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- PDB-6wpd: NMR Structure of HSP1-NH2 antimicrobial peptide in presence of DP... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6wpd | |||||||||
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Title | NMR Structure of HSP1-NH2 antimicrobial peptide in presence of DPC-d38 micelles | |||||||||
![]() | HSP1-NH2 | |||||||||
![]() | ANTIMICROBIAL PROTEIN / antimicrobial peptide | |||||||||
Function / homology | defense response to fungus / killing of cells of another organism / defense response to bacterium / extracellular region / Hylaseptin-P1![]() | |||||||||
Biological species | Boana punctata (polka-dot treefrog) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
![]() | Verly, R.M. / Gomes, I.P. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Membrane interactions of the anuran antimicrobial peptide HSP1-NH2: Different aspects of the association to anionic and zwitterionic biomimetic systems. Authors: Gomes, I.P. / Santos, T.L. / de Souza, A.N. / Nunes, L.O. / Cardoso, G.A. / Matos, C.O. / Costa, L.M.F. / Liao, L.M. / Resende, J.M. / Verly, R.M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.2 KB | Display | ![]() |
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PDB format | ![]() | 28.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 371.5 KB | Display | ![]() |
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Full document | ![]() | 409.4 KB | Display | |
Data in XML | ![]() | 4.4 KB | Display | |
Data in CIF | ![]() | 6.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6wpbC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 1311.594 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Boana punctata (polka-dot treefrog) / References: UniProt: P84292 |
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Has ligand of interest | Y |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: micelle / Contents: 1.0 mM HSP1-NH2, 90% H2O/10% D2O / Details: 200 mM DPC-d38 micelles / Label: natural abundance / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1.0 mM / Component: HSP1-NH2 / Isotopic labeling: natural abundance |
Sample conditions | Details: peptide in presence of 200 mM DPC-d38 micelles / Ionic strength: 0 Not defined / Label: DPC-d38 / pH: 6.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 500 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing / 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: 10 |