BMRB Entry 6263
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR6263
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Title: Solution Structure of a Loop Truncated Mutant from D. gigas Rubredoxin, NMR PubMed: 15691333
Deposition date: 2004-07-16 Original release date: 2005-03-15
Authors: Pais, T.; Lamosa, P.; dos Santos, W.; LeGall, J.; Turner, D.; Santos, H.
Citation: Pais, T.; Lamosa, P.; dos Santos, W.; LeGall, J.; Turner, D.; Santos, H.. "Structural Determinants of Protein Stabilization by Solutes: The Important of the Hair-pin Loop in Rubredoxins" FEBS J. 272, 999-1011 (2005).
Assembly members:
Rubredoxin, polymer, 39 residues, Formula weight is not available
Natural source: Common Name: Desulfovibrio gigas Taxonomy ID: 879 Superkingdom: Bacteria Kingdom: not available Genus/species: Desulfovibrio gigas
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Rubredoxin: MDIYVCTVCGYEYDPAFEDL
PDDWACPVCGASKDAFEKQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 219 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Rubredoxin | 1 |
Entities:
Entity 1, Rubredoxin 39 residues - Formula weight is not available
| 1 | MET | ASP | ILE | TYR | VAL | CYS | THR | VAL | CYS | GLY | ||||
| 2 | TYR | GLU | TYR | ASP | PRO | ALA | PHE | GLU | ASP | LEU | ||||
| 3 | PRO | ASP | ASP | TRP | ALA | CYS | PRO | VAL | CYS | GLY | ||||
| 4 | ALA | SER | LYS | ASP | ALA | PHE | GLU | LYS | GLN |
Samples:
sample_1: Rubredoxin 4 mM; H2O 90%; D2O 10%; NaCl 20 mM
sample_cond_1: ionic strength: 20 mM; pH: 7.6; pressure: 1 atm; temperature: 303 K
sample_cond_2: ionic strength: 20 mM; pH: 7.6; pressure: 1 atm; temperature: 313 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | not available |
| 2D TOCSY | not available | not available | not available |
| COSY | not available | not available | not available |
Software:
xwinnmr v3.1 - processing
DYANA v1.4 with modifications - iterative matrix relaxation
XEASY v1.3.10 - data analysis
GLOMSA - refinement
ProcheckNMR v3.4.4 - data analysis
NMR spectrometers:
- Bruker DRX 500 MHz
Related Database Links:
| PDB |