Published August 18, 2020
| Version v1
Dataset
Open
3x 5 µs all-atom MD trajectories; AMBER ff99SB*-ILDN & TIP4P/2005; T4 Lysozyme; 'Fitting side-chain NMR relaxation data using molecular simulations'
Creators
- 1. University of Copenhagen
- 2. Ruhr University Bochum
Description
Simulation data for "Fitting side-chain NMR relaxation data using molecular simulations" (https://doi.org/10.1101/2020.08.18.256024).
- 3 x 5 µs all-atom MD simulations of T4 Lysozyme
- Force field: AMBER ff99SB*-ILDN with modified methyl rotation barriers1
- Water model: TIP4P/2005
- Compressed protein coordinates saved every 1 ps to enable calculation of side-chain NMR relaxation parameters
Contains:
- 3 x GROMACS .xtc trajectory files for 3 independent simulations
- 3 x corresponding GROMACS .tpr topology files
1 Hoffmann, F., Mulder, F. A. A., & Schäfer, L. V. (2018). Accurate Methyl Group Dynamics in Protein Simulations with AMBER Force Fields. The Journal of Physical Chemistry B, 122(19), 5038–5048. https://doi.org/10.1021/acs.jpcb.8b02769
Files
Files
(153.5 GB)
| Name | Size | Download all |
|---|---|---|
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md5:dd51d8afdc51b3fa0fad97e30d068a1d
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2.3 MB | Download |
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md5:e6ff69a2f28d70a8d908d3263d9a5af0
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51.3 GB | Download |
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md5:15c58cff51eb3b4b57f58b4a605937bf
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2.3 MB | Download |
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md5:e436f20be0b9276cb0fdd7640c8ef717
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51.3 GB | Download |
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md5:322d96a7bf5ebc42f4aa4cf140cdecda
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2.3 MB | Download |
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md5:a683da009b75b68ea356916030d67058
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51.0 GB | Download |
Additional details
Related works
- Is supplement to
- Preprint: 10.1101/2020.08.18.256024 (DOI)