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 50786

Title: N-terminal domain of human HSP90 alpha1 form   PubMed: 34041691

Deposition date: 2021-02-23 Original release date: 2021-05-27

Authors: Henot, Faustine; Kerfah, Rime; Gans, Pierre; Boisbouvier, Jerome

Citation: Henot, Faustine; Kerfah, Rime; Torner, Ricarda; Macek, Pavel; Crublet, Elodie; Gans, Pierre; Frech, Matthias; Hamelin, Olivier; Boisbouvier, Jerome. "Optimized precursor to simplify assignment transfer between backbone resonances and stereospecifically labelled valine and leucine methyl groups: application to human Hsp90 N-terminal domain"  J. Biomol. NMR ., .-. (2021).

Assembly members:
entity_1, polymer, 236 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
entity_1: FENLYFQGDQPMEEEEVETF AFQAEIAQLMSLIINTFYSN KEIFLRELISNSSDALDKIR YESLTDPSKLDSGKELHINL IPNKQDRTLTIVDTGIGMTK ADLINNLGTIAKSGTKAFME ALQAGADISMIGQFGVGFYS AYLVAEKVTVITKHNDDEQY AWESSAGGSFTVRTDTGEPM GRGTKVILHLKEDQTEYLEE RRIKEIVKKHSQFIGYPITL FVEKERDKEVSDDEAE

Data sets:
Data typeCount
13C chemical shifts626
15N chemical shifts167
1H chemical shifts428

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain1

Entities:

Entity 1, N-terminal domain 236 residues - Formula weight is not available

1   PHEGLUASNLEUTYRPHEGLNGLYASPGLN
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   SERASPASPGLUALAGLU

Samples:

sample_1: N-terminal domain of HSP90-alpha, [U-100% 13C; U-100% 15N; U-80% 2H], 0.5 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_2: TCEP 1 mM; HEPES 20 mM; sodium chloride 150 mM; N-terminal domain of HSP90-alpha, U-[2H, 15N, 12C], Ala-[13C1H3]b, Met-[13C1H3]e, Leu/Val-[13C1H3]proS, Ile-[13C1H3]d1, Thr-[13C1H3]g, 0.5 mM

sample_3: N-terminal domain of HSP90-alpha, U-[2H, 15N, 13C], Val-[1,2,3-13C, 13C1H3-proS], Leu-[1,2,3,4-13C, 13C1H3-proS], Ile-[1,2,3,4-13C, 13C1H3- d1], 0.5 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_4: N-terminal domain of HSP90-alpha, U-[2H, 15N, 12C]-Ala-[13C1H3]b, 0.15 – 0.18 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_5: N-terminal domain of HSP90-alpha, U-[2H, 15N, 12C]-Met-[13C1H3]e, 0.07 – 0.38 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_6: N-terminal domain of HSP90-alpha, U-[2H, 15N, 12C]-Ile-[13C1H3]d1, 0.17 – 0.41 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_8: N-terminal domain of HSP90-alpha, U-[2H, 15N, 12C]-Thr-[13C1H3]g, 0.11 – 0.35 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_9: N-terminal domain of HSP90-alpha, U-[2H, 15N, 12C]-Leu/Val-[13C1H3]proS, 0.1 – 0.28 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.15 M; pH*: 7.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)CBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D 1H-13C HMQCsample_2isotropicsample_conditions_2
3D CCH HMQC-NOESY-HMQCsample_2isotropicsample_conditions_2
2D 1H-13C HMQCsample_3isotropicsample_conditions_2
3D HCCsample_3isotropicsample_conditions_2
3D HC(C)Csample_3isotropicsample_conditions_2
3D HC(CC)Csample_3isotropicsample_conditions_2
2D 1H-13C HMQCsample_4isotropicsample_conditions_2
2D 1H-13C HMQCsample_5isotropicsample_conditions_2
2D 1H-13C HMQCsample_6isotropicsample_conditions_2
2D 1H-13C HMQCsample_8isotropicsample_conditions_2
2D 1H-13C HMQCsample_9isotropicsample_conditions_2

Software:

TOPSPIN v3.5 - collection

NMRPipe - processing

CcpNMR v2 - data analysis

MAGIC - methyl assignment

NMR spectrometers:

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

Related Database Links:

UNIPROT P07900

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