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Biological Magnetic Resonance Data BankA Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules |
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Entry ID | Data summary | Entry Title | Citation Title | Authors |
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4800 | Chemical Shifts: 4 sets |
Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, and of Trp109 of the isolated c domain of Paracoccus pantotrophus in the reduced state |
Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase
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Elles Steensma, Euan Gordon, Janos Hajdu, Linda M Oster, Stuart J Ferguson |
4801 | Chemical Shifts: 4 sets T1 Relaxation Values: 2 sets |
Chemical shifts of 1H resonances of the heme protons and of the side chain protons of the two axial ligands, His69 and Met106, of the isolated c domain of Paracoccus pantotrophus in the oxidized state |
Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase
|
Elles Steensma, Euan Gordon, Janos Hajdu, Linda M Oster, Stuart J Ferguson |