BMRB Entry 15591

Name: NMR structure of the ubiquitin associated (UBA) domain of p62 (SQSTM1). RDC refined
Published: 2008-01-02

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PDB ID: 2jy7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15591
MolProbity Validation Chart

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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:

NMR structure of the ubiquitin associated (UBA) domain of p62 (SQSTM1). RDC refined

Deposition date:

2007-12-12

Original release date:

2008-01-02

Authors:

Long, Jed; Layfield, Robert; Searle, Mark

Citation:

Citation: Long, Jed; Gallagher, Thomas; Cavey, James; Sheppard, Paul; Ralston, Stuart; Layfield, Robert; Searle, Mark. "Ubiquitin recognition by the ubiquitin-associated domain of p62 involves a novel conformational switch" J. Biol. Chem. 283, 5427-5440 (2008).
PubMed: 18083707

Assembly members:

Assembly members:
P62_UBA, polymer, 52 residues, 5747.476 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T-1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
P62_UBA: GSPPEADPRLIESLSQMLSM GFSDEGGWLTRLLQTKNYDI GAALDTIQYSKH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs
- RDC_list_1

Data type	Count
13C chemical shifts	227
15N chemical shifts	53
1H chemical shifts	344
residual dipolar couplings	45

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	P62_UBA	1

Entities:

Entity 1, P62_UBA 52 residues - 5747.476 Da.

Residues 1-2 are cloning artifacts. This is the UBA domain of P62, residues 387-436

1

GLY

SER

PRO

GLU

ALA

ASP

PRO

ARG

LEU

2

ILE

GLU

SER

LEU

SER

GLN

MET

LEU

SER

MET

3

GLY

PHE

SER

ASP

GLU

GLY

TRP

LEU

THR

4

ARG

LEU

GLN

THR

LYS

ASN

TYR

ASP

ILE

5

GLY

ALA

LEU

ASP

THR

ILE

GLN

TYR

SER

6

LYS

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	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 CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC-IPAP	sample_3	anisotropic	sample_conditions_1

BMRB	11149 11443 15592
PDB	1Q02 2JY7 2JY8 2K0B 2KNV 2RRU 3B0F
DBJ	BAC26183 BAG35358 BAG53577 BAG65614 BAI46491
EMBL	CAA69642 CAH90955
GB	AAA93299 AAB02908 AAB17127 AAC50535 AAC52070
REF	NP_001125548 NP_001135770 NP_001135771 NP_001156515 NP_001253287
SP	O08623 Q13501 Q5RBA5 Q64337
TPG	DAA28341
AlphaFold	O08623 Q13501 Q5RBA5 Q64337 O08623 Q13501 Q5RBA5 Q64337

BMRB Entry 15591

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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