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Yorodumi- PDB-1tv0: Solution structure of cryptdin-4, the most potent alpha-defensin ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1tv0 | ||||||
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Title | Solution structure of cryptdin-4, the most potent alpha-defensin from mouse Paneth cells | ||||||
Components | Cryptdin-4 | ||||||
Keywords | ANTIMICROBIAL PROTEIN / beta sheet / beta hairpin | ||||||
Function / homology | Function and homology information pore-forming activity / disruption of plasma membrane integrity in another organism / azurophil granule / transport vesicle / innate immune response in mucosa / phospholipid binding / antimicrobial humoral immune response mediated by antimicrobial peptide / antibacterial humoral response / killing of cells of another organism / cellular response to lipopolysaccharide ...pore-forming activity / disruption of plasma membrane integrity in another organism / azurophil granule / transport vesicle / innate immune response in mucosa / phospholipid binding / antimicrobial humoral immune response mediated by antimicrobial peptide / antibacterial humoral response / killing of cells of another organism / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium / protein homodimerization activity / extracellular space Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Jing, W. / Hunter, H.N. / Tanabe, H. / Ouellette, A.J. / Vogel, H.J. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: Solution Structure of Cryptdin-4, a Mouse Paneth Cell alpha-Defensin. Authors: Jing, W. / Hunter, H.N. / Tanabe, H. / Ouellette, A.J. / Vogel, H.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tv0.cif.gz | 203.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tv0.ent.gz | 177.3 KB | Display | PDB format |
PDBx/mmJSON format | 1tv0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tv/1tv0 ftp://data.pdbj.org/pub/pdb/validation_reports/tv/1tv0 | 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/peptide | Mass: 3771.609 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: DEFCR4 / Cell line (production host): BL21(DE3)-codon-Plus-RIL / Production host: Escherichia coli (E. coli) / References: UniProt: P28311 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: BRUCKER MODEL EQUIPPED WITH TRIPPLE RESONANCE PROBE |
-Sample preparation
Details | Contents: 3.2 mg protein H2O/D2O / Solvent system: H2O/D2O |
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Sample conditions | pH: 4.2 / Temperature: 303 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker Bruker Advance 700 / Manufacturer: Bruker / Model: Bruker Advance 700 / Field strength: 700 MHz |
-Processing
NMR software |
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NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformers calculated total number: 100 / Conformers submitted total number: 20 |