Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26722
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
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Citation: Correa, Fernando; Gardner, Kevin. "Basis of Mutual Domain Inhibition in a Bacterial Response Regulator" Cell Chem. Biol. 23, 945-954 (2016).
PubMed: 27524295
Assembly members:
ELI10215, polymer, 270 residues, Formula weight is not available
Natural source: Common Name: a-proteobacteria Taxonomy ID: 39960 Superkingdom: Bacteria Kingdom: not available Genus/species: Erythrobacter litoralis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHis - parallel
Entity Sequences (FASTA):
ELI10215: GAMGMSASQKIAANLPYLRR
YARALTGSQQTGDTFVRATL
EAAIADESLKQDVSEGRVPL
YKAFNALWSSSYLEVEGDDG
GDVVSAKEAGAGDRLKAVTP
LNRQALLLTTLEDFSVEDAA
EIMGLAPADVEGLVREAVAE
IDRESSTNVLIIEDEPLISM
QLEDLVRSLGHDIAGTAATR
TQAQEAVAKEKPGLVLADIQ
LADGSSGIDAVEDILGQFDV
PVIFITAYPERLLTGDRPEP
TYLVTKPFQESTVRTTISQA
LFFQNSPTAV
| Data type | Count |
| 13C chemical shifts | 497 |
| 15N chemical shifts | 252 |
| 1H chemical shifts | 257 |
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ELI10215 | 1 |
Entity 1, ELI10215 270 residues - Formula weight is not available
Residues 1-4 (GAMG) are cloning artifacts derived from the expression vector
| 1 | GLY | ALA | MET | GLY | MET | SER | ALA | SER | GLN | LYS | |
| 2 | ILE | ALA | ALA | ASN | LEU | PRO | TYR | LEU | ARG | ARG | |
| 3 | TYR | ALA | ARG | ALA | LEU | THR | GLY | SER | GLN | GLN | |
| 4 | THR | GLY | ASP | THR | PHE | VAL | ARG | ALA | THR | LEU | |
| 5 | GLU | ALA | ALA | ILE | ALA | ASP | GLU | SER | LEU | LYS | |
| 6 | GLN | ASP | VAL | SER | GLU | GLY | ARG | VAL | PRO | LEU | |
| 7 | TYR | LYS | ALA | PHE | ASN | ALA | LEU | TRP | SER | SER | |
| 8 | SER | TYR | LEU | GLU | VAL | GLU | GLY | ASP | ASP | GLY | |
| 9 | GLY | ASP | VAL | VAL | SER | ALA | LYS | GLU | ALA | GLY | |
| 10 | ALA | GLY | ASP | ARG | LEU | LYS | ALA | VAL | THR | PRO | |
| 11 | LEU | ASN | ARG | GLN | ALA | LEU | LEU | LEU | THR | THR | |
| 12 | LEU | GLU | ASP | PHE | SER | VAL | GLU | ASP | ALA | ALA | |
| 13 | GLU | ILE | MET | GLY | LEU | ALA | PRO | ALA | ASP | VAL | |
| 14 | GLU | GLY | LEU | VAL | ARG | GLU | ALA | VAL | ALA | GLU | |
| 15 | ILE | ASP | ARG | GLU | SER | SER | THR | ASN | VAL | LEU | |
| 16 | ILE | ILE | GLU | ASP | GLU | PRO | LEU | ILE | SER | MET | |
| 17 | GLN | LEU | GLU | ASP | LEU | VAL | ARG | SER | LEU | GLY | |
| 18 | HIS | ASP | ILE | ALA | GLY | THR | ALA | ALA | THR | ARG | |
| 19 | THR | GLN | ALA | GLN | GLU | ALA | VAL | ALA | LYS | GLU | |
| 20 | LYS | PRO | GLY | LEU | VAL | LEU | ALA | ASP | ILE | GLN | |
| 21 | LEU | ALA | ASP | GLY | SER | SER | GLY | ILE | ASP | ALA | |
| 22 | VAL | GLU | ASP | ILE | LEU | GLY | GLN | PHE | ASP | VAL | |
| 23 | PRO | VAL | ILE | PHE | ILE | THR | ALA | TYR | PRO | GLU | |
| 24 | ARG | LEU | LEU | THR | GLY | ASP | ARG | PRO | GLU | PRO | |
| 25 | THR | TYR | LEU | VAL | THR | LYS | PRO | PHE | GLN | GLU | |
| 26 | SER | THR | VAL | ARG | THR | THR | ILE | SER | GLN | ALA | |
| 27 | LEU | PHE | PHE | GLN | ASN | SER | PRO | THR | ALA | VAL |
sample_1: ELI10215, [U-13C; U-15N; U-2H], 0.5 1 mM; TRIS 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_2: ELI10215, [U-99% 13C; U-99% 15N], 0.5 1 mM; TRIS 10 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 7; pressure: 1 atm; temperature: 298.15 K
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | 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 HN(CA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY HSQC | sample_2 | isotropic | sample_conditions_1 |
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRView, Johnson, One Moon Scientific - chemical shift assignment
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks