BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 50470

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignment for Human Atg3 without N-terminal 25 resides   PubMed: 33446636

Deposition date: 2020-09-17 Original release date: 2020-11-25

Authors: Ye, Yansheng; Tyndall, Erin; Tian, Fang

Citation: Ye, Yansheng; Tyndall, Erin; Bui, Van; Tang, Zhenyuan; Shen, Yan; Jiang, Xuejun; Flanagan, John; Wang, Hong-Gang; Tian, Fang. "An N-terminal conserved region in human Atg3 couples membrane curvature sensitivity to conjugase activity during autophagy"  Nat. Commun. 12, 374-374 (2021).

Assembly members:
entity_1, polymer, 289 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):
entity_1: SKFKETGVITPEEFVAAGDH LVHHCPTWQWATGEELKVKA YLPTGKQFLVTKNVPCYKRC KQMEYSDELEAIIEEDDGDG GWVDTYHNTGITGITEAVKE ITLENKDNIRLQDCSALCEE EEDEDEGEAADMEEYEESGL LETDEATLDTRKIVEACKAK TDAGGEDAILQTRTYDLYIT YDKYYQTPRLWLFGYDEQRQ PLTVEHMYEDISQDHVKKTV TIENHPHLPPPPMCSVHPCR HAEVMKKIIETVAEGGGELG VHMYLLIFLKFVQAVIPTIE YDYTRHFTM

Data sets:
Data typeCount
13C chemical shifts727
15N chemical shifts220
1H chemical shifts220

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Atg31

Entities:

Entity 1, Atg3 289 residues - Formula weight is not available

1   SERLYSPHELYSGLUTHRGLYVALILETHR
2   PROGLUGLUPHEVALALAALAGLYASPHIS
3   LEUVALHISHISCYSPROTHRTRPGLNTRP
4   ALATHRGLYGLUGLULEULYSVALLYSALA
5   TYRLEUPROTHRGLYLYSGLNPHELEUVAL
6   THRLYSASNVALPROCYSTYRLYSARGCYS
7   LYSGLNMETGLUTYRSERASPGLULEUGLU
8   ALAILEILEGLUGLUASPASPGLYASPGLY
9   GLYTRPVALASPTHRTYRHISASNTHRGLY
10   ILETHRGLYILETHRGLUALAVALLYSGLU
11   ILETHRLEUGLUASNLYSASPASNILEARG
12   LEUGLNASPCYSSERALALEUCYSGLUGLU
13   GLUGLUASPGLUASPGLUGLYGLUALAALA
14   ASPMETGLUGLUTYRGLUGLUSERGLYLEU
15   LEUGLUTHRASPGLUALATHRLEUASPTHR
16   ARGLYSILEVALGLUALACYSLYSALALYS
17   THRASPALAGLYGLYGLUASPALAILELEU
18   GLNTHRARGTHRTYRASPLEUTYRILETHR
19   TYRASPLYSTYRTYRGLNTHRPROARGLEU
20   TRPLEUPHEGLYTYRASPGLUGLNARGGLN
21   PROLEUTHRVALGLUHISMETTYRGLUASP
22   ILESERGLNASPHISVALLYSLYSTHRVAL
23   THRILEGLUASNHISPROHISLEUPROPRO
24   PROPROMETCYSSERVALHISPROCYSARG
25   HISALAGLUVALMETLYSLYSILEILEGLU
26   THRVALALAGLUGLYGLYGLYGLULEUGLY
27   VALHISMETTYRLEULEUILEPHELEULYS
28   PHEVALGLNALAVALILEPROTHRILEGLU
29   TYRASPTYRTHRARGHISPHETHRMET

Samples:

sample_1: Human Atg3 without N-terminal 25 residues, [U-13C; U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe - processing

NMRView - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz MHz

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