BMRB Entry 15784
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15784
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Title: 1H, 13C, and 15N Chemical Shift Assignments for NikA(1-51) PubMed: 18929573
Deposition date: 2008-05-28 Original release date: 2008-11-25
Authors: Yoshida, Hitoshi; Furuya, Nobuhisa; Lin, Yi-Jan; Guntert, Peter; Komano, Teruya; Kainosho, Masatsune
Citation: Yoshida, Hitoshi; Furuya, Nobuhisa; Lin, Yi-Jan; Guntert, Peter; Komano, Teruya; Kainosho, Masatsune. "Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation." J. Mol. Biol. 384, 690-701 (2008).
Assembly members:
NikA(1-51), polymer, 51 residues, Formula weight is not available
Natural source: Common Name: R64 plasmid Taxonomy ID: 602 Superkingdom: Bacteria Kingdom: not available Genus/species: Salmonella typhimurium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NikA(1-51): SDSAVRKKSEVRQKTVVRTL
RFSPVEDETIRKKAEDSGLT
VSAYIRNAALN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 201 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 316 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NikA(1-51) | 1 |
Entities:
Entity 1, NikA(1-51) 51 residues - Formula weight is not available
| 1 | SER | ASP | SER | ALA | VAL | ARG | LYS | LYS | SER | GLU | ||||
| 2 | VAL | ARG | GLN | LYS | THR | VAL | VAL | ARG | THR | LEU | ||||
| 3 | ARG | PHE | SER | PRO | VAL | GLU | ASP | GLU | THR | ILE | ||||
| 4 | ARG | LYS | LYS | ALA | GLU | ASP | SER | GLY | LEU | THR | ||||
| 5 | VAL | SER | ALA | TYR | ILE | ARG | ASN | ALA | ALA | LEU | ||||
| 6 | ASN |
Samples:
sample_1: NikA(1-51), [U-13C; U-15N], 2 mM; phosphate buffer 50 mM; sodium chloride 50 mM; sodium azide 0.02% w/v; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| triple resonance | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
SPARKY, Goddard - chemical shift assignment, peak picking
CYANA, Guntert - structure solution
OPALp, Koradi, Billeter, Guntert - refinement
NMR spectrometers:
- Bruker AV 500 MHz
- Bruker DRX 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA75139 BAA78022 BAB91643 BAG80276 BAK64475 |
| EMBL | CBL93594 CCE57555 CCQ26867 CDH80849 CDO67566 |
| GB | AAS76382 AAZ05364 ACF56917 ACF65722 ACQ42156 |
| REF | NP_052500 NP_863435 WP_000325007 WP_001283946 WP_001283947 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts