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Three-disulfide variant of hen lysozyme: C64A/C80A
Authors
Yokota, A., Hirai, K., Miyauchi, H., Noda, Y., Inoue, K., Akasaka, K., Tachibana, H., Segawa, S.
Assembly
hen egg white lysozyme
Entity
1. hen egg white lysozyme (polymer, Thiol state: all disulfide bound), 130 monomers, 14380.07 Da Detail

MKVFGRCELA AAMKRHGLDN YRGYSLGNWV CAAKFESNFN TQATNRNTDG STDYGILQIN SRWWANDGRT PGSRNLCNIP ASALLSSDIT ASVNCAKKIV SDGNGMNAWV AWRNRCKGTD VQAWIRGCRL


Formula weight
14380.07 Da
Entity Connection
disulfide 3 Detail

IDTypeValue orderAtom ID 1Atom ID 2
1disulfidesing1:CYS7:SG1:CYS128:SG
2disulfidesing1:CYS31:SG1:CYS116:SG
3disulfidesing1:CYS77:SG1:CYS95:SG

Source organism
Gallus gallus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 90.8 %, Completeness: 76.9 %, Completeness (bb): 83.3 % Detail

Polymer type: polypeptide(L)

Total1H
All76.9 % (582 of 757)76.9 % (582 of 757)
Backbone83.3 % (215 of 258)83.3 % (215 of 258)
Sidechain73.5 % (367 of 499)73.5 % (367 of 499)
Aromatic90.8 % (59 of 65)90.8 % (59 of 65)
Methyl82.0 % (50 of 61)82.0 % (50 of 61)

1. three-disulfide variant of hen lysozyme

MKVFGRCELA AAMKRHGLDN YRGYSLGNWV CAAKFESNFN TQATNRNTDG STDYGILQIN SRWWANDGRT PGSRNLCNIP ASALLSSDIT ASVNCAKKIV SDGNGMNAWV AWRNRCKGTD VQAWIRGCRL

Sample

Temperature 298 (±0.1) K, pH 3.8 (±0.1)


#NameIsotope labelingTypeConcentration
1three-disulfide variant of hen lysozyme[U-15N]0.3 ~ 1.0 mM

Release date
2004-09-13
Citation 1
NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins
Yokota, A., Hirai, K., Miyauchi, H., Iimura, S., Noda, Y., Inoue, K., Akasaka, K., Tachibana, H., Segawa, S.
Biochemistry (2004), 43, 6663-6669, PubMed 15157100 , DOI 10.1021/bi049967w ,
Citation 2
Characterisation of the dominant oxidative folding intermediate of hen lysozyme
van den Berg, B., Chung, E.W., Robinson, C.V., Dobson, C.M.
J. Mol. Biol. (1999), 290, 781-796, PubMed 10395829 , DOI 10.1006/jmbi.1999.2915 ,
Citation 3
NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure
Noda, Y., Yokota, A., Horii, D., Tominaga, T., Tanisaka, Y., Tachibana, H., Segawa, S.
Biochemistry (2002), 41, 2130-2139, PubMed 11841203 , DOI 10.1021/bi0113418 ,
Related entities 1. hen egg white lysozyme, : 1 : 103 : 99 entities Detail
Interaction partners 1. hen egg white lysozyme, : 8 interactors Detail
Keywords Lysozyme Variants, NMR, Protein Folding, Three-Disulfide Intermediate