  The equilibrium free energy landscape of an off-lattice model protein as a
function of an internal (reaction) coordinate is reconstructed from
out-of-equilibrium mechanical unfolding manipulations. This task is
accomplished via two independent methods: by employing an extended version of
the Jarzynski equality (EJE) and the protein inherent structures (ISs). In a
range of temperatures around the ``folding transition'' we find a good
quantitative agreement between the free energies obtained via EJE and IS
approaches. This indicates that the two methodologies are consistent and able
to reproduce equilibrium properties of the examined system. Moreover, for the
studied model the structural transitions induced by pulling can be related to
thermodynamical aspects of folding.
