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 27581

Title: 1H, 13C, and 15N chemical shift assignments of the Sushi 1 domain of GABAbR1a   PubMed: 30630900

Authors: Volkov, Alexander; Rice, Heather; Van Molle, Inge; De Strooper, Bart; de Wit, Joris

Citation: Rice, Heather; de Malmazet, Daniel; Schreurs, An; Frere, Samuel; Van Molle, Inge; Volkov, Alexander; Creemers, Eline; Vertkin, Irena; Nys, Julie; Ranaivoson, Fanomezana; Comoletti, Davide; Savas, Jeffrey; Remaut, Han; Balschun, Detlef; Wierda, Keimpe; Slutsky, Inna; Farrow, Karl; De Strooper, Bart; de Wit, Joris. "Secreted amyloid-beta precursor protein functions as a GABA"  Science 363, 4827-4827 (2019).

Assembly members:
Sushi1, polymer, 75 residues, Formula weight is not available
APPP, polymer, 9 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

Entity Sequences (FASTA):
Sushi1: GPTSEGCQIIHPPWEGGIRY RGLTRDQVKAINFLPVDYEI EYVCRGEREVVGPKVRKCLA NGSWTDMDTPSRCVR
APPP: DDSDVWWGG

Data sets:
Data typeCount
13C chemical shifts326
15N chemical shifts73
1H chemical shifts515

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sushi11
2APPP2

Entities:

Entity 1, Sushi1 75 residues - Formula weight is not available

1   GLYPROTHRSERGLUGLYCYSGLNILEILE
2   HISPROPROTRPGLUGLYGLYILEARGTYR
3   ARGGLYLEUTHRARGASPGLNVALLYSALA
4   ILEASNPHELEUPROVALASPTYRGLUILE
5   GLUTYRVALCYSARGGLYGLUARGGLUVAL
6   VALGLYPROLYSVALARGLYSCYSLEUALA
7   ASNGLYSERTRPTHRASPMETASPTHRPRO
8   SERARGCYSVALARG

Entity 2, APPP 9 residues - Formula weight is not available

1   ASPASPSERASPVALTRPTRPGLYGLY

Samples:

sample_1: Sushi1, [U-13C; U-15N], 1 mM; APP 3 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.01%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

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

CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

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