BMRB Entry 19628
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19628
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Title: NMR structure of the protein NP_419126.1 from CAULOBACTER CRESCENTUS
Deposition date: 2013-11-21 Original release date: 2014-03-03
Authors: Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt
Citation: Serrano, Pedro; Dutta, Samit; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein NP_419126.1 from CAULOBACTER CRESCENTUS" Not known ., .-..
Assembly members:
entity, polymer, 74 residues, 16470.863 Da.
Natural source: Common Name: Caulobacter vibrioides Taxonomy ID: 155892 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter crescentus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MPDKQLLHIVVGGELKDVAG
VEFRDLSKVEFVGAYPSYDE
AHKAWKAKAQATVDNAHARY
FIIHAHKLLDPSEG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 302 |
| 15N chemical shifts | 74 |
| 1H chemical shifts | 491 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 74 residues - 16470.863 Da.
| 1 | MET | PRO | ASP | LYS | GLN | LEU | LEU | HIS | ILE | VAL | ||||
| 2 | VAL | GLY | GLY | GLU | LEU | LYS | ASP | VAL | ALA | GLY | ||||
| 3 | VAL | GLU | PHE | ARG | ASP | LEU | SER | LYS | VAL | GLU | ||||
| 4 | PHE | VAL | GLY | ALA | TYR | PRO | SER | TYR | ASP | GLU | ||||
| 5 | ALA | HIS | LYS | ALA | TRP | LYS | ALA | LYS | ALA | GLN | ||||
| 6 | ALA | THR | VAL | ASP | ASN | ALA | HIS | ALA | ARG | TYR | ||||
| 7 | PHE | ILE | ILE | HIS | ALA | HIS | LYS | LEU | LEU | ASP | ||||
| 8 | PRO | SER | GLU | GLY |
Samples:
sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; entity, [U-99% 13C; U-99% 15N], 1.2 mM
sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D HACANH APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D HACACONH APSY | sample_1 | isotropic | sample_conditions_1 |
| 5D CBCACONH APSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al., Keller and Wuthrich - chemical shift assignment, data analysis, refinement
j-UNIO, Herrmann and Wuthrich - chemical shift assignment, chemical shift calculation, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| GB | AAK22294 ACL93776 |
| REF | NP_419126 WP_010918196 WP_012639934 YP_002515684 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts