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273 a.a.
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255 a.a.
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236 a.a.
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40 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structural analysis of antiviral agents that interact with the capsid of human rhinoviruses.
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Authors
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J.Badger,
I.Minor,
M.A.Oliveira,
T.J.Smith,
M.G.Rossmann.
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Ref.
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Proteins, 1989,
6,
1.
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PubMed id
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Abstract
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X-Ray diffraction data have been obtained for nine related antiviral agents
("WIN compounds") while bound to human rhinovirus 14 (HRV14). These compounds
can inhibit both viral attachment to host cells and uncoating. To calculate
interpretable electron density maps it was necessary to account for (1) the low
(approximately 60%) occupancies of these compounds in the crystal, (2) the large
(up to 7.9 A) conformational changes induced at the attachment site, and (3) the
incomplete diffraction data. Application of a density difference map technique,
which exploits the 20-fold noncrystallographic redundancy in HRV14, resulted in
clear images of the HRV14:WIN complexes. A real-space refinement procedure was
used to fit atomic models to these maps. The binding site of WIN compounds in
HRV14 is a hydrophobic pocket composed mainly from residues that form the
beta-barrel of VP1. Among rhinoviruses, the residues associated with the binding
pocket are far more conserved than external residues and are mostly contained
within regular secondary structural elements. Molecular dynamics simulations of
three HRV14:WIN complexes suggest that portions of the WIN compounds and viral
protein near the entrance of the binding pocket are more flexible than portions
deeper within the beta-barrel.
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Secondary reference #1
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Title
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The use of molecular replacement phases for the refinement of the human rhinovirus 14 structure
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Authors
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E.Arnold,
M.G.Rossmann.
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Ref.
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TO BE PUBLISHED ...
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Secondary reference #2
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Title
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Analysis of the structure of a common cold virus, Human rhinovirus 14, Refined at a resolution of 3.0 a.
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Authors
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E.Arnold,
M.G.Rossmann.
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Ref.
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J Mol Biol, 1990,
211,
763-801.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
95%.
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Secondary reference #3
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Title
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Three-Dimensional structures of drug-Resistant mutants of human rhinovirus 14.
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Authors
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J.Badger,
S.Krishnaswamy,
M.J.Kremer,
M.A.Oliveira,
M.G.Rossmann,
B.A.Heinz,
R.R.Rueckert,
F.J.Dutko,
M.A.Mckinlay.
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Ref.
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J Mol Biol, 1989,
207,
163-174.
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PubMed id
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Secondary reference #4
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Title
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Structural analysis of a series of antiviral agents complexed with human rhinovirus 14
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Authors
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J.Badger,
I.Minor,
M.J.Kremer,
M.A.Oliveira,
T.J.Smith,
J.P.Griffith,
D.M.A.Guerin,
S.Krishnaswamy,
M.Luo,
M.G.Rossmann,
M.A.Mckinlay,
G.D.Diana,
F.J.Dutko,
M.Fancher,
R.R.Rueckert,
B.A.Heinz.
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Ref.
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proc natl acad sci usa, 1988,
85,
3304.
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Secondary reference #5
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Title
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The structure determination of a common cold virus, Human rhinovirus 14
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Authors
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E.Arnold,
G.Vriend,
M.Luo,
J.P.Griffith,
G.Kamer,
J.W.Erickson,
J.E.Johnson,
M.G.Rossmann.
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Ref.
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acta crystallogr ,sect a, 1987,
43,
346.
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Secondary reference #6
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Title
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Implications of the picornavirus capsid structure for polyprotein structure
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Authors
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E.Arnold,
M.Luo,
G.Vriend,
M.G.Rossmann,
A.C.Palmenberg,
G.D.Parks,
M.J.H.Nicklin,
E.Wimmer.
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Ref.
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proc natl acad sci usa, 1987,
84,
21.
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Secondary reference #7
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Title
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The site of attachment in human rhinovirus 14 for antiviral agents that inhibit uncoating.
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Authors
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T.J.Smith,
M.J.Kremer,
M.Luo,
G.Vriend,
E.Arnold,
G.Kamer,
M.G.Rossmann,
M.A.Mckinlay,
G.D.Diana,
M.J.Otto.
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Ref.
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Science, 1986,
233,
1286-1293.
[DOI no: ]
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PubMed id
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Secondary reference #8
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Title
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The structure of a human common cold virus (rhinovirus 14) and its evolutionary relations to other viruses
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Authors
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M.G.Rossmann,
E.Arnold,
J.W.Erickson,
E.A.Frankenberger,
J.P.Griffith,
H.-J.Hecht,
J.E.Johnson,
G.Kamer,
M.Luo,
G.Vriend.
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Ref.
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chem scr, 1987,
26,
313.
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Secondary reference #9
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Title
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Structure of a human common cold virus and functional relationship to other picornaviruses.
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Authors
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M.G.Rossmann,
E.Arnold,
J.W.Erickson,
E.A.Frankenberger,
J.P.Griffith,
H.J.Hecht,
J.E.Johnson,
G.Kamer,
M.Luo,
A.G.Mosser.
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Ref.
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Nature, 1985,
317,
145-153.
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PubMed id
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Secondary reference #10
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Title
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Virion orientation in cubic crystals of the human common cold virus hrv14.
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Authors
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E.Arnold,
J.W.Erickson,
G.S.Fout,
E.A.Frankenberger,
H.J.Hecht,
M.Luo,
M.G.Rossman,
R.R.Rueckert.
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Ref.
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J Mol Biol, 1984,
177,
417-430.
[DOI no: ]
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PubMed id
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Figure 1.
Fro. 1. Cubic RlP rystals in a hanging drop within a vapor diffusion well. The prncipal faces of the
csrystals correspond to octahedral geometry. These crystals were approximately 0.3 mm in diameter.
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Figure 3.
Fro. 3. Stereographic projction illustrating the data collection scheme
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #11
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Title
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Picornaviruses of two different genera have similar structures.
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Authors
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M.Luo,
E.Arnold,
J.W.Erickson,
M.G.Rossmann,
U.Boege,
D.G.Scraba.
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Ref.
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J Mol Biol, 1984,
180,
703-714.
[DOI no: ]
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PubMed id
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Figure 1.
MING Luo, EDWARD ARNOLD, JOHN W. ERICKSON?, MICHAEL G. ROSSMANN
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Figure 7.
FIG. 7. Cross-rotation functions between Mengo and rhinovirus crystals. (a) Mengo stationary
(compund 1) with rhino (compoun 2) rotted by -6. (b) Rhino tationary (compound 1) with
Mengo (compound 2) rotated by -6. R = 0 corresponds approximately to the mean value of the
rotation functions.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #12
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Title
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Crystallization of a common cold virus, Human rhinovirus 14. (Quote)isomorphism(quote) with poliovirus crystals
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Authors
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J.W.Erickson,
E.A.Frankenberger,
M.G.Rossmann,
G.S.Fout,
K.C.Medappa,
R.R.Rueckert.
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Ref.
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proc natl acad sci usa, 1983,
80,
931.
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