+Open data
-Basic information
Entry | Database: PDB / ID: 1qtu | ||||||
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Title | SOLUTION STRUCTURE OF THE ONCOPROTEIN P13MTCP1 | ||||||
Components | PROTEIN (PRODUCT OF THE MTCP1 ONCOGENE) | ||||||
Keywords | GENE REGULATION / BETA BARREL | ||||||
Function / homology | Function and homology information protein serine/threonine kinase activator activity / positive regulation of peptidyl-serine phosphorylation / intracellular signal transduction / protein kinase binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | Guignard, L. / Padilla, A. / Mispelter, J. / Yang, Y.-S. / Stern, M.-H. / Lhoste, J.-M. / Roumestand, C. | ||||||
Citation | Journal: J.Biomol.NMR / Year: 2000 Title: Backbone dynamics and solution structure refinement of the 15N-labeled human oncogenic protein p13MTCP1: comparison with X-ray data. Authors: Guignard, L. / Padilla, A. / Mispelter, J. / Yang, Y.S. / Stern, M.H. / Lhoste, J.M. / Roumestand, C. #1: Journal: J.Biomol.NMR / Year: 1998 Title: Solution structure of the recombinant human oncoprotein p13MTCP1 Authors: Yang, Y.-S. / Guignard, L. / Padilla, A. / Hoh, F. / Strub, M.-P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qtu.cif.gz | 47.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qtu.ent.gz | 33.8 KB | Display | PDB format |
PDBx/mmJSON format | 1qtu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qt/1qtu ftp://data.pdbj.org/pub/pdb/validation_reports/qt/1qtu | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13680.420 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell: T-CELLS / Cell (production host): BL21 / Production host: Escherichia coli (E. coli) / References: UniProt: P56278 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2mM p13MTCP1 U-15N; 20mM phosphate buffer NA;90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software | Name: Amber / Version: 4.1 / Developer: Kollman. P-A. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 1773 NOE restraints, 80 dihedral angle restraints |
NMR representative | Selection criteria: minimized average structure |
NMR ensemble | Conformers submitted total number: 1 |