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BMRB Entry 34758 BMRB - Biological Magnetic Resonance Bank

BMRB Entry 34758

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
BMRB Entry DOI: doi:10.13018/BMR34758
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Human HSP90 alpha ATP Binding Domain, ATP-lid open conformation, R60A
Deposition date:
2022-09-30
Original release date:
2022-11-08
Authors:
Rioual, E.; Henot, F.; Favier, A.; Macek, P.; Crublet, E.; Josso, P.; Brutscher, B.; Frech, M.; Gans, P.; Loison, C.; Boisbouvier, J.
Citation:

Citation: Henot, Faustine; Rioual, Elisa; Favier, Adrien; Macek, Pavel; Crublet, Elodie; Josso, Pierre; Brutscher, Bernhard; Frech, Matthias; Gans, Pierre; Loison, Claire; Boisbouvier, Jerome. "Visualizing the transiently populated closed-state of human HSP90 ATP binding domain"  Nat. Commun. 13, 7601-7601 (2022).
PubMed: 36494347

Assembly members:

Assembly members:
entity_1, polymer, 266 residues, 29934.477 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)   Vector: pET-28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH NQTSLYKKAGFENLYFQGDQ PMEEEEVETFAFQAEIAQLM SLIINTFYSNKEIFLRELIS NSSDALDKIRYETLTDPSKL DSGKELHINLIPNKQDRTLT IVDTGIGMTKADLINNLGTI AKSGTKAFMEALQAGADISM IGQFGVGFYSAYLVAEKVTV ITKHNDDEQYAWESSAGGSF TVRTDTGEPMGRGTKVILHL KEDQTEYLEERRIKEIVKKH SQFIGYPITLFVEKERDKEV SDDEAE

Data sets:
Data typeCount
13C chemical shifts624
15N chemical shifts166
1H chemical shifts427

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 266 residues - 29934.477 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   ASNGLNTHRSERLEUTYRLYSLYSALAGLY
4   PHEGLUASNLEUTYRPHEGLNGLYASPGLN
5   PROMETGLUGLUGLUGLUVALGLUTHRPHE
6   ALAPHEGLNALAGLUILEALAGLNLEUMET
7   SERLEUILEILEASNTHRPHETYRSERASN
8   LYSGLUILEPHELEUARGGLULEUILESER
9   ASNSERSERASPALALEUASPLYSILEARG
10   TYRGLUTHRLEUTHRASPPROSERLYSLEU
11   ASPSERGLYLYSGLULEUHISILEASNLEU
12   ILEPROASNLYSGLNASPARGTHRLEUTHR
13   ILEVALASPTHRGLYILEGLYMETTHRLYS
14   ALAASPLEUILEASNASNLEUGLYTHRILE
15   ALALYSSERGLYTHRLYSALAPHEMETGLU
16   ALALEUGLNALAGLYALAASPILESERMET
17   ILEGLYGLNPHEGLYVALGLYPHETYRSER
18   ALATYRLEUVALALAGLULYSVALTHRVAL
19   ILETHRLYSHISASNASPASPGLUGLNTYR
20   ALATRPGLUSERSERALAGLYGLYSERPHE
21   THRVALARGTHRASPTHRGLYGLUPROMET
22   GLYARGGLYTHRLYSVALILELEUHISLEU
23   LYSGLUASPGLNTHRGLUTYRLEUGLUGLU
24   ARGARGILELYSGLUILEVALLYSLYSHIS
25   SERGLNPHEILEGLYTYRPROILETHRLEU
26   PHEVALGLULYSGLUARGASPLYSGLUVAL
27   SERASPASPGLUALAGLU

Samples:

sample_1: HSP90 alpha NTD, [U-15N; U-2H; 13C(1H)3 ALA-b, ILE-d1, LEU-d2, MET-e, THR-g, VAL-g2], 0.5 mM; Na+ 150 mM; Cl- 150 mM; TCEP 1 mM; HEPES, [U-2H], 20 mM

sample_2: HSP90 alpha NTD, [U-2; U-15N; LEU U-13C, U-2H, 13C(1H)3d2, 12C(2H)3d1; VAL U-13C, U-2H, 13C(1H)3g2, 12C(2H)3g1; ILE U-13C, U-2H, 13C(1H)3d1, 12C(2H)3g2] , 0.5 mM; Na+ 150 mM; Cl- 150 mM; TCEP 1 mM; HEPES, [U-2H], 20 mM

sample_3: HSP90 alpha NTD, [U-15N; THR U-13C; ALA U-13C], 0.5 mM; Na+ 150 mM; Cl- 150 mM; TCEP 1 mM; HEPES 20 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 bar; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCC-COSYsample_2isotropicsample_conditions_1
2D Methyl-TROSYsample_1isotropicsample_conditions_1
3D HCC-COSYsample_3isotropicsample_conditions_1
3D HC(C)C-COSYsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis v2.5.2, CCPN - chemical shift assignment

CcpNmr Analysis, CCPN - peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 950 MHz
  • Bruker AVANCE III HD 850 MHz
  • Bruker AVANCE III HD 600 MHz

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