BMRB Entry 5920
            Chem Shift validation:  AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5920
            
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Title: 1H, 13C and 15N backbone and side-chain chemical shift assignments of PrrA effector domain from R. sphaeroides PubMed: 14627811
Deposition date: 2003-08-26 Original release date: 2003-12-19
Authors: Laguri, Cedric; Phillips-jones, Mary; Williamson, Mike
Citation: Laguri, Cedric; Phillips-jones, Mary; Williamson, Mike. "Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from R. sphaeroides: insights into binding specificity " Nucleic Acids Res. 31, 6778-6787 (2003).
Assembly members:
PrrA, polymer, 81 residues,  Formula weight is not available
Natural source: Common Name: Rhodobacter sphaeroides Taxonomy ID: 1063 Superkingdom: Eubacteria Kingdom: not available Genus/species: Rhodobacter sphaeroides
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PrrA: MGSSHHHHHHSSGLVPRGSH
MLAKGESLPPPPENPMSADR
VRWEHIQRIYEMCDRNVSET
ARRLNMHRRTLQRILAKRSP
R
- assigned_chemical_shifts
 
| Data type | Count | 
| 1H chemical shifts | 548 | 
| 13C chemical shifts | 344 | 
| 15N chemical shifts | 89 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | PrrAC | 1 | 
Entities:
Entity 1, PrrAC 81 residues - Formula weight is not available
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | LEU | ALA | LYS | GLY | GLU | SER | LEU | PRO | PRO | ||||
| 4 | PRO | PRO | GLU | ASN | PRO | MET | SER | ALA | ASP | ARG | ||||
| 5 | VAL | ARG | TRP | GLU | HIS | ILE | GLN | ARG | ILE | TYR | ||||
| 6 | GLU | MET | CYS | ASP | ARG | ASN | VAL | SER | GLU | THR | ||||
| 7 | ALA | ARG | ARG | LEU | ASN | MET | HIS | ARG | ARG | THR | ||||
| 8 | LEU | GLN | ARG | ILE | LEU | ALA | LYS | ARG | SER | PRO | ||||
| 9 | ARG | 
Samples:
sample_1: PrrA, [U-95% 13C; U-95% 15N], 1.0 mM; ammonium sulfate 200 mM; NaCl 50 mM; sodium phosphate 50 mM; DTT 10 mM
Standard_condition: pH: 6.0; temperature: 275 K; ionic strength: 0.6 M
Experiments:
| Name | Sample | Sample state | Sample conditions | 
|---|
Software:
felix v2000 -
NMR spectrometers:
- Bruker DRX 500 MHz
 - Bruker DRX 600 MHz
 
Related Database Links:
| PDB | |
| EMBL | CAA54059 | 
| GB | AAA16649 ABA77661 ABN75289 ABP71845 ACM02772 | 
| REF | WP_002722225 WP_011909904 WP_015921751 YP_001042061 YP_001169150 | 
| SP | Q53228 | 
Download simulated HSQC data in one of the following formats:
            
CSV: Backbone
            or all simulated shifts
            
SPARKY: Backbone
            or all simulated shifts