The precision of a protein structure determined by NMR spectroscopy is strongly influenced by the number of longrange NOE interactions per residue. Aromatic and methylcontaining residues are frequently located in the hydrophobic interior of proteins and yield long-range NOE interactions. Methyl groups have become the major focus in the structure determination of large proteins in recent years. [1] On the other hand, aromatic groups have not received equal attention because their sequence-specific assignment is extremely difficult, especially for proteins larger than 25 kDa. In cases in which aromatic proton resonances are well dispersed and the protein is small, assignments can be made on the basis of 2D NOESY experiments (linking resonances between aromatic protons and side-chain a and/or b protons) and 2D COSY-type experiments (linking resonances within the ring). [2] When the chemical shifts of H atoms are degenerate and hence assignment is ambiguous, 13 C-edited experiments allow ambiguities to be resolved through better dispersion of 13 C spins. In all these 13 C-edited experiments, aromatic protons correlate with aliphatic protons and/or carbon atoms through a multiple-relay or TOCSY scheme. [3] These experiments may fail for larger proteins owing to increased decay of magnetization during the lengthy transfer steps. To improve the sensitivity, a suite of experiments with fewer transfer steps that correlate C g with either H b or aromatic protons in two sets of spectra was proposed. [4] With these experiments, about 70 % of the aromatic protons of the Phe and Tyr residues in F. solani pisi cutinase ( % 22 kDa with 1 His, 6 Phe, 1 Trp, and