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- PDB-2i8f: Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2i8f | ||||||
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Title | Solution Conformation of the H47A Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551 | ||||||
![]() | Cytochrome c-551 | ||||||
![]() | ELECTRON TRANSPORT / helix-turn-helix / cytochrome | ||||||
Function / homology | ![]() periplasmic space / electron transfer activity / iron ion binding / heme binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
![]() | Liang, Q. / Timkovich, R. | ||||||
![]() | ![]() Title: Solution Conformation of the His-47 to Ala-47 Mutant of Pseudomonas stutzeri ZoBell Ferrocytochrome c-551. Authors: Liang, Q. / Miller, G.T. / Beeghley, C.A. / Graf, C.B. / Timkovich, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 35.2 KB | Display | ![]() |
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PDB format | ![]() | 27.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 8505.787 Da / Num. of mol.: 1 / Mutation: H47A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-HEC / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.5 mM H47A c-551, 50 mM sodium phosphate buffer, 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 50 mM / pH: 7 / 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 AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1511 restraints, 1414 are NOE-derived distance constraints, 67 dihedral angle restraints, 30 distance restraints from hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |