BMRB Entry 7435
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR7435
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Title: HVS ORF57 8-120 backbone assignment, in complex with REF2-I 54-155. PubMed: 21253573
Deposition date: 2010-01-29 Original release date: 2011-01-25
Authors: Tunnicliffe, Richard; Golovanov, Alexander; Wilson, Stuart; Hautbergue, Guillaume
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).
Assembly members:
REF_54-155, polymer, 124 residues, 13596.237 Da.
ORF57_8-120, polymer, 135 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
ORF57_8-120: MASMTGGQQMGRDPGISSDD
DFDSSDSSSDEEESDTSPQI
MKSDVTMASPPSTPEPSLDV
SASTSNLKRERQRSPITWEH
QSPLSRVYRSPSPMRFGKRP
RISSNSTSRSCKTSWADRVR
EAAAQRRLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 104 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | REF_54-155 | 1 |
| 2 | ORF57_8-120 | 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, ORF57_8-120 135 residues - 4268.970 Da.
The construct contains the following non-ORF57 sequence at N-termini: MASMTGGQQMGRDP (assigned residue numbers -4 to 7) Plus the following at C-termini: LEHHHHHH (assigned residue numbers 121 to 128)
| 1 | MET | ALA | SER | MET | THR | GLY | GLY | GLN | GLN | MET | ||||
| 2 | GLY | ARG | ASP | PRO | GLY | ILE | SER | SER | ASP | ASP | ||||
| 3 | ASP | PHE | ASP | SER | SER | ASP | SER | SER | SER | ASP | ||||
| 4 | GLU | GLU | GLU | SER | ASP | THR | SER | PRO | GLN | ILE | ||||
| 5 | MET | LYS | SER | ASP | VAL | THR | MET | ALA | SER | PRO | ||||
| 6 | PRO | SER | THR | PRO | GLU | PRO | SER | LEU | ASP | VAL | ||||
| 7 | SER | ALA | SER | THR | SER | ASN | LEU | LYS | ARG | GLU | ||||
| 8 | ARG | GLN | ARG | SER | PRO | ILE | THR | TRP | GLU | HIS | ||||
| 9 | GLN | SER | PRO | LEU | SER | ARG | VAL | TYR | ARG | SER | ||||
| 10 | PRO | SER | PRO | MET | ARG | PHE | GLY | LYS | ARG | PRO | ||||
| 11 | ARG | ILE | SER | SER | ASN | SER | THR | SER | ARG | SER | ||||
| 12 | CYS | LYS | THR | SER | TRP | ALA | ASP | ARG | VAL | ARG | ||||
| 13 | GLU | ALA | ALA | ALA | GLN | ARG | ARG | LEU | GLU | HIS | ||||
| 14 | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: ORF57 8-120, [U-99% 13C; U-99% 15N], 1 ± 0.05 mM; REF 54-155 2 ± 0.05 mM; 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
sample_conditions_1: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 288 K
sample_conditions_2: ionic strength: 50 mM; pH: 6.2; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_2 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_2 |
Software:
SPARKY v2.1, Goddard - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance II+ 700 MHz
Related Database Links:
| BMRB | 16683 16697 17693 16698 |
| PDB | |
| EMBL | CAA45680 CAC84353 CAC84354 |
| GB | AAA46125 AAA66558 |
| PIR | WMBEHA |
| REF | NP_040259 |
| SP | P13199 |
| AlphaFold | P13199 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts