cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccdc.csd.cc27kx91
title: CCDC 2072793: Experimental Crystal Structure Determination

description: Related Article: Allegra Franchino, Àlex Martí, Stefano Nejrotti, Antonio M. Echavarren|2021|Chem.-Eur.J.|27|11989|doi:10.1002/chem.202101751
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.cc27kxb2
title: CCDC 2072794: Experimental Crystal Structure Determination

description: Related Article: Allegra Franchino, Àlex Martí, Stefano Nejrotti, Antonio M. Echavarren|2021|Chem.-Eur.J.|27|11989|doi:10.1002/chem.202101751
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.cc2bdr8s
title: CCDC 2157205: Experimental Crystal Structure Determination

description: Related Article: De-Bing Pu, Jing Lin, Xiao-Jia Pu, Qi Wang, Xiao-Ning Li, Yan Qi, Xiao-Si Li, Xiao-Li Li, Rui-Han Zhang, Xing-Jie Zhang, Chun-Ping Wan, Wei-Lie Xiao|2022|Bioorg.Chem.|128|106022|doi:10.1016/j.bioorg.2022.106022
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.cc2bdr9t
title: CCDC 2157206: Experimental Crystal Structure Determination

description: Related Article: De-Bing Pu, Jing Lin, Xiao-Jia Pu, Qi Wang, Xiao-Ning Li, Yan Qi, Xiao-Si Li, Xiao-Li Li, Rui-Han Zhang, Xing-Jie Zhang, Chun-Ping Wan, Wei-Lie Xiao|2022|Bioorg.Chem.|128|106022|doi:10.1016/j.bioorg.2022.106022
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.cc2bdrbv
title: CCDC 2157207: Experimental Crystal Structure Determination

description: Related Article: De-Bing Pu, Jing Lin, Xiao-Jia Pu, Qi Wang, Xiao-Ning Li, Yan Qi, Xiao-Si Li, Xiao-Li Li, Rui-Han Zhang, Xing-Jie Zhang, Chun-Ping Wan, Wei-Lie Xiao|2022|Bioorg.Chem.|128|106022|doi:10.1016/j.bioorg.2022.106022
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.cc2bdrcw
title: CCDC 2157208: Experimental Crystal Structure Determination

description: Related Article: De-Bing Pu, Jing Lin, Xiao-Jia Pu, Qi Wang, Xiao-Ning Li, Yan Qi, Xiao-Si Li, Xiao-Li Li, Rui-Han Zhang, Xing-Jie Zhang, Chun-Ping Wan, Wei-Lie Xiao|2022|Bioorg.Chem.|128|106022|doi:10.1016/j.bioorg.2022.106022
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.cc2bdrdx
title: CCDC 2157209: Experimental Crystal Structure Determination

description: Related Article: De-Bing Pu, Jing Lin, Xiao-Jia Pu, Qi Wang, Xiao-Ning Li, Yan Qi, Xiao-Si Li, Xiao-Li Li, Rui-Han Zhang, Xing-Jie Zhang, Chun-Ping Wan, Wei-Lie Xiao|2022|Bioorg.Chem.|128|106022|doi:10.1016/j.bioorg.2022.106022
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.cc2bhvpd
title: CCDC 2160194: Experimental Crystal Structure Determination

description: Related Article: Stephen Raja Rubina, Philip Raja Stalin, C. Selva Meenatchi, Sepperumal Murugesan, Raju Ranjith Kumar|2022|J.Mol.Struct.|1269|133724|doi:10.1016/j.molstruc.2022.133724
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.cc2bm246
title: CCDC 2163277: Experimental Crystal Structure Determination

description: Related Article: Yingqi Wang, Sheng Zhang, Xiujuan Feng, Xiaoqiang Yu, Masahiko Yamaguchi, Ming Bao|2022|J.Org.Chem.|87|10531|doi:10.1021/acs.joc.2c01233
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: 10.5281/zenodo.6907480
title: Hebban Reviews

description: This dataset consists of 200k+ Dutch book reviews taken from hebban.nl accompanied with a five-point rating (1-5) as well as negative, neutral, and positive sentiment scores. The dataset is intended for Dutch sentiment analysis. In addition to review text and rating, metadata for the reviews was also collected such as the review title, the number of likes and comments this review received, the number of quotes in the review, and its publication date. Every review has a book_id, which can be used in conjunction with the `hebban-books` dataset. That accompanying dataset contains books (which can be queried with the same IDs as the IDs in the current dataset) and their metadata. See the Hugging Face dataset page for more information.
description: It is very likely that there is regional bias in the dataset: considering that the website is Dutch (`hebban.nl`), its contents are especially of the variant of Dutch that is written in the Netherlands, which may differ from Dutch in e.g., Flanders or Suriname. Take this into account when training a model on this dataset and then applying it to other varieties of Dutch!
DOI: 10.5281/zenodo.6907481
title: Hebban Reviews

description: This dataset consists of 200k+ Dutch book reviews taken from hebban.nl accompanied with a five-point rating (1-5) as well as negative, neutral, and positive sentiment scores. The dataset is intended for Dutch sentiment analysis. In addition to review text and rating, metadata for the reviews was also collected such as the review title, the number of likes and comments this review received, the number of quotes in the review, and its publication date. Every review has a book_id, which can be used in conjunction with the `hebban-books` dataset. That accompanying dataset contains books (which can be queried with the same IDs as the IDs in the current dataset) and their metadata. See the Hugging Face dataset page for more information.
description: It is very likely that there is regional bias in the dataset: considering that the website is Dutch (`hebban.nl`), its contents are especially of the variant of Dutch that is written in the Netherlands, which may differ from Dutch in e.g., Flanders or Suriname. Take this into account when training a model on this dataset and then applying it to other varieties of Dutch!
DOI: 10.21942/uva.20485017
title: EntF*-L

description: Molecular dynamics simulation of the EntF* peptide, all residues in L 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide <br> -analysis files frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains)) <br> <br>
DOI: 10.21942/uva.20485017.v3
title: EntF*-L

description: Molecular dynamics simulation of the EntF* peptide, all residues in L 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide <br> -analysis files frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains)) <br> <br>
DOI: 10.21942/uva.20485017.v2
title: EntF*-L

description: molecular dynamics simulation of the EntF* peptide, all residues in L 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 = 7, [NaCl] = 50 mM, disulfide bond generated between residues 14 and 6 -md settings md.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.gro frame rate 1 ps, water and ions removed, box centered on peptide <br> -analysis files: radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains)) <br> <br>
DOI: 10.21942/uva.20485035
title: EntF*-D1

description: Molecular dynamics simulation of the EntF* peptide, residue 1 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide <br> -analysis files frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485035.v2
title: EntF*-D1

description: Molecular dynamics simulation of the EntF* peptide, residue 1 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar <br> -1 microsecond trajectory dry.xtc, dry.gro frame rate 10 ps, water and ions removed, box centered on peptide <br> -analysis files frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485035.v1
title: EntF*-D1

description: molecular dynamics simulation of the EntF* peptide, residue 1 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame 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.20485056
title: EntF*-D2

description: Molecular dynamics simulation of the EntF* peptide, residue 2 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485056.v2
title: EntF*-D2

description: Molecular dynamics simulation of the EntF* peptide, residue 2 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485056.v1
title: EntF*-D2

description: molecular dynamics simulation of the EntF* peptide, residue 2 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame 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.20485188
title: EntF*-D5

description: Molecular dynamics simulation of the EntF* peptide, residue 5 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485188.v2
title: EntF*-D5

description: Molecular dynamics simulation of the EntF* peptide, residue 5 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485188.v1
title: EntF*-D5

description: molecular dynamics simulation of the EntF* peptide, residue 5 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.20485164
title: EntF*-D4

description: Molecular dynamics simulation of the EntF* peptide, residue 4 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485164.v3
title: EntF*-D4

description: Molecular dynamics simulation of the EntF* peptide, residue 4 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485164.v2
title: EntF*-D4

description: molecular dynamics simulation of the EntF* peptide, residue 4 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame 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.20485059
title: EntF*-D3

description: Molecular dynamics simulation of the EntF* peptide, residue 3 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485059.v2
title: EntF*-D3

description: Molecular dynamics simulation of the EntF* peptide, residue 3 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.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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))
DOI: 10.21942/uva.20485059.v1
title: EntF*-D3

description: molecular dynamics simulation of the EntF* peptide, residue 3 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.mdp time step 2 fs, temperature = 298 K, pressure = 1 bar -1 microsecond trajectory dry.xtc, dry.gro frame 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.20485194
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 -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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))<br>
DOI: 10.21942/uva.20485194.v2
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 -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 frame rate 1 ps radius of gyration, solvent accessible surface area (hydrophilic parts (backbone + hydrophilic side chains), hydrophobic parts (hydrophobic side chains))<br>