BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 27563

Title: 14-3-3 Sigma Backbone Assignment   PubMed: 30377945

Deposition date: 2018-07-26 Original release date: 2018-11-15

Authors: Neves, Joao; Merzougui, Hamida; Boll, Emmanuelle; Hanoulle, Xavier; Landrieu, Isabelle; Cantrelle, Francois-Xavier

Citation: Neves, Joao Filipe; Landrieu, Isabelle; Merzougui, Hamida; Boll, Emmanuelle; Hanoulle, Xavier; Cantrelle, Francois-Xavier. "Backbone chemical shift assignments of human 14-3-3sigma."  Biomol. NMR Assign. 13, 103-107 (2019).

Assembly members:
14-3-3_Sigma, polymer, 236 residues, Formula weight is not available

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
14-3-3_Sigma: GAMGSMERASLIQKAKLAEQ AERYEDMAAFMKGAVEKGEE LSCEERNLLSVAYKNVVGGQ RAAWRVLSSIEQKSNEEGSE EKGPEVREYREKVETELQGV CDTVLGLLDSHLIKEAGDAE SRVFYLKMKGDYYRYLAEVA TGDDKKRIIDSARSAYQEAM DISKKEMPPTNPIRLGLALN FSVFHYEIANSPEEAISLAK TTFDEAMADLHTLSEDSYKD STLIMQLLRDNLTLWT

Data sets:
Data typeCount
13C chemical shifts563
15N chemical shifts177
1H chemical shifts177

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
114-3-3_Sigma, chain 11
214-3-3_Sigma, chain 21

Entities:

Entity 1, 14-3-3_Sigma, chain 1 236 residues - Formula weight is not available

Residues 'GAMGS' represent a linker between the cleaved tag and the protein. Therefore M6 corresponds to M1.

1   GLYALAMETGLYSERMETGLUARGALASER
2   LEUILEGLNLYSALALYSLEUALAGLUGLN
3   ALAGLUARGTYRGLUASPMETALAALAPHE
4   METLYSGLYALAVALGLULYSGLYGLUGLU
5   LEUSERCYSGLUGLUARGASNLEULEUSER
6   VALALATYRLYSASNVALVALGLYGLYGLN
7   ARGALAALATRPARGVALLEUSERSERILE
8   GLUGLNLYSSERASNGLUGLUGLYSERGLU
9   GLULYSGLYPROGLUVALARGGLUTYRARG
10   GLULYSVALGLUTHRGLULEUGLNGLYVAL
11   CYSASPTHRVALLEUGLYLEULEUASPSER
12   HISLEUILELYSGLUALAGLYASPALAGLU
13   SERARGVALPHETYRLEULYSMETLYSGLY
14   ASPTYRTYRARGTYRLEUALAGLUVALALA
15   THRGLYASPASPLYSLYSARGILEILEASP
16   SERALAARGSERALATYRGLNGLUALAMET
17   ASPILESERLYSLYSGLUMETPROPROTHR
18   ASNPROILEARGLEUGLYLEUALALEUASN
19   PHESERVALPHEHISTYRGLUILEALAASN
20   SERPROGLUGLUALAILESERLEUALALYS
21   THRTHRPHEASPGLUALAMETALAASPLEU
22   HISTHRLEUSERGLUASPSERTYRLYSASP
23   SERTHRLEUILEMETGLNLEULEUARGASP
24   ASNLEUTHRLEUTRPTHR

Samples:

sample_1: 14-3-3 Sigma, [U-13C; U-15N; U-2H], 0.9 mM; sodium phosphate 100 mM; sodium chloride 50 mM; DTT 1 mM; H2O 90 % v/v; D2O, [U-2H], 10 % v/v; TMSP 0.1 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 6.8; pressure: 1 atm; temperature: 305 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSY HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESY HMQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.5, Bruker Biospin - collection, processing

SPARKY v3.12, Goddard - chemical shift assignment, chemical shift calculation, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts