 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 7]](wd5140fig7mag.jpg)
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Figure 7
Surface packing along the polypeptide chain of TM1081. (a) Plots versus the amino-acid sequence of the per-residue occluded surface packing (OSP, a dimensionless quantity covering the range from 0.0 to 1.0; Pattabiraman et al., 1995  ) for the NMR (red), crystal (blue), reference NMR (green) and reference crystal (black) structures. For the NMR structure and the two reference structures, the OSP values for the conformer closest to the mean atom coordinates of the bundles are shown. At the top, the locations of the regular secondary structures are indicated and asterisks identify the residues with solvent accessibility below 15% in the NMR structure. (b) Plot versus the amino-acid sequence of the mean per-residue OSP values in the NMR structure and the standard deviations among the 20 NMR conformers. Shading indentifies the conserved residues in anti-σ factor antagonists, as in Fig. 9(b). |
![[Figure 7]](wd5140fig7.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
