BMRB Entry 18124
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18124
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Title: Solution Structure of D. radiodurans RecQ HRDC domain 1 PubMed: 23831579
Deposition date: 2011-12-08 Original release date: 2014-04-23
Authors: Cao, Chunyang; Dong, Yuhui; Liu, Shanshan
Citation: Liu, Shanshan; Zhang, Wen; Gao, Zengqiang; Ming, Qianqian; Hou, Haifeng; Lan, Wenxian; Wu, Houming; Cao, Chunyang; Dong, Yuhui. "NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans." FEBS Lett. 587, 2635-2642 (2013).
Assembly members:
D._radiodurans_RecQ, polymer, 75 residues, 8054.224 Da.
Natural source: Common Name: Deinococcus radiodurans Taxonomy ID: 1299 Superkingdom: Bacteria Kingdom: not available Genus/species: Deinococcus radiodurans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
D._radiodurans_RecQ: HDAPLFEALRAWRLQKAKEL
SLPPYTIFHDATLKTIAELR
PGSHATLGTVSGVGGRKLAA
YGDEVLQVVRDSSGG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 287 |
| 15N chemical shifts | 71 |
| 1H chemical shifts | 514 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | D. radiodurans RecQ | 1 |
Entities:
Entity 1, D. radiodurans RecQ 75 residues - 8054.224 Da.
| 1 | HIS | ASP | ALA | PRO | LEU | PHE | GLU | ALA | LEU | ARG | ||||
| 2 | ALA | TRP | ARG | LEU | GLN | LYS | ALA | LYS | GLU | LEU | ||||
| 3 | SER | LEU | PRO | PRO | TYR | THR | ILE | PHE | HIS | ASP | ||||
| 4 | ALA | THR | LEU | LYS | THR | ILE | ALA | GLU | LEU | ARG | ||||
| 5 | PRO | GLY | SER | HIS | ALA | THR | LEU | GLY | THR | VAL | ||||
| 6 | SER | GLY | VAL | GLY | GLY | ARG | LYS | LEU | ALA | ALA | ||||
| 7 | TYR | GLY | ASP | GLU | VAL | LEU | GLN | VAL | VAL | ARG | ||||
| 8 | ASP | SER | SER | GLY | GLY |
Samples:
sample_1: D._radiodurans_RecQ, [U-100% 13C; U-100% 15N], 2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 760 mmHg; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N 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 HCCH-TOCSY | 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts