BMRB Entry 16193
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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/BMR16193
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Title: Structure of the second 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.
second qRRM of hnRNP F, polymer, 92 residues, 10228.562 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
second qRRM of hnRNP F: NSADSANDGFVRLRGLPFGC
TKEEIVQFFSGLEIVPNGIT
LPVDPEGKITGEAFVQFASQ
ELAEKALGKHKERIGHRYIE
VFKSSQEEVRSY
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 357 |
15N chemical shifts | 97 |
1H chemical shifts | 680 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | AGGGAU G-tract RNA | 1 |
2 | second 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, second qRRM of hnRNP F 92 residues - 10228.562 Da.
1 | ASN | SER | ALA | ASP | SER | ALA | ASN | ASP | GLY | PHE | ||||
2 | VAL | ARG | LEU | ARG | GLY | LEU | PRO | PHE | GLY | CYS | ||||
3 | THR | LYS | GLU | GLU | ILE | VAL | GLN | PHE | PHE | SER | ||||
4 | GLY | LEU | GLU | ILE | VAL | PRO | ASN | GLY | ILE | THR | ||||
5 | LEU | PRO | VAL | ASP | PRO | GLU | GLY | LYS | ILE | THR | ||||
6 | GLY | GLU | ALA | PHE | VAL | GLN | PHE | ALA | SER | GLN | ||||
7 | GLU | LEU | ALA | GLU | LYS | ALA | LEU | GLY | LYS | HIS | ||||
8 | LYS | GLU | ARG | ILE | GLY | HIS | ARG | TYR | ILE | GLU | ||||
9 | VAL | PHE | LYS | SER | SER | GLN | GLU | GLU | VAL | ARG | ||||
10 | SER | TYR |
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: 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 500 MHz
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 900 MHz
Related Database Links:
PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts