Structural Basis for the Recognition of Human Cytomegalovirus Glycoprotein B by a Neutralizing Human Antibody
Figure 6
Conformational flexibility of SM5-1 and SM5-1*.
(A) Plot of the root mean square fluctuations (RMSF) per residue indicating the enhanced flexibility of residues 102–112 (CDR H3) in SM5-1* (red line) compared to SM5-1 (black line). Sequence positions that differ between SM5-1 and SM5-1* are marked by a yellow asterisk. (B, C) Overlay of 6 structures collected every 20 ns over the simulation time for SM5-1 (B) and SM5-1* (C). Note that the CDR H3 loop in SM5-1* exhibits a higher flexibility and deviates further from the Dom-II-bound conformation which served as starting structure. The six residues that are different between SM5-1 and SM5-1* are shown in stick presentation and a pink arrow points towards the CDR H3 loop.