BMRB Entry 17693
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17693
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Title: RRM domain of mRNA export adaptor REF2-I bound to HVS ORF57 peptide PubMed: 21253573
Deposition date: 2011-06-07 Original release date: 2012-06-11
Authors: Tunnicliffe, Richard; Hautbergue, G.; Kalra, P.; Wilson, S.; Golovanov, A.; Golova, A.
Citation: Tunnicliffe, Richard; Hautbergue, G.; Kalra, P.; Jackson, B.; Whitehouse, A.; Wilson, S.; Golovanov, A.. "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-e1001244 (2011).
Assembly members:
RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2, polymer, 124 residues, 13567.0128 Da.
52_KDA_IMMEDIATE-EARLY_PHOSPHOPROTEIN, polymer, 23 residues, 2504.8024 Da.
Natural source: Common Name: herpesvirus saimiri HVS Taxonomy ID: 10381 Superkingdom: Viruses Kingdom: not available Genus/species: Rhadinovirus Saimiriine herpesvirus 2
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2: MASMTGGQQMGRDPDKWQHD
LFDSGCGGGEGVETGAKLLV
SNLDFGVSDADIQELFAEFG
TLKKAAVDYDRSGRSLGTAD
VHFERRADALKAMKQYKGVP
LDGRPMDIQLVASQIDLEHH
HHHH
52_KDA_IMMEDIATE-EARLY_PHOSPHOPROTEIN: GPLGSSCKTSWADRVREAAA
QRR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 535 |
| 15N chemical shifts | 153 |
| 1H chemical shifts | 922 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RNA AND EXPORT FACTOR-BINDING PROTEIN 2 | 1 |
| 2 | 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN | 2 |
Entities:
Entity 1, RNA AND EXPORT FACTOR-BINDING PROTEIN 2 124 residues - 13567.0128 Da.
| 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, 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN 23 residues - 2504.8024 Da.
| 1 | GLY | PRO | LEU | GLY | SER | SER | CYS | LYS | THR | SER | ||||
| 2 | TRP | ALA | ASP | ARG | VAL | ARG | GLU | ALA | ALA | ALA | ||||
| 3 | GLN | ARG | ARG |
Samples:
sample_1: RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2, [U-99% 13C; U-99% 15N], 1 mM; 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN, [U-99% 13C; U-99% 15N], 3 mM; NaCl 50 mM
sample_2: RNA_AND_EXPORT_FACTOR-BINDING_PROTEIN_2, [U-99% 13C; U-99% 15N], 3 mM; 52 KDA IMMEDIATE-EARLY PHOSPHOPROTEIN, [U-99% 13C; U-99% 15N], 1 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 50.000 mM; pH: 6.200; pressure: 1.000 atm; temperature: 303.000 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HSQC | sample_1 | solution | sample_conditions_1 |
| HNCA | sample_1 | solution | sample_conditions_1 |
| CBCA(CO)NH | sample_1 | solution | sample_conditions_1 |
| HNCACB | sample_1 | solution | sample_conditions_1 |
| HNCO | sample_1 | solution | sample_conditions_1 |
| HN(CA)CO | sample_1 | solution | sample_conditions_1 |
| TOCSY-HSQC | sample_1 | solution | sample_conditions_1 |
| HBHA(CO)NH | sample_1 | solution | sample_conditions_1 |
| HCCH-TOCSY | sample_1 | solution | sample_conditions_1 |
| CCH-TOCSY | sample_1 | solution | sample_conditions_1 |
| NOESY-HSQC | sample_1 | solution | sample_conditions_1 |
| Filtered 13C-NOESY | sample_1 | solution | sample_conditions_1 |
| HSQC | sample_2 | solution | sample_conditions_1 |
| HNCA | sample_2 | solution | sample_conditions_1 |
| CBCA(CO)NH | sample_2 | solution | sample_conditions_1 |
| HNCACB | sample_2 | solution | sample_conditions_1 |
| HNCO | sample_2 | solution | sample_conditions_1 |
| TOCSY-HSQC | sample_2 | solution | sample_conditions_1 |
| HBHA(CO)NH | sample_2 | solution | sample_conditions_1 |
| NOESY-HSQC | sample_2 | solution | sample_conditions_1 |
| NOESY-HSQC HSQC | sample_1 | solution | sample_conditions_1 |
Software:
AutoDep v4.3, PDBe - collection
CYANA v2.1, P. Guntert et al. - chemical shift assignment
NMR spectrometers:
- Bruker DRX 600 MHz
- Varian Inova 800 MHz
Related Database Links:
| UNP | REFP2_MOUSE IE63_SHV21 |
| BMRB | 16683 16697 16698 17663 17664 7435 |
| PDB | |
| 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