BMRB Entry 30627
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30627
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Title: Structural Basis for Client Recognition and Activity of Hsp40 Chaperones
Deposition date: 2019-07-08 Original release date: 2019-09-11
Authors: Jiang, Y.; Rossi, P.; Kalodimos, C.
Citation: Jiang, Y.; Rossi, P.; Kalodimos, C.. "Structural Basis for Client Recognition and Activity of Hsp40 Chaperones" . ., .-..
Assembly members:
entity_1, polymer, 90 residues, 9138.532 Da.
Natural source: Common Name: E. coli Taxonomy ID: 83333 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3)
Entity Sequences (FASTA):
entity_1: MSTIALALLPLGSGGSGGSG
GSGRDLRAELPLTLEEAFHG
GERVVEVAGRRVSVRIPPGV
REGSVIRVPGMGGQGNPPGD
LLLVVRLLPH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 338 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 537 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 90 residues - 9138.532 Da.
| 1 | MET | SER | THR | ILE | ALA | LEU | ALA | LEU | LEU | PRO | |
| 2 | LEU | GLY | SER | GLY | GLY | SER | GLY | GLY | SER | GLY | |
| 3 | GLY | SER | GLY | ARG | ASP | LEU | ARG | ALA | GLU | LEU | |
| 4 | PRO | LEU | THR | LEU | GLU | GLU | ALA | PHE | HIS | GLY | |
| 5 | GLY | GLU | ARG | VAL | VAL | GLU | VAL | ALA | GLY | ARG | |
| 6 | ARG | VAL | SER | VAL | ARG | ILE | PRO | PRO | GLY | VAL | |
| 7 | ARG | GLU | GLY | SER | VAL | ILE | ARG | VAL | PRO | GLY | |
| 8 | MET | GLY | GLY | GLN | GLY | ASN | PRO | PRO | GLY | ASP | |
| 9 | LEU | LEU | LEU | VAL | VAL | ARG | LEU | LEU | PRO | HIS |
Samples:
sample_1: PhoA-CBD1, [U-13C; U-15N], 1 mM; potassium phosphate 20 mM; potassium chloride 75 mM; sodium azide 0.04%
sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | 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 CCH-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
Sparky, Goddard & Kneller - peak picking
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TopSpin v4.0, Bruker Biospin - collection
NMR spectrometers:
- Bruker AVANCE NEO 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts