BMRB Entry 15835
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15835
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Title: Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195
Deposition date: 2008-06-27 Original release date: 2008-08-19
Authors: SINGARAPU, KIRAN KUMAR; ELETSKY, ALEX; SATHYAMOORTHY, BHARATHWAJ; SUKUMARAN, DINESH; Wang, Dongyan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS
Citation: SINGARAPU, KIRAN KUMAR; ELETSKY, ALEX; SATHYAMOORTHY, BHARATHWAJ; SUKUMARAN, DINESH; Wang, Dongyan; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; SZYPERSKI, THOMAS. "Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195" Not known ., .-..
Assembly members:
BpR195, polymer, 191 residues, 21168.037 Da.
Natural source: Common Name: Bordetella parapertussis Taxonomy ID: 519 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella parapertussis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
BpR195: MTSPSSAFPDGHGARLDAQS
IRFERLLPGPIERVWAWLAD
ADKRARWLAGGELPRQPGQT
FELHFNHAALTAETAPARYA
QYDRPIVARHTLLRCEPPRV
LALTWGGGAGEAPSEVLFEL
SEAGEQVRLVLTHTRLADRA
AMLDVAGGWHAHLAVLAGKL
AGQAPPPFWTTLAQAEQDYE
QRLLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 738 |
| 15N chemical shifts | 175 |
| 1H chemical shifts | 1224 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BpR195 | 1 |
Entities:
Entity 1, BpR195 191 residues - 21168.037 Da.
| 1 | MET | THR | SER | PRO | SER | SER | ALA | PHE | PRO | ASP | ||||
| 2 | GLY | HIS | GLY | ALA | ARG | LEU | ASP | ALA | GLN | SER | ||||
| 3 | ILE | ARG | PHE | GLU | ARG | LEU | LEU | PRO | GLY | PRO | ||||
| 4 | ILE | GLU | ARG | VAL | TRP | ALA | TRP | LEU | ALA | ASP | ||||
| 5 | ALA | ASP | LYS | ARG | ALA | ARG | TRP | LEU | ALA | GLY | ||||
| 6 | GLY | GLU | LEU | PRO | ARG | GLN | PRO | GLY | GLN | THR | ||||
| 7 | PHE | GLU | LEU | HIS | PHE | ASN | HIS | ALA | ALA | LEU | ||||
| 8 | THR | ALA | GLU | THR | ALA | PRO | ALA | ARG | TYR | ALA | ||||
| 9 | GLN | TYR | ASP | ARG | PRO | ILE | VAL | ALA | ARG | HIS | ||||
| 10 | THR | LEU | LEU | ARG | CYS | GLU | PRO | PRO | ARG | VAL | ||||
| 11 | LEU | ALA | LEU | THR | TRP | GLY | GLY | GLY | ALA | GLY | ||||
| 12 | GLU | ALA | PRO | SER | GLU | VAL | LEU | PHE | GLU | LEU | ||||
| 13 | SER | GLU | ALA | GLY | GLU | GLN | VAL | ARG | LEU | VAL | ||||
| 14 | LEU | THR | HIS | THR | ARG | LEU | ALA | ASP | ARG | ALA | ||||
| 15 | ALA | MET | LEU | ASP | VAL | ALA | GLY | GLY | TRP | HIS | ||||
| 16 | ALA | HIS | LEU | ALA | VAL | LEU | ALA | GLY | LYS | LEU | ||||
| 17 | ALA | GLY | GLN | ALA | PRO | PRO | PRO | PHE | TRP | THR | ||||
| 18 | THR | LEU | ALA | GLN | ALA | GLU | GLN | ASP | TYR | GLU | ||||
| 19 | GLN | ARG | LEU | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 20 | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.069 mM; H2O 95%; D2O, [U-100% 2H], 5%
sample_2: entity, [U-100% 15N; U-5% 13C], 1.1 mM; H2O 95%; D2O, [U-100% 2H], 5%
sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | 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 |
| 4,3D GFT HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 15N-13C simultanious NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol, Koradi, Billeter and Wuthrich - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
PSVS, Bhattacharya and Montelione - geometry optimization
TALOS, Cornilescu, Delaglio and Bax - data analysis
VNMRJ, Varian - collection
XEASY, Bartels et al. - data analysis
NMR spectrometers:
- Varian INOVA 750 MHz
Related Database Links:
| PDB | |
| DBJ | BAO68965 |
| EMBL | CAE32895 CAE36637 CAE42423 CCJ49648 CCJ52144 |
| GB | AEE67412 AIW92288 AIW95609 AJB27454 ALH49292 |
| REF | NP_880798 WP_003812218 WP_003816973 WP_010927985 WP_010930760 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts