BMRB Entry 11250
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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/BMR11250
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Title: Structure and function of the N-terminal nucleolin binding domain of nuclear valocine containing protein like 2 (NVL2) harboring a nucleolar localization signal. PubMed: 21474449
Deposition date: 2010-08-02 Original release date: 2011-06-24
Authors: Fujiwara, Yoshie; Fujiwara, Ken-ichiro; Goda, Natsuko; Iwaya, Naoko; Tenno, Takeshi; Shirakawa, Masahiro; Hiroaki, Hidekazu
Citation: Fujiwara, Yoshie; Fujiwara, Ken-Ichiro; Goda, Natsuko; Iwaya, Naoko; Tenno, Takeshi; Shirakawa, Masahiro; Hiroaki, Hidekazu. "Structure and Function of the N-terminal Nucleolin Binding Domain of Nuclear Valosin-containing Protein-like 2 (NVL2) Harboring a Nucleolar Localization Signal." J. Biol. Chem. 286, 21732-21741 (2011).
Assembly members:
NVL2 N-terminal domain, polymer, 74 residues, 8711.235 Da.
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):
NVL2 N-terminal domain: MKPRPGVFVDRKLKQRVIQY
LSSNRCGKYVDTGILASDLQ
RLYSVDYGRRKRNAFRIQVE
KVFSIISSEKELKN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 265 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 525 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NVL2 N-terminal domain | 1 |
Entities:
Entity 1, NVL2 N-terminal domain 74 residues - 8711.235 Da.
| 1 | MET | LYS | PRO | ARG | PRO | GLY | VAL | PHE | VAL | ASP | ||||
| 2 | ARG | LYS | LEU | LYS | GLN | ARG | VAL | ILE | GLN | TYR | ||||
| 3 | LEU | SER | SER | ASN | ARG | CYS | GLY | LYS | TYR | VAL | ||||
| 4 | ASP | THR | GLY | ILE | LEU | ALA | SER | ASP | LEU | GLN | ||||
| 5 | ARG | LEU | TYR | SER | VAL | ASP | TYR | GLY | ARG | ARG | ||||
| 6 | LYS | ARG | ASN | ALA | PHE | ARG | ILE | GLN | VAL | GLU | ||||
| 7 | LYS | VAL | PHE | SER | ILE | ILE | SER | SER | GLU | LYS | ||||
| 8 | GLU | LEU | LYS | ASN |
Samples:
sample_1: NVL2 N-terminal domain, [U-99% 15N], 1.2 mM; sodium phosphate 25 mM; H2O 95%; D2O 5%
sample_2: NVL2 N-terminal domain, [U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate 25 mM; D2O 100%
sample_conditions_1: ionic strength: 25 mM; pH: 6.4; 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 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.0.17, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DMX 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB23464 BAB29099 BAE24409 |
| GB | AAH31847 EDL13131 |
| REF | NP_080447 XP_006497028 XP_006497030 |
| SP | Q9DBY8 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts