Nuclear magnetic resonance (NMR) is a powerful probe of relationships between biomolecular function and intramolecular motions. Motions on the μs-ms timescale often coordinate with catalytic events and can be characterized by ¹⁵N spin relaxation using the so-called relaxation-compensated (rc) class of Carr-Purcell-Meiboom-Gill (CPMG) experiments. These measure motional rates from ~100 to 3,000 s^-1 by combining results from the original rcCPMG [Loria, et al, JACS (1999)] with those from related Even-Echo (EE) and Hahn-Echo (HE) experiments [Millet, et al, JACS (2000)]. Each measures the ¹⁵N transverse relaxation rate (R₂) as a function of the repetition rate (ν_CP) of ¹⁵N 180^o pulses during a CPMG relaxation period. Motional rates near ν_CP can yield variation of R₂ with ν_CP, and fits to such profiles reveal the rates and populations of conformational equilibria. Accurate measurement depends on several experimental factors, notably including the suppression of a secondary relaxation effect: cross-relaxation due to interference between the ¹⁵N chemical-shift anisotropy (CSA) and ¹H-¹⁵N dipole-dipole (DD) interaction. The three experiments are each optimized for CSA-DD suppression at different ν_CP values. However, detailed comparison of their suppression quality is lacking, and the validity of their combined application is thus open to question. We determined variations in R₂ collected from these experiments at matching ν_CP values using the enzyme RNase A. Differences in R₂ observed between experiment pairs are consistent with the predicted quality of CSA-DD suppression and are acceptable for subsequent determination of the chemical parameters of exchange.