cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.21942/uva.20485194.v1
title: EntF*-D6

description: molecular dynamics simulation of the EntF* peptide, residue 6 in D form <br> starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide <br> topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 7, [NaCl] = 50 mM <br> md settings md.mdp: time step 2 fs, temperature = 298 K, pressure = 1 bar <br> 1 microsecond trajectory dry.xtc, dry.groframe rate 1 ps, water and ions removed, box centered on peptide <br> analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))<br>
DOI: 10.21942/uva.20485206
title: EntF*-D7

description: molecular dynamics simulation of the EntF* peptide, residue 7 in D form <br> -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485206.v2
title: EntF*-D7

description: molecular dynamics simulation of the EntF* peptide, residue 7 in D form <br> -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485206.v1
title: EntF*-D7

description: molecular dynamics simulation of the EntF* peptide, residue 7 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 7, [NaCl] = 50 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 1 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485209
title: EntF*-D8

description: molecular dynamics simulation of the EntF* peptide, residue 8 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485209.v2
title: EntF*-D8

description: molecular dynamics simulation of the EntF* peptide, residue 8 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485209.v1
title: EntF*-D8

description: molecular dynamics simulation of the EntF* peptide, residue 8 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 7, [NaCl] = 50 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 1 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485257
title: EntF*-D9

description: molecular dynamics simulation of the EntF* peptide, residue 9 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485257.v2
title: EntF*-D9

description: molecular dynamics simulation of the EntF* peptide, residue 9 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485257.v1
title: EntF*-D9

description: molecular dynamics simulation of the EntF* peptide, residue 9 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 7, [NaCl] = 50 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 1 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485338
title: EntF*-D10

description: molecular dynamics simulation of the EntF* peptide, residue 10 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485338.v1
title: EntF*-D10

description: molecular dynamics simulation of the EntF* peptide, residue 10 in D form-starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide-topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 7, [NaCl] = 50 mM, disulfide bond generated between residues 14 and 6-md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar-1 microsecond trajectory dry.xtc, dry.groframe rate 1 ps, water and ions removed, box centered on peptide-analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485338.v2
title: EntF*-D10

description: molecular dynamics simulation of the EntF* peptide, residue 10 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485395
title: EntF*-D11

description: molecular dynamics simulation of the EntF* peptide, residue 11 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485395.v1
title: EntF*-D11

description: molecular dynamics simulation of the EntF* peptide, residue 11 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485401
title: EntF*-D12

description: molecular dynamics simulation of the EntF* peptide, residue 12 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485401.v2
title: EntF*-D12

description: molecular dynamics simulation of the EntF* peptide, residue 12 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485401.v1
title: EntF*-D12

description: molecular dynamics simulation of the EntF* peptide, residue 12 in D form-starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide-topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 7, [NaCl] = 50 mM, disulfide bond generated between residues 14 and 6-md settings md.mdptime step 2 fs, temperature = 298 K, pressure = 1 bar-1 microsecond trajectory dry.xtc, dry.groframe rate 1 ps, water and ions removed, box centered on peptide-analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.5281/zenodo.6969801
title: Closed

description: Closed
DOI: 10.5281/zenodo.6969802
title: Closed

description: Closed
DOI: 10.21942/uva.20485407
title: EntF*-D13

description: molecular dynamics simulation of the EntF* peptide, residue 13 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485407.v1
title: EntF*-D13

description: molecular dynamics simulation of the EntF* peptide, residue 13 in D form -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485419
title: EntF*-D15

description: molecular dynamics simulation of the EntF* peptide, residue 15 in D form <br> -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide <br> -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 <br> -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide <br> -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485419.v1
title: EntF*-D15

description: molecular dynamics simulation of the EntF* peptide, residue 15 in D form <br> -starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide <br> -topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 <br> -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide <br> -analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains)) <br>
DOI: 10.21942/uva.20485416
title: EntF*-D14

description: molecular dynamics simulation of the EntF* peptide, residue 14 in D form starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 md settings md.mdp: time step 2 fs, temperature = 298 K, pressure = 1 bar 1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.21942/uva.20485416.v1
title: EntF*-D14

description: molecular dynamics simulation of the EntF* peptide, residue 14 in D form starting coordinates posre.gro: energy minimized and water+ions equilibrated around peptide topology topol.top: force field AMBER99SB-ILDB, TIP3P water, protonation states at pH = 3 (E,K protonated), [NaCl] = 25 mM, disulfide bond generated between residues 14 and 6 md settings md.mdp: time step 2 fs, temperature = 298 K, pressure = 1 bar 1 microsecond trajectory dry.xtc, dry.groframe rate 10 ps, water and ions removed, box centered on peptide analysis files: radius of gyration, solvent accessible surface area (hydrophilic (backbone + hydrophilic side chains), hydrophobic (hydrophobic side chains))
DOI: 10.5281/zenodo.6894974
title: Closed

description: Closed.
DOI: 10.5281/zenodo.6894975
title: Closed

description: Closed.
DOI: 10.18112/openneuro.ds003721.v1.0.1
title: A naturalistic paradigm to investigate post-encoding neural activation patterns in relation to subsequent voluntary and intrusive recall of distressing events
DOI: 10.6084/m9.figshare.20488980.v1
title: Wheelchair-Group 1.csv

description: This is the vibration data of wheelchair experiment, collected by EPH-V11 vibration sensor.
DOI: 10.6084/m9.figshare.20488980
title: Wheelchair vibration data

description: This is the vibration data of wheelchair experiment, collected by EPH-V11 vibration sensor.
DOI: 10.6084/m9.figshare.20488962
title: Rehabilitation training vibration data

description: This is the vibration data of rehabilitation training, collected by EPH_V11 vibration sensor.
DOI: 10.6084/m9.figshare.20488980.v2
title: Wheelchair vibration data.csv

description: This is the vibration data of wheelchair experiment, collected by EPH-V11 vibration sensor.
DOI: 10.6084/m9.figshare.20488905
title: Human fall vibration data

description: It is the physical human fall vibration data, collected by EPH-V11 vibration sensor.
DOI: 10.6084/m9.figshare.20488905.v2
title: Human fall vibration data.csv

description: It is the physical human fall vibration data, collected by EPH-V11 vibration sensor.
DOI: 10.6084/m9.figshare.20488962.v1
title: Rehabilitation training vibration data.csv

description: This is the vibration data of rehabilitation training, collected by EPH_V11 vibration sensor.
DOI: 10.5517/cctwnkw
title: CCDC 771359: Experimental Crystal Structure Determination

description: Related Article: G.Laus, K.Wurst, V.Kahlenberg, H.Kopacka, C.Kreutz, H.Schottenberger|2010|Z.Naturforsch.,B:Chem.Sci.|65|776|
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc251gpd
title: CCDC 1997413: Experimental Crystal Structure Determination

description: Related Article: Uwe Monkowius|2020|CSD Communication|||
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc251nhd
title: CCDC 1997593: Experimental Crystal Structure Determination

description: Related Article: Marina Saab, David J. Nelson, Nikolaos V. Tzouras, Tahani A. C. A. Bayrakdar, Steven P. Nolan, Fady Nahra, Kristof Van Hecke|2020|Dalton Trans.|49|12068|doi:10.1039/D0DT02558E
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc251njf
title: CCDC 1997594: Experimental Crystal Structure Determination

description: Related Article: Marina Saab, David J. Nelson, Nikolaos V. Tzouras, Tahani A. C. A. Bayrakdar, Steven P. Nolan, Fady Nahra, Kristof Van Hecke|2020|Dalton Trans.|49|12068|doi:10.1039/D0DT02558E
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc251nkg
title: CCDC 1997595: Experimental Crystal Structure Determination

description: Related Article: Marina Saab, David J. Nelson, Nikolaos V. Tzouras, Tahani A. C. A. Bayrakdar, Steven P. Nolan, Fady Nahra, Kristof Van Hecke|2020|Dalton Trans.|49|12068|doi:10.1039/D0DT02558E
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc25m9bg
title: CCDC 2014545: Experimental Crystal Structure Determination

description: Related Article: Jan-Erik Siewert, André Schumann, Malte Fischer, Christoph Schmidt, Tobias Taeufer, Christian Hering-Junghans|2020|Dalton Trans.|49|12354|doi:10.1039/D0DT02435J
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc25m9ch
title: CCDC 2014546: Experimental Crystal Structure Determination

description: Related Article: Jan-Erik Siewert, André Schumann, Malte Fischer, Christoph Schmidt, Tobias Taeufer, Christian Hering-Junghans|2020|Dalton Trans.|49|12354|doi:10.1039/D0DT02435J
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.