TLP - BACSU - GREMLIN Contacts

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TLP - Small, acid-soluble spore protein Tlp

UniProt:	Q45060	Sequences: MTKNQNQYQQPNPDDRSDNVEKLQDMVQNTIENIEEAEASMEFASGEDKQRIKEKNARREQSIEAFRNEIQDESAARQNGYRS	Download Alignment We filter this alignment to remove sites that have many gaps before running GREMLIN. Date: 2015_01
Length:	83 (69)
Sequences:	162 (130)
Seq/√Len:	15.7

GREMLIN Results:

Legend: The darker and larger the blue dots, the higher coevolution strength.

Residue pairs sorted by coevolution strength:

i	j	Sco	Prob
18_D	22_K	4.000	1.00
40_S	48_D	3.200	0.99
23_L	26_M	2.735	0.97
25_D	29_N	2.526	0.95
39_A	44_A	2.399	0.93
27_V	70_I	2.175	0.89
57_A	60_E	2.091	0.87
38_E	60_E	2.071	0.86
28_Q	34_I	2.043	0.85
40_S	44_A	2.016	0.85
22_K	26_M	1.961	0.83
34_I	37_A	1.736	0.74
31_I	67_R	1.693	0.72
23_L	52_I	1.658	0.71
46_G	71_Q	1.596	0.68
58_R	74_S	1.448	0.60
29_N	77_R	1.298	0.52
49_K	53_K	1.285	0.51
47_E	51_R	1.246	0.49
50_Q	53_K	1.230	0.48
48_D	51_R	1.222	0.47
38_E	57_A	1.221	0.47
40_S	43_F	1.218	0.47
40_S	62_S	1.198	0.46
37_A	52_I	1.169	0.44
62_S	65_A	1.156	0.43
54_E	58_R	1.155	0.43
37_A	65_A	1.136	0.42
20_V	74_S	1.122	0.42
12_N	72_D	1.108	0.41
49_K	54_E	1.087	0.40
60_E	78_Q	1.046	0.37
10_Q	36_E	1.006	0.35
66_F	72_D	0.992	0.35
20_V	24_Q	0.985	0.34
25_D	34_I	0.958	0.33
29_N	34_I	0.956	0.33
28_Q	32_E	0.947	0.32
44_A	48_D	0.926	0.31
12_N	68_N	0.922	0.31
40_S	72_D	0.863	0.28
50_Q	68_N	0.855	0.28
35_E	40_S	0.855	0.28
28_Q	63_I	0.846	0.27
31_I	66_F	0.837	0.27
67_R	71_Q	0.832	0.27
67_R	74_S	0.826	0.26
37_A	60_E	0.812	0.26
31_I	63_I	0.808	0.26
35_E	42_E	0.799	0.25
61_Q	64_E	0.797	0.25
52_I	75_A	0.782	0.25
22_K	63_I	0.776	0.24
34_I	64_E	0.772	0.24
11_P	43_F	0.765	0.24
45_S	54_E	0.761	0.24
21_E	77_R	0.722	0.22
25_D	54_E	0.721	0.22
46_G	50_Q	0.721	0.22
65_A	68_N	0.716	0.22
71_Q	75_A	0.713	0.22
37_A	53_K	0.708	0.22
26_M	66_F	0.703	0.21
11_P	44_A	0.689	0.21
43_F	48_D	0.688	0.21
11_P	47_E	0.687	0.21
25_D	77_R	0.667	0.20
57_A	61_Q	0.666	0.20
25_D	51_R	0.665	0.20
32_E	51_R	0.662	0.20
57_A	71_Q	0.638	0.19
57_A	76_A	0.636	0.19
46_G	62_S	0.631	0.19
49_K	72_D	0.630	0.19
36_E	65_A	0.627	0.19
40_S	52_I	0.626	0.19
25_D	78_Q	0.614	0.18
41_M	49_K	0.613	0.18
45_S	74_S	0.612	0.18
43_F	65_A	0.607	0.18
12_N	43_F	0.601	0.18
15_D	76_A	0.596	0.18
64_E	74_S	0.589	0.17
41_M	44_A	0.589	0.17
20_V	76_A	0.587	0.17
35_E	62_S	0.583	0.17
27_V	35_E	0.581	0.17
26_M	63_I	0.578	0.17
23_L	66_F	0.576	0.17
71_Q	74_S	0.573	0.17
17_S	42_E	0.564	0.16
45_S	78_Q	0.559	0.16
23_L	27_V	0.539	0.16
32_E	54_E	0.519	0.15
40_S	46_G	0.519	0.15
34_I	60_E	0.514	0.15
28_Q	49_K	0.513	0.15
22_K	46_G	0.511	0.15
41_M	51_R	0.510	0.15
35_E	67_R	0.509	0.15
45_S	50_Q	0.507	0.15
27_V	31_I	0.501	0.15
53_K	78_Q	0.501	0.15
17_S	26_M	0.500	0.15

Legend: The i and j are positions as given in the UniProt sequence. Only predictions with Prob ≥ 0.7 are listed. For all 3L/2 predictions, click on one of the links below.

Sco = ((raw_sco - min_sco)/(avg_sco - min_sco))/2 + 0.5
Prob = P(contact | Sco, seq80/√len)
seq80 = effective number of sequences, after reducing redundancy to 80% identity

Text file of predictions (all 3L/2 predictions)
Generate restraints for ROSETTA Structure Modeling
Upload PDB model overlay contacts on the model

HHsearch Results:

Legend: GREMLIN results (Prob ≥ 0.7) overlaid on top PDB hits. The grey/red filled circles underneath are pdb residue contacts (min distance < 5 Angstroms). The shade of the circles is based on the top 10 (or top 20 if e-value < 1E-20) HHsearch results which uses the overall probability and per-site alignment prob. Inter oligomeric contacts in the pdb are in shades of red.

PDB	Chains	Cov	%	HHΔ
2azeA	1	0.4578	8.8	0.927	Contact Map
4cfgA	2	0.8193	3.7	0.939	Contact Map
3tyyA	2	0.6265	3.4	0.94	Contact Map
4pxuA	3	0.3855	2.9	0.942	Contact Map
3m4iA	2	0.4337	2.2	0.946	Contact Map
4yv4A	3	0.4699	2.1	0.946	Contact Map
3b5nB	1	0.4578	2.1	0.946	Contact Map
2npsB	1	0.494	2.1	0.946	Contact Map
4tn3A	2	1	1.9	0.947	Contact Map
3c01A	1	0	1.8	0.948	Contact Map

Sequence Conservation (Image Generated using WebLogo v3)

Legend: Color is used to show Hydrophobicity (Blue: Hydrophilic, Green: Neutral and Black: Hydrophobic). Amount of gaps is represented by width.

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