BMRB Entry 16379

Title:
Solution structure of Interleukin 1a
Deposition date:
2009-06-30
Original release date:
2010-03-10
Authors:
Mohan, Sepuru; Chang, Hsuan-Kuo; Chin, Yu
Citation:

Citation: Chang, Hsuan-Kuo; Mohan, Sepuru; Chin, Yu. "1H, 13C and 15N backbone and side chain resonance assignments of human interleukin 1alpha."  Biomol. NMR Assignments 4, 59-60 (2010).
PubMed: 20108067

Assembly members:

Assembly members:
human interleukin 1alpha, polymer, 151 residues, 17227.705 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(20b)+

Data sets:
Data typeCount
13C chemical shifts493
15N chemical shifts129
1H chemical shifts759

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 151 residues - 17227.705 Da.

1   ASNVALLYSTYRASNPHEMETARGILEILE
2   LYSTYRGLUPHEILELEUASNASPALALEU
3   ASNGLNSERILEILEARGALAASNASPGLN
4   TYRLEUTHRALAALAALALEUHISASNLEU
5   ASPGLUALAVALLYSPHEASPMETGLYALA
6   TYRLYSSERSERLYSASPASPALALYSILE
7   THRVALILELEUARGILESERLYSTHRGLN
8   LEUTYRVALTHRALAGLNASPGLUASPGLN
9   PROVALLEULEULYSGLUMETPROGLUILE
10   PROLYSTHRILETHRGLYSERGLUTHRASN
11   LEULEUPHEPHETRPGLUTHRHISGLYTHR
12   LYSASNTYRPHETHRSERVALALAHISPRO
13   ASNLEUPHEILEALATHRLYSGLNASPTYR
14   TRPVALCYSLEUALAGLYGLYPROPROSER
15   ILETHRASPPHEGLNILELEUGLUASNGLN
16   ALA

Samples:

sample_1: TRIS 10 mM; sodium chloride 100 mM; human interleukin 1alpha 1.4 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - Automated NOE assignment, NMR structure calculation

SPARKY, Goddard - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - dihedral angles

VNMRJ vVNMRJ_2.2C, Varian - processing

NMR spectrometers:

  • Varian VNMRS 700 MHz

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