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 15171

Title: H1 chemical shift assignment of putative membrane-anchoring domain of alMGS (S65-L87)   PubMed: 17444657

Deposition date: 2007-03-11 Original release date: 2007-06-06

Authors: Lind, Jesper; Barany-Wallje, Elsa; Maler, Lena

Citation: Lind, Jesper; Ramo, Tuulia; Rosen Klement, Maria; Barany-Wallje, Elsa; Epand, Richard; Epand, Raquel; Maler, Lena; Wieslander, Ake. "High cationic charge and bilayer interface-binding helices in a regulatory lipid glycosyltransferase"  Biochemistry 46, 5664-5677 (2007).

Assembly members:
alMGS, polymer, 23 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: 2148   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acholeplasma laidlawii

Experimental source:   Production method: chemical synthesis   Host organism: Acholeplasma laidlawii

Entity Sequences (FASTA):

Data typeCount
1H chemical shifts232

Additional metadata:

  • Assembly
  • Samples and Experiments
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  • Spectrometers
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Entity Assembly IDEntity NameEntity ID
1S65-L87 binding domain of alMGS1


Entity 1, S65-L87 binding domain of alMGS 23 residues - Formula weight is not available



alMGS_in_DHPC: alMGS binding domain 1 mM

alMGS_in_NeutralBicelle: alMGS binding domain 1 mM; DMPC 50 mM; DHPC 200 mM; phosphate buffer 50 mM

alMGS_in_ChargedBicelle: alMGS binding domain 1 mM; DMPC 45 mM; DMPG 5 mM; DHPC 200 mM; phosphate buffer 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.7; pressure: 1 atm; temperature: 310 K


NameSampleSample stateSample conditions
2D 1H-1H NOESYalMGS_in_DHPCisotropicsample_conditions_1
2D 1H-1H TOCSYalMGS_in_DHPCisotropicsample_conditions_1
2D 1H-1H NOESYalMGS_in_NeutralBicelleisotropicsample_conditions_1
2D 1H-1H TOCSYalMGS_in_NeutralBicelleisotropicsample_conditions_1
2D 1H-1H NOESYalMGS_in_ChargedBicelleisotropicsample_conditions_1
2D 1H-1H TOCSYalMGS_in_ChargedBicelleisotropicsample_conditions_1


FELIX, Accelrys - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

GB AAK38877
SP Q93P60
AlphaFold Q93P60