BMRB Entry 27286

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27286

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for VSV8 peptide bound to a truncated MHC H-2Kb (VSV8/Kb-t)
Deposition date:
2017-10-18
Original release date:
2017-12-14
Authors:
Mallis, Robert; Arthanari, Haribabu; Lang, Matt; Reinherz, Ellis; Wagner, Gerhard
Citation:

Citation: Mallis, Robert; Arthanari, Haribabu; Lang, Matt; Reinherz, Ellis; Wagner, Gerhard. "NMR-Directed Design of PreTCRbeta and pMHC Molecules Implies a Distinct Geometry for preTCR Relative to alphabetaTCR Recognition of pMHC"  J. Biol. Chem. 293, 754-766 (2018).
PubMed: 29101227

Assembly members:

Assembly members:
H-2Kb-t, polymer, 186 residues, 21452.86 Da.
VSV8, polymer, 8 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: 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):
H-2Kb-t: MGPHSLRYFVTAVSRPGLGE PRYMEVGYVDDTEFVRFDSD AENPRYEPRARWMEQEGPEY WERETQKAKGNEQSFRVDLR TLLGYYNQSKGGSHTIQVIS GCEVGSDGRLLRGYQQYAYD GCDYIALNEDLKTWTAADMA ALITKHKWEQAGEAERLRAY LEGTCVEWLRRYLKNGNATL LRTDSP
VSV8: RGYVYQGL

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts140
1H chemical shifts140

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1H-2Kb-t1
2VSV82

Entities:

Entity 1, H-2Kb-t 186 residues - 21452.86 Da.

1   METGLYPROHISSERLEUARGTYRPHEVAL
2   THRALAVALSERARGPROGLYLEUGLYGLU
3   PROARGTYRMETGLUVALGLYTYRVALASP
4   ASPTHRGLUPHEVALARGPHEASPSERASP
5   ALAGLUASNPROARGTYRGLUPROARGALA
6   ARGTRPMETGLUGLNGLUGLYPROGLUTYR
7   TRPGLUARGGLUTHRGLNLYSALALYSGLY
8   ASNGLUGLNSERPHEARGVALASPLEUARG
9   THRLEULEUGLYTYRTYRASNGLNSERLYS
10   GLYGLYSERHISTHRILEGLNVALILESER
11   GLYCYSGLUVALGLYSERASPGLYARGLEU
12   LEUARGGLYTYRGLNGLNTYRALATYRASP
13   GLYCYSASPTYRILEALALEUASNGLUASP
14   LEULYSTHRTRPTHRALAALAASPMETALA
15   ALALEUILETHRLYSHISLYSTRPGLUGLN
16   ALAGLYGLUALAGLUARGLEUARGALATYR
17   LEUGLUGLYTHRCYSVALGLUTRPLEUARG
18   ARGTYRLEULYSASNGLYASNALATHRLEU
19   LEUARGTHRASPSERPRO

Entity 2, VSV8 8 residues - Formula weight is not available

1   ARGGLYTYRVALTYRGLNGLYLEU

Samples:

sample_1: H-2Kb-t, [U-13C; U-15N; U-2H], 400 uM; VSV8 400 uM; sodium phosphate 50 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 470 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection

Cara, Keller - chemical shift assignment, data analysis, peak picking

RASP, MacRaild - chemical shift assignment

SPARTA+, Shen and Bax - chemical shift calculation

NMR spectrometers:

  • Bruker UnityPlus 750 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 500 MHz

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