To further utilize the possibility to rapidly extract magnetic field-independent descriptors of molecular dynamics from experimental spin relaxation data, we use the linear approximation to calculate total effective correlation times for all proteins from the BMBR database () that have experimental R2 values available in four different magnetic fields, see Figure . Effective correlation times calculated from different magnetic fields are generally in good agreement with each others, particularly with higher fields and lower effective correlation time values. This can be explained by the increased experimental resolution in higher fields and the higher sensitivity of R2 values to small errors in T2 (inverse of R2) with slow dynamics (i.e. small T2 leading to large R2). However, inconsistencies between magnetic fields are observed in some cases. For example, C. symbiosum archaeal parvulin, CsPinA (BMRB 18864) exhibit inconsistencies for some residues between 400 MHz and 600 MHz, 400 MHz and 700 MHz, 600 MHz and 700 MHz, and 500 MHz and 700 MHz. These may arise from inaccuracies in spin relaxation measurements or the influence of chemical exchange, Rex, to R2 values .