NMR frequency assignments are usually considered a prerequisite for the analysis of NOESY spectra, in turn required for the calculation of biomolecular structures. In contrast, as we propose here, relatively high numbers of unambiguous NOE identities can be consistently achieved in an automated manner by relying only on grouping resonances into connected spin systems. To achieve this goal, we have developed for proteins two protocols, SPI and BACUS, based on Bayesian inference. SPI (Grishaev and Llinás, 2002c) produces a list of the (1)H resonance frequencies from homo- and hetero-nuclear multidimensional spectra, grouped into effective spin systems. BACUS automatically establishes probabilistic identities of NOESY cross-peaks in terms of the chemical shifts provided by SPI. BACUS requires neither assignment of resonances nor an initial structural model. It successfully copes with chemical shift overlap and does so without cycling through 3D structure calculations. The method exploits the self-consistency of the NOESY graph by taking advantage of a network of J- as well as NOE-connected "reporter" protons sorted via SPI. BACUS was validated by tests on experimental NOESY data recorded for the col 2 and kringle 2 domains.