Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains

Dataset corresponding to the manuscript Loop Plasticity Drives Paralog-Specific Recognition in BET ET Domains. The bromodomain and extraterminal domain (BET) family of proteins recognizes diverse peptide motifs through their conserved ET domains, yet exhibits paralog-specific binding preferences. In this study, we use extensive molecular dynamics simulations to investigate how known peptide epitopes binders interacts with the ET domain of the paralogs BRD3 and BRD4. Data content in the .zip files: Molecular Dynamic trajectories (dry): Contains the concatenated triplicates for the 14 systems initially studied, saved each 15 frames for storage purposes, in .xtc format. Representative structures: Includes .pdb files that correspond to centroids obtained by PCA-based clustering analysis for the six systems under detail study. Namely, BRD3-ET and BRD4-ET in their unboud forms and in their bounded forms with TP and NSD3 peptide.