BMRB Entry 19618
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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/BMR19618
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Title: 1H, 15N and 13C resonance assignment of a transport protein PubMed: 24699374
Deposition date: 2013-11-18 Original release date: 2014-04-28
Authors: Zhang, Yi; Wang, Lei; Hu, Yunfei; Jin, Changwen
Citation: Zhang, Yi; Wang, Lei; Hu, Yunfei; Jin, Changwen. "Solution structure of the TatB component of the twin-arginine translocation system." Biochim. Biophys. Acta 1838, 1881-1888 (2014).
Assembly members:
protein, polymer, 109 residues, Formula weight is not available
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):
protein: MFDIGFSELLLVFIIGLVVL
GPQRLPVAVKTVAGWIRALR
SLATTVQNELTQELKLQEFQ
DSLKKVEKASLTNLTPELKA
SMDELRQAAESMKRSYVAND
PLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 469 |
| 15N chemical shifts | 116 |
| 1H chemical shifts | 753 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | transport protein | 1 |
Entities:
Entity 1, transport protein 109 residues - Formula weight is not available
| 1 | MET | PHE | ASP | ILE | GLY | PHE | SER | GLU | LEU | LEU | ||||
| 2 | LEU | VAL | PHE | ILE | ILE | GLY | LEU | VAL | VAL | LEU | ||||
| 3 | GLY | PRO | GLN | ARG | LEU | PRO | VAL | ALA | VAL | LYS | ||||
| 4 | THR | VAL | ALA | GLY | TRP | ILE | ARG | ALA | LEU | ARG | ||||
| 5 | SER | LEU | ALA | THR | THR | VAL | GLN | ASN | GLU | LEU | ||||
| 6 | THR | GLN | GLU | LEU | LYS | LEU | GLN | GLU | PHE | GLN | ||||
| 7 | ASP | SER | LEU | LYS | LYS | VAL | GLU | LYS | ALA | SER | ||||
| 8 | LEU | THR | ASN | LEU | THR | PRO | GLU | LEU | LYS | ALA | ||||
| 9 | SER | MET | ASP | GLU | LEU | ARG | GLN | ALA | ALA | GLU | ||||
| 10 | SER | MET | LYS | ARG | SER | TYR | VAL | ALA | ASN | ASP | ||||
| 11 | PRO | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: transport protein, [U-100% 13C; U-100% 15N], 1 mM; sodium acetate 20 mM; DPC 40 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.02 M; pH: 5.5; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- 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