As a RDC provides spatially and temporally averaged information about an angle between the external magnetic field and a bond vector in a molecule, it may provide rich geometrical information about dynamics on a slow timescale (>10 s) in proteins. In particular, due to its radial dependence the RDC is in particular sensitive to large-amplitude angular processes  An early example by Tolman et al. found previously published structures of myoglobin insufficient to explain measured RDC data, and devised a simple model of slow dynamics to remedy this. However, for many classes of proteins, including intrinsically disordered proteins, analysis of RDCs becomes more involved, as defining an alignment frame is not trivial. The problem can be addressed by circumventing the necessity of explicitly defining the alignment frame.