Magnetically aligned bicelles represent a nearly ideal mimetic for the structural studies of membrane proteins in their native lipid environment. Structures of several proteins reconstituted in bicelles have been obtained by solid-state NMR, including MerF, VPU, and Pf1.However, the assignment of NMR spectra of membrane proteins is usually performed by a laborious preparation of multiple selectively labeled samples, and a helical wheel-like arrangement of peaks is assumed. Here we have used a novel spectroscopic technique [1,2] to obtain spin correlations between the resonances and assigned the spectrum of uniformly 15N labeled Pf1 protein reconstituted in aligned bicelles. The peaks generally follow the (i, i+1) connectivity pattern, and yield the assignment identical to the previously established, albeit without using multiple labeled samples [3]. The method is generally applicable to membrane proteins of arbitrary topology. Long-range correlations (up to 6.7 A) can be observed that have a potential for establishing spectroscopic contacts between the neighboring transmembrane helices.Furthermore, we have developed an algorithm [4] that calculates three-dimensional structures of membrane proteins solely based on the dipolar couplings between the covalently bound spins. Structures of protein G and a helical hairpin of bacteriorhodopsin have been calculated from simulated solid-state NMR spectra as illustrative examples. Effect of experimental uncertainty has been assessed. Application of the algorithm to fully assigned three-dimensional NMR data of doubly (15N, 13C) labeled membrane proteins may allow one to obtain the entire backbone structure from a single spectrum.[1] A.A. Nevzorov, J. Am. Chem. Soc. 130 (2008) 11282-11283.[2] R.W. Knox, J. Lu, S.J. Opella, A.A. Nevzorov, J. Am. Chem. Soc. 132 (2010) 8255-8257.[3] S.J. Opella, A.C. Zeri, S.H. Park, Annu. Rev. Phys. Chem. 59 (2008) 635-57.[4] Y.Y. Yin, A.A. Nevzorov, J. Magn. Reson. 212 (2011) 64-73.