A pulse sequence that yields three-dimensional ¹H chemical shift / ¹H-¹⁵N heteronuclear dipolar coupling / ¹⁵N chemical shift solid-state NMR spectra is demonstrated on a uniformly ¹⁵N labeled membrane protein in magnetically aligned phospholipid bilayers. Based on SAMPI4, the pulse sequence yields high resolution in all three dimensions at a ¹H resonance frequency of 900 MHz with the relatively low rf field strength (33 kHz) available for a lossy aqueous sample with a commercial spectrometer and probe. The ¹H chemical shift frequency dimension is shown to select among amide resonances, which will be useful in studies of larger polytopic membrane proteins where the resonances overlap in two-dimensional spectra. Moreover, the ¹H chemical shift, which can be measured from these spectra, provides an additional orientationally dependent frequency as input for structure calculations.