BMRB Entry 15439
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15439
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Title: URN1 FF domain yeast PubMed: 18536009
Deposition date: 2007-08-21 Original release date: 2008-06-26
Authors: Bonet, Roman; Ramirez-Espain, Ximena; Macias, Maria
Citation: Bonet, Roman; Ramirez-Espain, Ximena; Macias, Maria. "Solution structure of the yeast URN1 splicing factor FF domain: Comparative analysis of charge distributions in FF domain structures-FFs and SURPs, two domains with a similar fold" Proteins 73, 1001-1009 (2008).
Assembly members:
FF, polymer, 58 residues, 6868.629 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
FF: AMGDIDERNIFFELFDRYKL
DKFSTWSLQSKKIENDPDFY
KIRDDTVRESLFEEWCGE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 397 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 58 residues - 6868.629 Da.
| 1 | ALA | MET | GLY | ASP | ILE | ASP | GLU | ARG | ASN | ILE | ||||
| 2 | PHE | PHE | GLU | LEU | PHE | ASP | ARG | TYR | LYS | LEU | ||||
| 3 | ASP | LYS | PHE | SER | THR | TRP | SER | LEU | GLN | SER | ||||
| 4 | LYS | LYS | ILE | GLU | ASN | ASP | PRO | ASP | PHE | TYR | ||||
| 5 | LYS | ILE | ARG | ASP | ASP | THR | VAL | ARG | GLU | SER | ||||
| 6 | LEU | PHE | GLU | GLU | TRP | CYS | GLY | GLU |
Samples:
sample_1: FF 0.5 mM; sodium phosphate 20 mM; sodium chloride 130 mM; sodium azide 0.03%; D2O 10%; H2O 90%
sample2: FF, [U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 130 mM; sodium azide 0.03%; D2O 10%; H2O 90%
sample3: FF, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 130 mM; sodium azide 0.03%; D2O 10%; H2O 90%
sample_conditions_1: pH: 5.8; pressure: 1 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample3 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
CARA, Keller and Wuthrich - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz