Correction for Yanaka et al., Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches

Fig. 5. MD simulations of galactosyl and nongalactosyl Fc glycoforms.(A) The superposition of 256 structures extracted every 100 ns from the MD trajectory.The structures were visualized by PyMOL (https://www.pymol.org).IgG1-Fc polypeptide chains are shown in yellow (C H 2) and gray (C H 3), and the glycan residues are shown in blue except for galactose resides (magenta).(B) The RMSF for each amino acid C atom of IgG1-Fc for FG0 (black) and FG2 (red) are shown.(C)Pairs of contact residues found within 4 in the ensemble model derived from the MD simulation are connected by different types of line segments according to incidence as follows: More than 24,000 pairs (thick solid line), 24,000 to 16,000 pairs (thin solid line), and 16,000 to 8,000 pairs (dashed line).The amino acid residues that exhibited chemical shift perturbations are highlighted using the same color scheme as in Fig. 4B.(D) RMSF for sugar residues of N-glycans of FG0 (black) and FG2 (red) are shown.(E) Distribution of intrachain domain-orientation angles between C H 2 and C H 3 (defined by C atoms of Y300, M428, and Q362) for the ensemble models of IgG1-Fc are shown.The angles between the C H 2 and C H 3 domains of chain A and chain B were plotted on the X axis and Y axis, respectively.