PDBsum entry 1g6j

Gene regulation, cell cycle

PDB id

1g6j

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Contents

			Protein chain

					76 a.a. *

* Residue conservation analysis

PDB id:

1g6j

Links

Name:

Gene regulation, cell cycle

Title:

Structure of recombinant human ubiquitin in aot reverse micelles

Structure:

Ubiquitin. Chain: a. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

32 models

Authors:

C.R.Babu,P.F.Flynn,A.J.Wand

Key ref:

C.R.Babu et al. (2001). Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids. J Am Chem Soc, 123, 2691-2692. PubMed id: 11456950 DOI: 10.1021/ja005766d

Date:

06-Nov-00

Release date:

28-Mar-01

PROCHECK

	Headers

	References

Protein chain

P0CG48 (UBC_HUMAN) - Polyubiquitin-C from Homo sapiens

Seq: Struc:

Seq: Struc:					685 a.a. 76 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.?

[IntEnz] [ExPASy] [KEGG] [BRENDA]

DOI no: 10.1021/ja005766d	J Am Chem Soc 123:2691-2692 (2001)
PubMed id: 11456950

Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids.
C.R.Babu, P.F.Flynn, A.J.Wand.

ABSTRACT

No abstract given.

Literature references that cite this PDB file's key reference

PubMed id

Reference

21196937

N.V.Nucci, M.S.Pometun, and A.J.Wand (2011).
Site-resolved measurement of water-protein interactions by solution NMR.

Nat Struct Mol Biol, 18, 245-249.

21034466

A.F.Angyán, B.Szappanos, A.Perczel, and Z.Gáspári (2010).
CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.

BMC Struct Biol, 10, 39.

20160991

B.R.Donald, and J.Martin (2009).
Automated NMR Assignment and Protein Structure Determination using Sparse Dipolar Coupling Constraints.

Prog Nucl Magn Reson Spectrosc, 55, 101-127.

20161395

H.J.Kim, S.C.Howell, W.D.Van Horn, Y.H.Jeon, and C.R.Sanders (2009).
Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.

Prog Nucl Magn Reson Spectrosc, 55, 335-360.

18297402

W.D.Van Horn, M.E.Ogilvie, and P.F.Flynn (2008).
Use of reverse micelles in membrane protein structural biology.

J Biomol NMR, 40, 203-211.

17876709

D.A.Snyder, F.Zhang, and R.Brüschweiler (2007).
Covariance NMR in higher dimensions: application to 4D NOESY spectroscopy of proteins.

J Biomol NMR, 39, 165-175.

17165694

K.G.Valentine, M.S.Pometun, J.M.Kielec, R.E.Baigelman, J.K.Staub, K.L.Owens, and A.J.Wand (2006).
Magnetic susceptibility-induced alignment of proteins in reverse micelles.

J Am Chem Soc, 128, 15930-15931.

16910639

M.S.Pometun, R.W.Peterson, C.R.Babu, and A.J.Wand (2006).
Cold denaturation of encapsulated ubiquitin.

J Am Chem Soc, 128, 10652-10653.

16258827

K.Simon, J.Xu, C.Kim, and N.R.Skrynnikov (2005).
Estimating the accuracy of protein structures using residual dipolar couplings.

J Biomol NMR, 33, 83-93.

15285893

C.J.Langmead, A.Yan, R.Lilien, L.Wang, and B.R.Donald (2004).
A polynomial-time nuclear vector replacement algorithm for automated NMR resonance assignments.

J Comput Biol, 11, 277-298.

14990997

C.R.Babu, V.J.Hilser, and A.J.Wand (2004).
Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation.

Nat Struct Mol Biol, 11, 352-357.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.