Molecular graphic views of the 15-bp insertion mutation (L213-D217ins) in the VII catalytic domain.

(A) In native VIIa (PDB code, 1cvw), the polypeptide main-chain backbone is shown in light blue, with the exception of residues L213-D217, which are shown in yellow. The calcium ion is shown in magenta, with its 6 ligands being the side-chain carboxyl oxygen atoms of E210 and E220, the main-chain carbonyl oxygen atoms of D212 and E215, and 2 water molecules. With the exceptions of E210 and E220, the side chains are not shown. (B) Structural comparison of native VIIa (left) with a model of VIIa containing the 15-bp insertion mutation (right) (PDB code, 1dan). In native VIIa, the sequence of the β-strands G and H (underlined) and the loop between them isLIAVLGEHDLSEHDGDEQSRRVAQVIIP. In the mutant this sequence becomesLIAVLGEHDLSEHDLSEHDGDEQSRRVAQVIIP.7The 2 structures are shown in ribbon views, where the N-terminal and C-terminal subdomains of the catalytic domain are shown in white and magenta, respectively. The EGF-1 and EGF-2 domains are shown in green and are proximate to the 2 TF domains at the bottom (not shown). The insertion mutation is shown as a yellow ribbon, while the catalytic triad is represented by 3 red spheres on the opposite side of the domain to that of the 15-bp insertion.