BMRB Entry 15702
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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/BMR15702
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Title: Solution NMR Structure of Bordatella pertussis protein BP2786, a Mth938-like domain: Northeast Structural Genomics Consortium target BeR31
Deposition date: 2008-04-01 Original release date: 2009-10-12
Authors: Cort, John; Ho, Chi; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation: Cort, John; Kennedy, Michael. "Solution structure of Bordatella pertussis protein BP2786" Not known ., .-..
Assembly members:
BP2786, polymer, 158 residues, 15800 Da.
Natural source: Common Name: Bordetella pertussis Taxonomy ID: 520 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordatella pertussis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BP2786: MKLHTDPATALNTVTAYGDG
YIEVNQVRFSHAIAFAPEGP
VASWPVQRPADITASLLQQA
AGLAEVVRDPLAFLDEPEAG
AGARPANAPEVLLVGTGRRQ
HLLGPEQVRPLLAMGVGVEA
MDTQAAARTYNILMAEGRRV
VVALLPDGDSLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 532 |
| 15N chemical shifts | 132 |
| 1H chemical shifts | 839 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BP2786 | 1 |
Entities:
Entity 1, BP2786 158 residues - 15800 Da.
contains C-terminal 6X His tag and linker: LEHHHHHH
| 1 | MET | LYS | LEU | HIS | THR | ASP | PRO | ALA | THR | ALA | ||||
| 2 | LEU | ASN | THR | VAL | THR | ALA | TYR | GLY | ASP | GLY | ||||
| 3 | TYR | ILE | GLU | VAL | ASN | GLN | VAL | ARG | PHE | SER | ||||
| 4 | HIS | ALA | ILE | ALA | PHE | ALA | PRO | GLU | GLY | PRO | ||||
| 5 | VAL | ALA | SER | TRP | PRO | VAL | GLN | ARG | PRO | ALA | ||||
| 6 | ASP | ILE | THR | ALA | SER | LEU | LEU | GLN | GLN | ALA | ||||
| 7 | ALA | GLY | LEU | ALA | GLU | VAL | VAL | ARG | ASP | PRO | ||||
| 8 | LEU | ALA | PHE | LEU | ASP | GLU | PRO | GLU | ALA | GLY | ||||
| 9 | ALA | GLY | ALA | ARG | PRO | ALA | ASN | ALA | PRO | GLU | ||||
| 10 | VAL | LEU | LEU | VAL | GLY | THR | GLY | ARG | ARG | GLN | ||||
| 11 | HIS | LEU | LEU | GLY | PRO | GLU | GLN | VAL | ARG | PRO | ||||
| 12 | LEU | LEU | ALA | MET | GLY | VAL | GLY | VAL | GLU | ALA | ||||
| 13 | MET | ASP | THR | GLN | ALA | ALA | ALA | ARG | THR | TYR | ||||
| 14 | ASN | ILE | LEU | MET | ALA | GLU | GLY | ARG | ARG | VAL | ||||
| 15 | VAL | VAL | ALA | LEU | LEU | PRO | ASP | GLY | ASP | SER | ||||
| 16 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: BP2786 mM; sodium chloride 100 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM
sample_2: BP2786 mM; sodium chloride 100 mM; MES 20 mM; DTT 10 mM; sodium azide 0.02%; calcium chloride 5 mM
sample_conditions_1: ionic strength: 135 mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 1H-13C-13C-1H HMQC-NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
FELIX v97, Accelrys Software Inc. - chemical shift assignment, data analysis, processing
SPARKY, Goddard - chemical shift assignment, data analysis
AutoStruct, Huang, Tejero, Powers and Montelione - refinement, structure solution
PSVS, Bhattacharya and Montelione - refinement, structure analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Varian INOVA 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAO68551 |
| EMBL | CAE32421 CAE37772 CAE43059 CCJ49135 CCJ53508 |
| GB | AEE67991 AIW91535 AIW96550 AJB27175 ALH48586 |
| REF | NP_881386 WP_003813077 WP_010926333 WP_033453456 WP_033462228 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts