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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26723
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kilpatrick, Adina; Gurrola, Theodore; Sterner, Robert; Sleister, Heidi; Honts, Jerry; Fowler, C. Andrew. "Backbone and side-chain chemical shift assignments for the C-terminal domain of Tcb2, a cytoskeletal calcium-binding protein from Tetrahymena thermophila" Biomol. NMR Assign. 10, 281-285 (2016).
PubMed: 27155947
Assembly members:
Tcb2-C, polymer, 102 residues, Formula weight is not available
Natural source: Common Name: Tetrahymena thermophila Taxonomy ID: 5911 Superkingdom: Eukaryota Kingdom: not available Genus/species: Tetrahymena thermophila
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pJ411: T7 promoter, inducible
Entity Sequences (FASTA):
Tcb2-C: SSKPKYNPEVEAKLDVARRL
FKRYDKDGSGQLQDDEIAGL
LKDTYAEMGMSNFTPTKEDV
KIWLQMADTNSDGSVSLEEY
EDLIIKSLQKAGIRVEKQSL
VF
Data type | Count |
13C chemical shifts | 450 |
15N chemical shifts | 101 |
1H chemical shifts | 677 |
T1 relaxation values | 87 |
T2 relaxation values | 84 |
heteronuclear NOE values | 87 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Tcb2-C | 1 |
Entity 1, Tcb2-C 102 residues - Formula weight is not available
C-terminal domain of Tetrahymena calcium-binding protein 2 (Tcb2)
1 | SER | SER | LYS | PRO | LYS | TYR | ASN | PRO | GLU | VAL | ||||
2 | GLU | ALA | LYS | LEU | ASP | VAL | ALA | ARG | ARG | LEU | ||||
3 | PHE | LYS | ARG | TYR | ASP | LYS | ASP | GLY | SER | GLY | ||||
4 | GLN | LEU | GLN | ASP | ASP | GLU | ILE | ALA | GLY | LEU | ||||
5 | LEU | LYS | ASP | THR | TYR | ALA | GLU | MET | GLY | MET | ||||
6 | SER | ASN | PHE | THR | PRO | THR | LYS | GLU | ASP | VAL | ||||
7 | LYS | ILE | TRP | LEU | GLN | MET | ALA | ASP | THR | ASN | ||||
8 | SER | ASP | GLY | SER | VAL | SER | LEU | GLU | GLU | TYR | ||||
9 | GLU | ASP | LEU | ILE | ILE | LYS | SER | LEU | GLN | LYS | ||||
10 | ALA | GLY | ILE | ARG | VAL | GLU | LYS | GLN | SER | LEU | ||||
11 | VAL | PHE |
sample_1: Tcb2-C, [U-98% 13C; U-98% 15N], 0.75 mM; TRIS 25 mM; potassium chloride 50 mM; magnesium chloride 5 mM; EGTA 1 mM
sample_2: Tcb2-C, [U-98% 13C; U-98% 15N], 0.75 mM; TRIS 25 mM; potassium chloride 50 mM; magnesium chloride 5 mM; EGTA 1 mM
sample_3: Tcb2-C, [U-98% 15N], 0.75 mM; TRIS 25 mM; potassium chloride 50 mM; magnesium chloride 5 mM; EGTA 1 mM
sample_4: Tcb2-C 1.1 mM; TRIS 25 mM; potassium chloride 50 mM; magnesium chloride 5 mM; EGTA 1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 298 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
2D 1H-13C HMQC | sample_2 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
2D 1H-1H COSY | sample_4 | isotropic | sample_conditions_1 |
2D 1H-1H TOCSY | sample_4 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
2D (HB)CB(CGCD)HD | sample_2 | isotropic | sample_conditions_1 |
2D (HB)CB(CGCDCE)HE | sample_2 | isotropic | sample_conditions_1 |
Heteronuclear NOE ratio | sample_1 | isotropic | sample_conditions_1 |
T1 experiments | sample_1 | isotropic | sample_conditions_1 |
T2 experiments | sample_1 | isotropic | sample_conditions_1 |
CcpNmr_Analysis, CCPN - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMRJ, Varian - collection
NCBI | P09226.2 XP_001007754.3 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks