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Figure 2.
Fig. 2. Structural representations of the determined solution
structure of hSOS1 PH domain. A, overlap of 20 structures with
the lowest target functions. In panels A-C, blue indicates an
 -helical
secondary structural element, yellow indicates the first  -sheet, and
green the second. The RMSD (Å) for the ensemble of^ 20
lowest target function structures are, for the backbone heavy
atoms (C , N  , C ) in the
secondary structure elements, residues 446-453 ( 1), 457-464
( 2), 467-471
( 3), 490-494
( 4), 498-504^
( 5), 512-518
( 6), 522-528
( 7), 531-548
( C), 0.33
Å, for all atoms in the secondary structures is 1.18
Å, for all backbone^ heavy atoms is 1.4 Å, and for
all atoms is 2.16 Å. Note the well defined secondary
structural elements, and the highly variable^ loops. B, ribbon
trace of one structure of A. The orientation is identical to
that of A. C, ribbon trace of the same structure^ as in B
rotated about the C- helix axis,
to show the specific^ relationship of the N-terminal -helix to
loop 3/4. There are^ 50 NOE distance constraints between the
N-terminal part (422-433) to the rest of the protein (446-551).
Five strong and absolutely unambiguous NOEs between backbone
protons are indicated in gray between the two substructures and
are (from top to bottom), Asn428 H -Ala^486 H
(nominal
upper limit NOE, 2.9 Å), Asn428 H -Glu487 HN
(3.23 Å), Ile^429 HN-Tyr488 HN (5.0 Å), Asp430
HN-Leu490 HN (4.14 Å), and Asp430 H -Arg489 H
(3.47
Å). D, grasp (14) charge surface of the SOS PH domain, in
the orientation of panels A and B.
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