BMRB Entry 4893
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4893
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
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Citation: Hsu, Chun-Hua; Liao, You-Di; Wu, Shih-Hsiung; Chen, Chinpan. "Letter to the Editor: 1H, 13C and 15N Resonance Assignments and Secondary
Structure of the Cytotoxic Protein RNase 4 from Bullfrog Rana catesbeiana Oocytes" J. Biomol. NMR 20, 93-94 (2001).
PubMed: 11430762
Assembly members:
rRC-RNase4[M(-1),Q1], polymer, 107 residues, 12217 Da.
Natural source: Common Name: bullfrog Taxonomy ID: 8400 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rana catesbeiana
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11d
Entity Sequences (FASTA):
rRC-RNase4[M(-1),Q1]: MQDWATFKKKHLTDTWDVDC
DNLMPTSLFDCKDKNTFIYS
LPGPVKALCRGVIFSADVLS
NSEFYLAECNVKPRKPCKYK
LKKSSNRICIRCEHELPVHF
AGVGICP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 494 |
| 15N chemical shifts | 111 |
| 1H chemical shifts | 766 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rRC-RNase4 | 1 |
Entities:
Entity 1, rRC-RNase4 107 residues - 12217 Da.
| 1 | MET | GLN | ASP | TRP | ALA | THR | PHE | LYS | LYS | LYS | ||||
| 2 | HIS | LEU | THR | ASP | THR | TRP | ASP | VAL | ASP | CYS | ||||
| 3 | ASP | ASN | LEU | MET | PRO | THR | SER | LEU | PHE | ASP | ||||
| 4 | CYS | LYS | ASP | LYS | ASN | THR | PHE | ILE | TYR | SER | ||||
| 5 | LEU | PRO | GLY | PRO | VAL | LYS | ALA | LEU | CYS | ARG | ||||
| 6 | GLY | VAL | ILE | PHE | SER | ALA | ASP | VAL | LEU | SER | ||||
| 7 | ASN | SER | GLU | PHE | TYR | LEU | ALA | GLU | CYS | ASN | ||||
| 8 | VAL | LYS | PRO | ARG | LYS | PRO | CYS | LYS | TYR | LYS | ||||
| 9 | LEU | LYS | LYS | SER | SER | ASN | ARG | ILE | CYS | ILE | ||||
| 10 | ARG | CYS | GLU | HIS | GLU | LEU | PRO | VAL | HIS | PHE | ||||
| 11 | ALA | GLY | VAL | GLY | ILE | CYS | PRO |
Samples:
sample_1: rRC-RNase4[M(-1),Q1], [U-15N; U-13C], 1.5 mM
cond-sample_1: pH: 3.5; temperature: 310 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | not available | not available | not available |
| 2D 1H-15N HSQC | not available | not available | not available |
| 3D CBCANH | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
| 3D HBHA(CO)NH | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| 3D HN(CA)CO | not available | not available | not available |
| 3D 15N NOESY-HSQC | not available | not available | not available |
| 3D 15N TOCSY-HSQC | not available | not available | not available |
| 3D HCCH-TOCSY | not available | not available | not available |
| 3D C(CO)NH | not available | not available | not available |
Software:
XWINNMR - data processing
AURELIA - 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