BMRB Entry 11149

Name: Structural study of the UBA domain of p62 and its interaction with ubiquitin
Published: 2012-08-02

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11149

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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:

Structural study of the UBA domain of p62 and its interaction with ubiquitin

Deposition date:

2010-04-13

Original release date:

2012-08-02

Authors:

Isogai, Shin; Tochio, Hidehito; Tenno, Takeshi; Morimoto, Daichi

Citation:

Citation: Isogai, Shin; Tenno, Takeshi; Morimoto, Daichi; Tochio, Hidehito. "Structural study of the UBA domain of p62 and its interaction with ubiquitin" .

Assembly members:

Assembly members:
p62 UBA domain, polymer, 53 residues, 5817.546 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-6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
p62 UBA domain: GPLGSEADPRLIESLSQMLS MGFSDEGGWLTRLLQTKNYD IGAALDTIQYSKH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	219
15N chemical shifts	51
1H chemical shifts	356

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	p62 UBA domain	1

Entities:

Entity 1, p62 UBA domain 53 residues - 5817.546 Da.

1

GLY

PRO

LEU

GLY

SER

GLU

ALA

ASP

PRO

ARG

2

LEU

ILE

GLU

SER

LEU

SER

GLN

MET

LEU

SER

3

MET

GLY

PHE

SER

ASP

GLU

GLY

TRP

LEU

4

THR

ARG

LEU

GLN

THR

LYS

ASN

TYR

ASP

5

ILE

GLY

ALA

LEU

ASP

THR

ILE

GLN

TYR

6

SER

LYS

HIS

Samples:

sample_1: p62 UBA domain, [U-95% 13C; U-95% 15N], 400 uM; ubiquitin 2.4 mM; EDTA 1 mM; potassium phosphate 20 mM; potassium chloride 5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.025 M; pH: 6.8; 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_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

NMR spectrometers:

Bruker Avance 700 MHz

BMRB	11443 15591 15592
PDB	1Q02 2JY7 2JY8 2K0B 2KNV 2RRU 3B0F
DBJ	BAC26183
GB	AAH06019 AKI70216 EDL33719 EHH27114 EHH54825
REF	NP_001277698 XP_006246276 XP_006246277 XP_008273207 XP_008987787