Fig. S5.
Conformational differences between complexes ABC and DEF for (A) receptor, (B) Fab heavy chain, (C) Fab light chain. Deviations in 5-HT2B receptor do not exceed 1.5 Å for the backbone Cα atoms, and 2.5 Å for all nonhydrogen atoms, except for a few residues. Deviations in Fab chains were measured for the ABC and DEF complexes superimposed using the receptor only. Cα rmsd values for Fab residues contacting with the receptor are within 1 Å. Larger rmsd values in other Fab parts are because of an ∼4° tilt between Fabs in ABC and DEF complexes.