BMRB Entry 27440

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27440

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Title:
Long-range effects induced by peptide-MHC binding to a human T cell receptor: Implications for the initiation of T cell signaling
Deposition date:
2018-03-30
Original release date:
2018-08-22
Authors:
He, Yanan; Rangarajan, Sneha; Chen, Yihong; Kerzic, Melissa; Ma, Buyong; Gowthaman, Ragul; Pierce, Brian; Nussinov, Ruth; Mariuzza, Roy; Orban, John
Citation:

Citation: Rangarajan, Sneha; He, Yanan; Chen, Yihong; Kerzic, Melissa; Ma, Buyong; Gowthaman, Ragul; Pierce, Brian; Nussinov, Ruth; Mariuzza, Roy; Orban, John. "Peptide-MHC (pMHC) binding to a human antiviral T cell receptor induces long-range allosteric communication between pMHC- and CD3-binding sites"  J. Biol. Chem. 293, 15991-16005 (2018).
PubMed: 30135211

Assembly members:

Assembly members:
A6TCR_alpha, polymer, 206 residues, Formula weight is not available
A6TCR_beta, polymer, 245 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-26b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
A6TCR_alpha: MQKEVEQNSGPLSVPEGAIA SLNCTYSDRGSQSFFWYRQY SGKSPELIMSIYSNGDKEDG RFTAQLNKASQYVSLLIRDS QPSDSATYLCAVTTDSWGKL QFGAGTQVVVTPDIQNPDPA VYQLRDSKSSDKSVCLFTDF DSQTNVSQSKDSDVYITDKC VLDMRSMDFKSNSAVAWSNK SDFACANAFNNSIIPEDTFF PSPESS
A6TCR_beta: NAGVTQTPKFQVLKTGQSMT LQCAQDMNHEYMSWYRQDPG MGLRLIHYSVGAGITDQGEV PNGYNVSRSTTEDFPLRLLS AAPSQTSVYFCASRPGLAGG RPEQYFGPGTRLTVTEDLKN VFPPEVAVFEPSEAEISHTQ KATLVCLATGFYPDHVELSW WVNGKEVHSGVCTDPQPLKE QPALNDSRYALSSRLRVSAT FWQDPRNHFRCQVQFYGLSE NDEWTQDRAKPVTQIVSAEA WGRAD

Data sets:
Data typeCount
13C chemical shifts398
15N chemical shifts115
1H chemical shifts117

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1A6TCR alpha1
2A6TCR beta2

Entities:

Entity 1, A6TCR alpha 206 residues - Formula weight is not available

1   METGLNLYSGLUVALGLUGLNASNSERGLY
2   PROLEUSERVALPROGLUGLYALAILEALA
3   SERLEUASNCYSTHRTYRSERASPARGGLY
4   SERGLNSERPHEPHETRPTYRARGGLNTYR
5   SERGLYLYSSERPROGLULEUILEMETSER
6   ILETYRSERASNGLYASPLYSGLUASPGLY
7   ARGPHETHRALAGLNLEUASNLYSALASER
8   GLNTYRVALSERLEULEUILEARGASPSER
9   GLNPROSERASPSERALATHRTYRLEUCYS
10   ALAVALTHRTHRASPSERTRPGLYLYSLEU
11   GLNPHEGLYALAGLYTHRGLNVALVALVAL
12   THRPROASPILEGLNASNPROASPPROALA
13   VALTYRGLNLEUARGASPSERLYSSERSER
14   ASPLYSSERVALCYSLEUPHETHRASPPHE
15   ASPSERGLNTHRASNVALSERGLNSERLYS
16   ASPSERASPVALTYRILETHRASPLYSCYS
17   VALLEUASPMETARGSERMETASPPHELYS
18   SERASNSERALAVALALATRPSERASNLYS
19   SERASPPHEALACYSALAASNALAPHEASN
20   ASNSERILEILEPROGLUASPTHRPHEPHE
21   PROSERPROGLUSERSER

Entity 2, A6TCR beta 245 residues - Formula weight is not available

1   ASNALAGLYVALTHRGLNTHRPROLYSPHE
2   GLNVALLEULYSTHRGLYGLNSERMETTHR
3   LEUGLNCYSALAGLNASPMETASNHISGLU
4   TYRMETSERTRPTYRARGGLNASPPROGLY
5   METGLYLEUARGLEUILEHISTYRSERVAL
6   GLYALAGLYILETHRASPGLNGLYGLUVAL
7   PROASNGLYTYRASNVALSERARGSERTHR
8   THRGLUASPPHEPROLEUARGLEULEUSER
9   ALAALAPROSERGLNTHRSERVALTYRPHE
10   CYSALASERARGPROGLYLEUALAGLYGLY
11   ARGPROGLUGLNTYRPHEGLYPROGLYTHR
12   ARGLEUTHRVALTHRGLUASPLEULYSASN
13   VALPHEPROPROGLUVALALAVALPHEGLU
14   PROSERGLUALAGLUILESERHISTHRGLN
15   LYSALATHRLEUVALCYSLEUALATHRGLY
16   PHETYRPROASPHISVALGLULEUSERTRP
17   TRPVALASNGLYLYSGLUVALHISSERGLY
18   VALCYSTHRASPPROGLNPROLEULYSGLU
19   GLNPROALALEUASNASPSERARGTYRALA
20   LEUSERSERARGLEUARGVALSERALATHR
21   PHETRPGLNASPPROARGASNHISPHEARG
22   CYSGLNVALGLNPHETYRGLYLEUSERGLU
23   ASNASPGLUTRPTHRGLNASPARGALALYS
24   PROVALTHRGLNILEVALSERALAGLUALA
25   TRPGLYARGALAASP

Samples:

sample_1: A6TCR_alpha, [U-13C; U-15N; U-2H], 250 mM; sodium phosphate 50 mM; sodium chloride 100 mM; Pefabloc 0.1 mg/mL

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - chemical shift assignment, collection, data analysis, processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

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