Fig. 12

3D models of wildtype and mutated tubulin molecules. a. Superimposition of wildtype (blue) and Tubb2b ^p.A248V (red) models. The alanine residue is rendered with Van der Waals radii (green, gray arrows). Models generated with different modeling algorithms are indicated. b. Structural comparison between wildtype (blue) and Tubb2b ^p.R380L (red) models. The arginine residue rendered with Van der Waals radii (green, gray arrows). Graphical representation of algorithm scores. c. Absolute values of algorithm scores obtained from pairs; negative control (left, light gray; score: 2.129), wildtype against Tubb2b ^p.A248V (middle, light gray; score: 2.485) and wildtype against Tubb2b ^p.R380L (right, light gray; score: 3.721). For comparison, algorithm scores generated using models from PHYRE2 is also indicated. Like black bars, these are raw MODICT scores generated without conservation and weight parameters. d. Sequence logo of conserved Tubb2b regions. Residues 91-100 and 139-144 of Tubb2b have been conserved since their divergence from the FtsZ proteins. Consequently, during algorithm calculations they have received a weight score of 20 instead of default value. Scores with/without conservation or weight attributes are indicated in C. MODICT scores were generated taking into account the entire backbone (residues 1-445,UNIPROT, Q9BVA1). (W = wildtype, W ^R = refined wildtype, c = conservation, w = weight score)