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MM-PBSA analysis of WT TPH2 and its variants.
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创建时间：
2020-03-02
相关数据集
MM/PBSA binding free energies (kJ/mol) of wild-type and mutant AIRE-PHD1/H3K4me0 complexes.
1experimental binding free energy as measured in [15], [20]. 2difference between wild-type and mutant experimental binding free energies. 3computational binding free energies. 4difference between comp
NIAID Data Ecosystem60
Results of thermodynamic integration calculations to test Rosetta predictions for better binding non-canonical mutations.
Left row lists the initial residue starting points. Top row header shows the non-canonical residue mutation identity. Binding energy change units are kcal/mol. The most significant energy changes are
Figshare2017-11-07 更新40
Binding energy of trypsin-BPTI complex with PyGBe and APBS
This file bundle includes data, figures and plotting scripts of solvation energy and binding energy calculations for trypsin-BPTI complex using PyGBe and APBS. Errors were calculated with respect to t
Figshare2016-01-18 更新30
Binding energy calculation results on subunit and local level.
Local contribution to protein binding, secondary structure element assignment, and details of the conservation calculation are given for each PTM added to a protein complex in either normal or stress
Figshare2021-05-12 更新50
The effect of charge neutralizing kinesin mutations on ΔGelec and ΔΔGelec highlight sites important for kinesin-tubulin association.
The effect of charge neutralizing kinesin mutations on ΔGelec and ΔΔGelec highlight sites important for kinesin-tubulin association.
Figshare2015-12-02 更新30
