BMRB Entry 28043
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28043
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Title: Backbone 13C and 15N assignment of lambdaQ PubMed: 32313022
Deposition date: 2019-11-13 Original release date: 2021-07-16
Authors: Dudenhoeffer, Benjamin; Knauer, Stefan
Citation: Dudenhoeffer, Benjamin; Borggraefe, Jan; Schweimer, Kristian; Knauer, Stefan. "NusA directly interacts with antitermination factor Q from phage lambda" Sci. Rep. 10, 6607-6607 (2020).
Assembly members:
lambdaQ, polymer, 172 residues, 18722 Da.
Natural source: Common Name: Bacteriophage lambda Taxonomy ID: 10710 Superkingdom: Virus Kingdom: not available Genus/species: Bacteriophage lambda
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETGb1a
Entity Sequences (FASTA):
lambdaQ: GAMGMAQSQAGFGMAAFCGK
HELSQNDKQKAINYLMQFAH
KVSGKYRGVAKLEGNTKAKV
LQVLATFAYADYCRSAATPG
ARCRDCHGTGRAVDIAKTEL
WGRVVEKECGRCKGVGYSRM
PASAAYRAVTMLIPNLTQPT
WSRTVKPLYDALVVQCHKEE
SIADNILNAVTR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 390 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 126 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | lambdaQ | 1 |
Entities:
Entity 1, lambdaQ 172 residues - 18722 Da.
Residue 0 represents a leftover of TEV-cleavage site
| 1 | GLY | ALA | MET | GLY | MET | ALA | GLN | SER | GLN | ALA | ||||
| 2 | GLY | PHE | GLY | MET | ALA | ALA | PHE | CYS | GLY | LYS | ||||
| 3 | HIS | GLU | LEU | SER | GLN | ASN | ASP | LYS | GLN | LYS | ||||
| 4 | ALA | ILE | ASN | TYR | LEU | MET | GLN | PHE | ALA | HIS | ||||
| 5 | LYS | VAL | SER | GLY | LYS | TYR | ARG | GLY | VAL | ALA | ||||
| 6 | LYS | LEU | GLU | GLY | ASN | THR | LYS | ALA | LYS | VAL | ||||
| 7 | LEU | GLN | VAL | LEU | ALA | THR | PHE | ALA | TYR | ALA | ||||
| 8 | ASP | TYR | CYS | ARG | SER | ALA | ALA | THR | PRO | GLY | ||||
| 9 | ALA | ARG | CYS | ARG | ASP | CYS | HIS | GLY | THR | GLY | ||||
| 10 | ARG | ALA | VAL | ASP | ILE | ALA | LYS | THR | GLU | LEU | ||||
| 11 | TRP | GLY | ARG | VAL | VAL | GLU | LYS | GLU | CYS | GLY | ||||
| 12 | ARG | CYS | LYS | GLY | VAL | GLY | TYR | SER | ARG | MET | ||||
| 13 | PRO | ALA | SER | ALA | ALA | TYR | ARG | ALA | VAL | THR | ||||
| 14 | MET | LEU | ILE | PRO | ASN | LEU | THR | GLN | PRO | THR | ||||
| 15 | TRP | SER | ARG | THR | VAL | LYS | PRO | LEU | TYR | ASP | ||||
| 16 | ALA | LEU | VAL | VAL | GLN | CYS | HIS | LYS | GLU | GLU | ||||
| 17 | SER | ILE | ALA | ASP | ASN | ILE | LEU | ASN | ALA | VAL | ||||
| 18 | THR | ARG |
Samples:
sample_1: lambdaQ, [U-80% 2H; U-98% 13C; U-98% 15N], 270 uM; NaCl 100 mM
sample_2: lambdaQ, [U-98% 13C; U-98% 15N], 500 uM; NaCl 100 mM
lambdaQ_conditions: ionic strength: 0.1 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
lambdaQ_N-Terminus_conditions: ionic strength: 0.3 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | lambdaQ_conditions |
| 3D HNCA | sample_1 | isotropic | lambdaQ_conditions |
| 3D HNCACB | sample_1 | isotropic | lambdaQ_conditions |
| 3D HNCO | sample_1 | isotropic | lambdaQ_conditions |
| 3D HN(CA)CO | sample_1 | isotropic | lambdaQ_conditions |
| 3D HN(CO)CA | sample_1 | isotropic | lambdaQ_conditions |
| 3D HN(COCA)CB | sample_1 | isotropic | lambdaQ_conditions |
| 2D 1H-15N HSQC | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
| 3D HNCA | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
| 3D HNCACB | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
| 3D HNCO | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
| 3D HCACO | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
| 3D HN(CO)CA | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
| 3D HN(COCA)CB | sample_2 | isotropic | lambdaQ_N-Terminus_conditions |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 700 MHz
Related Database Links:
| PDB |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts