BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 31065

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31065
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Backbone and sidechain resonance assignments of human Atg3 with deletions of resides 1 to 25 and residues 90 to 190

Deposition date: 2022-12-21 Original release date: 2023-07-27

Authors: Ye, Y.; Tian, F.

Citation: Ye, Y.; Tian, F.; Tyndall, E.; Bui, V.; Bewley, M.; Wang, G.; Hong, X.; Shen, Y.; Flanagan, J.; Wang, H.. "Translating Membrane Geometry into Protein Function: Multifaceted Membrane Interactions of Human Atg3 Promote LC3-Phosphatidylethanolamine Conjugation during Autophagy"  .

Assembly members:
entity_1, polymer, 189 residues, 22091.420 Da.

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

Entity Sequences (FASTA):
entity_1: GSKFKETGVITPEEFVAAGD HLVHHCPTWQWATGEELKVK AYLPTGKQFLVTKNVPCYKR CKQMEEDAILQTRTYDLYIT YDKYYQTPRLWLFGYDEQRQ PLTVEHMYEDISQDHVKKTV TIENHPHLPPPPMCSVHPCR HAEVMKKIIETVAEGGGELG VHMYLLIFLKFVQAVIPTIE YDYTRHFTM

Data sets:
Data typeCount
13C chemical shifts804
15N chemical shifts165
1H chemical shifts1123

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 189 residues - 22091.420 Da.

1   GLYSERLYSPHELYSGLUTHRGLYVALILE
2   THRPROGLUGLUPHEVALALAALAGLYASP
3   HISLEUVALHISHISCYSPROTHRTRPGLN
4   TRPALATHRGLYGLUGLULEULYSVALLYS
5   ALATYRLEUPROTHRGLYLYSGLNPHELEU
6   VALTHRLYSASNVALPROCYSTYRLYSARG
7   CYSLYSGLNMETGLUGLUASPALAILELEU
8   GLNTHRARGTHRTYRASPLEUTYRILETHR
9   TYRASPLYSTYRTYRGLNTHRPROARGLEU
10   TRPLEUPHEGLYTYRASPGLUGLNARGGLN
11   PROLEUTHRVALGLUHISMETTYRGLUASP
12   ILESERGLNASPHISVALLYSLYSTHRVAL
13   THRILEGLUASNHISPROHISLEUPROPRO
14   PROPROMETCYSSERVALHISPROCYSARG
15   HISALAGLUVALMETLYSLYSILEILEGLU
16   THRVALALAGLUGLYGLYGLYGLULEUGLY
17   VALHISMETTYRLEULEUILEPHELEULYS
18   PHEVALGLNALAVALILEPROTHRILEGLU
19   TYRASPTYRTHRARGHISPHETHRMET

Samples:

sample_1: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM

sample_2: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM; Pf1 phage 6.5 mg/mL

sample_3: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM; positive gel 7%

sample_4: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM; negative gel 5%

sample_5: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM; neutral gel 5%

sample_6: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM

sample_7: NaCl 150 mM; HEPES 50 mM; TCEP 2 mM; human Atg3, [U-13C; U-15N], 0.5 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 Pa; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_6isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_6isotropicsample_conditions_1
2D ARTSYsample_7anisotropicsample_conditions_1
2D ARTSYsample_5anisotropicsample_conditions_1
2D ARTSYsample_4anisotropicsample_conditions_1
2D ARTSYsample_3anisotropicsample_conditions_1
2D ARTSYsample_2anisotropicsample_conditions_1
HBHA(CO)NHsample_1isotropicsample_conditions_1
2D Hb(CbCgCd)Hdsample_6isotropicsample_conditions_1
2D Hb(CbCgCdCe)Hesample_6isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_6isotropicsample_conditions_1

Software:

CNX, NIH - refinement

NMRViewJ, One Moon Scientific - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMRView, Johnson, One Moon Scientific - peak picking

TopSpin, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AVANCE II 600 MHz
  • Bruker AVANCE III 850 MHz

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