BMRB Entry 25498
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25498
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Title: NMR structure of the RRM2 domain of Hrb1 PubMed: 26602689
Deposition date: 2015-02-23 Original release date: 2015-11-30
Authors: Martinez-Lumbreras, Santiago; Seraphin, Bertrand; Perez-Canadillas, Jose Manuel
Citation: Martinez-Lumbreras, Santiago; Taverniti, Valerio; Zorrilla, Silvia; Seraphin, Bertrand; Perez-Canadillas, Jose Manuel. "Gbp2 interacts with THO/TREX through a novel type of RRM domain" Nucleic Acids Res. 44, 437-448 (2016).
Assembly members:
RRM2, polymer, 99 residues, 10701.727 Da.
Natural source: Common Name: Baker's 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):
RRM2: GSEVIVKNLPASVNWQALKD
IFKECGNVAHADVELDGDGV
STGSGTVSFYDIKDLHRAIE
KYNGYSIEGNVLDVKSKESV
HNHSDGDDVDIPMDDSPVN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 409 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 635 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RRM2 | 1 |
Entities:
Entity 1, RRM2 99 residues - 10701.727 Da.
From 262 to 358
| 1 | GLY | SER | GLU | VAL | ILE | VAL | LYS | ASN | LEU | PRO | ||||
| 2 | ALA | SER | VAL | ASN | TRP | GLN | ALA | LEU | LYS | ASP | ||||
| 3 | ILE | PHE | LYS | GLU | CYS | GLY | ASN | VAL | ALA | HIS | ||||
| 4 | ALA | ASP | VAL | GLU | LEU | ASP | GLY | ASP | GLY | VAL | ||||
| 5 | SER | THR | GLY | SER | GLY | THR | VAL | SER | PHE | TYR | ||||
| 6 | ASP | ILE | LYS | ASP | LEU | HIS | ARG | ALA | ILE | GLU | ||||
| 7 | LYS | TYR | ASN | GLY | TYR | SER | ILE | GLU | GLY | ASN | ||||
| 8 | VAL | LEU | ASP | VAL | LYS | SER | LYS | GLU | SER | VAL | ||||
| 9 | HIS | ASN | HIS | SER | ASP | GLY | ASP | ASP | VAL | ASP | ||||
| 10 | ILE | PRO | MET | ASP | ASP | SER | PRO | VAL | ASN |
Samples:
sample_1: RRM2, [U-100% 13C; U-100% 15N], 0.2 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 10%; H2O 90%
sample_2: RRM2, [U-100% 13C; U-100% 15N], 0.2 mM; potassium phosphate 25 mM; sodium chloride 25 mM; DTT 0.1 mM; D2O 100%
sample_conditions_1: ionic strength: 50 mM; 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-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement
TOPSPIN, Bruker Biospin - collection
CcpNMR_Analysis, CCPN - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts