Knowledge about protein dynamics is crucial for the understanding of protein function.[1] NMR spectroscopy can characterize the amplitudes and rates of motions that are either faster than the rotational correlation time tc (sub-tc motion) with heteronuclear relaxation experiments or between approximately 50 μs and 10ms (μs/ms motion) with relaxation dispersion.[2, 3] The extent of motions occurring in folded proteins on the time scale between the rotational correlation time tc and the μs/ms range (supra-tc motion) has been a matter of debate.[4] However, the functional relevance of such motions has recently been shown for the aggregation rate of natively unfolded proteins involved in neurodegenerative diseases.[5] Very recently, motions on this supra-tc time scale have been observed in a 0.2 μs molecular dynamics simulation of ubiquitin.[6] Residual dipolar couplings (rdcs) were recognized early on as an ideal tool to widen the time window of dynamics that can be characterized by NMR spectroscopy, since they are sensitive to motional averaging occurring over the sub-and supra-tc time scales (ps to ms).[4] We recently analyzed NH rdcs of ubiquitin measured in 31 different alignment conditions and derived the order parameters