BMRB Entry 19317
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19317
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Title: Solution structure of HRDC1 domain of RecQ helicase from Deinococcus radiodurans PubMed: 23831579
Deposition date: 2013-06-24 Original release date: 2013-07-08
Authors: Liu, Shanshan; Zhang, Wen; Gao, Zengqiang; Ming, Qianqian; Hou, Haifeng; Lan, Wenxian; Wu, Houming; Cao, Chunyang; Dong, Yuhui
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:
DNA_helicase_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):
DNA_helicase_RecQ: HDAPLFEALRAWRLQKAKEL
SLPPYTIFHDATLKTIAELR
PGSHATLGTVSGVGGRKLAA
YGDEVLQVVRDSSGG
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 283 |
15N chemical shifts | 70 |
1H chemical shifts | 511 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | DNA helicase RecQ | 1 |
Entities:
Entity 1, DNA helicase 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: HRDC1, [U-98% 13C; U-98% 15N], 2 mM; phosphate buffer 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D 1H-15N NOESY | sample | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
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