BMRB Entry 36775
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36775
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Xu, Zhe; Singkaravanit-Ogawa, Suthitar; Takano, Yoshitaka; Ohki, Shinya. "Identification and NMR-based structural characterization of the functional domain of EPC3, a virulence effector of the phytopathogenic fungus Colletotrichum orbiculare." Front. Plant Sci. 16, 1691993-1691993 (2025).
PubMed: 41140374
Assembly members:
EPC3, polymer, 68 residues, 7783.827 Da.
Natural source: Common Name: not available Taxonomy ID: 5465 Superkingdom: not available Kingdom: Fungi Genus/species: Colletotrichum orbiculare
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
EPC3: GPDRTCPAGQTYDRSVCYKY
NTIRRFCVANPRSNREDIKN
TPCRADEICVQRNLSNGKSF
AQCIELVK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 188 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 400 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 68 residues - 7783.827 Da.
| 1 | GLY | PRO | ASP | ARG | THR | CYS | PRO | ALA | GLY | GLN | ||||
| 2 | THR | TYR | ASP | ARG | SER | VAL | CYS | TYR | LYS | TYR | ||||
| 3 | ASN | THR | ILE | ARG | ARG | PHE | CYS | VAL | ALA | ASN | ||||
| 4 | PRO | ARG | SER | ASN | ARG | GLU | ASP | ILE | LYS | ASN | ||||
| 5 | THR | PRO | CYS | ARG | ALA | ASP | GLU | ILE | CYS | VAL | ||||
| 6 | GLN | ARG | ASN | LEU | SER | ASN | GLY | LYS | SER | PHE | ||||
| 7 | ALA | GLN | CYS | ILE | GLU | LEU | VAL | LYS |
Samples:
sample_1: 13C_15N_sample, [U-100% 13C; U-100% 15N], 800 uM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY, Lee, Tonelli, Markley - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
NMR spectrometers:
- Bruker AVANCE III 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks