Fig. 1: High-quality methyl TROSY NMR spectrum and sequence-specific isoleucine δ1-methyl chemical shift assignments of non-polymerizable (DVD) G-actin.
From: Bound nucleotide can control the dynamic architecture of monomeric actin
a, Cartoon representation of TEV protease cleavable, (His)6-tagged DVD G-actin fused with thymosin β4. aa, amino acid. b, δ1 13C-methyl labeling of isoleucine in P. pastoris using precursor α-ketobutyrate (4-13C-3,3-D2) (Methods). c, Ribbon diagram of G-actin (PDB 2HF4) showing isoleucine residues as black spheres. Elements of actin are colored as follows: SD1, cyan; SD2, magenta; SD3, yellow; SD4, corn blue; P1 and P2 nucleotide binding loops, red; sensor loop, blue; hydrophobic plug, green; WH2 binding motif in the hydrophobic groove, violet. Sites in SD3 mutated to block polymerization (D286A/V287A/D288A) are shown as red spheres. d, 1H/13C methyl TROSY NMR spectrum of perdeuterated, 1H/13C-Ile δ1-methyl-labeled G-actin showing assigned isoleucine residues (Extended Data Fig. 1).
