BMRB Entry 19680
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19680
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Title: ASD-1 RRM domain
Deposition date: 2013-12-13 Original release date: 2014-08-29
Authors: Amrane, Samir; Mackereth, Cameron
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
Entity Sequences (FASTA):
ASD-1: GAMGPVAPNDRSTSSSSTDG
PRRLHVSNIPFKYREPDLTA
MFEKVGPVVDVEIIFNERGS
KGFGFVTMQNPDDADRARAE
FNGTTIEGRRVEVNLATQR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 277 |
| 15N chemical shifts | 86 |
| 1H chemical shifts | 171 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ASD-1 | 1 |
Entities:
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 |
Samples:
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
Experiments:
| 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 |
Software:
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
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz
Related Database Links:
| UNP | G5EEW7 |
| BMRB | 19609 19686 |
| PDB | |
| EMBL | CAA85276 CAD82915 CCU83325 |
| GB | ABF22491 |
| REF | NP_001293646 NP_497841 NP_871667 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts