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872 results for “ligand”
Helical dinuclear 3d metal complexes with bis(bidentate) [S,N] ligands: synthesis, structural and computational studies
<h1>Raw data for the publication entitled:</h1> <h2>Helical dinuclear 3d metal complexes with bis(bidentate)<br>[S,N] ligands: synthesis, structural and computational<br>studies</h2> <p><em>Dalton Transactions</em>, <strong>2024</strong>, DOI: 10.1039/D4DT02395A</p> <p>Authors:<br>Jamie Allen, Jörg Saßmannshausen, Kuldip Singh, Alexander F. R. Kilpatrick*</p> <p>These folders contain the raw data which were used to prepare the above publication.</p> <h1>Information regarding the raw files of the DFT calculations.</h1> <p>The zip-files in this section containing the raw-data of the DFT calculations leading to the Zn, Co and Fe calculated structures. As filenames are notoriously bad in handling special characters, the names of the folder appear different from what is being used in the final publication. We try to provide as much information as possible to facilitate the usage of these results.</p> <p>Thus:</p> <table> <tbody> <tr> <th>Abbreviation publication</th> <th>Abbreviation folder</th> <th>Abbreviation filename</th> </tr> </tbody> <tbody> <tr> <td>[Zn(<strong>3</strong>)<sub>2</sub>]</td> <td>Zn3-2</td> <td>SNdipp2Zn</td> </tr> <tr> <td>[Co(<strong>3</strong>) <sub>2</sub>]</td> <td>Co3-2</td> <td>SNdipp2Co</td> </tr> <tr> <td>[Fe(<strong>3</strong>) <sub>2</sub>]</td> <td>Fe3-2</td> <td>SNdipp2Fe</td> </tr> <tr> <td>[Zn<sub>2</sub>(μ-<strong>2</strong>)<sub>2</sub>]</td> <td>Zn2-2</td> <td>zn2</td> </tr> <tr> <td>[Co<sub>2</sub>(μ-<strong>2</strong>)<sub>2</sub>]</td> <td>Co2-2</td> <td>co2</td> </tr> <tr> <td>[Fe<sub>2</sub>(μ-<strong>2</strong>)<sub>2</sub>]</td> <td>Fe2-2</td> <td>fe2</td> </tr> </tbody> </table> <p>Some test calculations were performed as well utilizing Gaussian-09. They can be found in a folders with the suffix <em>-G09</em> or <em>-g09</em>.</p> <p>The closed shell compound [Zn<sub>2</sub>(μ-<strong>2</strong>)<sub>2</sub>] was investigated further. In order to look into the influence of the used Grimme dispersion correction, we re-calculated the final result without that correction. These files are in the Zn2-2-pbe0 folder. Furthermore, we used [Zn<sub>2</sub>(μ-<strong>2</strong>)<sub>2</sub>] and removed one of the Zn atoms and replaced the dangling bonds with H. We then fully optimized that structure. The results are in the Zn2-2-cut folder.</p> <h1> </h1> <h1>Information regarding the raw characterisation data</h1> <p>The raw characterisation data files for all nuclear magnetic resonance (NMR) spectroscopy, infrared (IR) spectroscopy, cyclic voltammetry (CV), single crystal X-ray diffraction (XRD) and solution magnetometry studies are enclosed in separate .zip files.</p>
Structures of S-protein in complex with ligands deposited in the PDB between the 1st January 2021 and the 13th May 2021
<p>All 174 structures of SARS-CoV-2 S-protein in complex with a ligand released on the PDB between the 1<sup>st</sup> January 2021 and the 13<sup>th</sup> May 2021 were categorised by ligand type: hACE2, antibody Fab fragments, VHH antibody fragments or <em>de novo</em> designed peptide scaffolds. Information concerning the method by which the structures were determined and their resolution were retrieved from the PDB. The categorisation of ligands by S-protein binding site were achieved by visual analysis of all the structures using molecular visualisation software PyMOL, in which no new binding sites were found beyond those already categorised for the structures released on the PDB until the 1<sup>st</sup> January 2021 (10.5281/zenodo.5503855).</p> <p>The Pure project is funded by the European Union’s Horizon 2020 program under grant agreement No. 899732.</p> <p> </p>
List of the structures of S-protein in complex with ligands deposited in the Protein Data Bank until the 1st January 2021.
<p>All 131 structures of SARS-CoV-2 S-protein in complex with a ligand released on the PDB until the 1<sup>st</sup> January 2021 were categorised by ligand type: hACE2, antibody Fab fragments, VHH antibody fragments or <em>de novo</em> designed peptide scaffolds. The ligands’ amino acid sequences, the method by which the structures were determined and their resolution were retrieved from the PDB. Information regarding the ligands' production method, dissociation constants (K<sub>D</sub>), S-protein segment against which the K<sub>D</sub> were measured and the determination methods were retrieved from the respective references. The categorisation of ligands by S-protein binding site and listing of S-protein conformation in each structure were achieved by visual analysis of all the structures using molecular visualisation software PyMOL.</p>
LOBSTER (Ligand Overlays from Binding SiTe Ensemble Representatives)
<p>LOBSTER ("Ligand Overlays from Binding SiTe Ensemble Representatives") is a dataset of ligand overlays designed to evaluate small molecule superposition tools.</p> <p><br>Based on all structures from the RCSB PDB, the dataset generation and filtering protocols are fully automated to avoid subjectivity in the selection of protein-ligand complexes and to gain the largest possible set of refined compounds. Affinity and activity data have been processed to select ligands with a high ligand efficiency.<br>Ligands were superimposed in their crystal pose by aligning the corresponding binding pockets to so-called ensembles. For poses generated in benchmark experiments, this offers an objective comparison to the superimposed ligand crystal poses. A clustering of ensembles created with the same protein-ligand complexes ensures the diversity of the LOBSTER set.<br>The 671 ligand ensembles comprise a total of 3212 unique ligands from 3521 different protein-ligand complexes. A total of 72 734 ligand pairs have been derived from the ensembles. Ten subsets were generated from the pairs according to the shape overlap of the pairs, quantified by the Shape Tversky Index.</p>
LigPCDS: Labeled Dataset of X-ray Protein Ligand Images in 3D Point Cloud and Validated Deep Learning Models
<p>The difference electron density from X-ray protein crystallography was used to create the first dataset of labeled ligand images in 3D point clouds, named <strong>LigPCDS</strong>. The dataset contain 244,226 entries of free organic ligands containing 3D representations labeled with two major labeling approaches: SP-based and AtomSymbol-based.</p> <p> </p> <p>The data from free organic molecules (non-covalent ligands) was retrieved from the Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB PDB) in december 2019 with resolutions ranging from 1.5 to 2.2 Å. The ligand images (blobs) were interpolated from their calculated difference electron density map in a 3D grid-like bounding box, around their atomic positions, and stored in point clouds. These ligand grid representations were further processed to retrive the final ligands representation in 3D point clouds using a mask of the shape of the ligand. A grid spacing of 0.5 Å gave the best results. The density value of the grid points was used as feature. The labeling approach used the structure of the ligands to propose vocabularies of chemical classes based on the chemical atoms themselves and their cyclic substructures. These structure annotations were applied pointwise to the ligand 3D representations using an atomic sphere model. Four proposed vocabularies were validated by successfully training good performance deep learning models for the semantic segmentation of a stratified dataset from LigPCDS, using 78902 entries.</p> <p>The four validated deep learning models are: (i) the LigandRegion, composed by generic atoms of any type; (ii) the AtomCycle, composed by generic atoms outside cycles and generic cycles; (iii) the AtomC347CA56, composed by generic atoms outside cycles, not aromatic cycles of size 3 to 7 and aromatic cycles of size 5 and 6; and (iv) the AtomSymbolGroups, composed by the atoms symbols with groupings. The mean accuracy of these models in their cross-validation was between 49.7% <span lang="EN-GB">[-19.4,20.</span><span lang="EN-GB">2]</span> and 77.4% <span lang="EN-GB">[-11.7,12.1]</span> in terms of Intersection over Union (mIoU) metric and between 62.4% <span lang="EN-GB">[-18.8,19.</span><span lang="EN-GB">7]</span> and 87.0% <span lang="EN-GB">[-8.4,8.8]</span> in F1-score (mF1), confidence interval between squared brackets. The models i, ii and iii and the used labeled representations in 3D point cloud are contained in the SP-based record; and model iv and its used labeled representations are contained in the AtomSymbol-based record.</p> <p>The dataset and validated models may be used to tackle problems regarding known and unknown ligand building to drug discovery and fragment screening pipelines. </p> <p>The code used to create and validated the LigPCDS is available at the following repository: https://github.com/danielatrivella/np3_ligand</p> <p>This repository also contains the NP³ Blob Label application for ligand building using the validated deep learning models from LigPCDS.</p>
Ligand binding remodels protein side chain conformational heterogeneity
<p>While protein conformational heterogeneity plays an important role in many aspects of biological function, including ligand binding, its impact has been difficult to quantify. Macromolecular X-ray diffraction is commonly interpreted with a static structure, but it can provide information on both the anharmonic and harmonic contributions to conformational heterogeneity. Here, through multiconformer modeling of time- and space-averaged electron density, we measure conformational heterogeneity of 743 stringently matched pairs of crystallographic datasets that reflect unbound/apo and ligand-bound/holo states. When comparing the conformational heterogeneity of side chains, we observe that when binding site residues become more rigid upon ligand binding, distant residues tend to become more flexible, especially in non-solvent exposed regions. Among ligand properties, we observe increased protein flexibility as the number of hydrogen bonds decrease and relative hydrophobicity increases. Across a series of 13 inhibitor bound structures of CDK2, we find that conformational heterogeneity is correlated with inhibitor features and identify how conformational changes propagate differences in conformational heterogeneity away from the binding site. Collectively, our findings agree with models emerging from NMR studies suggesting that residual side chain entropy can modulate affinity and point to the need to integrate both static conformational changes and conformational heterogeneity in models of ligand binding.</p>
Geometric Frustration Directs the Self-assembly of Nanoparticles with Crystallized Ligand Bundles
<p>This is the supporting dataset of the publication "Geometric Frustration Directs the Self-assembly of Nanoparticles with Crystallized Ligand Bundles".</p> <p><a href="https://doi.org/10.1021/acs.jpcb.4c04562">https://doi.org/10.1021/acs.jpcb.4c04562</a></p> <p>The description of the dataset can be found in the file README.txt</p>
Data set for the journal article: Colloidal-ALD Grown Metal Oxide Shells Enable the Synthesis of Photoactive Ligand/ Nanocrystal Composite Materials
<p>The data for each figure of the main manuscript is included in this folder.</p> <p>Figure 1 is not included as it contains no data.</p> <p>The folder for Figure 2 contains a sub-folder for the EDX and NMR data of 9-ACA/PbS@AlOx. The NMR data was processed by Mestrenova.</p> <p>The folder for Figure 3 contains optical absorption spectrum data of 9-ACA/PbS@AlOx.</p> <p>The folder for Figure 4 contains NMR data which was processed by Mestrenova. It contains the data for 9-ACA/CuInS2@AlOx, 1-PCA/CsPbBr3@AlOx and 9-PTA/CsPbBr3@AlOx.</p> <p>The folder for Figure 5 is made of three sub-folders for figure 5A, 5B and 5C. 5A and 5B contain optical absorption for the CuInS2 and CsPbBr3 datasets while 5C contain time resolved data for CsPbBr3.</p> <p>The folder for Figure 6 contains time resolved PL for the as synthesized CsPbBr3, 1-PCA/CsPbBr3@AlOx and 9-PTA/CsPbBr3@AlOx. The 9-PTA/CsPbBr3@AlOx data contain two decays that span 200 ns (short) or 13.5 us (long).</p> <p>The folder for Figure 7 contains time resolved PL for the as synthesized 9-PTA/CsPbBr3@AlOx and 1-PCA/9-PTA/CsPbBr3@AlOx. For both samples the data contain two decays that span 200 ns (short) or 13.5 us (long). Also an NMR folder is present with the 1H spectrum for 9-PTA/CsPbBr3@AlOx and 1-PCA/9-PTA/CsPbBr3@AlOx.</p> <p> </p> <p> </p>
Dataset for Precursor Nuclearity and Ligand Effects in Atomically-Dispersed Heterogeneous Iron Catalysts for Alkyne Semi-Hydrogenation
<p>This dataset complements the publication entitled "Precursor Nuclearity and Ligand Effects in Atomically-Dispersed Heterogeneous Iron Catalysts for Alkyne Semi-Hydrogenation" by Dario Faust Akl, Andrea Ruiz-Ferrando, Dr. Edvin Fako, Dr. Roland Hauert, Dr. Olga Safonova, Dr. Sharon Mitchell, Prof. Núria López, Prof. Javier Pérez-Ramírez. Please refer to the Readme.txt file for information about the file structure and content.<br> </p>
Project files provided as supporting information to the manuscript "Ligand-protein interactions in lysozyme investigated through a dual-resolution model"
<p><strong>README file for the project files provided as supporting information to the manuscript "Ligand-protein interactions in lysozyme investigated through a dual-resolution model"</strong></p> <p>February 12, 2020</p> <p>Authors: Raffaele Fiorentini, Kurt Kremer and Raffaello Potestio</p> <p>================================</p> <p>Overview</p> <p>The dataset is organised in three (compressed) subfolders (see the tree diagrams in each section):</p> <p>- annihilation<br> - decoupling<br> - density</p> <p>The figure deltaG_binding_ann_dec_comparison.png shows the results of binding free energy calculations comparing the values obtained both for annihilation and decoupling.</p> <p>The figure deltaG_binding_annih_gromacs_espp.png displays the results for Binding FE, comparing the values obtained in GROMACS and ESPResSo++.</p> <p>The README.pdf file contains detailed information about these folders and their content.</p> <p>================================</p> <p>The "annihilation" folder contains all results concerning the calculation of binding free energy in case of annihilation and it is divided in two parts: </p> <p>- complex<br> - ligand</p> <p>In "complex" are reported the results of Ligand-Protein FE both in ESPResSo++ and GROMACS. All simulations are fully-atomistic. </p> <p>In "ligand" are reported the results of ligand solvation free energy both in ESPResSo++ and GROMACS. All simulations are fully-atomistic. </p> <p>====</p> <p>The "decoupling" folder contains all results concerning the calculation of binding free energy in case of decoupling and it is divided in three parts: </p> <p>- complex-DualRes<br> - complex-FullyAT<br> - ligand</p> <p>In "complex-DualRes" are reported the results of Ligand-Protein FE only in ESPResSo++ (GROMACS cannot do decoupling). The system is simulated in Dual-Resolution. It is possible to find the trajectory files in the sub-directories "lambdaindex-0" and "lambdaindex-30".</p> <p>In "complex-fullyAT" are reported the results of Ligand-Protein FE only in ESPResSo++. The system simulated is fully-atomistic. It is possible to find the trajectory file in the sub-directories "lambdaindex-0" and "lambdaindex-30".</p> <p>In "ligand" are reported the results of ligand solvation free energy only in ESPResSo++. All simulations are fully-atomistic. It is possible to find the trajectory file in the sub-directories "lambdaindex-0" and "lambdaindex-20".</p> <p>====</p> <p>The "density" folder contains the data for the tuning of the c parameter of the steric repulsion among residues. This parameter is tuned so that the water density attains the value computed in all-atom simulations.</p>
RNAPosers: Machine Learning Classifiers For RNA-Ligand Poses [Data Set]
<ul> <li>This dataset contains the decoys poses used to train and test RNAPosers, a set of RNA-ligand pose classifiers.</li> <li>The folder of each RNA-ligand complex (identified using its PDB ID) contains: <ul> <li>Ligand SMILES: lig.smi</li> <li>Ligand coordinate: lig.sd</li> <li>Receptor coordinate: receptor.mol2</li> <li>Pose coordinates: poses.sd</li> <li>Pose similarity data: rmsd.txt</li> </ul> </li> </ul>
Associated Data: RASPD+: Fast protein-ligand binding free energy prediction using simplified physicochemical features
<p>Additional digital data to "RASPD+: Fast protein-ligand binding free energy prediction using simplified physicochemical features" (ChemRxiv preprint:<a href="https://doi.org/10.26434/chemrxiv.12636704.v1">https://doi.org/10.26434/chemrxiv.12636704</a>).</p> <p>Associated code can be found at: <a href="https://github.com/HITS-MCM/RASPDplus">https://github.com/HITS-MCM/RASPDplus</a></p> <p>Files:</p> <ul> <li>weights.tar.gz: contains the model weights of one random dataset split and its associated crossvalidation folds. Used for standard RASPD+ evaluation.</li> <li>additional_model_replicates.tar.gz: contains the remaining models trained on the full set of descriptors.</li> <li>external_test_sets.tar.gz: contains the descriptor tables for all external test sets used</li> <li>dude.tar.gz: contains the descriptor tables for and several identifier lists for evaluation on the Directory of Useful Decoys - Enhanced (DUD-E)</li> <li>run_outputs.tar.gz: Performance metric data and predicted values created during the model training and evaluation runs. Basis for the figures and metrics in the manuscript.</li> </ul> <p> </p>
Data: Steering photoinduced electron transfer in intramolecular photocatalysts by peripheral ligand control
<p>The data presented herein is analysed and showcased within the <i>ChemRxiv</i> article titled "<i>Steering photoinduced electron transfer in intramolecular photocatalysts by peripheral ligand control</i>" (<a href="10.26434/chemrxiv-2023-vspb5"><strong>DOI </strong></a><a href="https://doi.org/10.26434/chemrxiv-2023-vspb5"><strong>10.26434/chemrxiv-2023-vspb5</strong></a>). Kindly acknowledge and cite this article when referencing or utilizing the provided data.</p>
The coupling mechanism of ligands with SERT distinguishes substrates from inhibitors (raw data)
<p>Raw data of the manuscript: Ligand coupling mechanism of the human serotonin transporter differentiates substrates from inhibitors</p> <p><strong>Abstract:</strong></p> <p>The presynaptic serotonin transporter (SERT) reuptakes the serotonin (5HT) released into the synaptic cleft, thus ensuring temporal and spatial regulation of serotonergic signalling. Clinically approved drugs used for the treatment of neurological disorders, including depression and anxiety modulate SERT by trapping the transporter in the outward-open conformation. Illicit drugs of abuse as amphetamines act as substrates but reverse the transport direction, thereby releasing intracellular accumulated 5HT. Both mechanisms increase extracellular 5HT levels. Stoichiometry of the transport cycle has been described by kinetic schemes, the structures of the main conformations within the transport cycle revealed static coordinates. By combining <em>in-silico</em> approaches with <em>in-vitro</em> experiments and making use of a homologous series of 5HT analogues, we decoded the essential coupling mechanism between the substrate and the transporter which triggers uptake. The free energy calculations showed that only scaffold-bound substrates can correctly close the extracellular gate by pulling on the bundle domain through long-range electrostatic interactions. The associated spatial and physico-chemical requirements define substrate and inhibitor properties, opening new possibilities for rational drug design approaches.</p>
Siloxide tripodal ligands as a scaffold for stabilizing lanthanides in the +IV oxidation state
<p>This upload contains raw data (NMR, X-Ray, EPR, Cyclic Voltammetry, UV, IR, Magnetism) files for the article</p>
Data for Publication: "Automated Investigation of Metal-Ligand Interactions by a Newly Established Robotic Workflow for Titrations"
<p>This dataset contains the whole primary and raw (original) data for the manuscript "Automated investigation of metal-ligand interactions by a newly established robotic workflow for titrations".</p>
A workflow for exploring ligand dissociation from a macromolecule: Efficient random acceleration molecular dynamics simulation and interaction fingerprint analysis of ligand trajectories
<p>Containes input data for MD simulations of 3 HSP90- small compound complexes from the paper</p> <p>A workflow for exploring ligand dissociation from a macromolecule: Efficient random acceleration molecular dynamics simulation and interaction fingerprint analysis of ligand trajectories" from Daria B. Kokh, Bernd Doser , Stefan Richter , Fabian Ormersbach , Xingyi Cheng, Rebecca C. Wade, publishe in J. Chem. Phys. <strong>153</strong>, 125102 (2020); <a href="https://doi.org/10.1063/5.0019088">https://doi.org/10.1063/5.0019088</a></p> <ul> <li>ref.pdb - structure of the complex in PDB format</li> <li>ref.prmtop - topology file in AMBER</li> <li>ref-equal-NTP.pdb - structure after NTP equilibration </li> <li>ref-equal-NTP.rst7 - coordinates after NTP equilibration</li> <li>ref-equal-NTP.crd - coordinates after NTP equilibration </li> <li>gromacs.gro - coordinates in Gromacs format (after NTP equalibration)</li> <li>gromacs.top - Gromacs topology </li> </ul> <p> </p>
G-Protein Coupled Receptor-Ligand Dissociation Rates and Mechanisms from tauRAMD Simulations
<p>Data and Python scripts used for generation and analysis of RAMD dissociation trajectories for several GPCR complexes (including example showing generation of the Protein-Ligand Interaction Fingerprints, IFP, for several representative RAMD trajectories),</p> <p>reported in the manuscript</p> <p>"G-Protein Coupled Receptor-Ligand Dissociation Rates and Mechanisms from tRAMD Simulations" "G-Protein Coupled Receptor-Ligand Dissociation Rates and Mechanisms from tauRAMD Simulations"</p> <p>by Daria B. Kokh, Rebecca C. Wade</p> <p>submitted to the Journal of Chemical Theory and Computation</p> <p> </p> <p>1. <strong>README.txt </strong>- instruction for script usage</p> <p>2. <strong>PDBs.zip</strong> - PDB structures of complexes in water box used in the analysis, ligand PDB and mol2 structures</p> <p>3. <strong>tauRAMD_v2.py </strong>- Python sctipt for estimation relative residence times from Gromacs-RAMD output </p> <p>4. <strong>IFP_preprocess_Gromacs.py</strong> and <strong>IFP_SL-B2AR-WB-EX.py - </strong>Python scripts for preprocessing of RAMD trajectories and generation of IFPs</p> <p>5. <strong>Scripts.zip</strong> - additional python functions </p> <p>6. <strong>IXO-CHL.zip, IXO-ALO-CHL.zip, ACh-CHL.zip, b2AR.zip</strong> - Protein-Ligand Interaction Fingerprints (PL IFPs) generated from RAMD trajectories for <em>mAChR M2 with iperoxo</em>, <em>mAChR M2 </em><em> with iperoxo and PAM, mAChR M2 with ACh, and </em>β<em>2AR with alprenolol </em><em>.</em> </p> <p>7. <strong>Topology.zip</strong> - Gromacs topology, index.ndx, and coordinate gro files for all four systems</p> <p>8. <strong>Example_b2AR-alprenolol.zip </strong>- a set of data for a test example showing how IFP can be generated from RAMD trajectories (including several representative trajectories)</p> <p>9. <strong>Example_b2AR-alprenolol.tar </strong>- almost the same set of data as above (compressed in Windows) but for Linux users. The only difference between tar and zip archive: a short equilibration trajectory that is missing in the zip set but is included in the tar archive.</p> <p>10.<strong> Gromacs-IFP-GPCR.ipynb</strong> - Jupyter Notebook for analysis of trajectories using generated IFP data</p> <p>11. <strong>Auxi-Plots-GPCR.ipynb - </strong>Jupyter Notebook for generation additional plots from the paper</p> <p>12. <strong>Waters.zip</strong> - number of water molecules in the binding pocket in dissociation trajectories of the <em> </em>β<em>2AR - alprenolol system</em></p> <p>13. <strong>GPCR.yml</strong> - JN environment file</p> <p> </p>
Analysis of the interacting residues between wild type SARS-CoV-2 spike protein and natural ligand hACE2, as well as three engineered alternative ligands
<p>The analysis of residue interactions between the SARS-CoV-2 spike protein and its natural (hACE2 <sup>1</sup>) and engineered binders P17 Fab <sup>2</sup>, Ty1 VHH <sup>3</sup> and LCB1 peptide <sup>4</sup> reveals that glutamine, serine and especially tyrosine residues on the ligand side are more frequent and influence spike binding efficiency, and that spike residues Glu484, Phe486, Tyr489 and Gln493 are more recurrent targets for interactions with ligands. The list of residues establishing contacts between the wild type structure of the SARS-CoV-2 spike protein and the binders defined above are described in Table 1. In Figure 1, the frequency and type of amino acids that interact with each spike residue is illustrated.</p>
A Ligand Field Molecular Mechanics Study of CO2 Induced Breathing in the metal-organic framework DUT-8(Ni)
<p>Raw Data, scripts and processed data for the publication "A Ligand Field Molecular Mechanics Study of CO2 Induced Breathing in metal-organic framework DUT-8(Ni)"</p>
ScienceDex guides
Understand access before you commit
These curated guides explain access requirements, typical timelines, costs, and reuse considerations for widely used research datasets.
Allen Brain Atlas
Allen Brain Atlas is an Allen Institute collection of brain map atlases, datasets, APIs, and analysis tools covering mouse, human, and non-human primate brain resources.
Annotated Behaviour and Observability Dataset (ABODe)
ABODe is a University of Edinburgh DataShare dataset for behavior classification in group-housed mice using home-cage video, identities, bounding boxes, ground-plate positions, and annotator labels.
DANDI Archive for NWB datasets
DANDI is a BRAIN Initiative archive for publishing and sharing neurophysiology data, including electrophysiology, optophysiology, and behavioral data packaged as NWB and related standards.
International Brain Laboratory public data
The International Brain Laboratory public data releases expose standardized mouse decision-making experiments, including Neuropixels recordings, widefield calcium imaging, behavior, and session metadata accessed through the ONE API.
OpenNeuro
OpenNeuro is a free, open platform for sharing neuroimaging datasets, with public search, dataset pages, and download paths for web, S3, DataLad, and the OpenNeuro CLI.