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Found 1 Document (1.351 seconds)

BMRB: 4875

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, 5-14)Ser BPTI folding intermediate

Entity

1. (30-51, 5-14)Ser BPTI folding intermediate (polymer, Thiol state: all disulfide bound), 58 monomers, 6510.345 Da Detail

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGSRA 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:CYS14: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: 100.0 %, Completeness: 91.0 %, Completeness (bb): 97.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H
All	91.0 % (322 of 354)	91.0 % (322 of 354)
Backbone	97.5 % (115 of 118)	97.5 % (115 of 118)
Sidechain	87.7 % (207 of 236)	87.7 % (207 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, 5-14)Ser BPTI folding intermediate

RPDFCLEPPY TGPCKARIIR YFYNAKAGLC QTFVYGGSRA 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, 5-14)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)

#	Name	Isotope labeling	Type	Concentration
4	(30-51, 5-14)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 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

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 6 citaions

Related entities 1. (30-51, 5-14)Ser BPTI folding intermediate, : 1 : 91 : 268 entities Detail

Interaction partners 1. (30-51, 5-14)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

Properties

Input source #1: Assigned chemical shifts - Assigned chemical shifts	bmr4875_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	1:14:CYS:SG	unknown	unknown	n/a
1:30:CYS:SG	1:51: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: bmr4875_3.str

#	Content subtype	Saveframe	Status	# of rows	Experiment type	Sequence coverage (%)
1	Assigned chemical shifts	CSR_1	Warning	370		100.0 (chain: 1, length: 58)
1	Chemical shift references	chemical_shift_reference	Warning	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%
- Total number of assignments
  - ¹H chemical shifts: 370
- Completeness of assignments
  - Entity_assemble_ID: 1
- Histogram of normalized assigned chemical shifts
- Random coil index and derived parameters (S² and NMR RMSD)
  - Chain_ID: 1

Comp_index_ID	Comp_ID	Atom_ID	CS value (ppm)
15	LYS	HZ1	7.62
15	LYS	HZ2	7.62
15	LYS	HZ3	7.62
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	6.74
52	ARG	HH12	6.96

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	354	321	90.7

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	118	114	96.6

Atom group	# of target shifts	# of assigned shifts	Completeness (%)
¹H chemical shifts	236	207	87.7

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

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Found 1 Document (1.351 seconds)

BMRB: 4875

Sample #1

Sample #2

Related entities 1. (30-51, 5-14)Ser BPTI folding intermediate, : 1 : 91 : 268 entities Detail

Interaction partners 1. (30-51, 5-14)Ser BPTI folding intermediate, : 8 interactors Detail

Experiments performed 1 experiments Detail

Instrument

Sample #1

Sample #2

Chemical shift validation 3 contents Detail