BMRB Entry 15171

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15171

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Title:
H1 chemical shift assignment of putative membrane-anchoring domain of alMGS (S65-L87)
Deposition date:
2007-03-11
Original release date:
2007-06-06
Authors:
Lind, Jesper; Barany-Wallje, Elsa; Maler, Lena
Citation:

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).
PubMed: 17444657

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alMGS: SLKGFRLVLFVKRYVRKMRK LKL

Data typeCount
1H chemical shifts232

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S65-L87 binding domain of alMGS1

Entities:

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

1   SERLEULYSGLYPHEARGLEUVALLEUPHE
2   VALLYSARGTYRVALARGLYSMETARGLYS
3   LEULYSLEU

Samples:

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

Experiments:

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

Software:

FELIX, Accelrys - processing

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
GB AAK38877
SP Q93P60
AlphaFold Q93P60