FIGURE 5. a, Topology of bold beta-chain (green) and bold gamma-chain (red) C-terminal domains.

From the following article:

Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

Glen Spraggon, Stephen J. Everse and Russell F. Doolittle

Nature 389, 455-462(2 October 1997)

doi:10.1038/38947

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The first residue in each segment of secondary structure is numbered. b, Stereo depiction of superposed Calpha backbone structures from globular portions of beta-chains (green) and gamma-chains (red); the numbers on the strands and letters on the helices correspond to the secondary structure designations in Fig. 4. c, GRASP representation of binding cavities of beta-chains (left) and gamma-chains (right) showing charge distribution; red, negatively charged; blue, positively charged47. Domains have been reorientated to show equivalent projections.

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