BMRB Entry 27241
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27241
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Title: E.coli GcvH backbone chemical shift assignments PubMed: 29335837
Deposition date: 2017-08-31 Original release date: 2018-01-29
Authors: Yadav, Usha; Sundd, Monica
Citation: Yadav, Usha; Sundd, Monica. "Backbone chemical shift assignments of the glycine cleavage complex H protein of Escherichia coli" Biomol. NMR Assign. 12, 163-165 (2018).
Assembly members:
Glycine_cleavage_complex_H_protein, polymer, 128 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 Vector: pET28a
Entity Sequences (FASTA):
Glycine_cleavage_complex_H_protein: SNVPAELKYSKEHEWLRKEA
DGTYTVGITEHAQELLGDMV
FVDLPEVGATVSAGDDCAVA
ESVKAASDIYAPVSGEIVAV
NDALSDSPELVNSEPYAGGW
IFKIKASDESELESLLDATA
YEALLEDE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 369 |
| 15N chemical shifts | 120 |
| 1H chemical shifts | 120 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Glycine cleavage complex H protein polypeptide | 1 |
Entities:
Entity 1, Glycine cleavage complex H protein polypeptide 128 residues - Formula weight is not available
| 1 | SER | ASN | VAL | PRO | ALA | GLU | LEU | LYS | TYR | SER | ||||
| 2 | LYS | GLU | HIS | GLU | TRP | LEU | ARG | LYS | GLU | ALA | ||||
| 3 | ASP | GLY | THR | TYR | THR | VAL | GLY | ILE | THR | GLU | ||||
| 4 | HIS | ALA | GLN | GLU | LEU | LEU | GLY | ASP | MET | VAL | ||||
| 5 | PHE | VAL | ASP | LEU | PRO | GLU | VAL | GLY | ALA | THR | ||||
| 6 | VAL | SER | ALA | GLY | ASP | ASP | CYS | ALA | VAL | ALA | ||||
| 7 | GLU | SER | VAL | LYS | ALA | ALA | SER | ASP | ILE | TYR | ||||
| 8 | ALA | PRO | VAL | SER | GLY | GLU | ILE | VAL | ALA | VAL | ||||
| 9 | ASN | ASP | ALA | LEU | SER | ASP | SER | PRO | GLU | LEU | ||||
| 10 | VAL | ASN | SER | GLU | PRO | TYR | ALA | GLY | GLY | TRP | ||||
| 11 | ILE | PHE | LYS | ILE | LYS | ALA | SER | ASP | GLU | SER | ||||
| 12 | GLU | LEU | GLU | SER | LEU | LEU | ASP | ALA | THR | ALA | ||||
| 13 | TYR | GLU | ALA | LEU | LEU | GLU | ASP | GLU |
Samples:
sample_1: Glycine cleavage complex H protein, [U-99% 13C; U-99% 15N], 2 mM; Tris HCl buffer 50 mM; soduim chloride 200 mM
sample_conditions_1: ionic strength: 0.2 M; pH: 7.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts