BMRB Entry 11544

Title:
DESIGNED ARMADILLO REPEAT PROTEIN SELF-ASSEMBLED COMPLEX (YIIM2-MAII)
Deposition date:
2013-11-22
Original release date:
2014-07-21
Authors:
Zerbe, Oliver; Christen, Martin; Plueckthun, Andreas; Watson, Randall
Citation:

Citation: Watson, Randall; Christen, Martin; Ewald, Christina; Bumback, Fabian; Reichen, Christian; Mihajlovic, Maja; Schmidt, E.; Guntert, Peter; Caflisch, Amedeo; Plueckthun, Andreas; Zerbe, Oliver. "Spontaneous Self-Assembly of Fragments of Engineered Armadillo Repeat Proteins into Folded Proteins"  Structure 22, 985-995 (2014).
PubMed: 24931467

Assembly members:

Assembly members:
YM2, polymer, 115 residues, 12193.641 Da.
MA, polymer, 84 residues, 9104.170 Da.

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: pLIC_CR

Data sets:
Data typeCount
13C chemical shifts632
15N chemical shifts186
1H chemical shifts1081

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1YM21
2MA2

Entities:

Entity 1, YM2 115 residues - 12193.641 Da.

1   GLYGLULEUPROGLNMETTHRGLNGLNLEU
2   ASNSERASPASPMETGLNGLUGLNLEUSER
3   ALATHRARGLYSPHESERGLNILELEUSER
4   ASPGLYASNGLUGLNILEGLNALAVALILE
5   ASPALAGLYALALEUPROALALEUVALGLN
6   LEULEUSERSERPROASNGLUGLNILELEU
7   GLNGLUALALEUTRPALALEUSERASNILE
8   ALASERGLYGLYASNGLUGLNILEGLNALA
9   VALILEASPALAGLYALALEUPROALALEU
10   VALGLNLEULEUSERSERPROASNGLUGLN
11   ILELEUGLNGLUALALEUTRPALALEUSER
12   ASNILEALASERGLY

Entity 2, MA 84 residues - 9104.170 Da.

1   GLYASNGLUGLNILEGLNALAVALILEASP
2   ALAGLYALALEUPROALALEUVALGLNLEU
3   LEUSERSERPROASNGLUGLNILELEUGLN
4   GLUALALEUTRPALALEUSERASNILEALA
5   SERGLYGLYASNGLUGLNLYSGLNALAVAL
6   LYSGLUALAGLYALALEUGLULYSLEUGLU
7   GLNLEUGLNSERHISGLUASNGLULYSILE
8   GLNLYSGLUALAGLNGLUALALEUGLULYS
9   LEUGLNSERHIS

Samples:

sample_1: YM2, [U-13C; U-15N], 1.0 mM; MA 1.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; glycerol 2%; TMSP 1 mM; sodium azide 0.02%; H2O 88%; D2O 10%

sample_2: YM2 0.90 mM; MA, [U-13C; U-15N], 0.75 mM; sodium phosphate 50 mM; sodium chloride 150 mM; glycerol 2%; TMSP 1 mM; sodium azide 0.02%; H2O 88%; D2O 10%

sample_conditions_1: ionic strength: 285 mM; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
4D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D-13C edited/filtered NOESYsample_1isotropicsample_conditions_1
3D-13C-edited/filtered NOESYsample_2isotropicsample_conditions_1
3D-15N-edited/filtered NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment

CcpNMR v2.3.1, CCPN - chemical shift assignment, data analysis, peak picking

UNIO v2.0.2, (UNIO) Herrmann - data analysis, peak picking, structure solution

CYANA v3.96a, Guntert, Mumenthaler and Wuthrich - geometry optimization, structure solution

X-PLOR_NIH v2.32, Schwieters, Kuszewski, Tjandra and Clore - refinement

TALOS-N v4.01, Shen and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz
  • Varian DirectDrive 700 MHz

Related Database Links:

PDB
BMRB 11548

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