BMRB Entry 27279

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27279

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Title:
Backbone 1H, 13C, 15N chemical shift assignments for T cell receptor N30 beta subunit C domain mutant c1
Deposition date:
2017-10-11
Original release date:
2017-11-14
Authors:
Mallis, Robert; Arthanari, Haribabu; Reinherz, Ellis; Wagner, Gerhard
Citation:

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).
PubMed: 26056289

Assembly members:

Assembly members:
N30b-c1, polymer, 241 residues, 27003.96 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet11d

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N30b-c1: MEAGVTQSPRYAVLQEGQSV SFWCDPISGHDTLYWYQQPR DQGPQLLVYFRDEAVIDNSQ LPSDRFSAVRPKGTNSTLKI QSAKQGDTATYLCASSSGVG TEVFFGKGTRLTVVEDLRNV TPPKVSLREPSKAEIANKQK ATLQCQARGFFPDHVELSWW VNGKEVHSGVSTDPQAYKES NYSYSLSSRLRVSATFWHNP RNHFRCQVQFHGLSEEDKWP EGSPKPVTQNISAEAWGRAD S

Data sets:
Data typeCount
13C chemical shifts610
15N chemical shifts213
1H chemical shifts213

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N30 beta subunit C domain mutant c1 (F128R/V144Q/L146Q)1

Entities:

Entity 1, N30 beta subunit C domain mutant c1 (F128R/V144Q/L146Q) 241 residues - 27003.96 Da.

1   METGLUALAGLYVALTHRGLNSERPROARG
2   TYRALAVALLEUGLNGLUGLYGLNSERVAL
3   SERPHETRPCYSASPPROILESERGLYHIS
4   ASPTHRLEUTYRTRPTYRGLNGLNPROARG
5   ASPGLNGLYPROGLNLEULEUVALTYRPHE
6   ARGASPGLUALAVALILEASPASNSERGLN
7   LEUPROSERASPARGPHESERALAVALARG
8   PROLYSGLYTHRASNSERTHRLEULYSILE
9   GLNSERALALYSGLNGLYASPTHRALATHR
10   TYRLEUCYSALASERSERSERGLYVALGLY
11   THRGLUVALPHEPHEGLYLYSGLYTHRARG
12   LEUTHRVALVALGLUASPLEUARGASNVAL
13   THRPROPROLYSVALSERLEUARGGLUPRO
14   SERLYSALAGLUILEALAASNLYSGLNLYS
15   ALATHRLEUGLNCYSGLNALAARGGLYPHE
16   PHEPROASPHISVALGLULEUSERTRPTRP
17   VALASNGLYLYSGLUVALHISSERGLYVAL
18   SERTHRASPPROGLNALATYRLYSGLUSER
19   ASNTYRSERTYRSERLEUSERSERARGLEU
20   ARGVALSERALATHRPHETRPHISASNPRO
21   ARGASNHISPHEARGCYSGLNVALGLNPHE
22   HISGLYLEUSERGLUGLUASPLYSTRPPRO
23   GLUGLYSERPROLYSPROVALTHRGLNASN
24   ILESERALAGLUALATRPGLYARGALAASP
25   SER

Samples:

sample_1: N30b-c1, [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:

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

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

NMR spectrometers:

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

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