+Open data
-Basic information
Entry | Database: PDB / ID: 2x1f | ||||||
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Title | Structure of Rna15 RRM with bound RNA (GU) | ||||||
Components |
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Keywords | TRANSCRIPTION/RNA / TRANSCRIPTION-RNA COMPLEX / MRNA PROCESSING | ||||||
Function / homology | Function and homology information mRNA cleavage stimulating factor complex / mRNA cleavage factor complex / mRNA cleavage and polyadenylation specificity factor complex / : / mRNA processing / molecular adaptor activity / mRNA binding Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / OTHER / Resolution: 1.6 Å | ||||||
Authors | Pancevac, C. / Goldstone, D.C. / Ramos, A. / Taylor, I.A. | ||||||
Citation | Journal: Nucleic Acids Res. / Year: 2010 Title: Structure of the RNA15 Rrm-RNA Complex Reveals the Molecular Basis of Gu Specificity in Transcriptional 3-End Processing Factors. Authors: Pancevac, C. / Goldstone, D.C. / Ramos, A. / Taylor, I.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2x1f.cif.gz | 34.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2x1f.ent.gz | 22.5 KB | Display | PDB format |
PDBx/mmJSON format | 2x1f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x1/2x1f ftp://data.pdbj.org/pub/pdb/validation_reports/x1/2x1f | HTTPS FTP |
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-Related 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: 10769.002 Da / Num. of mol.: 1 / Fragment: RNA RECOGNITION MODULE, RESIDUES 16-103 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P25299 |
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#2: RNA chain | Mass: 1563.952 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#3: Water | ChemComp-HOH / |
Sequence details | P16 TO S103 WITH C-TERMINAL HISTAG |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 1.9 Å3/Da / Density % sol: 35.3 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Wavelength: 1.5418 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.6→20 Å / Num. obs: 12488 / % possible obs: 99.3 % / Observed criterion σ(I): 3 / Redundancy: 13 % / Biso Wilson estimate: 13.52 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 52.1 |
-Processing
Software |
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Refinement | Method to determine structure: OTHER / Resolution: 1.6→56.7 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.94 / SU B: 2.094 / SU ML: 0.075 / Cross valid method: THROUGHOUT / ESU R: 0.113 / ESU R Free: 0.108 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.154 Å2
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Refinement step | Cycle: LAST / Resolution: 1.6→56.7 Å
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Refine LS restraints |
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