BMRB Entry 16618
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16618
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Title: NMR structure of the J-domain (residues 2-72) in the Escherichia coli CbpA PubMed: 20226195
Deposition date: 2009-11-25 Original release date: 2010-05-05
Authors: Ekiel, Irena; Sarri-Sarraf, Naghmeh
Citation: Sarraf, Naghmeh; Baardsnes, Jason; Cheng, Jing; Cygler, Maureen; Ekiel, Miroslaw. "Structural basis of the regulation of the CbpA co-chaperone by its specific modulator CbpM." J. Mol. Biol. 398, 111-121 (2010).
Assembly members:
J-domain of CbpA, polymer, 73 residues, 8720.918 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
J-domain of CbpA: GSELKDYYAIMGVKPTDDLK
TIKTAYRRLARKYHPDVSKE
PDAEARFKEVAEAWEVLSDE
QRRAEYDQMWQHR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 331 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 484 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | J-domain of CbpA | 1 |
Entities:
Entity 1, J-domain of CbpA 73 residues - 8720.918 Da.
GS at the beginning of the sequence is the cloning artifact.
| 1 | GLY | SER | GLU | LEU | LYS | ASP | TYR | TYR | ALA | ILE | ||||
| 2 | MET | GLY | VAL | LYS | PRO | THR | ASP | ASP | LEU | LYS | ||||
| 3 | THR | ILE | LYS | THR | ALA | TYR | ARG | ARG | LEU | ALA | ||||
| 4 | ARG | LYS | TYR | HIS | PRO | ASP | VAL | SER | LYS | GLU | ||||
| 5 | PRO | ASP | ALA | GLU | ALA | ARG | PHE | LYS | GLU | VAL | ||||
| 6 | ALA | GLU | ALA | TRP | GLU | VAL | LEU | SER | ASP | GLU | ||||
| 7 | GLN | ARG | ARG | ALA | GLU | TYR | ASP | GLN | MET | TRP | ||||
| 8 | GLN | HIS | ARG |
Samples:
sample_1: J-domain of CbpA, [U-13C; U-15N], 1 mM; sodium phosphate 50 mM; sodium chloride 250 mM; DTT 1 mM
sample_conditions_1: ionic strength: 300 mM; pH: 6.8; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | 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 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAA03950 BAA36142 BAB34578 BAG76586 BAI24855 |
| EMBL | CAD08237 CAP75502 CAQ31527 CAQ88675 CAQ97907 |
| GB | AAC45599 AAC74085 AAG55547 AAL20044 AAN42630 |
| PIR | AB0632 |
| REF | NP_309182 NP_415520 NP_455607 NP_460085 NP_706923 |
| SP | A1A9Q7 A7ZKA5 A7ZYV2 A8AI78 A9MH53 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts