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. Author manuscript; available in PMC: 2012 Feb 1.
Published in final edited form as: Nat Chem Biol. 2011 Jul 3;7(8):531–537. doi: 10.1038/nchembio.598

Figure 3.

Figure 3

. NMR analysis of FKBP and the LID domain. 1H/15N HSQC spectra of (a) FKBP (red) compared to LID (cyan), (b) FKBP (red) compared to FKBP bound to Shield-1 (orange), and (c) FKBP bound to Shield-1 (orange) compared to LID bound to Shield-1 (blue). (d) Relative chemical shift perturbations of FKBP compared to LID (blue bars) as well as FKBP compared to the FKBP•Shield-1 complex (red bars). Residues that could not be assigned in the HSQC-spectra are indicated with negative bars. (e) Chemical shift perturbations mapped onto the structure of FKBP complexed with a Shield-1 analog (PDB:1BL4). Residues experiencing significant chemical shift perturbations (δavg/δmax > 0.2) are colored red, moderate perturbations are colored purple (0.1 < δavg/δmax < 0.2), and minor perturbations are shown in blue (δavg/δmax <0.1).