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The types of data accepted include: NMR spectral parameters, relaxation data, and kinetic and thermodynamic data. Data must be entered in the NMR-STAR format, conversion from other common formats can be carried out using the STARch file converter provided at the site. [13] The site also contains an NMR-STAR template generator which produces ...
The NMR sample is prepared in a thin-walled glass tube.. Protein nuclear magnetic resonance is performed on aqueous samples of highly purified protein. Usually, the sample consists of between 300 and 600 microlitres with a protein concentration in the range 0.1 – 3 millimolar.
The Protein Data Bank was announced in October 1971 in Nature New Biology [10] as a joint venture between Cambridge Crystallographic Data Centre, UK and Brookhaven National Laboratory, US. Upon Hamilton's death in 1973, Tom Koetzle took over direction of the PDB for the subsequent 20 years.
database of intrinsic protein disorder annotation 3D structure protein databases, Protein sequence databases ModBase: Database of Comparative Protein Structure Models: Ursula Pieper, Ben Webb, Narayanan Eswar, Andrej Sali Roberto Sanchez UCSF, Sali Lab 3D structure protein databases PDBsum: Pictorial database of 3D structures in the Protein ...
Protein Data Bank in Europe EMBL-EBI: has some chemicals as well as proteins "PDBe". PATENTSCOPE: WIPO "PATENTSCOPE". 16,000,000 PDB RSCB Protein Data Bank "PDB". 166,891 PharmGKB Shriram Center for Bioengineering and Chemical Engineering drugs targets prescribing info curated "PharmGKB". PHAROS Illuminating the Druggable Genome
Protein Data Bank in Europe (PDBe) Protein Data Bank Japan (PDBj) Biological Magnetic Resonance Data Bank (BMRB) Electron Microscopy Data Bank (EMDB). The wwPDB was founded in 2003 by RCSB PDB (USA), PDBe (Europe) and PDBj (Japan). In 2006 BMRB (USA) joined the wwPDB. EMDB (UK) joined in 2021. Each member's site can accept structural data and ...
The database was assembled by using a structure-based chemical shift calculation program (called SHIFTX) to calculate expected protein (1)H, (13)C and (15)N chemical shifts from X-ray or NMR coordinate data of previously assigned proteins reported in the BMRB.
Example of chemical shift index. The chemical shift index or CSI is a widely employed technique in protein nuclear magnetic resonance spectroscopy that can be used to display and identify the location (i.e. start and end) as well as the type of protein secondary structure (beta strands, helices and random coil regions) found in proteins using only backbone chemical shift data [1] [2] The ...
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