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The rationale behind including these restraints is twofold: (1) they are easily measured and therefore represent a useful source of additional structural restraints and (2) it is generally found that the agreement between observed and calculated values for these various parameters is better for high-resolution X-ray structures than for the corresponding high-resolution NMR structures refined in the absence of these restraints. Inclusion of these restraints has little impact on precision but does increase the accuracy of the structures.

Chem. Soc. 119:1803. Huth, J. , Bewley, C. , Nissen, M. , Evans, J. N. , Gronenborn, A. , and Clore, G. , 1997, Nature Struct. Biol. , Kay, L. , 1990, Biochemistry 29:4659. , Clore, G. , Gronenborn, A. , Klee, C. , 1992, Science 256:632. Kay, L. , Clore, G. , 1990, Science 249:411. Kay, L. , 1992, J. Am. Chem. Soc. 114:10663. , and Sykes, B. , 1994, J. Biol. Chem. 269:32909. , Gronenborn, A. , and Clore, G. , 1995a, J. Magn. Reson. Ser. B 106:92. , Gronenborn, A. , and Clore, G. , 1995b, J. Magn.

Despite these advances, it should always be borne in mind that there are a number of key requirements that have to be satisfied to permit a successful structure determination of larger proteins and protein complexes by NMR. 5– 1 mM; it must be stable at room temperature or slightly higher for considerable periods of time (particularly as it may take several months of measurement time to acquire all of the necessary NMR data); it should not exhibit significant conformational heterogeneity that could result in extensive line broadening; and finally it must be amenable to uniform 15N and 13C labeling.

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