  Intrinsically disordered proteins participate in many biological processes by
folding upon binding with other proteins. However, coupled folding and binding
processes are not well understood from an atomistic point of view. One of the
main questions is whether folding occurs prior to or after binding. Here we use
a novel unbiased high-throughput adaptive sampling approach to reconstruct the
binding and folding between the disordered transactivation domain of
\mbox{c-Myb} and the KIX domain of the CREB-binding protein. The reconstructed
long-term dynamical process highlights the binding of a short stretch of amino
acids on \mbox{c-Myb} as a folded $\alpha$-helix. Leucine residues, specially
Leu298 to Leu302, establish initial native contacts that prime the binding and
folding of the rest of the peptide, with a mixture of conformational selection
on the N-terminal region with an induced fit of the C-terminal.
