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The resource centers on the RBD of the ancestral Wuhan-Hu-1 spike protein and includes a systematically generated set of all possible single-point missense variants (3,705 in total). All variants are annotated with structural descriptors derived from AlphaFold-2 predicted structures and augmented with sequence-based biophysical predictors such as disorder, flexibility, and amyloid aggregation propensity from the Bio2Byte suite. To complement structural predictions, empirical measurements of ACE2 binding affinity and surface expression levels were integrated for each 1-step variant, based on deep mutational scanning (DMS) data published by Starr et al. This pairing of theoretical and experimental annotations provides a foundation for analyzing structure–function relationships across the spike mutational landscape and supports downstream applications in protein modeling, variant characterization, and structure-guided surveillance.
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