Fig. 6: ECHT decomposition of a STEAP4 structure (6hcy).
From: A method for intuitively extracting macromolecular dynamics from structural disorder
Atoms are show as lines and ellipsoids, coloured by B-factor for each structure independently from blue (zero) to green to red (maximum). B-factor ellipsoids are contoured at p = 0.95. a Deposited structure (3.1 Å resolution; one i-ADP per residue; B-factors 55.4–146.7 Å2). b–f Disorder components of each ECHT level (maximum B-factor in brackets): b molecule (44.7 Å2), c domain (65.8 Å2), d secondary structure (51.7 Å2), e residue (28.7 Å2), & (f) atomic (13.8 Å2). The backbone/sidechain level was excluded due to resolution and the group i-ADPs; the atomic level was included to stabilise the optimisation, and has a negligible disorder component (see also Supplementary Table 3). For domain definitions see Supplementary Table 4. b The global disorder component is largely isotropic. c The extracellular domains display increased flexibility relative to the membrane-embedded domains (d) The two outermost transmembrane helices are significantly more disordered than the two inner helices. d, e The loops surrounding the substrate/co-factor binding sites display significant flexibility, which suggest links to function. Images rendered in pymol29.
