 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 5]](wd5126fig5mag.jpg)
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Figure 5
Surface packing along the polypeptide chain. (a) Plots versus the amino-acid sequence of the per-residue occluded surface packing (OSP, a dimensionless quantity covering the range 0.0–1.0; Pattabiraman et al., 1995  ) for the NMR structure, the crystal structure and the two reference structures of NP_247299.1 (Fig. 2). For the NMR structure and the two reference structures, the OSP value for the conformer closest to the mean atomic coordinates are shown. Color code: NMR structure, red; crystal structure, blue; reference NMR structure, green; reference crystal structure, black. 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 conformers (red). |
![[Figure 5]](wd5126fig5.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
