BMRB Entry 26026
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR26026
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Title: Solution Structure of the PriC DNA replication restart protein PubMed: 27382050
Deposition date: 2016-04-07 Original release date: 2016-07-05
Authors: Cornilescu, Claudia; Cornilescu, Gabriel; Wessel, Sarah; Keck, James; Markley, John
Citation: Wessel, Sarah; Cornilescu, Claudia; Cornilescu, Gabriel; Hu, Kaifeng; Sandler, Steven; Markley, John; Keck, James. "Structure and Function of the PriC DNA Replication Restart Protein" J. Biol. Chem. 291, 18384-18396 (2016).
Assembly members:
PriC, polymer, 171 residues, 19733.648 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 Host organism: Escherichia coli
Entity Sequences (FASTA):
PriC: MRTPLLLQSLKTRVAALHTL
IGPLASQRHFSPRFDRQLFA
CRGARLGDYLTEAEESLTHL
EAAVNQGDATRVAWLAERLA
AQIEALQREAATATLRRHEN
AHLPGGRLHARLAEYQEYER
RLLAMKNEREQRYAERHDPQ
LAREITALDERLTRCRTAIA
RTERALERITR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 568 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 794 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PriC DNA replication restart protein | 1 |
Entities:
Entity 1, PriC DNA replication restart protein 171 residues - 19733.648 Da.
| 1 | MET | ARG | THR | PRO | LEU | LEU | LEU | GLN | SER | LEU | ||||
| 2 | LYS | THR | ARG | VAL | ALA | ALA | LEU | HIS | THR | LEU | ||||
| 3 | ILE | GLY | PRO | LEU | ALA | SER | GLN | ARG | HIS | PHE | ||||
| 4 | SER | PRO | ARG | PHE | ASP | ARG | GLN | LEU | PHE | ALA | ||||
| 5 | CYS | ARG | GLY | ALA | ARG | LEU | GLY | ASP | TYR | LEU | ||||
| 6 | THR | GLU | ALA | GLU | GLU | SER | LEU | THR | HIS | LEU | ||||
| 7 | GLU | ALA | ALA | VAL | ASN | GLN | GLY | ASP | ALA | THR | ||||
| 8 | ARG | VAL | ALA | TRP | LEU | ALA | GLU | ARG | LEU | ALA | ||||
| 9 | ALA | GLN | ILE | GLU | ALA | LEU | GLN | ARG | GLU | ALA | ||||
| 10 | ALA | THR | ALA | THR | LEU | ARG | ARG | HIS | GLU | ASN | ||||
| 11 | ALA | HIS | LEU | PRO | GLY | GLY | ARG | LEU | HIS | ALA | ||||
| 12 | ARG | LEU | ALA | GLU | TYR | GLN | GLU | TYR | GLU | ARG | ||||
| 13 | ARG | LEU | LEU | ALA | MET | LYS | ASN | GLU | ARG | GLU | ||||
| 14 | GLN | ARG | TYR | ALA | GLU | ARG | HIS | ASP | PRO | GLN | ||||
| 15 | LEU | ALA | ARG | GLU | ILE | THR | ALA | LEU | ASP | GLU | ||||
| 16 | ARG | LEU | THR | ARG | CYS | ARG | THR | ALA | ILE | ALA | ||||
| 17 | ARG | THR | GLU | ARG | ALA | LEU | GLU | ARG | ILE | THR | ||||
| 18 | ARG |
Samples:
sample_PriC: PriC, [U-13C; U-15N], 0.5 mM; MES 20 mM; DTT 5 mM; EDTA 1 mM
aligned-PriC: PriC, [U-13C; U-15N], 0.5 mM
MES: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_PriC | isotropic | MES |
| 3D HNCO | sample_PriC | isotropic | MES |
| 3D CBCA(CO)NH | sample_PriC | isotropic | MES |
| 3D HNCACB | sample_PriC | isotropic | MES |
| 3D C(CO)NH | sample_PriC | isotropic | MES |
| 3D H(CCO)NH | sample_PriC | isotropic | MES |
| 3D HBHA(CO)NH | sample_PriC | isotropic | MES |
| 3D HCCH-TOCSY | sample_PriC | isotropic | MES |
| 3D 1H-15N NOESY | sample_PriC | isotropic | MES |
| 3D 1H-13C NOESY aliphatic | sample_PriC | isotropic | MES |
| 3D 1H-13C NOESY aromatic | sample_PriC | isotropic | MES |
| (HB)CB(CGCD)HD | sample_PriC | isotropic | MES |
| (HB)CB(CGCDCE)HE | sample_PriC | isotropic | MES |
| 2D 1H-13C HSQC aliphatic | sample_PriC | isotropic | MES |
| 2D ARTSY | sample_PriC | isotropic | MES |
| 2D ARTSY | aligned-PriC | anisotropic | MES |
| 3D HCA(CO)N | sample_PriC | isotropic | MES |
| 3D HCA(CO)N | aligned-PriC | anisotropic | MES |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP, Garrett - chemical shift assignment, data analysis, peak picking
TALOS, Cornilescu, Delaglio and Bax - dihedral angle prediction
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization, refinement, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Varian INOVA 600 MHz
- Varian INOVA 800 MHz
- Bruker Avance 750 MHz
- Varian INOVA 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts