BMRB Entry 17325

Title:
1H, 13C and 15N resonance assignment of the 117 residue fragment of Engrailed 2, a partially disordered protein.
Deposition date:
2010-11-27
Original release date:
2011-05-05
Authors:
Augustyniak, Rafal; Ferrage, Fabien; Bodenhausen, Geoffrey; Lequin, Olivier
Citation:

Citation: Augustyniak, Rafal; Balayssac, Stephane; Ferrage, Fabien; Bodenhausen, Geoffrey; Lequin, Olivier. "1H, 13C and 15N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered protein."  Biomol. NMR Assignments 5, 229-231 (2011).
PubMed: 21516336

Assembly members:

Assembly members:
Engrailed_2, polymer, 117 residues, 13457.1 Da.

Natural source:

Natural source:   Common Name: chicken   Taxonomy ID: 9031   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Gallus gallus

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts520
15N chemical shifts127
1H chemical shifts792

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Engrailed 21

Entities:

Entity 1, Engrailed 2 117 residues - 13457.1 Da.

1   GLYPROMETGLULEUSERVALSERSERASP
2   SERASPSERSERGLNALAGLYSERASNALA
3   GLYASNGLNPROMETLEUTRPPROALATRP
4   VALTYRCYSTHRARGTYRSERASPARGPRO
5   SERSERGLYPROARGSERARGLYSPROLYS
6   LYSLYSASNPROASNLYSGLUASPLYSARG
7   PROARGTHRALAPHETHRALAGLUGLNLEU
8   GLNARGLEULYSALAGLUPHEGLNTHRASN
9   ARGTYRLEUTHRGLUGLNARGARGGLNSER
10   LEUALAGLNGLULEUGLYLEUASNGLUSER
11   GLNILELYSILETRPPHEGLNASNLYSARG
12   ALALYSILELYSLYSALATHR

Samples:

sample_1: Engrailed 2, [U-15N], 0.6 ± 0.1 mM; D2O 10%; DSS 0.111 mM; TCEP 10 mM; AEBSF protease inhibitor 1 uM; leupeptin 2 uM; pepstatin A 2 uM; EDTA 0.02 mM; sodium azide 0.02%; sodium succinat 40 mM; H2O 90%

sample_2: Engrailed 2, [U-13C; U-15N], 0.6 mM; D2O 10%; DSS 0.111 mM; TCEP 10 mM; AEBSF protease inhibitor 1 uM; leupeptin 2 uM; pepstatin A 2 uM; EDTA 0.02 mM; sodium azide 0.02%; sodium succinat 40 mM; H2O 90%

sample_3: Engrailed 2, [U-13C; U-15N], 0.6 mM; D2O 100%; DSS 0.111 mM; TCEP 10 mM; AEBSF protease inhibitor 1 uM; leupeptin 2 uM; pepstatin A 2 uM; EDTA 0.02 mM; sodium azide 0.02%; sodium succinat 40 mM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HBCB(CGCD)HDsample_3isotropicsample_conditions_1
3D HBCB(CGCE)HEsample_3isotropicsample_conditions_1
4D HC(CC-TOCSY)CONHsample_2isotropicsample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection

ANALYSIS v2.0, CCPN - chemical shift assignment

VNMR, Varian - collection

NMR spectrometers:

  • Bruker Avance III 500 MHz
  • Varian INOVA 700 MHz

Related Database Links:

DBJ BAE34186
EMBL CAA68362
GB AAA53438 AAA53527 AAF68670 AAI41439 AAI46582
REF NP_001102684 NP_001254648 NP_034264 XP_002187765 XP_002687029
SP P09066 Q05917
TPG DAA30339
AlphaFold P09066 Q05917

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