BMRB Entry 5847
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5847
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Title: Backbone and sidechain 1H, 13C, and 15N chemical shifts for Sda PubMed: 15023339
Deposition date: 2003-06-26 Original release date: 2003-11-21
Authors: Rowland, Susan; Maciejewski, Mark; King, Glenn
Citation: Rowland, Susan; Burkholder, William; Cunningham, K; Maciejewski, Mark; Grossman, Alan; King, Glenn. "Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis" Mol. Cell. 13, 689-701 (2004).
Assembly members:
Sda, polymer, 46 residues, Formula weight is not available
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Eubacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
Sda: MRKLSDELLIESYFKATEMN
LNRDFIELIENEIKRRSLGH
IISVSS
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 353 |
| 13C chemical shifts | 201 |
| 15N chemical shifts | 49 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Sda | 1 |
Entities:
Entity 1, Sda 46 residues - Formula weight is not available
| 1 | MET | ARG | LYS | LEU | SER | ASP | GLU | LEU | LEU | ILE | ||||
| 2 | GLU | SER | TYR | PHE | LYS | ALA | THR | GLU | MET | ASN | ||||
| 3 | LEU | ASN | ARG | ASP | PHE | ILE | GLU | LEU | ILE | GLU | ||||
| 4 | ASN | GLU | ILE | LYS | ARG | ARG | SER | LEU | GLY | HIS | ||||
| 5 | ILE | ILE | SER | VAL | SER | SER |
Samples:
Sample_1: Sda, [U-13C; U-15N], 1.0 mM
cond_H2O: pH: 6.85 na; temperature: 298 K; ionic strength: 0.125 M
cond_D2O: pH: 6.85 na; temperature: 298 K; ionic strength: 0.125 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCACB | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
| 3D HC(CO)NH-TOCSY | not available | not available | not available |
| 3D C(CO)NH-TOCSY | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| 3D HNHA | not available | not available | not available |
| 3D HNHB | not available | not available | not available |
| 3D HCCH-COSY | not available | not available | not available |
| 2D 1H-1H TOCSY | not available | not available | not available |
| 2D 1H-1H DQF-COSY | not available | not available | not available |
| 3D 15N-separated NOESY-HSQC | not available | not available | not available |
| 3D 13C-separated NOESY-HSQC | not available | not available | not available |
| 3D 15N-separated TOCSY-HSQC | not available | not available | not available |
Software:
NMRpipe v1.0 - NMR data processing
XEASY v1.3.13 - Spectral analysis, peak assignment
NMR spectrometers:
- INOVA Varian 500 MHz
- INOVA Varian 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAI86094 GAK78421 |
| EMBL | CAE01463 CCU59089 |
| GB | ADM38587 ADP33164 ADV93314 AEP87448 AEP91604 |
| REF | WP_003226124 WP_003325380 WP_010886571 YP_003866896 YP_003974095 |
| SP | Q7WY62 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts