BMRB Entry 15045
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15045
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Title: NMR SOLUTION STRUCTURE OF A MINIMAL TRANSMEMBRANE BETA-BARREL PLATFORM PROTEIN PubMed: 17260943
Deposition date: 2006-11-20 Original release date: 2007-05-21
Authors: Johansson, Maria; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin
Citation: Johansson, Maria; Alioth, Simon; Hu, Kaifeng; Walser, Reto; Koebnik, Ralf; Pervushin, Konstantin. "A Minimal Transmembrane Beta-Barrel Platform Protein Studied by NMR" Biochemistry 46, 1128-1140 (2007).
Assembly members:
BBP+EF, polymer, 156 residues, 17206.318 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BBP+EF: MPKDNTWYTGAKLGWSQYSR
ENQLGAGAFGGYQVNPYVGF
EMGYDWLGRMPRKAQGVQLT
AKLGYPKLGTDDLDIYTRLG
GMVWRADTSDKDGNGYISAA
EASVSPVFAGGVEYVIRRRI
TPEIATRLEYQWTNNASDNG
MLSLGVSYRFGQGEAA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 308 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 110 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BBP+EF in DHPC micelles | 1 |
Entities:
Entity 1, BBP+EF in DHPC micelles 156 residues - 17206.318 Da.
| 1 | MET | PRO | LYS | ASP | ASN | THR | TRP | TYR | THR | GLY | ||||
| 2 | ALA | LYS | LEU | GLY | TRP | SER | GLN | TYR | SER | ARG | ||||
| 3 | GLU | ASN | GLN | LEU | GLY | ALA | GLY | ALA | PHE | GLY | ||||
| 4 | GLY | TYR | GLN | VAL | ASN | PRO | TYR | VAL | GLY | PHE | ||||
| 5 | GLU | MET | GLY | TYR | ASP | TRP | LEU | GLY | ARG | MET | ||||
| 6 | PRO | ARG | LYS | ALA | GLN | GLY | VAL | GLN | LEU | THR | ||||
| 7 | ALA | LYS | LEU | GLY | TYR | PRO | LYS | LEU | GLY | THR | ||||
| 8 | ASP | ASP | LEU | ASP | ILE | TYR | THR | ARG | LEU | GLY | ||||
| 9 | GLY | MET | VAL | TRP | ARG | ALA | ASP | THR | SER | ASP | ||||
| 10 | LYS | ASP | GLY | ASN | GLY | TYR | ILE | SER | ALA | ALA | ||||
| 11 | GLU | ALA | SER | VAL | SER | PRO | VAL | PHE | ALA | GLY | ||||
| 12 | GLY | VAL | GLU | TYR | VAL | ILE | ARG | ARG | ARG | ILE | ||||
| 13 | THR | PRO | GLU | ILE | ALA | THR | ARG | LEU | GLU | TYR | ||||
| 14 | GLN | TRP | THR | ASN | ASN | ALA | SER | ASP | ASN | GLY | ||||
| 15 | MET | LEU | SER | LEU | GLY | VAL | SER | TYR | ARG | PHE | ||||
| 16 | GLY | GLN | GLY | GLU | ALA | ALA |
Samples:
sample_1: BBP+EF, [U-100% 13C; U-100% 15N; 80% 2H], 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
GROMACS, Lindahl, Hess and van der Spoel - structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB |
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