BMRB Entry 17574
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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/BMR17574
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Title: Structure of a yeast RNase III dsRBD complex with a non-canonical RNA substrate provides new insights into substrate recognition
Deposition date: 2011-04-06 Original release date: 2011-08-03
Authors: Wang, Zhonghua; Hartman, Elon; Roy, Kevin; Chanfreau, Guillaume; Feigon, Juli
Citation: Wang, Zhonghua; Hartman, Elon; Roy, Kevin; Chanfreau, Guillaume; Feigon, Juli. "Structure of a yeast RNase III dsRBD complex with a non-canonical RNA substrate provides new insights into substrate recognition" Not known ., .-..
Assembly members:
yeast RNase III dsRBD, polymer, 90 residues, 9822.442 Da.
non-canonical RNA substrate, polymer, 32 residues, Formula weight is not available
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):
yeast RNase III dsRBD: GSLDMNAKRQLYSLIGYASL
RLHYVTVKKPTAVDPNSIVE
CRVGDGTVLGTGVGRNIKIA
GIRAAENALRDKKMLDFYAK
QRAAIPRSES
non-canonical RNA substrate: GGGAUACCAUGUUCAAGUGA
ACGUGGUAUCUC
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 326 |
15N chemical shifts | 87 |
1H chemical shifts | 547 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | yeast RNase III dsRBD | 1 |
2 | non-canonical RNA substrate | 2 |
Entities:
Entity 1, yeast RNase III dsRBD 90 residues - 9822.442 Da.
1 | GLY | SER | LEU | ASP | MET | ASN | ALA | LYS | ARG | GLN | |
2 | LEU | TYR | SER | LEU | ILE | GLY | TYR | ALA | SER | LEU | |
3 | ARG | LEU | HIS | TYR | VAL | THR | VAL | LYS | LYS | PRO | |
4 | THR | ALA | VAL | ASP | PRO | ASN | SER | ILE | VAL | GLU | |
5 | CYS | ARG | VAL | GLY | ASP | GLY | THR | VAL | LEU | GLY | |
6 | THR | GLY | VAL | GLY | ARG | ASN | ILE | LYS | ILE | ALA | |
7 | GLY | ILE | ARG | ALA | ALA | GLU | ASN | ALA | LEU | ARG | |
8 | ASP | LYS | LYS | MET | LEU | ASP | PHE | TYR | ALA | LYS | |
9 | GLN | ARG | ALA | ALA | ILE | PRO | ARG | SER | GLU | SER |
Entity 2, non-canonical RNA substrate 32 residues - Formula weight is not available
1 | G | G | G | A | U | A | C | C | A | U | ||||
2 | G | U | U | C | A | A | G | U | G | A | ||||
3 | A | C | G | U | G | G | U | A | U | C | ||||
4 | U | C |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.8 1 mM; entity_21 2 mM; NaCl 150 mM; phosphate buffer 20 mM
sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 1 mM; entity_21 2 mM; NaCl 150 mM; phosphate buffer 20 mM
sample_3: entity_10.8 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 2 mM; NaCl 150 mM; phosphate buffer 20 mM
sample_4: entity_10.8 1 mM; entity_2, [U-100% 13C; U-100% 15N], 1 2 mM; NaCl 150 mM; phosphate buffer 20 mM
sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_3 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H COSY | sample_4 | isotropic | sample_conditions_1 |
2D FILTERED/EDITED NOESY | sample_4 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC IPAP | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.24, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMRView v5.2.2, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - data analysis
TOPSPIN v2.0, Bruker Biospin - collection
xwinnmr, Bruker Biospin - collection
ProcheckNMR, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
BMRB | 18534 18535 |
PDB | |
DBJ | GAA25690 |
EMBL | CAA90210 CAY82070 |
GB | AAB04172 AHY76694 AJP40933 AJS62105 AJS62540 |
REF | NP_013966 |
SP | Q02555 |
TPG | DAA10139 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
SPARKY: Backbone
or all simulated shifts