BMRB Entry 4371
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4371
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NMR-STAR v3 text file.
XML gzip file.
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Citation: Gorbatyuk, Vitaliy; Chen, Yi-Cheng; Wu, Yung-Jean; Youle, Richard; Huang, Tai-huang. "Sequence-specific 1H, 13C and 15N Resonance Assignments of Recombinant
Onconase/P-30 Protein" J. Biomol. NMR 15, 343-344 (1999).
Assembly members:
Recombinant Onconase/ranpirnase, polymer, 105 residues, 11958 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 Vector: pET-11d
Entity Sequences (FASTA):
Recombinant Onconase/ranpirnase: MQDWLTFQKKHITNTRDVDC
DNILSTNLFHCKDKNTFIYS
RPEPVKAICKGIIASKNVLT
TSEFYLSDCNVTSRPCKYKL
KKSTNKFCVTCENQAPVHFV
GVGSC
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 470 |
| 15N chemical shifts | 223 |
| 1H chemical shifts | 825 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | (M-1,Q1,M23L)rOnc | 1 |
Entities:
Entity 1, (M-1,Q1,M23L)rOnc 105 residues - 11958 Da.
| 1 | MET | GLN | ASP | TRP | LEU | THR | PHE | GLN | LYS | LYS | ||||
| 2 | HIS | ILE | THR | ASN | THR | ARG | ASP | VAL | ASP | CYS | ||||
| 3 | ASP | ASN | ILE | LEU | SER | THR | ASN | LEU | PHE | HIS | ||||
| 4 | CYS | LYS | ASP | LYS | ASN | THR | PHE | ILE | TYR | SER | ||||
| 5 | ARG | PRO | GLU | PRO | VAL | LYS | ALA | ILE | CYS | LYS | ||||
| 6 | GLY | ILE | ILE | ALA | SER | LYS | ASN | VAL | LEU | THR | ||||
| 7 | THR | SER | GLU | PHE | TYR | LEU | SER | ASP | CYS | ASN | ||||
| 8 | VAL | THR | SER | ARG | PRO | CYS | LYS | TYR | LYS | LEU | ||||
| 9 | LYS | LYS | SER | THR | ASN | LYS | PHE | CYS | VAL | THR | ||||
| 10 | CYS | GLU | ASN | GLN | ALA | PRO | VAL | HIS | PHE | VAL | ||||
| 11 | GLY | VAL | GLY | SER | CYS |
Samples:
sample_1: Recombinant Onconase/ranpirnase, [U-15N; U-13C], 1.5 mM
sample_conditions_set_1: pH*: 4.1; temperature: 310 K
sample_conditions_set_2: pH*: 7.0; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | not available | not available |
| 2D 13C CT-HSQC | sample_1 | not available | not available |
| 3D CBCANH | sample_1 | not available | not available |
| 3D CBCA(CO)NH | sample_1 | not available | not available |
| 3D HBHA(CO)NH | sample_1 | not available | not available |
| 3D HNCO | sample_1 | not available | not available |
| 3D HN(CA)CO | sample_1 | not available | not available |
| 3D 15N-res. [1H,1H]-TOCSY (mixing time: 60.4 ms) | sample_1 | not available | not available |
| 3D HCCH-COSY | sample_1 | not available | not available |
| 3D HCCH-TOCSY (mixing time: 24.8 ms) | sample_1 | not available | not available |
| 3D 15N-res. NOESY-HSQC (mixing time 100 ms) | sample_1 | not available | not available |
| 3D 13C-res. NOESY-HSQC (mixing time 100 ms) | sample_1 | not available | not available |
| 2D 13C-filtered NOESY (mixing time 100 ms) | sample_1 | not available | not available |
| 2D 13C-filtered TOCSY | sample_1 | not available | not available |
Software:
XWINNMR - data processing
AURELIA - assignment
Sparky - assignment
NMR spectrometers:
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks