BMRB Entry 50361
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR50361
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Title: 1H, 13C and 15N chemical shift assignment of an intein protein from a cyanobacterium Spirulina platensis PubMed: 33289560
Deposition date: 2020-06-25 Original release date: 2020-12-31
Authors: Boral, Soumendu; De, Soumya
Citation: Boral, Soumendu; Maiti, Snigdha; Basak, Aditya; Lee, Woonghee; De, Soumya. "Structural, Dynamic, and Functional Characterization of a DnaX Mini-intein Derived from Spirulina platensis Provides Important Insights into Intein-Mediated Catalysis of Protein Splicing" Biochemistry 59, 4711-4724 (2020).
Assembly members:
entity_1, polymer, 137 residues, Formula weight is not available
Natural source: Common Name: Arthrospira platensis Taxonomy ID: 118562 Superkingdom: Bacteria Kingdom: not available Genus/species: Arthrospira platensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28(a)
Entity Sequences (FASTA):
entity_1: EALTGDALILSDRGWLRIDD
PTLQECRVLSYNESTQQWEW
QQVLRWLDQGVRETWKIKTF
QTEIKCTGNHLIRTDKGWIK
AANITPKMKILSPEIDAAVK
TALQDVESIEKLGVNHVYDI
EVEHNHNFVANGLLVHN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 594 |
| 15N chemical shifts | 157 |
| 1H chemical shifts | 968 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Spl DnaX mini-intein | 1 |
Entities:
Entity 1, Spl DnaX mini-intein 137 residues - Formula weight is not available
| 1 | GLU | ALA | LEU | THR | GLY | ASP | ALA | LEU | ILE | LEU | ||||
| 2 | SER | ASP | ARG | GLY | TRP | LEU | ARG | ILE | ASP | ASP | ||||
| 3 | PRO | THR | LEU | GLN | GLU | CYS | ARG | VAL | LEU | SER | ||||
| 4 | TYR | ASN | GLU | SER | THR | GLN | GLN | TRP | GLU | TRP | ||||
| 5 | GLN | GLN | VAL | LEU | ARG | TRP | LEU | ASP | GLN | GLY | ||||
| 6 | VAL | ARG | GLU | THR | TRP | LYS | ILE | LYS | THR | PHE | ||||
| 7 | GLN | THR | GLU | ILE | LYS | CYS | THR | GLY | ASN | HIS | ||||
| 8 | LEU | ILE | ARG | THR | ASP | LYS | GLY | TRP | ILE | LYS | ||||
| 9 | ALA | ALA | ASN | ILE | THR | PRO | LYS | MET | LYS | ILE | ||||
| 10 | LEU | SER | PRO | GLU | ILE | ASP | ALA | ALA | VAL | LYS | ||||
| 11 | THR | ALA | LEU | GLN | ASP | VAL | GLU | SER | ILE | GLU | ||||
| 12 | LYS | LEU | GLY | VAL | ASN | HIS | VAL | TYR | ASP | ILE | ||||
| 13 | GLU | VAL | GLU | HIS | ASN | HIS | ASN | PHE | VAL | ALA | ||||
| 14 | ASN | GLY | LEU | LEU | VAL | HIS | ASN |
Samples:
sample_1: Spl DnaX mini-intein, [U-100% 13C; U-100% 15N], 0.65 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 0.02%
sample_conditions_1: pH: 6.5; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRFAM-SPARKY - chemical shift assignment
NMR spectrometers:
- Bruker AVANCE III 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts