Structural model of full-length rat Sryα protein. A) The modeled C-terminal end containing the Q-rich region of Sryα showing the electrostatic surface as determined with Poisson-Boltzmann Solver (blue is positive charge and red is negative charge). The model was rotated 90° on the Y-axis for four views yielding a 360° structural analysis. The model had a quality score (z-score) of −1.564 as determined with the YASARA2 force field (anything greater than −2 is considered a fair model), and contains no wrong isomers or cis-peptide bonds. B) Ribbon view of the structure of the C-terminal segment (as seen in the left most image in A) added to the HMG box of Sryα bound to DNA (cyan). Amino acid variations between the multiple rat Sry loci falling outside the HMG box are shown in red with the rat numbering system used (Figure 2).