BMRB Entry 16683
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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/BMR16683
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Tunnicliffe, Richard; Hautbergue, Guillaume; Kalra, Priti; Jackson, Brian; Whitehouse, Adrian; Wilson, Stuart; Golovanov, Alexander. "Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57." PLoS Pathog. 7, e1001244-. (2011).
PubMed: 21253573
Assembly members:
REF_54-155, polymer, 124 residues, 13596.237 Da.
ICP27_103-138, polymer, 40 residues, 4268.970 Da.
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24b
Entity Sequences (FASTA):
REF_54-155: MASMTGGQQMGRDPDKWQHD
LFDSGCGGGEGVETGAKLLV
SNLDFGVSDADIQELFAEFG
TLKKAAVDYDRSGRSLGTAD
VHFERRADALKAMKQYKGVP
LDGRPMDIQLVASQIDLEHH
HHHH
ICP27_103-138: GPLGSVWSRLGARRPSCSPE
RHGGKVARLQPPPTKAQPAR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 627 |
| 15N chemical shifts | 159 |
| 1H chemical shifts | 1049 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | REF_54-155 | 1 |
| 2 | ICP27_103-138 | 2 |
Entities:
Entity 1, REF_54-155 124 residues - 13596.237 Da.
Construct contains the following non-REF sequences: N-terminal T7 tag: MASMTGGQQMGRDP (assigned residue numbers 40-53) C-terminal His tag: LEHHHHHH (assigned residue numbers 156-163)
| 1 | MET | ALA | SER | MET | THR | GLY | GLY | GLN | GLN | MET | ||||
| 2 | GLY | ARG | ASP | PRO | ASP | LYS | TRP | GLN | HIS | ASP | ||||
| 3 | LEU | PHE | ASP | SER | GLY | CYS | GLY | GLY | GLY | GLU | ||||
| 4 | GLY | VAL | GLU | THR | GLY | ALA | LYS | LEU | LEU | VAL | ||||
| 5 | SER | ASN | LEU | ASP | PHE | GLY | VAL | SER | ASP | ALA | ||||
| 6 | ASP | ILE | GLN | GLU | LEU | PHE | ALA | GLU | PHE | GLY | ||||
| 7 | THR | LEU | LYS | LYS | ALA | ALA | VAL | ASP | TYR | ASP | ||||
| 8 | ARG | SER | GLY | ARG | SER | LEU | GLY | THR | ALA | ASP | ||||
| 9 | VAL | HIS | PHE | GLU | ARG | ARG | ALA | ASP | ALA | LEU | ||||
| 10 | LYS | ALA | MET | LYS | GLN | TYR | LYS | GLY | VAL | PRO | ||||
| 11 | LEU | ASP | GLY | ARG | PRO | MET | ASP | ILE | GLN | LEU | ||||
| 12 | VAL | ALA | SER | GLN | ILE | ASP | LEU | GLU | HIS | HIS | ||||
| 13 | HIS | HIS | HIS | HIS |
Entity 2, ICP27_103-138 40 residues - 4268.970 Da.
The construct contains the following non-ICP27 sequence remaining from protease cleavage site at N-termini: GPLG (assigned residue numbers 99-102)
| 1 | GLY | PRO | LEU | GLY | SER | VAL | TRP | SER | ARG | LEU | |
| 2 | GLY | ALA | ARG | ARG | PRO | SER | CYS | SER | PRO | GLU | |
| 3 | ARG | HIS | GLY | GLY | LYS | VAL | ALA | ARG | LEU | GLN | |
| 4 | PRO | PRO | PRO | THR | LYS | ALA | GLN | PRO | ALA | ARG |
Samples:
sample_1: REF 54-155, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; ICP27 103-138 2 ± 0.05 mM; Na phosphate buffer 20 mM; NaCl 50 mM; L-Arg 50 mM; L-Glu 50 mM; 2-mercaptoethanol 50 mM; DTT 10 mM; EDTA 10 mM; H2O 90%; D2O 10%
sample_2: ICP27 103-138, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; REF 54-155 2 ± 0.05 mM; Na phosphate buffer 20 mM; NaCl 50 mM; L-Arg 50 mM; L-Glu 50 mM; 2-mercaptoethanol 50 mM; DTT 10 mM; EDTA 10 mM; H2O 90%; D2O 10%
sample_conditions: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | isotropic | sample_conditions |
| 3D 15N-separated NOESY | sample_1 | isotropic | sample_conditions |
| filtered 13C-NOESY | sample_1 | isotropic | sample_conditions |
| filtered 13C-NOESY | sample_2 | isotropic | sample_conditions |
| 3D 13C-separated NOESY | sample_2 | isotropic | sample_conditions |
| 3D 15N-separated NOESY | sample_2 | isotropic | sample_conditions |
| 3D Standard triple-resonance | sample_1 | isotropic | sample_conditions |
| 3d Standard triple-resonance | sample_2 | isotropic | sample_conditions |
Software:
CYANA v2.1, P.GUNTERT ET AL. - structure solution
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance II+ 700 MHz
- Varian INOVA 800 MHz
Related Database Links:
| BMRB | 16697 17693 16696 |
| PDB | |
| DBJ | BAE44978 BAE44979 BAE44980 BAE44981 BAE44982 |
| EMBL | CAA32290 |
| GB | AAF43147 ACM62278 ACU57136 ADD60047 ADD60124 |
| REF | NP_044657 |
| SP | P10238 P36295 |
| AlphaFold | P10238 P36295 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks