Backbone and side–chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c
Protein Sci
Liu et al. 12 (9): 2104.
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15N- and 13C-HSQC spectra of reduced (Panel a) and oxidized (Panel b)
recombinant [H26N, H33N] horse cytochrome c. 13C-HSQC spectra of
reduced (Panel c) and oxidized (Panel d) 13C,15N-enriched recombinant [H26N, H33N] horse cytochrome c. Natural abundance 15N-HSQC spectra of reduced (Panel e) and oxidized (Panel f) wild type horse heart cytochrome c. All spectra were obtained at 750 MHz (1H) and 293 K.
