Figure 1.
Figure 1. (A) A ribbon representation of the fold of the
Npun_R1517 monomer. The elements of secondary structure are
indicated, as well as the position of the N- and C-termini. (B)
A ribbon representation of the homodimer of Npun_R1517 looking
down onto the two symmetry-related 2
helices. The dimer is formed by a symmetry operation belonging
to the P4[3]2[1]2 space group as described in the text. (C) The
same dimer as shown in (B) rotated by 90° along the long
axis of the dimer. All hydrophobic residues including L, I, V,
and F are represented as sticks to illustrated how the
hydrophobic core is formed between each 2
helix and hydrophobic residues from -strands
of both chains, as described in the text. (D) A zoomed-in
illustration of the position of the nest residues, E51, G52, and
S53 (represented as sticks color-coded by atom type), as well as
the location of the R84 and R86 (represented as sticks colored
red).
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
74,
794-798)
copyright 2009.
2
helices. The dimer is formed by a symmetry operation belonging
to the P4[3]2[1]2 space group as described in the text. (C) The
same dimer as shown in (B) rotated by 90° along the long
axis of the dimer. All hydrophobic residues including L, I, V,
and F are represented as sticks to illustrated how the
hydrophobic core is formed between each 
-strands
of both chains, as described in the text. (D) A zoomed-in
illustration of the position of the nest residues, E51, G52, and
S53 (represented as sticks color-coded by atom type), as well as
the location of the R84 and R86 (represented as sticks colored
red).