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Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Basic Pancreatic Trypsin Inhibitor)
Authors
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 primigenius
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 94.8 %, Completeness: 82.4 %, Completeness (bb): 96.6 % Detail

Polymer type: polypeptide(L)

Total1H
All82.4 % (290 of 352)82.4 % (290 of 352)
Backbone96.6 % (114 of 118)96.6 % (114 of 118)
Sidechain75.2 % (176 of 234)75.2 % (176 of 234)
Aromatic94.4 % (34 of 36)94.4 % (34 of 36)
Methyl100.0 % (19 of 19)100.0 % (19 of 19)

1. basic pancreatic trypsin inhibitor

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CMRTCGGA

Sample

Temperature 341 K, pH 4.6



Release date
1995-07-30
Citation
Solution NMR structure determination of proteins revisited
Wagner, G., Wuthrich, K.
J. Biomol. NMR (2008), 42, 155-158, PubMed 18827972 , DOI 10.1007/s10858-008-9277-8 ,
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