Rotational dynamics of individual residues in proteins can be probed using nuclear magnetic resonance (NMR) experiments that detect spin relaxation rates, R1, R2 and heteronuclear Overhauser effect (hetNOE), of backbone N atoms. For folded proteins, residual dynamics can be described by order parameters and timescales representing internal and overall motions, which can be then solved from experimental spin relaxation rates using so called Lipari-Szabo approach . However, the dynamics of proteins with disordered regions or peptides in complex biomolecular environments cannot be described by just a few parameters, thus interpretation of their dynamics requires molecular dynamics (MD) simulations or other elaborate models . Interpretation of protein or peptide rotational dynamics from NMR experiments is usually based on Redfield equations that relate the spin relaxation rates to molecular dynamics