hae12298-sup-0001-FigS1.tiffTIFF image1521KFigure S1. Gene structure of F13A and the positions of mutations (a), and domain structure of FXIII-A (b). Panel a: the human F13A gene spans about 177 kb. Exons are indicated by grey squares and Roman numerals. Positions of identified mutations (boxed) and polymorphisms are indicated by straight lines (*SNP ID [ver] Sequencing directions are indicated by arrows. Panel b: from the N-terminal of FXIII-A protein, there are an activation peptide (AP), β-sandwich, core, and two β-barrel domains. Positions of mutations are indicated by arrows.
hae12298-sup-0002-FigS2.tiffTIFF image1521KFigure S2. Mutated nucleotide sequences of parts of exons IV and VII including W187X (a) and G273V (b) substitutions respectively. Red arrows indicate where the mutations were identified, the abnormal sequences are underlined and coloured in red.
hae12298-sup-0003-FigS3.tiffTIFF image1521KFigure S3. Molecular modelling for FXIII-A mutants (colour version). Panel a shows the crystal structure of the FXIII-A dimeric subunit as a ribbon representation. The native Gly273 residue is depicted as van der Waals spheres. The truncated β-sandwich domain resulting from the nonsense mutation W187X is highlighted on the left side of the dimer symmetry as a red coloured ribbon. On the right side of the symmetry, the individual domains are represented in differently coloured ribbons. Panels b & c show the close-up view of the local molecular environment for the native Gly273 and mutated Val273 residue respectively. The backbone is represented as a grey ribbon. The native and the mutated residues are depicted in blue stick format surrounded by their van der Waals spheres (also illustrated with blue colour). In Panel b one can observe the reverse turn (the participating residues depicted in red stick format; the intra-motif hydrogen bonds depicted as yellow dots) leading to the Gly273 residue. In Panel c the residues putatively clashing with the mutated Val273 are depicted as red sticks along with their van der Waals spheres. In both Panels b and c the catalytic triad is depicted as a triangle with the participating residues in stick representation to highlight its proximity to the native/mutated residue. Panel d shows the close-up view for Panel c. The colour combinations and representations are similar to Panel c, the backbone is removed for the sake of visual simplification. The overlapping van der Waals surfaces are outlined by dotted lines i.e. the regions where the blue and red colours merge.

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