Extended Data Fig. 1: Structural features of ALK-ECRABR.
From: Mechanism for the activation of the anaplastic lymphoma kinase receptor
a, 1H-15N–correlated (left panel) and 1H-13C–correlated (right panel) spectra of [U-2H,15N; Ala-13CH3; Met-13CH3; Ile-δ1-13CH3; Leu,Val-13CH3/13CH3; Thr-13CH3]-labelled ALK-ECRABR. b, 1H-13C–correlated spectra of [U-2H; Phe-δ-13CH; Tyr-ε-13CH]-labelled ALK-ECRABR. c, Select strips from 13C-edited NOESY experiments highlighting intra-domain NOEs between TNF-like and EGF-like. d, Close-up view of the TNF-like−EGF-like interface and close-range inter-proton contacts (within ~7 Å) observed from the NOESY NMR analysis of spectra shown in (c). e, Asymmetric unit content of ALK-ECRABR(ΔEGF) crystals. f, 2Fo-Fc map of ALK-ECRABR(ΔEGF) depicted at 0.951 contour level for chain A. g, B-factors of ALK-ECRABR(ΔEGF) (chain A) are mapped on its structure. The tube radius is proportional to the B-factor. Low-to-high B-factors are also denoted in a blue-to-red colour gradient. h, Topology diagram of ALK-ECRABR(ΔEGF). PGII helices are shown in green tubes, β-strands in arrows and α helices in cylinders. i, Superposition of the following structures: ALK-ECRABR GlyR (grey, this work), glycine rich domain of GTP-binding protein Obg (red, PDB ID 1LNZ), acetophenone carboxylase (blue, PDB ID 5L9W), antifreeze protein (yellow, PDB ID 3BOG), and gp38 bacteriophage adhesin tip (green, PDB ID 6F45). j, Schematic representation of the GlyR PGII array shown in a top view. Solid hexagons denote PGII helices with an N-to-C direction towards the reader whereas open hexagons denote PGII helices in the opposite direction. k, Side view of the GlyR PGII array in ball-and-stick representation. l, Top view of GlyR PGII array showing inter-chain hydrogen bond network (grey dashes). m, Close-up view of the TNF-like−EGF-like interface.
