Q9HQ53 - HALSA - GREMLIN Contacts

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Q9HQ53 - Uncharacterized protein

UniProt:	Q9HQ53	Sequences: MIRRLLRRANSGPTATRLRRFAAVGVVAAGAQMALLWVFVDAVEVAYIPSAVAAIEATIVLTYVLNNAWTFQAIRNSGRVEYAVGLVKTNVVRGTAIPIQLGVLFALVEWYSLPYLLSNAVGILVSGGYRFVLDLRWTWSTSAN	Download Alignment We filter this alignment to remove sites that have many gaps before running GREMLIN. Date: 2015_01
Length:	144 (125)
Sequences:	1810 (1369)
Seq/√Len:	122.5

BACSU - YNGA YWCD
HALSA - Q9HQ53 Q9HNK2
SULSO - Q97ZX3

GREMLIN Results:

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

Residue pairs sorted by coevolution strength:

i	j	Sco	Prob
134_D	138_T	3.366	1.00
28_A	62_T	3.108	1.00
35_L	57_A	2.780	1.00
60_V	86_L	2.718	1.00
122_G	126_S	2.538	1.00
61_L	65_L	2.531	1.00
27_V	61_L	2.514	1.00
17_R	135_L	2.392	1.00
36_L	54_A	2.315	1.00
67_N	85_G	2.210	1.00
32_Q	51_A	2.150	1.00
51_A	119_N	2.085	1.00
20_R	69_W	2.024	1.00
16_T	20_R	1.911	1.00
67_N	139_W	1.893	1.00
36_L	115_Y	1.875	1.00
32_Q	54_A	1.805	1.00
51_A	104_L	1.795	1.00
106_A	110_W	1.765	1.00
56_E	90_N	1.755	1.00
66_N	70_T	1.739	1.00
39_F	53_A	1.709	1.00
32_Q	100_Q	1.685	1.00
107_L	118_S	1.594	1.00
17_R	131_F	1.589	1.00
94_G	98_P	1.582	1.00
62_T	93_R	1.532	1.00
55_I	59_I	1.507	1.00
92_V	133_L	1.483	1.00
31_A	61_L	1.482	1.00
33_M	119_N	1.477	1.00
88_K	137_W	1.474	1.00
63_Y	85_G	1.473	1.00
52_V	101_L	1.463	1.00
32_Q	119_N	1.411	1.00
47_Y	108_V	1.387	1.00
55_I	97_I	1.376	1.00
36_L	119_N	1.373	1.00
39_F	50_S	1.365	1.00
96_A	129_Y	1.360	1.00
41_D	115_Y	1.326	1.00
40_V	115_Y	1.295	1.00
37_W	116_L	1.260	1.00
28_A	61_L	1.258	1.00
99_I	129_Y	1.235	0.99
103_V	122_G	1.213	0.99
14_T	17_R	1.194	0.99
131_F	135_L	1.186	0.99
64_V	68_A	1.158	0.99
120_A	124_L	1.156	0.99
99_I	126_S	1.148	0.99
21_F	130_R	1.148	0.99
36_L	40_V	1.133	0.99
124_L	128_G	1.096	0.99
18_L	130_R	1.086	0.99
26_V	30_G	1.081	0.99
33_M	123_I	1.064	0.98
37_W	115_Y	1.062	0.98
47_Y	109_E	1.059	0.98
35_L	39_F	1.056	0.98
59_I	93_R	1.049	0.98
51_A	101_L	1.049	0.98
24_V	65_L	1.046	0.98
21_F	24_V	1.029	0.98
22_A	26_V	1.016	0.98
29_A	32_Q	0.976	0.97
86_L	90_N	0.973	0.97
59_I	90_N	0.964	0.97
87_V	91_V	0.956	0.97
93_R	134_D	0.926	0.96
37_W	41_D	0.925	0.96
34_A	38_V	0.919	0.96
62_T	89_T	0.917	0.96
78_G	83_A	0.905	0.96
28_A	93_R	0.886	0.95
100_Q	118_S	0.882	0.95
119_N	123_I	0.882	0.95
28_A	123_I	0.882	0.95
48_I	101_L	0.874	0.95
100_Q	126_S	0.872	0.95
36_L	104_L	0.870	0.94
100_Q	123_I	0.870	0.94
98_P	102_G	0.864	0.94
18_L	22_A	0.862	0.94
19_R	23_A	0.855	0.94
60_V	90_N	0.852	0.94
104_L	119_N	0.842	0.93
84_V	88_K	0.842	0.93
71_F	89_T	0.828	0.93
14_T	131_F	0.805	0.92
71_F	131_F	0.804	0.92
128_G	132_V	0.802	0.92
107_L	117_L	0.800	0.92
63_Y	82_Y	0.799	0.92
63_Y	67_N	0.787	0.91
89_T	97_I	0.782	0.91
89_T	93_R	0.779	0.91
47_Y	104_L	0.764	0.90
29_A	62_T	0.762	0.90
32_Q	36_L	0.757	0.89
133_L	138_T	0.757	0.89
55_I	93_R	0.748	0.89
38_V	43_V	0.745	0.88
32_Q	58_T	0.739	0.88
132_V	136_R	0.733	0.88
17_R	73_A	0.733	0.88
45_V	50_S	0.724	0.87
38_V	42_A	0.720	0.87
94_G	105_F	0.714	0.86
15_A	19_R	0.714	0.86
51_A	62_T	0.710	0.86
56_E	60_V	0.707	0.86
54_A	119_N	0.707	0.86
39_F	43_V	0.703	0.85
103_V	126_S	0.703	0.85
23_A	69_W	0.702	0.85
88_K	134_D	0.698	0.85
28_A	134_D	0.696	0.85
39_F	45_V	0.688	0.84
27_V	65_L	0.687	0.84
26_V	29_A	0.686	0.84
63_Y	76_N	0.681	0.84
21_F	126_S	0.670	0.83
29_A	127_G	0.670	0.83
59_I	89_T	0.666	0.82
29_A	63_Y	0.665	0.82
43_V	49_P	0.665	0.82
103_V	107_L	0.663	0.82
40_V	47_Y	0.659	0.82
119_N	122_G	0.652	0.81
129_Y	139_W	0.646	0.80
107_L	121_V	0.642	0.80
55_I	130_R	0.640	0.80
37_W	102_G	0.640	0.80
112_S	124_L	0.634	0.79
29_A	33_M	0.631	0.79
24_V	27_V	0.628	0.78
22_A	127_G	0.627	0.78
62_T	66_N	0.624	0.78
71_F	136_R	0.622	0.78
66_N	134_D	0.621	0.78
97_I	104_L	0.618	0.77
34_A	42_A	0.617	0.77
64_V	82_Y	0.611	0.76
23_A	27_V	0.606	0.76
106_A	112_S	0.606	0.76
137_W	140_S	0.603	0.76
40_V	54_A	0.603	0.76
55_I	58_T	0.600	0.75
113_L	118_S	0.598	0.75
52_V	83_A	0.591	0.74
32_Q	62_T	0.589	0.74
114_P	117_L	0.586	0.73
93_R	138_T	0.582	0.73
48_I	52_V	0.582	0.73
33_M	37_W	0.574	0.72
83_A	87_V	0.574	0.72
28_A	70_T	0.562	0.70
101_L	104_L	0.558	0.70
30_G	124_L	0.557	0.70
104_L	108_V	0.555	0.69
106_A	111_Y	0.553	0.69
108_V	118_S	0.551	0.69
129_Y	133_L	0.549	0.69
28_A	65_L	0.544	0.68
55_I	90_N	0.539	0.67
100_Q	104_L	0.536	0.67
27_V	30_G	0.536	0.67
48_I	105_F	0.535	0.67
133_L	137_W	0.534	0.67
65_L	134_D	0.534	0.67
18_L	65_L	0.531	0.66
21_F	127_G	0.530	0.66
85_G	90_N	0.530	0.66
38_V	41_D	0.529	0.66
107_L	113_L	0.527	0.66
28_A	66_N	0.524	0.65
48_I	109_E	0.523	0.65
97_I	101_L	0.519	0.64
14_T	18_L	0.517	0.64
34_A	112_S	0.514	0.64
24_V	70_T	0.514	0.64
40_V	52_V	0.512	0.63
90_N	139_W	0.510	0.63
21_F	134_D	0.508	0.63
56_E	139_W	0.506	0.62
82_Y	86_L	0.501	0.62
96_A	99_I	0.500	0.61

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
4tq3A	1	0.8472	7.7	0.933	Contact Map
4od4A	1	0.7708	3.4	0.943	Contact Map
1rh5B	1	0.2917	2.7	0.946	Contact Map
3ixzA	1	0.9236	2.7	0.946	Contact Map
2zxeA	1	0.9653	2.5	0.947	Contact Map
4ytpD	1	0.375	2.4	0.948	Contact Map
4ysxD	1	0.375	2.4	0.948	Contact Map
3mp7B	1	0.2708	2	0.949	Contact Map
4av3A	2	0.6042	1.8	0.951	Contact Map
3mktA	1	0.9167	1.8	0.951	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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