BMRB Entry 36797

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36797
MolProbity Validation Chart

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Title:
the closed-form Hsp90a NTD
Deposition date:
2025-10-16
Original release date:
2026-02-12
Authors:
Wan, C.
Citation:

Citation: Wan, C.; Huang, C.. "Phosphorylation regulates Hsp90's ATPase activity"  .

Assembly members:

Assembly members:
Heat shock protein HSP 90-alpha, polymer, 237 residues, 26730.887 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Heat shock protein HSP 90-alpha: MPEETQTQDQPMEEEEVETF AFQAEIAQLMSLIINTFYSN KEIFLRELISNSSDALDKIR YESLTDPSKLDSGKELHINL IPNKQDRTLTIVDTGIGMTK ADLINNLGTIAKSGTKAFME ALQAGADISMIGQFGVGFYS AYLVAEKVTVITKHNDDEQY AWESSAGGSFTVRTDTGEPM GRGTKVILHLKEDQTEYLEE RRIKEIVKKHSQFIGYPITL FVEKERDKEVSDDEAEE

Data sets:
Data typeCount
13C chemical shifts112
1H chemical shifts336

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 237 residues - 26730.887 Da.

1   METPROGLUGLUTHRGLNTHRGLNASPGLN
2   PROMETGLUGLUGLUGLUVALGLUTHRPHE
3   ALAPHEGLNALAGLUILEALAGLNLEUMET
4   SERLEUILEILEASNTHRPHETYRSERASN
5   LYSGLUILEPHELEUARGGLULEUILESER
6   ASNSERSERASPALALEUASPLYSILEARG
7   TYRGLUSERLEUTHRASPPROSERLYSLEU
8   ASPSERGLYLYSGLULEUHISILEASNLEU
9   ILEPROASNLYSGLNASPARGTHRLEUTHR
10   ILEVALASPTHRGLYILEGLYMETTHRLYS
11   ALAASPLEUILEASNASNLEUGLYTHRILE
12   ALALYSSERGLYTHRLYSALAPHEMETGLU
13   ALALEUGLNALAGLYALAASPILESERMET
14   ILEGLYGLNPHEGLYVALGLYPHETYRSER
15   ALATYRLEUVALALAGLULYSVALTHRVAL
16   ILETHRLYSHISASNASPASPGLUGLNTYR
17   ALATRPGLUSERSERALAGLYGLYSERPHE
18   THRVALARGTHRASPTHRGLYGLUPROMET
19   GLYARGGLYTHRLYSVALILELEUHISLEU
20   LYSGLUASPGLNTHRGLUTYRLEUGLUGLU
21   ARGARGILELYSGLUILEVALLYSLYSHIS
22   SERGLNPHEILEGLYTYRPROILETHRLEU
23   PHEVALGLULYSGLUARGASPLYSGLUVAL
24   SERASPASPGLUALAGLUGLU

Samples:

sample_1: Hsp90a NTD, [U-100% 15N], 300 uM; PBS 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: Hsp90a NTD, [U-100% 13C; U-100% 15N], 300 uM; PBS 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_3: Hsp90a NTD, [U-100% 13C Leu,Thr,Val,Ala,Ile,Met], 300 uM; PBS 50 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment

NMRFAM-SPARKY, Lee W, Tonelli M, Markley JL - peak picking

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 850 MHz