Figure 2 - full size

 

Figure 2.
Diagrams of the DUF16 domain of MPN010. (A) A stereo view of a refined electron-density map around a phenyalanine-rich region countered at 1.5[sigma]. The 2Fo-Fc map from finally refined phases was calculated using all reflection data between 20 A and 1.8 A. The figure was generated using the program RIBBONS (Carson 1991). The residues around the phenylalanine-rich region are represented by ball-and-stick models (blue, nitrogen atoms; red, oxygen; green, carbon). The front phenylalanines are Phe75 and the ones below are Phe72. (B) A stereo drawing of a C[alpha] atom trace of the DUF16 domain of MPN010. Each model was colored differently. Every 20th residue is numbered and represented by a dot. The phenylalanine (blue) and glutamine (pink) residues that occupy trimer interfaces are represented by a ball-and-stick model. The figure was generated by MOLSCRIPT (Kraulis 1991). (C) The electrostatic surface potential of the DUF16 domain of MPN010. A molecular surface is created by the program GRASP (red, negative; blue, positive; white, uncharged) (Nicholls et al. 1991). (D) Local coiled-coil parameters plotted against the residue numbers. The gray squares represent a coiled-coil radius and the black diamonds indicate coiled-coil pitch. "SH" and "LH" represent the range of the short and the long helical bundles, respectively. The small arrows indicate the positions showing properties of stutters.

The above figure is reprinted from an Open Access publication published by the Protein Society: Protein Sci (2006, 15, 921-928) copyright 2006.