BMRB Entry 26780

Title:
Chemical Shift Assignments for Interleukin-36alpha
Deposition date:
2016-04-18
Original release date:
2017-04-25
Authors:
Ohlenschlaeger, Oliver; Goradia, Nishit
Citation:

Citation: Goradia, Nishit; Wissbrock, Amelie; Wiedemann, Christoph; Bordusa, Frank; Ramachandran, Ramadurai; Imhof, Diana; Ohlenschlaeger, Oliver. "(1)H, (13)C, and (15)N resonance assignments for the pro-inflammatory cytokine interleukin-36alpha"  Biomol. NMR Assign. 10, 329-333 (2016).
PubMed: 27351892

Assembly members:

Assembly members:
Interleukin-36alpha, polymer, 161 residues, 17965.6 Da.

Natural source:

Natural source:   Common Name: humans   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-28a

Data sets:
Data typeCount
13C chemical shifts645
15N chemical shifts144
1H chemical shifts1030

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1IL36A1

Entities:

Entity 1, IL36A 161 residues - 17965.6 Da.

Residues 1-3 represent a non-native cloning artifact

1   GLYSERHISMETGLULYSALALEULYSILE
2   ASPTHRPROGLNGLNGLYSERILEGLNASP
3   ILEASNHISARGVALTRPVALLEUGLNASP
4   GLNTHRLEUILEALAVALPROARGLYSASP
5   ARGMETSERPROVALTHRILEALALEUILE
6   SERCYSARGHISVALGLUTHRLEUGLULYS
7   ASPARGGLYASNPROILETYRLEUGLYLEU
8   ASNGLYLEUASNLEUCYSLEUMETCYSALA
9   LYSVALGLYASPGLNPROTHRLEUGLNLEU
10   LYSGLULYSASPILEMETASPLEUTYRASN
11   GLNPROGLUPROVALLYSSERPHELEUPHE
12   TYRHISSERGLNSERGLYARGASNSERTHR
13   PHEGLUSERVALALAPHEPROGLYTRPPHE
14   ILEALAVALSERSERGLUGLYGLYCYSPRO
15   LEUILELEUTHRGLNGLULEUGLYLYSALA
16   ASNTHRTHRASPPHEGLYLEUTHRMETLEU
17   PHE

Samples:

sample_1: Interleukin-36alpha, [U-100% 13C; U-100% 15N], 1.3 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_2: Interleukin-36alpha, [U-100% 15N], 1.3 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0 M; pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, processing

CCPN, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 750 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP Q9UHA7
AlphaFold Q7RTZ8

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