+Open data
-Basic information
Entry | Database: PDB / ID: 1bu9 | ||||||
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Title | SOLUTION STRUCTURE OF P18-INK4C, 21 STRUCTURES | ||||||
Components | PROTEIN (CYCLIN-DEPENDENT KINASE 6 INHIBITOR) | ||||||
Keywords | HORMONE/GROWTH FACTOR / CELL CYCLE INHIBITOR / P18INK4C / TUMOR / SUPPRESSOR / CYCLIN-DEPENDENT KINASE / HORMONE-GROWTH FACTOR COMPLEX | ||||||
Function / homology | Function and homology information negative regulation of phosphorylation / cyclin-dependent protein serine/threonine kinase inhibitor activity / oligodendrocyte differentiation / regulation of cyclin-dependent protein serine/threonine kinase activity / regulation of G1/S transition of mitotic cell cycle / negative regulation of stem cell proliferation / stem cell proliferation / Oncogene Induced Senescence / negative regulation of cell growth / Cyclin D associated events in G1 ...negative regulation of phosphorylation / cyclin-dependent protein serine/threonine kinase inhibitor activity / oligodendrocyte differentiation / regulation of cyclin-dependent protein serine/threonine kinase activity / regulation of G1/S transition of mitotic cell cycle / negative regulation of stem cell proliferation / stem cell proliferation / Oncogene Induced Senescence / negative regulation of cell growth / Cyclin D associated events in G1 / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / cell cycle / negative regulation of cell population proliferation / protein kinase binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Byeon, I.-J.L. / Li, J. / Tsai, M.-D. | ||||||
Citation | Journal: Biochemistry / Year: 1999 Title: Tumor suppressor INK4: determination of the solution structure of p18INK4C and demonstration of the functional significance of loops in p18INK4C and p16INK4A. Authors: Li, J. / Byeon, I.J. / Ericson, K. / Poi, M.J. / O'Maille, P. / Selby, T. / Tsai, M.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bu9.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1bu9.ent.gz | 861.8 KB | Display | PDB format |
PDBx/mmJSON format | 1bu9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bu/1bu9 ftp://data.pdbj.org/pub/pdb/validation_reports/bu/1bu9 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 18149.357 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: DL21(DE3) / Production host: Escherichia coli (E. coli) / Strain (production host): DL21(DE3) / References: UniProt: P42773 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE SOLUTION STRUCTURE OF P18-INK4C HAS BEEN DETERMINED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR. THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) ...Text: THE SOLUTION STRUCTURE OF P18-INK4C HAS BEEN DETERMINED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR. THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER). THE CALCULATION IS BASED ON 3175 EXPERIMENTAL NMR RESTRAINTS (3062 DISTANCE AND 113 TORSION ANGLE RESTRAINTS). |
-Sample preparation
Sample conditions | pH: 7.5 / Temperature: 293 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: CLOSEST TO MEAN STRUCTURE WHICH SHOWS GOOD AGREEMENT WITH THE CONSTRAINTS Conformers calculated total number: 50 / Conformers submitted total number: 21 |