BMRB: 415

The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor

Authors

Brown, L.R., De Marco, A., Richarz, R., Wagner, G., Wuthrich, K.

Assembly

basic pancreatic trypsin inhibitor

Entity

1. basic pancreatic trypsin inhibitor (polymer), 58 monomers, 6517.485 Da Detail

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CMRTCGGA

Formula weight

6517.485 Da

Source organism

Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 3.4 %, Completeness: 1.6 %, Completeness (bb): 2.4 % Detail

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Polymer type: polypeptide(L)

	Total	13C
All	1.6 % (4 of 258)	1.6 % (4 of 258)
Backbone	2.4 % (4 of 168)	2.4 % (4 of 168)
Sidechain	0.7 % (1 of 142)	0.7 % (1 of 142)
Aromatic	0.0 % (0 of 36)	0.0 % (0 of 36)
Methyl	5.3 % (1 of 19)	5.3 % (1 of 19)

1. basic pancreatic trypsin inhibitor

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CMRTCGGA

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Sample

Temperature 308 K, pH 5.5

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Release date

1995-07-30

Citation

The influence of a single salt bridge on static and dynamic features of the globular solution conformation of the basic pancreatic trypsin inhibitor. 1H and 13C nuclear-magnetic-resonance studies of the native and the transaminated inhibitor
Brown, L.R., De Marco, A., Richarz, R., Wagner, G., Wuthrich, K.
Eur. J. Biochem. (1978), 88, 87-95, PubMed 27364 , DOI 10.1111/j.1432-1033.1978.tb12425.x

Related entities 1. basic pancreatic trypsin inhibitor, : 1 : 47 : 4 : 27 : 284 entities Detail

Interaction partners 1. basic pancreatic trypsin inhibitor, : 8 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail