BMRB Entry 53246

Title:
A human ATG3 deletion construct (D89-192)
Deposition date:
2025-06-26
Original release date:
2025-07-29
Authors:
Ohashi, Kazuto; Otomo, Takanori
Citation:

Citation: Ohashi, Kazuto; Kroon, Gerard; Otomo, Takanori. "Structural Insights into the GABARAP-ATG3 Backside Interaction and Apo ATG3 Conformation"  Biochemistry 64, 3178-3189 (2025).
PubMed: 40628661

Assembly members:

Assembly members:
entity_1, polymer, 215 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   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

Data sets:
Data typeCount
13C chemical shifts550
15N chemical shifts175
1H chemical shifts175

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ATG3 monomer1

Entities:

Entity 1, ATG3 monomer 215 residues - Formula weight is not available

GHMAMAQ+(ATG3 residues 2-188+193-314)

1   GLYHISMETALAMETALAGLNASNVALILE
2   ASNTHRVALLYSGLYLYSALALEUGLUVAL
3   ALAGLUTYRLEUTHRPROVALLEULYSGLU
4   SERLYSPHELYSGLUTHRGLYVALILETHR
5   PROGLUGLUPHEVALALAALAGLYASPHIS
6   LEUVALHISHISCYSPROTHRTRPGLNTRP
7   ALATHRGLYGLUGLULEULYSVALLYSALA
8   TYRLEUPROTHRGLYLYSGLNPHELEUVAL
9   THRLYSASNVALPROCYSTYRLYSARGCYS
10   LYSGLNMETALAILELEUGLNTHRARGTHR
11   TYRASPLEUTYRILETHRTYRASPLYSTYR
12   TYRGLNTHRPROARGLEUTRPLEUPHEGLY
13   TYRASPGLUGLNARGGLNPROLEUTHRVAL
14   GLUHISMETTYRGLUASPILESERGLNASP
15   HISVALLYSLYSTHRVALTHRILEGLUASN
16   HISPROHISLEUPROPROPROPROMETCYS
17   SERVALHISPROCYSARGHISALAGLUVAL
18   METLYSLYSILEILEGLUTHRVALALAGLU
19   GLYGLYGLYGLULEUGLYVALHISMETTYR
20   LEULEUILEPHELEULYSPHEVALGLNALA
21   VALILEPROTHRILEGLUTYRASPTYRTHR
22   ARGHISPHETHRMET

Samples:

sample_1: ATG3 double-labeled, [U-100% 13C; U-100% 15N], 1.2 M

sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRDraw - processing

NMRPipe - processing

NMRViewJ - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

UNP Q9NT62

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