BMRB Entry 17825
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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/BMR17825
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Title: Solution Structure of the J Domain of HSJ1a PubMed: 22219199
Deposition date: 2011-08-02 Original release date: 2012-01-09
Authors: Zhou, Chenjie; Gao, Xuechao; Cao, Chunyang; Hu, Hongyu
Citation: Gao, Xue-Chao; Zhou, Chen-Jie; Zhou, Zi-Ren; Wu, Meng; Cao, Chun-Yang; Hu, Hong-Yu. "The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation." J. Biol. Chem. 287, 6044-6052 (2012).
Assembly members:
entity, polymer, 99 residues, 8556.679 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MASYYEILDVPRSASADDIK
KAYRRKALQWHPDKNPDNKE
FAEKKFKEVAEAYEVLSDKH
KREIYDRYGREPLTGTGTGP
SRAEAGSGGPGLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 185 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 367 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HSJ1a | 1 |
Entities:
Entity 1, HSJ1a 99 residues - 8556.679 Da.
| 1 | MET | ALA | SER | TYR | TYR | GLU | ILE | LEU | ASP | VAL | ||||
| 2 | PRO | ARG | SER | ALA | SER | ALA | ASP | ASP | ILE | LYS | ||||
| 3 | LYS | ALA | TYR | ARG | ARG | LYS | ALA | LEU | GLN | TRP | ||||
| 4 | HIS | PRO | ASP | LYS | ASN | PRO | ASP | ASN | LYS | GLU | ||||
| 5 | PHE | ALA | GLU | LYS | LYS | PHE | LYS | GLU | VAL | ALA | ||||
| 6 | GLU | ALA | TYR | GLU | VAL | LEU | SER | ASP | LYS | HIS | ||||
| 7 | LYS | ARG | GLU | ILE | TYR | ASP | ARG | TYR | GLY | ARG | ||||
| 8 | GLU | PRO | LEU | THR | GLY | THR | GLY | THR | GLY | PRO | ||||
| 9 | SER | ARG | ALA | GLU | ALA | GLY | SER | GLY | GLY | PRO | ||||
| 10 | GLY | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: HSJ1a, [U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_2: HSJ1a, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: 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 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
SPARKY, Goddard - peak picking
ARIA, Linge, O, . - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAE87866 BAE88406 BAF82315 BAF85450 BAG35597 |
| EMBL | CAA44968 CAA44969 |
| GB | AAA09034 AAA09035 AAH11609 AAH47056 AAP35751 |
| REF | NP_001034639 NP_001162567 NP_001253510 NP_001267342 NP_001271020 |
| SP | P25686 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts