BMRB Entry 31025

Title:
TPX2 Minimal Active Domain on Microtubules
Deposition date:
2022-05-19
Original release date:
2023-06-27
Authors:
Guo, C.; Alfaro-Aco, R.; Russell, R.; Zhang, C.; Petry, S.; Polenova, T.
Citation:

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:

Assembly members:
entity_1, polymer, 240 residues, 28443.770 Da.

Natural source:

Natural source:   Common Name: African clawed frog   Taxonomy ID: 8355   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Xenopus laevis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Data sets:
Data typeCount
13C chemical shifts507
15N chemical shifts173
1H chemical shifts171

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 240 residues - 28443.770 Da.

1   VALPROVALILELYSALATHRARGMETPRO
2   HISTYRGLYVALPROPHELYSPROLYSLEU
3   VALGLUGLNARGGLNVALASPVALCYSPRO
4   PHESERPHECYSASPARGASPLYSGLUARG
5   GLNLEUGLNLYSGLULYSARGLEUASPGLU
6   LEUARGLYSASPGLUVALPROLYSPHELYS
7   ALAGLNPROLEUPROGLNPHEASPASNILE
8   ARGLEUPROGLULYSLYSVALLYSMETPRO
9   THRGLNGLNGLUPROPHEASPLEUGLUILE
10   GLULYSARGGLYALASERLYSLEUGLNARG
11   TRPGLNGLNGLNILEGLNGLUGLULEULYS
12   GLNGLNLYSGLUMETVALVALPHELYSALA
13   ARGPROASNTHRVALVALHISGLNGLUPRO
14   PHEVALPROLYSLYSGLUASNARGSERLEU
15   THRGLUSERLEUSERGLYSERILEVALGLN
16   GLUGLYPHEGLULEUALATHRALALYSARG
17   ALALYSGLUARGGLNGLUPHEASPLYSCYS
18   LEUALAGLUTHRGLUALAGLNLYSSERLEU
19   LEUGLUGLUGLUILEARGLYSARGARGGLU
20   GLUGLUGLULYSGLUGLUILESERGLNLEU
21   ARGGLNGLULEUVALHISLYSALALYSPRO
22   ILEARGLYSTYRARGALAVALGLUVALLYS
23   ALASERASPVALPROLEUTHRVALPROARG
24   SERPROASNPHESERASPARGPHELYSCYS

Samples:

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

Experiments:

NameSampleSample stateSample conditions
2D NH HETCORsample_2isotropicsample_conditions_2
2D CH HETCORsample_2isotropicsample_conditions_2
3D (H)CANHsample_2isotropicsample_conditions_2
3D (H)(CO)CA(CO)NHsample_2isotropicsample_conditions_2
3D (H)CONHsample_2isotropicsample_conditions_2
2D RFDR 2.4 mssample_2isotropicsample_conditions_2
2D CORD (200ms mixing)sample_1isotropicsample_conditions_1
2D CORD (50ms mixing)sample_1isotropicsample_conditions_1
2D CH HETCORsample_2isotropicsample_conditions_4
2D CH HETCORsample_2isotropicsample_conditions_2
2D CH HETCOR (2.8 ms/2.7 ms CP)sample_2isotropicsample_conditions_3
2D CH HETCOR (2.1 ms/2.1 ms CP)sample_2isotropicsample_conditions_3
2D CH HETCORsample_1isotropicsample_conditions_5
2D CH HETCORsample_1isotropicsample_conditions_5
2D HN HETCORsample_1isotropicsample_conditions_1
2D NCAsample_1isotropicsample_conditions_1
2D RFDRsample_1isotropicsample_conditions_1
2D NCACXsample_1isotropicsample_conditions_5
2D CORD (200ms mixing)sample_1isotropicsample_conditions_5
2D RFDRsample_1isotropicsample_conditions_5
3D (H)CONHsample_1isotropicsample_conditions_5
3D (H)CANHsample_1isotropicsample_conditions_5
2D NH HETCORsample_1isotropicsample_conditions_5
2D NCOCXsample_1isotropicsample_conditions_5

Software:

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

NMR spectrometers:

  • Agilent VARIAN 600 MHz
  • Bruker AVANCE III HD 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks