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- PDB-1i6d: SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1i6d | ||||||
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Title | SOLUTION STRUCTURE OF THE FUNCTIONAL DOMAIN OF PARACOCCUS DENITRIFICANS CYTOCHROME C552 IN THE REDUCED STATE | ||||||
![]() | CYTOCHROME C552 | ||||||
![]() | ELECTRON TRANSPORT / CYTOCHROME C552 / HEME / REDOX STATES / ISOTOPE ENRICHMENT {13C/15N} / NMR SPECTROSCOPY / SOLUTION STRUCTURE | ||||||
Function / homology | ![]() electron transfer activity / heme binding / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, ENERGY MINIMIZATION | ||||||
![]() | Reincke, B. / Perez, C. / Pristovsek, P. / Luecke, C. / Ludwig, C. / Loehr, F. / Rogov, V.V. / Ludwig, B. / Rueterjans, H. | ||||||
![]() | ![]() Title: Solution structure and dynamics of the functional domain of Paracoccus denitrificans cytochrome c(552) in both redox states. Authors: Reincke, B. / Perez, C. / Pristovsek, P. / Lucke, C. / Ludwig, C. / Lohr, F. / Rogov, V.V. / Ludwig, B. / Ruterjans, H. #1: ![]() Title: Solution Structure of the Functional Domain of Paracoccus Denitrificans Cytochrome C552 in the Reduced State Authors: Pristovsek, P. / Luecke, C. / Reincke, B. / Ludwig, B. / Rueterjans, H. #2: ![]() Title: Structure of the Soluble Domain of Cytochrome C552 from Paracoccus Denitrificans in the Oxidized and Reduced States Authors: Harrenga, A. / Reincke, B. / Rueterjans, H. / Ludwig, B. / Michel, H. #3: ![]() Title: Heterologous Expression of Soluble Fragments of Cytochrome C552 Acting as Electron Donor to the Paracoccus Denitrificans Cytochrome C Oxidase Authors: Reincke, B. / Thoeny-Meyer, L. / Dannehl, C. / Odenwald, A. / Aidim, M. / Witt, H. / Rueterjans, H. / Ludwig, B. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 599.9 KB | Display | ![]() |
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PDB format | ![]() | 515.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 461.9 KB | Display | ![]() |
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Full document | ![]() | 543.3 KB | Display | |
Data in XML | ![]() | 34 KB | Display | |
Data in CIF | ![]() | 58.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 10553.977 Da / Num. of mol.: 1 / Fragment: SOLUBLE FUNCTIONAL DOMAIN Source method: isolated from a genetically manipulated source Details: COVALENT THIOETHER LINKAGES FROM HEME COFACTOR TO BOTH CYS14 AND CYS17 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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NMR details | Text: THE EXPERIMENTS WERE PERFORMED WITH REDUCED UNLABELED, 15N-LABELED OR 13C-LABELED CYTOCHROME C552. |
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Sample preparation
Details | Contents: 20 MM PHOSPHATE, 90% H2O/ 10% D2O |
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Sample conditions | pH: 5.50 / Temperature: 298.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, ENERGY MINIMIZATION / Software ordinal: 1 / Details: ENERGY MINIMIZATION. | ||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATIONS / Conformers calculated total number: 100 / Conformers submitted total number: 20 |