BMRB Entry 15850
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: LACS
BMRB Entry DOI: doi:10.13018/BMR15850
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Title: Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A.
Deposition date: 2008-06-30 Original release date: 2008-10-13
Authors: Conover, Kenith; Swapna, G.V.T.; Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jingfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Conover, Kenith; Swapna, G.V.T.; Rossi, Paolo; Wang, Dongyan; Janjua, Haleema; Owens, Leah; Xiao, Rong; Liu, Jingfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A." .
Assembly members:
BcR103A, polymer, 117 residues, 13091.908 Da.
Natural source: Common Name: Bacillus cereus Taxonomy ID: 1396 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus cereus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C
Entity Sequences (FASTA):
BcR103A: MERASLNRIGKDVYYMQIKG
EGTIEKVDGRNLRNYTLPAY
DEDGVKKQITFRSTKKENDH
KLNKYAFLRLYVDQDDNSKN
EISSIEVKSYEEIQKADLPE
KVKDKFTIKLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 436 |
| 15N chemical shifts | 95 |
| 1H chemical shifts | 680 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BcR103A | 1 |
Entities:
Entity 1, BcR103A 117 residues - 13091.908 Da.
21 residues lipobox was removed.
| 1 | MET | GLU | ARG | ALA | SER | LEU | ASN | ARG | ILE | GLY | ||||
| 2 | LYS | ASP | VAL | TYR | TYR | MET | GLN | ILE | LYS | GLY | ||||
| 3 | GLU | GLY | THR | ILE | GLU | LYS | VAL | ASP | GLY | ARG | ||||
| 4 | ASN | LEU | ARG | ASN | TYR | THR | LEU | PRO | ALA | TYR | ||||
| 5 | ASP | GLU | ASP | GLY | VAL | LYS | LYS | GLN | ILE | THR | ||||
| 6 | PHE | ARG | SER | THR | LYS | LYS | GLU | ASN | ASP | HIS | ||||
| 7 | LYS | LEU | ASN | LYS | TYR | ALA | PHE | LEU | ARG | LEU | ||||
| 8 | TYR | VAL | ASP | GLN | ASP | ASP | ASN | SER | LYS | ASN | ||||
| 9 | GLU | ILE | SER | SER | ILE | GLU | VAL | LYS | SER | TYR | ||||
| 10 | GLU | GLU | ILE | GLN | LYS | ALA | ASP | LEU | PRO | GLU | ||||
| 11 | LYS | VAL | LYS | ASP | LYS | PHE | THR | ILE | LYS | LEU | ||||
| 12 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: BcR103A, [U-100% 13C; U-100% 15N], 0.6 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM
sample_2: BcR103A, [5% 13C; U-100% 15N], 1.37 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM
sample_3: BcR103A, [U-100% 13C; U-100% 15N], 0.5 mM; DSS 50 uM; DTT 10 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; sodium chloride 100 mM
sample_conditions_1: ionic strength: 0.1 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-13C NOESY ARO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C-15N SIM NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | 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 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC stereo | sample_2 | isotropic | sample_conditions_1 |
| HETNOE | sample_2 | isotropic | sample_conditions_1 |
| slow exch 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_3 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
TOPSPIN v2.1, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TALOS, Cornilescu, Delaglio and Bax - geometry optimization
SPARKY v3.113, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - validation
PDBStat v5.1, Tejero R.; Montelione GT - validation
Molmol v2k2, Koradi, Billeter and Wuthrich - visualization
Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation
MolProbity, Richardson - Validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- Varian INOVA 500 MHz
Related Database Links:
| PDB | |
| EMBL | CGG02256 CJA31281 CJB35032 CJC25384 CJC28010 |
| GB | AAP09401 ADH07006 EEL11492 EJR35492 EJR82496 |
| REF | NP_832200 WP_000713860 WP_000713863 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts