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PDBsum entry 1spf
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Lipoprotein(surface film)
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PDB id
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1spf
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DOI no:
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Biochemistry
33:6015-6023
(1994)
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PubMed id:
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The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix.
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J.Johansson,
T.Szyperski,
T.Curstedt,
K.Wüthrich.
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ABSTRACT
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The nuclear magnetic resonance (NMR) structure of the pulmonary
surfactant-associated lipoplypeptide C (SP-C) was determined in a mixed solvent
of C2H3Cl/C2H3OH/ 1 M HCl 32:64:5 (v/v). Sequence-specific 1H NMR assignments
and the collection of conformational constraints were achieved with
two-dimensional 1H NMR, and the structure was calculated with the distance
geometry program DIANA. The root mean square deviations for the well-defined
polypeptide segment of residues 9-34 calculated for the 20 best energy-minimized
DIANA conformers relative to their mean are 0.5 and 1.3 A for the polypeptide
backbone atoms N, C alpha, and C', and for all heavy atoms, respectively. The
35-residue polypeptide chain of SP-C forms an alpha-helix between positions 9
and 34, which includes two segments of seven and four consecutive valyls that
are separated by a single leucyl residue. The N-terminal hexapeptide segment,
which includes two palmitoylcysteinyls, is flexibly disordered. The length of
the alpha-helix is about 37 A, and the helical segment of residues 13-28, which
contains exclusively aliphatic residues with branched side chains, is 23-A long
and about 10 A in diameter. The alpha-helix is outstandingly regular, with
virtually identical chi 1 angles for all valyl residues. The observation of a
helical structure of SP-C was rather unexpected, considering that Val is
generally underrepresented in alpha-helices, and it provides intriguing novel
insights into the structural basis of SP-C functions as well as into general
structural aspects of protein-lipid interactions in biological membranes.
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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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A.Gonzalez-Horta,
D.Andreu,
M.R.Morrow,
and
J.Perez-Gil
(2008).
Effects of palmitoylation on dynamics and phospholipid-bilayer-perturbing properties of the N-terminal segment of pulmonary surfactant protein SP-C as shown by 2H-NMR.
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Biophys J,
95,
2308-2317.
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L.Martínez-Gil,
J.Pérez-Gil,
and
I.Mingarro
(2008).
The surfactant peptide KL4 sequence is inserted with a transmembrane orientation into the endoplasmic reticulum membrane.
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Biophys J,
95,
L36-L38.
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M.Saleem,
M.C.Meyer,
D.Breitenstein,
and
H.J.Galla
(2008).
The surfactant peptide KL4 in lipid monolayers: phase behavior, topography, and chemical distribution.
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J Biol Chem,
283,
5195-5207.
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C.M.Gabrys,
and
D.P.Weliky
(2007).
Chemical shift assignment and structural plasticity of a HIV fusion peptide derivative in dodecylphosphocholine micelles.
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Biochim Biophys Acta,
1768,
3225-3234.
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Z.Leonenko,
S.Gill,
S.Baoukina,
L.Monticelli,
J.Doehner,
L.Gunasekara,
F.Felderer,
M.Rodenstein,
L.M.Eng,
and
M.Amrein
(2007).
An elevated level of cholesterol impairs self-assembly of pulmonary surfactant into a functional film.
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Biophys J,
93,
674-683.
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E.Ramírez,
A.Santana,
A.Cruz,
I.Plasencia,
and
G.E.López
(2006).
Molecular dynamics of surfactant protein C: from single molecule to heptameric aggregates.
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Biophys J,
90,
2698-2705.
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J.K.Rainey,
L.Fliegel,
and
B.D.Sykes
(2006).
Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.
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Biochem Cell Biol,
84,
918-929.
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L.Wang,
P.Cai,
H.J.Galla,
H.He,
C.R.Flach,
and
R.Mendelsohn
(2005).
Monolayer-multilayer transitions in a lung surfactant model: IR reflection-absorption spectroscopy and atomic force microscopy.
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Eur Biophys J,
34,
243-254.
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M.F.Beers,
and
S.Mulugeta
(2005).
Surfactant protein C biosynthesis and its emerging role in conformational lung disease.
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Annu Rev Physiol,
67,
663-696.
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R.Wüstneck,
J.Perez-Gil,
N.Wüstneck,
A.Cruz,
V.B.Fainerman,
and
U.Pison
(2005).
Interfacial properties of pulmonary surfactant layers.
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Adv Colloid Interface Sci,
117,
33-58.
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B.Luy,
A.Diener,
R.P.Hummel,
E.Sturm,
W.R.Ulrich,
and
C.Griesinger
(2004).
Structure and potential C-terminal dimerization of a recombinant mutant of surfactant-associated protein C in chloroform/methanol.
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Eur J Biochem,
271,
2076-2085.
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L.M.Gordon,
P.W.Mobley,
W.Lee,
S.Eskandari,
Y.N.Kaznessis,
M.A.Sherman,
and
A.J.Waring
(2004).
Conformational mapping of the N-terminal peptide of HIV-1 gp41 in lipid detergent and aqueous environments using 13C-enhanced Fourier transform infrared spectroscopy.
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Protein Sci,
13,
1012-1030.
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PDB code:
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V.Kairys,
M.K.Gilson,
and
B.Luy
(2004).
Structural model for an AxxxG-mediated dimer of surfactant-associated protein C.
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Eur J Biochem,
271,
2086-2092.
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C.W.Wu,
S.L.Seurynck,
K.Y.Lee,
and
A.E.Barron
(2003).
Helical peptoid mimics of lung surfactant protein C.
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Chem Biol,
10,
1057-1063.
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J.M.Brockman,
Z.Wang,
R.H.Notter,
and
R.A.Dluhy
(2003).
Effect of hydrophobic surfactant proteins SP-B and SP-C on binary phospholipid monolayers: II. Infrared external reflectance-absorption spectroscopy.
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Biophys J,
84,
326-340.
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J.P.Bridges,
S.E.Wert,
L.M.Nogee,
and
T.E.Weaver
(2003).
Expression of a human surfactant protein C mutation associated with interstitial lung disease disrupts lung development in transgenic mice.
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J Biol Chem,
278,
52739-52746.
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N.Wüstneck,
R.Wüstneck,
J.Perez-Gil,
and
U.Pison
(2003).
Effects of oligomerization and secondary structure on the surface behavior of pulmonary surfactant proteins SP-B and SP-C.
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Biophys J,
84,
1940-1949.
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R.A.Dluhy,
S.Shanmukh,
J.B.Leapard,
P.Krüger,
and
J.E.Baatz
(2003).
Deacylated pulmonary surfactant protein SP-C transforms from alpha-helical to amyloid fibril structure via a pH-dependent mechanism: an infrared structural investigation.
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Biophys J,
85,
2417-2429.
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D.Knebel,
M.Sieber,
R.Reichelt,
H.J.Galla,
and
M.Amrein
(2002).
Fluorescence light microscopy of pulmonary surfactant at the air-water interface of an air bubble of adjustable size.
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Biophys J,
83,
547-555.
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S.Shanmukh,
P.Howell,
J.E.Baatz,
and
R.A.Dluhy
(2002).
Effect of hydrophobic surfactant proteins SP-B and SP-C on phospholipid monolayers. Protein structure studied using 2D IR and beta correlation analysis.
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Biophys J,
83,
2126-2141.
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W.J.Wang,
S.J.Russo,
S.Mulugeta,
and
M.F.Beers
(2002).
Biosynthesis of surfactant protein C (SP-C). Sorting of SP-C proprotein involves homomeric association via a signal anchor domain.
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J Biol Chem,
277,
19929-19937.
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X.Bi,
C.R.Flach,
J.Pérez-Gil,
I.Plasencia,
D.Andreu,
E.Oliveira,
and
R.Mendelsohn
(2002).
Secondary structure and lipid interactions of the N-terminal segment of pulmonary surfactant SP-C in Langmuir films: IR reflection-absorption spectroscopy and surface pressure studies.
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Biochemistry,
41,
8385-8395.
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M.Palmblad,
M.Gustafsson,
T.Curstedt,
J.Johansson,
and
S.Schürch
(2001).
Surface activity and film formation from the surface associated material of artificial surfactant preparations.
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Biochim Biophys Acta,
1510,
106-117.
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R.Zangi,
H.Kovacs,
W.F.van Gunsteren,
J.Johansson,
and
A.E.Mark
(2001).
Free energy barrier estimation of unfolding the alpha-helical surfactant-associated polypeptide C.
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Proteins,
43,
395-402.
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T.E.Weaver,
and
J.J.Conkright
(2001).
Function of surfactant proteins B and C.
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Annu Rev Physiol,
63,
555-578.
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E.J.Veldhuizen,
A.J.Waring,
F.J.Walther,
J.J.Batenburg,
L.M.van Golde,
and
H.P.Haagsman
(2000).
Dimeric N-terminal segment of human surfactant protein B (dSP-B(1-25)) has enhanced surface properties compared to monomeric SP-B(1-25).
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Biophys J,
79,
377-384.
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E.J.Veldhuizen,
and
H.P.Haagsman
(2000).
Role of pulmonary surfactant components in surface film formation and dynamics.
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Biochim Biophys Acta,
1467,
255-270.
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N.Bourdos,
F.Kollmer,
A.Benninghoven,
M.Ross,
M.Sieber,
and
H.J.Galla
(2000).
Analysis of lung surfactant model systems with time-of-flight secondary ion mass spectrometry.
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Biophys J,
79,
357-369.
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X.Zhou,
F.Alber,
G.Folkers,
G.H.Gonnet,
and
G.Chelvanayagam
(2000).
An analysis of the helix-to-strand transition between peptides with identical sequence.
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Proteins,
41,
248-256.
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J.P.Duneau,
S.Crouzy,
N.Garnier,
Y.Chapron,
and
M.Genest
(1999).
Molecular dynamics simulations of the ErbB-2 transmembrane domain within an explicit membrane environment: comparison with vacuum simulations.
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Biophys Chem,
76,
35-53.
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R.G.Efremov,
D.E.Nolde,
G.Vergoten,
and
A.S.Arseniev
(1999).
A solvent model for simulations of peptides in bilayers. II. Membrane-spanning alpha-helices.
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Biophys J,
76,
2460-2471.
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J.J.Batenburg,
and
H.P.Haagsman
(1998).
The lipids of pulmonary surfactant: dynamics and interactions with proteins.
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Prog Lipid Res,
37,
235-276.
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J.Johansson
(1998).
Structure and properties of surfactant protein C.
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Biochim Biophys Acta,
1408,
161-172.
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L.M.Gregoret,
and
R.T.Sauer
(1998).
Tolerance of a protein helix to multiple alanine and valine substitutions.
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Fold Des,
3,
119-126.
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P.Mayer-Fligge,
J.Volz,
U.Krüger,
E.Sturm,
W.Gernandt,
K.P.Schäfer,
and
M.Przybylski
(1998).
Synthesis and structural characterization of human-identical lung surfactant SP-C protein.
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J Pept Sci,
4,
355-363.
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T.Szyperski,
G.Vandenbussche,
T.Curstedt,
J.M.Ruysschaert,
K.Wüthrich,
and
J.Johansson
(1998).
Pulmonary surfactant-associated polypeptide C in a mixed organic solvent transforms from a monomeric alpha-helical state into insoluble beta-sheet aggregates.
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Protein Sci,
7,
2533-2540.
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A.Gericke,
C.R.Flach,
and
R.Mendelsohn
(1997).
Structure and orientation of lung surfactant SP-C and L-alpha-dipalmitoylphosphatidylcholine in aqueous monolayers.
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Biophys J,
73,
492-499.
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A.von Nahmen,
M.Schenk,
M.Sieber,
and
M.Amrein
(1997).
The structure of a model pulmonary surfactant as revealed by scanning force microscopy.
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Biophys J,
72,
463-469.
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J.Johansson,
and
T.Curstedt
(1997).
Molecular structures and interactions of pulmonary surfactant components.
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Eur J Biochem,
244,
675-693.
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K.Nag,
S.G.Taneva,
J.Perez-Gil,
A.Cruz,
and
K.M.Keough
(1997).
Combinations of fluorescently labeled pulmonary surfactant proteins SP-B and SP-C in phospholipid films.
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Biophys J,
72,
2638-2650.
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J.Johansson,
T.Curstedt,
and
B.Robertson
(1996).
Synthetic protein analogues in artificial surfactants.
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Acta Paediatr,
85,
642-646.
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K.Nag,
J.Perez-Gil,
A.Cruz,
and
K.M.Keough
(1996).
Fluorescently labeled pulmonary surfactant protein C in spread phospholipid monolayers.
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Biophys J,
71,
246-256.
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L.A.Creuwels,
L.M.van Golde,
and
H.P.Haagsman
(1996).
Surfactant protein B: effects on lipid domain formation and intermembrane lipid flow.
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Biochim Biophys Acta,
1285,
1-8.
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Z.Wang,
O.Gurel,
J.E.Baatz,
and
R.H.Notter
(1996).
Acylation of pulmonary surfactant protein-C is required for its optimal surface active interactions with phospholipids.
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J Biol Chem,
271,
19104-19109.
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A.Clercx,
G.Vandenbussche,
T.Curstedt,
J.Johansson,
H.Jörnvall,
and
J.M.Ruysschaert
(1995).
Structural and functional importance of the C-terminal part of the pulmonary surfactant polypeptide SP-C.
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Eur J Biochem,
229,
465-472.
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A.D.Horowitz
(1995).
Exclusion of SP-C, but not SP-B, by gel phase palmitoyl lipids.
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Chem Phys Lipids,
76,
27-39.
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B.Pastrana-Rios,
S.Taneva,
K.M.Keough,
A.J.Mautone,
and
R.Mendelsohn
(1995).
External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface.
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Biophys J,
69,
2531-2540.
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S.Hawgood,
and
F.R.Poulain
(1995).
Functions of the surfactant proteins: a perspective.
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Pediatr Pulmonol,
19,
99.
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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.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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