BMRB Entry 34365
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34365
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Title: Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers PubMed: 32817429
Deposition date: 2019-03-06 Original release date: 2020-03-16
Authors: Schubeis, T.; Andreas, L.; Pintacuda, G.
Citation: Schubeis, Tobias; Le Marchand, Tanguy; Daday, Csaba; Kopec, Wojciech; Tekwani Movellan, Kumar; Stanek, Jan; Schwarzer, Tom; Castiglione, Kathrin; de Groot, Bert; Pintacuda, Guido; Andreas, Loren. "A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL" Proc. Natl. Acad. Sci. U.S.A. 117, 21014-21021 (2020).
Assembly members:
entity_1, polymer, 219 residues, 24087.912 Da.
Natural source: Common Name: Pseudomonas oleovorans Taxonomy ID: 301 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas oleovorans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MNENYPAKSAGYNQGDWVAS
FNFSKVYVGEELGDLNVGGG
ALPNADVSIGNDTTLTFDIA
YFVSSNIAVDFFVGVPARAK
FQGEKSISSLGRVSEVDYGP
AILSLQYHYDSFERLYPYVG
VGVGRVLFFDKTDGALSSFD
IKDKWAPAFQVGLRYDLGNS
WMLNSDVRYIPFKTDVTGTL
GPVPVSTKIEVDPFILSLGA
SYVFKLAAALEHHHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 591 |
| 15N chemical shifts | 172 |
| 1H chemical shifts | 804 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 219 residues - 24087.912 Da.
| 1 | MET | ASN | GLU | ASN | TYR | PRO | ALA | LYS | SER | ALA | ||||
| 2 | GLY | TYR | ASN | GLN | GLY | ASP | TRP | VAL | ALA | SER | ||||
| 3 | PHE | ASN | PHE | SER | LYS | VAL | TYR | VAL | GLY | GLU | ||||
| 4 | GLU | LEU | GLY | ASP | LEU | ASN | VAL | GLY | GLY | GLY | ||||
| 5 | ALA | LEU | PRO | ASN | ALA | ASP | VAL | SER | ILE | GLY | ||||
| 6 | ASN | ASP | THR | THR | LEU | THR | PHE | ASP | ILE | ALA | ||||
| 7 | TYR | PHE | VAL | SER | SER | ASN | ILE | ALA | VAL | ASP | ||||
| 8 | PHE | PHE | VAL | GLY | VAL | PRO | ALA | ARG | ALA | LYS | ||||
| 9 | PHE | GLN | GLY | GLU | LYS | SER | ILE | SER | SER | LEU | ||||
| 10 | GLY | ARG | VAL | SER | GLU | VAL | ASP | TYR | GLY | PRO | ||||
| 11 | ALA | ILE | LEU | SER | LEU | GLN | TYR | HIS | TYR | ASP | ||||
| 12 | SER | PHE | GLU | ARG | LEU | TYR | PRO | TYR | VAL | GLY | ||||
| 13 | VAL | GLY | VAL | GLY | ARG | VAL | LEU | PHE | PHE | ASP | ||||
| 14 | LYS | THR | ASP | GLY | ALA | LEU | SER | SER | PHE | ASP | ||||
| 15 | ILE | LYS | ASP | LYS | TRP | ALA | PRO | ALA | PHE | GLN | ||||
| 16 | VAL | GLY | LEU | ARG | TYR | ASP | LEU | GLY | ASN | SER | ||||
| 17 | TRP | MET | LEU | ASN | SER | ASP | VAL | ARG | TYR | ILE | ||||
| 18 | PRO | PHE | LYS | THR | ASP | VAL | THR | GLY | THR | LEU | ||||
| 19 | GLY | PRO | VAL | PRO | VAL | SER | THR | LYS | ILE | GLU | ||||
| 20 | VAL | ASP | PRO | PHE | ILE | LEU | SER | LEU | GLY | ALA | ||||
| 21 | SER | TYR | VAL | PHE | LYS | LEU | ALA | ALA | ALA | LEU | ||||
| 22 | GLU | HIS | HIS | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Outer membrane protein AlkL, [U-13C; U-15N], 0.5 w/w
sample_2: Outer membrane protein AlkL, [U-13C; U-15N; U-2H], 0.5 w/w
sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D hCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D hCONH | sample_1 | isotropic | sample_conditions_1 |
| 3D hcoCAcoNH | sample_1 | isotropic | sample_conditions_1 |
| 3D hcaCBcaNH | sample_1 | isotropic | sample_conditions_1 |
| 3D hcaCBcacoNH | sample_1 | isotropic | sample_conditions_1 |
| 3D hNCAHa | sample_1 | isotropic | sample_conditions_1 |
| 3D hNcoCAHa | sample_1 | isotropic | sample_conditions_1 |
| 3D hCOCAHa | sample_1 | isotropic | sample_conditions_1 |
| 3D hCOnCAHa | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D hCANH | sample_2 | isotropic | sample_conditions_1 |
| 3D hCONH | sample_2 | isotropic | sample_conditions_1 |
| 3D hcoCAcoNH | sample_2 | isotropic | sample_conditions_1 |
| 3D hCOcaNH | sample_2 | isotropic | sample_conditions_1 |
| 3D hNHH BASS-SD | sample_1 | isotropic | sample_conditions_1 |
| 3D hNNH BASS-SD | sample_1 | isotropic | sample_conditions_1 |
| 3D hCCH BASS-SD | sample_1 | isotropic | sample_conditions_1 |
| 3D hNHH RFDR | sample_1 | isotropic | sample_conditions_1 |
| 3D hCHH RFDR | sample_1 | isotropic | sample_conditions_1 |
| 4D HNNH RFDR | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
Sparky, Goddard - chemical shift assignment
CcpNmr Analysis, CCPN - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
NMR spectrometers:
- Bruker AVANCE III 1000 MHz
- Bruker AVANCE III 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts