Extended Data Fig. 8: Lowest energy docking model of phospho-peptide interacting with VSP.

a, Molecular docking of PTEN phosphorylated C-tail (aa 353–403) with VSP (PDB:3V0G) showing the lowest energy model. For VSP structure: Cα2 segment in cyan, CBRIII loop in green, active site P-loop in red, and site of previous determined crosslinking in yellow. For phosphorylated C-tail, the black region represents segment of tail not used in NMR experiments whereas magenta is the phospho-cluster, dark blue is the second acidic patch spanning residues 386–390, and orange is the third acidic patch spanning residues 391–394. b, Surface representation of VSP and tetra-phosphorylated PTEN C-tail from HADDOCK model colored as electrostatic potential showing complementarity of the surfaces for binding. Basic surfaces in blue, neutral in white, and acidic in red. c, Residues in the Cα2 segment including Lys553, Lys555 and Lys558 which correspond to Lys330, Lys332 and Arg335 in PTEN that are important for tail binding from Haddock model, respectively (PDB:3V0G). d, Residues in the catalytic domain including Lys364 and Lys367 which correspond to Lys125 and Lys128 in PTEN that are important for tail binding, respectively.