+Open data
-Basic information
Entry | Database: PDB / ID: 6hne | ||||||
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Title | Peptide-membrane interaction between targeting and lysis | ||||||
Components | GLY-LEU-PHE-ASP-ILE-VAL-LYS-LYS-VAL-LEU-LYS-LEU-LEU-LYS-NHE | ||||||
Keywords | CELL CYCLE / PROTEIN | ||||||
Biological species | synthetic construct (others) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Schneider, G. / Blatter, M. / Mueller, A. | ||||||
Citation | Journal: To Be Published Title: Peptide-membrane interaction between targeting and lysis Authors: Blatter, M. / Schneider, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6hne.cif.gz | 90.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6hne.ent.gz | 63 KB | Display | PDB format |
PDBx/mmJSON format | 6hne.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6hne_validation.pdf.gz | 409.3 KB | Display | wwPDB validaton report |
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Full document | 6hne_full_validation.pdf.gz | 471 KB | Display | |
Data in XML | 6hne_validation.xml.gz | 10.5 KB | Display | |
Data in CIF | 6hne_validation.cif.gz | 13.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hn/6hne ftp://data.pdbj.org/pub/pdb/validation_reports/hn/6hne | HTTPS FTP |
-Related structure data
Related structure data | 6hngC 6hnhC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1616.106 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli) |
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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.abundance / Solvent system: trifluoroethanol/water |
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Sample | Conc.: 10 mM / Component: peptide / Isotopic labeling: none |
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: 6 | ||||||||||||||||
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 |