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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/BMR19502
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Barraud, Pierre; Banerjee, Silpi; Mohamed, Weaam; Jantsch, Michael; Allain, Frederic H-T. "A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1." Proc. Natl. Acad. Sci. U.S.A. ., .-. (2014).
PubMed: 24753571
Assembly members:
dsRBD3, polymer, 113 residues, 10452.122 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 Vector: pET28a
Entity Sequences (FASTA):
dsRBD3: GSSHHHHHHSSGLVPRGSHM
MPNKVRKIGELVRYLNTNPV
GGLLEYARSHGFAAEFKLVD
QSGPPHEPKFVYQAKVGGRW
FPAVCAHSKKQGKQEAADAA
LRVLIGENEKAER
Data type | Count |
13C chemical shifts | 284 |
15N chemical shifts | 93 |
1H chemical shifts | 604 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | dsRBD3 | 1 |
Entity 1, dsRBD3 113 residues - 10452.122 Da.
1 | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | SER | ||||
2 | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | MET | ||||
3 | MET | PRO | ASN | LYS | VAL | ARG | LYS | ILE | GLY | GLU | ||||
4 | LEU | VAL | ARG | TYR | LEU | ASN | THR | ASN | PRO | VAL | ||||
5 | GLY | GLY | LEU | LEU | GLU | TYR | ALA | ARG | SER | HIS | ||||
6 | GLY | PHE | ALA | ALA | GLU | PHE | LYS | LEU | VAL | ASP | ||||
7 | GLN | SER | GLY | PRO | PRO | HIS | GLU | PRO | LYS | PHE | ||||
8 | VAL | TYR | GLN | ALA | LYS | VAL | GLY | GLY | ARG | TRP | ||||
9 | PHE | PRO | ALA | VAL | CYS | ALA | HIS | SER | LYS | LYS | ||||
10 | GLN | GLY | LYS | GLN | GLU | ALA | ALA | ASP | ALA | ALA | ||||
11 | LEU | ARG | VAL | LEU | ILE | GLY | GLU | ASN | GLU | LYS | ||||
12 | ALA | GLU | ARG |
13C-15N_H2O: dsRBD3, [U-99% 13C; U-99% 15N], 0.7 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%
13C-15N_D20: dsRBD3, [U-99% 13C; U-99% 15N], 0.7 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; D2O 100%
15N_H20: dsRBD3, [U-99% 15N], 0.7 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%
1H_D2O: dsRBD30.7 0.9 mM; sodium phosphate 20 mM; potassium chloride 100 mM; DTT 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 120 mM; pH: 7.0; pressure: 1 atm; temperature: 313.0 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 15N_H20 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | 13C-15N_H2O | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | 13C-15N_D20 | isotropic | sample_conditions_1 |
3D HNCA | 13C-15N_H2O | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 13C-15N_H2O | isotropic | sample_conditions_1 |
3D HNCACB | 13C-15N_H2O | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | 13C-15N_D20 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | 1H_D2O | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | 1H_D2O | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | 15N_H20 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | 13C-15N_H2O | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | 13C-15N_H2O | isotropic | sample_conditions_1 |
15N{1H}-HeteroNOE | 15N_H20 | isotropic | sample_conditions_1 |
long-range 2D 1H-15N HSQC | 15N_H20 | isotropic | sample_conditions_1 |
TOPSPIN v3.0, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
ATNOS, Herrmann, Guntert and Wuthrich - peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
ProcheckNMR, Laskowski and MacArthur - structure validation
CING, Nabuurs, Spronk, Krieger, Maassen, Vriend and Vuister - structure validation
PDB |
Download HSQC peak lists in one of the following formats:
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