+Open data
-Basic information
Entry | Database: PDB / ID: 3nmu | ||||||
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Title | Crystal Structure of substrate-bound halfmer box C/D RNP | ||||||
Components |
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Keywords | Transferase/RNA / Kink-turn motif / RNA assembly motif / Transferase-RNA complex | ||||||
Function / homology | Function and homology information box C/D methylation guide snoRNP complex / ribonuclease P activity / tRNA 5'-leader removal / tRNA processing / snoRNA binding / Transferases; Transferring one-carbon groups; Methyltransferases / methyltransferase activity / rRNA processing / methylation / rRNA binding ...box C/D methylation guide snoRNP complex / ribonuclease P activity / tRNA 5'-leader removal / tRNA processing / snoRNA binding / Transferases; Transferring one-carbon groups; Methyltransferases / methyltransferase activity / rRNA processing / methylation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / RNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | Pyrococcus furiosus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.729 Å | ||||||
Authors | Li, H. / Xue, S. / Wang, R. | ||||||
Citation | Journal: Mol.Cell / Year: 2010 Title: Structural basis for substrate placement by an archaeal box C/D ribonucleoprotein particle. Authors: Xue, S. / Wang, R. / Yang, F. / Terns, R.M. / Terns, M.P. / Zhang, X. / Maxwell, E.S. / Li, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3nmu.cif.gz | 344.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3nmu.ent.gz | 275.2 KB | Display | PDB format |
PDBx/mmJSON format | 3nmu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3nmu_validation.pdf.gz | 945.5 KB | Display | wwPDB validaton report |
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Full document | 3nmu_full_validation.pdf.gz | 1 MB | Display | |
Data in XML | 3nmu_validation.xml.gz | 63.8 KB | Display | |
Data in CIF | 3nmu_validation.cif.gz | 88.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nm/3nmu ftp://data.pdbj.org/pub/pdb/validation_reports/nm/3nmu | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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Unit cell |
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-Components
-Protein , 3 types, 6 molecules ABCGFJ
#1: Protein | Mass: 43937.555 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Gene: PF0060 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8U4M1 #2: Protein | Mass: 14243.545 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Gene: rpl7ae, PF1367 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8U160 #4: Protein | Mass: 26760.844 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Gene: flpA, PF0059 / Production host: Escherichia coli (E. coli) References: UniProt: Q8U4M2, Transferases; Transferring one-carbon groups; Methyltransferases |
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-RNA chain , 2 types, 4 molecules DEIK
#3: RNA chain | Mass: 11009.606 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: box C/D RNA / Source: (gene. exp.) Pyrococcus furiosus (archaea) #5: RNA chain | Mass: 4156.542 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: The RNA was chemically synthesized |
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-Non-polymers , 2 types, 29 molecules
#6: Chemical | #7: Water | ChemComp-HOH / | |
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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: 3.4 Å3/Da / Density % sol: 63.86 % |
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Crystal grow | Temperature: 303 K / Method: vapor diffusion, hanging drop / pH: 7 Details: The complex was equilibrated with reservoir solutions containing 0-400 mM potassium chloride, 200 mM-1.5 M sodium chloride, 150-250 mM magnesium acetate, 200 mM ammonium acetate, 50 mM HEPES- ...Details: The complex was equilibrated with reservoir solutions containing 0-400 mM potassium chloride, 200 mM-1.5 M sodium chloride, 150-250 mM magnesium acetate, 200 mM ammonium acetate, 50 mM HEPES-NaOH (pH 7.0), and 0 5% PEG 4000, VAPOR DIFFUSION, HANGING DROP, temperature 303K |
-Data collection
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
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Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. all: 63177 / Num. obs: 61445 / % possible obs: 89.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 3 / Redundancy: 5.8 % / Biso Wilson estimate: 56.33 Å2 / Rsym value: 0.074 |
Reflection shell | Resolution: 2.7→2.8 Å / % possible all: 58.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.729→33.572 Å / SU ML: 0.34 / σ(F): 0 / Phase error: 34.75 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 45.602 Å2 / ksol: 0.297 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.729→33.572 Å
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Refine LS restraints |
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LS refinement shell |
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