Published August 19, 2020
| Version v1
Dataset
Open
3x 1 µs all-atom MD trajectories; AMBER ff15ipq & SPC/Eb; T4 Lysozyme; 'Fitting side-chain NMR relaxation data using molecular simulations'
Authors/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 1 µs all-atom MD simulations of T4 Lysozyme
- Force field: AMBER ff15ipq with modified methyl rotation barriers1
- Water model: SPC/Eb
- 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. (2020). Predicting NMR relaxation of proteins from molecular dynamics simulations with accurate methyl rotation barriers. Journal of Chemical Physics, 152(8). https://doi.org/10.1063/1.5135379
Files
Files
(35.3 GB)
| Name | Size | |
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md5:7a127d37d6bf3530c9a9917885d42c1d
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2.0 MB | Download |
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md5:83b44f5c90b0110fd67468e5fc745d95
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10.8 GB | Download |
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md5:b23c0f953b87cdd4fc50deb4a7b617ab
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2.0 MB | Download |
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md5:8092a179d467a72261c26f1b3937f03e
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11.5 GB | Download |
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md5:242f6934602da6003c8310354d241c7d
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2.0 MB | Download |
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md5:969aead9007de9096aa65cd8edcf871b
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13.0 GB | Download |
Additional details
Related works
- Is supplement to
- Preprint: 10.1101/2020.08.18.256024 (DOI)