BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6547

Title: structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection

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"  . ., .-..

Assembly members:
polyhistidine rich peptide, polymer, 27 residues, 2796 Da.
NH2, non-polymer, 16.023 Da.

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

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):
polyhistidine rich peptide: KKALLALALHHLAHLALHLA LALKKAX

Data sets:
Data typeCount
1H chemical shifts334

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1polyhistidine peptide1

Entities:

Entity 1, polyhistidine peptide 27 residues - 2796 Da.

1   LYSLYSALALEULEUALALEUALALEUHIS
2   HISLEUALAHISLEUALALEUHISLEUALA
3   LEUALALEULYSLYSALANH2

Samples:

sample_1: polyhistidine rich peptide 2.0 mM

exp_cond_1: pH: 4.1; temperature: 317 K

exp_cond_2: pH: 6.8; temperature: 317 K

Experiments:

NameSampleSample stateSample conditions
2D NOESYsample_1not availablenot available
2D TOCSYsample_1not availablenot available
2D ROESYsample_1not availablenot available
2D COSYsample_1not availablenot available

Software:

CCNMR - assignment

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

BMRB 16332 16333 6827 6886
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