  The distribution of inequivalent geometries occurring during self-assembly of
the major capsid protein in thermodynamic equilibrium is determined based on a
master equation approach. These results are implemented to characterize the
assembly of SV40 virus and to obtain information on the putative pathways
controlling the progressive build-up of the SV40 capsid. The experimental
testability of the predictions is assessed and an analysis of the geometries of
the assembly intermediates on the dominant pathways is used to identify targets
for antiviral drug design.
