The bulk thermodynamic properties of proteins originate from a varied and complex combination ofinteractions. We propose a simple model for the formation of ordered two-dimensional aggregates basedon the interactions between pairs of annexin V molecules. Simulations of this model are shown to reproducethe experimental observations of a honeycomb (p6) and a triangular (p3) crystalline phase. The simulationsindicate that the transition between these two phases is first order. While this model is extremely simplein that it relies only on hard body and short-range directional interactions, it nevertheless captures theessential physics of the interactions between the protein molecules and reproduces the phase behaviorobserved in electron microscopy and atomic force microscopy experiments.