Figure 6.
Figure 6. Polypeptide chain tracing errors that were corrected by examination of the AlphaFold2 (group 427) structure. (A) The incorrect model in the vicinity of two neighboring proline residues (Pro236 and Pro239) together with the associated difference electron density map with the coefficient 2Fo-Fccolored blue (left) and the model corrected based on the AlphaFold2 predicted structure with the associated 2Fo-Fc difference electron density map (right). The cis bond conformations are highlighted in green (B) The incorrect placement of Ile247 with the associated 2Fo-Fc difference electron density map colored blue and the Fo-Fc difference electron density map colored green (left). Correcting the positions of Pro236 and Pro239 allowed placement of Tyr249 instead of Ile247 and eliminated the residual Fo-Fc difference electron density (right).