BMRB Entry 50826

Title:
Amide NH assignments of the S20C mutant of the armadillo designed protein YMA tagged with the diamagnetic PCS tag Lu-4R4S-DOTA-M8 and their corresponding PCSs upon tagging with the paramagnetic tag Tm-4R4S_DOTA-M8
Deposition date:
2021-03-13
Original release date:
2021-08-09
Authors:
Cucuzza, Stefano; Guntert, Peter; Pluckthun, Andreas; Zerbe, Oliver
Citation:

Citation: Cucuzza, Stefano; Guntert, Peter; Pluckthun, Andreas; Zerbe, Oliver. "An automated iterative approach for protein structure refinement using pseudocontact shifts"  J. Biomol. NMR 75, 319-334 (2021).
PubMed: 34338940

Assembly members:

Assembly members:
entity_1, polymer, 114 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: pEM3BT2

Data sets:
Data typeCount
15N chemical shifts107
1H chemical shifts107

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1S20C_YMA1

Entities:

Entity 1, S20C_YMA 114 residues - Formula weight is not available

1   GLULEUPROGLNMETVALGLNGLNLEUASN
2   SERPROASPGLNGLNGLULEUGLNCYSALA
3   LEUARGLYSLEUSERGLNILEALASERGLY
4   GLYASNGLUGLNILEGLNALAVALILEASP
5   ALAGLYALALEUPROALALEUVALGLNLEU
6   LEUSERSERPROASNGLUGLNILELEUGLN
7   GLUALALEUTRPALALEUSERASNILEALA
8   SERGLYGLYASNGLUGLNLYSGLNALAVAL
9   LYSGLUALAGLYALALEUGLULYSLEUGLU
10   GLNLEUGLNSERHISGLUASNGLULYSILE
11   GLNLYSGLUALAGLNGLUALALEUGLULYS
12   LEUGLNSERHIS

Samples:

sample_1: S20C_YMA, [U-99% 15N], 150 uM; Na2HPO4 20 mM; trimethylsilylpropanoate 2 mM

sample_2: S20C_YMA, [U-99% 15N], 150 uM; Na2HPO4 20 mM; trimethylsilylpropanoate 2 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN v4.0.4 - collection, processing

CARA - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AVANCE NEO 600 MHz

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