Interference between dipolar interactions in covalently linked C-13-H-1 and nonlinked H-1-H-1 pairs can be used to generate antiphase magnetization between noncoupled spins. The buildup rate of such antiphase terms is highly sensitive to local geometry, in particular the interproton distance and the C-13-H-1-H-1 internuclear angle. These rates have been measured for opposing CalphaHalpha pairs in antiparallel beta-sheets in the third Igg-binding domain of protein G (GB3) and in HIV protease, complexed with the inhibitor DMP323. For GB3, good agreement with the 1.1-Angstrom crystal structure is found. However, this agreement rapidly deteriorates with decreasing resolution of the corresponding X-ray structure. For HIV protease, two separate crystal structures that differ by less than 0.2 Angstrom from one another exhibit lower agreement in their predicted cross-correlated relaxation rates relative to one another than is found between experimental rates and the average of the rates predicted for the two structures. These data indicate that quantitative measurement of these cross-correlated relaxation rates can provide highly accurate structural information in macromolecules.