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. Author manuscript; available in PMC: 2016 Jan 6.
Published in final edited form as: Structure. 2014 Dec 24;23(1):237–247. doi: 10.1016/j.str.2014.11.009

Figure 5. Design and results of the restrained simulations.

Figure 5

(A) Pin1 as a tripartite molecule, with its three modules, the WW domain, the PPIase core, and the α1-α2 appendage, shown in green, blue, and red, respectively. Left: 3-dimensioanl structure; right: schematic representation.

(B) Four sets of intra-module (shown as Cα spheres in single color) and inter-module (shown as Cα spheres in mixed color) restraints. The restrained residues are: WW, residues 6-34; β4β7, residues 55-62 and 156-161; interface(PPI), residues 86, 87, 90, 91, 93, 94, 97, 136-138, 140-142, and 145-151; interface(Pin1), all interface(PPI) residues and residues 28-31.

(C,D) The Cα RMSFs of the four restrained simulations, compared to those of the unrestrained apo Pin1 simulation.