BMRB Entry 15403
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15403
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NMR-STAR v3 text file.
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Citation: Hartl, Maximilian; Wohrl, Birgitta; Schweimer, Kristian. "Sequence-specific (1)H, (13)C and (15)N resonance assignments and secondary structure of a truncated protease from Simian Foamy Virus" Biomol. NMR Assignments 1, 175-177 (2007).
PubMed: 19636858
Assembly members:
SFVmac_Pol_1-101_6His, polymer, 107 residues, Formula weight is not available
Natural source: Common Name: simian foamy virus Taxonomy ID: 11642 Superkingdom: Viruses Kingdom: not available Genus/species: Spumavirus simian foamy virus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28c
Entity Sequences (FASTA):
SFVmac_Pol_1-101_6His: MDPLQLLQPLEAEIKGTKLK
AHWDSGATITCVPEAFLEDE
RPIQTMLIKTIHGEKQQDVY
YLTFKVQGRKVEAEVLASPY
DYILLNPSDVPWLMKKPLQL
THHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 442 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 698 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SFVmac Pol 1-101 6His | 1 |
Entities:
Entity 1, SFVmac Pol 1-101 6His 107 residues - Formula weight is not available
| 1 | MET | ASP | PRO | LEU | GLN | LEU | LEU | GLN | PRO | LEU | ||||
| 2 | GLU | ALA | GLU | ILE | LYS | GLY | THR | LYS | LEU | LYS | ||||
| 3 | ALA | HIS | TRP | ASP | SER | GLY | ALA | THR | ILE | THR | ||||
| 4 | CYS | VAL | PRO | GLU | ALA | PHE | LEU | GLU | ASP | GLU | ||||
| 5 | ARG | PRO | ILE | GLN | THR | MET | LEU | ILE | LYS | THR | ||||
| 6 | ILE | HIS | GLY | GLU | LYS | GLN | GLN | ASP | VAL | TYR | ||||
| 7 | TYR | LEU | THR | PHE | LYS | VAL | GLN | GLY | ARG | LYS | ||||
| 8 | VAL | GLU | ALA | GLU | VAL | LEU | ALA | SER | PRO | TYR | ||||
| 9 | ASP | TYR | ILE | LEU | LEU | ASN | PRO | SER | ASP | VAL | ||||
| 10 | PRO | TRP | LEU | MET | LYS | LYS | PRO | LEU | GLN | LEU | ||||
| 11 | THR | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SFVmac Pol 1-101 6His, [U-100% 13C; U-100% 15N], 1 mM; phosphate buffer 7.4 50 mM; NaCl 100 mM; DTT mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| EMBL | CAA41394 |
| GB | AGM61336 |
| PIR | S18738 |
| REF | YP_001961122 |
| SP | P23074 |
| AlphaFold | P23074 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks