Data associated with the publication: Global protein dynamics as communication sensors in peptide synthetase domains

Data accompanying “Global protein dynamics as communication sensors in peptide synthetase domains.” The data was used to demonstrate the function of protein dynamics in molecular recognition and allostery. We used the Yersiniabactin Synthetase cyclization domain Cy1 as a model system and predominantly employed NMR. The data was used to determine the solution structure of Cy1. For wild-type and the mutant D391N, the data was used to monitor the molecular response of Cy1 when presented to its partner carrier protein ArCP as ArCP is modified from holo to substrate-loaded form. Other data was used to describe Cy1 dynamics through relaxation dispersion and Hahn-Echo, assess its stability through thermal melts, and compare Cy1 wild-type and mutant data. (2024-06)