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. Author manuscript; available in PMC: 2012 Dec 3.
Published in final edited form as: Nat Struct Mol Biol. 2011 Feb 13;18(4):463–470. doi: 10.1038/nsmb.2018

Figure 3.

Figure 3

Heteronuclear NMR spectroscopy used to map the C3d and dp8 binding sites on FH19–20. (a) The percentage broadening observed for unequivocally assigned backbone amides upon addition of C3d is indicated: Red bars signify > 90% broadening; white bars indicate proline residues; and grey bars indicate residues whose assignments were missing or whose intensities were weak in free FH19–20. (b) Amides which experience a line-broadening > 90% are schematically shown as red spheres on the structure of FH19–20 (2G7I). The sizes of the spheres have been adjusted to correlate with the degree of line-broadening that each amide cross-peak experiences: Larger spheres represent complete disappearance of the signal; smaller spheres represent signals broadened by > 90% but which are still detectable. (c) Combined amide chemical shift changes upon addition of 8.5-fold excess of dp8. Blue bars indicate shift changes larger than the threshold (double the average shift change; corresponding residues mapped onto the structure of FH19–20 in Fig. 5d), white and grey bar have the same meaning as in (a).