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- PDB-1sjg: Solution Structure of T4moC, the Rieske Ferredoxin Component of t... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1sjg | ||||||
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Title | Solution Structure of T4moC, the Rieske Ferredoxin Component of the Toluene 4-Monooxygenase Complex | ||||||
![]() | Toluene-4-monooxygenase system protein C | ||||||
![]() | ELECTRON TRANSPORT / Rieske [2Fe-2S] domain / ferredoxin / Pfam PF00355 | ||||||
Function / homology | ![]() toluene catabolic process / 2 iron, 2 sulfur cluster binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Skjeldal, L. / Peterson, F.C. / Doreleijers, J.F. / Moe, L.A. / Pikus, J.D. / Volkman, B.F. / Westler, W.M. / Markley, J.L. / Fox, B.G. | ||||||
![]() | ![]() Title: Solution structure of T4moC, the Rieske ferredoxin component of the toluene 4-monooxygenase complex Authors: Skjeldal, L. / Peterson, F.C. / Doreleijers, J.F. / Moe, L.A. / Pikus, J.D. / Westler, W.M. / Markley, J.L. / Volkman, B.F. / Fox, B.G. #1: Journal: Biochemistry / Year: 1996 Title: Recombinant toluene-4-monooxygenase: catalytic and Mossbauer studies of the purified diiron and rieske components of a four-protein complex Authors: Pikus, J.D. / Studts, J.M. / Achim, C. / Kauffmann, K.E. / Munck, E. / Steffan, R.J. / McClay, K. / Fox, B.G. #2: Journal: Biochemistry / Year: 1999 Title: Detection and classification of hyperfine-shifted 1H, 2H, and 15N resonances of the Rieske ferredoxin component from toluene 4-monooxygenase Authors: Xia, B. / Pikus, J.D. / Xia, W. / McClay, K. / Steffan, R.J. / Chae, Y.K. / Westler, W.M. / Markley, J.L. / Fox, B.G. #3: Journal: Protein Expr.Purif. / Year: 1999 Title: Application of fed-batch fermentation to the preparation of isotopically labeled or selenomethionyl-labeled proteins Authors: Studts, J.M. / Fox, B.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 655.4 KB | Display | ![]() |
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PDB format | ![]() | 544.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 373 KB | Display | ![]() |
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Full document | ![]() | 490.9 KB | Display | |
Data in XML | ![]() | 35.5 KB | Display | |
Data in CIF | ![]() | 61.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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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: 12336.695 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-FES / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 20 mM phosphate, 90% H2O, 10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 20 mM phosphate / pH: 6.4 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |