Fig. 5: ECHT decompositions of SARS-CoV-2 surface glycoprotein structures (6vxx & 6vyb).
From: A method for intuitively extracting macromolecular dynamics from structural disorder
Atoms are shown 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. Side and top views of trimer for (a–d) the closed state (6vxx), and (e–h) the open state (6vyb). a Deposited structure for 6vxx (2.8 Å resolution; individual i-ADPs, B-factors 3.5–102.4 Å2). b–d Disorder components of each ECHT level (maximum B-factor in brackets): b molecule (32.0 Å2), (c) domain (45.5 Å2), (d) secondary structure (20.7 Å2). (e) Deposited structure for 6vyb (3.2 Å resolution; individual i-ADPs, 16.4–181.1 Å2). f–h Disorder components of each ECHT level (maximum B-factor in brackets): (f) molecule (67.2 Å2), (g) domain (85.3 Å2), (h) secondary structure (44.3 Å2). b, f The molecular components for both structures show similar profiles, with a gradient of disorder across the molecule. c The domain-level disorder reveals hinge-like components for the closed RBDs. g The domain-level disorder reveals conservation of the hinge-like disorder for chain C, but a loss of this component for chain A. Inset images show the disorder for the RBDs only. d, h The secondary-structure level reveals intra-domain flexibility. Images rendered in pymol29.
