+Open data
-Basic information
Entry | Database: PDB / ID: 1koy | ||||||
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Title | NMR structure of DFF-C domain | ||||||
Components | DNA fragmentation factor alpha subunit | ||||||
Keywords | APOPTOSIS / DFF / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | Function and homology information negative regulation of deoxyribonuclease activity / deoxyribonuclease inhibitor activity / negative regulation of apoptotic DNA fragmentation / apoptotic DNA fragmentation / negative regulation of execution phase of apoptosis / Apoptosis induced DNA fragmentation / thymocyte apoptotic process / chaperone-mediated protein folding / protein folding chaperone / positive regulation of apoptotic process ...negative regulation of deoxyribonuclease activity / deoxyribonuclease inhibitor activity / negative regulation of apoptotic DNA fragmentation / apoptotic DNA fragmentation / negative regulation of execution phase of apoptosis / Apoptosis induced DNA fragmentation / thymocyte apoptotic process / chaperone-mediated protein folding / protein folding chaperone / positive regulation of apoptotic process / protein domain specific binding / chromatin / protein-containing complex / nucleoplasm / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Fukushima, K. / Kikuchi, J. / Koshiba, S. / Kigawa, T. / Kuroda, Y. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2002 Title: Solution structure of the DFF-C domain of DFF45/ICAD. A structural basis for the regulation of apoptotic DNA fragmentation. Authors: Fukushima, K. / Kikuchi, J. / Koshiba, S. / Kigawa, T. / Kuroda, Y. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1koy.cif.gz | 28.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1koy.ent.gz | 19.2 KB | Display | PDB format |
PDBx/mmJSON format | 1koy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ko/1koy ftp://data.pdbj.org/pub/pdb/validation_reports/ko/1koy | HTTPS FTP |
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-Related structure data
Related structure data | 1iyrC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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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: 7009.962 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: O00273 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Details | Contents: U-13C, 15N |
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Sample conditions | pH: 6.50 / Temperature: 298.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 10 / Conformers submitted total number: 1 |