Fig. 6: Comparison of hydrophobic interaction in HCDR2, HCDR3, and LCDR3 among 047-09_4F04, 241_2F04, 346-54, and SFV009_3G01 in complex with CA04 H1 HA.
CA04 HA is shown with white for HA1 and gray for HA2. a Residues involved in hydrophobic interactions from the CDR loops are represented in sticks and labeled. A pi-pi interaction is shown as blue dashes. b Key residues involved in the interaction between HCDR3 and upper and middle hydrophobic pockets in HA are indicated as sticks on CDR backbone tubes. c Binding affinity of each Fab with alanine substitutions for residues interacting with upper hydrophobic pocket in HA. +++++, KD < 1 nM; ++++, KD = 1-10 nM; +++ KD = 10-100 nM; ++, KD = 100-1000 nM; +, KD = > 1000 nM; -, No binding; gray background, residues not involved in HA interaction. These data are related to Supplementary Fig. 4. Sensorgrams for binding are shown in Supplementary Figs. 11–14.
