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. Author manuscript; available in PMC: 2013 Apr 24.
Published in final edited form as: Biochemistry. 2012 Apr 10;51(16):3383–3393. doi: 10.1021/bi300007r

Figure 1.

Figure 1

Chemical shift perturbations observed in 1H,15N TROSY-HSQC spectra upon removal of substrate from reduced and CO-bound CYP101A1 displayed as a function of sequence and secondary structure. Both 1H (orange bars) and 15N (green bars) shifts are shown, so the y-axis value is the sum of perturbations in sec-1 (Hz) observed in both dimensions for a given correlation. Secondary structural features with which perturbed residues are associated are indicated above, with solid arrow representing β structure, zig-zag green lines for helix, and straight blue lines for loop or irregular structure. Secondary structural features are named using the conventions of Poulos et al. (21). The Ax Cys label refers to Cys 357 and Leu 358.