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) 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):
alMGS: SLKGFRLVLFVKRYVRKMRK
LKL
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 232 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | S65-L87 binding domain of alMGS | 1 |
Entities:
Entity 1, S65-L87 binding domain of alMGS 23 residues - Formula weight is not available
| 1 | SER | LEU | LYS | GLY | PHE | ARG | LEU | VAL | LEU | PHE | ||||
| 2 | VAL | LYS | ARG | TYR | VAL | ARG | LYS | MET | ARG | LYS | ||||
| 3 | LEU | LYS | LEU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | alMGS_in_DHPC | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | alMGS_in_DHPC | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | alMGS_in_NeutralBicelle | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | alMGS_in_NeutralBicelle | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | alMGS_in_ChargedBicelle | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | alMGS_in_ChargedBicelle | isotropic | sample_conditions_1 |
Software:
FELIX, Accelrys - processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 500 MHz