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Found 1 Document (1.405 seconds)

BMRB: 4877

4BNR

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

Authors

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

Assembly

(30-51, 5-38)Ser BPTI folding intermediate

Entity

1. (30-51, 5-38)Ser BPTI folding intermediate (polymer, Thiol state: all disulfide bound), 58 monomers, 6510.345 Da Detail

RPDFCLEPPY TGPSKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CRRTSGGA

Formula weight

6510.345 Da

Entity Connection

disulfide 2 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS5:SG	1:CYS38:SG
2	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: 98.3 %, Completeness: 92.4 %, Completeness (bb): 94.9 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	92.4 % (327 of 354)	92.4 % (327 of 354)
Backbone	94.9 % (112 of 118)	94.9 % (112 of 118)
Sidechain	91.1 % (215 of 236)	91.1 % (215 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. (30-51, 5-38)Ser BPTI folding intermediate

RPDFCLEPPY TGPSKARIIR YFYNAKAGLC QTFVYGGCRA KRNNFKSAED CRRTSGGA

Show sample condition

Sample #1

Temperature 271 (±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	Concentration
1	(30-51, 5-38)Ser BPTI folding intermediate	1.5 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 271 (±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
4	(30-51, 5-38)Ser BPTI folding intermediate			1.5 ~ 3.0 mM
5	D2O			100 %

Release date

2000-11-28

Citation 1

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.M., 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

Show more 5 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

Hide non-primary 5 citaions

Entries sharing articles BMRB: 5 entries Detail

  BMRB: 4855 released on 2000-11-28
    Title (14-38, 30-51) Double-disulphide intermediate in folding of Bovine Pancreatic Trypsin Inhibitor: A two-dimensional 1H nuclear magnetic resonance study
  BMRB: 4873 released on 2000-11-28
    Title 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
  BMRB: 4875 released on 2000-11-28
    Title 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
  BMRB: 4868 released on 2000-10-18
    Title Sequential 1H assignments for BPTI-R52 (= BPTI with Met to Arg mutation at position 52)
  BMRB: 2169 released on 1995-07-30
    Title Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor

Related entities 1. (30-51, 5-38)Ser BPTI folding intermediate, : 1 : 91 : 273 entities Detail

Interaction partners 1. (30-51, 5-38)Ser BPTI folding intermediate, : 8 interactors Detail

More details for 8 interactors identified by 8 citations

Experiments performed 1 experiments Detail

Chemical shift validation 3 contents Detail

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:5:CYS:SG	1:38:CYS:SG	unknown	unknown	n/a
1:30:CYS:SG	1:51:CYS:SG	unknown	unknown	n/a

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	CSR_1	Warning	381		98.3 (chain: 1, length: 58)
1	Chemical shift references	chemical_shift_reference	OK	1		No information

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
15	LYS	HZ1	7.6
15	LYS	HZ2	7.6
15	LYS	HZ3	7.6
26	LYS	HZ1	7.65
26	LYS	HZ2	7.65
26	LYS	HZ3	7.65
46	LYS	HZ1	7.72
46	LYS	HZ2	7.72
46	LYS	HZ3	7.72
52	ARG	HH11	6.71
52	ARG	HH12	6.94

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	354	332	93.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	118	115	97.5

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	236	217	91.9

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	19	19	100.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	36	36	100.0

Keywords bovine pancreatic trypsin inhibitor (BPTI), disulphide bonds, folding intermediate, NMR, protein folding

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4877_3.str
Diamagnetism of the molecular assembly	True (excluding Oxygen atoms)
Whether the assembly has a disulfide bond	True (see coordinates for details)
Whether the assembly has a other bond	None
Whether the assembly contains a cyclic polymer	None
Overall data processing status	Warning

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Found 1 Document (1.405 seconds)

BMRB: 4877

Sample #1

Sample #2

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. (30-51, 5-38)Ser BPTI folding intermediate, : 1 : 91 : 273 entities Detail

Interaction partners 1. (30-51, 5-38)Ser BPTI folding intermediate, : 8 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail