BMRB: 4868

Sequential 1H assignments for BPTI-R52 (= BPTI with Met to Arg mutation at position 52)

Authors

van Mierlo, C.P.M., Darby, N.J., Neuhaus, D., Creighton, T.E.

Assembly

BPTI-R52

Entity

1. BPTI-R52 (polymer, Thiol state: all disulfide bound), 58 monomers, 6542.475 Da Detail

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CRRTCGGA

Formula weight

6542.475 Da

Entity Connection

disulfide 3 Detail

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ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS5:SG	1:CYS55:SG
2	disulfide	sing	1:CYS14:SG	1:CYS38:SG
3	disulfide	sing	1:CYS30:SG	1:CYS51:SG

Source organism

Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 95.5 %, Completeness (bb): 99.2 % Detail

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Polymer type: polypeptide(L)

	Total	1H
All	95.5 % (338 of 354)	95.5 % (338 of 354)
Backbone	99.2 % (117 of 118)	99.2 % (117 of 118)
Sidechain	93.6 % (221 of 236)	93.6 % (221 of 236)
Aromatic	100.0 % (36 of 36)	100.0 % (36 of 36)
Methyl	100.0 % (19 of 19)	100.0 % (19 of 19)

1. BPTI-R52

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CRRTCGGA

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Sample

Temperature 283 (±0.5) K, pH 4.6 (±0.1), Details no salt was added to the sample, pH 4.6, the pH was adjusted by adding small amounts of NaOH

#	Name	Isotope labeling	Type	Concentration
1	BPTI-R52			2.0 ~ 3.0 mM
2	H2O			90 %
3	D2O			10 %

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Release date

2000-10-18

Citation 1

Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor
van Mierlo, C.P.M., Darby, N.J., Neuhaus, D., Creighton, T.E.
J. Mol. Biol. (1991), 222, 373-390, PubMed 1960732 , DOI 10.1016/0022-2836(91)90217-t , Abstract

Show more 6 citaions

Citation 2

The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor
Darby, N.J., van Mierlo, C.P., Creighton, T.E.
FEBS Lett. (1991), 279, 61-64, PubMed 1704858 , DOI 10.1016/0014-5793(91)80251-w , Abstract

Citation 3

(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study
van Mierlo, C.P., Darby, N.J., Neuhaus, D., Creighton, T.E.
J. Mol. Biol. (1991), 222, 353-371, PubMed 1960731 , DOI 10.1016/0022-2836(91)90216-s , Abstract

Citation 4

Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor
Darby, N.J., van Mierlo, C.P., Scott, G.H., Neuhaus, D., Creighton, T.E.
J. Mol. Biol. (1992), 224, 905-911, PubMed 1373775 , DOI 10.1016/0022-2836(92)90458-v , Abstract

Citation 5

The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor
van Mierlo, C.P., Darby, N.J., Creighton, T.E.
Proc. Natl. Acad. Sci. U. S. A. (1992), 89, 6775-6779, PubMed 1379719 , DOI 10.1073/pnas.89.15.6775 , Abstract

Citation 6

Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements
van Mierlo, C.P., Darby, N.J., Keeler, J., Neuhaus, D., Creighton, T.E.
J. Mol. Biol. (1993), 229, 1125-1146, PubMed 7680380 , DOI 10.1006/jmbi.1993.1108 , Abstract

Citation 7

1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor
van Mierlo, C.P., Kemmink, J., Neuhaus, D., Darby, N.J., Creighton, T.E.
J. Mol. Biol. (1994), 235, 1044-1061, PubMed 7507172 , DOI 10.1006/jmbi.1994.1056 , Abstract

Hide non-primary 6 citaions

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. BPTI-R52, : 1 : 92 : 280 entities Detail

Interaction partners 1. BPTI-R52, : 8 interactors Detail

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail