BMRB Entry 16870
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16870
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Cofactor C PubMed: 20617401
Deposition date: 2010-04-15 Original release date: 2011-09-28
Authors: Garcia Mayoral, Maria Flor
Citation: Garcia Mayoral, Maria Flor; Castano, Raquel; Zabala, Juan Carlos; Santoro, Jorge; Rico, Manuel; Bruix, Marta. "1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C" Biomol. NMR Assignments 4, 219-221 (2010).
Assembly members:
Human Tubulin Cofactor C, polymer, 111 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Human Tubulin Cofactor C: MPERLQRREQERQLEVERRK
QKRQNQEVEKENSHFFVATF
ARERAAVEELLERAESVERL
EEAASRLQGLQKLINDSVFF
LAAYDLRQGQEALARLQAAL
AERRRGLQPKK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 370 |
15N chemical shifts | 108 |
1H chemical shifts | 797 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Human Tubulin Cofactor C | 1 |
Entities:
Entity 1, Human Tubulin Cofactor C 111 residues - Formula weight is not available
1 | MET | PRO | GLU | ARG | LEU | GLN | ARG | ARG | GLU | GLN | ||||
2 | GLU | ARG | GLN | LEU | GLU | VAL | GLU | ARG | ARG | LYS | ||||
3 | GLN | LYS | ARG | GLN | ASN | GLN | GLU | VAL | GLU | LYS | ||||
4 | GLU | ASN | SER | HIS | PHE | PHE | VAL | ALA | THR | PHE | ||||
5 | ALA | ARG | GLU | ARG | ALA | ALA | VAL | GLU | GLU | LEU | ||||
6 | LEU | GLU | ARG | ALA | GLU | SER | VAL | GLU | ARG | LEU | ||||
7 | GLU | GLU | ALA | ALA | SER | ARG | LEU | GLN | GLY | LEU | ||||
8 | GLN | LYS | LEU | ILE | ASN | ASP | SER | VAL | PHE | PHE | ||||
9 | LEU | ALA | ALA | TYR | ASP | LEU | ARG | GLN | GLY | GLN | ||||
10 | GLU | ALA | LEU | ALA | ARG | LEU | GLN | ALA | ALA | LEU | ||||
11 | ALA | GLU | ARG | ARG | ARG | GLY | LEU | GLN | PRO | LYS | ||||
12 | LYS |
Samples:
sample_1: TBCC_Nterm, [U-13C; U-15N], 0.5 1.0 mM; potassium phosphate 20 mM; potassium chloride 20 mM; TCEP 1.0 mM; EDTA 1.0 mM; DSS 0.05 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.02 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HA(CA)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection, processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
PDB | |
DBJ | BAG35561 |
EMBL | CAH92969 |
GB | AAB17539 AAH17479 AAH20170 AAP35648 AAP36382 |
REF | NP_001126753 NP_003183 XP_003833336 XP_004044073 XP_518477 |
SP | Q15814 Q5R5J7 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts