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 27280

Title: Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N15 beta subunit C domain mutant m22   PubMed: 26056289

Deposition date: 2017-10-11 Original release date: 2017-11-14

Authors: Mallis, Robert; Arthanari, Haribabu; Reinherz, Ellis; Wagner, Gerhard

Citation: Mallis, Robert; Bai, Ke; Arthanari, Haribabu; Hussey, Rebecca; Li, Zhenhai; Chingozha, Loice; Duke-Cohan, Jonathan; Lu, Hang; Wang, Jia-Huai; Zhu, Cheng; Wagner, Gerhard; Reinherz, Ellis. "Pre-TCR ligand binding impacts thymocyte development before TCR expression."  Proc. Natl. Acad. Sci. U.S.A. 112, 8373-8378 (2015).

Assembly members:
N15b-m22, polymer, 240 residues, 27278.55 Da.

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

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

Entity Sequences (FASTA):
N15b-m22: MDSGVVQSPRHIIKEKGGRS VLTCIPISGHSNVVWYQQTL GKELKFLIQHAAKVERDKGF LPSRFSVQQFDDYHSEMNMS ALELEDSAMYFCASSLRWGD EQYFGPGTRLTVLEDLRNVT PPKVSLREPSKAEIANKQKA TLQCQARGFFPDHVELSWWV NGKEVHSGVSTDPQAYKESN YSYSLSSRLRVSATFWHNPR NHFRCQVQFHGLSEEDKWPE GSPKPVTQNISAEAWGRADS

Data sets:
Data typeCount
13C chemical shifts593
15N chemical shifts206
1H chemical shifts206

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N15 beta subunit C domain mutant m22 (Y50A/E51A/F128R/V144Q/L146Q)1

Entities:

Entity 1, N15 beta subunit C domain mutant m22 (Y50A/E51A/F128R/V144Q/L146Q) 240 residues - 27278.55 Da.

1   METASPSERGLYVALVALGLNSERPROARG
2   HISILEILELYSGLULYSGLYGLYARGSER
3   VALLEUTHRCYSILEPROILESERGLYHIS
4   SERASNVALVALTRPTYRGLNGLNTHRLEU
5   GLYLYSGLULEULYSPHELEUILEGLNHIS
6   ALAALALYSVALGLUARGASPLYSGLYPHE
7   LEUPROSERARGPHESERVALGLNGLNPHE
8   ASPASPTYRHISSERGLUMETASNMETSER
9   ALALEUGLULEUGLUASPSERALAMETTYR
10   PHECYSALASERSERLEUARGTRPGLYASP
11   GLUGLNTYRPHEGLYPROGLYTHRARGLEU
12   THRVALLEUGLUASPLEUARGASNVALTHR
13   PROPROLYSVALSERLEUARGGLUPROSER
14   LYSALAGLUILEALAASNLYSGLNLYSALA
15   THRLEUGLNCYSGLNALAARGGLYPHEPHE
16   PROASPHISVALGLULEUSERTRPTRPVAL
17   ASNGLYLYSGLUVALHISSERGLYVALSER
18   THRASPPROGLNALATYRLYSGLUSERASN
19   TYRSERTYRSERLEUSERSERARGLEUARG
20   VALSERALATHRPHETRPHISASNPROARG
21   ASNHISPHEARGCYSGLNVALGLNPHEHIS
22   GLYLEUSERGLUGLUASPLYSTRPPROGLU
23   GLYSERPROLYSPROVALTHRGLNASNILE
24   SERALAGLUALATRPGLYARGALAASPSER

Samples:

sample_1: N15b-m22, [U-13C; U-15N; U-2H], 0.4 mM; sodium chloride 150 mM; sodium phosphate 50 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 250 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CARA v1.90, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz
  • Varian INOVA 600 MHz

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