BMRB Entry 11473
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11473
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Title: Solution structure of the CERT PH domain PubMed: 22869376
Deposition date: 2012-02-25 Original release date: 2012-08-13
Authors: Sugiki, Toshihiko; Takeuchi, Koh; Tokunaga, Yuji; Kumagai, Keigo; Kawano, Miyuki; Nishijima, Masahiro; Hanada, Kentaro; Takahashi, Hideo; Shimada, Ichio
Citation: Sugiki, Toshihiko; Takeuchi, Koh; Tokunaga, Yuji; Terasawa, Hiroaki; Kumagai, Keigo; Kawano, Miyuki; Nishijima, Masahiro; Hanada, Kentaro; Takahashi, Hideo; Shimada, Ichio. "Structural basis for the Golgi-association by the pleckstrin homology domain of the ceramide trafficking protein CERT" J. Biol. Chem. ., .-. (2012).
Assembly members:
CERT, polymer, 94 residues, 11180.480 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):
CERT: VERCGVLSKWTNYIHGWQDR
WVVLKNNALSYYKSEDETEY
GCRGSICLSKAVITPHDFDE
CRFDISVNDSVWYLRAQDPD
HRQQWIDAIEQHKT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 369 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 587 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CERT PH domain | 1 |
Entities:
Entity 1, CERT PH domain 94 residues - 11180.480 Da.
| 1 | VAL | GLU | ARG | CYS | GLY | VAL | LEU | SER | LYS | TRP | ||||
| 2 | THR | ASN | TYR | ILE | HIS | GLY | TRP | GLN | ASP | ARG | ||||
| 3 | TRP | VAL | VAL | LEU | LYS | ASN | ASN | ALA | LEU | SER | ||||
| 4 | TYR | TYR | LYS | SER | GLU | ASP | GLU | THR | GLU | TYR | ||||
| 5 | GLY | CYS | ARG | GLY | SER | ILE | CYS | LEU | SER | LYS | ||||
| 6 | ALA | VAL | ILE | THR | PRO | HIS | ASP | PHE | ASP | GLU | ||||
| 7 | CYS | ARG | PHE | ASP | ILE | SER | VAL | ASN | ASP | SER | ||||
| 8 | VAL | TRP | TYR | LEU | ARG | ALA | GLN | ASP | PRO | ASP | ||||
| 9 | HIS | ARG | GLN | GLN | TRP | ILE | ASP | ALA | ILE | GLU | ||||
| 10 | GLN | HIS | LYS | THR |
Samples:
sample_1: CERT, [U-98% 15N], 0.2 mM; HEPES 10 mM; sodium chloride 100 mM; DTT 5 mM; H2O 93%; D2O 7%
sample_2: CERT, [U-98% 13C; U-98% 15N], 0.2 mM; HEPES 10 mM; sodium chloride 100 mM; DTT 5 mM; H2O 93%; D2O 7%
sample_conditions_1: pH: 7.20; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C 15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAC03762 BAF84776 BAG53379 BAI45568 |
| EMBL | CAH92584 |
| GB | AAD30288 AAG42046 AAG42047 AAG42049 AAH00102 |
| REF | NP_001102405 NP_001123577 NP_001126514 NP_001230955 NP_005704 |
| SP | Q5R6M6 Q6VVX2 Q9GKI7 Q9Y5P4 |
| TPG | DAA25918 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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or all simulated shifts