1. The Structural Basis of Localization and Signaling by the Focal Adhesion Targeting Domain 
Stefan T Arold, Maria K Hoellerer, Martin E.M Noble 
Structure 
Volume 10, Issue 3, Pages (March 2002)
DOI: /S (02)

2. Figure 1 Crystal Structures of FAK892–1052
(A) Ribbon diagram of the FAT domain as found in crystal form I, color-ramped from the N terminus (blue) to the C terminus (red). Side chains for residues of the Grb2 binding site (Y925, N927, and V928; carbons colored orange) and those involved in linking helix 1 to helix 4 (R919, D922, D1039, and R1042; carbons colored green) are shown.
(B) Expanded view on the region surrounding Y925.
(C) Electron density for crystal form II in the region of domain exchange. The map is the cross-crystal averaged experimental map contoured at 0.22 e−.Å−3.
(D) Ribbon diagram of the helix-exchanged form found in crystal form II. Figures prepared with Aesop (M.E.M. Noble, unpublished data). Y925, a site of in vivo phosphorylation, and surrounding residues are indicated.
Structure  , DOI: ( /S (02) )

3. Figure 2 In Vitro Pull-Down Assays
The binding of phosphorylated FAK892–1052 (pFAT; columns 1, 3, and 5) and unphosphorylated FAK892–1052 (FAT; columns 2, 4, and 6) to either agarose-linked anti-phosphotyrosine antibody (anti-pY AB; columns 1 and 2) or GST-fused Grb2 SH2 (GST-Grb2 SH2; Columns 3, 4, 5, and 6) was assayed by pull-down as described in Experimental Procedures.
The gels are Coomassie stained, with the top line presenting the amounts of the FAT ligand used in the pull-down assay and the lower line demonstrating the amount of FAT bound.
Structure  , DOI: ( /S (02) )

4. Figure 3
Structure-Based Sequence Alignment of the FAT Domain Superfamily
Colors are by residue hydrophobicity (red, maximally hydrophobic; blue, maximally hydrophilic) and conservation (the most conserved columns have the most saturated colors, and the least conserved have the palest colors). The figure was prepared using Jalview. Secondary structure is taken from molecule C of crystal form I. FAK2 is also known as PYK2, RAFTK, CAKβ, or CADTK.
Structure  , DOI: ( /S (02) )

5. Figure 4
Sequence Conservation Mapped onto the Molecular Surface of the FAT Domain
The surface is colored according to sequence conservation (blue, 100%; red, 50% conserved).
(A) View onto helix 2 and 3 showing the conserved patch that is a likely candidate for the paxillin binding site.
(B) View onto helices 1 and 4, including PBS1 and PBS2, previously postulated by Tachibana et al. [16] to bind paxillin. The figure was prepared using Aesop (M.E.M Noble, unpublished data).
Structure  , DOI: ( /S (02) )