BMRB Entry 19318
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19318
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Title: Chemical shifts of the CPAP-interacting epitope of Danio rerio STIL PubMed: 24076405
Deposition date: 2013-06-24 Original release date: 2013-09-13
Authors: Hatzopoulos, Georgios; Vakonakis, Ioannis
Citation: Hatzopoulos, Georgios; Erat, Michele; Cutts, Erin; Rogala, Kacper; Slater, Leanne; Stansfeld, Philip; Vakonakis, Ioannis. "Structural Analysis of the G-Box Domain of the Microcephaly Protein CPAP Suggests a Role in Centriole Architecture." Structure 21, 2069-2077 (2013).
Assembly members:
drSTIL_N6, polymer, 60 residues, Formula weight is not available
Natural source: Common Name: Zebra fish Taxonomy ID: 7955 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Danio rerio
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
drSTIL_N6: GPLGSCYQNKLSISDHDSGV
EDEDLSPRPSPNPHPVSQQT
KRVHPLVPELSMVLDGSFLD
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 172 |
15N chemical shifts | 50 |
1H chemical shifts | 112 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | drSTIL | 1 |
Entities:
Entity 1, drSTIL 60 residues - Formula weight is not available
Residues 1-7 represent a cloning artifact
1 | GLY | PRO | LEU | GLY | SER | CYS | TYR | GLN | ASN | LYS | |
2 | LEU | SER | ILE | SER | ASP | HIS | ASP | SER | GLY | VAL | |
3 | GLU | ASP | GLU | ASP | LEU | SER | PRO | ARG | PRO | SER | |
4 | PRO | ASN | PRO | HIS | PRO | VAL | SER | GLN | GLN | THR | |
5 | LYS | ARG | VAL | HIS | PRO | LEU | VAL | PRO | GLU | LEU | |
6 | SER | MET | VAL | LEU | ASP | GLY | SER | PHE | LEU | ASP |
Samples:
sample_1: drSTIL_N6, [U-98% 13C; U-98% 15N], 0.25 mM; DSS 0.05 mM; sodium chloride 0.15 mM; sodium phosphate 0.02 mM; sodium azide 0.01%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.21 M; pH: 7; pressure: 1 atm; temperature: 273 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HCACO | sample_1 | isotropic | sample_conditions_1 |
3D HCA(CO)N | sample_1 | isotropic | sample_conditions_1 |
3D HBHANH | sample_1 | isotropic | sample_conditions_1 |
Software:
Omega Spectrometer Operating Software vBeta 6.03b2, General Electric - collection
NMRPipe v2.4 Rev 2006.095.11.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PIPP v4.3.7, Garrett - data analysis
NMR spectrometers:
- GE OMEGA PSG 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts