Fig 8. Significant, distant correlations that involve β-strands as observed in 1N55 and 1KKO.
In 1N55 (A) and 1KKO (B), the red sticks illustrate the correlations with scores within the 95th percentile and between Cα atoms at least 8 Å apart. Examples of a single continuous network of red sticks as shown in 1N55 (C) and 1KKO (D), illustrate the significant correlations implicated on the first β-strand extending to the α-helix via the loop. The yellow spheres show the active site residue positions. The Cα atoms of catalytic residues are represented as yellow spheres, the substrate binding by purple spheres, the phosphate binding by cyan spheres, and the metal ion binding by orange spheres.