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Fig. S1. Multiple sequence alignment of human S100 proteins. The secondary structure of S100A2 is indicated below. The Ca 2+ -coordinating residues are highlighted in red (coordination by side chains) and magenta (by backbone carbonyl). Hydrophobic residues at the dimer interface are highlighted in green. All sequences were obtained from the SWISS-PROT protein sequence database [2].

Table S1. Data collection and refinement statistics.

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