MOLE 2.0

1. show tunnel | cavity 2 | profile | lining residues
   

   Unique lining residues set - all

   73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C, 107 THR C, 200107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C, 106 VAL C, 110 LEU C, 300101 THR C

   Unique lining residues set - sidechains

   75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 107 THR C, 200107 THR C, 106 VAL C, 110 LEU C, 300101 THR C

   Physicochemical properties of lining side-chains

   Charge: 0 (0-0)
   Hydropathy: 1.4
   Hydrophobicity: 0.24
   Polarity: 1.55
   Mutability: 93
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.11	0.45	0.18	-0.36	2.43	79
   2	74 THR C, 75 THR C, 103 PHE C, 100 ILE C	2.3	0.65	1.55	0.4	1.38	87
   3	74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.4	1.88	0.33	-0.26	2.19	79
   4	75 THR C, 103 PHE C, 100 ILE C	2.72	2.22	2.2	0.8	0.71	87
   5	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	2.83	2.71	2.78	1.05	0.57	91
   6	75 THR C, 103 PHE C, 100 ILE C	3.06	3	2.2	0.8	0.71	87
   7	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	3.1	3.87	2.78	1.05	0.57	91
   8	103 PHE C, 100 ILE C, 300100 ILE C	3.11	4.48	3.93	1.66	0.2	85
   9	103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C	3.23	5.72	2.85	1.04	1	85
   10	100 ILE C, 104 GLY C, 107 THR C	3.6	5.79	1.13	0.08	1.72	105
   11	100 ILE C, 104 GLY C, 200107 THR C	3.58	5.97	1.13	0.08	1.72	105
   12	100 ILE C, 104 GLY C, 107 THR C	3.49	6.47	1.13	0.08	1.72	105
   13	103 PHE C, 300100 ILE C, 104 GLY C, 107 THR C	3.28	7.38	1.55	0.4	1.38	87
   14	103 PHE C, 300100 ILE C, 107 THR C	1.41	12	2.2	0.8	0.71	87
   15	300100 ILE C, 107 THR C, 103 PHE C	1.82	12.45	1.13	0.08	1.72	105
   16	300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C	1.83	12.6	0.75	-0.14	2.14	105
   17	107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C	1.78	12.74	-0.48	-0.79	2.95	107
   18	300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C	1.9	13.07	0.75	-0.14	2.14	105
   19	107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C, 106 VAL C	2	13.26	0.46	-0.41	2.39	102
   20	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.85	14.12	0.68	-0.31	2.14	102
   21	107 THR C, 300101 THR C, 106 VAL C	1.83	14.42	1.03	-0.15	1.72	102
   22	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.75	15.16	1.73	0.18	1.33	86
   23	106 VAL C, 110 LEU C, 300101 THR C	1.22	19.41	2.43	0.5	0.64	86

   layer with bottle neck

   layer with local minimum

2. show tunnel | cavity 2 | profile | lining residues
   

   Unique lining residues set - all

   73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C, 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C, 200110 LEU C, 101 THR C

   Unique lining residues set - sidechains

   75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200107 THR C, 200106 VAL C, 200110 LEU C, 101 THR C

   Physicochemical properties of lining side-chains

   Charge: 0 (0-0)
   Hydropathy: 1.6
   Hydrophobicity: 0.3
   Polarity: 1.49
   Mutability: 91
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.11	0.55	0.18	-0.36	2.43	79
   2	74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.34	1.79	0.33	-0.26	2.19	79
   3	75 THR C, 103 PHE C, 100 ILE C	2.7	2.21	2.2	0.8	0.71	87
   4	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	2.84	2.57	2.78	1.05	0.57	91
   5	75 THR C, 103 PHE C, 100 ILE C	3	3.02	2.2	0.8	0.71	87
   6	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	3.12	3.53	2.78	1.05	0.57	91
   7	103 PHE C, 100 ILE C, 300100 ILE C	3.13	4.98	3.93	1.66	0.2	85
   8	103 PHE C, 100 ILE C, 300100 ILE C, 104 GLY C	3.47	5.61	2.85	1.04	1	85
   9	103 PHE C, 100 ILE C, 104 GLY C	3.19	7.04	2.3	0.79	1.29	77
   10	100 ILE C, 104 GLY C, 200107 THR C	1.95	10.03	1.13	0.08	1.72	105
   11	100 ILE C, 104 GLY C, 200107 THR C, 200103 PHE C	1.5	11.2	0.75	-0.14	2.14	105
   12	100 ILE C, 200107 THR C, 200103 PHE C	1.47	12.52	1.13	0.08	1.72	105
   13	100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C	1.91	13.15	0.75	-0.14	2.14	105
   14	100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.96	13.37	0.46	-0.41	2.39	102
   15	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.87	14.09	0.68	-0.31	2.14	102
   16	200107 THR C, 101 THR C, 200106 VAL C	1.83	14.46	1.03	-0.15	1.72	102
   17	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.79	15.12	1.73	0.18	1.33	86
   18	200106 VAL C, 200110 LEU C, 101 THR C	1.21	19.42	2.43	0.5	0.64	86

   layer with bottle neck

   layer with local minimum

3. show tunnel | cavity 2 | profile | lining residues
   

   Unique lining residues set - all

   73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C, 107 THR C, 200107 THR C, 200104 GLY C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C

   Unique lining residues set - sidechains

   75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C, 107 THR C, 200107 THR C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C

   Physicochemical properties of lining side-chains

   Charge: 0 (0-0)
   Hydropathy: 1.8
   Hydrophobicity: 0.46
   Polarity: 1.18
   Mutability: 95
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.11	0.61	0.18	-0.36	2.43	79
   2	74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.38	2.05	0.33	-0.26	2.19	79
   3	75 THR C, 103 PHE C, 100 ILE C	2.82	2.5	2.2	0.8	0.71	87
   4	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	2.99	2.81	2.78	1.05	0.57	91
   5	103 PHE C, 100 ILE C, 300100 ILE C	2.94	3.19	3.93	1.66	0.2	85
   6	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	3.12	5.15	2.78	1.05	0.57	91
   7	75 THR C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C	3.99	6.63	1.38	0.26	1.05	105
   8	100 ILE C, 300100 ILE C, 100075 THR C, 100100 ILE C, 200100 ILE C	4.39	7.01	3.46	1.29	0.44	103
   9	100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C	4.48	7.35	3.46	1.29	0.44	103
   10	100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C	4.65	7.53	2.42	0.78	0.74	104
   11	100 ILE C, 300100 ILE C, 300107 THR C, 107 THR C, 200107 THR C	4.66	7.66	1.38	0.26	1.05	105
   12	100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C	4.68	7.68	2.42	0.78	0.74	104
   13	100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.66	7.74	2.42	0.78	0.74	104
   14	300100 ILE C, 100100 ILE C, 300107 THR C, 107 THR C, 200107 THR C	4.68	7.81	1.38	0.26	1.05	105
   15	100 ILE C, 300100 ILE C, 100100 ILE C, 300107 THR C, 107 THR C	4.63	7.82	2.42	0.78	0.74	104
   16	300100 ILE C, 100100 ILE C, 100107 THR C, 300107 THR C, 107 THR C	4.63	7.95	1.38	0.26	1.05	105
   17	100 ILE C, 200100 ILE C, 100107 THR C, 107 THR C, 200107 THR C	4.69	8.26	1.38	0.26	1.05	105
   18	100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C, 200104 GLY C	4.02	9.34	1.44	0.26	1.39	105
   19	100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C	3.82	9.56	1.98	0.51	1.33	104
   20	100 ILE C, 200100 ILE C, 200104 GLY C, 200103 PHE C	3.57	9.86	2.85	1.04	1	85
   21	200100 ILE C, 200104 GLY C, 200103 PHE C	3.17	11.13	2.3	0.79	1.29	77
   22	200100 ILE C, 100107 THR C, 200104 GLY C	1.68	14.74	1.13	0.08	1.72	105
   23	200100 ILE C, 100107 THR C, 100103 PHE C	1.43	16.45	1.13	0.08	1.72	105
   24	200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C	1.91	17	0.75	-0.14	2.14	105
   25	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.95	17.23	0.46	-0.41	2.39	102
   26	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.9	18	0.68	-0.31	2.14	102
   27	100107 THR C, 200101 THR C, 100106 VAL C	1.83	18.42	1.03	-0.15	1.72	102
   28	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.75	19.23	1.73	0.18	1.33	86
   29	100106 VAL C, 100110 LEU C, 200101 THR C	1.23	23.36	2.43	0.5	0.64	86

   layer with bottle neck

   layer with local minimum

4. show tunnel | cavity 2 | profile | lining residues
   

   Unique lining residues set - all

   73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100100 ILE C, 100075 THR C, 200100 ILE C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C, 100103 PHE C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C, 300110 LEU C, 100101 THR C

   Unique lining residues set - sidechains

   75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100100 ILE C, 100075 THR C, 200100 ILE C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100103 PHE C, 300106 VAL C, 300110 LEU C, 100101 THR C

   Physicochemical properties of lining side-chains

   Charge: 0 (0-0)
   Hydropathy: 1.7
   Hydrophobicity: 0.4
   Polarity: 1.29
   Mutability: 95
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.11	0.56	0.18	-0.36	2.43	79
   2	74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.35	2.03	0.33	-0.26	2.19	79
   3	75 THR C, 103 PHE C, 100 ILE C	2.8	2.46	2.2	0.8	0.71	87
   4	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	2.96	2.72	2.78	1.05	0.57	91
   5	75 THR C, 103 PHE C, 100 ILE C	2.96	2.95	2.2	0.8	0.71	87
   6	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	3	5.38	2.78	1.05	0.57	91
   7	75 THR C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C	4.1	6.15	1.38	0.26	1.05	105
   8	75 THR C, 100 ILE C, 300100 ILE C, 300075 THR C, 100100 ILE C	4.52	6.47	2.42	0.78	0.74	104
   9	200075 THR C, 300075 THR C, 100100 ILE C, 100075 THR C, 200100 ILE C	4.38	6.95	1.38	0.26	1.05	105
   10	75 THR C, 100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C	4.5	7.63	3.46	1.29	0.44	103
   11	100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 107 THR C	4.55	7.98	3.46	1.29	0.44	103
   12	100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.67	8.3	2.42	0.78	0.74	104
   13	100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C, 300107 THR C	4.55	8.64	1.38	0.26	1.05	105
   14	100100 ILE C, 200100 ILE C, 100107 THR C, 300107 THR C, 100104 GLY C	4.13	9.29	1.44	0.26	1.39	105
   15	100100 ILE C, 200100 ILE C, 100107 THR C, 100104 GLY C	3.93	9.53	1.98	0.51	1.33	104
   16	100100 ILE C, 200100 ILE C, 100104 GLY C, 100103 PHE C	3.57	9.96	2.85	1.04	1	85
   17	100100 ILE C, 100104 GLY C, 100103 PHE C	3.14	11.22	2.3	0.79	1.29	77
   18	100100 ILE C, 300107 THR C, 100104 GLY C	1.79	14.47	1.13	0.08	1.72	105
   19	100100 ILE C, 300107 THR C, 100104 GLY C, 300103 PHE C	1.44	15.6	0.75	-0.14	2.14	105
   20	100100 ILE C, 300107 THR C, 300103 PHE C	1.55	16.34	1.13	0.08	1.72	105
   21	100100 ILE C, 300107 THR C, 300103 PHE C, 100101 THR C	1.85	17.11	0.75	-0.14	2.14	105
   22	300107 THR C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C	1.96	17.33	0.46	-0.41	2.39	102
   23	300107 THR C, 300103 PHE C, 100101 THR C, 300106 VAL C	1.91	18.01	0.68	-0.31	2.14	102
   24	300107 THR C, 100101 THR C, 300106 VAL C	1.83	18.41	1.03	-0.15	1.72	102
   25	300107 THR C, 100101 THR C, 300106 VAL C, 300110 LEU C	1.81	19.12	1.73	0.18	1.33	86
   26	300106 VAL C, 300110 LEU C, 100101 THR C	1.21	23.46	2.43	0.5	0.64	86

   layer with bottle neck

   layer with local minimum

5. show tunnel | cavity 2 | profile | lining residues
   

   Unique lining residues set - all

   73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C

   Unique lining residues set - sidechains

   75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C

   Physicochemical properties of lining side-chains

   Charge: 0 (0-0)
   Hydropathy: 0.8
   Hydrophobicity: 0.16
   Polarity: 4.81
   Mutability: 96
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	73 ALA C, 74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.11	0.42	0.18	-0.36	2.43	79
   2	74 THR C, 75 THR C, 103 PHE C, 100 ILE C	2.28	0.61	1.55	0.4	1.38	87
   3	74 THR C, 75 THR C, 100 ILE C, 103 PHE C	2.38	1.86	0.33	-0.26	2.19	79
   4	75 THR C, 103 PHE C, 100 ILE C	2.75	2.48	2.2	0.8	0.71	87
   5	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	2.98	2.68	2.78	1.05	0.57	91
   6	75 THR C, 103 PHE C, 100 ILE C	3.05	2.82	2.2	0.8	0.71	87
   7	103 PHE C, 100 ILE C, 300100 ILE C	2.93	2.92	3.93	1.66	0.2	85
   8	75 THR C, 103 PHE C, 100 ILE C, 300100 ILE C	2.97	5.03	2.78	1.05	0.57	91
   9	75 THR C, 100 ILE C, 300100 ILE C, 200075 THR C, 300075 THR C	3.92	6.25	1.38	0.26	1.05	105
   10	200075 THR C, 300075 THR C, 100075 THR C, 100100 ILE C, 200100 ILE C	4.55	6.59	1.38	0.26	1.05	105
   11	100 ILE C, 300100 ILE C, 100075 THR C, 100100 ILE C, 200100 ILE C	4.42	6.84	3.46	1.29	0.44	103
   12	100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C	4.4	7.51	3.46	1.29	0.44	103
   13	300100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C	4.67	7.91	0.34	-0.25	1.35	106
   14	100 ILE C, 300100 ILE C, 100100 ILE C, 200100 ILE C, 100107 THR C	4.63	8.87	3.46	1.29	0.44	103
   15	300100 ILE C, 100107 THR C, 107 THR C, 200107 THR C, 300107 THR C	4.63	9.54	0.34	-0.25	1.35	106
   16	100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 104 GLY C	4.15	10.29	-0.64	-0.78	2	107
   17	100107 THR C, 107 THR C, 200107 THR C, 300107 THR C	1.45	19.92	-0.7	-0.77	1.66	107
   18	100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 100111 ALA C	2.22	20.79	-0.2	-0.61	1.33	105
   19	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.21	22.19	1.3	-0.14	0.33	101
   20	100107 THR C, 107 THR C, 200107 THR C, 300107 THR C, 300111 ALA C	2.15	24.11	-0.2	-0.61	1.33	105
   21	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.26	25.26	1.3	-0.14	0.33	101
   22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.75	27.64	1.8	0.02	0	100
   23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.2	28.49	2.28	0.24	0.03	99
   24	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.17	29.45	3.72	0.91	0.1	98
   25	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.44	29.76	3.72	0.91	0.1	98
   26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.27	30.18	2.28	0.24	0.03	99
   27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.31	30.95	2.28	0.24	0.03	99
   28	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.33	31.71	3.72	0.91	0.1	98
   29	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.71	39.38	4.2	1.13	0.13	98
   30	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.14	40.99	2.66	0.68	0.81	95
   31	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.91	41.83	-3.5	-1.1	3.53	84
   32	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	42.13	2.66	0.68	0.81	95
   33	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	3	42.23	-1.96	-0.65	2.85	86
   34	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.64	48.67	-3.5	-1.1	3.53	84
   35	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C	3.86	49.83	-3.44	-0.83	13.14	85
   36	200119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C	4.43	49.93	-3.26	-0.01	41.99	89
   37	300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C	4.41	50.15	-3.26	-0.01	41.99	89
   38	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.4	50.24	-3.44	-0.83	13.14	85
   39	100119 GLN C, 200119 GLN C, 124 HIS C, 100124 HIS C, 300124 HIS C	4.41	50.24	-3.32	-0.28	32.37	88

   layer with bottle neck

   layer with local minimum

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You can download all tunnels as PyMol script, PDB file or print the report.

This is an experimental feature.

Merged pores Created by merging tunnels from the selected start point.

No merged pores were found.

Auto pores Computed from pairs of exit points.

1. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100156 THR A, 100041 ASN B, 100155 VAL A, 100154 PRO A, 100113 THR A, 100093 VAL A, 100095 TYR A, 100039 GLN A, 100042 GLY A, 100041 PRO A, 100041 ASN B, 100038 GLN B, 100085 ASN B, 100040 THR B, 100040 THR B, 100165 ASP B, 100103 LYS B, 100010 ILE B

   Unique lining residues set - sidechains

   100156 THR A, 100041 ASN B, 100154 PRO A, 100113 THR A, 100093 VAL A, 100095 TYR A, 100039 GLN A, 100038 GLN B, 100085 ASN B, 100040 THR B, 100165 ASP B, 100103 LYS B, 100010 ILE B

   Physicochemical properties of lining side-chains

   Charge: 0 (1-1)
   Hydropathy: -1.7
   Hydrophobicity: -0.65
   Polarity: 7.41
   Mutability: 89
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100156 THR A, 100041 ASN B	2.78	0.83	-2.1	-0.77	2.52	105
   2	100156 THR A, 100041 ASN B, 100155 VAL A	2.66	2.73	-1.53	-0.78	2.81	105
   3	100156 THR A, 100041 ASN B, 100155 VAL A, 100154 PRO A	2.88	3	-1.55	-0.61	2.5	89
   4	100041 ASN B, 100154 PRO A	2.73	5.06	-2.55	-0.43	2.48	81
   5	100041 ASN B, 100154 PRO A, 100113 THR A	2.88	5.82	-1.93	-0.54	2.21	89
   6	100041 ASN B, 100154 PRO A, 100113 THR A, 100093 VAL A	2.9	6.11	-0.4	-0.13	1.69	91
   7	100041 ASN B, 100113 THR A, 100093 VAL A	2.85	6.9	0	-0.14	1.72	103
   8	100041 ASN B, 100093 VAL A	2.57	8.37	0.35	0.18	1.76	101
   9	100041 ASN B, 100093 VAL A, 100095 TYR A	2.4	10.95	-0.2	0.49	1.71	84
   10	100041 ASN B, 100093 VAL A, 100039 GLN A	2.99	11.27	-0.93	-0.25	2.35	95
   11	100041 ASN B, 100039 GLN A	2.97	12.23	-3.5	-0.94	3.46	94
   12	100041 ASN B, 100039 GLN A, 100042 GLY A	3.24	12.56	-2.47	-0.89	3.43	94
   13	100041 ASN B, 100039 GLN A, 100042 GLY A, 100041 PRO A	3.27	13	-1.95	-0.87	3.42	94
   14	100041 ASN B, 100039 GLN A, 100042 GLY A	3.11	13.51	-2.47	-0.89	3.43	94
   15	100039 GLN A, 100042 GLY A, 100041 ASN B	3.08	14.72	-1.43	-0.9	3.43	84
   16	100039 GLN A, 100041 ASN B, 100038 GLN B	3.11	14.97	-2.47	-1	3.48	84
   17	100039 GLN A, 100042 GLY A, 100041 ASN B, 100038 GLN B	3.14	15.15	-1.95	-0.95	3.46	84
   18	100039 GLN A, 100042 GLY A, 100041 ASN B, 100038 GLN B, 100085 ASN B	3.29	15.83	-2.26	-0.91	3.44	90
   19	100042 GLY A, 100041 ASN B, 100085 ASN B, 100040 THR B	3.29	16.55	-1.18	-0.79	3.38	104
   20	100042 GLY A, 100041 ASN B, 100085 ASN B, 100040 THR B	3.3	16.86	-1.25	-0.79	2.95	105
   21	100042 GLY A, 100085 ASN B, 100040 THR B	3.32	17.42	-1.53	-0.78	2.81	105
   22	100042 GLY A, 100085 ASN B, 100040 THR B, 100165 ASP B	3.29	17.53	-2.03	-0.85	14.53	99
   23	100042 GLY A, 100085 ASN B, 100165 ASP B	3.28	17.58	-2.47	-0.87	18.82	95
   24	100042 GLY A, 100085 ASN B, 100040 THR B, 100165 ASP B	3.29	17.83	-2.03	-0.85	14.53	99
   25	100085 ASN B, 100040 THR B, 100165 ASP B	3.11	18.44	-2.57	-0.86	18.25	99
   26	100042 GLY A, 100085 ASN B, 100165 ASP B	2.7	23.92	-2.47	-0.87	18.82	95
   27	100042 GLY A, 100085 ASN B, 100165 ASP B, 100103 LYS B	3.66	24.72	-2.83	-0.76	26.49	87
   28	100042 GLY A, 100165 ASP B, 100103 LYS B, 100010 ILE B	3.81	24.86	-0.83	-0.11	25.68	87

   pore with bottle neck

   pore with local minimum

2. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

   Unique lining residues set - sidechains

   100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

   Physicochemical properties of lining side-chains

   Charge: -1 (1-2)
   Hydropathy: -1.4
   Hydrophobicity: -0.5
   Polarity: 17.57
   Mutability: 98
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100165 SER A, 100168 VAL A, 100169 LYS B	1.57	0.75	-1.57	-0.67	18.75	72
   2	100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A	1.65	2.05	-1.28	-0.7	14.91	72
   3	100168 VAL A, 100169 LYS B, 100167 GLY A	1.69	2.94	-1.57	-0.67	18.75	72
   4	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.94	3.18	-1.98	-0.44	26.97	81
   5	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.9	3.36	-1.98	-0.44	26.97	81
   6	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.99	3.47	-1.98	-0.44	26.97	81
   7	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.81	3.8	-1.98	-0.44	26.97	81
   8	100168 VAL A, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.73	3.97	-1.88	-0.6	27.02	88
   9	100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.75	4.82	-2.75	-0.5	38.55	83
   10	100169 LYS B, 100167 GLY A, 100167 ASP B	1.63	6.39	-2.6	-0.75	34.19	79
   11	100169 LYS B, 100167 GLY A, 100166 SER A	1.58	8.05	-1.57	-0.67	18.75	72
   12	100169 LYS B, 100167 GLY A, 100166 SER A	1.81	8.24	-1.7	-0.73	18.18	94
   13	100169 LYS B, 100166 SER A	1.85	8.49	-2.35	-0.69	25.59	94
   14	100169 LYS B, 100167 GLY A, 100166 SER A	1.96	11.59	-1.7	-0.73	18.18	94
   15	100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B	3.53	13.1	-2.15	-0.81	26.06	91
   16	100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B	4.28	13.62	-1.28	-0.9	14.53	101
   17	100167 GLY A, 100166 SER A, 100170 ASP B	4.57	14.49	-1.57	-0.94	18.25	101
   18	100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A	5.02	15.37	-0.7	-0.45	14.05	98
   19	100167 GLY A, 100170 ASP B, 100140 MET A	4.2	17.11	-0.67	-0.28	18.17	89
   20	100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B	3.91	18.47	-1.38	-0.4	14.47	94
   21	100170 ASP B, 100140 MET A, 100138 ASN B	4	19.67	-1.7	-0.27	18.17	94
   22	100140 MET A, 100138 ASN B, 100187 THR A	3.52	21.81	-0.77	-0.18	2.16	101
   23	100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B	2.76	23.47	-0.75	-0.33	2.03	102
   24	100140 MET A, 100187 THR A, 100114 THR B	2.61	25.52	0.17	-0.18	1.58	102
   25	100140 MET A, 100114 THR B	2.71	26.28	0.6	0.12	1.55	100
   26	100140 MET A, 100114 THR B, 100138 ASN A	2.94	26.88	-0.77	-0.18	2.16	101
   27	100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A	2.9	27.78	-0.78	-0.38	2.04	105
   28	100140 MET A, 100114 THR B, 100138 ASN A	2.74	28.71	-0.77	-0.18	2.16	101

   pore with bottle neck

   pore with local minimum

3. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100171 PHE A, 100182 LEU A, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

   Unique lining residues set - sidechains

   100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100182 LEU A, 100170 THR A, 100156 THR A, 100168 VAL A, 100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A

   Physicochemical properties of lining side-chains

   Charge: -3 (1-4)
   Hydropathy: -1.3
   Hydrophobicity: -0.55
   Polarity: 11.65
   Mutability: 92
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.29	0.14	-2.03	-0.85	14.53	99
   2	100042 GLY A, 100040 THR B, 100165 ASP B	3.15	1.77	-1.53	-0.87	18.25	96
   3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.14	4.11	-2.03	-0.85	14.53	99
   4	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.66	4.73	-2.25	-0.68	14.51	82
   5	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.68	5.27	-1.78	-0.44	2.48	73
   6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.39	6.58	-1.78	-0.44	2.48	73
   7	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.47	6.97	-2.55	-0.52	14.11	74
   8	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.37	7.77	-2.55	-0.52	14.11	74
   9	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.32	11.33	-2.25	-0.7	14.56	79
   10	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.39	12.5	-1.95	-0.88	15.01	90
   11	100041 ASN B, 100153 GLU A, 100172 PRO A, 100171 PHE A, 100182 LEU A	2.65	12.81	-0.8	-0.47	12.03	78
   12	100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A	2.59	13.77	-0.13	-0.31	2.57	79
   13	100041 ASN B, 100171 PHE A, 100182 LEU A	2.75	14.01	-0.03	-0.14	2.3	79
   14	100041 ASN B, 100182 LEU A, 100170 THR A	2.77	14.18	-0.13	-0.13	1.72	88
   15	100041 ASN B, 100182 LEU A, 100170 THR A, 100155 VAL A	2.61	15.52	-0.2	-0.3	2.14	88
   16	100041 ASN B, 100170 THR A, 100155 VAL A	2.53	19.29	-1.53	-0.78	2.81	105
   17	100041 ASN B, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A	3.28	19.56	-1.14	-0.78	2.69	106
   18	100041 ASN B, 100156 THR A, 100157 VAL A	3.13	19.76	-1.53	-0.78	2.81	105
   19	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.23	19.96	-1.33	-0.78	2.52	106
   20	100041 ASN B, 100170 THR A, 100157 VAL A	3.26	20.08	-1.53	-0.78	2.81	105
   21	100041 ASN B, 100170 THR A, 100155 VAL A	3.17	20.22	-1.53	-0.78	2.81	105
   22	100041 ASN B, 100170 THR A, 100157 VAL A	3.24	20.4	-1.53	-0.78	2.81	105
   23	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.28	20.92	-1.33	-0.78	2.52	106
   24	100041 ASN B, 100170 THR A, 100157 VAL A	3.27	24.13	-1.53	-0.78	2.81	105
   25	100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B	4.22	24.75	-1.25	-0.79	2.95	105
   26	100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A	4.57	24.93	-1.08	-0.79	3.04	105
   27	100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A	4.62	25.1	0.68	-0.31	2.14	102
   28	100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B	4.58	25.23	-1.16	-0.72	12.26	89
   29	100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B	4.55	25.28	-0.13	-0.22	14.1	85
   30	100170 THR A, 100157 VAL A, 100168 VAL A, 100169 LYS B	4.41	25.99	-0.2	-0.21	13.67	92
   31	100157 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A	4.3	26.42	-0.13	-0.22	14.1	85
   32	100168 VAL A, 100169 LYS B, 100165 SER A	1.93	30.95	-0.03	-0.03	17.67	85
   33	100168 VAL A, 100169 LYS B, 100165 SER A	1.43	32.75	-1.57	-0.67	18.75	72
   34	100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A	1.58	34.24	-1.28	-0.7	14.91	72
   35	100168 VAL A, 100169 LYS B, 100167 GLY A	1.75	35.12	-1.57	-0.67	18.75	72
   36	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.9	35.39	-1.98	-0.44	26.97	81
   37	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	2.01	35.51	-1.98	-0.44	26.97	81
   38	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.75	35.87	-1.98	-0.44	26.97	81
   39	100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.79	36.58	-2.75	-0.5	38.55	83
   40	100169 LYS B, 100167 GLY A, 100167 ASP B	1.68	38.22	-2.6	-0.75	34.19	79
   41	100169 LYS B, 100167 GLY A	1.62	39.07	-2.15	-0.61	26.44	72
   42	100169 LYS B, 100167 GLY A, 100166 SER A	1.68	40.06	-1.57	-0.67	18.75	72
   43	100169 LYS B, 100167 GLY A, 100166 SER A	1.82	43.41	-1.7	-0.73	18.18	94
   44	100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B	3.41	44.72	-2.15	-0.81	26.06	91
   45	100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B	4.11	45.82	-1.28	-0.9	14.53	101
   46	100167 GLY A, 100166 SER A, 100170 ASP B	4.71	46.31	-1.57	-0.94	18.25	101
   47	100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A	5	47.38	-0.7	-0.45	14.05	98
   48	100167 GLY A, 100170 ASP B, 100140 MET A	4.34	48.88	-0.67	-0.28	18.17	89
   49	100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B	3.91	50.38	-1.38	-0.4	14.47	94
   50	100170 ASP B, 100140 MET A, 100138 ASN B	4.02	51.72	-1.7	-0.27	18.17	94
   51	100140 MET A, 100138 ASN B, 100187 THR A	3.52	53.72	-0.77	-0.18	2.16	101
   52	100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B	2.81	55.55	-0.75	-0.33	2.03	102
   53	100140 MET A, 100187 THR A, 100114 THR B	2.62	57.88	0.17	-0.18	1.58	102
   54	100140 MET A, 100114 THR B	2.84	58.63	0.6	0.12	1.55	100
   55	100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A	2.97	59.7	-0.78	-0.38	2.04	105
   56	100140 MET A, 100114 THR B, 100138 ASN A	2.75	60.69	-0.77	-0.18	2.16	101

   pore with bottle neck

   pore with local minimum

4. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100113 PRO B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A, 100135 ALA A, 100117 ILE B, 100116 SER B, 100117 ILE B, 100132 GLY A, 100208 SER B, 100209 PHE B, 100119 PRO B, 100210 ASN B, 100133 SER A, 100218 ARG A, 100211 ARG B, 100186 TYR B, 100211 ARG B, 100125 LEU B

   Unique lining residues set - sidechains

   100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100207 LYS B, 100116 SER B, 100135 ALA A, 100117 ILE B, 100209 PHE B, 100119 PRO B, 100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B

   Physicochemical properties of lining side-chains

   Charge: 2 (4-2)
   Hydropathy: -1.1
   Hydrophobicity: -0.41
   Polarity: 12.37
   Mutability: 88
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100165 SER A, 100168 VAL A, 100169 LYS B	1.57	0.7	-1.57	-0.67	18.75	72
   2	100165 SER A, 100168 VAL A, 100169 LYS B, 100167 GLY A	1.64	1.87	-1.28	-0.7	14.91	72
   3	100168 VAL A, 100169 LYS B, 100167 GLY A	1.67	3.08	-1.57	-0.67	18.75	72
   4	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.97	3.23	-1.98	-0.44	26.97	81
   5	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.92	3.37	-1.98	-0.44	26.97	81
   6	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.99	3.48	-1.98	-0.44	26.97	81
   7	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.78	3.81	-1.98	-0.44	26.97	81
   8	100168 VAL A, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.7	3.97	-1.88	-0.6	27.02	88
   9	100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.84	4.78	-2.75	-0.5	38.55	83
   10	100169 LYS B, 100167 GLY A, 100167 ASP B	1.66	6.27	-2.6	-0.75	34.19	79
   11	100169 LYS B, 100167 GLY A	1.58	7.01	-2.15	-0.61	26.44	72
   12	100169 LYS B, 100167 GLY A, 100166 SER A	1.71	7.97	-1.57	-0.67	18.75	72
   13	100169 LYS B, 100167 GLY A, 100166 SER A	1.82	11.69	-1.7	-0.73	18.18	94
   14	100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B	3.61	13.04	-2.15	-0.81	26.06	91
   15	100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B	4.26	13.53	-1.28	-0.9	14.53	101
   16	100167 GLY A, 100166 SER A, 100170 ASP B	4.54	14.4	-1.57	-0.94	18.25	101
   17	100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A	4.98	15.43	-0.7	-0.45	14.05	98
   18	100167 GLY A, 100170 ASP B, 100140 MET A	4.37	16.76	-0.67	-0.28	18.17	89
   19	100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B	3.92	18.42	-1.38	-0.4	14.47	94
   20	100170 ASP B, 100140 MET A, 100138 ASN B	4.03	19.8	-1.7	-0.27	18.17	94
   21	100140 MET A, 100138 ASN B, 100187 THR A	3.54	21.57	-0.77	-0.18	2.16	101
   22	100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B	2.88	23.13	-0.75	-0.33	2.03	102
   23	100140 MET A, 100187 THR A, 100114 THR B	2.65	25.62	0.17	-0.18	1.58	102
   24	100140 MET A, 100114 THR B	2.84	26.35	0.6	0.12	1.55	100
   25	100140 MET A, 100114 THR B, 100138 ASN A	3.06	26.87	-0.77	-0.18	2.16	101
   26	100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A	2.89	27.84	-0.78	-0.38	2.04	105
   27	100140 MET A, 100114 THR B, 100138 ASN A	2.42	30.45	-0.77	-0.18	2.16	101
   28	100114 THR B, 100138 ASN A	2.7	34	-2.1	-0.77	2.52	105
   29	100114 THR B, 100138 ASN A, 100113 PRO B	4.31	34.55	-1.53	-0.78	2.81	105
   30	100114 THR B, 100138 ASN A, 100113 PRO B, 100207 LYS B	4.3	35.21	-2.13	-0.69	14.48	94
   31	100114 THR B, 100138 ASN A, 100207 LYS B	3.18	37.26	-2.7	-0.65	18.18	94
   32	100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A	2.93	38.26	-2.13	-0.69	14.48	94
   33	100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B	2.79	39.58	-1.78	-0.71	12.26	94
   34	100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B	2.71	39.98	-1.35	-0.7	14.48	89
   35	100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B	2.54	40.61	-1.78	-0.71	12.26	94
   36	100114 THR B, 100138 ASN A, 100136 GLN A, 100115 VAL B, 100116 SER B	2.55	40.99	-1.16	-0.82	2.69	109
   37	100114 THR B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A	2.61	42.04	-0.54	-0.83	2.69	112
   38	100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B	2.66	42.71	-1.24	-0.75	11.92	98
   39	100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B	2.56	43.38	-1.38	-0.75	14.48	94
   40	100136 GLN A, 100115 VAL B, 100116 SER B	2.51	43.98	-0.53	-0.86	2.81	117
   41	100136 GLN A, 100115 VAL B, 100116 SER B, 100135 ALA A	2.33	44.84	0.05	-0.64	2.11	108
   42	100115 VAL B, 100116 SER B, 100135 ALA A	2.25	45.99	0.2	-0.58	1.68	108
   43	100116 SER B, 100135 ALA A, 100117 ILE B	1.92	48.79	0.2	-0.58	1.68	108
   44	100135 ALA A, 100116 SER B, 100117 ILE B	1.88	49.78	1.97	0.34	1.17	101
   45	100135 ALA A, 100117 ILE B	1.56	51.49	3.15	0.92	0.07	101
   46	100135 ALA A, 100117 ILE B, 100132 GLY A, 100208 SER B	1.62	52.45	1.38	0.06	1.72	101
   47	100135 ALA A, 100117 ILE B, 100132 GLY A	1.83	52.97	1.97	0.34	1.17	101
   48	100117 ILE B, 100132 GLY A, 100209 PHE B	1.59	54.29	2.3	0.79	1.29	77
   49	100117 ILE B, 100132 GLY A, 100209 PHE B, 100119 PRO B	1.57	54.77	0.1	-0.09	2.17	54
   50	100117 ILE B, 100132 GLY A, 100119 PRO B	1.58	54.93	-0.8	-0.56	2.78	58
   51	100117 ILE B, 100132 GLY A, 100119 PRO B	1.44	55.13	0.83	0.31	1.7	80
   52	100117 ILE B, 100132 GLY A, 100119 PRO B	1.66	55.54	-0.8	-0.56	2.78	58
   53	100132 GLY A, 100209 PHE B, 100119 PRO B	1.15	59.77	0.27	0.15	1.77	54
   54	100132 GLY A, 100209 PHE B, 100119 PRO B, 100210 ASN B	2.06	60.19	0.1	-0.09	2.17	54
   55	100132 GLY A, 100209 PHE B, 100119 PRO B, 100210 ASN B, 100133 SER A	2.2	60.69	0	-0.23	2.41	54
   56	100132 GLY A, 100119 PRO B, 100210 ASN B, 100133 SER A, 100218 ARG A	2.21	61.68	-1.46	-0.58	12.74	70
   57	100119 PRO B, 100210 ASN B, 100218 ARG A	2.05	63.26	-2.17	-0.44	18.99	70
   58	100209 PHE B, 100119 PRO B, 100210 ASN B, 100218 ARG A	2.04	63.76	-0.93	0.01	14.33	64
   59	100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B	2.01	64.39	-1.73	-0.53	15.09	70
   60	100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B, 100186 TYR B	1.97	64.74	-1.64	-0.2	12.39	63
   61	100119 PRO B, 100218 ARG A, 100211 ARG B, 100186 TYR B	1.9	66.44	-1.95	-0.05	14.64	63
   62	100218 ARG A, 100186 TYR B, 100211 ARG B	1.91	68.04	-3.43	0.09	35.2	72
   63	100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B	2.41	68.04	-1.63	0.35	26.44	67

   pore with bottle neck

   pore with local minimum

5. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100182 LEU A, 100171 PHE A, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A, 100169 HIS A, 100167 ASP B, 100166 SER A, 100166 SER A, 100170 ASP B, 100169 LYS B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100113 PRO B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A, 100135 ALA A, 100117 ILE B, 100116 SER B, 100117 ILE B, 100208 SER B, 100132 GLY A, 100209 PHE B, 100119 PRO B, 100133 SER A, 100210 ASN B, 100218 ARG A, 100211 ARG B, 100186 TYR B, 100211 ARG B, 100125 LEU B

   Unique lining residues set - sidechains

   100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100182 LEU A, 100170 THR A, 100156 THR A, 100168 VAL A, 100169 LYS B, 100169 HIS A, 100167 ASP B, 100166 SER A, 100170 ASP B, 100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B, 100138 ASN A, 100139 SER A, 100207 LYS B, 100116 SER B, 100135 ALA A, 100117 ILE B, 100209 PHE B, 100119 PRO B, 100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B

   Physicochemical properties of lining side-chains

   Charge: 0 (4-4)
   Hydropathy: -1.1
   Hydrophobicity: -0.45
   Polarity: 10.87
   Mutability: 87
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.3	0.12	-2.03	-0.85	14.53	99
   2	100042 GLY A, 100040 THR B, 100165 ASP B	3.17	2.12	-1.53	-0.87	18.25	96
   3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.21	3.92	-2.03	-0.85	14.53	99
   4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.65	4.21	-1.94	-0.69	11.94	88
   5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.68	4.76	-2.25	-0.68	14.51	82
   6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.67	5.29	-1.78	-0.44	2.48	73
   7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.42	6.55	-1.78	-0.44	2.48	73
   8	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.48	7.26	-2.55	-0.52	14.11	74
   9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.44	7.66	-2.55	-0.52	14.11	74
   10	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.3	11.67	-2.25	-0.7	14.56	79
   11	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.54	12.25	-1.95	-0.88	15.01	90
   12	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100182 LEU A	2.72	12.61	-0.8	-0.47	12.03	78
   13	100041 ASN B, 100153 GLU A, 100172 PRO A, 100182 LEU A, 100171 PHE A	2.73	12.83	-0.8	-0.47	12.03	78
   14	100041 ASN B, 100172 PRO A, 100182 LEU A, 100171 PHE A	2.61	13.74	-0.13	-0.31	2.57	79
   15	100041 ASN B, 100182 LEU A, 100171 PHE A	2.77	13.97	-0.03	-0.14	2.3	79
   16	100041 ASN B, 100182 LEU A, 100170 THR A	2.77	14.15	-0.13	-0.13	1.72	88
   17	100041 ASN B, 100182 LEU A, 100170 THR A, 100155 VAL A	2.53	15.95	-0.2	-0.3	2.14	88
   18	100041 ASN B, 100170 THR A, 100155 VAL A	2.45	19.41	-1.53	-0.78	2.81	105
   19	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.25	19.6	-1.33	-0.78	2.52	106
   20	100041 ASN B, 100156 THR A, 100157 VAL A	3.27	19.83	-1.53	-0.78	2.81	105
   21	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.2	20.02	-1.33	-0.78	2.52	106
   22	100041 ASN B, 100170 THR A, 100157 VAL A	3.17	20.14	-1.53	-0.78	2.81	105
   23	100041 ASN B, 100170 THR A, 100155 VAL A	3.17	20.35	-1.53	-0.78	2.81	105
   24	100041 ASN B, 100170 THR A, 100157 VAL A	3.26	20.51	-1.53	-0.78	2.81	105
   25	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.27	21.04	-1.33	-0.78	2.52	106
   26	100041 ASN B, 100170 THR A, 100157 VAL A	3.26	24.14	-1.53	-0.78	2.81	105
   27	100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B	4.16	24.95	-1.25	-0.79	2.95	105
   28	100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A	4.6	25.18	0.68	-0.31	2.14	102
   29	100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B	4.56	25.31	-1.16	-0.72	12.26	89
   30	100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B	4.53	25.36	-0.13	-0.22	14.1	85
   31	100170 THR A, 100157 VAL A, 100168 VAL A, 100169 LYS B	4.46	26.07	-0.2	-0.21	13.67	92
   32	100157 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A	4.27	26.48	-0.13	-0.22	14.1	85
   33	100168 VAL A, 100169 LYS B, 100165 SER A	2.21	30.78	-0.03	-0.03	17.67	85
   34	100168 VAL A, 100169 LYS B, 100165 SER A	1.43	32.78	-1.57	-0.67	18.75	72
   35	100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A	1.55	33.97	-1.28	-0.7	14.91	72
   36	100168 VAL A, 100169 LYS B, 100167 GLY A	1.76	34.96	-1.57	-0.67	18.75	72
   37	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.9	35.23	-1.98	-0.44	26.97	81
   38	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.91	35.44	-1.98	-0.44	26.97	81
   39	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.96	35.57	-1.98	-0.44	26.97	81
   40	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.88	35.92	-1.98	-0.44	26.97	81
   41	100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.7	36.53	-2.75	-0.5	38.55	83
   42	100169 LYS B, 100167 GLY A, 100167 ASP B	1.64	38.03	-2.6	-0.75	34.19	79
   43	100169 LYS B, 100167 GLY A	1.7	38.86	-2.15	-0.61	26.44	72
   44	100169 LYS B, 100167 GLY A, 100166 SER A	1.81	40.02	-1.57	-0.67	18.75	72
   45	100169 LYS B, 100167 GLY A, 100166 SER A	1.84	43.56	-1.7	-0.73	18.18	94
   46	100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B	3.49	45.2	-2.15	-0.81	26.06	91
   47	100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B	4.35	45.74	-1.28	-0.9	14.53	101
   48	100167 GLY A, 100166 SER A, 100170 ASP B	4.66	46.59	-1.57	-0.94	18.25	101
   49	100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A	5	47.51	-0.7	-0.45	14.05	98
   50	100167 GLY A, 100170 ASP B, 100140 MET A	4.27	48.98	-0.67	-0.28	18.17	89
   51	100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B	3.99	50.4	-1.38	-0.4	14.47	94
   52	100170 ASP B, 100140 MET A, 100138 ASN B	4.06	51.93	-1.7	-0.27	18.17	94
   53	100140 MET A, 100138 ASN B, 100187 THR A	3.56	53.54	-0.77	-0.18	2.16	101
   54	100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B	2.92	55.24	-0.75	-0.33	2.03	102
   55	100140 MET A, 100187 THR A, 100114 THR B	2.63	57.21	0.17	-0.18	1.58	102
   56	100140 MET A, 100114 THR B	2.73	58.76	0.6	0.12	1.55	100
   57	100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A	3.02	59.85	-0.78	-0.38	2.04	105
   58	100140 MET A, 100114 THR B, 100138 ASN A	2.25	62.78	-0.77	-0.18	2.16	101
   59	100114 THR B, 100138 ASN A	2.64	66.35	-2.1	-0.77	2.52	105
   60	100114 THR B, 100138 ASN A, 100113 PRO B, 100207 LYS B	4.42	66.93	-2.13	-0.69	14.48	94
   61	100114 THR B, 100138 ASN A, 100207 LYS B	3.51	69.02	-2.7	-0.65	18.18	94
   62	100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A	2.7	70.97	-2.13	-0.69	14.48	94
   63	100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B	2.71	71.65	-1.78	-0.71	12.26	94
   64	100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B	2.66	72.15	-1.35	-0.7	14.48	89
   65	100114 THR B, 100138 ASN A, 100207 LYS B, 100136 GLN A, 100115 VAL B	2.56	72.49	-1.78	-0.71	12.26	94
   66	100114 THR B, 100138 ASN A, 100136 GLN A, 100115 VAL B, 100116 SER B	2.52	72.88	-1.16	-0.82	2.69	109
   67	100114 THR B, 100136 GLN A, 100115 VAL B, 100116 SER B, 100140 MET A	2.58	73.96	-0.54	-0.83	2.69	112
   68	100114 THR B, 100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B	2.73	74.68	-1.24	-0.75	11.92	98
   69	100207 LYS B, 100136 GLN A, 100115 VAL B, 100116 SER B	2.72	75.41	-1.38	-0.75	14.48	94
   70	100136 GLN A, 100115 VAL B, 100116 SER B	2.66	76.06	-0.53	-0.86	2.81	117
   71	100136 GLN A, 100115 VAL B, 100116 SER B, 100135 ALA A	2.29	76.92	0.05	-0.64	2.11	108
   72	100115 VAL B, 100116 SER B, 100135 ALA A	2.25	78.02	0.2	-0.58	1.68	108
   73	100116 SER B, 100135 ALA A, 100117 ILE B	2.03	80.83	0.2	-0.58	1.68	108
   74	100135 ALA A, 100116 SER B, 100117 ILE B	1.9	81.91	1.97	0.34	1.17	101
   75	100135 ALA A, 100117 ILE B	1.64	83.15	3.15	0.92	0.07	101
   76	100135 ALA A, 100117 ILE B, 100208 SER B	1.57	83.77	1.97	0.34	1.17	101
   77	100135 ALA A, 100117 ILE B, 100208 SER B, 100132 GLY A	1.59	84.3	1.38	0.06	1.72	101
   78	100135 ALA A, 100117 ILE B, 100132 GLY A	1.69	84.95	1.97	0.34	1.17	101
   79	100117 ILE B, 100208 SER B, 100132 GLY A	1.85	85.17	1.23	0.07	2.3	103
   80	100117 ILE B, 100132 GLY A, 100209 PHE B	1.59	86.38	2.3	0.79	1.29	77
   81	100117 ILE B, 100132 GLY A, 100209 PHE B, 100119 PRO B	1.6	86.89	0.1	-0.09	2.17	54
   82	100117 ILE B, 100132 GLY A, 100119 PRO B	1.64	87.03	-0.8	-0.56	2.78	58
   83	100117 ILE B, 100132 GLY A, 100119 PRO B	1.41	87.43	0.83	0.31	1.7	80
   84	100117 ILE B, 100132 GLY A, 100209 PHE B, 100119 PRO B	1.22	88.15	0.1	-0.09	2.17	54
   85	100132 GLY A, 100209 PHE B, 100119 PRO B	1.1	91.89	0.27	0.15	1.77	54
   86	100132 GLY A, 100209 PHE B, 100119 PRO B, 100133 SER A, 100210 ASN B	2.22	92.63	0	-0.23	2.41	54
   87	100132 GLY A, 100119 PRO B, 100133 SER A, 100210 ASN B, 100218 ARG A	2.2	93.74	-1.46	-0.58	12.74	70
   88	100119 PRO B, 100210 ASN B, 100218 ARG A	2.05	95.25	-2.17	-0.44	18.99	70
   89	100209 PHE B, 100119 PRO B, 100210 ASN B, 100218 ARG A	2.04	95.79	-0.93	0.01	14.33	64
   90	100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B	2.03	96.45	-1.73	-0.53	15.09	70
   91	100119 PRO B, 100210 ASN B, 100218 ARG A, 100211 ARG B, 100186 TYR B	1.98	96.63	-1.64	-0.2	12.39	63
   92	100119 PRO B, 100218 ARG A, 100211 ARG B, 100186 TYR B	1.86	98.33	-1.95	-0.05	14.64	63
   93	100218 ARG A, 100186 TYR B, 100211 ARG B	2	100.05	-3.43	0.09	35.2	72
   94	100218 ARG A, 100186 TYR B, 100211 ARG B, 100125 LEU B	2.41	100.05	-1.63	0.35	26.44	67

   pore with bottle neck

   pore with local minimum

6. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C

   Unique lining residues set - sidechains

   100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C,

   Physicochemical properties of lining side-chains

   Charge: 4 (8-4)
   Hydropathy: -1.5
   Hydrophobicity: -0.4
   Polarity: 15.01
   Mutability: 85
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.27	-1.33	-0.78	2.52	106
   2	100157 VAL A, 100170 THR A, 100041 ASN B	3.24	0.44	-1.53	-0.78	2.81	105
   3	100170 THR A, 100041 ASN B, 100155 VAL A	3.16	0.68	-1.53	-0.78	2.81	105
   4	100157 VAL A, 100170 THR A, 100041 ASN B	3.17	0.83	-1.53	-0.78	2.81	105
   5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.19	0.97	-1.33	-0.78	2.52	106
   6	100156 THR A, 100157 VAL A, 100041 ASN B	3.24	1.57	-1.53	-0.78	2.81	105
   7	100170 THR A, 100041 ASN B, 100155 VAL A	2.43	5.59	-1.53	-0.78	2.81	105
   8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.48	6.65	-0.2	-0.3	2.14	88
   9	100170 THR A, 100041 ASN B, 100182 LEU A	2.76	6.98	-0.13	-0.13	1.72	88
   10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.75	7.15	-0.03	-0.14	2.3	79
   11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.6	7.91	-0.13	-0.31	2.57	79
   12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.6	8.65	-0.8	-0.47	12.03	78
   13	100041 ASN B, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.57	9.12	-1.64	-0.86	12.68	90
   14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.51	9.66	-1.95	-0.88	15.01	90
   15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.38	12.73	-2.25	-0.7	14.56	79
   16	100041 ASN B, 100153 GLU A, 100172 PRO A	3.08	13.37	-2.87	-0.67	18.29	79
   17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.34	13.86	-2.55	-0.52	14.11	74
   18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.44	14.41	-2.55	-0.52	14.11	74
   19	100153 GLU A, 100172 PRO A, 100041 PRO A	3.45	14.72	-2.23	-0.44	17.69	64
   20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.32	16.8	-1.78	-0.53	14.11	64
   21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.28	19.02	-1.7	-0.23	14.12	61
   22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.62	20.92	-1.1	0.07	2.19	54
   23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.34	21.41	0.13	0.34	1.68	54
   24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.38	22.04	0.3	0.72	1.11	54
   25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.44	22.59	0.13	0.34	1.68	54
   26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.22	27.17	0.3	0.72	1.11	54
   27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.15	27.74	-0.06	0.08	1.67	69
   28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.09	28.07	0.02	0.3	1.25	69
   29	100180 TYR A, 100091 SER A, 100088 SER A	4.05	28.21	-0.97	-0.28	1.65	94
   30	100091 SER A, 100088 SER A	4.06	28.28	-0.8	-0.97	1.67	117
   31	100180 TYR A, 100091 SER A, 100088 SER A	4.13	28.58	-0.97	-0.28	1.65	94
   32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.4	28.8	0.23	0.08	1.27	84
   33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.52	29.43	0.02	0.3	1.25	69
   34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.63	29.84	0.15	-0.22	1.26	86
   35	100041 PRO A, 100091 SER A, 100088 SER A	4.64	30.74	-1.07	-0.68	1.64	97
   36	100041 PRO A, 100088 SER A	4.76	31.82	-1.2	-0.53	1.63	87
   37	100041 PRO A, 100088 SER A, 100040 ARG A	4.59	34.04	-2.3	-0.49	18.42	86
   38	100041 PRO A, 100088 SER A, 100040 ARG A	2.76	36.57	-2.17	-0.44	18.99	70
   39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.6	36.88	-1.73	-0.53	15.09	70
   40	100088 SER A, 100040 ARG A, 100091 SER A	2.32	38.39	-1.77	-0.67	19.59	83
   41	100088 SER A, 100040 ARG A	1.98	39.38	-2.45	-0.61	27.69	83
   42	100040 ARG A	0.38	45.98	-4.5	-0.42	52	83
   43	100040 ARG A, 100043 HIS A	1.49	46.92	-3.85	-0.08	51.8	87
   44	100040 ARG A, 100046 GLU A	2.37	50.01	-4	-0.78	50.95	80
   45	100040 ARG A, 100046 GLU A, 100064 ILE A	4.71	50.63	-1.17	0.08	34.01	87
   46	100040 ARG A, 100046 GLU A, 300018 ARG B	4.01	52.55	-4.17	-0.66	51.3	81
   47	100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B	3.47	56.45	-2	-0.04	38.51	86
   48	100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A	3.56	59.51	-0.98	-0.14	26.35	87
   49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.4	60.25	0.2	-0.04	17.8	90
   50	100046 GLU A, 100064 ILE A, 100063 LYS A	2.98	65.05	-0.97	0.09	33.18	84
   51	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.41	65.4	-0.93	-0.18	25.3	92
   52	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.59	65.72	-1.1	-0.35	25.3	80
   53	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.8	69.38	0.23	0.35	24.92	76
   54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.44	70.32	-1	-0.3	25.73	67
   55	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.15	71	-1.5	-0.4	21.26	76
   56	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.98	71.37	-2.4	-0.78	21.56	90
   57	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.91	71.7	-2.03	-0.87	14.58	96
   58	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.03	71.89	-2.4	-0.78	21.56	90
   59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4.06	72.69	-0.94	-0.32	11.61	84
   60	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.94	73.06	-0.3	-0.21	13.67	77
   61	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.79	73.47	-1.08	-0.2	13.67	84
   62	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.43	75.29	-1.08	-0.27	25.25	79
   63	100063 LYS A, 100003 LEU B, 100001 ASP B	3.48	76.95	-1.2	-0.1	33.11	70
   64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.87	78.14	-1.08	-0.27	25.25	79
   65	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.18	78.32	-1.56	-0.42	30.14	81
   66	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.01	79.09	-0.98	-0.43	25.3	83
   67	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.96	79.23	-0.2	-0.37	13.72	82
   68	100003 LEU B, 300070 ASP B, 100001 ASP B	3	81.47	-0.03	-0.23	17.74	70
   69	100003 LEU B, 300070 ASP B	2.14	84.37	0.15	0.05	24.92	70
   70	100003 LEU B, 300070 ASP B, 100026 SER B	2.11	87.09	-0.17	-0.29	17.17	85
   71	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.57	88.69	-1.25	-0.32	25.88	85
   72	300070 ASP B, 100026 SER B, 300024 ARG B	3.2	90.47	-2.93	-0.81	34.46	95
   73	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	91.64	-2.8	-0.75	35.03	84
   74	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.76	93.1	-2.28	-0.76	26.69	92
   75	300024 ARG B, 100026 SER B, 300069 THR B	4.32	94.53	-1.87	-0.66	19.01	95
   76	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.87	95.55	-1.5	-0.7	15.11	95
   77	100026 SER B, 300069 THR B, 300026 SER B	4.42	98.34	-0.5	-0.79	2.81	107
   78	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.43	99.22	-0.48	-0.79	2.95	107
   79	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.51	101.31	-0.46	-0.79	3.04	107
   80	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.17	101.59	-1.28	-0.92	2.99	100
   81	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.16	104.44	-1.35	-0.91	2.56	102
   82	100026 SER B, 100027 GLN B, 300028 SER B	5.16	105.07	-1.57	-0.96	2.86	100
   83	300027 GLN B, 100027 GLN B, 300028 SER B	5.61	105.68	-1.57	-0.96	2.86	100
   84	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	6.04	106.63	-2.05	-0.99	3.03	95
   85	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.18	107.77	-2.05	-0.99	3.03	95
   86	100027 GLN B, 300028 SER B, 100028 SER B	4.99	111.19	-1.7	-1.01	2.29	106
   87	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.78	111.67	-2.4	-0.87	14.72	100
   88	100027 GLN B, 100028 SER B, 100093 ARG B	4.84	112.05	-2.93	-0.83	19.07	94
   89	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.64	112.93	-2.4	-0.87	14.72	100
   90	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.33	113.56	-2.3	-0.82	15.15	94
   91	100027 GLN B, 300028 SER B, 100093 ARG B	2.42	117.86	-2.93	-0.83	19.07	94
   92	300028 SER B, 100093 ARG B	2.76	118.55	-2.65	-0.7	26.84	100
   93	300028 SER B, 100093 ARG B, 100082 TYR C	3.08	120.21	-2.2	-0.09	18.43	83
   94	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.18	123.43	-2.78	-0.18	26.82	83
   95	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.1	123.81	-2.3	-0.3	22.13	83
   96	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.35	124.74	-2.22	-0.27	22.47	72
   97	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.87	124.97	-1.58	0.04	12.4	61
   98	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.77	125.3	-2.4	0.12	22.12	66
   99	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.36	126.13	-2.4	0.12	22.12	66
   100	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.69	127.77	-1.58	0.04	12.4	61
   101	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.25	128.7	-1.88	0.25	14.65	61
   102	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.26	131.64	-2.43	-0.3	15.13	72
   103	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.43	132.31	-2.2	-0.78	15.57	83
   104	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.73	133.36	-2.43	-0.3	15.13	72
   105	100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C	3.67	133.54	-2.43	-0.3	15.13	72
   106	100093 ARG B, 200082 TYR C, 100058 GLN C	3.63	134.47	-3.1	-0.14	19.05	72
   107	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.75	134.7	-2.43	-0.3	15.13	72
   108	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.68	135.12	-2.53	-0.35	14.7	83
   109	100028 SER B, 100093 ARG B, 100058 GLN C	3.61	135.35	-2.93	-0.83	19.07	94
   110	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.72	136.29	-2.53	-0.35	14.7	83
   111	100028 SER B, 100093 ARG B, 200082 TYR C	3.85	136.63	-2.2	-0.09	18.43	83
   112	100028 SER B, 200093 ARG B, 200082 TYR C	3.27	138.99	-2.2	-0.09	18.43	83
   113	200027 GLN B, 100028 SER B, 200093 ARG B	2.51	140.97	-2.93	-0.83	19.07	94

   pore with bottle neck

   pore with local minimum

7. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A

   Unique lining residues set - sidechains

   100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C, 200057 ARG A

   Physicochemical properties of lining side-chains

   Charge: 3 (10-7)
   Hydropathy: -1.5
   Hydrophobicity: -0.41
   Polarity: 15.94
   Mutability: 87
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.31	0.14	-2.03	-0.85	14.53	99
   2	100042 GLY A, 100040 THR B, 100165 ASP B	3.13	1.97	-1.53	-0.87	18.25	96
   3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.19	4.02	-2.03	-0.85	14.53	99
   4	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.69	4.8	-2.25	-0.68	14.51	82
   5	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.71	4.96	-1.78	-0.44	2.48	73
   6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.67	5.18	-1.78	-0.44	2.48	73
   7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.55	6.48	-1.78	-0.44	2.48	73
   8	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.52	7.03	-2.55	-0.52	14.11	74
   9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.48	7.88	-2.55	-0.52	14.11	74
   10	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.36	9.97	-1.78	-0.53	14.11	64
   11	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.31	12.26	-1.7	-0.23	14.12	61
   12	100041 PRO A, 100173 ALA A, 100180 TYR A	3.49	14.21	-1.1	0.07	2.19	54
   13	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.4	14.6	0.13	0.34	1.68	54
   14	100041 PRO A, 100180 TYR A, 100175 LEU A	4.37	15.38	0.3	0.72	1.11	54
   15	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.44	15.78	0.13	0.34	1.68	54
   16	100041 PRO A, 100180 TYR A, 100175 LEU A	4.32	20.45	0.3	0.72	1.11	54
   17	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.28	21.03	-0.06	0.08	1.67	69
   18	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.22	21.36	0.23	0.08	1.27	84
   19	100180 TYR A, 100091 SER A, 100088 SER A	4.17	21.49	-0.97	-0.28	1.65	94
   20	100091 SER A, 100088 SER A	4.13	21.56	-0.8	-0.97	1.67	117
   21	100180 TYR A, 100091 SER A, 100088 SER A	4.13	21.9	-0.97	-0.28	1.65	94
   22	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.25	22.13	0.23	0.08	1.27	84
   23	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.35	22.45	0.02	0.3	1.25	69
   24	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.47	23.28	0.15	-0.22	1.26	86
   25	100041 PRO A, 100091 SER A, 100088 SER A	4.68	23.75	-1.07	-0.68	1.64	97
   26	100041 PRO A, 100088 SER A	4.79	24.96	-1.2	-0.53	1.63	87
   27	100041 PRO A, 100088 SER A, 100040 ARG A	4.53	27.19	-2.3	-0.49	18.42	86
   28	100041 PRO A, 100088 SER A, 100040 ARG A	2.92	29.84	-2.17	-0.44	18.99	70
   29	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.75	30.16	-1.73	-0.53	15.09	70
   30	100088 SER A, 100040 ARG A, 100091 SER A	2.42	31.09	-1.77	-0.67	19.59	83
   31	100088 SER A, 100040 ARG A	1.88	32.92	-2.45	-0.61	27.69	83
   32	100040 ARG A	0.81	38.56	-4.5	-0.42	52	83
   33	100040 ARG A, 100043 HIS A	1.23	39.67	-3.85	-0.08	51.8	87
   34	100040 ARG A, 100046 GLU A	1.87	43.67	-4	-0.78	50.95	80
   35	100040 ARG A, 100046 GLU A, 300018 ARG B	3.99	46.23	-4.17	-0.66	51.3	81
   36	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.53	49.84	-2	-0.04	38.51	86
   37	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.61	53.09	-0.98	-0.14	26.35	87
   38	100046 GLU A, 100064 ILE A, 100063 LYS A	3.34	53.83	0.2	-0.04	17.8	90
   39	100046 GLU A, 100064 ILE A, 100063 LYS A	2.94	58.17	-0.97	0.09	33.18	84
   40	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.33	58.6	-0.93	-0.18	25.3	92
   41	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.39	59.5	-1.1	-0.35	25.3	80
   42	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.8	62.59	0.23	0.35	24.92	76
   43	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.58	63.57	-1	-0.3	25.73	67
   44	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.39	64.27	-1.5	-0.4	21.26	76
   45	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.26	64.64	-2.4	-0.78	21.56	90
   46	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.17	64.99	-2.03	-0.87	14.58	96
   47	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.16	65.2	-2.4	-0.78	21.56	90
   48	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.9	66.07	-0.94	-0.32	11.61	84
   49	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.77	66.47	-0.3	-0.21	13.67	77
   50	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.65	66.89	-0.3	-0.21	13.67	77
   51	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.47	68.87	-1.08	-0.27	25.25	79
   52	100063 LYS A, 100003 LEU B, 100001 ASP B	3.61	70.52	-1.2	-0.1	33.11	70
   53	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	4.07	71.35	-1.08	-0.27	25.25	79
   54	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.19	71.55	-1.56	-0.42	30.14	81
   55	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.99	72.37	-0.98	-0.43	25.3	83
   56	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.94	72.53	-0.2	-0.37	13.72	82
   57	100003 LEU B, 300070 ASP B, 100001 ASP B	3.05	74.63	-0.03	-0.23	17.74	70
   58	100003 LEU B, 300070 ASP B	2.19	77.63	0.15	0.05	24.92	70
   59	100003 LEU B, 300070 ASP B, 100026 SER B	2.13	80.45	-0.17	-0.29	17.17	85
   60	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.58	82.11	-1.25	-0.32	25.88	85
   61	300070 ASP B, 100026 SER B, 300024 ARG B	3.25	83.72	-2.93	-0.81	34.46	95
   62	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	84.88	-2.8	-0.75	35.03	84
   63	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.76	86.4	-2.28	-0.76	26.69	92
   64	300024 ARG B, 100026 SER B, 300069 THR B	4.29	87.85	-1.87	-0.66	19.01	95
   65	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.89	88.98	-1.5	-0.7	15.11	95
   66	100026 SER B, 300069 THR B, 300026 SER B	4.38	92.12	-0.5	-0.79	2.81	107
   67	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.43	92.98	-0.48	-0.79	2.95	107
   68	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.58	94.52	-0.46	-0.79	3.04	107
   69	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.14	94.67	-0.58	-0.84	2.52	112
   70	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.18	94.81	-1.28	-0.92	2.99	100
   71	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.17	97.85	-1.35	-0.91	2.56	102
   72	100026 SER B, 300028 SER B, 100027 GLN B	5.22	98.49	-1.57	-0.96	2.86	100
   73	300028 SER B, 100027 GLN B, 300027 GLN B	5.51	99.11	-2.6	-1.06	2.91	95
   74	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	5.76	100	-2.05	-0.99	3.03	95
   75	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.16	100.85	-2.05	-0.99	3.03	95
   76	300028 SER B, 100027 GLN B, 100028 SER B	4.96	104.38	-1.7	-1.01	2.29	106
   77	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.78	104.92	-2.4	-0.87	14.72	100
   78	100027 GLN B, 100028 SER B, 100093 ARG B	4.85	105.31	-2.93	-0.83	19.07	94
   79	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.61	106.25	-2.4	-0.87	14.72	100
   80	300028 SER B, 100027 GLN B, 100093 ARG B	2.46	111.41	-2.93	-0.83	19.07	94
   81	300028 SER B, 100093 ARG B	2.96	112.11	-2.65	-0.7	26.84	100
   82	300028 SER B, 100093 ARG B, 100082 TYR C	3.27	113.69	-2.2	-0.09	18.43	83
   83	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.22	116.62	-2.78	-0.18	26.82	83
   84	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.19	117.02	-2.3	-0.3	22.13	83
   85	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.45	117.99	-2.22	-0.27	22.47	72
   86	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.75	118.23	-1.58	0.04	12.4	61
   87	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.45	118.58	-2.4	0.12	22.12	66
   88	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.34	118.93	-2.4	0.12	22.12	66
   89	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.2	119.54	-2.22	-0.27	22.47	72
   90	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.68	121.3	-1.58	0.04	12.4	61
   91	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.22	122.26	-1.88	0.25	14.65	61
   92	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.23	124.75	-2.43	-0.3	15.13	72
   93	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.33	125.44	-2.2	-0.78	15.57	83
   94	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.69	126.77	-2.43	-0.3	15.13	72
   95	100093 ARG B, 200082 TYR C, 100058 GLN C	3.55	127.79	-3.1	-0.14	19.05	72
   96	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.62	128.02	-2.43	-0.3	15.13	72
   97	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.68	128.51	-2.53	-0.35	14.7	83
   98	100028 SER B, 100093 ARG B, 200082 TYR C	3.85	128.54	-2.2	-0.09	18.43	83
   99	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.69	129.19	-2.53	-0.35	14.7	83
   100	100028 SER B, 200082 TYR C, 100058 GLN C	3.25	131.45	-1.87	-0.32	2.27	83
   101	100028 SER B, 200082 TYR C, 100058 GLN C, 100030 GLY B	3.11	132.58	-1.5	-0.44	2.55	83
   102	200082 TYR C, 100058 GLN C, 100030 GLY B, 100092 ASN B	3.11	134.6	-2.18	-0.39	2.98	79
   103	200082 TYR C, 100030 GLY B, 100092 ASN B	3.18	134.93	-1.73	-0.15	2.79	77
   104	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C	3.21	135.58	-0.25	0.17	2.13	84
   105	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C	3.28	135.84	-1.1	0.05	12.1	83
   106	100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B	3.11	137.06	-1.54	-0.38	21.72	92
   107	100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B	2.93	138.27	-1.05	-0.28	26.3	89
   108	100030 GLY B, 200084 VAL C, 100064 ARG C	2.93	138.35	-0.23	-0.03	18.5	90
   109	100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B	2.94	138.47	-0.35	-0.22	14.29	96
   110	100030 GLY B, 100064 ARG C, 100031 THR B	2.98	138.51	-1.87	-0.66	19.01	95
   111	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	2.99	138.56	-2.2	-0.77	27.12	84
   112	100030 GLY B, 100064 ARG C, 100032 ASP B	3	138.64	-2.8	-0.75	35.03	84
   113	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.67	139.41	-1.13	-0.28	25.87	93
   114	200084 VAL C, 100064 ARG C, 100031 THR B	2.42	140.17	-0.33	-0.02	17.93	96
   115	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.23	141.28	-1.13	-0.28	25.87	93
   116	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C	2.2	142.5	-2.28	-0.76	26.69	92
   117	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 201001 DGA C	2.32	143.54	-2.28	-0.76	26.69	92
   118	100064 ARG C, 100031 THR B, 200084 VAL C, 201001 DGA C	2.58	144.02	-1.87	-0.66	19.01	95
   119	100031 THR B, 200084 VAL C, 201001 DGA C	2.7	145.69	-0.55	-0.79	2.52	107
   120	100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C	2.88	146.22	-1.25	-0.88	14.58	92
   121	100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C	2.88	146.65	-1.33	-0.87	14.15	97
   122	100031 THR B, 200084 VAL C, 201001 DGA C, 200085 THR C, 200054 ALA C	2.79	147.33	0	-0.58	1.68	104
   123	100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C	2.89	148.47	-0.78	-0.67	13.31	97
   124	201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C	2.91	150.52	-0.8	-0.63	17.19	94
   125	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C	3.07	151.84	-0.7	-0.67	13.74	94
   126	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A	3.51	152.5	-1.46	-0.62	21.39	91
   127	100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A	3.78	152.96	-2.28	-0.78	26.74	89
   128	100053 GLU B, 200053 GLY C, 200057 ARG A	3.82	153.86	-2.8	-0.79	35.09	80

   pore with bottle neck

   pore with local minimum

8. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 58 GLN C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A

   Unique lining residues set - sidechains

   100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 58 GLN C, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C, 300057 ARG A

   Physicochemical properties of lining side-chains

   Charge: 3 (10-7)
   Hydropathy: -1.6
   Hydrophobicity: -0.41
   Polarity: 16.07
   Mutability: 88
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.31	0.14	-2.03	-0.85	14.53	99
   2	100042 GLY A, 100040 THR B, 100165 ASP B	3.13	2	-1.53	-0.87	18.25	96
   3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.19	4.06	-2.03	-0.85	14.53	99
   4	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.66	4.71	-2.25	-0.68	14.51	82
   5	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.72	5	-1.78	-0.44	2.48	73
   6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.7	5.23	-1.78	-0.44	2.48	73
   7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.58	6.23	-1.78	-0.44	2.48	73
   8	100041 ASN B, 100172 PRO A, 100041 PRO A	3.54	6.56	-2.23	-0.32	2.18	73
   9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.47	7.09	-2.55	-0.52	14.11	74
   10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.44	7.65	-2.55	-0.52	14.11	74
   11	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.42	10.11	-1.78	-0.53	14.11	64
   12	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.38	11.92	-1.7	-0.23	14.12	61
   13	100041 PRO A, 100173 ALA A, 100180 TYR A	3.53	14.32	-1.1	0.07	2.19	54
   14	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.33	14.65	0.13	0.34	1.68	54
   15	100041 PRO A, 100180 TYR A, 100175 LEU A	4.38	15.33	0.3	0.72	1.11	54
   16	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.46	15.64	0.13	0.34	1.68	54
   17	100041 PRO A, 100180 TYR A, 100175 LEU A	4.06	20.16	0.3	0.72	1.11	54
   18	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.14	20.84	-0.06	0.08	1.67	69
   19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.22	21.26	0.02	0.3	1.25	69
   20	100180 TYR A, 100091 SER A, 100088 SER A	4.29	21.45	-0.97	-0.28	1.65	94
   21	100091 SER A, 100088 SER A	4.35	21.52	-0.8	-0.97	1.67	117
   22	100180 TYR A, 100091 SER A, 100088 SER A	4.39	21.82	-0.97	-0.28	1.65	94
   23	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.45	22.04	0.23	0.08	1.27	84
   24	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.47	22.7	0.02	0.3	1.25	69
   25	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.52	23.14	0.15	-0.22	1.26	86
   26	100041 PRO A, 100091 SER A, 100088 SER A	4.57	24.08	-1.07	-0.68	1.64	97
   27	100041 PRO A, 100088 SER A	4.81	25.15	-1.2	-0.53	1.63	87
   28	100041 PRO A, 100088 SER A, 100040 ARG A	4.36	27.71	-2.3	-0.49	18.42	86
   29	100041 PRO A, 100088 SER A, 100040 ARG A	2.93	29.78	-2.17	-0.44	18.99	70
   30	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.77	30.11	-1.73	-0.53	15.09	70
   31	100088 SER A, 100040 ARG A, 100091 SER A	1.41	31.72	-1.77	-0.67	19.59	83
   32	100088 SER A, 100040 ARG A	0.78	32.8	-2.45	-0.61	27.69	83
   33	100040 ARG A	0.01	38.48	-4.5	-0.42	52	83
   34	100040 ARG A, 100043 HIS A	1.47	39.61	-3.85	-0.08	51.8	87
   35	100040 ARG A, 100046 GLU A	2.36	43.66	-4	-0.78	50.95	80
   36	100040 ARG A, 100046 GLU A, 300018 ARG B	4.17	45.7	-4.17	-0.66	51.3	81
   37	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.46	49.34	-2	-0.04	38.51	86
   38	100046 GLU A, 300018 ARG B, 100064 ILE A	3.77	49.91	-1.17	0.08	34.01	87
   39	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.5	53.22	-0.98	-0.14	26.35	87
   40	100046 GLU A, 100064 ILE A, 100063 LYS A	2.89	58.29	-0.97	0.09	33.18	84
   41	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.25	58.66	-0.93	-0.18	25.3	92
   42	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.42	59.01	-1.1	-0.35	25.3	80
   43	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.87	62.91	0.23	0.35	24.92	76
   44	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.58	63.82	-1	-0.3	25.73	67
   45	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.33	64.42	-1.5	-0.4	21.26	76
   46	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.17	64.69	-2.4	-0.78	21.56	90
   47	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.11	65.04	-2.03	-0.87	14.58	96
   48	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.11	65.25	-2.4	-0.78	21.56	90
   49	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.85	66.2	-0.94	-0.32	11.61	84
   50	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.73	66.62	-1.08	-0.2	13.67	84
   51	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.49	68.52	-1.08	-0.27	25.25	79
   52	100063 LYS A, 100003 LEU B, 100001 ASP B	3.55	70.25	-1.2	-0.1	33.11	70
   53	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	4	71.23	-1.08	-0.27	25.25	79
   54	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.21	71.43	-1.56	-0.42	30.14	81
   55	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.95	72.44	-0.98	-0.43	25.3	83
   56	100003 LEU B, 300070 ASP B, 100001 ASP B	3.07	74.5	-0.03	-0.23	17.74	70
   57	100003 LEU B, 300070 ASP B	2.15	77.51	0.15	0.05	24.92	70
   58	100003 LEU B, 300070 ASP B, 100026 SER B	2.07	80.36	-0.17	-0.29	17.17	85
   59	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.66	82.04	-1.25	-0.32	25.88	85
   60	300070 ASP B, 100026 SER B, 300024 ARG B	3.25	83.7	-2.93	-0.81	34.46	95
   61	300070 ASP B, 300024 ARG B, 100026 SER B	3.63	84.87	-2.8	-0.75	35.03	84
   62	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.76	86.4	-2.28	-0.76	26.69	92
   63	300024 ARG B, 100026 SER B, 300069 THR B	4.35	87.85	-1.87	-0.66	19.01	95
   64	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.89	88.61	-1.5	-0.7	15.11	95
   65	100026 SER B, 300069 THR B, 300026 SER B	4.42	91.31	-0.5	-0.79	2.81	107
   66	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.52	92.23	-0.48	-0.79	2.95	107
   67	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.68	94.53	-0.46	-0.79	3.04	107
   68	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.12	94.83	-1.28	-0.92	2.99	100
   69	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.17	98.02	-1.35	-0.91	2.56	102
   70	300027 GLN B, 100027 GLN B, 300028 SER B	5.41	98.67	-1.57	-0.96	2.86	100
   71	100027 GLN B, 300028 SER B, 300027 GLN B	5.87	99.27	-2.6	-1.06	2.91	95
   72	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	6.26	99.75	-2.05	-0.99	3.03	95
   73	100027 GLN B, 300028 SER B, 100028 SER B	6.54	100.07	-1.7	-1.01	2.29	106
   74	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.2	100.99	-2.05	-0.99	3.03	95
   75	100027 GLN B, 300028 SER B, 100028 SER B	4.98	104.5	-1.7	-1.01	2.29	106
   76	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.82	104.84	-2.4	-0.87	14.72	100
   77	100027 GLN B, 100028 SER B, 100093 ARG B	4.87	105.47	-2.93	-0.83	19.07	94
   78	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.81	105.98	-2.4	-0.87	14.72	100
   79	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.43	106.64	-2.3	-0.82	15.15	94
   80	100027 GLN B, 300028 SER B, 100093 ARG B	2.44	111.68	-2.93	-0.83	19.07	94
   81	300028 SER B, 100093 ARG B, 100082 TYR C	3.01	113.36	-2.2	-0.09	18.43	83
   82	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.84	114.08	-2.78	-0.18	26.82	83
   83	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.73	114.96	-2.53	-0.35	14.7	83
   84	300028 SER B, 300093 ARG B, 300058 GLN C	3.63	115.24	-2.93	-0.83	19.07	94
   85	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.64	115.86	-2.53	-0.35	14.7	83
   86	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.66	116.12	-2.43	-0.3	15.13	72
   87	100082 TYR C, 300093 ARG B, 300058 GLN C	3.66	116.98	-3.1	-0.14	19.05	72
   88	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.74	118.19	-2.43	-0.3	15.13	72
   89	300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C	3.36	118.87	-2.2	-0.78	15.57	83
   90	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.18	122.56	-2.43	-0.3	15.13	72
   91	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	5.24	123.48	-1.88	0.25	14.65	61
   92	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	5.64	124.76	-1.58	0.04	12.4	61
   93	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.25	125.17	-2.4	0.12	22.12	66
   94	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.78	125.37	-2.4	0.12	22.12	66
   95	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.85	125.61	-2.4	0.12	22.12	66
   96	300079 GLY C, 79 GLY C, 93 ARG B, 82 TYR C, 200079 GLY C	6.85	125.87	-1.4	-0.34	12.75	66
   97	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.39	126.9	-2.22	-0.27	22.47	72
   98	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.11	127.36	-2.3	-0.3	22.13	83
   99	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	4.61	129.85	-2.78	-0.18	26.82	83
   100	300082 TYR C, 93 ARG B, 28 SER B	4.02	130.99	-2.2	-0.09	18.43	83
   101	300082 TYR C, 93 ARG B, 28 SER B, 58 GLN C	3.7	132.27	-2.53	-0.35	14.7	83
   102	300082 TYR C, 28 SER B, 58 GLN C	3.38	134.58	-1.87	-0.32	2.27	83
   103	300082 TYR C, 28 SER B, 58 GLN C, 30 GLY B	3.15	135.69	-1.5	-0.44	2.55	83
   104	300082 TYR C, 58 GLN C, 30 GLY B, 92 ASN B	3.12	137.43	-2.18	-0.39	2.98	79
   105	300082 TYR C, 30 GLY B, 92 ASN B	3.23	138.1	-1.73	-0.15	2.79	77
   106	300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C	3.32	138.7	-0.25	0.17	2.13	84
   107	300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C	3.26	138.96	-1.1	0.05	12.1	83
   108	30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B	3.05	140.27	-1.54	-0.38	21.72	92
   109	30 GLY B, 300084 VAL C, 64 ARG C, 32 ASP B	2.96	141.28	-1.05	-0.28	26.3	89
   110	30 GLY B, 300084 VAL C, 64 ARG C	2.96	141.38	-0.23	-0.03	18.5	90
   111	30 GLY B, 300084 VAL C, 64 ARG C, 31 THR B	2.96	141.52	-0.35	-0.22	14.29	96
   112	30 GLY B, 64 ARG C, 31 THR B	2.98	141.56	-1.87	-0.66	19.01	95
   113	30 GLY B, 64 ARG C, 32 ASP B, 31 THR B	2.93	141.67	-2.2	-0.77	27.12	84
   114	30 GLY B, 64 ARG C, 32 ASP B, 31 THR B	2.89	141.77	-2.28	-0.76	26.69	92
   115	300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B	2.62	142.68	-1.13	-0.28	25.87	93
   116	300084 VAL C, 64 ARG C, 31 THR B	2.53	143.07	-0.33	-0.02	17.93	96
   117	300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B	2.41	144.75	-1.13	-0.28	25.87	93
   118	64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C	2.44	145.94	-2.28	-0.76	26.69	92
   119	64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C, 301001 DGA C	2.56	146.45	-2.28	-0.76	26.69	92
   120	64 ARG C, 31 THR B, 300084 VAL C, 301001 DGA C	2.62	147.45	-1.87	-0.66	19.01	95
   121	31 THR B, 300084 VAL C, 301001 DGA C	2.67	148.59	-0.55	-0.79	2.52	107
   122	31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B	2.67	149.15	-1.53	-0.9	18.31	92
   123	31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C	2.67	149.61	-1.33	-0.87	14.15	97
   124	31 THR B, 300084 VAL C, 301001 DGA C, 300085 THR C, 300054 ALA C	2.68	150.38	0	-0.58	1.68	104
   125	31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C	2.92	151.47	-0.78	-0.67	13.31	97
   126	301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C	2.92	153.53	-0.8	-0.63	17.19	94
   127	53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C	3.04	154.88	-0.7	-0.67	13.74	94
   128	53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A	3.51	155.56	-1.46	-0.62	21.39	91
   129	53 GLU B, 300085 THR C, 300053 GLY C, 300057 ARG A	3.78	156.02	-2.28	-0.78	26.74	89
   130	53 GLU B, 300053 GLY C, 300057 ARG A	3.83	156.93	-2.8	-0.79	35.09	80

   pore with bottle neck

   pore with local minimum

9. show pore | cavity 1 | profile | lining residues
   

   Unique lining residues set - all

   100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A

   Unique lining residues set - sidechains

   100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C, 200057 ARG A

   Physicochemical properties of lining side-chains

   Charge: 4 (10-6)
   Hydropathy: -1.5
   Hydrophobicity: -0.42
   Polarity: 15.45
   Mutability: 87
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.27	-1.33	-0.78	2.52	106
   2	100157 VAL A, 100170 THR A, 100041 ASN B	3.22	0.45	-1.53	-0.78	2.81	105
   3	100170 THR A, 100041 ASN B, 100155 VAL A	3.19	0.63	-1.53	-0.78	2.81	105
   4	100157 VAL A, 100170 THR A, 100041 ASN B	3.21	0.78	-1.53	-0.78	2.81	105
   5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.24	0.94	-1.33	-0.78	2.52	106
   6	100156 THR A, 100157 VAL A, 100041 ASN B	3.28	1.23	-1.53	-0.78	2.81	105
   7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.31	1.63	-1.33	-0.78	2.52	106
   8	100170 THR A, 100041 ASN B, 100155 VAL A	2.59	5.4	-1.53	-0.78	2.81	105
   9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.51	6.54	-0.2	-0.3	2.14	88
   10	100170 THR A, 100041 ASN B, 100182 LEU A	2.77	6.89	-0.13	-0.13	1.72	88
   11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.24	-0.03	-0.14	2.3	79
   12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.68	7.97	-0.13	-0.31	2.57	79
   13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.51	8.57	-0.8	-0.47	12.03	78
   14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.4	9.08	-0.8	-0.47	12.03	78
   15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.31	9.67	-1.95	-0.88	15.01	90
   16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.28	12.93	-2.25	-0.7	14.56	79
   17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.12	13.27	-2.87	-0.67	18.29	79
   18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.24	13.81	-2.55	-0.52	14.11	74
   19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.41	14.42	-2.55	-0.52	14.11	74
   20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.38	16.64	-1.78	-0.53	14.11	64
   21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.32	19.06	-1.7	-0.23	14.12	61
   22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.62	21.02	-1.1	0.07	2.19	54
   23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.31	21.38	0.13	0.34	1.68	54
   24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.39	22.1	0.3	0.72	1.11	54
   25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.47	22.56	0.13	0.34	1.68	54
   26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.04	26.75	0.3	0.72	1.11	54
   27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A	4	27.49	0.02	0.3	1.25	69
   28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	3.99	27.96	-0.06	0.08	1.67	69
   29	100180 TYR A, 100091 SER A, 100088 SER A	4	28.17	-0.97	-0.28	1.65	94
   30	100091 SER A, 100088 SER A	4.05	28.24	-0.8	-0.97	1.67	117
   31	100180 TYR A, 100091 SER A, 100088 SER A	4.13	28.56	-0.97	-0.28	1.65	94
   32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.33	28.8	0.23	0.08	1.27	84
   33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.44	29.52	0.02	0.3	1.25	69
   34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.62	29.99	0.15	-0.22	1.26	86
   35	100041 PRO A, 100091 SER A, 100088 SER A	4.7	30.48	-1.07	-0.68	1.64	97
   36	100041 PRO A, 100088 SER A	4.79	31.73	-1.2	-0.53	1.63	87
   37	100041 PRO A, 100088 SER A, 100040 ARG A	4.29	34.27	-2.3	-0.49	18.42	86
   38	100041 PRO A, 100088 SER A, 100040 ARG A	3.04	36.48	-2.17	-0.44	18.99	70
   39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.79	36.82	-1.73	-0.53	15.09	70
   40	100088 SER A, 100040 ARG A, 100091 SER A	1.76	37.8	-1.77	-0.67	19.59	83
   41	100088 SER A, 100040 ARG A	1.22	39.77	-2.45	-0.61	27.69	83
   42	100040 ARG A	1.2	45.65	-4.5	-0.42	52	83
   43	100040 ARG A, 100043 HIS A	2.63	46.73	-3.85	-0.08	51.8	87
   44	100040 ARG A, 100043 HIS A, 100046 GLU A	3.14	47.64	-3.73	-0.43	51.17	83
   45	100040 ARG A, 100046 GLU A	3.61	50.11	-4	-0.78	50.95	80
   46	100040 ARG A, 100046 GLU A, 300018 ARG B	3.74	52.86	-4.17	-0.66	51.3	81
   47	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.52	56.19	-2	-0.04	38.51	86
   48	100046 GLU A, 300018 ARG B, 100064 ILE A	3.88	56.79	-1.17	0.08	34.01	87
   49	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.57	59.52	-0.98	-0.14	26.35	87
   50	100046 GLU A, 100064 ILE A, 100063 LYS A	3.23	60.32	0.2	-0.04	17.8	90
   51	100046 GLU A, 100064 ILE A, 100063 LYS A	2.87	64.91	-0.97	0.09	33.18	84
   52	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.2	65.33	-0.93	-0.18	25.3	92
   53	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.32	65.67	-1.1	-0.35	25.3	80
   54	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.74	69.7	0.23	0.35	24.92	76
   55	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.48	70.62	-1	-0.3	25.73	67
   56	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.27	71.19	-1.5	-0.4	21.26	76
   57	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.13	71.42	-2.4	-0.78	21.56	90
   58	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.1	71.59	-2.03	-0.87	14.58	96
   59	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.18	71.8	-2.4	-0.78	21.56	90
   60	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4	72.68	-0.94	-0.32	11.61	84
   61	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.83	73.1	-0.3	-0.21	13.67	77
   62	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.65	73.55	-0.3	-0.21	13.67	77
   63	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.44	75.03	-1.08	-0.27	25.25	79
   64	100063 LYS A, 100003 LEU B, 100001 ASP B	3.49	76.85	-1.2	-0.1	33.11	70
   65	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.78	77.91	-1.08	-0.27	25.25	79
   66	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.05	78.11	-1.56	-0.42	30.14	81
   67	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4	79.04	-0.98	-0.43	25.3	83
   68	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.92	79.2	-0.2	-0.37	13.72	82
   69	100003 LEU B, 300070 ASP B, 100001 ASP B	3.13	81.2	-0.03	-0.23	17.74	70
   70	100003 LEU B, 300070 ASP B	2.18	84.35	0.15	0.05	24.92	70
   71	100003 LEU B, 300070 ASP B, 100026 SER B	2.12	86.83	-0.17	-0.29	17.17	85
   72	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.51	88.6	-1.25	-0.32	25.88	85
   73	300070 ASP B, 100026 SER B, 300024 ARG B	3.17	90.37	-2.93	-0.81	34.46	95
   74	300070 ASP B, 300024 ARG B, 100026 SER B	3.63	91.32	-2.8	-0.75	35.03	84
   75	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.69	93.37	-2.28	-0.76	26.69	92
   76	300024 ARG B, 100026 SER B, 300069 THR B	4.49	94.39	-1.87	-0.66	19.01	95
   77	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.76	95.63	-1.5	-0.7	15.11	95
   78	100026 SER B, 300069 THR B, 300026 SER B	4.31	97.99	-0.5	-0.79	2.81	107
   79	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.4	98.95	-0.48	-0.79	2.95	107
   80	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.6	101.24	-0.46	-0.79	3.04	107
   81	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.19	101.57	-1.28	-0.92	2.99	100
   82	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.16	104.53	-1.35	-0.91	2.56	102
   83	100026 SER B, 100027 GLN B, 300028 SER B	5.22	105.21	-1.57	-0.96	2.86	100
   84	100027 GLN B, 300028 SER B, 300027 GLN B	5.51	105.85	-2.6	-1.06	2.91	95
   85	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	5.76	106.72	-2.05	-0.99	3.03	95
   86	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.17	107.73	-2.05	-0.99	3.03	95
   87	100027 GLN B, 300028 SER B, 100028 SER B	4.89	111.28	-1.7	-1.01	2.29	106
   88	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.82	111.56	-2.4	-0.87	14.72	100
   89	100027 GLN B, 100028 SER B, 100093 ARG B	4.82	111.99	-2.93	-0.83	19.07	94
   90	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.63	112.42	-2.4	-0.87	14.72	100
   91	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.35	113.04	-2.3	-0.82	15.15	94
   92	100027 GLN B, 300028 SER B, 100093 ARG B	2.42	117.76	-2.93	-0.83	19.07	94
   93	300028 SER B, 100093 ARG B	2.79	118.51	-2.65	-0.7	26.84	100
   94	300028 SER B, 100093 ARG B, 100082 TYR C	3.2	120.25	-2.2	-0.09	18.43	83
   95	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.38	123.34	-2.78	-0.18	26.82	83
   96	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.17	123.75	-2.3	-0.3	22.13	83
   97	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.37	124.73	-2.22	-0.27	22.47	72
   98	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.51	124.95	-1.58	0.04	12.4	61
   99	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.49	125.39	-2.4	0.12	22.12	66
   100	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.46	125.93	-2.4	0.12	22.12	66
   101	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.99	127.71	-1.58	0.04	12.4	61
   102	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.47	128.73	-1.88	0.25	14.65	61
   103	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.23	131.41	-2.43	-0.3	15.13	72
   104	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.34	132.14	-2.2	-0.78	15.57	83
   105	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.74	133.3	-2.43	-0.3	15.13	72
   106	100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C	3.69	133.52	-2.43	-0.3	15.13	72
   107	100093 ARG B, 200082 TYR C, 100058 GLN C	3.57	134.35	-3.1	-0.14	19.05	72
   108	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.57	134.61	-2.43	-0.3	15.13	72
   109	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.6	135.14	-2.53	-0.35	14.7	83
   110	100028 SER B, 100093 ARG B, 200082 TYR C	3.77	135.18	-2.2	-0.09	18.43	83
   111	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.75	135.91	-2.53	-0.35	14.7	83
   112	100028 SER B, 200082 TYR C, 100058 GLN C	3.33	138.3	-1.87	-0.32	2.27	83
   113	100028 SER B, 200082 TYR C, 100058 GLN C, 100030 GLY B	3.17	139.1	-1.5	-0.44	2.55	83
   114	200082 TYR C, 100058 GLN C, 100030 GLY B, 100092 ASN B	3.12	141.32	-2.18	-0.39	2.98	79
   115	200082 TYR C, 100030 GLY B, 100092 ASN B	3.25	141.66	-1.73	-0.15	2.79	77
   116	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C	3.31	142.28	-0.25	0.17	2.13	84
   117	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C	3.31	142.56	-1.1	0.05	12.1	83
   118	100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B	3.04	143.97	-1.54	-0.38	21.72	92
   119	100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B	2.94	144.91	-1.05	-0.28	26.3	89
   120	100030 GLY B, 200084 VAL C, 100064 ARG C	2.93	144.98	-0.23	-0.03	18.5	90
   121	100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B	2.93	145.11	-0.35	-0.22	14.29	96
   122	100030 GLY B, 100064 ARG C, 100031 THR B	2.96	145.15	-1.87	-0.66	19.01	95
   123	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	2.99	145.23	-2.2	-0.77	27.12	84
   124	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	3	145.34	-2.28	-0.76	26.69	92
   125	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.78	145.97	-1.13	-0.28	25.87	93
   126	200084 VAL C, 100064 ARG C, 100031 THR B	2.54	146.74	-0.33	-0.02	17.93	96
   127	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.31	147.9	-1.13	-0.28	25.87	93
   128	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C	2.18	149.18	-2.28	-0.76	26.69	92
   129	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 201001 DGA C	2.16	150.26	-2.28	-0.76	26.69	92
   130	100064 ARG C, 100031 THR B, 200084 VAL C, 201001 DGA C	2.24	150.77	-1.87	-0.66	19.01	95
   131	100031 THR B, 200084 VAL C, 201001 DGA C	2.31	151.95	-0.55	-0.79	2.52	107
   132	100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B	2.49	152.54	-1.53	-0.9	18.31	92
   133	100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C	2.58	153.06	-1.25	-0.88	14.58	92
   134	100031 THR B, 200084 VAL C, 201001 DGA C, 100053 GLU B, 200085 THR C	2.66	153.44	-1.33	-0.87	14.15	97
   135	100031 THR B, 200084 VAL C, 201001 DGA C, 200085 THR C, 200054 ALA C	2.74	153.94	0	-0.58	1.68	104
   136	100031 THR B, 201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C	2.96	155.17	-0.78	-0.67	13.31	97
   137	201001 DGA C, 100053 GLU B, 200085 THR C, 200054 ALA C	2.89	156.81	-0.8	-0.63	17.19	94
   138	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C	2.95	158.58	-0.7	-0.67	13.74	94
   139	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A	3.61	159.08	-1.46	-0.62	21.39	91
   140	100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A	3.78	159.54	-2.28	-0.78	26.74	89
   141	100053 GLU B, 200053 GLY C, 200057 ARG A	3.83	160.49	-2.8	-0.79	35.09	80

   pore with bottle neck

   pore with local minimum

10. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 58 GLN C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 58 GLN C, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C, 300057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 4 (10-6)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 15.24
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.28	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.21	0.46	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.18	0.65	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.81	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.21	0.97	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.2	1.34	-1.53	-0.78	2.81	105
    7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	3.16	1.83	-1.14	-0.78	2.69	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.72	5.62	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.64	6.65	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.76	7.02	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.75	7.2	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.66	7.96	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.78	8.48	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.7	8.96	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.57	9.54	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.36	12.89	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.18	13.25	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.34	13.81	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.41	14.41	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100172 PRO A, 100041 PRO A	3.39	14.76	-2.23	-0.44	17.69	64
    21	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.39	16.66	-1.78	-0.53	14.11	64
    22	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.32	19.12	-1.7	-0.23	14.12	61
    23	100173 ALA A, 100041 PRO A, 100180 TYR A	3.7	21.08	-1.1	0.07	2.19	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.47	21.42	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.37	22.03	0.3	0.72	1.11	54
    26	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.32	22.73	0.13	0.34	1.68	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A	4.23	27.1	0.3	0.72	1.11	54
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.52	27.74	-0.06	0.08	1.67	69
    29	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.57	28.09	0.02	0.3	1.25	69
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.57	28.22	-0.97	-0.28	1.65	94
    31	100091 SER A, 100088 SER A	4.53	28.31	-0.8	-0.97	1.67	117
    32	100180 TYR A, 100091 SER A, 100088 SER A	4.47	28.48	-0.97	-0.28	1.65	94
    33	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.39	28.97	0.23	0.08	1.27	84
    34	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.39	29.34	0.02	0.3	1.25	69
    35	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	29.78	0.15	-0.22	1.26	86
    36	100041 PRO A, 100091 SER A, 100088 SER A	4.52	30.78	-1.07	-0.68	1.64	97
    37	100041 PRO A, 100088 SER A	4.82	31.91	-1.2	-0.53	1.63	87
    38	100041 PRO A, 100088 SER A, 100040 ARG A	4.53	34.08	-2.3	-0.49	18.42	86
    39	100041 PRO A, 100088 SER A, 100040 ARG A	3.15	36.4	-2.17	-0.44	18.99	70
    40	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.69	37.07	-1.73	-0.53	15.09	70
    41	100088 SER A, 100040 ARG A, 100091 SER A	2.11	38.42	-1.77	-0.67	19.59	83
    42	100088 SER A, 100040 ARG A	1.79	39.56	-2.45	-0.61	27.69	83
    43	100040 ARG A	0.97	45.52	-4.5	-0.42	52	83
    44	100040 ARG A, 100043 HIS A	1.5	46.65	-3.85	-0.08	51.8	87
    45	100040 ARG A, 100046 GLU A	2.15	50.09	-4	-0.78	50.95	80
    46	100040 ARG A, 100046 GLU A, 100064 ILE A	4.18	50.75	-1.17	0.08	34.01	87
    47	100040 ARG A, 100046 GLU A, 300018 ARG B	3.81	52.89	-4.17	-0.66	51.3	81
    48	100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B	3.57	56.3	-2	-0.04	38.51	86
    49	100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A	3.26	59.72	-0.98	-0.14	26.35	87
    50	100046 GLU A, 100064 ILE A, 100063 LYS A	3.01	60.52	0.2	-0.04	17.8	90
    51	100046 GLU A, 100064 ILE A, 100063 LYS A	2.88	65.1	-0.97	0.09	33.18	84
    52	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	5.17	65.91	-1.1	-0.35	25.3	80
    53	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.74	70.15	0.23	0.35	24.92	76
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	4.24	71.35	-1.5	-0.4	21.26	76
    55	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.13	71.74	-2.03	-0.87	14.58	96
    56	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.2	71.96	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.9	72.96	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.72	73.4	-1.08	-0.2	13.67	84
    59	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.44	75.46	-1.08	-0.27	25.25	79
    60	100063 LYS A, 100003 LEU B, 100001 ASP B	3.54	77.23	-1.2	-0.1	33.11	70
    61	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.84	78.1	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.05	78.31	-1.56	-0.42	30.14	81
    63	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.02	79.07	-0.98	-0.43	25.3	83
    64	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.95	79.23	-0.2	-0.37	13.72	82
    65	100003 LEU B, 300070 ASP B, 100001 ASP B	3.08	81.28	-0.03	-0.23	17.74	70
    66	100003 LEU B, 300070 ASP B	2.12	84.46	0.15	0.05	24.92	70
    67	100003 LEU B, 300070 ASP B, 100026 SER B	2.08	86.98	-0.17	-0.29	17.17	85
    68	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.65	88.76	-1.25	-0.32	25.88	85
    69	300070 ASP B, 100026 SER B, 300024 ARG B	3.3	90.43	-2.93	-0.81	34.46	95
    70	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	91.52	-2.8	-0.75	35.03	84
    71	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.73	93.12	-2.28	-0.76	26.69	92
    72	300024 ARG B, 100026 SER B, 300069 THR B	4.33	94.62	-1.87	-0.66	19.01	95
    73	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.95	95.5	-1.5	-0.7	15.11	95
    74	100026 SER B, 300069 THR B, 300026 SER B	4.48	98.67	-0.5	-0.79	2.81	107
    75	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.48	99.61	-0.48	-0.79	2.95	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.58	101.24	-0.46	-0.79	3.04	107
    77	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.05	101.39	-0.58	-0.84	2.52	112
    78	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.11	101.56	-1.28	-0.92	2.99	100
    79	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.2	104.5	-1.35	-0.91	2.56	102
    80	100026 SER B, 300028 SER B, 100027 GLN B	5.28	105.19	-1.57	-0.96	2.86	100
    81	300028 SER B, 100027 GLN B, 300027 GLN B	5.74	105.84	-2.6	-1.06	2.91	95
    82	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	6.16	106.75	-2.05	-0.99	3.03	95
    83	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.23	107.79	-2.05	-0.99	3.03	95
    84	300028 SER B, 100027 GLN B, 100028 SER B	4.95	111.35	-1.7	-1.01	2.29	106
    85	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.87	111.5	-2.4	-0.87	14.72	100
    86	100027 GLN B, 100028 SER B, 100093 ARG B	4.84	112.11	-2.93	-0.83	19.07	94
    87	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.74	112.61	-2.4	-0.87	14.72	100
    88	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.49	113.29	-2.3	-0.82	15.15	94
    89	300028 SER B, 100027 GLN B, 100093 ARG B	2.47	118.66	-2.93	-0.83	19.07	94
    90	300028 SER B, 100093 ARG B, 100082 TYR C	3.4	120.29	-2.2	-0.09	18.43	83
    91	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.83	120.66	-2.78	-0.18	26.82	83
    92	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.67	121.66	-2.53	-0.35	14.7	83
    93	300028 SER B, 300093 ARG B, 300058 GLN C	3.58	121.96	-2.93	-0.83	19.07	94
    94	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.69	122.64	-2.53	-0.35	14.7	83
    95	100082 TYR C, 300093 ARG B, 300058 GLN C	3.66	123.6	-3.1	-0.14	19.05	72
    96	100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C	3.71	123.79	-2.43	-0.3	15.13	72
    97	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.54	125.22	-2.43	-0.3	15.13	72
    98	300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C	3.31	125.57	-2.2	-0.78	15.57	83
    99	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.16	129.57	-2.43	-0.3	15.13	72
    100	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	5.36	131.21	-1.58	0.04	12.4	61
    101	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.05	131.62	-2.22	-0.27	22.47	72
    102	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.29	131.82	-2.4	0.12	22.12	66
    103	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.62	132	-2.4	0.12	22.12	66
    104	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.71	132.25	-2.4	0.12	22.12	66
    105	79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C	6.73	132.52	-2.22	-0.27	22.47	72
    106	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.38	133.59	-2.22	-0.27	22.47	72
    107	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.13	134.08	-2.3	-0.3	22.13	83
    108	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	4.68	136.72	-2.78	-0.18	26.82	83
    109	300082 TYR C, 93 ARG B, 28 SER B	4.01	137.86	-2.2	-0.09	18.43	83
    110	300082 TYR C, 93 ARG B, 28 SER B, 58 GLN C	3.7	138.89	-2.53	-0.35	14.7	83
    111	300082 TYR C, 28 SER B, 58 GLN C	3.3	141.31	-1.87	-0.32	2.27	83
    112	300082 TYR C, 28 SER B, 58 GLN C, 30 GLY B	3.15	142.21	-1.5	-0.44	2.55	83
    113	300082 TYR C, 58 GLN C, 30 GLY B, 92 ASN B	3.1	144.48	-2.18	-0.39	2.98	79
    114	300082 TYR C, 30 GLY B, 92 ASN B	3.25	144.82	-1.73	-0.15	2.79	77
    115	300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C	3.27	145.43	-0.25	0.17	2.13	84
    116	300082 TYR C, 30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C	3.23	145.72	-1.1	0.05	12.1	83
    117	30 GLY B, 92 ASN B, 300084 VAL C, 64 ARG C, 32 ASP B	3.07	146.83	-1.54	-0.38	21.72	92
    118	30 GLY B, 300084 VAL C, 64 ARG C, 32 ASP B	2.95	148.08	-1.05	-0.28	26.3	89
    119	30 GLY B, 300084 VAL C, 64 ARG C	2.96	148.14	-0.23	-0.03	18.5	90
    120	30 GLY B, 300084 VAL C, 64 ARG C, 31 THR B	2.96	148.23	-0.35	-0.22	14.29	96
    121	30 GLY B, 64 ARG C, 31 THR B	3	148.27	-1.87	-0.66	19.01	95
    122	30 GLY B, 64 ARG C, 32 ASP B, 31 THR B	3	148.34	-2.2	-0.77	27.12	84
    123	30 GLY B, 64 ARG C, 32 ASP B	2.97	148.41	-2.8	-0.75	35.03	84
    124	300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B	2.65	149.25	-1.13	-0.28	25.87	93
    125	300084 VAL C, 64 ARG C, 31 THR B	2.41	150.12	-0.33	-0.02	17.93	96
    126	300084 VAL C, 64 ARG C, 32 ASP B, 31 THR B	2.21	151.36	-1.13	-0.28	25.87	93
    127	64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C	2.15	152.62	-2.28	-0.76	26.69	92
    128	64 ARG C, 32 ASP B, 31 THR B, 300084 VAL C, 301001 DGA C	2.19	153.17	-2.28	-0.76	26.69	92
    129	64 ARG C, 31 THR B, 300084 VAL C, 301001 DGA C	2.26	153.67	-1.87	-0.66	19.01	95
    130	31 THR B, 300084 VAL C, 301001 DGA C	2.36	155.44	-0.55	-0.79	2.52	107
    131	31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C	2.68	156.01	-1.25	-0.88	14.58	92
    132	31 THR B, 300084 VAL C, 301001 DGA C, 53 GLU B, 300085 THR C	2.76	156.46	-1.33	-0.87	14.15	97
    133	31 THR B, 300084 VAL C, 301001 DGA C, 300085 THR C, 300054 ALA C	2.84	157.05	0	-0.58	1.68	104
    134	31 THR B, 301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C	2.94	158.2	-0.78	-0.67	13.31	97
    135	301001 DGA C, 53 GLU B, 300085 THR C, 300054 ALA C	2.87	159.85	-0.8	-0.63	17.19	94
    136	53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C	2.93	161.7	-0.7	-0.67	13.74	94
    137	53 GLU B, 300085 THR C, 300054 ALA C, 300053 GLY C, 300057 ARG A	3.61	162.21	-1.46	-0.62	21.39	91
    138	53 GLU B, 300085 THR C, 300053 GLY C, 300057 ARG A	3.79	162.68	-2.28	-0.78	26.74	89
    139	53 GLU B, 300053 GLY C, 300057 ARG A	3.83	163.63	-2.8	-0.79	35.09	80

    pore with bottle neck

    pore with local minimum

11. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 300082 TYR C, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C, 57 ARG A

    Physicochemical properties of lining side-chains

    Charge: 3 (10-7)
    Hydropathy: -1.6
    Hydrophobicity: -0.38
    Polarity: 16.43
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.31	0.13	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.13	1.87	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.16	3.94	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.62	4.15	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.65	4.74	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.72	5.04	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.71	5.29	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.61	6.27	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A	3.57	6.58	-2.23	-0.32	2.18	73
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.48	7.1	-2.55	-0.52	14.11	74
    11	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.4	7.63	-2.55	-0.52	14.11	74
    12	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.38	9.99	-1.78	-0.53	14.11	64
    13	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.38	12.23	-1.7	-0.23	14.12	61
    14	100041 PRO A, 100173 ALA A, 100180 TYR A	3.7	14.17	-1.1	0.07	2.19	54
    15	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.3	14.68	0.13	0.34	1.68	54
    16	100041 PRO A, 100180 TYR A, 100175 LEU A	4.38	15.32	0.3	0.72	1.11	54
    17	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.48	15.94	0.13	0.34	1.68	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A	4.11	20.63	0.3	0.72	1.11	54
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.07	21.13	-0.06	0.08	1.67	69
    20	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.04	21.4	0.23	0.08	1.27	84
    21	100180 TYR A, 100091 SER A, 100088 SER A	4.04	21.49	-0.97	-0.28	1.65	94
    22	100091 SER A, 100088 SER A	4.07	21.58	-0.8	-0.97	1.67	117
    23	100180 TYR A, 100091 SER A, 100088 SER A	4.12	21.93	-0.97	-0.28	1.65	94
    24	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.3	22.16	0.23	0.08	1.27	84
    25	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.41	22.48	0.02	0.3	1.25	69
    26	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.51	23.3	0.15	-0.22	1.26	86
    27	100041 PRO A, 100091 SER A, 100088 SER A	4.7	23.76	-1.07	-0.68	1.64	97
    28	100041 PRO A, 100088 SER A	4.8	24.94	-1.2	-0.53	1.63	87
    29	100041 PRO A, 100088 SER A, 100040 ARG A	4.19	27.69	-2.3	-0.49	18.42	86
    30	100041 PRO A, 100088 SER A, 100040 ARG A	3.01	29.73	-2.17	-0.44	18.99	70
    31	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.79	30.05	-1.73	-0.53	15.09	70
    32	100088 SER A, 100040 ARG A, 100091 SER A	1.7	31.45	-1.77	-0.67	19.59	83
    33	100088 SER A, 100040 ARG A	1.48	32.37	-2.45	-0.61	27.69	83
    34	100040 ARG A	1.36	39.05	-4.5	-0.42	52	83
    35	100040 ARG A, 100043 HIS A	2.45	40.04	-3.85	-0.08	51.8	87
    36	100040 ARG A, 100043 HIS A, 100046 GLU A	2.91	40.89	-3.73	-0.43	51.17	83
    37	100040 ARG A, 100046 GLU A	3.37	43.84	-4	-0.78	50.95	80
    38	100040 ARG A, 100046 GLU A, 300018 ARG B	3.84	45.79	-4.17	-0.66	51.3	81
    39	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.56	49.78	-2	-0.04	38.51	86
    40	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.26	52.92	-0.98	-0.14	26.35	87
    41	100046 GLU A, 100064 ILE A, 100063 LYS A	3.07	53.66	0.2	-0.04	17.8	90
    42	100046 GLU A, 100064 ILE A, 100063 LYS A	2.95	57.93	-0.97	0.09	33.18	84
    43	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.05	58.45	-0.93	-0.18	25.3	92
    44	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.46	59.17	-1.1	-0.35	25.3	80
    45	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.78	63.05	0.23	0.35	24.92	76
    46	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.38	63.9	-1	-0.3	25.73	67
    47	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.1	64.45	-1.5	-0.4	21.26	76
    48	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.97	64.71	-2.4	-0.78	21.56	90
    49	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.95	65.04	-2.03	-0.87	14.58	96
    50	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.06	65.25	-2.4	-0.78	21.56	90
    51	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.89	66.14	-0.94	-0.32	11.61	84
    52	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.79	66.54	-1.08	-0.2	13.67	84
    53	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.69	66.95	-0.3	-0.21	13.67	77
    54	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.51	68.33	-1.08	-0.27	25.25	79
    55	100063 LYS A, 100003 LEU B, 100001 ASP B	3.54	70.5	-1.2	-0.1	33.11	70
    56	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	4.07	71.33	-1.08	-0.27	25.25	79
    57	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.19	71.52	-1.56	-0.42	30.14	81
    58	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.94	72.46	-0.98	-0.43	25.3	83
    59	100003 LEU B, 300070 ASP B, 100001 ASP B	2.96	74.76	-0.03	-0.23	17.74	70
    60	100003 LEU B, 300070 ASP B	2.08	77.7	0.15	0.05	24.92	70
    61	100003 LEU B, 300070 ASP B, 100026 SER B	2.01	80.45	-0.17	-0.29	17.17	85
    62	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.76	82.07	-1.25	-0.32	25.88	85
    63	300070 ASP B, 100026 SER B, 300024 ARG B	3.39	83.71	-2.93	-0.81	34.46	95
    64	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	84.73	-2.8	-0.75	35.03	84
    65	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.71	86.66	-2.28	-0.76	26.69	92
    66	300024 ARG B, 100026 SER B, 300069 THR B	4.46	87.95	-1.87	-0.66	19.01	95
    67	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	5	88.68	-1.5	-0.7	15.11	95
    68	100026 SER B, 300069 THR B, 300026 SER B	4.33	91.37	-0.5	-0.79	2.81	107
    69	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.32	92.26	-0.48	-0.79	2.95	107
    70	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.44	94.52	-0.46	-0.79	3.04	107
    71	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.19	94.67	-0.58	-0.84	2.52	112
    72	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.21	94.81	-1.28	-0.92	2.99	100
    73	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.17	97.69	-1.35	-0.91	2.56	102
    74	100026 SER B, 300028 SER B, 100027 GLN B	5.19	98.32	-1.57	-0.96	2.86	100
    75	300027 GLN B, 300028 SER B, 100027 GLN B	5.49	98.94	-1.57	-0.96	2.86	100
    76	300028 SER B, 100027 GLN B, 100028 SER B, 300027 GLN B	5.73	99.89	-2.05	-0.99	3.03	95
    77	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.06	101.07	-2.05	-0.99	3.03	95
    78	300028 SER B, 100027 GLN B, 100028 SER B	4.96	104.5	-1.7	-1.01	2.29	106
    79	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.82	104.83	-2.4	-0.87	14.72	100
    80	100027 GLN B, 100028 SER B, 100093 ARG B	4.79	105.38	-2.93	-0.83	19.07	94
    81	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.61	105.79	-2.4	-0.87	14.72	100
    82	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.36	106.37	-2.3	-0.82	15.15	94
    83	300028 SER B, 100027 GLN B, 100093 ARG B	2.43	111.41	-2.93	-0.83	19.07	94
    84	300028 SER B, 100093 ARG B	2.98	112.1	-2.65	-0.7	26.84	100
    85	300028 SER B, 100093 ARG B, 100082 TYR C	3.38	113.65	-2.2	-0.09	18.43	83
    86	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.38	116.51	-2.78	-0.18	26.82	83
    87	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.06	117.28	-2.3	-0.3	22.13	83
    88	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.37	117.88	-2.22	-0.27	22.47	72
    89	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.5	118.12	-2.22	-0.27	22.47	72
    90	93 ARG B, 79 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C	6.56	118.3	-2.22	-0.27	22.47	72
    91	93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C	6.65	118.68	-2.4	0.12	22.12	66
    92	300093 ARG B, 93 ARG B, 79 GLY C, 300082 TYR C, 82 TYR C	6.85	119.13	-2.4	0.12	22.12	66
    93	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.75	121.54	-1.58	0.04	12.4	61
    94	100093 ARG B, 100082 TYR C, 100079 GLY C	5.08	122.44	-2.07	-0.04	19	66
    95	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3	124.8	-2.43	-0.3	15.13	72
    96	100093 ARG B, 100079 GLY C, 100058 GLN C	2.87	125.1	-2.8	-0.77	19.64	83
    97	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	2.88	126.41	-2.2	-0.78	15.57	83
    98	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.7	127.9	-2.43	-0.3	15.13	72
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.6	129.61	-2.2	-0.02	12.43	66
    100	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.45	130.39	-2.4	0.12	22.12	66
    101	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.82	131.52	-2.22	-0.27	22.47	72
    102	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.48	131.97	-2.22	-0.27	22.47	72
    103	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	7.03	132.28	-2.3	-0.3	22.13	83
    104	100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	7.19	132.69	-2.4	0.12	22.12	66
    105	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	7	133.33	-2.4	0.12	22.12	66
    106	100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.91	135.08	-1.58	0.04	12.4	61
    107	200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.18	136	-1.88	0.25	14.65	61
    108	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.24	138.49	-2.43	-0.3	15.13	72
    109	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3.28	139.46	-2.2	-0.78	15.57	83
    110	200093 ARG B, 82 TYR C, 200079 GLY C, 200058 GLN C	3.65	140.46	-2.43	-0.3	15.13	72
    111	200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C	3.66	140.66	-2.43	-0.3	15.13	72
    112	200093 ARG B, 82 TYR C, 200058 GLN C	3.58	141.68	-3.1	-0.14	19.05	72
    113	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.72	142.24	-2.53	-0.35	14.7	83
    114	200028 SER B, 200093 ARG B, 82 TYR C	3.84	142.29	-2.2	-0.09	18.43	83
    115	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.61	143.08	-2.53	-0.35	14.7	83
    116	200028 SER B, 82 TYR C, 200058 GLN C	3.25	145.32	-1.87	-0.32	2.27	83
    117	200028 SER B, 82 TYR C, 200058 GLN C, 200030 GLY B	3.12	146.37	-1.5	-0.44	2.55	83
    118	82 TYR C, 200058 GLN C, 200030 GLY B, 200092 ASN B	3.12	148.29	-2.18	-0.39	2.98	79
    119	82 TYR C, 200030 GLY B, 200092 ASN B	3.19	148.62	-1.73	-0.15	2.79	77
    120	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C	3.2	149.44	-0.25	0.17	2.13	84
    121	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C	3.24	149.7	-1.1	0.05	12.1	83
    122	200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B	3.1	151	-1.54	-0.38	21.72	92
    123	200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B	2.97	151.97	-1.05	-0.28	26.3	89
    124	200030 GLY B, 84 VAL C, 200064 ARG C	2.95	152.13	-0.23	-0.03	18.5	90
    125	200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B	2.95	152.25	-0.35	-0.22	14.29	96
    126	200030 GLY B, 200064 ARG C, 200031 THR B	2.95	152.28	-1.87	-0.66	19.01	95
    127	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	2.91	152.42	-2.2	-0.77	27.12	84
    128	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.89	152.55	-1.13	-0.28	25.87	93
    129	84 VAL C, 200064 ARG C, 200031 THR B	2.86	152.71	-0.33	-0.02	17.93	96
    130	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.77	153.2	-1.13	-0.28	25.87	93
    131	84 VAL C, 200064 ARG C, 200031 THR B	2.66	153.94	-0.33	-0.02	17.93	96
    132	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.52	155.03	-1.13	-0.28	25.87	93
    133	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C	2.39	156.22	-2.28	-0.76	26.69	92
    134	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 1001 DGA C	2.32	157.24	-2.28	-0.76	26.69	92
    135	200064 ARG C, 200031 THR B, 84 VAL C, 1001 DGA C	2.33	157.71	-1.87	-0.66	19.01	95
    136	200031 THR B, 84 VAL C, 1001 DGA C	2.36	159.33	-0.55	-0.79	2.52	107
    137	200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B	2.53	159.86	-1.53	-0.9	18.31	92
    138	200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C	2.58	160.31	-1.33	-0.87	14.15	97
    139	200031 THR B, 84 VAL C, 1001 DGA C, 85 THR C, 54 ALA C	2.64	161.07	0	-0.58	1.68	104
    140	200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C	2.94	162.42	-0.78	-0.67	13.31	97
    141	1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C	2.9	163.96	-0.8	-0.63	17.19	94
    142	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C	2.97	165.65	-0.7	-0.67	13.74	94
    143	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A	3.56	166.29	-1.46	-0.62	21.39	91
    144	200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A	3.79	166.75	-2.28	-0.78	26.74	89
    145	200053 GLU B, 53 GLY C, 57 ARG A	3.83	167.63	-2.8	-0.79	35.09	80

    pore with bottle neck

    pore with local minimum

12. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C, 57 ARG A

    Physicochemical properties of lining side-chains

    Charge: 4 (10-6)
    Hydropathy: -1.6
    Hydrophobicity: -0.4
    Polarity: 15.56
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.29	0.25	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.23	0.44	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.18	0.7	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.86	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.19	1	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.08	1.38	-1.53	-0.78	2.81	105
    7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	3.02	1.86	-1.14	-0.78	2.69	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.77	5.54	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.73	6.57	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.76	6.91	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.74	7.25	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.62	7.95	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.59	8.42	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.56	8.86	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.5	10	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.48	12.7	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.04	13.38	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.43	13.91	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.57	14.51	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.29	16.68	-1.78	-0.53	14.11	64
    21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.28	19.02	-1.7	-0.23	14.12	61
    22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.52	21	-1.1	0.07	2.19	54
    23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.31	21.38	0.13	0.34	1.68	54
    24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.39	22.07	0.3	0.72	1.11	54
    25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.46	22.73	0.13	0.34	1.68	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.08	26.92	0.3	0.72	1.11	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.04	27.6	-0.06	0.08	1.67	69
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.02	28.03	0.02	0.3	1.25	69
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.02	28.21	-0.97	-0.28	1.65	94
    30	100091 SER A, 100088 SER A	4.05	28.28	-0.8	-0.97	1.67	117
    31	100180 TYR A, 100091 SER A, 100088 SER A	4.09	28.6	-0.97	-0.28	1.65	94
    32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.24	28.83	0.23	0.08	1.27	84
    33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.34	29.52	0.02	0.3	1.25	69
    34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.55	29.97	0.15	-0.22	1.26	86
    35	100041 PRO A, 100091 SER A, 100088 SER A	4.66	30.45	-1.07	-0.68	1.64	97
    36	100041 PRO A, 100088 SER A	4.78	31.7	-1.2	-0.53	1.63	87
    37	100041 PRO A, 100088 SER A, 100040 ARG A	4.63	34.03	-2.3	-0.49	18.42	86
    38	100041 PRO A, 100088 SER A, 100040 ARG A	3.03	36.31	-2.17	-0.44	18.99	70
    39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.69	36.99	-1.73	-0.53	15.09	70
    40	100088 SER A, 100040 ARG A, 100091 SER A	1.7	38.06	-1.77	-0.67	19.59	83
    41	100088 SER A, 100040 ARG A	1.11	38.95	-2.45	-0.61	27.69	83
    42	100040 ARG A	-0.01	45.89	-4.5	-0.42	52	83
    43	100040 ARG A, 100043 HIS A	1.63	46.91	-3.85	-0.08	51.8	87
    44	100040 ARG A, 100046 GLU A	2.46	50.17	-4	-0.78	50.95	80
    45	100040 ARG A, 100046 GLU A, 300018 ARG B	4.11	52.84	-4.17	-0.66	51.3	81
    46	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.57	56.59	-2	-0.04	38.51	86
    47	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.12	59.94	-0.98	-0.14	26.35	87
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.01	60.69	0.2	-0.04	17.8	90
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.01	65.09	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.16	65.44	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.44	65.83	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.95	69.84	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.61	70.72	-1	-0.3	25.73	67
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.32	71.25	-1.5	-0.4	21.26	76
    55	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.16	71.48	-2.4	-0.78	21.56	90
    56	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.11	71.63	-2.03	-0.87	14.58	96
    57	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.17	72.06	-2.4	-0.78	21.56	90
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.98	72.67	-0.94	-0.32	11.61	84
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.82	73.08	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.66	73.51	-1.08	-0.2	13.67	84
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.45	75.5	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B	3.55	77.2	-1.2	-0.1	33.11	70
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.83	78.07	-1.08	-0.27	25.25	79
    64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.04	78.27	-1.56	-0.42	30.14	81
    65	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4	79.13	-0.98	-0.43	25.3	83
    66	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.93	79.29	-0.2	-0.37	13.72	82
    67	100003 LEU B, 300070 ASP B, 100001 ASP B	3.09	81.18	-0.03	-0.23	17.74	70
    68	100003 LEU B, 300070 ASP B	2.13	84.23	0.15	0.05	24.92	70
    69	100003 LEU B, 300070 ASP B, 100026 SER B	2.02	87.13	-0.17	-0.29	17.17	85
    70	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.68	88.83	-1.25	-0.32	25.88	85
    71	300070 ASP B, 100026 SER B, 300024 ARG B	3.41	90.44	-2.93	-0.81	34.46	95
    72	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	91.38	-2.8	-0.75	35.03	84
    73	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.72	93.37	-2.28	-0.76	26.69	92
    74	300024 ARG B, 100026 SER B, 300069 THR B	4.39	94.7	-1.87	-0.66	19.01	95
    75	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.77	95.54	-1.5	-0.7	15.11	95
    76	100026 SER B, 300069 THR B, 300026 SER B	4.45	98.59	-0.5	-0.79	2.81	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.66	99.5	-0.48	-0.79	2.95	107
    78	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.82	101.2	-0.46	-0.79	3.04	107
    79	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.16	101.36	-0.58	-0.84	2.52	112
    80	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.16	101.51	-1.28	-0.92	2.99	100
    81	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.16	104.66	-1.35	-0.91	2.56	102
    82	100026 SER B, 300028 SER B, 100027 GLN B	5.24	105.32	-1.57	-0.96	2.86	100
    83	300028 SER B, 100027 GLN B, 300027 GLN B	5.51	105.94	-2.6	-1.06	2.91	95
    84	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	5.76	106.78	-2.05	-0.99	3.03	95
    85	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.14	107.72	-2.05	-0.99	3.03	95
    86	300028 SER B, 100027 GLN B, 100028 SER B	5	111.26	-1.7	-1.01	2.29	106
    87	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.87	111.58	-2.4	-0.87	14.72	100
    88	100027 GLN B, 100028 SER B, 100093 ARG B	4.93	111.94	-2.93	-0.83	19.07	94
    89	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.53	112.77	-2.4	-0.87	14.72	100
    90	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.14	113.44	-2.3	-0.82	15.15	94
    91	300028 SER B, 100027 GLN B, 100093 ARG B	2.53	118.04	-2.93	-0.83	19.07	94
    92	300028 SER B, 100093 ARG B	2.81	118.76	-2.65	-0.7	26.84	100
    93	300028 SER B, 100093 ARG B, 100082 TYR C	3.1	120.39	-2.2	-0.09	18.43	83
    94	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.21	123.39	-2.78	-0.18	26.82	83
    95	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.18	123.8	-2.3	-0.3	22.13	83
    96	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.44	124.75	-2.22	-0.27	22.47	72
    97	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	7.03	124.97	-1.58	0.04	12.4	61
    98	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.96	125.33	-2.4	0.12	22.12	66
    99	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.71	125.75	-2.4	0.12	22.12	66
    100	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.33	126.43	-2.22	-0.27	22.47	72
    101	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.31	128.24	-1.58	0.04	12.4	61
    102	100093 ARG B, 100082 TYR C, 100079 GLY C	4.74	129.18	-2.07	-0.04	19	66
    103	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	2.99	131.58	-2.43	-0.3	15.13	72
    104	100093 ARG B, 100079 GLY C, 100058 GLN C	2.84	131.89	-2.8	-0.77	19.64	83
    105	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	2.86	132.76	-2.2	-0.78	15.57	83
    106	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.39	135.06	-2.43	-0.3	15.13	72
    107	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.8	135.96	-2.2	-0.02	12.43	66
    108	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.26	136.82	-2.4	0.12	22.12	66
    109	100093 ARG B, 100079 GLY C, 200079 GLY C, 200093 ARG B, 200082 TYR C	5.7	138.11	-2.22	-0.27	22.47	72
    110	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.46	138.66	-2.22	-0.27	22.47	72
    111	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	7.03	138.96	-2.3	-0.3	22.13	83
    112	100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	7.17	139.38	-2.4	0.12	22.12	66
    113	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	6.97	140.05	-2.4	0.12	22.12	66
    114	100079 GLY C, 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C	5.9	141.89	-1.58	0.04	12.4	61
    115	82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C	5.17	142.85	-1.88	0.25	14.65	61
    116	200079 GLY C, 200093 ARG B, 200082 TYR C, 200058 GLN C	3.29	145.31	-2.43	-0.3	15.13	72
    117	200079 GLY C, 200093 ARG B, 200058 GLN C, 200080 ASP C	3.41	146.01	-2.2	-0.78	15.57	83
    118	82 TYR C, 200079 GLY C, 200093 ARG B, 200058 GLN C	3.69	147.12	-2.43	-0.3	15.13	72
    119	82 TYR C, 200093 ARG B, 200058 GLN C, 200080 ASP C	3.7	147.33	-2.43	-0.3	15.13	72
    120	82 TYR C, 200093 ARG B, 200058 GLN C	3.56	148.39	-3.1	-0.14	19.05	72
    121	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.58	148.95	-2.53	-0.35	14.7	83
    122	200028 SER B, 82 TYR C, 200093 ARG B	3.76	149	-2.2	-0.09	18.43	83
    123	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.76	149.55	-2.53	-0.35	14.7	83
    124	200028 SER B, 82 TYR C, 200058 GLN C	3.43	151.82	-1.87	-0.32	2.27	83
    125	200028 SER B, 82 TYR C, 200058 GLN C, 200030 GLY B	3.2	153.03	-1.5	-0.44	2.55	83
    126	82 TYR C, 200058 GLN C, 200030 GLY B, 200092 ASN B	3.16	155.15	-2.18	-0.39	2.98	79
    127	82 TYR C, 200030 GLY B, 200092 ASN B	3.18	155.48	-1.73	-0.15	2.79	77
    128	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C	3.2	156.1	-0.25	0.17	2.13	84
    129	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C	3.25	156.36	-1.1	0.05	12.1	83
    130	200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B	3.1	157.7	-1.54	-0.38	21.72	92
    131	200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B	2.98	158.7	-1.05	-0.28	26.3	89
    132	200030 GLY B, 84 VAL C, 200064 ARG C	2.97	158.8	-0.23	-0.03	18.5	90
    133	200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B	2.96	158.93	-0.35	-0.22	14.29	96
    134	200030 GLY B, 200064 ARG C, 200031 THR B	2.97	158.97	-1.87	-0.66	19.01	95
    135	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	2.94	159.03	-2.2	-0.77	27.12	84
    136	200030 GLY B, 200064 ARG C, 200032 ASP B	2.92	159.09	-2.8	-0.75	35.03	84
    137	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	2.88	159.21	-2.28	-0.76	26.69	92
    138	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.67	159.87	-1.13	-0.28	25.87	93
    139	84 VAL C, 200064 ARG C, 200031 THR B	2.46	160.64	-0.33	-0.02	17.93	96
    140	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.3	161.78	-1.13	-0.28	25.87	93
    141	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C	2.27	163.03	-2.28	-0.76	26.69	92
    142	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 1001 DGA C	2.35	164.08	-2.28	-0.76	26.69	92
    143	200064 ARG C, 200031 THR B, 84 VAL C, 1001 DGA C	2.54	164.57	-1.87	-0.66	19.01	95
    144	200031 THR B, 84 VAL C, 1001 DGA C	2.65	165.71	-0.55	-0.79	2.52	107
    145	200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B	2.85	166.29	-1.53	-0.9	18.31	92
    146	200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C	2.92	166.81	-1.25	-0.88	14.58	92
    147	200031 THR B, 84 VAL C, 1001 DGA C, 200053 GLU B, 85 THR C	2.97	167.22	-1.33	-0.87	14.15	97
    148	200031 THR B, 84 VAL C, 1001 DGA C, 85 THR C, 54 ALA C	2.92	167.75	0	-0.58	1.68	104
    149	200031 THR B, 1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C	2.9	168.76	-0.78	-0.67	13.31	97
    150	1001 DGA C, 200053 GLU B, 85 THR C, 54 ALA C	2.85	170.84	-0.8	-0.63	17.19	94
    151	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C	2.99	172.46	-0.7	-0.67	13.74	94
    152	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A	3.64	172.95	-1.46	-0.62	21.39	91
    153	200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A	3.8	173.41	-2.28	-0.78	26.74	89
    154	200053 GLU B, 53 GLY C, 57 ARG A	3.84	174.33	-2.8	-0.79	35.09	80

    pore with bottle neck

    pore with local minimum

13. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100031 THR B, 100064 ARG C, 200084 VAL C, 201001 DGA C, 100032 ASP B, 200084 VAL C, 100030 GLY B, 100031 THR B, 100092 ASN B, 200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B, 100028 SER B, 100080 ASP C, 100079 GLY C, 100082 TYR C, 300079 GLY C, 93 ARG B, 200093 ARG B, 300093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 200028 SER B, 300082 TYR C, 300058 GLN C, 300080 ASP C, 28 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 200027 GLN B, 200028 SER B, 27 GLN B, 27 GLN B, 300026 SER B, 69 THR B, 26 SER B, 28 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A, 300169 HIS A, 300167 ASP B, 300166 SER A, 300166 SER A, 300170 ASP B, 300169 LYS B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300207 LYS B, 300115 VAL B, 300136 GLN A, 300140 MET A, 300116 SER B, 300135 ALA A, 300117 ILE B, 300116 SER B, 300117 ILE B, 300132 GLY A, 300208 SER B, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A, 300211 ARG B, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Unique lining residues set - sidechains

    100031 THR B, 100064 ARG C, 201001 DGA C, 100032 ASP B, 200084 VAL C, 100092 ASN B, 200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B, 100082 TYR C, 93 ARG B, 200093 ARG B, 300093 ARG B, 82 TYR C, 200028 SER B, 300082 TYR C, 300058 GLN C, 28 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 200027 GLN B, 27 GLN B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A, 300168 VAL A, 300169 LYS B, 300169 HIS A, 300167 ASP B, 300166 SER A, 300170 ASP B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300207 LYS B, 300116 SER B, 300135 ALA A, 300117 ILE B, 300209 PHE B, 300119 PRO B, 300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 6 (13-7)
    Hydropathy: -1.4
    Hydrophobicity: -0.39
    Polarity: 14.31
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100031 THR B, 100064 ARG C, 200084 VAL C, 201001 DGA C	2.77	0.73	-1.87	-0.66	19.01	95
    2	100031 THR B, 100064 ARG C, 200084 VAL C, 201001 DGA C, 100032 ASP B	2.71	1.45	-2.28	-0.76	26.69	92
    3	100031 THR B, 100064 ARG C, 200084 VAL C, 100032 ASP B	2.66	2.12	-2.28	-0.76	26.69	92
    4	100031 THR B, 100064 ARG C, 100032 ASP B, 200084 VAL C	2.58	4.9	-1.13	-0.28	25.87	93
    5	100064 ARG C, 100032 ASP B, 100030 GLY B, 100031 THR B	2.86	4.98	-2.2	-0.77	27.12	84
    6	100031 THR B, 100064 ARG C, 100030 GLY B	2.96	5.02	-1.87	-0.66	19.01	95
    7	100031 THR B, 100064 ARG C, 200084 VAL C, 100030 GLY B	2.94	5.25	-0.35	-0.22	14.29	96
    8	100064 ARG C, 200084 VAL C, 100030 GLY B	2.95	5.45	-0.23	-0.03	18.5	90
    9	100064 ARG C, 100032 ASP B, 200084 VAL C, 100030 GLY B	2.98	6.5	-1.05	-0.28	26.3	89
    10	100064 ARG C, 100032 ASP B, 200084 VAL C, 100030 GLY B, 100092 ASN B	3.12	7.78	-1.54	-0.38	21.72	92
    11	100064 ARG C, 200084 VAL C, 100030 GLY B, 100092 ASN B, 200082 TYR C	3.26	7.95	-1.1	0.05	12.1	83
    12	200084 VAL C, 100030 GLY B, 100092 ASN B, 200082 TYR C	3.26	8.86	-0.25	0.17	2.13	84
    13	100030 GLY B, 100092 ASN B, 200082 TYR C	3.26	9.28	-1.73	-0.15	2.79	77
    14	100030 GLY B, 100092 ASN B, 200082 TYR C, 100058 GLN C	3.08	11.29	-2.18	-0.39	2.98	79
    15	100030 GLY B, 200082 TYR C, 100058 GLN C, 100028 SER B	3.18	12.49	-1.5	-0.44	2.55	83
    16	200082 TYR C, 100058 GLN C, 100028 SER B	3.41	14.77	-1.87	-0.32	2.27	83
    17	200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B	3.78	14.95	-2.53	-0.35	14.7	83
    18	200082 TYR C, 100028 SER B, 100093 ARG B	3.76	15.04	-2.2	-0.09	18.43	83
    19	200082 TYR C, 100058 GLN C, 100028 SER B, 100093 ARG B	3.68	15.6	-2.53	-0.35	14.7	83
    20	200082 TYR C, 100058 GLN C, 100093 ARG B, 100028 SER B	3.7	15.91	-2.43	-0.3	15.13	72
    21	200082 TYR C, 100058 GLN C, 100093 ARG B	3.76	16.79	-3.1	-0.14	19.05	72
    22	200082 TYR C, 100058 GLN C, 100093 ARG B, 100080 ASP C	3.93	17.01	-2.43	-0.3	15.13	72
    23	200082 TYR C, 100058 GLN C, 100093 ARG B, 100079 GLY C	3.18	18.21	-2.43	-0.3	15.13	72
    24	100058 GLN C, 100093 ARG B, 100080 ASP C, 100079 GLY C	2.98	18.95	-2.2	-0.78	15.57	83
    25	100058 GLN C, 100093 ARG B, 100079 GLY C, 100082 TYR C	3.1	21.86	-2.43	-0.3	15.13	72
    26	100093 ARG B, 100079 GLY C, 100082 TYR C	5.36	22.99	-2.07	-0.04	19	66
    27	200082 TYR C, 100093 ARG B, 100079 GLY C, 100082 TYR C, 300079 GLY C	6.05	24.69	-1.58	0.04	12.4	61
    28	93 ARG B, 200093 ARG B, 300093 ARG B, 79 GLY C, 82 TYR C	7.07	25.09	-3.04	-0.19	32.2	74
    29	93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C	7.3	25.23	-2.22	-0.27	22.47	72
    30	93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200028 SER B	7.34	25.39	-2.3	-0.3	22.13	83
    31	93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C	6.92	26.44	-2.22	-0.27	22.47	72
    32	100093 ARG B, 100079 GLY C, 100082 TYR C, 300079 GLY C, 300093 ARG B	6.49	27.33	-2.22	-0.27	22.47	72
    33	100093 ARG B, 100082 TYR C, 300079 GLY C, 300093 ARG B, 300082 TYR C	5.28	29.39	-2.4	0.12	22.12	66
    34	100082 TYR C, 300079 GLY C, 300093 ARG B, 300082 TYR C, 300058 GLN C	4.59	30.34	-2.2	-0.02	12.43	66
    35	100082 TYR C, 300079 GLY C, 300093 ARG B, 300058 GLN C	3.36	31.68	-2.43	-0.3	15.13	72
    36	300079 GLY C, 300093 ARG B, 300058 GLN C, 300080 ASP C	2.8	32.47	-2.2	-0.78	15.57	83
    37	300079 GLY C, 300093 ARG B, 300058 GLN C	2.93	32.95	-2.8	-0.77	19.64	83
    38	300079 GLY C, 300093 ARG B, 300082 TYR C, 300058 GLN C	3.31	35.72	-2.43	-0.3	15.13	72
    39	300079 GLY C, 300093 ARG B, 300082 TYR C	5.24	36.81	-2.07	-0.04	19	66
    40	100082 TYR C, 300079 GLY C, 300093 ARG B, 79 GLY C, 300082 TYR C	5.88	38.42	-1.58	0.04	12.4	61
    41	200082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C	6.75	38.73	-2.4	0.12	22.12	66
    42	200082 TYR C, 100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C	6.96	38.95	-2.4	0.12	22.12	66
    43	200082 TYR C, 100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C	7.04	39.2	-2.22	-0.27	22.47	72
    44	200082 TYR C, 100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C	6.96	39.53	-1.58	0.04	12.4	61
    45	300079 GLY C, 93 ARG B, 300093 ARG B, 79 GLY C, 300082 TYR C	6.63	40.37	-2.22	-0.27	22.47	72
    46	93 ARG B, 300093 ARG B, 79 GLY C, 300082 TYR C, 28 SER B	6.14	41.37	-2.3	-0.3	22.13	83
    47	93 ARG B, 300093 ARG B, 300082 TYR C, 28 SER B	4.05	43.86	-2.78	-0.18	26.82	83
    48	300093 ARG B, 300082 TYR C, 28 SER B	2.82	46.07	-2.2	-0.09	18.43	83
    49	300093 ARG B, 28 SER B	2.64	46.9	-2.65	-0.7	26.84	100
    50	300093 ARG B, 28 SER B, 300027 GLN B	2.64	51.36	-2.93	-0.83	19.07	94
    51	300093 ARG B, 28 SER B, 300027 GLN B, 300028 SER B	4.49	51.85	-2.3	-0.82	15.15	94
    52	300093 ARG B, 28 SER B, 300027 GLN B, 300028 SER B	4.64	52.07	-2.4	-0.87	14.72	100
    53	300093 ARG B, 300027 GLN B, 300028 SER B	4.71	52.46	-2.93	-0.83	19.07	94
    54	300093 ARG B, 28 SER B, 300027 GLN B, 300028 SER B	4.79	53.3	-2.4	-0.87	14.72	100
    55	28 SER B, 300027 GLN B, 300028 SER B	5.09	56.63	-1.7	-1.01	2.29	106
    56	100028 SER B, 100027 GLN B, 200027 GLN B, 200028 SER B	6.12	57.42	-2.05	-0.99	3.03	95
    57	28 SER B, 300027 GLN B, 300028 SER B, 27 GLN B	5.64	58.75	-2.05	-0.99	3.03	95
    58	28 SER B, 300027 GLN B, 27 GLN B	5.37	59.52	-1.57	-0.96	2.86	100
    59	28 SER B, 300027 GLN B, 300026 SER B	5.12	60.22	-1.57	-0.96	2.86	100
    60	28 SER B, 300027 GLN B, 300026 SER B, 69 THR B	4.49	62.51	-1.35	-0.91	2.56	102
    61	28 SER B, 300027 GLN B, 27 GLN B, 300026 SER B	4.8	62.73	-1.28	-0.92	2.99	100
    62	27 GLN B, 300026 SER B, 69 THR B, 26 SER B, 28 SER B	4.91	66.1	-0.46	-0.79	3.04	107
    63	300026 SER B, 69 THR B, 26 SER B	5	68.77	-0.5	-0.79	2.81	107
    64	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.65	69.55	-1.5	-0.7	15.11	95
    65	300026 SER B, 69 THR B, 24 ARG B	4.3	71.45	-1.87	-0.66	19.01	95
    66	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.93	72.79	-2.28	-0.76	26.69	92
    67	300026 SER B, 24 ARG B, 70 ASP B	3.7	73.45	-2.8	-0.75	35.03	84
    68	24 ARG B, 70 ASP B, 300026 SER B	3.3	75.49	-2.93	-0.81	34.46	95
    69	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.49	77.56	-1.25	-0.32	25.88	85
    70	70 ASP B, 300026 SER B, 300003 LEU B	2.08	80.41	-0.17	-0.29	17.17	85
    71	70 ASP B, 300003 LEU B	2.18	82.74	0.15	0.05	24.92	70
    72	70 ASP B, 300003 LEU B, 300001 ASP B	3	84.74	-0.03	-0.23	17.74	70
    73	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.83	84.89	-0.2	-0.37	13.72	82
    74	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.91	85.93	-0.98	-0.43	25.3	83
    75	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.76	87.27	-1.08	-0.27	25.25	79
    76	300003 LEU B, 300001 ASP B, 300063 LYS A	3.54	89.3	-1.2	-0.1	33.11	70
    77	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.55	90.84	-1.08	-0.27	25.25	79
    78	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.84	91.3	-1.08	-0.2	13.67	84
    79	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	3.97	92.17	-0.94	-0.32	11.61	84
    80	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.25	92.35	-2.4	-0.78	21.56	90
    81	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.28	92.7	-2.03	-0.87	14.58	96
    82	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.29	93.48	-2.4	-0.78	21.56	90
    83	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.29	94.65	-1.5	-0.4	21.26	76
    84	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	4.3	98.45	0.23	0.35	24.92	76
    85	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	4.42	98.96	-1.1	-0.35	25.3	80
    86	300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B	4.42	99.78	-0.93	-0.18	25.3	92
    87	300063 LYS A, 300046 GLU A, 300064 ILE A	3.85	104.3	-0.97	0.09	33.18	84
    88	300046 GLU A, 300064 ILE A, 300063 LYS A	3.74	105.19	0.2	-0.04	17.8	90
    89	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.59	107.98	-0.98	-0.14	26.35	87
    90	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.61	111.37	-2	-0.04	38.51	86
    91	300046 GLU A, 18 ARG B, 300040 ARG A	3.97	113.97	-4.17	-0.66	51.3	81
    92	300046 GLU A, 300064 ILE A, 300040 ARG A	4.03	114.67	-1.17	0.08	34.01	87
    93	300046 GLU A, 300040 ARG A	3	117.42	-4	-0.78	50.95	80
    94	300040 ARG A	1.06	124.22	-4.5	-0.42	52	83
    95	300040 ARG A, 300088 SER A	1	124.93	-2.45	-0.61	27.69	83
    96	300040 ARG A, 300088 SER A, 300091 SER A	1.15	125.27	-1.77	-0.67	19.59	83
    97	300040 ARG A, 300088 SER A, 300041 PRO A, 300091 SER A	1.47	125.54	-1.83	-0.57	14.66	86
    98	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	1.9	126.37	-1.73	-0.53	15.09	70
    99	300040 ARG A, 300088 SER A, 300041 PRO A	2.95	129.18	-2.17	-0.44	18.99	70
    100	300040 ARG A, 300041 PRO A, 300088 SER A	4.78	131.14	-2.3	-0.49	18.42	86
    101	300041 PRO A, 300088 SER A	4.89	132.22	-1.2	-0.53	1.63	87
    102	300041 PRO A, 300091 SER A, 300088 SER A	4.7	132.76	-1.07	-0.68	1.64	97
    103	300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A	4.53	133.22	0.15	-0.22	1.26	86
    104	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.31	133.82	0.02	0.3	1.25	69
    105	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.26	134.01	0.23	0.08	1.27	84
    106	300091 SER A, 300088 SER A, 300180 TYR A	4.24	134.12	-0.97	-0.28	1.65	94
    107	300091 SER A, 300088 SER A	4.24	134.27	-0.8	-0.97	1.67	117
    108	300091 SER A, 300088 SER A, 300180 TYR A	4.26	134.71	-0.97	-0.28	1.65	94
    109	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.29	135.51	0.02	0.3	1.25	69
    110	300041 PRO A, 300091 SER A, 300175 LEU A, 300180 TYR A	4.33	136.55	0.02	0.3	1.25	69
    111	300041 PRO A, 300175 LEU A, 300180 TYR A	4.37	140.14	0.3	0.72	1.11	54
    112	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.41	140.34	0.13	0.34	1.68	54
    113	300041 PRO A, 300175 LEU A, 300180 TYR A	4.36	141.04	0.3	0.72	1.11	54
    114	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.23	141.85	0.13	0.34	1.68	54
    115	300041 PRO A, 300180 TYR A, 300173 ALA A	3.62	143.78	-1.1	0.07	2.19	54
    116	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.28	145.86	-1.7	-0.23	14.12	61
    117	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.3	147.92	-1.78	-0.53	14.11	64
    118	300041 PRO A, 300153 GLU A, 300172 PRO A	3.48	148.27	-2.23	-0.44	17.69	64
    119	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.44	148.89	-2.55	-0.52	14.11	74
    120	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.37	149.24	-2.55	-0.52	14.11	74
    121	300153 GLU A, 300172 PRO A, 300041 ASN B	3.14	150.18	-2.87	-0.67	18.29	79
    122	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.52	152.87	-2.25	-0.7	14.56	79
    123	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.38	153.99	-1.95	-0.88	15.01	90
    124	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.39	154.3	-0.8	-0.47	12.03	78
    125	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.44	154.5	-0.8	-0.47	12.03	78
    126	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.59	155.24	-0.13	-0.31	2.57	79
    127	300041 ASN B, 300182 LEU A, 300171 PHE A	2.73	155.66	-0.03	-0.14	2.3	79
    128	300041 ASN B, 300182 LEU A, 300170 THR A	2.71	155.82	-0.13	-0.13	1.72	88
    129	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.59	157.11	-0.2	-0.3	2.14	88
    130	300041 ASN B, 300170 THR A, 300155 VAL A	2.59	161.07	-1.53	-0.78	2.81	105
    131	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	2.9	161.25	-1.33	-0.78	2.52	106
    132	300041 ASN B, 300156 THR A, 300157 VAL A	3.01	161.44	-1.53	-0.78	2.81	105
    133	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.21	161.62	-1.33	-0.78	2.52	106
    134	300041 ASN B, 300170 THR A, 300157 VAL A	3.28	161.75	-1.53	-0.78	2.81	105
    135	300041 ASN B, 300170 THR A, 300155 VAL A	3.3	161.93	-1.53	-0.78	2.81	105
    136	300041 ASN B, 300170 THR A, 300157 VAL A	3.26	162.15	-1.53	-0.78	2.81	105
    137	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.21	162.53	-1.33	-0.78	2.52	106
    138	300041 ASN B, 300170 THR A, 300157 VAL A	3.2	165.63	-1.53	-0.78	2.81	105
    139	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B	4.1	166.49	-1.25	-0.79	2.95	105
    140	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.44	166.64	-1.08	-0.79	3.04	105
    141	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.52	166.79	0.68	-0.31	2.14	102
    142	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.51	166.93	-1.16	-0.72	12.26	89
    143	300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.51	166.98	-0.13	-0.22	14.1	85
    144	300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B	4.49	167.74	-0.2	-0.21	13.67	92
    145	300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A	4.26	168.12	-0.13	-0.22	14.1	85
    146	300168 VAL A, 300169 LYS B, 300165 SER A	1.99	173.04	-0.03	-0.03	17.67	85
    147	300168 VAL A, 300169 LYS B, 300165 SER A	1.27	174.45	-1.57	-0.67	18.75	72
    148	300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A	1.34	175.57	-1.28	-0.7	14.91	72
    149	300168 VAL A, 300169 LYS B, 300167 GLY A	1.79	176.51	-1.57	-0.67	18.75	72
    150	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.9	176.81	-1.98	-0.44	26.97	81
    151	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.89	177.09	-1.98	-0.44	26.97	81
    152	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.85	177.12	-1.98	-0.44	26.97	81
    153	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.74	177.56	-1.98	-0.44	26.97	81
    154	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.72	178.09	-2.75	-0.5	38.55	83
    155	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.73	178.68	-2.75	-0.5	38.55	83
    156	300169 LYS B, 300167 GLY A, 300167 ASP B	1.75	179.41	-2.6	-0.75	34.19	79
    157	300169 LYS B, 300167 GLY A	1.78	180.19	-2.15	-0.61	26.44	72
    158	300169 LYS B, 300167 GLY A, 300166 SER A	1.81	181.75	-1.57	-0.67	18.75	72
    159	300169 LYS B, 300167 GLY A, 300166 SER A	1.86	181.92	-1.7	-0.73	18.18	94
    160	300169 LYS B, 300166 SER A	1.91	182.13	-2.35	-0.69	25.59	94
    161	300169 LYS B, 300167 GLY A, 300166 SER A	1.98	185.52	-1.7	-0.73	18.18	94
    162	300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B	3.28	186.43	-2.15	-0.81	26.06	91
    163	300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B	4.47	187.38	-1.28	-0.9	14.53	101
    164	300167 GLY A, 300166 SER A, 300170 ASP B	4.68	188.2	-1.57	-0.94	18.25	101
    165	300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A	4.89	189.22	-0.7	-0.45	14.05	98
    166	300167 GLY A, 300170 ASP B, 300140 MET A	4.32	190.58	-0.67	-0.28	18.17	89
    167	300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B	4.08	191.89	-1.38	-0.4	14.47	94
    168	300170 ASP B, 300140 MET A, 300138 ASN B	3.9	193.58	-1.7	-0.27	18.17	94
    169	300140 MET A, 300138 ASN B, 300187 THR A	3.62	195.37	-0.77	-0.18	2.16	101
    170	300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B	3.07	196.92	-0.75	-0.33	2.03	102
    171	300140 MET A, 300187 THR A, 300114 THR B	2.7	198.68	0.17	-0.18	1.58	102
    172	300140 MET A, 300114 THR B	2.53	200.2	0.6	0.12	1.55	100
    173	300140 MET A, 300114 THR B, 300138 ASN A	2.48	200.67	-0.77	-0.18	2.16	101
    174	300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A	2.48	201.65	-0.78	-0.38	2.04	105
    175	300140 MET A, 300114 THR B, 300138 ASN A	2.73	204.39	-0.77	-0.18	2.16	101
    176	300114 THR B, 300138 ASN A	3.5	207.84	-2.1	-0.77	2.52	105
    177	300114 THR B, 300138 ASN A, 300207 LYS B	3.41	210.06	-2.7	-0.65	18.18	94
    178	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B	3.24	211.15	-2.13	-0.69	14.48	94
    179	300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A	3.07	212.12	-2.13	-0.69	14.48	94
    180	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.68	213.33	-1.78	-0.71	12.26	94
    181	300114 THR B, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.65	213.75	-1.35	-0.7	14.48	89
    182	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.63	214.39	-1.78	-0.71	12.26	94
    183	300114 THR B, 300115 VAL B, 300136 GLN A, 300140 MET A, 300116 SER B	2.57	215.86	-0.54	-0.83	2.69	112
    184	300114 THR B, 300115 VAL B, 300136 GLN A, 300116 SER B	2.54	216.53	-0.58	-0.84	2.52	112
    185	300207 LYS B, 300115 VAL B, 300136 GLN A, 300116 SER B	2.51	217.2	-1.38	-0.75	14.48	94
    186	300115 VAL B, 300136 GLN A, 300116 SER B	2.47	217.78	-0.53	-0.86	2.81	117
    187	300115 VAL B, 300136 GLN A, 300116 SER B, 300135 ALA A	2.37	218.59	0.05	-0.64	2.11	108
    188	300115 VAL B, 300116 SER B, 300135 ALA A	2.28	219.75	0.2	-0.58	1.68	108
    189	300116 SER B, 300135 ALA A, 300117 ILE B	1.96	222.07	0.2	-0.58	1.68	108
    190	300135 ALA A, 300117 ILE B, 300116 SER B	1.91	222.57	0.33	-0.53	2.25	100
    191	300135 ALA A, 300116 SER B, 300117 ILE B	1.81	223.56	1.97	0.34	1.17	101
    192	300135 ALA A, 300117 ILE B	1.68	225.27	3.15	0.92	0.07	101
    193	300135 ALA A, 300117 ILE B, 300132 GLY A, 300208 SER B	1.66	226.21	1.38	0.06	1.72	101
    194	300135 ALA A, 300117 ILE B, 300132 GLY A	1.67	226.72	1.97	0.34	1.17	101
    195	300117 ILE B, 300132 GLY A, 300209 PHE B	1.71	228.04	2.3	0.79	1.29	77
    196	300117 ILE B, 300132 GLY A, 300209 PHE B, 300119 PRO B	1.72	228.52	0.1	-0.09	2.17	54
    197	300117 ILE B, 300132 GLY A, 300119 PRO B	1.63	228.67	-0.8	-0.56	2.78	58
    198	300117 ILE B, 300132 GLY A, 300119 PRO B	1.38	228.88	0.83	0.31	1.7	80
    199	300117 ILE B, 300132 GLY A, 300119 PRO B	1.25	229.3	-0.8	-0.56	2.78	58
    200	300132 GLY A, 300209 PHE B, 300119 PRO B	1.1	233.53	0.27	0.15	1.77	54
    201	300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B	1.58	233.94	0.1	-0.09	2.17	54
    202	300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A	1.81	234.43	0	-0.23	2.41	54
    203	300132 GLY A, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A	2.32	235.42	-1.46	-0.58	12.74	70
    204	300119 PRO B, 300210 ASN B, 300218 ARG A	2.09	237	-2.17	-0.44	18.99	70
    205	300209 PHE B, 300119 PRO B, 300210 ASN B, 300218 ARG A	2.05	237.5	-0.93	0.01	14.33	64
    206	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B	1.95	238.12	-1.73	-0.53	15.09	70
    207	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B, 300186 TYR B	1.95	238.48	-1.64	-0.2	12.39	63
    208	300119 PRO B, 300218 ARG A, 300211 ARG B, 300186 TYR B	2.02	240.18	-1.95	-0.05	14.64	63
    209	300218 ARG A, 300186 TYR B, 300211 ARG B	2.23	241.77	-3.43	0.09	35.2	72
    210	300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B	2.41	241.77	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

14. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 100027 GLN B, 200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200002 ILE B, 200098 PHE B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200042 GLY A, 200165 ASP B, 200040 THR B, 200085 ASN B, 200103 LYS B, 200010 ILE B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200165 ASP B, 200040 THR B, 200085 ASN B, 200103 LYS B, 200010 ILE B

    Physicochemical properties of lining side-chains

    Charge: 4 (13-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 15.06
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.26	0.26	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.45	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.2	0.61	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.22	0.74	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.2	1.03	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3	1.51	-1.53	-0.78	2.81	105
    7	100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	2.89	2.08	-1.25	-0.79	2.95	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.51	5.72	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.52	6.66	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.78	7.02	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.2	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.57	7.93	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.41	8.34	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.34	8.75	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.31	9.88	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.37	12.65	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.11	13.36	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.36	13.89	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.47	14.5	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.31	16.7	-1.78	-0.53	14.11	64
    21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.3	19.09	-1.7	-0.23	14.12	61
    22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.75	21.04	-1.1	0.07	2.19	54
    23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.42	21.41	0.13	0.34	1.68	54
    24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.37	22.12	0.3	0.72	1.11	54
    25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.46	22.49	0.13	0.34	1.68	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.21	27.28	0.3	0.72	1.11	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.2	27.85	-0.06	0.08	1.67	69
    28	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.2	28.15	0.23	0.08	1.27	84
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.23	28.26	-0.97	-0.28	1.65	94
    30	100091 SER A, 100088 SER A	4.27	28.35	-0.8	-0.97	1.67	117
    31	100180 TYR A, 100091 SER A, 100088 SER A	4.33	28.52	-0.97	-0.28	1.65	94
    32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.41	29	0.23	0.08	1.27	84
    33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.6	29.36	0.02	0.3	1.25	69
    34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.71	29.8	0.15	-0.22	1.26	86
    35	100041 PRO A, 100091 SER A, 100088 SER A	4.82	30.76	-1.07	-0.68	1.64	97
    36	100041 PRO A, 100088 SER A	5	31.9	-1.2	-0.53	1.63	87
    37	100041 PRO A, 100088 SER A, 100040 ARG A	4.55	33.89	-2.3	-0.49	18.42	86
    38	100041 PRO A, 100088 SER A, 100040 ARG A	3.28	36.63	-2.17	-0.44	18.99	70
    39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.9	36.96	-1.73	-0.53	15.09	70
    40	100088 SER A, 100040 ARG A, 100091 SER A	1.5	38	-1.77	-0.67	19.59	83
    41	100088 SER A, 100040 ARG A	0.61	40.1	-2.45	-0.61	27.69	83
    42	100040 ARG A	0.21	45.88	-4.5	-0.42	52	83
    43	100040 ARG A, 100043 HIS A	1.27	46.91	-3.85	-0.08	51.8	87
    44	100040 ARG A, 100046 GLU A	1.98	50.22	-4	-0.78	50.95	80
    45	100040 ARG A, 100046 GLU A, 300018 ARG B	4.43	52.92	-4.17	-0.66	51.3	81
    46	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.53	56.18	-2	-0.04	38.51	86
    47	100046 GLU A, 300018 ARG B, 100064 ILE A	3.51	56.77	-1.17	0.08	34.01	87
    48	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.15	59.42	-0.98	-0.14	26.35	87
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.18	60.22	0.2	-0.04	17.8	90
    50	100046 GLU A, 100064 ILE A, 100063 LYS A	3.32	64.79	-0.97	0.09	33.18	84
    51	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.97	65.29	-0.93	-0.18	25.3	92
    52	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.84	66.16	-1.1	-0.35	25.3	80
    53	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.35	69.35	0.23	0.35	24.92	76
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.23	70.36	-1	-0.3	25.73	67
    55	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.16	71.06	-1.5	-0.4	21.26	76
    56	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.14	71.41	-2.4	-0.78	21.56	90
    57	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.15	71.78	-2.03	-0.87	14.58	96
    58	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.2	72	-2.4	-0.78	21.56	90
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4	72.97	-0.94	-0.32	11.61	84
    60	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.88	73.4	-1.08	-0.2	13.67	84
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.56	75.37	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B	3.58	77.13	-1.2	-0.1	33.11	70
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.83	78.06	-1.08	-0.27	25.25	79
    64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.1	78.27	-1.56	-0.42	30.14	81
    65	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.84	79.15	-0.98	-0.43	25.3	83
    66	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.8	79.32	-0.2	-0.37	13.72	82
    67	100003 LEU B, 300070 ASP B, 100001 ASP B	3.09	81.29	-0.03	-0.23	17.74	70
    68	100003 LEU B, 300070 ASP B	2.21	84.4	0.15	0.05	24.92	70
    69	100003 LEU B, 300070 ASP B, 100026 SER B	2.09	86.85	-0.17	-0.29	17.17	85
    70	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.4	89.03	-1.25	-0.32	25.88	85
    71	300070 ASP B, 100026 SER B, 300024 ARG B	3.34	90.45	-2.93	-0.81	34.46	95
    72	300070 ASP B, 300024 ARG B, 100026 SER B	3.57	91.62	-2.8	-0.75	35.03	84
    73	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.84	93.2	-2.28	-0.76	26.69	92
    74	300024 ARG B, 100026 SER B, 300069 THR B	4.57	94.65	-1.87	-0.66	19.01	95
    75	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.67	95.48	-1.5	-0.7	15.11	95
    76	100026 SER B, 300069 THR B, 300026 SER B	4.48	98.47	-0.5	-0.79	2.81	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.7	99.4	-0.48	-0.79	2.95	107
    78	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.86	101.19	-0.46	-0.79	3.04	107
    79	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.16	101.38	-0.58	-0.84	2.52	112
    80	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.12	101.52	-1.28	-0.92	2.99	100
    81	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.23	104.74	-1.35	-0.91	2.56	102
    82	100026 SER B, 300028 SER B, 100027 GLN B	5.43	105.41	-1.57	-0.96	2.86	100
    83	300028 SER B, 100027 GLN B, 300027 GLN B	5.72	106.03	-2.6	-1.06	2.91	95
    84	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	5.98	106.52	-2.05	-0.99	3.03	95
    85	300028 SER B, 100027 GLN B, 100028 SER B	6.21	106.84	-1.7	-1.01	2.29	106
    86	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.39	107.84	-2.05	-0.99	3.03	95
    87	300028 SER B, 100027 GLN B, 100028 SER B	4.99	111.36	-1.7	-1.01	2.29	106
    88	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.79	111.63	-2.4	-0.87	14.72	100
    89	100027 GLN B, 100028 SER B, 100093 ARG B	4.76	112.05	-2.93	-0.83	19.07	94
    90	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.57	113.05	-2.4	-0.87	14.72	100
    91	300028 SER B, 100027 GLN B, 100093 ARG B	2.5	118.44	-2.93	-0.83	19.07	94
    92	300028 SER B, 100093 ARG B	2.73	119.14	-2.65	-0.7	26.84	100
    93	300028 SER B, 100093 ARG B, 100082 TYR C	3.04	120.22	-2.2	-0.09	18.43	83
    94	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.85	123.27	-2.78	-0.18	26.82	83
    95	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.1	124.07	-2.3	-0.3	22.13	83
    96	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.53	124.71	-2.22	-0.27	22.47	72
    97	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.94	124.95	-1.58	0.04	12.4	61
    98	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	7.09	125.33	-2.4	0.12	22.12	66
    99	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.97	125.73	-2.4	0.12	22.12	66
    100	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.66	126.41	-2.22	-0.27	22.47	72
    101	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.63	128.3	-1.58	0.04	12.4	61
    102	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.02	129.27	-1.88	0.25	14.65	61
    103	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.12	131.63	-2.43	-0.3	15.13	72
    104	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.16	132.35	-2.2	-0.78	15.57	83
    105	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.47	133.45	-2.43	-0.3	15.13	72
    106	100093 ARG B, 200082 TYR C, 100058 GLN C	3.65	134.43	-3.1	-0.14	19.05	72
    107	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.57	134.68	-2.43	-0.3	15.13	72
    108	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.47	135.14	-2.53	-0.35	14.7	83
    109	100028 SER B, 100093 ARG B, 100058 GLN C	3.48	135.45	-2.93	-0.83	19.07	94
    110	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.83	136.7	-2.53	-0.35	14.7	83
    111	100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C	3.98	137.11	-2.78	-0.18	26.82	83
    112	100028 SER B, 200093 ARG B, 200082 TYR C	3.3	139.03	-2.2	-0.09	18.43	83
    113	100028 SER B, 200027 GLN B, 200093 ARG B	2.48	144.2	-2.93	-0.83	19.07	94
    114	100028 SER B, 200027 GLN B, 200093 ARG B, 200028 SER B	4.08	144.73	-2.3	-0.82	15.15	94
    115	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.49	145.04	-2.4	-0.87	14.72	100
    116	200027 GLN B, 200028 SER B, 200093 ARG B	4.83	145.53	-2.93	-0.83	19.07	94
    117	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	5.08	146.2	-2.4	-0.87	14.72	100
    118	100028 SER B, 200027 GLN B, 200028 SER B	5.07	149.7	-1.7	-1.01	2.29	106
    119	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.99	150.68	-2.05	-0.99	3.03	95
    120	100027 GLN B, 100028 SER B, 200027 GLN B, 200028 SER B	5.49	151.9	-2.05	-0.99	3.03	95
    121	100028 SER B, 200027 GLN B, 100027 GLN B	5.22	152.57	-1.57	-0.96	2.86	100
    122	100028 SER B, 200027 GLN B, 200026 SER B	4.97	153.19	-1.57	-0.96	2.86	100
    123	100028 SER B, 200027 GLN B, 200026 SER B, 100069 THR B	4.51	155.54	-1.35	-0.91	2.56	102
    124	100028 SER B, 200027 GLN B, 100027 GLN B, 200026 SER B	4.82	155.94	-1.28	-0.92	2.99	100
    125	100026 SER B, 100028 SER B, 100027 GLN B, 200026 SER B, 100069 THR B	4.92	158.97	-0.46	-0.79	3.04	107
    126	100026 SER B, 100027 GLN B, 200026 SER B, 100069 THR B	5.01	159.9	-0.48	-0.79	2.95	107
    127	100026 SER B, 200026 SER B, 100069 THR B	4.97	161.67	-0.5	-0.79	2.81	107
    128	100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B	4.68	162.93	-1.5	-0.7	15.11	95
    129	200026 SER B, 100069 THR B, 100024 ARG B	4.34	164.65	-1.87	-0.66	19.01	95
    130	200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B	3.91	165.83	-2.28	-0.76	26.69	92
    131	200026 SER B, 100024 ARG B, 100070 ASP B	3.63	166.55	-2.8	-0.75	35.03	84
    132	100024 ARG B, 100070 ASP B, 200026 SER B	3.45	168.59	-2.93	-0.81	34.46	95
    133	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.76	170.37	-1.25	-0.32	25.88	85
    134	100070 ASP B, 200026 SER B, 200003 LEU B	2.09	173.36	-0.17	-0.29	17.17	85
    135	100070 ASP B, 200003 LEU B	2.18	175.9	0.15	0.05	24.92	70
    136	100070 ASP B, 200003 LEU B, 200001 ASP B	2.96	177.9	-0.03	-0.23	17.74	70
    137	100070 ASP B, 200003 LEU B, 200001 ASP B, 100072 THR B	3.93	178.02	-0.2	-0.37	13.72	82
    138	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	3.95	179.03	-0.98	-0.43	25.3	83
    139	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	4.09	179.27	-1.56	-0.42	30.14	81
    140	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	4.04	180.1	-1.08	-0.27	25.25	79
    141	200003 LEU B, 200001 ASP B, 200063 LYS A	3.72	182.44	-1.2	-0.1	33.11	70
    142	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.51	183.8	-1.08	-0.27	25.25	79
    143	200003 LEU B, 200063 LYS A, 200097 THR B, 200002 ILE B	3.49	184.21	-0.3	-0.21	13.67	77
    144	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B	3.49	184.58	-0.3	-0.21	13.67	77
    145	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A	3.53	185.3	-0.94	-0.32	11.61	84
    146	200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	3.83	185.46	-2.4	-0.78	21.56	90
    147	200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.01	185.69	-2.03	-0.87	14.58	96
    148	200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.44	186.2	-2.4	-0.78	21.56	90
    149	200003 LEU B, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.66	187.06	-1.5	-0.4	21.26	76
    150	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	4.84	188.16	-1	-0.3	25.73	67
    151	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	4.83	191.54	0.23	0.35	24.92	76
    152	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	4.61	191.89	-1.1	-0.35	25.3	80
    153	200063 LYS A, 200046 GLU A, 200064 ILE A, 100020 SER B	4.36	192.52	-0.93	-0.18	25.3	92
    154	200063 LYS A, 200046 GLU A, 200064 ILE A	3.54	197.14	-0.97	0.09	33.18	84
    155	200046 GLU A, 200064 ILE A, 200063 LYS A	3.75	197.93	0.2	-0.04	17.8	90
    156	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.85	201.07	-0.98	-0.14	26.35	87
    157	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.53	204.28	-2	-0.04	38.51	86
    158	200046 GLU A, 100018 ARG B, 200040 ARG A	3.93	207	-4.17	-0.66	51.3	81
    159	200046 GLU A, 200064 ILE A, 200040 ARG A	4.08	207.52	-1.17	0.08	34.01	87
    160	200046 GLU A, 200040 ARG A	1.96	211	-4	-0.78	50.95	80
    161	200040 ARG A	-0.05	217.1	-4.5	-0.42	52	83
    162	200040 ARG A, 200088 SER A	0.06	217.87	-2.45	-0.61	27.69	83
    163	200040 ARG A, 200088 SER A, 200091 SER A	0.38	218.29	-1.77	-0.67	19.59	83
    164	200040 ARG A, 200088 SER A, 200091 SER A	0.88	218.52	-1.9	-0.73	19.02	100
    165	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	1.48	218.78	-1.83	-0.57	14.66	86
    166	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.13	219.52	-1.73	-0.53	15.09	70
    167	200040 ARG A, 200088 SER A, 200041 PRO A	3.36	221.99	-2.17	-0.44	18.99	70
    168	200040 ARG A, 200041 PRO A, 200088 SER A	4.91	224.13	-2.3	-0.49	18.42	86
    169	200041 PRO A, 200088 SER A	4.72	225.5	-1.2	-0.53	1.63	87
    170	200091 SER A, 200041 PRO A, 200088 SER A	4.6	225.97	-1.07	-0.68	1.64	97
    171	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.4	226.68	0.15	-0.22	1.26	86
    172	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.31	226.92	0.02	0.3	1.25	69
    173	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.24	227.11	0.23	0.08	1.27	84
    174	200091 SER A, 200088 SER A, 200180 TYR A	4.12	227.32	-0.97	-0.28	1.65	94
    175	200091 SER A, 200088 SER A	4.08	227.5	-0.8	-0.97	1.67	117
    176	200091 SER A, 200088 SER A, 200180 TYR A	4.04	227.93	-0.97	-0.28	1.65	94
    177	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.03	228.62	0.02	0.3	1.25	69
    178	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.02	229.51	-0.06	0.08	1.67	69
    179	200041 PRO A, 200175 LEU A, 200180 TYR A	4.03	233.18	0.3	0.72	1.11	54
    180	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.28	233.62	0.13	0.34	1.68	54
    181	200041 PRO A, 200175 LEU A, 200180 TYR A	4.44	234.19	0.3	0.72	1.11	54
    182	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.29	235.04	0.13	0.34	1.68	54
    183	200041 PRO A, 200180 TYR A, 200173 ALA A	3.79	237.29	-1.1	0.07	2.19	54
    184	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.31	239.06	-1.7	-0.23	14.12	61
    185	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.24	241.46	-1.78	-0.53	14.11	64
    186	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.43	241.98	-2.55	-0.52	14.11	74
    187	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.49	242.64	-2.55	-0.52	14.11	74
    188	200041 PRO A, 200172 PRO A, 200041 ASN B, 200042 GLY A	3.55	243.64	-1.78	-0.44	2.48	73
    189	200041 PRO A, 200172 PRO A, 200041 ASN B, 200042 GLY A	3.65	243.85	-1.78	-0.44	2.48	73
    190	200041 PRO A, 200172 PRO A, 200041 ASN B, 200042 GLY A	3.68	244.11	-1.78	-0.44	2.48	73
    191	200172 PRO A, 200041 ASN B, 200042 GLY A, 200165 ASP B	3.61	244.86	-2.25	-0.68	14.51	82
    192	200172 PRO A, 200041 ASN B, 200042 GLY A, 200165 ASP B, 200040 THR B	3.54	245.14	-1.94	-0.69	11.94	88
    193	200041 ASN B, 200042 GLY A, 200165 ASP B, 200040 THR B	3.22	247.53	-2.03	-0.85	14.53	99
    194	200042 GLY A, 200165 ASP B, 200040 THR B	3.21	248.74	-1.53	-0.87	18.25	96
    195	200042 GLY A, 200165 ASP B, 200085 ASN B	3.27	248.81	-2.47	-0.87	18.82	95
    196	200042 GLY A, 200165 ASP B, 200040 THR B, 200085 ASN B	3.23	249.13	-2.03	-0.85	14.53	99
    197	200165 ASP B, 200040 THR B, 200085 ASN B	2.89	249.65	-2.57	-0.86	18.25	99
    198	200042 GLY A, 200165 ASP B, 200085 ASN B	2.67	254.9	-2.47	-0.87	18.82	95
    199	200042 GLY A, 200165 ASP B, 200085 ASN B, 200103 LYS B	3.54	255.95	-2.83	-0.76	26.49	87
    200	200042 GLY A, 200165 ASP B, 200103 LYS B, 200010 ILE B	3.93	256.16	-0.83	-0.11	25.68	87

    pore with bottle neck

    pore with local minimum

15. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 200026 SER B, 100069 THR B, 100027 GLN B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A, 200170 THR A, 200155 VAL A, 200156 THR A, 200157 VAL A, 200040 THR B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 4 (12-8)
    Hydropathy: -1.5
    Hydrophobicity: -0.44
    Polarity: 14.39
    Mutability: 86
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.26	0.27	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.45	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.19	0.62	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.77	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.19	1.05	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.04	1.59	-1.53	-0.78	2.81	105
    7	100170 THR A, 100041 ASN B, 100155 VAL A	2.62	5.8	-1.53	-0.78	2.81	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.61	6.54	-0.2	-0.3	2.14	88
    9	100170 THR A, 100041 ASN B, 100182 LEU A	2.8	6.87	-0.13	-0.13	1.72	88
    10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.23	-0.03	-0.14	2.3	79
    11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.57	7.96	-0.13	-0.31	2.57	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.4	8.49	-0.8	-0.47	12.03	78
    13	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.32	8.97	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.26	9.54	-1.95	-0.88	15.01	90
    15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.24	12.84	-2.25	-0.7	14.56	79
    16	100041 ASN B, 100153 GLU A, 100172 PRO A	3.13	13.2	-2.87	-0.67	18.29	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.33	13.76	-2.55	-0.52	14.11	74
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.6	14.67	-2.55	-0.52	14.11	74
    19	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.4	16.96	-1.78	-0.53	14.11	64
    20	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.35	18.88	-1.7	-0.23	14.12	61
    21	100173 ALA A, 100041 PRO A, 100180 TYR A	3.49	20.95	-1.1	0.07	2.19	54
    22	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.09	21.36	0.13	0.34	1.68	54
    23	100041 PRO A, 100180 TYR A, 100175 LEU A	4.38	22.07	0.3	0.72	1.11	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.4	22.43	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.3	27.21	0.3	0.72	1.11	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.26	27.8	-0.06	0.08	1.67	69
    27	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.22	28.12	0.23	0.08	1.27	84
    28	100180 TYR A, 100091 SER A, 100088 SER A	4.18	28.23	-0.97	-0.28	1.65	94
    29	100091 SER A, 100088 SER A	4.17	28.32	-0.8	-0.97	1.67	117
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.17	28.49	-0.97	-0.28	1.65	94
    31	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.2	28.97	0.23	0.08	1.27	84
    32	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.32	29.34	0.02	0.3	1.25	69
    33	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	29.78	0.15	-0.22	1.26	86
    34	100041 PRO A, 100091 SER A, 100088 SER A	4.58	30.75	-1.07	-0.68	1.64	97
    35	100041 PRO A, 100088 SER A	4.94	31.89	-1.2	-0.53	1.63	87
    36	100041 PRO A, 100088 SER A, 100040 ARG A	4.51	33.93	-2.3	-0.49	18.42	86
    37	100041 PRO A, 100088 SER A, 100040 ARG A	3	36.29	-2.17	-0.44	18.99	70
    38	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.38	36.98	-1.73	-0.53	15.09	70
    39	100088 SER A, 100040 ARG A, 100091 SER A	1.85	38.11	-1.77	-0.67	19.59	83
    40	100088 SER A, 100040 ARG A	1.81	39.07	-2.45	-0.61	27.69	83
    41	100040 ARG A	1.85	44.91	-4.5	-0.42	52	83
    42	100040 ARG A, 100043 HIS A	2.59	46.14	-3.85	-0.08	51.8	87
    43	100040 ARG A, 100046 GLU A	2.83	50.39	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	3.68	52.52	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.55	56.4	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.66	59.77	-0.98	-0.14	26.35	87
    47	100046 GLU A, 100064 ILE A, 100063 LYS A	3.53	60.56	0.2	-0.04	17.8	90
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.32	65.06	-0.97	0.09	33.18	84
    49	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.51	65.41	-0.93	-0.18	25.3	92
    50	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.82	65.84	-1.1	-0.35	25.3	80
    51	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.06	69.97	0.23	0.35	24.92	76
    52	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.93	70.81	-1	-0.3	25.73	67
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.69	71.29	-1.5	-0.4	21.26	76
    54	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.43	71.46	-2.4	-0.78	21.56	90
    55	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.94	71.67	-2.03	-0.87	14.58	96
    56	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.75	71.89	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.48	72.8	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.46	73.23	-0.3	-0.21	13.67	77
    59	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.48	73.67	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.52	75.18	-1.08	-0.27	25.25	79
    61	100063 LYS A, 100003 LEU B, 100001 ASP B	3.77	76.98	-1.2	-0.1	33.11	70
    62	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	4.02	77.98	-1.08	-0.27	25.25	79
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.12	78.19	-1.56	-0.42	30.14	81
    64	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.9	79.1	-0.98	-0.43	25.3	83
    65	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.88	79.26	-0.2	-0.37	13.72	82
    66	100003 LEU B, 300070 ASP B, 100001 ASP B	2.99	81.27	-0.03	-0.23	17.74	70
    67	100003 LEU B, 300070 ASP B	2.24	84.4	0.15	0.05	24.92	70
    68	100003 LEU B, 300070 ASP B, 100026 SER B	2.18	86.87	-0.17	-0.29	17.17	85
    69	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.57	88.63	-1.25	-0.32	25.88	85
    70	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	90.42	-2.93	-0.81	34.46	95
    71	300070 ASP B, 300024 ARG B, 100026 SER B	3.57	91.33	-2.8	-0.75	35.03	84
    72	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.78	93.35	-2.28	-0.76	26.69	92
    73	300024 ARG B, 100026 SER B, 300069 THR B	4.66	94.39	-1.87	-0.66	19.01	95
    74	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.6	95.6	-1.5	-0.7	15.11	95
    75	100026 SER B, 300069 THR B, 300026 SER B	4.51	98.85	-0.5	-0.79	2.81	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.83	101.26	-0.46	-0.79	3.04	107
    77	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.05	101.57	-1.28	-0.92	2.99	100
    78	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.22	104.42	-1.35	-0.91	2.56	102
    79	100026 SER B, 100027 GLN B, 300028 SER B	5.35	105.1	-1.57	-0.96	2.86	100
    80	300027 GLN B, 100027 GLN B, 300028 SER B	5.66	105.75	-1.57	-0.96	2.86	100
    81	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.95	106.7	-2.05	-0.99	3.03	95
    82	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.42	107.65	-2.05	-0.99	3.03	95
    83	100027 GLN B, 300028 SER B, 100028 SER B	5.2	111.25	-1.7	-1.01	2.29	106
    84	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.76	111.57	-2.4	-0.87	14.72	100
    85	100027 GLN B, 100028 SER B, 100093 ARG B	4.45	111.95	-2.93	-0.83	19.07	94
    86	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.27	112.87	-2.4	-0.87	14.72	100
    87	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.14	113.57	-2.3	-0.82	15.15	94
    88	100027 GLN B, 300028 SER B, 100093 ARG B	2.77	118.3	-2.93	-0.83	19.07	94
    89	300028 SER B, 100093 ARG B	2.84	119.02	-2.65	-0.7	26.84	100
    90	300028 SER B, 100093 ARG B, 100082 TYR C	3.03	120.14	-2.2	-0.09	18.43	83
    91	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.68	123.21	-2.78	-0.18	26.82	83
    92	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.24	124.03	-2.3	-0.3	22.13	83
    93	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.67	124.67	-2.22	-0.27	22.47	72
    94	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.94	124.91	-1.58	0.04	12.4	61
    95	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.96	125.3	-2.4	0.12	22.12	66
    96	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.83	125.71	-2.4	0.12	22.12	66
    97	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.61	126.41	-2.22	-0.27	22.47	72
    98	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.89	128.32	-1.58	0.04	12.4	61
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.21	131.64	-2.43	-0.3	15.13	72
    100	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.06	132.35	-2.2	-0.78	15.57	83
    101	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.14	133.45	-2.43	-0.3	15.13	72
    102	100093 ARG B, 200082 TYR C, 100058 GLN C	3.87	134.45	-3.1	-0.14	19.05	72
    103	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.79	135.03	-2.53	-0.35	14.7	83
    104	100028 SER B, 100093 ARG B, 100058 GLN C	3.79	135.31	-2.93	-0.83	19.07	94
    105	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.65	136.41	-2.53	-0.35	14.7	83
    106	100028 SER B, 100093 ARG B, 200082 TYR C	3.58	136.79	-2.2	-0.09	18.43	83
    107	100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C	3.5	137.24	-2.78	-0.18	26.82	83
    108	100028 SER B, 200093 ARG B, 200082 TYR C	3.28	139.27	-2.2	-0.09	18.43	83
    109	200027 GLN B, 100028 SER B, 200093 ARG B	3.16	144.42	-2.93	-0.83	19.07	94
    110	200027 GLN B, 100028 SER B, 200093 ARG B, 200028 SER B	3.77	144.86	-2.3	-0.82	15.15	94
    111	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	3.99	145.08	-2.4	-0.87	14.72	100
    112	200027 GLN B, 200028 SER B, 200093 ARG B	4.22	145.43	-2.93	-0.83	19.07	94
    113	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.94	145.92	-2.4	-0.87	14.72	100
    114	200027 GLN B, 200028 SER B, 100028 SER B	5.36	149.53	-1.7	-1.01	2.29	106
    115	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.43	150.46	-2.05	-0.99	3.03	95
    116	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6.24	151.61	-2.05	-0.99	3.03	95
    117	100027 GLN B, 200027 GLN B, 100028 SER B	5.9	152.29	-2.6	-1.06	2.91	95
    118	200027 GLN B, 100028 SER B, 200026 SER B	5.51	152.94	-1.57	-0.96	2.86	100
    119	200027 GLN B, 100028 SER B, 200026 SER B, 100069 THR B	4.14	155.6	-1.35	-0.91	2.56	102
    120	200027 GLN B, 100028 SER B, 200026 SER B, 100027 GLN B	5.1	155.81	-1.28	-0.92	2.99	100
    121	100026 SER B, 100028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.51	158.74	-0.46	-0.79	3.04	107
    122	100026 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.38	159.68	-0.48	-0.79	2.95	107
    123	100026 SER B, 200026 SER B, 100069 THR B	4.32	161.57	-0.5	-0.79	2.81	107
    124	100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B	4.64	162.84	-1.5	-0.7	15.11	95
    125	200026 SER B, 100069 THR B, 100024 ARG B	4.39	164.56	-1.87	-0.66	19.01	95
    126	200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B	3.71	165.77	-2.28	-0.76	26.69	92
    127	200026 SER B, 100024 ARG B, 100070 ASP B	3.59	166.51	-2.8	-0.75	35.03	84
    128	100024 ARG B, 100070 ASP B, 200026 SER B	3.22	168.58	-2.93	-0.81	34.46	95
    129	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.46	170.38	-1.25	-0.32	25.88	85
    130	100070 ASP B, 200026 SER B, 200003 LEU B	2.09	173.4	-0.17	-0.29	17.17	85
    131	100070 ASP B, 200003 LEU B	2.29	175.95	0.15	0.05	24.92	70
    132	100070 ASP B, 200003 LEU B, 200001 ASP B	3.03	177.91	-0.03	-0.23	17.74	70
    133	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	3.83	178.86	-0.98	-0.43	25.3	83
    134	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	4.19	179.08	-1.56	-0.42	30.14	81
    135	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.99	180.32	-1.08	-0.27	25.25	79
    136	200003 LEU B, 200001 ASP B, 200063 LYS A	3.67	182.13	-1.2	-0.1	33.11	70
    137	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.53	183.98	-1.08	-0.27	25.25	79
    138	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A	3.63	184.38	-1.08	-0.2	13.67	84
    139	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B	3.72	185.17	-0.94	-0.32	11.61	84
    140	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.07	185.36	-2.4	-0.78	21.56	90
    141	200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.19	185.93	-2.03	-0.87	14.58	96
    142	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.48	186.67	-2.4	-0.78	21.56	90
    143	200003 LEU B, 200063 LYS A, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.54	187.7	-1.5	-0.4	21.26	76
    144	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	4.57	188.86	-1	-0.3	25.73	67
    145	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	4.47	191.42	0.23	0.35	24.92	76
    146	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	4.29	192.26	-1.1	-0.35	25.3	80
    147	200063 LYS A, 200046 GLU A, 200064 ILE A, 100020 SER B	4.19	193.02	-0.93	-0.18	25.3	92
    148	200063 LYS A, 200046 GLU A, 200064 ILE A	3.81	197.71	-0.97	0.09	33.18	84
    149	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.74	200.93	-0.98	-0.14	26.35	87
    150	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.58	204.2	-2	-0.04	38.51	86
    151	200046 GLU A, 100018 ARG B, 200040 ARG A	3.91	206.96	-4.17	-0.66	51.3	81
    152	200046 GLU A, 200064 ILE A, 200040 ARG A	4.12	207.47	-1.17	0.08	34.01	87
    153	200046 GLU A, 200040 ARG A	2.19	210.96	-4	-0.78	50.95	80
    154	200040 ARG A	0.21	217.1	-4.5	-0.42	52	83
    155	200040 ARG A, 200088 SER A	0.25	217.87	-2.45	-0.61	27.69	83
    156	200040 ARG A, 200088 SER A, 200091 SER A	0.5	218.28	-1.77	-0.67	19.59	83
    157	200040 ARG A, 200088 SER A, 200091 SER A	0.92	218.51	-1.9	-0.73	19.02	100
    158	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	1.45	218.78	-1.83	-0.57	14.66	86
    159	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.05	219.53	-1.73	-0.53	15.09	70
    160	200040 ARG A, 200088 SER A, 200041 PRO A	3.24	222.04	-2.17	-0.44	18.99	70
    161	200040 ARG A, 200041 PRO A, 200088 SER A	4.9	224.17	-2.3	-0.49	18.42	86
    162	200041 PRO A, 200088 SER A	4.86	225.09	-1.2	-0.53	1.63	87
    163	200091 SER A, 200041 PRO A, 200088 SER A	4.55	226.03	-1.07	-0.68	1.64	97
    164	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.42	226.42	0.15	-0.22	1.26	86
    165	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.23	226.95	0.02	0.3	1.25	69
    166	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.16	227.13	0.23	0.08	1.27	84
    167	200091 SER A, 200088 SER A, 200180 TYR A	4.08	227.33	-0.97	-0.28	1.65	94
    168	200091 SER A, 200088 SER A	4.07	227.57	-0.8	-0.97	1.67	117
    169	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.07	228.08	0.23	0.08	1.27	84
    170	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.09	228.85	-0.06	0.08	1.67	69
    171	200041 PRO A, 200175 LEU A, 200180 TYR A	4.12	233.23	0.3	0.72	1.11	54
    172	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.33	233.51	0.13	0.34	1.68	54
    173	200041 PRO A, 200175 LEU A, 200180 TYR A	4.42	234.21	0.3	0.72	1.11	54
    174	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.1	234.8	0.13	0.34	1.68	54
    175	200041 PRO A, 200180 TYR A, 200173 ALA A	3.66	237.01	-1.1	0.07	2.19	54
    176	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.39	239.27	-1.7	-0.23	14.12	61
    177	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.4	241.37	-1.78	-0.53	14.11	64
    178	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.45	241.92	-2.55	-0.52	14.11	74
    179	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.18	242.54	-2.55	-0.52	14.11	74
    180	200153 GLU A, 200172 PRO A, 200041 ASN B	3.01	242.94	-2.87	-0.67	18.29	79
    181	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.4	246.36	-2.25	-0.7	14.56	79
    182	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.42	246.87	-1.95	-0.88	15.01	90
    183	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A	2.47	247.26	-1.64	-0.86	12.68	90
    184	200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.52	247.66	-0.8	-0.47	12.03	78
    185	200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.64	248.56	-0.13	-0.31	2.57	79
    186	200041 ASN B, 200171 PHE A, 200182 LEU A	2.76	248.75	-0.03	-0.14	2.3	79
    187	200041 ASN B, 200182 LEU A, 200170 THR A	2.78	249.03	-0.13	-0.13	1.72	88
    188	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.69	250.61	-0.2	-0.3	2.14	88
    189	200041 ASN B, 200170 THR A, 200155 VAL A	2.8	254.19	-1.53	-0.78	2.81	105
    190	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.17	254.4	-1.33	-0.78	2.52	106
    191	200041 ASN B, 200156 THR A, 200157 VAL A	3.21	254.68	-1.53	-0.78	2.81	105
    192	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.21	254.84	-1.33	-0.78	2.52	106
    193	200041 ASN B, 200170 THR A, 200157 VAL A	3.19	254.95	-1.53	-0.78	2.81	105
    194	200041 ASN B, 200170 THR A, 200155 VAL A	3.17	255.18	-1.53	-0.78	2.81	105
    195	200041 ASN B, 200170 THR A, 200157 VAL A	3.24	255.35	-1.53	-0.78	2.81	105
    196	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.18	255.74	-1.33	-0.78	2.52	106
    197	200041 ASN B, 200170 THR A, 200157 VAL A	3.21	255.89	-1.53	-0.78	2.81	105
    198	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.27	256.6	-1.33	-0.78	2.52	106
    199	200041 ASN B, 200156 THR A, 200157 VAL A	3.46	259.11	-1.53	-0.78	2.81	105
    200	200041 ASN B, 200156 THR A, 200157 VAL A, 200040 THR B	4.05	259.11	-1.25	-0.79	2.95	105

    pore with bottle neck

    pore with local minimum

16. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 200028 SER B, 69 THR B, 27 GLN B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300002 ILE B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300157 VAL A, 300156 THR A, 300040 THR B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 3 (12-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 14.62
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.24	0.13	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.2	1.95	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.31	4.01	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.6	4.22	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.63	4.79	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.68	4.94	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.64	5.44	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.56	6.45	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.49	7.25	-2.55	-0.52	14.11	74
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.44	7.84	-2.55	-0.52	14.11	74
    11	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.26	10.32	-1.78	-0.53	14.11	64
    12	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.29	12.17	-1.7	-0.23	14.12	61
    13	100041 PRO A, 100173 ALA A, 100180 TYR A	3.78	14.16	-1.1	0.07	2.19	54
    14	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.44	14.68	0.13	0.34	1.68	54
    15	100041 PRO A, 100180 TYR A, 100175 LEU A	4.39	15.35	0.3	0.72	1.11	54
    16	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.39	15.69	0.13	0.34	1.68	54
    17	100041 PRO A, 100180 TYR A, 100175 LEU A	4.02	20.24	0.3	0.72	1.11	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.02	20.89	-0.06	0.08	1.67	69
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.03	21.28	0.02	0.3	1.25	69
    20	100180 TYR A, 100091 SER A, 100088 SER A	4.07	21.46	-0.97	-0.28	1.65	94
    21	100091 SER A, 100088 SER A	4.11	21.52	-0.8	-0.97	1.67	117
    22	100180 TYR A, 100091 SER A, 100088 SER A	4.17	21.83	-0.97	-0.28	1.65	94
    23	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.3	22.05	0.23	0.08	1.27	84
    24	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.37	22.7	0.02	0.3	1.25	69
    25	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.53	23.13	0.15	-0.22	1.26	86
    26	100041 PRO A, 100091 SER A, 100088 SER A	4.62	24.06	-1.07	-0.68	1.64	97
    27	100041 PRO A, 100088 SER A	4.82	25.14	-1.2	-0.53	1.63	87
    28	100041 PRO A, 100088 SER A, 100040 ARG A	4.8	27.6	-2.3	-0.49	18.42	86
    29	100041 PRO A, 100088 SER A, 100040 ARG A	3.35	29.71	-2.17	-0.44	18.99	70
    30	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.3	30.33	-1.73	-0.53	15.09	70
    31	100088 SER A, 100040 ARG A, 100091 SER A	0.78	31.49	-1.77	-0.67	19.59	83
    32	100088 SER A, 100040 ARG A	0.46	32.45	-2.45	-0.61	27.69	83
    33	100040 ARG A	0.3	39.24	-4.5	-0.42	52	83
    34	100040 ARG A, 100043 HIS A	2.11	40.21	-3.85	-0.08	51.8	87
    35	100040 ARG A, 100046 GLU A	2.69	43.39	-4	-0.78	50.95	80
    36	100040 ARG A, 100046 GLU A, 300018 ARG B	3.76	45.99	-4.17	-0.66	51.3	81
    37	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.49	49.55	-2	-0.04	38.51	86
    38	100046 GLU A, 300018 ARG B, 100064 ILE A	3.9	50.12	-1.17	0.08	34.01	87
    39	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.64	52.68	-0.98	-0.14	26.35	87
    40	100046 GLU A, 100064 ILE A, 100063 LYS A	3.47	53.45	0.2	-0.04	17.8	90
    41	100046 GLU A, 100064 ILE A, 100063 LYS A	3.17	58.39	-0.97	0.09	33.18	84
    42	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	5.01	59.12	-1.1	-0.35	25.3	80
    43	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.24	63.04	0.23	0.35	24.92	76
    44	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.93	63.91	-1	-0.3	25.73	67
    45	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.6	64.46	-1.5	-0.4	21.26	76
    46	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.26	64.71	-2.4	-0.78	21.56	90
    47	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.67	65.05	-2.03	-0.87	14.58	96
    48	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.62	65.26	-2.4	-0.78	21.56	90
    49	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.62	66.2	-0.94	-0.32	11.61	84
    50	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.73	66.61	-1.08	-0.2	13.67	84
    51	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.75	67.03	-0.3	-0.21	13.67	77
    52	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.72	68.48	-1.08	-0.27	25.25	79
    53	100063 LYS A, 100003 LEU B, 100001 ASP B	3.7	70.19	-1.2	-0.1	33.11	70
    54	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.74	71.2	-1.08	-0.27	25.25	79
    55	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.92	71.4	-1.56	-0.42	30.14	81
    56	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.97	72.39	-0.98	-0.43	25.3	83
    57	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.9	72.55	-0.2	-0.37	13.72	82
    58	100003 LEU B, 300070 ASP B, 100001 ASP B	3.04	74.73	-0.03	-0.23	17.74	70
    59	100003 LEU B, 300070 ASP B	2.11	77.72	0.15	0.05	24.92	70
    60	100003 LEU B, 300070 ASP B, 100026 SER B	2.07	80.07	-0.17	-0.29	17.17	85
    61	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.44	82.17	-1.25	-0.32	25.88	85
    62	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	83.7	-2.93	-0.81	34.46	95
    63	300070 ASP B, 300024 ARG B, 100026 SER B	3.65	84.58	-2.8	-0.75	35.03	84
    64	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.68	86.45	-2.28	-0.76	26.69	92
    65	300024 ARG B, 100026 SER B, 300069 THR B	4.39	87.86	-1.87	-0.66	19.01	95
    66	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.86	88.61	-1.5	-0.7	15.11	95
    67	100026 SER B, 300069 THR B, 300026 SER B	4.31	91.26	-0.5	-0.79	2.81	107
    68	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.34	92.17	-0.48	-0.79	2.95	107
    69	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.45	94.51	-0.46	-0.79	3.04	107
    70	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.08	94.65	-0.58	-0.84	2.52	112
    71	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.11	94.8	-1.28	-0.92	2.99	100
    72	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.17	97.83	-1.35	-0.91	2.56	102
    73	100026 SER B, 300028 SER B, 100027 GLN B	5.39	98.48	-1.57	-0.96	2.86	100
    74	300028 SER B, 100027 GLN B, 300027 GLN B	5.73	99.09	-2.6	-1.06	2.91	95
    75	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	6.05	99.98	-2.05	-0.99	3.03	95
    76	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.52	100.83	-2.05	-0.99	3.03	95
    77	300028 SER B, 100027 GLN B, 100028 SER B	5.24	104.34	-1.7	-1.01	2.29	106
    78	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.75	104.89	-2.4	-0.87	14.72	100
    79	100027 GLN B, 100028 SER B, 100093 ARG B	4.66	105.29	-2.93	-0.83	19.07	94
    80	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.5	106.25	-2.4	-0.87	14.72	100
    81	300028 SER B, 100027 GLN B, 100093 ARG B	2.49	111.91	-2.93	-0.83	19.07	94
    82	300028 SER B, 100093 ARG B, 100082 TYR C	2.72	113.47	-2.2	-0.09	18.43	83
    83	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.48	113.83	-2.78	-0.18	26.82	83
    84	300028 SER B, 100082 TYR C, 300093 ARG B	3.71	114.16	-2.2	-0.09	18.43	83
    85	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.86	114.97	-2.53	-0.35	14.7	83
    86	300028 SER B, 300093 ARG B, 300058 GLN C	3.56	115.26	-2.93	-0.83	19.07	94
    87	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.47	115.89	-2.53	-0.35	14.7	83
    88	100082 TYR C, 300093 ARG B, 300058 GLN C	3.49	116.81	-3.1	-0.14	19.05	72
    89	100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C	3.73	116.99	-2.43	-0.3	15.13	72
    90	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.81	118.18	-2.43	-0.3	15.13	72
    91	300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C	3.59	118.85	-2.2	-0.78	15.57	83
    92	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.43	122.45	-2.43	-0.3	15.13	72
    93	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	4.71	123.37	-1.88	0.25	14.65	61
    94	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	5.21	124.7	-1.58	0.04	12.4	61
    95	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.13	125.08	-2.4	0.12	22.12	66
    96	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.71	125.59	-2.4	0.12	22.12	66
    97	79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C	6.75	125.88	-2.22	-0.27	22.47	72
    98	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.45	126.58	-2.22	-0.27	22.47	72
    99	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.06	127.4	-2.3	-0.3	22.13	83
    100	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	4.06	130.34	-2.78	-0.18	26.82	83
    101	300093 ARG B, 300082 TYR C, 28 SER B	2.88	132.23	-2.2	-0.09	18.43	83
    102	300093 ARG B, 28 SER B	2.6	132.94	-2.65	-0.7	26.84	100
    103	300027 GLN B, 300093 ARG B, 28 SER B	2.44	137.35	-2.93	-0.83	19.07	94
    104	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.42	137.89	-2.3	-0.82	15.15	94
    105	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.69	138.41	-2.4	-0.87	14.72	100
    106	300028 SER B, 300027 GLN B, 300093 ARG B	4.85	138.73	-2.93	-0.83	19.07	94
    107	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.83	139.19	-2.4	-0.87	14.72	100
    108	300028 SER B, 300027 GLN B, 28 SER B	4.93	143	-1.7	-1.01	2.29	106
    109	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6.37	143.91	-2.05	-0.99	3.03	95
    110	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.93	145.05	-2.05	-0.99	3.03	95
    111	300027 GLN B, 27 GLN B, 28 SER B	5.65	145.7	-2.6	-1.06	2.91	95
    112	300026 SER B, 300027 GLN B, 28 SER B	5.35	146.31	-1.57	-0.96	2.86	100
    113	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.21	148.85	-1.35	-0.91	2.56	102
    114	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	5.12	149	-1.28	-0.92	2.99	100
    115	300026 SER B, 28 SER B, 69 THR B, 27 GLN B	5.13	149.29	-0.58	-0.84	2.52	112
    116	300026 SER B, 28 SER B, 69 THR B, 27 GLN B, 26 SER B	4.57	152.29	-0.46	-0.79	3.04	107
    117	300026 SER B, 69 THR B, 27 GLN B, 26 SER B	4.43	153.17	-0.48	-0.79	2.95	107
    118	300026 SER B, 69 THR B, 26 SER B	4.36	154.9	-0.5	-0.79	2.81	107
    119	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.64	156.03	-1.5	-0.7	15.11	95
    120	300026 SER B, 69 THR B, 24 ARG B	4.46	157.64	-1.87	-0.66	19.01	95
    121	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.77	158.93	-2.28	-0.76	26.69	92
    122	300026 SER B, 24 ARG B, 70 ASP B	3.61	159.83	-2.8	-0.75	35.03	84
    123	24 ARG B, 70 ASP B, 300026 SER B	3.25	161.77	-2.93	-0.81	34.46	95
    124	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.42	163.93	-1.25	-0.32	25.88	85
    125	70 ASP B, 300026 SER B, 300003 LEU B	2.1	166.29	-0.17	-0.29	17.17	85
    126	70 ASP B, 300003 LEU B	2.13	169.22	0.15	0.05	24.92	70
    127	70 ASP B, 300003 LEU B, 300001 ASP B	3.05	171.11	-0.03	-0.23	17.74	70
    128	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.87	171.24	-0.2	-0.37	13.72	82
    129	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.95	172.11	-0.98	-0.43	25.3	83
    130	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.9	172.55	-1.56	-0.42	30.14	81
    131	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.68	173.88	-1.08	-0.27	25.25	79
    132	300003 LEU B, 300001 ASP B, 300063 LYS A	3.64	175.59	-1.2	-0.1	33.11	70
    133	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.71	176.91	-1.08	-0.27	25.25	79
    134	300003 LEU B, 300063 LYS A, 300097 THR B, 300002 ILE B	3.84	177.32	-0.3	-0.21	13.67	77
    135	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.85	177.7	-1.08	-0.2	13.67	84
    136	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	3.71	178.46	-0.94	-0.32	11.61	84
    137	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	3.68	178.65	-2.4	-0.78	21.56	90
    138	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	3.68	179.06	-2.03	-0.87	14.58	96
    139	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.19	179.63	-2.4	-0.78	21.56	90
    140	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.54	180.52	-1.5	-0.4	21.26	76
    141	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	4.92	181.58	-1	-0.3	25.73	67
    142	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	5.3	184.81	0.23	0.35	24.92	76
    143	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	5.35	185.71	-1.1	-0.35	25.3	80
    144	300063 LYS A, 300046 GLU A, 300064 ILE A	2.98	190.86	-0.97	0.09	33.18	84
    145	300046 GLU A, 300064 ILE A, 300063 LYS A	3.24	191.6	0.2	-0.04	17.8	90
    146	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.43	193.98	-0.98	-0.14	26.35	87
    147	300046 GLU A, 300064 ILE A, 18 ARG B	3.85	194.53	-1.17	0.08	34.01	87
    148	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.54	197.51	-2	-0.04	38.51	86
    149	300046 GLU A, 18 ARG B, 300040 ARG A	3.95	200.14	-4.17	-0.66	51.3	81
    150	300046 GLU A, 300064 ILE A, 300040 ARG A	3.92	201.17	-1.17	0.08	34.01	87
    151	300046 GLU A, 300040 ARG A	2.92	203.41	-4	-0.78	50.95	80
    152	300040 ARG A	0.71	210.6	-4.5	-0.42	52	83
    153	300040 ARG A, 300088 SER A	0.73	211.26	-2.45	-0.61	27.69	83
    154	300040 ARG A, 300088 SER A, 300091 SER A	0.92	211.62	-1.77	-0.67	19.59	83
    155	300040 ARG A, 300088 SER A, 300091 SER A	1.24	211.84	-1.9	-0.73	19.02	100
    156	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	1.66	212.09	-1.83	-0.57	14.66	86
    157	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.15	212.8	-1.73	-0.53	15.09	70
    158	300040 ARG A, 300088 SER A, 300041 PRO A	3.17	215.17	-2.17	-0.44	18.99	70
    159	300040 ARG A, 300041 PRO A, 300088 SER A	4.77	217.25	-2.3	-0.49	18.42	86
    160	300041 PRO A, 300088 SER A	4.8	218.5	-1.2	-0.53	1.63	87
    161	300091 SER A, 300041 PRO A, 300088 SER A	4.55	219.39	-1.07	-0.68	1.64	97
    162	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.46	219.76	0.15	-0.22	1.26	86
    163	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.3	220.25	0.02	0.3	1.25	69
    164	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.24	220.43	0.23	0.08	1.27	84
    165	300091 SER A, 300088 SER A, 300180 TYR A	4.13	220.62	-0.97	-0.28	1.65	94
    166	300091 SER A, 300088 SER A	4.08	220.81	-0.8	-0.97	1.67	117
    167	300091 SER A, 300088 SER A, 300180 TYR A	4.04	221.21	-0.97	-0.28	1.65	94
    168	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.02	221.87	0.02	0.3	1.25	69
    169	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.01	222.71	-0.06	0.08	1.67	69
    170	300041 PRO A, 300175 LEU A, 300180 TYR A	4.01	226.59	0.3	0.72	1.11	54
    171	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.36	226.85	0.13	0.34	1.68	54
    172	300041 PRO A, 300175 LEU A, 300180 TYR A	4.41	227.5	0.3	0.72	1.11	54
    173	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.44	228.31	0.13	0.34	1.68	54
    174	300041 PRO A, 300180 TYR A, 300173 ALA A	3.8	230.46	-1.1	0.07	2.19	54
    175	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.29	232.18	-1.7	-0.23	14.12	61
    176	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.27	234.59	-1.78	-0.53	14.11	64
    177	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.41	235.13	-2.55	-0.52	14.11	74
    178	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.31	235.67	-2.55	-0.52	14.11	74
    179	300153 GLU A, 300172 PRO A, 300041 ASN B	3.12	236.42	-2.87	-0.67	18.29	79
    180	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.43	239.73	-2.25	-0.7	14.56	79
    181	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.39	240.21	-1.95	-0.88	15.01	90
    182	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.39	240.57	-0.8	-0.47	12.03	78
    183	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.41	240.97	-0.8	-0.47	12.03	78
    184	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.59	241.75	-0.13	-0.31	2.57	79
    185	300041 ASN B, 300182 LEU A, 300171 PHE A	2.75	242.11	-0.03	-0.14	2.3	79
    186	300041 ASN B, 300182 LEU A, 300170 THR A	2.78	242.36	-0.13	-0.13	1.72	88
    187	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.53	243.76	-0.2	-0.3	2.14	88
    188	300041 ASN B, 300170 THR A, 300155 VAL A	2.53	247.32	-1.53	-0.78	2.81	105
    189	300041 ASN B, 300170 THR A, 300155 VAL A, 300157 VAL A	2.93	247.63	-1.25	-0.79	2.95	105
    190	300041 ASN B, 300157 VAL A, 300156 THR A	3.03	247.89	-1.53	-0.78	2.81	105
    191	300041 ASN B, 300170 THR A, 300157 VAL A, 300156 THR A	3.19	248.19	-1.33	-0.78	2.52	106
    192	300041 ASN B, 300170 THR A, 300157 VAL A	3.2	248.28	-1.53	-0.78	2.81	105
    193	300041 ASN B, 300170 THR A, 300155 VAL A	3.17	248.49	-1.53	-0.78	2.81	105
    194	300041 ASN B, 300170 THR A, 300157 VAL A	3.22	248.66	-1.53	-0.78	2.81	105
    195	300041 ASN B, 300170 THR A, 300157 VAL A, 300156 THR A	3.19	249.09	-1.33	-0.78	2.52	106
    196	300170 THR A, 300157 VAL A, 300156 THR A	3.22	249.27	-0.6	-0.78	2.23	107
    197	300041 ASN B, 300170 THR A, 300157 VAL A, 300156 THR A	3.28	249.58	-1.33	-0.78	2.52	106
    198	300041 ASN B, 300157 VAL A, 300156 THR A	3.37	252.43	-1.53	-0.78	2.81	105
    199	300041 ASN B, 300157 VAL A, 300156 THR A, 300040 THR B	4.05	252.43	-1.25	-0.79	2.95	105

    pore with bottle neck

    pore with local minimum

17. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100079 GLY C, 28 SER B, 200028 SER B, 69 THR B, 27 GLN B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 4 (12-8)
    Hydropathy: -1.4
    Hydrophobicity: -0.43
    Polarity: 14.35
    Mutability: 86
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.26	0.27	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.45	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.19	0.62	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.77	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.19	1.05	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.04	1.59	-1.53	-0.78	2.81	105
    7	100170 THR A, 100041 ASN B, 100155 VAL A	2.62	5.8	-1.53	-0.78	2.81	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.61	6.54	-0.2	-0.3	2.14	88
    9	100170 THR A, 100041 ASN B, 100182 LEU A	2.8	6.87	-0.13	-0.13	1.72	88
    10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.23	-0.03	-0.14	2.3	79
    11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.57	7.96	-0.13	-0.31	2.57	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.4	8.49	-0.8	-0.47	12.03	78
    13	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.32	8.97	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.26	9.54	-1.95	-0.88	15.01	90
    15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.24	12.84	-2.25	-0.7	14.56	79
    16	100041 ASN B, 100153 GLU A, 100172 PRO A	3.13	13.2	-2.87	-0.67	18.29	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.33	13.76	-2.55	-0.52	14.11	74
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.6	14.67	-2.55	-0.52	14.11	74
    19	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.4	16.96	-1.78	-0.53	14.11	64
    20	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.35	18.88	-1.7	-0.23	14.12	61
    21	100173 ALA A, 100041 PRO A, 100180 TYR A	3.49	20.95	-1.1	0.07	2.19	54
    22	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.09	21.36	0.13	0.34	1.68	54
    23	100041 PRO A, 100180 TYR A, 100175 LEU A	4.38	22.07	0.3	0.72	1.11	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.4	22.43	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.3	27.21	0.3	0.72	1.11	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.26	27.8	-0.06	0.08	1.67	69
    27	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.22	28.12	0.23	0.08	1.27	84
    28	100180 TYR A, 100091 SER A, 100088 SER A	4.18	28.23	-0.97	-0.28	1.65	94
    29	100091 SER A, 100088 SER A	4.17	28.32	-0.8	-0.97	1.67	117
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.17	28.49	-0.97	-0.28	1.65	94
    31	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.2	28.97	0.23	0.08	1.27	84
    32	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.32	29.34	0.02	0.3	1.25	69
    33	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	29.78	0.15	-0.22	1.26	86
    34	100041 PRO A, 100091 SER A, 100088 SER A	4.58	30.75	-1.07	-0.68	1.64	97
    35	100041 PRO A, 100088 SER A	4.94	31.89	-1.2	-0.53	1.63	87
    36	100041 PRO A, 100088 SER A, 100040 ARG A	4.51	33.93	-2.3	-0.49	18.42	86
    37	100041 PRO A, 100088 SER A, 100040 ARG A	3	36.29	-2.17	-0.44	18.99	70
    38	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.38	36.98	-1.73	-0.53	15.09	70
    39	100088 SER A, 100040 ARG A, 100091 SER A	1.85	38.11	-1.77	-0.67	19.59	83
    40	100088 SER A, 100040 ARG A	1.81	39.07	-2.45	-0.61	27.69	83
    41	100040 ARG A	1.85	44.91	-4.5	-0.42	52	83
    42	100040 ARG A, 100043 HIS A	2.59	46.14	-3.85	-0.08	51.8	87
    43	100040 ARG A, 100046 GLU A	2.83	50.39	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	3.68	52.52	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.55	56.4	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.66	59.77	-0.98	-0.14	26.35	87
    47	100046 GLU A, 100064 ILE A, 100063 LYS A	3.53	60.56	0.2	-0.04	17.8	90
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.32	65.06	-0.97	0.09	33.18	84
    49	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.51	65.41	-0.93	-0.18	25.3	92
    50	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.82	65.84	-1.1	-0.35	25.3	80
    51	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.06	69.97	0.23	0.35	24.92	76
    52	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.93	70.81	-1	-0.3	25.73	67
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.69	71.29	-1.5	-0.4	21.26	76
    54	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.43	71.46	-2.4	-0.78	21.56	90
    55	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.94	71.67	-2.03	-0.87	14.58	96
    56	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.75	71.89	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.48	72.8	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.46	73.23	-0.3	-0.21	13.67	77
    59	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.48	73.67	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.52	75.18	-1.08	-0.27	25.25	79
    61	100063 LYS A, 100003 LEU B, 100001 ASP B	3.77	76.98	-1.2	-0.1	33.11	70
    62	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	4.02	77.98	-1.08	-0.27	25.25	79
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.12	78.19	-1.56	-0.42	30.14	81
    64	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.9	79.1	-0.98	-0.43	25.3	83
    65	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.88	79.26	-0.2	-0.37	13.72	82
    66	100003 LEU B, 300070 ASP B, 100001 ASP B	2.99	81.27	-0.03	-0.23	17.74	70
    67	100003 LEU B, 300070 ASP B	2.24	84.4	0.15	0.05	24.92	70
    68	100003 LEU B, 300070 ASP B, 100026 SER B	2.18	86.87	-0.17	-0.29	17.17	85
    69	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.57	88.63	-1.25	-0.32	25.88	85
    70	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	90.42	-2.93	-0.81	34.46	95
    71	300070 ASP B, 300024 ARG B, 100026 SER B	3.57	91.33	-2.8	-0.75	35.03	84
    72	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.78	93.35	-2.28	-0.76	26.69	92
    73	300024 ARG B, 100026 SER B, 300069 THR B	4.66	94.39	-1.87	-0.66	19.01	95
    74	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.6	95.6	-1.5	-0.7	15.11	95
    75	100026 SER B, 300069 THR B, 300026 SER B	4.51	98.85	-0.5	-0.79	2.81	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.83	101.26	-0.46	-0.79	3.04	107
    77	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.05	101.57	-1.28	-0.92	2.99	100
    78	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.22	104.42	-1.35	-0.91	2.56	102
    79	100026 SER B, 100027 GLN B, 300028 SER B	5.35	105.1	-1.57	-0.96	2.86	100
    80	300027 GLN B, 100027 GLN B, 300028 SER B	5.66	105.75	-1.57	-0.96	2.86	100
    81	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.95	106.7	-2.05	-0.99	3.03	95
    82	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.41	107.65	-2.05	-0.99	3.03	95
    83	100027 GLN B, 300028 SER B, 100028 SER B	5.21	111.25	-1.7	-1.01	2.29	106
    84	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.75	111.57	-2.4	-0.87	14.72	100
    85	100027 GLN B, 100028 SER B, 100093 ARG B	4.4	111.97	-2.93	-0.83	19.07	94
    86	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.21	112.93	-2.4	-0.87	14.72	100
    87	100027 GLN B, 300028 SER B, 100093 ARG B	2.78	118.18	-2.93	-0.83	19.07	94
    88	300028 SER B, 100093 ARG B	2.79	118.9	-2.65	-0.7	26.84	100
    89	300028 SER B, 100093 ARG B, 100082 TYR C	2.88	120.4	-2.2	-0.09	18.43	83
    90	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.44	120.76	-2.78	-0.18	26.82	83
    91	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.64	121.67	-2.53	-0.35	14.7	83
    92	300028 SER B, 300093 ARG B, 300058 GLN C	3.82	121.98	-2.93	-0.83	19.07	94
    93	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.75	122.65	-2.53	-0.35	14.7	83
    94	100082 TYR C, 300093 ARG B, 300058 GLN C	3.76	123.6	-3.1	-0.14	19.05	72
    95	100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C	3.72	123.78	-2.43	-0.3	15.13	72
    96	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.36	125.17	-2.43	-0.3	15.13	72
    97	300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C	3.43	125.8	-2.2	-0.78	15.57	83
    98	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.78	129.31	-2.43	-0.3	15.13	72
    99	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	5.35	130.26	-1.88	0.25	14.65	61
    100	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	5.67	131.52	-1.58	0.04	12.4	61
    101	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.25	131.75	-2.4	0.12	22.12	66
    102	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.47	132.16	-2.4	0.12	22.12	66
    103	200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100079 GLY C	6.78	132.45	-1.58	0.04	12.4	61
    104	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.44	133.57	-2.22	-0.27	22.47	72
    105	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.21	134.01	-2.3	-0.3	22.13	83
    106	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	3.95	137.11	-2.78	-0.18	26.82	83
    107	300093 ARG B, 300082 TYR C, 28 SER B	3.25	139.15	-2.2	-0.09	18.43	83
    108	300093 ARG B, 28 SER B	3.13	139.88	-2.65	-0.7	26.84	100
    109	300027 GLN B, 300093 ARG B, 28 SER B	3.07	144.46	-2.93	-0.83	19.07	94
    110	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	3.84	144.88	-2.3	-0.82	15.15	94
    111	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.05	145.08	-2.4	-0.87	14.72	100
    112	300028 SER B, 300027 GLN B, 300093 ARG B	4.27	145.42	-2.93	-0.83	19.07	94
    113	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.94	145.92	-2.4	-0.87	14.72	100
    114	300028 SER B, 300027 GLN B, 28 SER B	5.35	149.53	-1.7	-1.01	2.29	106
    115	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6.44	150.46	-2.05	-0.99	3.03	95
    116	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.24	151.6	-2.05	-0.99	3.03	95
    117	300027 GLN B, 27 GLN B, 28 SER B	5.9	152.28	-2.6	-1.06	2.91	95
    118	300026 SER B, 300027 GLN B, 28 SER B	5.5	152.94	-1.57	-0.96	2.86	100
    119	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.14	155.6	-1.35	-0.91	2.56	102
    120	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	5.1	155.81	-1.28	-0.92	2.99	100
    121	300026 SER B, 28 SER B, 69 THR B, 27 GLN B, 26 SER B	4.51	158.73	-0.46	-0.79	3.04	107
    122	300026 SER B, 69 THR B, 27 GLN B, 26 SER B	4.38	159.68	-0.48	-0.79	2.95	107
    123	300026 SER B, 69 THR B, 26 SER B	4.32	161.57	-0.5	-0.79	2.81	107
    124	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.64	162.83	-1.5	-0.7	15.11	95
    125	300026 SER B, 69 THR B, 24 ARG B	4.39	164.56	-1.87	-0.66	19.01	95
    126	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.71	165.77	-2.28	-0.76	26.69	92
    127	300026 SER B, 24 ARG B, 70 ASP B	3.59	166.51	-2.8	-0.75	35.03	84
    128	24 ARG B, 70 ASP B, 300026 SER B	3.22	168.58	-2.93	-0.81	34.46	95
    129	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.46	170.38	-1.25	-0.32	25.88	85
    130	70 ASP B, 300026 SER B, 300003 LEU B	2.09	173.4	-0.17	-0.29	17.17	85
    131	70 ASP B, 300003 LEU B	2.29	175.94	0.15	0.05	24.92	70
    132	70 ASP B, 300003 LEU B, 300001 ASP B	3.03	177.91	-0.03	-0.23	17.74	70
    133	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.83	178.86	-0.98	-0.43	25.3	83
    134	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	4.19	179.08	-1.56	-0.42	30.14	81
    135	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.99	180.32	-1.08	-0.27	25.25	79
    136	300003 LEU B, 300001 ASP B, 300063 LYS A	3.67	182.13	-1.2	-0.1	33.11	70
    137	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.53	183.98	-1.08	-0.27	25.25	79
    138	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.63	184.38	-1.08	-0.2	13.67	84
    139	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	3.72	185.17	-0.94	-0.32	11.61	84
    140	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.07	185.36	-2.4	-0.78	21.56	90
    141	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.19	185.93	-2.03	-0.87	14.58	96
    142	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.48	186.67	-2.4	-0.78	21.56	90
    143	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.54	187.7	-1.5	-0.4	21.26	76
    144	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	4.57	188.86	-1	-0.3	25.73	67
    145	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	4.47	191.42	0.23	0.35	24.92	76
    146	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	4.29	192.26	-1.1	-0.35	25.3	80
    147	300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B	4.19	193.01	-0.93	-0.18	25.3	92
    148	300063 LYS A, 300046 GLU A, 300064 ILE A	3.81	197.71	-0.97	0.09	33.18	84
    149	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.74	200.92	-0.98	-0.14	26.35	87
    150	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.58	204.19	-2	-0.04	38.51	86
    151	300046 GLU A, 18 ARG B, 300040 ARG A	3.91	206.96	-4.17	-0.66	51.3	81
    152	300046 GLU A, 300064 ILE A, 300040 ARG A	4.12	207.47	-1.17	0.08	34.01	87
    153	300046 GLU A, 300040 ARG A	2.19	210.96	-4	-0.78	50.95	80
    154	300040 ARG A	0.21	217.1	-4.5	-0.42	52	83
    155	300040 ARG A, 300088 SER A	0.25	217.86	-2.45	-0.61	27.69	83
    156	300040 ARG A, 300088 SER A, 300091 SER A	0.5	218.27	-1.77	-0.67	19.59	83
    157	300040 ARG A, 300088 SER A, 300091 SER A	0.92	218.51	-1.9	-0.73	19.02	100
    158	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	1.45	218.78	-1.83	-0.57	14.66	86
    159	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.05	219.53	-1.73	-0.53	15.09	70
    160	300040 ARG A, 300088 SER A, 300041 PRO A	3.24	222.04	-2.17	-0.44	18.99	70
    161	300040 ARG A, 300041 PRO A, 300088 SER A	4.9	224.17	-2.3	-0.49	18.42	86
    162	300041 PRO A, 300088 SER A	4.86	225.08	-1.2	-0.53	1.63	87
    163	300091 SER A, 300041 PRO A, 300088 SER A	4.55	226.03	-1.07	-0.68	1.64	97
    164	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.42	226.42	0.15	-0.22	1.26	86
    165	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.23	226.95	0.02	0.3	1.25	69
    166	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.16	227.13	0.23	0.08	1.27	84
    167	300091 SER A, 300088 SER A, 300180 TYR A	4.08	227.32	-0.97	-0.28	1.65	94
    168	300091 SER A, 300088 SER A	4.07	227.57	-0.8	-0.97	1.67	117
    169	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.07	228.08	0.23	0.08	1.27	84
    170	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.09	228.85	-0.06	0.08	1.67	69
    171	300041 PRO A, 300175 LEU A, 300180 TYR A	4.12	233.23	0.3	0.72	1.11	54
    172	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.33	233.51	0.13	0.34	1.68	54
    173	300041 PRO A, 300175 LEU A, 300180 TYR A	4.42	234.21	0.3	0.72	1.11	54
    174	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.1	234.79	0.13	0.34	1.68	54
    175	300041 PRO A, 300180 TYR A, 300173 ALA A	3.66	237.01	-1.1	0.07	2.19	54
    176	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.39	239.27	-1.7	-0.23	14.12	61
    177	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.4	241.37	-1.78	-0.53	14.11	64
    178	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.45	241.92	-2.55	-0.52	14.11	74
    179	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.18	242.54	-2.55	-0.52	14.11	74
    180	300153 GLU A, 300172 PRO A, 300041 ASN B	3.01	242.93	-2.87	-0.67	18.29	79
    181	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.4	246.36	-2.25	-0.7	14.56	79
    182	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.42	246.87	-1.95	-0.88	15.01	90
    183	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A	2.47	247.26	-1.64	-0.86	12.68	90
    184	300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A	2.52	247.66	-0.8	-0.47	12.03	78
    185	300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A	2.64	248.56	-0.13	-0.31	2.57	79
    186	300041 ASN B, 300171 PHE A, 300182 LEU A	2.76	248.75	-0.03	-0.14	2.3	79
    187	300041 ASN B, 300182 LEU A, 300170 THR A	2.78	249.03	-0.13	-0.13	1.72	88
    188	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.69	250.61	-0.2	-0.3	2.14	88
    189	300041 ASN B, 300170 THR A, 300155 VAL A	2.8	254.19	-1.53	-0.78	2.81	105
    190	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.17	254.4	-1.33	-0.78	2.52	106
    191	300041 ASN B, 300156 THR A, 300157 VAL A	3.21	254.68	-1.53	-0.78	2.81	105
    192	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.21	254.84	-1.33	-0.78	2.52	106
    193	300041 ASN B, 300170 THR A, 300157 VAL A	3.19	254.95	-1.53	-0.78	2.81	105
    194	300041 ASN B, 300170 THR A, 300155 VAL A	3.17	255.18	-1.53	-0.78	2.81	105
    195	300041 ASN B, 300170 THR A, 300157 VAL A	3.24	255.35	-1.53	-0.78	2.81	105
    196	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.18	255.74	-1.33	-0.78	2.52	106
    197	300041 ASN B, 300170 THR A, 300157 VAL A	3.21	255.89	-1.53	-0.78	2.81	105
    198	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.27	256.6	-1.33	-0.78	2.52	106
    199	300041 ASN B, 300156 THR A, 300157 VAL A	3.46	259.11	-1.53	-0.78	2.81	105
    200	300041 ASN B, 300156 THR A, 300157 VAL A, 300040 THR B	4.05	259.11	-1.25	-0.79	2.95	105

    pore with bottle neck

    pore with local minimum

18. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200002 ILE B, 200061 ASN A, 200098 PHE B, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A, 200170 THR A, 200155 VAL A, 200157 VAL A, 200156 THR A, 200040 THR B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 3 (12-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 14.55
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.24	0.13	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.2	1.95	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.31	4.01	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.6	4.22	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.63	4.79	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.68	4.94	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.64	5.44	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.56	6.45	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.49	7.25	-2.55	-0.52	14.11	74
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.44	7.84	-2.55	-0.52	14.11	74
    11	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.26	10.32	-1.78	-0.53	14.11	64
    12	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.29	12.17	-1.7	-0.23	14.12	61
    13	100041 PRO A, 100173 ALA A, 100180 TYR A	3.78	14.16	-1.1	0.07	2.19	54
    14	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.44	14.68	0.13	0.34	1.68	54
    15	100041 PRO A, 100180 TYR A, 100175 LEU A	4.39	15.35	0.3	0.72	1.11	54
    16	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.39	15.69	0.13	0.34	1.68	54
    17	100041 PRO A, 100180 TYR A, 100175 LEU A	4.02	20.24	0.3	0.72	1.11	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.02	20.89	-0.06	0.08	1.67	69
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.03	21.28	0.02	0.3	1.25	69
    20	100180 TYR A, 100091 SER A, 100088 SER A	4.07	21.46	-0.97	-0.28	1.65	94
    21	100091 SER A, 100088 SER A	4.11	21.52	-0.8	-0.97	1.67	117
    22	100180 TYR A, 100091 SER A, 100088 SER A	4.17	21.83	-0.97	-0.28	1.65	94
    23	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.3	22.05	0.23	0.08	1.27	84
    24	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.37	22.7	0.02	0.3	1.25	69
    25	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.53	23.13	0.15	-0.22	1.26	86
    26	100041 PRO A, 100091 SER A, 100088 SER A	4.62	24.06	-1.07	-0.68	1.64	97
    27	100041 PRO A, 100088 SER A	4.82	25.14	-1.2	-0.53	1.63	87
    28	100041 PRO A, 100088 SER A, 100040 ARG A	4.8	27.6	-2.3	-0.49	18.42	86
    29	100041 PRO A, 100088 SER A, 100040 ARG A	3.35	29.71	-2.17	-0.44	18.99	70
    30	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.3	30.33	-1.73	-0.53	15.09	70
    31	100088 SER A, 100040 ARG A, 100091 SER A	0.78	31.49	-1.77	-0.67	19.59	83
    32	100088 SER A, 100040 ARG A	0.46	32.45	-2.45	-0.61	27.69	83
    33	100040 ARG A	0.3	39.24	-4.5	-0.42	52	83
    34	100040 ARG A, 100043 HIS A	2.11	40.21	-3.85	-0.08	51.8	87
    35	100040 ARG A, 100046 GLU A	2.69	43.39	-4	-0.78	50.95	80
    36	100040 ARG A, 100046 GLU A, 300018 ARG B	3.76	45.99	-4.17	-0.66	51.3	81
    37	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.49	49.55	-2	-0.04	38.51	86
    38	100046 GLU A, 300018 ARG B, 100064 ILE A	3.9	50.12	-1.17	0.08	34.01	87
    39	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.64	52.68	-0.98	-0.14	26.35	87
    40	100046 GLU A, 100064 ILE A, 100063 LYS A	3.47	53.45	0.2	-0.04	17.8	90
    41	100046 GLU A, 100064 ILE A, 100063 LYS A	3.17	58.39	-0.97	0.09	33.18	84
    42	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	5.01	59.12	-1.1	-0.35	25.3	80
    43	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.24	63.04	0.23	0.35	24.92	76
    44	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.93	63.91	-1	-0.3	25.73	67
    45	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.6	64.46	-1.5	-0.4	21.26	76
    46	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.26	64.71	-2.4	-0.78	21.56	90
    47	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.67	65.05	-2.03	-0.87	14.58	96
    48	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.62	65.26	-2.4	-0.78	21.56	90
    49	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.62	66.2	-0.94	-0.32	11.61	84
    50	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.73	66.61	-1.08	-0.2	13.67	84
    51	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.75	67.03	-0.3	-0.21	13.67	77
    52	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.72	68.48	-1.08	-0.27	25.25	79
    53	100063 LYS A, 100003 LEU B, 100001 ASP B	3.7	70.19	-1.2	-0.1	33.11	70
    54	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.74	71.2	-1.08	-0.27	25.25	79
    55	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.92	71.4	-1.56	-0.42	30.14	81
    56	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.97	72.39	-0.98	-0.43	25.3	83
    57	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.9	72.55	-0.2	-0.37	13.72	82
    58	100003 LEU B, 300070 ASP B, 100001 ASP B	3.04	74.73	-0.03	-0.23	17.74	70
    59	100003 LEU B, 300070 ASP B	2.11	77.72	0.15	0.05	24.92	70
    60	100003 LEU B, 300070 ASP B, 100026 SER B	2.07	80.07	-0.17	-0.29	17.17	85
    61	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.44	82.17	-1.25	-0.32	25.88	85
    62	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	83.7	-2.93	-0.81	34.46	95
    63	300070 ASP B, 300024 ARG B, 100026 SER B	3.65	84.58	-2.8	-0.75	35.03	84
    64	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.68	86.45	-2.28	-0.76	26.69	92
    65	300024 ARG B, 100026 SER B, 300069 THR B	4.39	87.86	-1.87	-0.66	19.01	95
    66	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.86	88.61	-1.5	-0.7	15.11	95
    67	100026 SER B, 300069 THR B, 300026 SER B	4.31	91.26	-0.5	-0.79	2.81	107
    68	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.34	92.17	-0.48	-0.79	2.95	107
    69	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.45	94.51	-0.46	-0.79	3.04	107
    70	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.08	94.65	-0.58	-0.84	2.52	112
    71	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.11	94.8	-1.28	-0.92	2.99	100
    72	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.17	97.84	-1.35	-0.91	2.56	102
    73	100026 SER B, 300028 SER B, 100027 GLN B	5.39	98.48	-1.57	-0.96	2.86	100
    74	300028 SER B, 100027 GLN B, 300027 GLN B	5.73	99.09	-2.6	-1.06	2.91	95
    75	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	6.05	99.98	-2.05	-0.99	3.03	95
    76	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.52	100.83	-2.05	-0.99	3.03	95
    77	300028 SER B, 100027 GLN B, 100028 SER B	5.01	104.63	-1.7	-1.01	2.29	106
    78	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.76	104.89	-2.4	-0.87	14.72	100
    79	100027 GLN B, 100028 SER B, 100093 ARG B	4.7	105.27	-2.93	-0.83	19.07	94
    80	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.54	106.19	-2.4	-0.87	14.72	100
    81	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.33	106.85	-2.3	-0.82	15.15	94
    82	300028 SER B, 100027 GLN B, 100093 ARG B	2.5	111.32	-2.93	-0.83	19.07	94
    83	300028 SER B, 100093 ARG B	2.62	112.02	-2.65	-0.7	26.84	100
    84	300028 SER B, 100093 ARG B, 100082 TYR C	2.87	113.62	-2.2	-0.09	18.43	83
    85	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.02	116.54	-2.78	-0.18	26.82	83
    86	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.1	117.31	-2.3	-0.3	22.13	83
    87	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.5	117.93	-2.22	-0.27	22.47	72
    88	300079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.84	118.17	-1.58	0.04	12.4	61
    89	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.91	118.52	-2.4	0.12	22.12	66
    90	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.41	119.39	-2.4	0.12	22.12	66
    91	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.45	121.11	-1.58	0.04	12.4	61
    92	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	4.9	122.07	-1.88	0.25	14.65	61
    93	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.28	124.99	-2.43	-0.3	15.13	72
    94	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.45	125.67	-2.2	-0.78	15.57	83
    95	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.77	126.7	-2.43	-0.3	15.13	72
    96	100093 ARG B, 200082 TYR C, 100058 GLN C	3.54	127.63	-3.1	-0.14	19.05	72
    97	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.49	127.88	-2.43	-0.3	15.13	72
    98	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.45	128.36	-2.53	-0.35	14.7	83
    99	100028 SER B, 100093 ARG B, 100058 GLN C	3.51	128.63	-2.93	-0.83	19.07	94
    100	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.87	129.69	-2.53	-0.35	14.7	83
    101	100028 SER B, 100093 ARG B, 200082 TYR C	3.8	130.05	-2.2	-0.09	18.43	83
    102	100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C	3.59	130.47	-2.78	-0.18	26.82	83
    103	100028 SER B, 200093 ARG B, 200082 TYR C	2.76	132.34	-2.2	-0.09	18.43	83
    104	200027 GLN B, 100028 SER B, 200093 ARG B	2.43	137.86	-2.93	-0.83	19.07	94
    105	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.67	138.4	-2.4	-0.87	14.72	100
    106	200027 GLN B, 200028 SER B, 200093 ARG B	4.83	138.73	-2.93	-0.83	19.07	94
    107	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.82	139.18	-2.4	-0.87	14.72	100
    108	200027 GLN B, 200028 SER B, 100028 SER B	4.93	142.99	-1.7	-1.01	2.29	106
    109	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.37	143.91	-2.05	-0.99	3.03	95
    110	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	5.93	145.05	-2.05	-0.99	3.03	95
    111	100027 GLN B, 200027 GLN B, 100028 SER B	5.65	145.7	-2.6	-1.06	2.91	95
    112	200027 GLN B, 100028 SER B, 200026 SER B	5.35	146.31	-1.57	-0.96	2.86	100
    113	200027 GLN B, 100028 SER B, 200026 SER B, 100069 THR B	4.21	148.85	-1.35	-0.91	2.56	102
    114	200027 GLN B, 100028 SER B, 200026 SER B, 100027 GLN B	5.12	149	-1.28	-0.92	2.99	100
    115	100028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	5.13	149.29	-0.58	-0.84	2.52	112
    116	100026 SER B, 100028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.57	152.29	-0.46	-0.79	3.04	107
    117	100026 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.43	153.17	-0.48	-0.79	2.95	107
    118	100026 SER B, 200026 SER B, 100069 THR B	4.36	154.9	-0.5	-0.79	2.81	107
    119	100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B	4.64	156.03	-1.5	-0.7	15.11	95
    120	200026 SER B, 100069 THR B, 100024 ARG B	4.46	157.64	-1.87	-0.66	19.01	95
    121	200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B	3.77	158.93	-2.28	-0.76	26.69	92
    122	200026 SER B, 100024 ARG B, 100070 ASP B	3.61	159.83	-2.8	-0.75	35.03	84
    123	100024 ARG B, 100070 ASP B, 200026 SER B	3.25	161.76	-2.93	-0.81	34.46	95
    124	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.42	163.93	-1.25	-0.32	25.88	85
    125	100070 ASP B, 200026 SER B, 200003 LEU B	2.1	166.29	-0.17	-0.29	17.17	85
    126	100070 ASP B, 200003 LEU B	2.13	169.22	0.15	0.05	24.92	70
    127	100070 ASP B, 200003 LEU B, 200001 ASP B	3.05	171.11	-0.03	-0.23	17.74	70
    128	100070 ASP B, 200003 LEU B, 200001 ASP B, 100072 THR B	3.87	171.24	-0.2	-0.37	13.72	82
    129	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	3.95	172.11	-0.98	-0.43	25.3	83
    130	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.9	172.54	-1.56	-0.42	30.14	81
    131	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.68	173.87	-1.08	-0.27	25.25	79
    132	200003 LEU B, 200001 ASP B, 200063 LYS A	3.64	175.58	-1.2	-0.1	33.11	70
    133	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.71	176.91	-1.08	-0.27	25.25	79
    134	200003 LEU B, 200063 LYS A, 200097 THR B, 200002 ILE B	3.84	177.32	-0.3	-0.21	13.67	77
    135	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A	3.85	177.69	-1.08	-0.2	13.67	84
    136	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B	3.71	178.46	-0.94	-0.32	11.61	84
    137	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	3.68	178.65	-2.4	-0.78	21.56	90
    138	200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	3.68	179.06	-2.03	-0.87	14.58	96
    139	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.19	179.63	-2.4	-0.78	21.56	90
    140	200003 LEU B, 200063 LYS A, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.54	180.52	-1.5	-0.4	21.26	76
    141	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	4.92	181.58	-1	-0.3	25.73	67
    142	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	5.3	184.81	0.23	0.35	24.92	76
    143	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	5.35	185.71	-1.1	-0.35	25.3	80
    144	200063 LYS A, 200046 GLU A, 200064 ILE A	2.98	190.86	-0.97	0.09	33.18	84
    145	200046 GLU A, 200064 ILE A, 200063 LYS A	3.24	191.6	0.2	-0.04	17.8	90
    146	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.43	193.98	-0.98	-0.14	26.35	87
    147	200046 GLU A, 200064 ILE A, 100018 ARG B	3.85	194.52	-1.17	0.08	34.01	87
    148	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.54	197.5	-2	-0.04	38.51	86
    149	200046 GLU A, 100018 ARG B, 200040 ARG A	3.95	200.13	-4.17	-0.66	51.3	81
    150	200046 GLU A, 200064 ILE A, 200040 ARG A	3.92	201.17	-1.17	0.08	34.01	87
    151	200046 GLU A, 200040 ARG A	2.92	203.4	-4	-0.78	50.95	80
    152	200040 ARG A	0.71	210.6	-4.5	-0.42	52	83
    153	200040 ARG A, 200088 SER A	0.73	211.26	-2.45	-0.61	27.69	83
    154	200040 ARG A, 200088 SER A, 200091 SER A	0.92	211.61	-1.77	-0.67	19.59	83
    155	200040 ARG A, 200088 SER A, 200091 SER A	1.24	211.84	-1.9	-0.73	19.02	100
    156	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	1.66	212.09	-1.83	-0.57	14.66	86
    157	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.15	212.8	-1.73	-0.53	15.09	70
    158	200040 ARG A, 200088 SER A, 200041 PRO A	3.17	215.17	-2.17	-0.44	18.99	70
    159	200040 ARG A, 200041 PRO A, 200088 SER A	4.77	217.24	-2.3	-0.49	18.42	86
    160	200041 PRO A, 200088 SER A	4.8	218.5	-1.2	-0.53	1.63	87
    161	200091 SER A, 200041 PRO A, 200088 SER A	4.55	219.39	-1.07	-0.68	1.64	97
    162	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.46	219.75	0.15	-0.22	1.26	86
    163	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.3	220.25	0.02	0.3	1.25	69
    164	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.24	220.43	0.23	0.08	1.27	84
    165	200091 SER A, 200088 SER A, 200180 TYR A	4.13	220.62	-0.97	-0.28	1.65	94
    166	200091 SER A, 200088 SER A	4.08	220.8	-0.8	-0.97	1.67	117
    167	200091 SER A, 200088 SER A, 200180 TYR A	4.04	221.21	-0.97	-0.28	1.65	94
    168	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.02	221.87	0.02	0.3	1.25	69
    169	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.01	222.71	-0.06	0.08	1.67	69
    170	200041 PRO A, 200175 LEU A, 200180 TYR A	4.01	226.58	0.3	0.72	1.11	54
    171	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.36	226.85	0.13	0.34	1.68	54
    172	200041 PRO A, 200175 LEU A, 200180 TYR A	4.41	227.5	0.3	0.72	1.11	54
    173	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.44	228.3	0.13	0.34	1.68	54
    174	200041 PRO A, 200180 TYR A, 200173 ALA A	3.8	230.45	-1.1	0.07	2.19	54
    175	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.29	232.17	-1.7	-0.23	14.12	61
    176	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.27	234.59	-1.78	-0.53	14.11	64
    177	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.41	235.12	-2.55	-0.52	14.11	74
    178	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.31	235.67	-2.55	-0.52	14.11	74
    179	200153 GLU A, 200172 PRO A, 200041 ASN B	3.12	236.42	-2.87	-0.67	18.29	79
    180	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.43	239.73	-2.25	-0.7	14.56	79
    181	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.39	240.21	-1.95	-0.88	15.01	90
    182	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A	2.39	240.57	-0.8	-0.47	12.03	78
    183	200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A	2.41	240.96	-0.8	-0.47	12.03	78
    184	200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A	2.59	241.75	-0.13	-0.31	2.57	79
    185	200041 ASN B, 200182 LEU A, 200171 PHE A	2.75	242.11	-0.03	-0.14	2.3	79
    186	200041 ASN B, 200182 LEU A, 200170 THR A	2.78	242.35	-0.13	-0.13	1.72	88
    187	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.53	243.75	-0.2	-0.3	2.14	88
    188	200041 ASN B, 200170 THR A, 200155 VAL A	2.53	247.31	-1.53	-0.78	2.81	105
    189	200041 ASN B, 200170 THR A, 200155 VAL A, 200157 VAL A	2.93	247.63	-1.25	-0.79	2.95	105
    190	200041 ASN B, 200157 VAL A, 200156 THR A	3.03	247.89	-1.53	-0.78	2.81	105
    191	200041 ASN B, 200170 THR A, 200157 VAL A, 200156 THR A	3.19	248.19	-1.33	-0.78	2.52	106
    192	200041 ASN B, 200170 THR A, 200157 VAL A	3.2	248.28	-1.53	-0.78	2.81	105
    193	200041 ASN B, 200170 THR A, 200155 VAL A	3.17	248.49	-1.53	-0.78	2.81	105
    194	200041 ASN B, 200170 THR A, 200157 VAL A	3.22	248.65	-1.53	-0.78	2.81	105
    195	200041 ASN B, 200170 THR A, 200157 VAL A, 200156 THR A	3.19	249.09	-1.33	-0.78	2.52	106
    196	200170 THR A, 200157 VAL A, 200156 THR A	3.22	249.27	-0.6	-0.78	2.23	107
    197	200041 ASN B, 200170 THR A, 200157 VAL A, 200156 THR A	3.28	249.58	-1.33	-0.78	2.52	106
    198	200041 ASN B, 200157 VAL A, 200156 THR A	3.37	252.42	-1.53	-0.78	2.81	105
    199	200041 ASN B, 200157 VAL A, 200156 THR A, 200040 THR B	4.05	252.42	-1.25	-0.79	2.95	105

    pore with bottle neck

    pore with local minimum

19. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B, 200028 SER B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 1 ASP B, 200072 THR B, 1 ASP B, 63 LYS A, 97 THR B, 2 ILE B, 61 ASN A, 98 PHE B, 46 GLU A, 64 ILE A, 200020 SER B, 63 LYS A, 200018 ARG B, 40 ARG A, 88 SER A, 91 SER A, 41 PRO A, 91 SER A, 88 SER A, 175 LEU A, 180 TYR A, 173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A, 40 THR B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200069 THR B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A, 97 THR B, 61 ASN A, 46 GLU A, 64 ILE A, 200020 SER B, 200018 ARG B, 40 ARG A, 41 PRO A, 91 SER A, 88 SER A, 175 LEU A, 180 TYR A, 153 GLU A, 172 PRO A, 41 ASN B, 182 LEU A, 170 THR A, 156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 3 (12-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 15.04
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.23	0.13	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.18	1.91	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.29	3.97	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.6	4.19	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.64	4.76	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.68	5.1	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.66	5.36	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.58	6.36	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A	3.56	6.67	-2.23	-0.32	2.18	73
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.54	7.17	-2.55	-0.52	14.11	74
    11	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.53	7.73	-2.55	-0.52	14.11	74
    12	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.33	10.16	-1.78	-0.53	14.11	64
    13	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.29	11.93	-1.7	-0.23	14.12	61
    14	100041 PRO A, 100173 ALA A, 100180 TYR A	3.46	14.3	-1.1	0.07	2.19	54
    15	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.3	14.63	0.13	0.34	1.68	54
    16	100041 PRO A, 100180 TYR A, 100175 LEU A	4.35	15.29	0.3	0.72	1.11	54
    17	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.38	15.82	0.13	0.34	1.68	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A	4.48	20.47	0.3	0.72	1.11	54
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.47	21.04	-0.06	0.08	1.67	69
    20	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.45	21.36	0.23	0.08	1.27	84
    21	100180 TYR A, 100091 SER A, 100088 SER A	4.43	21.49	-0.97	-0.28	1.65	94
    22	100091 SER A, 100088 SER A	4.41	21.56	-0.8	-0.97	1.67	117
    23	100180 TYR A, 100091 SER A, 100088 SER A	4.4	21.89	-0.97	-0.28	1.65	94
    24	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	22.12	0.23	0.08	1.27	84
    25	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.49	22.42	0.02	0.3	1.25	69
    26	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.58	23.24	0.15	-0.22	1.26	86
    27	100041 PRO A, 100091 SER A, 100088 SER A	4.82	23.7	-1.07	-0.68	1.64	97
    28	100041 PRO A, 100088 SER A	4.96	24.91	-1.2	-0.53	1.63	87
    29	100041 PRO A, 100088 SER A, 100040 ARG A	4.13	27.67	-2.3	-0.49	18.42	86
    30	100041 PRO A, 100088 SER A, 100040 ARG A	2.99	29.73	-2.17	-0.44	18.99	70
    31	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.73	30.06	-1.73	-0.53	15.09	70
    32	100088 SER A, 100040 ARG A, 100091 SER A	1.91	31.5	-1.77	-0.67	19.59	83
    33	100088 SER A, 100040 ARG A	1.79	32.45	-2.45	-0.61	27.69	83
    34	100040 ARG A	1.73	39.18	-4.5	-0.42	52	83
    35	100040 ARG A, 100043 HIS A	2.39	40.16	-3.85	-0.08	51.8	87
    36	100040 ARG A, 100046 GLU A	2.74	43.32	-4	-0.78	50.95	80
    37	100040 ARG A, 100046 GLU A, 100064 ILE A	4.21	43.94	-1.17	0.08	34.01	87
    38	100040 ARG A, 100046 GLU A, 300018 ARG B	4.44	45.91	-4.17	-0.66	51.3	81
    39	100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B	3.49	49.41	-2	-0.04	38.51	86
    40	100046 GLU A, 100064 ILE A, 300018 ARG B	3.62	49.97	-1.17	0.08	34.01	87
    41	100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A	2.78	53.21	-0.98	-0.14	26.35	87
    42	100046 GLU A, 100064 ILE A, 100063 LYS A	2.73	58.2	-0.97	0.09	33.18	84
    43	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.72	58.61	-0.93	-0.18	25.3	92
    44	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.88	59.52	-1.1	-0.35	25.3	80
    45	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.15	62.57	0.23	0.35	24.92	76
    46	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.81	63.54	-1	-0.3	25.73	67
    47	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.24	64.62	-1.5	-0.4	21.26	76
    48	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.95	64.97	-2.03	-0.87	14.58	96
    49	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.96	65.17	-2.4	-0.78	21.56	90
    50	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.99	66	-0.94	-0.32	11.61	84
    51	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.99	66.4	-0.3	-0.21	13.67	77
    52	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.93	66.81	-0.3	-0.21	13.67	77
    53	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.61	68.73	-1.08	-0.27	25.25	79
    54	100063 LYS A, 100003 LEU B, 100001 ASP B	3.56	70.39	-1.2	-0.1	33.11	70
    55	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.66	71.29	-1.08	-0.27	25.25	79
    56	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.93	71.48	-1.56	-0.42	30.14	81
    57	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.91	72.45	-0.98	-0.43	25.3	83
    58	100003 LEU B, 300070 ASP B, 100001 ASP B	3.02	74.78	-0.03	-0.23	17.74	70
    59	100003 LEU B, 300070 ASP B	2.11	77.75	0.15	0.05	24.92	70
    60	100003 LEU B, 300070 ASP B, 100026 SER B	2.08	80.07	-0.17	-0.29	17.17	85
    61	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.44	82.15	-1.25	-0.32	25.88	85
    62	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	83.72	-2.93	-0.81	34.46	95
    63	300070 ASP B, 300024 ARG B, 100026 SER B	3.71	84.85	-2.8	-0.75	35.03	84
    64	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.79	86.32	-2.28	-0.76	26.69	92
    65	300024 ARG B, 100026 SER B, 300069 THR B	4.2	87.79	-1.87	-0.66	19.01	95
    66	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.8	88.87	-1.5	-0.7	15.11	95
    67	100026 SER B, 300069 THR B, 300026 SER B	4.41	91.84	-0.5	-0.79	2.81	107
    68	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.38	92.72	-0.48	-0.79	2.95	107
    69	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.42	94.43	-0.46	-0.79	3.04	107
    70	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	4.77	94.62	-0.58	-0.84	2.52	112
    71	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	4.89	94.75	-1.28	-0.92	2.99	100
    72	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.26	97.51	-1.35	-0.91	2.56	102
    73	100026 SER B, 300028 SER B, 100027 GLN B	5	98.14	-1.57	-0.96	2.86	100
    74	300027 GLN B, 300028 SER B, 100027 GLN B	5.37	98.77	-1.57	-0.96	2.86	100
    75	300028 SER B, 100027 GLN B, 300027 GLN B	5.74	99.35	-2.6	-1.06	2.91	95
    76	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	6.08	99.8	-2.05	-0.99	3.03	95
    77	300028 SER B, 100027 GLN B, 100028 SER B	6.36	100.1	-1.7	-1.01	2.29	106
    78	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.29	100.99	-2.05	-0.99	3.03	95
    79	300028 SER B, 100027 GLN B, 100028 SER B	5.42	104.46	-1.7	-1.01	2.29	106
    80	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	5.06	104.94	-2.4	-0.87	14.72	100
    81	100027 GLN B, 100028 SER B, 100093 ARG B	4.37	105.36	-2.93	-0.83	19.07	94
    82	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.08	105.77	-2.4	-0.87	14.72	100
    83	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	3.78	106.34	-2.3	-0.82	15.15	94
    84	300028 SER B, 100027 GLN B, 100093 ARG B	2.91	111.43	-2.93	-0.83	19.07	94
    85	300028 SER B, 100093 ARG B	3.27	112.13	-2.65	-0.7	26.84	100
    86	300028 SER B, 100093 ARG B, 100082 TYR C	3.47	113.68	-2.2	-0.09	18.43	83
    87	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.21	116.57	-2.78	-0.18	26.82	83
    88	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.09	117.34	-2.3	-0.3	22.13	83
    89	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.46	117.94	-2.22	-0.27	22.47	72
    90	300079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.67	118.17	-1.58	0.04	12.4	61
    91	93 ARG B, 79 GLY C, 82 TYR C, 200093 ARG B, 200079 GLY C	6.71	118.33	-2.22	-0.27	22.47	72
    92	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.45	118.77	-2.4	0.12	22.12	66
    93	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.25	119.28	-2.4	0.12	22.12	66
    94	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.67	120.87	-1.58	0.04	12.4	61
    95	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.3	121.79	-1.88	0.25	14.65	61
    96	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.23	124.9	-2.43	-0.3	15.13	72
    97	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	2.95	126.04	-2.2	-0.78	15.57	83
    98	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.36	128.23	-2.43	-0.3	15.13	72
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.91	129.1	-2.2	-0.02	12.43	66
    100	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.5	130.69	-2.4	0.12	22.12	66
    101	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	6.54	131.27	-2.22	-0.27	22.47	72
    102	100093 ARG B, 300093 ARG B, 93 ARG B, 79 GLY C, 200093 ARG B	6.93	131.68	-3.68	-0.5	42.28	83
    103	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	7.2	131.91	-2.22	-0.27	22.47	72
    104	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	7.37	132.15	-2.3	-0.3	22.13	83
    105	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	7.34	132.46	-2.22	-0.27	22.47	72
    106	100093 ARG B, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	7.14	132.98	-3.04	-0.19	32.2	74
    107	100079 GLY C, 82 TYR C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.81	135.57	-1.58	0.04	12.4	61
    108	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.05	138.67	-2.43	-0.3	15.13	72
    109	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3	139.34	-2.2	-0.78	15.57	83
    110	82 TYR C, 200093 ARG B, 200079 GLY C, 200058 GLN C	3.2	140.41	-2.43	-0.3	15.13	72
    111	82 TYR C, 200093 ARG B, 200058 GLN C, 200080 ASP C	3.97	140.59	-2.43	-0.3	15.13	72
    112	82 TYR C, 200093 ARG B, 200058 GLN C	3.75	141.55	-3.1	-0.14	19.05	72
    113	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.55	142.2	-2.53	-0.35	14.7	83
    114	200028 SER B, 200093 ARG B, 200058 GLN C	3.54	142.48	-2.93	-0.83	19.07	94
    115	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.74	143.61	-2.53	-0.35	14.7	83
    116	200028 SER B, 93 ARG B, 82 TYR C, 200093 ARG B	4.04	143.98	-2.78	-0.18	26.82	83
    117	200028 SER B, 93 ARG B, 82 TYR C	3.78	145.64	-2.2	-0.09	18.43	83
    118	200028 SER B, 93 ARG B	3.56	146.35	-2.65	-0.7	26.84	100
    119	27 GLN B, 200028 SER B, 93 ARG B	2.69	151.22	-2.93	-0.83	19.07	94
    120	27 GLN B, 28 SER B, 200028 SER B, 93 ARG B	3.67	151.75	-2.3	-0.82	15.15	94
    121	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	4.04	152.22	-2.4	-0.87	14.72	100
    122	27 GLN B, 93 ARG B, 28 SER B	4.73	152.55	-2.93	-0.83	19.07	94
    123	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	5.22	153.04	-2.4	-0.87	14.72	100
    124	27 GLN B, 200028 SER B, 28 SER B	5.29	156.52	-1.7	-1.01	2.29	106
    125	300028 SER B, 27 GLN B, 28 SER B	5.99	156.81	-1.7	-1.01	2.29	106
    126	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	6.15	157.72	-2.05	-0.99	3.03	95
    127	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.64	158.85	-2.05	-0.99	3.03	95
    128	27 GLN B, 200027 GLN B, 200028 SER B	5.33	159.49	-2.6	-1.06	2.91	95
    129	27 GLN B, 200028 SER B, 26 SER B	5.02	160.1	-1.57	-0.96	2.86	100
    130	27 GLN B, 200028 SER B, 26 SER B, 200069 THR B	4.41	162.64	-1.35	-0.91	2.56	102
    131	27 GLN B, 200028 SER B, 26 SER B, 200027 GLN B	4.74	163.03	-1.28	-0.92	2.99	100
    132	26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B, 200028 SER B	4.57	165.91	-0.46	-0.79	3.04	107
    133	26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B	4.62	166.8	-0.48	-0.79	2.95	107
    134	26 SER B, 200069 THR B, 200026 SER B	4.7	168.9	-0.5	-0.79	2.81	107
    135	26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B	4.76	169.7	-1.5	-0.7	15.11	95
    136	26 SER B, 200069 THR B, 200024 ARG B	4.28	171.26	-1.87	-0.66	19.01	95
    137	26 SER B, 200069 THR B, 200024 ARG B, 200070 ASP B	3.84	172.9	-2.28	-0.76	26.69	92
    138	26 SER B, 200024 ARG B, 200070 ASP B	3.72	173.66	-2.8	-0.75	35.03	84
    139	200024 ARG B, 200070 ASP B, 26 SER B	3.23	175.77	-2.93	-0.81	34.46	95
    140	200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B	2.56	177.47	-1.25	-0.32	25.88	85
    141	200070 ASP B, 26 SER B, 3 LEU B	2.06	180.29	-0.17	-0.29	17.17	85
    142	200070 ASP B, 3 LEU B	2.12	183.15	0.15	0.05	24.92	70
    143	200070 ASP B, 3 LEU B, 1 ASP B	3.1	184.94	-0.03	-0.23	17.74	70
    144	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B	3.93	185.06	-0.2	-0.37	13.72	82
    145	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B	3.99	185.93	-0.98	-0.43	25.3	83
    146	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.97	186.13	-1.56	-0.42	30.14	81
    147	3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.68	187.7	-1.08	-0.27	25.25	79
    148	3 LEU B, 1 ASP B, 63 LYS A	3.65	189.39	-1.2	-0.1	33.11	70
    149	3 LEU B, 1 ASP B, 63 LYS A, 97 THR B	3.73	190.7	-1.08	-0.27	25.25	79
    150	3 LEU B, 63 LYS A, 97 THR B, 2 ILE B	3.87	191.11	-0.3	-0.21	13.67	77
    151	3 LEU B, 63 LYS A, 97 THR B, 61 ASN A	3.88	191.49	-1.08	-0.2	13.67	84
    152	3 LEU B, 63 LYS A, 97 THR B, 61 ASN A, 98 PHE B	3.75	192.25	-0.94	-0.32	11.61	84
    153	63 LYS A, 97 THR B, 61 ASN A, 98 PHE B, 46 GLU A	3.7	192.44	-2.4	-0.78	21.56	90
    154	97 THR B, 61 ASN A, 98 PHE B, 46 GLU A	3.7	192.82	-2.03	-0.87	14.58	96
    155	63 LYS A, 97 THR B, 61 ASN A, 98 PHE B, 46 GLU A	4.12	193.34	-2.4	-0.78	21.56	90
    156	3 LEU B, 63 LYS A, 61 ASN A, 98 PHE B, 46 GLU A	4.45	194.19	-1.5	-0.4	21.26	76
    157	3 LEU B, 63 LYS A, 98 PHE B, 46 GLU A	4.84	195.23	-1	-0.3	25.73	67
    158	3 LEU B, 63 LYS A, 46 GLU A, 64 ILE A	5.24	198.56	0.23	0.35	24.92	76
    159	3 LEU B, 63 LYS A, 46 GLU A, 200020 SER B	5.79	199.38	-1.1	-0.35	25.3	80
    160	63 LYS A, 46 GLU A, 64 ILE A, 200020 SER B	5.4	200.09	-0.93	-0.18	25.3	92
    161	63 LYS A, 46 GLU A, 64 ILE A	2.75	204.45	-0.97	0.09	33.18	84
    162	46 GLU A, 64 ILE A, 63 LYS A	2.84	205.2	0.2	-0.04	17.8	90
    163	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.01	208.14	-0.98	-0.14	26.35	87
    164	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.52	211.61	-2	-0.04	38.51	86
    165	46 GLU A, 200018 ARG B, 40 ARG A	4.24	214.12	-4.17	-0.66	51.3	81
    166	46 GLU A, 64 ILE A, 40 ARG A	4.07	214.62	-1.17	0.08	34.01	87
    167	46 GLU A, 40 ARG A	3.37	217.89	-4	-0.78	50.95	80
    168	40 ARG A	2.37	223.84	-4.5	-0.42	52	83
    169	40 ARG A, 88 SER A	2.21	224.72	-2.45	-0.61	27.69	83
    170	40 ARG A, 88 SER A, 91 SER A	2.09	225.51	-1.77	-0.67	19.59	83
    171	40 ARG A, 88 SER A, 41 PRO A, 91 SER A	2.15	225.73	-1.83	-0.57	14.66	86
    172	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.29	226.77	-1.73	-0.53	15.09	70
    173	40 ARG A, 88 SER A, 41 PRO A	3	229.16	-2.17	-0.44	18.99	70
    174	40 ARG A, 41 PRO A, 88 SER A	4.29	231.13	-2.3	-0.49	18.42	86
    175	41 PRO A, 88 SER A	4.98	232.41	-1.2	-0.53	1.63	87
    176	41 PRO A, 91 SER A, 88 SER A	4.66	233.27	-1.07	-0.68	1.64	97
    177	41 PRO A, 91 SER A, 88 SER A, 175 LEU A	4.52	233.62	0.15	-0.22	1.26	86
    178	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.43	233.88	0.02	0.3	1.25	69
    179	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.33	234.26	0.23	0.08	1.27	84
    180	91 SER A, 88 SER A, 180 TYR A	4.33	234.44	-0.97	-0.28	1.65	94
    181	91 SER A, 88 SER A	4.35	234.65	-0.8	-0.97	1.67	117
    182	91 SER A, 88 SER A, 180 TYR A	4.38	235.08	-0.97	-0.28	1.65	94
    183	88 SER A, 41 PRO A, 91 SER A, 175 LEU A, 180 TYR A	4.4	235.76	-0.06	0.08	1.67	69
    184	41 PRO A, 91 SER A, 175 LEU A, 180 TYR A	4.43	236.6	0.02	0.3	1.25	69
    185	41 PRO A, 175 LEU A, 180 TYR A	4.44	240.39	0.3	0.72	1.11	54
    186	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.38	240.66	0.13	0.34	1.68	54
    187	41 PRO A, 175 LEU A, 180 TYR A	4.36	241.3	0.3	0.72	1.11	54
    188	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.1	242.06	0.13	0.34	1.68	54
    189	41 PRO A, 180 TYR A, 173 ALA A	3.49	244.18	-1.1	0.07	2.19	54
    190	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.33	246.3	-1.7	-0.23	14.12	61
    191	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.41	248.32	-1.78	-0.53	14.11	64
    192	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.6	249.11	-2.55	-0.52	14.11	74
    193	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.34	249.71	-2.55	-0.52	14.11	74
    194	153 GLU A, 172 PRO A, 41 ASN B	3.15	250.09	-2.87	-0.67	18.29	79
    195	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.25	253.33	-2.25	-0.7	14.56	79
    196	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.26	254.25	-1.95	-0.88	15.01	90
    197	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.36	254.53	-0.8	-0.47	12.03	78
    198	153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.44	254.75	-0.8	-0.47	12.03	78
    199	41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.6	255.64	-0.13	-0.31	2.57	79
    200	41 ASN B, 182 LEU A, 171 PHE A	2.76	255.82	-0.03	-0.14	2.3	79
    201	41 ASN B, 182 LEU A, 170 THR A	2.78	256.11	-0.13	-0.13	1.72	88
    202	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.72	257.79	-0.2	-0.3	2.14	88
    203	41 ASN B, 170 THR A, 155 VAL A	2.78	261.24	-1.53	-0.78	2.81	105
    204	41 ASN B, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A	3.1	261.49	-1.14	-0.78	2.69	106
    205	41 ASN B, 156 THR A, 157 VAL A	3.15	261.75	-1.53	-0.78	2.81	105
    206	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.19	262.04	-1.33	-0.78	2.52	106
    207	41 ASN B, 170 THR A, 157 VAL A	3.18	262.12	-1.53	-0.78	2.81	105
    208	41 ASN B, 170 THR A, 155 VAL A	3.17	262.33	-1.53	-0.78	2.81	105
    209	41 ASN B, 170 THR A, 157 VAL A	3.24	262.49	-1.53	-0.78	2.81	105
    210	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.18	262.92	-1.33	-0.78	2.52	106
    211	170 THR A, 156 THR A, 157 VAL A	3.23	263.1	-0.6	-0.78	2.23	107
    212	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.29	263.42	-1.33	-0.78	2.52	106
    213	41 ASN B, 156 THR A, 157 VAL A	3.38	266.24	-1.53	-0.78	2.81	105
    214	41 ASN B, 156 THR A, 157 VAL A, 40 THR B	4.05	266.24	-1.25	-0.79	2.95	105

    pore with bottle neck

    pore with local minimum

20. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 79 GLY C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200028 SER B, 26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 1 ASP B, 1 ASP B, 200072 THR B, 63 LYS A, 97 THR B, 2 ILE B, 98 PHE B, 61 ASN A, 46 GLU A, 64 ILE A, 200020 SER B, 63 LYS A, 200018 ARG B, 40 ARG A, 88 SER A, 91 SER A, 91 SER A, 41 PRO A, 88 SER A, 175 LEU A, 180 TYR A, 173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A, 40 THR B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200069 THR B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 1 ASP B, 200072 THR B, 63 LYS A, 97 THR B, 61 ASN A, 46 GLU A, 64 ILE A, 200020 SER B, 200018 ARG B, 40 ARG A, 91 SER A, 41 PRO A, 88 SER A, 175 LEU A, 180 TYR A, 153 GLU A, 172 PRO A, 41 ASN B, 182 LEU A, 170 THR A, 156 THR A,

    Physicochemical properties of lining side-chains

    Charge: 4 (12-8)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 14.62
    Mutability: 86
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.27	0.25	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.21	0.43	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.18	0.69	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.19	0.84	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.99	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.15	1.34	-1.53	-0.78	2.81	105
    7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	3.11	1.79	-1.14	-0.78	2.69	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.82	5.47	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.74	6.55	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.78	6.87	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.74	7.22	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.64	7.92	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.61	8.32	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.58	8.73	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.52	9.83	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.51	12.96	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	2.96	13.29	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.1	13.82	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.32	14.4	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100172 PRO A, 100041 PRO A	3.42	14.73	-2.23	-0.44	17.69	64
    21	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.27	16.95	-1.78	-0.53	14.11	64
    22	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.31	18.8	-1.7	-0.23	14.12	61
    23	100173 ALA A, 100041 PRO A, 100180 TYR A	3.77	20.87	-1.1	0.07	2.19	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.24	21.43	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.42	22.11	0.3	0.72	1.11	54
    26	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.33	22.52	0.13	0.34	1.68	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A	4.03	27.28	0.3	0.72	1.11	54
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.04	27.84	-0.06	0.08	1.67	69
    29	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.07	28.13	0.23	0.08	1.27	84
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.11	28.24	-0.97	-0.28	1.65	94
    31	100091 SER A, 100088 SER A	4.17	28.33	-0.8	-0.97	1.67	117
    32	100180 TYR A, 100091 SER A, 100088 SER A	4.25	28.49	-0.97	-0.28	1.65	94
    33	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.33	28.95	0.23	0.08	1.27	84
    34	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.55	29.29	0.02	0.3	1.25	69
    35	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.66	29.71	0.15	-0.22	1.26	86
    36	100041 PRO A, 100091 SER A, 100088 SER A	4.77	30.66	-1.07	-0.68	1.64	97
    37	100041 PRO A, 100088 SER A	4.95	31.82	-1.2	-0.53	1.63	87
    38	100041 PRO A, 100088 SER A, 100040 ARG A	4.4	34.29	-2.3	-0.49	18.42	86
    39	100041 PRO A, 100088 SER A, 100040 ARG A	3.25	36.45	-2.17	-0.44	18.99	70
    40	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.92	36.79	-1.73	-0.53	15.09	70
    41	100088 SER A, 100040 ARG A, 100091 SER A	1.74	38.33	-1.77	-0.67	19.59	83
    42	100088 SER A, 100040 ARG A	1.52	39.36	-2.45	-0.61	27.69	83
    43	100040 ARG A	1.3	45.08	-4.5	-0.42	52	83
    44	100040 ARG A, 100043 HIS A	1.71	46.25	-3.85	-0.08	51.8	87
    45	100040 ARG A, 100046 GLU A	2.08	50.37	-4	-0.78	50.95	80
    46	100040 ARG A, 100046 GLU A, 300018 ARG B	4.34	52.44	-4.17	-0.66	51.3	81
    47	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.45	56.14	-2	-0.04	38.51	86
    48	100046 GLU A, 300018 ARG B, 100064 ILE A	3.67	56.72	-1.17	0.08	34.01	87
    49	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	2.9	60.09	-0.98	-0.14	26.35	87
    50	100046 GLU A, 100064 ILE A, 100063 LYS A	2.78	65.16	-0.97	0.09	33.18	84
    51	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	5.53	65.92	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.33	69.97	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.96	70.8	-1	-0.3	25.73	67
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.56	71.29	-1.5	-0.4	21.26	76
    55	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.2	71.47	-2.4	-0.78	21.56	90
    56	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.68	71.65	-2.03	-0.87	14.58	96
    57	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.55	71.86	-2.4	-0.78	21.56	90
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.48	72.71	-0.94	-0.32	11.61	84
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.57	73.12	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.63	73.55	-0.3	-0.21	13.67	77
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.69	75.54	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B	3.85	77.23	-1.2	-0.1	33.11	70
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.93	78.08	-1.08	-0.27	25.25	79
    64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.99	78.28	-1.56	-0.42	30.14	81
    65	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.93	79.13	-0.98	-0.43	25.3	83
    66	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.9	79.29	-0.2	-0.37	13.72	82
    67	100003 LEU B, 300070 ASP B, 100001 ASP B	2.89	81.6	-0.03	-0.23	17.74	70
    68	100003 LEU B, 300070 ASP B	2.25	84.18	0.15	0.05	24.92	70
    69	100003 LEU B, 300070 ASP B, 100026 SER B	2.12	87.07	-0.17	-0.29	17.17	85
    70	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.54	88.76	-1.25	-0.32	25.88	85
    71	300070 ASP B, 100026 SER B, 300024 ARG B	3.25	90.43	-2.93	-0.81	34.46	95
    72	300070 ASP B, 300024 ARG B, 100026 SER B	3.59	91.66	-2.8	-0.75	35.03	84
    73	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.8	93.23	-2.28	-0.76	26.69	92
    74	300024 ARG B, 100026 SER B, 300069 THR B	4.5	94.64	-1.87	-0.66	19.01	95
    75	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.83	95.43	-1.5	-0.7	15.11	95
    76	100026 SER B, 300069 THR B, 300026 SER B	4.3	98.32	-0.5	-0.79	2.81	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.33	99.24	-0.48	-0.79	2.95	107
    78	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.43	101.32	-0.46	-0.79	3.04	107
    79	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5	101.45	-1.28	-0.92	2.99	100
    80	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.2	104.41	-1.35	-0.91	2.56	102
    81	100026 SER B, 100027 GLN B, 300028 SER B	5.15	105.07	-1.57	-0.96	2.86	100
    82	300027 GLN B, 100027 GLN B, 300028 SER B	5.54	105.71	-1.57	-0.96	2.86	100
    83	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.91	106.67	-2.05	-0.99	3.03	95
    84	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.29	107.55	-2.05	-0.99	3.03	95
    85	100027 GLN B, 300028 SER B, 100028 SER B	5.42	111.11	-1.7	-1.01	2.29	106
    86	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	5.2	111.64	-2.4	-0.87	14.72	100
    87	100027 GLN B, 100028 SER B, 100093 ARG B	4.55	112.08	-2.93	-0.83	19.07	94
    88	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.21	112.5	-2.4	-0.87	14.72	100
    89	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.85	113.11	-2.3	-0.82	15.15	94
    90	100027 GLN B, 300028 SER B, 100093 ARG B	2.67	118.4	-2.93	-0.83	19.07	94
    91	300028 SER B, 100093 ARG B	3.32	119.09	-2.65	-0.7	26.84	100
    92	300028 SER B, 100093 ARG B, 100082 TYR C	3.62	120.17	-2.2	-0.09	18.43	83
    93	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.22	123.16	-2.78	-0.18	26.82	83
    94	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	5.97	123.96	-2.3	-0.3	22.13	83
    95	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.39	124.6	-2.22	-0.27	22.47	72
    96	300093 ARG B, 300079 GLY C, 100079 GLY C, 79 GLY C, 300082 TYR C	6.67	124.85	-1.4	-0.34	12.75	66
    97	79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C	6.71	125.03	-2.22	-0.27	22.47	72
    98	79 GLY C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C	6.3	125.48	-2.4	0.12	22.12	66
    99	300093 ARG B, 79 GLY C, 300082 TYR C, 93 ARG B, 82 TYR C	5.97	126	-2.4	0.12	22.12	66
    100	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.13	127.66	-1.58	0.04	12.4	61
    101	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	4.68	128.61	-1.88	0.25	14.65	61
    102	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.32	131.7	-2.43	-0.3	15.13	72
    103	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.32	132.97	-2.2	-0.78	15.57	83
    104	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.8	135.37	-2.43	-0.3	15.13	72
    105	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.91	136.26	-2.2	-0.02	12.43	66
    106	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.33	137.08	-2.4	0.12	22.12	66
    107	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.73	138.25	-2.22	-0.27	22.47	72
    108	300093 ARG B, 300079 GLY C, 79 GLY C, 300082 TYR C, 93 ARG B	6.31	138.7	-2.22	-0.27	22.47	72
    109	300093 ARG B, 300079 GLY C, 300082 TYR C, 93 ARG B, 28 SER B	6.25	139.07	-2.3	-0.3	22.13	83
    110	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 93 ARG B	5.98	139.56	-2.4	0.12	22.12	66
    111	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.63	140.3	-2.22	-0.27	22.47	72
    112	100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	4.87	142.18	-1.58	0.04	12.4	61
    113	200093 ARG B, 200079 GLY C, 200082 TYR C	4.52	143.12	-2.07	-0.04	19	66
    114	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.78	145.4	-2.43	-0.3	15.13	72
    115	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3.78	146.1	-2.2	-0.78	15.57	83
    116	200093 ARG B, 82 TYR C, 200079 GLY C, 200058 GLN C	3.7	147.18	-2.43	-0.3	15.13	72
    117	200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C	3.66	147.37	-2.43	-0.3	15.13	72
    118	200093 ARG B, 82 TYR C, 200058 GLN C	3.54	148.12	-3.1	-0.14	19.05	72
    119	200093 ARG B, 82 TYR C, 200058 GLN C, 200028 SER B	3.51	148.38	-2.43	-0.3	15.13	72
    120	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.49	148.87	-2.53	-0.35	14.7	83
    121	200028 SER B, 200093 ARG B, 200058 GLN C	3.54	149.15	-2.93	-0.83	19.07	94
    122	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.88	150.27	-2.53	-0.35	14.7	83
    123	200028 SER B, 93 ARG B, 200093 ARG B, 82 TYR C	3.64	151.1	-2.78	-0.18	26.82	83
    124	200028 SER B, 93 ARG B, 82 TYR C	3.12	152.37	-2.2	-0.09	18.43	83
    125	200028 SER B, 93 ARG B	2.85	153.1	-2.65	-0.7	26.84	100
    126	27 GLN B, 200028 SER B, 93 ARG B	2.44	158.12	-2.93	-0.83	19.07	94
    127	27 GLN B, 28 SER B, 200028 SER B, 93 ARG B	4.33	158.59	-2.3	-0.82	15.15	94
    128	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	4.68	158.85	-2.4	-0.87	14.72	100
    129	27 GLN B, 93 ARG B, 28 SER B	4.94	159.32	-2.93	-0.83	19.07	94
    130	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	5.1	160.02	-2.4	-0.87	14.72	100
    131	27 GLN B, 200028 SER B, 28 SER B	5.1	163.46	-1.7	-1.01	2.29	106
    132	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	6.05	164.4	-2.05	-0.99	3.03	95
    133	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.53	165.57	-2.05	-0.99	3.03	95
    134	27 GLN B, 200027 GLN B, 200028 SER B	5.23	166.23	-2.6	-1.06	2.91	95
    135	27 GLN B, 200028 SER B, 26 SER B	4.94	166.86	-1.57	-0.96	2.86	100
    136	27 GLN B, 200028 SER B, 26 SER B, 200069 THR B	4.47	169.39	-1.35	-0.91	2.56	102
    137	27 GLN B, 200028 SER B, 26 SER B, 200027 GLN B	4.74	169.58	-1.28	-0.92	2.99	100
    138	200028 SER B, 26 SER B, 200069 THR B, 200027 GLN B	4.65	169.95	-0.58	-0.84	2.52	112
    139	200028 SER B, 26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B	4.45	172.29	-0.46	-0.79	3.04	107
    140	26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B	4.47	173.22	-0.48	-0.79	2.95	107
    141	26 SER B, 200069 THR B, 200026 SER B	4.55	175.55	-0.5	-0.79	2.81	107
    142	26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B	4.86	176.39	-1.5	-0.7	15.11	95
    143	26 SER B, 200069 THR B, 200024 ARG B	4.28	178	-1.87	-0.66	19.01	95
    144	26 SER B, 200069 THR B, 200024 ARG B, 200070 ASP B	3.75	179.65	-2.28	-0.76	26.69	92
    145	26 SER B, 200024 ARG B, 200070 ASP B	3.72	180.32	-2.8	-0.75	35.03	84
    146	200024 ARG B, 200070 ASP B, 26 SER B	3.22	182.34	-2.93	-0.81	34.46	95
    147	200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B	2.49	184.08	-1.25	-0.32	25.88	85
    148	200070 ASP B, 26 SER B, 3 LEU B	2.12	186.99	-0.17	-0.29	17.17	85
    149	200070 ASP B, 3 LEU B	2.24	189.93	0.15	0.05	24.92	70
    150	200070 ASP B, 3 LEU B, 1 ASP B	3.08	191.73	-0.03	-0.23	17.74	70
    151	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B	3.82	192.63	-0.98	-0.43	25.3	83
    152	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B, 63 LYS A	4.23	192.83	-1.56	-0.42	30.14	81
    153	3 LEU B, 1 ASP B, 200072 THR B, 63 LYS A	4.12	193.94	-1.08	-0.27	25.25	79
    154	3 LEU B, 1 ASP B, 63 LYS A	3.81	195.7	-1.2	-0.1	33.11	70
    155	3 LEU B, 1 ASP B, 63 LYS A, 97 THR B	3.46	197.56	-1.08	-0.27	25.25	79
    156	3 LEU B, 63 LYS A, 97 THR B, 2 ILE B	3.44	197.97	-0.3	-0.21	13.67	77
    157	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B	3.45	198.34	-0.3	-0.21	13.67	77
    158	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B, 61 ASN A	3.49	199.05	-0.94	-0.32	11.61	84
    159	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	3.83	199.22	-2.4	-0.78	21.56	90
    160	97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.02	199.42	-2.03	-0.87	14.58	96
    161	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.5	199.86	-2.4	-0.78	21.56	90
    162	3 LEU B, 63 LYS A, 98 PHE B, 61 ASN A, 46 GLU A	4.73	200.65	-1.5	-0.4	21.26	76
    163	3 LEU B, 63 LYS A, 98 PHE B, 46 GLU A	4.94	201.69	-1	-0.3	25.73	67
    164	3 LEU B, 63 LYS A, 46 GLU A, 64 ILE A	5.05	205.24	0.23	0.35	24.92	76
    165	3 LEU B, 63 LYS A, 46 GLU A, 200020 SER B	4.56	206.06	-1.1	-0.35	25.3	80
    166	63 LYS A, 46 GLU A, 64 ILE A, 200020 SER B	4.25	206.79	-0.93	-0.18	25.3	92
    167	63 LYS A, 46 GLU A, 64 ILE A	3.26	211.33	-0.97	0.09	33.18	84
    168	46 GLU A, 64 ILE A, 63 LYS A	3.5	212.09	0.2	-0.04	17.8	90
    169	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.62	214.52	-0.98	-0.14	26.35	87
    170	46 GLU A, 64 ILE A, 200018 ARG B	3.77	215.08	-1.17	0.08	34.01	87
    171	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.53	218.19	-2	-0.04	38.51	86
    172	46 GLU A, 200018 ARG B, 40 ARG A	4.15	220.82	-4.17	-0.66	51.3	81
    173	46 GLU A, 64 ILE A, 40 ARG A	4	221.34	-1.17	0.08	34.01	87
    174	46 GLU A, 40 ARG A	3.59	223.31	-4	-0.78	50.95	80
    175	40 ARG A	2.35	230.81	-4.5	-0.42	52	83
    176	40 ARG A, 88 SER A	2.2	231.6	-2.45	-0.61	27.69	83
    177	40 ARG A, 88 SER A, 91 SER A	2.12	232.04	-1.77	-0.67	19.59	83
    178	40 ARG A, 88 SER A, 91 SER A	2.14	232.28	-1.9	-0.73	19.02	100
    179	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.24	232.53	-1.83	-0.57	14.66	86
    180	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.41	233.22	-1.73	-0.53	15.09	70
    181	40 ARG A, 88 SER A, 41 PRO A	2.92	235.62	-2.17	-0.44	18.99	70
    182	40 ARG A, 41 PRO A, 88 SER A	4.14	237.77	-2.3	-0.49	18.42	86
    183	41 PRO A, 88 SER A	5.09	239.07	-1.2	-0.53	1.63	87
    184	91 SER A, 41 PRO A, 88 SER A	4.85	239.97	-1.07	-0.68	1.64	97
    185	91 SER A, 41 PRO A, 88 SER A, 175 LEU A	4.72	240.32	0.15	-0.22	1.26	86
    186	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.59	240.59	0.02	0.3	1.25	69
    187	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.41	240.97	0.23	0.08	1.27	84
    188	91 SER A, 88 SER A, 180 TYR A	4.3	241.16	-0.97	-0.28	1.65	94
    189	91 SER A, 88 SER A	4.28	241.42	-0.8	-0.97	1.67	117
    190	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.27	241.94	0.23	0.08	1.27	84
    191	88 SER A, 91 SER A, 41 PRO A, 175 LEU A, 180 TYR A	4.27	242.7	-0.06	0.08	1.67	69
    192	41 PRO A, 175 LEU A, 180 TYR A	4.29	247.02	0.3	0.72	1.11	54
    193	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.46	247.3	0.13	0.34	1.68	54
    194	41 PRO A, 175 LEU A, 180 TYR A	4.37	247.98	0.3	0.72	1.11	54
    195	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.45	248.79	0.13	0.34	1.68	54
    196	41 PRO A, 180 TYR A, 173 ALA A	3.78	250.98	-1.1	0.07	2.19	54
    197	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.27	252.73	-1.7	-0.23	14.12	61
    198	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.26	254.87	-1.78	-0.53	14.11	64
    199	41 PRO A, 153 GLU A, 172 PRO A	3.38	255.18	-2.23	-0.44	17.69	64
    200	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.26	255.71	-2.55	-0.52	14.11	74
    201	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.08	256.31	-2.55	-0.52	14.11	74
    202	153 GLU A, 172 PRO A, 41 ASN B	2.89	257.12	-2.87	-0.67	18.29	79
    203	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.73	260	-2.25	-0.7	14.56	79
    204	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.73	260.95	-1.95	-0.88	15.01	90
    205	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.74	261.23	-0.8	-0.47	12.03	78
    206	153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.72	261.45	-0.8	-0.47	12.03	78
    207	41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.68	262.24	-0.13	-0.31	2.57	79
    208	41 ASN B, 182 LEU A, 171 PHE A	2.77	262.6	-0.03	-0.14	2.3	79
    209	41 ASN B, 182 LEU A, 170 THR A	2.73	262.86	-0.13	-0.13	1.72	88
    210	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.58	264.38	-0.2	-0.3	2.14	88
    211	41 ASN B, 170 THR A, 155 VAL A	2.82	267.94	-1.53	-0.78	2.81	105
    212	41 ASN B, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A	3.25	268.19	-1.14	-0.78	2.69	106
    213	41 ASN B, 156 THR A, 157 VAL A	3.27	268.46	-1.53	-0.78	2.81	105
    214	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.24	268.62	-1.33	-0.78	2.52	106
    215	41 ASN B, 170 THR A, 157 VAL A	3.22	268.75	-1.53	-0.78	2.81	105
    216	41 ASN B, 170 THR A, 155 VAL A	3.18	268.97	-1.53	-0.78	2.81	105
    217	41 ASN B, 170 THR A, 157 VAL A	3.24	269.14	-1.53	-0.78	2.81	105
    218	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.17	269.59	-1.33	-0.78	2.52	106
    219	170 THR A, 156 THR A, 157 VAL A	3.22	269.75	-0.6	-0.78	2.23	107
    220	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.29	270.05	-1.33	-0.78	2.52	106
    221	41 ASN B, 156 THR A, 157 VAL A	3.38	272.94	-1.53	-0.78	2.81	105
    222	41 ASN B, 156 THR A, 157 VAL A, 40 THR B	4.05	272.94	-1.25	-0.79	2.95	105

    pore with bottle neck

    pore with local minimum

21. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 200028 SER B, 27 GLN B, 69 THR B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A, 300169 HIS A, 300167 ASP B, 300166 SER A, 300166 SER A, 300170 ASP B, 300169 LYS B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A, 300168 VAL A, 300169 LYS B, 300169 HIS A, 300167 ASP B, 300166 SER A, 300170 ASP B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A

    Physicochemical properties of lining side-chains

    Charge: 2 (13-11)
    Hydropathy: -1.4
    Hydrophobicity: -0.43
    Polarity: 15.03
    Mutability: 89
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.16	0.19	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.11	2.01	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.25	3.96	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.71	4.2	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.76	4.72	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.73	5.08	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.68	5.38	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.56	6.51	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.48	7.11	-2.55	-0.52	14.11	74
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.41	7.74	-2.55	-0.52	14.11	74
    11	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.26	10.1	-1.78	-0.53	14.11	64
    12	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.28	12.16	-1.7	-0.23	14.12	61
    13	100041 PRO A, 100173 ALA A, 100180 TYR A	3.68	14.29	-1.1	0.07	2.19	54
    14	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.33	14.68	0.13	0.34	1.68	54
    15	100041 PRO A, 100180 TYR A, 100175 LEU A	4.34	15.34	0.3	0.72	1.11	54
    16	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.32	15.83	0.13	0.34	1.68	54
    17	100041 PRO A, 100180 TYR A, 100175 LEU A	4.16	20.29	0.3	0.72	1.11	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.12	20.98	-0.06	0.08	1.67	69
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.1	21.35	0.02	0.3	1.25	69
    20	100180 TYR A, 100091 SER A, 100088 SER A	4.09	21.48	-0.97	-0.28	1.65	94
    21	100091 SER A, 100088 SER A	4.1	21.58	-0.8	-0.97	1.67	117
    22	100180 TYR A, 100091 SER A, 100088 SER A	4.15	21.76	-0.97	-0.28	1.65	94
    23	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.23	22.31	0.23	0.08	1.27	84
    24	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.46	22.73	0.02	0.3	1.25	69
    25	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.59	23.23	0.15	-0.22	1.26	86
    26	100041 PRO A, 100091 SER A, 100088 SER A	4.72	23.75	-1.07	-0.68	1.64	97
    27	100041 PRO A, 100088 SER A	4.84	25.06	-1.2	-0.53	1.63	87
    28	100041 PRO A, 100088 SER A, 100040 ARG A	4.47	27.27	-2.3	-0.49	18.42	86
    29	100041 PRO A, 100088 SER A, 100040 ARG A	3.09	29.7	-2.17	-0.44	18.99	70
    30	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.73	30.07	-1.73	-0.53	15.09	70
    31	100088 SER A, 100040 ARG A, 100091 SER A	2	31.15	-1.77	-0.67	19.59	83
    32	100088 SER A, 100040 ARG A	1.95	33.42	-2.45	-0.61	27.69	83
    33	100040 ARG A	2.12	38.25	-4.5	-0.42	52	83
    34	100040 ARG A, 100043 HIS A	2.76	39.53	-3.85	-0.08	51.8	87
    35	100040 ARG A, 100046 GLU A	2.98	43.24	-4	-0.78	50.95	80
    36	100040 ARG A, 100046 GLU A, 100064 ILE A	3.54	43.94	-1.17	0.08	34.01	87
    37	100040 ARG A, 100046 GLU A, 300018 ARG B	3.61	46.2	-4.17	-0.66	51.3	81
    38	100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B	3.47	49.3	-2	-0.04	38.51	86
    39	100046 GLU A, 100064 ILE A, 300018 ARG B	3.35	49.94	-1.17	0.08	34.01	87
    40	100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A	3.17	52.84	-0.98	-0.14	26.35	87
    41	100046 GLU A, 100064 ILE A, 100063 LYS A	3.39	53.69	0.2	-0.04	17.8	90
    42	100046 GLU A, 100064 ILE A, 100063 LYS A	3.64	57.88	-0.97	0.09	33.18	84
    43	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.45	58.46	-0.93	-0.18	25.3	92
    44	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.45	59.43	-1.1	-0.35	25.3	80
    45	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.85	62.9	0.23	0.35	24.92	76
    46	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.59	63.88	-1	-0.3	25.73	67
    47	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.34	64.46	-1.5	-0.4	21.26	76
    48	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.13	64.67	-2.4	-0.78	21.56	90
    49	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.86	64.9	-2.03	-0.87	14.58	96
    50	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.78	65.13	-2.4	-0.78	21.56	90
    51	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.71	66.17	-0.94	-0.32	11.61	84
    52	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.73	66.64	-1.08	-0.2	13.67	84
    53	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.76	68.84	-1.08	-0.27	25.25	79
    54	100063 LYS A, 100003 LEU B, 100001 ASP B	3.9	70.12	-1.2	-0.1	33.11	70
    55	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.97	71.21	-1.08	-0.27	25.25	79
    56	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.05	71.43	-1.56	-0.42	30.14	81
    57	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.83	72.28	-0.98	-0.43	25.3	83
    58	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.78	72.45	-0.2	-0.37	13.72	82
    59	100003 LEU B, 300070 ASP B, 100001 ASP B	2.93	74.86	-0.03	-0.23	17.74	70
    60	100003 LEU B, 300070 ASP B	2.12	77.69	0.15	0.05	24.92	70
    61	100003 LEU B, 300070 ASP B, 100026 SER B	2.11	80.33	-0.17	-0.29	17.17	85
    62	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.68	82.2	-1.25	-0.32	25.88	85
    63	300070 ASP B, 100026 SER B, 300024 ARG B	3.41	83.63	-2.93	-0.81	34.46	95
    64	300070 ASP B, 300024 ARG B, 100026 SER B	3.55	84.81	-2.8	-0.75	35.03	84
    65	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.91	86.54	-2.28	-0.76	26.69	92
    66	300024 ARG B, 100026 SER B, 300069 THR B	4.65	87.64	-1.87	-0.66	19.01	95
    67	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.89	88.6	-1.5	-0.7	15.11	95
    68	100026 SER B, 300069 THR B, 300026 SER B	4.33	91.82	-0.5	-0.79	2.81	107
    69	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.3	92.81	-0.48	-0.79	2.95	107
    70	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.35	94.47	-0.46	-0.79	3.04	107
    71	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.68	94.82	-1.28	-0.92	2.99	100
    72	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.63	97.51	-1.35	-0.91	2.56	102
    73	100026 SER B, 100027 GLN B, 300028 SER B	4.85	98.24	-1.57	-0.96	2.86	100
    74	300027 GLN B, 100027 GLN B, 300028 SER B	5.07	98.94	-1.57	-0.96	2.86	100
    75	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.33	99.94	-2.05	-0.99	3.03	95
    76	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.87	101.09	-2.05	-0.99	3.03	95
    77	100027 GLN B, 300028 SER B, 100028 SER B	5.15	104.4	-1.7	-1.01	2.29	106
    78	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.68	104.77	-2.4	-0.87	14.72	100
    79	100027 GLN B, 100028 SER B, 100093 ARG B	4.19	105.22	-2.93	-0.83	19.07	94
    80	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.07	105.67	-2.4	-0.87	14.72	100
    81	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.96	106.36	-2.3	-0.82	15.15	94
    82	100027 GLN B, 300028 SER B, 100093 ARG B	3.41	111.25	-2.93	-0.83	19.07	94
    83	300028 SER B, 100093 ARG B	3.39	112.03	-2.65	-0.7	26.84	100
    84	300028 SER B, 100093 ARG B, 100082 TYR C	3.38	113.64	-2.2	-0.09	18.43	83
    85	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.47	114.02	-2.78	-0.18	26.82	83
    86	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.52	114.81	-2.53	-0.35	14.7	83
    87	300028 SER B, 300093 ARG B, 300058 GLN C	3.64	115.13	-2.93	-0.83	19.07	94
    88	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.63	115.82	-2.53	-0.35	14.7	83
    89	100082 TYR C, 300093 ARG B, 300058 GLN C	3.63	116.83	-3.1	-0.14	19.05	72
    90	100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C	3.77	117.02	-2.43	-0.3	15.13	72
    91	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.81	118.22	-2.43	-0.3	15.13	72
    92	300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C	3.88	118.93	-2.2	-0.78	15.57	83
    93	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.89	122.63	-2.43	-0.3	15.13	72
    94	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	4.77	124.38	-1.58	0.04	12.4	61
    95	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	5.52	124.82	-2.22	-0.27	22.47	72
    96	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.9	124.97	-2.4	0.12	22.12	66
    97	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.24	125.54	-2.4	0.12	22.12	66
    98	300079 GLY C, 79 GLY C, 93 ARG B, 82 TYR C, 200079 GLY C	6.78	125.87	-1.4	-0.34	12.75	66
    99	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.62	126.71	-2.22	-0.27	22.47	72
    100	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.4	127.17	-2.3	-0.3	22.13	83
    101	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	3.49	130.54	-2.78	-0.18	26.82	83
    102	300093 ARG B, 300082 TYR C, 28 SER B	2.82	132.02	-2.2	-0.09	18.43	83
    103	300093 ARG B, 28 SER B	2.65	132.82	-2.65	-0.7	26.84	100
    104	300027 GLN B, 300093 ARG B, 28 SER B	2.62	137.72	-2.93	-0.83	19.07	94
    105	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.72	138.31	-2.4	-0.87	14.72	100
    106	300028 SER B, 300027 GLN B, 300093 ARG B	5	138.68	-2.93	-0.83	19.07	94
    107	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.99	139.44	-2.4	-0.87	14.72	100
    108	300028 SER B, 300027 GLN B, 28 SER B	5.02	142.72	-1.7	-1.01	2.29	106
    109	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6.01	143.82	-2.05	-0.99	3.03	95
    110	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.59	145.14	-2.05	-0.99	3.03	95
    111	300027 GLN B, 28 SER B, 27 GLN B	5.24	145.86	-1.57	-0.96	2.86	100
    112	300026 SER B, 300027 GLN B, 28 SER B	4.89	146.51	-1.57	-0.96	2.86	100
    113	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.24	148.69	-1.35	-0.91	2.56	102
    114	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	5.1	149.16	-1.28	-0.92	2.99	100
    115	300026 SER B, 28 SER B, 27 GLN B, 69 THR B, 26 SER B	4.83	151.59	-0.46	-0.79	3.04	107
    116	300026 SER B, 27 GLN B, 69 THR B, 26 SER B	4.69	152.61	-0.48	-0.79	2.95	107
    117	300026 SER B, 69 THR B, 26 SER B	4.46	155.02	-0.5	-0.79	2.81	107
    118	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.54	156.21	-1.5	-0.7	15.11	95
    119	300026 SER B, 69 THR B, 24 ARG B	4.62	157.46	-1.87	-0.66	19.01	95
    120	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	4.13	158.88	-2.28	-0.76	26.69	92
    121	300026 SER B, 24 ARG B, 70 ASP B	3.62	159.7	-2.8	-0.75	35.03	84
    122	24 ARG B, 70 ASP B, 300026 SER B	3.32	161.62	-2.93	-0.81	34.46	95
    123	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.52	163.54	-1.25	-0.32	25.88	85
    124	70 ASP B, 300026 SER B, 300003 LEU B	2.18	166.21	-0.17	-0.29	17.17	85
    125	70 ASP B, 300003 LEU B	2.25	168.99	0.15	0.05	24.92	70
    126	70 ASP B, 300003 LEU B, 300001 ASP B	2.89	171.03	-0.03	-0.23	17.74	70
    127	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.91	171.16	-0.2	-0.37	13.72	82
    128	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.93	172.11	-0.98	-0.43	25.3	83
    129	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.85	172.36	-1.56	-0.42	30.14	81
    130	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.71	173.24	-1.08	-0.27	25.25	79
    131	300003 LEU B, 300001 ASP B, 300063 LYS A	3.64	175.17	-1.2	-0.1	33.11	70
    132	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.68	177.17	-1.08	-0.27	25.25	79
    133	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.96	177.6	-1.08	-0.2	13.67	84
    134	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	4.04	178.42	-0.94	-0.32	11.61	84
    135	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.17	178.59	-2.4	-0.78	21.56	90
    136	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.19	178.86	-2.03	-0.87	14.58	96
    137	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.21	179.49	-2.4	-0.78	21.56	90
    138	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.21	180.5	-1.5	-0.4	21.26	76
    139	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	4.21	181.73	-1	-0.3	25.73	67
    140	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	4.21	184.56	0.23	0.35	24.92	76
    141	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	4.22	185.48	-1.1	-0.35	25.3	80
    142	300063 LYS A, 300046 GLU A, 300064 ILE A	4.14	190.54	-0.97	0.09	33.18	84
    143	300046 GLU A, 300064 ILE A, 300063 LYS A	4.09	191.38	0.2	-0.04	17.8	90
    144	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.72	194.05	-0.98	-0.14	26.35	87
    145	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.46	197.71	-2	-0.04	38.51	86
    146	300046 GLU A, 18 ARG B, 300040 ARG A	3.47	200.13	-4.17	-0.66	51.3	81
    147	300046 GLU A, 300064 ILE A, 300040 ARG A	3.03	200.71	-1.17	0.08	34.01	87
    148	300046 GLU A, 300040 ARG A	2.2	203.04	-4	-0.78	50.95	80
    149	300040 ARG A	1.58	209.81	-4.5	-0.42	52	83
    150	300040 ARG A, 300088 SER A	1.68	210.8	-2.45	-0.61	27.69	83
    151	300040 ARG A, 300088 SER A, 300091 SER A	1.85	211.32	-1.77	-0.67	19.59	83
    152	300040 ARG A, 300088 SER A, 300091 SER A	2.09	211.59	-1.9	-0.73	19.02	100
    153	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.39	211.87	-1.83	-0.57	14.66	86
    154	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.73	212.68	-1.73	-0.53	15.09	70
    155	300040 ARG A, 300088 SER A, 300041 PRO A	3.52	215.36	-2.17	-0.44	18.99	70
    156	300040 ARG A, 300041 PRO A, 300088 SER A	4.9	217.2	-2.3	-0.49	18.42	86
    157	300041 PRO A, 300088 SER A	4.7	218.69	-1.2	-0.53	1.63	87
    158	300091 SER A, 300041 PRO A, 300088 SER A	4.57	219.17	-1.07	-0.68	1.64	97
    159	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.45	219.58	0.15	-0.22	1.26	86
    160	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.35	219.88	0.02	0.3	1.25	69
    161	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.21	220.29	0.23	0.08	1.27	84
    162	300091 SER A, 300088 SER A, 300180 TYR A	4.17	220.39	-0.97	-0.28	1.65	94
    163	300091 SER A, 300088 SER A	4.15	220.53	-0.8	-0.97	1.67	117
    164	300091 SER A, 300088 SER A, 300180 TYR A	4.16	220.93	-0.97	-0.28	1.65	94
    165	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.18	221.66	0.02	0.3	1.25	69
    166	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.22	222.61	-0.06	0.08	1.67	69
    167	300041 PRO A, 300175 LEU A, 300180 TYR A	4.27	226.35	0.3	0.72	1.11	54
    168	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.43	226.66	0.13	0.34	1.68	54
    169	300041 PRO A, 300175 LEU A, 300180 TYR A	4.36	227.31	0.3	0.72	1.11	54
    170	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.48	227.96	0.13	0.34	1.68	54
    171	300041 PRO A, 300180 TYR A, 300173 ALA A	3.81	230.35	-1.1	0.07	2.19	54
    172	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.25	232.26	-1.7	-0.23	14.12	61
    173	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.24	234.19	-1.78	-0.53	14.11	64
    174	300041 PRO A, 300153 GLU A, 300172 PRO A	3.43	234.52	-2.23	-0.44	17.69	64
    175	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.33	235.1	-2.55	-0.52	14.11	74
    176	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.2	235.42	-2.55	-0.52	14.11	74
    177	300153 GLU A, 300172 PRO A, 300041 ASN B	2.88	236.27	-2.87	-0.67	18.29	79
    178	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.33	239.39	-2.25	-0.7	14.56	79
    179	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.34	239.95	-1.95	-0.88	15.01	90
    180	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A	2.37	240.37	-1.64	-0.86	12.68	90
    181	300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A	2.43	240.72	-0.8	-0.47	12.03	78
    182	300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A	2.57	241.64	-0.13	-0.31	2.57	79
    183	300041 ASN B, 300171 PHE A, 300182 LEU A	2.72	241.84	-0.03	-0.14	2.3	79
    184	300041 ASN B, 300182 LEU A, 300170 THR A	2.7	242.14	-0.13	-0.13	1.72	88
    185	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.66	243.44	-0.2	-0.3	2.14	88
    186	300041 ASN B, 300170 THR A, 300155 VAL A	2.69	247.28	-1.53	-0.78	2.81	105
    187	300041 ASN B, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A	2.9	247.51	-1.14	-0.78	2.69	106
    188	300041 ASN B, 300156 THR A, 300157 VAL A	2.96	247.82	-1.53	-0.78	2.81	105
    189	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.14	247.98	-1.33	-0.78	2.52	106
    190	300041 ASN B, 300170 THR A, 300157 VAL A	3.19	248.07	-1.53	-0.78	2.81	105
    191	300041 ASN B, 300170 THR A, 300155 VAL A	3.23	248.24	-1.53	-0.78	2.81	105
    192	300041 ASN B, 300170 THR A, 300157 VAL A	3.28	248.38	-1.53	-0.78	2.81	105
    193	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.28	248.92	-1.33	-0.78	2.52	106
    194	300041 ASN B, 300170 THR A, 300157 VAL A	3.27	251.95	-1.53	-0.78	2.81	105
    195	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B	4.02	252.76	-1.25	-0.79	2.95	105
    196	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.51	252.91	-1.08	-0.79	3.04	105
    197	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.62	253.11	0.68	-0.31	2.14	102
    198	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.57	253.24	-1.16	-0.72	12.26	89
    199	300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.63	253.28	-0.13	-0.22	14.1	85
    200	300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B	4.4	254.02	-0.2	-0.21	13.67	92
    201	300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A	4.1	254.37	-0.13	-0.22	14.1	85
    202	300168 VAL A, 300169 LYS B, 300165 SER A	1.98	259	-0.03	-0.03	17.67	85
    203	300168 VAL A, 300169 LYS B, 300165 SER A	1.23	260.69	-1.57	-0.67	18.75	72
    204	300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A	1.26	261.94	-1.28	-0.7	14.91	72
    205	300168 VAL A, 300169 LYS B, 300167 GLY A	1.74	262.82	-1.57	-0.67	18.75	72
    206	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.86	263.1	-1.98	-0.44	26.97	81
    207	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.9	263.37	-1.98	-0.44	26.97	81
    208	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	2	263.48	-1.98	-0.44	26.97	81
    209	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	2.05	263.93	-1.98	-0.44	26.97	81
    210	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	2.04	264.58	-2.75	-0.5	38.55	83
    211	300169 LYS B, 300167 GLY A, 300167 ASP B	1.93	265.91	-2.6	-0.75	34.19	79
    212	300169 LYS B, 300167 GLY A	1.86	266.64	-2.15	-0.61	26.44	72
    213	300169 LYS B, 300167 GLY A, 300166 SER A	1.71	268.06	-1.57	-0.67	18.75	72
    214	300169 LYS B, 300167 GLY A, 300166 SER A	1.73	271.63	-1.7	-0.73	18.18	94
    215	300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B	3.5	272.79	-2.15	-0.81	26.06	91
    216	300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B	4.14	273.7	-1.28	-0.9	14.53	101
    217	300167 GLY A, 300166 SER A, 300170 ASP B	4.41	274.48	-1.57	-0.94	18.25	101
    218	300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A	4.72	275.4	-0.7	-0.45	14.05	98
    219	300167 GLY A, 300170 ASP B, 300140 MET A	4.39	276.96	-0.67	-0.28	18.17	89
    220	300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B	4.12	278.19	-1.38	-0.4	14.47	94
    221	300170 ASP B, 300140 MET A, 300138 ASN B	3.89	279.79	-1.7	-0.27	18.17	94
    222	300140 MET A, 300138 ASN B, 300187 THR A	3.5	281.74	-0.77	-0.18	2.16	101
    223	300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B	3.11	283.2	-0.75	-0.33	2.03	102
    224	300140 MET A, 300187 THR A, 300114 THR B	2.84	285.39	0.17	-0.18	1.58	102
    225	300140 MET A, 300114 THR B	2.8	286.09	0.6	0.12	1.55	100
    226	300140 MET A, 300114 THR B, 300138 ASN A	2.77	286.69	-0.77	-0.18	2.16	101
    227	300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A	2.73	287.88	-0.78	-0.38	2.04	105
    228	300140 MET A, 300114 THR B, 300138 ASN A	2.75	288.73	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

22. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100088 SER A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 79 GLY C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 200026 SER B, 100069 THR B, 100027 GLN B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200002 ILE B, 200098 PHE B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A, 200170 THR A, 200155 VAL A, 200157 VAL A, 200156 THR A, 200040 THR B, 200168 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A, 200169 HIS A, 200167 ASP B, 200166 SER A, 200166 SER A, 200170 ASP B, 200169 LYS B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A, 200168 VAL A, 200169 LYS B, 200169 HIS A, 200167 ASP B, 200166 SER A, 200170 ASP B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A

    Physicochemical properties of lining side-chains

    Charge: 2 (13-11)
    Hydropathy: -1.4
    Hydrophobicity: -0.44
    Polarity: 14.73
    Mutability: 89
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.16	0.19	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.11	2	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.25	3.95	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.7	4.19	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.76	4.71	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.73	5.06	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.69	5.35	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.56	6.48	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.48	7.08	-2.55	-0.52	14.11	74
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.41	7.7	-2.55	-0.52	14.11	74
    11	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.26	10.04	-1.78	-0.53	14.11	64
    12	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.28	12.06	-1.7	-0.23	14.12	61
    13	100041 PRO A, 100173 ALA A, 100180 TYR A	3.65	14.24	-1.1	0.07	2.19	54
    14	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.31	14.66	0.13	0.34	1.68	54
    15	100041 PRO A, 100180 TYR A, 100175 LEU A	4.35	15.32	0.3	0.72	1.11	54
    16	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.32	15.74	0.13	0.34	1.68	54
    17	100041 PRO A, 100180 TYR A, 100175 LEU A	4.18	20.07	0.3	0.72	1.11	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A	4.13	20.84	0.02	0.3	1.25	69
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.1	21.29	0.02	0.3	1.25	69
    20	100180 TYR A, 100091 SER A, 100088 SER A	4.09	21.47	-0.97	-0.28	1.65	94
    21	100091 SER A, 100088 SER A	4.09	21.54	-0.8	-0.97	1.67	117
    22	100180 TYR A, 100091 SER A, 100088 SER A	4.13	21.93	-0.97	-0.28	1.65	94
    23	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.3	22.22	0.23	0.08	1.27	84
    24	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.42	22.6	0.02	0.3	1.25	69
    25	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.55	23.08	0.15	-0.22	1.26	86
    26	100041 PRO A, 100091 SER A, 100088 SER A	4.68	24.12	-1.07	-0.68	1.64	97
    27	100041 PRO A, 100088 SER A	4.91	24.96	-1.2	-0.53	1.63	87
    28	100041 PRO A, 100088 SER A, 100040 ARG A	4.28	27.76	-2.3	-0.49	18.42	86
    29	100041 PRO A, 100040 ARG A, 100088 SER A	3.22	29.56	-2.17	-0.44	18.99	70
    30	100041 PRO A, 100040 ARG A, 100088 SER A, 100091 SER A	2.52	30.28	-1.73	-0.53	15.09	70
    31	100040 ARG A, 100088 SER A, 100091 SER A	1.95	31.67	-1.77	-0.67	19.59	83
    32	100040 ARG A, 100088 SER A	1.97	32.88	-2.45	-0.61	27.69	83
    33	100040 ARG A	2.07	39.07	-4.5	-0.42	52	83
    34	100040 ARG A, 100043 HIS A	2.9	40.18	-3.85	-0.08	51.8	87
    35	100040 ARG A, 100046 GLU A	3.1	43.67	-4	-0.78	50.95	80
    36	100040 ARG A, 100046 GLU A, 300018 ARG B	3.58	45.95	-4.17	-0.66	51.3	81
    37	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.4	49.65	-2	-0.04	38.51	86
    38	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.17	53.29	-0.98	-0.14	26.35	87
    39	100046 GLU A, 100064 ILE A, 100063 LYS A	3.51	58.21	-0.97	0.09	33.18	84
    40	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.5	58.62	-0.93	-0.18	25.3	92
    41	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.49	59.04	-1.1	-0.35	25.3	80
    42	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.73	63.41	0.23	0.35	24.92	76
    43	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	4.47	64.22	-1.5	-0.4	21.26	76
    44	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.24	64.62	-2.4	-0.78	21.56	90
    45	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	3.82	65.03	-2.03	-0.87	14.58	96
    46	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	3.75	65.27	-2.4	-0.78	21.56	90
    47	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.71	65.95	-0.94	-0.32	11.61	84
    48	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.72	66.4	-0.3	-0.21	13.67	77
    49	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.74	66.87	-0.3	-0.21	13.67	77
    50	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.77	68.48	-1.08	-0.27	25.25	79
    51	100063 LYS A, 100003 LEU B, 100001 ASP B	3.87	70.36	-1.2	-0.1	33.11	70
    52	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.99	71.33	-1.08	-0.27	25.25	79
    53	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.06	71.54	-1.56	-0.42	30.14	81
    54	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.81	72.36	-0.98	-0.43	25.3	83
    55	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.77	72.55	-0.2	-0.37	13.72	82
    56	100003 LEU B, 300070 ASP B, 100001 ASP B	3.09	74.53	-0.03	-0.23	17.74	70
    57	100003 LEU B, 300070 ASP B	2.16	77.32	0.15	0.05	24.92	70
    58	100003 LEU B, 300070 ASP B, 100026 SER B	2.11	79.97	-0.17	-0.29	17.17	85
    59	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.55	81.86	-1.25	-0.32	25.88	85
    60	300070 ASP B, 100026 SER B, 300024 ARG B	3.28	83.66	-2.93	-0.81	34.46	95
    61	300070 ASP B, 300024 ARG B, 100026 SER B	3.56	84.91	-2.8	-0.75	35.03	84
    62	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.95	86.67	-2.28	-0.76	26.69	92
    63	300024 ARG B, 100026 SER B, 300069 THR B	4.69	87.73	-1.87	-0.66	19.01	95
    64	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.87	88.68	-1.5	-0.7	15.11	95
    65	100026 SER B, 300069 THR B, 300026 SER B	4.32	91.97	-0.5	-0.79	2.81	107
    66	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.3	92.94	-0.48	-0.79	2.95	107
    67	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.35	94.52	-0.46	-0.79	3.04	107
    68	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.69	94.87	-1.28	-0.92	2.99	100
    69	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.63	97.58	-1.35	-0.91	2.56	102
    70	100026 SER B, 100027 GLN B, 300028 SER B	4.86	98.3	-1.57	-0.96	2.86	100
    71	300027 GLN B, 100027 GLN B, 300028 SER B	5.08	99	-1.57	-0.96	2.86	100
    72	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.35	99.98	-2.05	-0.99	3.03	95
    73	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.88	101.13	-2.05	-0.99	3.03	95
    74	100027 GLN B, 300028 SER B, 100028 SER B	5.14	104.42	-1.7	-1.01	2.29	106
    75	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.7	104.79	-2.4	-0.87	14.72	100
    76	100027 GLN B, 100028 SER B, 100093 ARG B	4.28	105.22	-2.93	-0.83	19.07	94
    77	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.17	105.65	-2.4	-0.87	14.72	100
    78	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.06	106.3	-2.3	-0.82	15.15	94
    79	100027 GLN B, 300028 SER B, 100093 ARG B	3.27	111.35	-2.93	-0.83	19.07	94
    80	300028 SER B, 100093 ARG B	3.29	112.13	-2.65	-0.7	26.84	100
    81	300028 SER B, 100093 ARG B, 100082 TYR C	3.39	113.35	-2.2	-0.09	18.43	83
    82	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.82	116.63	-2.78	-0.18	26.82	83
    83	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.21	117.06	-2.3	-0.3	22.13	83
    84	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.45	117.79	-2.22	-0.27	22.47	72
    85	300093 ARG B, 300079 GLY C, 100079 GLY C, 79 GLY C, 300082 TYR C	6.71	118.07	-1.4	-0.34	12.75	66
    86	79 GLY C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C	6.4	118.5	-2.4	0.12	22.12	66
    87	300093 ARG B, 79 GLY C, 300082 TYR C, 93 ARG B, 82 TYR C	6.07	118.93	-2.4	0.12	22.12	66
    88	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	5.66	119.68	-2.22	-0.27	22.47	72
    89	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	4.72	121.74	-1.58	0.04	12.4	61
    90	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.28	124.69	-2.43	-0.3	15.13	72
    91	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.29	125.47	-2.2	-0.78	15.57	83
    92	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.49	126.68	-2.43	-0.3	15.13	72
    93	100093 ARG B, 200082 TYR C, 100058 GLN C	3.78	127.76	-3.1	-0.14	19.05	72
    94	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.78	128.3	-2.53	-0.35	14.7	83
    95	100028 SER B, 100093 ARG B, 100058 GLN C	3.92	128.66	-2.93	-0.83	19.07	94
    96	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.6	129.63	-2.53	-0.35	14.7	83
    97	100028 SER B, 100093 ARG B, 200082 TYR C	3.36	130.04	-2.2	-0.09	18.43	83
    98	100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C	3.12	130.53	-2.78	-0.18	26.82	83
    99	100028 SER B, 200093 ARG B, 200082 TYR C	2.7	131.95	-2.2	-0.09	18.43	83
    100	100028 SER B, 200093 ARG B	2.6	132.75	-2.65	-0.7	26.84	100
    101	200027 GLN B, 100028 SER B, 200093 ARG B	2.6	137.53	-2.93	-0.83	19.07	94
    102	200027 GLN B, 100028 SER B, 200093 ARG B, 200028 SER B	4.65	138.04	-2.3	-0.82	15.15	94
    103	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.85	138.28	-2.4	-0.87	14.72	100
    104	200027 GLN B, 200028 SER B, 200093 ARG B	4.96	138.66	-2.93	-0.83	19.07	94
    105	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.97	139.27	-2.4	-0.87	14.72	100
    106	200027 GLN B, 200028 SER B, 100028 SER B	4.99	142.61	-1.7	-1.01	2.29	106
    107	200027 GLN B, 200028 SER B, 100028 SER B, 28 SER B	5.94	142.93	-1.48	-1	2.14	108
    108	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.14	143.65	-2.05	-0.99	3.03	95
    109	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	5.72	144.88	-2.05	-0.99	3.03	95
    110	100027 GLN B, 200027 GLN B, 100028 SER B	5.37	145.6	-2.6	-1.06	2.91	95
    111	200027 GLN B, 100028 SER B, 200026 SER B	5.02	146.29	-1.57	-0.96	2.86	100
    112	200027 GLN B, 100028 SER B, 200026 SER B, 100069 THR B	4.23	148.79	-1.35	-0.91	2.56	102
    113	200027 GLN B, 100028 SER B, 200026 SER B, 100027 GLN B	5.12	149.01	-1.28	-0.92	2.99	100
    114	100026 SER B, 100028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.75	152.18	-0.46	-0.79	3.04	107
    115	100026 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.62	153.16	-0.48	-0.79	2.95	107
    116	100026 SER B, 200026 SER B, 100069 THR B	4.47	154.92	-0.5	-0.79	2.81	107
    117	100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B	4.51	155.96	-1.5	-0.7	15.11	95
    118	200026 SER B, 100069 THR B, 100024 ARG B	4.56	157.79	-1.87	-0.66	19.01	95
    119	200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B	4.04	159.03	-2.28	-0.76	26.69	92
    120	200026 SER B, 100024 ARG B, 100070 ASP B	3.62	159.75	-2.8	-0.75	35.03	84
    121	100024 ARG B, 100070 ASP B, 200026 SER B	3.24	161.83	-2.93	-0.81	34.46	95
    122	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.44	163.78	-1.25	-0.32	25.88	85
    123	100070 ASP B, 200026 SER B, 200003 LEU B	2.18	166.46	-0.17	-0.29	17.17	85
    124	100070 ASP B, 200003 LEU B	2.28	169.17	0.15	0.05	24.92	70
    125	100070 ASP B, 200003 LEU B, 200001 ASP B	2.96	171.09	-0.03	-0.23	17.74	70
    126	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	3.91	172.19	-0.98	-0.43	25.3	83
    127	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.7	173.41	-1.08	-0.27	25.25	79
    128	200003 LEU B, 200001 ASP B, 200063 LYS A	3.64	175.34	-1.2	-0.1	33.11	70
    129	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.69	176.84	-1.08	-0.27	25.25	79
    130	200003 LEU B, 200063 LYS A, 200097 THR B, 200002 ILE B	3.9	177.29	-0.3	-0.21	13.67	77
    131	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B	3.98	177.7	-0.3	-0.21	13.67	77
    132	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A	4.05	178.47	-0.94	-0.32	11.61	84
    133	200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.18	178.62	-2.4	-0.78	21.56	90
    134	200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.19	178.97	-2.03	-0.87	14.58	96
    135	200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.21	179.69	-2.4	-0.78	21.56	90
    136	200003 LEU B, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.21	180.76	-1.5	-0.4	21.26	76
    137	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	4.21	182	-1	-0.3	25.73	67
    138	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	4.21	184.63	0.23	0.35	24.92	76
    139	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	4.22	185.64	-1.1	-0.35	25.3	80
    140	200063 LYS A, 200046 GLU A, 200064 ILE A	4.14	190.69	-0.97	0.09	33.18	84
    141	200046 GLU A, 200064 ILE A, 200063 LYS A	4.09	191.52	0.2	-0.04	17.8	90
    142	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.7	194.15	-0.98	-0.14	26.35	87
    143	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.46	197.79	-2	-0.04	38.51	86
    144	200046 GLU A, 100018 ARG B, 200040 ARG A	3.43	200.18	-4.17	-0.66	51.3	81
    145	200046 GLU A, 200064 ILE A, 200040 ARG A	3	200.78	-1.17	0.08	34.01	87
    146	200046 GLU A, 200040 ARG A	2.18	203.16	-4	-0.78	50.95	80
    147	200040 ARG A	1.58	209.89	-4.5	-0.42	52	83
    148	200040 ARG A, 200088 SER A	1.68	210.84	-2.45	-0.61	27.69	83
    149	200040 ARG A, 200088 SER A, 200091 SER A	1.86	211.35	-1.77	-0.67	19.59	83
    150	200040 ARG A, 200088 SER A, 200091 SER A	2.1	211.62	-1.9	-0.73	19.02	100
    151	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.4	211.89	-1.83	-0.57	14.66	86
    152	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.74	212.71	-1.73	-0.53	15.09	70
    153	200040 ARG A, 200088 SER A, 200041 PRO A	3.52	215.38	-2.17	-0.44	18.99	70
    154	200040 ARG A, 200041 PRO A, 200088 SER A	4.9	217.21	-2.3	-0.49	18.42	86
    155	200041 PRO A, 200088 SER A	4.71	218.69	-1.2	-0.53	1.63	87
    156	200091 SER A, 200041 PRO A, 200088 SER A	4.57	219.18	-1.07	-0.68	1.64	97
    157	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.45	219.59	0.15	-0.22	1.26	86
    158	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.35	219.89	0.02	0.3	1.25	69
    159	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.21	220.3	0.23	0.08	1.27	84
    160	200091 SER A, 200088 SER A, 200180 TYR A	4.17	220.4	-0.97	-0.28	1.65	94
    161	200091 SER A, 200088 SER A	4.15	220.54	-0.8	-0.97	1.67	117
    162	200091 SER A, 200088 SER A, 200180 TYR A	4.16	220.92	-0.97	-0.28	1.65	94
    163	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.18	221.62	0.02	0.3	1.25	69
    164	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.22	222.55	-0.06	0.08	1.67	69
    165	200041 PRO A, 200175 LEU A, 200180 TYR A	4.27	226.35	0.3	0.72	1.11	54
    166	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.43	226.67	0.13	0.34	1.68	54
    167	200041 PRO A, 200175 LEU A, 200180 TYR A	4.36	227.31	0.3	0.72	1.11	54
    168	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.5	227.91	0.13	0.34	1.68	54
    169	200041 PRO A, 200180 TYR A, 200173 ALA A	3.85	230.27	-1.1	0.07	2.19	54
    170	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.26	232.19	-1.7	-0.23	14.12	61
    171	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.24	234.47	-1.78	-0.53	14.11	64
    172	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.35	235.05	-2.55	-0.52	14.11	74
    173	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.08	235.73	-2.55	-0.52	14.11	74
    174	200153 GLU A, 200172 PRO A, 200041 ASN B	2.92	236.17	-2.87	-0.67	18.29	79
    175	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.33	239.25	-2.25	-0.7	14.56	79
    176	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.33	240.29	-1.95	-0.88	15.01	90
    177	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A	2.41	240.58	-0.8	-0.47	12.03	78
    178	200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A	2.48	240.78	-0.8	-0.47	12.03	78
    179	200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A	2.61	241.59	-0.13	-0.31	2.57	79
    180	200041 ASN B, 200182 LEU A, 200171 PHE A	2.73	241.8	-0.03	-0.14	2.3	79
    181	200041 ASN B, 200182 LEU A, 200170 THR A	2.7	242.13	-0.13	-0.13	1.72	88
    182	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.66	243.22	-0.2	-0.3	2.14	88
    183	200041 ASN B, 200170 THR A, 200155 VAL A	2.69	247.14	-1.53	-0.78	2.81	105
    184	200041 ASN B, 200170 THR A, 200155 VAL A, 200157 VAL A	2.87	247.46	-1.25	-0.79	2.95	105
    185	200041 ASN B, 200157 VAL A, 200156 THR A	2.94	247.78	-1.53	-0.78	2.81	105
    186	200041 ASN B, 200170 THR A, 200157 VAL A, 200156 THR A	3.12	247.95	-1.33	-0.78	2.52	106
    187	200041 ASN B, 200170 THR A, 200157 VAL A	3.17	248.07	-1.53	-0.78	2.81	105
    188	200041 ASN B, 200170 THR A, 200155 VAL A	3.22	248.23	-1.53	-0.78	2.81	105
    189	200041 ASN B, 200170 THR A, 200157 VAL A	3.28	248.44	-1.53	-0.78	2.81	105
    190	200041 ASN B, 200170 THR A, 200157 VAL A, 200156 THR A	3.28	248.86	-1.33	-0.78	2.52	106
    191	200041 ASN B, 200170 THR A, 200157 VAL A	3.27	251.77	-1.53	-0.78	2.81	105
    192	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B	3.93	252.86	-1.25	-0.79	2.95	105
    193	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.57	252.98	-1.08	-0.79	3.04	105
    194	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.65	253.11	0.68	-0.31	2.14	102
    195	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.57	253.23	-1.16	-0.72	12.26	89
    196	200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.6	253.28	-0.13	-0.22	14.1	85
    197	200170 THR A, 200157 VAL A, 200168 VAL A, 200169 LYS B	4.29	254.16	-0.2	-0.21	13.67	92
    198	200157 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A	3.95	254.61	-0.13	-0.22	14.1	85
    199	200168 VAL A, 200169 LYS B, 200165 SER A	2.22	258.43	-0.03	-0.03	17.67	85
    200	200168 VAL A, 200169 LYS B, 200165 SER A	1.23	260.74	-1.57	-0.67	18.75	72
    201	200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A	1.28	262.13	-1.28	-0.7	14.91	72
    202	200168 VAL A, 200169 LYS B, 200167 GLY A	1.77	262.96	-1.57	-0.67	18.75	72
    203	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.87	263.18	-1.98	-0.44	26.97	81
    204	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.91	263.41	-1.98	-0.44	26.97	81
    205	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	2.01	263.44	-1.98	-0.44	26.97	81
    206	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	2.03	263.86	-1.98	-0.44	26.97	81
    207	200169 LYS B, 200167 GLY A, 200169 HIS A, 200167 ASP B	2.03	264.78	-2.75	-0.5	38.55	83
    208	200169 LYS B, 200167 GLY A, 200167 ASP B	1.91	266.15	-2.6	-0.75	34.19	79
    209	200169 LYS B, 200167 GLY A	1.84	266.87	-2.15	-0.61	26.44	72
    210	200169 LYS B, 200167 GLY A, 200166 SER A	1.71	268.13	-1.57	-0.67	18.75	72
    211	200169 LYS B, 200167 GLY A, 200166 SER A	1.74	268.27	-1.7	-0.73	18.18	94
    212	200169 LYS B, 200166 SER A	1.97	268.49	-2.35	-0.69	25.59	94
    213	200169 LYS B, 200167 GLY A, 200166 SER A	2.17	271.75	-1.7	-0.73	18.18	94
    214	200169 LYS B, 200167 GLY A, 200166 SER A, 200170 ASP B	3.53	272.91	-2.15	-0.81	26.06	91
    215	200167 GLY A, 200166 SER A, 200170 ASP B, 200169 LYS B	4.16	273.36	-1.28	-0.9	14.53	101
    216	200167 GLY A, 200166 SER A, 200170 ASP B	4.29	274.55	-1.57	-0.94	18.25	101
    217	200167 GLY A, 200166 SER A, 200170 ASP B, 200140 MET A	4.75	275.46	-0.7	-0.45	14.05	98
    218	200167 GLY A, 200170 ASP B, 200140 MET A	4.38	277.04	-0.67	-0.28	18.17	89
    219	200167 GLY A, 200170 ASP B, 200140 MET A, 200138 ASN B	4.11	278.25	-1.38	-0.4	14.47	94
    220	200170 ASP B, 200140 MET A, 200138 ASN B	3.88	279.84	-1.7	-0.27	18.17	94
    221	200140 MET A, 200138 ASN B, 200187 THR A	3.5	281.79	-0.77	-0.18	2.16	101
    222	200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B	3.1	283.24	-0.75	-0.33	2.03	102
    223	200140 MET A, 200187 THR A, 200114 THR B	2.84	285.44	0.17	-0.18	1.58	102
    224	200140 MET A, 200114 THR B	2.8	286.14	0.6	0.12	1.55	100
    225	200140 MET A, 200114 THR B, 200138 ASN A	2.76	286.73	-0.77	-0.18	2.16	101
    226	200140 MET A, 200114 THR B, 200138 ASN A, 200139 SER A	2.73	287.91	-0.78	-0.38	2.04	105
    227	200140 MET A, 200114 THR B, 200138 ASN A	2.75	288.75	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

23. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 200026 SER B, 100069 THR B, 100027 GLN B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A, 200170 THR A, 200155 VAL A, 200156 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A, 200169 HIS A, 200167 ASP B, 200166 SER A, 200166 SER A, 200170 ASP B, 200169 LYS B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A, 200168 VAL A, 200169 LYS B, 200169 HIS A, 200167 ASP B, 200166 SER A, 200170 ASP B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A

    Physicochemical properties of lining side-chains

    Charge: 3 (13-10)
    Hydropathy: -1.4
    Hydrophobicity: -0.44
    Polarity: 14.63
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.26	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.3	0.47	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.22	0.72	-1.53	-0.78	2.81	105
    4	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.08	1.04	-1.33	-0.78	2.52	106
    5	100156 THR A, 100157 VAL A, 100041 ASN B	2.9	1.25	-1.53	-0.78	2.81	105
    6	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	2.81	1.74	-1.33	-0.78	2.52	106
    7	100170 THR A, 100041 ASN B, 100155 VAL A	2.62	5.73	-1.53	-0.78	2.81	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.63	6.6	-0.2	-0.3	2.14	88
    9	100170 THR A, 100041 ASN B, 100182 LEU A	2.75	7.01	-0.13	-0.13	1.72	88
    10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.74	7.2	-0.03	-0.14	2.3	79
    11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.62	7.92	-0.13	-0.31	2.57	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.6	8.53	-0.8	-0.47	12.03	78
    13	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.59	9.08	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.58	9.74	-1.95	-0.88	15.01	90
    15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.59	12.79	-2.25	-0.7	14.56	79
    16	100041 ASN B, 100153 GLU A, 100172 PRO A	2.88	13.18	-2.87	-0.67	18.29	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	2.99	13.8	-2.55	-0.52	14.11	74
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.21	14.47	-2.55	-0.52	14.11	74
    19	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.36	16.98	-1.78	-0.53	14.11	64
    20	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.34	19.18	-1.7	-0.23	14.12	61
    21	100173 ALA A, 100041 PRO A, 100180 TYR A	3.58	20.88	-1.1	0.07	2.19	54
    22	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.07	21.37	0.13	0.34	1.68	54
    23	100041 PRO A, 100180 TYR A, 100175 LEU A	4.41	22.07	0.3	0.72	1.11	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.2	22.59	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.04	27.23	0.3	0.72	1.11	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.06	27.85	-0.06	0.08	1.67	69
    27	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.1	28.14	0.23	0.08	1.27	84
    28	100091 SER A, 100088 SER A	4.15	28.22	-0.8	-0.97	1.67	117
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.23	28.58	-0.97	-0.28	1.65	94
    30	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.45	28.85	0.23	0.08	1.27	84
    31	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.59	29.23	0.02	0.3	1.25	69
    32	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.73	29.71	0.15	-0.22	1.26	86
    33	100041 PRO A, 100091 SER A, 100088 SER A	4.88	30.79	-1.07	-0.68	1.64	97
    34	100041 PRO A, 100088 SER A	5.14	31.68	-1.2	-0.53	1.63	87
    35	100041 PRO A, 100088 SER A, 100040 ARG A	4.54	33.92	-2.3	-0.49	18.42	86
    36	100041 PRO A, 100088 SER A, 100040 ARG A	2.77	36.43	-2.17	-0.44	18.99	70
    37	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.19	36.81	-1.73	-0.53	15.09	70
    38	100088 SER A, 100040 ARG A, 100091 SER A	0.66	37.99	-1.77	-0.67	19.59	83
    39	100088 SER A, 100040 ARG A	0.37	39.04	-2.45	-0.61	27.69	83
    40	100040 ARG A	0.25	45.45	-4.5	-0.42	52	83
    41	100040 ARG A, 100043 HIS A	1.84	46.67	-3.85	-0.08	51.8	87
    42	100040 ARG A, 100043 HIS A, 100046 GLU A	2.52	47.67	-3.73	-0.43	51.17	83
    43	100040 ARG A, 100046 GLU A	3.19	50.34	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	4.39	52.71	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.43	55.99	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A	3.62	56.65	-1.17	0.08	34.01	87
    47	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.54	59.68	-0.98	-0.14	26.35	87
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.48	60.55	0.2	-0.04	17.8	90
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.38	64.86	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	3.84	65.31	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.02	65.73	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.2	70.25	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	4.59	71.02	-1.5	-0.4	21.26	76
    54	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.58	71.35	-2.4	-0.78	21.56	90
    55	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.46	71.54	-2.03	-0.87	14.58	96
    56	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.37	71.77	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	4.03	72.81	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.91	73.29	-1.08	-0.2	13.67	84
    59	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.59	75.57	-1.08	-0.27	25.25	79
    60	100063 LYS A, 100003 LEU B, 100001 ASP B	3.58	76.89	-1.2	-0.1	33.11	70
    61	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.65	77.95	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.89	78.18	-1.56	-0.42	30.14	81
    63	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.91	79.07	-0.98	-0.43	25.3	83
    64	100003 LEU B, 300070 ASP B, 100001 ASP B	3.03	81.05	-0.03	-0.23	17.74	70
    65	100003 LEU B, 300070 ASP B	2.25	83.94	0.15	0.05	24.92	70
    66	100003 LEU B, 300070 ASP B, 100026 SER B	2.19	86.69	-0.17	-0.29	17.17	85
    67	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.51	88.65	-1.25	-0.32	25.88	85
    68	300070 ASP B, 100026 SER B, 300024 ARG B	3.25	90.31	-2.93	-0.81	34.46	95
    69	300070 ASP B, 300024 ARG B, 100026 SER B	3.56	91.47	-2.8	-0.75	35.03	84
    70	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.88	93.27	-2.28	-0.76	26.69	92
    71	300024 ARG B, 100026 SER B, 300069 THR B	4.62	94.38	-1.87	-0.66	19.01	95
    72	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	5.01	95.41	-1.5	-0.7	15.11	95
    73	100026 SER B, 300069 THR B, 300026 SER B	4.56	97.9	-0.5	-0.79	2.81	107
    74	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.44	98.96	-0.48	-0.79	2.95	107
    75	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.35	101.05	-0.46	-0.79	3.04	107
    76	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	4.42	101.24	-0.58	-0.84	2.52	112
    77	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	4.5	101.42	-1.28	-0.92	2.99	100
    78	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.58	104.15	-1.35	-0.91	2.56	102
    79	100026 SER B, 300028 SER B, 100027 GLN B	5.15	104.9	-1.57	-0.96	2.86	100
    80	300027 GLN B, 300028 SER B, 100027 GLN B	5.32	105.63	-1.57	-0.96	2.86	100
    81	300028 SER B, 100027 GLN B, 100028 SER B, 300027 GLN B	5.53	106.64	-2.05	-0.99	3.03	95
    82	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6	107.37	-2.05	-0.99	3.03	95
    83	100027 GLN B, 200028 SER B, 100028 SER B	6.59	107.91	-1.7	-1.01	2.29	106
    84	300028 SER B, 100027 GLN B, 100028 SER B	5.71	111.2	-1.7	-1.01	2.29	106
    85	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	5.02	111.5	-2.4	-0.87	14.72	100
    86	100027 GLN B, 100028 SER B, 100093 ARG B	3.9	112.1	-2.93	-0.83	19.07	94
    87	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	3.56	112.71	-2.4	-0.87	14.72	100
    88	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	3.26	113.48	-2.3	-0.82	15.15	94
    89	300028 SER B, 100027 GLN B, 100093 ARG B	2.75	117.95	-2.93	-0.83	19.07	94
    90	300028 SER B, 100093 ARG B	3.21	118.76	-2.65	-0.7	26.84	100
    91	300028 SER B, 100093 ARG B, 100082 TYR C	3.47	120.02	-2.2	-0.09	18.43	83
    92	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.1	122.94	-2.78	-0.18	26.82	83
    93	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.04	123.86	-2.3	-0.3	22.13	83
    94	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.5	124.56	-2.22	-0.27	22.47	72
    95	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.77	124.83	-1.58	0.04	12.4	61
    96	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.81	125.04	-2.4	0.12	22.12	66
    97	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.59	126.01	-2.4	0.12	22.12	66
    98	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	6.06	128.08	-1.58	0.04	12.4	61
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.69	129.17	-1.88	0.25	14.65	61
    100	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	4.03	131.3	-2.43	-0.3	15.13	72
    101	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.46	132.1	-2.2	-0.78	15.57	83
    102	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.26	133.15	-2.43	-0.3	15.13	72
    103	100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C	3.51	133.36	-2.43	-0.3	15.13	72
    104	100093 ARG B, 200082 TYR C, 100058 GLN C	3.59	134.21	-3.1	-0.14	19.05	72
    105	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.65	134.49	-2.43	-0.3	15.13	72
    106	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.6	134.87	-2.53	-0.35	14.7	83
    107	100028 SER B, 100093 ARG B, 100058 GLN C	3.57	135.21	-2.93	-0.83	19.07	94
    108	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.68	136.58	-2.53	-0.35	14.7	83
    109	100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C	3.91	137.07	-2.78	-0.18	26.82	83
    110	100028 SER B, 200093 ARG B, 200082 TYR C	3.87	138.5	-2.2	-0.09	18.43	83
    111	100028 SER B, 200093 ARG B	3.79	139.33	-2.65	-0.7	26.84	100
    112	200027 GLN B, 100028 SER B, 200093 ARG B	3.36	144.29	-2.93	-0.83	19.07	94
    113	200027 GLN B, 100028 SER B, 200093 ARG B, 200028 SER B	3.57	144.75	-2.3	-0.82	15.15	94
    114	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	3.74	144.95	-2.4	-0.87	14.72	100
    115	200027 GLN B, 200028 SER B, 200093 ARG B	3.95	145.34	-2.93	-0.83	19.07	94
    116	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.77	146.18	-2.4	-0.87	14.72	100
    117	200027 GLN B, 200028 SER B, 100028 SER B	5.38	149.47	-1.7	-1.01	2.29	106
    118	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.94	150.21	-2.05	-0.99	3.03	95
    119	200027 GLN B, 200028 SER B, 100028 SER B	5.68	150.76	-1.7	-1.01	2.29	106
    120	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	5.4	151.45	-2.05	-0.99	3.03	95
    121	100027 GLN B, 200027 GLN B, 100028 SER B	5.12	152.21	-2.6	-1.06	2.91	95
    122	200027 GLN B, 100028 SER B, 200026 SER B	4.88	152.92	-1.57	-0.96	2.86	100
    123	200027 GLN B, 100028 SER B, 200026 SER B, 100069 THR B	4.59	155.32	-1.35	-0.91	2.56	102
    124	200027 GLN B, 100028 SER B, 200026 SER B, 100027 GLN B	4.82	155.8	-1.28	-0.92	2.99	100
    125	100026 SER B, 100028 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.45	158.34	-0.46	-0.79	3.04	107
    126	100026 SER B, 200026 SER B, 100069 THR B, 100027 GLN B	4.36	159.4	-0.48	-0.79	2.95	107
    127	100026 SER B, 200026 SER B, 100069 THR B	4.32	161.46	-0.5	-0.79	2.81	107
    128	100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B	4.53	162.53	-1.5	-0.7	15.11	95
    129	200026 SER B, 100069 THR B, 100024 ARG B	4.63	164.42	-1.87	-0.66	19.01	95
    130	200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B	4	165.69	-2.28	-0.76	26.69	92
    131	200026 SER B, 100024 ARG B, 100070 ASP B	3.59	166.33	-2.8	-0.75	35.03	84
    132	100024 ARG B, 100070 ASP B, 200026 SER B	3.31	168.28	-2.93	-0.81	34.46	95
    133	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.48	170.28	-1.25	-0.32	25.88	85
    134	100070 ASP B, 200026 SER B, 200003 LEU B	2.2	173.06	-0.17	-0.29	17.17	85
    135	100070 ASP B, 200003 LEU B	2.34	175.86	0.15	0.05	24.92	70
    136	100070 ASP B, 200003 LEU B, 200001 ASP B	2.98	177.66	-0.03	-0.23	17.74	70
    137	100070 ASP B, 200003 LEU B, 200001 ASP B, 100072 THR B	3.98	177.79	-0.2	-0.37	13.72	82
    138	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	4.02	178.81	-0.98	-0.43	25.3	83
    139	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.79	180.12	-1.08	-0.27	25.25	79
    140	200003 LEU B, 200001 ASP B, 200063 LYS A	3.57	182.11	-1.2	-0.1	33.11	70
    141	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.5	183.63	-1.08	-0.27	25.25	79
    142	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A	3.55	184.09	-1.08	-0.2	13.67	84
    143	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B	3.62	184.47	-0.3	-0.21	13.67	77
    144	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B	3.73	184.99	-0.94	-0.32	11.61	84
    145	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.07	185.19	-2.4	-0.78	21.56	90
    146	200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.31	185.46	-2.03	-0.87	14.58	96
    147	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.82	186.06	-2.4	-0.78	21.56	90
    148	200003 LEU B, 200063 LYS A, 200061 ASN A, 200098 PHE B, 200046 GLU A	5.05	187.09	-1.5	-0.4	21.26	76
    149	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	5.23	188.35	-1	-0.3	25.73	67
    150	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	5.22	191.23	0.23	0.35	24.92	76
    151	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	4.65	192.25	-1.1	-0.35	25.3	80
    152	200063 LYS A, 200046 GLU A, 200064 ILE A	2.85	197.53	-0.97	0.09	33.18	84
    153	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	2.93	200.4	-0.98	-0.14	26.35	87
    154	200046 GLU A, 200064 ILE A, 100018 ARG B	3.56	201.04	-1.17	0.08	34.01	87
    155	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.66	204.3	-2	-0.04	38.51	86
    156	200046 GLU A, 100018 ARG B, 200040 ARG A	3.97	206.83	-4.17	-0.66	51.3	81
    157	200046 GLU A, 200064 ILE A, 200040 ARG A	4.15	207.47	-1.17	0.08	34.01	87
    158	200046 GLU A, 200040 ARG A	3.52	210.03	-4	-0.78	50.95	80
    159	200040 ARG A	2.13	216.87	-4.5	-0.42	52	83
    160	200040 ARG A, 200088 SER A	1.97	217.69	-2.45	-0.61	27.69	83
    161	200040 ARG A, 200088 SER A, 200091 SER A	1.95	218.1	-1.77	-0.67	19.59	83
    162	200040 ARG A, 200088 SER A, 200091 SER A	2.05	218.36	-1.9	-0.73	19.02	100
    163	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.25	219.1	-1.73	-0.53	15.09	70
    164	200040 ARG A, 200088 SER A, 200041 PRO A	2.85	221.8	-2.17	-0.44	18.99	70
    165	200040 ARG A, 200041 PRO A, 200088 SER A	4.21	223.8	-2.3	-0.49	18.42	86
    166	200041 PRO A, 200088 SER A	4.94	225.32	-1.2	-0.53	1.63	87
    167	200091 SER A, 200041 PRO A, 200088 SER A	4.82	225.83	-1.07	-0.68	1.64	97
    168	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.67	226.25	0.15	-0.22	1.26	86
    169	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.52	226.56	0.02	0.3	1.25	69
    170	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.38	226.79	0.23	0.08	1.27	84
    171	200091 SER A, 200088 SER A, 200180 TYR A	4.17	227.05	-0.97	-0.28	1.65	94
    172	200091 SER A, 200088 SER A	4.12	227.24	-0.8	-0.97	1.67	117
    173	200091 SER A, 200088 SER A, 200180 TYR A	4.1	227.74	-0.97	-0.28	1.65	94
    174	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.11	228.57	-0.06	0.08	1.67	69
    175	200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.13	229.6	0.02	0.3	1.25	69
    176	200041 PRO A, 200175 LEU A, 200180 TYR A	4.17	233.05	0.3	0.72	1.11	54
    177	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.29	233.24	0.13	0.34	1.68	54
    178	200041 PRO A, 200175 LEU A, 200180 TYR A	4.32	233.93	0.3	0.72	1.11	54
    179	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.37	234.6	0.13	0.34	1.68	54
    180	200041 PRO A, 200180 TYR A, 200173 ALA A	3.67	237.06	-1.1	0.07	2.19	54
    181	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.3	239.02	-1.7	-0.23	14.12	61
    182	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.31	240.98	-1.78	-0.53	14.11	64
    183	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.3	241.6	-2.55	-0.52	14.11	74
    184	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.04	242.28	-2.55	-0.52	14.11	74
    185	200153 GLU A, 200172 PRO A, 200041 ASN B	2.89	242.72	-2.87	-0.67	18.29	79
    186	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.39	245.91	-2.25	-0.7	14.56	79
    187	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.39	246.96	-1.95	-0.88	15.01	90
    188	200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.46	247.35	-0.8	-0.47	12.03	78
    189	200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.57	248.34	-0.13	-0.31	2.57	79
    190	200041 ASN B, 200171 PHE A, 200182 LEU A	2.7	248.54	-0.03	-0.14	2.3	79
    191	200041 ASN B, 200182 LEU A, 200170 THR A	2.67	248.71	-0.13	-0.13	1.72	88
    192	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.61	250.56	-0.2	-0.3	2.14	88
    193	200041 ASN B, 200170 THR A, 200155 VAL A	2.88	253.83	-1.53	-0.78	2.81	105
    194	200041 ASN B, 200170 THR A, 200155 VAL A, 200156 THR A, 200157 VAL A	3.13	254.12	-1.14	-0.78	2.69	106
    195	200041 ASN B, 200156 THR A, 200157 VAL A	3.16	254.45	-1.53	-0.78	2.81	105
    196	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.18	254.62	-1.33	-0.78	2.52	106
    197	200041 ASN B, 200170 THR A, 200157 VAL A	3.18	254.71	-1.53	-0.78	2.81	105
    198	200041 ASN B, 200170 THR A, 200155 VAL A	3.18	254.89	-1.53	-0.78	2.81	105
    199	200041 ASN B, 200170 THR A, 200157 VAL A	3.23	255.04	-1.53	-0.78	2.81	105
    200	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.25	255.48	-1.33	-0.78	2.52	106
    201	200041 ASN B, 200170 THR A, 200157 VAL A	3.29	258.52	-1.53	-0.78	2.81	105
    202	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B	3.99	259.39	-1.25	-0.79	2.95	105
    203	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.32	259.55	-1.08	-0.79	3.04	105
    204	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.41	259.75	0.68	-0.31	2.14	102
    205	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.6	259.89	-1.16	-0.72	12.26	89
    206	200170 THR A, 200157 VAL A, 200168 VAL A, 200169 LYS B	4.04	260.82	-0.2	-0.21	13.67	92
    207	200157 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A	3.88	261.32	-0.13	-0.22	14.1	85
    208	200168 VAL A, 200169 LYS B, 200165 SER A	2.83	265.36	-0.03	-0.03	17.67	85
    209	200168 VAL A, 200169 LYS B, 200165 SER A	1.71	267.32	-1.57	-0.67	18.75	72
    210	200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A	1.48	268.59	-1.28	-0.7	14.91	72
    211	200168 VAL A, 200169 LYS B, 200167 GLY A	1.73	269.49	-1.57	-0.67	18.75	72
    212	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.94	269.77	-1.98	-0.44	26.97	81
    213	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.99	270.03	-1.98	-0.44	26.97	81
    214	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.94	270.05	-1.98	-0.44	26.97	81
    215	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.76	270.49	-1.98	-0.44	26.97	81
    216	200169 LYS B, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.71	270.98	-2.75	-0.5	38.55	83
    217	200169 LYS B, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.7	271.52	-2.75	-0.5	38.55	83
    218	200169 LYS B, 200167 GLY A, 200167 ASP B	1.71	272.22	-2.6	-0.75	34.19	79
    219	200169 LYS B, 200167 GLY A	1.73	273.7	-2.15	-0.61	26.44	72
    220	200169 LYS B, 200167 GLY A, 200166 SER A	1.79	274.63	-1.57	-0.67	18.75	72
    221	200169 LYS B, 200167 GLY A, 200166 SER A	1.89	278.26	-1.7	-0.73	18.18	94
    222	200169 LYS B, 200167 GLY A, 200166 SER A, 200170 ASP B	2.95	279.53	-2.15	-0.81	26.06	91
    223	200167 GLY A, 200166 SER A, 200170 ASP B, 200169 LYS B	4.37	279.99	-1.28	-0.9	14.53	101
    224	200167 GLY A, 200166 SER A, 200170 ASP B	4.55	281.2	-1.57	-0.94	18.25	101
    225	200167 GLY A, 200166 SER A, 200170 ASP B, 200140 MET A	4.96	281.95	-0.7	-0.45	14.05	98
    226	200167 GLY A, 200170 ASP B, 200140 MET A	4.48	283.51	-0.67	-0.28	18.17	89
    227	200167 GLY A, 200170 ASP B, 200140 MET A, 200138 ASN B	4.06	284.79	-1.38	-0.4	14.47	94
    228	200170 ASP B, 200140 MET A, 200138 ASN B	3.91	286.45	-1.7	-0.27	18.17	94
    229	200140 MET A, 200138 ASN B, 200187 THR A	3.64	288.17	-0.77	-0.18	2.16	101
    230	200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B	3.06	290.02	-0.75	-0.33	2.03	102
    231	200140 MET A, 200187 THR A, 200114 THR B	2.8	291.81	0.17	-0.18	1.58	102
    232	200140 MET A, 200114 THR B	2.7	293.2	0.6	0.12	1.55	100
    233	200140 MET A, 200114 THR B, 200138 ASN A, 200139 SER A	2.67	294.47	-0.78	-0.38	2.04	105
    234	200140 MET A, 200114 THR B, 200138 ASN A	2.72	295.34	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

24. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C, 100079 GLY C, 28 SER B, 200028 SER B, 27 GLN B, 69 THR B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300002 ILE B, 300098 PHE B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A, 300169 HIS A, 300167 ASP B, 300166 SER A, 300166 SER A, 300170 ASP B, 300169 LYS B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 82 TYR C, 200093 ARG B, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A, 300168 VAL A, 300169 LYS B, 300169 HIS A, 300167 ASP B, 300166 SER A, 300170 ASP B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A

    Physicochemical properties of lining side-chains

    Charge: 3 (13-10)
    Hydropathy: -1.4
    Hydrophobicity: -0.43
    Polarity: 14.56
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.26	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.3	0.46	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.23	0.69	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.17	0.87	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.09	1.02	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	2.83	1.63	-1.53	-0.78	2.81	105
    7	100170 THR A, 100041 ASN B, 100155 VAL A	2.62	5.64	-1.53	-0.78	2.81	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.63	6.58	-0.2	-0.3	2.14	88
    9	100170 THR A, 100041 ASN B, 100182 LEU A	2.75	6.97	-0.13	-0.13	1.72	88
    10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.74	7.17	-0.03	-0.14	2.3	79
    11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.63	7.9	-0.13	-0.31	2.57	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.6	8.36	-0.8	-0.47	12.03	78
    13	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.59	8.84	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.58	10.14	-1.95	-0.88	15.01	90
    15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.6	13.01	-2.25	-0.7	14.56	79
    16	100041 ASN B, 100153 GLU A, 100172 PRO A	2.93	13.37	-2.87	-0.67	18.29	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.05	13.96	-2.55	-0.52	14.11	74
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.26	14.66	-2.55	-0.52	14.11	74
    19	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.37	16.71	-1.78	-0.53	14.11	64
    20	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.34	18.78	-1.7	-0.23	14.12	61
    21	100173 ALA A, 100041 PRO A, 100180 TYR A	3.5	21.01	-1.1	0.07	2.19	54
    22	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.13	21.42	0.13	0.34	1.68	54
    23	100041 PRO A, 100180 TYR A, 100175 LEU A	4.4	22.11	0.3	0.72	1.11	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.19	22.7	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.03	27.34	0.3	0.72	1.11	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.06	27.92	-0.06	0.08	1.67	69
    27	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.1	28.17	0.23	0.08	1.27	84
    28	100091 SER A, 100088 SER A	4.16	28.25	-0.8	-0.97	1.67	117
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.24	28.62	-0.97	-0.28	1.65	94
    30	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.46	28.89	0.23	0.08	1.27	84
    31	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.6	29.28	0.02	0.3	1.25	69
    32	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.74	29.76	0.15	-0.22	1.26	86
    33	100041 PRO A, 100091 SER A, 100088 SER A	4.89	30.83	-1.07	-0.68	1.64	97
    34	100041 PRO A, 100088 SER A	5.14	31.7	-1.2	-0.53	1.63	87
    35	100041 PRO A, 100088 SER A, 100040 ARG A	4.55	33.9	-2.3	-0.49	18.42	86
    36	100041 PRO A, 100088 SER A, 100040 ARG A	2.8	36.42	-2.17	-0.44	18.99	70
    37	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.23	36.8	-1.73	-0.53	15.09	70
    38	100088 SER A, 100040 ARG A, 100091 SER A	0.7	37.93	-1.77	-0.67	19.59	83
    39	100088 SER A, 100040 ARG A	0.39	38.9	-2.45	-0.61	27.69	83
    40	100040 ARG A	0.26	45.24	-4.5	-0.42	52	83
    41	100040 ARG A, 100043 HIS A	1.73	46.5	-3.85	-0.08	51.8	87
    42	100040 ARG A, 100046 GLU A	2.4	50.2	-4	-0.78	50.95	80
    43	100040 ARG A, 100046 GLU A, 300018 ARG B	4.44	52.58	-4.17	-0.66	51.3	81
    44	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.43	56.46	-2	-0.04	38.51	86
    45	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.57	59.38	-0.98	-0.14	26.35	87
    46	100046 GLU A, 100064 ILE A, 100063 LYS A	3.5	60.26	0.2	-0.04	17.8	90
    47	100046 GLU A, 100064 ILE A, 100063 LYS A	3.37	65.18	-0.97	0.09	33.18	84
    48	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	3.94	66.17	-1.1	-0.35	25.3	80
    49	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.29	69.74	0.23	0.35	24.92	76
    50	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.58	70.71	-1	-0.3	25.73	67
    51	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.59	71.24	-1.5	-0.4	21.26	76
    52	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.56	71.41	-2.4	-0.78	21.56	90
    53	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.42	71.69	-2.03	-0.87	14.58	96
    54	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.33	71.94	-2.4	-0.78	21.56	90
    55	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4.1	72.61	-0.94	-0.32	11.61	84
    56	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.98	73.06	-0.3	-0.21	13.67	77
    57	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.87	73.55	-0.3	-0.21	13.67	77
    58	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.62	75.2	-1.08	-0.27	25.25	79
    59	100063 LYS A, 100003 LEU B, 100001 ASP B	3.58	77.13	-1.2	-0.1	33.11	70
    60	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.67	78.08	-1.08	-0.27	25.25	79
    61	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.92	78.99	-0.98	-0.43	25.3	83
    62	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.9	79.16	-0.2	-0.37	13.72	82
    63	100003 LEU B, 300070 ASP B, 100001 ASP B	3.01	81.16	-0.03	-0.23	17.74	70
    64	100003 LEU B, 300070 ASP B	2.25	84.03	0.15	0.05	24.92	70
    65	100003 LEU B, 300070 ASP B, 100026 SER B	2.19	86.76	-0.17	-0.29	17.17	85
    66	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.51	88.7	-1.25	-0.32	25.88	85
    67	300070 ASP B, 100026 SER B, 300024 ARG B	3.25	90.36	-2.93	-0.81	34.46	95
    68	300070 ASP B, 300024 ARG B, 100026 SER B	3.56	91.47	-2.8	-0.75	35.03	84
    69	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.86	93.21	-2.28	-0.76	26.69	92
    70	300024 ARG B, 100026 SER B, 300069 THR B	4.58	94.35	-1.87	-0.66	19.01	95
    71	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	5	95.36	-1.5	-0.7	15.11	95
    72	100026 SER B, 300069 THR B, 300026 SER B	4.47	98.74	-0.5	-0.79	2.81	107
    73	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.38	99.73	-0.48	-0.79	2.95	107
    74	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.35	101.25	-0.46	-0.79	3.04	107
    75	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.47	101.41	-1.28	-0.92	2.99	100
    76	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.55	104.65	-1.35	-0.91	2.56	102
    77	300027 GLN B, 100027 GLN B, 300028 SER B	5.24	105.39	-1.57	-0.96	2.86	100
    78	100027 GLN B, 300028 SER B, 300027 GLN B	5.44	106.05	-2.6	-1.06	2.91	95
    79	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	5.66	106.55	-2.05	-0.99	3.03	95
    80	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.89	107.69	-2.05	-0.99	3.03	95
    81	100027 GLN B, 300028 SER B, 100028 SER B	5.87	111.1	-1.7	-1.01	2.29	106
    82	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	5.21	111.5	-2.4	-0.87	14.72	100
    83	100027 GLN B, 100028 SER B, 100093 ARG B	4.07	111.96	-2.93	-0.83	19.07	94
    84	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.71	112.43	-2.4	-0.87	14.72	100
    85	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.38	113.14	-2.3	-0.82	15.15	94
    86	100027 GLN B, 300028 SER B, 100093 ARG B	2.72	118.18	-2.93	-0.83	19.07	94
    87	300028 SER B, 100093 ARG B	3.31	118.96	-2.65	-0.7	26.84	100
    88	300028 SER B, 100093 ARG B, 100082 TYR C	3.52	120.09	-2.2	-0.09	18.43	83
    89	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.84	120.5	-2.78	-0.18	26.82	83
    90	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.83	121.59	-2.53	-0.35	14.7	83
    91	300028 SER B, 300093 ARG B, 300058 GLN C	3.62	121.94	-2.93	-0.83	19.07	94
    92	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.64	122.44	-2.53	-0.35	14.7	83
    93	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.73	122.74	-2.43	-0.3	15.13	72
    94	100082 TYR C, 300093 ARG B, 300058 GLN C	3.78	123.5	-3.1	-0.14	19.05	72
    95	100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C	3.74	123.7	-2.43	-0.3	15.13	72
    96	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	2.99	124.89	-2.43	-0.3	15.13	72
    97	300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C	2.96	125.63	-2.2	-0.78	15.57	83
    98	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.25	129.38	-2.43	-0.3	15.13	72
    99	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	5.78	131.16	-1.58	0.04	12.4	61
    100	300079 GLY C, 79 GLY C, 93 ARG B, 82 TYR C, 200079 GLY C	6.7	131.57	-1.4	-0.34	12.75	66
    101	93 ARG B, 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C	6.97	131.7	-2.4	0.12	22.12	66
    102	100093 ARG B, 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C	7.11	132.03	-2.4	0.12	22.12	66
    103	82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C, 100079 GLY C	7.03	132.33	-1.58	0.04	12.4	61
    104	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.35	133.57	-2.22	-0.27	22.47	72
    105	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.04	134.05	-2.3	-0.3	22.13	83
    106	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	4.24	136.96	-2.78	-0.18	26.82	83
    107	300093 ARG B, 300082 TYR C, 28 SER B	3.63	139.18	-2.2	-0.09	18.43	83
    108	300027 GLN B, 300093 ARG B, 28 SER B	3.33	144.29	-2.93	-0.83	19.07	94
    109	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	3.63	144.78	-2.3	-0.82	15.15	94
    110	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	3.79	145.01	-2.4	-0.87	14.72	100
    111	300028 SER B, 300027 GLN B, 300093 ARG B	3.98	145.38	-2.93	-0.83	19.07	94
    112	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.71	146.1	-2.4	-0.87	14.72	100
    113	300028 SER B, 300027 GLN B, 28 SER B	5.28	149.45	-1.7	-1.01	2.29	106
    114	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	5.78	150.63	-2.05	-0.99	3.03	95
    115	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.22	152.01	-2.05	-0.99	3.03	95
    116	300027 GLN B, 28 SER B, 27 GLN B	4.97	152.74	-1.57	-0.96	2.86	100
    117	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.59	155.48	-1.35	-0.91	2.56	102
    118	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	4.87	155.7	-1.28	-0.92	2.99	100
    119	300026 SER B, 28 SER B, 27 GLN B, 69 THR B, 26 SER B	4.4	158.93	-0.46	-0.79	3.04	107
    120	300026 SER B, 69 THR B, 26 SER B	4.32	161.67	-0.5	-0.79	2.81	107
    121	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.59	162.84	-1.5	-0.7	15.11	95
    122	300026 SER B, 69 THR B, 24 ARG B	4.73	164.11	-1.87	-0.66	19.01	95
    123	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	4.14	165.6	-2.28	-0.76	26.69	92
    124	300026 SER B, 24 ARG B, 70 ASP B	3.59	166.44	-2.8	-0.75	35.03	84
    125	24 ARG B, 70 ASP B, 300026 SER B	3.27	168.47	-2.93	-0.81	34.46	95
    126	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.44	170.48	-1.25	-0.32	25.88	85
    127	70 ASP B, 300026 SER B, 300003 LEU B	2.19	173.23	-0.17	-0.29	17.17	85
    128	70 ASP B, 300003 LEU B	2.35	176	0.15	0.05	24.92	70
    129	70 ASP B, 300003 LEU B, 300001 ASP B	2.99	177.75	-0.03	-0.23	17.74	70
    130	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.98	177.88	-0.2	-0.37	13.72	82
    131	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	4.01	178.88	-0.98	-0.43	25.3	83
    132	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.96	179.15	-1.56	-0.42	30.14	81
    133	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.8	180.12	-1.08	-0.27	25.25	79
    134	300003 LEU B, 300001 ASP B, 300063 LYS A	3.58	182.1	-1.2	-0.1	33.11	70
    135	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.51	183.63	-1.08	-0.27	25.25	79
    136	300003 LEU B, 300063 LYS A, 300097 THR B, 300002 ILE B	3.54	184.09	-0.3	-0.21	13.67	77
    137	300003 LEU B, 300063 LYS A, 300097 THR B, 300098 PHE B	3.6	184.49	-0.3	-0.21	13.67	77
    138	300003 LEU B, 300063 LYS A, 300097 THR B, 300098 PHE B, 300061 ASN A	3.7	185.03	-0.94	-0.32	11.61	84
    139	300063 LYS A, 300097 THR B, 300098 PHE B, 300061 ASN A, 300046 GLU A	4.02	185.25	-2.4	-0.78	21.56	90
    140	300097 THR B, 300098 PHE B, 300061 ASN A, 300046 GLU A	4.24	185.95	-2.03	-0.87	14.58	96
    141	300003 LEU B, 300063 LYS A, 300098 PHE B, 300061 ASN A, 300046 GLU A	4.99	186.87	-1.5	-0.4	21.26	76
    142	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	5.19	188.07	-1	-0.3	25.73	67
    143	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	5.28	191.2	0.23	0.35	24.92	76
    144	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	4.77	192.08	-1.1	-0.35	25.3	80
    145	300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B	4.41	192.9	-0.93	-0.18	25.3	92
    146	300063 LYS A, 300046 GLU A, 300064 ILE A	2.84	197.26	-0.97	0.09	33.18	84
    147	300046 GLU A, 300064 ILE A, 300063 LYS A	2.89	198.13	0.2	-0.04	17.8	90
    148	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.01	200.86	-0.98	-0.14	26.35	87
    149	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.62	204.05	-2	-0.04	38.51	86
    150	300046 GLU A, 18 ARG B, 300040 ARG A	3.9	206.66	-4.17	-0.66	51.3	81
    151	300046 GLU A, 300064 ILE A, 300040 ARG A	4.05	207.91	-1.17	0.08	34.01	87
    152	300046 GLU A, 300040 ARG A	3.37	210.77	-4	-0.78	50.95	80
    153	300040 ARG A	2.06	217.29	-4.5	-0.42	52	83
    154	300040 ARG A, 300088 SER A	1.95	217.95	-2.45	-0.61	27.69	83
    155	300040 ARG A, 300088 SER A, 300091 SER A	1.97	218.27	-1.77	-0.67	19.59	83
    156	300040 ARG A, 300088 SER A, 300041 PRO A, 300091 SER A	2.1	218.54	-1.83	-0.57	14.66	86
    157	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.33	219.33	-1.73	-0.53	15.09	70
    158	300040 ARG A, 300088 SER A, 300041 PRO A	2.95	222.05	-2.17	-0.44	18.99	70
    159	300040 ARG A, 300041 PRO A, 300088 SER A	4.28	223.97	-2.3	-0.49	18.42	86
    160	300041 PRO A, 300088 SER A	5.02	224.97	-1.2	-0.53	1.63	87
    161	300041 PRO A, 300091 SER A, 300088 SER A	4.8	225.99	-1.07	-0.68	1.64	97
    162	300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A	4.65	226.39	0.15	-0.22	1.26	86
    163	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.5	226.68	0.02	0.3	1.25	69
    164	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.36	226.91	0.23	0.08	1.27	84
    165	300091 SER A, 300088 SER A, 300180 TYR A	4.16	227.15	-0.97	-0.28	1.65	94
    166	300091 SER A, 300088 SER A	4.12	227.36	-0.8	-0.97	1.67	117
    167	300091 SER A, 300088 SER A, 300180 TYR A	4.1	227.89	-0.97	-0.28	1.65	94
    168	300088 SER A, 300041 PRO A, 300091 SER A, 300175 LEU A, 300180 TYR A	4.11	228.73	-0.06	0.08	1.67	69
    169	300041 PRO A, 300175 LEU A, 300180 TYR A	4.14	233.15	0.3	0.72	1.11	54
    170	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.29	233.34	0.13	0.34	1.68	54
    171	300041 PRO A, 300175 LEU A, 300180 TYR A	4.32	234.02	0.3	0.72	1.11	54
    172	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.38	234.64	0.13	0.34	1.68	54
    173	300041 PRO A, 300180 TYR A, 300173 ALA A	3.69	237.06	-1.1	0.07	2.19	54
    174	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.3	239.02	-1.7	-0.23	14.12	61
    175	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.31	240.98	-1.78	-0.53	14.11	64
    176	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.32	241.62	-2.55	-0.52	14.11	74
    177	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.08	242.26	-2.55	-0.52	14.11	74
    178	300153 GLU A, 300172 PRO A, 300041 ASN B	2.78	243.17	-2.87	-0.67	18.29	79
    179	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.39	246.4	-2.25	-0.7	14.56	79
    180	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.41	246.91	-1.95	-0.88	15.01	90
    181	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.44	247.24	-0.8	-0.47	12.03	78
    182	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.49	247.48	-0.8	-0.47	12.03	78
    183	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.61	248.33	-0.13	-0.31	2.57	79
    184	300041 ASN B, 300182 LEU A, 300171 PHE A	2.71	248.54	-0.03	-0.14	2.3	79
    185	300041 ASN B, 300182 LEU A, 300170 THR A	2.65	248.86	-0.13	-0.13	1.72	88
    186	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.61	250.21	-0.2	-0.3	2.14	88
    187	300041 ASN B, 300170 THR A, 300155 VAL A	2.84	254.07	-1.53	-0.78	2.81	105
    188	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.14	254.26	-1.33	-0.78	2.52	106
    189	300041 ASN B, 300156 THR A, 300157 VAL A	3.17	254.41	-1.53	-0.78	2.81	105
    190	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.18	254.73	-1.33	-0.78	2.52	106
    191	300041 ASN B, 300170 THR A, 300155 VAL A	3.18	254.98	-1.53	-0.78	2.81	105
    192	300041 ASN B, 300170 THR A, 300157 VAL A	3.24	255.13	-1.53	-0.78	2.81	105
    193	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.25	255.59	-1.33	-0.78	2.52	106
    194	300041 ASN B, 300170 THR A, 300157 VAL A	3.3	258.65	-1.53	-0.78	2.81	105
    195	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B	4	259.48	-1.25	-0.79	2.95	105
    196	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.33	259.63	-1.08	-0.79	3.04	105
    197	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.42	259.83	0.68	-0.31	2.14	102
    198	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.6	259.97	-1.16	-0.72	12.26	89
    199	300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B	4.05	260.87	-0.2	-0.21	13.67	92
    200	300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A	3.89	261.35	-0.13	-0.22	14.1	85
    201	300168 VAL A, 300169 LYS B, 300165 SER A	2.86	265.32	-0.03	-0.03	17.67	85
    202	300168 VAL A, 300169 LYS B, 300165 SER A	1.74	267.38	-1.57	-0.67	18.75	72
    203	300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A	1.47	268.57	-1.28	-0.7	14.91	72
    204	300168 VAL A, 300169 LYS B, 300167 GLY A	1.71	269.79	-1.57	-0.67	18.75	72
    205	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	2	270.09	-1.98	-0.44	26.97	81
    206	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.89	270.2	-1.98	-0.44	26.97	81
    207	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.78	270.51	-1.98	-0.44	26.97	81
    208	300168 VAL A, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.73	270.67	-1.88	-0.6	27.02	88
    209	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.7	271.39	-2.75	-0.5	38.55	83
    210	300169 LYS B, 300167 GLY A, 300167 ASP B	1.7	272.79	-2.6	-0.75	34.19	79
    211	300169 LYS B, 300167 GLY A	1.74	273.53	-2.15	-0.61	26.44	72
    212	300169 LYS B, 300167 GLY A, 300166 SER A	1.78	274.82	-1.57	-0.67	18.75	72
    213	300169 LYS B, 300167 GLY A, 300166 SER A	1.92	274.97	-1.7	-0.73	18.18	94
    214	300169 LYS B, 300166 SER A	2.06	275.21	-2.35	-0.69	25.59	94
    215	300169 LYS B, 300167 GLY A, 300166 SER A	2.15	278.11	-1.7	-0.73	18.18	94
    216	300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B	2.86	279.81	-2.15	-0.81	26.06	91
    217	300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B	4.46	280.29	-1.28	-0.9	14.53	101
    218	300167 GLY A, 300166 SER A, 300170 ASP B	4.63	281.13	-1.57	-0.94	18.25	101
    219	300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A	4.9	282.1	-0.7	-0.45	14.05	98
    220	300167 GLY A, 300170 ASP B, 300140 MET A	4.44	283.71	-0.67	-0.28	18.17	89
    221	300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B	4.04	284.96	-1.38	-0.4	14.47	94
    222	300170 ASP B, 300140 MET A, 300138 ASN B	3.91	286.58	-1.7	-0.27	18.17	94
    223	300140 MET A, 300138 ASN B, 300187 THR A	3.63	288.3	-0.77	-0.18	2.16	101
    224	300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B	3.05	290.13	-0.75	-0.33	2.03	102
    225	300140 MET A, 300187 THR A, 300114 THR B	2.8	291.94	0.17	-0.18	1.58	102
    226	300140 MET A, 300114 THR B	2.74	292.67	0.6	0.12	1.55	100
    227	300140 MET A, 300114 THR B, 300138 ASN A	2.7	293.31	-0.77	-0.18	2.16	101
    228	300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A	2.67	294.56	-0.78	-0.38	2.04	105
    229	300140 MET A, 300114 THR B, 300138 ASN A	2.72	295.42	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

25. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B, 200028 SER B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 1 ASP B, 200072 THR B, 1 ASP B, 63 LYS A, 97 THR B, 2 ILE B, 98 PHE B, 61 ASN A, 46 GLU A, 64 ILE A, 200020 SER B, 63 LYS A, 200018 ARG B, 40 ARG A, 88 SER A, 91 SER A, 41 PRO A, 91 SER A, 88 SER A, 175 LEU A, 180 TYR A, 173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A, 40 THR B, 168 VAL A, 168 VAL A, 169 LYS B, 165 SER A, 167 GLY A, 169 HIS A, 167 ASP B, 166 SER A, 166 SER A, 170 ASP B, 169 LYS B, 140 MET A, 138 ASN B, 187 THR A, 114 THR B, 138 ASN A, 139 SER A

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100003 LEU B, 300020 SER B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 300082 TYR C, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200069 THR B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A, 97 THR B, 61 ASN A, 46 GLU A, 64 ILE A, 200020 SER B, 200018 ARG B, 40 ARG A, 41 PRO A, 91 SER A, 88 SER A, 175 LEU A, 180 TYR A, 153 GLU A, 172 PRO A, 41 ASN B, 182 LEU A, 170 THR A, 156 THR A, 168 VAL A, 169 LYS B, 169 HIS A, 167 ASP B, 166 SER A, 170 ASP B, 140 MET A, 138 ASN B, 187 THR A, 114 THR B, 138 ASN A, 139 SER A

    Physicochemical properties of lining side-chains

    Charge: 2 (13-11)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 15.28
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.16	0.18	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.1	1.94	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.22	3.89	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.68	4.14	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.75	4.81	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.74	4.99	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.7	5.25	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.56	6.35	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A	3.52	6.69	-2.23	-0.32	2.18	73
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.47	7.25	-2.55	-0.52	14.11	74
    11	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.41	7.91	-2.55	-0.52	14.11	74
    12	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.25	10.27	-1.78	-0.53	14.11	64
    13	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.25	12.34	-1.7	-0.23	14.12	61
    14	100041 PRO A, 100173 ALA A, 100180 TYR A	3.51	14.04	-1.1	0.07	2.19	54
    15	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	3.97	14.69	0.13	0.34	1.68	54
    16	100041 PRO A, 100180 TYR A, 100175 LEU A	4.42	15.34	0.3	0.72	1.11	54
    17	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.22	15.8	0.13	0.34	1.68	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A	4.03	20.17	0.3	0.72	1.11	54
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.04	20.89	-0.06	0.08	1.67	69
    20	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.07	21.31	0.02	0.3	1.25	69
    21	100180 TYR A, 100091 SER A, 100088 SER A	4.12	21.46	-0.97	-0.28	1.65	94
    22	100091 SER A, 100088 SER A	4.18	21.55	-0.8	-0.97	1.67	117
    23	100180 TYR A, 100091 SER A, 100088 SER A	4.27	21.94	-0.97	-0.28	1.65	94
    24	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.49	22.22	0.23	0.08	1.27	84
    25	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.63	22.6	0.02	0.3	1.25	69
    26	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.77	23.07	0.15	-0.22	1.26	86
    27	100041 PRO A, 100091 SER A, 100088 SER A	4.91	24.1	-1.07	-0.68	1.64	97
    28	100041 PRO A, 100088 SER A	5.15	24.94	-1.2	-0.53	1.63	87
    29	100041 PRO A, 100088 SER A, 100040 ARG A	4.24	27.64	-2.3	-0.49	18.42	86
    30	100041 PRO A, 100088 SER A, 100040 ARG A	2.53	29.87	-2.17	-0.44	18.99	70
    31	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.04	30.21	-1.73	-0.53	15.09	70
    32	100088 SER A, 100040 ARG A, 100091 SER A	0.89	31.43	-1.77	-0.67	19.59	83
    33	100088 SER A, 100040 ARG A	0.71	32.49	-2.45	-0.61	27.69	83
    34	100040 ARG A	0.69	38.63	-4.5	-0.42	52	83
    35	100040 ARG A, 100043 HIS A	2.15	39.82	-3.85	-0.08	51.8	87
    36	100040 ARG A, 100046 GLU A	2.7	43.38	-4	-0.78	50.95	80
    37	100040 ARG A, 100046 GLU A, 300018 ARG B	4.1	46.26	-4.17	-0.66	51.3	81
    38	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.55	49.27	-2	-0.04	38.51	86
    39	100046 GLU A, 300018 ARG B, 100064 ILE A	3.64	49.89	-1.17	0.08	34.01	87
    40	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.29	52.72	-0.98	-0.14	26.35	87
    41	100046 GLU A, 100064 ILE A, 100063 LYS A	3.18	53.56	0.2	-0.04	17.8	90
    42	100046 GLU A, 100064 ILE A, 100063 LYS A	3.08	58.33	-0.97	0.09	33.18	84
    43	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	4.24	59.17	-1.1	-0.35	25.3	80
    44	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.74	62.47	0.23	0.35	24.92	76
    45	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	5	63.55	-1	-0.3	25.73	67
    46	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.94	64.29	-1.5	-0.4	21.26	76
    47	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.83	64.63	-2.4	-0.78	21.56	90
    48	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.32	65.04	-2.03	-0.87	14.58	96
    49	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.15	65.27	-2.4	-0.78	21.56	90
    50	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.85	65.95	-0.94	-0.32	11.61	84
    51	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.73	66.39	-0.3	-0.21	13.67	77
    52	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.64	66.86	-0.3	-0.21	13.67	77
    53	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.52	68.44	-1.08	-0.27	25.25	79
    54	100063 LYS A, 100003 LEU B, 100001 ASP B	3.54	70.31	-1.2	-0.1	33.11	70
    55	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.73	71.29	-1.08	-0.27	25.25	79
    56	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.99	71.5	-1.56	-0.42	30.14	81
    57	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4	72.31	-0.98	-0.43	25.3	83
    58	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.97	72.48	-0.2	-0.37	13.72	82
    59	100003 LEU B, 300070 ASP B, 100001 ASP B	2.91	74.79	-0.03	-0.23	17.74	70
    60	100003 LEU B, 300070 ASP B	2.3	77.58	0.15	0.05	24.92	70
    61	100003 LEU B, 300070 ASP B, 100026 SER B	2.18	80.18	-0.17	-0.29	17.17	85
    62	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.46	82.02	-1.25	-0.32	25.88	85
    63	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	83.64	-2.93	-0.81	34.46	95
    64	300070 ASP B, 300024 ARG B, 100026 SER B	3.62	84.58	-2.8	-0.75	35.03	84
    65	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	4.06	86.11	-2.28	-0.76	26.69	92
    66	300024 ARG B, 100026 SER B, 300069 THR B	4.58	87.76	-1.87	-0.66	19.01	95
    67	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.51	88.68	-1.5	-0.7	15.11	95
    68	100026 SER B, 300069 THR B, 300026 SER B	4.4	91.93	-0.5	-0.79	2.81	107
    69	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.56	92.89	-0.48	-0.79	2.95	107
    70	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.68	94.49	-0.46	-0.79	3.04	107
    71	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.01	94.83	-1.28	-0.92	2.99	100
    72	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.42	97.41	-1.35	-0.91	2.56	102
    73	100026 SER B, 100027 GLN B, 300028 SER B	4.78	98.11	-1.57	-0.96	2.86	100
    74	300027 GLN B, 100027 GLN B, 300028 SER B	5.04	98.82	-1.57	-0.96	2.86	100
    75	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.33	99.88	-2.05	-0.99	3.03	95
    76	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.89	100.93	-2.05	-0.99	3.03	95
    77	100027 GLN B, 300028 SER B, 100028 SER B	4.89	104.58	-1.7	-1.01	2.29	106
    78	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.59	104.85	-2.4	-0.87	14.72	100
    79	100027 GLN B, 100028 SER B, 100093 ARG B	4.33	105.39	-2.93	-0.83	19.07	94
    80	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.24	105.93	-2.4	-0.87	14.72	100
    81	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.14	106.64	-2.3	-0.82	15.15	94
    82	100027 GLN B, 300028 SER B, 100093 ARG B	3.26	111.64	-2.93	-0.83	19.07	94
    83	300028 SER B, 100093 ARG B	3.28	112.38	-2.65	-0.7	26.84	100
    84	300028 SER B, 100093 ARG B, 100082 TYR C	3.39	113.5	-2.2	-0.09	18.43	83
    85	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.86	116.27	-2.78	-0.18	26.82	83
    86	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6	117.15	-2.3	-0.3	22.13	83
    87	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.53	117.84	-2.22	-0.27	22.47	72
    88	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.81	118.09	-2.22	-0.27	22.47	72
    89	93 ARG B, 79 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C	6.81	118.27	-2.22	-0.27	22.47	72
    90	93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C	6.5	118.49	-2.4	0.12	22.12	66
    91	300093 ARG B, 93 ARG B, 79 GLY C, 300082 TYR C, 82 TYR C	6.16	118.92	-2.4	0.12	22.12	66
    92	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	5.73	119.65	-2.22	-0.27	22.47	72
    93	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	4.74	121.61	-1.58	0.04	12.4	61
    94	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.28	124.61	-2.43	-0.3	15.13	72
    95	100093 ARG B, 100079 GLY C, 100058 GLN C	3.21	124.95	-2.8	-0.77	19.64	83
    96	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.28	126.45	-2.2	-0.78	15.57	83
    97	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.07	128.22	-2.43	-0.3	15.13	72
    98	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.9	129.19	-2.2	-0.02	12.43	66
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.34	130.1	-2.4	0.12	22.12	66
    100	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.78	131.42	-2.22	-0.27	22.47	72
    101	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.53	131.89	-2.22	-0.27	22.47	72
    102	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	6.98	132.02	-2.3	-0.3	22.13	83
    103	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	7.03	132.37	-2.22	-0.27	22.47	72
    104	100093 ARG B, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	6.94	132.99	-3.04	-0.19	32.2	74
    105	100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.28	134.9	-1.58	0.04	12.4	61
    106	200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.77	135.95	-1.88	0.25	14.65	61
    107	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.23	138.59	-2.43	-0.3	15.13	72
    108	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	2.94	139.34	-2.2	-0.78	15.57	83
    109	200093 ARG B, 82 TYR C, 200079 GLY C, 200058 GLN C	2.98	140.29	-2.43	-0.3	15.13	72
    110	200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C	3.73	140.49	-2.43	-0.3	15.13	72
    111	200093 ARG B, 82 TYR C, 200058 GLN C	3.76	141.56	-3.1	-0.14	19.05	72
    112	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.63	142.08	-2.53	-0.35	14.7	83
    113	200028 SER B, 200093 ARG B, 200058 GLN C	3.64	142.43	-2.93	-0.83	19.07	94
    114	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.88	143.4	-2.53	-0.35	14.7	83
    115	200028 SER B, 200093 ARG B, 82 TYR C	3.87	143.8	-2.2	-0.09	18.43	83
    116	200028 SER B, 93 ARG B, 200093 ARG B, 82 TYR C	3.76	144.29	-2.78	-0.18	26.82	83
    117	200028 SER B, 93 ARG B, 82 TYR C	3.38	145.67	-2.2	-0.09	18.43	83
    118	200028 SER B, 93 ARG B	3.15	146.46	-2.65	-0.7	26.84	100
    119	27 GLN B, 200028 SER B, 93 ARG B	2.61	151.2	-2.93	-0.83	19.07	94
    120	27 GLN B, 28 SER B, 200028 SER B, 93 ARG B	3.39	151.74	-2.3	-0.82	15.15	94
    121	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	3.74	152.02	-2.4	-0.87	14.72	100
    122	27 GLN B, 93 ARG B, 28 SER B	4.11	152.56	-2.93	-0.83	19.07	94
    123	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	5.48	152.91	-2.4	-0.87	14.72	100
    124	27 GLN B, 200028 SER B, 28 SER B	5.74	156.61	-1.7	-1.01	2.29	106
    125	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.99	157.73	-2.05	-0.99	3.03	95
    126	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.83	158.36	-2.05	-0.99	3.03	95
    127	27 GLN B, 200027 GLN B, 200028 SER B	5.66	159.07	-2.6	-1.06	2.91	95
    128	27 GLN B, 200028 SER B, 200027 GLN B	5.49	159.77	-1.57	-0.96	2.86	100
    129	27 GLN B, 200028 SER B, 26 SER B, 200069 THR B	4.42	162.48	-1.35	-0.91	2.56	102
    130	27 GLN B, 200028 SER B, 200027 GLN B, 26 SER B	4.42	162.93	-1.28	-0.92	2.99	100
    131	200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B, 200028 SER B	4.48	165.28	-0.46	-0.79	3.04	107
    132	200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B	4.72	166.29	-0.48	-0.79	2.95	107
    133	26 SER B, 200069 THR B, 200026 SER B	4.83	168.77	-0.5	-0.79	2.81	107
    134	26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B	4.78	169.85	-1.5	-0.7	15.11	95
    135	26 SER B, 200069 THR B, 200024 ARG B	4.36	171.06	-1.87	-0.66	19.01	95
    136	26 SER B, 200069 THR B, 200024 ARG B, 200070 ASP B	3.68	172.84	-2.28	-0.76	26.69	92
    137	26 SER B, 200024 ARG B, 200070 ASP B	3.62	173.47	-2.8	-0.75	35.03	84
    138	200024 ARG B, 200070 ASP B, 26 SER B	3.4	175.59	-2.93	-0.81	34.46	95
    139	200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B	2.71	177.51	-1.25	-0.32	25.88	85
    140	200070 ASP B, 26 SER B, 3 LEU B	2.09	180.13	-0.17	-0.29	17.17	85
    141	200070 ASP B, 3 LEU B	2.12	182.84	0.15	0.05	24.92	70
    142	200070 ASP B, 3 LEU B, 1 ASP B	2.99	184.81	-0.03	-0.23	17.74	70
    143	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B	3.79	184.95	-0.2	-0.37	13.72	82
    144	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B	3.84	185.84	-0.98	-0.43	25.3	83
    145	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.99	186.08	-1.56	-0.42	30.14	81
    146	3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.9	187.43	-1.08	-0.27	25.25	79
    147	3 LEU B, 1 ASP B, 63 LYS A	3.85	189.32	-1.2	-0.1	33.11	70
    148	3 LEU B, 1 ASP B, 63 LYS A, 97 THR B	3.85	190.76	-1.08	-0.27	25.25	79
    149	3 LEU B, 63 LYS A, 97 THR B, 2 ILE B	3.86	191.2	-0.3	-0.21	13.67	77
    150	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B	3.87	191.58	-0.3	-0.21	13.67	77
    151	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B, 61 ASN A	3.89	192.09	-0.94	-0.32	11.61	84
    152	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	3.95	192.3	-2.4	-0.78	21.56	90
    153	97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	3.99	192.88	-2.03	-0.87	14.58	96
    154	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.17	193.66	-2.4	-0.78	21.56	90
    155	3 LEU B, 63 LYS A, 98 PHE B, 61 ASN A, 46 GLU A	4.26	194.76	-1.5	-0.4	21.26	76
    156	3 LEU B, 63 LYS A, 46 GLU A, 64 ILE A	4.36	198.47	0.23	0.35	24.92	76
    157	3 LEU B, 63 LYS A, 46 GLU A, 200020 SER B	4.72	198.84	-1.1	-0.35	25.3	80
    158	63 LYS A, 46 GLU A, 64 ILE A, 200020 SER B	4.77	199.52	-0.93	-0.18	25.3	92
    159	63 LYS A, 46 GLU A, 64 ILE A	4.16	204.49	-0.97	0.09	33.18	84
    160	46 GLU A, 64 ILE A, 63 LYS A	4	205.31	0.2	-0.04	17.8	90
    161	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.49	207.91	-0.98	-0.14	26.35	87
    162	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.38	211.47	-2	-0.04	38.51	86
    163	46 GLU A, 200018 ARG B, 40 ARG A	3.43	213.86	-4.17	-0.66	51.3	81
    164	46 GLU A, 64 ILE A, 40 ARG A	2.99	214.37	-1.17	0.08	34.01	87
    165	46 GLU A, 40 ARG A	2.15	216.44	-4	-0.78	50.95	80
    166	40 ARG A	1.45	224.32	-4.5	-0.42	52	83
    167	40 ARG A, 88 SER A	1.68	224.99	-2.45	-0.61	27.69	83
    168	40 ARG A, 88 SER A, 91 SER A	1.91	225.33	-1.77	-0.67	19.59	83
    169	40 ARG A, 88 SER A, 41 PRO A, 91 SER A	2.2	225.57	-1.83	-0.57	14.66	86
    170	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.54	226.29	-1.73	-0.53	15.09	70
    171	40 ARG A, 88 SER A, 41 PRO A	3.32	228.85	-2.17	-0.44	18.99	70
    172	40 ARG A, 41 PRO A, 88 SER A	4.81	231.18	-2.3	-0.49	18.42	86
    173	41 PRO A, 88 SER A	4.82	232.16	-1.2	-0.53	1.63	87
    174	41 PRO A, 91 SER A, 88 SER A	4.55	233.13	-1.07	-0.68	1.64	97
    175	41 PRO A, 91 SER A, 88 SER A, 175 LEU A	4.47	233.5	0.15	-0.22	1.26	86
    176	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.42	233.78	0.02	0.3	1.25	69
    177	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.4	233.99	0.23	0.08	1.27	84
    178	91 SER A, 88 SER A, 180 TYR A	4.4	234.23	-0.97	-0.28	1.65	94
    179	91 SER A, 88 SER A	4.44	234.41	-0.8	-0.97	1.67	117
    180	91 SER A, 88 SER A, 180 TYR A	4.47	234.85	-0.97	-0.28	1.65	94
    181	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.49	235.6	0.02	0.3	1.25	69
    182	41 PRO A, 91 SER A, 175 LEU A, 180 TYR A	4.5	236.56	0.02	0.3	1.25	69
    183	41 PRO A, 175 LEU A, 180 TYR A	4.48	240.19	0.3	0.72	1.11	54
    184	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.45	240.49	0.13	0.34	1.68	54
    185	41 PRO A, 175 LEU A, 180 TYR A	4.37	241.12	0.3	0.72	1.11	54
    186	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.21	241.68	0.13	0.34	1.68	54
    187	41 PRO A, 180 TYR A, 173 ALA A	3.86	244	-1.1	0.07	2.19	54
    188	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.49	245.91	-1.7	-0.23	14.12	61
    189	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.42	248.19	-1.78	-0.53	14.11	64
    190	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.57	248.78	-2.55	-0.52	14.11	74
    191	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.45	249.41	-2.55	-0.52	14.11	74
    192	153 GLU A, 172 PRO A, 41 ASN B	3.17	250.3	-2.87	-0.67	18.29	79
    193	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.38	253.41	-2.25	-0.7	14.56	79
    194	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.32	253.92	-1.95	-0.88	15.01	90
    195	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.31	254.28	-0.8	-0.47	12.03	78
    196	153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.34	254.56	-0.8	-0.47	12.03	78
    197	41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.48	255.48	-0.13	-0.31	2.57	79
    198	41 ASN B, 182 LEU A, 171 PHE A	2.79	255.68	-0.03	-0.14	2.3	79
    199	41 ASN B, 182 LEU A, 170 THR A	2.73	255.97	-0.13	-0.13	1.72	88
    200	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.63	257.19	-0.2	-0.3	2.14	88
    201	41 ASN B, 170 THR A, 155 VAL A	2.72	261.03	-1.53	-0.78	2.81	105
    202	41 ASN B, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A	3.06	261.31	-1.14	-0.78	2.69	106
    203	41 ASN B, 156 THR A, 157 VAL A	3.11	261.62	-1.53	-0.78	2.81	105
    204	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.2	261.78	-1.33	-0.78	2.52	106
    205	41 ASN B, 170 THR A, 157 VAL A	3.2	261.89	-1.53	-0.78	2.81	105
    206	41 ASN B, 170 THR A, 155 VAL A	3.21	262.05	-1.53	-0.78	2.81	105
    207	41 ASN B, 170 THR A, 157 VAL A	3.22	262.26	-1.53	-0.78	2.81	105
    208	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.18	262.65	-1.33	-0.78	2.52	106
    209	41 ASN B, 170 THR A, 157 VAL A	3.19	265.87	-1.53	-0.78	2.81	105
    210	41 ASN B, 170 THR A, 157 VAL A, 40 THR B	4.21	266.63	-1.25	-0.79	2.95	105
    211	41 ASN B, 170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.44	266.77	-1.08	-0.79	3.04	105
    212	170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.48	266.95	0.68	-0.31	2.14	102
    213	170 THR A, 157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.56	267.08	-1.16	-0.72	12.26	89
    214	157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.71	267.12	-0.13	-0.22	14.1	85
    215	170 THR A, 157 VAL A, 168 VAL A, 169 LYS B	3.86	267.83	-0.2	-0.21	13.67	92
    216	157 VAL A, 168 VAL A, 169 LYS B, 165 SER A	3.59	268.15	-0.13	-0.22	14.1	85
    217	168 VAL A, 169 LYS B, 165 SER A	2.27	272.61	-0.03	-0.03	17.67	85
    218	168 VAL A, 169 LYS B, 165 SER A	1.73	274.51	-1.57	-0.67	18.75	72
    219	168 VAL A, 169 LYS B, 165 SER A, 167 GLY A	1.62	275.59	-1.28	-0.7	14.91	72
    220	168 VAL A, 169 LYS B, 167 GLY A	1.71	276.83	-1.57	-0.67	18.75	72
    221	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.86	277.02	-1.98	-0.44	26.97	81
    222	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.89	277.24	-1.98	-0.44	26.97	81
    223	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.86	277.27	-1.98	-0.44	26.97	81
    224	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.76	277.69	-1.98	-0.44	26.97	81
    225	169 LYS B, 167 GLY A, 169 HIS A, 167 ASP B	1.69	278.62	-2.75	-0.5	38.55	83
    226	169 LYS B, 167 GLY A, 167 ASP B	1.69	279.98	-2.6	-0.75	34.19	79
    227	169 LYS B, 167 GLY A	1.72	280.69	-2.15	-0.61	26.44	72
    228	169 LYS B, 167 GLY A, 166 SER A	1.75	281.94	-1.57	-0.67	18.75	72
    229	169 LYS B, 167 GLY A, 166 SER A	1.95	282.09	-1.7	-0.73	18.18	94
    230	169 LYS B, 166 SER A	2.14	282.29	-2.35	-0.69	25.59	94
    231	169 LYS B, 167 GLY A, 166 SER A	2.26	285.51	-1.7	-0.73	18.18	94
    232	169 LYS B, 167 GLY A, 166 SER A, 170 ASP B	3.07	286.62	-2.15	-0.81	26.06	91
    233	167 GLY A, 166 SER A, 170 ASP B, 169 LYS B	4.21	287.51	-1.28	-0.9	14.53	101
    234	167 GLY A, 166 SER A, 170 ASP B	4.55	288.29	-1.57	-0.94	18.25	101
    235	167 GLY A, 166 SER A, 170 ASP B, 140 MET A	4.84	289.19	-0.7	-0.45	14.05	98
    236	167 GLY A, 170 ASP B, 140 MET A	4.48	290.68	-0.67	-0.28	18.17	89
    237	167 GLY A, 170 ASP B, 140 MET A, 138 ASN B	4.04	292.21	-1.38	-0.4	14.47	94
    238	170 ASP B, 140 MET A, 138 ASN B	3.89	293.53	-1.7	-0.27	18.17	94
    239	140 MET A, 138 ASN B, 187 THR A	3.62	295.37	-0.77	-0.18	2.16	101
    240	140 MET A, 138 ASN B, 187 THR A, 114 THR B	3.1	297.12	-0.75	-0.33	2.03	102
    241	140 MET A, 187 THR A, 114 THR B	2.8	299.34	0.17	-0.18	1.58	102
    242	140 MET A, 114 THR B	2.75	300.02	0.6	0.12	1.55	100
    243	140 MET A, 114 THR B, 138 ASN A	2.71	300.59	-0.77	-0.18	2.16	101
    244	140 MET A, 114 THR B, 138 ASN A, 139 SER A	2.69	301.74	-0.78	-0.38	2.04	105
    245	140 MET A, 114 THR B, 138 ASN A	2.73	302.57	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

26. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B, 100002 ILE B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200028 SER B, 200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 1 ASP B, 200072 THR B, 1 ASP B, 63 LYS A, 97 THR B, 61 ASN A, 98 PHE B, 46 GLU A, 64 ILE A, 200020 SER B, 63 LYS A, 200018 ARG B, 40 ARG A, 88 SER A, 91 SER A, 41 PRO A, 91 SER A, 88 SER A, 175 LEU A, 180 TYR A, 173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A, 40 THR B, 168 VAL A, 168 VAL A, 169 LYS B, 165 SER A, 167 GLY A, 169 HIS A, 167 ASP B, 166 SER A, 166 SER A, 170 ASP B, 169 LYS B, 140 MET A, 138 ASN B, 187 THR A, 114 THR B, 138 ASN A, 139 SER A

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 300082 TYR C, 200093 ARG B, 82 TYR C, 200082 TYR C, 100058 GLN C, 28 SER B, 200058 GLN C, 200069 THR B, 200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A, 97 THR B, 61 ASN A, 46 GLU A, 64 ILE A, 200020 SER B, 200018 ARG B, 40 ARG A, 41 PRO A, 91 SER A, 88 SER A, 175 LEU A, 180 TYR A, 153 GLU A, 172 PRO A, 41 ASN B, 182 LEU A, 170 THR A, 156 THR A, 168 VAL A, 169 LYS B, 169 HIS A, 167 ASP B, 166 SER A, 170 ASP B, 140 MET A, 138 ASN B, 187 THR A, 114 THR B, 138 ASN A, 139 SER A

    Physicochemical properties of lining side-chains

    Charge: 3 (13-10)
    Hydropathy: -1.5
    Hydrophobicity: -0.42
    Polarity: 14.87
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.27	0.25	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.3	0.45	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.29	0.67	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.23	0.84	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.14	1	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	2.82	1.51	-1.53	-0.78	2.81	105
    7	100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	2.71	2.15	-1.25	-0.79	2.95	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.52	5.49	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.53	6.69	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.79	6.89	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.75	7.27	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.64	7.97	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.7	8.56	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.75	9.1	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.79	9.74	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.83	12.75	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.08	13.48	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.2	13.77	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.26	14.41	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100172 PRO A, 100041 PRO A	3.37	14.77	-2.23	-0.44	17.69	64
    21	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.41	16.83	-1.78	-0.53	14.11	64
    22	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.49	18.91	-1.7	-0.23	14.12	61
    23	100173 ALA A, 100041 PRO A, 100180 TYR A	3.59	21.05	-1.1	0.07	2.19	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	3.97	21.44	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.41	22.11	0.3	0.72	1.11	54
    26	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.47	22.68	0.13	0.34	1.68	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A	4.48	27.26	0.3	0.72	1.11	54
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.5	27.87	-0.06	0.08	1.67	69
    29	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.48	28.16	0.23	0.08	1.27	84
    30	100091 SER A, 100088 SER A	4.44	28.24	-0.8	-0.97	1.67	117
    31	100180 TYR A, 100091 SER A, 100088 SER A	4.39	28.59	-0.97	-0.28	1.65	94
    32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.38	28.85	0.23	0.08	1.27	84
    33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.4	29.2	0.02	0.3	1.25	69
    34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	29.66	0.15	-0.22	1.26	86
    35	100041 PRO A, 100091 SER A, 100088 SER A	4.53	30.71	-1.07	-0.68	1.64	97
    36	100041 PRO A, 100088 SER A	4.82	31.62	-1.2	-0.53	1.63	87
    37	100041 PRO A, 100088 SER A, 100040 ARG A	4.67	34.41	-2.3	-0.49	18.42	86
    38	100041 PRO A, 100088 SER A, 100040 ARG A	3.42	36.27	-2.17	-0.44	18.99	70
    39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.63	37.01	-1.73	-0.53	15.09	70
    40	100088 SER A, 100040 ARG A, 100091 SER A	2.02	38.42	-1.77	-0.67	19.59	83
    41	100088 SER A, 100040 ARG A	1.99	39.65	-2.45	-0.61	27.69	83
    42	100040 ARG A	2.02	45.93	-4.5	-0.42	52	83
    43	100040 ARG A, 100043 HIS A	2.57	47.03	-3.85	-0.08	51.8	87
    44	100040 ARG A, 100046 GLU A	2.76	50.54	-4	-0.78	50.95	80
    45	100040 ARG A, 100046 GLU A, 300018 ARG B	3.5	52.84	-4.17	-0.66	51.3	81
    46	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.39	56	-2	-0.04	38.51	86
    47	100046 GLU A, 300018 ARG B, 100064 ILE A	3.22	56.64	-1.17	0.08	34.01	87
    48	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	2.91	59.59	-0.98	-0.14	26.35	87
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.08	60.45	0.2	-0.04	17.8	90
    50	100046 GLU A, 100064 ILE A, 100063 LYS A	3.34	64.69	-0.97	0.09	33.18	84
    51	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.75	65.24	-0.93	-0.18	25.3	92
    52	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.94	66.28	-1.1	-0.35	25.3	80
    53	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.32	69.83	0.23	0.35	24.92	76
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.97	70.76	-1	-0.3	25.73	67
    55	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.59	71.26	-1.5	-0.4	21.26	76
    56	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.24	71.41	-2.4	-0.78	21.56	90
    57	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.7	71.71	-2.03	-0.87	14.58	96
    58	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.53	71.94	-2.4	-0.78	21.56	90
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.38	72.6	-0.94	-0.32	11.61	84
    60	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.37	73.06	-0.3	-0.21	13.67	77
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.4	73.53	-0.3	-0.21	13.67	77
    62	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.45	75.16	-1.08	-0.27	25.25	79
    63	100063 LYS A, 100003 LEU B, 100001 ASP B	3.66	77.08	-1.2	-0.1	33.11	70
    64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.88	78.05	-1.08	-0.27	25.25	79
    65	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.05	78.27	-1.56	-0.42	30.14	81
    66	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4	79.12	-0.98	-0.43	25.3	83
    67	100003 LEU B, 300070 ASP B, 100001 ASP B	2.9	81.46	-0.03	-0.23	17.74	70
    68	100003 LEU B, 300070 ASP B	2.27	84.33	0.15	0.05	24.92	70
    69	100003 LEU B, 300070 ASP B, 100026 SER B	2.15	87.01	-0.17	-0.29	17.17	85
    70	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.49	88.9	-1.25	-0.32	25.88	85
    71	300070 ASP B, 100026 SER B, 300024 ARG B	3.33	90.37	-2.93	-0.81	34.46	95
    72	300070 ASP B, 300024 ARG B, 100026 SER B	3.59	91.59	-2.8	-0.75	35.03	84
    73	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	4.18	93.37	-2.28	-0.76	26.69	92
    74	300024 ARG B, 100026 SER B, 300069 THR B	4.76	94.44	-1.87	-0.66	19.01	95
    75	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.65	95.43	-1.5	-0.7	15.11	95
    76	100026 SER B, 300069 THR B, 300026 SER B	4.29	98.84	-0.5	-0.79	2.81	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.32	101.27	-0.46	-0.79	3.04	107
    78	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.69	101.42	-1.28	-0.92	2.99	100
    79	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.79	104.59	-1.35	-0.91	2.56	102
    80	100026 SER B, 100027 GLN B, 300028 SER B	5.05	105.33	-1.57	-0.96	2.86	100
    81	100027 GLN B, 300028 SER B, 300027 GLN B	5.25	106	-2.6	-1.06	2.91	95
    82	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	5.49	106.51	-2.05	-0.99	3.03	95
    83	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.74	107.6	-2.05	-0.99	3.03	95
    84	100027 GLN B, 300028 SER B, 100028 SER B	5.54	111.31	-1.7	-1.01	2.29	106
    85	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.86	111.59	-2.4	-0.87	14.72	100
    86	100027 GLN B, 100028 SER B, 100093 ARG B	4.14	111.86	-2.93	-0.83	19.07	94
    87	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.49	112.84	-2.4	-0.87	14.72	100
    88	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.21	113.61	-2.3	-0.82	15.15	94
    89	100027 GLN B, 300028 SER B, 100093 ARG B	2.75	117.97	-2.93	-0.83	19.07	94
    90	300028 SER B, 100093 ARG B	3.18	118.77	-2.65	-0.7	26.84	100
    91	300028 SER B, 100093 ARG B, 100082 TYR C	3.43	120.03	-2.2	-0.09	18.43	83
    92	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.04	123.36	-2.78	-0.18	26.82	83
    93	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.29	123.81	-2.3	-0.3	22.13	83
    94	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.5	124.53	-2.22	-0.27	22.47	72
    95	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.77	124.8	-2.22	-0.27	22.47	72
    96	93 ARG B, 79 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C	6.81	124.98	-2.22	-0.27	22.47	72
    97	93 ARG B, 79 GLY C, 300082 TYR C, 200093 ARG B, 82 TYR C	6.7	125.22	-2.4	0.12	22.12	66
    98	300093 ARG B, 93 ARG B, 79 GLY C, 300082 TYR C, 82 TYR C	6.53	125.68	-2.4	0.12	22.12	66
    99	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.3	126.46	-2.22	-0.27	22.47	72
    100	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.99	127.44	-1.58	0.04	12.4	61
    101	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.6	128.5	-1.88	0.25	14.65	61
    102	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.82	131.43	-2.43	-0.3	15.13	72
    103	100093 ARG B, 100079 GLY C, 100058 GLN C	3.5	131.78	-2.8	-0.77	19.64	83
    104	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.29	132.75	-2.2	-0.78	15.57	83
    105	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.47	134.41	-2.43	-0.3	15.13	72
    106	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.3	135.4	-2.2	-0.02	12.43	66
    107	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	4.84	137.26	-2.4	0.12	22.12	66
    108	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.89	137.93	-2.22	-0.27	22.47	72
    109	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.28	138.57	-2.22	-0.27	22.47	72
    110	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	6.36	138.95	-2.3	-0.3	22.13	83
    111	100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	6.04	139.5	-2.4	0.12	22.12	66
    112	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.61	140.36	-2.22	-0.27	22.47	72
    113	100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.14	141.4	-1.58	0.04	12.4	61
    114	200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	4.65	142.48	-1.88	0.25	14.65	61
    115	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.46	145.29	-2.43	-0.3	15.13	72
    116	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3.49	146.05	-2.2	-0.78	15.57	83
    117	200093 ARG B, 82 TYR C, 200079 GLY C, 200058 GLN C	3.68	147.03	-2.43	-0.3	15.13	72
    118	200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C	3.89	147.24	-2.43	-0.3	15.13	72
    119	200093 ARG B, 82 TYR C, 200058 GLN C	3.8	148.08	-3.1	-0.14	19.05	72
    120	200093 ARG B, 82 TYR C, 200058 GLN C, 200028 SER B	3.78	148.36	-2.43	-0.3	15.13	72
    121	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.79	148.71	-2.53	-0.35	14.7	83
    122	200028 SER B, 200093 ARG B, 200058 GLN C	3.89	149.04	-2.93	-0.83	19.07	94
    123	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.56	150.37	-2.53	-0.35	14.7	83
    124	200028 SER B, 93 ARG B, 200093 ARG B, 82 TYR C	3.32	150.84	-2.78	-0.18	26.82	83
    125	200028 SER B, 93 ARG B, 82 TYR C	2.61	153.02	-2.2	-0.09	18.43	83
    126	27 GLN B, 200028 SER B, 93 ARG B	2.41	157.92	-2.93	-0.83	19.07	94
    127	27 GLN B, 28 SER B, 200028 SER B, 93 ARG B	4.04	158.46	-2.3	-0.82	15.15	94
    128	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	4.42	158.73	-2.4	-0.87	14.72	100
    129	27 GLN B, 93 ARG B, 28 SER B	4.77	159.11	-2.93	-0.83	19.07	94
    130	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	5.46	159.73	-2.4	-0.87	14.72	100
    131	27 GLN B, 200028 SER B, 28 SER B	5.69	163.1	-1.7	-1.01	2.29	106
    132	300028 SER B, 300027 GLN B, 28 SER B	6.02	163.42	-1.7	-1.01	2.29	106
    133	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	6.08	164.2	-2.05	-0.99	3.03	95
    134	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.01	165.49	-2.05	-0.99	3.03	95
    135	27 GLN B, 200028 SER B, 200027 GLN B	5.86	166.23	-1.57	-0.96	2.86	100
    136	27 GLN B, 200028 SER B, 26 SER B	5.67	166.9	-1.57	-0.96	2.86	100
    137	27 GLN B, 200028 SER B, 26 SER B, 200069 THR B	4.28	169.16	-1.35	-0.91	2.56	102
    138	27 GLN B, 200028 SER B, 200027 GLN B, 26 SER B	4.33	169.63	-1.28	-0.92	2.99	100
    139	200028 SER B, 200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B	4.5	172.11	-0.46	-0.79	3.04	107
    140	200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B	4.85	173.14	-0.48	-0.79	2.95	107
    141	26 SER B, 200069 THR B, 200026 SER B	4.96	175.25	-0.5	-0.79	2.81	107
    142	26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B	4.9	176.25	-1.5	-0.7	15.11	95
    143	26 SER B, 200069 THR B, 200024 ARG B	4.27	178.06	-1.87	-0.66	19.01	95
    144	26 SER B, 200069 THR B, 200024 ARG B, 200070 ASP B	3.73	179.42	-2.28	-0.76	26.69	92
    145	26 SER B, 200024 ARG B, 200070 ASP B	3.61	180.2	-2.8	-0.75	35.03	84
    146	200024 ARG B, 200070 ASP B, 26 SER B	3.24	182.28	-2.93	-0.81	34.46	95
    147	200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B	2.56	184.27	-1.25	-0.32	25.88	85
    148	200070 ASP B, 26 SER B, 3 LEU B	2.21	186.99	-0.17	-0.29	17.17	85
    149	200070 ASP B, 3 LEU B	2.24	189.72	0.15	0.05	24.92	70
    150	200070 ASP B, 3 LEU B, 1 ASP B	2.94	191.46	-0.03	-0.23	17.74	70
    151	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B	3.92	191.61	-0.2	-0.37	13.72	82
    152	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B	3.95	192.55	-0.98	-0.43	25.3	83
    153	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.95	192.8	-1.56	-0.42	30.14	81
    154	3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.69	194.29	-1.08	-0.27	25.25	79
    155	3 LEU B, 1 ASP B, 63 LYS A	3.56	195.62	-1.2	-0.1	33.11	70
    156	3 LEU B, 1 ASP B, 63 LYS A, 97 THR B	3.51	197.65	-1.08	-0.27	25.25	79
    157	3 LEU B, 63 LYS A, 97 THR B, 61 ASN A	3.66	198.08	-1.08	-0.2	13.67	84
    158	3 LEU B, 63 LYS A, 97 THR B, 61 ASN A, 98 PHE B	3.76	198.9	-0.94	-0.32	11.61	84
    159	63 LYS A, 97 THR B, 61 ASN A, 98 PHE B, 46 GLU A	4.27	199.07	-2.4	-0.78	21.56	90
    160	97 THR B, 61 ASN A, 98 PHE B, 46 GLU A	4.49	199.37	-2.03	-0.87	14.58	96
    161	63 LYS A, 97 THR B, 61 ASN A, 98 PHE B, 46 GLU A	4.91	200.05	-2.4	-0.78	21.56	90
    162	3 LEU B, 63 LYS A, 61 ASN A, 98 PHE B, 46 GLU A	5.08	201.12	-1.5	-0.4	21.26	76
    163	3 LEU B, 63 LYS A, 98 PHE B, 46 GLU A	5.2	202.37	-1	-0.3	25.73	67
    164	3 LEU B, 63 LYS A, 46 GLU A, 64 ILE A	5.03	205.08	0.23	0.35	24.92	76
    165	3 LEU B, 63 LYS A, 46 GLU A, 200020 SER B	4.47	206.11	-1.1	-0.35	25.3	80
    166	63 LYS A, 46 GLU A, 64 ILE A	2.86	211.27	-0.97	0.09	33.18	84
    167	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	2.93	214.74	-0.98	-0.14	26.35	87
    168	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.62	217.88	-2	-0.04	38.51	86
    169	46 GLU A, 200018 ARG B, 40 ARG A	3.85	220.43	-4.17	-0.66	51.3	81
    170	46 GLU A, 64 ILE A, 40 ARG A	4.1	220.91	-1.17	0.08	34.01	87
    171	46 GLU A, 40 ARG A	3.4	224.57	-4	-0.78	50.95	80
    172	40 ARG A	2.24	231.01	-4.5	-0.42	52	83
    173	40 ARG A, 88 SER A	2.11	231.68	-2.45	-0.61	27.69	83
    174	40 ARG A, 88 SER A, 91 SER A	2.11	232	-1.77	-0.67	19.59	83
    175	40 ARG A, 88 SER A, 41 PRO A, 91 SER A	2.23	232.26	-1.83	-0.57	14.66	86
    176	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.45	233.03	-1.73	-0.53	15.09	70
    177	40 ARG A, 88 SER A, 41 PRO A	3.1	235.71	-2.17	-0.44	18.99	70
    178	40 ARG A, 41 PRO A, 88 SER A	4.44	237.62	-2.3	-0.49	18.42	86
    179	41 PRO A, 88 SER A	4.78	239.12	-1.2	-0.53	1.63	87
    180	41 PRO A, 91 SER A, 88 SER A	4.67	239.62	-1.07	-0.68	1.64	97
    181	41 PRO A, 91 SER A, 88 SER A, 175 LEU A	4.55	240.04	0.15	-0.22	1.26	86
    182	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.43	240.35	0.02	0.3	1.25	69
    183	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.21	240.77	0.23	0.08	1.27	84
    184	91 SER A, 88 SER A, 180 TYR A	4.13	240.86	-0.97	-0.28	1.65	94
    185	91 SER A, 88 SER A	4.08	241.01	-0.8	-0.97	1.67	117
    186	91 SER A, 88 SER A, 180 TYR A	4.07	241.42	-0.97	-0.28	1.65	94
    187	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.09	242.16	0.02	0.3	1.25	69
    188	88 SER A, 41 PRO A, 91 SER A, 175 LEU A, 180 TYR A	4.13	243.13	-0.06	0.08	1.67	69
    189	41 PRO A, 175 LEU A, 180 TYR A	4.2	246.84	0.3	0.72	1.11	54
    190	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.47	247.16	0.13	0.34	1.68	54
    191	41 PRO A, 175 LEU A, 180 TYR A	4.38	247.81	0.3	0.72	1.11	54
    192	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.34	248.6	0.13	0.34	1.68	54
    193	41 PRO A, 180 TYR A, 173 ALA A	3.87	251.03	-1.1	0.07	2.19	54
    194	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.47	252.46	-1.7	-0.23	14.12	61
    195	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.35	254.83	-1.78	-0.53	14.11	64
    196	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.53	255.44	-2.55	-0.52	14.11	74
    197	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.46	256.1	-2.55	-0.52	14.11	74
    198	153 GLU A, 172 PRO A, 41 ASN B	3.34	256.53	-2.87	-0.67	18.29	79
    199	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.51	259.63	-2.25	-0.7	14.56	79
    200	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.34	260.72	-1.95	-0.88	15.01	90
    201	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.32	261.02	-0.8	-0.47	12.03	78
    202	153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.35	261.24	-0.8	-0.47	12.03	78
    203	41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.47	262.08	-0.13	-0.31	2.57	79
    204	41 ASN B, 182 LEU A, 171 PHE A	2.81	262.29	-0.03	-0.14	2.3	79
    205	41 ASN B, 182 LEU A, 170 THR A	2.77	262.61	-0.13	-0.13	1.72	88
    206	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.64	263.87	-0.2	-0.3	2.14	88
    207	41 ASN B, 170 THR A, 155 VAL A	2.68	267.76	-1.53	-0.78	2.81	105
    208	41 ASN B, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A	3	267.99	-1.14	-0.78	2.69	106
    209	41 ASN B, 156 THR A, 157 VAL A	3.07	268.3	-1.53	-0.78	2.81	105
    210	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.22	268.46	-1.33	-0.78	2.52	106
    211	41 ASN B, 170 THR A, 157 VAL A	3.24	268.54	-1.53	-0.78	2.81	105
    212	41 ASN B, 170 THR A, 155 VAL A	3.25	268.72	-1.53	-0.78	2.81	105
    213	41 ASN B, 170 THR A, 157 VAL A	3.26	268.86	-1.53	-0.78	2.81	105
    214	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.22	269.27	-1.33	-0.78	2.52	106
    215	41 ASN B, 170 THR A, 157 VAL A	3.21	272.57	-1.53	-0.78	2.81	105
    216	41 ASN B, 170 THR A, 157 VAL A, 40 THR B	4.16	273.3	-1.25	-0.79	2.95	105
    217	41 ASN B, 170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.58	273.43	-1.08	-0.79	3.04	105
    218	170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.64	273.56	0.68	-0.31	2.14	102
    219	170 THR A, 157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.58	273.69	-1.16	-0.72	12.26	89
    220	157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.61	273.73	-0.13	-0.22	14.1	85
    221	170 THR A, 157 VAL A, 168 VAL A, 169 LYS B	4.51	274.41	-0.2	-0.21	13.67	92
    222	157 VAL A, 168 VAL A, 169 LYS B, 165 SER A	4	275.22	-0.13	-0.22	14.1	85
    223	168 VAL A, 169 LYS B, 165 SER A	2.4	279.21	-0.03	-0.03	17.67	85
    224	168 VAL A, 169 LYS B, 165 SER A	1.32	281.15	-1.57	-0.67	18.75	72
    225	168 VAL A, 169 LYS B, 165 SER A, 167 GLY A	1.26	282.34	-1.28	-0.7	14.91	72
    226	168 VAL A, 169 LYS B, 167 GLY A	1.65	283.55	-1.57	-0.67	18.75	72
    227	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.92	283.84	-1.98	-0.44	26.97	81
    228	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	2	283.95	-1.98	-0.44	26.97	81
    229	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.85	284.41	-1.98	-0.44	26.97	81
    230	169 LYS B, 167 GLY A, 169 HIS A, 167 ASP B	1.72	285.07	-2.75	-0.5	38.55	83
    231	169 LYS B, 167 GLY A, 167 ASP B	1.61	286.43	-2.6	-0.75	34.19	79
    232	169 LYS B, 167 GLY A	1.58	287.17	-2.15	-0.61	26.44	72
    233	169 LYS B, 167 GLY A, 166 SER A	1.56	288.55	-1.57	-0.67	18.75	72
    234	169 LYS B, 167 GLY A, 166 SER A	1.64	288.7	-1.7	-0.73	18.18	94
    235	169 LYS B, 166 SER A	1.82	288.91	-2.35	-0.69	25.59	94
    236	169 LYS B, 167 GLY A, 166 SER A	1.94	292.19	-1.7	-0.73	18.18	94
    237	169 LYS B, 167 GLY A, 166 SER A, 170 ASP B	3.14	293.4	-2.15	-0.81	26.06	91
    238	167 GLY A, 166 SER A, 170 ASP B, 169 LYS B	4.64	293.86	-1.28	-0.9	14.53	101
    239	167 GLY A, 166 SER A, 170 ASP B	4.8	295.04	-1.57	-0.94	18.25	101
    240	167 GLY A, 166 SER A, 170 ASP B, 140 MET A	4.97	295.97	-0.7	-0.45	14.05	98
    241	167 GLY A, 170 ASP B, 140 MET A	4.48	297.26	-0.67	-0.28	18.17	89
    242	167 GLY A, 170 ASP B, 140 MET A, 138 ASN B	3.98	298.84	-1.38	-0.4	14.47	94
    243	170 ASP B, 140 MET A, 138 ASN B	3.93	300.19	-1.7	-0.27	18.17	94
    244	140 MET A, 138 ASN B, 187 THR A	3.65	302.14	-0.77	-0.18	2.16	101
    245	140 MET A, 138 ASN B, 187 THR A, 114 THR B	3.02	303.95	-0.75	-0.33	2.03	102
    246	140 MET A, 187 THR A, 114 THR B	2.75	305.78	0.17	-0.18	1.58	102
    247	140 MET A, 114 THR B	2.69	306.5	0.6	0.12	1.55	100
    248	140 MET A, 114 THR B, 138 ASN A	2.66	307.12	-0.77	-0.18	2.16	101
    249	140 MET A, 114 THR B, 138 ASN A, 139 SER A	2.64	308.34	-0.78	-0.38	2.04	105
    250	140 MET A, 114 THR B, 138 ASN A	2.7	309.19	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

27. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 28 SER B, 200028 SER B, 27 GLN B, 69 THR B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300002 ILE B, 300098 PHE B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A, 300169 HIS A, 300167 ASP B, 300166 SER A, 300166 SER A, 300170 ASP B, 300169 LYS B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300113 PRO B, 300207 LYS B, 300136 GLN A, 300115 VAL B, 300116 SER B, 300140 MET A, 300135 ALA A, 300117 ILE B, 300116 SER B, 300117 ILE B, 300132 GLY A, 300208 SER B, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A, 300211 ARG B, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A, 300168 VAL A, 300169 LYS B, 300169 HIS A, 300167 ASP B, 300166 SER A, 300170 ASP B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300207 LYS B, 300116 SER B, 300135 ALA A, 300117 ILE B, 300209 PHE B, 300119 PRO B, 300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 5 (16-11)
    Hydropathy: -1.4
    Hydrophobicity: -0.42
    Polarity: 14.25
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.23	0.1	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.12	1.76	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.15	3.9	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.47	4.17	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.55	4.73	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.73	5.13	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.73	5.47	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.67	6.28	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A	3.63	6.66	-2.23	-0.32	2.18	73
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.51	7.27	-2.55	-0.52	14.11	74
    11	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.45	7.61	-2.55	-0.52	14.11	74
    12	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.29	10.09	-1.78	-0.53	14.11	64
    13	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.43	12.29	-1.7	-0.23	14.12	61
    14	100041 PRO A, 100173 ALA A, 100180 TYR A	4	14.1	-1.1	0.07	2.19	54
    15	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.42	14.64	0.13	0.34	1.68	54
    16	100041 PRO A, 100180 TYR A, 100175 LEU A	4.27	15.36	0.3	0.72	1.11	54
    17	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.16	15.97	0.13	0.34	1.68	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A	4.1	20.74	0.3	0.72	1.11	54
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.12	21.26	-0.06	0.08	1.67	69
    20	100180 TYR A, 100091 SER A, 100088 SER A	4.16	21.46	-0.97	-0.28	1.65	94
    21	100091 SER A, 100088 SER A	4.21	21.55	-0.8	-0.97	1.67	117
    22	100180 TYR A, 100091 SER A, 100088 SER A	4.29	21.73	-0.97	-0.28	1.65	94
    23	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.39	22.3	0.23	0.08	1.27	84
    24	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.66	22.74	0.02	0.3	1.25	69
    25	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.83	23.26	0.15	-0.22	1.26	86
    26	100041 PRO A, 100091 SER A, 100088 SER A	5	23.82	-1.07	-0.68	1.64	97
    27	100041 PRO A, 100088 SER A	5.15	25.15	-1.2	-0.53	1.63	87
    28	100041 PRO A, 100088 SER A, 100040 ARG A	4.41	27.76	-2.3	-0.49	18.42	86
    29	100041 PRO A, 100088 SER A, 100040 ARG A	3.31	29.64	-2.17	-0.44	18.99	70
    30	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.93	30.04	-1.73	-0.53	15.09	70
    31	100088 SER A, 100040 ARG A, 100091 SER A	1.96	31.21	-1.77	-0.67	19.59	83
    32	100088 SER A, 100040 ARG A	1.71	32.24	-2.45	-0.61	27.69	83
    33	100040 ARG A	1.38	38.78	-4.5	-0.42	52	83
    34	100040 ARG A, 100043 HIS A	1.58	40.01	-3.85	-0.08	51.8	87
    35	100040 ARG A, 100043 HIS A, 100046 GLU A	1.81	41.04	-3.73	-0.43	51.17	83
    36	100040 ARG A, 100046 GLU A	2.1	43.73	-4	-0.78	50.95	80
    37	100040 ARG A, 100046 GLU A, 300018 ARG B	3.15	46.15	-4.17	-0.66	51.3	81
    38	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.41	49.6	-2	-0.04	38.51	86
    39	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	2.78	52.59	-0.98	-0.14	26.35	87
    40	100046 GLU A, 100064 ILE A, 100063 LYS A	2.75	53.5	0.2	-0.04	17.8	90
    41	100046 GLU A, 100064 ILE A, 100063 LYS A	2.8	57.97	-0.97	0.09	33.18	84
    42	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.65	58.52	-0.93	-0.18	25.3	92
    43	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.98	59.7	-1.1	-0.35	25.3	80
    44	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.41	63.41	0.23	0.35	24.92	76
    45	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	5.28	64.24	-1.5	-0.4	21.26	76
    46	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	5.09	64.61	-2.4	-0.78	21.56	90
    47	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.62	64.82	-2.03	-0.87	14.58	96
    48	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.38	65.06	-2.4	-0.78	21.56	90
    49	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.82	66.13	-0.94	-0.32	11.61	84
    50	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.71	66.62	-1.08	-0.2	13.67	84
    51	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.56	68.29	-1.08	-0.27	25.25	79
    52	100063 LYS A, 100003 LEU B, 100001 ASP B	3.56	70.3	-1.2	-0.1	33.11	70
    53	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.69	71.3	-1.08	-0.27	25.25	79
    54	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.87	72.26	-0.98	-0.43	25.3	83
    55	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.81	72.45	-0.2	-0.37	13.72	82
    56	100003 LEU B, 300070 ASP B, 100001 ASP B	3.05	74.76	-0.03	-0.23	17.74	70
    57	100003 LEU B, 300070 ASP B	2.21	77.76	0.15	0.05	24.92	70
    58	100003 LEU B, 300070 ASP B, 100026 SER B	2.15	80	-0.17	-0.29	17.17	85
    59	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.52	82	-1.25	-0.32	25.88	85
    60	300070 ASP B, 100026 SER B, 300024 ARG B	3.27	83.59	-2.93	-0.81	34.46	95
    61	300070 ASP B, 300024 ARG B, 100026 SER B	3.57	84.53	-2.8	-0.75	35.03	84
    62	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	4.19	86.22	-2.28	-0.76	26.69	92
    63	300024 ARG B, 100026 SER B, 300069 THR B	4.69	87.85	-1.87	-0.66	19.01	95
    64	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.68	88.55	-1.5	-0.7	15.11	95
    65	100026 SER B, 300069 THR B, 300026 SER B	4.31	92	-0.5	-0.79	2.81	107
    66	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.25	94.5	-0.46	-0.79	3.04	107
    67	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.38	94.67	-1.28	-0.92	2.99	100
    68	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.47	97.51	-1.35	-0.91	2.56	102
    69	100026 SER B, 100027 GLN B, 300028 SER B	5.58	98.28	-1.57	-0.96	2.86	100
    70	300027 GLN B, 100027 GLN B, 300028 SER B	5.68	99.01	-1.57	-0.96	2.86	100
    71	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.76	99.98	-2.05	-0.99	3.03	95
    72	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.86	100.79	-2.05	-0.99	3.03	95
    73	100027 GLN B, 300028 SER B, 100028 SER B	5.76	104.29	-1.7	-1.01	2.29	106
    74	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	5.57	104.71	-2.4	-0.87	14.72	100
    75	100027 GLN B, 100028 SER B, 100093 ARG B	5.03	105.21	-2.93	-0.83	19.07	94
    76	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.76	105.74	-2.4	-0.87	14.72	100
    77	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.45	106.5	-2.3	-0.82	15.15	94
    78	100027 GLN B, 300028 SER B, 100093 ARG B	2.63	111.73	-2.93	-0.83	19.07	94
    79	300028 SER B, 100093 ARG B, 100082 TYR C	2.63	113.52	-2.2	-0.09	18.43	83
    80	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.01	113.92	-2.78	-0.18	26.82	83
    81	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.2	114.76	-2.53	-0.35	14.7	83
    82	300028 SER B, 300093 ARG B, 300058 GLN C	3.72	115.11	-2.93	-0.83	19.07	94
    83	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.79	115.91	-2.53	-0.35	14.7	83
    84	100082 TYR C, 300093 ARG B, 300058 GLN C	3.47	116.7	-3.1	-0.14	19.05	72
    85	100082 TYR C, 300093 ARG B, 300058 GLN C, 300080 ASP C	3.36	116.91	-2.43	-0.3	15.13	72
    86	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.17	118.18	-2.43	-0.3	15.13	72
    87	300093 ARG B, 300058 GLN C, 300080 ASP C, 300079 GLY C	3.52	118.91	-2.2	-0.78	15.57	83
    88	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	4.21	121.93	-2.43	-0.3	15.13	72
    89	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	6.01	123.05	-1.88	0.25	14.65	61
    90	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	6.4	124.61	-1.58	0.04	12.4	61
    91	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.93	124.88	-2.4	0.12	22.12	66
    92	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	7.02	125.4	-2.4	0.12	22.12	66
    93	79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C	6.89	125.75	-2.22	-0.27	22.47	72
    94	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.44	126.63	-2.22	-0.27	22.47	72
    95	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.13	127.12	-2.3	-0.3	22.13	83
    96	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	3.93	130.13	-2.78	-0.18	26.82	83
    97	300093 ARG B, 300082 TYR C, 28 SER B	3.5	131.57	-2.2	-0.09	18.43	83
    98	300093 ARG B, 28 SER B	3.41	132.43	-2.65	-0.7	26.84	100
    99	300027 GLN B, 300093 ARG B, 28 SER B	3.42	137.65	-2.93	-0.83	19.07	94
    100	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.5	138.23	-2.4	-0.87	14.72	100
    101	300028 SER B, 300027 GLN B, 300093 ARG B	4.68	138.49	-2.93	-0.83	19.07	94
    102	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.81	139.01	-2.4	-0.87	14.72	100
    103	300028 SER B, 300027 GLN B, 28 SER B	4.97	142.51	-1.7	-1.01	2.29	106
    104	100027 GLN B, 300028 SER B, 100028 SER B	5.97	142.84	-1.7	-1.01	2.29	106
    105	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6.2	143.71	-2.05	-0.99	3.03	95
    106	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.35	145.12	-2.05	-0.99	3.03	95
    107	300027 GLN B, 28 SER B, 27 GLN B	6.11	145.88	-1.57	-0.96	2.86	100
    108	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.09	148.69	-1.35	-0.91	2.56	102
    109	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	4.25	148.98	-1.28	-0.92	2.99	100
    110	300026 SER B, 28 SER B, 27 GLN B, 69 THR B, 26 SER B	4.37	151.49	-0.46	-0.79	3.04	107
    111	300026 SER B, 27 GLN B, 69 THR B, 26 SER B	4.82	152.58	-0.48	-0.79	2.95	107
    112	300026 SER B, 69 THR B, 26 SER B	4.96	154.71	-0.5	-0.79	2.81	107
    113	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	5.01	155.85	-1.5	-0.7	15.11	95
    114	300026 SER B, 69 THR B, 24 ARG B	4.62	157.14	-1.87	-0.66	19.01	95
    115	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.97	158.72	-2.28	-0.76	26.69	92
    116	300026 SER B, 24 ARG B, 70 ASP B	3.58	159.6	-2.8	-0.75	35.03	84
    117	24 ARG B, 70 ASP B, 300026 SER B	3.2	161.79	-2.93	-0.81	34.46	95
    118	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.52	163.32	-1.25	-0.32	25.88	85
    119	70 ASP B, 300026 SER B, 300003 LEU B	2.11	166.16	-0.17	-0.29	17.17	85
    120	70 ASP B, 300003 LEU B	2.26	169.05	0.15	0.05	24.92	70
    121	70 ASP B, 300003 LEU B, 300001 ASP B	2.98	170.93	-0.03	-0.23	17.74	70
    122	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.89	171.06	-0.2	-0.37	13.72	82
    123	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.94	171.91	-0.98	-0.43	25.3	83
    124	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.98	172.16	-1.56	-0.42	30.14	81
    125	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.9	173.68	-1.08	-0.27	25.25	79
    126	300003 LEU B, 300001 ASP B, 300063 LYS A	3.87	175.06	-1.2	-0.1	33.11	70
    127	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.87	176.68	-1.08	-0.27	25.25	79
    128	300003 LEU B, 300063 LYS A, 300097 THR B, 300002 ILE B	3.93	177.17	-0.3	-0.21	13.67	77
    129	300003 LEU B, 300063 LYS A, 300097 THR B, 300098 PHE B	3.97	177.59	-0.3	-0.21	13.67	77
    130	300003 LEU B, 300063 LYS A, 300097 THR B, 300098 PHE B, 300061 ASN A	4.04	178.17	-0.94	-0.32	11.61	84
    131	300063 LYS A, 300097 THR B, 300098 PHE B, 300061 ASN A, 300046 GLU A	4.21	178.39	-2.4	-0.78	21.56	90
    132	300097 THR B, 300098 PHE B, 300061 ASN A, 300046 GLU A	4.3	179.15	-2.03	-0.87	14.58	96
    133	300003 LEU B, 300063 LYS A, 300098 PHE B, 300061 ASN A, 300046 GLU A	4.49	180.12	-1.5	-0.4	21.26	76
    134	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	4.49	181.39	-1	-0.3	25.73	67
    135	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	4.21	184.45	0.23	0.35	24.92	76
    136	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	3.85	185.46	-1.1	-0.35	25.3	80
    137	300063 LYS A, 300046 GLU A, 300064 ILE A	3.13	190.88	-0.97	0.09	33.18	84
    138	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.22	193.79	-0.98	-0.14	26.35	87
    139	300046 GLU A, 300064 ILE A, 18 ARG B	3.58	194.43	-1.17	0.08	34.01	87
    140	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.65	197.82	-2	-0.04	38.51	86
    141	300046 GLU A, 18 ARG B, 300040 ARG A	3.87	199.87	-4.17	-0.66	51.3	81
    142	300046 GLU A, 300064 ILE A, 300040 ARG A	3.85	200.41	-1.17	0.08	34.01	87
    143	300046 GLU A, 300040 ARG A	3.59	202.68	-4	-0.78	50.95	80
    144	300040 ARG A	2.67	209.8	-4.5	-0.42	52	83
    145	300040 ARG A, 300088 SER A	2.49	210.78	-2.45	-0.61	27.69	83
    146	300040 ARG A, 300088 SER A, 300091 SER A	2.39	211.27	-1.77	-0.67	19.59	83
    147	300040 ARG A, 300088 SER A, 300091 SER A	2.37	211.54	-1.9	-0.73	19.02	100
    148	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.48	211.85	-1.83	-0.57	14.66	86
    149	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.71	212.8	-1.73	-0.53	15.09	70
    150	300040 ARG A, 300088 SER A, 300041 PRO A	3.44	215	-2.17	-0.44	18.99	70
    151	300040 ARG A, 300041 PRO A, 300088 SER A	4.71	217.07	-2.3	-0.49	18.42	86
    152	300041 PRO A, 300088 SER A	5.09	218.09	-1.2	-0.53	1.63	87
    153	300091 SER A, 300041 PRO A, 300088 SER A	4.7	219.15	-1.07	-0.68	1.64	97
    154	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.52	219.56	0.15	-0.22	1.26	86
    155	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.38	219.85	0.02	0.3	1.25	69
    156	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.27	220.07	0.23	0.08	1.27	84
    157	300091 SER A, 300088 SER A, 300180 TYR A	4.14	220.31	-0.97	-0.28	1.65	94
    158	300091 SER A, 300088 SER A	4.11	220.6	-0.8	-0.97	1.67	117
    159	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.1	221.24	0.23	0.08	1.27	84
    160	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.1	222.18	-0.06	0.08	1.67	69
    161	300041 PRO A, 300175 LEU A, 300180 TYR A	4.12	226.22	0.3	0.72	1.11	54
    162	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.29	226.56	0.13	0.34	1.68	54
    163	300041 PRO A, 300175 LEU A, 300180 TYR A	4.45	227.23	0.3	0.72	1.11	54
    164	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.29	227.75	0.13	0.34	1.68	54
    165	300041 PRO A, 300180 TYR A, 300173 ALA A	3.62	230.25	-1.1	0.07	2.19	54
    166	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.31	232.26	-1.7	-0.23	14.12	61
    167	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.33	234.25	-1.78	-0.53	14.11	64
    168	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.41	234.88	-2.55	-0.52	14.11	74
    169	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.15	235.6	-2.55	-0.52	14.11	74
    170	300153 GLU A, 300172 PRO A, 300041 ASN B	2.98	236.08	-2.87	-0.67	18.29	79
    171	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.27	239.38	-2.25	-0.7	14.56	79
    172	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.24	239.94	-1.95	-0.88	15.01	90
    173	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.26	240.32	-0.8	-0.47	12.03	78
    174	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.3	240.6	-0.8	-0.47	12.03	78
    175	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.47	241.49	-0.13	-0.31	2.57	79
    176	300041 ASN B, 300182 LEU A, 300171 PHE A	2.85	241.71	-0.03	-0.14	2.3	79
    177	300041 ASN B, 300182 LEU A, 300170 THR A	2.78	242.01	-0.13	-0.13	1.72	88
    178	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.49	243.74	-0.2	-0.3	2.14	88
    179	300041 ASN B, 300170 THR A, 300155 VAL A	2.51	247.07	-1.53	-0.78	2.81	105
    180	300041 ASN B, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A	2.85	247.35	-1.14	-0.78	2.69	106
    181	300041 ASN B, 300156 THR A, 300157 VAL A	2.96	247.69	-1.53	-0.78	2.81	105
    182	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.26	247.85	-1.33	-0.78	2.52	106
    183	300041 ASN B, 300170 THR A, 300155 VAL A	3.32	248.12	-1.53	-0.78	2.81	105
    184	300041 ASN B, 300170 THR A, 300157 VAL A	3.32	248.27	-1.53	-0.78	2.81	105
    185	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.22	248.8	-1.33	-0.78	2.52	106
    186	300041 ASN B, 300170 THR A, 300157 VAL A	3.38	251.63	-1.53	-0.78	2.81	105
    187	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B	3.96	252.74	-1.25	-0.79	2.95	105
    188	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.28	252.96	0.68	-0.31	2.14	102
    189	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.53	253.11	-1.16	-0.72	12.26	89
    190	300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B	3.85	253.8	-0.2	-0.21	13.67	92
    191	300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A	3.1	254.7	-0.13	-0.22	14.1	85
    192	300168 VAL A, 300169 LYS B, 300165 SER A	1.76	258.91	-0.03	-0.03	17.67	85
    193	300168 VAL A, 300169 LYS B, 300165 SER A	1.4	260.57	-1.57	-0.67	18.75	72
    194	300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A	1.43	261.57	-1.28	-0.7	14.91	72
    195	300168 VAL A, 300169 LYS B, 300167 GLY A	1.72	262.89	-1.57	-0.67	18.75	72
    196	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.92	263.06	-1.98	-0.44	26.97	81
    197	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.96	263.22	-1.98	-0.44	26.97	81
    198	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.97	263.35	-1.98	-0.44	26.97	81
    199	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.88	263.67	-1.98	-0.44	26.97	81
    200	300168 VAL A, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.82	263.83	-1.88	-0.6	27.02	88
    201	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.7	264.65	-2.75	-0.5	38.55	83
    202	300169 LYS B, 300167 GLY A, 300167 ASP B	1.61	266.13	-2.6	-0.75	34.19	79
    203	300169 LYS B, 300167 GLY A	1.59	266.88	-2.15	-0.61	26.44	72
    204	300169 LYS B, 300167 GLY A, 300166 SER A	1.59	267.84	-1.57	-0.67	18.75	72
    205	300169 LYS B, 300167 GLY A, 300166 SER A	1.65	271.56	-1.7	-0.73	18.18	94
    206	300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B	3.04	272.9	-2.15	-0.81	26.06	91
    207	300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B	4.54	273.4	-1.28	-0.9	14.53	101
    208	300167 GLY A, 300166 SER A, 300170 ASP B	4.7	274.26	-1.57	-0.94	18.25	101
    209	300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A	4.86	275.3	-0.7	-0.45	14.05	98
    210	300167 GLY A, 300170 ASP B, 300140 MET A	4.51	276.63	-0.67	-0.28	18.17	89
    211	300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B	4.17	278.29	-1.38	-0.4	14.47	94
    212	300170 ASP B, 300140 MET A, 300138 ASN B	3.9	279.66	-1.7	-0.27	18.17	94
    213	300140 MET A, 300138 ASN B, 300187 THR A	3.43	281.44	-0.77	-0.18	2.16	101
    214	300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B	2.82	282.99	-0.75	-0.33	2.03	102
    215	300140 MET A, 300187 THR A, 300114 THR B	2.49	285.49	0.17	-0.18	1.58	102
    216	300140 MET A, 300114 THR B	2.46	286.22	0.6	0.12	1.55	100
    217	300140 MET A, 300114 THR B, 300138 ASN A	2.47	286.74	-0.77	-0.18	2.16	101
    218	300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A	2.51	287.71	-0.78	-0.38	2.04	105
    219	300140 MET A, 300114 THR B, 300138 ASN A	2.94	290.32	-0.77	-0.18	2.16	101
    220	300114 THR B, 300138 ASN A	3.96	293.86	-2.1	-0.77	2.52	105
    221	300114 THR B, 300138 ASN A, 300113 PRO B	4.41	294.41	-1.53	-0.78	2.81	105
    222	300114 THR B, 300138 ASN A, 300113 PRO B, 300207 LYS B	4.39	295.07	-2.13	-0.69	14.48	94
    223	300114 THR B, 300138 ASN A, 300207 LYS B	4.1	297.12	-2.7	-0.65	18.18	94
    224	300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A	3.88	298.12	-2.13	-0.69	14.48	94
    225	300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A, 300115 VAL B	2.88	299.44	-1.78	-0.71	12.26	94
    226	300114 THR B, 300207 LYS B, 300136 GLN A, 300115 VAL B	2.56	299.84	-1.35	-0.7	14.48	89
    227	300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A, 300115 VAL B	2.54	300.47	-1.78	-0.71	12.26	94
    228	300114 THR B, 300138 ASN A, 300136 GLN A, 300115 VAL B, 300116 SER B	2.59	300.85	-1.16	-0.82	2.69	109
    229	300114 THR B, 300136 GLN A, 300115 VAL B, 300116 SER B, 300140 MET A	2.63	301.91	-0.54	-0.83	2.69	112
    230	300114 THR B, 300207 LYS B, 300136 GLN A, 300115 VAL B, 300116 SER B	2.68	302.58	-1.24	-0.75	11.92	98
    231	300207 LYS B, 300136 GLN A, 300115 VAL B, 300116 SER B	2.67	303.25	-1.38	-0.75	14.48	94
    232	300136 GLN A, 300115 VAL B, 300116 SER B	2.65	303.85	-0.53	-0.86	2.81	117
    233	300136 GLN A, 300115 VAL B, 300116 SER B, 300135 ALA A	2.51	304.7	0.05	-0.64	2.11	108
    234	300115 VAL B, 300116 SER B, 300135 ALA A	2.19	305.85	0.2	-0.58	1.68	108
    235	300116 SER B, 300135 ALA A, 300117 ILE B	2.05	308.65	0.2	-0.58	1.68	108
    236	300135 ALA A, 300116 SER B, 300117 ILE B	1.9	309.65	1.97	0.34	1.17	101
    237	300135 ALA A, 300117 ILE B	1.69	311.36	3.15	0.92	0.07	101
    238	300135 ALA A, 300117 ILE B, 300132 GLY A, 300208 SER B	1.61	312.31	1.38	0.06	1.72	101
    239	300135 ALA A, 300117 ILE B, 300132 GLY A	1.58	312.84	1.97	0.34	1.17	101
    240	300117 ILE B, 300132 GLY A, 300209 PHE B	1.59	314.16	2.3	0.79	1.29	77
    241	300117 ILE B, 300132 GLY A, 300209 PHE B, 300119 PRO B	1.62	314.64	0.1	-0.09	2.17	54
    242	300117 ILE B, 300132 GLY A, 300119 PRO B	1.62	314.8	-0.8	-0.56	2.78	58
    243	300117 ILE B, 300132 GLY A, 300119 PRO B	1.62	315	0.83	0.31	1.7	80
    244	300117 ILE B, 300132 GLY A, 300119 PRO B	1.65	315.4	-0.8	-0.56	2.78	58
    245	300132 GLY A, 300209 PHE B, 300119 PRO B	1.69	319.64	0.27	0.15	1.77	54
    246	300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B	2.02	320.06	0.1	-0.09	2.17	54
    247	300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A	2.09	320.56	0	-0.23	2.41	54
    248	300132 GLY A, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A	2.27	321.55	-1.46	-0.58	12.74	70
    249	300119 PRO B, 300210 ASN B, 300218 ARG A	2.03	323.13	-2.17	-0.44	18.99	70
    250	300209 PHE B, 300119 PRO B, 300210 ASN B, 300218 ARG A	1.99	323.63	-0.93	0.01	14.33	64
    251	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B	1.98	324.25	-1.73	-0.53	15.09	70
    252	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B, 300186 TYR B	2.05	324.61	-1.64	-0.2	12.39	63
    253	300119 PRO B, 300218 ARG A, 300211 ARG B, 300186 TYR B	2.13	326.31	-1.95	-0.05	14.64	63
    254	300218 ARG A, 300186 TYR B, 300211 ARG B	2.29	327.9	-3.43	0.09	35.2	72
    255	300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B	2.41	327.9	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

28. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 200028 SER B, 28 SER B, 100027 GLN B, 100069 THR B, 200026 SER B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A, 200170 THR A, 200155 VAL A, 200156 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A, 200169 HIS A, 200167 ASP B, 200166 SER A, 200166 SER A, 200170 ASP B, 200169 LYS B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A, 200113 PRO B, 200207 LYS B, 200136 GLN A, 200115 VAL B, 200116 SER B, 200140 MET A, 200135 ALA A, 200117 ILE B, 200116 SER B, 200117 ILE B, 200208 SER B, 200132 GLY A, 200209 PHE B, 200119 PRO B, 200133 SER A, 200210 ASN B, 200218 ARG A, 200211 ARG B, 200186 TYR B, 200211 ARG B, 200125 LEU B

    Unique lining residues set - sidechains

    100040 THR B, 100085 ASN B, 100165 ASP B, 100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A, 200168 VAL A, 200169 LYS B, 200169 HIS A, 200167 ASP B, 200166 SER A, 200170 ASP B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A, 200207 LYS B, 200116 SER B, 200135 ALA A, 200117 ILE B, 200209 PHE B, 200119 PRO B, 200218 ARG A, 200186 TYR B, 200211 ARG B, 200125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 5 (16-11)
    Hydropathy: -1.3
    Hydrophobicity: -0.42
    Polarity: 14.01
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100042 GLY A, 100040 THR B, 100085 ASN B, 100165 ASP B	3.23	0.09	-2.03	-0.85	14.53	99
    2	100042 GLY A, 100040 THR B, 100165 ASP B	3.12	1.73	-1.53	-0.87	18.25	96
    3	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B	3.14	3.87	-2.03	-0.85	14.53	99
    4	100042 GLY A, 100040 THR B, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.46	4.14	-1.94	-0.69	11.94	88
    5	100042 GLY A, 100165 ASP B, 100041 ASN B, 100172 PRO A	3.54	4.71	-2.25	-0.68	14.51	82
    6	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.73	5.08	-1.78	-0.44	2.48	73
    7	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.73	5.4	-1.78	-0.44	2.48	73
    8	100042 GLY A, 100041 ASN B, 100172 PRO A, 100041 PRO A	3.68	6.2	-1.78	-0.44	2.48	73
    9	100041 ASN B, 100172 PRO A, 100041 PRO A	3.64	6.59	-2.23	-0.32	2.18	73
    10	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.53	7.2	-2.55	-0.52	14.11	74
    11	100041 ASN B, 100172 PRO A, 100041 PRO A, 100153 GLU A	3.41	7.89	-2.55	-0.52	14.11	74
    12	100172 PRO A, 100041 PRO A, 100153 GLU A, 100173 ALA A	3.3	9.95	-1.78	-0.53	14.11	64
    13	100041 PRO A, 100153 GLU A, 100173 ALA A, 100180 TYR A	3.4	12.08	-1.7	-0.23	14.12	61
    14	100041 PRO A, 100173 ALA A, 100180 TYR A	3.95	14.31	-1.1	0.07	2.19	54
    15	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.49	14.7	0.13	0.34	1.68	54
    16	100041 PRO A, 100180 TYR A, 100175 LEU A	4.29	15.29	0.3	0.72	1.11	54
    17	100041 PRO A, 100173 ALA A, 100180 TYR A, 100175 LEU A	4.17	15.73	0.13	0.34	1.68	54
    18	100041 PRO A, 100180 TYR A, 100175 LEU A	4.1	20.31	0.3	0.72	1.11	54
    19	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.11	21.01	-0.06	0.08	1.67	69
    20	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.14	21.37	0.23	0.08	1.27	84
    21	100180 TYR A, 100091 SER A, 100088 SER A	4.18	21.81	-0.97	-0.28	1.65	94
    22	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	22.08	0.23	0.08	1.27	84
    23	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.58	22.45	0.02	0.3	1.25	69
    24	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.73	22.93	0.15	-0.22	1.26	86
    25	100041 PRO A, 100091 SER A, 100088 SER A	4.9	24.02	-1.07	-0.68	1.64	97
    26	100041 PRO A, 100088 SER A	5.2	24.93	-1.2	-0.53	1.63	87
    27	100041 PRO A, 100088 SER A, 100040 ARG A	4.62	27.22	-2.3	-0.49	18.42	86
    28	100041 PRO A, 100088 SER A, 100040 ARG A	3.19	29.74	-2.17	-0.44	18.99	70
    29	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.82	30.12	-1.73	-0.53	15.09	70
    30	100088 SER A, 100040 ARG A, 100091 SER A	1.89	31.41	-1.77	-0.67	19.59	83
    31	100088 SER A, 100040 ARG A	1.66	32.56	-2.45	-0.61	27.69	83
    32	100040 ARG A	1.38	39.06	-4.5	-0.42	52	83
    33	100040 ARG A, 100043 HIS A	1.62	40.22	-3.85	-0.08	51.8	87
    34	100040 ARG A, 100046 GLU A	1.86	43.83	-4	-0.78	50.95	80
    35	100040 ARG A, 100046 GLU A, 300018 ARG B	3.21	46.22	-4.17	-0.66	51.3	81
    36	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.4	49.62	-2	-0.04	38.51	86
    37	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	2.78	52.6	-0.98	-0.14	26.35	87
    38	100046 GLU A, 100064 ILE A, 100063 LYS A	2.75	53.5	0.2	-0.04	17.8	90
    39	100046 GLU A, 100064 ILE A, 100063 LYS A	2.8	57.93	-0.97	0.09	33.18	84
    40	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.64	58.49	-0.93	-0.18	25.3	92
    41	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.97	59.62	-1.1	-0.35	25.3	80
    42	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.4	63.3	0.23	0.35	24.92	76
    43	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	5.29	64.17	-1.5	-0.4	21.26	76
    44	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	5.11	64.58	-2.4	-0.78	21.56	90
    45	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.65	64.79	-2.03	-0.87	14.58	96
    46	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.4	65.02	-2.4	-0.78	21.56	90
    47	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.84	66.05	-0.94	-0.32	11.61	84
    48	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.73	66.54	-1.08	-0.2	13.67	84
    49	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.56	68.85	-1.08	-0.27	25.25	79
    50	100063 LYS A, 100003 LEU B, 100001 ASP B	3.58	70.18	-1.2	-0.1	33.11	70
    51	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.68	71.25	-1.08	-0.27	25.25	79
    52	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.88	71.48	-1.56	-0.42	30.14	81
    53	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.89	72.21	-0.98	-0.43	25.3	83
    54	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.83	72.39	-0.2	-0.37	13.72	82
    55	100003 LEU B, 300070 ASP B, 100001 ASP B	3.13	74.53	-0.03	-0.23	17.74	70
    56	100003 LEU B, 300070 ASP B	2.26	77.48	0.15	0.05	24.92	70
    57	100003 LEU B, 300070 ASP B, 100026 SER B	2.14	80.26	-0.17	-0.29	17.17	85
    58	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.61	82.22	-1.25	-0.32	25.88	85
    59	300070 ASP B, 100026 SER B, 300024 ARG B	3.33	83.58	-2.93	-0.81	34.46	95
    60	300070 ASP B, 300024 ARG B, 100026 SER B	3.56	84.66	-2.8	-0.75	35.03	84
    61	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	4.25	86.44	-2.28	-0.76	26.69	92
    62	300024 ARG B, 100026 SER B, 300069 THR B	4.73	87.6	-1.87	-0.66	19.01	95
    63	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.66	88.66	-1.5	-0.7	15.11	95
    64	100026 SER B, 300069 THR B, 300026 SER B	4.36	91.17	-0.5	-0.79	2.81	107
    65	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.29	92.24	-0.48	-0.79	2.95	107
    66	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.26	94.35	-0.46	-0.79	3.04	107
    67	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	4.33	94.53	-0.58	-0.84	2.52	112
    68	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	4.4	94.71	-1.28	-0.92	2.99	100
    69	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.49	97.59	-1.35	-0.91	2.56	102
    70	100026 SER B, 300028 SER B, 100027 GLN B	5.59	98.36	-1.57	-0.96	2.86	100
    71	300028 SER B, 100027 GLN B, 300027 GLN B	5.69	99.07	-2.6	-1.06	2.91	95
    72	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	5.76	99.65	-2.05	-0.99	3.03	95
    73	300028 SER B, 100027 GLN B, 100028 SER B	5.82	100	-1.7	-1.01	2.29	106
    74	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.86	100.81	-2.05	-0.99	3.03	95
    75	300028 SER B, 100027 GLN B, 100028 SER B	5.79	104.29	-1.7	-1.01	2.29	106
    76	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	5.62	104.71	-2.4	-0.87	14.72	100
    77	100027 GLN B, 100028 SER B, 100093 ARG B	5.06	105.17	-2.93	-0.83	19.07	94
    78	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.77	105.66	-2.4	-0.87	14.72	100
    79	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.42	106.38	-2.3	-0.82	15.15	94
    80	300028 SER B, 100027 GLN B, 100093 ARG B	2.68	110.9	-2.93	-0.83	19.07	94
    81	300028 SER B, 100093 ARG B	2.68	111.75	-2.65	-0.7	26.84	100
    82	300028 SER B, 100093 ARG B, 100082 TYR C	2.81	113.62	-2.2	-0.09	18.43	83
    83	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.81	116.59	-2.78	-0.18	26.82	83
    84	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.32	117.04	-2.3	-0.3	22.13	83
    85	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.57	117.78	-2.22	-0.27	22.47	72
    86	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.84	118.06	-1.58	0.04	12.4	61
    87	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.54	118.57	-2.4	0.12	22.12	66
    88	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.24	119.19	-2.4	0.12	22.12	66
    89	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.39	121.26	-1.58	0.04	12.4	61
    90	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	4.91	122.37	-1.88	0.25	14.65	61
    91	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.26	124.56	-2.43	-0.3	15.13	72
    92	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	2.97	125.38	-2.2	-0.78	15.57	83
    93	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	2.97	126.44	-2.43	-0.3	15.13	72
    94	100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C	3.6	126.65	-2.43	-0.3	15.13	72
    95	100093 ARG B, 200082 TYR C, 100058 GLN C	3.71	127.52	-3.1	-0.14	19.05	72
    96	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.81	127.81	-2.43	-0.3	15.13	72
    97	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.74	128.17	-2.53	-0.35	14.7	83
    98	100028 SER B, 100093 ARG B, 100058 GLN C	3.5	128.53	-2.93	-0.83	19.07	94
    99	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.39	129.56	-2.53	-0.35	14.7	83
    100	100028 SER B, 100093 ARG B, 200082 TYR C	3.37	130	-2.2	-0.09	18.43	83
    101	100028 SER B, 200093 ARG B, 200082 TYR C	3.38	132.08	-2.2	-0.09	18.43	83
    102	100028 SER B, 200027 GLN B, 200093 ARG B	3.55	137.22	-2.93	-0.83	19.07	94
    103	100028 SER B, 200027 GLN B, 200093 ARG B, 200028 SER B	4.4	137.83	-2.3	-0.82	15.15	94
    104	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.48	138.14	-2.4	-0.87	14.72	100
    105	200027 GLN B, 200028 SER B, 200093 ARG B	4.55	138.54	-2.93	-0.83	19.07	94
    106	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.76	139.19	-2.4	-0.87	14.72	100
    107	100028 SER B, 200027 GLN B, 200028 SER B	4.98	142.63	-1.7	-1.01	2.29	106
    108	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.06	143.87	-2.05	-0.99	3.03	95
    109	100027 GLN B, 100028 SER B, 200027 GLN B, 200028 SER B	6.48	144.55	-2.05	-0.99	3.03	95
    110	100027 GLN B, 100028 SER B, 200027 GLN B	6.3	145.31	-2.6	-1.06	2.91	95
    111	100028 SER B, 200027 GLN B, 100027 GLN B	6.04	146.05	-1.57	-0.96	2.86	100
    112	100028 SER B, 200027 GLN B, 100069 THR B, 200026 SER B	4.09	148.58	-1.35	-0.91	2.56	102
    113	100028 SER B, 200027 GLN B, 100027 GLN B, 200026 SER B	4.16	149.05	-1.28	-0.92	2.99	100
    114	100026 SER B, 100028 SER B, 100027 GLN B, 100069 THR B, 200026 SER B	4.39	151.61	-0.46	-0.79	3.04	107
    115	100026 SER B, 100027 GLN B, 100069 THR B, 200026 SER B	4.83	152.68	-0.48	-0.79	2.95	107
    116	100026 SER B, 100069 THR B, 200026 SER B	4.97	154.75	-0.5	-0.79	2.81	107
    117	100026 SER B, 100069 THR B, 200026 SER B, 100024 ARG B	5.01	155.88	-1.5	-0.7	15.11	95
    118	100069 THR B, 200026 SER B, 100024 ARG B	4.62	157.16	-1.87	-0.66	19.01	95
    119	100069 THR B, 200026 SER B, 100024 ARG B, 100070 ASP B	3.97	158.73	-2.28	-0.76	26.69	92
    120	200026 SER B, 100024 ARG B, 100070 ASP B	3.58	159.62	-2.8	-0.75	35.03	84
    121	100024 ARG B, 100070 ASP B, 200026 SER B	3.23	161.74	-2.93	-0.81	34.46	95
    122	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.36	163.81	-1.25	-0.32	25.88	85
    123	100070 ASP B, 200026 SER B, 200003 LEU B	2.11	166.05	-0.17	-0.29	17.17	85
    124	100070 ASP B, 200003 LEU B	2.23	168.95	0.15	0.05	24.92	70
    125	100070 ASP B, 200003 LEU B, 200001 ASP B	2.95	170.89	-0.03	-0.23	17.74	70
    126	100070 ASP B, 200003 LEU B, 200001 ASP B, 100072 THR B	3.87	171.04	-0.2	-0.37	13.72	82
    127	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	3.93	172.07	-0.98	-0.43	25.3	83
    128	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.96	172.36	-1.56	-0.42	30.14	81
    129	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.91	173.38	-1.08	-0.27	25.25	79
    130	200003 LEU B, 200001 ASP B, 200063 LYS A	3.87	175.4	-1.2	-0.1	33.11	70
    131	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.87	176.94	-1.08	-0.27	25.25	79
    132	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A	3.95	177.4	-1.08	-0.2	13.67	84
    133	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B	4	177.78	-0.3	-0.21	13.67	77
    134	200003 LEU B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B	4.07	178.29	-0.94	-0.32	11.61	84
    135	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.25	178.48	-2.4	-0.78	21.56	90
    136	200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.34	178.78	-2.03	-0.87	14.58	96
    137	200063 LYS A, 200097 THR B, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.47	179.48	-2.4	-0.78	21.56	90
    138	200003 LEU B, 200063 LYS A, 200061 ASN A, 200098 PHE B, 200046 GLU A	4.5	180.6	-1.5	-0.4	21.26	76
    139	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	4.48	181.9	-1	-0.3	25.73	67
    140	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	4.15	184.56	0.23	0.35	24.92	76
    141	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	3.97	184.99	-1.1	-0.35	25.3	80
    142	200063 LYS A, 200046 GLU A, 200064 ILE A, 100020 SER B	3.78	185.76	-0.93	-0.18	25.3	92
    143	200063 LYS A, 200046 GLU A, 200064 ILE A	3.13	190.24	-0.97	0.09	33.18	84
    144	200046 GLU A, 200064 ILE A, 200063 LYS A	3.18	191.14	0.2	-0.04	17.8	90
    145	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.25	193.96	-0.98	-0.14	26.35	87
    146	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.6	197.3	-2	-0.04	38.51	86
    147	200046 GLU A, 100018 ARG B, 200040 ARG A	3.84	199.93	-4.17	-0.66	51.3	81
    148	200046 GLU A, 200064 ILE A, 200040 ARG A	3.84	200.5	-1.17	0.08	34.01	87
    149	200046 GLU A, 200040 ARG A	3.57	202.86	-4	-0.78	50.95	80
    150	200040 ARG A	2.66	209.89	-4.5	-0.42	52	83
    151	200040 ARG A, 200088 SER A	2.49	210.83	-2.45	-0.61	27.69	83
    152	200040 ARG A, 200088 SER A, 200091 SER A	2.38	211.3	-1.77	-0.67	19.59	83
    153	200040 ARG A, 200088 SER A, 200091 SER A	2.38	211.56	-1.9	-0.73	19.02	100
    154	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.49	211.88	-1.83	-0.57	14.66	86
    155	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.72	212.82	-1.73	-0.53	15.09	70
    156	200040 ARG A, 200088 SER A, 200041 PRO A	3.45	215	-2.17	-0.44	18.99	70
    157	200040 ARG A, 200041 PRO A, 200088 SER A	4.71	217.05	-2.3	-0.49	18.42	86
    158	200041 PRO A, 200088 SER A	4.91	218.61	-1.2	-0.53	1.63	87
    159	200091 SER A, 200041 PRO A, 200088 SER A	4.72	219.12	-1.07	-0.68	1.64	97
    160	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.54	219.53	0.15	-0.22	1.26	86
    161	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.39	219.83	0.02	0.3	1.25	69
    162	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.28	220.06	0.23	0.08	1.27	84
    163	200091 SER A, 200088 SER A, 200180 TYR A	4.14	220.3	-0.97	-0.28	1.65	94
    164	200091 SER A, 200088 SER A	4.11	220.55	-0.8	-0.97	1.67	117
    165	200091 SER A, 200088 SER A, 200180 TYR A	4.1	221.12	-0.97	-0.28	1.65	94
    166	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.1	222.02	-0.06	0.08	1.67	69
    167	200041 PRO A, 200175 LEU A, 200180 TYR A	4.11	226.19	0.3	0.72	1.11	54
    168	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.28	226.54	0.13	0.34	1.68	54
    169	200041 PRO A, 200175 LEU A, 200180 TYR A	4.43	227.22	0.3	0.72	1.11	54
    170	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.18	228.12	0.13	0.34	1.68	54
    171	200041 PRO A, 200180 TYR A, 200173 ALA A	3.67	230.06	-1.1	0.07	2.19	54
    172	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.31	232.1	-1.7	-0.23	14.12	61
    173	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.32	234.12	-1.78	-0.53	14.11	64
    174	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.35	235.08	-2.55	-0.52	14.11	74
    175	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.23	235.44	-2.55	-0.52	14.11	74
    176	200153 GLU A, 200172 PRO A, 200041 ASN B	2.89	236.38	-2.87	-0.67	18.29	79
    177	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.31	239.06	-2.25	-0.7	14.56	79
    178	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.24	240.17	-1.95	-0.88	15.01	90
    179	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A	2.27	240.46	-0.8	-0.47	12.03	78
    180	200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A	2.33	240.66	-0.8	-0.47	12.03	78
    181	200041 ASN B, 200172 PRO A, 200182 LEU A, 200171 PHE A	2.51	241.39	-0.13	-0.31	2.57	79
    182	200041 ASN B, 200182 LEU A, 200171 PHE A	2.84	241.81	-0.03	-0.14	2.3	79
    183	200041 ASN B, 200182 LEU A, 200170 THR A	2.8	241.97	-0.13	-0.13	1.72	88
    184	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.49	243.19	-0.2	-0.3	2.14	88
    185	200041 ASN B, 200170 THR A, 200155 VAL A	2.5	247.18	-1.53	-0.78	2.81	105
    186	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	2.87	247.4	-1.33	-0.78	2.52	106
    187	200041 ASN B, 200156 THR A, 200157 VAL A	2.99	247.54	-1.53	-0.78	2.81	105
    188	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.19	247.87	-1.33	-0.78	2.52	106
    189	200041 ASN B, 200170 THR A, 200155 VAL A	3.32	248.05	-1.53	-0.78	2.81	105
    190	200041 ASN B, 200170 THR A, 200157 VAL A	3.32	248.27	-1.53	-0.78	2.81	105
    191	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.22	248.8	-1.33	-0.78	2.52	106
    192	200041 ASN B, 200170 THR A, 200157 VAL A	3.38	251.61	-1.53	-0.78	2.81	105
    193	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B	3.96	252.72	-1.25	-0.79	2.95	105
    194	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.28	252.95	0.68	-0.31	2.14	102
    195	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.52	253.09	-1.16	-0.72	12.26	89
    196	200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.85	253.14	-0.13	-0.22	14.1	85
    197	200170 THR A, 200157 VAL A, 200168 VAL A, 200169 LYS B	3.55	254.04	-0.2	-0.21	13.67	92
    198	200157 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A	3.17	254.55	-0.13	-0.22	14.1	85
    199	200168 VAL A, 200169 LYS B, 200165 SER A	1.82	258.67	-0.03	-0.03	17.67	85
    200	200168 VAL A, 200169 LYS B, 200165 SER A	1.39	260.54	-1.57	-0.67	18.75	72
    201	200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A	1.41	261.91	-1.28	-0.7	14.91	72
    202	200168 VAL A, 200169 LYS B, 200167 GLY A	1.78	262.79	-1.57	-0.67	18.75	72
    203	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.9	263.02	-1.98	-0.44	26.97	81
    204	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.95	263.24	-1.98	-0.44	26.97	81
    205	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.99	263.3	-1.98	-0.44	26.97	81
    206	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.84	263.77	-1.98	-0.44	26.97	81
    207	200169 LYS B, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.72	264.4	-2.75	-0.5	38.55	83
    208	200169 LYS B, 200167 GLY A, 200167 ASP B	1.62	265.79	-2.6	-0.75	34.19	79
    209	200169 LYS B, 200167 GLY A	1.59	266.56	-2.15	-0.61	26.44	72
    210	200169 LYS B, 200167 GLY A, 200166 SER A	1.58	267.95	-1.57	-0.67	18.75	72
    211	200169 LYS B, 200167 GLY A, 200166 SER A	1.68	268.11	-1.7	-0.73	18.18	94
    212	200169 LYS B, 200166 SER A	1.86	268.36	-2.35	-0.69	25.59	94
    213	200169 LYS B, 200167 GLY A, 200166 SER A	1.98	271.32	-1.7	-0.73	18.18	94
    214	200169 LYS B, 200167 GLY A, 200166 SER A, 200170 ASP B	2.91	272.65	-2.15	-0.81	26.06	91
    215	200167 GLY A, 200166 SER A, 200170 ASP B, 200169 LYS B	4.43	273.6	-1.28	-0.9	14.53	101
    216	200167 GLY A, 200166 SER A, 200170 ASP B	4.75	274.38	-1.57	-0.94	18.25	101
    217	200167 GLY A, 200166 SER A, 200170 ASP B, 200140 MET A	4.92	275.16	-0.7	-0.45	14.05	98
    218	200167 GLY A, 200170 ASP B, 200140 MET A	4.49	276.74	-0.67	-0.28	18.17	89
    219	200167 GLY A, 200170 ASP B, 200140 MET A, 200138 ASN B	4.21	278.04	-1.38	-0.4	14.47	94
    220	200170 ASP B, 200140 MET A, 200138 ASN B	3.89	279.72	-1.7	-0.27	18.17	94
    221	200140 MET A, 200138 ASN B, 200187 THR A	3.42	281.5	-0.77	-0.18	2.16	101
    222	200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B	2.82	283.03	-0.75	-0.33	2.03	102
    223	200140 MET A, 200187 THR A, 200114 THR B	2.48	285.53	0.17	-0.18	1.58	102
    224	200140 MET A, 200114 THR B	2.46	286.25	0.6	0.12	1.55	100
    225	200140 MET A, 200114 THR B, 200138 ASN A	2.47	286.76	-0.77	-0.18	2.16	101
    226	200140 MET A, 200114 THR B, 200138 ASN A, 200139 SER A	2.51	287.72	-0.78	-0.38	2.04	105
    227	200140 MET A, 200114 THR B, 200138 ASN A	2.94	290.27	-0.77	-0.18	2.16	101
    228	200114 THR B, 200138 ASN A	3.95	293.83	-2.1	-0.77	2.52	105
    229	200114 THR B, 200138 ASN A, 200113 PRO B	4.4	294.39	-1.53	-0.78	2.81	105
    230	200114 THR B, 200138 ASN A, 200113 PRO B, 200207 LYS B	4.4	295.02	-2.13	-0.69	14.48	94
    231	200114 THR B, 200138 ASN A, 200207 LYS B	4.13	297.03	-2.7	-0.65	18.18	94
    232	200114 THR B, 200138 ASN A, 200207 LYS B, 200136 GLN A	3.65	298.78	-2.13	-0.69	14.48	94
    233	200114 THR B, 200138 ASN A, 200207 LYS B, 200136 GLN A, 200115 VAL B	2.91	299.45	-1.78	-0.71	12.26	94
    234	200114 THR B, 200207 LYS B, 200136 GLN A, 200115 VAL B	2.54	300.1	-1.35	-0.7	14.48	89
    235	200114 THR B, 200138 ASN A, 200207 LYS B, 200136 GLN A, 200115 VAL B	2.55	300.43	-1.78	-0.71	12.26	94
    236	200114 THR B, 200138 ASN A, 200136 GLN A, 200115 VAL B, 200116 SER B	2.58	300.79	-1.16	-0.82	2.69	109
    237	200114 THR B, 200136 GLN A, 200115 VAL B, 200116 SER B, 200140 MET A	2.62	301.79	-0.54	-0.83	2.69	112
    238	200114 THR B, 200207 LYS B, 200136 GLN A, 200115 VAL B, 200116 SER B	2.68	302.44	-1.24	-0.75	11.92	98
    239	200207 LYS B, 200136 GLN A, 200115 VAL B, 200116 SER B	2.68	303.12	-1.38	-0.75	14.48	94
    240	200136 GLN A, 200115 VAL B, 200116 SER B	2.66	303.73	-0.53	-0.86	2.81	117
    241	200136 GLN A, 200115 VAL B, 200116 SER B, 200135 ALA A	2.53	304.69	0.05	-0.64	2.11	108
    242	200115 VAL B, 200116 SER B, 200135 ALA A	2.2	305.8	0.2	-0.58	1.68	108
    243	200116 SER B, 200135 ALA A, 200117 ILE B	2.08	308.45	0.2	-0.58	1.68	108
    244	200135 ALA A, 200117 ILE B, 200116 SER B	2.02	308.94	0.33	-0.53	2.25	100
    245	200135 ALA A, 200116 SER B, 200117 ILE B	1.94	309.43	1.97	0.34	1.17	101
    246	200135 ALA A, 200117 ILE B	1.72	311.09	3.15	0.92	0.07	101
    247	200135 ALA A, 200117 ILE B, 200208 SER B	1.66	311.65	1.97	0.34	1.17	101
    248	200135 ALA A, 200117 ILE B, 200208 SER B, 200132 GLY A	1.62	312.14	1.38	0.06	1.72	101
    249	200135 ALA A, 200117 ILE B, 200132 GLY A	1.59	312.95	1.97	0.34	1.17	101
    250	200117 ILE B, 200132 GLY A, 200209 PHE B	1.59	314.26	2.3	0.79	1.29	77
    251	200117 ILE B, 200132 GLY A, 200209 PHE B, 200119 PRO B	1.62	314.73	0.1	-0.09	2.17	54
    252	200117 ILE B, 200132 GLY A, 200119 PRO B	1.62	314.86	-0.8	-0.56	2.78	58
    253	200117 ILE B, 200132 GLY A, 200119 PRO B	1.62	315.11	0.83	0.31	1.7	80
    254	200117 ILE B, 200132 GLY A, 200209 PHE B, 200119 PRO B	1.66	315.63	0.1	-0.09	2.17	54
    255	200132 GLY A, 200209 PHE B, 200119 PRO B	1.71	319.8	0.27	0.15	1.77	54
    256	200132 GLY A, 200209 PHE B, 200119 PRO B, 200133 SER A, 200210 ASN B	2.04	320.46	0	-0.23	2.41	54
    257	200132 GLY A, 200119 PRO B, 200133 SER A, 200210 ASN B, 200218 ARG A	2.23	321.6	-1.46	-0.58	12.74	70
    258	200119 PRO B, 200210 ASN B, 200218 ARG A	2.02	323.16	-2.17	-0.44	18.99	70
    259	200209 PHE B, 200119 PRO B, 200210 ASN B, 200218 ARG A	1.99	323.66	-0.93	0.01	14.33	64
    260	200119 PRO B, 200210 ASN B, 200218 ARG A, 200211 ARG B	1.98	324.26	-1.73	-0.53	15.09	70
    261	200119 PRO B, 200210 ASN B, 200218 ARG A, 200211 ARG B, 200186 TYR B	2.05	324.63	-1.64	-0.2	12.39	63
    262	200119 PRO B, 200218 ARG A, 200211 ARG B, 200186 TYR B	2.14	326.33	-1.95	-0.05	14.64	63
    263	200218 ARG A, 200186 TYR B, 200211 ARG B	2.3	327.91	-3.43	0.09	35.2	72
    264	200218 ARG A, 200186 TYR B, 200211 ARG B, 200125 LEU B	2.41	327.91	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

29. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C, 300082 TYR C, 79 GLY C, 93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100079 GLY C, 28 SER B, 200028 SER B, 69 THR B, 27 GLN B, 26 SER B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 300001 ASP B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A, 300064 ILE A, 20 SER B, 300063 LYS A, 18 ARG B, 300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A, 300169 HIS A, 300167 ASP B, 300166 SER A, 300166 SER A, 300170 ASP B, 300169 LYS B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300113 PRO B, 300207 LYS B, 300115 VAL B, 300136 GLN A, 300116 SER B, 300140 MET A, 300135 ALA A, 300117 ILE B, 300116 SER B, 300117 ILE B, 300208 SER B, 300132 GLY A, 300209 PHE B, 300119 PRO B, 300133 SER A, 300210 ASN B, 300218 ARG A, 300211 ARG B, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300082 TYR C, 93 ARG B, 200093 ARG B, 82 TYR C, 200082 TYR C, 28 SER B, 69 THR B, 24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300046 GLU A, 300064 ILE A, 20 SER B, 18 ARG B, 300040 ARG A, 300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A, 300153 GLU A, 300172 PRO A, 300041 ASN B, 300182 LEU A, 300170 THR A, 300156 THR A, 300168 VAL A, 300169 LYS B, 300169 HIS A, 300167 ASP B, 300166 SER A, 300170 ASP B, 300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B, 300138 ASN A, 300139 SER A, 300207 LYS B, 300116 SER B, 300135 ALA A, 300117 ILE B, 300209 PHE B, 300119 PRO B, 300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 6 (16-10)
    Hydropathy: -1.3
    Hydrophobicity: -0.42
    Polarity: 13.74
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.27	0.28	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.42	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.26	0.62	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.24	0.78	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.22	0.96	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.08	1.43	-1.53	-0.78	2.81	105
    7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	3.02	2.05	-1.14	-0.78	2.69	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.79	5.5	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.71	6.58	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.74	6.97	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.18	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.61	7.94	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.56	8.51	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.54	9.06	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.53	9.72	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.53	12.83	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	2.81	13.23	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	2.92	13.85	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.13	14.55	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.33	17.13	-1.78	-0.53	14.11	64
    21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.5	18.75	-1.7	-0.23	14.12	61
    22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.55	21.03	-1.1	0.07	2.19	54
    23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	3.87	21.44	0.13	0.34	1.68	54
    24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.32	22.03	0.3	0.72	1.11	54
    25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.5	22.45	0.13	0.34	1.68	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.12	27.02	0.3	0.72	1.11	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.06	27.74	-0.06	0.08	1.67	69
    28	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.03	28.11	0.23	0.08	1.27	84
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.03	28.56	-0.97	-0.28	1.65	94
    30	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.28	28.82	0.23	0.08	1.27	84
    31	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.42	29.19	0.02	0.3	1.25	69
    32	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.58	29.67	0.15	-0.22	1.26	86
    33	100041 PRO A, 100091 SER A, 100088 SER A	4.73	30.77	-1.07	-0.68	1.64	97
    34	100041 PRO A, 100088 SER A	4.99	31.68	-1.2	-0.53	1.63	87
    35	100041 PRO A, 100088 SER A, 100040 ARG A	4.39	34	-2.3	-0.49	18.42	86
    36	100041 PRO A, 100088 SER A, 100040 ARG A	2.7	36.51	-2.17	-0.44	18.99	70
    37	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.14	36.89	-1.73	-0.53	15.09	70
    38	100088 SER A, 100040 ARG A, 100091 SER A	0.61	38.21	-1.77	-0.67	19.59	83
    39	100088 SER A, 100040 ARG A	0.26	39.4	-2.45	-0.61	27.69	83
    40	100040 ARG A	-0.03	45.91	-4.5	-0.42	52	83
    41	100040 ARG A, 100043 HIS A	0.9	47.06	-3.85	-0.08	51.8	87
    42	100040 ARG A, 100046 GLU A	1.48	50.65	-4	-0.78	50.95	80
    43	100040 ARG A, 100046 GLU A, 300018 ARG B	3.93	52.41	-4.17	-0.66	51.3	81
    44	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.04	56.47	-2	-0.04	38.51	86
    45	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	2.73	59.5	-0.98	-0.14	26.35	87
    46	100046 GLU A, 100064 ILE A, 100063 LYS A	2.84	60.4	0.2	-0.04	17.8	90
    47	100046 GLU A, 100064 ILE A, 100063 LYS A	3.02	64.82	-0.97	0.09	33.18	84
    48	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.06	65.31	-0.93	-0.18	25.3	92
    49	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.34	65.71	-1.1	-0.35	25.3	80
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.5	70.29	0.23	0.35	24.92	76
    51	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	5.32	71.06	-1.5	-0.4	21.26	76
    52	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	5.11	71.38	-2.4	-0.78	21.56	90
    53	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.6	71.57	-2.03	-0.87	14.58	96
    54	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.35	71.82	-2.4	-0.78	21.56	90
    55	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.81	72.9	-0.94	-0.32	11.61	84
    56	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.71	73.4	-1.08	-0.2	13.67	84
    57	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.59	75.08	-1.08	-0.27	25.25	79
    58	100063 LYS A, 100003 LEU B, 100001 ASP B	3.59	77.07	-1.2	-0.1	33.11	70
    59	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.71	78.05	-1.08	-0.27	25.25	79
    60	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.89	79	-0.98	-0.43	25.3	83
    61	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.84	79.18	-0.2	-0.37	13.72	82
    62	100003 LEU B, 300070 ASP B, 100001 ASP B	2.99	81.47	-0.03	-0.23	17.74	70
    63	100003 LEU B, 300070 ASP B	2.23	84.45	0.15	0.05	24.92	70
    64	100003 LEU B, 300070 ASP B, 100026 SER B	2.11	86.68	-0.17	-0.29	17.17	85
    65	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.36	88.68	-1.25	-0.32	25.88	85
    66	300070 ASP B, 100026 SER B, 300024 ARG B	3.23	90.32	-2.93	-0.81	34.46	95
    67	300070 ASP B, 300024 ARG B, 100026 SER B	3.6	91.2	-2.8	-0.75	35.03	84
    68	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.72	92.83	-2.28	-0.76	26.69	92
    69	300024 ARG B, 100026 SER B, 300069 THR B	4.22	94.53	-1.87	-0.66	19.01	95
    70	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.83	95.66	-1.5	-0.7	15.11	95
    71	100026 SER B, 300069 THR B, 300026 SER B	5.33	98.48	-0.5	-0.79	2.81	107
    72	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	5.26	99.52	-0.48	-0.79	2.95	107
    73	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.87	101.19	-0.46	-0.79	3.04	107
    74	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.69	101.35	-1.28	-0.92	2.99	100
    75	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.08	104.78	-1.35	-0.91	2.56	102
    76	300027 GLN B, 100027 GLN B, 300028 SER B	5.32	105.53	-1.57	-0.96	2.86	100
    77	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.62	106.61	-2.05	-0.99	3.03	95
    78	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.12	107.37	-2.05	-0.99	3.03	95
    79	200027 GLN B, 200028 SER B, 100028 SER B	6.21	107.91	-1.7	-1.01	2.29	106
    80	100027 GLN B, 300028 SER B, 100028 SER B	5.02	111.22	-1.7	-1.01	2.29	106
    81	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.72	111.39	-2.4	-0.87	14.72	100
    82	100027 GLN B, 100028 SER B, 100093 ARG B	3.86	111.82	-2.93	-0.83	19.07	94
    83	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.41	112.92	-2.4	-0.87	14.72	100
    84	100027 GLN B, 300028 SER B, 100093 ARG B	3.06	118.11	-2.93	-0.83	19.07	94
    85	300028 SER B, 100093 ARG B	3.44	118.91	-2.65	-0.7	26.84	100
    86	300028 SER B, 100093 ARG B, 100082 TYR C	3.57	120.06	-2.2	-0.09	18.43	83
    87	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.8	120.48	-2.78	-0.18	26.82	83
    88	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.87	121.54	-2.53	-0.35	14.7	83
    89	300028 SER B, 300093 ARG B, 300058 GLN C	3.85	121.77	-2.93	-0.83	19.07	94
    90	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.8	122.49	-2.53	-0.35	14.7	83
    91	100082 TYR C, 300093 ARG B, 300058 GLN C	3.8	123.54	-3.1	-0.14	19.05	72
    92	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.78	125.11	-2.43	-0.3	15.13	72
    93	300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C	3.78	125.48	-2.2	-0.78	15.57	83
    94	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.8	129.17	-2.43	-0.3	15.13	72
    95	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	4.73	130.23	-1.88	0.25	14.65	61
    96	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	5.1	131.05	-1.58	0.04	12.4	61
    97	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	5.48	131.49	-2.22	-0.27	22.47	72
    98	93 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.87	131.64	-2.4	0.12	22.12	66
    99	100093 ARG B, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	6.22	131.97	-2.4	0.12	22.12	66
    100	200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C, 100079 GLY C	6.73	132.29	-1.58	0.04	12.4	61
    101	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.65	133.57	-2.22	-0.27	22.47	72
    102	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.4	134.07	-2.3	-0.3	22.13	83
    103	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	4.14	137.1	-2.78	-0.18	26.82	83
    104	300093 ARG B, 300082 TYR C, 28 SER B	3.61	138.63	-2.2	-0.09	18.43	83
    105	300093 ARG B, 28 SER B	3.43	139.48	-2.65	-0.7	26.84	100
    106	300027 GLN B, 300093 ARG B, 28 SER B	3.17	143.97	-2.93	-0.83	19.07	94
    107	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	3.43	144.57	-2.3	-0.82	15.15	94
    108	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	3.59	144.89	-2.4	-0.87	14.72	100
    109	300028 SER B, 300027 GLN B, 300093 ARG B	3.77	145.28	-2.93	-0.83	19.07	94
    110	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.47	145.92	-2.4	-0.87	14.72	100
    111	300028 SER B, 300027 GLN B, 28 SER B	5.02	149.37	-1.7	-1.01	2.29	106
    112	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6.16	150.62	-2.05	-0.99	3.03	95
    113	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.94	151.3	-2.05	-0.99	3.03	95
    114	300027 GLN B, 27 GLN B, 28 SER B	5.67	152.06	-2.6	-1.06	2.91	95
    115	300026 SER B, 300027 GLN B, 28 SER B	5.36	152.81	-1.57	-0.96	2.86	100
    116	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.07	155.34	-1.35	-0.91	2.56	102
    117	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	4.45	155.82	-1.28	-0.92	2.99	100
    118	300026 SER B, 28 SER B, 69 THR B, 27 GLN B, 26 SER B	4.79	158.44	-0.46	-0.79	3.04	107
    119	300026 SER B, 69 THR B, 27 GLN B, 26 SER B	5.19	159.51	-0.48	-0.79	2.95	107
    120	300026 SER B, 69 THR B, 26 SER B	5.27	161.53	-0.5	-0.79	2.81	107
    121	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.85	162.69	-1.5	-0.7	15.11	95
    122	300026 SER B, 69 THR B, 24 ARG B	4.45	163.98	-1.87	-0.66	19.01	95
    123	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.87	165.52	-2.28	-0.76	26.69	92
    124	300026 SER B, 24 ARG B, 70 ASP B	3.59	166.38	-2.8	-0.75	35.03	84
    125	24 ARG B, 70 ASP B, 300026 SER B	3.19	168.58	-2.93	-0.81	34.46	95
    126	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.52	170.11	-1.25	-0.32	25.88	85
    127	70 ASP B, 300026 SER B, 300003 LEU B	2.1	172.93	-0.17	-0.29	17.17	85
    128	70 ASP B, 300003 LEU B	2.25	175.81	0.15	0.05	24.92	70
    129	70 ASP B, 300003 LEU B, 300001 ASP B	3.05	177.69	-0.03	-0.23	17.74	70
    130	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.85	177.82	-0.2	-0.37	13.72	82
    131	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.9	178.65	-0.98	-0.43	25.3	83
    132	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.88	178.9	-1.56	-0.42	30.14	81
    133	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.69	180.35	-1.08	-0.27	25.25	79
    134	300003 LEU B, 300001 ASP B, 300063 LYS A	3.58	181.74	-1.2	-0.1	33.11	70
    135	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.54	183.86	-1.08	-0.27	25.25	79
    136	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.66	184.29	-1.08	-0.2	13.67	84
    137	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	3.77	185.12	-0.94	-0.32	11.61	84
    138	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.34	185.26	-2.4	-0.78	21.56	90
    139	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.61	185.77	-2.03	-0.87	14.58	96
    140	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	5.16	186.65	-1.5	-0.4	21.26	76
    141	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	5.41	187.88	-1	-0.3	25.73	67
    142	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	5.6	191.11	0.23	0.35	24.92	76
    143	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	5.49	192.03	-1.1	-0.35	25.3	80
    144	300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B	5.21	192.89	-0.93	-0.18	25.3	92
    145	300063 LYS A, 300046 GLU A, 300064 ILE A	3.09	197.4	-0.97	0.09	33.18	84
    146	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	2.73	201.01	-0.98	-0.14	26.35	87
    147	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3	204.38	-2	-0.04	38.51	86
    148	300046 GLU A, 18 ARG B, 300040 ARG A	3.62	206.49	-4.17	-0.66	51.3	81
    149	300046 GLU A, 300064 ILE A, 300040 ARG A	2.27	207.7	-1.17	0.08	34.01	87
    150	300046 GLU A, 300040 ARG A	0.97	210.56	-4	-0.78	50.95	80
    151	300040 ARG A	-0.04	217.24	-4.5	-0.42	52	83
    152	300040 ARG A, 300088 SER A	0.26	217.89	-2.45	-0.61	27.69	83
    153	300040 ARG A, 300088 SER A, 300091 SER A	0.64	218.2	-1.77	-0.67	19.59	83
    154	300040 ARG A, 300088 SER A, 300041 PRO A, 300091 SER A	1.12	218.48	-1.83	-0.57	14.66	86
    155	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	1.66	219.33	-1.73	-0.53	15.09	70
    156	300040 ARG A, 300088 SER A, 300041 PRO A	2.81	221.46	-2.17	-0.44	18.99	70
    157	300040 ARG A, 300041 PRO A, 300088 SER A	4.17	223.65	-2.3	-0.49	18.42	86
    158	300041 PRO A, 300088 SER A	4.95	225.16	-1.2	-0.53	1.63	87
    159	300041 PRO A, 300091 SER A, 300088 SER A	4.83	225.69	-1.07	-0.68	1.64	97
    160	300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A	4.69	226.15	0.15	-0.22	1.26	86
    161	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.39	226.74	0.02	0.3	1.25	69
    162	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.25	226.93	0.23	0.08	1.27	84
    163	300091 SER A, 300088 SER A, 300180 TYR A	4.14	227.03	-0.97	-0.28	1.65	94
    164	300091 SER A, 300088 SER A	4.07	227.19	-0.8	-0.97	1.67	117
    165	300091 SER A, 300088 SER A, 300180 TYR A	4.03	227.65	-0.97	-0.28	1.65	94
    166	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.03	228.45	0.02	0.3	1.25	69
    167	300041 PRO A, 300091 SER A, 300175 LEU A, 300180 TYR A	4.07	229.49	0.02	0.3	1.25	69
    168	300041 PRO A, 300175 LEU A, 300180 TYR A	4.12	233.05	0.3	0.72	1.11	54
    169	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.5	233.25	0.13	0.34	1.68	54
    170	300041 PRO A, 300175 LEU A, 300180 TYR A	4.32	233.95	0.3	0.72	1.11	54
    171	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	3.83	234.74	0.13	0.34	1.68	54
    172	300041 PRO A, 300180 TYR A, 300173 ALA A	3.54	236.66	-1.1	0.07	2.19	54
    173	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.46	238.74	-1.7	-0.23	14.12	61
    174	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.33	241.16	-1.78	-0.53	14.11	64
    175	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.13	241.77	-2.55	-0.52	14.11	74
    176	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.02	242.12	-2.55	-0.52	14.11	74
    177	300153 GLU A, 300172 PRO A, 300041 ASN B	2.79	243.04	-2.87	-0.67	18.29	79
    178	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.51	246.35	-2.25	-0.7	14.56	79
    179	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.51	246.86	-1.95	-0.88	15.01	90
    180	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.53	247.18	-0.8	-0.47	12.03	78
    181	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.56	247.4	-0.8	-0.47	12.03	78
    182	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.62	248.33	-0.13	-0.31	2.57	79
    183	300041 ASN B, 300182 LEU A, 300171 PHE A	2.76	248.54	-0.03	-0.14	2.3	79
    184	300041 ASN B, 300182 LEU A, 300170 THR A	2.76	248.71	-0.13	-0.13	1.72	88
    185	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.72	249.9	-0.2	-0.3	2.14	88
    186	300041 ASN B, 300170 THR A, 300155 VAL A	2.77	253.92	-1.53	-0.78	2.81	105
    187	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.04	254.15	-1.33	-0.78	2.52	106
    188	300041 ASN B, 300156 THR A, 300157 VAL A	3.1	254.29	-1.53	-0.78	2.81	105
    189	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.2	254.62	-1.33	-0.78	2.52	106
    190	300041 ASN B, 300170 THR A, 300155 VAL A	3.26	254.8	-1.53	-0.78	2.81	105
    191	300041 ASN B, 300170 THR A, 300157 VAL A	3.28	255.03	-1.53	-0.78	2.81	105
    192	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.24	255.56	-1.33	-0.78	2.52	106
    193	300041 ASN B, 300170 THR A, 300157 VAL A	3.4	258.4	-1.53	-0.78	2.81	105
    194	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B	3.95	259.49	-1.25	-0.79	2.95	105
    195	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.26	259.71	0.68	-0.31	2.14	102
    196	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.51	259.85	-1.16	-0.72	12.26	89
    197	300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B	4	260.54	-0.2	-0.21	13.67	92
    198	300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A	3.24	261.42	-0.13	-0.22	14.1	85
    199	300168 VAL A, 300169 LYS B, 300165 SER A	1.75	265.6	-0.03	-0.03	17.67	85
    200	300168 VAL A, 300169 LYS B, 300165 SER A	1.24	267.31	-1.57	-0.67	18.75	72
    201	300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A	1.26	268.77	-1.28	-0.7	14.91	72
    202	300168 VAL A, 300169 LYS B, 300167 GLY A	1.72	269.61	-1.57	-0.67	18.75	72
    203	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.87	269.79	-1.98	-0.44	26.97	81
    204	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.92	269.97	-1.98	-0.44	26.97	81
    205	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.98	270.08	-1.98	-0.44	26.97	81
    206	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.87	270.55	-1.98	-0.44	26.97	81
    207	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.77	271.3	-2.75	-0.5	38.55	83
    208	300169 LYS B, 300167 GLY A, 300167 ASP B	1.69	272.75	-2.6	-0.75	34.19	79
    209	300169 LYS B, 300167 GLY A	1.68	273.51	-2.15	-0.61	26.44	72
    210	300169 LYS B, 300167 GLY A, 300166 SER A	1.69	274.54	-1.57	-0.67	18.75	72
    211	300169 LYS B, 300167 GLY A, 300166 SER A	1.79	278.2	-1.7	-0.73	18.18	94
    212	300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B	3	279.53	-2.15	-0.81	26.06	91
    213	300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B	4.21	280.01	-1.28	-0.9	14.53	101
    214	300167 GLY A, 300166 SER A, 300170 ASP B	4.4	280.92	-1.57	-0.94	18.25	101
    215	300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A	4.75	281.97	-0.7	-0.45	14.05	98
    216	300167 GLY A, 300170 ASP B, 300140 MET A	4.13	283.62	-0.67	-0.28	18.17	89
    217	300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B	3.96	284.91	-1.38	-0.4	14.47	94
    218	300170 ASP B, 300140 MET A, 300138 ASN B	4	286.32	-1.7	-0.27	18.17	94
    219	300140 MET A, 300138 ASN B, 300187 THR A	3.58	288.37	-0.77	-0.18	2.16	101
    220	300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B	3.14	289.92	-0.75	-0.33	2.03	102
    221	300140 MET A, 300187 THR A, 300114 THR B	2.94	291.86	0.17	-0.18	1.58	102
    222	300140 MET A, 300114 THR B	2.81	293.28	0.6	0.12	1.55	100
    223	300140 MET A, 300114 THR B, 300138 ASN A	2.76	293.63	-0.77	-0.18	2.16	101
    224	300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A	2.61	294.67	-0.78	-0.38	2.04	105
    225	300140 MET A, 300114 THR B, 300138 ASN A	2.56	297.72	-0.77	-0.18	2.16	101
    226	300114 THR B, 300138 ASN A	2.6	300.92	-2.1	-0.77	2.52	105
    227	300114 THR B, 300138 ASN A, 300113 PRO B, 300207 LYS B	2.74	301.44	-2.13	-0.69	14.48	94
    228	300114 THR B, 300138 ASN A, 300207 LYS B	2.79	303.3	-2.7	-0.65	18.18	94
    229	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B	2.87	304.37	-2.13	-0.69	14.48	94
    230	300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A	2.89	305.25	-2.13	-0.69	14.48	94
    231	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.8	306.25	-1.78	-0.71	12.26	94
    232	300114 THR B, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.63	306.71	-1.35	-0.7	14.48	89
    233	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.57	307.03	-1.78	-0.71	12.26	94
    234	300114 THR B, 300207 LYS B, 300115 VAL B, 300136 GLN A, 300116 SER B	2.52	307.38	-1.24	-0.75	11.92	98
    235	300114 THR B, 300115 VAL B, 300136 GLN A, 300116 SER B, 300140 MET A	2.4	308.93	-0.54	-0.83	2.69	112
    236	300207 LYS B, 300115 VAL B, 300136 GLN A, 300116 SER B	2.37	309.61	-1.38	-0.75	14.48	94
    237	300115 VAL B, 300136 GLN A, 300116 SER B	2.33	310.8	-0.53	-0.86	2.81	117
    238	300115 VAL B, 300136 GLN A, 300116 SER B, 300135 ALA A	2.3	311.5	0.05	-0.64	2.11	108
    239	300115 VAL B, 300116 SER B, 300135 ALA A	2.28	312.68	0.2	-0.58	1.68	108
    240	300116 SER B, 300135 ALA A, 300117 ILE B	1.88	315.05	0.2	-0.58	1.68	108
    241	300135 ALA A, 300117 ILE B, 300116 SER B	1.8	315.55	0.33	-0.53	2.25	100
    242	300135 ALA A, 300116 SER B, 300117 ILE B	1.67	316.54	1.97	0.34	1.17	101
    243	300135 ALA A, 300117 ILE B	1.61	317.68	3.15	0.92	0.07	101
    244	300135 ALA A, 300117 ILE B, 300208 SER B	1.61	318.25	1.97	0.34	1.17	101
    245	300135 ALA A, 300117 ILE B, 300208 SER B, 300132 GLY A	1.63	319.15	1.38	0.06	1.72	101
    246	300135 ALA A, 300117 ILE B, 300132 GLY A	1.7	319.64	1.97	0.34	1.17	101
    247	300117 ILE B, 300132 GLY A, 300209 PHE B	1.67	320.95	2.3	0.79	1.29	77
    248	300117 ILE B, 300132 GLY A, 300209 PHE B, 300119 PRO B	1.48	321.42	0.1	-0.09	2.17	54
    249	300117 ILE B, 300132 GLY A, 300119 PRO B	1.44	321.57	-0.8	-0.56	2.78	58
    250	300117 ILE B, 300132 GLY A, 300119 PRO B	1.42	321.79	0.83	0.31	1.7	80
    251	300117 ILE B, 300132 GLY A, 300119 PRO B	1.46	322.26	-0.8	-0.56	2.78	58
    252	300132 GLY A, 300209 PHE B, 300119 PRO B	1.52	326.46	0.27	0.15	1.77	54
    253	300132 GLY A, 300209 PHE B, 300119 PRO B, 300133 SER A, 300210 ASN B	2.01	327.17	0	-0.23	2.41	54
    254	300132 GLY A, 300119 PRO B, 300133 SER A, 300210 ASN B, 300218 ARG A	2.25	328.32	-1.46	-0.58	12.74	70
    255	300119 PRO B, 300210 ASN B, 300218 ARG A	2.02	329.88	-2.17	-0.44	18.99	70
    256	300209 PHE B, 300119 PRO B, 300210 ASN B, 300218 ARG A	2	330.39	-0.93	0.01	14.33	64
    257	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B	1.99	331	-1.73	-0.53	15.09	70
    258	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B, 300186 TYR B	2.07	331.36	-1.64	-0.2	12.39	63
    259	300119 PRO B, 300218 ARG A, 300211 ARG B, 300186 TYR B	2.15	333.06	-1.95	-0.05	14.64	63
    260	300218 ARG A, 300186 TYR B, 300211 ARG B	2.3	334.64	-3.43	0.09	35.2	72
    261	300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B	2.41	334.64	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

30. show pore | cavity 1 | profile | lining residues
    

    Unique lining residues set - all

    100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A, 100088 SER A, 100040 ARG A, 100091 SER A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100001 ASP B, 100026 SER B, 300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B, 27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200028 SER B, 100027 GLN B, 200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 200001 ASP B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200002 ILE B, 200098 PHE B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A, 200170 THR A, 200155 VAL A, 200156 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A, 200169 HIS A, 200167 ASP B, 200166 SER A, 200166 SER A, 200170 ASP B, 200169 LYS B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A, 200113 PRO B, 200207 LYS B, 200115 VAL B, 200136 GLN A, 200116 SER B, 200140 MET A, 200135 ALA A, 200117 ILE B, 200116 SER B, 200117 ILE B, 200208 SER B, 200132 GLY A, 200209 PHE B, 200119 PRO B, 200133 SER A, 200210 ASN B, 200218 ARG A, 200211 ARG B, 200186 TYR B, 200211 ARG B, 200125 LEU B

    Unique lining residues set - sidechains

    100156 THR A, 100170 THR A, 100041 ASN B, 100182 LEU A, 100153 GLU A, 100172 PRO A, 100041 PRO A, 100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A, 100040 ARG A, 100043 HIS A, 100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A, 300020 SER B, 100003 LEU B, 100061 ASN A, 100097 THR B, 100001 ASP B, 300072 THR B, 300070 ASP B, 100026 SER B, 300024 ARG B, 300069 THR B, 100027 GLN B, 300028 SER B, 300027 GLN B, 27 GLN B, 200027 GLN B, 200028 SER B, 100028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 93 ARG B, 82 TYR C, 300082 TYR C, 200093 ARG B, 200082 TYR C, 100058 GLN C, 28 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A, 200097 THR B, 200061 ASN A, 200046 GLU A, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A, 200153 GLU A, 200172 PRO A, 200041 ASN B, 200182 LEU A, 200170 THR A, 200156 THR A, 200168 VAL A, 200169 LYS B, 200169 HIS A, 200167 ASP B, 200166 SER A, 200170 ASP B, 200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B, 200138 ASN A, 200139 SER A, 200207 LYS B, 200116 SER B, 200135 ALA A, 200117 ILE B, 200209 PHE B, 200119 PRO B, 200218 ARG A, 200186 TYR B, 200211 ARG B, 200125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 6 (16-10)
    Hydropathy: -1.3
    Hydrophobicity: -0.42
    Polarity: 13.77
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.27	0.28	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.28	0.42	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.26	0.62	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.24	0.78	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.22	0.96	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.08	1.41	-1.53	-0.78	2.81	105
    7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	3.02	2.03	-1.14	-0.78	2.69	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.79	5.48	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.71	6.57	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.74	6.96	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.17	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.61	7.93	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.56	8.48	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.54	9.02	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.53	9.68	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.53	12.8	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	2.81	13.53	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.02	13.83	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.13	14.52	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.32	17.09	-1.78	-0.53	14.11	64
    21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.5	18.7	-1.7	-0.23	14.12	61
    22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.54	21	-1.1	0.07	2.19	54
    23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	3.86	21.43	0.13	0.34	1.68	54
    24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.31	22.02	0.3	0.72	1.11	54
    25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.5	22.42	0.13	0.34	1.68	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.13	26.93	0.3	0.72	1.11	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.07	27.68	-0.06	0.08	1.67	69
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.04	28.09	0.02	0.3	1.25	69
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.03	28.22	-0.97	-0.28	1.65	94
    30	100091 SER A, 100088 SER A	4.07	28.33	-0.8	-0.97	1.67	117
    31	100180 TYR A, 100091 SER A, 100088 SER A	4.15	28.53	-0.97	-0.28	1.65	94
    32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.26	28.79	0.23	0.08	1.27	84
    33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.41	29.15	0.02	0.3	1.25	69
    34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.56	30.15	0.15	-0.22	1.26	86
    35	100041 PRO A, 100091 SER A, 100088 SER A	4.86	30.71	-1.07	-0.68	1.64	97
    36	100041 PRO A, 100088 SER A	4.98	31.64	-1.2	-0.53	1.63	87
    37	100041 PRO A, 100088 SER A, 100040 ARG A	4.43	33.9	-2.3	-0.49	18.42	86
    38	100041 PRO A, 100088 SER A, 100040 ARG A	2.77	36.46	-2.17	-0.44	18.99	70
    39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.22	36.84	-1.73	-0.53	15.09	70
    40	100088 SER A, 100040 ARG A, 100091 SER A	0.67	38.09	-1.77	-0.67	19.59	83
    41	100088 SER A, 100040 ARG A	0.3	39.21	-2.45	-0.61	27.69	83
    42	100040 ARG A	-0.03	45.73	-4.5	-0.42	52	83
    43	100040 ARG A, 100043 HIS A	0.83	46.91	-3.85	-0.08	51.8	87
    44	100040 ARG A, 100046 GLU A	1.39	50.55	-4	-0.78	50.95	80
    45	100040 ARG A, 100046 GLU A, 300018 ARG B	3.85	52.95	-4.17	-0.66	51.3	81
    46	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.07	56.37	-2	-0.04	38.51	86
    47	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	2.73	59.35	-0.98	-0.14	26.35	87
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	2.82	60.25	0.2	-0.04	17.8	90
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	2.98	64.69	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5	65.25	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.29	66.4	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	5.52	70.09	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	5.36	70.94	-1.5	-0.4	21.26	76
    54	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	5.15	71.34	-2.4	-0.78	21.56	90
    55	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.65	71.55	-2.03	-0.87	14.58	96
    56	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.4	71.78	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.84	72.83	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.73	73.32	-1.08	-0.2	13.67	84
    59	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.59	75.65	-1.08	-0.27	25.25	79
    60	100063 LYS A, 100003 LEU B, 100001 ASP B	3.61	76.97	-1.2	-0.1	33.11	70
    61	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.7	78.02	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.88	78.25	-1.56	-0.42	30.14	81
    63	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.91	78.97	-0.98	-0.43	25.3	83
    64	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.86	79.16	-0.2	-0.37	13.72	82
    65	100003 LEU B, 300070 ASP B, 100001 ASP B	3.02	81.36	-0.03	-0.23	17.74	70
    66	100003 LEU B, 300070 ASP B	2.26	84.33	0.15	0.05	24.92	70
    67	100003 LEU B, 300070 ASP B, 100026 SER B	2.11	87.11	-0.17	-0.29	17.17	85
    68	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.51	88.57	-1.25	-0.32	25.88	85
    69	300070 ASP B, 100026 SER B, 300024 ARG B	3.17	90.33	-2.93	-0.81	34.46	95
    70	300070 ASP B, 300024 ARG B, 100026 SER B	3.6	91.51	-2.8	-0.75	35.03	84
    71	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.82	93.34	-2.28	-0.76	26.69	92
    72	300024 ARG B, 100026 SER B, 300069 THR B	4.37	94.45	-1.87	-0.66	19.01	95
    73	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.78	95.53	-1.5	-0.7	15.11	95
    74	100026 SER B, 300069 THR B, 300026 SER B	5.34	98.2	-0.5	-0.79	2.81	107
    75	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	5.29	99.26	-0.48	-0.79	2.95	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.92	101.16	-0.46	-0.79	3.04	107
    77	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.56	101.52	-1.28	-0.92	2.99	100
    78	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.08	104.57	-1.35	-0.91	2.56	102
    79	100026 SER B, 100027 GLN B, 300028 SER B	5.23	105.33	-1.57	-0.96	2.86	100
    80	100027 GLN B, 300028 SER B, 300027 GLN B	5.54	106.02	-2.6	-1.06	2.91	95
    81	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	5.82	106.52	-2.05	-0.99	3.03	95
    82	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.07	107.75	-2.05	-0.99	3.03	95
    83	100027 GLN B, 300028 SER B, 100028 SER B	5.11	111.16	-1.7	-1.01	2.29	106
    84	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.53	111.5	-2.4	-0.87	14.72	100
    85	100027 GLN B, 100028 SER B, 100093 ARG B	3.75	112.06	-2.93	-0.83	19.07	94
    86	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.53	112.65	-2.4	-0.87	14.72	100
    87	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.35	113.43	-2.3	-0.82	15.15	94
    88	100027 GLN B, 300028 SER B, 100093 ARG B	3.04	117.98	-2.93	-0.83	19.07	94
    89	300028 SER B, 100093 ARG B	3.34	118.81	-2.65	-0.7	26.84	100
    90	300028 SER B, 100093 ARG B, 100082 TYR C	3.54	120.08	-2.2	-0.09	18.43	83
    91	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.1	123.05	-2.78	-0.18	26.82	83
    92	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.42	123.97	-2.3	-0.3	22.13	83
    93	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.86	124.66	-2.22	-0.27	22.47	72
    94	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.82	124.91	-1.58	0.04	12.4	61
    95	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.3	125.14	-2.4	0.12	22.12	66
    96	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	5.93	125.56	-2.4	0.12	22.12	66
    97	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	5.52	126.34	-2.22	-0.27	22.47	72
    98	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	4.69	128.53	-1.58	0.04	12.4	61
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.69	131.51	-2.43	-0.3	15.13	72
    100	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.67	132.31	-2.2	-0.78	15.57	83
    101	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.74	133.31	-2.43	-0.3	15.13	72
    102	100093 ARG B, 200082 TYR C, 100058 GLN C	3.78	134.44	-3.1	-0.14	19.05	72
    103	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.76	134.99	-2.53	-0.35	14.7	83
    104	100028 SER B, 100093 ARG B, 100058 GLN C	3.79	135.21	-2.93	-0.83	19.07	94
    105	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.88	136.54	-2.53	-0.35	14.7	83
    106	100028 SER B, 100093 ARG B, 200093 ARG B, 200082 TYR C	3.85	137.03	-2.78	-0.18	26.82	83
    107	100028 SER B, 200093 ARG B, 200082 TYR C	3.68	138.44	-2.2	-0.09	18.43	83
    108	100028 SER B, 200093 ARG B	3.56	139.29	-2.65	-0.7	26.84	100
    109	200027 GLN B, 100028 SER B, 200093 ARG B	3.19	144.35	-2.93	-0.83	19.07	94
    110	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	3.44	144.99	-2.4	-0.87	14.72	100
    111	200027 GLN B, 200028 SER B, 200093 ARG B	3.83	145.4	-2.93	-0.83	19.07	94
    112	200027 GLN B, 200028 SER B, 100028 SER B, 200093 ARG B	4.61	145.73	-2.4	-0.87	14.72	100
    113	200027 GLN B, 200028 SER B, 100028 SER B	4.9	149.58	-1.7	-1.01	2.29	106
    114	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	6.23	150.4	-2.05	-0.99	3.03	95
    115	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	5.78	151.75	-2.05	-0.99	3.03	95
    116	200027 GLN B, 100028 SER B, 100027 GLN B	5.49	152.52	-1.57	-0.96	2.86	100
    117	200027 GLN B, 100028 SER B, 200026 SER B	5.17	153.2	-1.57	-0.96	2.86	100
    118	200027 GLN B, 100028 SER B, 200026 SER B, 100069 THR B	4.08	155.43	-1.35	-0.91	2.56	102
    119	200027 GLN B, 100028 SER B, 100027 GLN B, 200026 SER B	4.55	155.66	-1.28	-0.92	2.99	100
    120	100026 SER B, 100028 SER B, 100027 GLN B, 200026 SER B, 100069 THR B	4.72	157.98	-0.46	-0.79	3.04	107
    121	100026 SER B, 100027 GLN B, 200026 SER B, 100069 THR B	5.15	159.06	-0.48	-0.79	2.95	107
    122	100026 SER B, 200026 SER B, 100069 THR B	5.24	161.68	-0.5	-0.79	2.81	107
    123	100026 SER B, 200026 SER B, 100069 THR B, 100024 ARG B	4.93	162.46	-1.5	-0.7	15.11	95
    124	200026 SER B, 100069 THR B, 100024 ARG B	4.33	164.36	-1.87	-0.66	19.01	95
    125	200026 SER B, 100069 THR B, 100024 ARG B, 100070 ASP B	3.78	165.69	-2.28	-0.76	26.69	92
    126	200026 SER B, 100024 ARG B, 100070 ASP B	3.59	166.36	-2.8	-0.75	35.03	84
    127	100024 ARG B, 100070 ASP B, 200026 SER B	3.29	168.36	-2.93	-0.81	34.46	95
    128	100024 ARG B, 100070 ASP B, 200026 SER B, 200003 LEU B	2.42	170.42	-1.25	-0.32	25.88	85
    129	100070 ASP B, 200026 SER B, 200003 LEU B	2.1	173.26	-0.17	-0.29	17.17	85
    130	100070 ASP B, 200003 LEU B	2.32	176.05	0.15	0.05	24.92	70
    131	100070 ASP B, 200003 LEU B, 200001 ASP B	3.12	177.77	-0.03	-0.23	17.74	70
    132	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B	3.88	178.78	-0.98	-0.43	25.3	83
    133	100070 ASP B, 200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.85	179.05	-1.56	-0.42	30.14	81
    134	200003 LEU B, 100072 THR B, 200001 ASP B, 200063 LYS A	3.72	180.03	-1.08	-0.27	25.25	79
    135	200003 LEU B, 200001 ASP B, 200063 LYS A	3.57	182.06	-1.2	-0.1	33.11	70
    136	200003 LEU B, 200001 ASP B, 200063 LYS A, 200097 THR B	3.54	183.62	-1.08	-0.27	25.25	79
    137	200003 LEU B, 200063 LYS A, 200097 THR B, 200002 ILE B	3.62	184.09	-0.3	-0.21	13.67	77
    138	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B	3.71	184.49	-0.3	-0.21	13.67	77
    139	200003 LEU B, 200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A	3.83	185.02	-0.94	-0.32	11.61	84
    140	200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.21	185.22	-2.4	-0.78	21.56	90
    141	200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	4.47	185.5	-2.03	-0.87	14.58	96
    142	200063 LYS A, 200097 THR B, 200098 PHE B, 200061 ASN A, 200046 GLU A	5.02	186.14	-2.4	-0.78	21.56	90
    143	200003 LEU B, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200046 GLU A	5.28	187.21	-1.5	-0.4	21.26	76
    144	200003 LEU B, 200063 LYS A, 200098 PHE B, 200046 GLU A	5.5	188.51	-1	-0.3	25.73	67
    145	200003 LEU B, 200063 LYS A, 200046 GLU A, 200064 ILE A	5.67	191.3	0.23	0.35	24.92	76
    146	200003 LEU B, 200063 LYS A, 200046 GLU A, 100020 SER B	5.6	191.7	-1.1	-0.35	25.3	80
    147	200063 LYS A, 200046 GLU A, 200064 ILE A, 100020 SER B	5.37	192.44	-0.93	-0.18	25.3	92
    148	200063 LYS A, 200046 GLU A, 200064 ILE A	3.23	196.93	-0.97	0.09	33.18	84
    149	200046 GLU A, 200064 ILE A, 200063 LYS A	2.99	197.84	0.2	-0.04	17.8	90
    150	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	2.74	200.69	-0.98	-0.14	26.35	87
    151	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	2.91	204.04	-2	-0.04	38.51	86
    152	200046 GLU A, 100018 ARG B, 200040 ARG A	3.34	206.69	-4.17	-0.66	51.3	81
    153	200046 GLU A, 200064 ILE A, 200040 ARG A	2.67	207.25	-1.17	0.08	34.01	87
    154	200046 GLU A, 200040 ARG A	1.32	209.58	-4	-0.78	50.95	80
    155	200040 ARG A	-0.04	216.64	-4.5	-0.42	52	83
    156	200040 ARG A, 200088 SER A	0.11	217.59	-2.45	-0.61	27.69	83
    157	200040 ARG A, 200088 SER A, 200091 SER A	0.41	218.07	-1.77	-0.67	19.59	83
    158	200040 ARG A, 200088 SER A, 200091 SER A	0.83	218.33	-1.9	-0.73	19.02	100
    159	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	1.34	218.65	-1.83	-0.57	14.66	86
    160	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	1.9	219.6	-1.73	-0.53	15.09	70
    161	200040 ARG A, 200088 SER A, 200041 PRO A	3.03	221.78	-2.17	-0.44	18.99	70
    162	200040 ARG A, 200041 PRO A, 200088 SER A	4.3	223.84	-2.3	-0.49	18.42	86
    163	200041 PRO A, 200088 SER A	4.9	225.4	-1.2	-0.53	1.63	87
    164	200091 SER A, 200041 PRO A, 200088 SER A	4.77	225.91	-1.07	-0.68	1.64	97
    165	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.63	226.32	0.15	-0.22	1.26	86
    166	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.48	226.61	0.02	0.3	1.25	69
    167	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.33	226.84	0.23	0.08	1.27	84
    168	200091 SER A, 200088 SER A, 200180 TYR A	4.11	227.08	-0.97	-0.28	1.65	94
    169	200091 SER A, 200088 SER A	4.05	227.34	-0.8	-0.97	1.67	117
    170	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.03	227.94	0.23	0.08	1.27	84
    171	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.04	228.85	-0.06	0.08	1.67	69
    172	200041 PRO A, 200175 LEU A, 200180 TYR A	4.08	232.98	0.3	0.72	1.11	54
    173	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.46	233.32	0.13	0.34	1.68	54
    174	200041 PRO A, 200175 LEU A, 200180 TYR A	4.28	234	0.3	0.72	1.11	54
    175	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	3.79	234.96	0.13	0.34	1.68	54
    176	200041 PRO A, 200180 TYR A, 200173 ALA A	3.52	236.91	-1.1	0.07	2.19	54
    177	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.46	238.93	-1.7	-0.23	14.12	61
    178	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.38	240.95	-1.78	-0.53	14.11	64
    179	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.2	241.59	-2.55	-0.52	14.11	74
    180	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.97	242.27	-2.55	-0.52	14.11	74
    181	200153 GLU A, 200172 PRO A, 200041 ASN B	2.86	242.72	-2.87	-0.67	18.29	79
    182	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.52	245.95	-2.25	-0.7	14.56	79
    183	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.51	247.01	-1.95	-0.88	15.01	90
    184	200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.54	247.38	-0.8	-0.47	12.03	78
    185	200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.6	248.2	-0.13	-0.31	2.57	79
    186	200041 ASN B, 200171 PHE A, 200182 LEU A	2.76	248.62	-0.03	-0.14	2.3	79
    187	200041 ASN B, 200182 LEU A, 200170 THR A	2.75	248.77	-0.13	-0.13	1.72	88
    188	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.72	250.15	-0.2	-0.3	2.14	88
    189	200041 ASN B, 200170 THR A, 200155 VAL A	2.78	254.04	-1.53	-0.78	2.81	105
    190	200041 ASN B, 200156 THR A, 200157 VAL A	3.06	254.4	-1.53	-0.78	2.81	105
    191	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.21	254.58	-1.33	-0.78	2.52	106
    192	200041 ASN B, 200170 THR A, 200157 VAL A	3.25	254.71	-1.53	-0.78	2.81	105
    193	200041 ASN B, 200170 THR A, 200155 VAL A	3.27	254.88	-1.53	-0.78	2.81	105
    194	200041 ASN B, 200170 THR A, 200157 VAL A	3.29	255.04	-1.53	-0.78	2.81	105
    195	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.24	255.49	-1.33	-0.78	2.52	106
    196	200041 ASN B, 200170 THR A, 200157 VAL A	3.36	258.57	-1.53	-0.78	2.81	105
    197	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B	3.97	259.43	-1.25	-0.79	2.95	105
    198	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.2	259.58	-1.08	-0.79	3.04	105
    199	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.28	259.74	0.68	-0.31	2.14	102
    200	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.45	259.88	-1.16	-0.72	12.26	89
    201	200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.89	259.92	-0.13	-0.22	14.1	85
    202	200170 THR A, 200157 VAL A, 200168 VAL A, 200169 LYS B	3.92	260.66	-0.2	-0.21	13.67	92
    203	200157 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A	3.54	261.02	-0.13	-0.22	14.1	85
    204	200168 VAL A, 200169 LYS B, 200165 SER A	1.68	265.89	-0.03	-0.03	17.67	85
    205	200168 VAL A, 200169 LYS B, 200165 SER A	1.24	267.39	-1.57	-0.67	18.75	72
    206	200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A	1.28	268.44	-1.28	-0.7	14.91	72
    207	200168 VAL A, 200169 LYS B, 200167 GLY A	1.65	269.73	-1.57	-0.67	18.75	72
    208	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.88	270.03	-1.98	-0.44	26.97	81
    209	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.99	270.05	-1.98	-0.44	26.97	81
    210	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.9	270.48	-1.98	-0.44	26.97	81
    211	200168 VAL A, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.86	270.64	-1.88	-0.6	27.02	88
    212	200169 LYS B, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.76	271.48	-2.75	-0.5	38.55	83
    213	200169 LYS B, 200167 GLY A, 200167 ASP B	1.69	272.96	-2.6	-0.75	34.19	79
    214	200169 LYS B, 200167 GLY A	1.68	273.7	-2.15	-0.61	26.44	72
    215	200169 LYS B, 200167 GLY A, 200166 SER A	1.7	274.65	-1.57	-0.67	18.75	72
    216	200169 LYS B, 200167 GLY A, 200166 SER A	1.8	278.34	-1.7	-0.73	18.18	94
    217	200169 LYS B, 200167 GLY A, 200166 SER A, 200170 ASP B	3.03	279.67	-2.15	-0.81	26.06	91
    218	200167 GLY A, 200166 SER A, 200170 ASP B, 200169 LYS B	4.25	280.16	-1.28	-0.9	14.53	101
    219	200167 GLY A, 200166 SER A, 200170 ASP B	4.43	281.04	-1.57	-0.94	18.25	101
    220	200167 GLY A, 200166 SER A, 200170 ASP B, 200140 MET A	4.77	282.06	-0.7	-0.45	14.05	98
    221	200167 GLY A, 200170 ASP B, 200140 MET A	4.11	283.75	-0.67	-0.28	18.17	89
    222	200167 GLY A, 200170 ASP B, 200140 MET A, 200138 ASN B	3.96	285.02	-1.38	-0.4	14.47	94
    223	200170 ASP B, 200140 MET A, 200138 ASN B	4.01	286.41	-1.7	-0.27	18.17	94
    224	200140 MET A, 200138 ASN B, 200187 THR A	3.67	288.15	-0.77	-0.18	2.16	101
    225	200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B	3.13	290.04	-0.75	-0.33	2.03	102
    226	200140 MET A, 200187 THR A, 200114 THR B	2.93	292.03	0.17	-0.18	1.58	102
    227	200140 MET A, 200114 THR B	2.87	292.81	0.6	0.12	1.55	100
    228	200140 MET A, 200114 THR B, 200138 ASN A	2.81	293.4	-0.77	-0.18	2.16	101
    229	200140 MET A, 200114 THR B, 200138 ASN A, 200139 SER A	2.61	294.78	-0.78	-0.38	2.04	105
    230	200140 MET A, 200114 THR B, 200138 ASN A	2.56	297.96	-0.77	-0.18	2.16	101
    231	200114 THR B, 200138 ASN A	2.6	301.04	-2.1	-0.77	2.52	105
    232	200114 THR B, 200138 ASN A, 200113 PRO B, 200207 LYS B	2.74	301.59	-2.13	-0.69	14.48	94
    233	200114 THR B, 200138 ASN A, 200207 LYS B	2.79	303.49	-2.7	-0.65	18.18	94
    234	200114 THR B, 200138 ASN A, 200207 LYS B, 200115 VAL B	2.87	304.55	-2.13	-0.69	14.48	94
    235	200114 THR B, 200138 ASN A, 200207 LYS B, 200136 GLN A	2.89	305.39	-2.13	-0.69	14.48	94
    236	200114 THR B, 200138 ASN A, 200207 LYS B, 200115 VAL B, 200136 GLN A	2.79	306.32	-1.78	-0.71	12.26	94
    237	200114 THR B, 200207 LYS B, 200115 VAL B, 200136 GLN A	2.62	306.81	-1.35	-0.7	14.48	89
    238	200114 THR B, 200138 ASN A, 200207 LYS B, 200115 VAL B, 200136 GLN A	2.56	307.13	-1.78	-0.71	12.26	94
    239	200114 THR B, 200138 ASN A, 200115 VAL B, 200136 GLN A, 200116 SER B	2.51	307.48	-1.16	-0.82	2.69	109
    240	200114 THR B, 200115 VAL B, 200136 GLN A, 200116 SER B, 200140 MET A	2.4	309.06	-0.54	-0.83	2.69	112
    241	200207 LYS B, 200115 VAL B, 200136 GLN A, 200116 SER B	2.37	309.74	-1.38	-0.75	14.48	94
    242	200115 VAL B, 200136 GLN A, 200116 SER B	2.33	310.91	-0.53	-0.86	2.81	117
    243	200115 VAL B, 200136 GLN A, 200116 SER B, 200135 ALA A	2.3	311.56	0.05	-0.64	2.11	108
    244	200115 VAL B, 200116 SER B, 200135 ALA A	2.28	312.76	0.2	-0.58	1.68	108
    245	200116 SER B, 200135 ALA A, 200117 ILE B	1.88	315.15	0.2	-0.58	1.68	108
    246	200135 ALA A, 200117 ILE B, 200116 SER B	1.8	315.64	0.33	-0.53	2.25	100
    247	200135 ALA A, 200116 SER B, 200117 ILE B	1.67	316.64	1.97	0.34	1.17	101
    248	200135 ALA A, 200117 ILE B	1.6	317.78	3.15	0.92	0.07	101
    249	200135 ALA A, 200117 ILE B, 200208 SER B	1.61	318.35	1.97	0.34	1.17	101
    250	200135 ALA A, 200117 ILE B, 200208 SER B, 200132 GLY A	1.63	319.23	1.38	0.06	1.72	101
    251	200135 ALA A, 200117 ILE B, 200132 GLY A	1.7	319.71	1.97	0.34	1.17	101
    252	200117 ILE B, 200132 GLY A, 200209 PHE B	1.67	321.02	2.3	0.79	1.29	77
    253	200117 ILE B, 200132 GLY A, 200209 PHE B, 200119 PRO B	1.48	321.49	0.1	-0.09	2.17	54
    254	200117 ILE B, 200132 GLY A, 200119 PRO B	1.44	321.64	-0.8	-0.56	2.78	58
    255	200117 ILE B, 200132 GLY A, 200119 PRO B	1.42	321.86	0.83	0.31	1.7	80
    256	200117 ILE B, 200132 GLY A, 200119 PRO B	1.46	322.34	-0.8	-0.56	2.78	58
    257	200132 GLY A, 200209 PHE B, 200119 PRO B	1.53	326.54	0.27	0.15	1.77	54
    258	200132 GLY A, 200209 PHE B, 200119 PRO B, 200133 SER A, 200210 ASN B	2.02	327.24	0	-0.23	2.41	54
    259	200132 GLY A, 200119 PRO B, 200133 SER A, 200210 ASN B, 200218 ARG A	2.26	328.38	-1.46	-0.58	12.74	70
    260	200119 PRO B, 200210 ASN B, 200218 ARG A	2.02	329.94	-2.17	-0.44	18.99	70
    261	200209 PHE B, 200119 PRO B, 200210 ASN B, 200218 ARG A	1.99	330.45	-0.93	0.01	14.33	64
    262	200119 PRO B, 200210 ASN B, 200218 ARG A, 200211 ARG B	1.99	331.05	-1.73	-0.53	15.09	70
    263	200119 PRO B, 200210 ASN B, 200218 ARG A, 200211 ARG B, 200186 TYR B	2.07	331.41	-1.64	-0.2	12.39	63
    264	200119 PRO B, 200218 ARG A, 200211 ARG B, 200186 TYR B	2.15	333.12	-1.95	-0.05	14.64	63
    265	200218 ARG A, 200186 TYR B, 200211 ARG B	2.3	334.7	-3.43	0.09	35.2	72
    266	200218 ARG A, 200186 TYR B, 200211 ARG B, 200125 LEU B	2.41	334.7	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

31. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.24
    Polarity: 1.4
    Mutability: 83
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.68	2.08	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.71	3.07	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.92	3.5	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	2.98	9.36	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.19	10.17	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	3.84	13.78	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.12	20.45	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.75	21.1	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.83	21.64	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.88	22.22	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.95	22.46	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.88	23.42	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.43	25.62	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.57	26.45	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.9	28.9	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.26	29.59	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.38	29.92	1.63	0.39	1.81	77
    18	100104 GLY C, 100103 PHE C, 200100 ILE C	3.29	30.11	2.3	0.79	1.29	77
    19	100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C	2.99	30.67	1.55	0.4	1.38	87
    20	100104 GLY C, 100103 PHE C, 100107 THR C	2.85	30.9	0.57	-0.07	1.8	79
    21	100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C	2.67	31.19	1.55	0.4	1.38	87
    22	100103 PHE C, 200100 ILE C, 100107 THR C	1.4	35.34	2.2	0.8	0.71	87
    23	200100 ILE C, 100107 THR C, 100103 PHE C	1.69	35.71	1.13	0.08	1.72	105
    24	200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C	1.84	36.39	0.75	-0.14	2.14	105
    25	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.97	36.67	0.46	-0.41	2.39	102
    26	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.88	37.38	0.68	-0.31	2.14	102
    27	100107 THR C, 200101 THR C, 100106 VAL C	1.84	37.88	1.03	-0.15	1.72	102
    28	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.75	38.46	1.73	0.18	1.33	86
    29	100106 VAL C, 100110 LEU C, 200101 THR C	1.12	45.82	2.43	0.5	0.64	86
    30	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	3.84	48.79	1.6	0.8	1.01	71
    31	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.19	49.65	0.48	0.33	1.39	84
    32	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.98	55.67	1.75	0.18	0.9	102
    33	100103 PHE C, 100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.92	56.06	1.96	0.41	0.79	92
    34	100103 PHE C, 100106 VAL C, 100033 THR C, 200097 VAL C	2.71	56.93	2.63	0.71	0.57	88
    35	100103 PHE C, 100033 THR C, 200097 VAL C	2.68	58.74	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

32. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C, 101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C, 100 ILE C, 104 GLY C, 103 PHE C, 300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C

    Unique lining residues set - sidechains

    97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C, 200107 THR C, 100 ILE C, 103 PHE C, 300100 ILE C, 107 THR C, 106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.24
    Polarity: 1.4
    Mutability: 83
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	97 VAL C, 200033 THR C, 200103 PHE C	2.68	2.08	2.1	0.57	0.71	85
    2	97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C	2.71	3.07	2.63	0.71	0.57	88
    3	97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C	2.92	3.5	1.96	0.41	0.79	92
    4	97 VAL C, 200033 THR C, 200106 VAL C, 101 THR C	2.98	9.36	1.75	0.18	0.9	102
    5	200033 THR C, 200106 VAL C, 101 THR C, 200026 TRP C	6.19	10.17	0.48	0.33	1.39	84
    6	200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C	3.84	13.78	1.6	0.8	1.01	71
    7	200106 VAL C, 101 THR C, 200110 LEU C	1.12	20.45	2.43	0.5	0.64	86
    8	200106 VAL C, 200110 LEU C, 101 THR C, 200107 THR C	1.75	21.1	1.73	0.18	1.33	86
    9	200106 VAL C, 101 THR C, 200107 THR C	1.83	21.64	1.03	-0.15	1.72	102
    10	200106 VAL C, 101 THR C, 200107 THR C, 200103 PHE C	1.88	22.22	0.68	-0.31	2.14	102
    11	200106 VAL C, 101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.95	22.46	0.46	-0.41	2.39	102
    12	101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.88	23.42	0.75	-0.14	2.14	105
    13	200107 THR C, 200103 PHE C, 100 ILE C	1.43	25.62	1.13	0.08	1.72	105
    14	200107 THR C, 200103 PHE C, 100 ILE C, 104 GLY C	1.57	26.45	0.75	-0.14	2.14	105
    15	200107 THR C, 100 ILE C, 104 GLY C	1.9	28.9	1.13	0.08	1.72	105
    16	100 ILE C, 104 GLY C, 103 PHE C	3.26	29.59	2.3	0.79	1.29	77
    17	100 ILE C, 104 GLY C, 103 PHE C, 300100 ILE C	3.38	29.92	1.63	0.39	1.81	77
    18	104 GLY C, 103 PHE C, 300100 ILE C	3.29	30.11	2.3	0.79	1.29	77
    19	104 GLY C, 103 PHE C, 300100 ILE C, 107 THR C	2.99	30.67	1.55	0.4	1.38	87
    20	104 GLY C, 103 PHE C, 107 THR C	2.85	30.9	0.57	-0.07	1.8	79
    21	104 GLY C, 103 PHE C, 300100 ILE C, 107 THR C	2.67	31.19	1.55	0.4	1.38	87
    22	103 PHE C, 300100 ILE C, 107 THR C	1.4	35.35	2.2	0.8	0.71	87
    23	300100 ILE C, 107 THR C, 103 PHE C	1.69	35.71	1.13	0.08	1.72	105
    24	300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C	1.84	36.39	0.75	-0.14	2.14	105
    25	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.97	36.67	0.46	-0.41	2.39	102
    26	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.88	37.38	0.68	-0.31	2.14	102
    27	107 THR C, 300101 THR C, 106 VAL C	1.84	37.88	1.03	-0.15	1.72	102
    28	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.75	38.46	1.73	0.18	1.33	86
    29	106 VAL C, 110 LEU C, 300101 THR C	1.12	45.82	2.43	0.5	0.64	86
    30	106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C	3.84	48.79	1.6	0.8	1.01	71
    31	106 VAL C, 300101 THR C, 26 TRP C, 33 THR C	6.19	49.65	0.48	0.33	1.39	84
    32	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.98	55.67	1.75	0.18	0.9	102
    33	103 PHE C, 106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.92	56.06	1.96	0.41	0.79	92
    34	103 PHE C, 106 VAL C, 33 THR C, 300097 VAL C	2.71	56.93	2.63	0.71	0.57	88
    35	103 PHE C, 33 THR C, 300097 VAL C	2.68	58.74	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

33. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C, 101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C, 100 ILE C, 200104 GLY C, 200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Unique lining residues set - sidechains

    97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C, 200107 THR C, 100 ILE C, 200100 ILE C, 100107 THR C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.22
    Polarity: 1.39
    Mutability: 83
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	97 VAL C, 200033 THR C, 200103 PHE C	2.68	2.06	2.1	0.57	0.71	85
    2	97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C	2.71	3.04	2.63	0.71	0.57	88
    3	97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C	2.92	3.47	1.96	0.41	0.79	92
    4	97 VAL C, 200033 THR C, 200106 VAL C, 101 THR C	2.98	9.51	1.75	0.18	0.9	102
    5	200033 THR C, 200106 VAL C, 101 THR C, 200026 TRP C	6.07	10.41	0.48	0.33	1.39	84
    6	200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C	4.01	13.58	1.6	0.8	1.01	71
    7	200106 VAL C, 101 THR C, 200110 LEU C	1.13	20.4	2.43	0.5	0.64	86
    8	200106 VAL C, 200110 LEU C, 101 THR C, 200107 THR C	1.72	21.27	1.73	0.18	1.33	86
    9	200106 VAL C, 101 THR C, 200107 THR C	1.83	21.54	1.03	-0.15	1.72	102
    10	200106 VAL C, 101 THR C, 200107 THR C, 200103 PHE C	1.86	22.31	0.68	-0.31	2.14	102
    11	200106 VAL C, 101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.98	22.42	0.46	-0.41	2.39	102
    12	101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.85	23.23	0.75	-0.14	2.14	105
    13	200107 THR C, 200103 PHE C, 100 ILE C	1.56	24.39	1.13	0.08	1.72	105
    14	200103 PHE C, 200107 THR C, 100 ILE C	1.4	27.3	2.2	0.8	0.71	87
    15	200103 PHE C, 200107 THR C, 200104 GLY C	2.25	28.52	0.57	-0.07	1.8	79
    16	200103 PHE C, 100 ILE C, 200104 GLY C	2.95	29.22	2.3	0.79	1.29	77
    17	200103 PHE C, 200104 GLY C, 200100 ILE C	3.2	30.56	2.3	0.79	1.29	77
    18	200104 GLY C, 200100 ILE C, 100107 THR C	1.74	33.8	1.13	0.08	1.72	105
    19	200104 GLY C, 200100 ILE C, 100107 THR C, 100103 PHE C	1.49	34.61	0.75	-0.14	2.14	105
    20	200100 ILE C, 100107 THR C, 100103 PHE C	1.44	36.15	1.13	0.08	1.72	105
    21	200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C	1.91	36.77	0.75	-0.14	2.14	105
    22	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.95	37.06	0.46	-0.41	2.39	102
    23	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.85	37.79	0.68	-0.31	2.14	102
    24	100107 THR C, 200101 THR C, 100106 VAL C	1.82	38.05	1.03	-0.15	1.72	102
    25	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.71	38.86	1.73	0.18	1.33	86
    26	100106 VAL C, 100110 LEU C, 200101 THR C	1.13	46.34	2.43	0.5	0.64	86
    27	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	4.01	48.95	1.6	0.8	1.01	71
    28	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.07	49.75	0.48	0.33	1.39	84
    29	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.97	56.03	1.75	0.18	0.9	102
    30	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.92	56.41	1.96	0.41	0.79	92
    31	100106 VAL C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.71	57.28	2.63	0.71	0.57	88
    32	100033 THR C, 200097 VAL C, 100103 PHE C	2.68	59.07	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

34. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 300104 GLY C, 300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 300100 ILE C, 107 THR C, 106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.22
    Polarity: 1.39
    Mutability: 83
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.68	2.06	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.71	3.04	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.92	3.47	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	2.98	9.51	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.07	10.41	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	4.01	13.58	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.13	20.4	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.72	21.27	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.83	21.54	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.86	22.31	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.98	22.42	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.85	23.23	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.56	24.39	1.13	0.08	1.72	105
    14	300103 PHE C, 300107 THR C, 100100 ILE C	1.4	27.3	2.2	0.8	0.71	87
    15	300103 PHE C, 300107 THR C, 300104 GLY C	2.25	28.52	0.57	-0.07	1.8	79
    16	300103 PHE C, 100100 ILE C, 300104 GLY C	2.95	29.22	2.3	0.79	1.29	77
    17	300103 PHE C, 300104 GLY C, 300100 ILE C	3.2	30.56	2.3	0.79	1.29	77
    18	300104 GLY C, 300100 ILE C, 107 THR C	1.74	33.8	1.13	0.08	1.72	105
    19	300104 GLY C, 300100 ILE C, 107 THR C, 103 PHE C	1.49	34.61	0.75	-0.14	2.14	105
    20	300100 ILE C, 107 THR C, 103 PHE C	1.44	36.16	1.13	0.08	1.72	105
    21	300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C	1.91	36.77	0.75	-0.14	2.14	105
    22	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.95	37.06	0.46	-0.41	2.39	102
    23	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.85	37.79	0.68	-0.31	2.14	102
    24	107 THR C, 300101 THR C, 106 VAL C	1.82	38.05	1.03	-0.15	1.72	102
    25	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.71	38.86	1.73	0.18	1.33	86
    26	106 VAL C, 110 LEU C, 300101 THR C	1.13	46.34	2.43	0.5	0.64	86
    27	106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C	4.01	48.95	1.6	0.8	1.01	71
    28	106 VAL C, 300101 THR C, 26 TRP C, 33 THR C	6.07	49.75	0.48	0.33	1.39	84
    29	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.97	56.03	1.75	0.18	0.9	102
    30	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C, 103 PHE C	2.92	56.41	1.96	0.41	0.79	92
    31	106 VAL C, 33 THR C, 300097 VAL C, 103 PHE C	2.71	57.28	2.63	0.71	0.57	88
    32	33 THR C, 300097 VAL C, 103 PHE C	2.68	59.07	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

35. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C, 103 PHE C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 103 PHE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.27
    Polarity: 1.35
    Mutability: 84
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.7	2.21	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.73	3.01	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.94	3.51	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	3.02	9.47	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.19	10.26	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	3.78	14.02	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.14	20.43	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.75	21.27	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.83	21.59	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.87	22.26	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.96	22.4	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.91	23.26	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.52	24.83	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.44	25.82	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.64	28.92	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.28	29.49	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.56	30.04	2.85	1.04	1	85
    18	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.86	30.25	1.98	0.51	1.33	104
    19	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.01	31.31	1.44	0.26	1.39	105
    20	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.65	31.46	1.38	0.26	1.05	105
    21	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.62	31.64	1.38	0.26	1.05	105
    22	100100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.67	31.71	1.38	0.26	1.05	105
    23	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.62	31.98	1.38	0.26	1.05	105
    24	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.65	32.2	1.38	0.26	1.05	105
    25	200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C	4.01	33.25	1.44	0.26	1.39	105
    26	100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C	3.86	33.42	1.98	0.51	1.33	104
    27	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.56	33.83	2.85	1.04	1	85
    28	100 ILE C, 104 GLY C, 103 PHE C	3.28	34.65	2.3	0.79	1.29	77
    29	200107 THR C, 100 ILE C, 104 GLY C	1.64	38.46	1.13	0.08	1.72	105
    30	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.44	39.35	0.75	-0.14	2.14	105
    31	200107 THR C, 100 ILE C, 200103 PHE C	1.52	40.41	1.13	0.08	1.72	105
    32	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.91	41.02	0.75	-0.14	2.14	105
    33	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.96	41.19	0.46	-0.41	2.39	102
    34	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.87	42.02	0.68	-0.31	2.14	102
    35	200107 THR C, 101 THR C, 200106 VAL C	1.83	42.33	1.03	-0.15	1.72	102
    36	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.75	43.07	1.73	0.18	1.33	86
    37	200106 VAL C, 200110 LEU C, 101 THR C	1.14	50.3	2.43	0.5	0.64	86
    38	200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C	3.78	53.32	1.6	0.8	1.01	71
    39	200106 VAL C, 101 THR C, 200026 TRP C, 200033 THR C	6.19	54.07	0.48	0.33	1.39	84
    40	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C	3.02	60.28	1.75	0.18	0.9	102
    41	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C, 200103 PHE C	2.94	60.72	1.96	0.41	0.79	92
    42	200106 VAL C, 200033 THR C, 97 VAL C, 200103 PHE C	2.73	61.4	2.63	0.71	0.57	88
    43	200033 THR C, 97 VAL C, 200103 PHE C	2.7	63.28	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

36. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C, 300101 THR C, 26 TRP C, 110 LEU C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C, 300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C, 300107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Unique lining residues set - sidechains

    33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C, 300101 THR C, 26 TRP C, 110 LEU C, 107 THR C, 300100 ILE C, 300103 PHE C, 100100 ILE C, 300107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.26
    Polarity: 1.37
    Mutability: 84
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	33 THR C, 103 PHE C, 300097 VAL C	2.73	1.98	2.1	0.57	0.71	85
    2	33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C	2.72	3.22	2.63	0.71	0.57	88
    3	33 THR C, 300097 VAL C, 106 VAL C, 300101 THR C	2.95	9.46	1.75	0.18	0.9	102
    4	33 THR C, 106 VAL C, 300101 THR C, 26 TRP C	6.16	10.31	0.48	0.33	1.39	84
    5	106 VAL C, 300101 THR C, 26 TRP C, 110 LEU C	3.46	14.42	1.6	0.8	1.01	71
    6	106 VAL C, 300101 THR C, 110 LEU C	1.19	20.53	2.43	0.5	0.64	86
    7	106 VAL C, 110 LEU C, 107 THR C, 300101 THR C	1.84	21.22	1.73	0.18	1.33	86
    8	106 VAL C, 107 THR C, 300101 THR C	1.84	21.56	1.03	-0.15	1.72	102
    9	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C	1.85	22.26	0.68	-0.31	2.14	102
    10	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.97	22.4	0.46	-0.41	2.39	102
    11	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.88	23.45	0.75	-0.14	2.14	105
    12	107 THR C, 103 PHE C, 300100 ILE C	1.45	25.24	1.13	0.08	1.72	105
    13	107 THR C, 103 PHE C, 300100 ILE C, 300104 GLY C	1.51	26.28	0.75	-0.14	2.14	105
    14	107 THR C, 300100 ILE C, 300104 GLY C	1.84	28.82	1.13	0.08	1.72	105
    15	300100 ILE C, 300104 GLY C, 300103 PHE C	3.23	29.47	2.3	0.79	1.29	77
    16	300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C	3.57	29.9	2.85	1.04	1	85
    17	300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	3.79	30.35	1.98	0.51	1.33	104
    18	107 THR C, 300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	4.08	31.2	1.44	0.26	1.39	105
    19	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.61	31.39	1.38	0.26	1.05	105
    20	107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C	4.62	31.6	1.38	0.26	1.05	105
    21	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.68	31.65	1.38	0.26	1.05	105
    22	107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C	4.68	31.72	1.38	0.26	1.05	105
    23	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.62	32.09	1.38	0.26	1.05	105
    24	107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C	4.61	32.35	1.38	0.26	1.05	105
    25	100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C	4.08	33.19	1.44	0.26	1.39	105
    26	100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C	3.79	33.55	1.98	0.51	1.33	104
    27	100 ILE C, 200100 ILE C, 200104 GLY C, 200103 PHE C	3.57	33.86	2.85	1.04	1	85
    28	200100 ILE C, 200104 GLY C, 200103 PHE C	3.23	34.82	2.3	0.79	1.29	77
    29	100107 THR C, 200100 ILE C, 200104 GLY C	1.84	38.05	1.13	0.08	1.72	105
    30	100107 THR C, 200100 ILE C, 200104 GLY C, 100103 PHE C	1.51	39.04	0.75	-0.14	2.14	105
    31	100107 THR C, 200100 ILE C, 100103 PHE C	1.45	40.34	1.13	0.08	1.72	105
    32	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.88	41.04	0.75	-0.14	2.14	105
    33	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.97	41.21	0.46	-0.41	2.39	102
    34	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.85	42.07	0.68	-0.31	2.14	102
    35	100107 THR C, 200101 THR C, 100106 VAL C	1.84	42.39	1.03	-0.15	1.72	102
    36	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.84	42.93	1.73	0.18	1.33	86
    37	100106 VAL C, 100110 LEU C, 200101 THR C	1.19	49.97	2.43	0.5	0.64	86
    38	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	3.46	53.3	1.6	0.8	1.01	71
    39	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.16	54.1	0.48	0.33	1.39	84
    40	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.95	60.57	1.75	0.18	0.9	102
    41	100106 VAL C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.72	61.65	2.63	0.71	0.57	88
    42	100033 THR C, 200097 VAL C, 100103 PHE C	2.73	63.29	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

37. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C, 200119 GLN C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 300103 PHE C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Unique lining residues set - sidechains

    119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C, 200119 GLN C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.2
    Polarity: 1.06
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C	3.01	0.07	-0.42	-0.21	2.17	89
    2	200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C	2.9	0.4	2.66	0.68	0.81	95
    3	119 GLN C, 100119 GLN C, 300119 GLN C, 200119 GLN C	2.92	1.33	-3.5	-1.1	3.53	84
    4	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.52	2.9	2.66	0.68	0.81	95
    5	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.7	10.48	4.2	1.13	0.13	98
    6	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.09	11.62	3.72	0.91	0.1	98
    7	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	12.01	2.28	0.24	0.03	99
    8	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.32	12.45	2.28	0.24	0.03	99
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 111 ALA C	2.47	12.73	3.72	0.91	0.1	98
    10	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.17	14.16	3.72	0.91	0.1	98
    11	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.35	15.1	2.28	0.24	0.03	99
    12	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.73	18.23	1.8	0.02	0	100
    13	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.22	18.95	1.3	-0.14	0.33	101
    14	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.2	20.48	-0.2	-0.61	1.33	105
    15	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.19	22.1	1.3	-0.14	0.33	101
    16	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.19	23.21	-0.2	-0.61	1.33	105
    17	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.53	32.43	-0.7	-0.77	1.66	107
    18	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	4.02	33.56	-0.64	-0.78	2	107
    19	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.74	33.87	0.34	-0.25	1.35	106
    20	200107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.56	34.44	3.46	1.29	0.44	103
    21	107 THR C, 100107 THR C, 300107 THR C, 100100 ILE C, 300100 ILE C	4.59	34.84	1.38	0.26	1.05	105
    22	107 THR C, 300107 THR C, 300104 GLY C, 100100 ILE C, 300100 ILE C	4.03	35.72	1.44	0.26	1.39	105
    23	300107 THR C, 300104 GLY C, 100100 ILE C, 300100 ILE C	3.81	36.01	1.98	0.51	1.33	104
    24	300104 GLY C, 100100 ILE C, 300100 ILE C, 300103 PHE C	3.57	36.34	2.85	1.04	1	85
    25	300104 GLY C, 300100 ILE C, 300103 PHE C	3.16	37.38	2.3	0.79	1.29	77
    26	107 THR C, 300104 GLY C, 300100 ILE C	1.71	40.66	1.13	0.08	1.72	105
    27	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.47	41.44	0.75	-0.14	2.14	105
    28	107 THR C, 300100 ILE C, 103 PHE C	1.44	42.92	1.13	0.08	1.72	105
    29	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.91	43.51	0.75	-0.14	2.14	105
    30	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.96	43.79	0.46	-0.41	2.39	102
    31	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.87	44.51	0.68	-0.31	2.14	102
    32	107 THR C, 300101 THR C, 106 VAL C	1.83	44.77	1.03	-0.15	1.72	102
    33	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.74	45.56	1.73	0.18	1.33	86
    34	106 VAL C, 110 LEU C, 300101 THR C	1.13	52.77	2.43	0.5	0.64	86
    35	106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C	3.72	55.82	1.6	0.8	1.01	71
    36	106 VAL C, 300101 THR C, 26 TRP C, 33 THR C	6.17	56.61	0.48	0.33	1.39	84
    37	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.98	62.85	1.75	0.18	0.9	102
    38	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C, 103 PHE C	2.9	63.22	1.96	0.41	0.79	92
    39	106 VAL C, 33 THR C, 300097 VAL C, 103 PHE C	2.71	64.06	2.63	0.71	0.57	88
    40	33 THR C, 300097 VAL C, 103 PHE C	2.7	65.82	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

38. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C, 200119 GLN C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Unique lining residues set - sidechains

    119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C, 200119 GLN C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.17
    Polarity: 1.04
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C	3.01	0.07	-0.42	-0.21	2.17	89
    2	200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C	2.91	0.45	2.66	0.68	0.81	95
    3	119 GLN C, 100119 GLN C, 300119 GLN C, 200119 GLN C	2.91	1.67	-3.5	-1.1	3.53	84
    4	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.23	3.51	2.66	0.68	0.81	95
    5	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.69	10.82	4.2	1.13	0.13	98
    6	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.19	11.42	3.72	0.91	0.1	98
    7	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	11.95	2.28	0.24	0.03	99
    8	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	12.67	2.28	0.24	0.03	99
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 111 ALA C	2.39	12.91	3.72	0.91	0.1	98
    10	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 300111 ALA C	2.18	14.22	3.72	0.91	0.1	98
    11	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.3	15.24	2.28	0.24	0.03	99
    12	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.75	17.5	1.8	0.02	0	100
    13	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.05	18.46	1.36	-0.14	0.68	100
    14	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.31	19.11	1.3	-0.14	0.33	101
    15	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.19	20.29	-0.2	-0.61	1.33	105
    16	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.21	20.9	1.3	-0.14	0.33	101
    17	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.21	21.9	1.3	-0.14	0.33	101
    18	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.31	23.03	-0.2	-0.61	1.33	105
    19	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.5	32.24	-0.7	-0.77	1.66	107
    20	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	3.95	33.46	-0.64	-0.78	2	107
    21	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.67	33.8	0.34	-0.25	1.35	106
    22	300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.63	34.3	3.46	1.29	0.44	103
    23	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.7	34.34	0.34	-0.25	1.35	106
    24	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200100 ILE C	4.69	34.46	0.34	-0.25	1.35	106
    25	107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 300100 ILE C	4.62	34.69	2.42	0.78	0.74	104
    26	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.6	35.08	1.38	0.26	1.05	105
    27	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	4.01	36	1.44	0.26	1.39	105
    28	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.78	36.29	1.98	0.51	1.33	104
    29	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.56	36.62	2.85	1.04	1	85
    30	200104 GLY C, 200100 ILE C, 200103 PHE C	3.28	37.41	2.3	0.79	1.29	77
    31	100107 THR C, 200104 GLY C, 200100 ILE C	1.9	40.5	1.13	0.08	1.72	105
    32	100107 THR C, 200104 GLY C, 200100 ILE C, 100103 PHE C	1.57	41.36	0.75	-0.14	2.14	105
    33	100107 THR C, 200100 ILE C, 100103 PHE C	1.43	43.12	1.13	0.08	1.72	105
    34	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.9	43.79	0.75	-0.14	2.14	105
    35	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.96	44.09	0.46	-0.41	2.39	102
    36	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.85	44.86	0.68	-0.31	2.14	102
    37	100107 THR C, 200101 THR C, 100106 VAL C	1.83	45.12	1.03	-0.15	1.72	102
    38	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.8	45.75	1.73	0.18	1.33	86
    39	100106 VAL C, 100110 LEU C, 200101 THR C	1.15	53.12	2.43	0.5	0.64	86
    40	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	3.8	56.17	1.6	0.8	1.01	71
    41	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.23	56.78	0.48	0.33	1.39	84
    42	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.93	63.29	1.75	0.18	0.9	102
    43	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.88	63.65	1.96	0.41	0.79	92
    44	100106 VAL C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.76	64.22	2.63	0.71	0.57	88
    45	100033 THR C, 200097 VAL C, 100103 PHE C	2.69	66.09	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

39. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C, 200119 GLN C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Unique lining residues set - sidechains

    119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C, 200119 GLN C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 103 PHE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.19
    Polarity: 1.07
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C	3.01	0.07	-0.42	-0.21	2.17	89
    2	200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C, 100115 VAL C	2.91	0.42	2.66	0.68	0.81	95
    3	119 GLN C, 100119 GLN C, 300119 GLN C, 200119 GLN C	2.91	1.45	-3.5	-1.1	3.53	84
    4	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.38	3.15	2.66	0.68	0.81	95
    5	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.71	10.98	4.2	1.13	0.13	98
    6	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.35	11.53	3.72	0.91	0.1	98
    7	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.24	12	2.28	0.24	0.03	99
    8	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.28	12.71	2.28	0.24	0.03	99
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 111 ALA C	2.27	13.07	3.72	0.91	0.1	98
    10	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 300111 ALA C	2.22	14.14	3.72	0.91	0.1	98
    11	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.18	15.1	2.28	0.24	0.03	99
    12	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.73	18.29	1.8	0.02	0	100
    13	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.41	19.01	1.3	-0.14	0.33	101
    14	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.15	20.21	-0.2	-0.61	1.33	105
    15	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.22	22.47	1.3	-0.14	0.33	101
    16	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.07	23.69	-0.2	-0.61	1.33	105
    17	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.51	32.3	-0.7	-0.77	1.66	107
    18	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	3.93	33.51	-0.64	-0.78	2	107
    19	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.68	33.86	0.34	-0.25	1.35	106
    20	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.62	34.34	3.46	1.29	0.44	103
    21	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.68	34.44	0.34	-0.25	1.35	106
    22	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.64	34.72	1.38	0.26	1.05	105
    23	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.61	34.92	1.38	0.26	1.05	105
    24	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.07	35.84	1.44	0.26	1.39	105
    25	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.81	36.15	1.98	0.51	1.33	104
    26	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.58	36.51	2.85	1.04	1	85
    27	100 ILE C, 104 GLY C, 103 PHE C	3.27	37.33	2.3	0.79	1.29	77
    28	200107 THR C, 100 ILE C, 104 GLY C	1.6	41.17	1.13	0.08	1.72	105
    29	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.43	41.93	0.75	-0.14	2.14	105
    30	200107 THR C, 100 ILE C, 200103 PHE C	1.49	42.97	1.13	0.08	1.72	105
    31	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.87	43.65	0.75	-0.14	2.14	105
    32	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.95	43.92	0.46	-0.41	2.39	102
    33	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.88	44.62	0.68	-0.31	2.14	102
    34	200107 THR C, 101 THR C, 200106 VAL C	1.84	45.13	1.03	-0.15	1.72	102
    35	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.75	45.72	1.73	0.18	1.33	86
    36	200106 VAL C, 200110 LEU C, 101 THR C	1.16	53.05	2.43	0.5	0.64	86
    37	200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C	3.82	56.06	1.6	0.8	1.01	71
    38	200106 VAL C, 101 THR C, 200026 TRP C, 200033 THR C	6.2	56.91	0.48	0.33	1.39	84
    39	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C	3.01	62.93	1.75	0.18	0.9	102
    40	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C, 200103 PHE C	2.91	63.32	1.96	0.41	0.79	92
    41	200106 VAL C, 200033 THR C, 97 VAL C, 200103 PHE C	2.73	64.2	2.63	0.71	0.57	88
    42	200033 THR C, 97 VAL C, 200103 PHE C	2.69	66.01	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

40. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 0.7
    Hydrophobicity: 0.07
    Polarity: 4.32
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.73	1.95	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.72	2.96	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.89	3.41	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	3	9.52	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.21	10.2	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	3.53	14.22	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.15	20.47	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.77	21.21	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.84	21.5	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.84	22.18	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.96	22.44	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.84	23.55	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.45	25.1	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.48	26	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.72	28.85	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.23	29.52	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.57	29.99	2.85	1.04	1	85
    18	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.81	30.39	1.98	0.51	1.33	104
    19	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.08	31.35	1.44	0.26	1.39	105
    20	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.66	31.47	1.38	0.26	1.05	105
    21	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	31.64	1.38	0.26	1.05	105
    22	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.69	31.74	0.34	-0.25	1.35	106
    23	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.64	32.54	3.46	1.29	0.44	103
    24	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.58	33.13	0.34	-0.25	1.35	106
    25	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.33	33.85	-0.64	-0.78	2	107
    26	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.64	43.81	-0.7	-0.77	1.66	107
    27	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	2.07	44.61	-0.2	-0.61	1.33	105
    28	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.23	45.94	1.3	-0.14	0.33	101
    29	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.18	47.61	-0.2	-0.61	1.33	105
    30	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.42	48.66	1.3	-0.14	0.33	101
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.75	51.96	1.8	0.02	0	100
    32	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.34	52.57	2.28	0.24	0.03	99
    33	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.21	53.04	3.72	0.91	0.1	98
    34	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.34	53.61	3.72	0.91	0.1	98
    35	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.34	53.93	2.28	0.24	0.03	99
    36	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.27	54.87	2.28	0.24	0.03	99
    37	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.33	55.64	3.72	0.91	0.1	98
    38	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	63.73	4.2	1.13	0.13	98
    39	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.38	64.96	2.66	0.68	0.81	95
    40	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.92	65.54	-3.5	-1.1	3.53	84
    41	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	3.01	65.68	-1.96	-0.65	2.85	86
    42	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	65.96	2.66	0.68	0.81	95
    43	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	66.05	-1.96	-0.65	2.85	86
    44	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.66	72.13	-3.5	-1.1	3.53	84
    45	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C	3.65	73.68	-3.44	-0.83	13.14	85
    46	200119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C	4.44	73.76	-3.26	-0.01	41.99	89
    47	300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C	4.41	73.97	-3.26	-0.01	41.99	89
    48	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.4	74.05	-3.44	-0.83	13.14	85
    49	100119 GLN C, 200119 GLN C, 124 HIS C, 100124 HIS C, 300124 HIS C	4.41	74.05	-3.32	-0.28	32.37	88

    pore with bottle neck

    pore with local minimum

41. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C, 200124 HIS C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C,

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.3
    Hydrophobicity: 0
    Polarity: 6.03
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.7	1.97	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.73	2.99	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.95	3.45	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	2.99	9.36	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.16	10.27	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	4.07	13.54	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.15	20.52	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.8	21.32	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.84	21.62	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.88	22.24	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.95	22.48	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.9	23.28	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.43	25.56	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.59	26.46	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.92	28.73	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.16	29.5	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.56	29.94	2.85	1.04	1	85
    18	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.79	30.32	1.98	0.51	1.33	104
    19	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.02	31.3	1.44	0.26	1.39	105
    20	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.61	31.44	1.38	0.26	1.05	105
    21	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	31.62	1.38	0.26	1.05	105
    22	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.68	31.71	0.34	-0.25	1.35	106
    23	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.64	32.47	3.46	1.29	0.44	103
    24	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.55	33.04	0.34	-0.25	1.35	106
    25	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.35	33.75	-0.64	-0.78	2	107
    26	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.74	43.81	-0.7	-0.77	1.66	107
    27	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	1.94	44.61	-0.2	-0.61	1.33	105
    28	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	45.96	1.3	-0.14	0.33	101
    29	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.2	47.69	-0.2	-0.61	1.33	105
    30	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	48.77	1.3	-0.14	0.33	101
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.93	52.06	1.8	0.02	0	100
    32	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.08	52.62	2.28	0.24	0.03	99
    33	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.25	53.11	3.72	0.91	0.1	98
    34	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.31	53.68	3.72	0.91	0.1	98
    35	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.36	53.96	2.28	0.24	0.03	99
    36	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	55.04	2.28	0.24	0.03	99
    37	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.23	55.84	3.72	0.91	0.1	98
    38	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.66	63.15	4.2	1.13	0.13	98
    39	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.12	64.76	2.66	0.68	0.81	95
    40	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.81	65.1	-1.96	-0.65	2.85	86
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.92	65.65	-3.5	-1.1	3.53	84
    42	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.92	65.96	2.66	0.68	0.81	95
    43	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	66.05	-1.96	-0.65	2.85	86
    44	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.65	72.53	-3.5	-1.1	3.53	84
    45	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.88	73.66	-3.44	-0.83	13.14	85
    46	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.41	73.97	-3.26	-0.01	41.99	89
    47	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	74.01	-3.44	-0.83	13.14	85
    48	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.38	74.09	-3.38	-0.56	22.76	86
    49	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.34	74.38	-3.38	-0.56	22.76	86
    50	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.16	75.53	-3.38	-0.56	22.76	86
    51	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.11	76.34	-3.38	-0.56	22.76	86
    52	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	3.02	78.27	-3.35	-0.42	27.57	87
    53	100119 GLN C, 100124 HIS C, 200124 HIS C	2.4	81.43	-3.3	-0.19	35.58	88
    54	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.28	82.36	-2.9	-0.52	27.63	86
    55	100124 HIS C, 100122 ARG C, 200124 HIS C	2.23	82.95	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

42. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C, 101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C, 100 ILE C, 104 GLY C, 103 PHE C, 300100 ILE C, 107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C, 200100 ILE C, 100104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C, 200124 HIS C

    Unique lining residues set - sidechains

    97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C, 200107 THR C, 100 ILE C, 103 PHE C, 300100 ILE C, 107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C, 200100 ILE C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C,

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.3
    Hydrophobicity: 0
    Polarity: 6.03
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	97 VAL C, 200033 THR C, 200103 PHE C	2.7	1.97	2.1	0.57	0.71	85
    2	97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C	2.73	2.99	2.63	0.71	0.57	88
    3	97 VAL C, 200033 THR C, 200103 PHE C, 200106 VAL C, 101 THR C	2.95	3.45	1.96	0.41	0.79	92
    4	97 VAL C, 200033 THR C, 200106 VAL C, 101 THR C	2.99	9.36	1.75	0.18	0.9	102
    5	200033 THR C, 200106 VAL C, 101 THR C, 200026 TRP C	6.16	10.27	0.48	0.33	1.39	84
    6	200106 VAL C, 101 THR C, 200026 TRP C, 200110 LEU C	4.07	13.54	1.6	0.8	1.01	71
    7	200106 VAL C, 101 THR C, 200110 LEU C	1.15	20.52	2.43	0.5	0.64	86
    8	200106 VAL C, 200110 LEU C, 101 THR C, 200107 THR C	1.8	21.32	1.73	0.18	1.33	86
    9	200106 VAL C, 101 THR C, 200107 THR C	1.84	21.62	1.03	-0.15	1.72	102
    10	200106 VAL C, 101 THR C, 200107 THR C, 200103 PHE C	1.88	22.24	0.68	-0.31	2.14	102
    11	200106 VAL C, 101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.95	22.48	0.46	-0.41	2.39	102
    12	101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.9	23.28	0.75	-0.14	2.14	105
    13	200107 THR C, 200103 PHE C, 100 ILE C	1.43	25.56	1.13	0.08	1.72	105
    14	200107 THR C, 200103 PHE C, 100 ILE C, 104 GLY C	1.59	26.46	0.75	-0.14	2.14	105
    15	200107 THR C, 100 ILE C, 104 GLY C	1.92	28.73	1.13	0.08	1.72	105
    16	100 ILE C, 104 GLY C, 103 PHE C	3.16	29.5	2.3	0.79	1.29	77
    17	100 ILE C, 104 GLY C, 103 PHE C, 300100 ILE C	3.56	29.94	2.85	1.04	1	85
    18	100 ILE C, 104 GLY C, 300100 ILE C, 107 THR C	3.79	30.32	1.98	0.51	1.33	104
    19	200107 THR C, 100 ILE C, 104 GLY C, 300100 ILE C, 107 THR C	4.02	31.3	1.44	0.26	1.39	105
    20	200107 THR C, 100 ILE C, 300100 ILE C, 107 THR C, 300107 THR C	4.61	31.44	1.38	0.26	1.05	105
    21	200107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C, 200100 ILE C	4.64	31.62	1.38	0.26	1.05	105
    22	200107 THR C, 107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C	4.68	31.71	0.34	-0.25	1.35	106
    23	100 ILE C, 300100 ILE C, 107 THR C, 100100 ILE C, 200100 ILE C	4.64	32.47	3.46	1.29	0.44	103
    24	200107 THR C, 107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C	4.55	33.04	0.34	-0.25	1.35	106
    25	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C, 100104 GLY C	4.35	33.75	-0.64	-0.78	2	107
    26	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C	1.74	43.81	-0.7	-0.77	1.66	107
    27	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C, 100111 ALA C	1.94	44.61	-0.2	-0.61	1.33	105
    28	300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	45.96	1.3	-0.14	0.33	101
    29	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C, 300111 ALA C	2.2	47.69	-0.2	-0.61	1.33	105
    30	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	48.77	1.3	-0.14	0.33	101
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.93	52.06	1.8	0.02	0	100
    32	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.08	52.62	2.28	0.24	0.03	99
    33	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.25	53.11	3.72	0.91	0.1	98
    34	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.31	53.68	3.72	0.91	0.1	98
    35	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.36	53.96	2.28	0.24	0.03	99
    36	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	55.04	2.28	0.24	0.03	99
    37	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.23	55.84	3.72	0.91	0.1	98
    38	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.66	63.15	4.2	1.13	0.13	98
    39	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.12	64.76	2.66	0.68	0.81	95
    40	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.81	65.1	-1.96	-0.65	2.85	86
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.92	65.65	-3.5	-1.1	3.53	84
    42	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.92	65.96	2.66	0.68	0.81	95
    43	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	66.05	-1.96	-0.65	2.85	86
    44	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.65	72.53	-3.5	-1.1	3.53	84
    45	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.88	73.66	-3.44	-0.83	13.14	85
    46	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.41	73.97	-3.26	-0.01	41.99	89
    47	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	74.01	-3.44	-0.83	13.14	85
    48	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.38	74.09	-3.38	-0.56	22.76	86
    49	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.34	74.38	-3.38	-0.56	22.76	86
    50	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.16	75.53	-3.38	-0.56	22.76	86
    51	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.11	76.34	-3.38	-0.56	22.76	86
    52	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	3.02	78.27	-3.35	-0.42	27.57	87
    53	100119 GLN C, 100124 HIS C, 200124 HIS C	2.4	81.43	-3.3	-0.19	35.58	88
    54	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.28	82.36	-2.9	-0.52	27.63	86
    55	100124 HIS C, 100122 ARG C, 200124 HIS C	2.23	82.95	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

43. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Unique lining residues set - sidechains

    200122 ARG C, 200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.6
    Hydrophobicity: 0.05
    Polarity: 5.39
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.23	0.83	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.28	1.88	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.4	5.61	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	3	7.38	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.09	7.96	-3.38	-0.56	22.76	86
    6	119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.17	8.71	-3.38	-0.56	22.76	86
    7	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.33	8.96	-3.38	-0.56	22.76	86
    8	200124 HIS C, 124 HIS C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.41	9.42	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.57	11.6	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.64	16.92	-3.5	-1.1	3.53	84
    11	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 200115 VAL C	3	17.01	-1.96	-0.65	2.85	86
    12	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.92	17.37	2.66	0.68	0.81	95
    13	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 300115 VAL C	2.93	17.57	-1.96	-0.65	2.85	86
    14	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.91	18.54	-3.5	-1.1	3.53	84
    15	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.22	20.42	2.66	0.68	0.81	95
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.68	27.48	4.2	1.13	0.13	98
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.16	28.65	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.28	28.85	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.33	29.56	2.28	0.24	0.03	99
    20	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.33	29.82	3.72	0.91	0.1	98
    21	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.17	31.21	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.97	32.28	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.89	34.63	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.13	35.57	1.36	-0.14	0.68	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.2	36.15	1.3	-0.14	0.33	101
    26	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.21	37.39	-0.2	-0.61	1.33	105
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.33	38	1.3	-0.14	0.33	101
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.06	39.59	1.3	-0.14	0.33	101
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.71	49.44	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	4.16	50.6	-0.64	-0.78	2	107
    31	300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.61	51.23	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.69	51.3	0.34	-0.25	1.35	106
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200100 ILE C	4.69	51.43	0.34	-0.25	1.35	106
    34	107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 300100 ILE C	4.63	51.67	2.42	0.78	0.74	104
    35	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.58	52.08	1.38	0.26	1.05	105
    36	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.97	53.02	1.44	0.26	1.39	105
    37	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.86	53.18	1.98	0.51	1.33	104
    38	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.58	53.57	2.85	1.04	1	85
    39	200104 GLY C, 200100 ILE C, 200103 PHE C	3.27	54.42	2.3	0.79	1.29	77
    40	100107 THR C, 200104 GLY C, 200100 ILE C	1.82	57.75	1.13	0.08	1.72	105
    41	100107 THR C, 200104 GLY C, 200100 ILE C, 100103 PHE C	1.52	58.62	0.75	-0.14	2.14	105
    42	100107 THR C, 200100 ILE C, 100103 PHE C	1.43	60.2	1.13	0.08	1.72	105
    43	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.91	60.72	0.75	-0.14	2.14	105
    44	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.95	61.02	0.46	-0.41	2.39	102
    45	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.87	61.8	0.68	-0.31	2.14	102
    46	100107 THR C, 200101 THR C, 100106 VAL C	1.84	62.08	1.03	-0.15	1.72	102
    47	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.78	62.74	1.73	0.18	1.33	86
    48	100106 VAL C, 100110 LEU C, 200101 THR C	1.14	70.56	2.43	0.5	0.64	86
    49	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	4.18	73.09	1.6	0.8	1.01	71
    50	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.19	73.73	0.48	0.33	1.39	84
    51	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.99	80.09	1.75	0.18	0.9	102
    52	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.94	80.49	1.96	0.41	0.79	92
    53	100106 VAL C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.72	81.4	2.63	0.71	0.57	88
    54	100033 THR C, 200097 VAL C, 100103 PHE C	2.7	83.06	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

44. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Unique lining residues set - sidechains

    300122 ARG C, 300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.6
    Hydrophobicity: 0.06
    Polarity: 5.29
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100124 HIS C, 300122 ARG C, 300124 HIS C	2.23	0.83	-2.7	-0.32	35.66	87
    2	100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C	2.28	1.88	-2.9	-0.52	27.63	86
    3	300124 HIS C, 300119 GLN C, 100124 HIS C	2.4	5.61	-3.3	-0.19	35.58	88
    4	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C	3	7.38	-3.35	-0.42	27.57	87
    5	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	4.08	7.96	-3.38	-0.56	22.76	86
    6	100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C	4.17	8.71	-3.38	-0.56	22.76	86
    7	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	4.33	8.96	-3.38	-0.56	22.76	86
    8	300124 HIS C, 100124 HIS C, 124 HIS C, 200119 GLN C, 200124 HIS C	4.41	9.42	-3.26	-0.01	41.99	89
    9	300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 200119 GLN C	3.57	11.6	-3.44	-0.83	13.14	85
    10	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.64	16.92	-3.5	-1.1	3.53	84
    11	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C, 200115 VAL C	3	17.01	-1.96	-0.65	2.85	86
    12	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.92	17.21	2.66	0.68	0.81	95
    13	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.95	17.37	2.66	0.68	0.81	95
    14	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C, 300115 VAL C	2.93	17.57	-1.96	-0.65	2.85	86
    15	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.91	18.54	-3.5	-1.1	3.53	84
    16	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.22	20.42	2.66	0.68	0.81	95
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.68	27.48	4.2	1.13	0.13	98
    18	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.16	28.65	3.72	0.91	0.1	98
    19	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.28	28.85	2.28	0.24	0.03	99
    20	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.33	29.56	2.28	0.24	0.03	99
    21	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.33	29.82	3.72	0.91	0.1	98
    22	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.17	31.21	3.72	0.91	0.1	98
    23	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.97	32.28	2.28	0.24	0.03	99
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.89	34.63	1.8	0.02	0	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.13	35.57	1.36	-0.14	0.68	100
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.2	36.15	1.3	-0.14	0.33	101
    27	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.21	37.39	-0.2	-0.61	1.33	105
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.33	38	1.3	-0.14	0.33	101
    29	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.06	39.59	1.3	-0.14	0.33	101
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.71	49.44	-0.7	-0.77	1.66	107
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	4.16	50.6	-0.64	-0.78	2	107
    32	300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.61	51.23	3.46	1.29	0.44	103
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.69	51.3	0.34	-0.25	1.35	106
    34	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200100 ILE C	4.69	51.43	0.34	-0.25	1.35	106
    35	107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 300100 ILE C	4.63	51.67	2.42	0.78	0.74	104
    36	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.58	52.08	1.38	0.26	1.05	105
    37	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.97	53.02	1.44	0.26	1.39	105
    38	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.86	53.18	1.98	0.51	1.33	104
    39	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.58	53.57	2.85	1.04	1	85
    40	200104 GLY C, 200100 ILE C, 200103 PHE C	3.27	54.42	2.3	0.79	1.29	77
    41	100107 THR C, 200104 GLY C, 200100 ILE C	1.82	57.75	1.13	0.08	1.72	105
    42	100107 THR C, 200104 GLY C, 200100 ILE C, 100103 PHE C	1.52	58.62	0.75	-0.14	2.14	105
    43	100107 THR C, 200100 ILE C, 100103 PHE C	1.43	60.2	1.13	0.08	1.72	105
    44	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.91	60.72	0.75	-0.14	2.14	105
    45	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.95	61.02	0.46	-0.41	2.39	102
    46	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.87	61.8	0.68	-0.31	2.14	102
    47	100107 THR C, 200101 THR C, 100106 VAL C	1.84	62.08	1.03	-0.15	1.72	102
    48	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.78	62.74	1.73	0.18	1.33	86
    49	100106 VAL C, 100110 LEU C, 200101 THR C	1.14	70.56	2.43	0.5	0.64	86
    50	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	4.18	73.09	1.6	0.8	1.01	71
    51	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.19	73.73	0.48	0.33	1.39	84
    52	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.99	80.09	1.75	0.18	0.9	102
    53	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.94	80.49	1.96	0.41	0.79	92
    54	100106 VAL C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.72	81.4	2.63	0.71	0.57	88
    55	100033 THR C, 200097 VAL C, 100103 PHE C	2.7	83.06	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

45. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100033 THR C, 100103 PHE C, 200097 VAL C, 100106 VAL C, 200101 THR C, 100026 TRP C, 100110 LEU C, 100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C, 200100 ILE C, 200104 GLY C, 200103 PHE C, 100 ILE C, 200107 THR C, 107 THR C, 100100 ILE C, 300100 ILE C, 300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C, 200124 HIS C

    Unique lining residues set - sidechains

    100033 THR C, 100103 PHE C, 200097 VAL C, 100106 VAL C, 200101 THR C, 100026 TRP C, 100110 LEU C, 100107 THR C, 200100 ILE C, 200103 PHE C, 100 ILE C, 200107 THR C, 107 THR C, 100100 ILE C, 300100 ILE C, 300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C,

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.3
    Hydrophobicity: 0
    Polarity: 6.52
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100033 THR C, 100103 PHE C, 200097 VAL C	2.7	2	2.1	0.57	0.71	85
    2	100033 THR C, 100103 PHE C, 200097 VAL C, 100106 VAL C	2.72	3.07	2.63	0.71	0.57	88
    3	100033 THR C, 100103 PHE C, 200097 VAL C, 100106 VAL C, 200101 THR C	2.97	3.54	1.96	0.41	0.79	92
    4	100033 THR C, 200097 VAL C, 100106 VAL C, 200101 THR C	3.02	9.44	1.75	0.18	0.9	102
    5	100033 THR C, 100106 VAL C, 200101 THR C, 100026 TRP C	6.07	10.43	0.48	0.33	1.39	84
    6	100106 VAL C, 200101 THR C, 100026 TRP C, 100110 LEU C	3.65	14.1	1.6	0.8	1.01	71
    7	100106 VAL C, 200101 THR C, 100110 LEU C	1.19	20.47	2.43	0.5	0.64	86
    8	100106 VAL C, 100110 LEU C, 100107 THR C, 200101 THR C	1.77	21.26	1.73	0.18	1.33	86
    9	100106 VAL C, 100107 THR C, 200101 THR C	1.84	21.56	1.03	-0.15	1.72	102
    10	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C	1.85	22.21	0.68	-0.31	2.14	102
    11	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.96	22.46	0.46	-0.41	2.39	102
    12	100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.89	23.27	0.75	-0.14	2.14	105
    13	100107 THR C, 100103 PHE C, 200100 ILE C	1.48	25.61	1.13	0.08	1.72	105
    14	100107 THR C, 100103 PHE C, 200100 ILE C, 200104 GLY C	1.59	26.52	0.75	-0.14	2.14	105
    15	100107 THR C, 200100 ILE C, 200104 GLY C	1.89	28.76	1.13	0.08	1.72	105
    16	200100 ILE C, 200104 GLY C, 200103 PHE C	3.18	29.5	2.3	0.79	1.29	77
    17	200100 ILE C, 200104 GLY C, 200103 PHE C, 100 ILE C	3.57	30	2.85	1.04	1	85
    18	200100 ILE C, 200104 GLY C, 100 ILE C, 200107 THR C	3.84	30.42	1.98	0.51	1.33	104
    19	100107 THR C, 200100 ILE C, 200104 GLY C, 100 ILE C, 200107 THR C	4.11	31.19	1.44	0.26	1.39	105
    20	100107 THR C, 200100 ILE C, 100 ILE C, 200107 THR C, 107 THR C	4.56	31.48	1.38	0.26	1.05	105
    21	100 ILE C, 107 THR C, 100100 ILE C, 300100 ILE C, 300107 THR C	4.64	31.67	2.42	0.78	0.74	104
    22	100107 THR C, 200100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.69	31.75	0.34	-0.25	1.35	106
    23	100107 THR C, 100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.7	31.83	0.34	-0.25	1.35	106
    24	200100 ILE C, 100 ILE C, 100100 ILE C, 300100 ILE C, 300107 THR C	4.65	32.57	3.46	1.29	0.44	103
    25	100107 THR C, 100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.6	33.13	0.34	-0.25	1.35	106
    26	100107 THR C, 200104 GLY C, 200107 THR C, 107 THR C, 300107 THR C	4.04	34.59	-0.64	-0.78	2	107
    27	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C	1.77	44.17	-0.7	-0.77	1.66	107
    28	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C, 100111 ALA C	2.01	44.89	-0.2	-0.61	1.33	105
    29	100107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	45.16	1.3	-0.14	0.33	101
    30	300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.28	46.28	1.3	-0.14	0.33	101
    31	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C, 300111 ALA C	2.28	47.36	-0.2	-0.61	1.33	105
    32	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.98	49.44	1.3	-0.14	0.33	101
    33	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.95	51.77	1.8	0.02	0	100
    34	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.11	52.57	2.28	0.24	0.03	99
    35	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.16	53.48	3.72	0.91	0.1	98
    36	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.38	53.78	3.72	0.91	0.1	98
    37	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.33	54.2	2.28	0.24	0.03	99
    38	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.32	54.95	2.28	0.24	0.03	99
    39	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.17	55.71	3.72	0.91	0.1	98
    40	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.64	64.15	4.2	1.13	0.13	98
    41	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.6	64.87	2.66	0.68	0.81	95
    42	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.85	65.24	-1.96	-0.65	2.85	86
    43	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.9	65.82	-3.5	-1.1	3.53	84
    44	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	66.14	2.66	0.68	0.81	95
    45	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.98	66.23	-1.96	-0.65	2.85	86
    46	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.68	72.34	-3.5	-1.1	3.53	84
    47	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.64	73.73	-3.44	-0.83	13.14	85
    48	200119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.43	73.89	-3.26	-0.01	41.99	89
    49	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.42	74.13	-3.26	-0.01	41.99	89
    50	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	74.18	-3.44	-0.83	13.14	85
    51	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.39	74.25	-3.38	-0.56	22.76	86
    52	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.35	74.51	-3.38	-0.56	22.76	86
    53	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.18	75.54	-3.38	-0.56	22.76	86
    54	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.13	76.32	-3.38	-0.56	22.76	86
    55	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	3.12	78.26	-3.35	-0.42	27.57	87
    56	100119 GLN C, 100124 HIS C, 200124 HIS C	2.4	81.84	-3.3	-0.19	35.58	88
    57	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.28	82.52	-2.9	-0.52	27.63	86
    58	100124 HIS C, 100122 ARG C, 200124 HIS C	2.23	83.11	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

46. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Unique lining residues set - sidechains

    122 ARG C, 124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.6
    Hydrophobicity: 0.04
    Polarity: 4.98
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	122 ARG C, 124 HIS C, 300124 HIS C	2.25	0.98	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.33	1.66	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.45	5.54	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	3	7.21	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	3.87	8.18	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.21	8.34	-3.38	-0.56	22.76	86
    7	124 HIS C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.23	8.97	-3.32	-0.28	32.37	88
    8	119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C	3.54	10.96	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.63	16.44	-3.5	-1.1	3.53	84
    10	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.99	16.52	-1.96	-0.65	2.85	86
    11	100119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.9	16.8	2.66	0.68	0.81	95
    12	119 GLN C, 300119 GLN C, 100119 GLN C, 300115 VAL C, 200115 VAL C	3.01	16.97	-0.42	-0.21	2.17	89
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.92	18.09	-3.5	-1.1	3.53	84
    14	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.26	19.81	2.66	0.68	0.81	95
    15	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.73	27.36	4.2	1.13	0.13	98
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.29	27.94	3.72	0.91	0.1	98
    17	300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C, 111 ALA C	2.55	28.3	3.24	0.69	0.08	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	28.61	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.39	29.11	2.28	0.24	0.03	99
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.26	30.28	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.98	32.14	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.9	34.29	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.03	35.14	1.36	-0.14	0.68	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.19	35.69	1.3	-0.14	0.33	101
    25	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.24	36.76	-0.2	-0.61	1.33	105
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.2	38.19	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.63	39.16	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.51	49.27	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	4.24	49.82	-0.64	-0.78	2	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C	4.51	50.21	0.34	-0.25	1.35	106
    31	200107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C	4.59	50.81	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 300107 THR C, 300100 ILE C, 100100 ILE C	4.64	51.19	1.38	0.26	1.05	105
    33	107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	4.08	52.08	1.44	0.26	1.39	105
    34	300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	3.84	52.39	1.98	0.51	1.33	104
    35	300104 GLY C, 300100 ILE C, 100100 ILE C, 300103 PHE C	3.58	52.75	2.85	1.04	1	85
    36	300104 GLY C, 300100 ILE C, 300103 PHE C	3.19	53.72	2.3	0.79	1.29	77
    37	107 THR C, 300104 GLY C, 300100 ILE C	1.76	56.89	1.13	0.08	1.72	105
    38	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.52	57.7	0.75	-0.14	2.14	105
    39	107 THR C, 300100 ILE C, 103 PHE C	1.45	59.29	1.13	0.08	1.72	105
    40	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.9	59.91	0.75	-0.14	2.14	105
    41	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.95	60.18	0.46	-0.41	2.39	102
    42	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.88	60.88	0.68	-0.31	2.14	102
    43	107 THR C, 300101 THR C, 106 VAL C	1.84	61.38	1.03	-0.15	1.72	102
    44	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.75	61.95	1.73	0.18	1.33	86
    45	106 VAL C, 110 LEU C, 300101 THR C	1.2	69.09	2.43	0.5	0.64	86
    46	106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C	3.67	72.22	1.6	0.8	1.01	71
    47	106 VAL C, 300101 THR C, 26 TRP C, 33 THR C	6.15	73.01	0.48	0.33	1.39	84
    48	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.99	79.25	1.75	0.18	0.9	102
    49	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C, 103 PHE C	2.88	79.63	1.96	0.41	0.79	92
    50	106 VAL C, 33 THR C, 300097 VAL C, 103 PHE C	2.73	80.47	2.63	0.71	0.57	88
    51	33 THR C, 300097 VAL C, 103 PHE C	2.72	82.24	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

47. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Unique lining residues set - sidechains

    122 ARG C, 124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C, 100033 THR C, 200097 VAL C, 100103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.6
    Hydrophobicity: 0.03
    Polarity: 4.68
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	122 ARG C, 124 HIS C, 300124 HIS C	2.24	0.81	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.27	1.77	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.41	5.12	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	2.8	6.93	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	3.78	8.1	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.18	8.39	-3.38	-0.56	22.76	86
    7	124 HIS C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.2	8.95	-3.32	-0.28	32.37	88
    8	119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C	3.55	11.04	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.66	16.46	-3.5	-1.1	3.53	84
    10	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	3.01	16.54	-1.96	-0.65	2.85	86
    11	100119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.9	16.86	2.66	0.68	0.81	95
    12	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.98	17.05	-1.96	-0.65	2.85	86
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.92	17.83	-3.5	-1.1	3.53	84
    14	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.41	19.47	2.66	0.68	0.81	95
    15	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.71	27.66	4.2	1.13	0.13	98
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.19	28.16	3.72	0.91	0.1	98
    17	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.31	28.58	2.28	0.24	0.03	99
    18	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.32	29.06	2.28	0.24	0.03	99
    19	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 111 ALA C	2.38	29.55	3.72	0.91	0.1	98
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300111 ALA C	2.21	30.29	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.19	32.21	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	34.44	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.11	35.82	1.3	-0.14	0.33	101
    24	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.21	36.99	-0.2	-0.61	1.33	105
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.25	37.56	1.3	-0.14	0.33	101
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.45	38.84	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.11	40.06	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.51	48.98	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	4.13	50.13	-0.64	-0.78	2	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.6	50.4	0.34	-0.25	1.35	106
    31	300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.65	50.87	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.7	50.91	0.34	-0.25	1.35	106
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200100 ILE C	4.69	50.99	0.34	-0.25	1.35	106
    34	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.69	51.03	0.34	-0.25	1.35	106
    35	107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 300100 ILE C	4.62	51.28	2.42	0.78	0.74	104
    36	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.57	51.69	1.38	0.26	1.05	105
    37	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.99	52.6	1.44	0.26	1.39	105
    38	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.87	52.75	1.98	0.51	1.33	104
    39	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.55	53.18	2.85	1.04	1	85
    40	200104 GLY C, 200100 ILE C, 200103 PHE C	3.25	54.02	2.3	0.79	1.29	77
    41	100107 THR C, 200104 GLY C, 200100 ILE C	1.83	57.21	1.13	0.08	1.72	105
    42	100107 THR C, 200104 GLY C, 200100 ILE C, 100103 PHE C	1.56	58.05	0.75	-0.14	2.14	105
    43	100107 THR C, 200100 ILE C, 100103 PHE C	1.44	59.71	1.13	0.08	1.72	105
    44	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.91	60.36	0.75	-0.14	2.14	105
    45	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.96	60.5	0.46	-0.41	2.39	102
    46	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.85	61.45	0.68	-0.31	2.14	102
    47	100107 THR C, 200101 THR C, 100106 VAL C	1.83	61.71	1.03	-0.15	1.72	102
    48	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.76	62.33	1.73	0.18	1.33	86
    49	100106 VAL C, 100110 LEU C, 200101 THR C	1.16	69.75	2.43	0.5	0.64	86
    50	100106 VAL C, 100110 LEU C, 200101 THR C, 100026 TRP C	3.88	72.52	1.6	0.8	1.01	71
    51	100106 VAL C, 200101 THR C, 100026 TRP C, 100033 THR C	6.07	73.35	0.48	0.33	1.39	84
    52	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C	2.92	79.86	1.75	0.18	0.9	102
    53	100106 VAL C, 200101 THR C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.86	80.21	1.96	0.41	0.79	92
    54	100106 VAL C, 100033 THR C, 200097 VAL C, 100103 PHE C	2.77	80.78	2.63	0.71	0.57	88
    55	100033 THR C, 200097 VAL C, 100103 PHE C	2.72	82.64	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

48. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Unique lining residues set - sidechains

    200122 ARG C, 200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.02
    Polarity: 5.79
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.24	0.8	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.27	1.76	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.42	6.07	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	3.24	6.93	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	3.79	8.09	-3.38	-0.56	22.76	86
    6	119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.15	8.7	-3.38	-0.56	22.76	86
    7	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.33	8.93	-3.38	-0.56	22.76	86
    8	200124 HIS C, 124 HIS C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.39	9.63	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.71	11.26	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.67	16.88	-3.5	-1.1	3.53	84
    11	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 200115 VAL C	3	16.97	-1.96	-0.65	2.85	86
    12	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.91	17.44	2.66	0.68	0.81	95
    13	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.8	18.73	-3.5	-1.1	3.53	84
    14	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.22	20.58	2.66	0.68	0.81	95
    15	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.68	27.82	4.2	1.13	0.13	98
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.16	28.41	3.72	0.91	0.1	98
    17	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	29.1	2.28	0.24	0.03	99
    18	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.41	29.64	2.28	0.24	0.03	99
    19	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.24	31.21	3.72	0.91	0.1	98
    20	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.26	32.23	2.28	0.24	0.03	99
    21	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.76	34.49	1.8	0.02	0	100
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.12	35.44	1.36	-0.14	0.68	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.48	36.08	1.3	-0.14	0.33	101
    24	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.2	37.26	-0.2	-0.61	1.33	105
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.29	38.86	1.3	-0.14	0.33	101
    26	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.03	39.98	-0.2	-0.61	1.33	105
    27	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.63	49.16	-0.7	-0.77	1.66	107
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	3.95	50.4	-0.64	-0.78	2	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C	4.52	50.76	0.34	-0.25	1.35	106
    30	200107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C	4.6	51.37	3.46	1.29	0.44	103
    31	107 THR C, 100107 THR C, 300107 THR C, 300100 ILE C, 100100 ILE C	4.59	51.8	1.38	0.26	1.05	105
    32	107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	4	52.7	1.44	0.26	1.39	105
    33	300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	3.88	52.85	1.98	0.51	1.33	104
    34	300104 GLY C, 300100 ILE C, 100100 ILE C, 300103 PHE C	3.55	53.27	2.85	1.04	1	85
    35	300104 GLY C, 300100 ILE C, 300103 PHE C	3.25	54.11	2.3	0.79	1.29	77
    36	107 THR C, 300104 GLY C, 300100 ILE C	1.83	57.3	1.13	0.08	1.72	105
    37	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.56	58.14	0.75	-0.14	2.14	105
    38	107 THR C, 300100 ILE C, 103 PHE C	1.44	59.8	1.13	0.08	1.72	105
    39	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.91	60.45	0.75	-0.14	2.14	105
    40	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.96	60.59	0.46	-0.41	2.39	102
    41	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.85	61.54	0.68	-0.31	2.14	102
    42	107 THR C, 300101 THR C, 106 VAL C	1.83	61.8	1.03	-0.15	1.72	102
    43	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.76	62.41	1.73	0.18	1.33	86
    44	106 VAL C, 110 LEU C, 300101 THR C	1.16	69.84	2.43	0.5	0.64	86
    45	106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C	3.88	72.61	1.6	0.8	1.01	71
    46	106 VAL C, 300101 THR C, 26 TRP C, 33 THR C	6.07	73.44	0.48	0.33	1.39	84
    47	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.92	79.95	1.75	0.18	0.9	102
    48	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C, 103 PHE C	2.86	80.3	1.96	0.41	0.79	92
    49	106 VAL C, 33 THR C, 300097 VAL C, 103 PHE C	2.77	80.87	2.63	0.71	0.57	88
    50	33 THR C, 300097 VAL C, 103 PHE C	2.72	82.73	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

49. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Unique lining residues set - sidechains

    300122 ARG C, 300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C, 33 THR C, 300097 VAL C, 103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.04
    Polarity: 5.68
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100124 HIS C, 300122 ARG C, 300124 HIS C	2.24	0.8	-2.7	-0.32	35.66	87
    2	100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C	2.27	1.76	-2.9	-0.52	27.63	86
    3	300124 HIS C, 300119 GLN C, 100124 HIS C	2.42	6.07	-3.3	-0.19	35.58	88
    4	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C	3.24	6.93	-3.35	-0.42	27.57	87
    5	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	3.79	8.09	-3.38	-0.56	22.76	86
    6	100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C	4.15	8.7	-3.38	-0.56	22.76	86
    7	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	4.33	8.93	-3.38	-0.56	22.76	86
    8	300124 HIS C, 100124 HIS C, 124 HIS C, 200119 GLN C, 200124 HIS C	4.39	9.63	-3.26	-0.01	41.99	89
    9	300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 200119 GLN C	3.71	11.26	-3.44	-0.83	13.14	85
    10	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.67	16.88	-3.5	-1.1	3.53	84
    11	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C, 200115 VAL C	3	16.97	-1.96	-0.65	2.85	86
    12	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.91	17.15	2.66	0.68	0.81	95
    13	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.95	17.44	2.66	0.68	0.81	95
    14	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.8	18.73	-3.5	-1.1	3.53	84
    15	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.22	20.58	2.66	0.68	0.81	95
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.68	27.82	4.2	1.13	0.13	98
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.16	28.41	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	29.1	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.41	29.64	2.28	0.24	0.03	99
    20	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.24	31.21	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.26	32.23	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.76	34.49	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.12	35.44	1.36	-0.14	0.68	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.48	36.08	1.3	-0.14	0.33	101
    25	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.2	37.26	-0.2	-0.61	1.33	105
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.29	38.86	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.03	39.98	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.63	49.16	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	3.95	50.4	-0.64	-0.78	2	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C	4.52	50.76	0.34	-0.25	1.35	106
    31	200107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C	4.6	51.37	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 300107 THR C, 300100 ILE C, 100100 ILE C	4.59	51.8	1.38	0.26	1.05	105
    33	107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	4	52.7	1.44	0.26	1.39	105
    34	300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	3.88	52.85	1.98	0.51	1.33	104
    35	300104 GLY C, 300100 ILE C, 100100 ILE C, 300103 PHE C	3.55	53.27	2.85	1.04	1	85
    36	300104 GLY C, 300100 ILE C, 300103 PHE C	3.25	54.11	2.3	0.79	1.29	77
    37	107 THR C, 300104 GLY C, 300100 ILE C	1.83	57.3	1.13	0.08	1.72	105
    38	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.56	58.14	0.75	-0.14	2.14	105
    39	107 THR C, 300100 ILE C, 103 PHE C	1.44	59.8	1.13	0.08	1.72	105
    40	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.91	60.45	0.75	-0.14	2.14	105
    41	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.96	60.59	0.46	-0.41	2.39	102
    42	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.85	61.54	0.68	-0.31	2.14	102
    43	107 THR C, 300101 THR C, 106 VAL C	1.83	61.8	1.03	-0.15	1.72	102
    44	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.76	62.41	1.73	0.18	1.33	86
    45	106 VAL C, 110 LEU C, 300101 THR C	1.16	69.84	2.43	0.5	0.64	86
    46	106 VAL C, 110 LEU C, 300101 THR C, 26 TRP C	3.88	72.61	1.6	0.8	1.01	71
    47	106 VAL C, 300101 THR C, 26 TRP C, 33 THR C	6.07	73.44	0.48	0.33	1.39	84
    48	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C	2.92	79.95	1.75	0.18	0.9	102
    49	106 VAL C, 300101 THR C, 33 THR C, 300097 VAL C, 103 PHE C	2.86	80.3	1.96	0.41	0.79	92
    50	106 VAL C, 33 THR C, 300097 VAL C, 103 PHE C	2.77	80.87	2.63	0.71	0.57	88
    51	33 THR C, 300097 VAL C, 103 PHE C	2.72	82.73	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

50. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C, 300101 THR C, 26 TRP C, 110 LEU C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C, 300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C, 300107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C, 200124 HIS C

    Unique lining residues set - sidechains

    33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C, 300101 THR C, 26 TRP C, 110 LEU C, 107 THR C, 300100 ILE C, 300103 PHE C, 100100 ILE C, 300107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 100122 ARG C,

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.3
    Hydrophobicity: -0.02
    Polarity: 6.25
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	33 THR C, 103 PHE C, 300097 VAL C	2.71	2.19	2.1	0.57	0.71	85
    2	33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C	2.79	2.88	2.63	0.71	0.57	88
    3	33 THR C, 103 PHE C, 300097 VAL C, 106 VAL C, 300101 THR C	2.9	3.32	1.96	0.41	0.79	92
    4	33 THR C, 300097 VAL C, 106 VAL C, 300101 THR C	2.95	9.42	1.75	0.18	0.9	102
    5	33 THR C, 106 VAL C, 300101 THR C, 26 TRP C	6.13	10.33	0.48	0.33	1.39	84
    6	106 VAL C, 300101 THR C, 26 TRP C, 110 LEU C	4.04	13.61	1.6	0.8	1.01	71
    7	106 VAL C, 300101 THR C, 110 LEU C	1.23	20.49	2.43	0.5	0.64	86
    8	106 VAL C, 110 LEU C, 107 THR C, 300101 THR C	1.79	21.23	1.73	0.18	1.33	86
    9	106 VAL C, 107 THR C, 300101 THR C	1.85	21.52	1.03	-0.15	1.72	102
    10	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C	1.85	22.17	0.68	-0.31	2.14	102
    11	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.97	22.43	0.46	-0.41	2.39	102
    12	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.83	23.48	0.75	-0.14	2.14	105
    13	107 THR C, 103 PHE C, 300100 ILE C	1.5	24.96	1.13	0.08	1.72	105
    14	107 THR C, 103 PHE C, 300100 ILE C, 300104 GLY C	1.47	25.84	0.75	-0.14	2.14	105
    15	107 THR C, 300100 ILE C, 300104 GLY C	1.63	28.78	1.13	0.08	1.72	105
    16	300100 ILE C, 300104 GLY C, 300103 PHE C	3.18	29.52	2.3	0.79	1.29	77
    17	300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C	3.59	30.04	2.85	1.04	1	85
    18	300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	3.88	30.23	1.98	0.51	1.33	104
    19	107 THR C, 300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	3.99	31.19	1.44	0.26	1.39	105
    20	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.6	31.56	1.38	0.26	1.05	105
    21	300100 ILE C, 100100 ILE C, 100 ILE C, 200100 ILE C, 200107 THR C	4.59	32.48	3.46	1.29	0.44	103
    22	107 THR C, 300100 ILE C, 300107 THR C, 100107 THR C, 200107 THR C	4.46	33.09	0.34	-0.25	1.35	106
    23	107 THR C, 300104 GLY C, 300107 THR C, 100107 THR C, 200107 THR C	4.2	33.8	-0.64	-0.78	2	107
    24	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C	1.73	43.49	-0.7	-0.77	1.66	107
    25	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C, 100111 ALA C	1.91	44.34	-0.2	-0.61	1.33	105
    26	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	45.72	1.3	-0.14	0.33	101
    27	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C, 100111 ALA C	2.2	47.14	-0.2	-0.61	1.33	105
    28	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.3	48.09	1.3	-0.14	0.33	101
    29	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.17	49.23	1.36	-0.14	0.68	100
    30	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.81	51.44	1.8	0.02	0	100
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.01	52.19	2.28	0.24	0.03	99
    32	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.25	53.33	3.72	0.91	0.1	98
    33	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.42	53.75	2.28	0.24	0.03	99
    34	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	54.34	2.28	0.24	0.03	99
    35	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.24	55.8	3.72	0.91	0.1	98
    36	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.69	63.68	4.2	1.13	0.13	98
    37	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.54	64.84	2.66	0.68	0.81	95
    38	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.91	65.41	-3.5	-1.1	3.53	84
    39	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	65.54	-1.96	-0.65	2.85	86
    40	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.91	65.82	2.66	0.68	0.81	95
    41	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.98	65.91	-1.96	-0.65	2.85	86
    42	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.67	72.3	-3.5	-1.1	3.53	84
    43	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.87	73.45	-3.44	-0.83	13.14	85
    44	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.42	73.76	-3.26	-0.01	41.99	89
    45	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	73.8	-3.44	-0.83	13.14	85
    46	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.39	73.87	-3.38	-0.56	22.76	86
    47	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.33	74.11	-3.38	-0.56	22.76	86
    48	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.15	74.95	-3.38	-0.56	22.76	86
    49	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	3.94	76.45	-3.38	-0.56	22.76	86
    50	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	2.9	78.35	-3.35	-0.42	27.57	87
    51	100119 GLN C, 100124 HIS C, 200124 HIS C	2.41	81.29	-3.3	-0.19	35.58	88
    52	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.28	82.19	-2.9	-0.52	27.63	86
    53	100124 HIS C, 100122 ARG C, 200124 HIS C	2.24	82.77	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

51. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Unique lining residues set - sidechains

    122 ARG C, 124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 103 PHE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.02
    Polarity: 4.88
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	122 ARG C, 124 HIS C, 300124 HIS C	2.24	0.79	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.26	1.72	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.43	5.8	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	3.11	7.43	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	4.01	7.97	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.16	8.37	-3.38	-0.56	22.76	86
    7	124 HIS C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.2	9.13	-3.32	-0.28	32.37	88
    8	119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C	3.73	10.67	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.66	16.46	-3.5	-1.1	3.53	84
    10	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.99	16.54	-1.96	-0.65	2.85	86
    11	100119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.91	16.84	2.66	0.68	0.81	95
    12	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.95	17.02	-1.96	-0.65	2.85	86
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.9	17.7	-3.5	-1.1	3.53	84
    14	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.85	18.34	-1.96	-0.65	2.85	86
    15	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.22	20.18	2.66	0.68	0.81	95
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.67	27.17	4.2	1.13	0.13	98
    17	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.2	28.23	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.28	28.43	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.3	29.06	2.28	0.24	0.03	99
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 111 ALA C	2.32	29.51	3.72	0.91	0.1	98
    21	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300111 ALA C	2.22	30.27	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.09	32.18	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.84	34.37	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2	35.73	1.3	-0.14	0.33	101
    25	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.22	36.85	-0.2	-0.61	1.33	105
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.2	38.46	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.42	39.58	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.45	49.16	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.23	49.75	-0.64	-0.78	2	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.48	50.17	0.34	-0.25	1.35	106
    31	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.62	50.8	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.69	50.85	0.34	-0.25	1.35	106
    33	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.64	51.09	1.38	0.26	1.05	105
    34	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.65	51.28	1.38	0.26	1.05	105
    35	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.11	52.21	1.44	0.26	1.39	105
    36	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.85	52.53	1.98	0.51	1.33	104
    37	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.55	52.95	2.85	1.04	1	85
    38	100 ILE C, 104 GLY C, 103 PHE C	3.15	54.01	2.3	0.79	1.29	77
    39	200107 THR C, 100 ILE C, 104 GLY C	1.65	57.42	1.13	0.08	1.72	105
    40	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.44	58.21	0.75	-0.14	2.14	105
    41	200107 THR C, 100 ILE C, 200103 PHE C	1.48	59.32	1.13	0.08	1.72	105
    42	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.81	60.05	0.75	-0.14	2.14	105
    43	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.95	60.32	0.46	-0.41	2.39	102
    44	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.84	61.27	0.68	-0.31	2.14	102
    45	200107 THR C, 101 THR C, 200106 VAL C	1.85	61.52	1.03	-0.15	1.72	102
    46	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.78	62.11	1.73	0.18	1.33	86
    47	200106 VAL C, 200110 LEU C, 101 THR C	1.18	69.38	2.43	0.5	0.64	86
    48	200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C	3.73	72.46	1.6	0.8	1.01	71
    49	200106 VAL C, 101 THR C, 200026 TRP C, 200033 THR C	6.2	73.3	0.48	0.33	1.39	84
    50	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C	3.02	79.34	1.75	0.18	0.9	102
    51	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C, 200103 PHE C	2.9	79.73	1.96	0.41	0.79	92
    52	200106 VAL C, 200033 THR C, 97 VAL C, 200103 PHE C	2.75	80.61	2.63	0.71	0.57	88
    53	200033 THR C, 97 VAL C, 200103 PHE C	2.72	82.43	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

52. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 122 ARG C, 300124 HIS C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C, 122 ARG C,

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.02
    Polarity: 4.88
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.72	2.09	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.75	3.09	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.9	3.52	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	3.02	9.39	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.2	10.21	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	3.73	13.92	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.18	20.48	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.78	21.16	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.85	21.43	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.84	22.26	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.95	22.48	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.81	23.56	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.48	25.01	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.45	25.85	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.65	28.74	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.15	29.5	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.55	30.04	2.85	1.04	1	85
    18	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.85	30.43	1.98	0.51	1.33	104
    19	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.11	31.34	1.44	0.26	1.39	105
    20	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.65	31.46	1.38	0.26	1.05	105
    21	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	31.62	1.38	0.26	1.05	105
    22	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.69	31.69	0.34	-0.25	1.35	106
    23	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.62	32.68	3.46	1.29	0.44	103
    24	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.48	33.27	0.34	-0.25	1.35	106
    25	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.23	33.95	-0.64	-0.78	2	107
    26	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.45	43.97	-0.7	-0.77	1.66	107
    27	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	2.42	44.7	-0.2	-0.61	1.33	105
    28	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.2	45.94	1.3	-0.14	0.33	101
    29	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.22	47.22	-0.2	-0.61	1.33	105
    30	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2	49.12	1.3	-0.14	0.33	101
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.84	51.3	1.8	0.02	0	100
    32	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.09	52.68	2.28	0.24	0.03	99
    33	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.22	53.1	3.72	0.91	0.1	98
    34	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.32	53.64	3.72	0.91	0.1	98
    35	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.37	54	2.28	0.24	0.03	99
    36	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	54.61	2.28	0.24	0.03	99
    37	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.2	56.03	3.72	0.91	0.1	98
    38	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.67	63.22	4.2	1.13	0.13	98
    39	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.22	64.72	2.66	0.68	0.81	95
    40	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.85	65.06	-1.96	-0.65	2.85	86
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.9	65.59	-3.5	-1.1	3.53	84
    42	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.95	65.71	-1.96	-0.65	2.85	86
    43	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100119 GLN C	2.91	65.97	2.66	0.68	0.81	95
    44	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	66.06	-1.96	-0.65	2.85	86
    45	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.66	72.37	-3.5	-1.1	3.53	84
    46	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.73	73.6	-3.44	-0.83	13.14	85
    47	100119 GLN C, 200119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.2	74.16	-3.32	-0.28	32.37	88
    48	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.16	75	-3.38	-0.56	22.76	86
    49	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.01	75.75	-3.38	-0.56	22.76	86
    50	119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	3.11	77.54	-3.35	-0.42	27.57	87
    51	119 GLN C, 300124 HIS C, 124 HIS C	2.43	81.02	-3.3	-0.19	35.58	88
    52	119 GLN C, 124 HIS C, 122 ARG C, 300124 HIS C	2.26	81.87	-2.9	-0.52	27.63	86
    53	124 HIS C, 122 ARG C, 300124 HIS C	2.24	82.43	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

53. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C, 124 HIS C, 200122 ARG C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C, 200122 ARG C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0
    Polarity: 5.34
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.71	2.18	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.79	2.86	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.9	3.29	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	2.95	9.4	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.15	10.28	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	4.14	13.46	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.23	20.46	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.78	21.17	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.85	21.45	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.84	22.28	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.97	22.4	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.88	23.33	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.46	25.59	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.56	26.46	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.88	28.94	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.28	29.51	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.57	29.98	2.85	1.04	1	85
    18	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.82	30.37	1.98	0.51	1.33	104
    19	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.07	31.32	1.44	0.26	1.39	105
    20	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.64	31.45	1.38	0.26	1.05	105
    21	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	31.62	1.38	0.26	1.05	105
    22	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.69	31.7	0.34	-0.25	1.35	106
    23	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.65	32.38	3.46	1.29	0.44	103
    24	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.57	32.91	0.34	-0.25	1.35	106
    25	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.07	34.29	-0.64	-0.78	2	107
    26	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	2.6	36.43	-0.7	-0.77	1.66	107
    27	300107 THR C, 100107 THR C, 107 THR C	2.97	36.76	-0.7	-0.77	1.66	107
    28	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.65	44.11	-0.7	-0.77	1.66	107
    29	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	2.02	44.78	-0.2	-0.61	1.33	105
    30	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	46.09	1.3	-0.14	0.33	101
    31	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.21	47.73	-0.2	-0.61	1.33	105
    32	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.34	48.77	1.3	-0.14	0.33	101
    33	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.8	52.02	1.8	0.02	0	100
    34	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.16	52.64	2.28	0.24	0.03	99
    35	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.25	53.1	3.72	0.91	0.1	98
    36	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.28	53.66	3.72	0.91	0.1	98
    37	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.38	54.02	2.28	0.24	0.03	99
    38	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.27	54.75	2.28	0.24	0.03	99
    39	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.12	56.28	3.72	0.91	0.1	98
    40	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	64.09	4.2	1.13	0.13	98
    41	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.65	64.77	2.66	0.68	0.81	95
    42	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.93	65.12	-1.96	-0.65	2.85	86
    43	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.91	65.67	-3.5	-1.1	3.53	84
    44	300115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.97	65.78	-0.42	-0.21	2.17	89
    45	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	66.07	2.66	0.68	0.81	95
    46	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.98	66.16	-1.96	-0.65	2.85	86
    47	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.66	72.58	-3.5	-1.1	3.53	84
    48	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C	3.89	73.7	-3.44	-0.83	13.14	85
    49	300119 GLN C, 124 HIS C, 100124 HIS C, 200124 HIS C, 300124 HIS C	4.4	74.03	-3.26	-0.01	41.99	89
    50	119 GLN C, 100119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	4.33	74.3	-3.38	-0.56	22.76	86
    51	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.16	75.17	-3.38	-0.56	22.76	86
    52	119 GLN C, 100119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	3.91	76.69	-3.38	-0.56	22.76	86
    53	119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	2.88	78.58	-3.35	-0.42	27.57	87
    54	200119 GLN C, 124 HIS C, 200124 HIS C	2.41	81.49	-3.3	-0.19	35.58	88
    55	200119 GLN C, 200124 HIS C, 124 HIS C, 200122 ARG C	2.27	82.38	-2.9	-0.52	27.63	86
    56	200124 HIS C, 124 HIS C, 200122 ARG C	2.24	82.96	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

54. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Unique lining residues set - sidechains

    200122 ARG C, 200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 103 PHE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0
    Polarity: 5.34
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.24	0.82	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.27	1.81	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.41	5.32	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	2.88	7.12	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	3.91	8.17	-3.38	-0.56	22.76	86
    6	119 GLN C, 100119 GLN C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.16	8.76	-3.38	-0.56	22.76	86
    7	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.33	9	-3.38	-0.56	22.76	86
    8	200124 HIS C, 124 HIS C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.4	9.48	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.89	10.99	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.66	16.89	-3.5	-1.1	3.53	84
    11	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 200115 VAL C	2.98	16.98	-1.96	-0.65	2.85	86
    12	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.9	17.29	2.66	0.68	0.81	95
    13	119 GLN C, 100119 GLN C, 300119 GLN C, 200115 VAL C, 300115 VAL C	2.97	17.47	-0.42	-0.21	2.17	89
    14	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.91	18.19	-3.5	-1.1	3.53	84
    15	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 200115 VAL C	2.93	18.86	-1.96	-0.65	2.85	86
    16	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.65	19.78	2.66	0.68	0.81	95
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.7	27.5	4.2	1.13	0.13	98
    18	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.12	28.68	3.72	0.91	0.1	98
    19	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.35	28.94	2.28	0.24	0.03	99
    20	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	29.58	2.28	0.24	0.03	99
    21	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.28	30.03	3.72	0.91	0.1	98
    22	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.25	30.94	3.72	0.91	0.1	98
    23	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	31.89	2.28	0.24	0.03	99
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.8	35.22	1.8	0.02	0	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.34	35.97	1.3	-0.14	0.33	101
    26	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.21	37.23	-0.2	-0.61	1.33	105
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.29	38.84	1.3	-0.14	0.33	101
    28	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.02	39.95	-0.2	-0.61	1.33	105
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.65	46.53	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 300107 THR C	2.97	46.8	-0.7	-0.77	1.66	107
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.6	49.38	-0.7	-0.77	1.66	107
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.07	50.57	-0.64	-0.78	2	107
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.57	50.87	0.34	-0.25	1.35	106
    34	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.65	51.34	3.46	1.29	0.44	103
    35	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.69	51.38	0.34	-0.25	1.35	106
    36	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.64	51.64	1.38	0.26	1.05	105
    37	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.64	51.84	1.38	0.26	1.05	105
    38	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.07	52.8	1.44	0.26	1.39	105
    39	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.82	53.12	1.98	0.51	1.33	104
    40	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.57	53.48	2.85	1.04	1	85
    41	100 ILE C, 104 GLY C, 103 PHE C	3.28	54.26	2.3	0.79	1.29	77
    42	200107 THR C, 100 ILE C, 104 GLY C	1.88	57.36	1.13	0.08	1.72	105
    43	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.56	58.24	0.75	-0.14	2.14	105
    44	200107 THR C, 100 ILE C, 200103 PHE C	1.46	60	1.13	0.08	1.72	105
    45	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.88	60.68	0.75	-0.14	2.14	105
    46	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.97	60.82	0.46	-0.41	2.39	102
    47	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.84	61.79	0.68	-0.31	2.14	102
    48	200107 THR C, 101 THR C, 200106 VAL C	1.85	62.05	1.03	-0.15	1.72	102
    49	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.78	62.68	1.73	0.18	1.33	86
    50	200106 VAL C, 200110 LEU C, 101 THR C	1.23	70.38	2.43	0.5	0.64	86
    51	200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C	4.14	72.94	1.6	0.8	1.01	71
    52	200106 VAL C, 101 THR C, 200026 TRP C, 200033 THR C	6.15	73.82	0.48	0.33	1.39	84
    53	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C	2.95	80.1	1.75	0.18	0.9	102
    54	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C, 200103 PHE C	2.9	80.47	1.96	0.41	0.79	92
    55	200106 VAL C, 200033 THR C, 97 VAL C, 200103 PHE C	2.79	81.05	2.63	0.71	0.57	88
    56	200033 THR C, 97 VAL C, 200103 PHE C	2.71	82.96	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum

55. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C, 100124 HIS C, 300122 ARG C

    Unique lining residues set - sidechains

    100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C, 300107 THR C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C, 300122 ARG C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.02
    Polarity: 5.25
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100097 VAL C, 300033 THR C, 300103 PHE C	2.71	2.18	2.1	0.57	0.71	85
    2	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C	2.79	2.86	2.63	0.71	0.57	88
    3	100097 VAL C, 300033 THR C, 300103 PHE C, 300106 VAL C, 100101 THR C	2.9	3.29	1.96	0.41	0.79	92
    4	100097 VAL C, 300033 THR C, 300106 VAL C, 100101 THR C	2.95	9.4	1.75	0.18	0.9	102
    5	300033 THR C, 300106 VAL C, 100101 THR C, 300026 TRP C	6.15	10.28	0.48	0.33	1.39	84
    6	300106 VAL C, 100101 THR C, 300026 TRP C, 300110 LEU C	4.14	13.46	1.6	0.8	1.01	71
    7	300106 VAL C, 100101 THR C, 300110 LEU C	1.23	20.46	2.43	0.5	0.64	86
    8	300106 VAL C, 300110 LEU C, 100101 THR C, 300107 THR C	1.78	21.17	1.73	0.18	1.33	86
    9	300106 VAL C, 100101 THR C, 300107 THR C	1.85	21.45	1.03	-0.15	1.72	102
    10	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C	1.84	22.28	0.68	-0.31	2.14	102
    11	300106 VAL C, 100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.97	22.4	0.46	-0.41	2.39	102
    12	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.88	23.33	0.75	-0.14	2.14	105
    13	300107 THR C, 300103 PHE C, 100100 ILE C	1.46	25.59	1.13	0.08	1.72	105
    14	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.56	26.46	0.75	-0.14	2.14	105
    15	300107 THR C, 100100 ILE C, 100104 GLY C	1.88	28.94	1.13	0.08	1.72	105
    16	100100 ILE C, 100104 GLY C, 100103 PHE C	3.28	29.51	2.3	0.79	1.29	77
    17	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.57	29.98	2.85	1.04	1	85
    18	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.82	30.37	1.98	0.51	1.33	104
    19	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.07	31.32	1.44	0.26	1.39	105
    20	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.64	31.45	1.38	0.26	1.05	105
    21	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	31.62	1.38	0.26	1.05	105
    22	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.69	31.7	0.34	-0.25	1.35	106
    23	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.65	32.38	3.46	1.29	0.44	103
    24	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.57	32.91	0.34	-0.25	1.35	106
    25	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.07	34.29	-0.64	-0.78	2	107
    26	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	2.6	36.43	-0.7	-0.77	1.66	107
    27	300107 THR C, 100107 THR C, 107 THR C	2.97	36.76	-0.7	-0.77	1.66	107
    28	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.65	44.11	-0.7	-0.77	1.66	107
    29	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	2.02	44.78	-0.2	-0.61	1.33	105
    30	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	46.09	1.3	-0.14	0.33	101
    31	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.21	47.73	-0.2	-0.61	1.33	105
    32	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.34	48.77	1.3	-0.14	0.33	101
    33	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.8	52.02	1.8	0.02	0	100
    34	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.16	52.64	2.28	0.24	0.03	99
    35	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.25	53.1	3.72	0.91	0.1	98
    36	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.28	53.66	3.72	0.91	0.1	98
    37	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.38	54.02	2.28	0.24	0.03	99
    38	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.27	54.75	2.28	0.24	0.03	99
    39	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.12	56.28	3.72	0.91	0.1	98
    40	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	64.09	4.2	1.13	0.13	98
    41	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.65	64.77	2.66	0.68	0.81	95
    42	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.93	65.12	-1.96	-0.65	2.85	86
    43	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.91	65.67	-3.5	-1.1	3.53	84
    44	300115 VAL C, 200115 VAL C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.97	65.78	-0.42	-0.21	2.17	89
    45	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.93	65.83	2.66	0.68	0.81	95
    46	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.9	66.07	2.66	0.68	0.81	95
    47	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.98	66.16	-1.96	-0.65	2.85	86
    48	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.66	72.58	-3.5	-1.1	3.53	84
    49	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C	3.89	73.7	-3.44	-0.83	13.14	85
    50	200119 GLN C, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C	4.4	74.03	-3.26	-0.01	41.99	89
    51	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.33	74.3	-3.38	-0.56	22.76	86
    52	119 GLN C, 100119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	4.16	75.17	-3.38	-0.56	22.76	86
    53	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	3.91	76.69	-3.38	-0.56	22.76	86
    54	100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	2.88	78.58	-3.35	-0.42	27.57	87
    55	300119 GLN C, 100124 HIS C, 300124 HIS C	2.41	81.49	-3.3	-0.19	35.58	88
    56	300119 GLN C, 300124 HIS C, 100124 HIS C, 300122 ARG C	2.27	82.38	-2.9	-0.52	27.63	86
    57	300124 HIS C, 100124 HIS C, 300122 ARG C	2.24	82.96	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

56. show pore | cavity 2 | profile | lining residues
    

    Unique lining residues set - all

    100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Unique lining residues set - sidechains

    300122 ARG C, 300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C, 103 PHE C, 200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C, 200033 THR C, 97 VAL C, 200103 PHE C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.02
    Polarity: 5.25
    Mutability: 91
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100124 HIS C, 300122 ARG C, 300124 HIS C	2.24	0.82	-2.7	-0.32	35.66	87
    2	100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C	2.27	1.81	-2.9	-0.52	27.63	86
    3	300124 HIS C, 300119 GLN C, 100124 HIS C	2.41	5.32	-3.3	-0.19	35.58	88
    4	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C	2.88	7.12	-3.35	-0.42	27.57	87
    5	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	3.91	8.17	-3.38	-0.56	22.76	86
    6	100119 GLN C, 119 GLN C, 124 HIS C, 200119 GLN C, 200124 HIS C	4.16	8.76	-3.38	-0.56	22.76	86
    7	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	4.33	9	-3.38	-0.56	22.76	86
    8	300124 HIS C, 100124 HIS C, 124 HIS C, 200119 GLN C, 200124 HIS C	4.4	9.48	-3.26	-0.01	41.99	89
    9	300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 200119 GLN C	3.89	10.99	-3.44	-0.83	13.14	85
    10	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.66	16.89	-3.5	-1.1	3.53	84
    11	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C, 200115 VAL C	2.98	16.98	-1.96	-0.65	2.85	86
    12	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.9	17.17	2.66	0.68	0.81	95
    13	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.93	17.29	2.66	0.68	0.81	95
    14	300119 GLN C, 100119 GLN C, 119 GLN C, 200115 VAL C, 300115 VAL C	2.97	17.47	-0.42	-0.21	2.17	89
    15	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.91	18.19	-3.5	-1.1	3.53	84
    16	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C, 300115 VAL C	2.93	18.86	-1.96	-0.65	2.85	86
    17	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.65	19.78	2.66	0.68	0.81	95
    18	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.7	27.5	4.2	1.13	0.13	98
    19	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.12	28.68	3.72	0.91	0.1	98
    20	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.35	28.94	2.28	0.24	0.03	99
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	29.58	2.28	0.24	0.03	99
    22	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.28	30.03	3.72	0.91	0.1	98
    23	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.25	30.94	3.72	0.91	0.1	98
    24	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	31.89	2.28	0.24	0.03	99
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.8	35.22	1.8	0.02	0	100
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.34	35.97	1.3	-0.14	0.33	101
    27	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.21	37.23	-0.2	-0.61	1.33	105
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.29	38.84	1.3	-0.14	0.33	101
    29	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.02	39.95	-0.2	-0.61	1.33	105
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.65	46.53	-0.7	-0.77	1.66	107
    31	107 THR C, 100107 THR C, 300107 THR C	2.97	46.8	-0.7	-0.77	1.66	107
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.6	49.38	-0.7	-0.77	1.66	107
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.07	50.57	-0.64	-0.78	2	107
    34	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.57	50.87	0.34	-0.25	1.35	106
    35	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.65	51.34	3.46	1.29	0.44	103
    36	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.69	51.38	0.34	-0.25	1.35	106
    37	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.64	51.64	1.38	0.26	1.05	105
    38	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.64	51.84	1.38	0.26	1.05	105
    39	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.07	52.8	1.44	0.26	1.39	105
    40	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.82	53.12	1.98	0.51	1.33	104
    41	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.57	53.48	2.85	1.04	1	85
    42	100 ILE C, 104 GLY C, 103 PHE C	3.28	54.26	2.3	0.79	1.29	77
    43	200107 THR C, 100 ILE C, 104 GLY C	1.88	57.36	1.13	0.08	1.72	105
    44	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.56	58.24	0.75	-0.14	2.14	105
    45	200107 THR C, 100 ILE C, 200103 PHE C	1.46	60	1.13	0.08	1.72	105
    46	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.88	60.68	0.75	-0.14	2.14	105
    47	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.97	60.82	0.46	-0.41	2.39	102
    48	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.84	61.79	0.68	-0.31	2.14	102
    49	200107 THR C, 101 THR C, 200106 VAL C	1.85	62.05	1.03	-0.15	1.72	102
    50	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.78	62.68	1.73	0.18	1.33	86
    51	200106 VAL C, 200110 LEU C, 101 THR C	1.23	70.38	2.43	0.5	0.64	86
    52	200106 VAL C, 200110 LEU C, 101 THR C, 200026 TRP C	4.14	72.94	1.6	0.8	1.01	71
    53	200106 VAL C, 101 THR C, 200026 TRP C, 200033 THR C	6.15	73.82	0.48	0.33	1.39	84
    54	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C	2.95	80.1	1.75	0.18	0.9	102
    55	200106 VAL C, 101 THR C, 200033 THR C, 97 VAL C, 200103 PHE C	2.9	80.47	1.96	0.41	0.79	92
    56	200106 VAL C, 200033 THR C, 97 VAL C, 200103 PHE C	2.79	81.05	2.63	0.71	0.57	88
    57	200033 THR C, 97 VAL C, 200103 PHE C	2.71	82.96	2.1	0.57	0.71	85

    pore with bottle neck

    pore with local minimum