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Found 1 Document (1.674 seconds)

BMRB: 6335

1XJH

Near complete chemical shift assignments for the zinc-bound redox switch domain of the E. coli Hsp33

Authors

Won, H., Low, L.Y., Guzman, R., Martinez-Yamout, M., Jakob, U., Dyson, H.JANE.

Assembly

redox-switch domain of Hsp33

Entity

1. E. coli heat shock protein 33 redox-switch domain (polymer, Thiol state: free and other bound), 62 monomers, 7032.746 Da Detail

MDVEFKCTCS RERCADALKT LPDEEVDSIL AEDGEIDMHC DYCGNHYLFN AMDIAEIRNN AS

2. ZN (non-polymer), 65.409 Da

Total weight

7098.1553 Da

Max. entity weight

7032.746 Da

Entity Connection

na 4 Detail

ID	Type	Value order	Atom ID 1	Atom ID 2
1	na	sing	1:CYS7:SG	2:ZN1:ZN
2	na	sing	1:CYS9:SG	2:ZN1:ZN
3	na	sing	1:CYS40:SG	2:ZN1:ZN
4	na	sing	1:CYS43:SG	2:ZN1:ZN

Source organism

Escherichia coli

Exptl. method

NMR

Refine. method

simulated annealing, torsion angle dynamics, molecular dynamics

Data set

assigned_chemical_shifts

Chem. Shift Complete

Sequence coverage: 98.4 %, Completeness: 95.0 %, Completeness (bb): 97.3 % Detail

Polymer type: polypeptide(L)

	Total	¹H	¹³C	¹⁵N
All	95.0 % (643 of 677)	96.6 % (337 of 349)	92.4 % (243 of 263)	96.9 % (63 of 65)
Backbone	97.3 % (360 of 370)	97.6 % (122 of 125)	97.3 % (179 of 184)	96.7 % (59 of 61)
Sidechain	93.2 % (342 of 367)	96.0 % (215 of 224)	88.5 % (123 of 139)	100.0 % (4 of 4)
Aromatic	72.7 % (32 of 44)	100.0 % (22 of 22)	45.5 % (10 of 22)
Methyl	100.0 % (56 of 56)	100.0 % (28 of 28)	100.0 % (28 of 28)

1. E. coli heat shock protein 33 redox-switch domain

MDVEFKCTCS RERCADALKT LPDEEVDSIL AEDGEIDMHC DYCGNHYLFN AMDIAEIRNN AS

Show sample condition

Sample

Temperature 298 (±1) K, pH 7.0 (±0.2)

#	Name	Isotope labeling	Type	Concentration
1	E. coli heat shock protein 33 redox-switch domain	[U-99% 13C; U-99% 15N]		1.0 ~ 2.0 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: -0.39 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: -0.39 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: 0.01 ppm, Outliers: 1 Detail

LACS Plot; CO

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: -0.19 ppm, Outliers: 3 Detail

Protein Blocks Logo

Calculated from 20 models in PDB: 1XJH, Strand ID: A Detail

Release date

2004-10-11

Citation

The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold
Won, H., Low, L.Y., De Guzman, R., Martinez-Yamout, M., Jakob, U., Dyson, H.JANE.
J. Mol. Biol. (2004), 341, 893-899, PubMed 15328602 , DOI: , Abstract

Related entities 1. E. coli heat shock protein 33 redox-switch domain, : 1 : 7 : 101 entities Detail

Interaction partners 1. E. coli heat shock protein 33 redox-switch domain, : 4 interactors Detail

More details for 4 interactors identified by 2 citations

Experiments performed 1 experiments Detail

#	Name	Isotope labeling	Type	Concentration
2	E. coli heat shock protein 33 redox-switch domain	[U-99% 15N]		1.0 ~ 2.0 mM

null

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Found 1 Document (1.674 seconds)

BMRB: 6335

Sample

Chemical shift reference

Chemical shift reference

Chemical shift reference

Chemical shift reference

Related entities 1. E. coli heat shock protein 33 redox-switch domain, : 1 : 7 : 101 entities Detail

Interaction partners 1. E. coli heat shock protein 33 redox-switch domain, : 4 interactors Detail

Experiments performed 1 experiments Detail

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