BMRB Entry 34759
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
BMRB Entry DOI: doi:10.13018/BMR34759
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Human HSP90 alpha ATP Binding Domain, ATP-lid closed conformation, R46A PubMed: 36494347
Deposition date: 2022-09-30 Original release date: 2022-11-08
Authors: Rioual, E.; Henot, F.; Favier, A.; Macek, P.; Crublet, E.; Josso, P.; Brustcher, B.; Frech, M.; Gans, P.; Loison, C.; Boisbouvier, J.
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).
Assembly members:
entity_1, polymer, 266 residues, 29934.477 Da.
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 BL21(DE3) Vector: pET-28
Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH
NQTSLYKKAGFENLYFQGDQ
PMEEEEVETFAFQAEIAQLM
SLIINTFYSNKEIFLRELIS
NSSDALDKIRYETLTDPSKL
DSGKELHINLIPNKQDRTLT
IVDTGIGMTKADLINNLGTI
AKSGTKAFMEALQAGADISM
IGQFGVGFYSAYLVAEKVTV
ITKHNDDEQYAWESSAGGSF
TVRTDTGEPMGRGTKVILHL
KEDQTEYLEERRIKEIVKKH
SQFIGYPITLFVEKERDKEV
SDDEAE
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 624 |
| 15N chemical shifts | 166 |
| 1H chemical shifts | 427 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 266 residues - 29934.477 Da.
| 1 | MET | GLY | SER | SER | HIS | HIS | HIS | HIS | HIS | HIS | ||||
| 2 | SER | SER | GLY | LEU | VAL | PRO | ARG | GLY | SER | HIS | ||||
| 3 | ASN | GLN | THR | SER | LEU | TYR | LYS | LYS | ALA | GLY | ||||
| 4 | PHE | GLU | ASN | LEU | TYR | PHE | GLN | GLY | ASP | GLN | ||||
| 5 | PRO | MET | GLU | GLU | GLU | GLU | VAL | GLU | THR | PHE | ||||
| 6 | ALA | PHE | GLN | ALA | GLU | ILE | ALA | GLN | LEU | MET | ||||
| 7 | SER | LEU | ILE | ILE | ASN | THR | PHE | TYR | SER | ASN | ||||
| 8 | LYS | GLU | ILE | PHE | LEU | ARG | GLU | LEU | ILE | SER | ||||
| 9 | ASN | SER | SER | ASP | ALA | LEU | ASP | LYS | ILE | ARG | ||||
| 10 | TYR | GLU | THR | LEU | THR | ASP | PRO | SER | LYS | LEU | ||||
| 11 | ASP | SER | GLY | LYS | GLU | LEU | HIS | ILE | ASN | LEU | ||||
| 12 | ILE | PRO | ASN | LYS | GLN | ASP | ARG | THR | LEU | THR | ||||
| 13 | ILE | VAL | ASP | THR | GLY | ILE | GLY | MET | THR | LYS | ||||
| 14 | ALA | ASP | LEU | ILE | ASN | ASN | LEU | GLY | THR | ILE | ||||
| 15 | ALA | LYS | SER | GLY | THR | LYS | ALA | PHE | MET | GLU | ||||
| 16 | ALA | LEU | GLN | ALA | GLY | ALA | ASP | ILE | SER | MET | ||||
| 17 | ILE | GLY | GLN | PHE | GLY | VAL | GLY | PHE | TYR | SER | ||||
| 18 | ALA | TYR | LEU | VAL | ALA | GLU | LYS | VAL | THR | VAL | ||||
| 19 | ILE | THR | LYS | HIS | ASN | ASP | ASP | GLU | GLN | TYR | ||||
| 20 | ALA | TRP | GLU | SER | SER | ALA | GLY | GLY | SER | PHE | ||||
| 21 | THR | VAL | ARG | THR | ASP | THR | GLY | GLU | PRO | MET | ||||
| 22 | GLY | ARG | GLY | THR | LYS | VAL | ILE | LEU | HIS | LEU | ||||
| 23 | LYS | GLU | ASP | GLN | THR | GLU | TYR | LEU | GLU | GLU | ||||
| 24 | ARG | ARG | ILE | LYS | GLU | ILE | VAL | LYS | LYS | HIS | ||||
| 25 | SER | GLN | PHE | ILE | GLY | TYR | PRO | ILE | THR | LEU | ||||
| 26 | PHE | VAL | GLU | LYS | GLU | ARG | ASP | LYS | GLU | VAL | ||||
| 27 | SER | ASP | ASP | GLU | ALA | GLU |
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-15N; U-2H; 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: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCC-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D Methyl-TROSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCC-COSY | sample_3 | isotropic | sample_conditions_1 |
| 3D HC(C)C-COSY | sample_2 | isotropic | sample_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, 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 shifts
SPARKY: Backbone
or all simulated shifts