BMRB Entry 15672
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15672
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kyere, Sampson; Joseph, Prem Raj; Summers, Michael. "The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct" PLoS. ONE. 3, 1902-1902 (2008).
PubMed: 18382677
Assembly members:
MMLV_p12CAN_protein, polymer, 224 residues, 24630.2 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pNCA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 156 |
| 15N chemical shifts | 158 |
| 1H chemical shifts | 158 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
Entities:
Entity 1, subunit 1 224 residues - 24630.2 Da.
Residues 217-224 represent a non-native affinity tag.
| 1 | PRO | ALA | LEU | THR | PRO | SER | LEU | GLY | ALA | LYS | ||||
| 2 | PRO | LYS | PRO | GLN | VAL | LEU | SER | ASP | SER | GLY | ||||
| 3 | GLY | PRO | LEU | ILE | ASP | LEU | LEU | THR | GLU | ASP | ||||
| 4 | PRO | PRO | PRO | TYR | ARG | ASP | PRO | ARG | PRO | PRO | ||||
| 5 | PRO | SER | ASP | ARG | ASP | GLY | ASN | GLY | GLY | GLU | ||||
| 6 | ALA | THR | PRO | ALA | GLY | GLU | ALA | PRO | ASP | PRO | ||||
| 7 | SER | PRO | MET | ALA | SER | ARG | LEU | ARG | GLY | ARG | ||||
| 8 | ARG | GLU | PRO | PRO | VAL | ALA | ASP | SER | THR | THR | ||||
| 9 | SER | GLN | ALA | PHE | PRO | LEU | ARG | ALA | GLY | GLY | ||||
| 10 | ASN | GLY | GLN | LEU | GLN | TYR | TRP | PRO | PHE | SER | ||||
| 11 | SER | SER | ASP | LEU | TYR | ASN | TRP | LYS | ASN | ASN | ||||
| 12 | ASN | PRO | SER | PHE | SER | GLU | ASP | PRO | GLY | LYS | ||||
| 13 | LEU | THR | ALA | LEU | ILE | GLU | SER | VAL | LEU | ILE | ||||
| 14 | THR | HIS | GLN | PRO | THR | TRP | ASP | ASP | CYS | GLN | ||||
| 15 | GLN | LEU | LEU | GLY | THR | LEU | LEU | THR | GLY | GLU | ||||
| 16 | GLU | LYS | GLN | ARG | VAL | LEU | LEU | GLU | ALA | ARG | ||||
| 17 | LYS | ALA | VAL | ARG | GLY | ASP | ASP | GLY | ARG | PRO | ||||
| 18 | THR | GLN | LEU | PRO | ASN | GLU | VAL | ASP | ALA | ALA | ||||
| 19 | PHE | PRO | LEU | GLU | ARG | PRO | ASP | TRP | ASP | TYR | ||||
| 20 | THR | THR | GLN | ALA | GLY | ARG | ASN | HIS | LEU | VAL | ||||
| 21 | HIS | TYR | ARG | GLN | LEU | LEU | LEU | ALA | GLY | LEU | ||||
| 22 | GLN | ASN | ALA | GLY | ARG | SER | HIS | HIS | HIS | HIS | ||||
| 23 | HIS | HIS | HIS | HIS |
Samples:
sample_1: MMLV p12CAN protein, [U-99% 13C; U-99% 15N], 1 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - data analysis, peak picking
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker AMX 600 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks