Figure S5.
Interactions at the BG505 SOSIP-7-269 Fab interface. (A–D) Potential hydrogen bonds formed at the interface of the BG505 SOSIP-7-269 IgA Fab complex. The table in A indicates the atoms involved in forming potential hydrogen bonds at the complex interface and the distance between them. This information is also represented in B–D, where the electron density in which the glycans were built is also shown. (E) Stick representation of residues forming Van der Waals contacts between 7-269 and the gp120 protein subunit. The disulfide bond between C105 and C110 in the CDRH3 is also represented as sticks. For better clarity, glycans are not shown.

Interactions at the BG505 SOSIP-7-269 Fab interface. (A–D) Potential hydrogen bonds formed at the interface of the BG505 SOSIP-7-269 IgA Fab complex. The table in A indicates the atoms involved in forming potential hydrogen bonds at the complex interface and the distance between them. This information is also represented in B–D, where the electron density in which the glycans were built is also shown. (E) Stick representation of residues forming Van der Waals contacts between 7-269 and the gp120 protein subunit. The disulfide bond between C105 and C110 in the CDRH3 is also represented as sticks. For better clarity, glycans are not shown.

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