Conformational variability of matrix metalloproteinases: Beyond a single 3D structure

Bertini et al. 10.1073/pnas.0407106102.

Supporting Information

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Supporting Table 1
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Supporting Figure 4
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Supporting Figure 4

Fig. 4. ¹⁵N relaxation data for the MMP12-NNGH adduct measured at 700 MHz ¹H frequency, 298 K: R₁ (A), R₂ (B), R₁/R₂ (C), and NOE (D). The slight systematic inflation of the NOE ratios is possibly ascribed to a nonperfect recovery of the water signal for the unsaturated reference spectra under a relaxation delay of 3 s (1) and has no consequence on the qualitative conclusions on subnanosecond mobility.

1. Renner, C., Schleicher, M., Moroder, L. & Holak, T. A. (2002) J. Biomed. NMR 23, 23-33.

Supporting Figure 5

Fig. 5. Group-averaged temperature factors for different x-ray structures of MMP12 with various active site ligands and structure resolutions: AHA, 1.0 Å (A); batimastat, 1.2 Å (PDB ID code 1JK3) (B); NNGH, 1.3 Å (C); Met-105/AHA, 2.1 Å (PDB ID code 1OS2) (D-F); and Met-105/H₂O, 1.8 Å (PDB ID code 1OS9) (G-I). In C the residues showing ¹⁵N NOEs below the average (outside the experimental error) are indicated by vertical bars.

Supporting Figure 6

Fig. 6. Difference (D ) between calculated and experimental RDC absolute values. The error bars represent the standard deviation of the values calculated for the different structures in the family with respect to an average value. Residues for which NH signal splitting is observed are not reported in the histogram.