BMRB: 237

Systematic Application of Two-Dimensional 1H Nuclear-Magnetic-Resonance Techniques for Studies of Proteins 1. Combined Use of Spin-Echo-Correlated Spectroscopy and J-Resolved Spectroscopy for the Identification of Complete Spin Systems of

Authors

Nagayama, K., 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: 53.4 %, Completeness: 25.9 %, Completeness (bb): 28.8 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	25.9 % (91 of 352)	25.9 % (91 of 352)
Backbone	28.8 % (34 of 118)	28.8 % (34 of 118)
Sidechain	24.4 % (57 of 234)	24.4 % (57 of 234)
Aromatic	0.0 % (0 of 36)	0.0 % (0 of 36)
Methyl	78.9 % (15 of 19)	78.9 % (15 of 19)

1. basic pancreatic trypsin inhibitor

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CMRTCGGA

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Sample

Temperature 297 K, pH 4.6

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Release date

1995-07-30

Citation

Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 1. Combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labile protons in amino-acid residues
Nagayama, K., Wuthrich, K.
Eur. J. Biochem. (1981), 114, 365-374, PubMed 6163630 , DOI: , 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