Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19680
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Citation: Amrane, Samir; Rebora, Karine; Zniber, Ilyass; Dupuy, Denis; Mackereth, Cameron. "BACKBONE-INDEPENDENT NUCLEIC ACID BINDING BY SPLICING FACTOR SUP-12 REVEALS KEY ASPECTS OF MOLECULAR RECOGNITION" Nat. Commun. ., .-. (2014).
Assembly members:
ASD-1, polymer, 99 residues, Formula weight is not available
Natural source: Common Name: nematode Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETHis1a
Entity Sequences (FASTA):
ASD-1: GAMGPVAPNDRSTSSSSTDG
PRRLHVSNIPFKYREPDLTA
MFEKVGPVVDVEIIFNERGS
KGFGFVTMQNPDDADRARAE
FNGTTIEGRRVEVNLATQR
Data type | Count |
13C chemical shifts | 277 |
15N chemical shifts | 86 |
1H chemical shifts | 171 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | ASD-1 | 1 |
Entity 1, ASD-1 99 residues - Formula weight is not available
The N-terminal Gly-Ala-Met remains following removal of the His6-tag by TEV potease
1 | GLY | ALA | MET | GLY | PRO | VAL | ALA | PRO | ASN | ASP | ||||
2 | ARG | SER | THR | SER | SER | SER | SER | THR | ASP | GLY | ||||
3 | PRO | ARG | ARG | LEU | HIS | VAL | SER | ASN | ILE | PRO | ||||
4 | PHE | LYS | TYR | ARG | GLU | PRO | ASP | LEU | THR | ALA | ||||
5 | MET | PHE | GLU | LYS | VAL | GLY | PRO | VAL | VAL | ASP | ||||
6 | VAL | GLU | ILE | ILE | PHE | ASN | GLU | ARG | GLY | SER | ||||
7 | LYS | GLY | PHE | GLY | PHE | VAL | THR | MET | GLN | ASN | ||||
8 | PRO | ASP | ASP | ALA | ASP | ARG | ALA | ARG | ALA | GLU | ||||
9 | PHE | ASN | GLY | THR | THR | ILE | GLU | GLY | ARG | ARG | ||||
10 | VAL | GLU | VAL | ASN | LEU | ALA | THR | GLN | ARG |
sample_1: ASD-1, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O, [U-2H], 10%; H2O 10%
sample_2: ASD-1, [U-99% 15N], 3.28 mM; sodium phosphate 20 mM; sodium chloride 300 mM; D2O, [U-2H], 10%; H2O 10%
sample_conditions_1: ionic strength: 320 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
TOPSPIN v2.1, Bruker Biospin - collection, processing
NMRPipe v2007, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing, processing
SPARKY v3.113, Goddard - chemical shift assignment, data analysis, peak picking
UNP | G5EEW7 |
BMRB | 19609 19686 |
PDB | |
EMBL | CAA85276 CAD82915 CCU83325 |
GB | ABF22491 |
REF | NP_001293646 NP_497841 NP_871667 |
AlphaFold | G5EEW7 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks