BMRB Entry 19624
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19624
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H and 15N chemical shift assignments for circular sortase A
Deposition date: 2013-11-20 Original release date: 2013-12-20
Authors: Jaudzems, Kristaps; Zhulenkovs, Dmitrijs
Citation: Zhulenkovs, Dmitrijs; Jaudzems, Kristaps; Zajakina, Anna; Leonchiks, Ainars. "1H and 15N chemical shift assignments for circular sortase A" to be published ., .-..
Assembly members:
circular_sortase_A, polymer, 156 residues, Formula weight is not available
Natural source: Common Name: firmicutes Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: Firmicutes Genus/species: Staphylococcus aureus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
circular_sortase_A: QAKPQIPKDKSKVAGYIEIP
DADIKEPVYPGPATPEQLNR
GVSFAEENESLDDQNISIAG
HTFIDRPNYQFTNLKAAKKG
SMVYFKVGNETRKYKMTSIR
DVKPTDVEVLDEQKGKDKQL
TLITCDDYNEKTGVWEKRKI
FVATEVKTRESGSIEF
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 159 |
| 1H chemical shifts | 892 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | circular sortase A | 1 |
Entities:
Entity 1, circular sortase A 156 residues - Formula weight is not available
Residues 148-156 represent a non-native linker connecting the N- and C-termini of the catalytic domain (residues 59-206) of full length sortase A
| 1 | GLN | ALA | LYS | PRO | GLN | ILE | PRO | LYS | ASP | LYS | ||||
| 2 | SER | LYS | VAL | ALA | GLY | TYR | ILE | GLU | ILE | PRO | ||||
| 3 | ASP | ALA | ASP | ILE | LYS | GLU | PRO | VAL | TYR | PRO | ||||
| 4 | GLY | PRO | ALA | THR | PRO | GLU | GLN | LEU | ASN | ARG | ||||
| 5 | GLY | VAL | SER | PHE | ALA | GLU | GLU | ASN | GLU | SER | ||||
| 6 | LEU | ASP | ASP | GLN | ASN | ILE | SER | ILE | ALA | GLY | ||||
| 7 | HIS | THR | PHE | ILE | ASP | ARG | PRO | ASN | TYR | GLN | ||||
| 8 | PHE | THR | ASN | LEU | LYS | ALA | ALA | LYS | LYS | GLY | ||||
| 9 | SER | MET | VAL | TYR | PHE | LYS | VAL | GLY | ASN | GLU | ||||
| 10 | THR | ARG | LYS | TYR | LYS | MET | THR | SER | ILE | ARG | ||||
| 11 | ASP | VAL | LYS | PRO | THR | ASP | VAL | GLU | VAL | LEU | ||||
| 12 | ASP | GLU | GLN | LYS | GLY | LYS | ASP | LYS | GLN | LEU | ||||
| 13 | THR | LEU | ILE | THR | CYS | ASP | ASP | TYR | ASN | GLU | ||||
| 14 | LYS | THR | GLY | VAL | TRP | GLU | LYS | ARG | LYS | ILE | ||||
| 15 | PHE | VAL | ALA | THR | GLU | VAL | LYS | THR | ARG | GLU | ||||
| 16 | SER | GLY | SER | ILE | GLU | PHE |
Samples:
sample_1: circular sortase A, [U-100% 15N], 0.5 mM; sodium phosphate 10 mM; sodium chloride 20 mM; D2O, [U-100% 2H], 5%; H2O, [U-100% 2H], 95%
sample_conditions_1: ionic strength: 0.0363 M; pH: 6.5; pressure: 1 atm; temperature: 308 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 16270 19826 |
| PDB | |
| DBJ | BAB43619 BAB58690 BAB96313 BAF68698 BAF79395 |
| EMBL | CAG41587 CAG44229 CAI82090 CAQ50958 CBI50513 |
| GB | AAD48437 AAW37316 ABD22861 ABD31836 ABQ50328 |
| REF | WP_000759357 WP_000759358 WP_000759359 WP_000759360 WP_000759361 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts