BMRB Entry 17663
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17663
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: HVS ORF57 56-140 backbone assignment PubMed: 21253573
Deposition date: 2011-05-25 Original release date: 2011-09-01
Authors: Tunnicliffe, Richard; Hautbergue, Guillaume; Wilson, Stuart; Golovanov, Alexander
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, .-. (2011).
Assembly members:
HVS_ORF57, polymer, 107 residues, Formula weight is not available
Natural source: Common Name: Herpesvirus saimiri Taxonomy ID: 10381 Superkingdom: Viruses Kingdom: not available Genus/species: Herpesvirus saimiri
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HVS_ORF57: MASMTGGQQMGRDPSTSNLK
RERQRSPITWEHQSPLSRVY
RSPSPMRFGKRPRISSNSTS
RSCKTSWADRVREAAAQRRP
SRPFRKPYSHPRNGPLRNGL
EHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 229 |
15N chemical shifts | 73 |
1H chemical shifts | 224 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ORF57 56-140 | 1 |
Entities:
Entity 1, ORF57 56-140 107 residues - Formula weight is not available
N-terminal sequence masmtggqqmgrdp and C-terminal sequence lehhhhhh are non-native from cloning
1 | MET | ALA | SER | MET | THR | GLY | GLY | GLN | GLN | MET | ||||
2 | GLY | ARG | ASP | PRO | SER | THR | SER | ASN | LEU | LYS | ||||
3 | ARG | GLU | ARG | GLN | ARG | SER | PRO | ILE | THR | TRP | ||||
4 | GLU | HIS | GLN | SER | PRO | LEU | SER | ARG | VAL | TYR | ||||
5 | ARG | SER | PRO | SER | PRO | MET | ARG | PHE | GLY | LYS | ||||
6 | ARG | PRO | ARG | ILE | SER | SER | ASN | SER | THR | SER | ||||
7 | ARG | SER | CYS | LYS | THR | SER | TRP | ALA | ASP | ARG | ||||
8 | VAL | ARG | GLU | ALA | ALA | ALA | GLN | ARG | ARG | PRO | ||||
9 | SER | ARG | PRO | PHE | ARG | LYS | PRO | TYR | SER | HIS | ||||
10 | PRO | ARG | ASN | GLY | PRO | LEU | ARG | ASN | GLY | LEU | ||||
11 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: HVS ORF57, [U-95% 13C; U-95% 15N], 1.0 ± 0.05 mM; H2O 90%; D2O 10%; NaCl 50 mM
sample_conditions_1: ionic strength: 0.05 M; 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_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 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 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.113, Goddard - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 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