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With the exception of R247eIF4AI and T328eIF4AI/II, all the hippuristanol binding residues are present in murine eIF4AI, eIF4AII, and the yeast eIF4A homolog Tif1/2p (Fig. S1).
All conserved catalytic and heme binding residues are present in LlonKat1 sequence, suggesting a full catalytic activity, and the presence of residues Leu298, Met349 indicate that His70 is above the ring III of the heme molecule (His-III orientation), as seen in other clade 3 catalases [41].
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In all these identified proteins, multiple cysteine residues are present for arsenic binding.
Similarly, correlation spectra of His side chains Hε/δ, Nε/δ (∼160 200 ppm in the N dimension) can provide information on different protonation states of the imidazole rings, particularly useful especially in cases when these residues are present in the binding sites.
The amino acid residues involved in iron (His222, His285, Asp224) and α-KG-binding (Arg295, Ser297), as well as other conserved residues are present within the cF6H sequence.
Nonetheless, the catalytic residues are present.
These residues are presented in Table 1.
The metal binding residues are not conserved.
Here, the metal binding residues are contributed by two subunits.
Government scientists confirmed this week that no pork-related residues were present in Ajinomoto's MSG.
The logarithm of the free binding energy and the binding residues is shown in Table S2 (Supplementary data).
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