BMRB Entry 5854
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5854
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Title: 1H, 13C, and 15N backbone assignments for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis PubMed: 14752265
Deposition date: 2003-06-26 Original release date: 2004-02-10
Authors: Markus, Michelle; Doliveira, Lisa; Malakian, Karl; Keeney, David; Severin, Anatoly; Underwood, Kathryn; Tsao, Desiree
Citation: Markus, Michelle; Doliveira, Lisa; Malakian, Karl; Keeney, David; Severin, Anatoly; Underwood, Kathryn; Tsao, Desiree. "Letter to the Editor: 1H , 13C, and 15N backbone assignments and secondary structure for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis " J. Biomol. NMR 28, 301-302 (2004).
Assembly members:
NAD+ synthetase, polymer, 272 residues, 30395 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Eubacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NAD+ synthetase: MSMQEKIMRELHVKPSIDPK
QEIEDRVNFLKQYVKKTGAK
GFVLGISGGQDSTLAGRLAQ
LAVESIREEGGDAQFIAVRL
PHGTQQDEDDAQLALKFIKP
DKSWKFDIKSTVSAFSDQYQ
QETGDQLTDFNKGNVKARTR
MIAQYAIGGQEGLLVLGTDH
AAEAVTGFFTKYGDGGADLL
PLTGLTKRQGRTLLKELGAP
ERLYLKEPTADLLDEKPQQS
DETELGISYDEIDDYLEGKE
VSAKVSEALEKRYSMTEHKR
QVPASMFDDWWK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 250 |
| 13C chemical shifts | 759 |
| 15N chemical shifts | 250 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NAD+ synthetase subunit 1 | 1 |
| 2 | NAD+ synthetase subunit 2 | 1 |
Entities:
Entity 1, NAD+ synthetase subunit 1 272 residues - 30395 Da.
| 1 | MET | SER | MET | GLN | GLU | LYS | ILE | MET | ARG | GLU | ||||
| 2 | LEU | HIS | VAL | LYS | PRO | SER | ILE | ASP | PRO | LYS | ||||
| 3 | GLN | GLU | ILE | GLU | ASP | ARG | VAL | ASN | PHE | LEU | ||||
| 4 | LYS | GLN | TYR | VAL | LYS | LYS | THR | GLY | ALA | LYS | ||||
| 5 | GLY | PHE | VAL | LEU | GLY | ILE | SER | GLY | GLY | GLN | ||||
| 6 | ASP | SER | THR | LEU | ALA | GLY | ARG | LEU | ALA | GLN | ||||
| 7 | LEU | ALA | VAL | GLU | SER | ILE | ARG | GLU | GLU | GLY | ||||
| 8 | GLY | ASP | ALA | GLN | PHE | ILE | ALA | VAL | ARG | LEU | ||||
| 9 | PRO | HIS | GLY | THR | GLN | GLN | ASP | GLU | ASP | ASP | ||||
| 10 | ALA | GLN | LEU | ALA | LEU | LYS | PHE | ILE | LYS | PRO | ||||
| 11 | ASP | LYS | SER | TRP | LYS | PHE | ASP | ILE | LYS | SER | ||||
| 12 | THR | VAL | SER | ALA | PHE | SER | ASP | GLN | TYR | GLN | ||||
| 13 | GLN | GLU | THR | GLY | ASP | GLN | LEU | THR | ASP | PHE | ||||
| 14 | ASN | LYS | GLY | ASN | VAL | LYS | ALA | ARG | THR | ARG | ||||
| 15 | MET | ILE | ALA | GLN | TYR | ALA | ILE | GLY | GLY | GLN | ||||
| 16 | GLU | GLY | LEU | LEU | VAL | LEU | GLY | THR | ASP | HIS | ||||
| 17 | ALA | ALA | GLU | ALA | VAL | THR | GLY | PHE | PHE | THR | ||||
| 18 | LYS | TYR | GLY | ASP | GLY | GLY | ALA | ASP | LEU | LEU | ||||
| 19 | PRO | LEU | THR | GLY | LEU | THR | LYS | ARG | GLN | GLY | ||||
| 20 | ARG | THR | LEU | LEU | LYS | GLU | LEU | GLY | ALA | PRO | ||||
| 21 | GLU | ARG | LEU | TYR | LEU | LYS | GLU | PRO | THR | ALA | ||||
| 22 | ASP | LEU | LEU | ASP | GLU | LYS | PRO | GLN | GLN | SER | ||||
| 23 | ASP | GLU | THR | GLU | LEU | GLY | ILE | SER | TYR | ASP | ||||
| 24 | GLU | ILE | ASP | ASP | TYR | LEU | GLU | GLY | LYS | GLU | ||||
| 25 | VAL | SER | ALA | LYS | VAL | SER | GLU | ALA | LEU | GLU | ||||
| 26 | LYS | ARG | TYR | SER | MET | THR | GLU | HIS | LYS | ARG | ||||
| 27 | GLN | VAL | PRO | ALA | SER | MET | PHE | ASP | ASP | TRP | ||||
| 28 | TRP | LYS |
Samples:
sample_1: NAD+ synthetase, [U-2H; U-13C; U-15N], 1.0 mM
sample_2: NAD+ synthetase, [U-2H; U-15N], 210 – 270 uM
conditions_1: pH: 7.5 na; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| The spectrometer was equipped with a triple resonance probe with x, y, and z | not available | not available | conditions_1 |
| gradients. | not available | not available | conditions_1 |
Software:
nmrPipe v2.1 - processing, inital visualization with nmrDraw
PIPP v4.2.2 - analysis of spectra, specifically peak-picking
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA08947 BAI83777 BAM49243 BAM56513 GAK81413 |
| EMBL | CAB12107 CCU56768 CEI55431 CEJ75856 |
| GB | AAA22635 ADV95243 AEP89377 AFI26860 AFQ56248 |
| REF | NP_388195 WP_003241188 WP_003246440 WP_010332951 WP_014662699 |
| SP | P08164 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts