SARS-CoV-2 Protease Structures 6Y2E and 6LU7 with Rigidity and Motion Analysis

Simulations and analysis performed on two protein structures from the SARS-CoV-2 virus, PDB entries 6Y2E and 6LU7. The study includes rigidity analysis, elastic network modelling to identify normal modes, and all-atom geometric simulations of flexible motion. The data was produced by Stephen A. Wells at the University of Bath using tools like FIRST, FRODA, and Elnemo.

Use Cases

• Study protein rigidity and flexibility based on the described rigidity analysis.
• Identify key vibrational modes of a viral protease based on the elastic network modelling.
• Simulate conformational changes in a drug target based on the all-atom geometric simulations.
• Compare the dynamics of a free protease versus an inhibitor-bound complex based on the two provided structures.

Strengths

• Analysis is performed on two distinct, well-defined Protein Data Bank structures (6Y2E and 6LU7).
• The study employs multiple established computational biology tools (FIRST, FRODA, Elnemo).
• Includes processed results from both a free protease and an inhibitor-bound complex.

Limitations

• Column-level documentation is absent; field semantics must be inferred after download.
• Row count and file size are unknown, which may limit suitability assessment.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Bath

Collection Method

Computational analysis of public Protein Data Bank entries using specialized software.