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346 results for “structural complexity”
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>
Synthesis, Structure and Redox Properties of Single-atom Bridged Diuranium Complexes Supported by Aryloxides
<p>This upload contains raw data (NMR, X-Ray Diffraction, Electrochemistry, SQUID and Elemental Analysis) files for the article</p>
Data from: Complex population structure and haplotype patterns in Western Europe honey bee from sequencing a large panel of haploid drones
<p>This vcf file contains 7.023.689 SNPs and 870 honey bee samples, as described in the paper "Complex population structure and haplotype patterns in Western Europe honey bee from sequencing a large panel of haploid drones" by Wragg et al., available at https://doi.org/10.1101/2021.09.20.460798 as preprint.</p> <p>Eight hundred and seventy haploid drone samples from several honey bee subspecies hybrids were sequenced and aligned to the HAv3.1 reference genome. Sequence read alignment and genotyping quality filters were used to obtain a selection of 7.023.689 high-quality SNPs. The file Diversity_Study_629_Samples.txt corresponds to the 629 unique samples that were used for the diversity study described in the paper and can be used to recreate the restricted diversity dataset using bcftools or an equivalent software.</p> <p>Having sequenced haploid drones, heterozygous SNPs resulting from duplicated regions could be filtered out and the data is phased.</p>
Integrative structure determination of PTBP1-viral IRES complex in solution
<p>Ensemble structure model of the RNA-binding protein PTBP1 in complex with the internal ribosome entry site (IRES) of encephalomyocarditis virus (EMCV) RNA and data underlying these models.</p> <ul> <li>Main ensemble based on all restraints (corresponding to Figure 2 in the associated paper)</li> <li>Ensemble obtained with only DEER distance distribution restraints corresponding to Figure S7(A) in the Supplementary Material of the associated paper</li> <li>Validation ensemble obtained with all restraints after removing the conformers of the main ensemble from the raw ensemble corresponding to Figure S7(B) inthe Supplementary Material of the associated paper</li> <li>Ensemble obtianed with all restraints by fitting populations with a non-negative linear least squares (NNLLSQ) approach corresponding to Figure S8(A) in ths Supplementary Material of the associated paper</li> <li>Primary DEER-EPR data underlying site-to-site distance distributions for 35 spin-label pairs and corresponding distanace distributions</li> <li>Small-angle neutron scattering (SANS) curves a two detector distances with corresponding resolution files and a small-angle x-ray scattering (SAXS) curve</li> <li>Restraint file for the ensemble fit with MMMx software, specifying the mean distances and standrad deviations of distance distributions that were also used for specifying lower and upper distance bounds in CYANA generation of the raw ensemble</li> <li>Source data for the figures in the associated paper</li> <li>Source data for the tables in the associated paper</li> </ul> <p>All ensembles are ZIP files containing single PDB files for all conformers and an ensemble specification that reports populations for all conformers.</p>
Data for investigating structural complexity of individual Scots pine trees
<p>Tree functional traits together with processes such as forest regeneration, growth, and mortality affect forest and tree structure. Forest management inherently impacts these processes. Moreover, forest structure, biodiversity, resilience, and carbon uptake can be sustained and enhanced with forest management activities. To assess structural complexity of individual trees, comprehensive and quantitative measures are needed, and they are often lacking for current forest management practices. Fractal analysis and a single scale, independent metric called box dimension offer means for assessing structural complexity of individual trees. Terrestrial laser scanning (TLS) point clouds provide three-dimensional (3D) information on trees that can be utilized in generating the box dimension metric. This data set includes information needed for generating the box dimension from 741 individual Scots pine (<em>Pinus sylvestris</em> L.) trees from 9 sample plots with different thinning treatments located in southern boreal forests. The thinning treatments include two intensities of thinning and control treatment (i.e., no thinning treatment since the establishment). The data set can be used in characterizing structural complexity of individual Scots pine trees of various size as well as assessing effects of various thinning treatments on it.</p> <p>Please see the data descriptor for more information on the data structure and its possibilities.</p> <p>Please keep the designated corresponding author informed of any plans to use the data. Consultation or collaboration with the original investigators is strongly encouraged. Publications and data products that make use of the data must include proper acknowledgement.</p>
Radiative transfer modeling in structurally-complex stands: what aspects matter most?: Dataset
<p>This repository is linked to the paper "Radiative transfer modeling in structurally-complex stands: what aspects matter most?" submitted to Annals of Forest Science and written by Frédéric ANDRÉ (corresponding author), Louis DE WERGIFOSSE, François DE COLIGNY, Nicolas BEUDEZ, Gauthier LIGOT, Vincent GAUTHRAY-GUYÉNET, Benoit COURBAUD and Mathieu JONARD.</p> <p>The repository contains the three following files :</p> <ul> <li>CalibrationResults.csv: Bayes factors and summary statistics of parameter estimates for each calibration run</li> <li>ParameterPosteriorDistributions.csv: median values and 90% credible intervals for the parameter posterior distributions</li> <li>StatisticalComparison.csv: statistics (Fractional bias, Root mean square error, Paired Student test, Pearson correlation coefficient, Parameters of the Deming regression between observed and predicted values) used to compare the 'Best model configurations'</li> </ul> <p>For more information concerning this repository or the study, please do not hesitate to contact Frédéric ANDRÉ (frederic.andre@uclouvain.be) or Mathieu JONARD (mathieu.jonard@uclouvain.be).</p>
Datasets of sequences, alignments and structural models generated for the structural prediction of complexes mediated by intrinsically disordered regions.
<p>This repository contains input and ouput files used and generated for the scanning of intrinsically disordered region and the prediction of their binding sites to receptor proteins using the <a href="https://github.com/i2bc/SCAN_IDR">SCAN_IDR</a> pipeline with AlphaFold2-Multimer.</p><p>It contains two archives: </p><ol><li><a href="https://zenodo.org/api/records/10068949/draft/files/scanidr_data_repository_corr6J08.tar/content"><i><strong>scanidr_data_repository_corr6J08.tar</strong></i></a> dedicated to the analysis of a dataset of 42 protein complexes non redundant with the dataset used for AlphaFold2 training,</li><li><a href="https://zenodo.org/api/records/10068949/draft/files/923_elm_cases_repository.tar.gz/content"><i><strong>923_elm_cases_repository.tar.gz</strong></i></a> dedicated to the analysis of 923 complexes from the ELM database.</li></ol><p>These data can be used to rerun specific sections of the pipeline and scripts provided in: <a href="https://github.com/i2bc/SCAN_IDR">https://github.com/i2bc/SCAN_IDR</a></p><h4><strong>Dataset of 42 non redundant complexes</strong></h4><p>The first archive <a href="https://zenodo.org/api/records/10068949/draft/files/scanidr_data_repository_corr6J08.tar/content"><i><strong>scanidr_data_repository_corr6J08.tar</strong></i></a> contains 3 compressed directories and a README file detailing their contents :</p><ul><li>the initial raw sequence and alignment data for every chain -> DIRECTORY <strong>fasta_msa/</strong></li><li>the input and output data of every Alphafold run for every complex -> DIRECTORY <strong>af2_runs/</strong></li><li>the native reference structures -> DIRECTORY <strong>ref_capri_curated/</strong></li></ul><p>The protein-peptide complex cases have been assigned a distinct index number, from 1 to 42, consistent across the several directories of the archive. Their corresponding directories are labelled as <i><index>_<pdbcode></i>.</p><p><i>The models in this archive were generated using AlphaFold2-Multimer v2.2</i></p><h4><strong>Dataset of 923 complexes selected from the ELM database</strong></h4><p>The second archive <a href="https://zenodo.org/api/records/10068949/draft/files/923_elm_cases_repository.tar.gz/content"><i><strong>923_elm_cases_repository.tar.gz</strong></i></a> contains input and ouput files used and generated for the analysis of 923 Eukaryotic Linear Motifs (ELM) database entries.</p><p>Each ELM entry is indexed with specific integer id and is composed of a receptor and a ligand protein. </p><p>The archive contains a Table associating ELM indexes with the ELM entry information, 5 directories and a README file detailing their contents:</p><ul><li>the table describing ELM entries -> FILE <strong>Table_923ELM_uid_delimitations_info_for_archive.txt</strong></li><li>the initial raw sequence and multiple sequence alignment (MSA) data for every chain -> DIRECTORY <strong>fasta_msa/</strong></li><li>the concatenated MSA model for every ELM complex and protocol used -> DIRECTORY <strong>af2_elm_coali_inputs/</strong></li><li>the best model of every AF2 protocol for every complex according to the AF2 -> DIRECTORY <strong>af2_elm_models/</strong></li><li>the best model cut in the ligand part to select only the ELM motifs as used for the evaluation of the models -> DIRECTORY <strong>elm_cut_models/</strong></li><li>the reference structures used for the evaluation of the models -> DIRECTORY <strong>ref_capri_curated/</strong></li></ul><p><i>The models in this archive were generated using AlphaFold2-Multimer v2.3</i></p>
Spatial structure, chemotaxis and quorum sensing shape bacterial biomass accumulation in complex porous media
<p>Dataset associated to the publication</p><p>"Spatial structure, chemotaxis and quorum sensing shape bacterial biomass accumulation in complex porous media"</p><p>By</p><p>David Scheidweiler, Ankur Deep Bordoloi, Wenqiao Jiao, Vladimir Sentchilo, Monica Bollani, Audam Chhun, Philipp Engel and Pietro de Anna</p><p>Folder named "Figure_X" contains the original raw data, analysed data and source data for each plot within figure "X" on the manuscript and supplementary information.</p><p>We do not provide raw data for each replica as one flow&growth experiment consists in 50 large images for a total of about 12 GB per dataset. Thus, we provide here the original data for the Wild Type experiment and the control D-luxS mutant. The data for the replicas and other control experiment can be available upon request.</p><p>We provide Matlab scripts to read and analyze the original images.</p>
An Integrated Structural Model of the DNA Damage Responsive H3K4me3 Binding WDR76:SPIN1 Complex with the Nucleosome
<p>Serial Capture Affinity Purification (SCAP) is a powerful method to isolate a specific protein complex. When combined with cross linking mass spectrometry (XL-MS) and computational approaches one can build an integrated structural model of the isolated complex. Here, we applied SCAP to dissect a subpopulation of WDR76 in complex with SPIN1, a histone marker reader that specifically recognizes trimethylated histone H3 lysine4 (H3K4me3). In contrast to a previous SCAP analysis of the SPIN1:SPINDOC complex, histones and the H3K4me3 mark were copurified with the WDR76:SPIN1 complex. Next, interaction network analysis of copurifying proteins and microscopy analysis revealed a potential role of the WDR76:SPIN1 complex in the DNA damage response. Since we detected an extensive number of cross-linked sites were found between WDR76, SPIN1, and histones, we first built an integrated structural model of the complex which revealed that SPIN1 recognized the H3K4me3 epigenetic mark while interacting with WDR76. Finally, we then used the powerful Integrative Modeling Platform to build a structural model of WDR76 and SPIN1 bound to the nucleosome.</p>
PhasAGE Training School 1 - Structure and protein interactions of repeated and low complexity regions - LECTURE
<p>The Training School 1 <strong>“Computational Methods to Study Protein Phase Separation”</strong> is the first edition of a series of PhasAGE training activities.</p> <p>The goal of this course is to provide participants with the basic knowledge to understand the phenomenon of <strong>Phase Separation</strong>, its role in biological processes and diseases. In addition, the course will provide <strong>an overview of the available computational resources</strong> to navigate this knowledge. Participants will have <strong>hands-on training</strong> in tools and resources available for life sciences, to collect information from the literature on biomolecular phase transitions, identify features triggering phase transitions, mutations associated with diseases, known or predicted PTMs and molecular interaction sites.</p>
Supplementary Materials to the publication Wood structure explained by complex spatial source-sink interactions
<p>Model output and visualisation scripts to the publication Wood structure explained by complex spatial source-sink interactions. A readme explains the file origin. model output files and their variables and units are described within the .R analysis code.</p>
Raw Data for the Article "Cyclopentadienone triisocyanide iron complexes: general synthesis and crystal structures of tris(2,6-dimethylphenyl isocyanide)(η4-tetraphenylcyclopentadienone)iron and tris(naphthalen-2-yl isocyanide)(η4-tetraphenylcyclopentadienone)iron acetone hemisolvate"
<p>This data set contains the raw data (NMR, HRMS, Elemental analysis) for the article "Cyclo­penta­dienone triisocyanide iron complexes: general synthesis and crystal structures of tris­­(2,6-di­methyl­phenyl isocyanide)(η<sup>4</sup>-tetra­phenyl­cyclo­penta­dienone)iron and tris­­(naphthalen-2-yl iso­cyanide)(η<sup>4</sup>-tetra­phenyl­cyclo­penta­dienone)iron acetone hemisolvate" published in <em>Acta Crystallographica Section E: Crystallographic Communications</em>, DOI:</p> <p><a href="https://doi.org/10.1107/S205698902300498X">https://doi.org/10.1107/S205698902300498X</a></p>
Data for: Brain structural connectivity predicts brain functional complexity
<p>Data used in analyses for "Brain structural connectivity predicts brain functional complexity: DTI derived centrality accounts for variance in fractal properties of fMRI signal"</p>
Simple structural views of the SARS spike glycoprotein complex with human angiotensin-converting enzyme 2 (ACE2)
<p>A set of 5 screenshots of UnityMol running the first example system. Three screenshots are from a multi-user virtual reality session with 3 participants, two screenshots illustrate a custom menu to drive the example more efficiently and make it simple for the end user.</p>
Data from: Genomic data reveal deep genetic structure but no support for current taxonomic designation in a grasshopper species complex
<p>Taxonomy has traditionally relied on morphological and ecological traits to interpret and classify biological diversity. Over the last decade, technological advances and conceptual developments in the field of molecular ecology and systematics have eased the generation of genomic data and changed the paradigm of biodiversity analysis. Here we illustrate how traditional taxonomy has led to species designations that are supported neither by high throughput sequencing data nor by the quantitative integration of genomic information with other sources of evidence. Specifically, we focus on <em>Omocestus antigai </em>and<em> O. navasi</em>, two montane grasshoppers from the Pyrenean region that were originally described based on quantitative phenotypic differences and distinct habitat associations (alpine vs. Mediterranean-montane habitats). To validate current taxonomic designations, test species boundaries, and understand the factors that have contributed to genetic divergence, we obtained phenotypic (geometric morphometrics) and genome-wide SNP data (ddRADSeq) from populations covering the entire known distribution of the two taxa. Coalescent-based phylogenetic reconstructions, integrative Bayesian model-based species delimitation, and landscape genetic analyses revealed that populations assigned to the two taxa show a spatial distribution of genetic variation that do not match with current taxonomic designations and is incompatible with ecological/environmental speciation. Our results support little phenotypic variation among populations and a marked genetic structure that is mostly explained by geographic distances and limited population connectivity across the abrupt landscapes characterizing the study region. Overall, this study highlights the importance of integrative approaches to identify taxonomic units and elucidate the evolutionary history of species.</p>
Dataset from the paper entitled "Complex structure of molten FLiBe (2 LiF – BeF2) examined by experimental neutron scattering, X-ray scattering, and deep neural network-based molecular dynamics"
<p>Dataset from the paper entitled "Complex structure of molten FLiBe (2 LiF – BeF2) examined by experimental neutron scattering, X-ray scattering, and deep neural network-based molecular dynamics". These data include experimental total scattering measurements and molecular dynamics simulations on the molten structure of FLiBe. </p>
Fig. 4 in Changes In The Structure Of Nest Complexes Of The Red Wood Ants Formica Rufa And F. Polyctena (Hymenoptera, Formicidae) In Urban Forests
Fig. 4. Degradation of the Formica rufa complex No. 1 (Feofaniya) in terms of average height (4, A) and diameter (4, B) under conditions of intensive construction and recreation; 4, С, D — diameter and height near the nest complex of F. polyctena No. 4 (surroundings of the Observatory), under conditions of felling of the shrub layer and processing of fallen trunks and branches into wood chips.
Figure 4 in Changes In The Structure Of Nest Complexes Of The Red Wood Ants Formica Rufa And F. Polyctena (Hymenoptera, Formicidae) In Urban Forests
Figure 4 shows the degradation trends for the nest complexes of F. rufa No. 1 (4, A, B), F. polyctena No. 4 (4, C, D). For F. rufa No. 1, there was a sharp decrease in the average diameter of anthills in 2014, and on the contrary, an increase since 2015 (fig. 4, A). In 2016, this indicator remained at approximately the same level, and in 2021 it decreased again. In 2022, this nest complex
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Allen Brain Atlas
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DANDI Archive for NWB datasets
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International Brain Laboratory public data
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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.