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A 1H-NMR study of human interleukin-1beta Sequence-specific assignment of aromatic residues using site-directed mutant proteins
Authors
Gronenborn, A.M., Clore, G.MARIUS., Schmeissner, U., Wingfield, P.
Assembly
interleukin 1-beta
Entity
1. interleukin 1-beta (polymer), 153 monomers, 17376.66 Da Detail

APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVAL GLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS


Formula weight
17376.66 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 5.2 %, Completeness: 2.6 %, Completeness (bb): 3.3 % Detail

Polymer type: polypeptide(L)

Total1H
All 2.6 % (25 of 974) 2.6 % (25 of 974)
Backbone 3.3 % (10 of 306) 3.3 % (10 of 306)
Sidechain 2.2 % (15 of 668) 2.2 % (15 of 668)
Aromatic 2.9 % (2 of 69) 2.9 % (2 of 69)
Methyl 4.1 % (3 of 73) 4.1 % (3 of 73)

1. interleukin 1-beta

APVRSLNCTL RDSQQKSLVM SGPYELKALH LQGQDMEQQV VFSMSFVQGE ESNDKIPVAL GLKEKNLYLS CVLKDDKPTL QLESVDPKNY PKKKMEKRFV FNKIEINNKL EFESAQFPNW YISTSQAENM PVFLGGTKGG QDITDFTMQF VSS

Sample

Temperature 298 K, pH 7.42



Release date
1995-07-30
Citation
A 1H-NMR study of human interleukin-1 beta. Sequence-specific assignment of aromatic residues using site-directed mutant proteins
Gronenborn, A.M., Clore, G.MARIUS., Schmeissner, U., Wingfield, P.
Eur. J. Biochem. (1986), 161, 37-43, PubMed 3023086 , DOI 10.1111/j.1432-1033.1986.tb10121.x ,
Related entities 1. interleukin 1-beta, : 1 : 47 : 7 : 5 : 83 entities Detail
Interaction partners 1. interleukin 1-beta, : 9 interactors Detail
Experiments performed 1 experiments Detail
Chemical shift validation 3 contents Detail