BMRB Entry 16561
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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/BMR16561
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Title: Solution NMR structure of a Bacterial Ig-like (Big_3) domain from Bacillus cereus. Northeast Structural Genomics Consortium target BcR147A.
Deposition date: 2009-10-16 Original release date: 2010-09-17
Authors: Aramini, James; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, Gurla; Everett, John; Montelione, Gaetano
Citation: Aramini, James; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, Gurla; Everett, John; Montelione, Gaetano. "Solution NMR structure of a Bacterial Ig-like (Big_3) domain from Bacillus cereus. Northeast Structural Genomics Consortium target BcR147A." Not known ., .-..
Assembly members:
BcR147A, polymer, 103 residues, 11244.687 Da.
CA, non-polymer, 40.078 Da.
Natural source: Common Name: Bacillus cereus Taxonomy ID: 1396 Superkingdom: Eubacteria Kingdom: not available Genus/species: Bacillus cereus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BcR147A: MGNGETSDLEPKLTVPVGAT
IHVGDSFVPMAEVLAIDKED
GDLTSKIKVDGEVDTTKAGT
YVLTYTVTDSKGHEVTAKQT
VTVKVREEVKNDKPILEHHH
HHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 422 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 671 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BcR147A | 1 |
| 2 | CALCIUM ION | 2 |
Entities:
Entity 1, BcR147A 103 residues - 11244.687 Da.
contains additional N-terminal Met and C-terminal LEHHHHHH affinity tag due to cloning.
| 1 | MET | GLY | ASN | GLY | GLU | THR | SER | ASP | LEU | GLU | ||||
| 2 | PRO | LYS | LEU | THR | VAL | PRO | VAL | GLY | ALA | THR | ||||
| 3 | ILE | HIS | VAL | GLY | ASP | SER | PHE | VAL | PRO | MET | ||||
| 4 | ALA | GLU | VAL | LEU | ALA | ILE | ASP | LYS | GLU | ASP | ||||
| 5 | GLY | ASP | LEU | THR | SER | LYS | ILE | LYS | VAL | ASP | ||||
| 6 | GLY | GLU | VAL | ASP | THR | THR | LYS | ALA | GLY | THR | ||||
| 7 | TYR | VAL | LEU | THR | TYR | THR | VAL | THR | ASP | SER | ||||
| 8 | LYS | GLY | HIS | GLU | VAL | THR | ALA | LYS | GLN | THR | ||||
| 9 | VAL | THR | VAL | LYS | VAL | ARG | GLU | GLU | VAL | LYS | ||||
| 10 | ASN | ASP | LYS | PRO | ILE | LEU | GLU | HIS | HIS | HIS | ||||
| 11 | HIS | HIS | HIS |
Entity 2, CALCIUM ION - Ca - 40.078 Da.
| 1 | CA |
Samples:
sample_2: BcR147A, [U-5% 13C; U-100% 15N], 0.78 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%
sample_1: BcR147A, [U-100% 13C; U-100% 15N], 0.94 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 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 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high resolution (L/V methyl stereoassignment) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 1D 1H-15N T1 and T2 | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, data analysis
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.112, Goddard - data analysis, peak picking
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis
PSVS v1.3, Bhattacharya and Montelione - structure quality analysis
MolProbity v3.15, Richardson - structure quality analysis
PDBStat v5.1, Tejero and Montelione - PDB coordinate analysis
TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts