BMRB Entry 18693

Title:
1H, 13C, and 15N resonance assignments of mouse peptide ESP4
Deposition date:
2012-08-31
Original release date:
2013-02-12
Authors:
Taniguchi, Masahiro
Citation:

Citation: Taniguchi, Masahiro; Yoshinaga, Sosuke; Haga-Yamanaka, Sachiko; Touhara, Kazushige; Terasawa, Hiroaki. "Backbone and side-chain H, 15N and 13C assignments of mouse peptide ESP4."  Biomol. NMR Assignments 8, 7-9 (2014).
PubMed: 23179060

Assembly members:

Assembly members:
ESP4, polymer, 104 residues, Formula weight is not available

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   Vector: pET28A

Data sets:
Data typeCount
13C chemical shifts410
15N chemical shifts100
1H chemical shifts645

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Exocrine gland-secreting peptide 41

Entities:

Entity 1, Exocrine gland-secreting peptide 4 104 residues - Formula weight is not available

1   GLYSERGLYARGVALLEUTHRGLNTHRGLY
2   LYSGLUTHRTHRMETSERALAASPHISLYS
3   THRASNHISLYSALAASPLEUGLULYSASN
4   ASPSERGLNGLYGLUARGASNTHRGLNGLU
5   ALAPHEGLUMETILELEUCYSALAPHEASN
6   GLNGLULYSMETLEULEULYSASPGLNALA
7   ASNSERGLYGLNHISGLULEULYSLEUSER
8   LYSPHEPHETHRALALEUSERLYSCYSGLY
9   ALAGLNASNTYRGLNVALASPTHRVALASN
10   TYRARGILEILEPROHISILETYRPROLEU
11   HISSERPROLYS

Samples:

sample_1: ESP4, [U-100% 13C; U-100% 15N], 100 uM; H2O 90%; D2O 10%

sample_2: ESP4, [U-100% 15N], 100 uM; H2O 90%; D2O 10%

sample_3: ESP4, [U-100% 13C; U-100% 15N], 100 uM; D2O 100%

sample_conditions_1: pH: 3.5; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - collection, peak picking, processing

Olivia, Yokochi, Sekiguchi and Inagaki - chemical shift assignment, chemical shift calculation, data analysis

TOPSPIN, Bruker Biospin - collection, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

DBJ BAF92721
REF NP_001171054

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