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 16835

Title: The NMR structure of the autophagy-related protein Atg8   PubMed: 20428927

Deposition date: 2010-04-05 Original release date: 2010-05-11

Authors: Kumeta, Hiroyuki; Watanabe, Masahiro; Nakatogawa, Hitoshi; Yamaguchi, Masaya; Ogura, Kenji; Adachi, Wakana; Fujioka, Yuko; Noda, Nobuo; Ohsumi, Yoshinori; Inagaki, Fuyuhiko

Citation: Kumeta, Hiroyuki; Watanabe, Masahiro; Nakatogawa, Hitoshi; Yamaguchi, Masaya; Ogura, Kenji; Adachi, Wakana; Fujioka, Yuko; Noda, Nobuo; Ohsumi, Yoshinori; Inagaki, Fuyuhiko. "The NMR structure of the autophagy-related protein Atg8."  J. Biomol. NMR 47, 237-241 (2010).

Assembly members:
Atg8_K26P, polymer, 116 residues, 13459.674 Da.

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX6p

Entity Sequences (FASTA):
Atg8_K26P: MKSTFKSEYPFEKRKAESER IADRFPNRIPVICEKAEKSD IPEIDKRKYLVPADLTVGQF VYVIRKRIMLPPEKAIFIFV NDTLPPTAALMSAIYQEHKD KDGFLYVTYSGENTFG

Data sets:
Data typeCount
13C chemical shifts521
15N chemical shifts113
1H chemical shifts863

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Atg81

Entities:

Entity 1, Atg8 116 residues - 13459.674 Da.

1   METLYSSERTHRPHELYSSERGLUTYRPRO
2   PHEGLULYSARGLYSALAGLUSERGLUARG
3   ILEALAASPARGPHEPROASNARGILEPRO
4   VALILECYSGLULYSALAGLULYSSERASP
5   ILEPROGLUILEASPLYSARGLYSTYRLEU
6   VALPROALAASPLEUTHRVALGLYGLNPHE
7   VALTYRVALILEARGLYSARGILEMETLEU
8   PROPROGLULYSALAILEPHEILEPHEVAL
9   ASNASPTHRLEUPROPROTHRALAALALEU
10   METSERALAILETYRGLNGLUHISLYSASP
11   LYSASPGLYPHELEUTYRVALTHRTYRSER
12   GLYGLUASNTHRPHEGLY

Samples:

CN-label: Atg8 K26P, [U-99% 13C; U-99% 15N], 0.6 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 170 mM; pH: 6.8; pressure: 1 atm; temperature: 297 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCCN-labelisotropicsample_conditions_1
2D 1H-13C HSQCCN-labelisotropicsample_conditions_1
3D HNCOCN-labelisotropicsample_conditions_1
3D HN(CO)CACN-labelisotropicsample_conditions_1
3D HNCACN-labelisotropicsample_conditions_1
3D HBHA(CO)NHCN-labelisotropicsample_conditions_1
3D HN(CA)HACN-labelisotropicsample_conditions_1
3D C(CO)NHCN-labelisotropicsample_conditions_1
3D HCCH-TOCSYCN-labelisotropicsample_conditions_1
3D CCH-TOCSYCN-labelisotropicsample_conditions_1
2D HbCbCgCdHdCN-labelisotropicsample_conditions_1
2D HbCbCgCdCeHeCN-labelisotropicsample_conditions_1
3D 1H-15N NOESYCN-labelisotropicsample_conditions_1
3D 1H-13C NOESYCN-labelisotropicsample_conditions_1

Software:

VNMR v6.1C, Varian - collection

NMRPipe v5.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS v2007.068.09.07, Cornilescu, Delaglio and Bax - data analysis

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16120 17879
PDB
DBJ GAA21477
EMBL CAA56032 CAA84899 CAY77706
GB AAT92889 AHY74413 AJP37015 AJP81917 AJP82297
REF NP_009475
SP A6ZKM4 P38182
TPG DAA07045
AlphaFold P38182 A6ZKM4

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