BMRB Entry 15844
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15844
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Title: NMR Solution Structure of a Thiamine Biosynthesis Protein from Geobacter Metallireducens: Northeast Structural Genomics Consortium Target GmR137
Deposition date: 2008-06-30 Original release date: 2008-08-25
Authors: Mani, Rajeswari; Wang, Huang; Jiang, Mei; Magliaqui, Melissa; Xiao, Rong; Nair, Rajesh; Baran, Michael; G., Swapna; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Mani, Rajeswari; Wang, Huang; Jiang, Mei; Magliaqui, Melissa; Xiao, Rong; Nair, Rajesh; Baran, Michael; G., Swapna; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "NMR Solution Structure of a Thiamine Biosynthesis Protein from Geobacter Metallireducens: Northeast Structural Genomics Consortium Target GmR137" Not known ., .-..
Assembly members:
GmR137, polymer, 78 residues, 8530.543 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: Escherichia coli
Entity Sequences (FASTA):
GmR137: MNLTVNGKPSTVDGAESLNV
TELLSALKVAQAEYVTVELN
GEVLEREAFDATTVKDGDAV
EFLYFMGGGKLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 311 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 498 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GmR137 | 1 |
Entities:
Entity 1, GmR137 78 residues - 8530.543 Da.
Last 8 residues LEHHHHHH is a C-terminal tag
| 1 | MET | ASN | LEU | THR | VAL | ASN | GLY | LYS | PRO | SER | ||||
| 2 | THR | VAL | ASP | GLY | ALA | GLU | SER | LEU | ASN | VAL | ||||
| 3 | THR | GLU | LEU | LEU | SER | ALA | LEU | LYS | VAL | ALA | ||||
| 4 | GLN | ALA | GLU | TYR | VAL | THR | VAL | GLU | LEU | ASN | ||||
| 5 | GLY | GLU | VAL | LEU | GLU | ARG | GLU | ALA | PHE | ASP | ||||
| 6 | ALA | THR | THR | VAL | LYS | ASP | GLY | ASP | ALA | VAL | ||||
| 7 | GLU | PHE | LEU | TYR | PHE | MET | GLY | GLY | GLY | LYS | ||||
| 8 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: GmR137, THiS protein, [U-100% 13C; U-100% 15N], 1.06 ± 0.2 mM; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 100 mM; MES 20 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_2: GmR137, THiS protein, [U-10% 13C; U-99% 15N], 1.26 ± 0.2 mM; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 100 mM; MES 20 mM; H2O 90%; D2O, [U-100% 2H], 10%
sample_conditions_1: ionic strength: 105 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D GFT-HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D GFT-CABCA(CO)NHN | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D GFT-HABCAB(CO)NHN | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D-CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C aliph NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (NH2 only) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (Large SW) | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts