BMRB Entry 19854
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19854
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Title: Structural Characterization of the Mengovirus Leader Protein Bound to Ran GTPase by Nuclear Magnetic Resonance
Deposition date: 2014-03-15 Original release date: 2014-10-07
Authors: Bacot-Davis, Valjean; Palmenberg, Ann; Cornilescu, Claudia; Markley, John
Citation: Bacot-Davis, Valjean; Ciomperlik, J.; Basta, H.; Cornilescu, Claudia; Palmenberg, Ann. "Solution Structures of Mengovirus Leader Protein, its Phosphorylated Derivatives, and in Complex with Nuclear Transport Protein, RanGTPase" Proc. Nat. Acad. Sci, U.S.A. ., .-. (2014).
Assembly members:
entity, polymer, 216 residues, 24456.295 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MAAQGEPQVQFKLVLVGDGG
TGKTTFVKRHLTGEFEKKYV
ATLGVEVHPLVFHTNRGPIK
FNVWDTAGQEKFGGLRDGYY
IQAQCAIIMFDVTSRVTYKN
VPNWHRDLVRVCENIPIVLC
GNKVDIKDRKVKAKSIVFHR
KKNLQYYDISAKSNYNFEKP
FLWLARKLIGDPNLEFVAMP
ALAPPEVVMDPALAAQYEHD
LEVAQTTALPDEDDDL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 899 |
| 15N chemical shifts | 294 |
| 1H chemical shifts | 1438 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 216 residues - 24456.295 Da.
| 1 | MET | ALA | ALA | GLN | GLY | GLU | PRO | GLN | VAL | GLN | ||||
| 2 | PHE | LYS | LEU | VAL | LEU | VAL | GLY | ASP | GLY | GLY | ||||
| 3 | THR | GLY | LYS | THR | THR | PHE | VAL | LYS | ARG | HIS | ||||
| 4 | LEU | THR | GLY | GLU | PHE | GLU | LYS | LYS | TYR | VAL | ||||
| 5 | ALA | THR | LEU | GLY | VAL | GLU | VAL | HIS | PRO | LEU | ||||
| 6 | VAL | PHE | HIS | THR | ASN | ARG | GLY | PRO | ILE | LYS | ||||
| 7 | PHE | ASN | VAL | TRP | ASP | THR | ALA | GLY | GLN | GLU | ||||
| 8 | LYS | PHE | GLY | GLY | LEU | ARG | ASP | GLY | TYR | TYR | ||||
| 9 | ILE | GLN | ALA | GLN | CYS | ALA | ILE | ILE | MET | PHE | ||||
| 10 | ASP | VAL | THR | SER | ARG | VAL | THR | TYR | LYS | ASN | ||||
| 11 | VAL | PRO | ASN | TRP | HIS | ARG | ASP | LEU | VAL | ARG | ||||
| 12 | VAL | CYS | GLU | ASN | ILE | PRO | ILE | VAL | LEU | CYS | ||||
| 13 | GLY | ASN | LYS | VAL | ASP | ILE | LYS | ASP | ARG | LYS | ||||
| 14 | VAL | LYS | ALA | LYS | SER | ILE | VAL | PHE | HIS | ARG | ||||
| 15 | LYS | LYS | ASN | LEU | GLN | TYR | TYR | ASP | ILE | SER | ||||
| 16 | ALA | LYS | SER | ASN | TYR | ASN | PHE | GLU | LYS | PRO | ||||
| 17 | PHE | LEU | TRP | LEU | ALA | ARG | LYS | LEU | ILE | GLY | ||||
| 18 | ASP | PRO | ASN | LEU | GLU | PHE | VAL | ALA | MET | PRO | ||||
| 19 | ALA | LEU | ALA | PRO | PRO | GLU | VAL | VAL | MET | ASP | ||||
| 20 | PRO | ALA | LEU | ALA | ALA | GLN | TYR | GLU | HIS | ASP | ||||
| 21 | LEU | GLU | VAL | ALA | GLN | THR | THR | ALA | LEU | PRO | ||||
| 22 | ASP | GLU | ASP | ASP | ASP | LEU |
Samples:
sample_1: RAN GTPASE, [U-100% 13C; U-100% 15N], 0.5 mM; L MENGO 0.5 mM; HEPES 20 mM; potassium chloride 100 mM; magnesium chloride 2 mM; DTT 2 mM; sodium azide 0.04%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 102 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 31-P | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
SPARTA+, Shen and Bax - geometry optimization
SPARKY, Goddard - peak picking
CARA, Kurt W. Thrich, Swiss Federal Institute of Technology ETH - peak picking
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 19852 |
| PDB | |
| DBJ | BAA89696 BAB27034 BAB27105 BAB93486 BAC36040 |
| EMBL | CAA10191 CAA47355 CAA77980 CAG29343 CAH92646 |
| GB | AAA36546 AAA64247 AAB24940 AAB50841 AAC05840 |
| PRF | 1814339A |
| REF | NP_001004829 NP_001029877 NP_001080182 NP_001126549 NP_001128547 |
| SP | P42558 P52301 P62825 P62826 P62827 |
| TPG | DAA20795 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts