BMRB Entry 19987
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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/BMR19987
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Title: Characterization and structure of the MIT1 domain of a chitin synthase from the Oomycete Saprolegnia monoica
Deposition date: 2014-05-27 Original release date: 2015-05-26
Authors: Bulone, Vincent; Szpryngiel, Scarlett; Brown, Christian; Ye, Weihua
Citation: Bulone, Vincent; Maler, Lena; Brown, Christian; Szpryngiel, Scarlett; KUANG, Guanglin; SRIVASTAVA, Vaibhav; Ye, Weihua; Tu, Yaoquan. "Characterization and structure of the MIT domains of two chitin synthases from the Oomycete Saprolegnia monoica" Biochem. J. ., .-..
Assembly members:
SmChs_MIT1, polymer, 74 residues, 8527.742 Da.
Natural source: Common Name: oomycetes Taxonomy ID: 37553 Superkingdom: Eukaryota Kingdom: not available Genus/species: Saprolegnia monoica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SmChs_MIT1: MGTIDDAFRAIERAIQAENE
GRYREALKHFLDGGEMIVTA
AEKEASQKVRNLLLHKGKEV
LEWAEHLAEWILEH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 278 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 494 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SmChs MIT1 | 1 |
Entities:
Entity 1, SmChs MIT1 74 residues - 8527.742 Da.
| 1 | MET | GLY | THR | ILE | ASP | ASP | ALA | PHE | ARG | ALA | ||||
| 2 | ILE | GLU | ARG | ALA | ILE | GLN | ALA | GLU | ASN | GLU | ||||
| 3 | GLY | ARG | TYR | ARG | GLU | ALA | LEU | LYS | HIS | PHE | ||||
| 4 | LEU | ASP | GLY | GLY | GLU | MET | ILE | VAL | THR | ALA | ||||
| 5 | ALA | GLU | LYS | GLU | ALA | SER | GLN | LYS | VAL | ARG | ||||
| 6 | ASN | LEU | LEU | LEU | HIS | LYS | GLY | LYS | GLU | VAL | ||||
| 7 | LEU | GLU | TRP | ALA | GLU | HIS | LEU | ALA | GLU | TRP | ||||
| 8 | ILE | LEU | GLU | HIS |
Samples:
sample_1: SmChs_MIT1, [U-100% 13C; U-100% 15N], 0.3 – 1.0 mM; D2O 10%; sodium phosphate 50 mM; sodium chloride 150 mM; H2O 90%
sample_conditions_1: ionic strength: 200 mM; pH: 5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection, processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
ProcheckNMR, Laskowski and MacArthur - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts