BMRB Entry 26620
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26620
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Caro, Jose; Harpole, Kyle; Kasinath, Vignesh; Lim, Jackwee; Granja, Jeffrey; Valentine, Kathleen; Sharp, Kim; Wand, A Joshua. "Entropy in molecular recognition by proteins" Proc. Natl. Acad. Sci. U.S.A. 114, 6563-6568 (2017).
PubMed: 28584100
Assembly members:
Barnase, polymer, 110 residues, Formula weight is not available
DNA_dCGAC, polymer, 4 residues, Formula weight is not available
Natural source: Common Name: Bacillus amyloliquefaciens Taxonomy ID: 1390 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus amyloliquefaciens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETDUET
Entity Sequences (FASTA):
Barnase: AQVINTFDGVADYLQTYHKL
PDNYITKSEAQALGWVASKG
NLADVAPGKSIGGDIFSNRE
GKLPGKSGRTWREADINYTS
GFRNSDRILYSSDWLIYKTT
DHYQTFTKIR
DNA_dCGAC: CGAC
- assigned_chemical_shifts
- order_parameters
| Data type | Count |
| 13C chemical shifts | 55 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 274 |
| order parameters | 149 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Barnase | 1 |
| 2 | dCGAC | 2 |
Entities:
Entity 1, Barnase 110 residues - Formula weight is not available
| 1 | ALA | GLN | VAL | ILE | ASN | THR | PHE | ASP | GLY | VAL | |
| 2 | ALA | ASP | TYR | LEU | GLN | THR | TYR | HIS | LYS | LEU | |
| 3 | PRO | ASP | ASN | TYR | ILE | THR | LYS | SER | GLU | ALA | |
| 4 | GLN | ALA | LEU | GLY | TRP | VAL | ALA | SER | LYS | GLY | |
| 5 | ASN | LEU | ALA | ASP | VAL | ALA | PRO | GLY | LYS | SER | |
| 6 | ILE | GLY | GLY | ASP | ILE | PHE | SER | ASN | ARG | GLU | |
| 7 | GLY | LYS | LEU | PRO | GLY | LYS | SER | GLY | ARG | THR | |
| 8 | TRP | ARG | GLU | ALA | ASP | ILE | ASN | TYR | THR | SER | |
| 9 | GLY | PHE | ARG | ASN | SER | ASP | ARG | ILE | LEU | TYR | |
| 10 | SER | SER | ASP | TRP | LEU | ILE | TYR | LYS | THR | THR | |
| 11 | ASP | HIS | TYR | GLN | THR | PHE | THR | LYS | ILE | ARG |
Entity 2, dCGAC 4 residues - Formula weight is not available
| 1 | DC | DG | DA | DC |
Samples:
sample_1: Barnase, [U-100% 13C; U-100% 15N], 0.5 mM; Barnase, [65% of U-100% 13C 60% 2H; 35% of U-100% 15N], 0.5 mM; DNA (oligonucleotide) 1.4 mM
sample_conditions_1: ionic strength: 10 mM; pH: 6.2; pressure: 1 atm; temperature: 308.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D methyl CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 15N T1 relaxation | sample_1 | isotropic | sample_conditions_1 |
| 15N T2 relaxation | sample_1 | isotropic | sample_conditions_1 |
| 15N-1H NOE | sample_1 | isotropic | sample_conditions_1 |
| DZ (IZCZ compensated) relaxation | sample_1 | isotropic | sample_conditions_1 |
| DY (IZCZ compensated) relaxation | sample_1 | isotropic | sample_conditions_1 |
Software:
Felix, Accelrys Software Inc., Goddard - chemical shift assignment, data analysis
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks