BMRB Entry 5217
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5217
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Title: Solution Structure and DNA Binding Properties of the C-Terminal Domain of UvrC from E. coli PubMed: 12426397
Deposition date: 2001-11-23 Original release date: 2003-01-14
Authors: Singh, Shanteri; Folkers, Gert; Bonvin, Alexandre; Wechselberger, Rainer; Niztayev, Alidin; Boelens, Rolf; Kaptein, Robert
Citation: Singh, Shanteri; Folkers, Gert; Bonvin, Alexandre; Boelens, Rolf; Wechselberger, Rainer; Niztayev, Alidin; Kaptein, Robert. "Solution Structure and DNA-binding Properties of the C-Terminal Domain of UvrC from E. coli" EMBO J. 21, 6257-6266 (2002).
Assembly members:
UV Repair protein C, polymer, 78 residues, 8562.82 Da.
Natural source: Common Name: Escherichia coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology
Entity Sequences (FASTA):
UV Repair protein C: MGSSHHHHHHSSGLVPRGSH
MNTSSLETIEGVGPKRRQML
LKYMGGLQGLRNASVEEIAK
VPGISQGLAEKIFWSLKH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 261 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 447 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UvrC CTD | 1 |
Entities:
Entity 1, UvrC CTD 78 residues - 8562.82 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | ASN | THR | SER | SER | LEU | GLU | THR | ILE | GLU | ||||
| 4 | GLY | VAL | GLY | PRO | LYS | ARG | ARG | GLN | MET | LEU | ||||
| 5 | LEU | LYS | TYR | MET | GLY | GLY | LEU | GLN | GLY | LEU | ||||
| 6 | ARG | ASN | ALA | SER | VAL | GLU | GLU | ILE | ALA | LYS | ||||
| 7 | VAL | PRO | GLY | ILE | SER | GLN | GLY | LEU | ALA | GLU | ||||
| 8 | LYS | ILE | PHE | TRP | SER | LEU | LYS | HIS |
Samples:
sample_1: UV Repair protein C, [U-15N], 1.0 mM; NaCl 300 mM; sodium phosphate buffer 50 mM
sample_2: UV Repair protein C, [U-15N; U-13C], 1.0 mM; NaCl 300 mM; sodium phosphate buffer 50 mM
Ex-cond_1: ionic strength: 0.3 M; pH: 6.8 na; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HNCA | not available | not available | Ex-cond_1 |
| HNCO | not available | not available | Ex-cond_1 |
| HN(CO)CA | not available | not available | Ex-cond_1 |
| CBCANH | not available | not available | Ex-cond_1 |
| 1H-15N TOCSY HSQC | not available | not available | Ex-cond_1 |
| 1H-15N NOESY HSQC | not available | not available | Ex-cond_1 |
| 1H-13C-H(C)CH TOCSY | not available | not available | Ex-cond_1 |
| 1H-13C-(H)CCH TOCSY | not available | not available | Ex-cond_1 |
| 1H-15N NOESY HSQC | not available | not available | Ex-cond_1 |
| 2D-NOESY | not available | not available | Ex-cond_1 |
Software:
NMRPipe v1.8 - NMR data processing
NMRView v4.1.3 - NMR data analysis
ARIA v1.0 - ambiguous NOE assignment, structure calculation
CNS v1.0 - structure calculation
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker AMX 600 MHz
- Varian INOVA 750 MHz
Related Database Links:
| PDB | |
| GB | AHR43889 AHS24459 AHS50436 AHS52317 EFZ51080 |
| REF | WP_001345512 WP_023252848 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts