Fig. 2
The consensus sequence-based ConM SOSIP.v7 trimer shares structural similarity to other Env structures. a Crystal structure of ConM SOSIP.v7 trimer (gp120 green, gp41 blue) in complex with Fabs PGT124 (cyan) and 35O22 (orange) at 3.9 Å resolution. For clarity, two other ConM SOSIP.v7 protomers are represented as white surface and mesh. b Superimposition of the soluble ConM SOSIP.v7 monomer (gp120 green, gp41 blue), clade A BG505 SOSIP.664 (PDB: 5CEZ), clade B JRFL Env ΔCT (PDB: 5FUU), clade C 16055 NFL TD CC (PDB: 5UM8), and clade G X1193.c1 SOSIP.664 (PDB: 5FYJ). c Comparison of rarer amino acid residues of ConM and BG505. After analyzing amino acid conservation for each residue among all the HIV-1 envelope glycoprotein sequences (n = 6112) available from the Los Alamos HIV database 2017, amino acid residues in ConM and BG505 that are rarer than equipositional residues in BG505 and ConM, respectively, are represented in red. There are 14 and 51 rarer residues in each ConM and BG505 protomer, respectively. d Visualization of the glycan shield of ConM Env, containing no glycan holes (top), and the prototypic BG505 Env, which contains the 241/289 glycan hole (bottom). Glycan shields were modeled using the Glycan Shield Mapping tool42
