BMRB Entry 16192
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16192
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Title: NMR structure of the first qRRM of hnRNP F in complex with AGGGAU G-tract RNA PubMed: 20526337
Deposition date: 2009-03-02 Original release date: 2010-06-15
Authors: Allain, Frederic; Dominguez, Cyril
Citation: Dominguez, Cyril; Fisette, Jean-Francois; Chabot, Benoit; Allain, Frederic H-T. "Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs." Nat. Struct. Mol. Biol. 17, 853-861 (2010).
Assembly members:
entity_1, polymer, 6 residues, 1955.251 Da.
first qRRM of hnRNP F, polymer, 102 residues, 11475.048 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: AGGGAU
first qRRM of hnRNP F: MMLGPEGGEGFVVKLRGLPW
SCSVEDVQNFLSDCTIHDGA
AGVHFIYTREGRQSGEAFVE
LGSEDDVKMALKKDRESMGH
RYIEVFKSHRTEMDWVLKHS
GP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 258 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 685 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AGGGAU G-tract RNA | 1 |
| 2 | first qRRM of hnRNP F | 2 |
Entities:
Entity 1, AGGGAU G-tract RNA 6 residues - 1955.251 Da.
| 1 | A | G | G | G | A | U |
Entity 2, first qRRM of hnRNP F 102 residues - 11475.048 Da.
| 1 | MET | MET | LEU | GLY | PRO | GLU | GLY | GLY | GLU | GLY | ||||
| 2 | PHE | VAL | VAL | LYS | LEU | ARG | GLY | LEU | PRO | TRP | ||||
| 3 | SER | CYS | SER | VAL | GLU | ASP | VAL | GLN | ASN | PHE | ||||
| 4 | LEU | SER | ASP | CYS | THR | ILE | HIS | ASP | GLY | ALA | ||||
| 5 | ALA | GLY | VAL | HIS | PHE | ILE | TYR | THR | ARG | GLU | ||||
| 6 | GLY | ARG | GLN | SER | GLY | GLU | ALA | PHE | VAL | GLU | ||||
| 7 | LEU | GLY | SER | GLU | ASP | ASP | VAL | LYS | MET | ALA | ||||
| 8 | LEU | LYS | LYS | ASP | ARG | GLU | SER | MET | GLY | HIS | ||||
| 9 | ARG | TYR | ILE | GLU | VAL | PHE | LYS | SER | HIS | ARG | ||||
| 10 | THR | GLU | MET | ASP | TRP | VAL | LEU | LYS | HIS | SER | ||||
| 11 | GLY | PRO |
Samples:
sample_1: entity_11 – 1.5 mM; entity_2, [U-13C; U-15N], 1 – 1.5 mM; NACL 50 mM; Na2HPO4 20 mM
sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 303 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.113, Goddard - chemical shift assignment
CYANA v2.1, Herrmann, Guntert and Wuthrich - structure solution
AMBER v7.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts