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393 results for “Molecular dynamics simulations”

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zenodo36/100

Supplementary Data for "Molecular dynamics simulations provide structural insight into binding of cyclic dinucleotides to human STING protein"

<p>Supplementary Data for &quot;Molecular dynamics simulations provide structural insight into binding of cyclic dinucleotides to human STING protein&quot;,&nbsp;Journal of Biomolecular Structure and Dynamics, 2021,&nbsp;10.1080/07391102.2021.1942213</p> <p>A random selection of 10 representative structures from each MSM state of STING/CDN complexes is provided in .pdb file format. The selected MSM representatives are aligned and available as PyMOL session files.</p>

opencc-by-4.0Jul 2021View details →
zenodo36/100

Structural determinants of ligands recognition by the human mitochondrial basic amino acids transporter SLC25A29. Insights from molecular dynamics simulations of the c-state.

<p>Initial coordinates, molecular dynamics trajectories and representative snapshots resulting from the study &quot;Structural determinants of ligands recognition by the human mitochondrial basic amino acids transporter SLC25A29. Insights from molecular dynamics simulations of the c-state.&quot; by Pasquadibisceglie and Polticelli.</p> <p>The MD folders contain the parameter/topology (parm7) and initial coordinates (rst7) for the molecular dynamics simulations. Moreover, a NetCDF trajectory &quot;prod.nc&quot; of the production phase is also included.<br> In detail:<br> - MD0 -&gt; SLC25A29 in absence of ligands;<br> - MD1, MD3, MD4 -&gt; SLC25A29-ARG complex;<br> - MD1-LYS, MD3-LYS, MD4-LYS -&gt; SLC25A29-LYS complex.</p> <p>The folder PDB_figures contains the PDB files used to produce the figures presented in the manuscript.</p>

opencc-by-4.0Sep 2021View details →
zenodo36/100

Molecular Dynamics Simulation on the Effect of Transition Metal Binding to the N-Terminal Fragment of Amyloid-β

<p>Molecular dynamics trajectories in PDB format for 3x Cu-A&beta;, 3x Zn-A&beta; and 9x Fe-A&beta;<strong>&nbsp;</strong>simulations.</p>

opencc-by-4.0Oct 2018View details →
zenodo36/100

Molecular dynamics simulation of the permeation of 5ALA across the lipid bilayers of the stratum corneum

<p>Input and output files for US-REST3 MD simulations of the permeation of 5ALA across a lipid bilayer representative of the lipid bilayers of the stratum corneum. Each folder corresponds to US-REST3 and conventional US calculations performer at different distances between the permeant and the centre of mass of the lipid bilayer.</p>

opencc-by-4.0Nov 2022View details →
zenodo36/100

Molecular dynamics simulation of the permeation of Me-5ALA across the lipid bilayers of the stratum corneum

<p>Input and output files for US-REST3 MD simulations of the permeation of Me-5ALA across a lipid bilayer representative of the lipid bilayers of the stratum corneum. Each folder corresponds to US-REST3 and conventional US calculations performer at different distances between the permeant and the centre of mass of the lipid bilayer.</p>

opencc-by-4.0Nov 2022View details →
dryad36/100

Molecular dynamics simulations in: High-resolution structures with bound Mn2+ and Cd2+ map the metal import pathway in an Nramp transporter

<p>Transporters of the Nramp (Natural resistance-associated macrophage protein) family import divalent transition metal ions into cells of most organisms. By supporting metal homeostasis, Nramps prevent disorders related to metal insufficiency or overload. Previous studies revealed that Nramps take on a LeuT fold and identified the metal-binding site. We present high- resolution structures of <em>Deinococcus radiodurans</em> Nramp in three stable conformations of the transport cycle revealing that global conformational changes are supported by distinct coordination geometries of its physiological substrate, Mn2+, across conformations and conserved networks of polar residues lining the inner and outer gates. A Cd2+-bound structure highlights differences in coordination geometry for Mn2+ and Cd2+. Measurements of metal binding using isothermal titration calorimetry indicate that the thermodynamic landscape for binding and transporting physiological metals like Mn2+ is different and more robust to perturbation than for transporting the toxic Cd2+ metal.</p>

opencc-zeroNov 2022View details →
zenodo36/100

On equilibrating non-periodic molecular dynamics samples for coupled particle-continuum simulations of amorphous polymers: dataset

<p><strong>Abstract:</strong><br> (from [1])<br> In the context of fracture simulations of polymers, the molecular mechanisms in the vicinity of the<br> crack tip are of particular interest. Nevertheless, to keep the computational cost to a minimum, a<br> coarser resolution must be used in the remaining regions of the numerical sample. For the specific<br> case of amorphous polymers, the Capriccio method bridges the gap between the length and time scales<br> involved at the different levels of resolution by concurrently coupling molecular dynamics (MD) with<br> the finite element method (FEM). Within the scope of the Capriccio approach, the coupling to the<br> molecular MD region introduces non-periodic, so-called stochastic boundary conditions (SBC). In<br> similarity to typical simulations under periodic boundary conditions (PBC), the SBC MD simulations<br> must reach an equilibrium state before mechanical loads are exerted on the coupled systems. In this<br> contribution, we hence extensively study the equilibration properties of non-periodic MD samples<br> using the Capriccio method. We demonstrate that the relaxation behavior of an MD-FE coupled<br> MD domain utilizing non-periodic boundary conditions is rather insensitive to the specific coupling<br> parameters of the method chosen to implement the boundary conditions. The behavior of an exemplary<br> system equilibrated with the parameter set considered as optimal is further studied under uniaxial<br> tension and we observe some peculiarities in view of creep and relaxation phenomena. This raises<br> important questions to be addressed in the further development of the Capriccio method.<br> &nbsp;<br> <strong>Contact:</strong><br> Felix Weber<br> Institute of Applied Mechanics<br> Friedrich-Alexander-Universit&auml;t Erlangen-N&uuml;rnberg<br> Egerlandstr. 5<br> 91058 Erlangen<br> Germany<br> &nbsp;<br> <strong>Context:</strong><br> This dataset contains the results presented in [1] and related data.</p> <p><strong>Content:</strong><br> Throughout this data set, Lammps [2] real units are used. The following folders contain the results obtained under periodic boundary conditions:<br> - biax_PBC: biaxial loading&nbsp;<br> - equil_PBC: equilibration<br> - ut_PBC: uniaxial tension<br> Each simulation directory contains:<br> - input.prm: input parameters of the specific simulation (read by the input file)<br> - job.out: simulation log file<br> - meta.info: meta data of the specific simulation run<br> - Lammps input file (*.in) of the specific simulation<br> - Lammps data file (*.data, molecular style) of the investigated sample<br> - LAMMPS_out: resulting Lammps data and restart (*.rst) files and simulation results (Lammps thermo_out) in&nbsp;<br> tabulated form, an overview of the columns is given in the respective folders</p> <p>The following folders contain the results obtained under stochastic boundary conditions using the Capriccio method [3]:<br> - best: equilibration with the parameter set considered to be most suitable for the MD-FE coupled equilibration<br> - biax: biaxial loading<br> - bridging: equilibration with different adaptivity levels of the bridging domain<br> - descr_obs: equilibration with a Lagrangian frame for the description of the observation region<br> - dpd: equilibration with different thicknesses of the dissipative particle dynamics (DPD) region<br> - friccoeff: equilibration with different friction coefficients applied in the dissipative particle dynamics region<br> - fur: equilibration with different numbers of fur beads&nbsp;<br> - gausspoints: equilibration with different numbers of quadrature points per direction&nbsp;<br> - min: equilibration applying an initial, static energy minimization<br> - nodes: equilibration with a higher number of finite element nodes<br> - shifted: equilibration with particle systems obtained at different positions and points in time within the periodic master system<br> - smdcub: equilibration with different remaining stiffness ratios for the cubic modified weighting factor<br> - smdlin: equilibration with different remaining stiffness ratios for the linear modified weighting factor<br> - timestepsize: equilibration with different molecular dynamics time step sizes<br> - ut: uniaxial tension<br> - ut_friccoeff: uniaxial tension with different friction coefficients applied in the dissipative particle dynamics region<br> - weighting: equilibration with different energy weighting functions<br> - youngsmod: equilibration with different Young&#39;s moduli<br> Each simulation directory contains:<br> - input_files: Abaqus [4] input file (*.inp) and Lammps data file (*.data, molecular style) of the investigated sample<br> - MD_data: Results evaluated in the molecular dynamics region. MD_data contains the following subfolders:&nbsp;<br> anchorforces (dumped force components on the anchor points (AP) in kcal/mol, files anchorforce_[load step]_[MD-FE iteration].AF),&nbsp;<br> data (resulting Lammps data files *.[load step].[MD-FE iteration].data), Density (dumped mass density in the observation region in kg/m^3),&nbsp;<br> Energy (dumped total (kinetic + potential), angle, bond, and pair energies in kcal/(mol*Angstrom)), Strain (integral strains in the<br> observation region in x-, y-, and z-direction calculated by means of the Matlab [5] script calc_OBSstrain.m),<br> Stress (stresses in the observation region in MPa), and Temperature (temperature in the observation region in K)<br> - job.out: simulation log file<br> - meta.info: meta data of the specific Lammps simulation<br> Information on the subfolders is given in the respective folders.</p> <p><strong>References:</strong><br> [1] F. Weber, M. Ries, C. Bauer, C. R. Wick, S. Pfaller, &quot;On equilibrating non-periodic molecular dynamics samples for coupled<br> particle-continuum simulations of amorphous polymers&quot;, Forces in Mechanics, 2023, 10, 100159.<br> [2] A. P. Thompson, H. M. Aktulga, R. Berger, D. S. Bolintineanu, W. M. Brown, P. S. Crozier, P. J. in &#39;t Veld, A. Kohlmeyer,&nbsp;<br> S. G. Moore, T. D. Nguyen, R. Shan, M. J. Stevens, J. Tranchida, C. Trott, S. J. Plimpton, &quot;LAMMPS - a flexible simulation tool&nbsp;<br> for particle-based materials modeling at the atomic, meso, and continuum scales&quot;, Computer Physics Communications, 2022, 271, 108171.<br> [3] S. Pfaller, M. Rahimi, G. Possart, P. Steinmann, F. M&uuml;ller-Plathe, M. C. B&ouml;hm, &quot;An Arlequin-based method to couple molecular dynamics&nbsp;<br> and finite element simulations of amorphous polymers and nanocomposites&quot;, Computer Methods in Applied Mechanics and Engineering,&nbsp;<br> 2013, 260, 109-129.&nbsp;<br> [4] Dassault Syst&egrave;mes, &quot;Abaqus documentation&quot;, URL: https://abaqus-docs.mit.edu/2017/English/SIMACAEEXCRefMap/simaexc-c-docproc.htm.<br> [5] The MathWorks, Inc, &quot;MATLAB. The Language of Technical Computing&quot;, URL: https://de.mathworks.com/help/matlab/.</p> <p><strong>Funding:</strong><br> This research was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) -<br> 377472739/GRK 2423/1-2019. The authors are very grateful for this support. Sebastian Pfaller is furthermore<br> funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) - 396414850 (Individual<br> Research Grant &rsquo;Identifikation von Interphaseneigenschaften in Nanokompositen&rsquo;).</p>

opencc-by-4.0Dec 2022View details →
zenodo36/100

ConforMine Molecular Dynamics Data: Conformational Variability, Secondary Structure Propensities and Molecular Dynamics Simulations

<pre>This dataset contains all the data used to calculate Conformational Variability (ConVa) and Conformational Propensities as well as to train ConforMine. Each directory one level below this document contains another readme for further explanation on the contained data. The following information can be found in this dataset: </pre> <ul> <li>ConforMine_MD_training_sequences.fasta: FASTA file with the amino acid sequences of all used proteins.</li> <li>simulations (directory): Contains all the raw data derived from the MD simulations.</li> <li>ConforMine_training_MD_dihedrals (directory): Contains .xvg files with the dihedral angles of each amino acid at each step of the MD simulation.</li> <li>ConforMine_training_data_conformational_variability (directory): Contains the Conformational Variability values for all amino acids. Each file contains all ConVa values for a whole protein. The data is provided in .csv and .npy format.</li> <li>ConforMine_training_data_conformational_propensities (directory): Contains the Conformational Propensities values for all amino acids. Each file contains all propensities for a whole protein. The data is provided in .csv and .npy format.</li> </ul>

opencc-by-4.0Jan 2023View details →
zenodo36/100

Input data for Reversible Unwrapping Algorithm for Constant-Pressure Molecular Dynamics Simulations

<p>As described in the main text, here is the input data used for simulation, as well as analysis directories.&nbsp;The archive was generated in my project folder with &quot;tar --exclude=*trr --exclude=pbctools --exclude=qtwrap --exclude=old* --exclude=*npz --exclude=*pdf --exclude=*png --exclude=*ppm --exclude=*dcd* --exclude=*xtc --exclude=*slurm* --exclude=core* --exclude=*sh --exclude=*xvg --exclude=*out --exclude=*git* --exclude=*edr --exclude=*log --dereference -zcvf kulke-$(date +&quot;%F&quot;).tar.gz data figures scripts Simulations&quot;. Big data and trajectory files were excluded to keep the archive size small. The archive includes all necessary files to reproduce the simulations, analysis and figures for the publication.</p>

opencc-by-4.0Feb 2023View details →
zenodo36/100

Effect of Single-Residue Mutations on CTCF Binding to DNA: Insights from Molecular Dynamics Simulations

<p>Supplementary dataset for manuscript &quot;Effect of Single-Residue Mutations on CTCF Binding to DNA: Insights from Molecular Dynamics Simulations&quot;.&nbsp;</p>

opencc-by-4.0Mar 2023View details →
zenodo36/100

Movie of the molecular dynamics simulation of a crucial step in the activation of the STING protein

<p>STING (stimulator of interferon genes) is a homodimer protein involved in regulation of the innate immune system and plays a role in antitumor immunity by inducing the production of cytokines. Activation of STING stems from binding of endogenous cyclic dinucleotides (CDNs), which induce a conformational change to initiate signaling. The MP4 movie shows a molecular dynamics simulation of a crucial step of the activation process.</p>

opencc-by-4.0Mar 2023View details →
zenodo36/100

Movie of the molecular dynamics simulation of the opening and closing of the Cullin-RING protein complex

<p>Heterobifunctional degraders, which consist of two separate protein binding moieties (the warhead and the E3-ligand) joined by a linker, are a class of molecules that &quot;induce proximity&quot; between a target protein of interest (POI) and a E3 ubiquitin ligase. This induced proximity can lead to ubiquitination of the POI and its subsequent proteosomal degradation through a complex machinery of proteins. TPD present a novel approach to drug protein targets, since a single degrader molecule can induce catalytic degradation of the POI and potentially offer an avenue to eliminate targets traditionally labeled as undruggable by classical therapeutic strategies. Here we probe the conformational landscape of the full CRL macromolecular assembly and present a MP4 trajectory movie showing the molecular dynamics simulation of the large-scale conformational change during the opening and closing of the Cullin-RING protein complex.</p>

opencc-by-4.0Mar 2023View details →
zenodo36/100

Molecular dynamics (MD) simulations methods and results on cyclooctene oxides in ACN/water hybrid electrolytes

<p><strong>Molecular dynamics (MD) simulations methods and extended results used for the <em>Perspective</em> article entitled</strong></p> <p>&ldquo;Fine tuning of electrosynthesis pathways by modulation of electrolyte solvation structure&rdquo;</p>

opencc-by-4.0Apr 2023View details →
zenodo36/100

Molecular Simulation Data Associated with the Manuscript "Function and dynamics of the intrinsically disordered carboxyl terminus of β2 adrenergic receptor"

<p>Molecular Simulation Data Associated with the Manuscript<br> <br> &quot;Function and dynamics of the intrinsically disordered carboxyl terminus of &beta;2 adrenergic receptor&quot;<br> <br> by Jie Heng, Yunfei Hu, Guillermo P&eacute;rez-Hern&aacute;ndez, Asuka Inoue, Jiawei Zhao, Xiuyan Ma, Xiaoou Sun, Kouki Kawakami, Tatsuya Ikuta, Jienv Ding, Yujie Yang, Lujia Zhang, Sijia Peng, Xiaogang Niu, Hongwei Li, Ramon Guix&agrave;-Gonz&aacute;lez, Changwen Jin, Peter W. Hildebrand, Chunlai Chen &amp; Brian K. Kobilka</p> <p>Nature Communications 2023, <a href="https://doi.org/10.1038/s41467-023-37233-1">https://doi.org/10.1038/s41467-023-37233-1</a><br> <br> The representative molecular dynamics (MD) trajectories shown in the <strong>Supplementary Fig. 8,<br> Variable contacts of the &beta;2AR CT</strong> can be 3D visualized in the browser in the following link:</p> <ul> <li><a href="https://proteinformatics.uni-leipzig.de/mdsrv.html?load=file://base/B2CT/variants.ngl">&nbsp;https://proteinformatics.uni-leipzig.de/mdsrv.html?load=file://base/B2CT/variants.ngl</a></li> </ul>

opencc-by-4.0Apr 2023View details →
zenodo36/100

EMD data for the paper "Impact of ad-hoc post-processing parameters on the lubricant viscosity calculated with equilibrium molecular dynamics simulations"

<p>This archive contains the post-processing data obtained from EMD simulations of <strong>2,2,4-Trimethylhexane</strong> lubricant molecule under various operating conditions. The EMD simulations were performed using LAMMPS with COMPASS force field. (See manuscript and README for details.)</p>

opencc-by-4.0Mar 2023View details →
zenodo36/100

Protein Structure Files and Galaxy Workflows for Conducting Molecular Dynamics Simulations of Flavivirus Helicases -- Output Files

<p>These are the output files generated using the input files and Galaxy workflows for flavivirus helicase simulations,&nbsp;from:&nbsp;</p> <pre>https://doi.org/10.5281/zenodo.7493015</pre>

opencc-zeroApr 2023View details →
zenodo36/100

Molecular dynamics simulation input files: Histone Tail Electrostatics Modulate E2-E3 Enzyme Dynamics: A Gateway to Regulate Ubiquitination Machinery

<p>Molecular dynamics simulation input files:&nbsp;Histone Tail Electrostatics Modulate E2-E3 Enzyme Dynamics: A Gateway to Regulate Ubiquitination Machinery (<a href="https://zenodo.org/record/7423328">https://zenodo.org/record/7423328</a>)</p>

opencc-by-4.0Dec 2022View details →
zenodo36/100

Molecular dynamics simulations of CD59 and CD59-inhibited Membrane Attack Complex

<p>Coarse-grain (CG) trajectories of CD59-C5b8 (last 1,500 ns):</p> <ul> <li>cd59-c5b8_1500ns_rep1.xtc</li> <li>cd59-c5b8_1500ns_rep2.xtc</li> <li>cd59-c5b8_1500ns_rep3.xtc</li> </ul> <p>PyLipID analysis results from CG CD59-C5b8 simulations:</p> <ul> <li>Interactions_CHOL.csv</li> <li>Interactions_DOPC.csv</li> </ul> <p>Atomistic CD59 simulations in DOPC membrane:</p> <ul> <li>cd59_at_rep1_light.trr</li> <li>cd59_at_rep2_light.trr</li> <li>cd59_at_rep3_light.trr</li> </ul> <p>CD59 Euler angles relative to the membrane:&nbsp;</p> <ul> <li>rep1.csv</li> <li>rep2.csv</li> <li>rep3.csv</li> </ul> <p>All xtc and trr files were down-sampled (frames removed) to decrease file size.</p>

opencc-by-4.0Jun 2023View details →
zenodo36/100

AutoParams: An Automated Web-Based Tool To Generate Parameters for Molecular Dynamics Simulations

<p>Dataset of thirteen (13) compounds used to test the AutoParams webserver.&nbsp; Includes initial PDB files, generated parameters (mol2/frcmod files), and resulting AMBER-formatted MD inputs (prmtop/inpcrd).&nbsp; Additionally, includes 2D structure in PNG format and canonical SMILES string in .smi file format.</p>

opencc-by-4.0Jul 2023View details →
zenodo36/100

Supporting data for:"An accurate and efficient SAXS/SANS implementation including solvation layer effects suitable for restrained Molecular Dynamics simulations."

<p>PLUMED_NEST_REPO.zip contains the plumed.dat file and the template PDB used to perform the metainference MD simulations of Gelsolin and UP1-RNA, with and without the Solvation Layer Contribution.</p> <p>TRAJECTORIES.zip contains the Gelsolin and UP1-RNA trajectories and additional data generated with GROMACS. In details:</p> <p>-Gelsolin. Production Molecular Dynamics Parameter file (production.mdp), a&nbsp;topology file (topol.top), and 3 folders: TPRs (with 10 TPR files -one for each replica-), TRJ_SLC_OFF (with data from simulations without Solvation Layer Contribution), and TRJ_SLC_ON (with data from simulations with Solvation Layer Contribution). The last two contain an index file, a trajectory obtained from the concatenation of the 10 replicas (concat.xtc), and a template PDB file.</p> <p>-UP1-RNA. TPR file (md.tpr) and 2 folders: TRJ_SLC_OFF (with data from simulations without solvent correction), and TRJ_SLC_ON (with data from simulations with solvent correction). Each folder contains an index file, a template PDB file and a trajectory file (trj.xtc)</p> <p>&nbsp;</p>

opencc-by-4.0Jul 2023View details →

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