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Found 1 Document (2.231 seconds)

BMRB: 5298

1L1P

1H, 13C, and 15N Chemical Shift Assignments for the PPIase domain from E. coli trigger factor

Authors

Kozlov, G., Trempe, J., Perreault, A., Wong, M., Denisov, A., Ghandi, S., Gehring, K., Ekiel, I.

Assembly

PPIase monomer

Entity

1. PPIase monomer (polymer, Thiol state: not present), 106 monomers, 11646.80 Da Detail

GSHMQATWKE KDGAVEAEDR VTIDFTGSVD GEEFEGGKAS DFVLAMGQGR MIPGFEDGIK GHKAGEEFTI DVTFPEEYHA ENLKGKAAKF AINLKKVEER ELPELT

Formula weight

11646.8 Da

Source organism

Escherichia coli

Exptl. method

NMR

Refine. method

simulated annealing

Data set

assigned_chemical_shifts, coupling_constants

Chem. Shift Complete

Sequence coverage: 95.3 %, Completeness: 64.8 %, Completeness (bb): 80.5 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	64.8 % (779 of 1202)	73.8 % (461 of 625)	46.9 % (220 of 469)	90.7 % (98 of 108)
Backbone	80.5 % (507 of 630)	93.2 % (207 of 222)	66.2 % (202 of 305)	95.1 % (98 of 103)
Sidechain	54.3 % (361 of 665)	63.0 % (254 of 403)	41.6 % (107 of 257)	0.0 % (0 of 5)
Aromatic	17.6 % (18 of 102)	35.3 % (18 of 51)	0.0 % (0 of 50)	0.0 % (0 of 1)
Methyl	65.6 % (63 of 96)	95.8 % (46 of 48)	35.4 % (17 of 48)

1. peptidyl-prolyl isomerase

GSHMQATWKE KDGAVEAEDR VTIDFTGSVD GEEFEGGKAS DFVLAMGQGR MIPGFEDGIK GHKAGEEFTI DVTFPEEYHA ENLKGKAAKF AINLKKVEER ELPELT

Show sample condition

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

LACS Plot; CA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: 0.43 ppm, Outliers: 1 Detail

LACS Plot; CB

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: 0.43 ppm, Outliers: 1 Detail

LACS Plot; HA

Atom type	Mol. common name	Atom group	Ref. method	Ref. type	Shift ratio
¹H	DSS	methyl protons	internal	direct	1.0
¹⁵N	DSS	methyl protons	null	indirect	0.1013291
¹³C	DSS	methyl protons	null	indirect	0.2514495

Referencing offset: -0.28 ppm, Outliers: 2 Detail

Protein Blocks Logo

Calculated from 30 models in PDB: 1L1P, Strand ID: A Detail

Coupling constant

82 J values in 1 lists
Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1) Detail

Release date

2003-06-24

Citation

Solution structure of the closed form of a peptidyl-prolyl isomerase reveals the mechanism of protein folding
Kozlov, G., Trempe, J., Perreault, A., Wong, M., Denisov, A., Ghandi, S., Gehring, K., Ekiel, I.

Related entities 1. PPIase monomer, : 1 : 18 : 108 entities Detail

Interaction partners 1. PPIase monomer, : 44 interactors Detail

More details for 44 interactors identified by 5 citations

Experiments performed 6 experiments Detail

1 2D 1H-1H NOESY

Instrument

Model Bruker DRX (500 MHz)

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

2 3D 1H-1H-15N NOESY

Instrument

Model Bruker DRX (500 MHz)

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

3 3D 1H-1H-15N TOCSY

Instrument

Model Bruker DRX (500 MHz)

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

4 3D HNHA

Instrument

Model Bruker DRX (500 MHz)

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

5 3D CBCA(CO)NH

Instrument

Model Bruker DRX (500 MHz)

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

6 3D HNCACB

Instrument

Model Bruker DRX (500 MHz)

Sample #1

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
1	peptidyl-prolyl isomerase			2.0 ~ 3.0 mM
2	NaCl			100 mM

Sample #2

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
3	peptidyl-prolyl isomerase	[U-15N]		2.0 ~ 3.0 mM
4	NaCl			100 mM

Sample #3

Pressure 1 atm, Temperature 303 (±1) K, pH 6.8 (±0.1)

#	Name	Isotope labeling	Type	Concentration
5	peptidyl-prolyl isomerase	[U-13C; U-15N]		2.0 ~ 3.0 mM
6	NaCl			100 mM

nullKeywords NMR, PPIase, trigger factor

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Found 1 Document (2.231 seconds)

BMRB: 5298

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Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. PPIase monomer, : 1 : 18 : 108 entities Detail

Interaction partners 1. PPIase monomer, : 44 interactors Detail

Experiments performed 6 experiments Detail

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