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- PDB-2kjo: pH dependent structures of LAH4 in micellar environment: mode of ... -

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Basic information

Entry
Database: PDB / ID: 2kjo
TitlepH dependent structures of LAH4 in micellar environment: mode of acting
Componentslah4
KeywordsDE NOVO PROTEIN / lah4 neutral
Biological speciesartificial gene (others)
MethodSOLUTION NMR
AuthorsGeorgescu, J. / Bechinger, B.
CitationJournal: Biophys.J. / Year: 2010
Title: NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.
Authors: Georgescu, J. / Munhoz, V.H. / Bechinger, B.
History
DepositionJun 4, 2009Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jun 23, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 26, 2020Group: Data collection / Other / Category: pdbx_database_status / pdbx_nmr_software
Item: _pdbx_database_status.status_code_cs / _pdbx_nmr_software.name
Revision 1.3Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.4May 8, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: lah4


Theoretical massNumber of molelcules
Total (without water)2,7881
Polymers2,7881
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 20structures with the lowest energy
RepresentativeModel #1minimized average

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Components

#1: Protein/peptide lah4


Mass: 2787.523 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) artificial gene (others)

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H TOCSY
1212D 1H-1H NOESY
1312D DQF-COSY
1412D ROESY

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Sample preparation

DetailsContents: 2 mM lah4-1, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O
SampleConc.: 2 mM / Component: lah4-1
Sample conditionsIonic strength: 8 mM KH2PO4 / pH: 6.8 / Pressure: ambient / Temperature: 317 K

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz

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Processing

NMR software
NameDeveloperClassification
CCNMRCieslar C. et alchemical shift assignment
CCNMRCieslar C. et aldata analysis
CCNMRCieslar C. et alstructure solution
CCNMRCieslar C. et alprocessing
CCNMRCieslar C. et alvisualisation
CCNMRRullmann, Doreleijers and Kapteinchemical shift assignment
CCNMRRullmann, Doreleijers and Kapteindata analysis
CCNMRRullmann, Doreleijers and Kapteinstructure solution
CCNMRRullmann, Doreleijers and Kapteinprocessing
CCNMRRullmann, Doreleijers and Kapteinvisualisation
CCNMRBrunger, Adams, Clore, Gros, Nilges and Readchemical shift assignment
CCNMRBrunger, Adams, Clore, Gros, Nilges and Readdata analysis
CCNMRBrunger, Adams, Clore, Gros, Nilges and Readstructure solution
CCNMRBrunger, Adams, Clore, Gros, Nilges and Readprocessing
CCNMRBrunger, Adams, Clore, Gros, Nilges and Readvisualisation
CCNMRLaskowski and MacArthurchemical shift assignment
CCNMRLaskowski and MacArthurdata analysis
CCNMRLaskowski and MacArthurstructure solution
CCNMRLaskowski and MacArthurprocessing
CCNMRLaskowski and MacArthurvisualisation
CCNMRBruker Biospinchemical shift assignment
CCNMRBruker Biospindata analysis
CCNMRBruker Biospinstructure solution
CCNMRBruker Biospinprocessing
CCNMRBruker Biospinvisualisation
CCNMRKoradi, Billeter and Wuthrichchemical shift assignment
CCNMRKoradi, Billeter and Wuthrichdata analysis
CCNMRKoradi, Billeter and Wuthrichstructure solution
CCNMRKoradi, Billeter and Wuthrichprocessing
CCNMRKoradi, Billeter and Wuthrichvisualisation
CCNMRKoradi, Billeter and Wuthrichrefinement
NMR representativeSelection criteria: minimized average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 20 / Conformers submitted total number: 20

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