BMRB Entry 25970
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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/BMR25970
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Title: NMR structure of the Acidic domain of SYNCRIP (24-140) PubMed: 27081926
Deposition date: 2016-02-02 Original release date: 2016-05-31
Authors: Serrano, Pedro; Wuthrich, Kurt; Beuck, Christine
Citation: Beuck, Christine; Williamson, James; Wuthrich, Kurt; Serrano, Pedro. "The acidic domain is a unique structural feature of the splicing factor SYNCRIP" Protein Sci. 25, 1545-1550 (2016).
Assembly members:
entity, polymer, 118 residues, 12932.589 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
Entity Sequences (FASTA):
entity: GSENFQTLLDAGLPQKVAEK
LDEIYVAGLVAHSDLDERAI
EALKEFNEDGALAVLQQFKD
SDLSHVQNKSAFLCGVMKTY
RQREKQGTKVADSSKGPDEA
KIKALLERTGYTLDVTTG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 478 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 777 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 118 residues - 12932.589 Da.
| 1 | GLY | SER | GLU | ASN | PHE | GLN | THR | LEU | LEU | ASP | ||||
| 2 | ALA | GLY | LEU | PRO | GLN | LYS | VAL | ALA | GLU | LYS | ||||
| 3 | LEU | ASP | GLU | ILE | TYR | VAL | ALA | GLY | LEU | VAL | ||||
| 4 | ALA | HIS | SER | ASP | LEU | ASP | GLU | ARG | ALA | ILE | ||||
| 5 | GLU | ALA | LEU | LYS | GLU | PHE | ASN | GLU | ASP | GLY | ||||
| 6 | ALA | LEU | ALA | VAL | LEU | GLN | GLN | PHE | LYS | ASP | ||||
| 7 | SER | ASP | LEU | SER | HIS | VAL | GLN | ASN | LYS | SER | ||||
| 8 | ALA | PHE | LEU | CYS | GLY | VAL | MET | LYS | THR | TYR | ||||
| 9 | ARG | GLN | ARG | GLU | LYS | GLN | GLY | THR | LYS | VAL | ||||
| 10 | ALA | ASP | SER | SER | LYS | GLY | PRO | ASP | GLU | ALA | ||||
| 11 | LYS | ILE | LYS | ALA | LEU | LEU | GLU | ARG | THR | GLY | ||||
| 12 | TYR | THR | LEU | ASP | VAL | THR | THR | GLY |
Samples:
sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM
sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
DYANA, G??ntert P. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts