+Open data
-Basic information
Entry | Database: PDB / ID: 1rqu | ||||||
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Title | NMR structure of L7 dimer from E.coli | ||||||
Components | 50S ribosomal protein L7/L12 | ||||||
Keywords | RIBOSOME / protein L7/L12 | ||||||
Function / homology | Function and homology information large ribosomal subunit / ribosome binding / cytoplasmic translation / cytosolic large ribosomal subunit / structural constituent of ribosome / translation / mRNA binding / protein homodimerization activity / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics in torsion angle space | ||||||
Authors | Bocharov, E.V. / Sobol, A.G. / Pavlov, K.V. / Korzhnev, D.M. / Jaravine, V.A. / Gudkov, A.T. / Arseniev, A.S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2004 Title: From structure and dynamics of protein L7/L12 to molecular switching in ribosome. Authors: Bocharov, E.V. / Sobol, A.G. / Pavlov, K.V. / Korzhnev, D.M. / Jaravine, V.A. / Gudkov, A.T. / Arseniev, A.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rqu.cif.gz | 78.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rqu.ent.gz | 60.7 KB | Display | PDB format |
PDBx/mmJSON format | 1rqu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rqu_validation.pdf.gz | 245.1 KB | Display | wwPDB validaton report |
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Full document | 1rqu_full_validation.pdf.gz | 244.9 KB | Display | |
Data in XML | 1rqu_validation.xml.gz | 5.5 KB | Display | |
Data in CIF | 1rqu_validation.cif.gz | 7.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rq/1rqu ftp://data.pdbj.org/pub/pdb/validation_reports/rq/1rqu | HTTPS FTP |
-Related structure data
Related structure data | 1rqsC 1rqtC 1rqvC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12177.960 Da / Num. of mol.: 2 / Fragment: L7 dimer Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: pPR1 / Production host: Escherichia coli (E. coli) / Strain (production host): XL1 / References: UniProt: P0A7K2 |
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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 structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0.15 / pH: 6.9 / Pressure: ambient / Temperature: 303 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics in torsion angle space Software ordinal: 1 Details: Representative structure of L7 dimer with two unordered and extended hinge regions was calculated using the mean structures of its N- and C-terminal domains and NMR derived constraints ...Details: Representative structure of L7 dimer with two unordered and extended hinge regions was calculated using the mean structures of its N- and C-terminal domains and NMR derived constraints obtained for U-15N protein L7 | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,target function Conformers calculated total number: 100 / Conformers submitted total number: 1 |