BMRB Entry 17124
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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/BMR17124
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Wahab, Atia-Tul; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the Bordetella bronchiseptica protein NP_888769.1 establishes a new phage-related protein family PF13554." Protein Sci. 20, 1137-1144 (2011).
PubMed: 21520320
Assembly members:
NP_888769.1, polymer, 141 residues, 15260.356 Da.
Natural source: Common Name: B. bronchiseptica Taxonomy ID: 518 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella bronchiseptica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSpeedET
Entity Sequences (FASTA):
NP_888769.1: GMSQDLIRAAFEKRLSDWAK
ARTPALPVAWQNTKFTPPAA
GVYLRAYVMPAATISRDAAG
DHRQYRGVFQVNVVMPIGDG
SRSAEQVAAELDALFPVNLV
MQSGGLAVRVRTPISNGQPT
TGDADHTVPISLGYDVQFYP
E
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 565 |
| 15N chemical shifts | 142 |
| 1H chemical shifts | 947 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NP_888769.1 | 1 |
Entities:
Entity 1, NP_888769.1 141 residues - 15260.356 Da.
| 1 | GLY | MET | SER | GLN | ASP | LEU | ILE | ARG | ALA | ALA | ||||
| 2 | PHE | GLU | LYS | ARG | LEU | SER | ASP | TRP | ALA | LYS | ||||
| 3 | ALA | ARG | THR | PRO | ALA | LEU | PRO | VAL | ALA | TRP | ||||
| 4 | GLN | ASN | THR | LYS | PHE | THR | PRO | PRO | ALA | ALA | ||||
| 5 | GLY | VAL | TYR | LEU | ARG | ALA | TYR | VAL | MET | PRO | ||||
| 6 | ALA | ALA | THR | ILE | SER | ARG | ASP | ALA | ALA | GLY | ||||
| 7 | ASP | HIS | ARG | GLN | TYR | ARG | GLY | VAL | PHE | GLN | ||||
| 8 | VAL | ASN | VAL | VAL | MET | PRO | ILE | GLY | ASP | GLY | ||||
| 9 | SER | ARG | SER | ALA | GLU | GLN | VAL | ALA | ALA | GLU | ||||
| 10 | LEU | ASP | ALA | LEU | PHE | PRO | VAL | ASN | LEU | VAL | ||||
| 11 | MET | GLN | SER | GLY | GLY | LEU | ALA | VAL | ARG | VAL | ||||
| 12 | ARG | THR | PRO | ILE | SER | ASN | GLY | GLN | PRO | THR | ||||
| 13 | THR | GLY | ASP | ALA | ASP | HIS | THR | VAL | PRO | ILE | ||||
| 14 | SER | LEU | GLY | TYR | ASP | VAL | GLN | PHE | TYR | PRO | ||||
| 15 | GLU |
Samples:
sample_1: NP_888769.1, [U-98% 13C; U-98% 15N], 1.0 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; D2O 5%; H2O 95%
sample_conditions_1: ionic strength: 0.11 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 15N-1H HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 15N-resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13C(aliphatic)-resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13C(aromatic)-resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
UNIO v2.0.0, Torsten Herrmann - chemical shift assignment, peak picking, structure calculation
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - Structure calculation
TOPSPIN v1.3, Bruker Biospin - data collection, data processing
Molmol v2K.1, Koradi, Billeter and Wuthrich - analysis and display of molecule
CARA v1.8.4_linux, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAO70052 |
| EMBL | CAE32722 CAE33988 CCN17196 |
| GB | KAK74699 KCV36321 KCV51124 KDB85184 KDB90075 |
| REF | WP_004566287 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks