BMRB Entry 18292
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18292
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Title: NMR structure of the RNA binding motif 39 (RBM39) from Mus musculus
Deposition date: 2012-02-23 Original release date: 2012-03-22
Authors: Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt
Citation: Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the RNA binding motif 39 (RBM39) from Mus musculus" Not known ., .-..
Assembly members:
entity, polymer, 113 residues, 12516.306 Da.
Natural source: Common Name: House mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: VQPLATQCFQLSNMFNPQTE
EEVGWDTEIKDDVIEECNKH
GGVIHIYVDKNSAQGNVYVK
CPSIAAAIAAVNALHGRWFA
GKMITAAYVPLPTYHNLFPD
SMTATQLLVPSRR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 476 |
15N chemical shifts | 120 |
1H chemical shifts | 756 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RBM39 | 1 |
Entities:
Entity 1, RBM39 113 residues - 12516.306 Da.
1 | VAL | GLN | PRO | LEU | ALA | THR | GLN | CYS | PHE | GLN | ||||
2 | LEU | SER | ASN | MET | PHE | ASN | PRO | GLN | THR | GLU | ||||
3 | GLU | GLU | VAL | GLY | TRP | ASP | THR | GLU | ILE | LYS | ||||
4 | ASP | ASP | VAL | ILE | GLU | GLU | CYS | ASN | LYS | HIS | ||||
5 | GLY | GLY | VAL | ILE | HIS | ILE | TYR | VAL | ASP | LYS | ||||
6 | ASN | SER | ALA | GLN | GLY | ASN | VAL | TYR | VAL | LYS | ||||
7 | CYS | PRO | SER | ILE | ALA | ALA | ALA | ILE | ALA | ALA | ||||
8 | VAL | ASN | ALA | LEU | HIS | GLY | ARG | TRP | PHE | ALA | ||||
9 | GLY | LYS | MET | ILE | THR | ALA | ALA | TYR | VAL | PRO | ||||
10 | LEU | PRO | THR | TYR | HIS | ASN | LEU | PHE | PRO | ASP | ||||
11 | SER | MET | THR | ALA | THR | GLN | LEU | LEU | VAL | PRO | ||||
12 | SER | ARG | ARG |
Samples:
sample_1: RBM39, [U-95% 13C; U-95% 15N], 1.2 mM; sodium azide 4.5 mM; sodium chloride 50 mM; sodium phosphate 25 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.083 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
4D APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
5D APSY CBCACONH | sample_1 | isotropic | sample_conditions_1 |
5D APSY HACACONH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection, data analysis, processing
UNIO, Unio Herrmann Wuthrich - chemical shift assignment, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
PDB | |
DBJ | BAE22009 BAE22477 BAE27657 BAE32977 BAG54289 |
EMBL | CAD97833 CAE45833 CAE45890 CAH18281 CAH90627 |
GB | AAA16346 AAA16347 AAH04000 AAH30493 AAH82607 |
REF | NP_001013225 NP_001125339 NP_001162566 NP_001164806 NP_001193433 |
SP | Q14498 Q5RC80 Q8VH51 |
TPG | DAA23046 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts