Partial site-specific assignments are reported for the solid state NMR spectra of light-harvesting complex 1, a 160 kDa integral membrane protein. The assignments were derived from 600 MHz 15 N– 13 CO– 13 Cα and 15 N– 13 Cα– 13 CX correlation spectra, using uniformly 13 C, 15 N enriched hydrated material, in an intact and precipitated form. Sequential assignments were verified using characteristic 15 N– 13 Cα– 13 Cβ side chain chemical shifts observed in 3D experiments. Tertiary contacts found in 2D DARR spectra of the selectively 13 C enriched sample provided further confirmatory evidence for the assignments. The assignments include the region of the Histidine ligands binding the Bacteriochlorophyll chromophore. The chemical shifts of Cα and Cβ resonances indicated the presence of typical α-helical secondary structure, consistent with previous studies.