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PDB ID: 6snj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34427
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Jutzi, Daniel; Campagne, Sebastien; Schmidt, Ralf; Reber, Stefan; Mechtersheimer, Jonas; Gypas, Foivos; Schweingruber, Christoph; Colombo, Martino; von Schroetter, Christine; Loughlin, Fionna; Devoy, Anny; Hedlund, Eva; Zavolan, Mihaela; Allain, Frederic H-T; Ruepp, Marc-David. "Aberrant interaction of FUS with the U1 snRNA provides a molecular mechanism of FUS induced amyotrophic lateral sclerosis" Nat. Commun. 11, 6341-6341 (2020).
PubMed: 33311468
Assembly members:
entity_1, polymer, 131 residues, 14137.444 Da.
entity_2, polymer, 28 residues, 8954.375 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 BL21(DE3)
Entity Sequences (FASTA):
entity_1: GGFNKFGGPRDQGSRHDSEQ
DNSDNNTIFVQGLGENVTIE
SVADYFKQIGIIKTNKKTGQ
PMINLYTDRETGKLKGEATV
SFDDPPSAKAAIDWFDGKEF
SGNPIKVSFATRRADFNRGG
GNGRGGRGRGG
entity_2: GGGAUUUCCCCAAAUGUGGG
AAACUCCC
Data type | Count |
13C chemical shifts | 641 |
15N chemical shifts | 139 |
1H chemical shifts | 981 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
2 | entity_2 | 2 |
Entity 1, entity_1 131 residues - 14137.444 Da.
1 | GLY | GLY | PHE | ASN | LYS | PHE | GLY | GLY | PRO | ARG | ||||
2 | ASP | GLN | GLY | SER | ARG | HIS | ASP | SER | GLU | GLN | ||||
3 | ASP | ASN | SER | ASP | ASN | ASN | THR | ILE | PHE | VAL | ||||
4 | GLN | GLY | LEU | GLY | GLU | ASN | VAL | THR | ILE | GLU | ||||
5 | SER | VAL | ALA | ASP | TYR | PHE | LYS | GLN | ILE | GLY | ||||
6 | ILE | ILE | LYS | THR | ASN | LYS | LYS | THR | GLY | GLN | ||||
7 | PRO | MET | ILE | ASN | LEU | TYR | THR | ASP | ARG | GLU | ||||
8 | THR | GLY | LYS | LEU | LYS | GLY | GLU | ALA | THR | VAL | ||||
9 | SER | PHE | ASP | ASP | PRO | PRO | SER | ALA | LYS | ALA | ||||
10 | ALA | ILE | ASP | TRP | PHE | ASP | GLY | LYS | GLU | PHE | ||||
11 | SER | GLY | ASN | PRO | ILE | LYS | VAL | SER | PHE | ALA | ||||
12 | THR | ARG | ARG | ALA | ASP | PHE | ASN | ARG | GLY | GLY | ||||
13 | GLY | ASN | GLY | ARG | GLY | GLY | ARG | GLY | ARG | GLY | ||||
14 | GLY |
Entity 2, entity_2 28 residues - 8954.375 Da.
1 | G | G | G | A | U | U | U | C | C | C | ||||
2 | C | A | A | A | U | G | U | G | G | G | ||||
3 | A | A | A | C | U | C | C | C |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks