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).