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- PDB-2mf2: Structural and biophysical characterization of the mRNA interfera... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2mf2 | ||||||
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Title | Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus. | ||||||
![]() | mRNA interferase MazF | ||||||
![]() | HYDROLASE / CcdB/MazF fold / ribonuclease | ||||||
Function / homology | ![]() rRNA catabolic process / mRNA catabolic process / RNA endonuclease activity / endonuclease activity / Hydrolases; Acting on ester bonds / DNA binding / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model1 | ||||||
![]() | Zorzini, V. / Cheung, A. / Loris, R. / van Nuland, N.A.J. | ||||||
![]() | ![]() Title: Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics Authors: Zorzini, V. / Buts, L. / Sleutel, M. / Garcia-Pino, A. / Talavera, A. / Haesaerts, S. / De Greve, H. / Cheung, A. / van Nuland, N.A.J. / Loris, R. #1: ![]() Title: 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase. Authors: Zorzini, V. / Haesaerts, S. / Cheung, A. / Loris, R. / van Nuland, N.A. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.6 MB | Display | ![]() |
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PDB format | ![]() | 1.3 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 557 KB | Display | ![]() |
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Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 298.6 KB | Display | |
Data in CIF | ![]() | 245.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 14821.011 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q7A0D7, UniProt: Q2FWI8*PLUS, Hydrolases; Acting on ester bonds |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1 mM [U-99% 13C; U-99% 15N] SaMazF, 90 % H2O, 10 % D2O, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | pH: 6.6 / Pressure: 1 atm / Temperature: 308 K |
-NMR measurement
NMR spectrometer | Type: Varian Uniform NMR System / Manufacturer: Varian / Model: Uniform NMR System / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: Final refinement in water | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |