BMRB Entry 11443

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR11443
MolProbity Validation Chart

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Title:
Crystal structure of the UBA domain of p62 and its interaction with ubiquitin
Deposition date:
2011-06-09
Original release date:
2011-07-05
Authors:
Isogai, Shin; Morimoto, Daichi; Arita, Kyouhei; Unzai, Satoru; Tenno, Takeshi; Hasegawa, Jun; Sou, Yu-shin; Komatsu, Masaaki; Tanaka, Keiji; Shirakawa, Masahiro; Tochio, Hidehito
Citation:

Citation: Isogai, Shin; Morimoto, Daichi; Arita, Kyouhei; Unzai, Satoru; Tenno, Takeshi; Sou, Yu-shin; Komatsu, Masaaki; Tanaka, Keiji; Shirakawa, Masahiro; Tochio, Hidehito. "Crystal structure of the UBA domain of p62 and its interaction with ubiquitin"  To be Published ., .-..

Assembly members:

Assembly members:
P62/SEQUESTOSOME-1, 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/SEQUESTOSOME-1: GPLGSEADPRLIESLSQMLS MGFSDEGGWLTRLLQTKNYD IGAALDTIQYSKH

Data sets:
Data typeCount
13C chemical shifts219
15N chemical shifts51
1H chemical shifts356

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1P62/SEQUESTOSOME-11

Entities:

Entity 1, P62/SEQUESTOSOME-1 53 residues - 5817.546 Da.

Expression Tag sequence GPLGS

1   GLYPROLEUGLYSERGLUALAASPPROARG
2   LEUILEGLUSERLEUSERGLNMETLEUSER
3   METGLYPHESERASPGLUGLYGLYTRPLEU
4   THRARGLEULEUGLNTHRLYSASNTYRASP
5   ILEGLYALAALALEUASPTHRILEGLNTYR
6   SERLYSHIS

Samples:

sample_1: P62/SEQUESTOSOME-1, [U-95% 13C; U-95% 15N], 0.4 mM; Ubiquitin 2.4 mM; potassium phosphate 20 mM; potassium chloride 5 mM; EDTA 1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 0.025 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)N 3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, GUNTERT, MUMENTHALER - refinement, structure solution

SPARKY v3.113, Goddard - data analysis, peak picking

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

TOPSPIN, Bruker Biospin - collection

CANDID, Herrmann, Guntert and Wuthrich - chemical shift assignment

ATNOS, Herrmann and Wuthrich - peak picking

CARA, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • BRUKER AVANCE 700 MHz

Related Database Links:

BMRB 11149 15591 15592
PDB
DBJ BAC26183
GB AAH06019 AKI70216 EDL33719 EHH27114 EHH54825
REF NP_001277698 XP_006246276 XP_006246277 XP_008273207 XP_008987787

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