This shows you the differences between two versions of the page.
mm:parameters:manganese:hhdhwa [2013/07/26 14:17] ruineves |
mm:parameters:manganese:hhdhwa [2013/10/03 18:57] (current) ruineves |
||
---|---|---|---|
Line 1: | Line 1: | ||
====== Manganese(III) - HHDHWa ====== | ====== Manganese(III) - HHDHWa ====== | ||
- | + | ### | |
- | + | The coordination sphere of Manganese Superoxide Dismutase is located in a hydrophobic pocket formed by two subunits. In the resting state the manganese coordination geometry presents distorted trigonal bipyramidal geometry with two histidine and an aspartate equatorial ligands and a histidine and water/hydroxide in axial positions. | |
- | + | ### | |
- | | **Coordination Sphere** | **Oxidation State:** Mn(III) \\ **Spin Multiplicity:** 5 | | + | | **COORDINATION SPHERE** || |
- | | {{ :mm:parameters:manganese:non-parameterized_hhdhw_.png?200 |}} | IMAGE2 ((The schemes represent geometrical dispositions for crystal lattices. These should be roughly similar to the corresponding distorted geometries in enzymatic coordination spheres.)) | | + | | {{ :mm:parameters:manganese:non-parameterized_hhdhw_.png?120 |}} | \\ **Oxidation State:** Mn(III) \\ **Spin Multiplicity:** 5 | |
Line 108: | Line 108: | ||
| D1 | 1.6612 | 0.21 | | | D1 | 1.6612 | 0.21 | | ||
| W1 | 1.7683 | 0.152 | | | W1 | 1.7683 | 0.152 | | ||
- | | HM | 0.6000 | 0.0157 | [[LINK | [Cornel, 1995]]] | | + | | HM | 0.6000 | 0.0157 | [[http://pubs.acs.org/doi/abs/10.1021/ja00124a002 | [Cornell, 1995]]] | |
Line 151: | Line 151: | ||
===== References ===== | ===== References ===== | ||
+ | ### | ||
Neves, R.P.P.; Sousa, S.F.; Fernandes, P.A.; Ramos, M.J.. [[http://pubs.acs.org/doi/abs/10.1021/ct400055v | Parameters for Molecular Dynamics Simulations of Manganese-Containing Metalloproteins]] . //J. Chem. Theory Comput.//, **2013**, 9 (6), 2718–2732 | Neves, R.P.P.; Sousa, S.F.; Fernandes, P.A.; Ramos, M.J.. [[http://pubs.acs.org/doi/abs/10.1021/ct400055v | Parameters for Molecular Dynamics Simulations of Manganese-Containing Metalloproteins]] . //J. Chem. Theory Comput.//, **2013**, 9 (6), 2718–2732 | ||
+ | ### |