BMRB Entry 16576
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16576
MolProbity Validation Chart
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Title: Solution Structure Of Protein BH0266 From Bacillus halodurans. Northeast Structural Genomics Consortium Target BhR97a PubMed: 21154411
Deposition date: 2009-10-23 Original release date: 2010-01-07
Authors: Wu, Yibing; Eletsky, Alexander; Lee, Dan; Sathyamoorthy, Bharathwaj; Buchwald, William; Hua, Jia; Ciccosanti, Colleen; He, Yunfen; Hamilton, Keith; Acton, T.B.; Xiao, R.; Everett, J.K.; Lee, Hsiau-Wei; Prestegard, Jim; Montelione, G.T.; Szyperski, Thomas
Citation: Barb, Adam; Cort, John; Seetharaman, Jayaraman; Lew, Scott; Lee, Hsiau-Wei; Acton, Thomas; Xiao, Rong; Kennedy, Michael; Tong, Liang; Montelione, Gaetano; Prestegard, James. "Structures of domains I and IV from YbbR are representative of a widely distributed protein family" Protein Sci. 20, 396-405 (2011).
Assembly members:
BH0266, polymer, 119 residues, 13589.194 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BH0266: MPTFDHGNLSLGELELTVLY
DEERYDIVEQTETVQVDLEG
PRGVLTVFRFARPSYEVFVD
LTEAGEGSHTVDVEHRGFPG
DLAVTVEPRMARVQLEERQT
VSVPVTVEMINLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 358 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 763 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BH0266 | 1 |
Entities:
Entity 1, BH0266 119 residues - 13589.194 Da.
| 1 | MET | PRO | THR | PHE | ASP | HIS | GLY | ASN | LEU | SER | ||||
| 2 | LEU | GLY | GLU | LEU | GLU | LEU | THR | VAL | LEU | TYR | ||||
| 3 | ASP | GLU | GLU | ARG | TYR | ASP | ILE | VAL | GLU | GLN | ||||
| 4 | THR | GLU | THR | VAL | GLN | VAL | ASP | LEU | GLU | GLY | ||||
| 5 | PRO | ARG | GLY | VAL | LEU | THR | VAL | PHE | ARG | PHE | ||||
| 6 | ALA | ARG | PRO | SER | TYR | GLU | VAL | PHE | VAL | ASP | ||||
| 7 | LEU | THR | GLU | ALA | GLY | GLU | GLY | SER | HIS | THR | ||||
| 8 | VAL | ASP | VAL | GLU | HIS | ARG | GLY | PHE | PRO | GLY | ||||
| 9 | ASP | LEU | ALA | VAL | THR | VAL | GLU | PRO | ARG | MET | ||||
| 10 | ALA | ARG | VAL | GLN | LEU | GLU | GLU | ARG | GLN | THR | ||||
| 11 | VAL | SER | VAL | PRO | VAL | THR | VAL | GLU | MET | ILE | ||||
| 12 | ASN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 90%; D2O 10%
sample_2: entity, [U-5% 13C; U-99% 15N], 1.0 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| simNOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker DMX 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts