BMRB Entry 19982
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19982
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Title: NPM-N (Nucleophosmin) pentamer assignment PubMed: 1321007111
Deposition date: 2014-05-20 Original release date: 2014-06-18
Authors: Mitrea, Diana; Grace, Christy; Buljan, Marija; Yun, Mi-Kyung; Pytel, Nicholas; Satumba, John; Nourse, Amanda; Park, Cheon-Gil; Babu, Madan; White, Stephen; Kriwacki, Richard
Citation: Mitrea, Diana; Grace, Christy; Buljan, Marija; Yun, Mi-Kyung; Pytel, Nicholas; Satumba, John; Nourse, Amanda; Park, Cheon-Gil; Babu, Madan; White, Stephen; Kriwacki, Richard. "Structural polymorphism in the N-terminal oligomerization domain of NPM1" Proc. Natl. Acad. Sci. U.S.A. 111, 4466-4471 (2014).
Assembly members:
NPM, polymer, 133 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NPM: GSHWEDSMDMDMSPLRPQNY
LFGCELKADKDYHFKVDNDE
NEHQLSLRTVSLGAGAKDEL
HIVEAEAMNYEGSPIKVTLA
TLKMSVQPTVSLGGFEITPP
VVLRLKCGSGPVHISGQHLV
AVEEDAESEDEDE
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 122 |
| 13C chemical shifts | 300 |
| 15N chemical shifts | 122 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NPM1, chain 1 | 1 |
| 2 | NPM1, chain 2 | 1 |
| 3 | NPM1, chain 3 | 1 |
| 4 | NPM1, chain 4 | 1 |
| 5 | NPM1, chain 5 | 1 |
Entities:
Entity 1, NPM1, chain 1 133 residues - Formula weight is not available
| 1 | GLY | SER | HIS | TRP | GLU | ASP | SER | MET | ASP | MET | ||||
| 2 | ASP | MET | SER | PRO | LEU | ARG | PRO | GLN | ASN | TYR | ||||
| 3 | LEU | PHE | GLY | CYS | GLU | LEU | LYS | ALA | ASP | LYS | ||||
| 4 | ASP | TYR | HIS | PHE | LYS | VAL | ASP | ASN | ASP | GLU | ||||
| 5 | ASN | GLU | HIS | GLN | LEU | SER | LEU | ARG | THR | VAL | ||||
| 6 | SER | LEU | GLY | ALA | GLY | ALA | LYS | ASP | GLU | LEU | ||||
| 7 | HIS | ILE | VAL | GLU | ALA | GLU | ALA | MET | ASN | TYR | ||||
| 8 | GLU | GLY | SER | PRO | ILE | LYS | VAL | THR | LEU | ALA | ||||
| 9 | THR | LEU | LYS | MET | SER | VAL | GLN | PRO | THR | VAL | ||||
| 10 | SER | LEU | GLY | GLY | PHE | GLU | ILE | THR | PRO | PRO | ||||
| 11 | VAL | VAL | LEU | ARG | LEU | LYS | CYS | GLY | SER | GLY | ||||
| 12 | PRO | VAL | HIS | ILE | SER | GLY | GLN | HIS | LEU | VAL | ||||
| 13 | ALA | VAL | GLU | GLU | ASP | ALA | GLU | SER | GLU | ASP | ||||
| 14 | GLU | ASP | GLU |
Samples:
sample_1: NPM, [U-13C; U-15N; U-2H], 1.0 mM; NPM, [U-100% 13C; U-100% 15N; U-80% 2H], 0.2 mM; NaCl 200 mM; H2O 90%; D2O 10%
sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm; ionic strength: 200 mM
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.1, Keller and Wuthrich - chemical shift assignment, collection, data analysis, peak picking, processing
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA08343 BAB24014 BAB40600 BAC25844 BAC25910 |
| EMBL | CAA34809 CAH90204 |
| GB | AAA36380 AAA36385 AAA39801 AAA40794 AAA40795 |
| REF | NP_001030518 NP_001032827 NP_001125077 NP_001164790 NP_001238905 |
| SP | P06748 P13084 Q3T160 Q61937 |
| TPG | DAA18048 DAA26330 DAA26331 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts