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Found 1 Document (1.469 seconds)

BMRB: 4873

2FI3

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

Authors

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

Assembly

(30-51)Ser BPTI folding intermediate

Entity

1. (30-51)Ser BPTI folding intermediate (polymer, Thiol state: all disulfide bound), 59 monomers, 6609.410 Da Detail

MRPDFSLEPP YTGPSKARII RYFYNAKAGL CQTFVYGGSR AKRNNFKSAE DCRRTSGGA

Formula weight

6609.41 Da

Entity Connection

disulfide 1 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	disulfide	sing	1:CYS31:SG	1:CYS52:SG

Source organism

Bos taurus

Exptl. method

NMR

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 100.0 %, Completeness: 93.8 %, Completeness (bb): 98.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹⁵N
All	93.8 % (394 of 420)	94.2 % (340 of 361)	91.5 % (54 of 59)
Backbone	98.3 % (172 of 175)	98.3 % (118 of 120)	98.2 % (54 of 55)
Sidechain	90.6 % (222 of 245)	92.1 % (222 of 241)	0.0 % (0 of 4)
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)Ser BPTI folding intermediate

MRPDFSLEPP YTGPSKARII RYFYNAKAGL CQTFVYGGSR AKRNNFKSAE DCRRTSGGA

Show sample condition

Sample

Temperature 271 (±0.5) K, pH 4.6 (±0.1), Details 15N-enriched (30-51), Met residue at position -1. no salt was added to the sample, pH 4.6, the pH was adjusted by adding small amounts of NaOH

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

Release date

2000-11-28

Citation 1

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.M., 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

Show more 6 citaions

Citation 2

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

Citation 3

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: , Abstract

Citation 4

(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: , Abstract

Citation 5

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: , Abstract

Citation 6

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: , 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

  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: 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: 4877 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)Ser BPTI folding intermediate, : 1 : 90 : 196 entities Detail

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

More details for 8 interactors identified by 8 citations

Experiments performed 13 experiments Detail

1 DQF-COSY

Instrument

Bruker AMX - 500 MHz

Sample

State isotropic, Temperature 271 (±0.5) K, pH 4.6 (±0.1), Details 15N-enriched (30-51), Met residue at position -1. no salt was added to the sample, pH 4.6, the pH was adjusted by adding small amounts of NaOH

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

2 DQ

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

3 NOESY

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

4 ROESY

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

5 TOCSY

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

6 HMQC

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

7 HSQC

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

8 2D HMQC-NOESY

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

9 2D HSQC-NOESY

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

10 2D HSQC-TOCSY

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

11 {1H-15N} NOE

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

12 15N T1

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

13 15N T2

Instrument

Bruker AMX - 500 MHz

Sample

#	Name	Isotope labeling	Concentration
1	(30-51)Ser BPTI folding intermediate	[U-15N]	2.0 ~ 3.0 mM
2	H2O		90 %
3	D2O		10 %

Chemical shift validation 3 contents Detail

Ptnr_site_1	Ptnr_site_2	Redox_state_prediction_1	Redox_state_prediction_2	Distance (Å)
1:31:CYS:SG	1:52:CYS:SG	unknown	unknown	n/a

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	CSR_1	Warning	443		100.0 (chain: 1, length: 59)
1	Chemical shift references	chemical_shift_reference	Warning	1		No information

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
16	LYS	HZ1	7.59
16	LYS	HZ2	7.59
16	LYS	HZ3	7.59
27	LYS	HZ1	7.64
27	LYS	HZ2	7.64
27	LYS	HZ3	7.64
47	LYS	HZ1	7.71
47	LYS	HZ2	7.71
47	LYS	HZ3	7.71
53	ARG	HH11	6.72
53	ARG	HH12	6.95

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	361	338	93.6
¹⁵N chemical shifts	66	54	81.8

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	120	118	98.3
¹⁵N chemical shifts	55	54	98.2

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	241	220	91.3
¹⁵N chemical shifts	11	0	0.0

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	20	20	100.0

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

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

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4873_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 (1.469 seconds)

BMRB: 4873

Sample

Entries sharing articles BMRB: 5 entries Detail

Related entities 1. (30-51)Ser BPTI folding intermediate, : 1 : 90 : 196 entities Detail

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

Experiments performed 13 experiments Detail

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Chemical shift validation 3 contents Detail