BMRB Entry 26802
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26802
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Title: Cold Shock Protein A PubMed: 29197185
Deposition date: 2016-05-17 Original release date: 2017-05-30
Authors: Caruso, Icaro; Panwalkar, Vineet; Arni, Raghuvir; Cornelio, Marinonio
Citation: Caruso, Icaro; Panwalkar, Vineet; Coronado, Monika; Dingley, Andrew; Cornelio, Marinonio; Willbold, Dieter; Arni, Raghuvir; Eberle, Raphael. "Structure and interaction of Corynebacterium pseudotuberculosis cold shock protein A with Y-box single-stranded DNA fragment." FEBS J. 285, 372-390 (2018).
Assembly members:
Molecule_1, polymer, 82 residues, 9118.9276 Da.
Natural source: Common Name: high GC Gram+ Taxonomy ID: 1719 Superkingdom: Bacteria Kingdom: not available Genus/species: Corynebacterium pseudotuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Molecule_1: MAQGTVKWFNAEKGFGFIAP
DDGSADVFVHYSEIQGNGFR
TLEENQKVEFEIGEGAKGPQ
AQQVHALGGENLYFQGHHHH
HH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 322 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 494 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Cold Shock Protein A | 1 |
Entities:
Entity 1, Cold Shock Protein A 82 residues - 9118.9276 Da.
| 1 | MET | ALA | GLN | GLY | THR | VAL | LYS | TRP | PHE | ASN | ||||
| 2 | ALA | GLU | LYS | GLY | PHE | GLY | PHE | ILE | ALA | PRO | ||||
| 3 | ASP | ASP | GLY | SER | ALA | ASP | VAL | PHE | VAL | HIS | ||||
| 4 | TYR | SER | GLU | ILE | GLN | GLY | ASN | GLY | PHE | ARG | ||||
| 5 | THR | LEU | GLU | GLU | ASN | GLN | LYS | VAL | GLU | PHE | ||||
| 6 | GLU | ILE | GLY | GLU | GLY | ALA | LYS | GLY | PRO | GLN | ||||
| 7 | ALA | GLN | GLN | VAL | HIS | ALA | LEU | GLY | GLY | GLU | ||||
| 8 | ASN | LEU | TYR | PHE | GLN | GLY | HIS | HIS | HIS | HIS | ||||
| 9 | HIS | HIS |
Samples:
CspA: Molecule 1, [U-13C; U-15N], 0.8 mM; K2HPO4 50.0 mM; NaCl 50.0 mM; DSS 0.1 mM; H2O 90%; D2O 10%
CspA_1: ionic strength: 0.050 M; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | CspA | isotropic | CspA_1 |
| 2D 1H-13C HSQC/HMQC | CspA | isotropic | CspA_1 |
| hbcbcgcdhd (hbCBcgcdHD) | CspA | isotropic | CspA_1 |
| hbcbcgcdcehe (hbCBcgcdceHE) | CspA | isotropic | CspA_1 |
| 3D 1H-13C NOESY | CspA | isotropic | CspA_1 |
| 3D HNCO | CspA | isotropic | CspA_1 |
Software:
CcpNmr_Analysis v2.4, CCPN - Chemical shift assignment
NMR spectrometers:
- Varian VNMRS 900 MHz
- Bruker Avance 599 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts