BMRB Entry 16378
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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/BMR16378
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Title: Chemical shift assignment of GtR34C from Geobacillus thermodenitrificans. North East Structural Genomics Consortium Target GtR34C
Deposition date: 2009-06-29 Original release date: 2009-07-07
Authors: Lee, Hsiau-Wei; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, GVT; Evertt, John; Montelione, Gaetano; Prestegard, James
Citation: Lee, Hsiau-Wei; Montelione, Gaetano; Prestegard, James. "Solution Structure of GtR34C" Not known ., .-..
Assembly members:
GtR34C, polymer, 174 residues, 19278.225 Da.
Natural source: Common Name: Geobacillus thermodenitrificans Taxonomy ID: 33940 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacillus thermodenitrificans
Experimental source: Production method: recombinant technology Host organism: Geobacillus thermodenitrificans
Entity Sequences (FASTA):
GtR34C: MNEAKGVYVMSVLPNMPAAG
RLEAGDRIAAIDGQPINTSE
QIVSYVREKQAGDRVRVTFI
RDRKQHEAELVLKPFPHHPN
QIGLGVTMNEAKGVYVMSVL
PNMPAAGRLEAGDRIAAIDG
QPINTSEQIVSYVREKQAGD
RVRVTFIRDRKQHEAELVLK
PFPHHPNQIGLGVT
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 324 |
| 15N chemical shifts | 76 |
| 1H chemical shifts | 523 |
| residual dipolar couplings | 125 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GtR34C | 1 |
Entities:
Entity 1, GtR34C 174 residues - 19278.225 Da.
LEHHHHHH are at the C-terminal as part of Hig-Tag. It is not included in the coordinate file.
| 1 | MET | ASN | GLU | ALA | LYS | GLY | VAL | TYR | VAL | MET | ||||
| 2 | SER | VAL | LEU | PRO | ASN | MET | PRO | ALA | ALA | GLY | ||||
| 3 | ARG | LEU | GLU | ALA | GLY | ASP | ARG | ILE | ALA | ALA | ||||
| 4 | ILE | ASP | GLY | GLN | PRO | ILE | ASN | THR | SER | GLU | ||||
| 5 | GLN | ILE | VAL | SER | TYR | VAL | ARG | GLU | LYS | GLN | ||||
| 6 | ALA | GLY | ASP | ARG | VAL | ARG | VAL | THR | PHE | ILE | ||||
| 7 | ARG | ASP | ARG | LYS | GLN | HIS | GLU | ALA | GLU | LEU | ||||
| 8 | VAL | LEU | LYS | PRO | PHE | PRO | HIS | HIS | PRO | ASN | ||||
| 9 | GLN | ILE | GLY | LEU | GLY | VAL | THR | MET | ASN | GLU | ||||
| 10 | ALA | LYS | GLY | VAL | TYR | VAL | MET | SER | VAL | LEU | ||||
| 11 | PRO | ASN | MET | PRO | ALA | ALA | GLY | ARG | LEU | GLU | ||||
| 12 | ALA | GLY | ASP | ARG | ILE | ALA | ALA | ILE | ASP | GLY | ||||
| 13 | GLN | PRO | ILE | ASN | THR | SER | GLU | GLN | ILE | VAL | ||||
| 14 | SER | TYR | VAL | ARG | GLU | LYS | GLN | ALA | GLY | ASP | ||||
| 15 | ARG | VAL | ARG | VAL | THR | PHE | ILE | ARG | ASP | ARG | ||||
| 16 | LYS | GLN | HIS | GLU | ALA | GLU | LEU | VAL | LEU | LYS | ||||
| 17 | PRO | PHE | PRO | HIS | HIS | PRO | ASN | GLN | ILE | GLY | ||||
| 18 | LEU | GLY | VAL | THR |
Samples:
sample_1: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; H2O 95%; D2O 5%
PEG: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; C12E5 PEG/Hexanol 4.2%; H2O 95%; D2O 5%
GEL: GtR34C, [U-100% 13C; U-100% 15N], 1.14 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; Negatively Charged Compressed Polyacrylamide Gel 7%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: ambient atm; temperature: 298 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 C(CO)NH | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | 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-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N HSQCTROSY | PEG | isotropic | sample_conditions_1 |
| 2D 15N HSQCTROSY | GEL | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement
SPARKY, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - data analysis
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts