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Biological Magnetic Resonance Data Bank


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BMRB Entry 51370

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51370

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Title: 15N-1H chemical shifts for the murine Syk tandem SH2 domains phosphorylation mimic construct (tSH2-PM, Ser 8 to Gln 264 with Y130E) complexed with N-IHP peptide   PubMed: 26468009

Deposition date: 2022-03-17 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, 257 residues, Formula weight is not available
entity_2, polymer, 11 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 RPPGVQPKTGPFEDLKENLI REEVKQTWNLQGQALEQAII SQKPQLEKLIATTAHEKMPW FHGNISRDESEQTVLIGSKT NGKFLIRARDNSGSYALCLL HEGKVLHYRIDRDKTGKLSI PEGKKFDTLWQLVEHYSYKP DGLLRVLTVPCQKIGAQ
entity_2: XPDXEPIRKGX

Data sets:
Data typeCount
15N chemical shifts142
1H chemical shifts142

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1murine Syk tandem SH2 domains phosphorylation mimic construct (tSH2-PM, Ser 8 to Gln 264 with Y130E)1
2N-IHP peptide2

Entities:

Entity 1, murine Syk tandem SH2 domains phosphorylation mimic construct (tSH2-PM, Ser 8 to Gln 264 with Y130E) 257 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   PROPHEGLUASPLEULYSGLUASNLEUILE
13   ARGGLUGLUVALLYSGLNTHRTRPASNLEU
14   GLNGLYGLNALALEUGLUGLNALAILEILE
15   SERGLNLYSPROGLNLEUGLULYSLEUILE
16   ALATHRTHRALAHISGLULYSMETPROTRP
17   PHEHISGLYASNILESERARGASPGLUSER
18   GLUGLNTHRVALLEUILEGLYSERLYSTHR
19   ASNGLYLYSPHELEUILEARGALAARGASP
20   ASNSERGLYSERTYRALALEUCYSLEULEU
21   HISGLUGLYLYSVALLEUHISTYRARGILE
22   ASPARGASPLYSTHRGLYLYSLEUSERILE
23   PROGLUGLYLYSLYSPHEASPTHRLEUTRP
24   GLNLEUVALGLUHISTYRSERTYRLYSPRO
25   ASPGLYLEULEUARGVALLEUTHRVALPRO
26   CYSGLNLYSILEGLYALAGLN

Entity 2, N-IHP peptide 11 residues - Formula weight is not available

1   ACEPROASPPTRGLUPROILEARGLYSGLY
2   NH2

Samples:

sample_1: murine Syk tandem SH2 domains phosphorylation mimic construct (tSH2-PM, Ser 8 to Gln 264 with Y130E), [U-99% 15N], 0.3 mM; sodium phosphate 50 mM; DTT 5 mM; sodium azide 0.02%; N-IHP peptide 6 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