Figure 4. PCAs of resonances comprising the KD or entire Abl core.

(A) PCA scores of the KD resonances of all complexes shown in Figure 3B. (B) PCA scores of the KD resonances of only type I and type II inhibitor complexes. The respective loadings are shown in Figure 4—figure supplement 1. (C) Residues with absolute PC1 loadings larger than 0.15 for the analysis in panel B are shown as red spheres in the assembled core structure (PDB 2FO0). The P-loop is shown in orange and the A-loop in its active (green, PDB 2FO0) as well as inactive (magenta, PDB 2HYY Cowan-Jacob et al., 2007) conformation. (D) PCA scores of the resonances of the entire Abl core for the apo forms of all αI-helix variants. The respective loadings are shown in Figure 4—figure supplement 1. (E) Residues with absolute PC1 loadings larger than 0.1 of the analysis in panel D are shown as red spheres in the assembled core structure (PDB 2FO0).

Figure 4—figure supplement 1. PCA loadings showing the contributions of the ¹H and ¹⁵N chemical shifts of individual residues to PC1 and PC2.

(A) PCA of all KD chemical shifts of all investigated complexes corresponding to Figure 4A. (B) PCA of KD chemical shifts for type I and type II inhibitor complexes (Figure 4B and C). Residues with absolute PC1 values larger than 0.15 are indicated in red. (C) PCA of all SH3SH2KD shifts of all apo forms (Figure 4D and E). Residues with sizeable absolute PC1 values larger than 0.1 or sizeable PC2 (< -0.1 or > 0.125) are indicated in red and blue, respectively. V151, N316, and K438 have both sizeable PC1 and PC2 and is shown in magenta.