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-Structure paper
Title | Ph-Dependent Conformational Flexibility of the Sars-Cov Main Proteinase (M(Pro)) Dimer: Molecular Dynamics Simulations and Multiple X-Ray Structure Analyses. |
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Journal, issue, pages | J. Mol. Biol., Vol. 354, Page 25-, Year 2005 |
Publish date | Jul 22, 2005 (structure data deposition date) |
Authors | Tan, J. / Verschueren, K.H.G. / Anand, K. / Shen, J. / Yang, M. / Xu, Y. / Rao, Z. / Bigalke, J. / Heisen, B. / Mesters, J.R. ...Tan, J. / Verschueren, K.H.G. / Anand, K. / Shen, J. / Yang, M. / Xu, Y. / Rao, Z. / Bigalke, J. / Heisen, B. / Mesters, J.R. / Chen, K. / Shen, X. / Jiang, H. / Hilgenfeld, R. |
External links | J. Mol. Biol. / PubMed:16242152 |
Methods | X-ray diffraction |
Resolution | 2 - 2.79 Å |
Structure data | PDB-2bx3: PDB-2bx4: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / SARS / ANTI-PARALLEL B-BARREL / ANTI-PARALLEL A- HELICES / VIRAL PROTEIN |