BMRB: 2426

Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S

Authors

Kuwajima, K., Baldwin, R.L.

Assembly

ribonuclease A

Entity

1. ribonuclease A (polymer), 19 monomers, 2095.248 Da Detail

KETAAAKFER QHMDSSTSA

Formula weight

2095.248 Da

Source organism

Bos primigenius

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 5.3 %, Completeness: 0.9 %, Completeness (bb): 2.6 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	0.9 % (1 of 107)	0.9 % (1 of 107)
Backbone	2.6 % (1 of 38)	2.6 % (1 of 38)
Sidechain	0.0 % (0 of 69)	0.0 % (0 of 69)
Aromatic	0.0 % (0 of 7)	0.0 % (0 of 7)
Methyl	0.0 % (0 of 6)	0.0 % (0 of 6)

1. ribonuclease A

KETAAAKFER QHMDSSTSA

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Sample

Temperature 277 K, pH 2.7

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Release date

1995-07-30

Citation

Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S
Kuwajima, K., Baldwin, R.L.
Mol. Biol. (1983), 169, 281-297, DOI 10.1016/s0022-2836(83)80184-3

Related entities 1. ribonuclease A, : 1 : 101 : 26 entities Detail

Interaction partners 1. ribonuclease A, : 8 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail