BMRB Entry 16746
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16746
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Title: Chemical shift assignment of GmR58A from Geobacter metallireducens. Northeast Structural Genomics Consortium Target GmR58A
Deposition date: 2010-02-28 Original release date: 2010-03-31
Authors: Lee, Hsiau-Wei; Wang, Huang; Buchwald, William; Janjua, Haleema; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James
Citation: Lee, Hsiau-Wei; Montelione, Gaetano; Prestegard, James. "Solution Structure of GmR58A" Not known ., .-..
Assembly members:
GmR58A, polymer, 122 residues, 13133.925 Da.
Natural source: Common Name: Geobacter metallireducens Taxonomy ID: 28232 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacter metallireducens
Experimental source: Production method: recombinant technology Host organism: Geobacter metallireducens
Entity Sequences (FASTA):
GmR58A: MDLPITLSKETPFEGEEITV
SARVTNRGAAEAHNVPVAVY
LGNPAQGGVEIGRDTISRIP
VGGTGLARVQWKATRKLAGR
AANPGVPVYAVVDPDNRVAE
SDKANNVFSRIVKVLEHHHH
HH
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 451 |
| 15N chemical shifts | 107 |
| 1H chemical shifts | 717 |
| residual dipolar couplings | 155 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GmR58A | 1 |
Entities:
Entity 1, GmR58A 122 residues - 13133.925 Da.
LEHHHHHH are at the C-terminal as part of Hig-Tag
| 1 | MET | ASP | LEU | PRO | ILE | THR | LEU | SER | LYS | GLU | ||||
| 2 | THR | PRO | PHE | GLU | GLY | GLU | GLU | ILE | THR | VAL | ||||
| 3 | SER | ALA | ARG | VAL | THR | ASN | ARG | GLY | ALA | ALA | ||||
| 4 | GLU | ALA | HIS | ASN | VAL | PRO | VAL | ALA | VAL | TYR | ||||
| 5 | LEU | GLY | ASN | PRO | ALA | GLN | GLY | GLY | VAL | GLU | ||||
| 6 | ILE | GLY | ARG | ASP | THR | ILE | SER | ARG | ILE | PRO | ||||
| 7 | VAL | GLY | GLY | THR | GLY | LEU | ALA | ARG | VAL | GLN | ||||
| 8 | TRP | LYS | ALA | THR | ARG | LYS | LEU | ALA | GLY | ARG | ||||
| 9 | ALA | ALA | ASN | PRO | GLY | VAL | PRO | VAL | TYR | ALA | ||||
| 10 | VAL | VAL | ASP | PRO | ASP | ASN | ARG | VAL | ALA | GLU | ||||
| 11 | SER | ASP | LYS | ALA | ASN | ASN | VAL | PHE | SER | ARG | ||||
| 12 | ILE | VAL | LYS | VAL | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 13 | HIS | HIS |
Samples:
NC_Sample: GmR58A, [U-100% 13C; U-100% 15N], 0.77 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; H2O 95%; D2O 5%
PEG: GmR58A, [U-100% 13C; U-100% 15N], 0.65 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; C12E5 4.2%; H2O 95%; D2O 5%
Negative_Gel: GmR58A, [U-100% 13C; U-100% 15N], 0.65 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%
Stretch_Gel: GmR58A, [U-100% 13C; U-100% 15N], 0.65 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; Neutral stretched polyacrylamide gel 5%; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC_Sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC_Sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC_Sample | isotropic | sample_conditions_1 |
| 3D HNCO | NC_Sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_Sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC_Sample | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | NC_Sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_Sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC_Sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_Sample | isotropic | sample_conditions_1 |
| NH J-modulation | PEG | anisotropic | sample_conditions_1 |
| NH J-modulation | Negative_Gel | anisotropic | sample_conditions_1 |
| NH J-modulation | Stretch_Gel | anisotropic | 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 v3.115, 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