Abstract
The principal source of geometric information used to solve three dimensional structures of macromolecules by NMR resides in short (< 5A) approximate interproton distance restraints derived from nuclear Overhauser enhancement (NOE) measurements (1–5). In order to extract this information it is essential to first completely assign the 1H spectrum of the macromolecule in question and then to assign as many structurally useful NOE interactions as possible. The larger the number of NOE restraints, the higher the precision and accuracy of the resulting structures (5–7). Indeed, with current state-of-the-art methodology it is now possible to obtain NMR structures of proteins at a precision and accuracy comparable to 2 A resolution crystal structures (7–9)
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