BMRB Entry 4677
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4677
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Title: Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ
Deposition date: 2000-03-02 Original release date: 2001-05-03
Authors: Martinez-Yamout, Maria; Legge, Glen; Zhang, Ouwen; Wright, Peter; Dyson, Jane
Citation: Martinez-Yamout, Maria; Legge, Glen; Zhang, Ouwen; Wright, Peter; Dyson, Jane. "Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ" J. Mol. Biol. 300, 805-818 (2000).
Assembly members:
cysteine-rich domain of DnaJ, polymer, 79 residues, 8518 Da.
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
cysteine-rich domain of DnaJ: GVTKEIRIPTLEECDVCHGS
GAKPGTQPQTCPTCHGSGQV
QMRQGFFAVQQTCPHCQGRG
TLIKDPCNKCHGHGRVERS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 300 |
| 15N chemical shifts | 81 |
| 1H chemical shifts | 482 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CRD monomer | 1 |
| 2 | Zn1 | 2 |
| 3 | Zn2 | 2 |
Entities:
Entity 1, CRD monomer 79 residues - 8518 Da.
| 1 | GLY | VAL | THR | LYS | GLU | ILE | ARG | ILE | PRO | THR | ||||
| 2 | LEU | GLU | GLU | CYS | ASP | VAL | CYS | HIS | GLY | SER | ||||
| 3 | GLY | ALA | LYS | PRO | GLY | THR | GLN | PRO | GLN | THR | ||||
| 4 | CYS | PRO | THR | CYS | HIS | GLY | SER | GLY | GLN | VAL | ||||
| 5 | GLN | MET | ARG | GLN | GLY | PHE | PHE | ALA | VAL | GLN | ||||
| 6 | GLN | THR | CYS | PRO | HIS | CYS | GLN | GLY | ARG | GLY | ||||
| 7 | THR | LEU | ILE | LYS | ASP | PRO | CYS | ASN | LYS | CYS | ||||
| 8 | HIS | GLY | HIS | GLY | ARG | VAL | GLU | ARG | SER |
Entity 2, Zn1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: cysteine-rich domain of DnaJ, [U-95% 13C; U-90% 15N], 0.6 mM
ex-cond_1: pH: 7.0; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| CBCA(CO)NH | sample_1 | not available | ex-cond_1 |
| HNCACB | sample_1 | not available | ex-cond_1 |
| C(CO)NH-TOOCSY | sample_1 | not available | ex-cond_1 |
| HNCO | sample_1 | not available | ex-cond_1 |
| HCCH-TOCSY | sample_1 | not available | ex-cond_1 |
| 15N-edited NOESY | sample_1 | not available | ex-cond_1 |
| 15N-edited TOCSY | sample_1 | not available | ex-cond_1 |
| 13C-edited NOESY | sample_1 | not available | ex-cond_1 |
| 13C, 15N-edited NOESY | sample_1 | not available | ex-cond_1 |
Software:
Felix v97 - transform and plotting
NMRPipe - transform
NMRView - plotting and analysis
NMR spectrometers:
- Brruker DMX 750 MHz
- Brruker DRX 600 MHz
- Brruker AMX 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAB33438 BAB96590 BAF79748 BAF79749 BAF79793 |
| GenBank | AAA00009 AAA23693 AAC73126 AAG54315 AAN41681 |
| REF | AP_000679 NP_285707 NP_308042 NP_414556 NP_705974 |
| SWISS-PROT | A7ZHA5 A7ZVV8 B1IRF9 P08622 Q0T8H5 |
Download simulated HSQC data in one of the following formats:
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