BDBC - BACSU - GREMLIN Contacts

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BDBC - Disulfide bond formation protein C

UniProt:	O32217	Sequences: MKNRIVFLYASWVVALIAMLGSLYFSEIRKFIPCELCWYQRILMYPLVLILGIATFQGDTRVKKYVLPMAIIGAFISIMHYLEQKVPGFSGIKPCVSGVPCSGQYINWFGFITIPFLALIAFILIIIFMCLLKGEKSE	Download Alignment We filter this alignment to remove sites that have many gaps before running GREMLIN. Date: 2015_01
Length:	138 (129)
Sequences:	450 (347)
Seq/√Len:	30.6

BACSU - BDBC BDBB

GREMLIN Results:

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

Residue pairs sorted by coevolution strength:

i	j	Sco	Prob
77_S	118_A	3.266	1.00
66_V	129_M	3.119	1.00
24_Y	29_R	2.988	1.00
25_F	106_I	2.940	1.00
39_Y	43_L	2.879	1.00
81_Y	116_F	2.780	1.00
14_V	124_L	2.539	0.99
71_I	126_I	2.482	0.99
109_F	112_I	2.400	0.99
74_A	123_I	2.377	0.99
81_Y	85_K	2.371	0.99
25_F	117_L	2.280	0.99
70_A	126_I	2.156	0.98
22_S	26_S	2.062	0.98
57_Q	64_K	1.982	0.97
95_C	98_G	1.922	0.96
22_S	45_Y	1.868	0.96
82_L	86_V	1.784	0.95
10_A	14_V	1.724	0.94
74_A	78_I	1.693	0.93
107_N	111_F	1.633	0.92
57_Q	65_Y	1.610	0.91
32_I	35_E	1.596	0.91
71_I	75_F	1.595	0.91
26_S	45_Y	1.587	0.90
8_L	54_A	1.565	0.90
59_D	65_Y	1.530	0.89
79_M	83_E	1.524	0.88
82_L	89_F	1.493	0.87
11_S	51_L	1.477	0.87
74_A	119_L	1.462	0.86
32_I	98_G	1.440	0.85
8_L	62_V	1.371	0.82
10_A	128_F	1.351	0.81
11_S	129_M	1.339	0.81
54_A	62_V	1.332	0.80
49_L	69_M	1.325	0.80
108_W	117_L	1.306	0.79
66_V	133_K	1.305	0.79
17_I	48_V	1.280	0.78
83_E	93_K	1.268	0.77
22_S	25_F	1.268	0.77
94_P	98_G	1.214	0.74
67_L	126_I	1.205	0.73
18_A	21_G	1.196	0.73
35_E	39_Y	1.194	0.73
50_I	62_V	1.188	0.72
24_Y	28_I	1.181	0.72
63_K	133_K	1.178	0.71
47_L	68_P	1.173	0.71
127_I	130_C	1.164	0.71
25_F	31_F	1.158	0.70
10_A	124_L	1.156	0.70
12_W	52_G	1.120	0.68
117_L	120_I	1.119	0.67
15_A	48_V	1.118	0.67
18_A	121_A	1.099	0.66
86_V	89_F	1.067	0.64
92_I	95_C	1.060	0.63
21_G	114_I	1.059	0.63
19_M	42_I	1.051	0.63
120_I	124_L	1.045	0.62
43_L	72_I	1.043	0.62
78_I	82_L	1.037	0.61
74_A	126_I	1.018	0.60
68_P	129_M	1.008	0.59
47_L	52_G	1.001	0.59
11_S	65_Y	0.961	0.56
54_A	90_S	0.953	0.55
13_V	120_I	0.943	0.54
5_I	58_G	0.931	0.53
106_I	117_L	0.917	0.52
31_F	45_Y	0.914	0.52
51_L	65_Y	0.912	0.52
77_S	119_L	0.909	0.51
108_W	111_F	0.892	0.50
17_I	120_I	0.892	0.50
112_I	116_F	0.889	0.50
11_S	47_L	0.883	0.49
14_V	128_F	0.883	0.49
43_L	74_A	0.880	0.49
81_Y	84_Q	0.866	0.48
84_Q	113_T	0.863	0.48
25_F	105_Y	0.861	0.48
43_L	76_I	0.856	0.47
63_K	66_V	0.850	0.47
50_I	130_C	0.842	0.46
81_Y	86_V	0.839	0.46
10_A	131_L	0.836	0.46
54_A	65_Y	0.830	0.45
21_G	44_M	0.820	0.44
18_A	44_M	0.816	0.44
70_A	74_A	0.808	0.43
102_S	129_M	0.806	0.43
51_L	66_V	0.801	0.43
106_I	116_F	0.784	0.41
25_F	108_W	0.776	0.41
14_V	17_I	0.776	0.41
39_Y	42_I	0.772	0.41
107_N	114_I	0.758	0.39
26_S	113_T	0.757	0.39
9_Y	90_S	0.757	0.39
21_G	25_F	0.751	0.39
7_F	124_L	0.749	0.39
19_M	39_Y	0.747	0.39
21_G	106_I	0.746	0.39
47_L	66_V	0.742	0.38
13_V	49_L	0.741	0.38
9_Y	55_T	0.738	0.38
111_F	116_F	0.728	0.37
11_S	59_D	0.726	0.37
53_I	68_P	0.725	0.37
77_S	80_H	0.724	0.37
11_S	94_P	0.723	0.37
55_T	128_F	0.713	0.36
78_I	109_F	0.711	0.36
36_L	76_I	0.709	0.36
104_Q	107_N	0.709	0.36
11_S	16_L	0.708	0.36
52_G	55_T	0.705	0.35
81_Y	89_F	0.704	0.35
19_M	48_V	0.700	0.35
25_F	113_T	0.690	0.34
49_L	70_A	0.688	0.34
23_L	45_Y	0.685	0.34
68_P	126_I	0.684	0.34
72_I	121_A	0.682	0.34
75_F	90_S	0.680	0.34
53_I	64_K	0.674	0.33
120_I	123_I	0.669	0.33
31_F	113_T	0.662	0.32
53_I	62_V	0.661	0.32
47_L	51_L	0.656	0.32
22_S	105_Y	0.656	0.32
44_M	122_F	0.655	0.32
86_V	92_I	0.654	0.32
53_I	72_I	0.650	0.32
45_Y	105_Y	0.646	0.31
129_M	133_K	0.641	0.31
78_I	121_A	0.639	0.31
22_S	113_T	0.639	0.31
55_T	60_T	0.638	0.31
80_H	118_A	0.637	0.31
75_F	130_C	0.632	0.30
11_S	14_V	0.631	0.30
25_F	107_N	0.630	0.30
26_S	31_F	0.630	0.30
29_R	104_Q	0.627	0.30
29_R	35_E	0.618	0.29
63_K	129_M	0.614	0.29
14_V	66_V	0.610	0.29
14_V	119_L	0.608	0.29
36_L	51_L	0.600	0.28
128_F	131_L	0.593	0.28
100_P	116_F	0.586	0.27
25_F	114_I	0.583	0.27
59_D	128_F	0.580	0.27
6_V	55_T	0.577	0.27
77_S	100_P	0.576	0.27
12_W	67_L	0.575	0.27
84_Q	105_Y	0.572	0.26
100_P	103_G	0.571	0.26
64_K	68_P	0.569	0.26
78_I	119_L	0.566	0.26
38_W	44_M	0.565	0.26
33_P	44_M	0.564	0.26
87_P	94_P	0.559	0.26
63_K	83_E	0.557	0.26
60_T	76_I	0.555	0.25
119_L	123_I	0.554	0.25
49_L	72_I	0.554	0.25
65_Y	129_M	0.553	0.25
35_E	76_I	0.550	0.25
9_Y	83_E	0.548	0.25
51_L	129_M	0.547	0.25
50_I	65_Y	0.546	0.25
43_L	90_S	0.546	0.25
12_W	54_A	0.545	0.25
7_F	17_I	0.545	0.25
108_W	113_T	0.540	0.24
9_Y	97_S	0.539	0.24
85_K	110_G	0.532	0.24
53_I	65_Y	0.528	0.24
11_S	63_K	0.527	0.24
9_Y	63_K	0.525	0.24
68_P	95_C	0.523	0.23
59_D	62_V	0.523	0.23
72_I	76_I	0.521	0.23
13_V	130_C	0.519	0.23
35_E	128_F	0.516	0.23
107_N	110_G	0.514	0.23
18_A	89_F	0.510	0.23
84_Q	89_F	0.508	0.23
22_S	42_I	0.500	0.22

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
2hi7B	1	0.7826	99.9	0.564	Contact Map
4nv5A	1	0.5	87.1	0.916	Contact Map
2l0lA	1	0.1957	54.9	0.935	Contact Map
1xioA	2	0.6594	18.3	0.95	Contact Map
3qapA	1	0.7029	9.6	0.956	Contact Map
3am6A	3	0.6667	9	0.956	Contact Map
4qi1A	3	0.7174	8.5	0.957	Contact Map
3wu2M	2	0.2319	8	0.957	Contact Map
2l0nA	1	0.1884	7.7	0.958	Contact Map
3wt9A	1	0.7101	7	0.959	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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