BMRB Entry 26861
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26861
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kozlyuk, Natalia; Sengupta, Suvrajit; Bierma, Jan; Martin, Rachel. "Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in tunicate beta gamma crystallin" Biochemistry 55, 6961-6968 (2016).
PubMed: 27992995
Assembly members:
Tunicate, polymer, 84 residues, 9057 Da.
CALCIUM ION, non-polymer, 40.078 Da.
Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Pet28a(+)
Entity Sequences (FASTA):
Tunicate: MGKIILFEDVEFGGKKLELE
TSVSDLNVHGFNDIVSSIIV
ESGTWFVFDDEGFSGPSYKL
TPGKYPNPGSWGGNDDELSS
VKQQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 225 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 79 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Tunicate beta gamma crystallin | 1 |
| 2 | Calcium ion | 2 |
Entities:
Entity 1, Tunicate beta gamma crystallin 84 residues - 9057 Da.
| 1 | MET | GLY | LYS | ILE | ILE | LEU | PHE | GLU | ASP | VAL | ||||
| 2 | GLU | PHE | GLY | GLY | LYS | LYS | LEU | GLU | LEU | GLU | ||||
| 3 | THR | SER | VAL | SER | ASP | LEU | ASN | VAL | HIS | GLY | ||||
| 4 | PHE | ASN | ASP | ILE | VAL | SER | SER | ILE | ILE | VAL | ||||
| 5 | GLU | SER | GLY | THR | TRP | PHE | VAL | PHE | ASP | ASP | ||||
| 6 | GLU | GLY | PHE | SER | GLY | PRO | SER | TYR | LYS | LEU | ||||
| 7 | THR | PRO | GLY | LYS | TYR | PRO | ASN | PRO | GLY | SER | ||||
| 8 | TRP | GLY | GLY | ASN | ASP | ASP | GLU | LEU | SER | SER | ||||
| 9 | VAL | LYS | GLN | GLN |
Entity 2, Calcium ion - 40.078 Da.
| 1 | CA |
Samples:
sample_1: Tunicate beta gamma crystallin, [U-13C; U-15N], 1.7 mM; H2O 90%; D2O 10%; CaCl2 10 mM
sample_conditions_1: ionic strength: 0.01 M; pH: 7.1; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| CBCA(CO)NH (H[N[co[{CA|ca[C]}]]]) | sample_1 | isotropic | sample_conditions_1 |
| Expt_14 (H[N[ca[CO]]]) | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNmr_Analysis v2.4, CCPN - chemical shift assignment
CcpNmr_Entry_Completion_Interface v2.1, PDBe & CCPN - data deposition
NMR spectrometers:
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks