BMRB Entry 25483
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25483
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Title: Metal Binding of Glutaredoxins
Deposition date: 2015-02-11 Original release date: 2016-04-12
Authors: Bilinovich, Stephanie; Caporoso, Joel; Taraboletti, Alexandra; Duangjumpa, Nilubol; Panzner, Matthew; Prokop, Jeremy; Shriver, Leah; Leeper, Thomas
Citation: Bilinovich, Stephanie; Caporoso, Joel; Taraboletti, Alexandra; Duangjumpa, Nilubol; Panzner, Matthew; Prokop, Jeremy; Shriver, Leah; Leeper, Thomas. "Metal Binding of Glutaredoxins" Not known ., .-..
Assembly members:
Glutaredoxin, polymer, 92 residues, 9940.369 Da.
SILVER ION, non-polymer, 107.868 Da.
Natural source: Common Name: a-proteobacteria 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
FIGSVHVGGSDDLYALEDEG
KLDSLLKTGKLI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 361 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 581 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1_1 | 1 |
| 2 | entity_1_2 | 1 |
| 3 | SILVER ION | 2 |
Entities:
Entity 1, entity_1_1 92 residues - 9940.369 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 | SER | ||||
| 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 |
Entity 2, SILVER ION - Ag - 107.868 Da.
| 1 | AG |
Samples:
sample_1: Glutaredoxin, [U-99% 13C; U-99% 15N], 1.0 mM; SILVER ION 0.5 mM; MES 50 mM; TCEP 0.01 mM; D2O, [U-99% 2H], 5%; H2O 95%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR, CCPN - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
NMR spectrometers:
- Agilent 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