BMRB Entry 16093
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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/BMR16093
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Title: Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855). Northeast Structural Genomics Consortium target SrR106
Deposition date: 2008-12-28 Original release date: 2009-03-05
Authors: Wu, Yibing; Eletsky, Alexander; Zhao, Li; Hua, Jia; Sukumaran, Dinesh; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh; Everett, John; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS
Citation: Wu, Yibing; Eletsky, Alexander; Zhao, Li; Hua, Jia; Sukumaran, Dinesh; Jiang, Mei; Foote, Erica; Xiao, Rong; Nair, Rajesh. "Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855) . Northeast Structural Genomics Consortium target SrR106" Not known ., .-..
Assembly members:
SRU_2040, polymer, 153 residues, 17088.771 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SRU_2040: MKTTPDILDQIRVHGADAYP
EEGCGFLLGTVTDDGDNRVA
ALHRATNRRSEQRTRRYELT
ADDYRAADAAAQEQGLDVVG
VYHSHPDHPARPSATDLEEA
TFPGFTYVIVSVRDGAPEAL
TAWALAPDRSEFHREDIVRP
DPEAPLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 895 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SRU_2040 | 1 |
Entities:
Entity 1, SRU_2040 153 residues - 17088.771 Da.
| 1 | MET | LYS | THR | THR | PRO | ASP | ILE | LEU | ASP | GLN | ||||
| 2 | ILE | ARG | VAL | HIS | GLY | ALA | ASP | ALA | TYR | PRO | ||||
| 3 | GLU | GLU | GLY | CYS | GLY | PHE | LEU | LEU | GLY | THR | ||||
| 4 | VAL | THR | ASP | ASP | GLY | ASP | ASN | ARG | VAL | ALA | ||||
| 5 | ALA | LEU | HIS | ARG | ALA | THR | ASN | ARG | ARG | SER | ||||
| 6 | GLU | GLN | ARG | THR | ARG | ARG | TYR | GLU | LEU | THR | ||||
| 7 | ALA | ASP | ASP | TYR | ARG | ALA | ALA | ASP | ALA | ALA | ||||
| 8 | ALA | GLN | GLU | GLN | GLY | LEU | ASP | VAL | VAL | GLY | ||||
| 9 | VAL | TYR | HIS | SER | HIS | PRO | ASP | HIS | PRO | ALA | ||||
| 10 | ARG | PRO | SER | ALA | THR | ASP | LEU | GLU | GLU | ALA | ||||
| 11 | THR | PHE | PRO | GLY | PHE | THR | TYR | VAL | ILE | VAL | ||||
| 12 | SER | VAL | ARG | ASP | GLY | ALA | PRO | GLU | ALA | LEU | ||||
| 13 | THR | ALA | TRP | ALA | LEU | ALA | PRO | ASP | ARG | SER | ||||
| 14 | GLU | PHE | HIS | ARG | GLU | ASP | ILE | VAL | ARG | PRO | ||||
| 15 | ASP | PRO | GLU | ALA | PRO | LEU | GLU | HIS | HIS | HIS | ||||
| 16 | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.7 mM; MES 20 mM; NACL 100 mM; CaCl2 5.0 mM; DTT 10 mM; NaN3 5%; D2O 10%; Protease Inhibitors 1
sample_2: entity, [U-5% 13C; U-99% 15N], 1.0 mM; MES 20 mM; NACL 100 mM; CaCl2 5.0 mM; DTT 10 mM; NaN3 5%; D2O 5%; Protease Inhibitors 1
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1.0 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D HABCAB(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| (4,3)D HCCH | sample_1 | isotropic | sample_conditions_1 |
| (N15-H1, C13-H1) simNOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
XEASY, Bartels et al. - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts