YQJC - BACSU - GREMLIN Contacts

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YQJC - Uncharacterized protein YqjC

UniProt:	P54540	Sequences: MNRLDHIGIAVFSIKDARSFYENVLGLAFLHQETVEEQKVNVAFFQAGSVKLELIEPLTADSPVHLFLEKKGQGLHHIAFLCNCLSEQLQALSDQHVQLIDRFPRQGANGKKIAFISPRETNGVLVELCEPKGDQHNEHE	Download Alignment We filter this alignment to remove sites that have many gaps before running GREMLIN. Date: 2015_01
Length:	140 (128)
Sequences:	5980 (3015)
Seq/√Len:	266.5

ECOLI - YAER LGUL
BACSU - YQJC YWKD YWBC YURT
HALSA - Q9HRZ3
SULSO - Q97W20

GREMLIN Results:

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

Residue pairs sorted by coevolution strength:

i	j	Sco	Prob
19_S	23_N	4.511	1.00
90_Q	94_D	3.592	1.00
91_A	95_Q	3.495	1.00
84_C	87_E	3.146	1.00
89_L	99_L	3.137	1.00
93_S	102_R	2.416	1.00
13_S	16_D	2.359	1.00
3_R	81_L	2.234	1.00
29_F	43_A	2.094	1.00
92_L	97_V	2.055	1.00
39_K	59_T	1.968	1.00
30_L	46_Q	1.794	1.00
46_Q	51_K	1.755	1.00
77_H	127_E	1.718	1.00
5_D	131_P	1.717	1.00
89_L	93_S	1.712	1.00
30_L	51_K	1.700	1.00
87_E	91_A	1.692	1.00
86_S	90_Q	1.691	1.00
98_Q	117_S	1.675	1.00
65_H	69_E	1.638	1.00
34_T	41_N	1.618	1.00
66_L	69_E	1.599	1.00
14_I	43_A	1.539	1.00
12_F	73_Q	1.525	1.00
86_S	112_K	1.478	1.00
32_Q	41_N	1.454	1.00
4_L	78_I	1.437	1.00
92_L	128_L	1.436	1.00
117_S	125_L	1.405	1.00
22_E	29_F	1.317	1.00
88_Q	91_A	1.315	1.00
107_G	112_K	1.309	1.00
57_P	68_L	1.290	1.00
18_R	45_F	1.286	1.00
42_V	55_I	1.277	1.00
22_E	45_F	1.262	1.00
47_A	50_V	1.233	1.00
93_S	99_L	1.226	1.00
15_K	32_Q	1.223	1.00
28_A	46_Q	1.218	1.00
19_S	22_E	1.205	1.00
18_R	22_E	1.201	1.00
62_S	65_H	1.191	1.00
27_L	47_A	1.190	1.00
88_Q	92_L	1.180	1.00
82_C	88_Q	1.168	1.00
80_F	126_V	1.166	1.00
29_F	32_Q	1.165	1.00
75_L	78_I	1.149	1.00
79_A	129_C	1.149	1.00
57_P	62_S	1.149	1.00
16_D	19_S	1.135	1.00
41_N	58_L	1.125	1.00
57_P	65_H	1.115	1.00
10_A	64_V	1.095	1.00
41_N	56_E	1.087	1.00
4_L	50_V	1.087	1.00
3_R	49_S	1.082	1.00
15_K	43_A	1.074	1.00
17_A	21_Y	1.067	1.00
11_V	54_L	1.065	1.00
14_I	18_R	1.052	1.00
23_N	95_Q	1.051	1.00
5_D	81_L	1.050	1.00
15_K	19_S	1.048	1.00
101_D	104_P	1.033	1.00
86_S	103_F	1.025	1.00
19_S	24_V	1.014	1.00
115_F	127_E	1.011	1.00
114_A	117_S	1.007	1.00
40_V	55_I	1.006	1.00
20_F	24_V	1.004	1.00
6_H	79_A	1.000	1.00
11_V	14_I	0.998	1.00
81_L	131_P	0.997	1.00
91_A	94_D	0.996	1.00
35_V	38_Q	0.981	1.00
67_F	74_G	0.961	1.00
67_F	72_G	0.957	1.00
18_R	43_A	0.942	1.00
8_G	55_I	0.938	1.00
87_E	90_Q	0.935	1.00
42_V	53_E	0.922	1.00
36_E	39_K	0.913	1.00
13_S	19_S	0.898	1.00
17_A	20_F	0.898	1.00
22_E	28_A	0.896	1.00
85_L	130_E	0.891	1.00
90_Q	93_S	0.890	1.00
5_D	79_A	0.875	1.00
101_D	105_R	0.862	1.00
98_Q	120_E	0.860	1.00
89_L	114_A	0.856	1.00
86_S	114_A	0.840	0.99
72_G	79_A	0.834	0.99
127_E	130_E	0.833	0.99
100_I	117_S	0.832	0.99
85_L	89_L	0.829	0.99
35_V	40_V	0.828	0.99
17_A	54_L	0.825	0.99
18_R	29_F	0.825	0.99
47_A	80_F	0.820	0.99
24_V	95_Q	0.818	0.99
12_F	16_D	0.817	0.99
10_A	74_G	0.816	0.99
39_K	58_L	0.798	0.99
120_E	123_G	0.796	0.99
12_F	68_L	0.794	0.99
32_Q	43_A	0.788	0.99
100_I	125_L	0.768	0.99
10_A	76_H	0.767	0.99
7_I	78_I	0.748	0.99
107_G	115_F	0.721	0.98
62_S	67_F	0.710	0.98
11_V	52_L	0.705	0.98
120_E	124_V	0.699	0.98
121_T	124_V	0.695	0.98
117_S	128_L	0.693	0.98
61_D	65_H	0.690	0.98
85_L	103_F	0.686	0.98
9_I	75_L	0.677	0.98
112_K	116_I	0.673	0.98
92_L	116_I	0.672	0.98
29_F	45_F	0.672	0.98
104_P	107_G	0.665	0.97
46_Q	49_S	0.664	0.97
9_I	78_I	0.661	0.97
117_S	127_E	0.661	0.97
78_I	126_V	0.658	0.97
5_D	51_K	0.658	0.97
42_V	45_F	0.657	0.97
13_S	56_E	0.649	0.97
85_L	88_Q	0.647	0.97
85_L	128_L	0.644	0.97
38_Q	105_R	0.629	0.96
7_I	113_I	0.626	0.96
9_I	21_Y	0.624	0.96
63_P	76_H	0.617	0.96
110_G	116_I	0.607	0.96
116_I	121_T	0.604	0.95
101_D	106_Q	0.602	0.95
92_L	99_L	0.601	0.95
39_K	61_D	0.598	0.95
107_G	113_I	0.596	0.95
67_F	124_V	0.593	0.95
10_A	68_L	0.588	0.95
17_A	122_N	0.586	0.95
111_K	114_A	0.585	0.95
11_V	17_A	0.577	0.94
12_F	69_E	0.575	0.94
9_I	52_L	0.573	0.94
68_L	76_H	0.567	0.94
20_F	121_T	0.565	0.94
89_L	101_D	0.565	0.94
82_C	85_L	0.564	0.93
70_K	73_Q	0.563	0.93
25_L	49_S	0.562	0.93
110_G	113_I	0.560	0.93
15_K	56_E	0.559	0.93
55_I	64_V	0.552	0.93
67_F	76_H	0.550	0.93
64_V	67_F	0.547	0.92
4_L	9_I	0.547	0.92
66_L	72_G	0.545	0.92
86_S	105_R	0.544	0.92
44_F	53_E	0.543	0.92
104_P	115_F	0.541	0.92
69_E	72_G	0.541	0.92
121_T	126_V	0.538	0.92
11_V	68_L	0.538	0.92
33_E	55_I	0.535	0.92
14_I	56_E	0.534	0.92
33_E	40_V	0.534	0.92
111_K	115_F	0.534	0.92
20_F	25_L	0.531	0.91
112_K	130_E	0.526	0.91
16_D	122_N	0.526	0.91
113_I	117_S	0.525	0.91
67_F	73_Q	0.525	0.91
8_G	76_H	0.524	0.91
103_F	106_Q	0.521	0.91
112_K	132_K	0.516	0.90
110_G	114_A	0.516	0.90
44_F	108_A	0.516	0.90
106_Q	112_K	0.516	0.90
99_L	116_I	0.515	0.90
104_P	109_N	0.514	0.90
92_L	95_Q	0.512	0.90
21_Y	54_L	0.511	0.90
68_L	74_G	0.506	0.89
113_I	116_I	0.500	0.89

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
3isqA	2	1	99.9	0.357	Contact Map
1jc4A	2	0.95	99.8	0.386	Contact Map
1sqdA	2	0.9643	99.8	0.387	Contact Map
1sp8A	2	0.9786	99.8	0.393	Contact Map
2r5vA	1	0.9643	99.8	0.396	Contact Map
3hdpA	2	0.9071	99.8	0.398	Contact Map
3gm5A	2	0.9071	99.8	0.4	Contact Map
3oa4A	2	0.9786	99.8	0.407	Contact Map
1ss4A	4	0.9214	99.8	0.414	Contact Map
1t47A	2	1	99.8	0.416	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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