Simple and convenient method of protein dynamics evaluation from the insufficient experimental ¹⁵N relaxation data is presented basing on the ratios, products, and differences of longitudinal and transverse ¹⁵N relaxation rates obtained at a single magnetic field. Firstly, the proposed approach allows evaluating overall tumbling correlation time (nanosecond time scale). Next, local parameters of the model-free approach characterizing local mobility of backbone amide N–H vectors on two different time scales, S² and R_ex, can be elucidated. The generalized order parameter, S², describes motions on the time scale faster than the overall tumbling correlation time (pico- to nanoseconds), while the chemical exchange term, R_ex, identifies processes slower than the overall tumbling correlation time (micro- to milliseconds). Advantages and disadvantages of different methods of data handling are thoroughly discussed.