BMRB: 48

Protein Structures in Solution by Nuclear Magnetic Resonance and Distance Geometry (The Polypeptide Fold of the Basic Pancreatic Trypsin Inhibitor Determined using Two Different Algorithms, DISGEO and DISMAN)

Authors

Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Go, N., 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: 100.0 %, Completeness: 94.9 %, Completeness (bb): 99.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	94.9 % (334 of 352)	94.9 % (334 of 352)
Backbone	99.2 % (117 of 118)	99.2 % (117 of 118)
Sidechain	92.7 % (217 of 234)	92.7 % (217 of 234)
Aromatic	88.9 % (32 of 36)	88.9 % (32 of 36)
Methyl	100.0 % (19 of 19)	100.0 % (19 of 19)

1. basic pancreatic trypsin inhibitor

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CMRTCGGA

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Sample

Temperature 309 K, pH 4.6

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Release date

1995-07-30

Citation

Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
Wagner, G., Braun, W., Havel, T.F., Schaumann, T., Go, N., Wuthrich, K.
J. Mol. Biol. (1987), 196, 611-639, PubMed 2445992 , Abstract

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