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- PDB-6hnh: Peptide-membrane interaction between targeting and lysis -

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Entry
Database: PDB / ID: 6hnh
TitlePeptide-membrane interaction between targeting and lysis
ComponentsLYS-LEU-LEU-LYS-LEU-LEU-LYS-LYS-VAL-VAL-GLY-ALA-LEU-GLY-NHE
KeywordsCELL CYCLE / PROTEIN
Biological speciessynthetic construct (others)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsSchneider, G. / Blatter, M.
CitationJournal: To Be Published
Title: Peptide-membrane interaction between targeting and lysis
Authors: Blatter, M. / Schneider, G.
History
DepositionSep 14, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 24, 2018Provider: repository / Type: Initial release
Revision 1.1May 8, 2019Group: Data collection / Category: pdbx_nmr_software / Item: _pdbx_nmr_software.name
Revision 1.2Nov 20, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_spectrometer.model

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Assembly

Deposited unit
A: LYS-LEU-LEU-LYS-LEU-LEU-LYS-LYS-VAL-VAL-GLY-ALA-LEU-GLY-NHE


Theoretical massNumber of molelcules
Total (without water)1,4821
Polymers1,4821
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: microscopy
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area120 Å2
ΔGint1 kcal/mol
Surface area1680 Å2
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 30structures with the least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide LYS-LEU-LEU-LYS-LEU-LEU-LYS-LYS-VAL-VAL-GLY-ALA-LEU-GLY-NHE


Mass: 1481.974 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)
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic1NOESY
121isotropic12D 1H-13C HSQC
131isotropic12D DQF-COSY

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Sample preparation

DetailsType: solution / Contents: 10 mM peptide, trifluoroethanol/water / Label: 1 / Solvent system: trifluoroethanol/water
SampleConc.: 10 mM / Component: peptide / Isotopic labeling: natural abundance
Sample conditionsIonic strength: 0 mM / Label: 1 / pH: 5 / Pressure: AMBIENT Pa / Temperature: 291 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Amber3.97Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollmanrefinement
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
SparkyGoddardchemical shift assignment
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 30 / Conformers submitted total number: 20

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