1bds

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1bds

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DETERMINATION OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE ANTIHYPERTENSIVE AND ANTIVIRAL PROTEIN BDS-I FROM THE SEA ANEMONE ANEMONIA SULCATA. A STUDY USING NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING

OverviewOverview

The three-dimensional solution structure of the antihypertensive and, antiviral protein BDS-I from the sea anemone Anemonia sulcata has been, determined on the basis of 489 interproton and 24 hydrogen-bonding, distance restraints supplemented by 23 phi backbone and 21 chi 1, side-chain torsion angle restraints derived from nuclear magnetic, resonance (NMR) measurements. A total of 42 structures is calculated by a, hybrid metric matrix distance geometry-dynamical simulated annealing, approach. Both the backbone and side-chain atom positions are well, defined. The average atomic rms difference between the 42 individual SA, structures and the mean structure obtained by averaging their coordinates, is 0.67 +/- 0.12 A for the backbone atoms and 0.90 +/- 0.17 A for all, atoms. The core of the protein is formed by a triple-stranded antiparallel, beta-sheet composed of residues 14-16 (strand 1), 30-34 (strand 2), and, 37-41 (strand 3) with an additional mini-antiparallel beta-sheet at the, N-terminus (residues 6-9). The first and second strands of the, triple-stranded antiparallel beta-sheet are connected by a long exposed, loop (residues 17-30). A number of side-chain interactions are discussed, in light of the structure.

About this StructureAbout this Structure

1BDS is a Single protein structure of sequence from Anemonia sulcata. Full crystallographic information is available from OCA.

ReferenceReference

Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing., Driscoll PC, Gronenborn AM, Beress L, Clore GM, Biochemistry. 1989 Mar 7;28(5):2188-98. PMID:2566326

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