Table 1.
Pairs of protein structures, DDMs, their characteristics and types of movements.
Pair # | Pair PDB | Resid. includ | Biomol d | Unit cell e | RMSDD Å | Δ % | δ % | Max move | Rigid motions | RMSDD / Δ final (Å / %) | Type |
---|---|---|---|---|---|---|---|---|---|---|---|
1 | 1cll1ctr | 138c | m | 12.83 | 54.92 | 4.08 | 46.7 | 5 | 0.44 / 2.70 | tweezers | |
2 | 4cd21cd2 | 202 | m | 1.25 | 2.62 | 11.7 | 11 | 0.44 / 4.74 | tweezers | ||
3 | 4ake1ank | 214 | m | 2 | 6.45 | 59.62 | 16.75 | 24.8 | >12 | glove/tweezers | |
4 | 1akz1ssp | 223 | m/tr | 1.14 | 21.89 | 3.19 | 5.5 | 11 | 0.31 / 0.61 | tweezers | |
4’ | 7 | 0.45 / 4.07 | |||||||||
5 | 2tbv2tbva | 287 | v. shell | 3 | 1.37 | 32.22 | 2.67 | 6.5 | 3 | 0.27 / 1.11 | hinge |
5’ | 2 | 0.43 / 3.35 | |||||||||
6 | 1l3f3tmn | 316 | m/tetr | 0.46 | 3.35 | 0.38 | 1.8 | 2 | 0.36 / 0.69 | pliers | |
7 | 4ape5er2 | 330 | m/d | 0.45 | 5.21 | 0.54 | 2.7 | 2 | 0.40 / 2.47 | pliers | |
8 | 6ldh1ldm | 329b | tetr | 1.25 | 15.37 | 4.53 | 12.3 | 10 | 0.41 / 2.86 | tweezers | |
8’ | 7 | 0.45 / 4.14 | |||||||||
8”g | 8 | 0.43 / 3.70 | |||||||||
9 | 2gd11gd1 | 334 | tetr | 0.49 | 6.14 | 0.74 | 3.1 | 2 | 0.36 / 1.89 | pliers | |
10 | 1erk2erk | 353 | m | 2.24 | 27.88 | 3.81 | 13.8f | >12 | glove/tweezers | ||
11 | 8adh6adh | 374b | d | 1/2 | 1.05 | 21.90 | 2.89 | 5.7 | 12 | 0.45 / 2.61 | tweezers |
12 | 9aat1ama | 401 | d | 2/1 | 1.20 | 22.96 | 7.48 | 6.7 | 7 | 0.36 / 2.52 | tweezers |
12’ | 3 | 0.43 / 4.12 | |||||||||
13 | 16pk13pk | 415b | m/d | 1/4 | 3.07 | 45.61 | 4.39 | 13.3 | >12 | glove/tweezers | |
14 | 1v4t1v4s | 424 | m | 6.90 | 49.24 | 5.66 | 38.9 | >12 | glove/tweezers | ||
15 | 4cts1cts | 437 | d | 2 | 1.58 | 26.30 | 12.20 | 9.6 | >12 | glove/tweezers | |
16 | 1hrd1bgv | 449 | h | 4 | 1.89 | 32.85 | 1.15 | 8.5 | 5 | 0.22 / 0.01 | pliers |
16’ | 2 | 0.35 / 1.84 | |||||||||
17 | 1lfh1lfg | 691b | m | 4.77 | 41.43 | 1.51 | 24.9 | 11 | 0.37 / 2.00 | tweezers | |
17’ | 7 | 0.45 / 3.19 |
there are 3 molecules in the 2tbv unit cell; 2 of them (A and B) do not have 102 residues or Cα atoms on the N-terminus; the 3rd (C) molecule is missing only 66 residues; we used A and C (shortened) molecules with the same number of resolved residues in the calculation.
for #13 3 N-terminal and 2 C-terminal residues, which dramatically change their conformation, were not included in the fitting and RMSDD evaluation; such non-included residues can be denoted by -3N, -2C for #13 and similarly indicate non-included residues in other structures; #17: -4N, -1C; #17’: -4N, -7C; #8 -5C; #11: -4N;
to make molecules comparable residues 1-3 and 148, missing in 1cll, and residues 76-80, missing in 1ctr, are not included in the DDM comparison.
likely but not fully reliable oligomerization state of biologically active molecule, estimates from PQS; notations in the table: m=monomeric, d=dimeric, tr=trimeric, tetr=tetrameric, h=hexameric.
number of molecules in the crystallographic unit cell; not shown – means 1; 1/2 means that 1st PDB entry (e.g., 8adh) has 1 molecule in the unit cell, and the second (e.g., 6adh) has 2 molecules in the unit cell.
9 N-terminal and 3 C-terminal residues move very far in a non-rigid manner; the value is given for the maximum DD closer to the middle of the chain.
characteristics of the transformation identical to 8’ except dividing 96-104 into 96-100 and 101-104 rigid fragments.