BMRB Entry 16698
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16698
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Title: HVS ORF57 8-120 backbone assignment 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:
ORF57_8-120, polymer, 135 residues, 4268.970 Da.
Natural source: Common Name: Human herpesvirus 1 Taxonomy ID: 10298 Superkingdom: Viruses Kingdom: not available Genus/species: Simplexvirus Human herpesvirus 1
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
ORF57_8-120: MASMTGGQQMGRDPGISSDD
DFDSSDSSSDEEESDTSPQI
MKSDVTMASPPSTPEPSPDV
SASTSNLKRERQRSPITWEH
QSPLSRVYRSPSPMRFGKRP
RISSNSTSRSCKTSWADRVR
EAAAQRRLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 361 |
15N chemical shifts | 229 |
1H chemical shifts | 515 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ORF57_8-120 | 1 |
Entities:
Entity 1, 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 | PRO | 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; 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 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
2D CON | sample_1 | isotropic | sample_conditions_1 |
2D CaCO | sample_1 | isotropic | sample_conditions_1 |
2D CbCaCO | sample_1 | isotropic | sample_conditions_1 |
2D CbCaCO(N) | sample_1 | isotropic | sample_conditions_1 |
3D CbCaCO(N) | sample_1 | isotropic | sample_conditions_1 |
3D CbCaNCO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v2.1, Goddard - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance II+ 700 MHz
Related Database Links:
EMBL | CAA45680 CAC84353 CAC84354 |
GB | AAA46125 AAA66558 |
PIR | WMBEHA |
REF | NP_040259 |
SP | P13199 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts