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The structure of equine apolactoferrin has been determined at 303 K. Both N and C lobes have been found in the closed conformations similar to those observed in various metal-saturated lactoferrin forms and in apolactoferrin at 277 K.

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The structure of the complex formed between Russell's viper phospholipase A2 and a designed peptide LAIYS has been determined at 2.0 Å resolution. The peptide binds to phospholipase A2 specifically and fills the hydrophobic channel completely.
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