The peptide is enriched in polar residue such as Asparagine (Asn) and Threonine (Thr), negatively charged Aspartic acid (Asp), and positively charged large-sized Arginine (Arg) and Lysine (Lys), and with a few Prolines (Pro) distributed along the C-terminal half of the peptide. Experimental observations indicate that in vitro DHH1N does not undergo LLPS on its own at physiological pH, despite its composition is characteristic of low complexity domains involved in LLPS, and the fact that it participates in the formation of molecular adhesives to promote LLPS of chimera proteins . In this work, we investigate a relatively short IDP that does not undergo phase separation, demonstrating how information from multiple sampling algorithms and forcefields reveal a detailed and congruent multi-dimensional FES within microsecond timescales.