BMRB Entry 51011

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51011

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

Title:
1H, 15N, 13C resonance assignment of the N-terminal domain (1-285) of yeast Atg9
Deposition date:
2021-07-08
Original release date:
2022-01-24
Authors:
Coudevylle, Nicolas; Banas, Bartlomiej; Baumann, Verena; Schuschnig, Martina; Zawadzka - Kazimierczuk, Anna; Kozminski, Witkor; Martens, Sascha
Citation:

Citation: Coudevylle, Nicolas; Banas, Bartlomiej; Baumann, Verena; Schuschnig, Martina; Zawadzka - Kazimierczuk, Anna; Kozminski, Wiktor; Martens, Sascha. "Mechanism of Atg9 recruitment by Atg11 in the cytoplasm-to-vacuole targeting pathway"  J. Biol. Chem. 298, 101573-101573 (2022).
PubMed: 35007534

Assembly members:

Assembly members:
entity_1, polymer, 293 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-M11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MERDEYQLPNSHGKNTFLSR IFGLQSDEVNPSLNSQEMSN FPLPDIERGSSLLHSTNDSR EDVDENDLRVPESDQGTSTE EEDEVDEEQVQAYAPQISDG LDGDHQLNSVTSKENVLETE KSNLERLVEGSTDDSVPKVG QLSSEEEEDNEFINNDGFDD DTPLFQKSKIHEFSSKKSNT IEDGKRPLFFRHILQNNRPQ RDTQKLFTSSNAIHHDKDKS ANNGPRNINGNQKHGTKYFG SATQPRFTGSPLNNTNRFTK LFPLRKPNLLSNISVLNNTP EDRINHMLEVLFQ

Data sets:
Data typeCount
13C chemical shifts612
15N chemical shifts216
1H chemical shifts784

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Atg9-NTD1

Entities:

Entity 1, Atg9-NTD 293 residues - Formula weight is not available

1   METGLUARGASPGLUTYRGLNLEUPROASN
2   SERHISGLYLYSASNTHRPHELEUSERARG
3   ILEPHEGLYLEUGLNSERASPGLUVALASN
4   PROSERLEUASNSERGLNGLUMETSERASN
5   PHEPROLEUPROASPILEGLUARGGLYSER
6   SERLEULEUHISSERTHRASNASPSERARG
7   GLUASPVALASPGLUASNASPLEUARGVAL
8   PROGLUSERASPGLNGLYTHRSERTHRGLU
9   GLUGLUASPGLUVALASPGLUGLUGLNVAL
10   GLNALATYRALAPROGLNILESERASPGLY
11   LEUASPGLYASPHISGLNLEUASNSERVAL
12   THRSERLYSGLUASNVALLEUGLUTHRGLU
13   LYSSERASNLEUGLUARGLEUVALGLUGLY
14   SERTHRASPASPSERVALPROLYSVALGLY
15   GLNLEUSERSERGLUGLUGLUGLUASPASN
16   GLUPHEILEASNASNASPGLYPHEASPASP
17   ASPTHRPROLEUPHEGLNLYSSERLYSILE
18   HISGLUPHESERSERLYSLYSSERASNTHR
19   ILEGLUASPGLYLYSARGPROLEUPHEPHE
20   ARGHISILELEUGLNASNASNARGPROGLN
21   ARGASPTHRGLNLYSLEUPHETHRSERSER
22   ASNALAILEHISHISASPLYSASPLYSSER
23   ALAASNASNGLYPROARGASNILEASNGLY
24   ASNGLNLYSHISGLYTHRLYSTYRPHEGLY
25   SERALATHRGLNPROARGPHETHRGLYSER
26   PROLEUASNASNTHRASNARGPHETHRLYS
27   LEUPHEPROLEUARGLYSPROASNLEULEU
28   SERASNILESERVALLEUASNASNTHRPRO
29   GLUASPARGILEASNHISMETLEUGLUVAL
30   LEUPHEGLN

Samples:

sample_1: Atg9-NTD, [U-95% 13C; U-95% 15N], 0,4 mM; Bis-Tris 25 mM; sodium chloride 300 mM

sample_conditions_1: ionic strength: 325 mM; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
5D HN(CA)CONHsample_1isotropicsample_conditions_1
5D (HACA)CON(CA)CONHsample_1isotropicsample_conditions_1
5D HabCabCONHsample_1isotropicsample_conditions_1

Software:

TOPSPIN - experiments setup and acquisition

SPARKY - spectra display, peak picking

TSAR - resonance assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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