BMRB Entry 26745
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR26745
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Title: Backbone 1H, 13C, and 15N assignments for Sortase C1 (SrtC1) from Streptococcus pneumoniae PubMed: 27109553
Deposition date: 2016-02-13 Original release date: 2016-07-14
Authors: Jacobitz, Alex; Clubb, Robert
Citation: Jacobitz, Alex; Naziga, Emmanuel; Sung Wook, Yi; McConnell, Scott; Peterson, Robert; Jung, Michael; Clubb, Robert; Wereszczynski, Jeff. "The "Lid" in the Streptococcus pneumoniae SrtC1 Sortase Adopts a Rigid Structure that Regulates Substrate Access to the Active Site" J. Phys. Chem. B 120, 8302-8312 (2016).
Assembly members:
SrtC1, polymer, 213 residues, 23812.9 Da.
Natural source: Common Name: fermicutes Taxonomy ID: 170187 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pneumoniae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SrtC1: SESNQQIADFDKEKATLDEA
DIDERMKLAQAFNDSLNNVV
SGDPWSEEMKKKGRAEYARM
LEIHERMGHVEIPVIDVDLP
VYAGTAEEVLQQGAGHLEGT
SLPIGGNSTHAVITAHTGLP
TAKMFTDLTKLKVGDKFYVH
NIKEVMAYQVDQVKVIEPTN
FDDLLIVPGHDYVTLLTCTP
YMINTHRLLVRGHRIPYVAE
VEEEFIAANKLSH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 310 |
15N chemical shifts | 192 |
1H chemical shifts | 339 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | SrtC1 | 1 |
Entities:
Entity 1, SrtC1 213 residues - 23812.9 Da.
Sequence matches PDB ID 2W1J. First 15 residues in this sequence are part of a membrane anchor and were removed to generate a soluble construct. First residue, S-16, is a remnant of a cleaved purification tag.
1 | SER | GLU | SER | ASN | GLN | GLN | ILE | ALA | ASP | PHE | ||||
2 | ASP | LYS | GLU | LYS | ALA | THR | LEU | ASP | GLU | ALA | ||||
3 | ASP | ILE | ASP | GLU | ARG | MET | LYS | LEU | ALA | GLN | ||||
4 | ALA | PHE | ASN | ASP | SER | LEU | ASN | ASN | VAL | VAL | ||||
5 | SER | GLY | ASP | PRO | TRP | SER | GLU | GLU | MET | LYS | ||||
6 | LYS | LYS | GLY | ARG | ALA | GLU | TYR | ALA | ARG | MET | ||||
7 | LEU | GLU | ILE | HIS | GLU | ARG | MET | GLY | HIS | VAL | ||||
8 | GLU | ILE | PRO | VAL | ILE | ASP | VAL | ASP | LEU | PRO | ||||
9 | VAL | TYR | ALA | GLY | THR | ALA | GLU | GLU | VAL | LEU | ||||
10 | GLN | GLN | GLY | ALA | GLY | HIS | LEU | GLU | GLY | THR | ||||
11 | SER | LEU | PRO | ILE | GLY | GLY | ASN | SER | THR | HIS | ||||
12 | ALA | VAL | ILE | THR | ALA | HIS | THR | GLY | LEU | PRO | ||||
13 | THR | ALA | LYS | MET | PHE | THR | ASP | LEU | THR | LYS | ||||
14 | LEU | LYS | VAL | GLY | ASP | LYS | PHE | TYR | VAL | HIS | ||||
15 | ASN | ILE | LYS | GLU | VAL | MET | ALA | TYR | GLN | VAL | ||||
16 | ASP | GLN | VAL | LYS | VAL | ILE | GLU | PRO | THR | ASN | ||||
17 | PHE | ASP | ASP | LEU | LEU | ILE | VAL | PRO | GLY | HIS | ||||
18 | ASP | TYR | VAL | THR | LEU | LEU | THR | CYS | THR | PRO | ||||
19 | TYR | MET | ILE | ASN | THR | HIS | ARG | LEU | LEU | VAL | ||||
20 | ARG | GLY | HIS | ARG | ILE | PRO | TYR | VAL | ALA | GLU | ||||
21 | VAL | GLU | GLU | GLU | PHE | ILE | ALA | ALA | ASN | LYS | ||||
22 | LEU | SER | HIS |
Samples:
sample_1: SrtC1, [U-99% 13C; U-99% 15N], 2 mM; sodium chloride 50 mM; potassium phosphate 50 mM; sodium azide 0.01%; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 310 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA v1.9.0, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts