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. 2025 Aug 14;122(33):e2506491122. doi: 10.1073/pnas.2506491122

Fig. 1.

Fig. 1.

DNA aptamer modification and 3D structure of 1301b_v1–ATP complex. (A) The secondary structure and KD values of the wild-type 1301b (Left) and 1301b_v1 (Right). Residues to be deleted and mutated in the wild-type 1301b are indicated by grey and black rectangular boxes, respectively. The two internal loops are shown in pink. (B) 1D 1H NMR spectra showing G H1 and T H3 signals of 1301b_v1 upon ATP titration. [DNA] = 0.1 mM, [ATP] = 0/0.05/0.1/0.2 mM, [NaPi, pH 7] = 10 mM, [NaCl] = 50 mM, [MgCl2] = 10 mM, 90% H2O/10% D2O, T = 20 °C. (C) The superimposed 10 solution NMR structures of 1301b_v1–ATP complex in different views (PDB ID: 9KTJ). (D) The cartoon mode showing one of the 10 solution NMR structures. (E) The electrostatic potential mapped on the van der Waals surface. (F) Schematic showing the secondary structure of 1301b_v1–ATP complex. Black lines denote Watson–Crick base pairs.