BMRB Entry 30286
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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/BMR30286
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Title: Solution NMR structure of the membrane electron transporter CcdA PubMed: 29379172
Deposition date: 2017-04-24 Original release date: 2018-01-25
Authors: Zhou, Y.; Bushweller, J.
Citation: Zhou, Y.; Bushweller, J.. "Solution structure and elevator mechanism of the membrane electron transporter CcdA" Nat. Struct. Mol. Biol. 25, 163-169 (2018).
Assembly members:
entity_1, polymer, 232 residues, 25292.143 Da.
Natural source: Common Name: Thermus thermophilus Taxonomy ID: 300852 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MSLSLTAAFLAGVLSFLSPC
VLPLVPTYLFYLGGARGRPL
FNALFFILGFGAVFFLLGLP
FTLLGGLLFEHRQTLARVGG
VVLVLFGLYMLGLRPRWGVS
LRYEGETSRPLGAFLLGATL
ALGWTPCIGPILGAILTLTA
VGGGVGFLLAYILGLAVPFF
VVALFADRIKGWLRRAGRIS
HYVEVLAGVVLVLVGVLLFT
GTFTALNTFFLRITPEWLQR
YLPSHHHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 509 |
| 15N chemical shifts | 185 |
| 1H chemical shifts | 186 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 232 residues - 25292.143 Da.
| 1 | MET | SER | LEU | SER | LEU | THR | ALA | ALA | PHE | LEU | ||||
| 2 | ALA | GLY | VAL | LEU | SER | PHE | LEU | SER | PRO | CYS | ||||
| 3 | VAL | LEU | PRO | LEU | VAL | PRO | THR | TYR | LEU | PHE | ||||
| 4 | TYR | LEU | GLY | GLY | ALA | ARG | GLY | ARG | PRO | LEU | ||||
| 5 | PHE | ASN | ALA | LEU | PHE | PHE | ILE | LEU | GLY | PHE | ||||
| 6 | GLY | ALA | VAL | PHE | PHE | LEU | LEU | GLY | LEU | PRO | ||||
| 7 | PHE | THR | LEU | LEU | GLY | GLY | LEU | LEU | PHE | GLU | ||||
| 8 | HIS | ARG | GLN | THR | LEU | ALA | ARG | VAL | GLY | GLY | ||||
| 9 | VAL | VAL | LEU | VAL | LEU | PHE | GLY | LEU | TYR | MET | ||||
| 10 | LEU | GLY | LEU | ARG | PRO | ARG | TRP | GLY | VAL | SER | ||||
| 11 | LEU | ARG | TYR | GLU | GLY | GLU | THR | SER | ARG | PRO | ||||
| 12 | LEU | GLY | ALA | PHE | LEU | LEU | GLY | ALA | THR | LEU | ||||
| 13 | ALA | LEU | GLY | TRP | THR | PRO | CYS | ILE | GLY | PRO | ||||
| 14 | ILE | LEU | GLY | ALA | ILE | LEU | THR | LEU | THR | ALA | ||||
| 15 | VAL | GLY | GLY | GLY | VAL | GLY | PHE | LEU | LEU | ALA | ||||
| 16 | TYR | ILE | LEU | GLY | LEU | ALA | VAL | PRO | PHE | PHE | ||||
| 17 | VAL | VAL | ALA | LEU | PHE | ALA | ASP | ARG | ILE | LYS | ||||
| 18 | GLY | TRP | LEU | ARG | ARG | ALA | GLY | ARG | ILE | SER | ||||
| 19 | HIS | TYR | VAL | GLU | VAL | LEU | ALA | GLY | VAL | VAL | ||||
| 20 | LEU | VAL | LEU | VAL | GLY | VAL | LEU | LEU | PHE | THR | ||||
| 21 | GLY | THR | PHE | THR | ALA | LEU | ASN | THR | PHE | PHE | ||||
| 22 | LEU | ARG | ILE | THR | PRO | GLU | TRP | LEU | GLN | ARG | ||||
| 23 | TYR | LEU | PRO | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 24 | HIS | HIS |
Samples:
sample_2: CcdA, [U-13C; U-15N; U-2H], 0.37 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM
sample_3: CcdA, [U-15N; U-2H], 0.7 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM
sample_4: CcdA, [U-15N; U-2H], 0.7 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM
sample_5: CcdA single Cys mutants labeled with MTSL, [U-15N], 0.2 mM; potassium phosphate 25 mM; sodium acetate 25 mM; sodium azide 0.05%; sodium chloride 50 mM
sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 343 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_3 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_4 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_5 | isotropic | sample_conditions_1 |
Software:
Analysis v2.4.2, CCPN - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS-N, Yang Shen, and Ad Bax - data analysis
TOPSPIN, Bruker Biospin - collection
X-PLOR NIH v2.39, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
XPLOR-NIH v2.39, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker AvanceIII 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts