BMRB Entry 18091
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18091
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Title: Solution structure of the yeast Sti1 DP2 domain PubMed: 22227520
Deposition date: 2011-11-17 Original release date: 2012-01-11
Authors: Schmid, Andreas; Lagleder, Stephan; Graewert, Melissa; Roehl, Alina; Hagn, Franz; Wandinger, Sebastian; Cox, Marc; Demmer, Oliver; Richter, Klaus; Groll, Michael; Kessler, Horst; Buchner, Johannes
Citation: Schmid, Andreas; Lagleder, Stephan; Grawert, Melissa Ann; Rohl, Alina; Hagn, Franz; Wandinger, Sebastian; Cox, Marc; Demmer, Oliver; Richter, Klaus; Groll, Michael; Kessler, Horst; Buchner, Johannes. "The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop." EMBO J. 31, 1506-1517 (2012).
Assembly members:
DP2, polymer, 71 residues, 7926.069 Da.
Natural source: Common Name: Baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
DP2: QPGTSNETPEETYQRAMKDP
EVAAIMQDPVMQSILQQAQQ
NPAALQEHMKNPEVFKKIQT
LIAAGIIRTGR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 307 |
15N chemical shifts | 76 |
1H chemical shifts | 516 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | DP2 | 1 |
Entities:
Entity 1, DP2 71 residues - 7926.069 Da.
1 | GLN | PRO | GLY | THR | SER | ASN | GLU | THR | PRO | GLU | ||||
2 | GLU | THR | TYR | GLN | ARG | ALA | MET | LYS | ASP | PRO | ||||
3 | GLU | VAL | ALA | ALA | ILE | MET | GLN | ASP | PRO | VAL | ||||
4 | MET | GLN | SER | ILE | LEU | GLN | GLN | ALA | GLN | GLN | ||||
5 | ASN | PRO | ALA | ALA | LEU | GLN | GLU | HIS | MET | LYS | ||||
6 | ASN | PRO | GLU | VAL | PHE | LYS | LYS | ILE | GLN | THR | ||||
7 | LEU | ILE | ALA | ALA | GLY | ILE | ILE | ARG | THR | GLY | ||||
8 | ARG |
Samples:
sample_1: DP2, [U-99% 13C; U-99% 15N], 0.5-3 mM; potassium chloride 50 mM; potassium phosphate 50 mM; sodium azide 0.2 w/v; H2O 95%; D2O 5%
sample_2: DP2 1 mM; potassium chloride 50 mM; potassium phosphate 50 mM; sodium azide 0.2 w/v; H2O 95%; D2O 5%
sample_3: DP2, [U-99% 15N], 0.5 mM; potassium chloride 50 mM; potassium phosphate 50 mM; sodium azide 0.2 w/v; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.35 M; pH: 7.5; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HNHB | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D CCH NOESY | sample_1 | isotropic | sample_conditions_1 |
3D CNH NOESY | sample_1 | isotropic | sample_conditions_1 |
3D NNH NOESY | sample_3 | isotropic | sample_conditions_1 |
2D HBCBCGCDHD | sample_1 | isotropic | sample_conditions_1 |
2D HBCBCGCDCEHE | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSCQ-IPAP | sample_3 | anisotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - peak picking
TALOS, Cornilescu, Delaglio and Bax - data analysis
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
ProcheckNMR, Laskowski and MacArthur - data analysis, geometry optimization
NMR spectrometers:
- Bruker Avance 900 MHz
- Bruker DMX 750 MHz
- Bruker DMX 600 MHz
Related Database Links:
PDB | |
DBJ | GAA26351 |
EMBL | CAA60743 CAA99217 |
GB | AAA35121 AHY77333 AJP41564 AJT70985 AJT71475 |
REF | NP_014670 |
SP | P15705 |
TPG | DAA10809 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts