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Open data
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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 informationprotein serine/threonine kinase activator activity / 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: 2000Title: 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: 1998Title: Solution structure of the recombinant human oncoprotein p13MTCP1 Authors: Yang, Y.-S. / Guignard, L. / Padilla, A. / Hoh, F. / Strub, M.-P. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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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
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Links
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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: ![]() |
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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 |
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Homo sapiens (human)
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