BMRB Entry 16194
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16194
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Title: Structure of the third qRRM domain of hnRNP F in complex with a 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. "Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs." Nat. Struct. Mol. Biol. 17, 853-861 (2010).
Assembly members:
AGGGAU G-tract RNA, polymer, 6 residues, 1955.251 Da.
third qRRM of hnRNP F, polymer, 105 residues, 11508.767 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):
AGGGAU G-tract RNA: AGGGAU
third qRRM of hnRNP F: GDSEFTVQSTTGHCVHMRGL
PYKATENDIYNFFSPLNPVR
VHIEIGPDGRVTGEADVEFA
THEEAVAAMSKDRANMQHRY
IELFLNSTTGASNGAYSSQV
MQGMG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 283 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 700 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AGGGAU G-tract RNA | 1 |
| 2 | third 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, third qRRM of hnRNP F 105 residues - 11508.767 Da.
| 1 | GLY | ASP | SER | GLU | PHE | THR | VAL | GLN | SER | THR | ||||
| 2 | THR | GLY | HIS | CYS | VAL | HIS | MET | ARG | GLY | LEU | ||||
| 3 | PRO | TYR | LYS | ALA | THR | GLU | ASN | ASP | ILE | TYR | ||||
| 4 | ASN | PHE | PHE | SER | PRO | LEU | ASN | PRO | VAL | ARG | ||||
| 5 | VAL | HIS | ILE | GLU | ILE | GLY | PRO | ASP | GLY | ARG | ||||
| 6 | VAL | THR | GLY | GLU | ALA | ASP | VAL | GLU | PHE | ALA | ||||
| 7 | THR | HIS | GLU | GLU | ALA | VAL | ALA | ALA | MET | SER | ||||
| 8 | LYS | ASP | ARG | ALA | ASN | MET | GLN | HIS | ARG | TYR | ||||
| 9 | ILE | GLU | LEU | PHE | LEU | ASN | SER | THR | THR | GLY | ||||
| 10 | ALA | SER | ASN | GLY | ALA | TYR | SER | SER | GLN | VAL | ||||
| 11 | MET | GLN | GLY | MET | GLY |
Samples:
sample_1: entity_11 – 1.5 mM; entity_2, [U-13C; U-15N], 1 – 1.5 mM; NaH2PO4 20 mM; NaCl 50 mM
sample_conditions_1: ionic strength: 70 mM; pH: 7.0; pressure: 1 atm; temperature: 293 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, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
- 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