BMRB Entry 18348
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18348
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for EB1 CH domain PubMed: 23128140
Deposition date: 2012-03-26 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_CH_domain, polymer, 133 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_CH_domain: GPGMAVNVYSTSVTSDNLSR
HDMLAWINESLQLNLTKIEQ
LCSGAAYCQFMDMLFPGSIA
LKKVKFQAKLEHEYIQNFKI
LQAGFKRMGVDKIIPVDKLV
KGKFQDNFEFVQWFKKFFDA
NYDGKDYDPVAAR
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 367 |
15N chemical shifts | 126 |
1H chemical shifts | 126 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | EB1 CH domain | 1 |
Entities:
Entity 1, EB1 CH domain 133 residues - Formula weight is not available
1 | GLY | PRO | GLY | MET | ALA | VAL | ASN | VAL | TYR | SER | ||||
2 | THR | SER | VAL | THR | SER | ASP | ASN | LEU | SER | ARG | ||||
3 | HIS | ASP | MET | LEU | ALA | TRP | ILE | ASN | GLU | SER | ||||
4 | LEU | GLN | LEU | ASN | LEU | THR | LYS | ILE | GLU | GLN | ||||
5 | LEU | CYS | SER | GLY | ALA | ALA | TYR | CYS | GLN | PHE | ||||
6 | MET | ASP | MET | LEU | PHE | PRO | GLY | SER | ILE | ALA | ||||
7 | LEU | LYS | LYS | VAL | LYS | PHE | GLN | ALA | LYS | LEU | ||||
8 | GLU | HIS | GLU | TYR | ILE | GLN | ASN | PHE | LYS | ILE | ||||
9 | LEU | GLN | ALA | GLY | PHE | LYS | ARG | MET | GLY | VAL | ||||
10 | ASP | LYS | ILE | ILE | PRO | VAL | ASP | LYS | LEU | VAL | ||||
11 | LYS | GLY | LYS | PHE | GLN | ASP | ASN | PHE | GLU | PHE | ||||
12 | VAL | GLN | TRP | PHE | LYS | LYS | PHE | PHE | ASP | ALA | ||||
13 | ASN | TYR | ASP | GLY | LYS | ASP | TYR | ASP | PRO | VAL | ||||
14 | ALA | ALA | ARG |
Samples:
sample_1: EB1 CH domain, [U-13C; U-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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | 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 | BAE32461 BAE89438 BAG35484 BAG73401 |
EMBL | CAG31466 CAH92115 |
GB | AAA96320 AAC09471 AAH52405 AAH64444 AAH81726 |
REF | NP_001026031 NP_001038078 NP_001068802 NP_001126236 NP_001238875 |
SP | Q15691 Q3ZBD9 Q5R7Z5 Q5ZLC7 Q61166 |
TPG | DAA23186 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts