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Open data
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Basic information
Entry | Database: PDB / ID: 6hng | ||||||
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Title | Peptide-membrane interaction between targeting and lysis | ||||||
![]() | LYS-LEU-LEU-LYS-LEU-LEU-LYS-LYS-LEU-LEU-LYS-LEU-LEU-LYS-NHE | ||||||
![]() | CELL CYCLE / PROTEIN | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Schneider, G. / Blatter, M. / Mueller, A. | ||||||
![]() | ![]() Title: Peptide-membrane interaction between targeting and lysis Authors: Blatter, M. / Schneider, G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 102.9 KB | Display | ![]() |
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PDB format | ![]() | 73.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 408.3 KB | Display | ![]() |
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Full document | ![]() | 464.6 KB | Display | |
Data in XML | ![]() | 9.2 KB | Display | |
Data in CIF | ![]() | 12.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6hneC ![]() 6hnhC C: citing same article ( |
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Similar structure data | |
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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: 1696.364 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution / Contents: 10 mM peptide, trifluoroethanol/water / Label: nat.abund. / Solvent system: trifluoroethanol/water |
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Sample | Conc.: 10 mM / Component: peptide / Isotopic labeling: natural abundance |
Sample conditions | Ionic strength: 0 mM / Label: 1 / pH: 5 / Pressure: AMBIENT Pa / Temperature: 291 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: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 30 / Conformers submitted total number: 20 |