BMRB Entry 16230
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16230
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Title: Solution Structure of Yeast Prp24-RRM2 Bound to a Fragment of U6 RNA PubMed: 19693704
Deposition date: 2009-03-27 Original release date: 2009-09-04
Authors: Martin-Tumasz, Stephen; Butcher, Samuel
Citation: Martin-Tumasz, Stephen; Butcher, Samuel. "(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA." Biomol NMR Assign 3, 227-230 (2009).
Assembly members:
Prp24-RRM2, polymer, 92 residues, 10012.586 Da.
AGAGAU, polymer, 6 residues, 1826.235 Da.
Natural source: Common Name: yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Prp24-RRM2: MTECTLWMTNFPPSYTQRNI
RDLLQDINVVALSIRLPSLR
FNTSRRFAYIDVTSKEDARY
CVEKLNGLKIEGYTLVTKVS
NPLELEHHHHHH
AGAGAU: AGAGAU
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 367 |
15N chemical shifts | 91 |
1H chemical shifts | 642 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Prp24-RRM2 | 1 |
2 | AGAGAU | 2 |
Entities:
Entity 1, Prp24-RRM2 92 residues - 10012.586 Da.
Final 8 residues are non-native due to 6x His tag
1 | MET | THR | GLU | CYS | THR | LEU | TRP | MET | THR | ASN | ||||
2 | PHE | PRO | PRO | SER | TYR | THR | GLN | ARG | ASN | ILE | ||||
3 | ARG | ASP | LEU | LEU | GLN | ASP | ILE | ASN | VAL | VAL | ||||
4 | ALA | LEU | SER | ILE | ARG | LEU | PRO | SER | LEU | ARG | ||||
5 | PHE | ASN | THR | SER | ARG | ARG | PHE | ALA | TYR | ILE | ||||
6 | ASP | VAL | THR | SER | LYS | GLU | ASP | ALA | ARG | TYR | ||||
7 | CYS | VAL | GLU | LYS | LEU | ASN | GLY | LEU | LYS | ILE | ||||
8 | GLU | GLY | TYR | THR | LEU | VAL | THR | LYS | VAL | SER | ||||
9 | ASN | PRO | LEU | GLU | LEU | GLU | HIS | HIS | HIS | HIS | ||||
10 | HIS | HIS |
Entity 2, AGAGAU 6 residues - 1826.235 Da.
1 | A | G | A | G | A | U |
Samples:
Unlabeled: Prp24-RRM2 300 uM; AGAGAU 3 mM; TRIS, [U-2H], 10 mM; potassium chloride 50 mM; D20 100%
Fully_Labeled_D2O: Prp24-RRM2, [U-99% 15N], 500 uM; AGAGAU 5 mM; TRIS, [U-2H], 10 mM; potassium chloride 50 mM; D20 100%
Fully_Labeled: Prp24-RRM2, [U-99% 13C; U-99% 15N], 500 mM; AGAGAU 5 mM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; H20 90%; D20 10%
Referencing: Prp24-RRM2, [U-99% 13C; U-99% 15N], 500 uM; AGAGAU 5 mM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; DSS 10 uM; H20 90%; D20 10%
Aligned: Prp24-RRM2, [U-99% 13C; U-99% 15N], 300 uM; AGAGAU 3 mM; TRIS 10 mM; potassium chloride 50 mM; DTT 1 mM; DMPC/DHPC 3:1 6.5%; H20 90%; D20 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1.0 atm; temperature: 298.15 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-13C HSQC | Referencing | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | Fully_Labeled | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | Fully_Labeled_D2O | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | Fully_Labeled | isotropic | sample_conditions_1 |
3D C(CO)NH | Fully_Labeled | isotropic | sample_conditions_1 |
3D HNCO | Fully_Labeled | isotropic | sample_conditions_1 |
3D HNCACB | Fully_Labeled | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | Fully_Labeled | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | Fully_Labeled | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | Fully_Labeled | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | Fully_Labeled_D2O | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | Fully_Labeled_D2O | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | Unlabeled | isotropic | sample_conditions_1 |
2D 1H-15N HSQC-IPAP | Fully_Labeled | isotropic | sample_conditions_1 |
2D 1H-15N HSQC-IPAP | Aligned | anisotropic | sample_conditions_1 |
3D J modulated CHSQC | Fully_Labeled | isotropic | sample_conditions_1 |
3D J modulated CHSQC | Aligned | isotropic | sample_conditions_1 |
Software:
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
xwinnmr, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
ATHNOS-CANDID, Herrmann, T; Guentert, P; Wuethrich, K - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
HADDOCK v2, Dominguez, C; Boelens, R; Bonvin, A M M J - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian DMX 750 MHz
- Varian INOVA 900 MHz
- Varian INOVA 800 MHz
Related Database Links:
BMRB | 16243 16244 16246 |
PDB | |
DBJ | GAA25719 |
EMBL | CAA89251 CAY82100 |
GB | AAU09775 AHY76723 AJP40962 AJS62134 AJS62569 |
REF | NP_013995 |
SP | P49960 |
TPG | DAA10168 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts