BMRB Entry 15353
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15353
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Title: Solution NMR Structure of Bordetella bronchiseptica protein BB2007: Northeast Structural Genomics Consortium Target BoR54
Deposition date: 2007-06-29 Original release date: 2007-08-10
Authors: Eletsky, Alexander; Sukumaran, Dinesh; Wu, Yibing; Singarapu, Kiran; Parish, David; Xu, Duanxiang; Wang, Dongyan; Nwosu, Chioma; Cunningham, Kellie; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Szyperski, Thomas. "NMR Solution Structure of Bordetella bronchiseptica protein BB2007" Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
BoR54, polymer, 70 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: 518 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella bronchiseptica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BoR54: MESRLLDILVCPVCKGRLEF
QRAQAELVCNADRLAFPVRD
GVPIMLEAEARSLDAEAPAQ
PSLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 262 |
| 15N chemical shifts | 65 |
| 1H chemical shifts | 446 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BoR54 | 1 |
Entities:
Entity 1, BoR54 70 residues - Formula weight is not available
C-terminal His-tag LEHHHHHH
| 1 | MET | GLU | SER | ARG | LEU | LEU | ASP | ILE | LEU | VAL | |
| 2 | CYS | PRO | VAL | CYS | LYS | GLY | ARG | LEU | GLU | PHE | |
| 3 | GLN | ARG | ALA | GLN | ALA | GLU | LEU | VAL | CYS | ASN | |
| 4 | ALA | ASP | ARG | LEU | ALA | PHE | PRO | VAL | ARG | ASP | |
| 5 | GLY | VAL | PRO | ILE | MET | LEU | GLU | ALA | GLU | ALA | |
| 6 | ARG | SER | LEU | ASP | ALA | GLU | ALA | PRO | ALA | GLN | |
| 7 | PRO | SER | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC: BoR54, [U-100% 13C; U-100% 15N], 1.3 mM; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 100 mM; MES 20 mM; H2O 95%; D2O 5%
NC5: BoR54, [U-5% 13C; U-100% 15N], 0.8 mM; NaN3 0.02%; DTT 100 mM; CaCl2 5 mM; NaCl 100 mM; MES 20 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.115 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY | NC | isotropic | sample_conditions_1 |
| 3D 1H-13C,15N NOESY | NC | isotropic | sample_conditions_1 |
| 3D (H)CCH-COSY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5 | isotropic | sample_conditions_1 |
Software:
VNMR v6.1C, Varian - collection
TOPSPIN v1.3, Bruker Biospin - collection, processing
PROSA v6.0.2, Guntert - processing
CARA v1.8.4, R. Keller - chemical shift assignment, data analysis
CSI v2.0, Brian Sykes, David Wishart - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.0.0, Huang, Tejero, Powers and Montelione - structure solution
AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CNSSOLVE v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 750 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts