Representations of Whole Molecule

In protein 2, the two component structures, one red and the other yellow, forming two domains, are packed to form a V shape. The intradomain disulfide bonds are in cyan. 

In protein 3, the numbers 142-177 and 198 31 indicate amino acid residues. The a-helices are in red and p-strands are in green, including the two novel p-strands, pi and pi, that complete the five-stranded antiparallel P-sheet. 

Protein 1 shows the binding in a cavity of positive charge. The charge distribution is color coded with blue for positive, red for negative, and white for neutral. 

Protein 2 shows the surface features of the interface area of two domains in cyan and yellow. The shape of the interface of one molecule complements that of the other. 

Protein 3 shows electrostatic surface potentials. A cutaway view of the binding cavity, including electrostatic surface potentials (positive in blue, negative in red), reveals a relatively smooth, uncharged surface. The cavity is enclosed by portions of five a-helices, three p-strands, and three loops. 

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