BMRB Entry 50120

Title:
Intramolecular synergy enhances the microtubule end-binding affinity of EB1
Deposition date:
2019-12-10
Original release date:
2020-02-19
Authors:
Xue, Yi; Pan, Ying
Citation:

Citation: Liang, .; Song, .; Zhang, .; Pan, .; He, .; Wang, .; Chen, .; Guo, .; Deng, .; Xue, Yi; Fang, Ying. "Intramolecular synergy enhances the microtubule end-binding affinity of EB1"  .

Assembly members:

Assembly members:
entity_1, polymer, 61 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet28a-SUMO

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts116
15N chemical shifts51
1H chemical shifts50
T1 relaxation values45
T2 relaxation values47
heteronuclear NOE values45

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EB1linker-4D1

Entities:

Entity 1, EB1linker-4D 61 residues - Formula weight is not available

1   GLNGLYGLNGLUTHRALAVALALAPROSER
2   LEUVALALAPROALALEUASNLYSPROLYS
3   LYSPROLEUASPASPASPASPALAALAPRO
4   GLNARGPROILESERTHRGLNARGTHRALA
5   ALAALAPROLYSALAGLYPROGLYVALVAL
6   ARGLYSASNPROGLYVALGLYASNGLYASP
7   ASP

Samples:

sample_1: entity_1, [U-99% 15N], 0.5 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%; sodium azide 0.01%; DSS 20 uM

sample_2: entity_1, [U-99% 13C; U-99% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%; sodium azide 0.01%; DSS 20 uM

sample_conditions_1: ionic strength: 0.17 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
15N-(1H) NOEsample_1isotropicsample_conditions_1
15N R1sample_1isotropicsample_conditions_1
15N R2sample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.01, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz

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