In both cases, the two Ror2 TKD molecules form an antiparallel dimer, burying a total surface area of 1725 Å (our structure) and 2640 Å (3ZZW) on the two TKDs.
The extensive interaction between MCM2 and H3-H4 buries a total surface area of 1918 Å2.
The packing buries a total surface area of 1 007 Å, which indicates a moderate binding affinity between the two eTud modules.
The interface buries a total surface of approximately 2300 Å (calculated using CNS with probe radius of 1.5 Å; Brunger et al, 1998).
The contact interface encompasses six protein segments, including residues 53 59, 177 179, 276 305, 449 466, 509 519 and 584 596, that buries a total surface area of 4330 Å on each monomer.
A detailed examination of the Crm1 dimer reveals an extensive interface that buries a total surface area of 2170 Å in the crystal structure and corresponds to functionally important residues.
The interactions are dominantly hydrophobic that bury a total of solvent accessible surface area of 2664 Å.
With nearly half of the PER2 residues involved in binding, the two proteins bury a total 2800 Å of solvent accessible surface area at the interface, which stretches over a distance of more than 215 Å.
The dimer interface is formed by the juxtamembrane helix and one side of the GAP domain, burying a total of ∼3200 Å surface area.
For example, monomer A interacts extensively with monomers B and C in anti-parallel which buries a total of solvent accessible surface area of 1880 Å and 1692 Å, respectively, and interacts with monomer D through their C-terminal regions in parallel which buries a total of solvent accessible surface area of 490 Å.
