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 25385

Title: NMR assignments of Ssa1 substrate binding domain   PubMed: 25682100

Deposition date: 2014-12-08 Original release date: 2016-06-30

Authors: Hu, Wanhui; Wu, Huiwen; Zhang, Hong; Gong, Weibin; Perrett, Sarah

Citation: Hu, Wanhui; Wu, Huiwen; Zhang, Hong; Gong, Weibin; Perrett, Sarah. "Resonance assignments for the substrate binding domain of Hsp70 chaperone Ssa1 from Saccharomyces cerevisiae"  Biomol. NMR Assign. 9, 329-332 (2015).

Assembly members:
Ssa1_substrate_binding_domain, polymer, 174 residues, 18838.3 Da.

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

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

Entity Sequences (FASTA):
Ssa1_substrate_binding_domain: SSSKTQDLLLLDVAPLSLGI ETAGGVMTKLIPRNSTIPTK KSEIFSTYADNQPGVLIQVF EGERAKTKDNNLLGKFELSG IPPAPRGVPQIEVTFDVDSN GILNVSAVEKGTGKSNKITI TNDKGRLSKEDIEKMVAEAE KFKEEDEKESQRIASKNQLE SIAYSLKNTISEAG

Data sets:
Data typeCount
13C chemical shifts727
15N chemical shifts176
1H chemical shifts1109

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ssa1 substrate binding domain1

Entities:

Entity 1, Ssa1 substrate binding domain 174 residues - 18838.3 Da.

1   SERSERSERLYSTHRGLNASPLEULEULEU
2   LEUASPVALALAPROLEUSERLEUGLYILE
3   GLUTHRALAGLYGLYVALMETTHRLYSLEU
4   ILEPROARGASNSERTHRILEPROTHRLYS
5   LYSSERGLUILEPHESERTHRTYRALAASP
6   ASNGLNPROGLYVALLEUILEGLNVALPHE
7   GLUGLYGLUARGALALYSTHRLYSASPASN
8   ASNLEULEUGLYLYSPHEGLULEUSERGLY
9   ILEPROPROALAPROARGGLYVALPROGLN
10   ILEGLUVALTHRPHEASPVALASPSERASN
11   GLYILELEUASNVALSERALAVALGLULYS
12   GLYTHRGLYLYSSERASNLYSILETHRILE
13   THRASNASPLYSGLYARGLEUSERLYSGLU
14   ASPILEGLULYSMETVALALAGLUALAGLU
15   LYSPHELYSGLUGLUASPGLULYSGLUSER
16   GLNARGILEALASERLYSASNGLNLEUGLU
17   SERILEALATYRSERLEULYSASNTHRILE
18   SERGLUALAGLY

Samples:

sample_1: Ssa1 substrate binding domain, [U-99% 15N], 1 mM; D2O, [U-99% 2H], 10 % v/v; H2O 90 % v/v; DTT 4 mM; DSS 0.002 % w/v; sodium phosphate 50 mM; sodium chloride 150 mM; EDTA 2 mM

sample_2: Ssa1 substrate binding domain, [U-99% 13C; U-99% 15N], 1 mM; D2O, [U-99% 2H], 10 % v/v; H2O 90 % v/v; DTT 4 mM; sodium phosphate 50 mM; sodium chloride 150 mM; EDTA 2 mM

sample_conditions_1: ionic strength: 250 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

NMRPipe v9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView vNMRViewJ 8.0, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Varian DD2 600 MHz

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