Structural Drift in the SARS-CoV-2 Spike RBD and Furin Cleavage Region

This dataset analyzes 693,699 high-quality SARS-CoV-2 spike protein sequences selected from approximately 9.3 million genomes, revealing extensive structural drift in the Receptor Binding Domain (RBD). We identified over 1,200 unique RBD mutations with a 9% indel frequency, indicating substantial structural plasticity. Dominant substitutions (including L513F, C538V, and K529S) cluster proximal to the furin cleavage region, suggesting coordinated destabilization of the RBD structural scaffold. These patterns indicate significant structural remodeling under persistent immune pressure, with potential implications for ACE2 binding affinity and monoclonal antibody therapeutic efficacy. Data processed via local python scripts on jupyter notebook & curation by: Tahir HB