Histidine structure and chemistry lie at the heart of many enzyme active sites, ion channels, and metalloproteins. While solid-state NMR spectroscopy has been used to study histidine chemical shifts, the full pH dependence of the complete panel of N-15, C-13, and H-1 chemical shifts and the sensitivity of these chemical shifts to tautomeric structure have not been reported. Here we use magic-angle-spinning solid-state NMR spectroscopy to determine the N-15, C-13, and H-1 chemical shifts of histidine from pH 4.5 to 11. Two-dimensional homonuclear and heteronuclear correlation spectra indicate that these chemical shifts depend sensitively on the protonation state and tautomeric structure. The chemical shifts of the rare pi tautomer were observed for the first time, at the most basic pH used. Intra- and intermolecular hydrogen bonding between the imidazole nitrogens and the histidine backbone or water was detected, and N-H bond length measurements indicated the strength of the hydrogen bond. We also demonstrate the accurate measurement of the histidine side-chain torsion angles chi(1) and chi(2) through backbone-side chain C-13-N-15 distances; the resulting torsion angles were within 4 degrees of the crystal structure values. These results provide a comprehensive set of benchmark values for NMR parameters of histidine over a wide pH range and should facilitate the study of functionally important histidines in proteins.