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Focal adhesion kinase (FAK) is a tyrosine kinase associated to focal adhesions with a downstream effect on cell migration and other important biological functions. The phospholipid PI(4,5)P2 is known as a moderator for FAK activation. PI(4,5)P2 induces clustering of FAK molecules, but the impact of clustering on the protein conformation of FAK is still not understood. Since an overexpression of FAK is associated with invasive tumours, insights into the clustering process could give rise to new cancer treatments. In previous studies, coarse-grained MD simulations led to an unnatural falling of FAK on the membrane. During the course of this project, we were able to rule out an underestimation of the binding strength of FAK to PI(4,5)P2 as the cause using umbrella simulations. Because the exact reason for FAK falling could not be identified, we introduced a stabilising force acting on the FERM domain of FAK. With this approach, we obtain reasonable results for FAK bound to PI(4,5)P2 as well as for multiple FAK interactions. Our observations indicate that FAK arranges into chain-like clusters. However, we do not observe FAK activation upon clustering within the time-scale of our simulations.