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Yorodumi- PDB-2hr9: Solution structure of human translationally controlled tumor protein -
+Open data
-Basic information
Entry | Database: PDB / ID: 2hr9 | |||||||||
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Title | Solution structure of human translationally controlled tumor protein | |||||||||
Components | Translationally-controlled tumor protein | |||||||||
Keywords | APOPTOSIS / METAL BINDING PROTEIN / TUMOR PROTEIN | |||||||||
Function / homology | Function and homology information negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / cytoplasmic microtubule / multivesicular body / response to virus / spindle pole / intracellular calcium ion homeostasis / calcium ion transport / regulation of apoptotic process / calcium ion binding / negative regulation of apoptotic process ...negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage / cytoplasmic microtubule / multivesicular body / response to virus / spindle pole / intracellular calcium ion homeostasis / calcium ion transport / regulation of apoptotic process / calcium ion binding / negative regulation of apoptotic process / RNA binding / extracellular space / extracellular exosome / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Feng, Y. / Liu, D. / Yao, H. / Wang, J. | |||||||||
Citation | Journal: Arch.Biochem.Biophys. / Year: 2007 Title: Solution structure and mapping of a very weak calcium-binding site of human translationally controlled tumor protein by NMR Authors: Feng, Y. / Liu, D. / Yao, H. / Wang, J. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hr9.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2hr9.ent.gz | 895.5 KB | Display | PDB format |
PDBx/mmJSON format | 2hr9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2hr9_validation.pdf.gz | 342.2 KB | Display | wwPDB validaton report |
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Full document | 2hr9_full_validation.pdf.gz | 503 KB | Display | |
Data in XML | 2hr9_validation.xml.gz | 75.4 KB | Display | |
Data in CIF | 2hr9_validation.cif.gz | 94.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hr/2hr9 ftp://data.pdbj.org/pub/pdb/validation_reports/hr/2hr9 | HTTPS FTP |
-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: 20690.498 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TPT1 / Plasmid: pET22b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): Bl21(DE3) / References: UniProt: P13693 |
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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: 1-2MM TCTP U-15N,13C; 200mM potassium phosphate buffer; 10mM EDTA; 0.01% DSS; 0.01% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 200mM / pH: 7.8 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |