+
Open data
-
Basic information
Entry | Database: PDB / ID: 1rqu | ||||||
---|---|---|---|---|---|---|---|
Title | NMR structure of L7 dimer from E.coli | ||||||
![]() | 50S ribosomal protein L7/L12 | ||||||
![]() | RIBOSOME / protein L7/L12 | ||||||
Function / homology | ![]() large ribosomal subunit / ribosome binding / cytosolic large ribosomal subunit / cytoplasmic translation / structural constituent of ribosome / translation / mRNA binding / protein homodimerization activity / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics in torsion angle space | ||||||
![]() | Bocharov, E.V. / Sobol, A.G. / Pavlov, K.V. / Korzhnev, D.M. / Jaravine, V.A. / Gudkov, A.T. / Arseniev, A.S. | ||||||
![]() | ![]() 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 78.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 60.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 245.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 244.9 KB | Display | |
Data in XML | ![]() | 5.5 KB | Display | |
Data in CIF | ![]() | 7.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1rqsC ![]() 1rqtC ![]() 1rqvC C: citing same article ( |
---|---|
Similar structure data | |
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
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.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||
NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-
Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITY / Manufacturer: Varian / Model: UNITY / Field strength: 600 MHz |
-
Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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 |