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. 2007 Nov 27;104(49):19547–19552. doi: 10.1073/pnas.0708946104

Fig. 1.

Fig. 1.

Diagram of P2 configuration predicted from primary amino acid analysis. (A) Structural features and domains of P2 identified by using computer-assisted programs. (B) Helical wheel representation of amino acids 26–43 of P2. Each panel represents an α-helix viewed along the helix axis with the indicated amino acid residues. The P2 sequence was searched for the presence of amphipathic structures initially by using the program Moment of the GCG software package. The program Helical Wheel was then used to plot a helical wheel representation of the N-terminal amino acids of P2. (C) Transmembrane domain prediction of P2 using PSORT version 6.4 (WWW). Amino acids 802–818 surrounded with solid line have a high possibility to be a transmembrane domain. (D and E) LearnCoil-VMF detects two HR regions in P2 (D), and sequence analysis shows these two regions contain additional leucine zipper motifs (E).