BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 51375

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51375

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Title: 15N-1H chemical shifts for the murine Syk tandem SH2 domains flexible linker construct [tSH2-FX, Ser 8 to Gln 264 with interdomain residues 119-162 replaced by a 20-amino-acid flexible linker (GGS)3GS(GGS)3] complexed with C-IHP peptide   PubMed: 26468009

Deposition date: 2022-03-18 Original release date: 2022-04-18

Authors: Feng, Chao; Post, Carol

Citation: Feng, Chao; Post, Carol Beth. "Insights into the allosteric regulation of Syk association with receptor ITAM, a multi-state equilibrium."  Phys. Chem. Chem. Phys. 18, 5807-5818 (2016).

Assembly members:
entity_1, polymer, 233 residues, Formula weight is not available
entity_2, polymer, 13 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-30a(+)

Entity Sequences (FASTA):
entity_1: SANHLTYFFGNITREEAEDY LVQGGMTDGLYLLRQSRNYL GGFALSVAHNRKAHHYTIER ELNGTYAISGGRAHASPADL CHYHSQEPDGLICLLKKPFN RPPGVQPKTGPGGSGGSGGS GSGGSGGSGGSEKMPWFHGN ISRDESEQTVLIGSKTNGKF LIRARDNSGSYALCLLHEGK VLHYRIDRDKTGKLSIPEGK KFDTLWQLVEHYSYKPDGLL RVLTVPCQKIGTQ
entity_2: XQRDLXSGLNQRX

Data sets:
Data typeCount
15N chemical shifts130
1H chemical shifts130

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1murine Syk tandem SH2 domains flexible linker construct1
2C-IHP peptide2

Entities:

Entity 1, murine Syk tandem SH2 domains flexible linker construct 233 residues - Formula weight is not available

1   SERALAASNHISLEUTHRTYRPHEPHEGLY
2   ASNILETHRARGGLUGLUALAGLUASPTYR
3   LEUVALGLNGLYGLYMETTHRASPGLYLEU
4   TYRLEULEUARGGLNSERARGASNTYRLEU
5   GLYGLYPHEALALEUSERVALALAHISASN
6   ARGLYSALAHISHISTYRTHRILEGLUARG
7   GLULEUASNGLYTHRTYRALAILESERGLY
8   GLYARGALAHISALASERPROALAASPLEU
9   CYSHISTYRHISSERGLNGLUPROASPGLY
10   LEUILECYSLEULEULYSLYSPROPHEASN
11   ARGPROPROGLYVALGLNPROLYSTHRGLY
12   PROGLYGLYSERGLYGLYSERGLYGLYSER
13   GLYSERGLYGLYSERGLYGLYSERGLYGLY
14   SERGLULYSMETPROTRPPHEHISGLYASN
15   ILESERARGASPGLUSERGLUGLNTHRVAL
16   LEUILEGLYSERLYSTHRASNGLYLYSPHE
17   LEUILEARGALAARGASPASNSERGLYSER
18   TYRALALEUCYSLEULEUHISGLUGLYLYS
19   VALLEUHISTYRARGILEASPARGASPLYS
20   THRGLYLYSLEUSERILEPROGLUGLYLYS
21   LYSPHEASPTHRLEUTRPGLNLEUVALGLU
22   HISTYRSERTYRLYSPROASPGLYLEULEU
23   ARGVALLEUTHRVALPROCYSGLNLYSILE
24   GLYTHRGLN

Entity 2, C-IHP peptide 13 residues - Formula weight is not available

1   ACEGLNARGASPLEUPTRSERGLYLEUASN
2   GLNARGNH2

Samples:

sample_1: murine Syk tandem SH2 domains flexible linker construct, [U-99% 15N], 0.3 mM; sodium phosphate 50 mM; DTT 5 mM; sodium azide 0.02%; C-IHP peptide 12 mM

sample_conditions_1: ionic strength: 0.13 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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