BMRB Entry 30926
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30926
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Title: Solution NMR structure of peptidase domain from Clostridium thermocellum PCAT1 PubMed: 34865273
Deposition date: 2021-06-13 Original release date: 2021-12-31
Authors: Bhattacharya, S.; Palillo, A.
Citation: Bhattacharya, S.; Pallilo, A.. "Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1" Protein Sci. 31, 498-512 (2022).
Assembly members:
entity_1, polymer, 151 residues, 16635.389 Da.
Natural source: Common Name: Clostridium thermocellum Taxonomy ID: 203119 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium thermocellum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pMSCG20
Entity Sequences (FASTA):
entity_1: SNAMLRRLFKKKYVCVRQYD
LTDAGAACLSSIAQYYGLKM
SLAKIREMTGTDTQGTNAYG
LIHAAKQLGFSAKGVKASKE
DLLKDFRLPAIANVIVDNRL
AHFVVIYSIKNRIITVADPG
KGIVRYSMDDFCSIWTGGLV
LLEPGEAFQKG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 622 |
| 15N chemical shifts | 151 |
| 1H chemical shifts | 1057 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 151 residues - 16635.389 Da.
| 1 | SER | ASN | ALA | MET | LEU | ARG | ARG | LEU | PHE | LYS | ||||
| 2 | LYS | LYS | TYR | VAL | CYS | VAL | ARG | GLN | TYR | ASP | ||||
| 3 | LEU | THR | ASP | ALA | GLY | ALA | ALA | CYS | LEU | SER | ||||
| 4 | SER | ILE | ALA | GLN | TYR | TYR | GLY | LEU | LYS | MET | ||||
| 5 | SER | LEU | ALA | LYS | ILE | ARG | GLU | MET | THR | GLY | ||||
| 6 | THR | ASP | THR | GLN | GLY | THR | ASN | ALA | TYR | GLY | ||||
| 7 | LEU | ILE | HIS | ALA | ALA | LYS | GLN | LEU | GLY | PHE | ||||
| 8 | SER | ALA | LYS | GLY | VAL | LYS | ALA | SER | LYS | GLU | ||||
| 9 | ASP | LEU | LEU | LYS | ASP | PHE | ARG | LEU | PRO | ALA | ||||
| 10 | ILE | ALA | ASN | VAL | ILE | VAL | ASP | ASN | ARG | LEU | ||||
| 11 | ALA | HIS | PHE | VAL | VAL | ILE | TYR | SER | ILE | LYS | ||||
| 12 | ASN | ARG | ILE | ILE | THR | VAL | ALA | ASP | PRO | GLY | ||||
| 13 | LYS | GLY | ILE | VAL | ARG | TYR | SER | MET | ASP | ASP | ||||
| 14 | PHE | CYS | SER | ILE | TRP | THR | GLY | GLY | LEU | VAL | ||||
| 15 | LEU | LEU | GLU | PRO | GLY | GLU | ALA | PHE | GLN | LYS | ||||
| 16 | GLY |
Samples:
sample_1: C39 peptidase domain, [U-100% 13C; U-100% 15N], 675 uM; sodium phosphate 50 uM; sodium chloride 150 uM; DTT 5 mM; PBS buffer 50 mM
sample_conditions_1: ionic strength: 150 mM; pH: 7.0; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
TopSpin v2.1, 3.5, Bruker Biospin - collection
TopSpin v2.1, 3.6, Bruker Biospin - processing
CARA v1.5, Keller and Wuthrich - chemical shift assignment, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
ARIA v2.3, Linge, O'Donoghue and Nilges - refinement
NMR spectrometers:
- Bruker AVANCE 900.03 MHz
- Bruker AVANCE III HD 800.23 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts