BMRB Entry 26569

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26569

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Title:
Backbone chemical shift assignments for TCR_3c8m_t55a
Deposition date:
2015-05-01
Original release date:
2016-01-06
Authors:
He, Yanan; Rangarajan, Sneha; Kerzic, Melissa; Luo, Ming; Chen, Yihong; Vignali, Dario A.; Mariuzza, Roy A; Orban, John
Citation:

Citation: He, Yanan; Rangarajan, Sneha; Kerzic, Melissa; Luo, Ming; Chen, Yihong; Vignali, Dario A.; Mariuzza, Roy A; Orban, John. "Identification of the Docking Site for CD3 on the T Cell Receptor Beta Chain by Solution NMR"  J. Biol. Chem. 290, 19796-19805 (2015).
PubMed: 26109064

Assembly members:

Assembly members:
TCR_beta_alpha, polymer, 244 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):
TCR_beta_alpha: VVSQHPSWVIAKSGTSVKIE CRSLDFQATTMFWYRQFPKQ SLMLMATSNEGSKAAYEQGV EKDKFLINHASLTLSTLTVT SAHPEDSSFYICSARGGSYN SPLHFGNGTRLTVTEDLKNV FPPEVAVFEPSEAEISHTQK ATLVCLATGFYPDHVELSWW VNGKEVHSGVCTDPQPLKEQ PALNDSRYALSSRLRVSATF WQNPRNHFRCQVQFYGLSEN DEWTQDRAKPVTQIVSAEAW GRAD

Data sets:
Data typeCount
13C chemical shifts624
15N chemical shifts200
1H chemical shifts200

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TCR 3c8m t55a, TCR alpha1

Entities:

Entity 1, TCR 3c8m t55a, TCR alpha 244 residues - Formula weight is not available

1   VALVALSERGLNHISPROSERTRPVALILE
2   ALALYSSERGLYTHRSERVALLYSILEGLU
3   CYSARGSERLEUASPPHEGLNALATHRTHR
4   METPHETRPTYRARGGLNPHEPROLYSGLN
5   SERLEUMETLEUMETALATHRSERASNGLU
6   GLYSERLYSALAALATYRGLUGLNGLYVAL
7   GLULYSASPLYSPHELEUILEASNHISALA
8   SERLEUTHRLEUSERTHRLEUTHRVALTHR
9   SERALAHISPROGLUASPSERSERPHETYR
10   ILECYSSERALAARGGLYGLYSERTYRASN
11   SERPROLEUHISPHEGLYASNGLYTHRARG
12   LEUTHRVALTHRGLUASPLEULYSASNVAL
13   PHEPROPROGLUVALALAVALPHEGLUPRO
14   SERGLUALAGLUILESERHISTHRGLNLYS
15   ALATHRLEUVALCYSLEUALATHRGLYPHE
16   TYRPROASPHISVALGLULEUSERTRPTRP
17   VALASNGLYLYSGLUVALHISSERGLYVAL
18   CYSTHRASPPROGLNPROLEULYSGLUGLN
19   PROALALEUASNASPSERARGTYRALALEU
20   SERSERARGLEUARGVALSERALATHRPHE
21   TRPGLNASNPROARGASNHISPHEARGCYS
22   GLNVALGLNPHETYRGLYLEUSERGLUASN
23   ASPGLUTRPTHRGLNASPARGALALYSPRO
24   VALTHRGLNILEVALSERALAGLUALATRP
25   GLYARGALAASP

Samples:

sample_1: TCR 3c8m t55a, TCR alpha, [U-13C; U-15N; U-2H], 0.22 mM; NaPi 50 mM; NaCl 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 HNCOCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOCAsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

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

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

Molmol, Koradi, Billeter and Wuthrich - data analysis

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