Assessment of protein solution versus crystal structure determination using spin-diffusion-suppressed NOE and heteronuclear relaxation data

摘要: A spin-diffusion-suppressed NOE buildup series has been measured for E. coli thioredoxin.The extensive 13C and 15N relaxation data previously reported this protein allow fordirect interpretation of dynamical contributions to the 1H-1H cross-relaxation rates a largeproportion cross peaks. Estimates average accuracy these derived NOEdistances are bounded by 4% 10%, based on comparison corresponding X-raydistances. An independent fluctuation model is proposed prediction dynamicalcorrections rates, solely experimental structural andheteronuclear data. This analysis aided demonstration that heteronuclearorder parameters greater than 0.6 depend only variance H-X bond orientation,independent motional in either one- or two-dimensional diffusion (i.e., 1− S2 = 3/4 sin2 2 θσ). The combination NOEdata corrections onheteronuclear allowed detailed various discrepanciesbetween solution crystal structures.