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New methods of structure refinement for macromolecular structure detemination by NMR
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Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases
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J. Kuszewski, A. M. Gronenborn, and G. M. Clore, Improving the quality of NMR and crystallographic protein structures by means of a conformational database potential derived from structure databases, Prot. Sci. 5, 1067-1080 (1996).
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0031083293
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Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids
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J. Kuszewski, A. M. Gronenborn, and G. M. Clore, Improvements and extensions in the conformational database potential for the refinement of NMR and X-ray structures of proteins and nucleic acids, J. Magn. Reson. 125, 171-177 (1997).
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Calculation of conformation ensembles from potentials of mean force: An approach to the knowledge-based prediction of local structures in globular proteins
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A novel, highly stable fold of the immunoglobulin domain of streptococcal protein G
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A. M. Gronenborn, D. R. Filpula, N. Z. Essig, A. Achari, M. Whitlow, P. T. Wingfield, and G. M. Clore, A novel, highly stable fold of the immunoglobulin domain of streptococcal protein G, Science 253, 657-661 (1991).
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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations
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M. Nilges, G. M. Clore, and A. M. Gronenborn, Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations, FEBS Lett. 229, 317-324 (1988).
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Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration
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J. Kuszewski, A. M. Gronenborn, and G. M. Clore, Improving the packing and accuracy of NMR structures with a pseudopotential for the radius of gyration, J. Am. Chem. Soc. 121, 2337-2338 (1999).
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PROCHECK: A program to check the stereochemical quality of protein structures
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R. A. Laskowski, M. W. MacArthur, D. S. Moss, and J. M. Thornton, PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Cryst. 26, 283-291 (1993).
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Solution structure of the MEF2A-DNA complex: Structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors
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K. Huang, J. M. Louis, L. Donaldson, F.-L. Lim, A. D. Sharrocks, and G. M. Clore, Solution structure of the MEF2A-DNA complex: Structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors, EMBO J. 19, 2615-2628 (2000).
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0344258272
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Impact of residual dipolar couplings on the accuracy of NMR structures determined from a minimal number of NOE restraints
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G. M. Clore, M. R. Starich, C. A. Bewley, M. Cai, and J. Kuszewski, Impact of residual dipolar couplings on the accuracy of NMR structures determined from a minimal number of NOE restraints, J. Am. Chem. Soc. 121, 6513-6514 (1999).
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