| Table 2: Matrix of equivalent residue pairs of available AraC/XylS 3D structures(a). |
| | 1bl0 | 1xs9 | 1d5y | 3oou | 2k9s | 3gbg | 3mkl | 3mn2 | 3oio | 3lsg | 1u8b | 1wpk | 1zgw | |
| | 1bl0 | 100 | 100 | 100 | 96 | 84 | 81 | 88 | 82 | 94 | 97 | 47 | 44 | 42 | 1bl0 | | 0.0 | 0.7 | 0.9 | 1.8 | 1.9 | 2.2 | 1.9 | 2.2 | 1.9 | 1.3 | 1.6 | 2.2 | 2.3 | | | 100% | 100% | 50% | 18% | 16% | 15% | 16% | 14% | 19% | 25% | 15% | 13% | 15% | | | 1xs9 | | 100 | 100 | 93 | 82 | 78 | 88 | 84 | 93 | 97 | 48 | 45 | 45 | 1xs9 | | | 0.0 | 1.1 | 1.7 | 1.8 | 2.0 | 1.8 | 2.0 | 1.7 | 1.4 | 1.7 | 2.3 | 2.3 | | | | 100% | 50% | 18% | 16% | 15% | 16% | 14% | 19% | 25% | 15% | 13% | 15% | | | 1d5y | | | 100 | 95 | 80 | 81 | 88 | 88 | 95 | 97 | 45 | 44 | 41 | 1d5y | | | | 0.0 | 1.5 | 1.7 | 2.1 | 1.8 | 2.0 | 1.8 | 1.2 | 1.7 | 2.3 | 2.3 | | | | | 100% | 20% | 21% | 16% | 11% | 16% | 21% | 25% | 25% | 18% | 17% | | | 3oou | | | | 100 | 72 | 84 | 87 | 88 | 87 | 97 | 47 | 42 | 37 | 3oou | | | | | 0.0 | 2.0 | 2.3 | 1.8 | 1.8 | 1.9 | 1.4 | 1.7 | 2.3 | 2.3 | | | | | | 100% | 23% | 16% | 17% | 20% | 20% | 31% | 15% | 13% | 11% | | | 2k9s | | | | | 101 | 89 | 91 | 84 | 95 | 86 | 45 | 41 | 33 | 2k9s | | | | | | 0.0 | 2.0 | 2.0 | 2.3 | 1.8 | 1.9 | 2.1 | 2.3 | 2.6 | | | | | | | 100% | 21% | 24% | 22% | 25% | 26% | 23% | 10% | 9% | | | 3gbg | | | | | | 99 | 90 | 84 | 95 | 81 | 35 | 36 | 23 | 3gbg | | | | | | | 0.0 | 1.5 | 2.2 | 1.6 | 2.0 | 2.3 | 2.4 | 2.6 | | | | | | | | 100% | 28% | 15% | 20% | 23% | 8% | 3% | 6% | | | 3mkl | | | | | | | 99 | 96 | 95 | 88 | 45 | 32 | 35 | 3mkl | | | | | | | | 0.0 | 1.7 | 1.3 | 1.7 | 1.9 | 2.4 | 2.5 | | | | | | | | | 100% | 21% | 26% | 23% | 19% | 10% | 8% | | | 3mn2 | | | | | | | | 102 | 100 | 85 | 44 | 40 | 28 | 3mn2 | | | | | | | | | 0.0 | 1.6 | 2.0 | 2.1 | 2.2 | 2.8 | | | | | | | | | | 100% | 28% | 15% | 21% | 12% | 13% | | | 3oio | | | | | | | | | 100 | 93 | 51 | 45 | 35 | 3oio | | | | | | | | | | 0.0 | 1.8 | 2.0 | 2.0 | 2.7 | | | | | | | | | | | 100% | 18% | 33% | 22% | 21% | | | 3lsg | | | | | | | | | | 100 | 45 | 48 | 41 | 3lsg | | | | | | | | | | | 0.0 | 1.5 | 2.4 | 2.2 | | | | | | | | | | | | 100% | 15% | 13% | 19% | | | 1u8b | | | | | | | | | | | 52 | 41 | 36 | 1u8b | | | | | | | | | | | | 0.0 | 2.5 | 2.2 | | | | | | | | | | | | | 100% | 62% | 44% | | | 1wpk | | | | | | | | | | | | 60 | 28 | 1wpk | | | | | | | | | | | | | 0.0 | 2.5 | | | | | | | | | | | | | | 100% | 28% | | | 1zgw | | | | | | | | | | | | | 53 | 1zgw | | | | | | | | | | | | | | 0.0 | | | | | | | | | | | | | | | 100% | |
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(a)The top number indicates the number of equivalent positions of the aligned structures (length of the alignment). The middle number denotes the root mean square (RMS) deviation of equivalent atoms (3.5 Å distance cutoff) and the lower number denotes the sequence identity of equivalent residues. Structures were aligned with SALIGN [16]. Structures of unknown biological role are indicated in bold.
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