BMRB Entry 16333
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16333
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Title: pH dependent structures of LAH4 in micellar environment: mode of acting
Deposition date: 2009-06-04 Original release date: 2009-11-03
Authors: Georgescu, Julia; Bechinger, Burkhard
Citation: Georgescu, Julia; Bechinger, Burkhard. "Structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection" Biophys. J. ., .-..
Assembly members:
LAH4, polymer, 26 residues, 2787.555 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
LAH4: KKALLALALHHLAHLALHLA
LALKKA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 164 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | LAH4 | 1 |
Entities:
Entity 1, LAH4 26 residues - 2787.555 Da.
| 1 | LYS | LYS | ALA | LEU | LEU | ALA | LEU | ALA | LEU | HIS | ||||
| 2 | HIS | LEU | ALA | HIS | LEU | ALA | LEU | HIS | LEU | ALA | ||||
| 3 | LEU | ALA | LEU | LYS | LYS | ALA |
Samples:
sample_1: lah4 2 mM; H2O 90%; D2O 10%; NaCl 115 mM; Na2HPO4 20 mM; KH2PO4 8 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.8; pressure: 1 atm; temperature: 317 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D roesy | sample_1 | isotropic | sample_conditions_1 |
Software:
ccnmr, Bruker Biospin, Brunger, Adams, Clore, Gros, Nilges and Read, Cieslar C. et al, Koradi, Billeter and Wuthrich, Laskowski and MacArthur, Rullmann, Doreleijers and Kaptein - chemical shift assignment, data analysis, data analysis, processing, structure solution, visualisation
NMR spectrometers:
- Bruker DRX 500 MHz