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Vattulainen Ilpo - One of the best experts on this subject based on the ideXlab platform.

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Weak E-field Simulations, Upright Mode
    2018
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "E-field weak, upright mode" Simulations in Ref. [1]. There are 20 replicas marked with "_1" , "_2", etc. Files include: -trajectories (.xtc) that are saved every 100ps  -initial structures (.gro),  -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted)

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Weak E-field Simulations, Parallel Mode
    2018
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "E-field weak, parallel mode" Simulations in Ref. [1]. There are 20 replicas marked with "_1" , "_2", etc. Files include: -trajectories (.xtc) that are saved every 100ps  -initial structures (.gro),  -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted)

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Weak E-field Simulations, Crystallographic Mode
    2017
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "E-field weak, crystallographic mode" Simulations in Ref. [1]. There are 20 replicas marked with "_1" , "_2", etc. Files include: -trajectories (.xtc) that are saved every 100ps -initial structures (.gro), -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Gathering Simulations
    2017
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "Gathering" Simulations in Ref. [1]. Files include: -trajectories (.xtc) that are saved every 100ps -initial structures (.gro), -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Clustering Simulations
    2017
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "Clustering" Simulations in Ref. [1]. There are two replicas marked with "_1" and "_2". Files include: -trajectories (.xtc) that are saved every 100ps -initial structures (.gro), -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted

Javanainen Matti - One of the best experts on this subject based on the ideXlab platform.

  • Umbrella Sampling Simulations of TM Domain Dimerization
    2018
    Co-Authors: Javanainen Matti, Hector Martinez-seara, Ilpo Vattulainen
    Abstract:

    Umbrella sampling Simulations of dimer formation of 2 TM domain dimers in DMPC/DLPC bilayers. Simulations are performed in the coarse-grained scheme using different force fields; normal Martini (N), Martini with all protein–protein interactions scaled (U) by 10% (U_10) or 20% (U_20), Martini with interactions among water-interacting beads scaled (W) either by 60% (W_60), 80% (W_80), or 90% (W_90), or the polarizable Martini (P). The original Martini is also repeated with an older set of 'common' Simulation Parameters (C). The tar files are named after the PDB codes of the corresponding dimer and the type of force field employed (see above). The tar files contain the run input files (.tpr) and the corresponding Simulation Parameter files (.mdp) for all umbrella windows; i.e. "EPHA_U_80_18.tpr" is the run input file for the EPHA dimer with all protein–protein interactions scaled down by 20% and with a protein–protein distance restrained to 18 Å by the umbrella potential. This tpr is generated from the Simulation Parameter file, the topology file (here EPHA_U_80.top), the index file (here EPHA.ndx), and the initial structure (here EPHA_start_18.gro, available in the EPHA-frames.tar). The index and initial structures for the polarizable model differ, and are provided in "EPHA-P.ndx" and "EPHA-frames-P.tar", respectively. All topologies (.itp) are provided in TOP.tar. The scaling is achieved by adding 'p' to the bead types in the proteins; either all types (scaling U) or to those more in contact with water than the membrane (scaling W) The corresponding Parameters are given in the "martini_v2.2_scaled_X.itp" file. Note that for uniform style, the unscaled Parameters are given in a similar manner in a file "martini_v2.2_unscaled.itp". Here, the .itp files follow the naming convention of the paper (see below) so that X=1 means downscaling of LJ epsilon by 10%, i.e. it corresponds to files with "_10". For a more thorough explanation of the purporse of the files and the Simulation Parameters, see the related publication:

  • Umbrella Sampling Simulations of TM Domain Dimerization
    2017
    Co-Authors: Javanainen Matti, Hector Martinez-seara, Ilpo Vattulainen
    Abstract:

    Umbrella sampling Simulations of dimer formation of 2 TM domain dimers in DMPC/DLPC bilayers. Simulations are performed in the coarse-grained scheme using different force fields; normal Martini (N), Martini with all protein–protein interactions scaled (U) by 10% (U_10) or 20% (U_20), Martini with interactions among water-interacting beads scaled (W) either by 60% (W_60), 80% (W_80), or 90% (W_90), or the polarizable Martini (P). The original Martini is also repeated with an older set of 'common' Simulation Parameters (C). The tar files are named after the PDB codes of the corresponding dimer and the type of force field employed (see above). The tar files contain the run input files (.tpr) and the corresponding Simulation Parameter files (.mdp) for all umbrella windows; i.e. "EPHA_U_80_18.tpr" is the run input file for the EPHA dimer with all protein–protein interactions scaled down by 20% and with a protein–protein distance restrained to 18 Å by the umbrella potential. This tpr is generated from the Simulation Parameter file, the topology file (here EPHA_U_80.top), the index file (here EPHA.ndx), and the initial structure (here EPHA_start_18.gro, available in the EPHA-frames.tar). The index and initial structures for the polarizable model differ, and are provided in "EPHA-P.ndx" and "EPHA-frames-P.tar", respectively. All topologies (.itp) are provided in TOP.tar. The scaling is achieved by adding 'p' to the bead types in the proteins; either all types (scaling U) or to those more in contact with water than the membrane (scaling W) The corresponding Parameters are given in the "martini_v2.2_scaled_X.itp" file. Note that for uniform style, the unscaled Parameters are given in a similar manner in a file "martini_v2.2_unscaled.itp". Here, the .itp files follow the naming convention of the paper (see below) so that X=1 means downscaling of LJ epsilon by 10%, i.e. it corresponds to files with "_10". For a more thorough explanation of the purporse of the files and the Simulation Parameters, see the related publication: Javanainen M, Martinez-Seara H, Vattulainen I (2017) Excessive aggregation of membrane proteins in the Martini model. PLoS ONE 12(11): e0187936. https://doi.org/10.1371/journal.pone.018793

  • Simulations of GpA-based dimers of various lengths in DEPC, DOPC, and DLPC bilayers, part 1/2
    2017
    Co-Authors: Javanainen Matti, Kulig Waldemar, Vattulainen Ilpo
    Abstract:

    Dimers of transmembrane (TM) peptides based on the Glycophorin A (GpA) dimer are simulated in different membrane environments. Three different homodimers with varying TM domain lengths and one heterodimer are considered. The homodimers are formed of either 17L (GRPNLKLLLGVLLGVLLTLLLLEYP) 23L (GRPNLKLLLLLLGVLLGVLLTLLLLLLLEYP) 29L (GRPNLKLLLLLLLLLGVLLGVLLTLLLLLLLLLLEYP) peptides, while the heterodimer consists of one 17L peptide and one 29L peptide. In the sequences, the bold letters denote the amino acids involved in the GpA dimerization motif. The dimers are simulated in DLPC (12:0 PC), DOPC (18:1 PC), or DEPC (22:1 PC) bilayers. Additionally, a polyleucine dimer is simulated in a DOPC bilayer. Bilayers consist of 400 lipids and they are adequately hydrated with 24000 water molecules and 134 mM NaCl. The Simulations are 100 ns long with trajectories written every 100 ps. The files are named as XXX-YYYY.ZZZ, where XXX denotes to the peptide type ('het' for the heterodimer and 'polyl' for the polyleucine), YYYY denotes the bilayer type, and ZZZ denotes the file type. Files are in Gromacs format: .xtc for trajectories, .edr for energy data, .cpt for continue points, .ndx for index files, .top for topology files, and .tpr for run input files (Gromacs 5.1). The Simulation Parameter file (md.mdp) is common for all systems. The CHARMM36 force field is used; topologies are obtained from CHARMM-GUI, and those of the peptides are included in Gromacs format (.itp). More information on the systems is available in the publication, available here: (TO BE INCLUDED!) Note that the data for the heterodimer and for the polyleucine are in part 2/2, available at https://doi.org/10.5281/zenodo.57327

  • Simulations of GpA-based dimers of various lengths in DEPC, DOPC, and DLPC bilayers, part 2/2
    2017
    Co-Authors: Javanainen Matti, Kulig Waldemar, Vattulainen Ilpo
    Abstract:

    Dimers of transmembrane (TM) peptides based on the Glycophorin A (GpA) dimer are simulated in different membrane environments. Three different homodimers with varying TM domain lengths and one heterodimer are considered. The homodimers are formed of either 17L (GRPNLKLLLGVLLGVLLTLLLLEYP) 23L (GRPNLKLLLLLLGVLLGVLLTLLLLLLLEYP) 29L (GRPNLKLLLLLLLLLGVLLGVLLTLLLLLLLLLLEYP) peptides, while the heterodimer consists of one 17L peptide and one 29L peptide. In the sequences, the bold letters denote the amino acids involved in the GpA dimerization motif. The dimers are simulated in DLPC (12:0 PC), DOPC (18:1 PC), or DEPC (22:1 PC) bilayers. Additionally, a polyleucine dimer is simulated in a DOPC bilayer. Bilayers consist of 400 lipids and they are adequately hydrated with 24000 water molecules and 134 mM NaCl. The Simulations are 100 ns long with trajectories written every 100 ps. The files are named as XXX-YYYY.ZZZ, where XXX denotes to the peptide type ('het' for the heterodimer and 'polyl' for the polyleucine), YYYY denotes the bilayer type, and ZZZ denotes the file type. Files are in Gromacs format: .xtc for trajectories, .edr for energy data, .cpt for continue points, .ndx for index files, .top for topology files, and .tpr for run input files (Gromacs 5.1). The Simulation Parameter file (md.mdp) is common for all systems. The CHARMM36 force field is used; topologies are obtained from CHARMM-GUI, and those of the peptides are included in Gromacs format (.itp). More information on the systems is available in the publication, available here: (TO BE INCLUDED!) Note that the data for the homodimers (bar polyleucine) are in part 1/2, available at https://doi.org/10.5281/zenodo.57325

  • Simulations of DPPC/Cholesterol bilayers with the Slipids force field, part 1/2
    2017
    Co-Authors: Javanainen Matti, Martinez-seara Hector, Vattulainen Ilpo
    Abstract:

    Simulation data related to our publication "Nanoscale Membrane Domain Formation Driven by Cholesterol" (DOI:10.1038/s41598-017-01247-9), part 1/2. Part 2/2 of the data are in the Zenodo record (DOI:10.5281/zenodo.439080). Please note that the description below covers both parts. Data for both cholesterol-free calibration Simulations (letters in Table S1 and Fig. 1) and for cholesterol-containing Simulations (numbers in Table S1 and Fig. 1) are included. The files are named as "dppc-X-Y.Z", where X is the cholesterol concentration, Y the Simulation temperature (not shifted, see the paper), and Z defines the file type (in GROMACS formats): xtc for trajectory, edr for energy file, tpr for the Simulation input file, and .cpt for the checkpoint file. The index file (.ndx) and the topology file (.top) are common among systems with equal cholesterol concentration. The Simulation Parameter file (.mdp) is common for all Simulations, only the target temperature of the thermostat needs to be adjusted. Simulation lengths vary between 300 and 1400 ns, and the trajectories are written every 100 ps. Further information on the setup and composition of the simulated systems is available in the paper. The Slipids force field [1,2,3] is employed, and the topologies (.itp) are available at http://www.fos.su.se/~sasha/SLipids/ All Simulations were performed with Gromacs 4.6.x [1] Derivation and Systematic Validation of a Refined All-Atom Force Field for Phosphatidylcholine Lipids. Joakim P. M. Jämbeck and Alexander P. Lyubartsev, The Journal of Physical Chemistry B 2012 116 (10), 3164-3179, DOI: 10.1021/jp212503e [2] An Extension and Further Validation of an All-Atomistic Force Field for Biological Membranes. Joakim P. M. Jämbeck and Alexander P. Lyubartsev, Journal of Chemical Theory and Computation 2012 8 (8), 2938-2948, DOI: 10.1021/ct300342n [3] Another Piece of the Membrane Puzzle: Extending Slipids Further. Joakim P. M. Jämbeck and Alexander P. Lyubartsev, Journal of Chemical Theory and Computation 2013 9 (1), 774-784, DOI: 10.1021/ct300777

PeÓn Antonio - One of the best experts on this subject based on the ideXlab platform.

  • SLIPID POPG-POPE 1:3 Bilayer Simulation (Last 100 ns, 150 mM NaCl, 310 K )
    2019
    Co-Authors: PeÓn Antonio
    Abstract:

    Simulation of a POPG-POPE 1:3 bilayer of 500 lipids (126 L-POPG lipids and 374 POPE lipids, 250 per leaflet) is simulated for 500 ns using Gromacs v5.1.2 in water solution with Na+ counterions and 150 mM of NaCl. The SLIPID model is employed for lipids and TIP3P Water Model . Trajectory (.xtc) is for the last 100 ns of a Simulation of 500 ns with data saved every 10 ps. Additionally, the topology (.top) , Simulation Parameter file (.mdp), index file (.ndx), portable binary run input file (.tpr) and the energy output file (.edr) are provided

  • Gromos POPE Bilayer Simulation (Last 100 ns, 150 mM NaCl, 310 K )
    2019
    Co-Authors: PeÓn Antonio
    Abstract:

    Simulation of a POPE bilayer of 500 lipids (250 per leaflet) is simulated for 500 ns using Gromacs v5.1.2 in water solution with Na+ counterions and 150 mM of NaCl. The GROMOS-CKP model is employed for lipids and SCP Water Model . Trajectory (.xtc) is for the last 100 ns of a Simulation of 500 ns with data saved every 10 ps. Additionally, the topology (.top, .itp), Simulation Parameter file (.mdp), index file (.ndx), portable binary run input file (.tpr) and the energy output file (.edr) are provided

  • Gromos POPG Bilayer Simulation (Last 100 ns, 150 mM NaCl, 310 K )
    2019
    Co-Authors: PeÓn Antonio
    Abstract:

    Simulation of a POPG bilayer of 500 lipids (250 per leaflet) is simulated for 500 ns using Gromacs v5.1.2 in water solution with Na+ counterions and 150 mM of NaCl. The GROMOS-CKP-POPG-Tom_Piggot-v1 model wiht GROMOS57a7 is employed for lipids and the SCP model for water. Trajectory (.xtc) is for the last 100 ns of a Simulation of 500 ns with data saved every 10 ps. Additionally, the topology (.top), Simulation Parameter file (.mdp), and the energy output file (.edr) are provided

Nathan Ratliff - One of the best experts on this subject based on the ideXlab platform.

  • closing the sim to real loop adapting Simulation randomization with real world experience
    International Conference on Robotics and Automation, 2019
    Co-Authors: Yevgen Chebotar, Ankur Handa, Viktor Makoviychuk, Miles Macklin, Jan Issac, Nathan Ratliff
    Abstract:

    We consider the problem of transferring policies to the real world by training on a distribution of simulated scenarios. Rather than manually tuning the randomization of Simulations, we adapt the Simulation Parameter distribution using a few real world roll-outs interleaved with policy training. In doing so, we are able to change the distribution of Simulations to improve the policy transfer by matching the policy behavior in Simulation and the real world. We show that policies trained with our method are able to reliably transfer to different robots in two real world tasks: swing-peg-in-hole and opening a cabinet drawer. The video of our experiments can be found at https://sites.google.com/view/simopt.

  • closing the sim to real loop adapting Simulation randomization with real world experience
    arXiv: Robotics, 2018
    Co-Authors: Yevgen Chebotar, Ankur Handa, Viktor Makoviychuk, Miles Macklin, Jan Issac, Nathan Ratliff
    Abstract:

    We consider the problem of transferring policies to the real world by training on a distribution of simulated scenarios. Rather than manually tuning the randomization of Simulations, we adapt the Simulation Parameter distribution using a few real world roll-outs interleaved with policy training. In doing so, we are able to change the distribution of Simulations to improve the policy transfer by matching the policy behavior in Simulation and the real world. We show that policies trained with our method are able to reliably transfer to different robots in two real world tasks: swing-peg-in-hole and opening a cabinet drawer. The video of our experiments can be found at this https URL

Martinez-seara Monne Hector - One of the best experts on this subject based on the ideXlab platform.

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Weak E-field Simulations, Upright Mode
    2018
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "E-field weak, upright mode" Simulations in Ref. [1]. There are 20 replicas marked with "_1" , "_2", etc. Files include: -trajectories (.xtc) that are saved every 100ps  -initial structures (.gro),  -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted)

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Weak E-field Simulations, Parallel Mode
    2018
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "E-field weak, parallel mode" Simulations in Ref. [1]. There are 20 replicas marked with "_1" , "_2", etc. Files include: -trajectories (.xtc) that are saved every 100ps  -initial structures (.gro),  -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted)

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Weak E-field Simulations, Crystallographic Mode
    2017
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "E-field weak, crystallographic mode" Simulations in Ref. [1]. There are 20 replicas marked with "_1" , "_2", etc. Files include: -trajectories (.xtc) that are saved every 100ps -initial structures (.gro), -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Gathering Simulations
    2017
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "Gathering" Simulations in Ref. [1]. Files include: -trajectories (.xtc) that are saved every 100ps -initial structures (.gro), -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted

  • Atomistic Fingerprint of Hyaluronan-CD44 Binding: Clustering Simulations
    2017
    Co-Authors: Vuorio Joni, Vattulainen Ilpo, Martinez-seara Monne Hector
    Abstract:

    Simulation files (Gromacs 4.6.7 format) for the "Clustering" Simulations in Ref. [1]. There are two replicas marked with "_1" and "_2". Files include: -trajectories (.xtc) that are saved every 100ps -initial structures (.gro), -run input files (.tpr) -checkpoint files (.cpt) -Simulation Parameter files (.mdp) -system topology file (.top) -topology files included in the system topology file (.itp) [1] Vuorio J. et al., Atomistic Fingerprint of Hyaluronan-CD44 Binding, PLOS Comp. Biol., 2017. (Submitted