YJCF - BACSU - GREMLIN Contacts

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YJCF - Uncharacterized N-acetyltransferase YjcF

UniProt:	O31628	Sequences: MKAVIAKNEEQLKDAFYVREEVFVKEQNVPAEEEIDELENESEHIVVYDGEKPVGAGRWRMKDGYGKLERICVLKSHRSAGVGGIIMKALEKAAADGGASGFILNAQTQAVPFYKKHGYRVLSEKEFLDAGIPHLQMMKD	Download Alignment We filter this alignment to remove sites that have many gaps before running GREMLIN. Date: 2015_01
Length:	140 (128)
Sequences:	3244 (2493)
Seq/√Len:	220.4

ECOLI - ELAA YIID
BACSU - YJCF YYBD YYAT YITI
HALSA - Q9HPZ8

GREMLIN Results:

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

Residue pairs sorted by coevolution strength:

i	j	Sco	Prob
91_E	119_Y	3.115	1.00
57_G	90_L	2.986	1.00
111_V	121_V	2.612	1.00
105_N	127_F	2.392	1.00
20_E	34_E	2.151	1.00
89_A	92_K	2.150	1.00
108_T	126_E	2.137	1.00
126_E	133_P	2.075	1.00
18_V	72_C	1.972	1.00
84_G	117_H	1.964	1.00
54_V	77_H	1.802	1.00
60_R	69_E	1.802	1.00
111_V	135_L	1.801	1.00
18_V	74_L	1.791	1.00
14_D	48_Y	1.764	1.00
122_L	136_Q	1.735	1.00
12_L	16_F	1.728	1.00
46_V	53_P	1.713	1.00
87_M	117_H	1.698	1.00
47_V	82_V	1.680	1.00
21_E	74_L	1.637	1.00
68_L	87_M	1.621	1.00
56_A	72_C	1.615	1.00
48_Y	53_P	1.604	1.00
21_E	25_K	1.579	1.00
55_G	73_V	1.564	1.00
47_V	55_G	1.553	1.00
91_E	102_F	1.520	1.00
84_G	116_K	1.507	1.00
115_K	121_V	1.503	1.00
111_V	115_K	1.503	1.00
127_F	136_Q	1.479	1.00
101_G	138_M	1.473	1.00
128_L	131_G	1.458	1.00
122_L	138_M	1.439	1.00
128_L	133_P	1.430	1.00
112_P	115_K	1.410	1.00
84_G	88_K	1.400	1.00
105_N	136_Q	1.359	1.00
29_V	130_A	1.351	1.00
17_Y	21_E	1.318	1.00
52_K	76_S	1.314	1.00
29_V	132_I	1.311	1.00
123_S	136_Q	1.295	1.00
15_A	46_V	1.283	1.00
65_Y	103_I	1.283	1.00
45_I	93_A	1.277	1.00
103_I	136_Q	1.268	1.00
93_A	96_D	1.255	1.00
57_G	71_I	1.246	1.00
16_F	35_I	1.243	1.00
20_E	31_A	1.238	1.00
49_D	77_H	1.238	1.00
105_N	129_D	1.232	1.00
45_I	90_L	1.227	1.00
27_Q	107_Q	1.224	1.00
71_I	87_M	1.224	1.00
43_E	93_A	1.209	1.00
85_I	89_A	1.204	1.00
121_V	135_L	1.192	1.00
21_E	32_E	1.149	1.00
15_A	56_A	1.143	1.00
49_D	54_V	1.142	1.00
20_E	24_V	1.129	1.00
103_I	138_M	1.059	1.00
67_K	103_I	1.052	1.00
20_E	25_K	1.013	1.00
66_G	99_A	1.005	1.00
88_K	92_K	0.991	1.00
20_E	35_I	0.987	1.00
77_H	80_A	0.985	1.00
59_W	94_A	0.984	1.00
24_V	31_A	0.983	1.00
93_A	97_G	0.977	1.00
108_T	111_V	0.971	1.00
14_D	17_Y	0.963	1.00
13_K	16_F	0.942	1.00
92_K	96_D	0.934	1.00
107_Q	134_H	0.930	1.00
60_R	67_K	0.930	1.00
68_L	71_I	0.924	0.99
10_E	14_D	0.919	0.99
38_L	60_R	0.917	0.99
26_E	78_R	0.908	0.99
45_I	57_G	0.904	0.99
55_G	86_I	0.898	0.99
62_K	65_Y	0.894	0.99
94_A	102_F	0.885	0.99
61_M	99_A	0.884	0.99
43_E	97_G	0.876	0.99
37_E	40_N	0.873	0.99
65_Y	101_G	0.864	0.99
110_A	113_F	0.861	0.99
67_K	105_N	0.855	0.99
25_K	30_P	0.854	0.99
89_A	93_A	0.852	0.99
9_E	13_K	0.840	0.99
68_L	90_L	0.828	0.99
85_I	88_K	0.826	0.99
67_K	104_L	0.824	0.99
42_S	60_R	0.816	0.99
83_G	113_F	0.806	0.99
32_E	35_I	0.806	0.99
54_V	82_V	0.806	0.99
57_G	86_I	0.804	0.99
108_T	133_P	0.799	0.99
16_F	20_E	0.783	0.98
106_A	137_M	0.777	0.98
49_D	52_K	0.776	0.98
49_D	80_A	0.773	0.98
52_K	74_L	0.770	0.98
59_W	93_A	0.770	0.98
55_G	82_V	0.763	0.98
88_K	117_H	0.762	0.98
102_F	119_Y	0.751	0.98
48_Y	51_E	0.751	0.98
11_Q	46_V	0.738	0.97
18_V	53_P	0.738	0.97
38_L	62_K	0.737	0.97
74_L	77_H	0.734	0.97
21_E	76_S	0.729	0.97
17_Y	37_E	0.724	0.97
81_G	84_G	0.707	0.97
108_T	135_L	0.705	0.97
10_E	40_N	0.704	0.97
91_E	117_H	0.700	0.97
26_E	75_K	0.689	0.96
47_V	85_I	0.689	0.96
68_L	102_F	0.688	0.96
42_S	61_M	0.676	0.96
82_V	85_I	0.674	0.96
39_E	69_E	0.674	0.96
44_H	56_A	0.673	0.96
111_V	126_E	0.662	0.95
45_I	89_A	0.653	0.95
45_I	59_W	0.653	0.95
11_Q	15_A	0.646	0.95
23_F	26_E	0.645	0.95
80_A	83_G	0.642	0.94
18_V	56_A	0.641	0.94
36_D	58_R	0.635	0.94
30_P	34_E	0.635	0.94
47_V	54_V	0.627	0.94
13_K	35_I	0.620	0.93
129_D	132_I	0.619	0.93
126_E	135_L	0.618	0.93
121_V	126_E	0.617	0.93
68_L	119_Y	0.614	0.93
73_V	82_V	0.612	0.93
29_V	129_D	0.610	0.93
23_F	107_Q	0.609	0.93
20_E	30_P	0.604	0.92
38_L	41_E	0.602	0.92
104_L	114_Y	0.598	0.92
92_K	95_A	0.594	0.92
13_K	37_E	0.586	0.91
115_K	120_R	0.584	0.91
23_F	27_Q	0.579	0.91
24_V	34_E	0.577	0.91
104_L	137_M	0.576	0.91
12_L	39_E	0.574	0.90
86_I	89_A	0.571	0.90
20_E	32_E	0.566	0.90
66_G	97_G	0.563	0.90
94_A	99_A	0.561	0.89
55_G	83_G	0.556	0.89
69_E	107_Q	0.551	0.89
66_G	94_A	0.551	0.89
68_L	104_L	0.548	0.88
14_D	53_P	0.538	0.87
83_G	110_A	0.538	0.87
79_S	84_G	0.537	0.87
61_M	66_G	0.530	0.87
24_V	30_P	0.527	0.86
123_S	126_E	0.524	0.86
36_D	39_E	0.522	0.86
77_H	82_V	0.521	0.86
60_R	66_G	0.521	0.86
37_E	41_E	0.521	0.86
83_G	114_Y	0.519	0.86
13_K	17_Y	0.517	0.85
58_R	70_R	0.517	0.85
96_D	99_A	0.516	0.85
104_L	110_A	0.514	0.85
26_E	107_Q	0.511	0.85
27_Q	134_H	0.509	0.84
30_P	130_A	0.506	0.84
94_A	98_G	0.505	0.84
63_D	67_K	0.504	0.84
31_A	130_A	0.503	0.84
14_D	18_V	0.503	0.84
70_R	107_Q	0.500	0.83

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
2g0bA	4	0.9857	99.9	0.416	Contact Map
1q2yA	1	0.9929	99.9	0.42	Contact Map
3p2hA	1	0.9429	99.9	0.439	Contact Map
1kzfA	1	0.9071	99.9	0.441	Contact Map
1xebA	2	0.9857	99.9	0.451	Contact Map
2jdcA	1	0.9643	99.9	0.456	Contact Map
1ro5A	5	0.9929	99.9	0.459	Contact Map
3efaA	2	0.9929	99.9	0.467	Contact Map
1y9wA	2	0.9857	99.8	0.583	Contact Map
3gy9A	3	0.9429	99.7	0.599	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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