BMRB Entry 17008
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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/BMR17008
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Title: Solution NMR Structure of Peptide methionine sulfoxide reductase msrB from Bacillus subtilis, Northeast Structural Genomics Consortium Target SR10
Deposition date: 2010-06-18 Original release date: 2010-07-07
Authors: Ertekin, Asli; Cooper, Bonnie; Ciccosanti, Colleen; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Rossi, Paolo; Maglaqui, Melissa; Janjua, Haleema; Prestegard, James; Lee, Hsiau-Wei; Aramini, James
Citation: Ertekin, Asli; Xiao, R.; Montelione, G.. "Northeast Structural Genomics Consortium Target SR10" To be published ., .-..
Assembly members:
SR10, polymer, 151 residues, 17145.258 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SR10: MAYNKEEKIKSLNRMQYEVT
QNNGTEPPFQNEYWDHKEEG
LYVDIVSGKPLFTSKDKFDS
QCGWPSFTKPIEEEVEEKLD
TSHGMIRTEVRSRTADSHLG
HVFNDGPGPNGLRYCINSAA
LRFVPKHKLKEEGYESYLHL
FNKLEHHHHHH
| Data type | Count |
| 13C chemical shifts | 456 |
| 15N chemical shifts | 140 |
| 1H chemical shifts | 276 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SR10 | 1 |
Entities:
Entity 1, SR10 151 residues - 17145.258 Da.
The construct studied has LEHHHHHH purification tag on C-terminus.
| 1 | MET | ALA | TYR | ASN | LYS | GLU | GLU | LYS | ILE | LYS | ||||
| 2 | SER | LEU | ASN | ARG | MET | GLN | TYR | GLU | VAL | THR | ||||
| 3 | GLN | ASN | ASN | GLY | THR | GLU | PRO | PRO | PHE | GLN | ||||
| 4 | ASN | GLU | TYR | TRP | ASP | HIS | LYS | GLU | GLU | GLY | ||||
| 5 | LEU | TYR | VAL | ASP | ILE | VAL | SER | GLY | LYS | PRO | ||||
| 6 | LEU | PHE | THR | SER | LYS | ASP | LYS | PHE | ASP | SER | ||||
| 7 | GLN | CYS | GLY | TRP | PRO | SER | PHE | THR | LYS | PRO | ||||
| 8 | ILE | GLU | GLU | GLU | VAL | GLU | GLU | LYS | LEU | ASP | ||||
| 9 | THR | SER | HIS | GLY | MET | ILE | ARG | THR | GLU | VAL | ||||
| 10 | ARG | SER | ARG | THR | ALA | ASP | SER | HIS | LEU | GLY | ||||
| 11 | HIS | VAL | PHE | ASN | ASP | GLY | PRO | GLY | PRO | ASN | ||||
| 12 | GLY | LEU | ARG | TYR | CYS | ILE | ASN | SER | ALA | ALA | ||||
| 13 | LEU | ARG | PHE | VAL | PRO | LYS | HIS | LYS | LEU | LYS | ||||
| 14 | GLU | GLU | GLY | TYR | GLU | SER | TYR | LEU | HIS | LEU | ||||
| 15 | PHE | ASN | LYS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 16 | HIS |
Samples:
SR10.026: SR10, [U-100% 13C; U-100% 15N; U-100% 2H], 0.8 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 100 mM; protease inhibitor 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%
SR10.022: SR10, [U-5% 13C; U-100% 15N], 1.2 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 100 mM; protease inhibitor 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%
SR10.022_2: SR10, [U-5% 13C; U-100% 15N], 1.2 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM; sodium chloride 200 mM; protease inhibitor 1 x; MES 20 mM; DSS 50 uM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | SR10.026 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | SR10.026 | isotropic | sample_conditions_1 |
| 3D HNCO | SR10.026 | isotropic | sample_conditions_1 |
| 3D HNCA | SR10.026 | isotropic | sample_conditions_1 |
| 3D TRHNCACB 2H dec | SR10.026 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | SR10.026 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC - T1 | SR10.026 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC - T2 | SR10.026 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | SR10.026 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | SR10.026 | isotropic | sample_conditions_1 |
| 3D (N15)HSQC-NOESY-(N15)HSQC | SR10.026 | isotropic | sample_conditions_1 |
| 3D (C13)HSQC-NOESY-(C13)HSQC | SR10.026 | isotropic | sample_conditions_1 |
| 3D (N15)HSQC-NOESY-(C13)HSQC | SR10.026 | isotropic | sample_conditions_1 |
| 3D (C13)HSQC-NOESY-(N15)HSQC | SR10.026 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | SR10.022 | isotropic | sample_conditions_1 |
| 2D 1H-15N TROSY | SR10.022_2 | anisotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
SPARKY, Goddard - data analysis, peak picking
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAI85662 BAM52650 BAM58225 GAK79338 |
| EMBL | CAB14086 CCU58667 CEI57380 CEJ77805 CJS85990 |
| GB | AAA96648 ADV92894 AEP91184 AFQ58114 AGA23472 |
| REF | NP_390051 WP_003230813 WP_014477116 WP_014480061 WP_021481498 |
| SP | P54155 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts