BMRB Entry 25497
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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/BMR25497
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Title: NMR structure of the RRM1 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:
RRM1, polymer, 95 residues, 10934.025 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):
RRM1: GSARELDSTYEEKVNRNYSN
SIFVGNLTYDSTPEDLTEFF
SQIGKVVRADIITSRGHHRG
MGTVEFTNSDDVDRAIRQYD
GAFFMDRKIFVRQDN
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 371 |
15N chemical shifts | 89 |
1H chemical shifts | 576 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | RRM1 | 1 |
Entities:
Entity 1, RRM1 95 residues - 10934.025 Da.
From 144 to 236
1 | GLY | SER | ALA | ARG | GLU | LEU | ASP | SER | THR | TYR | ||||
2 | GLU | GLU | LYS | VAL | ASN | ARG | ASN | TYR | SER | ASN | ||||
3 | SER | ILE | PHE | VAL | GLY | ASN | LEU | THR | TYR | ASP | ||||
4 | SER | THR | PRO | GLU | ASP | LEU | THR | GLU | PHE | PHE | ||||
5 | SER | GLN | ILE | GLY | LYS | VAL | VAL | ARG | ALA | ASP | ||||
6 | ILE | ILE | THR | SER | ARG | GLY | HIS | HIS | ARG | GLY | ||||
7 | MET | GLY | THR | VAL | GLU | PHE | THR | ASN | SER | ASP | ||||
8 | ASP | VAL | ASP | ARG | ALA | ILE | ARG | GLN | TYR | ASP | ||||
9 | GLY | ALA | PHE | PHE | MET | ASP | ARG | LYS | ILE | PHE | ||||
10 | VAL | ARG | GLN | ASP | ASN |
Samples:
sample_1: RRM1, [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: RRM1, [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 HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | 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