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. 2013 Apr 17;110(18):7136–7141. doi: 10.1073/pnas.1302378110

Fig. 3.

Fig. 3.

Protein–protein interaction between the FMN-binding domain of Ndor1 and [2Fe-2S]-anamorsin as characterized by NMR. (A) TROSY 1H-15N HSQC at 308 K, acquired at 900 MHz, of the 15N-labeled oxidized FMN domain (construct 1–174 aa) before (red) and after (black) the addition of 1 eq of unlabeled oxidized [2Fe-2S]-anamorsin. (B) Overlay of 1H-15N HSQC spectra of 15N-labeled oxidized FMN-binding domain at 298 K, acquired at 800 MHz, before (black) and after (red) addition of 1 eq of [2Fe-2S]-CIAPIN1-single. (Inset) Chemical shift variations of selected FMN-binding domain residues upon addition of increasing amounts of [2Fe-2S]-CIAPIN1-single (0%, 50%, and 100%).