BMRB Entry 11250

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PDB ID: 2rre
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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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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.

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):

Entity Sequences (FASTA):
NVL2 N-terminal domain: MKPRPGVFVDRKLKQRVIQY LSSNRCGKYVDTGILASDLQ RLYSVDYGRRKRNAFRIQVE KVFSIISSEKELKN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	265
15N chemical shifts	77
1H chemical shifts	525

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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

6

LYS

ARG

ASN

ALA

PHE

ARG

ILE

GLN

VAL

GLU

7

LYS

VAL

PHE

SER

ILE

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

PDB	2RRE
DBJ	BAB23464 BAB29099 BAE24409
GB	AAH31847 EDL13131
REF	NP_080447 XP_006497028 XP_006497030
SP	Q9DBY8
AlphaFold	Q9DBY8