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Figure 1 | BMC Structural Biology

Figure 1

From: The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

Figure 1

Solution Structure of Arap3-Sam. Left panel. Superposition on the backbone atoms (residues 27-84) of the 20 NMR structures of Arap3-Sam. The flexible C-terminal tail (residues 88-100) has been omitted for clarity. The final structure calculation includes 1127 upper distance limits (382 intra-residue, 215 short-range, 252 medium-range, 278 long-range), 352 angle constraints and stereospecific assignments for the methyl groups of L33, L38, L50, L59, L64, L67, L79, L81, L82 and V36. Right panel. Ribbon drawing of the Arap3-Sam NMR conformer with the lowest CYANA target function. It presents the following secondary structure elements: α 1 (residues 29-36), α 2 (residues 39-47), α 3 (residues 53-56), α 4 (residues 61-67), α 5 (residues 72-82).

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