BMRB Entry 30398
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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/BMR30398
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Title: Solution structure of Musashi2 RRM1
Deposition date: 2018-01-25 Original release date: 2019-01-24
Authors: Xing, M.; Lan, L.; Douglas, J.; Gao, P.; Hanzlik, R.; Xu, L.
Citation: Xing, M.; Lan, L.; Douglas, J.; Gao, P.; Hanzlik, R.; Xu, L.. "Solution structure of Musashi2 RRM1" To be Published ., .-..
Assembly members:
entity_1, polymer, 115 residues, 13154.963 Da.
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
Entity Sequences (FASTA):
entity_1: MHHHHHHSTSVDLGTENLYF
QSNAGKMFIGGLSWQTSPDS
LRDYFSKFGEIRECMVMRDP
TTKRSRGFGFVTFADPASVD
KVLGQPHHELDSKTIDPKVA
FPRRAQPKMVTRTKK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 477 |
15N chemical shifts | 107 |
1H chemical shifts | 742 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 115 residues - 13154.963 Da.
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_1: MSI2-RRM1, [U-90% 15N], 0.5 mM; NaCl 150 mM
sample_2: MSI2-RRM1, [U-95% 13C; U-90% 15N], 0.7 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_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACO | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure calculation
CcpNMR, CCPN - chemical shift assignment, peak picking
NMRView, Johnson, One Moon Scientific - peak picking
TOPSPIN v2.1pl6, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker AvanceIII 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts