BMRB Entry 15591

NMR structure of the ubiquitin associated (UBA) domain of p62 (SQSTM1). RDC refined
Deposition date:
Original release date:
Long, Jed; Layfield, Robert; Searle, Mark

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):

Data sets:
Data typeCount
13C chemical shifts227
15N chemical shifts53
1H chemical shifts344
residual dipolar couplings45

Additional metadata:

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


Entity Assembly IDEntity NameEntity ID


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



sample_2: entity, [U-100% 13C; U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.04%; D2O, [U-100% 2H], 10%; H2O 90%

sample_3: entity, [U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.04%; D2O, [U-100% 2H], 10%; H2O 90%

sample_1: entity, [U-100% 15N], 1 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.04%; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K


NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
2D 1H-15N HSQC-IPAPsample_3anisotropicsample_conditions_1


X-PLOR NIH v2.14, Schwieters, Kuszewski, Tjandra and Clore - structure solution

xwinnmr v3.5, Bruker Biospin - collection, processing

CcpNMR v1.0.10, CCPN - chemical shift assignment, data analysis, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 11149 11443 15592
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 Q64337 O08623 O08623 Q13501 Q13501 Q5RBA5 Q5RBA5 Q64337

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