BMRB Entry 16426

Title:
NMR-derived structure of residues 29-138 of murine Ets-1, containing the PNT domain, along with phosphorylated Thr38 and Ser41
Deposition date:
2009-07-27
Original release date:
2009-12-18
Authors:
Kang, Hyun-Seo; Lee, Gregory; Nelson, Mary; Graves, Barbara; Blaszczak, Adam; McIntosh, Lawrence
Citation:

Citation: McIntosh, Lawrence; Kang, Hyun-Seo; Okon, Mark; Nelson, Mary; Graves, Barbara; Brutscher, Bernhard. "Detection and assignment of phosphoserine and phosphothreonine residues by (13)C- (31)P spin-echo difference NMR spectroscopy."  J. Biomol. NMR 43, 31-37 (2009).
PubMed: 19002654

Assembly members:

Assembly members:
murine Ets-1, polymer, 113 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts503
15N chemical shifts119
1H chemical shifts797
heteronuclear NOE values103
T1 relaxation values103
T2 relaxation values103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1murine Ets-11

Entities:

Entity 1, murine Ets-1 113 residues - Formula weight is not available

1   GLYSERHISMETGLUCYSALAASPVALPRO
2   LEULEUTPOPROSERSEPLYSGLUMETMET
3   SERGLNALALEULYSALATHRPHESERGLY
4   PHETHRLYSGLUGLNGLNARGLEUGLYILE
5   PROLYSASPPROARGGLNTRPTHRGLUTHR
6   HISVALARGASPTRPVALMETTRPALAVAL
7   ASNGLUPHESERLEULYSGLYVALASPPHE
8   GLNLYSPHECYSMETSERGLYALAALALEU
9   CYSALALEUGLYLYSGLUCYSPHELEUGLU
10   LEUALAPROASPPHEVALGLYASPILELEU
11   TRPGLUHISLEUGLUILELEUGLNLYSGLU
12   ASPVALLYS

Samples:

sample_1: 2P-ETS1PNT, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
IPAPsample_1isotropicsample_conditions_1
CLEANEXsample_1isotropicsample_conditions_1
T1_T2_HNNOEsample_1isotropicsample_conditions_1
HNCOCA_HACAsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SCULPTOR, (SCULPTOR)-Martin Blackledge - refinement

SPARKY, Goddard - chemical shift assignment

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

Molmol, Koradi, Billeter and Wuthrich - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

VNMR, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

BMRB 4205
PDB
DBJ BAE40197
EMBL CAA37904
GB AAA21093 AAA63299 AAH10588 AAH13089 AAI01928
REF NP_001033731 NP_035938 NP_036687 XP_003500343 XP_005347065
SP P27577 P41156
AlphaFold P27577 P41156

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