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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/BMR18048
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Gallo, Angelo; Lo Sterzo, Carlo; Mori, Mirko; Di Matteo, Adele; Bertini, Ivano; Banci, Lucia; Brunori, Maurizio; Federici, Luca. "Structure of nucleophosmin DNA-binding domain and analysis of its complex with a G-quadruplex sequence from the c-MYC promoter." J. Biol. Chem. 287, 26539-26548 (2012).
PubMed: 22707729
Assembly members:
entity, polymer, 70 residues, 8101.407 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 Vector: pET28+(a)
Entity Sequences (FASTA):
entity: QESFKKQEKTPKTPKGPSSV
EDIKAKMQASIEKGGSLPKV
EAKFINYVKNCFRMTDQEAI
QDLWQWRKSL
Data type | Count |
13C chemical shifts | 276 |
15N chemical shifts | 73 |
1H chemical shifts | 241 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | NPM1_C70 | 1 |
Entity 1, NPM1_C70 70 residues - 8101.407 Da.
1 | GLN | GLU | SER | PHE | LYS | LYS | GLN | GLU | LYS | THR | |
2 | PRO | LYS | THR | PRO | LYS | GLY | PRO | SER | SER | VAL | |
3 | GLU | ASP | ILE | LYS | ALA | LYS | MET | GLN | ALA | SER | |
4 | ILE | GLU | LYS | GLY | GLY | SER | LEU | PRO | LYS | VAL | |
5 | GLU | ALA | LYS | PHE | ILE | ASN | TYR | VAL | LYS | ASN | |
6 | CYS | PHE | ARG | MET | THR | ASP | GLN | GLU | ALA | ILE | |
7 | GLN | ASP | LEU | TRP | GLN | TRP | ARG | LYS | SER | LEU |
sample_1: NPM1_C70, [U-15N], 0.5 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%
sample_2: NPM1_C70, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 20 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K
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 HNCO | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA v2.1, Keller and Wuthrich - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AMBER v11.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement
PSVS, Bhattacharya and Montelione - validation
PDB | |
DBJ | BAC25844 BAE22562 BAE26248 BAE26667 BAE32244 |
EMBL | CAA34809 CAH90204 |
GB | AAA36380 AAA36385 AAA36473 AAA36474 AAA39801 |
REF | NP_001030518 NP_001125077 NP_001164790 NP_001238905 NP_001239100 |
SP | P06748 P13084 Q3T160 Q61937 |
TPG | DAA18048 DAA21326 DAA21327 DAA26330 DAA26331 |
AlphaFold | P06748 P13084 Q3T160 Q61937 |
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