Erratum: correction: Enabling the chemistry of life

Abstract

regions. Amino-acid side chains exhibiting weak electron density were built with steric and geometric constraints. We generated the ®gures with GRASP, Molscript and Raster3D. Structural comparisonsWe carried out structural comparisons against 251 Fab and 11 abTCR models. Superpositions were performed using LSQMAN 28. The inter-domain, intra-chain angles (for instance Vg±Cg) were calculated as the supplement of the rotation angle necessary for superposition of the conserved a-carbon atoms of the B and F strands of each domain. Because the Vg±Vd interface involves the A9GFCC9C0 b-sheet whereas the Cg±Cd interface involves the ABED b-sheet (Fig. 1), V domain strands B and F were explicitly superimposed onto C domain strands F and B. The elbow angle between the V and C domains was calculated as the angle between the pseudo-dyads, described by direction cosines, which result from a superposition of V or C domains. Buried interfaces were calculated with CNS using a probe radius of 1.4 A Ê . Structures of abTCRs and Fabs are referred to by their Protein Data Bank identi®cation codes