BMRB Entry 25714

Title:
Chemical shifts of the HLA-B2705 heavy chain in complex with the peptide pVIPR
Deposition date:
2015-07-16
Original release date:
2015-12-02
Authors:
Ballaschk, Martin; Schmieder, Peter; Ziegler, Andreas; Diehl, Anne; Uchanska-Ziegler, Barbara
Citation:

Citation: Ballaschk, Martin; Ziegler, Andreas; Uchanska-Ziegler, Barbara; Diehl, Anne; Schmieder, Peter. "Characterization of HLA-b27:05 and :09 complexed with TIS and pVIPR by NMR"  .

Assembly members:

Assembly members:
05_heavy_chain, polymer, 292 residues, 33798.1104 Da.
b2m, polymer, 100 residues, 11864.3434 Da.
pVIPR, polymer, 9 residues, 1393.6 Da.

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 46 Ek/LIC

Data sets:
Data typeCount
13C chemical shifts719
15N chemical shifts272
1H chemical shifts272

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
105p.hc1
205p.b2m2
305p.pVIPR3

Entities:

Entity 1, 05p.hc 292 residues - 33798.1104 Da.

Residues 1-15 (-14-0) represent a non-native affinity tag. This is the extracellular domain of a membrane protein.

1   METALAHISHISHISHISHISHISVALASP
2   ASPASPASPLYSILEGLYSERHISSERMET
3   ARGTYRPHEHISTHRSERVALSERARGPRO
4   GLYARGGLYGLUPROARGPHEILETHRVAL
5   GLYTYRVALASPASPTHRLEUPHEVALARG
6   PHEASPSERASPALAALASERPROARGGLU
7   GLUPROARGALAPROTRPILEGLUGLNGLU
8   GLYPROGLUTYRTRPASPARGGLUTHRGLN
9   ILECYSLYSALALYSALAGLNTHRASPARG
10   GLUASPLEUARGTHRLEULEUARGTYRTYR
11   ASNGLNSERGLUALAGLYSERHISTHRLEU
12   GLNASNMETTYRGLYCYSASPVALGLYPRO
13   ASPGLYARGLEULEUARGGLYTYRHISGLN
14   ASPALATYRASPGLYLYSASPTYRILEALA
15   LEUASNGLUASPLEUSERSERTRPTHRALA
16   ALAASPTHRALAALAGLNILETHRGLNARG
17   LYSTRPGLUALAALAARGVALALAGLUGLN
18   LEUARGALATYRLEUGLUGLYGLUCYSVAL
19   GLUTRPLEUARGARGTYRLEUGLUASNGLY
20   LYSGLUTHRLEUGLNARGALAASPPROPRO
21   LYSTHRHISVALTHRHISHISPROILESER
22   ASPHISGLUALATHRLEUARGCYSTRPALA
23   LEUGLYPHETYRPROALAGLUILETHRLEU
24   THRTRPGLNARGASPGLYGLUASPGLNTHR
25   GLNASPTHRGLULEUVALGLUTHRARGPRO
26   ALAGLYASPARGTHRPHEGLNLYSTRPALA
27   ALAVALVALVALPROSERGLYGLUGLUGLN
28   ARGTYRTHRCYSHISVALGLNHISGLUGLY
29   LEUPROLYSPROLEUTHRLEUARGTRPGLU
30   PROSER

Entity 2, 05p.b2m 100 residues - 11864.3434 Da.

The first residue (0, M) is the start codon from the bacterial expression system and hence not present in the native protein.

1   METILEGLNARGTHRPROLYSILEGLNVAL
2   TYRSERARGHISPROALAGLUASNGLYLYS
3   SERASNPHELEUASNCYSTYRVALSERGLY
4   PHEHISPROSERASPILEGLUVALASPLEU
5   LEULYSASNGLYGLUARGILEGLULYSVAL
6   GLUHISSERASPLEUSERPHESERLYSASP
7   TRPSERPHETYRLEULEUTYRTYRTHRGLU
8   PHETHRPROTHRGLULYSASPGLUTYRALA
9   CYSARGVALASNHISVALTHRLEUSERGLN
10   PROLYSILEVALLYSTRPASPARGASPMET

Entity 3, 05p.pVIPR 9 residues - 1393.6 Da.

1   ARGARGLYSTRPARGARGTRPHISLEU

Samples:

1: 05p.pVIPR 0.33 mM; 05p.b2m 0.33 mM; 05p.hc, [U-13C; U-15N; U-2H], 0.33 mM; Sodium Phosphate 10.00 mM; Sodium Chloride 150.00 mM; H2O 90%; D2O 10%

sample_condition1: ionic strength: 0.160 M; pH: 7.500; pressure: 1.000 atm; temperature: 310.000 K

Experiments:

NameSampleSample stateSample conditions
3D HNCA1isotropicsample_condition1
3D HN(CO)CA1isotropicsample_condition1
3D HNCACB1isotropicsample_condition1
3D HN(COCA)CB1isotropicsample_condition1
3D HNCO1isotropicsample_condition1
3D HN(CA)CO1isotropicsample_condition1
2D 1H-15N HSQC1isotropicsample_condition1

Software:

CcpNmr_Analysis v2.4, CCPN - assignments

Topspin v3.2, Bruker - Spectrum processing

nmrDraw vany, NIH - Spectrum analysis, Spectrum display

nmrPipe vany, NIH - Spectrum processing

NMR spectrometers:

  • 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