BMRB Entry 19031
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19031
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Citation: Yan, Si; Hou, Guangjin; Schwieters, Charles; Ahmed, Shubbir; Williams, John; Polenova, Tatyana. "Three-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1." J. Mol. Biol. 425, 4249-4266 (2013).
PubMed: 23648839
Assembly members:
CAP-Gly, polymer, 89 residues, 9513 Da.
EB1, polymer, 75 residues, 8747 Da.
Natural source: Common Name: Rat Taxonomy ID: 10116 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Rattus norvegicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28b-His6-SMT3
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 258 |
| 15N chemical shifts | 65 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CAP-Gly, 1 | 1 |
| 2 | CAP-Gly, 2 | 1 |
| 3 | EB1, 1 | 2 |
| 4 | EB1, 2 | 2 |
Entities:
Entity 1, CAP-Gly, 1 89 residues - 9513 Da.
The sequence starts from S19, and ends at E107. Residues S19-P26 and E98-E107 are not assigned due to the dynamics of the termini.
| 1 | SER | THR | GLU | ALA | SER | ALA | ARG | PRO | LEU | ARG | ||||
| 2 | VAL | GLY | SER | ARG | VAL | GLU | VAL | ILE | GLY | LYS | ||||
| 3 | GLY | HIS | ARG | GLY | THR | VAL | ALA | TYR | VAL | GLY | ||||
| 4 | ALA | THR | LEU | PHE | ALA | THR | GLY | LYS | TRP | VAL | ||||
| 5 | GLY | VAL | ILE | LEU | ASP | GLU | ALA | LYS | GLY | LYS | ||||
| 6 | ASN | ASP | GLY | THR | VAL | GLN | GLY | ARG | LYS | TYR | ||||
| 7 | PHE | THR | CYS | ASP | GLU | GLY | HIS | GLY | ILE | PHE | ||||
| 8 | VAL | ARG | GLN | SER | GLN | ILE | GLN | VAL | PHE | GLU | ||||
| 9 | ASP | GLY | ALA | ASP | THR | THR | SER | PRO | GLU |
Entity 2, EB1, 1 75 residues - 8747 Da.
This sequence starts from residue A193, and ends at residue Y268.
| 1 | ALA | GLU | LEU | MET | GLN | GLN | VAL | ASN | VAL | LEU | ||||
| 2 | LYS | LEU | THR | VAL | GLU | ASP | LEU | GLU | LYS | GLU | ||||
| 3 | ARG | ASP | PHE | TYR | PHE | GLY | LYS | LEU | ARG | ASN | ||||
| 4 | ILE | GLU | LEU | ILE | CYS | GLN | GLU | ASN | GLU | GLY | ||||
| 5 | GLU | ASN | ASP | PRO | VAL | LEU | GLN | ARG | ILE | VAL | ||||
| 6 | ASP | ILE | LEU | TYR | ALA | THR | ASP | GLU | GLY | PHE | ||||
| 7 | VAL | ILE | PRO | ASP | GLU | GLY | GLY | PRO | GLN | GLU | ||||
| 8 | GLU | GLN | GLU | GLU | TYR |
Samples:
sample_1: CAP-Gly, [U-13C; U-15N], 11.8 mg; EB1 10.2 mg; H2O 100%
sample_conditions_1: ionic strength: 90 mM; pH: 7.0; pressure: 1 atm; temperature: 277 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DARR | sample_1 | solid | sample_conditions_1 |
| 2D NCA | sample_1 | solid | sample_conditions_1 |
| 3D NCACX | sample_1 | solid | sample_conditions_1 |
| 3D NCOCX | sample_1 | solid | sample_conditions_1 |
| 3D CANCX | sample_1 | solid | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Ascend 850 MHz
Related Database Links:
| BMRB | 17937 17938 19025 25005 18371 |
| PDB | |
| DBJ | BAE34241 BAE37079 BAE42418 BAE42912 BAE87998 BAE32461 BAE89438 BAG35484 BAG59745 BAG73401 |
| EMBL | CAA44091 CAA67333 CAE45882 CAH10572 CAH10575 CAH92115 |
| GB | AAB57773 AAD03694 AAD55811 AAH66061 AAI42510 AAA96320 AAC09471 AAH52405 AAH64444 AAH81726 |
| REF | NP_001092404 NP_001127253 NP_001128512 NP_001177765 NP_001177766 NP_001038078 NP_001068802 NP_001126236 NP_001238875 NP_001253729 |
| SP | O08788 P28023 Q14203 Q15691 Q3ZBD9 Q5R7Z5 Q61166 Q66HR2 |
| TPG | DAA24857 DAA23186 |
| AlphaFold | O08788 P28023 Q14203 Q15691 Q3ZBD9 Q5R7Z5 Q61166 Q66HR2 |