SA-CONF

SA-CONF analyzes and quantifies structural variability across multiple target conformations to characterize amino-acid-level and local-region flexibility from macromolecular structures derived from the Protein Data Bank, NMR spectroscopy, X-ray crystallography, homology models, and molecular dynamics simulations.

Key Features:

• Quantification of Structural Variability: Quantifies structural variability across MTC sets at amino-acid and local-region levels.
• Localization of Variable Positions and Regions: Identifies specific amino-acid positions and local regions that exhibit structural variability.
• Diverse Data Compatibility: Processes MTC sets derived from PDB entries, NMR spectroscopy, X-ray crystallography, homology modeling, and molecular dynamics simulations.
• Analysis of Flexibility Sources: Compares different MTC subsets to distinguish sources of flexibility such as binding partners, mutations, or intrinsic structural properties.
• Linking Local and Residue-Level Variability: Captures and links amino-acid-level and local structural variability to represent the target's structural variability space.

Scientific Applications:

• Protein Flexibility: Understanding how proteins adapt their structures to accommodate different functional states or interactions.
• Mechanistic Insights: Exploring mechanisms that govern protein behavior in response to environmental changes or binding events.
• Functional Implications: Investigating how structural variability influences protein function and its impact on biological processes.

Methodology:

Processes MTC sets derived from PDB entries (including NMR and X-ray), homology models, and molecular dynamics simulations; captures and links amino-acid-level and local structural variability within MTC sets; and compares MTC subsets to identify sources of flexibility.