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Found 1 Document (1.328 seconds)

BMRB: 2169

2FI3

Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor

Authors

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

Assembly

(5-55)Ser BPTI folding intermediate

Entity

1. (5-55)Ser BPTI folding intermediate (polymer, Thiol state: all disulfide bound), 58 monomers, 6478.215 Da Detail

RPDFCLEPPY TGPSKARIIR YFYNAKAGLS QTFVYGGSRA KRNNFKSAED SRRTCGGA

Formula weight

6478.215 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	0:CYS5:SG	1:CYS55:SG

Source organism

Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 97.5 %, Completeness (bb): 98.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	97.5 % (345 of 354)	97.5 % (345 of 354)
Backbone	98.3 % (116 of 118)	98.3 % (116 of 118)
Sidechain	97.0 % (229 of 236)	97.0 % (229 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. (5-55)Ser BPTI folding intermediate

RPDFCLEPPY TGPSKARIIR YFYNAKAGLS QTFVYGGSRA KRNNFKSAED SRRTCGGA

Show sample condition

Sample #1

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate	2.0 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate			2.0 ~ 3.0 mM
5	D2O			100 %

Release date

1995-07-30

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: , Abstract

Show more 6 citaions

Citation 2

The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor
FEBS Lett. (1991), 279, 61-64, PubMed 1704858 , 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
J. Mol. Biol. (1991), 222, 353-371, PubMed 1960731 , Abstract

Citation 4

Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor
J. Mol. Biol. (1992), 224, 905-911, PubMed 1373775 , Abstract

Citation 5

The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor
Proc. Natl. Acad. Sci. U. S. A. (1992), 89, 6775-6779, PubMed 1379719 , 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
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
J. Mol. Biol. (1994), 235, 1044-1061, PubMed 7507172 , DOI 10.1006/jmbi.1994.1056 , Abstract

Hide non-primary 6 citaions

Related entities 1. (5-55)Ser BPTI folding intermediate, : 1 : 83 : 263 entities Detail

Interaction partners 1. (5-55)Ser BPTI folding intermediate, : 8 interactors Detail

More details for 8 interactors identified by 8 citations

Experiments performed 5 experiments Detail

1 DQF-COSY

Instrument

Model Bruker AMX (500 MHz)

Sample #1

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate	2.0 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate			2.0 ~ 3.0 mM
5	D2O			100 %

2 NOESY

Instrument

Model Bruker AMX (500 MHz)

Sample #1

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate	2.0 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate			2.0 ~ 3.0 mM
5	D2O			100 %

3 ROESY

Instrument

Model Bruker AMX (500 MHz)

Sample #1

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate	2.0 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate			2.0 ~ 3.0 mM
5	D2O			100 %

4 TOCSY

Instrument

Model Bruker AMX (500 MHz)

Sample #1

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate	2.0 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate			2.0 ~ 3.0 mM
5	D2O			100 %

5 1D Saturation transfer experiment

Instrument

Model Bruker AMX (500 MHz)

Sample #1

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate	2.0 ~ 3.0 mM
2	H2O	90 %
3	D2O	10 %

Sample #2

Temperature 276 (±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	(5-55)Ser BPTI folding intermediate			2.0 ~ 3.0 mM
5	D2O			100 %

Chemical shift validation 3 contents Detail

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr2169_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

Disulfide bonds

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:5:CYS:SG	1:55:CYS:SG	unknown	unknown	n/a

Other bonds (neither disulfide, covalent nor hydrogen bonds, e.g. Zinc–sulphur bond)

None

Non-standard residues

None

Content subtype: bmr2169_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	CSR_1	Warning	401		100.0 (chain: 1, length: 58)
1	Chemical shift references	chemical_shift_reference	OK	1		No information

Assigned chemical shifts

Saveframe: CSR_1

Status: Warning

Sequence coverage of experimental data

Entity_assembly_ID: 1, Chain length: 58, Sequence coverage: 100.0%

--------10--------20--------30--------40--------50--------
RPDFCLEPPYTGPSKARIIRYFYNAKAGLSQTFVYGGSRAKRNNFKSAEDSRRTCGGA
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
RPDFCLEPPYTGPSKARIIRYFYNAKAGLSQTFVYGGSRAKRNNFKSAEDSRRTCGGA

Total number of assignments
- ¹H chemical shifts: 401

Completeness of assignments

Entity_assemble_ID: 1

Excluded Atom_ID in statistics

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
15	LYS	HZ1	7.56
15	LYS	HZ2	7.56
15	LYS	HZ3	7.56
20	ARG	HH11	6.71
20	ARG	HH12	6.71
26	LYS	HZ1	7.65
26	LYS	HZ2	7.65
26	LYS	HZ3	7.65
35	TYR	HH	9.91
41	LYS	HZ1	7.29
41	LYS	HZ2	7.29
41	LYS	HZ3	7.29
46	LYS	HZ1	7.7
46	LYS	HZ2	7.7
46	LYS	HZ3	7.7
52	ARG	HH11	6.7
52	ARG	HH12	6.7
54	THR	HG1	3.16

All atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	354	345	97.5

Backbone atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	118	116	98.3

Side chain atoms

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	236	229	97.0

Methyl group atoms

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

Aromatic group atoms

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

Histogram of normalized assigned chemical shifts
Random coil index and derived parameters (S² and NMR RMSD)
- Chain_ID: 1

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

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Found 1 Document (1.328 seconds)

BMRB: 2169

Sample #1

Sample #2

Related entities 1. (5-55)Ser BPTI folding intermediate, : 1 : 83 : 263 entities Detail

Interaction partners 1. (5-55)Ser BPTI folding intermediate, : 8 interactors Detail

Experiments performed 5 experiments Detail

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail