BMRB Entry 27858

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27858

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Title:
Assignment of R32A mutant of yeast Hsp90 N-terminal domain
Deposition date:
2019-03-29
Original release date:
2021-07-21
Authors:
Lopez, Abraham; Sattler, Michael
Citation:

Citation: Mader, Sophie; Lopez, Abraham; Lawatscheck, Jannis; Luo, Qi; Rutz, Daniel; Gamiz-Hernandez, Ana; Sattler, Michael; Buchner, Johannes; Kaila, Ville. "Conformational dynamics modulate the catalytic activity of the molecular chaperone Hsp90"  Nat. Commun. 11, 1410-1410 (2020).
PubMed: 32179743

Assembly members:

Assembly members:
Hsp82_R32A_N-terminal_domain, polymer, 210 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hsp82_R32A_N-terminal_domain: MASETFEFQAEITQLMSLII NTVYSNKEIFLAELISNASD ALDKIRYKSLSDPKQLETEP DLFIRITPKPEQKVLEIRDS GIGMTKAELINNLGTIAKSG TKAFMEALSAGADVSMIGQF GVGFYSLFLVADRVQVISKS NDDEQYIWESNAGGSFTVTL DEVNERIGRGTILRLFLKDD QLEYLEEKRIKEVIKRHSEF VAYPIQLVVT

Data sets:
Data typeCount
13C chemical shifts534
15N chemical shifts184
1H chemical shifts183

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1NTD1

Entities:

Entity 1, NTD 210 residues - Formula weight is not available

1   METALASERGLUTHRPHEGLUPHEGLNALA
2   GLUILETHRGLNLEUMETSERLEUILEILE
3   ASNTHRVALTYRSERASNLYSGLUILEPHE
4   LEUALAGLULEUILESERASNALASERASP
5   ALALEUASPLYSILEARGTYRLYSSERLEU
6   SERASPPROLYSGLNLEUGLUTHRGLUPRO
7   ASPLEUPHEILEARGILETHRPROLYSPRO
8   GLUGLNLYSVALLEUGLUILEARGASPSER
9   GLYILEGLYMETTHRLYSALAGLULEUILE
10   ASNASNLEUGLYTHRILEALALYSSERGLY
11   THRLYSALAPHEMETGLUALALEUSERALA
12   GLYALAASPVALSERMETILEGLYGLNPHE
13   GLYVALGLYPHETYRSERLEUPHELEUVAL
14   ALAASPARGVALGLNVALILESERLYSSER
15   ASNASPASPGLUGLNTYRILETRPGLUSER
16   ASNALAGLYGLYSERPHETHRVALTHRLEU
17   ASPGLUVALASNGLUARGILEGLYARGGLY
18   THRILELEUARGLEUPHELEULYSASPASP
19   GLNLEUGLUTYRLEUGLUGLULYSARGILE
20   LYSGLUVALILELYSARGHISSERGLUPHE
21   VALALATYRPROILEGLNLEUVALVALTHR

Samples:

sample_1: Hsp82 R32A N-terminal domain, [U-100% 13C; U-100% 15N], 400 uM; sodium phosphate 20 mM; sodium chloride 100 mM; magnesium chloride 5 mM; sodium azide 0.02 % w/v; D2O, [U-2H], 5 % v/v

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

NMRPipe vCcpnmr 2.4.2, CCPN - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 950 MHz

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