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Found 7 result(s)

The Cambridge Structural Database

CSD

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Established in 1965, the CSD is the world’s repository for small-molecule organic and metal-organic crystal structures. Containing the results of over one million x-ray and neutron diffraction analyses this unique database of accurate 3D structures has become an essential resource to scientists around the world. The CSD records bibliographic, chemical and crystallographic information for:organic molecules, metal-organic compounds whose 3D structures have been determined using X-ray diffraction, neutron diffraction. The CSD records results of: single crystal studies, powder diffraction studies which yield 3D atomic coordinate data for at least all non-H atoms. In some cases the CCDC is unable to obtain coordinates, and incomplete entries are archived to the CSD. The CSD includes crystal structure data arising from: publications in the open literature and Private Communications to the CSD (via direct data deposition). The CSD contains directly deposited data that are not available anywhere else, known as CSD Communications.

CyberCell Database

CCDB

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The CyberCell database (CCDB) is a comprehensive collection of detailed enzymatic, biological, chemical, genetic, and molecular biological data about E. coli (strain K12, MG1655). It is intended to provide sufficient information and querying capacity for biologists and computer scientists to use computers or detailed mathematical models to simulate all or part of a bacterial cell at a nanoscopic (10-9 m), mesoscopic (10-8 m).The CyberCell database CCDB actually consists of 4 browsable databases: 1) the main CyberCell database (CCDB - containing gene and protein information), 2) the 3D structure database (CC3D – containing information for structural proteomics), 3) the RNA database (CCRD – containing tRNA and rRNA information), and 4) the metabolite database (CCMD – containing metabolite information). Each of these databases is accessible through hyperlinked buttons located at the top of the CCDB homepage. All CCDB sub-databases are fully web enabled, permitting a wide variety of interactive browsing, search and display operations. and microscopic (10-6 m) level.

Electron Microscopy Public Image Archive

EMPIAR

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EMPIAR, the Electron Microscopy Public Image Archive, is a public resource for raw, 2D electron microscopy images. Here, you can browse, upload, download and reprocess the thousands of raw, 2D images used to build a 3D structure. The purpose of EMPIAR is to provide an easy access to the state-of-the-art raw data to facilitate methods development and validation, which will lead to better 3D structures. It complements the Electron Microscopy Data Bank (EMDB), where 3D images are stored, and uses the fault-tolerant Aspera platform for data transfers

Conserved Domain database

CDD

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The Conserved Domain Database is a resource for the annotation of functional units in proteins. Its collection of domain models includes a set curated by NCBI, which utilizes 3D structure to provide insights into sequence/structure/function relationships

NeuroMorpho.Org

NeuroMorpho

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NeuroMorpho.Org is a centrally curated inventory of digitally reconstructed neurons associated with peer-reviewed publications. It contains contributions from over 80 laboratories worldwide and is continuously updated as new morphological reconstructions are collected, published, and shared. To date, NeuroMorpho.Org is the largest collection of publicly accessible 3D neuronal reconstructions and associated metadata which can be used for detailed single cell simulations.

Plant Transcription Factor Database

PlantTFDB

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Species included in PlantTFDB 4.0 covers the main lineages of green plants. Therefore, PlantTFDB provides genomic TF repertoires across Viridiplantae. To provide comprehensive information for the TF family, a brief introduction and key references are presented for each family. Comprehensive annotations are made for each identified TF, including functional domains, 3D structures, gene ontology (GO), plant ontology (PO), expression information, expert-curated functional description, regulation information, interaction, conserved elements, references, and annotations in various databases such as UniProt, RefSeq, TransFac, STRING, and VISTA. By inferring orthologous groups and constructing phylogenetic trees, evolutionary relationships among identified TFs were inferred. In addition, PlantTFDB has a simple and user-friendly interface to allow users to query based on combined conditions or make sequence similarity search using BLAST. The new version PlantTFDB 5.0 has been incorporated into PlantRegMap http://plantregmap.gao-lab.org/.

APID

Agile Protein Interactomes DataServer

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APID Interactomes is a database that provides a comprehensive collection of protein interactomes for more than 400 organisms based in the integration of known experimentally validated protein-protein physical interactions (PPIs). Construction of the interactomes is done with a methodological approach to report quality levels and coverage over the proteomes for each organism included. In this way, APID provides interactomes from specific organisms that in 25 cases have more than 500 proteins. As a whole APID includes a comprehensive compendium of 90,379 distinct proteins and 678,441 singular interactions. The analytical and integrative effort done in APID unifies PPIs from primary databases of molecular interactions (BIND, BioGRID, DIP, HPRD, IntAct, MINT) and also from experimentally resolved 3D structures (PDB) where more than two distinct proteins have been identified. In this way, 8,388 structures have been analyzed to find specific protein-protein interactions reported with details of their molecular interfaces. APID also includes a new data visualization web-tool that allows the construction of sub-interactomes using query lists of proteins of interest and the visual exploration of the corresponding networks, including an interactive selection of the properties of the interactions (i.e. the reliability of the "edges" in the network) and an interactive mapping of the functional environment of the proteins (i.e. the functional annotations of the "nodes" in the network).