BMRB Entry 15816
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15816
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Title: Solution NMR Structure of Allochromatium vinosum DsrR: Northeast Structural Genomics Consortium Target OP5
Deposition date: 2008-06-22 Original release date: 2008-07-03
Authors: Cort, John; Dahl, Christiane; Grimm, Frauke; Kennedy, Michael
Citation: Dahl, Christiane; Cort, John; Grimm, Frauke. "Solution NMR Structure of the IscA-like Protein DsrR Involved in Sulfur Oxidation in Allochromatium vinosum" Not known ., .-..
Assembly members:
DsrR, polymer, 125 residues, 13748.496 Da.
Natural source: Common Name: Allochromatium vinosum Taxonomy ID: 1049 Superkingdom: Bacteria Kingdom: not available Genus/species: Allochromatium vinosum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DsrR: MGSSHHHHHHSSGLVPRGSH
MMFKLTPAAAEQVLKAAKQG
GTEGMCLRLAAGRNPDGSID
YRMGFDDLTEDDIRLTSEGV
EIVIAPDYVSLLDQTTLDYV
ELEPGQFHFIFLNPRDPTYR
PPSGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 101 |
| 1H chemical shifts | 686 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | DsrR | 1 |
Entities:
Entity 1, DsrR 125 residues - 13748.496 Da.
sequence begins with residue -20. The first residue of the native DsrR sequence is Met 1
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | MET | PHE | LYS | LEU | THR | PRO | ALA | ALA | ALA | ||||
| 4 | GLU | GLN | VAL | LEU | LYS | ALA | ALA | LYS | GLN | GLY | ||||
| 5 | GLY | THR | GLU | GLY | MET | CYS | LEU | ARG | LEU | ALA | ||||
| 6 | ALA | GLY | ARG | ASN | PRO | ASP | GLY | SER | ILE | ASP | ||||
| 7 | TYR | ARG | MET | GLY | PHE | ASP | ASP | LEU | THR | GLU | ||||
| 8 | ASP | ASP | ILE | ARG | LEU | THR | SER | GLU | GLY | VAL | ||||
| 9 | GLU | ILE | VAL | ILE | ALA | PRO | ASP | TYR | VAL | SER | ||||
| 10 | LEU | LEU | ASP | GLN | THR | THR | LEU | ASP | TYR | VAL | ||||
| 11 | GLU | LEU | GLU | PRO | GLY | GLN | PHE | HIS | PHE | ILE | ||||
| 12 | PHE | LEU | ASN | PRO | ARG | ASP | PRO | THR | TYR | ARG | ||||
| 13 | PRO | PRO | SER | GLY | GLY |
Samples:
sample_1: DsrR, [U-10% 13C; U-100% 15N], 1 ± 0.1 mM; H2O 93%; D2O 7%; Tris HCl 50 mM; sodium chloride 500 mM; DTT 5 mM; sodium azide 0.02%
sample_2: DsrR, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; D2O 100%; Tris HCl 50 mM; sodium chloride 500 mM; DTT 5 mM; sodium azide 0.02%
sample_3: DsrR, [U-100% 13C; U-100% 15N], 1 ± 0.1 mM; H2O 93%; D2O 7%; Tris HCl 50 mM; sodium chloride 500 mM; DTT 5 mM; sodium azide 0.02%
sample_conditions_1: ionic strength: 625 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 1H-13C-13C-1H HMQC NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
FELIX, Accelrys Software Inc. - data analysis, processing
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
SPARKY, Goddard - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts