BMRB Entry 36136

Title:
Designed protein dRafX6
Deposition date:
2017-12-05
Original release date:
2018-12-03
Authors:
Liu, R.
Citation:

Citation: Liu, Ruicun; Wang, Jichao; Xiong, Peng; Chen, Quan; Liu, Haiyan. "De novo sequence redesign of a functional Ras-binding domain globally inverted the surface charge distribution and led to extreme thermostability"  Biotechnol. Bioeng. 118, 2031-2042 (2021).
PubMed: 33590881

Assembly members:

Assembly members:
dRafX6, polymer, 79 residues, 8763.368 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts261
15N chemical shifts69
1H chemical shifts550

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 79 residues - 8763.368 Da.

1   METALAASPARGTHRILEGLUVALGLULEU
2   PROASNLYSGLNARGTHRVALILEASNVAL
3   ARGPROGLYLEUTHRLEULYSGLUALALEU
4   LYSLYSALALEULYSVALARGGLYILEASP
5   PROASNLYSVALGLNVALTYRLEULEULEU
6   SERGLYASPASPGLYALAGLUGLNPROLEU
7   SERLEUASNHISPROALAGLUARGLEUILE
8   GLYLYSLYSLEULYSVALVALPROLEU

Samples:

sample_1: dRafX6, [U-13C; U-15N], 0.5 mM; EDTA 0.01 mM; sodium phosphate 0.02 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.05 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DMX 600 MHz

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