Dinámicas y estructuras de la chaperona Hsp90

Additionally, there are ten simulation files corresponding to different systems of the N-terminal domain structure, in which the ATP lid region is in the open conformation. These systems include the native N-terminal domain (NTD-native), the N-terminal domain with tyrosine 56 nitrated and protonated (NTD-nY56prot), and the N-terminal domain with tyrosine 56 nitrated and deprotonated (NTD-nY56deprot). In all these cases, ATP is bound as a ligand.

Finally, there are three additional systems of the N-terminal domain in which ATP is not bound: the native N-terminal domain (NTD-noATP-native), the domain with tyrosine 33 nitrated and protonated (NTD-noATP-nY33prot), and the domain with tyrosine 33 nitrated and deprotonated (NTD-noATP-nY33deprot). Each simulation runs for 1 microsecond and is summarized in 1000 frames. This dataset supports the findings of the article entitled “Nitration-driven structural changes in Hsp90 linked to gain of pathological functions”.