Interpreting dynamics in solid-state molecular systems requires characterization of the potentially heterogeneous environmental contexts of molecules. In particular, the analysis of solid-state nuclear magnetic resonance (ssNMR) data to elucidate molecular dynamics (MD) involves modeling the restriction to overall tumbling by neighbors, as well as the concentrations of water and buffer. In this exploration of the factors that influence motion, we utilize atomistic MD trajectories of peptide aggregates with varying hydration to mimic an amorphous solid-state environment and predict ssNMR relaxation rates. We also account for spin diffusion in multiply spin-labeled (up to 19 nuclei) residues, with several models of dipolar-coupling networks. The framework serves as a general approach to determine essential spin couplings affecting relaxation, benchmark MD force fields, and reveal the hydration dependence of dynamics in a crowded environment. We demonstrate the methodology on a previously characterized amphiphilic 14-residue lysine-leucine repeat peptide, LK alpha 14 (Ac-LKKLLKLLKKLLKL-c), which has an a-helical secondary structure and putatively forms leucine-burying tetramers in the solid state. We measure the R-1 relaxation rates of uniformly C-13-labeled and site-specific H-2-labeled leucines in the hydrophobic core of LK alpha 14 at multiple hydration levels. Studies of 9 and 18 tetramer bundles reveal the following: (a) for the incoherent component of C-13 relaxation, the nearest-neighbor spin interactions dominate, while the H-1-H-1 interactions have minimal impact; (b) the AMBER ff14SB dihedral barriers for the leucine C-gamma-C-delta bond ("methyl rotation barriers") must be lowered by a factor of 0.7 to better match the H-2 data; (c) proton-driven spin diffusion explains some of the discrepancy between experimental and simulated rates for the C-beta and C-alpha nuclei; and (d) C-13 relaxation rates are mostly underestimated in the MD simulations at all hydrations, and the discrepancies identify likely motions missing in the 50 ns MD trajectories.