Notes on SCOP classification:

d3mon.5
d3mon.6
d3mon.7
d3mon.8
d4mon.3
d4mon.4:
These five domains each contain the alpha and beta chains of
monellin.  There is structural evidence that the alpha and beta
chains are products of a single gene (see reference below), although
the gene has not currently been found.  Sequences containing both
chains appear in our genetic domain sequences (i.e. g3mon.5).

Murzin AG, 1993. Sweet-tasting protein monellin is related to the cystatin
family of thiol proteinase inhibitors. JMB, v.230:689-694.


For some pairs of domains, sequence and structural homology
suggests that the domains are more closely related than implied
by their SCOP classifications.  In some of these cases, there
is a comment on the SCOP site clarifying the classification.  The
following comments are the opinions of the ASTRAL authors, not
the SCOP authors.

d1b22a_ vs d1doqa_:  These are classified as having the same fold
(SAM domain-like); however, these appear to have higher sequence
similarity than other pairs in the same fold classification and
may have a common evolutionary origin.

d1b3oa1 vs d1gyla_
d1b3ob1    d1al7__
	   d1al7__
           d1al8__
           d1gox__
	   d1huva_:
The two domains in the left column are classified as having the same
fold (TIM beta/alpha-barrel) as the six domains in the right column;
however, all of them have high sequence and structural similarity near
the phosphate-binding sites, suggesting a common evolutionary origin.

d1f0ya2 vs d1f8ra1
d1f0yb2    d1f8rb1
d1f12a2    d1f8rc1
d1f12b2    d1f8rd1
d1f14a2    d1f8re1
d1f14b2    d1f8rf1
d1f17a2    d1f8rg1
d1f17b2    d1f8rh1
           d1f8sa1
           d1f8sb1
           d1f8sc1
           d1f8sd1
           d1f8se1
           d1f8sf1
           d1f8sg1
           d1f8sh1:
The 8 domains in the left column are classified as being
in the same class but having a different fold as the 16 domains
in the right column.  The first set contains NAD(P)-binding
Rossmann-fold domains, and the second set contains FAD/NAD(P)-binding
domains.  There is high sequence similarity in the phosphate
binding sites of all these domains, suggesting a common evolutionary
origin.

d2tmda3 vs d1f8ra1
d2tmdb3    d1f8rb1
d1djna3    d1f8rc1
d1djnb3    d1f8rd1
d1djqa3    d1f8re1
d1f1qb3    d1f8rf1
           d1f8rg1
           d1f8rh1
           d1f8sa1
           d1f8sb1
           d1f8sc1
           d1f8sd1
           d1f8se1
           d1f8sf1
           d1f8sg1
           d1f8sh1:
The 6 domains in the left column contains nucleotide binding domains,
which have high sequence and structural similarity to the FAD/NAD(P)-
binding domains in the right column in the region of the phosphate
binding sites.

d1cuoa_ vs d1qkzl1:  These are in the same class (All beta), but different
fold categories.  However, they have similar topologies and some sequence
similarity, implying the possibility of a distant evolutionary relationship.