BMRB Entry 27484
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27484
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Title: Backbone assignment of KSHV ORF57 68-178
Deposition date: 2018-05-15 Original release date: 2018-09-24
Authors: Tunnicliffe, Richard; Tian, Xiaochen; Storer, Joanna; Sandri-Goldin, Rozanne; Golovanov, Alexander
Citation: Tunnicliffe, Richard; Tian, Xiaochen; Storer, Joanna; Sandri-Goldin, Rozanne; Golovanov, Alexander. "Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIF" Sci. Rep. 8, 15005-15005 (2018).
Assembly members:
ORF57, polymer, 132 residues, Formula weight is not available
Natural source: Common Name: Human gammaherpesvirus 8 Taxonomy ID: 37296 Superkingdom: Viruses Kingdom: not available Genus/species: Rhadinovirus Human herpesvirus 8 type P
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-15b
Entity Sequences (FASTA):
ORF57: MGSSHHHHHHSSGLVPRGSH
MGRIPKKSQGRSQLRSEIQF
CSPLSRPRSPSPVNRYGKKI
KFGTAGQNTRPPPEKRPRRR
PRDRLQYGRTTRGGQCRAAP
KRATRRPQVNCQRQDDDVRQ
GVSDAVKKLRLP
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 93 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ORF57 68-178 | 1 |
Entities:
Entity 1, ORF57 68-178 132 residues - Formula weight is not available
N-terminal tag introdued in cloning is: MGSSHHHHHHSSGLVPRGSHM followed by KSHV ORF57 residues 68-178.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | MET | GLY | ARG | ILE | PRO | LYS | LYS | SER | GLN | GLY | ||||
| 4 | ARG | SER | GLN | LEU | ARG | SER | GLU | ILE | GLN | PHE | ||||
| 5 | CYS | SER | PRO | LEU | SER | ARG | PRO | ARG | SER | PRO | ||||
| 6 | SER | PRO | VAL | ASN | ARG | TYR | GLY | LYS | LYS | ILE | ||||
| 7 | LYS | PHE | GLY | THR | ALA | GLY | GLN | ASN | THR | ARG | ||||
| 8 | PRO | PRO | PRO | GLU | LYS | ARG | PRO | ARG | ARG | ARG | ||||
| 9 | PRO | ARG | ASP | ARG | LEU | GLN | TYR | GLY | ARG | THR | ||||
| 10 | THR | ARG | GLY | GLY | GLN | CYS | ARG | ALA | ALA | PRO | ||||
| 11 | LYS | ARG | ALA | THR | ARG | ARG | PRO | GLN | VAL | ASN | ||||
| 12 | CYS | GLN | ARG | GLN | ASP | ASP | ASP | VAL | ARG | GLN | ||||
| 13 | GLY | VAL | SER | ASP | ALA | VAL | LYS | LYS | LEU | ARG | ||||
| 14 | LEU | PRO |
Samples:
sample_1: ORF57, [U-100% 15N], 0.4 mM; sodium phosphate 20 mM; sodium chloride 50 mM; L-Arginine 50 mM; L-Glutamate 50 mM; EDTA 1 mM; TCEP 2 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.2; 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 |
Software:
TOPSPIN v3.2, Bruker Biospin - processing
SPARKY v3.12, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts