Calcium-Mediated Control of S100 Proteins: Allosteric Communication

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Addition/Correction Cite This: J. Am. Chem. Soc. XXXX, XXX, XXX−XXX

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Correction to “Calcium-Mediated Control of S100 Proteins: Allosteric Communication via an Agitator/Signal Blocking Mechanism” Yiming Xiao, Gary S. Shaw, and Lars Konermann*

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J. Am. Chem. Soc. 2017, 139, 11460−11470. DOI: 10.1021/jacs.7b04380 Page 11464. Panels (o) and (u) of Figure 4 did not cover the complete time range of interest. All statements made in the text refer to the correct axis scaling. This correction does not alter any of the results or conclusions of the paper. The corrected Figure 4 is shown below.

Figure 4. (a) 1 μs MD structure of [Ca4 S100]. Exposed nonpolar residues in the target binding site are highlighted in red. (b) 1 μs MD structure of apo-S100. (c) Atoms used for tracking protein conformational dynamics. (d−i) Atom distances for [Ca4 S100]. Panels (j−o) and (p−u) display two apo-S100 runs. Dashed lines indicate target binding site closing midpoint (panels n, t).

© XXXX American Chemical Society

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DOI: 10.1021/jacs.8b06612 J. Am. Chem. Soc. XXXX, XXX, XXX−XXX