+
Open data
-
Basic information
Entry | Database: PDB / ID: 2hfr | ||||||
---|---|---|---|---|---|---|---|
Title | solution structure of antimicrobial peptide Fowlicidin 3 | ||||||
![]() | Fowlicidin-3 | ||||||
![]() | ANTIMICROBIAL PROTEIN / ALPHA HELIX | ||||||
Function / homology | ![]() disruption of plasma membrane integrity in another organism / lipopolysaccharide binding / antimicrobial humoral immune response mediated by antimicrobial peptide / defense response to Gram-negative bacterium / membrane => GO:0016020 / defense response to Gram-positive bacterium / negative regulation of gene expression / innate immune response / extracellular space Similarity search - Function | ||||||
Method | SOLUTION NMR / annealing | ||||||
![]() | Bommineni, Y.R. / Dai, H. / Gong, Y. / Prakash, O. / Zhang, G. | ||||||
![]() | ![]() Title: Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities. Authors: Bommineni, Y.R. / Dai, H. / Gong, Y.X. / Soulages, J.L. / Fernando, S.C. / Desilva, U. / Prakash, O. / Zhang, G. #1: ![]() Title: Structure activity relationships of fowlicidin-1, a cathelicidin antimicrobial peptide in chicken Authors: Xiao, Y. / Dai, H. / Bommineni, Y.R. / Soulages, J.L. / Gong, Y. / Prakash, O. / Zhang, G. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 182.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 151.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 337.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 442.8 KB | Display | |
Data in XML | ![]() | 10.4 KB | Display | |
Data in CIF | ![]() | 16.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein/peptide | Mass: 3101.777 Da / Num. of mol.: 1 / Fragment: residues 125-151 / Source method: obtained synthetically Details: This sequence occurs naturally in Gallus gallus (chicken). References: UniProt: Q2IAL6 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||
NMR details | Text: This structure was determined using standard 2D homonuclear techniques |
-
Sample preparation
Details | Contents: 4mM Fowlicidin 3, 50%TFE, 50%H2O / Solvent system: 50%TFE, 50%H2O |
---|---|
Sample conditions | pH: 6.0 / Pressure: AMBIENT / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
---|---|
Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz |
-
Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: annealing / Software ordinal: 1 / Details: 205 NOE constraints | ||||||||||||
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 |