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Yorodumi- PDB-2nnw: Alternative conformations of Nop56/58-fibrillarin complex and imp... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2nnw | ||||||
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Title | Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs | ||||||
Components |
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Keywords | TRANSFERASE / box C/D | ||||||
Function / homology | Function and homology information box C/D methylation guide snoRNP complex / tRNA processing / snoRNA binding / S-adenosylmethionine-dependent methyltransferase activity / Transferases; Transferring one-carbon groups; Methyltransferases / small-subunit processome / rRNA processing / methylation / RNA binding Similarity search - Function | ||||||
Biological species | Pyrococcus furiosus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.7 Å | ||||||
Authors | Oruganti, S. / Zhang, Y. / Terns, R. / Terns, M.P. / Li, H. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Alternative Conformations of the Archaeal Nop56/58-Fibrillarin Complex Imply Flexibility in Box C/D RNPs. Authors: Oruganti, S. / Zhang, Y. / Li, H. / Robinson, H. / Terns, M.P. / Terns, R.M. / Yang, W. / Li, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2nnw.cif.gz | 234.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2nnw.ent.gz | 190.5 KB | Display | PDB format |
PDBx/mmJSON format | 2nnw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nn/2nnw ftp://data.pdbj.org/pub/pdb/validation_reports/nn/2nnw | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | The second part is generated by CNS |
-Components
#1: Protein | Mass: 43516.090 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus furiosus (archaea) / Production host: Escherichia coli (E. coli) / References: UniProt: Q8U4M1 #2: 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 / Production host: Escherichia coli (E. coli) References: UniProt: Q8U4M2, Transferases; Transferring one-carbon groups; Methyltransferases |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4.45 Å3/Da / Density % sol: 72.38 % |
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-Data collection
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-C |
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Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.7→49.33 Å / Num. obs: 68534 / Rsym value: 0.07 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.7→49.33 Å
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Refinement step | Cycle: LAST / Resolution: 2.7→49.33 Å
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