured in 5% PEG liquid crystal media (C12E5 + hexane, Ruckert and Otting, 2000, J. Am. Chem. Soc. 122, 7793) and used as SANI restraints in ARIA. | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 14 |