BMRB Entry 16333

Name: pH dependent structures of LAH4 in micellar environment: mode of acting
Published: 2009-11-03

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PDB ID: 2kjo
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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:

Assembly members:
LAH4, polymer, 26 residues, 2787.555 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
LAH4: KKALLALALHHLAHLALHLA LALKKA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LAH4	1

Entities:

Entity 1, LAH4 26 residues - 2787.555 Da.

1

LYS

ALA

LEU

ALA

LEU

ALA

LEU

HIS

2

HIS

LEU

ALA

HIS

LEU

ALA

LEU

HIS

LEU

ALA

3

LEU

ALA

LEU

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