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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31025
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Guo, C.; Alfaro-Aco, R.; Zhang, C.; Russell, R.; Petry, S.; Polenova, T.. "Structural basis of protein condensation on microtubules underlying branching microtubule nucleation" Nat. Commun. 14, 3682-3682 (2023).
PubMed: 37344496
Assembly members:
entity_1, polymer, 240 residues, 28443.770 Da.
Natural source: Common Name: African clawed frog Taxonomy ID: 8355 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Xenopus laevis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Data type | Count |
13C chemical shifts | 507 |
15N chemical shifts | 173 |
1H chemical shifts | 171 |
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | unit_1 | 1 |
Entity 1, unit_1 240 residues - 28443.770 Da.
1 | VAL | PRO | VAL | ILE | LYS | ALA | THR | ARG | MET | PRO | |
2 | HIS | TYR | GLY | VAL | PRO | PHE | LYS | PRO | LYS | LEU | |
3 | VAL | GLU | GLN | ARG | GLN | VAL | ASP | VAL | CYS | PRO | |
4 | PHE | SER | PHE | CYS | ASP | ARG | ASP | LYS | GLU | ARG | |
5 | GLN | LEU | GLN | LYS | GLU | LYS | ARG | LEU | ASP | GLU | |
6 | LEU | ARG | LYS | ASP | GLU | VAL | PRO | LYS | PHE | LYS | |
7 | ALA | GLN | PRO | LEU | PRO | GLN | PHE | ASP | ASN | ILE | |
8 | ARG | LEU | PRO | GLU | LYS | LYS | VAL | LYS | MET | PRO | |
9 | THR | GLN | GLN | GLU | PRO | PHE | ASP | LEU | GLU | ILE | |
10 | GLU | LYS | ARG | GLY | ALA | SER | LYS | LEU | GLN | ARG | |
11 | TRP | GLN | GLN | GLN | ILE | GLN | GLU | GLU | LEU | LYS | |
12 | GLN | GLN | LYS | GLU | MET | VAL | VAL | PHE | LYS | ALA | |
13 | ARG | PRO | ASN | THR | VAL | VAL | HIS | GLN | GLU | PRO | |
14 | PHE | VAL | PRO | LYS | LYS | GLU | ASN | ARG | SER | LEU | |
15 | THR | GLU | SER | LEU | SER | GLY | SER | ILE | VAL | GLN | |
16 | GLU | GLY | PHE | GLU | LEU | ALA | THR | ALA | LYS | ARG | |
17 | ALA | LYS | GLU | ARG | GLN | GLU | PHE | ASP | LYS | CYS | |
18 | LEU | ALA | GLU | THR | GLU | ALA | GLN | LYS | SER | LEU | |
19 | LEU | GLU | GLU | GLU | ILE | ARG | LYS | ARG | ARG | GLU | |
20 | GLU | GLU | GLU | LYS | GLU | GLU | ILE | SER | GLN | LEU | |
21 | ARG | GLN | GLU | LEU | VAL | HIS | LYS | ALA | LYS | PRO | |
22 | ILE | ARG | LYS | TYR | ARG | ALA | VAL | GLU | VAL | LYS | |
23 | ALA | SER | ASP | VAL | PRO | LEU | THR | VAL | PRO | ARG | |
24 | SER | PRO | ASN | PHE | SER | ASP | ARG | PHE | LYS | CYS |
sample_1: TPX2a5-7, [U-13C; U-15N], 1.5 ± 0.2 mM; Microtubules 100 ± 10 uM; phosphate 100 mM; MgCl2 100 mM; DTT 100 mM; EGTA 100 mM
sample_2: TPX2a5-7, [U-13C; U-15N, D; 100% back-exchanged], 1.5 ± 0.2 mM; Microtubules 100 ± 10 uM; phosphate 100 mM; MgCl2 100 mM; DTT 100 mM; EGTA 100 mM
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 276 K
sample_conditions_2: pH: 6.8; pressure: 1 atm; temperature: 283 K
sample_conditions_3: pH: 6.8; pressure: 1 atm; temperature: 285 K
sample_conditions_4: pH: 6.8; pressure: 1 atm; temperature: 288 K
sample_conditions_5: pH: 6.8; pressure: 1 atm; temperature: 288 K
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NH HETCOR | sample_2 | isotropic | sample_conditions_2 |
2D CH HETCOR | sample_2 | isotropic | sample_conditions_2 |
3D (H)CANH | sample_2 | isotropic | sample_conditions_2 |
3D (H)(CO)CA(CO)NH | sample_2 | isotropic | sample_conditions_2 |
3D (H)CONH | sample_2 | isotropic | sample_conditions_2 |
2D RFDR 2.4 ms | sample_2 | isotropic | sample_conditions_2 |
2D CORD (200ms mixing) | sample_1 | isotropic | sample_conditions_1 |
2D CORD (50ms mixing) | sample_1 | isotropic | sample_conditions_1 |
2D CH HETCOR | sample_2 | isotropic | sample_conditions_4 |
2D CH HETCOR | sample_2 | isotropic | sample_conditions_2 |
2D CH HETCOR (2.8 ms/2.7 ms CP) | sample_2 | isotropic | sample_conditions_3 |
2D CH HETCOR (2.1 ms/2.1 ms CP) | sample_2 | isotropic | sample_conditions_3 |
2D CH HETCOR | sample_1 | isotropic | sample_conditions_5 |
2D CH HETCOR | sample_1 | isotropic | sample_conditions_5 |
2D HN HETCOR | sample_1 | isotropic | sample_conditions_1 |
2D NCA | sample_1 | isotropic | sample_conditions_1 |
2D RFDR | sample_1 | isotropic | sample_conditions_1 |
2D NCACX | sample_1 | isotropic | sample_conditions_5 |
2D CORD (200ms mixing) | sample_1 | isotropic | sample_conditions_5 |
2D RFDR | sample_1 | isotropic | sample_conditions_5 |
3D (H)CONH | sample_1 | isotropic | sample_conditions_5 |
3D (H)CANH | sample_1 | isotropic | sample_conditions_5 |
2D NH HETCOR | sample_1 | isotropic | sample_conditions_5 |
2D NCOCX | sample_1 | isotropic | sample_conditions_5 |
TopSpin, Bruker Biospin - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
MestreLab (Mnova / MestReNova / MestReC), MestreLab - data analysis
CcpNmr Analysis, CCPN - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
TALOS, Cornilescu, Delaglio and Bax - data analysis
Sparky, Goddard - data analysis
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks