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PDBsum entry 2mrb
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Metallothionein
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PDB id
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2mrb
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J Mol Biol
201:637-657
(1988)
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PubMed id:
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Three-dimensional structure of rabbit liver [Cd7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance.
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A.Arseniev,
P.Schultze,
E.Wörgötter,
W.Braun,
G.Wagner,
M.Vasák,
J.H.Kägi,
K.Wüthrich.
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ABSTRACT
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In previous work the metal-polypeptide co-ordinative bonds in the major protein
species of a reconstituted [113Cd7]metallothionein-2 preparation from rabbit
liver in aqueous solution were determined, the secondary polypeptide structure
was found to contain several half-turns and 3(10)-helical segments, and a
preliminary characterization of the overall polypeptide backbone fold in the
beta-domain containing the three-metal cluster, and the alpha-domain containing
the four-metal cluster, was obtained. Using a new, more extensive set of nuclear
magnetic resonance data these earlier structures were improved by new structure
calculations. The new experimental data consist of distance constraints from
measurements of nuclear Overhauser effects, and dihedral angle constraints
derived from both coupling constants and nuclear Overhauser effects. The
structure calculations were performed with the program DISMAN. Since no
information on the orientation of the two domains relative to each other could
be obtained, the structure calculations were performed separately for the
alpha-domain and the beta-domain. The average of the pairwise root-mean-square
distances among the 20 structures with the least residual violations of input
constraints was 2.9 A for the beta-domain and 1.4 A for the alpha-domain (1 A =
0.1 nm). The overall chirality of the polypeptide fold is right-handed for the
beta-domain and left-handed for the alpha-domain. For each of the seven metal
ions the local chirality of the co-ordination of the four cysteinyl Sy atoms is
clearly defined. The improved structures of both domains show the previously
noted differences relative to the recently published crystal structure of
metallothionein-2a from rat liver.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.E.Sutherland,
and
M.J.Stillman
(2011).
The "magic numbers" of metallothionein.
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Metallomics,
3,
444-463.
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C.A.Blindauer,
and
O.I.Leszczyszyn
(2010).
Metallothioneins: unparalleled diversity in structures and functions for metal ion homeostasis and more.
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Nat Prod Rep,
27,
720-741.
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J.Zhu,
J.Meeusen,
S.Krezoski,
and
D.H.Petering
(2010).
Reactivity of Zn-, Cd-, and apo-metallothionein with nitric oxide compounds: in vitro and cellular comparison.
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Chem Res Toxicol,
23,
422-431.
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K.P.Jensen,
and
M.Rykaer
(2010).
The building blocks of metallothioneins: heterometallic Zn(2+) and Cd(2+) clusters from first-principles calculations.
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Dalton Trans,
39,
9684-9695.
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V.Mah,
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F.Jalilehvand
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Cadmium(II) complex formation with glutathione.
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J Biol Inorg Chem,
15,
441-458.
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B.K.Bitanihirwe,
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Zinc: the brain's dark horse.
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Synapse,
63,
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J.W.Brown,
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How to arm a supervillin: designing F-actin binding activity into supervillin headpiece.
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J Mol Biol,
393,
608-618.
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PDB codes:
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H.Wang,
H.Li,
B.Cai,
Z.X.Huang,
and
H.Sun
(2008).
The effect of nitric oxide on metal release from metallothionein-3: gradual unfolding of the protein.
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J Biol Inorg Chem,
13,
411-419.
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R.Orihuela,
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E.A.Mackay,
J.H.Kägi,
M.Capdevila,
and
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(2008).
The metal-binding features of the recombinant mussel Mytilus edulis MT-10-IV metallothionein.
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J Biol Inorg Chem,
13,
801-812.
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L.Banci,
I.Bertini,
F.Cantini,
S.Ciofi-Baffoni,
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A.I.Graham,
D.R.Harvie,
and
N.J.Robinson
(2007).
NMR structural analysis of cadmium sensing by winged helix repressor CmtR.
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J Biol Chem,
282,
30181-30188.
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PDB code:
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Q.Hao,
S.H.Hong,
and
W.Maret
(2007).
Lipid raft-dependent endocytosis of metallothionein in HepG2 cells.
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J Cell Physiol,
210,
428-435.
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K.E.Rigby,
J.Chan,
J.Mackie,
and
M.J.Stillman
(2006).
Molecular dynamics study on the folding and metallation of the individual domains of metallothionein.
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Proteins,
62,
159-172.
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A.M.Zimeri,
O.P.Dhankher,
B.McCaig,
and
R.B.Meagher
(2005).
The plant MT1 metallothioneins are stabilized by binding cadmiums and are required for cadmium tolerance and accumulation.
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Plant Mol Biol,
58,
839-855.
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Y.Guo,
Y.Ling,
B.A.Thomson,
and
K.W.Siu
(2005).
Combined ion-mobility and mass-spectrometry investigations of metallothionein complexes using a tandem mass spectrometer with a segmented second quadrupole.
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J Am Soc Mass Spectrom,
16,
1787-1794.
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L.Khatai,
W.Goessler,
H.Lorencova,
and
K.Zangger
(2004).
Modulation of nitric oxide-mediated metal release from metallothionein by the redox state of glutathione in vitro.
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Eur J Biochem,
271,
2408-2416.
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L.M.Malaiyandi,
K.E.Dineley,
and
I.J.Reynolds
(2004).
Divergent consequences arise from metallothionein overexpression in astrocytes: zinc buffering and oxidant-induced zinc release.
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Glia,
45,
346-353.
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P.A.Cobine,
R.T.McKay,
K.Zangger,
C.T.Dameron,
and
I.M.Armitage
(2004).
Solution structure of Cu6 metallothionein from the fungus Neurospora crassa.
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Eur J Biochem,
271,
4213-4221.
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PDB code:
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T.Newlove,
J.H.Konieczka,
and
M.H.Cordes
(2004).
Secondary structure switching in Cro protein evolution.
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Structure,
12,
569-581.
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PDB code:
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C.Capasso,
O.Abugo,
F.Tanfani,
A.Scire,
V.Carginale,
R.Scudiero,
E.Parisi,
and
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Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse.
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Proteins,
46,
259-267.
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C.D.Syme,
E.W.Blanch,
L.Hecht,
M.Vasák,
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Solution structure of native proteins with irregular folds from Raman optical activity.
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Biopolymers,
58,
138-151.
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I.Bertini,
D.A.Bryant,
S.Ciurli,
A.Dikiy,
C.O.Fernández,
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Backbone dynamics of plastocyanin in both oxidation states. Solution structure of the reduced form and comparison with the oxidized state.
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J Biol Chem,
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PDB codes:
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L.Kangur,
and
P.Palumaa
(2001).
The effects of physiologically important nonmetallic ligands in the reactivity of metallothionein towards 5,5'-dithiobis(2-nitrobenzoic acid). A new method for the determination of ligand interactions with metallothionein.
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Eur J Biochem,
268,
4979-4984.
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S.Hayward
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Peptide-plane flipping in proteins.
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Protein Sci,
10,
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C.D.Berweger,
W.Thiel,
and
W.F.van Gunsteren
(2000).
Molecular-dynamics simulation of the beta domain of metallothionein with a semi-empirical treatment of the metal core.
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Proteins,
41,
299-315.
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D.W.Hasler,
L.T.Jensen,
O.Zerbe,
D.R.Winge,
and
M.Vasák
(2000).
Effect of the two conserved prolines of human growth inhibitory factor (metallothionein-3) on its biological activity and structure fluctuation: comparison with a mutant protein.
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Biochemistry,
39,
14567-14575.
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I.Bertini,
H.J.Hartmann,
T.Klein,
G.Liu,
C.Luchinat,
and
U.Weser
(2000).
High resolution solution structure of the protein part of Cu7 metallothionein.
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Eur J Biochem,
267,
1008-1018.
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PDB code:
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L.J.Jiang,
M.Vasák,
B.L.Vallee,
and
W.Maret
(2000).
Zinc transfer potentials of the alpha - and beta-clusters of metallothionein are affected by domain interactions in the whole molecule.
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Proc Natl Acad Sci U S A,
97,
2503-2508.
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P.M.Gehrig,
C.You,
R.Dallinger,
C.Gruber,
M.Brouwer,
J.H.Kägi,
and
P.E.Hunziker
(2000).
Electrospray ionization mass spectrometry of zinc, cadmium, and copper metallothioneins: evidence for metal-binding cooperativity.
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Protein Sci,
9,
395-402.
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H.Sun,
H.Li,
I.Harvey,
and
P.J.Sadler
(1999).
Interactions of bismuth complexes with metallothionein(II).
|
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J Biol Chem,
274,
29094-29101.
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K.Zangger,
G.Oz,
J.D.Otvos,
and
I.M.Armitage
(1999).
Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy.
|
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Protein Sci,
8,
2630-2638.
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PDB codes:
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A.K.Kabziński
(1998).
Application of covalent affinity chromatography with thiol-disulphide interchange for determination of environmental exposure to heavy metals based on the quantitative isolation of Cd-thionein from human breast milk.
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Biomed Chromatogr,
12,
217-225.
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C.Jacob,
W.Maret,
and
B.L.Vallee
(1998).
Control of zinc transfer between thionein, metallothionein, and zinc proteins.
|
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Proc Natl Acad Sci U S A,
95,
3489-3494.
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L.J.Jiang,
W.Maret,
and
B.L.Vallee
(1998).
The ATP-metallothionein complex.
|
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Proc Natl Acad Sci U S A,
95,
9146-9149.
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W.Maret,
and
B.L.Vallee
(1998).
Thiolate ligands in metallothionein confer redox activity on zinc clusters.
|
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Proc Natl Acad Sci U S A,
95,
3478-3482.
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Y.Yang,
S.Jao,
S.Nanduri,
D.W.Starke,
J.J.Mieyal,
and
J.Qin
(1998).
Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.
|
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Biochemistry,
37,
17145-17156.
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PDB code:
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D.Bentrop,
I.Bertini,
F.Capozzi,
A.Dikiy,
L.Eltis,
and
C.Luchinat
(1996).
Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: comparison with the solution structure of the wild-type protein.
|
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Biochemistry,
35,
5928-5936.
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PDB code:
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M.Zweckstetter,
M.Czisch,
U.Mayer,
M.L.Chu,
W.Zinth,
R.Timpl,
and
T.A.Holak
(1996).
Structure and multiple conformations of the kunitz-type domain from human type VI collagen alpha3(VI) chain in solution.
|
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Structure,
4,
195-209.
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S.Saito,
and
P.E.Hunziker
(1996).
Differential sensitivity of metallothionein-1 and -2 in liver of zinc-injected rat toward proteolysis.
|
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Biochim Biophys Acta,
1289,
65-70.
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A.K.Kabziński,
and
T.Takagi
(1995).
The application of affinity chromatography for quantitative determination of metallothionein in physiological fluids by an indirect method based on analysis of metal contents.
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Biomed Chromatogr,
9,
123-129.
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A.Presta,
A.R.Green,
A.Zelazowski,
and
M.J.Stillman
(1995).
Copper binding to rabbit liver metallothionein. Formation of a continuum of copper(I)-thiolate stoichiometric species.
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Eur J Biochem,
227,
226-240.
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D.Lassen,
C.Lücke,
M.Kveder,
A.Mesgarzadeh,
J.M.Schmidt,
B.Specht,
A.Lezius,
F.Spener,
and
H.Rüterjans
(1995).
Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy.
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Eur J Biochem,
230,
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PDB code:
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I.Bertini,
I.C.Felli,
D.H.Kastrau,
C.Luchinat,
M.Piccioli,
and
M.S.Viezzoli
(1994).
Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high-potential iron-sulfur protein I from Ectothiorhodospira halophila.
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Eur J Biochem,
225,
703-714.
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X.Q.Ding,
C.Butzlaff,
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D.L.Pountney,
G.Henkel,
H.Winkler,
M.Vasák,
and
A.X.Trautwein
(1994).
Mössbauer and magnetic susceptibility studies on iron(II) metallothionein from rabbit liver. Evidence for the existence of an unusual type of [M3(CysS)9]3- cluster.
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Eur J Biochem,
220,
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H.M.Weir,
P.J.Kraulis,
C.S.Hill,
A.R.Raine,
E.D.Laue,
and
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(1993).
Structure of the HMG box motif in the B-domain of HMG1.
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EMBO J,
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PDB codes:
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I.Bertini,
C.Luchinat,
L.Messori,
and
M.Vasak
(1993).
A two-dimensional NMR study of Co(II)7 rabbit liver metallothionein.
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Eur J Biochem,
211,
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M.W.MacArthur,
and
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Conformational analysis of protein structures derived from NMR data.
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Proteins,
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D.L.Pountney,
and
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(1992).
Spectroscopic studies on metal distribution in Co(II)/Zn(II) mixed-metal clusters in rabbit liver metallothionein 2.
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Eur J Biochem,
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Y.Q.Qian,
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Precise vicinal coupling constants 3JHN alpha in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments.
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Determination of the structure of the nucleocapsid protein NCp7 from the human immunodeficiency virus type 1 by 1H NMR.
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P.Palumaa,
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Binding of inorganic phosphate to the cadmium-induced dimeric form of metallothionein from rabbit liver.
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Eur J Biochem,
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W.Braun,
M.Vasák,
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G.Wagner,
J.H.Kägi,
and
K.Wüthrich
(1992).
Comparison of the NMR solution structure and the x-ray crystal structure of rat metallothionein-2.
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| |
Proc Natl Acad Sci U S A,
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PDB code:
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M.Good,
R.Hollenstein,
and
M.Vasák
(1991).
Metal selectivity of clusters in rabbit liver metallothionein.
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Eur J Biochem,
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P.Güntert,
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J Biomol NMR,
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S.Elvin,
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Electroporation-induced transformation of Escherichia coli: evaluation of a square waveform pulse.
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G.Otting,
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Heteronuclear filters in two-dimensional [1H,1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions.
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23,
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M.Nilges,
G.M.Clore,
and
A.M.Gronenborn
(1990).
1H-NMR stereospecific assignments by conformational data-base searches.
|
| |
Biopolymers,
29,
813-822.
|
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M.P.Williamson
(1990).
Secondary-structure dependent chemical shifts in proteins.
|
| |
Biopolymers,
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1423-1431.
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G.M.Clore,
and
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(1989).
Determination of three-dimensional structures of proteins and nucleic acids in solution by nuclear magnetic resonance spectroscopy.
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| |
Crit Rev Biochem Mol Biol,
24,
479-564.
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J.H.Kägi,
and
P.Hunziker
(1989).
Mammalian metallothionein.
|
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Biol Trace Elem Res,
21,
111-118.
|
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only a partial list as not all journals are covered by
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
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shown on the right.
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