BMRB Entry 16264
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16264
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Title: Solution structure of Glutaredoxin from Brucella melitensis. Seattle Structure Genomics Center for Infectious Disease (SSGCID) (Target ID BrabA.00079.a)
Deposition date: 2009-04-25 Original release date: 2009-07-14
Authors: Zheng, Suxin; Leeper, Thomas; Varani, Gabriele
Citation: Zheng, Suxin; Leeper, Thomas; Varani, Gabriele. "." . ., .-..
Assembly members:
Glutaredoxin, polymer, 92 residues, 9956.430 Da.
Natural source: Common Name: Brucella melitensis Taxonomy ID: 29459 Superkingdom: Bacteria Kingdom: not available Genus/species: Brucella melitensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Glutaredoxin: GPGSMVDVIIYTRPGCPYCA
RAKALLARKGAEFNEIDASA
TPELRAEMQERSGRNTFPQI
FIGSVHVGGCDDLYALEDEG
KLDSLLKTGKLI
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 276 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 625 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Glutaredoxin | 1 |
Entities:
Entity 1, Glutaredoxin 92 residues - 9956.430 Da.
| 1 | GLY | PRO | GLY | SER | MET | VAL | ASP | VAL | ILE | ILE | ||||
| 2 | TYR | THR | ARG | PRO | GLY | CYS | PRO | TYR | CYS | ALA | ||||
| 3 | ARG | ALA | LYS | ALA | LEU | LEU | ALA | ARG | LYS | GLY | ||||
| 4 | ALA | GLU | PHE | ASN | GLU | ILE | ASP | ALA | SER | ALA | ||||
| 5 | THR | PRO | GLU | LEU | ARG | ALA | GLU | MET | GLN | GLU | ||||
| 6 | ARG | SER | GLY | ARG | ASN | THR | PHE | PRO | GLN | ILE | ||||
| 7 | PHE | ILE | GLY | SER | VAL | HIS | VAL | GLY | GLY | CYS | ||||
| 8 | ASP | ASP | LEU | TYR | ALA | LEU | GLU | ASP | GLU | GLY | ||||
| 9 | LYS | LEU | ASP | SER | LEU | LEU | LYS | THR | GLY | LYS | ||||
| 10 | LEU | ILE |
Samples:
sample_1: Glutaredoxin, [U-100% 15N], 2.0 mM; KHPO4 20 mM; KCL 100 mM; H20 95%; D20 5%
sample_2: Glutaredoxin, [U-100% 13C; U-100% 15N], 2.0 mM; KHPO4 20 mM; KCL 100 mM; H20 95%; D20 5%
sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 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 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ANALYSIS, Wayne Boucher,Tim Stevens and Wim Vranken - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| EMBL | CAJ11835 CDL77247 |
| GB | AAL51366 AAN30771 AAX75168 ABQ61193 ABX62910 |
| REF | WP_002964949 WP_004692121 WP_006173401 WP_008507665 WP_008934891 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts