Q9HNK2 - HALSA - GREMLIN Contacts

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Q9HNK2 - Uncharacterized protein

UniProt:	Q9HNK2	Sequences: MSERRDRIRAAVPARISALASRARFGKFVSVGAVGAVVDVTTLLVLTEAAGVWAAAANVASIEAAILVMFAVNDRWTFADAGSGSVGRRLVRSHVVRAGGSTLQYALFVGVFYGVTVDATVFGVDCWLIAVKGGAIAVAMLVNYVFESLFTWHVQE	Download Alignment We filter this alignment to remove sites that have many gaps before running GREMLIN. Date: 2015_01
Length:	156 (125)
Sequences:	1605 (1188)
Seq/√Len:	106.2

BACSU - YNGA
HALSA - Q9HNK2 Q9HQ53
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
147_E	151_T	3.418	1.00
35_G	69_M	2.958	1.00
67_L	90_L	2.836	1.00
34_V	68_V	2.587	1.00
135_A	139_A	2.453	1.00
42_T	64_A	2.414	1.00
68_V	72_V	2.406	1.00
24_R	148_S	2.363	1.00
43_L	61_S	2.358	1.00
39_D	58_N	2.272	1.00
58_N	132_K	2.252	1.00
27_K	76_W	2.235	1.00
74_D	89_R	2.230	1.00
39_D	61_S	2.004	1.00
74_D	152_W	1.989	1.00
63_E	94_H	1.881	1.00
46_L	60_A	1.875	1.00
110_G	114_G	1.721	1.00
23_A	27_K	1.687	1.00
69_M	97_R	1.648	1.00
58_N	108_F	1.647	1.00
73_N	77_T	1.610	1.00
43_L	128_L	1.591	1.00
40_V	132_K	1.584	1.00
70_F	89_R	1.570	1.00
103_L	142_V	1.564	1.00
98_A	102_T	1.551	1.00
62_I	66_I	1.535	1.00
111_V	131_V	1.508	1.00
24_R	144_Y	1.478	1.00
35_G	68_V	1.477	1.00
103_L	139_A	1.428	1.00
44_L	129_I	1.406	1.00
39_D	104_Q	1.403	1.00
59_V	105_Y	1.391	1.00
100_G	142_V	1.389	1.00
39_D	132_K	1.375	1.00
38_V	68_V	1.368	1.00
92_R	150_F	1.347	1.00
43_L	132_K	1.333	0.99
54_A	112_F	1.300	0.99
46_L	57_A	1.296	0.99
48_E	128_L	1.275	0.99
96_V	146_F	1.274	0.99
62_I	101_S	1.269	0.99
41_T	45_V	1.207	0.99
107_L	135_A	1.203	0.99
144_Y	148_S	1.169	0.99
33_A	37_V	1.169	0.99
31_V	72_V	1.157	0.98
44_L	128_L	1.156	0.98
66_I	94_H	1.150	0.98
132_K	136_I	1.099	0.98
141_L	145_V	1.095	0.98
42_T	46_L	1.093	0.98
58_N	105_Y	1.087	0.98
43_L	108_F	1.071	0.97
133_G	137_A	1.062	0.97
88_R	92_R	1.049	0.97
104_Q	139_A	1.047	0.97
25_F	143_N	1.030	0.97
40_V	136_I	1.026	0.97
21_S	24_R	1.022	0.97
66_I	97_R	1.006	0.96
104_Q	131_V	1.001	0.96
28_F	143_N	0.992	0.96
137_A	141_L	0.992	0.96
90_L	94_H	0.989	0.96
35_G	97_R	0.989	0.96
104_Q	136_I	0.979	0.96
69_M	93_S	0.977	0.96
43_L	47_T	0.973	0.96
29_V	33_A	0.973	0.96
30_S	34_V	0.969	0.95
26_G	30_S	0.961	0.95
78_F	93_S	0.956	0.95
47_T	128_L	0.948	0.95
111_V	134_G	0.948	0.95
107_L	139_A	0.933	0.94
44_L	48_E	0.916	0.94
61_S	132_K	0.916	0.94
91_V	95_V	0.911	0.94
111_V	130_A	0.911	0.94
93_S	97_R	0.889	0.93
54_A	108_F	0.887	0.93
70_F	86_V	0.868	0.92
71_A	75_R	0.864	0.92
97_R	147_E	0.861	0.92
24_R	80_D	0.854	0.91
78_F	149_L	0.847	0.91
102_T	106_A	0.844	0.91
55_A	105_Y	0.827	0.90
36_A	69_M	0.825	0.90
29_V	140_M	0.810	0.89
126_C	130_A	0.807	0.89
145_V	149_L	0.800	0.88
146_F	151_T	0.797	0.88
22_R	26_G	0.796	0.88
70_F	151_T	0.787	0.88
54_A	113_Y	0.786	0.88
108_F	132_K	0.783	0.87
39_D	43_L	0.781	0.87
100_G	103_L	0.778	0.87
39_D	65_A	0.773	0.87
45_V	50_A	0.760	0.86
36_A	39_D	0.758	0.86
62_I	65_A	0.752	0.85
53_W	57_A	0.739	0.84
36_A	40_V	0.730	0.83
28_F	65_A	0.704	0.81
45_V	49_A	0.703	0.81
98_A	109_V	0.702	0.81
102_T	107_L	0.699	0.81
63_E	67_L	0.689	0.80
126_C	129_I	0.687	0.79
67_L	94_H	0.687	0.79
105_Y	108_F	0.683	0.79
36_A	70_F	0.680	0.79
142_V	152_W	0.675	0.78
56_A	91_V	0.674	0.78
35_G	136_I	0.673	0.78
70_F	74_D	0.671	0.78
107_L	138_V	0.671	0.78
107_L	111_V	0.670	0.78
150_F	153_H	0.663	0.77
30_S	64_A	0.658	0.77
146_F	150_F	0.654	0.76
34_V	72_V	0.652	0.76
94_H	152_W	0.644	0.75
30_S	76_W	0.643	0.75
142_V	146_F	0.631	0.73
146_F	149_L	0.629	0.73
78_F	144_Y	0.627	0.73
89_R	152_W	0.623	0.73
35_G	77_T	0.622	0.72
35_G	147_E	0.621	0.72
58_N	69_M	0.613	0.71
62_I	144_Y	0.610	0.71
34_V	37_V	0.607	0.71
35_G	72_V	0.607	0.71
52_V	60_A	0.600	0.70
85_S	88_R	0.598	0.69
41_T	49_A	0.597	0.69
62_I	97_R	0.597	0.69
92_R	147_E	0.593	0.69
97_R	151_T	0.582	0.67
43_L	104_Q	0.578	0.67
55_A	113_Y	0.575	0.66
63_E	152_W	0.572	0.66
108_F	112_F	0.571	0.66
46_L	50_A	0.564	0.65
30_S	87_G	0.559	0.64
132_K	135_A	0.556	0.64
129_I	134_G	0.554	0.64
47_T	54_A	0.552	0.63
74_D	94_H	0.549	0.63
35_G	38_V	0.547	0.63
31_V	34_V	0.546	0.63
55_A	59_V	0.545	0.62
71_A	91_V	0.542	0.62
62_I	143_N	0.538	0.61
140_M	145_V	0.538	0.61
101_S	104_Q	0.538	0.61
66_I	90_L	0.533	0.61
45_V	48_E	0.532	0.61
44_L	106_A	0.531	0.60
102_T	105_Y	0.530	0.60
93_S	101_S	0.529	0.60
70_F	96_V	0.527	0.60
60_A	64_A	0.526	0.60
72_V	147_E	0.524	0.59
47_T	61_S	0.524	0.59
57_A	114_G	0.523	0.59
78_F	148_S	0.522	0.59
86_V	90_L	0.520	0.59
22_R	29_V	0.520	0.59
124_V	134_G	0.519	0.59
50_A	56_A	0.519	0.59
51_G	125_D	0.517	0.58
23_A	99_G	0.515	0.58
127_W	130_A	0.511	0.57
70_F	83_S	0.510	0.57
104_Q	143_N	0.509	0.57
35_G	73_N	0.505	0.57
45_V	63_E	0.501	0.56
37_V	137_A	0.501	0.56
92_R	96_V	0.500	0.56
34_V	38_V	0.500	0.56

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
1rh5B	1	0.25	11.5	0.937	Contact Map
4lz6A	1	0.8718	8.7	0.94	Contact Map
3mp7B	1	0.2628	8	0.941	Contact Map
2b2hA	3	0.7628	6.8	0.943	Contact Map
1u7gA	3	0.7372	6.2	0.944	Contact Map
4il3A	1	0.9295	5.9	0.944	Contact Map
3v2yA	1	0.5385	4.8	0.947	Contact Map
4humA	1	0.891	4.5	0.948	Contact Map
3ogkQ	1	0.0321	4.2	0.948	Contact Map
1m56D	1	0.2564	3.7	0.949	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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