To examine the dynamic information produced by the SBMOpenMM library, we tested the code in a dataset of 110 single-chain protein structures (Table ). The dataset is structurally diverse, representing a range of protein sizes and topologies (Figure ). Several simulations were carried out to estimate the temperatures at which the folding transitions (T f ) occur. Dynamic profiles (calculated as root-mean-square fluctuations) at different relative temperatures were compared to the corresponding crystallographic temperature factors to determine correlation values (Figure ). At temperatures lower than the T f , average correlations are high (0.66); however, they start to decrease significantly at temperatures above 0.85T f . At temperatures above the T f , the systems are mainly unfolded (Figure ), and correlations decrease significantly (see Section S-III for details on the simulations, dataset compilation, and further discussion). This result shows that SBMOpenMM can produce dynamic profiles with good correlations to experimental information for studying folded configurations and consistent behavior for studying folded to unfolded transitions in protein systems.