BMRB: 1541

Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein

Authors

Lecomte, J.T.J., De Marco, A., Llinas, M.

Assembly

crambin

Source organism

Crambe hispanica subsp. abyssinica

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 13.0 %, Completeness: 6.8 %, Completeness (bb): 6.7 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	6.8 % (16 of 234)	6.8 % (16 of 234)
Backbone	6.7 % (6 of 90)	6.7 % (6 of 90)
Sidechain	6.9 % (10 of 144)	6.9 % (10 of 144)
Aromatic	0.0 % (0 of 13)	0.0 % (0 of 13)
Methyl	22.2 % (6 of 27)	22.2 % (6 of 27)

1. crambin

TTCCPSIVAR SNFNVCRLPG TXEAICATYT GCIIIPGATC PGDYAN

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Sample

Temperature 298 K, pH 7.8

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Release date

1995-07-30

Citation

Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein
Lecomte, J.T.J., De Marco, A., Llinas, M.
Biochim. Biophys. Acta (1982), 703, 223-230, PubMed , DOI 10.1016/0167-4838(82)90052-8

Related entities 1. crambin, : 1 : 9 : 63 entities Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail