Find research datasets worth reusing
Search datasets from major research repositories and use ShareScore to quickly assess how well each record supports discovery, access, and reuse.
261
datasets available to search
ShareScore release 0.9.0
Dataset results
261 results for “Protein prediction”
Prediction of inter-chain distance maps of protein complexes with 2D attention-based deep neural networks
<p>Residue-residue distance information is useful for predicting tertiary structures of protein monomers or quaternary structures of protein complexes. Many deep learning methods have been developed to predict intra-chain residue-residue distances of monomers accurately, but few methods can accurately predict inter-chain residue-residue distances of complexes. We develop a deep learning method CDPred (i.e., Complex Distance Prediction) based on the 2D attention-powered residual network to address the gap. Tested on two homodimer datasets, CDPred achieves the precision of 60.94% and 42.93% for top L/5 inter-chain contact predictions (L: length of the monomer in homodimer), respectively, substantially higher than DeepHomo’s 37.40% and 23.08% and GLINTER’s 48.09% and 36.74%. Tested on the two heterodimer datasets, the top Ls/5 inter-chain contact prediction precision (Ls: length of the shorter monomer in heterodimer) of CDPred is 47.59% and 22.87% respectively, surpassing GLINTER’s 23.24% and 13.49%. Moreover, the prediction of CDPred is complementary with that of AlphaFold2-multimer.</p>
ESM Atlas v0 representative random sample of predicted protein structures
<p>A representative random sample of the ESM Atlas v0 dataset introduced in "Evolutionary-scale prediction of atomic level protein structure with a language model.".<br> All predictions can be accessed in the ESM Metagenomic Atlas (<a href="https://esmatlas.com/">https://esmatlas.com</a>) open science resource, released on 2022-11-01.<br> Sample size: 997,405.</p>
ESM Atlas v0 random sample of high confidence predicted protein structures
<p>A random sample out of the 225M high confidence predictions in the ESM Atlas v0 dataset introduced in "Evolutionary-scale prediction of atomic level protein structure with a language model.".<br> All predictions can be accessed in the ESM Metagenomic Atlas (<a href="https://esmatlas.com/">https://esmatlas.com</a>) open science resource, released on 2022-11-01.<br> High confidence is defined as mean pLDDT > 0.7 and pTM > 0.7 and corresponds to ∼36% of the total 617M proteins folded.<br> This is the random sample used for analysis in the paper as well as visualization on the <a href="http://esmatlas.com/">esmatlas.com</a> Explore page.<br> Sample size: 999,520 based on 999,996 unique randomly sampled IDs and 0.05% missing data in the processing pipeline.</p>
Prediction of inter-chain distance maps of protein complexes with 2D attention-based deep neural networks
<p>Residue-residue distance information is useful for predicting tertiary structures of protein monomers or quaternary structures of protein complexes. Many deep learning methods have been developed to predict intra-chain residue-residue distances of monomers accurately, but few methods can accurately predict inter-chain residue-residue distances of complexes. We develop a deep learning method CDPred (i.e., Complex Distance Prediction) based on the 2D attention-powered residual network to address the gap. Tested on two homodimer datasets, CDPred achieves the precision of 60.94% and 42.93% for top L/5 inter-chain contact predictions (L: length of the monomer in homodimer), respectively, substantially higher than DeepHomo’s 37.40% and 23.08% and GLINTER’s 48.09% and 36.74%. Tested on the two heterodimer datasets, the top Ls/5 inter-chain contact prediction precision (Ls: length of the shorter monomer in heterodimer) of CDPred is 47.59% and 22.87% respectively, surpassing GLINTER’s 23.24% and 13.49%. Moreover, the prediction of CDPred is complementary with that of AlphaFold2-multimer.</p>
DIPS-Plus: The Enhanced Database of Interacting Protein Structures for Interface Prediction (Supplementary Data)
<p>This dataset contains supplementary replication data for the paper titled "DIPS-Plus: The Enhanced Database of Interacting Protein Structures for Interface Prediction". In particular, it contains a new version of our `final_raw_dips.tar.gz` protein pair representations which now contain (1) residue-level annotations for intrinsic disorder regions (IDRs) as well as (2) a copy of each protein pair representation in the HDF5 file format for programming language-agnostic read capabilities. In addition, this record also contains (3) raw MSAs (in HDF5 file format) generated for each protein pair using Jackhmmer and AlphaFold's small version of the Big Fantastic Database (BFD). Lastly, this record contains (4) PDB metadata derived for each DIPS-Plus complex using Graphein's PDBManager API as well as (5) structure-based (i.e., FoldSeek-based) training and validation splits of the dataset's complexes in the form of respective text files containing the file paths of complexes assigned to each split.</p>
Interformer: An Interaction-Aware Model for Protein-Ligand Docking and Affinity Prediction
<p>The code, dataset, and model weights are described in the paper "Interformer: An Interaction-Aware Model for Protein-Ligand Docking and Affinity Prediction."</p> <p> </p> <p><strong>experiment_results.zip:</strong> Contains generated results that can reproduce the result from the reported paper.</p> <p><strong>benchmark.zip:</strong> Contains docking and affinity input data of the interformer. You can use the source code to make predictions and reproduce the number of the reported paper.</p> <p><strong>checkpoints.zip: </strong>Contains one weight for the Energy and four PoseScore and Affinity models.</p> <p><strong>source_code_1.0.zip:</strong> Contains the initial version of the source code.</p> <p><strong>interformer_train.tar.gz:</strong> Contains prepared training data for interformer. poses/ contains all structure need for training, poses/ligand contains the re-docking poses generated by interformer energy, poses/ligand/rcsb contains the conformation of reference ligand, poses/pocket contains all pocket extract by raw PDB from rcsb, poses/uff contains all ligand conformation minimized using UFF from reference ligand, and train/ contains the training csv.</p> <p><strong>baseline_results.tar.gz:</strong> Contains the predictions from three methods: Interformer, DiffDock, and DeepDock. The results align with the exact numbers reported in the paper. For further details, please refer to the <em>eda/ </em>directory.</p> <p> </p> <p>You can also find the newest version of the source code at <a href="https://github.com/tencent-ailab/Interformer" target="_blank" rel="noopener">https://github.com/tencent-ailab/Interformer</a></p> <p> </p>
Dataset for "Computational prediction of structure, function and interaction of Myzus persicae (green peach aphid) salivary effector proteins "
Open the record for dataset details and reuse information.
Improved protein complex prediction with AlphaFold-multimer by denoising the MSA profile
<p>Supporting data for AFProfile</p> <p>casp15.tar.zst - predicted structures and MSAs for the CASP15 set<br>native_afm_2_6_bench.tar.zst - native cif files for all complexes with ranking confidence <0.75 in the AFM 2-6 chains benchmark ( https://doi.org/10.1093/bioinformatics/btad424)<br>pred_top_models_afm_2_6_bench.tar.zst - predicted top ranked models and scores for all 100 samples.<br>afm_opt_metrics.csv - the best models, confidences and MMscores for the AFProfile run on the AFM 2-6 chains benchmark (n=427 structures)<br>msa_shapes.csv - the shape of the MSA as input to AFM for each structure<br>directed.tar.zst - contains all models for the AFProfile run on the AFM 2-6 chains benchmark (n=42700 samples)</p> <p>The directories are compressed with zstd: https://github.com/facebook/zstd<br>Uncompress:<br>tar --use-compress-program full/path/to/zstd -xvf file.tar.zst</p>
Our predicted Crinkler (CRN) family effector proteins and the corresponding GFF3 files across 128 Phytophthora isolates
<p>These files contain predicted Crinkler (CRN) family effector proteins and the corresponding GFF3 files across 128 Phytophthora isolates.</p>
Predictions of the SARS-CoV-2 B.1.1.529 Variant Spike Protein Receptor Binding Domain Structure and Neutralizing Antibody Interactions
<p>Using AlphaFold2 and HADDOCK, we have generated a predicted structure for the SARS-CoV-2 B.1.1.529 variant's Spike receptor binding domain and then predicted the binding interaction with neutralizing antibodies. This was performed to understand the potential structural changes in the receptor binding domain of B.1.1.529 and how this may affect vaccine efficacy through antibody interaction.</p>
Protein language model embeddings and predictions for the fly proteome (FlyBase)
<p>Residue and sequence embeddings of the fly (drosophila melanogaster) proteome (FlyBase for organism drosophila melanogaster, downloaded on 2022.03.01) computed using bio_embeddings (bioembeddings.com) using the ProtT5 embedder at full precision (https://www.biorxiv.org/content/10.1101/2020.07.12.199554v3). To open the embeddings file, please see <a href="https://github.com/sacdallago/bio_embeddings/blob/develop/notebooks/open_embedding_file.ipynb">this notebook</a>. The embeddings will be indexed by numbers according to the mapping file (mapping_file.csv) in this dataset. All following results will share the same mapping (for instance, to access the variation prediction results, by accessing index "0", you will query results for the sequence "FBpp0304622").</p> <p>Additionally:</p> <p>- Sequence-level predictions of subcellular localization in 10 classes using LA (https://www.biorxiv.org/content/10.1101/2021.04.25.441334v1)</p> <p>- Residue-level three state secondary structure prediction (alpha, sheet or other) using models reported in the ProtTrans paper (https://www.biorxiv.org/content/10.1101/2020.07.12.199554v3)</p> <p>- Residue-level prediction of conservation (in 9 states) and of variation effect (from 0 [no-effect] to 1 [effect]) using VESPAl (https://doi.org/10.1007/s00439-021-02411-y)</p> <p> </p> <p>Files included:</p> <p>- dmel-all-translation-r6.44.fasta --> FASTA-formatted sequences of drosophila melanogaster from FlyBase</p> <p>- mapping_file.csv --> A CSV file mapping the identifiers used in the following files (from 0 to 30737) to the identifiers in the FlyBase fasta file (dmel-all-translation-r6.44.fasta).</p> <p>- DSSP3_fly_ProtT5Sec.fasta --> Secondary structure predictions in three states for each residue of each protein in dmel-all-translation-r6.44.fasta. "H" stands for Helix; "E" stands for Sheet; "C" stands for Other.</p> <p>- subcell_fly_LA_ProtT5.csv --> Subcellular location (10 states) and memrane-boundness (2 states) for each protein in dmel-all-translation-r6.44.fasta</p> <p>- embeddings_file.h5 --> per-residue embeddings of sequences in dmel-all-translation-r6.44.fasta. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length Lx1024, with L being the length of the protein sequence. Datasets are indexed using integers. The original sequence identifier (from the FASTA header) can be accessed through the "original_id" attribute. See https://docs.bioembeddings.com/v0.2.0/notebooks/open_embedding_file.html for information on how to open the file.</p> <p>- reduced_embeddings_file.h5 --> per-sequence embeddings of sequences in dmel-all-translation-r6.44.fasta (obtained by mean-pooling the residue-embeddings along the length dimension of the protein sequence). Each dataset in the .h5 file represents a protein sequence and contains a vector of size 1024 (meaning, each sequence has the same dimension).</p> <p>- conspred_probs.h5 --> per-sequence conservation probability (softmax) prediction of sequences in dmel-all-translation-r6.44.fasta in 9 classes. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length 9xL, with L being the length of the protein sequence, and 9 being the predicted conservation class (index 0 = very variable; index 8 = very conserved)</p> <p>- vespal_SAVeffect_fly.zip --> zipped .h5 file of per-sequence variation predictions of sequences in dmel-all-translation-r6.44.fasta on a scale from 0 (neutral) to 1 (effect). -1 indicates WT substitution. Each dataset in the .h5 file represents a protein sequence and contains a matrix of length 20xL, with L being the length of the protein sequence, and 20 being the predicted variation score for each residue substitution (AAs in the following order: "<strong>ALGVSREDTIPKFQNYMHWC</strong>" . Meaning that index 0 = substitution of the residue to "A", index = 1 substitution to residue "L", aso.)</p>
Data for RAPPPID: Towards Generalisable Protein Interaction Prediction with AWD-LSTM Twin Networks
<p>Data for RAPPPID, a method for the Regularised Automative Prediction of Protein-Protein Interactions using Deep Learning.</p> <p>These datasets are in a format that RAPPPID is ready to read.<br> <br> <strong>Comparatives Dataset</strong><br> These datasets were derived from the STRING v11 <em>H. sapiens</em> dataset, according to the C1, C2, and C3 procedures outlined by Park and Marcotte, 2012. Negative samples are sampled randomly from the space of proteins not known to interact. See <a href="https://doi.org/10.1101/2021.08.13.456309">Szymborski & Emad</a> for details.<br> <br> <strong>Repeatability Datasets</strong><br> The following datasets are all derived from STRING in the manner as the comparatives dataset, but three different random seeds are used for drawing proteins.<br> <br> <strong>References</strong><br> Park,Y. and Marcotte,E.M. (2012) Flaws in evaluation schemes for pair-input computational predictions. Nat Methods, 9, 1134–1136.</p> <p>Szklarczyk, D., Gable, A. L., Lyon, D., Junge, A., Wyder, S., Huerta-Cepas, J., Simonovic, M., Doncheva, N. T., Morris, J. H., Bork, P., Jensen, L. J., and Mering, C. (2019). String v11: protein–protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets. Nucleic Acids Research, 47(D1), D607–D613.<br> <br> Szymborski,J. and Emad,A. (2021) RAPPPID: Towards Generalisable Protein Interaction Prediction with AWD-LSTM Twin Networks. bioRxiv https://doi.org/10.1101/2021.08.13.456309</p>
Prediction and Visualization of Human Transmembrane Proteins using AlphaFold and Protein Language Models
<p><strong>Description:</strong> <strong>TMvis</strong> ("TMvis496.tar.gz") is a dataset containing 496 3D-structures of predicted human transmembrane proteins (TMP) and their predicted membrane embedding. The method TMbed [1], based on the protein language model ProtT5 [2] predicted 4.967 TMP for the human proteome (20,375 proteins, UniProt [3] version April 2022; excluding TITIN_HUMAN due to length). For these proteins, we obtained AlphaFold [4] structures from AlphaFoldDB [5] with an average per-residue confidence score (pLDDT) of more than 90%. This resulted in the 496 proteins of TMvis, as can be found in "TMvis496.fasta". The membrane embedding was predicted using the methods ANVIL [6], PPM3 [7], and per-residue TMbed predictions. As the three methods are based on different approaches, we decided to publish results for all. The figure “TMvis_project_overview.png” provides a graphical overview for each step described above.</p> <p><strong>TMvis Folder Structure:</strong> TMvis is separated into “alpha” containing predicted alpha-helical TMPs, and “beta” containing predicted beta-barrel TMPs. Within these folders, each protein is assigned one folder, identifiable by the respective unique UniProt ID. Each protein folder consists of:<br> - “UniprotID.fasta” with UniProt ID, sequence, TMbed per-residue prediction<br> - “AF-UniprotID-F1-model_v2.pdb” with the AlphaFold structure<br> - “AF-UniprotID-F1-model_v2.cif” with the AlphaFold structure<br> - “AF-UniprotID-F1-model_v2_ANVIL.pdb” with predicted ANVIL membrane embedding<br> - “AF-UniprotID-F1-model_v2_ppm.pdb” predicted PPM3 membrane embedding</p> <p>TMvis <br> | <br> ├── alpha <br> │ │ <br> │ ├── A0A087X1C5 <br> │ │ ├── A0A087X1C5.fasta <br> │ │ ├── AF-A0A087X1C5-F1-model_v2.pdb <br> │ │ ├── AF-A0A087X1C5-F1-model_v2.cif <br> │ │ ├── AF-A0A087X1C5-F1-model_v2_ANVIL.pdb <br> │ │ └── AF-A0A087X1C5-F1-model_v2_ppm.PDB <br> │ └── ... <br> └── beta <br> └── P45880</p> <p><strong>TMvis visualization:</strong> The 3D-visualization of every protein in the dataset TMvis can be easily accessed using the Jupyter Notebook “TMvis.ipynb”. It contains detailed descriptions the different membrane prediction tools ANVIL, PPM3, and TMbed as well as the respective code. Additionally, it allows to visualize the per-residue confidence scores (pLDDT) of AlphaFold.</p> <p>——————————————————————————————————————————————————————————————————————————</p> <p><strong>References:</strong></p> <p>[1] TMbed - TMbed Bernhofer, Michael, and Burkhard Rost. 2022. “TMbed – Transmembrane Proteins Predicted through Language Model Embeddings.” bioRxiv.</p> <p>[2] ProtT5 - A. Elnaggar et al., "ProtTrans: Towards Cracking the Language of Lifes Code Through Self-Supervised Deep Learning and High Performance Computing," in IEEE Transactions on Pattern Analysis and Machine Intelligence, doi: 10.1109/TPAMI.2021.3095381.</p> <p>[3] UniProt - UniProt Consortium (2021). UniProt: the universal protein knowledgebase in 2021. Nucleic acids research, 49(D1), D480–D489.</p> <p>[4] AlphaFold - AlphaFold Jumper, John, Richard Evans, Alexander Pritzel, Tim Green, Michael Figurnov, Olaf Ronneberger, Kathryn Tunyasuvunakool, et al. 2021. “Highly Accurate Protein Structure Prediction with AlphaFold.” Nature 596 (7873): 583–89.</p> <p>[5] Alphafold DB - Varadi, Mihaly, Stephen Anyango, Mandar Deshpande, Sreenath Nair, Cindy Natassia, Galabina Yordanova, David Yuan, et al. 2022. “AlphaFold Protein Structure Database: Massively Expanding the Structural Coverage of Protein-Sequence Space with High-Accuracy Models.” Nucleic Acids Research 50 (D1): D439–44.</p> <p>[6] ANVIL - ANVIL Postic, Guillaume, Yassine Ghouzam, Vincent Guiraud, and Jean-Christophe Gelly. 2016. “Membrane Positioning for High- and Low-Resolution Protein Structures through a Binary Classification Approach.” Protein Engineering, Design & Selection: PEDS 29 (3): 87–91.</p> <p>[7] PPM3 - PPM3 Lomize, Mikhail A., Irina D. Pogozheva, Hyeon Joo, Henry I. Mosberg, and Andrei L. Lomize. 2012. “OPM Database and PPM Web Server: Resources for Positioning of Proteins in Membranes.” Nucleic Acids Research 40 (Database issue): D370–76.</p> <p>——————————————————————————————————————————————————————————————————————————</p> <p><strong>License:</strong></p> <p>This work is licensed under a Creative Commons Attribution 4.0 International License (CC-BY 4.0).</p> <p> </p>
Data for 'VespaG: Expert-guided protein language models enable accurate and blazingly fast fitness prediction'
<div>Datasets used for development of VespaG and VespaG predictions generated with <a href="https://github.com/JSchlensok/VespaG">https://github.com/JSchlensok/VespaG</a>. </div> <div> </div> <div>Uploads contain:</div> <div> <ol> <li><strong>Performance</strong> summaries for ProteinGym [1]:<br>- Spearman and Pearson correlation for VespaG: <em>proteingym_performance_vespag.csv </em>(columns: 'DMS_id', 'Spearman', 'Pearson')<br>- Spearman correlation for evaluated methods VespaG, GEMME [2], VESPA [3], TranceptEVE [4], AlphaMissense [5], PoET [6]: <em>proteingym_spearman_allmethods.csv </em>(columns: 'DMS_id', 'Trancept EVE-L', 'VESPA', 'VespaG', 'GEMME', 'AlphaMissense', 'PoET', 'UniProt_ID', 'coarse_selection_type' (function), 'taxon')</li> <li><strong>Fasta</strong> files with sequences for all train sets (<em>vespag_fasta_training_datasets.zip</em> with seq_all9k.fasta, seq_human5k.fasta, seq_droso4k.fasta, seq_ecoli2k.fasta, seq_virus1k.fasta) and test set (<em>proteingym_217.fasta</em>)</li> <li><strong>VespaG</strong> <strong>Predictions</strong> for test set: <em>vespag_proteingym_rawpreds_by_training_dataset.zip</em> with raw_preds_ecoli.csv, raw_preds_human.csv, raw_preds_virus.csv, raw_preds_all.csv, raw_preds_droso.csv (columns: 'DMS_id', 'mutation', 'DMS_score', 'VespaG'). Predictions are based on different training data, the final model VespaG was trained on a subset of the human proteome and <strong>raw VespaG predictions</strong> <strong>for</strong> <strong>the</strong> <strong>ProteinGym benchmark are in raw_preds_human.csv </strong>(used to calculate the performances above).</li> <li><strong>GEMME predictions</strong> for train sets: <em>vespag_proteingym_rawpreds_by_training_dataset.zip </em>with folders 'human', 'droso', 'ecoli', 'virus', 'all' for respective fasta file (each containing GEMME mutational landscape output files named '<em>ID' + '</em>_normPred_evolCombi.txt')</li> <li><strong>ESM-2</strong> <strong>embeddings</strong> [7] for test set (<em>proteingym_217_esm2.h5</em>)</li> </ol> </div> <div>For details on VespaG see:</div> <div> <div> <div>VespaG: Expert-guided protein Language Models enable accurate and blazingly fast fitness prediction</div> </div> <div>Celine Marquet, Julius Schlensok, Marina Abakarova, Burkhard Rost, Elodie Laine</div> <div>bioRxiv 2024.04.24.590982; doi: https://doi.org/10.1101/2024.04.24.590982</div> <div> </div> <div>For more information on data usage and generation please see <a href="https://github.com/JSchlensok/VespaG">https://github.com/JSchlensok/VespaG</a>.</div> <div> </div> <div>Abstract:</div> <div>Exhaustive experimental annotation of the effect of all known protein variants remains daunting and expensive, stressing the need for scalable effect predictions. We introduce VespaG, a blazingly fast single amino acid variant effect predictor, leveraging embeddings of protein Language Models as input to a minimal deep learning model. To overcome the sparsity of experimental training data, we created a dataset of 39 million single amino acid variants from the human proteome applying the multiple sequence alignment-based effect predictor GEMME as a pseudo standard-of-truth. Assessed against the ProteinGym Substitution Benchmark (217 multiplex assays of variant effect with 2.5 million variants), VespaG achieved a mean Spearman correlation of 0.48 +/- 0.01, matching state-of-the-art methods such as GEMME, TranceptEVE, PoET, AlphaMissense, and VESPA. VespaG reached its top-level performance several orders of magnitude faster, predicting all mutational landscapes of the human proteome in 30 minutes on a consumer laptop (12-core CPU, 16 GB RAM).</div> <div> </div> <div>[1] Notin, Pascal, et al. "ProteinGym: large-scale benchmarks for protein fitness prediction and design." <em>Advances in Neural Information Processing Systems</em> 36 (2024).<br>[2] Laine, Elodie, Yasaman Karami, and Alessandra Carbone. "GEMME: a simple and fast global epistatic model predicting mutational effects." <em>Molecular biology and evolution</em> 36.11 (2019): 2604-2619.</div> <div>[3] Marquet, Céline, et al. "Embeddings from protein language models predict conservation and variant effects." <em>Human genetics</em> 141.10 (2022): 1629-1647.</div> <div>[4] Notin, Pascal, et al. "TranceptEVE: Combining family-specific and family-agnostic models of protein sequences for improved fitness prediction." <em>bioRxiv</em> (2022): 2022-12.</div> <div>[5] Cheng, Jun, et al. "Accurate proteome-wide missense variant effect prediction with AlphaMissense." <em>Science</em> 381.6664 (2023): eadg7492.</div> <div>[6] Truong Jr, Timothy, and Tristan Bepler. "PoET: A generative model of protein families as sequences-of-sequences." <em>Advances in Neural Information Processing Systems</em> 36 (2024).</div> <div>[7] Lin, Zeming, et al. "Evolutionary-scale prediction of atomic-level protein structure with a language model." <em>Science</em>379.6637 (2023): 1123-1130.</div> </div>
[Accompanying Dataset for PHIStruct] ColabFold-Predicted Structures of Receptor-Binding Proteins
<p><strong>This dataset contains protein structures, computationally predicted via <a href="https://doi.org/10.1038/s41592-022-01488-1">ColabFold</a>, of 19,081 non-redundant (i.e., with duplicates removed) receptor-binding proteins from 8,525 phages across 238 host genera</strong>. We identified these receptor-binding proteins based on GenBank annotations. For phage sequences without GenBank annotations, we employed a pipeline that uses the viral protein library <a href="https://doi.org/10.1093/nargab/lqab067">PHROG</a> and the machine learning model <a href="https://doi.org/10.3390/v14061329">PhageRBPdetect</a>. </p> <p>More details can be found in our paper <strong>"PHIStruct: Improving phage-host interaction prediction at low sequence similarity settings using structure-aware protein embeddings."</strong> The project page is <a href="https://github.com/bioinfodlsu/PHIStruct">https://github.com/bioinfodlsu/PHIStruct</a>. Our paper is published in <em>Bioinformatics:</em> <a href="https://doi.org/10.1093/bioinformatics/btaf016" rel="nofollow">https://doi.org/10.1093/bioinformatics/btaf016</a></p> <p>Our research was supported with Cloud TPUs from <a href="https://sites.research.google/trc/about/" rel="nofollow">Google's TPU Research Cloud (TRC)</a> and with computing resources from the <a href="https://docs.mlerp.cloud.edu.au/" rel="nofollow">Machine Learning eResearch Platform (MLeRP)</a> of Monash University, University of Queensland, and Queensland Cyber Infrastructure Foundation Ltd.</p>
Predicting metal-protein interactions using cofolding methods: Status quo
<p>Metals play important roles for enzyme function and many therapeutically relevant proteins. Despite the fact that the first drugs developed via computer aided drug design were metalloprotein inhibitors, many computational pipelines still discard metalloproteins due to the difficulties of modelling them computationally. New "cofolding" methods such as AlphaFold3 (AF3) and RoseTTAfold-AllAtom (RFAA) promise to improve this issue by being able to dock small molecules in presence of multiple complex cofactors including metals or covalent modifications. Here, we analyze the current status for metal ion prediction using these methods. We find that currently only AF3 provides realistic predictions for metal ions, RFAA in contrast does perform worse than more specialized models such as AllMetal3D in predicting the location of metal ions accurately. We find that AF3 predictions are consistent with expected physico-chemical trends/intuition whereas RFAA often also predicts unrealistic metal ion locations.</p>
The state-of-the-art machine learning model for Plasma Protein Binding Prediction: computational modeling with OCHEM and experimental validation
<p><span>Institute of Materia Medica, Chinese Academy of Medical Sciences purchased 10,000 ChemDiv databases.</span></p>
Рис. 5. Варианты преΑсказанной Αоменной структуры скавенΑжер-рецепторов гемоцитов моΛΛюсков Planorbarius corneus. Сокращения (зΑесь и ΑаΛее): SR — богатый цистеином Αомен скавенΑжер-рецептора, Filament — Αомен промежуточного фиΛамента, TSP1 — повторы тромбоспонΑина типа 1, KR — крингΛ-Αомен, LDLa — Αомен рецептора Λипопротеинов низкой пΛотности кΛасса А Fig. 5. Variants of the predicted domain structure of scavenger receptors from hemocytes of Planorbarius corneus molluscs. Abbreviations (here and in what follows): SR — scavenger receptor Cys-rich domain, Filament — intermediate filament protein, TSP1 — thrombospondin type 1 repeats, KR — kringle domain, LDLa — low-density lipoprotein receptor domain class A in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 5. Варианты преΑсказанной Αоменной структуры скавенΑжер-рецепторов гемоцитов моΛΛюсков Planorbarius corneus. Сокращения (зΑесь и ΑаΛее): SR — богатый цистеином Αомен скавенΑжер-рецептора, Filament — Αомен промежуточного фиΛамента, TSP1 — повторы тромбоспонΑина типа 1, KR — крингΛ-Αомен, LDLa — Αомен рецептора Λипопротеинов низкой пΛотности кΛасса А Fig. 5. Variants of the predicted domain structure of scavenger receptors from hemocytes of Planorbarius corneus molluscs. Abbreviations (here and in what follows): SR — scavenger receptor Cys-rich domain, Filament — intermediate filament protein, TSP1 — thrombospondin type 1 repeats, KR — kringle domain, LDLa — low-density lipoprotein receptor domain class A
Рис. 2. Варианты преΑсказанной Αоменной структуры патогенраспознающих моΛекуΛ гемоцитов моΛΛюсков Planorbarius corneus. a — фибриногенпоΑобные беΛки, b — гаΛектины, c — F-Λектины. УсΛовные обозначения и сокращения, зΑесь и ΑаΛее: горизонтаΛьные красные поΛоски — сигнаΛьный пептиΑ, горизонтаΛьные розовые — обΛасть низкой сΛожности, вертикаΛьные синие поΛоски — трансмембранная обΛасть, FBG — фибриногеновый Αомен, FTP — Αомен фукоΛектина, EGF — Αомен эпиΑермаΛьного фактора роста, EGF_CA — каΛьцийсвязывающий EGF-поΑобный Αомен, PAN_AP — APPLE-поΑобный Αомен, SCAN — обΛасть, богатая Λейцином, GLECT — гаΛактозосвязывающий Λектин, CLECT — Λектин C-типа, Gal-bind — гаΛактозиΑ–связывающий Λектин, ML — MD-2- поΑробный Αомен распознавания ΛипиΑов Fig. 2. Variants of the predicted domain structure of pattern recognition molecules from hemocytes of Planorbarius corneus molluscs. a — fibrinogen-related proteins, b — galectins, c — F-lectins. Symbols and abbreviations (here and further): horizontal red stripes — signal peptide, horizontal pink stripes — a low complexity region, vertical blue stripes — transmembrane region, FBG — fibrinogen-related domain, FTP — fucolectin domain, EGF — epidermal growth factor-like domain, EGF_CA — calcium-binding EGF-like domain, PAN_AP — APPLE-like domain, SCAN — leucine rich region, Apple — APPLE domain, GLECT — galactose-binding lectin, CLECT — C-type lectin, Gal-bind — galactoside-binding lectin, ML — MD-2-related lipid-recognition domain in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 2. Варианты преΑсказанной Αоменной структуры патогенраспознающих моΛекуΛ гемоцитов моΛΛюсков Planorbarius corneus. a — фибриногенпоΑобные беΛки, b — гаΛектины, c — F-Λектины. УсΛовные обозначения и сокращения, зΑесь и ΑаΛее: горизонтаΛьные красные поΛоски — сигнаΛьный пептиΑ, горизонтаΛьные розовые — обΛасть низкой сΛожности, вертикаΛьные синие поΛоски — трансмембранная обΛасть, FBG — фибриногеновый Αомен, FTP — Αомен фукоΛектина, EGF — Αомен эпиΑермаΛьного фактора роста, EGF_CA — каΛьцийсвязывающий EGF-поΑобный Αомен, PAN_AP — APPLE-поΑобный Αомен, SCAN — обΛасть, богатая Λейцином, GLECT — гаΛактозосвязывающий Λектин, CLECT — Λектин C-типа, Gal-bind — гаΛактозиΑ–связывающий Λектин, ML — MD-2- поΑробный Αомен распознавания ΛипиΑов Fig. 2. Variants of the predicted domain structure of pattern recognition molecules from hemocytes of Planorbarius corneus molluscs. a — fibrinogen-related proteins, b — galectins, c — F-lectins. Symbols and abbreviations (here and further): horizontal red stripes — signal peptide, horizontal pink stripes — a low complexity region, vertical blue stripes — transmembrane region, FBG — fibrinogen-related domain, FTP — fucolectin domain, EGF — epidermal growth factor-like domain, EGF_CA — calcium-binding EGF-like domain, PAN_AP — APPLE-like domain, SCAN — leucine rich region, Apple — APPLE domain, GLECT — galactose-binding lectin, CLECT — C-type lectin, Gal-bind — galactoside-binding lectin, ML — MD-2-related lipid-recognition domain
Рис. 7. Варианты преΑсказанной Αоменной структуры моΛекуΛ аΑгезии гемоцитов моΛΛюсков Planorbarius corneus. УсΛовные обозначения и сокращения: 1–3 — β-интегрины, 4–5 — α-интегрины, 6–7 — сеΛектины, 8–11 — моΛекуΛы семейства САМ (сell adhesiom molecues), INB — субъеΑиницы β-интегрина, IntegrinBcyt — цитопΛазматический Αомен β-интегрина, CY — цистатинопоΑобный Αомен, Int alpha — Αомен α-интегрина, FN3 — Αомен фибронектина типа 3, CCP — Αомен контроΛя компΛемента Fig. 7. Variants of the predicted domain structure of adhesion molecules from hemocytes of Planorbarius corneus molluscs. Symbols and abbreviations: 1–3 — β-integrins, 4–5 — α–integrins, 6–7 — selectins, 8–11 — molecules of the СAM family (cell adhesion molecules), INB — β-integrin subunits, IntegrinBcyt — cytoplasmic domain of β-integrin, CY — cystatin-like domain, Int alpha — α-integrin domain, FN3 — fibronectin type 3 domain, CCP — complement control protein domain in Pathogen recognition molecules from hemocytes of Planorbarius corneus molluscs (Planorbidae, Pulmonata)
Рис. 7. Варианты преΑсказанной Αоменной структуры моΛекуΛ аΑгезии гемоцитов моΛΛюсков Planorbarius corneus. УсΛовные обозначения и сокращения: 1–3 — β-интегрины, 4–5 — α-интегрины, 6–7 — сеΛектины, 8–11 — моΛекуΛы семейства САМ (сell adhesiom molecues), INB — субъеΑиницы β-интегрина, IntegrinBcyt — цитопΛазматический Αомен β-интегрина, CY — цистатинопоΑобный Αомен, Int alpha — Αомен α-интегрина, FN3 — Αомен фибронектина типа 3, CCP — Αомен контроΛя компΛемента Fig. 7. Variants of the predicted domain structure of adhesion molecules from hemocytes of Planorbarius corneus molluscs. Symbols and abbreviations: 1–3 — β-integrins, 4–5 — α–integrins, 6–7 — selectins, 8–11 — molecules of the СAM family (cell adhesion molecules), INB — β-integrin subunits, IntegrinBcyt — cytoplasmic domain of β-integrin, CY — cystatin-like domain, Int alpha — α-integrin domain, FN3 — fibronectin type 3 domain, CCP — complement control protein domain
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.