+
Open data
-
Basic information
Entry | Database: PDB / ID: 1kj6 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of Human beta-Defensin 3 | ||||||
![]() | Beta-defensin 3 | ||||||
![]() | ANTIBIOTIC / defensin / antimicrobial protein / human beta-defensin 3 / beta-defensin / HBD3 | ||||||
Function / homology | ![]() CCR6 chemokine receptor binding / Beta defensins / Defensins / killing by host of symbiont cells / antimicrobial humoral response / chemoattractant activity / cell chemotaxis / Golgi lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / chemotaxis ...CCR6 chemokine receptor binding / Beta defensins / Defensins / killing by host of symbiont cells / antimicrobial humoral response / chemoattractant activity / cell chemotaxis / Golgi lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / chemotaxis / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / Distance geometry, Simulated Annealing, Molecular Dynamics | ||||||
![]() | Schibli, D.J. / Hunter, H.N. / Aseyev, V. / Starner, T.D. / Wiencek, J.M. / McCray Jr., P.B. / Tack, B.F. / Vogel, H.J. | ||||||
![]() | ![]() Title: The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. Authors: Schibli, D.J. / Hunter, H.N. / Aseyev, V. / Starner, T.D. / Wiencek, J.M. / McCray Jr., P.B. / Tack, B.F. / Vogel, H.J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 285.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 247.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 342.2 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 470.1 KB | Display | |
Data in XML | ![]() | 14.5 KB | Display | |
Data in CIF | ![]() | 23.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 5174.266 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||
NMR details | Text: This structure was determined using standard 2D homonuclear techniques. |
-
Sample preparation
Details |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Sample conditions | pH: 4.00 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
|
-
Processing
NMR software |
| ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: Distance geometry, Simulated Annealing, Molecular Dynamics Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |