BMRB Entry 18371
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18371
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: Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 C-terminal domain PubMed: 23128140
Deposition date: 2012-03-30 Original release date: 2012-11-15
Authors: Kanaba, Teppei; Mishima, Masaki
Citation: Kanaba, Teppei; Maesaki, Ryoko; Mori, Tomoyuki; Ito, Yutaka; Hakoshima, Toshio; Mishima, Masaki. "Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR." Biochim. Biophys. Acta 1834, 499-507 (2013).
Assembly members:
EB1_C-terminal_domain, polymer, 85 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):
EB1_C-terminal_domain: GPLGSGDDEAAELMQQVNVL
KLTVEDLEKERDFYFGKLRN
IELICQENEGENDPVLQRIV
DILYATDEGFVIPDEGGPQE
EQEEY
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 177 |
| 15N chemical shifts | 67 |
| 1H chemical shifts | 67 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | EB1 C-terminal domain | 1 |
Entities:
Entity 1, EB1 C-terminal domain 85 residues - Formula weight is not available
| 1 | GLY | PRO | LEU | GLY | SER | GLY | ASP | ASP | GLU | ALA | ||||
| 2 | ALA | GLU | LEU | MET | GLN | GLN | VAL | ASN | VAL | LEU | ||||
| 3 | LYS | LEU | THR | VAL | GLU | ASP | LEU | GLU | LYS | GLU | ||||
| 4 | ARG | ASP | PHE | TYR | PHE | GLY | LYS | LEU | ARG | ASN | ||||
| 5 | ILE | GLU | LEU | ILE | CYS | GLN | GLU | ASN | GLU | GLY | ||||
| 6 | GLU | ASN | ASP | PRO | VAL | LEU | GLN | ARG | ILE | VAL | ||||
| 7 | ASP | ILE | LEU | TYR | ALA | THR | ASP | GLU | GLY | PHE | ||||
| 8 | VAL | ILE | PRO | ASP | GLU | GLY | GLY | PRO | GLN | GLU | ||||
| 9 | GLU | GLN | GLU | GLU | TYR |
Samples:
sample_1: EB1 C-terminal domain, [U-100% 13C; U-100% 15N], 1.0 mM; H2O 93%; D2O 7%
sample_conditions_1: ionic strength: 0.4 M; pH: 7.0; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAE89438 BAG35484 BAG59745 BAG73401 |
| EMBL | CAH92115 |
| GB | AAC09471 AAI06069 AAI09282 AAY18920 ACE87787 |
| REF | NP_001126236 NP_001253729 NP_001271003 NP_036457 XP_002710850 |
| SP | Q15691 Q5R7Z5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts