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Open data
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Basic information
Entry | Database: PDB / ID: 1g10 | ||||||
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Title | TOLUENE-4-MONOOXYGENASE CATALYTIC EFFECTOR PROTEIN NMR STRUCTURE | ||||||
![]() | TOLUENE-4-MONOOXYGENASE CATALYTIC EFFECTOR | ||||||
![]() | OXIDOREDUCTASE / aromatic hydrocarbon catabolism / MONOOXYGENASE / TOLUENE OXIDATION | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY SIMULATED ANNEALING, TORSION ANGLE MOLECULAR DYNAMICS | ||||||
Model type details | minimized average | ||||||
![]() | Hemmi, H. / Studts, J.M. / Chae, Y.K. / Song, J. / Markley, J.L. / Fox, B.G. | ||||||
![]() | ![]() Title: Solution structure of the toluene 4-monooxygenase effector protein (T4moD). Authors: Hemmi, H. / Studts, J.M. / Chae, Y.K. / Song, J. / Markley, J.L. / Fox, B.G. #1: ![]() Title: Assignment of 1H, 13C and 15N NMR Signals in the Toluene 4-monooxygenase Effector Protein Authors: Hemmi, H. / Studts, J.M. / Chae, Y.K. / Fox, B.G. / Markley, J.L. #2: ![]() Title: Application of Fed-batch Fermentation to the Preparation of Isotopicaly Labeled or Selenomethionyl-labeled Proteins Authors: Studts, J.M. / Fox, B.G. #3: ![]() 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, M.M. / Markley, J.L. / Fox, B.G. #4: ![]() 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. / M Studts, J. / Achim, C. / Kauffmann, K.E. / Munck, E. / Steffan, R.J. / Mcclay, K. / Fox, B.G. #5: ![]() Title: Toluene-4-monooxygenase, a Three Component Enzyme System that Catalyzes the Oxidation of Toluene to p-Cresol in Pseudomonas mendocina KR1 Authors: Whited, G.M. / Gibson, D.T. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 41.3 KB | Display | ![]() |
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PDB format | ![]() | 28.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 244.6 KB | Display | ![]() |
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Full document | ![]() | 244.4 KB | Display | |
Data in XML | ![]() | 3.8 KB | Display | |
Data in CIF | ![]() | 4.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1g11C C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
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NMR ensembles |
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Components
#1: Protein | Mass: 11497.836 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q00459, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: H-15N ![]() ![]() ![]() ![]() |
NMR details | Text: 123 1H-15N CROSS PEAKS WERE ASSIGNED OUT OF THE EXPECTED 129 CROSS PEAKS (95% COMPLETE). 386 BACKBONE RESONANCES WERE ASSIGNED OUT OF THE EXPECTED 400 RESONANCES (97% COMPLETE). 789 SIDECHAIN ...Text: 123 1H-15N CROSS PEAKS WERE ASSIGNED OUT OF THE EXPECTED 129 CROSS PEAKS (95% COMPLETE). 386 BACKBONE RESONANCES WERE ASSIGNED OUT OF THE EXPECTED 400 RESONANCES (97% COMPLETE). 789 SIDECHAIN RESONANCES WERE ASSIGNED OUT OF THE EXPECTED 901 RESONANCES (88% COMPLETE). ARG SIDECHAIN ATOMS ACCOUNT FOR 51 OF 112 UNASSIGNED SIDECHAIN ATOMS (51%). |
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Sample preparation
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
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Refinement | Method: DISTANCE GEOMETRY SIMULATED ANNEALING, TORSION ANGLE MOLECULAR DYNAMICS Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |