BMRB Entry 16594
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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/BMR16594
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Title: Solution structure of DnaK suppressor protein from Agrobacterium tumefaciens C58. Northeast Structural Genomics Consortium target AtT12/Ontario Center for Structural Proteomics Target atc0888
Deposition date: 2009-11-02 Original release date: 2009-11-24
Authors: Wu, Bin; Yee, Adelinda; Fares, Christopher; Lemak, Alexander; Semest, Anthony; Arrowsmith, Cheryl
Citation: Wu, Bin; Yee, Adelinda; Fares, Christopher; Lemak, Alexander; Semest, Anthony; Arrowsmith, Cheryl. "Solution Structure of DnaK protein from Agrobacterium tumefaciens C58. Northeast Structural Genomics Consortium target AtT12/Ontario Center for Structural Proteomics Target atc0888" Not known ., .-..
Assembly members:
atc0888, polymer, 112 residues, 12636.203 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: Agrobacterium tumefaciens C58 Taxonomy ID: 176299 Superkingdom: Bacteria Kingdom: not available Genus/species: Agrobacterium not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
atc0888: LAGGKSMNVESYEKILRDRQ
RELYRRLHKIEADFEEPRNP
DDEDRASERSNDEVLDELGQ
VGQDELRAIDAALARIASGT
FGTCVKCGKRISEDRLKAVP
YTPFCQECAAAL
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 457 |
| 15N chemical shifts | 110 |
| 1H chemical shifts | 753 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | atc0888 | 1 |
| 2 | Zinc ion | 2 |
Entities:
Entity 1, atc0888 112 residues - 12636.203 Da.
| 1 | LEU | ALA | GLY | GLY | LYS | SER | MET | ASN | VAL | GLU | ||||
| 2 | SER | TYR | GLU | LYS | ILE | LEU | ARG | ASP | ARG | GLN | ||||
| 3 | ARG | GLU | LEU | TYR | ARG | ARG | LEU | HIS | LYS | ILE | ||||
| 4 | GLU | ALA | ASP | PHE | GLU | GLU | PRO | ARG | ASN | PRO | ||||
| 5 | ASP | ASP | GLU | ASP | ARG | ALA | SER | GLU | ARG | SER | ||||
| 6 | ASN | ASP | GLU | VAL | LEU | ASP | GLU | LEU | GLY | GLN | ||||
| 7 | VAL | GLY | GLN | ASP | GLU | LEU | ARG | ALA | ILE | ASP | ||||
| 8 | ALA | ALA | LEU | ALA | ARG | ILE | ALA | SER | GLY | THR | ||||
| 9 | PHE | GLY | THR | CYS | VAL | LYS | CYS | GLY | LYS | ARG | ||||
| 10 | ILE | SER | GLU | ASP | ARG | LEU | LYS | ALA | VAL | PRO | ||||
| 11 | TYR | THR | PRO | PHE | CYS | GLN | GLU | CYS | ALA | ALA | ||||
| 12 | ALA | LEU |
Entity 2, Zinc ion - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_2: atc0888, [U-7% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%
sample_1: atc0888, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MDDGUI v1.0, Gutmanas Arrowsmith - processing
SPARKY v3.95, Goddard - data analysis, peak picking
FAWN v1.0, Lemak and Arrowsmith - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment
PSVS, Bhattacharya and Montelione - NMR structure quality assessment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| GB | AAL41919 EGL61749 EHH03169 EMS97089 EPR08161 |
| REF | NP_528818 WP_003509276 WP_003522285 WP_006316614 WP_010971243 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts