Recent spectacular advances by AI programs in 3D structure predictions from protein sequences have revolutionized the field in terms of accuracy and speed. The resulting "folding frenzy" has already produced predicted protein structure databases for the entire human and other organisms' proteomes. However, rapidly ascertaining a predicted structure's reliability based on measured properties in solution should be considered. Shape-sensitive hydrodynamic parameters such as the diffusion and sedimentation coefficients (D0t(20,w),s0(20,w)) and the intrinsic viscosity (η) can provide a rapid assessment of the overall structure likeliness, and SAXS would yield the structure-related pair-wise distance distribution function p(r) vs. r. Using the extensively validated UltraScan SOlution MOdeler (US-SOMO) suite we have calculated from the AlphaFold structures the corresponding D0t(20,w), s0(20,w), η, p(r) vs. r, and other parameters. Circular dichroism spectra were also computed. The resulting US-SOMO-AF database should aid in rapidly evaluating the consistency in solution of AlphaFold predicted protein structures.