BMRB Entry 6611
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6611
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Title: 1H, 13C, and 15N chemical shift assignments for the receiver domain (residues 1-121) of NtrC4 from Aquifex aeolicus
Deposition date: 2005-04-26 Original release date: 2005-05-26
Authors: Matsubara, Koshi; Pelton, Jeffrey; Wemmer, David
Citation: Matsubara, Koshi; Pelton, Jeffrey; Wemmer, David. "1H, 13C, and 15N chemical shift assignments of the receiver domain of NtrC4 from Aquifex aeolicus" The BMRB entry is the only known published source for the data..
Assembly members:
receiver domain of NtrC4, polymer, 121 residues, 13627 Da.
Natural source: Common Name: Aquifex aeolicus Taxonomy ID: 224324 Superkingdom: Eubacteria Kingdom: Not applicable Genus/species: Aquifex aeolicus
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
receiver domain of NtrC4: MKRVLVVDDEESITSSLSAI
LEEEGYHPDTAKTLREAEKK
IKELFFPVIVLDVWMPDGDG
VNFIDFIKENSPDSVVIVIT
GHGSVDTAVKAIKKGAYEFL
EKPFSVERFLLTIKHAFEEY
S
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 360 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 746 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ntrc4r | 1 |
Entities:
Entity 1, Ntrc4r 121 residues - 13627 Da.
| 1 | MET | LYS | ARG | VAL | LEU | VAL | VAL | ASP | ASP | GLU | ||||
| 2 | GLU | SER | ILE | THR | SER | SER | LEU | SER | ALA | ILE | ||||
| 3 | LEU | GLU | GLU | GLU | GLY | TYR | HIS | PRO | ASP | THR | ||||
| 4 | ALA | LYS | THR | LEU | ARG | GLU | ALA | GLU | LYS | LYS | ||||
| 5 | ILE | LYS | GLU | LEU | PHE | PHE | PRO | VAL | ILE | VAL | ||||
| 6 | LEU | ASP | VAL | TRP | MET | PRO | ASP | GLY | ASP | GLY | ||||
| 7 | VAL | ASN | PHE | ILE | ASP | PHE | ILE | LYS | GLU | ASN | ||||
| 8 | SER | PRO | ASP | SER | VAL | VAL | ILE | VAL | ILE | THR | ||||
| 9 | GLY | HIS | GLY | SER | VAL | ASP | THR | ALA | VAL | LYS | ||||
| 10 | ALA | ILE | LYS | LYS | GLY | ALA | TYR | GLU | PHE | LEU | ||||
| 11 | GLU | LYS | PRO | PHE | SER | VAL | GLU | ARG | PHE | LEU | ||||
| 12 | LEU | THR | ILE | LYS | HIS | ALA | PHE | GLU | GLU | TYR | ||||
| 13 | SER |
Samples:
sample_1: receiver domain of NtrC4, [U-95% 13C; U-98% 15N], 1 ± 0.2 mM; potassium phosphate 10 ± 2 mM
conditions_1: pH: 7; pressure: 1 atm; temperature: 323 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1H15N_HSQC | sample_1 | not available | conditions_1 |
| 3D 15N-filtered NOESY-HSQC | sample_1 | not available | conditions_1 |
| 3D 13C-filtered NOESY-HSQC | sample_1 | not available | conditions_1 |
| HNCA | sample_1 | not available | conditions_1 |
| HNHA | sample_1 | not available | conditions_1 |
| H(CCO)NH | sample_1 | not available | conditions_1 |
| C(CCO)NH | sample_1 | not available | conditions_1 |
| HCCH-TOCSY | sample_1 | not available | conditions_1 |
| HBHA(CO)NH | sample_1 | not available | conditions_1 |
| HNCACB | sample_1 | not available | conditions_1 |
Software:
NMRPipe, Delaglio - data processing
NMRView, Bruce Johnson - assignments
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
- Bruker DRX 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts