BMRB Entry 11250

Title:
Structure and function of the N-terminal nucleolin binding domain of nuclear valocine containing protein like 2 (NVL2) harboring a nucleolar localization signal.
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:

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).
PubMed: 21474449

Assembly members:

Assembly members:
NVL2 N-terminal domain, polymer, 74 residues, 8711.235 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-PRESAT-NVL2

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts265
15N chemical shifts77
1H chemical shifts525

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1NVL2 N-terminal domain1

Entities:

Entity 1, NVL2 N-terminal domain 74 residues - 8711.235 Da.

1   METLYSPROARGPROGLYVALPHEVALASP
2   ARGLYSLEULYSGLNARGVALILEGLNTYR
3   LEUSERSERASNARGCYSGLYLYSTYRVAL
4   ASPTHRGLYILELEUALASERASPLEUGLN
5   ARGLEUTYRSERVALASPTYRGLYARGARG
6   LYSARGASNALAPHEARGILEGLNVALGLU
7   LYSVALPHESERILEILESERSERGLULYS
8   GLULEULYSASN

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_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
AlphaFold Q9DBY8

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks