To understand how a protein functions, it is essential to know the three-dimensional structure of the protein to atomic resolution. Multidimensional nuclear magnetic resonance (NMR) techniques provide one method for solving atomic resolution protein structures. These techniques have been applied to the 126-residue protein domain, villin 14T. The most challenging step is assigning each resonance line in the NMR spectrum to the correct proton within the protein. For villin 14T, this sequential assignment step was accomplished with triple-resonance, backbone-directed strategies. The structure reveals a unique fold shared only by domains from other proteins in the actin-severing family.