BMRB Entry 19025
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19025
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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, 9530 Da.
Natural source: Common Name: Norway 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
Entity Sequences (FASTA):
CAP-Gly: STEASARPLRVGSRVEVIGK
GHRGTVAYVGATLFATGKWV
GVILDEAKGKNDGTVQGRKY
FTCDEGHGIFVRQSQIQVFE
DGADTTSPE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 142 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CAP-Gly | 1 |
Entities:
Entity 1, CAP-Gly 89 residues - 9530 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 |
Samples:
sample_1: CAP-Gly, [U-13C; U-15N], 24.4 mg; H2O 100%
sample_conditions_1: ionic strength: 30 mM; pH: 6.0; 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 19031 25005 |
| PDB | |
| DBJ | BAE34241 BAE37079 BAE42418 BAE42912 BAE87998 |
| EMBL | CAA44091 CAA67333 CAE45882 CAH10572 CAH10575 |
| GB | AAB57773 AAD03694 AAD55811 AAH66061 AAI42510 |
| REF | NP_001092404 NP_001127253 NP_001128512 NP_001177765 NP_001177766 |
| SP | O08788 P28023 Q14203 |
| TPG | DAA24857 |
| AlphaFold | O08788 P28023 Q14203 |