+Open data
-Basic information
Entry | Database: PDB / ID: 2lxz | ||||||
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Title | Solution Structure of the Antimicrobial Peptide Human Defensin 5 | ||||||
Components | Defensin-5 | ||||||
Keywords | ANTIMICROBIAL PROTEIN / Human Defensin 5 / Cysteine Knot | ||||||
Function / homology | Function and homology information positive regulation of membrane permeability / Defensins / disruption of plasma membrane integrity in another organism / killing by host of symbiont cells / Alpha-defensins / defense response to fungus / transport vesicle / innate immune response in mucosa / secretory granule / positive regulation of interleukin-8 production ...positive regulation of membrane permeability / Defensins / disruption of plasma membrane integrity in another organism / killing by host of symbiont cells / Alpha-defensins / defense response to fungus / transport vesicle / innate immune response in mucosa / secretory granule / positive regulation of interleukin-8 production / Golgi lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / midbody / antibacterial humoral response / protein homotetramerization / secretory granule lumen / killing of cells of another organism / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / intracellular membrane-bounded organelle / innate immune response / protein homodimerization activity / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Wommack, A.J. / Robson, S.A. / Wanniarahchi, Y.A. / Wan, A. / Turner, C.J. / Nolan, E.M. | ||||||
Citation | Journal: Biochemistry / Year: 2012 Title: NMR solution structure and condition-dependent oligomerization of the antimicrobial Peptide human defensin 5. Authors: Wommack, A.J. / Robson, S.A. / Wanniarachchi, Y.A. / Wan, A. / Turner, C.J. / Wagner, G. / Nolan, E.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lxz.cif.gz | 190.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lxz.ent.gz | 160.3 KB | Display | PDB format |
PDBx/mmJSON format | 2lxz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lx/2lxz ftp://data.pdbj.org/pub/pdb/validation_reports/lx/2lxz | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3594.228 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DEFA5, DEF5 / Plasmid: pJ201-TEV-HD5 / Production host: Escherichia coli (E. coli) / References: UniProt: Q01523 |
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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: 0-1 mM TFA, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Units: mM / Component: TFA-1 / Conc. range: 0-1 |
Sample conditions | Ionic strength: 0.4 / pH: 4.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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-Processing
NMR software | Name: X-PLOR NIH / Developer: Schwieters, Kuszewski, Tjandra and Clore / Classification: refinement |
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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: 400 / Conformers submitted total number: 20 |