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- PDB-5t1o: Solution-state NMR and SAXS structural ensemble of NPr (1-85) in ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5t1o | |||||||||
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Title | Solution-state NMR and SAXS structural ensemble of NPr (1-85) in complex with EIN-Ntr (170-424) | |||||||||
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![]() | TRANSFERASE / PTSNtr / phosphotransfer / bacterial / complex | |||||||||
Function / homology | ![]() transferase activity, transferring phosphorus-containing groups / phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / : / kinase activity / phosphorylation / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | SOLUTION NMR / ![]() | |||||||||
![]() | Strickland, M. / Stanley, A.M. / Wang, G. / Schwieters, C.D. / Buchanan, S. / Peterkofsky, A. / Tjandra, N. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. Authors: Strickland, M. / Stanley, A.M. / Wang, G. / Botos, I. / Schwieters, C.D. / Buchanan, S.K. / Peterkofsky, A. / Tjandra, N. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2 MB | Display | ![]() |
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PDB format | ![]() | 1.7 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 721.6 KB | Display | ![]() |
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Full document | ![]() | 17.2 MB | Display | |
Data in XML | ![]() | 1.1 MB | Display | |
Data in CIF | ![]() | 1.5 MB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5t12C ![]() 5t1nC C: citing same article ( |
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Similar structure data | |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Details | Size exclusion gel filtration was used to determine that this is a 1:1 protein interaction and both proteins are monomers. Small angle X-ray scattering confirmed this and was used as a restraint in the structure calculation |
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Components
#1: Protein | Mass: 9254.570 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0A9N2, UniProt: P0A9N0*PLUS, Transferases; Transferring phosphorus-containing groups; Protein-serine/threonine kinases |
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#2: Protein | Mass: 28380.070 Da / Num. of mol.: 1 / Mutation: H356Q Source method: isolated from a genetically manipulated source Details: This molecule was mutated at position 356 from histidine to glutamine. In E. coli, when the native histidine is present, the sample can be phosphorylated. It was mutated to provide a ...Details: This molecule was mutated at position 356 from histidine to glutamine. In E. coli, when the native histidine is present, the sample can be phosphorylated. It was mutated to provide a homogeneous sample. Additionally, it comprises residues 170-424 of the larger Enzyme I-Ntr molecule. Residue 169 is mutated to glycine due to TEV protease cleavage. Source: (gene. exp.) ![]() ![]() Strain: K12 / Gene: ptsP, ygdF, ygdO, b2829, JW2797 / Plasmid: pET28a / Production host: ![]() ![]() References: UniProt: P37177, phosphoenolpyruvate-protein phosphotransferase |
-Experimental details
-Experiment
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NMR experiment |
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Sample preparation
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