BMRB

Biological Magnetic Resonance Data Bank


A 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
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 Download bibtex for citation iamge 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 Download bibtex for citation iamge Elles Steensma, Euan Gordon, Janos Hajdu, Linda M Oster, Stuart J Ferguson