BMRB Entry 27316
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27316
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Title: NMR assignment of the transmembrane helix of BclxL in phospholipid nanodiscs
Deposition date: 2017-11-24 Original release date: 2018-07-12
Authors: Raltchev, Kolio; Pipercevic, Joka; Hagn, Franz
Citation: Raltchev, Kolio; Pipercevic, Joka; Hagn, Franz. "Structural analysis of natively-folded membrane-anchored proteins obtained by SortaseA-mediated ligation" Not known ., .-..
Assembly members:
BclxL, polymer, 35 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BclxL: GSGESRKGQERFNRWFLTGM
TVAGVVLLGSLFSRK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 62 |
15N chemical shifts | 26 |
1H chemical shifts | 26 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | BclxL | 1 |
Entities:
Entity 1, BclxL 35 residues - Formula weight is not available
1 | GLY | SER | GLY | GLU | SER | ARG | LYS | GLY | GLN | GLU | ||||
2 | ARG | PHE | ASN | ARG | TRP | PHE | LEU | THR | GLY | MET | ||||
3 | THR | VAL | ALA | GLY | VAL | VAL | LEU | LEU | GLY | SER | ||||
4 | LEU | PHE | SER | ARG | LYS |
Samples:
sample_1: BclxL, [U-13C; U-15N; U-2H], 400 mM; DMPC, [U-2H], 15 mM; DPMG, [U-2H], 5 mM; potassium phosphate 20 mM; sodium chloride 50 mM; EDTA 0.5 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 318 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker - collection, processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts