BMRB Entry 27111
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27111
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Musashi2 RRM1 PubMed: 31603583
Deposition date: 2017-05-23 Original release date: 2017-12-12
Authors: Lan, Lan; Xing, Minli; Douglas, Justin; Gao, Philip; Hanzlik, Robert; Xu, Liang
Citation: Lan, Lan; Xing, Minli; Kashipathy, Maithri; Douglas, Justin; Gao, Philip; Battaile, Kevin; Hanzlik, Robert; Lovell, Scott; Xu, Liang. "Crystal and solution structures of human oncoprotein Musashi-2 N-terminal RNA recognition motif 1" Proteins 88, 573-583 (2020).
Assembly members:
MSI2_RRM1, polymer, 115 residues, Formula weight is not available
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: pTBSG
Entity Sequences (FASTA):
MSI2_RRM1: MHHHHHHSTSVDLGTENLYF
QSNAGKMFIGGLSWQTSPDS
LRDYFSKFGEIRECMVMRDP
TTKRSRGFGFVTFADPASVD
KVLGQPHHELDSKTIDPKVA
FPRRAQPKMVTRTKK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 216 |
15N chemical shifts | 99 |
1H chemical shifts | 99 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | MSI2 RRM1 | 1 |
Entities:
Entity 1, MSI2 RRM1 115 residues - Formula weight is not available
1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | THR | SER | ||||
2 | VAL | ASP | LEU | GLY | THR | GLU | ASN | LEU | TYR | PHE | ||||
3 | GLN | SER | ASN | ALA | GLY | LYS | MET | PHE | ILE | GLY | ||||
4 | GLY | LEU | SER | TRP | GLN | THR | SER | PRO | ASP | SER | ||||
5 | LEU | ARG | ASP | TYR | PHE | SER | LYS | PHE | GLY | GLU | ||||
6 | ILE | ARG | GLU | CYS | MET | VAL | MET | ARG | ASP | PRO | ||||
7 | THR | THR | LYS | ARG | SER | ARG | GLY | PHE | GLY | PHE | ||||
8 | VAL | THR | PHE | ALA | ASP | PRO | ALA | SER | VAL | ASP | ||||
9 | LYS | VAL | LEU | GLY | GLN | PRO | HIS | HIS | GLU | LEU | ||||
10 | ASP | SER | LYS | THR | ILE | ASP | PRO | LYS | VAL | ALA | ||||
11 | PHE | PRO | ARG | ARG | ALA | GLN | PRO | LYS | MET | VAL | ||||
12 | THR | ARG | THR | LYS | LYS |
Samples:
sample_2: MSI2 RRM1, [U-90% 15N], 0.5 mM; NaCl 150 mM
sample_1: MSI2 RRM1, [U-95% 13C; U-90% 15N], 0.7 mM; MSI2 RRM1, [U-95% 13C; U-90% 15N], 0.6 mM; MSI2 RRM1, [U-95% 13C; U-90% 15N], 0.8 mM; NaCl 150 mM
sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CCPN, CCPN - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts