BMRB Entry 25740
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25740
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Title: C-terminal domain of Cdc37 cochaperone PubMed: 26400850
Deposition date: 2015-08-02 Original release date: 2015-10-05
Authors: Keramisanou, Dimitra; Dudhat, Amit; Pare, Michael
Citation: Zhang, Ziming; Keramisanou, Dimitra; Dudhat, Amit; Pare, Michael; Gelis, Ioannis. "The C-terminal domain of human Cdc37 studied by solution NMR" J. Biomol. NMR 63, 315-321 (2015).
Assembly members:
Cdc37, polymer, 94 residues, 10197.445 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
Entity Sequences (FASTA):
Cdc37: GHMGPGGLDPVEVYESLPEE
LQKCFDVKDVQMLQDAISKM
DPTDAKYHMQRCIDSGLWVP
NSKASEAKEGEEAGPGDPLL
EAVPKTGDEKDVSV
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 351 |
15N chemical shifts | 86 |
1H chemical shifts | 583 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Cdc37 | 1 |
Entities:
Entity 1, Cdc37 94 residues - 10197.445 Da.
Residues 285-287 represent a non-native fragment after removal of purification tag
1 | GLY | HIS | MET | GLY | PRO | GLY | GLY | LEU | ASP | PRO | ||||
2 | VAL | GLU | VAL | TYR | GLU | SER | LEU | PRO | GLU | GLU | ||||
3 | LEU | GLN | LYS | CYS | PHE | ASP | VAL | LYS | ASP | VAL | ||||
4 | GLN | MET | LEU | GLN | ASP | ALA | ILE | SER | LYS | MET | ||||
5 | ASP | PRO | THR | ASP | ALA | LYS | TYR | HIS | MET | GLN | ||||
6 | ARG | CYS | ILE | ASP | SER | GLY | LEU | TRP | VAL | PRO | ||||
7 | ASN | SER | LYS | ALA | SER | GLU | ALA | LYS | GLU | GLY | ||||
8 | GLU | GLU | ALA | GLY | PRO | GLY | ASP | PRO | LEU | LEU | ||||
9 | GLU | ALA | VAL | PRO | LYS | THR | GLY | ASP | GLU | LYS | ||||
10 | ASP | VAL | SER | VAL |
Samples:
sample_1: Cdc37, [U-100% 13C; U-100% 15N], 0.3 0.5 mM; sodium chloride 100 mM; HEPES 50 mM; D2O, [U-100% 2H], 7%; H2O 93%; DTT 2 mM
sample_2: Cdc37, [U-100% 15N], 0.3 0.5 mM; sodium chloride 100 mM; HEPES 50 mM; D2O, [U-2H], 7%; H2O 93%; DTT 2 mM
sample_3: Cdc37, [U-10% 13C; U-100% 15N], 0.3 0.5 mM; sodium chloride 100 mM; HEPES 5 mM; D2O, [U-2H], 7%; H2O 93%; DTT 2 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aliphatic | sample_3 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Varian VNMRS 800 MHz
- Varian VNMRS 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts