A summary of 11 C-Tpr binding sites on CRM1-RanGTP-Snurportin complex predicted based on our simulations.

Binding sites are sorted according to their position in the amino acid sequence. There are nine binding sites on CRM1 with the total number of 42 residues and two binding sites on Snurportin with the total number of eight residues. In the second column, functional residues predicted by SPPIDER I, salt bridge-making residues, conserved residues, and residues belonging to Snurportin are distinguished by different notations (see below). Moreover, the average interaction energy and RASAS are shown for two simulations in next columns. Notations:Bold face: Residues which were predicted by SPPIDER as functional interfacial amino acids (21 AAs).†Residues which form a salt bridge (19 AAs). The cutoff is set to 3.2 Å.Underlined: Residues which are fully conserved (20 AAs).*Residues from Snurportin.