BMRB Entry 19598

Title:
1H, 13C, and 15N Chemical Shift Assignments for human EPRS WHEP domains
Deposition date:
2013-11-04
Original release date:
2014-02-11
Authors:
Shin, ChinHo
Citation:

Citation: Shin, Chinho; Hwang, Geum-Sook; Ahn, Hee-Chul; Kim, Sunghoon; Kim, Key-Sun. "(1)H, (13)C and (15)N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase."  Biomol. NMR Assignments 9, 25-30 (2015).
PubMed: 24378977

Assembly members:

Assembly members:
human_EPRS_WHEP_domains, polymer, 208 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts770
15N chemical shifts211
1H chemical shifts1299

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human EPRS WHEP domains1

Entities:

Entity 1, human EPRS WHEP domains 208 residues - Formula weight is not available

1   ASPSERLEUVALLEUTYRASNARGVALALA
2   VALGLNGLYASPVALVALARGGLULEULYS
3   ALALYSLYSALAPROLYSGLUASPVALASP
4   ALAALAVALLYSGLNLEULEUSERLEULYS
5   ALAGLUTYRLYSGLULYSTHRGLYGLNGLU
6   TYRLYSPROGLYASNPROPROALAGLUILE
7   GLYGLNASNILESERSERASNSERSERALA
8   SERILELEUGLUSERLYSSERLEUTYRASP
9   GLUVALALAALAGLNGLYGLUVALVALARG
10   LYSLEULYSALAGLULYSSERPROLYSALA
11   LYSILEASNGLUALAVALGLUCYSLEULEU
12   SERLEULYSALAGLNTYRLYSGLULYSTHR
13   GLYLYSGLUTYRILEPROGLYGLNPROPRO
14   LEUSERGLNSERSERASPSERSERPROTHR
15   ARGASNSERGLUPROALAGLYLEUGLUTHR
16   PROGLUALALYSVALLEUPHEASPLYSVAL
17   ALASERGLNGLYGLUVALVALARGLYSLEU
18   LYSTHRGLULYSALAPROLYSASPGLNVAL
19   ASPILEALAVALGLNGLULEULEUGLNLEU
20   LYSALAGLNTYRLYSSERLEUILEGLYVAL
21   GLUTYRLYSPROVALSERALATHR

Samples:

sample_1: human EPRS WHEP domains, [U-95% 13C; U-90% 15N], 2 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRPipe, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian Unity 900 MHz

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