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 16588

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16588

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Title: NMR Assignment of the C-terminal Domain of yeast Aha-1   PubMed: 20159554

Deposition date: 2009-10-27 Original release date: 2009-11-24

Authors: Hagn, Franz; Retzlaff, Marco; Mitschke, Lars; Hessling, Martin; Gugel, Frederik; Richter, Klaus; Buchner, Johannes; Kessler, Horst

Citation: Retzlaff, Marco; Hagn, Franz; Mitschke, Lars; Hessling, Martin; Gugel, Frederik; Kessler, Horst; Richter, Klaus; Buchner, Johannes. "Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1."  Mol. Cell 37, 344-354 (2010).

Assembly members:
Aha1, polymer, 198 residues, Formula weight is not available

Natural source:   Common Name: baker   Taxonomy ID: 4932   Superkingdom: not available   Kingdom: not available   Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
Aha1: GSHMPESQVKSNYTRGNQKS SFTEIKDSASKPKKNALPSS TSTSAPVSSTNKVPQNGSGN STSIYLEPTFNVPSSELYET FLDKQRILAWTRSAQFFNSG PKLETKEKFELFGGNVISEL VSCEKDKKLVFHWKLKDWSA PFNSTIEMTFHESQEFHETK LQVKWTGIPVGEEDRVRANF EEYYVRSIKLTFGFGAVL

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts122
1H chemical shifts122

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Aha1 C-terminal domain1

Entities:

Entity 1, Aha1 C-terminal domain 198 residues - Formula weight is not available

Resiudes 1-4 represent an artificial peptide sequence after His6 tag removal, residues 5-198 represent Aha1 residues 157-350

1   GLYSERHISMETPROGLUSERGLNVALLYS
2   SERASNTYRTHRARGGLYASNGLNLYSSER
3   SERPHETHRGLUILELYSASPSERALASER
4   LYSPROLYSLYSASNALALEUPROSERSER
5   THRSERTHRSERALAPROVALSERSERTHR
6   ASNLYSVALPROGLNASNGLYSERGLYASN
7   SERTHRSERILETYRLEUGLUPROTHRPHE
8   ASNVALPROSERSERGLULEUTYRGLUTHR
9   PHELEUASPLYSGLNARGILELEUALATRP
10   THRARGSERALAGLNPHEPHEASNSERGLY
11   PROLYSLEUGLUTHRLYSGLULYSPHEGLU
12   LEUPHEGLYGLYASNVALILESERGLULEU
13   VALSERCYSGLULYSASPLYSLYSLEUVAL
14   PHEHISTRPLYSLEULYSASPTRPSERALA
15   PROPHEASNSERTHRILEGLUMETTHRPHE
16   HISGLUSERGLNGLUPHEHISGLUTHRLYS
17   LEUGLNVALLYSTRPTHRGLYILEPROVAL
18   GLYGLUGLUASPARGVALARGALAASNPHE
19   GLUGLUTYRTYRVALARGSERILELYSLEU
20   THRPHEGLYPHEGLYALAVALLEU

Samples:

sample_1: Aha1, [U-100% 13C; U-100% 15N], 1.2 ± 0.1 mM; potassium phosphate 20 mM; KCl 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

PASTA v2, Gemmecker and Kessler - chemical shift assignment

SPARKY, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

DBJ GAA22442
EMBL CAA92357 CAA92365 CAY78716
GB AAA73862 AAS56020 AHY75197 AJP37925 AJU58047
REF NP_010500
SP Q12449
TPG DAA12058

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