BMRB Entry 16040
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16040
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Title: Solution structure of onconase C87A/C104A PubMed: 19655705
Deposition date: 2008-11-21 Original release date: 2009-11-02
Authors: Weininger, Ulrich; Schulenburg, Cindy; Arnold, Ulrich; Ulbrich-Hofmann, Renate; Balbach, Jochen
Citation: Schulenburg, Cindy; Low, Christian; Weininger, Ulrich; Mrestani-Klaus, Carmen; Hofmann, Hagen; Balbach, Jochen; Ulbrich-Hofmann, Renate; Arnold, Ulrich. "The folding pathway of onconase is directed by a conserved intermediate" Biochemistry 48, 8449-8457 (2009).
Assembly members:
onconase C87A/C104A, polymer, 104 residues, 11781.603 Da.
Natural source: Common Name: northern leopard frog Taxonomy ID: 8404 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: rana pipiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
onconase C87A/C104A: XDWLTFQKKHITNTRDVDCD
NIMSTNLFHCKDKNTFIYSR
PEPVKAICKGIIASKNVLTT
SEFYLSDCNVTSRPCKYKLK
KSTNKFAVTCENQAPVHFVG
VGSA
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 744 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | onconase C87A/C104A | 1 |
Entities:
Entity 1, onconase C87A/C104A 104 residues - 11781.603 Da.
| 1 | PCA | ASP | TRP | LEU | THR | PHE | GLN | LYS | LYS | HIS | ||||
| 2 | ILE | THR | ASN | THR | ARG | ASP | VAL | ASP | CYS | ASP | ||||
| 3 | ASN | ILE | MET | SER | THR | ASN | LEU | PHE | HIS | CYS | ||||
| 4 | LYS | ASP | LYS | ASN | THR | PHE | ILE | TYR | SER | ARG | ||||
| 5 | PRO | GLU | PRO | VAL | LYS | ALA | ILE | CYS | LYS | GLY | ||||
| 6 | ILE | ILE | ALA | SER | LYS | ASN | VAL | LEU | THR | THR | ||||
| 7 | SER | GLU | PHE | TYR | LEU | SER | ASP | CYS | ASN | VAL | ||||
| 8 | THR | SER | ARG | PRO | CYS | LYS | TYR | LYS | LEU | LYS | ||||
| 9 | LYS | SER | THR | ASN | LYS | PHE | ALA | VAL | THR | CYS | ||||
| 10 | GLU | ASN | GLN | ALA | PRO | VAL | HIS | PHE | VAL | GLY | ||||
| 11 | VAL | GLY | SER | ALA |
Samples:
sample_1: entity, [U-15N], 1.0 mM; H2O 90%; D2O 10%; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O, . - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts