BMRB Entry 4205

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4205

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Title:
Structure of the Ets-1 Pointed Domain and Mitogen-activiated Protein Kinase Phosphorylation Site.
Deposition date:
1998-09-22
Original release date:
1999-12-22
Authors:
Slupsky, C.; Gentile, L.; Donaldson, L.; Mackereth, C.; Seidel, J.; Graves, B.; Mcintosh, L.
Citation:

Citation: Slupsky, C.; Gentile, L.; Donaldson, L.; Mackereth, C.; Seidel, J.; Graves, B.; Mcintosh, L.. "Structure of the Ets-1 Pointed Domain and Mitogen-activiated Protein Kinase Phosphorylation Site."  Proc. Natl. Acad. Sci. U.S.A. 95, 12129-12134 (1998).

Assembly members:

Assembly members:
ETS-1 Pointed domain, polymer, 110 residues, 12553.5 Da.

Natural source:

Natural source:   Common Name: House Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ETS-1 Pointed domain: MECADVPLLTPSSKEMMSQA LKATFSGFTKEQQRLGIPKD PRQWTETHVRDWVMWAVNEF SLKGVDFQKFCMSGAALCAL GKECFLELAPDFVGDILWEH LEILQKEDVK

Data sets:
Data typeCount
13C chemical shifts485
15N chemical shifts116
1H chemical shifts769

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ets-1 PNT1

Entities:

Entity 1, Ets-1 PNT 110 residues - 12553.5 Da.

1   METGLUCYSALAASPVALPROLEULEUTHR
2   PROSERSERLYSGLUMETMETSERGLNALA
3   LEULYSALATHRPHESERGLYPHETHRLYS
4   GLUGLNGLNARGLEUGLYILEPROLYSASP
5   PROARGGLNTRPTHRGLUTHRHISVALARG
6   ASPTRPVALMETTRPALAVALASNGLUPHE
7   SERLEULYSGLYVALASPPHEGLNLYSPHE
8   CYSMETSERGLYALAALALEUCYSALALEU
9   GLYLYSGLUCYSPHELEUGLULEUALAPRO
10   ASPPHEVALGLYASPILELEUTRPGLUHIS
11   LEUGLUILELEUGLNLYSGLUASPVALLYS

Samples:

sample_1: ETS-1 Pointed domain, [U-99% 15N; U-99% 13C], mM; KPO4 10 mM; KCl 10 mM; DTT 10 mM

sample_cond_1: ionic strength: 20 mM; pH*: 6.5; pressure: 1.0 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
15N-HSQCsample_1not availablenot available
13C-HSQCsample_1not availablenot available
HNCACBsample_1not availablenot available
HNHBsample_1not availablenot available
CBCA(CO)NNHsample_1not availablenot available
H(CCO)NHsample_1not availablenot available
C(CO)NHsample_1not availablenot available
15N-EDITED-NOESYsample_1not availablenot available
13C-EDITED-NOESYsample_1not availablenot available
2D-NOESYsample_1not availablenot available
15N-EDITED TOCSYsample_1not availablenot available
HCCHTOCSYsample_1not availablenot available
HMBCsample_1not availablenot available
2D-COSYsample_1not availablenot available
HMQC-Jsample_1not availablenot available
HNHAsample_1not availablenot available
LONG RANGE 13Cg-15N and -13C' SPIN ECHOsample_1not availablenot available

Software:

NMRPipe -

PIPP -

NMR spectrometers:

  • VARIAN UNITY 500 MHz

Related Database Links:

BMRB 16426
PDB
DBJ BAC36266 BAE40197 BAF84529 BAG62940 BAG72856
EMBL CAA32903 CAA32904 CAA37904 CAE45783 CAG47050
GB AAA21093 AAA52410 AAA63299 AAH10588 AAH13089
REF NP_001033731 NP_001076130 NP_001092576 NP_001137292 NP_001156358
SP P14921 P27577 P41156
TPG DAA13872
AlphaFold P14921 P27577 P41156

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