| torsion angle dynamics/ simulated annealing |
The nineteen structures were determined by NMR and torsion angle dynamics/simulated annealing methods. The peptide dimer was treated as a single entity and symmetry elements were not utilized during structure calculations. The structures are based on a total of 276 NOE-derived restraints. The list of constraints is available in the file water_uppercons.txt. Structure calculations were performed with the program DYANA-1.5 (P. Guentert, C. Mumenthaler, K. Wuthrich, J. Mol. Biol.(1997)Vol.273, 283-298). No violation of distance constraints from NOEs exceeded 0.3Angstroms. The ensemble of structures is superimposed over the best-structured region encompasing residues V19-L34. Residues 1-11 were unstructured and their co-ordinates are not given. The average RMSDs between the superposed structures and the average structure are as follows: 1.04(chain A, residues 20-34, backbone atoms) 0.91(chain B, residues 20-34, backbone atoms). |
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