BMRB Entry 25367

Title:
Chemical Shifts of the designed Armadillo Repeat Protein YMRRA
Deposition date:
2014-11-26
Original release date:
2015-06-04
Authors:
Ewald, Christina; Zerbe, Oliver
Citation:

Citation: Ewald, Christina; Christen, Martin; Watson, Randall; Mihajlovic, Maja; Zhou, Ting; Honegger, Annemarie; Plueckthun, Andreas; Caflisch, Amedeo; Zerbe, Oliver. "A combined NMR and computational approach to investigate Peptide binding to a designed armadillo repeat protein"  J. Mol. Biol. 427, 1916-1933 (2015).
PubMed: 25816772

Assembly members:

Assembly members:
YMRRA, polymer, 211 residues, Formula weight is not available

Natural source:

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

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts445
15N chemical shifts160
1H chemical shifts160

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YMRRA1

Entities:

Entity 1, YMRRA 211 residues - Formula weight is not available

Residues 1-12 represent a non-native affifity tag for purification.

1   METARGGLYSERHISHISHISHISHISHIS
2   GLYSERGLULEUPROGLNMETTHRGLNGLN
3   LEUASNSERASPASPMETGLNGLUGLNLEU
4   SERALATHRVALLYSPHEARGGLNILELEU
5   SERARGASPGLYASNGLUGLNILEGLNALA
6   VALILEASPALAGLYALALEUPROALALEU
7   VALGLNLEULEUSERSERPROASNGLUGLN
8   ILELEUGLNGLUALALEUTRPALALEUSER
9   ASNILEALASERGLYGLYASNGLUGLNTHR
10   GLNALAVALILEASPALAGLYALALEUPRO
11   ALALEUVALGLNLEULEUSERSERPROASN
12   GLUGLNILELEUGLNTYRALALEUILEALA
13   LEUASNASNILEALAPHEALAGLYASNGLU
14   GLNTHRGLNALAVALILEASPALAGLYALA
15   LEUPROALALEUVALGLNLEULEUSERSER
16   PROASNGLYGLNILELEUGLNGLUTHRLEU
17   TRPALALEUTHRASNILEALAMETGLUGLY
18   ASNGLUGLNLYSGLNALAVALLYSGLUALA
19   GLYALALEUGLULYSLEUGLUGLNLEUGLN
20   SERHISGLUASNGLULYSILEGLNLYSGLU
21   ALAGLNGLUALALEUGLULYSLEUGLNSER
22   HIS

Samples:

sample_1: YMRRA, [U-13C; U-15N; U-2H], 800 uM; NaCl 150 mM; Na-phosphate 50 mM; glycerol 2%

sample_conditions_1: ionic strength: 0.425 M; pH: 7.4; pressure: 1 atm; temperature: 307 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
HN(CACO)NNHsample_1isotropicsample_conditions_1

Software:

CARA v1.9, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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