BMRB Entry 17029
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17029
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Title: 1H, 15N and 13C assignments for the potential GTPase binding domain of dictyostelium discoideum Fomin C PubMed: 21846933
Deposition date: 2010-06-30 Original release date: 2011-10-28
Authors: Dames, Sonja; Schoenichen, Andre; Stephan, Grzesiek; Geyer, Matthias
Citation: Dames, Sonja; Junemann, Alexander; Sass, Hans; Schonichen, Andre; Stopschinski, Barbara; Grzesiek, Stephan; Faix, Jan; Geyer, Matthias. "Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C." J. Biol. Chem. 286, 36907-36920 (2011).
Assembly members:
formin_C, polymer, 107 residues, 12057.7 Da.
Natural source: Common Name: Dictyostelium discoideum Taxonomy ID: 44689 Superkingdom: Eukaryota Kingdom: not available Genus/species: Dictyostelium discoideum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
formin_C: GAHMGGSMKIRVELINGNEH
RTSSTPQQPQQNPSVSHIFD
GETAVKDHIKVLLTHFKIPV
DKVSSYALQNPFTLAYVEDS
FLTPERLVEAEKSYFILRMK
PHAIADR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 482 |
15N chemical shifts | 111 |
1H chemical shifts | 782 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | formin C | 1 |
Entities:
Entity 1, formin C 107 residues - 12057.7 Da.
1 | GLY | ALA | HIS | MET | GLY | GLY | SER | MET | LYS | ILE | ||||
2 | ARG | VAL | GLU | LEU | ILE | ASN | GLY | ASN | GLU | HIS | ||||
3 | ARG | THR | SER | SER | THR | PRO | GLN | GLN | PRO | GLN | ||||
4 | GLN | ASN | PRO | SER | VAL | SER | HIS | ILE | PHE | ASP | ||||
5 | GLY | GLU | THR | ALA | VAL | LYS | ASP | HIS | ILE | LYS | ||||
6 | VAL | LEU | LEU | THR | HIS | PHE | LYS | ILE | PRO | VAL | ||||
7 | ASP | LYS | VAL | SER | SER | TYR | ALA | LEU | GLN | ASN | ||||
8 | PRO | PHE | THR | LEU | ALA | TYR | VAL | GLU | ASP | SER | ||||
9 | PHE | LEU | THR | PRO | GLU | ARG | LEU | VAL | GLU | ALA | ||||
10 | GLU | LYS | SER | TYR | PHE | ILE | LEU | ARG | MET | LYS | ||||
11 | PRO | HIS | ALA | ILE | ALA | ASP | ARG |
Samples:
sample_1: forC/ A, [U-100% 15N], 1.0 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%
sample_2: forC/ A, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%
sample_3: forC/ A, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2%
sample_4: forC/ A, [U-100% 13C; U-100% 15N], 0.8 mM; potassium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.2 % v/v; C12E5 8.6 % w/v; hexanol 2 % v/v
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
3D HNCA | sample_2 | isotropic | sample_conditions_1 |
3D CCONH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D CBCANH | sample_2 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D HNHB | sample_1 | isotropic | sample_conditions_1 |
3D HACAHB-COSY | sample_2 | isotropic | sample_conditions_1 |
3D HNCO | sample_2 | isotropic | sample_conditions_1 |
2D 13C-{13CO}-1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 13C-{15N}-1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_3 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC-IPAP | sample_4 | isotropic | sample_conditions_1 |
3D HN(CO)CA_Jcaha | sample_4 | isotropic | sample_conditions_1 |
3D HN(CO)CA_Jcacb | sample_4 | isotropic | sample_conditions_1 |
{1H}-15N-NOE | sample_1 | isotropic | sample_conditions_1 |
15N-T1 | sample_1 | isotropic | sample_conditions_1 |
15N-T2 | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_3 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts