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

show all | hide all

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

   300028 SER B, 300030 GLY B, 100082 TYR C, 300058 GLN C, 300092 ASN B, 100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B, 300031 THR B, 100084 VAL C, 300050 TYR B, 300053 GLU B, 100085 THR C, 100085 THR C, 100054 ALA C, 100053 GLY C, 100057 ARG A

   Unique lining residues set - sidechains

   300028 SER B, 100082 TYR C, 300058 GLN C, 300092 ASN B, 100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B, 300050 TYR B, 300053 GLU B, 100085 THR C, 100054 ALA C, 100057 ARG A

   Physicochemical properties of lining side-chains

   Charge: 0 (2-2)
   Hydropathy: -1.4
   Hydrophobicity: -0.41
   Polarity: 17.4
   Mutability: 88
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	300028 SER B, 300030 GLY B, 100082 TYR C, 300058 GLN C	3.26	0.48	-1.5	-0.44	2.55	83
   2	300030 GLY B, 100082 TYR C, 300058 GLN C, 300092 ASN B	3.15	2.57	-2.18	-0.39	2.98	79
   3	300030 GLY B, 100082 TYR C, 300092 ASN B	3.26	2.98	-1.73	-0.15	2.79	77
   4	300030 GLY B, 100082 TYR C, 300092 ASN B, 100084 VAL C	3.27	3.46	-0.25	0.17	2.13	84
   5	300030 GLY B, 100082 TYR C, 300092 ASN B, 100084 VAL C, 300064 ARG C	3.24	3.64	-1.1	0.05	12.1	83
   6	300030 GLY B, 300092 ASN B, 100084 VAL C, 300064 ARG C, 300032 ASP B	3.07	5	-1.54	-0.38	21.72	92
   7	300030 GLY B, 100084 VAL C, 300064 ARG C, 300032 ASP B	2.99	6.01	-1.05	-0.28	26.3	89
   8	300030 GLY B, 100084 VAL C, 300064 ARG C	2.95	6.13	-0.23	-0.03	18.5	90
   9	300030 GLY B, 100084 VAL C, 300064 ARG C, 300031 THR B	2.94	6.25	-0.35	-0.22	14.29	96
   10	300030 GLY B, 300064 ARG C, 300031 THR B	2.98	6.29	-1.87	-0.66	19.01	95
   11	300030 GLY B, 300064 ARG C, 300032 ASP B, 300031 THR B	2.94	6.33	-2.2	-0.77	27.12	84
   12	300030 GLY B, 300064 ARG C, 300031 THR B	2.97	6.42	-1.87	-0.66	19.01	95
   13	100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B	2.97	6.59	-1.13	-0.28	25.87	93
   14	100084 VAL C, 300064 ARG C, 300031 THR B	2.85	6.85	-0.33	-0.02	17.93	96
   15	100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B	2.7	7.24	-1.13	-0.28	25.87	93
   16	100084 VAL C, 300064 ARG C, 300031 THR B	2.58	7.81	-0.33	-0.02	17.93	96
   17	100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B	2.41	10.47	-1.13	-0.28	25.87	93
   18	300064 ARG C, 300032 ASP B, 300031 THR B, 100084 VAL C	2.54	11.3	-2.28	-0.76	26.69	92
   19	300064 ARG C, 300032 ASP B, 300031 THR B, 100084 VAL C, 300050 TYR B	2.83	11.89	-2.08	-0.38	21.67	81
   20	300064 ARG C, 300031 THR B, 100084 VAL C, 300050 TYR B	2.84	12.2	-1.73	-0.22	14.66	80
   21	300064 ARG C, 300031 THR B, 300050 TYR B	2.74	12.32	-2.17	-0.03	18.42	80
   22	300031 THR B, 300050 TYR B, 300053 GLU B	2.75	12.49	-1.83	-0.27	17.72	78
   23	300031 THR B, 100084 VAL C, 300050 TYR B, 300053 GLU B	2.85	13.91	-1.48	-0.4	14.14	78
   24	300031 THR B, 100084 VAL C, 300050 TYR B, 300053 GLU B, 100085 THR C	3.07	14.5	-1.26	-0.48	11.99	78
   25	300031 THR B, 100084 VAL C, 300053 GLU B, 100085 THR C	3.12	15.23	-1.33	-0.87	14.15	97
   26	300031 THR B, 100084 VAL C, 300053 GLU B, 100085 THR C, 100054 ALA C	3.01	16.52	-0.7	-0.69	11.32	97
   27	300031 THR B, 300053 GLU B, 100085 THR C, 100054 ALA C	2.9	17.34	-0.78	-0.67	13.31	97
   28	300053 GLU B, 100085 THR C, 100054 ALA C	2.86	18.2	-0.8	-0.63	17.19	94
   29	300053 GLU B, 100085 THR C, 100054 ALA C, 100053 GLY C	2.98	20.16	-0.7	-0.67	13.74	94
   30	300053 GLU B, 100085 THR C, 100054 ALA C, 100053 GLY C, 100057 ARG A	3.59	20.54	-1.46	-0.62	21.39	91
   31	300053 GLU B, 100085 THR C, 100053 GLY C, 100057 ARG A	3.8	21.14	-2.28	-0.78	26.74	89
   32	300053 GLU B, 100053 GLY C, 100057 ARG A	3.81	21.98	-2.8	-0.79	35.09	80

   pore with bottle neck

   pore with local minimum

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

   Unique lining residues set - all

   200028 SER B, 200030 GLY B, 82 TYR C, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B, 85 THR C, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A

   Unique lining residues set - sidechains

   200028 SER B, 82 TYR C, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200050 TYR B, 200053 GLU B, 85 THR C, 54 ALA C, 57 ARG A

   Physicochemical properties of lining side-chains

   Charge: 0 (2-2)
   Hydropathy: -1.4
   Hydrophobicity: -0.41
   Polarity: 17.4
   Mutability: 88
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	200028 SER B, 200030 GLY B, 82 TYR C, 200058 GLN C	3.26	0.48	-1.5	-0.44	2.55	83
   2	200030 GLY B, 82 TYR C, 200058 GLN C, 200092 ASN B	3.15	2.57	-2.18	-0.39	2.98	79
   3	200030 GLY B, 82 TYR C, 200092 ASN B	3.26	2.98	-1.73	-0.15	2.79	77
   4	200030 GLY B, 82 TYR C, 200092 ASN B, 84 VAL C	3.27	3.46	-0.25	0.17	2.13	84
   5	200030 GLY B, 82 TYR C, 200092 ASN B, 84 VAL C, 200064 ARG C	3.24	3.64	-1.1	0.05	12.1	83
   6	200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B	3.07	5	-1.54	-0.38	21.72	92
   7	200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B	2.99	6.01	-1.05	-0.28	26.3	89
   8	200030 GLY B, 84 VAL C, 200064 ARG C	2.95	6.13	-0.23	-0.03	18.5	90
   9	200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B	2.94	6.25	-0.35	-0.22	14.29	96
   10	200030 GLY B, 200064 ARG C, 200031 THR B	2.98	6.29	-1.87	-0.66	19.01	95
   11	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	2.94	6.33	-2.2	-0.77	27.12	84
   12	200030 GLY B, 200064 ARG C, 200031 THR B	2.97	6.42	-1.87	-0.66	19.01	95
   13	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.97	6.59	-1.13	-0.28	25.87	93
   14	84 VAL C, 200064 ARG C, 200031 THR B	2.85	6.85	-0.33	-0.02	17.93	96
   15	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.7	7.24	-1.13	-0.28	25.87	93
   16	84 VAL C, 200064 ARG C, 200031 THR B	2.58	7.81	-0.33	-0.02	17.93	96
   17	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.41	10.47	-1.13	-0.28	25.87	93
   18	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C	2.54	11.3	-2.28	-0.76	26.69	92
   19	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 200050 TYR B	2.83	11.89	-2.08	-0.38	21.67	81
   20	200064 ARG C, 200031 THR B, 84 VAL C, 200050 TYR B	2.84	12.2	-1.73	-0.22	14.66	80
   21	200064 ARG C, 200031 THR B, 200050 TYR B	2.74	12.32	-2.17	-0.03	18.42	80
   22	200031 THR B, 200050 TYR B, 200053 GLU B	2.75	12.49	-1.83	-0.27	17.72	78
   23	200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B	2.85	13.91	-1.48	-0.4	14.14	78
   24	200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B, 85 THR C	3.07	14.5	-1.26	-0.48	11.99	78
   25	200031 THR B, 84 VAL C, 200053 GLU B, 85 THR C	3.12	15.23	-1.33	-0.87	14.15	97
   26	200031 THR B, 84 VAL C, 200053 GLU B, 85 THR C, 54 ALA C	3.01	16.52	-0.7	-0.69	11.32	97
   27	200031 THR B, 200053 GLU B, 85 THR C, 54 ALA C	2.9	17.34	-0.78	-0.67	13.31	97
   28	200053 GLU B, 85 THR C, 54 ALA C	2.86	18.2	-0.8	-0.63	17.19	94
   29	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C	2.98	20.16	-0.7	-0.67	13.74	94
   30	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A	3.59	20.54	-1.46	-0.62	21.39	91
   31	200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A	3.8	21.14	-2.28	-0.78	26.74	89
   32	200053 GLU B, 53 GLY C, 57 ARG A	3.81	21.98	-2.8	-0.79	35.09	80

   pore with bottle neck

   pore with local minimum

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

   Unique lining residues set - all

   100028 SER B, 100030 GLY B, 100058 GLN C, 200082 TYR C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B, 200085 THR C, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A

   Unique lining residues set - sidechains

   100028 SER B, 100058 GLN C, 200082 TYR C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100050 TYR B, 100053 GLU B, 200085 THR C, 200054 ALA C, 200057 ARG A

   Physicochemical properties of lining side-chains

   Charge: 0 (2-2)
   Hydropathy: -1.4
   Hydrophobicity: -0.41
   Polarity: 17.4
   Mutability: 88
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100028 SER B, 100030 GLY B, 100058 GLN C, 200082 TYR C	3.26	0.48	-1.5	-0.44	2.55	83
   2	100030 GLY B, 100058 GLN C, 200082 TYR C, 100092 ASN B	3.15	2.57	-2.18	-0.39	2.98	79
   3	100030 GLY B, 200082 TYR C, 100092 ASN B	3.26	2.98	-1.73	-0.15	2.79	77
   4	100030 GLY B, 200082 TYR C, 100092 ASN B, 200084 VAL C	3.27	3.46	-0.25	0.17	2.13	84
   5	100030 GLY B, 200082 TYR C, 100092 ASN B, 200084 VAL C, 100064 ARG C	3.24	3.64	-1.1	0.05	12.1	83
   6	100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B	3.07	5	-1.54	-0.38	21.72	92
   7	100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B	2.99	6.01	-1.05	-0.28	26.3	89
   8	100030 GLY B, 200084 VAL C, 100064 ARG C	2.95	6.13	-0.23	-0.03	18.5	90
   9	100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B	2.94	6.25	-0.35	-0.22	14.29	96
   10	100030 GLY B, 100064 ARG C, 100031 THR B	2.98	6.29	-1.87	-0.66	19.01	95
   11	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	2.94	6.33	-2.2	-0.77	27.12	84
   12	100030 GLY B, 100064 ARG C, 100031 THR B	2.97	6.42	-1.87	-0.66	19.01	95
   13	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.97	6.59	-1.13	-0.28	25.87	93
   14	200084 VAL C, 100064 ARG C, 100031 THR B	2.85	6.85	-0.33	-0.02	17.93	96
   15	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.7	7.24	-1.13	-0.28	25.87	93
   16	200084 VAL C, 100064 ARG C, 100031 THR B	2.58	7.81	-0.33	-0.02	17.93	96
   17	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.41	10.47	-1.13	-0.28	25.87	93
   18	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C	2.54	11.3	-2.28	-0.76	26.69	92
   19	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 100050 TYR B	2.83	11.89	-2.08	-0.38	21.67	81
   20	100064 ARG C, 100031 THR B, 200084 VAL C, 100050 TYR B	2.84	12.2	-1.73	-0.22	14.66	80
   21	100064 ARG C, 100031 THR B, 100050 TYR B	2.74	12.32	-2.17	-0.03	18.42	80
   22	100031 THR B, 100050 TYR B, 100053 GLU B	2.75	12.49	-1.83	-0.27	17.72	78
   23	100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B	2.85	13.91	-1.48	-0.4	14.14	78
   24	100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B, 200085 THR C	3.07	14.5	-1.26	-0.48	11.99	78
   25	100031 THR B, 200084 VAL C, 100053 GLU B, 200085 THR C	3.12	15.23	-1.33	-0.87	14.15	97
   26	100031 THR B, 200084 VAL C, 100053 GLU B, 200085 THR C, 200054 ALA C	3.01	16.52	-0.7	-0.69	11.32	97
   27	100031 THR B, 100053 GLU B, 200085 THR C, 200054 ALA C	2.9	17.34	-0.78	-0.67	13.31	97
   28	100053 GLU B, 200085 THR C, 200054 ALA C	2.86	18.2	-0.8	-0.63	17.19	94
   29	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C	2.98	20.16	-0.7	-0.67	13.74	94
   30	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A	3.59	20.54	-1.46	-0.62	21.39	91
   31	100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A	3.8	21.14	-2.28	-0.78	26.74	89
   32	100053 GLU B, 200053 GLY C, 200057 ARG A	3.81	21.98	-2.8	-0.79	35.09	80

   pore with bottle neck

   pore with local minimum

4. 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

5. 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

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

   Unique lining residues set - all

   100046 GLU A, 100061 ASN A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100064 ILE A, 300020 SER B, 100063 LYS A, 300018 ARG B, 100040 ARG A, 100088 SER A, 100091 SER A, 100091 SER A, 100041 PRO A, 100088 SER A, 100175 LEU A, 100180 TYR A, 100173 ALA A, 100153 GLU A, 100172 PRO A, 100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A, 100170 THR A, 100155 VAL A, 100156 THR A, 100157 VAL A, 100040 THR B

   Unique lining residues set - sidechains

   100046 GLU A, 100061 ASN A, 100063 LYS A, 100003 LEU B, 100064 ILE A, 300020 SER B, 300018 ARG B, 100040 ARG A, 100091 SER A, 100041 PRO A, 100088 SER A, 100175 LEU A, 100180 TYR A, 100153 GLU A, 100172 PRO A, 100041 ASN B, 100182 LEU A, 100170 THR A, 100156 THR A,

   Physicochemical properties of lining side-chains

   Charge: 1 (3-2)
   Hydropathy: -1.2
   Hydrophobicity: -0.36
   Polarity: 12.09
   Mutability: 84
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	100046 GLU A, 100061 ASN A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.26	1.13	-1.5	-0.4	21.26	76
   2	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.28	2.22	-1	-0.3	25.73	67
   3	100046 GLU A, 100063 LYS A, 100003 LEU B, 100064 ILE A	4.39	5.15	0.23	0.35	24.92	76
   4	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	5.72	6.18	-1.1	-0.35	25.3	80
   5	100046 GLU A, 100063 LYS A, 100064 ILE A	2.91	11.16	-0.97	0.09	33.18	84
   6	100046 GLU A, 100064 ILE A, 100063 LYS A	3.3	11.82	0.2	-0.04	17.8	90
   7	100046 GLU A, 100064 ILE A, 100063 LYS A, 300018 ARG B	3.62	14.5	-0.98	-0.14	26.35	87
   8	100046 GLU A, 100064 ILE A, 300018 ARG B	3.63	14.98	-1.17	0.08	34.01	87
   9	100046 GLU A, 100064 ILE A, 300018 ARG B, 100040 ARG A	3.53	18.3	-2	-0.04	38.51	86
   10	100046 GLU A, 300018 ARG B, 100040 ARG A	4	20.56	-4.17	-0.66	51.3	81
   11	100046 GLU A, 100064 ILE A, 100040 ARG A	4.06	21.34	-1.17	0.08	34.01	87
   12	100046 GLU A, 100040 ARG A	2.89	24.13	-4	-0.78	50.95	80
   13	100040 ARG A	-0.27	30.72	-4.5	-0.42	52	83
   14	100040 ARG A, 100088 SER A	1.51	31.47	-2.45	-0.61	27.69	83
   15	100040 ARG A, 100088 SER A, 100091 SER A	2.16	32.2	-1.77	-0.67	19.59	83
   16	100040 ARG A, 100088 SER A, 100091 SER A	2.32	32.39	-1.9	-0.73	19.02	100
   17	100040 ARG A, 100088 SER A, 100091 SER A, 100041 PRO A	2.48	32.62	-1.83	-0.57	14.66	86
   18	100040 ARG A, 100088 SER A, 100091 SER A, 100041 PRO A	2.71	33.23	-1.73	-0.53	15.09	70
   19	100040 ARG A, 100088 SER A, 100041 PRO A	3.01	35.82	-2.17	-0.44	18.99	70
   20	100040 ARG A, 100041 PRO A, 100088 SER A	4.49	37.87	-2.3	-0.49	18.42	86
   21	100041 PRO A, 100088 SER A	4.81	39.01	-1.2	-0.53	1.63	87
   22	100091 SER A, 100041 PRO A, 100088 SER A	4.57	39.81	-1.07	-0.68	1.64	97
   23	100091 SER A, 100041 PRO A, 100088 SER A, 100175 LEU A	4.53	40.44	0.15	-0.22	1.26	86
   24	100041 PRO A, 100088 SER A, 100175 LEU A, 100180 TYR A	4.56	40.65	0.02	0.3	1.25	69
   25	100091 SER A, 100088 SER A, 100175 LEU A, 100180 TYR A	4.34	40.98	0.23	0.08	1.27	84
   26	100091 SER A, 100088 SER A, 100180 TYR A	4.07	41.15	-0.97	-0.28	1.65	94
   27	100091 SER A, 100088 SER A	4.13	41.29	-0.8	-0.97	1.67	117
   28	100091 SER A, 100088 SER A, 100180 TYR A	4.3	41.6	-0.97	-0.28	1.65	94
   29	100091 SER A, 100088 SER A, 100175 LEU A, 100180 TYR A	4.4	42.1	0.23	0.08	1.27	84
   30	100088 SER A, 100091 SER A, 100041 PRO A, 100175 LEU A, 100180 TYR A	4.35	42.78	-0.06	0.08	1.67	69
   31	100041 PRO A, 100175 LEU A, 100180 TYR A	4.04	47.08	0.3	0.72	1.11	54
   32	100041 PRO A, 100175 LEU A, 100180 TYR A, 100173 ALA A	4.46	47.41	0.13	0.34	1.68	54
   33	100041 PRO A, 100175 LEU A, 100180 TYR A	4.37	48.04	0.3	0.72	1.11	54
   34	100041 PRO A, 100175 LEU A, 100180 TYR A, 100173 ALA A	4.44	48.64	0.13	0.34	1.68	54
   35	100041 PRO A, 100180 TYR A, 100173 ALA A	3.47	50.97	-1.1	0.07	2.19	54
   36	100041 PRO A, 100180 TYR A, 100173 ALA A, 100153 GLU A	3.28	52.87	-1.7	-0.23	14.12	61
   37	100041 PRO A, 100173 ALA A, 100153 GLU A, 100172 PRO A	3.35	55.01	-1.78	-0.53	14.11	64
   38	100041 PRO A, 100153 GLU A, 100172 PRO A, 100041 ASN B	3.38	55.73	-2.55	-0.52	14.11	74
   39	100041 PRO A, 100153 GLU A, 100172 PRO A, 100041 ASN B	3.47	56.22	-2.55	-0.52	14.11	74
   40	100153 GLU A, 100172 PRO A, 100041 ASN B	3.11	56.87	-2.87	-0.67	18.29	79
   41	100173 ALA A, 100153 GLU A, 100172 PRO A, 100041 ASN B	2.27	60.27	-2.25	-0.7	14.56	79
   42	100173 ALA A, 100153 GLU A, 100041 ASN B, 100172 PRO A	2.44	60.7	-1.95	-0.88	15.01	90
   43	100173 ALA A, 100153 GLU A, 100041 ASN B, 100172 PRO A, 100171 PHE A	2.62	61.04	-1.64	-0.86	12.68	90
   44	100173 ALA A, 100153 GLU A, 100041 ASN B, 100172 PRO A, 100182 LEU A	2.74	61.28	-0.8	-0.47	12.03	78
   45	100153 GLU A, 100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A	2.62	61.48	-0.8	-0.47	12.03	78
   46	100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A	2.58	62.31	-0.13	-0.31	2.57	79
   47	100041 ASN B, 100171 PHE A, 100182 LEU A	2.75	62.63	-0.03	-0.14	2.3	79
   48	100041 ASN B, 100182 LEU A, 100170 THR A	2.76	62.87	-0.13	-0.13	1.72	88
   49	100041 ASN B, 100182 LEU A, 100170 THR A, 100155 VAL A	2.61	64.04	-0.2	-0.3	2.14	88
   50	100041 ASN B, 100170 THR A, 100155 VAL A	2.5	68.13	-1.53	-0.78	2.81	105
   51	100041 ASN B, 100156 THR A, 100157 VAL A	3.14	68.5	-1.53	-0.78	2.81	105
   52	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.22	68.76	-1.33	-0.78	2.52	106
   53	100041 ASN B, 100170 THR A, 100157 VAL A	3.23	68.84	-1.53	-0.78	2.81	105
   54	100041 ASN B, 100170 THR A, 100155 VAL A	3.17	69.01	-1.53	-0.78	2.81	105
   55	100041 ASN B, 100170 THR A, 100157 VAL A	3.23	69.22	-1.53	-0.78	2.81	105
   56	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.19	69.64	-1.33	-0.78	2.52	106
   57	100170 THR A, 100156 THR A, 100157 VAL A	3.23	69.79	-0.6	-0.78	2.23	107
   58	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.29	70.37	-1.33	-0.78	2.52	106
   59	100041 ASN B, 100156 THR A, 100157 VAL A	3.31	72.4	-1.53	-0.78	2.81	105
   60	100041 ASN B, 100156 THR A, 100157 VAL A, 100040 THR B	3.79	72.99	-1.25	-0.79	2.95	105

   pore with bottle neck

   pore with local minimum

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

   Unique lining residues set - all

   200046 GLU A, 200061 ASN A, 200063 LYS A, 200003 LEU B, 200098 PHE B, 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

   200046 GLU A, 200061 ASN A, 200063 LYS A, 200003 LEU B, 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: 1 (3-2)
   Hydropathy: -1.2
   Hydrophobicity: -0.36
   Polarity: 12.09
   Mutability: 84
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	200046 GLU A, 200061 ASN A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.26	1.13	-1.5	-0.4	21.26	76
   2	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.28	2.22	-1	-0.3	25.73	67
   3	200046 GLU A, 200063 LYS A, 200003 LEU B, 200064 ILE A	4.39	5.15	0.23	0.35	24.92	76
   4	200046 GLU A, 200063 LYS A, 200003 LEU B, 100020 SER B	5.72	6.18	-1.1	-0.35	25.3	80
   5	200046 GLU A, 200063 LYS A, 200064 ILE A	2.91	11.16	-0.97	0.09	33.18	84
   6	200046 GLU A, 200064 ILE A, 200063 LYS A	3.3	11.82	0.2	-0.04	17.8	90
   7	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.62	14.5	-0.98	-0.14	26.35	87
   8	200046 GLU A, 200064 ILE A, 100018 ARG B	3.63	14.98	-1.17	0.08	34.01	87
   9	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.53	18.3	-2	-0.04	38.51	86
   10	200046 GLU A, 100018 ARG B, 200040 ARG A	4	20.56	-4.17	-0.66	51.3	81
   11	200046 GLU A, 200064 ILE A, 200040 ARG A	4.06	21.34	-1.17	0.08	34.01	87
   12	200046 GLU A, 200040 ARG A	2.89	24.13	-4	-0.78	50.95	80
   13	200040 ARG A	-0.27	30.72	-4.5	-0.42	52	83
   14	200040 ARG A, 200088 SER A	1.51	31.47	-2.45	-0.61	27.69	83
   15	200040 ARG A, 200088 SER A, 200091 SER A	2.16	32.2	-1.77	-0.67	19.59	83
   16	200040 ARG A, 200088 SER A, 200091 SER A	2.32	32.39	-1.9	-0.73	19.02	100
   17	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.48	32.62	-1.83	-0.57	14.66	86
   18	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.71	33.23	-1.73	-0.53	15.09	70
   19	200040 ARG A, 200088 SER A, 200041 PRO A	3.01	35.82	-2.17	-0.44	18.99	70
   20	200040 ARG A, 200041 PRO A, 200088 SER A	4.49	37.87	-2.3	-0.49	18.42	86
   21	200041 PRO A, 200088 SER A	4.81	39.01	-1.2	-0.53	1.63	87
   22	200091 SER A, 200041 PRO A, 200088 SER A	4.57	39.81	-1.07	-0.68	1.64	97
   23	200091 SER A, 200041 PRO A, 200088 SER A, 200175 LEU A	4.53	40.44	0.15	-0.22	1.26	86
   24	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.56	40.65	0.02	0.3	1.25	69
   25	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.34	40.98	0.23	0.08	1.27	84
   26	200091 SER A, 200088 SER A, 200180 TYR A	4.07	41.15	-0.97	-0.28	1.65	94
   27	200091 SER A, 200088 SER A	4.13	41.29	-0.8	-0.97	1.67	117
   28	200091 SER A, 200088 SER A, 200180 TYR A	4.3	41.6	-0.97	-0.28	1.65	94
   29	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.4	42.11	0.23	0.08	1.27	84
   30	200088 SER A, 200091 SER A, 200041 PRO A, 200175 LEU A, 200180 TYR A	4.35	42.78	-0.06	0.08	1.67	69
   31	200041 PRO A, 200175 LEU A, 200180 TYR A	4.04	47.08	0.3	0.72	1.11	54
   32	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.46	47.42	0.13	0.34	1.68	54
   33	200041 PRO A, 200175 LEU A, 200180 TYR A	4.37	48.05	0.3	0.72	1.11	54
   34	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.44	48.64	0.13	0.34	1.68	54
   35	200041 PRO A, 200180 TYR A, 200173 ALA A	3.47	50.97	-1.1	0.07	2.19	54
   36	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.28	52.87	-1.7	-0.23	14.12	61
   37	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.35	55.01	-1.78	-0.53	14.11	64
   38	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.38	55.73	-2.55	-0.52	14.11	74
   39	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.47	56.22	-2.55	-0.52	14.11	74
   40	200153 GLU A, 200172 PRO A, 200041 ASN B	3.11	56.87	-2.87	-0.67	18.29	79
   41	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.27	60.27	-2.25	-0.7	14.56	79
   42	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.44	60.7	-1.95	-0.88	15.01	90
   43	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A	2.62	61.04	-1.64	-0.86	12.68	90
   44	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200182 LEU A	2.74	61.28	-0.8	-0.47	12.03	78
   45	200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.62	61.48	-0.8	-0.47	12.03	78
   46	200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.58	62.31	-0.13	-0.31	2.57	79
   47	200041 ASN B, 200171 PHE A, 200182 LEU A	2.75	62.63	-0.03	-0.14	2.3	79
   48	200041 ASN B, 200182 LEU A, 200170 THR A	2.76	62.87	-0.13	-0.13	1.72	88
   49	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.61	64.04	-0.2	-0.3	2.14	88
   50	200041 ASN B, 200170 THR A, 200155 VAL A	2.5	68.13	-1.53	-0.78	2.81	105
   51	200041 ASN B, 200156 THR A, 200157 VAL A	3.14	68.5	-1.53	-0.78	2.81	105
   52	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.22	68.76	-1.33	-0.78	2.52	106
   53	200041 ASN B, 200170 THR A, 200157 VAL A	3.23	68.84	-1.53	-0.78	2.81	105
   54	200041 ASN B, 200170 THR A, 200155 VAL A	3.17	69.01	-1.53	-0.78	2.81	105
   55	200041 ASN B, 200170 THR A, 200157 VAL A	3.23	69.23	-1.53	-0.78	2.81	105
   56	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.19	69.65	-1.33	-0.78	2.52	106
   57	200170 THR A, 200156 THR A, 200157 VAL A	3.23	69.79	-0.6	-0.78	2.23	107
   58	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.29	70.38	-1.33	-0.78	2.52	106
   59	200041 ASN B, 200156 THR A, 200157 VAL A	3.31	72.4	-1.53	-0.78	2.81	105
   60	200041 ASN B, 200156 THR A, 200157 VAL A, 200040 THR B	3.79	72.99	-1.25	-0.79	2.95	105

   pore with bottle neck

   pore with local minimum

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

   Unique lining residues set - all

   46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 98 PHE B, 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, 171 PHE A, 182 LEU A, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A, 40 THR B

   Unique lining residues set - sidechains

   46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 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: 1 (3-2)
   Hydropathy: -1.2
   Hydrophobicity: -0.36
   Polarity: 12.09
   Mutability: 84
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 98 PHE B	4.26	1.13	-1.5	-0.4	21.26	76
   2	46 GLU A, 63 LYS A, 3 LEU B, 98 PHE B	4.28	2.22	-1	-0.3	25.73	67
   3	46 GLU A, 63 LYS A, 3 LEU B, 64 ILE A	4.39	5.15	0.23	0.35	24.92	76
   4	46 GLU A, 63 LYS A, 3 LEU B, 200020 SER B	5.72	6.18	-1.1	-0.35	25.3	80
   5	46 GLU A, 63 LYS A, 64 ILE A	2.91	11.16	-0.97	0.09	33.18	84
   6	46 GLU A, 64 ILE A, 63 LYS A	3.3	11.82	0.2	-0.04	17.8	90
   7	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.62	14.5	-0.98	-0.14	26.35	87
   8	46 GLU A, 64 ILE A, 200018 ARG B	3.63	14.98	-1.17	0.08	34.01	87
   9	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.53	18.3	-2	-0.04	38.51	86
   10	46 GLU A, 200018 ARG B, 40 ARG A	4	20.56	-4.17	-0.66	51.3	81
   11	46 GLU A, 64 ILE A, 40 ARG A	4.06	21.34	-1.17	0.08	34.01	87
   12	46 GLU A, 40 ARG A	2.89	24.13	-4	-0.78	50.95	80
   13	40 ARG A	-0.27	30.72	-4.5	-0.42	52	83
   14	40 ARG A, 88 SER A	1.51	31.47	-2.45	-0.61	27.69	83
   15	40 ARG A, 88 SER A, 91 SER A	2.16	32.2	-1.77	-0.67	19.59	83
   16	40 ARG A, 88 SER A, 91 SER A	2.32	32.39	-1.9	-0.73	19.02	100
   17	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.48	32.62	-1.83	-0.57	14.66	86
   18	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.71	33.23	-1.73	-0.53	15.09	70
   19	40 ARG A, 88 SER A, 41 PRO A	3.01	35.82	-2.17	-0.44	18.99	70
   20	40 ARG A, 41 PRO A, 88 SER A	4.49	37.88	-2.3	-0.49	18.42	86
   21	41 PRO A, 88 SER A	4.81	39.01	-1.2	-0.53	1.63	87
   22	91 SER A, 41 PRO A, 88 SER A	4.57	39.81	-1.07	-0.68	1.64	97
   23	91 SER A, 41 PRO A, 88 SER A, 175 LEU A	4.53	40.44	0.15	-0.22	1.26	86
   24	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.56	40.66	0.02	0.3	1.25	69
   25	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.34	40.99	0.23	0.08	1.27	84
   26	91 SER A, 88 SER A, 180 TYR A	4.07	41.15	-0.97	-0.28	1.65	94
   27	91 SER A, 88 SER A	4.13	41.29	-0.8	-0.97	1.67	117
   28	91 SER A, 88 SER A, 180 TYR A	4.3	41.6	-0.97	-0.28	1.65	94
   29	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.4	42.11	0.23	0.08	1.27	84
   30	88 SER A, 91 SER A, 41 PRO A, 175 LEU A, 180 TYR A	4.35	42.78	-0.06	0.08	1.67	69
   31	41 PRO A, 175 LEU A, 180 TYR A	4.04	47.08	0.3	0.72	1.11	54
   32	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.46	47.42	0.13	0.34	1.68	54
   33	41 PRO A, 175 LEU A, 180 TYR A	4.37	48.05	0.3	0.72	1.11	54
   34	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.44	48.64	0.13	0.34	1.68	54
   35	41 PRO A, 180 TYR A, 173 ALA A	3.47	50.97	-1.1	0.07	2.19	54
   36	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.28	52.87	-1.7	-0.23	14.12	61
   37	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.35	55.01	-1.78	-0.53	14.11	64
   38	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.38	55.73	-2.55	-0.52	14.11	74
   39	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.47	56.22	-2.55	-0.52	14.11	74
   40	153 GLU A, 172 PRO A, 41 ASN B	3.11	56.88	-2.87	-0.67	18.29	79
   41	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.27	60.27	-2.25	-0.7	14.56	79
   42	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.44	60.7	-1.95	-0.88	15.01	90
   43	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 171 PHE A	2.62	61.04	-1.64	-0.86	12.68	90
   44	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.74	61.28	-0.8	-0.47	12.03	78
   45	153 GLU A, 41 ASN B, 172 PRO A, 171 PHE A, 182 LEU A	2.62	61.48	-0.8	-0.47	12.03	78
   46	41 ASN B, 172 PRO A, 171 PHE A, 182 LEU A	2.58	62.31	-0.13	-0.31	2.57	79
   47	41 ASN B, 171 PHE A, 182 LEU A	2.75	62.63	-0.03	-0.14	2.3	79
   48	41 ASN B, 182 LEU A, 170 THR A	2.76	62.87	-0.13	-0.13	1.72	88
   49	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.61	64.04	-0.2	-0.3	2.14	88
   50	41 ASN B, 170 THR A, 155 VAL A	2.5	68.13	-1.53	-0.78	2.81	105
   51	41 ASN B, 156 THR A, 157 VAL A	3.14	68.5	-1.53	-0.78	2.81	105
   52	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.22	68.76	-1.33	-0.78	2.52	106
   53	41 ASN B, 170 THR A, 157 VAL A	3.23	68.84	-1.53	-0.78	2.81	105
   54	41 ASN B, 170 THR A, 155 VAL A	3.17	69.01	-1.53	-0.78	2.81	105
   55	41 ASN B, 170 THR A, 157 VAL A	3.23	69.23	-1.53	-0.78	2.81	105
   56	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.19	69.65	-1.33	-0.78	2.52	106
   57	170 THR A, 156 THR A, 157 VAL A	3.23	69.79	-0.6	-0.78	2.23	107
   58	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.29	70.38	-1.33	-0.78	2.52	106
   59	41 ASN B, 156 THR A, 157 VAL A	3.31	72.4	-1.53	-0.78	2.81	105
   60	41 ASN B, 156 THR A, 157 VAL A, 40 THR B	3.79	72.99	-1.25	-0.79	2.95	105

   pore with bottle neck

   pore with local minimum

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

   Unique lining residues set - all

   300046 GLU A, 300061 ASN A, 300063 LYS A, 300003 LEU B, 300098 PHE B, 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

   300046 GLU A, 300061 ASN A, 300063 LYS A, 300003 LEU B, 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: 1 (3-2)
   Hydropathy: -1.2
   Hydrophobicity: -0.36
   Polarity: 12.09
   Mutability: 84
   

   Lining residues

   show all | hide all

   #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
   1	300046 GLU A, 300061 ASN A, 300063 LYS A, 300003 LEU B, 300098 PHE B	4.26	1.13	-1.5	-0.4	21.26	76
   2	300046 GLU A, 300063 LYS A, 300003 LEU B, 300098 PHE B	4.28	2.22	-1	-0.3	25.73	67
   3	300046 GLU A, 300063 LYS A, 300003 LEU B, 300064 ILE A	4.39	5.15	0.23	0.35	24.92	76
   4	300046 GLU A, 300063 LYS A, 300003 LEU B, 20 SER B	5.72	6.18	-1.1	-0.35	25.3	80
   5	300046 GLU A, 300063 LYS A, 300064 ILE A	2.91	11.16	-0.97	0.09	33.18	84
   6	300046 GLU A, 300064 ILE A, 300063 LYS A	3.3	11.82	0.2	-0.04	17.8	90
   7	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.62	14.5	-0.98	-0.14	26.35	87
   8	300046 GLU A, 300064 ILE A, 18 ARG B	3.63	14.98	-1.17	0.08	34.01	87
   9	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.53	18.3	-2	-0.04	38.51	86
   10	300046 GLU A, 18 ARG B, 300040 ARG A	4	20.56	-4.17	-0.66	51.3	81
   11	300046 GLU A, 300064 ILE A, 300040 ARG A	4.06	21.34	-1.17	0.08	34.01	87
   12	300046 GLU A, 300040 ARG A	2.89	24.13	-4	-0.78	50.95	80
   13	300040 ARG A	-0.27	30.72	-4.5	-0.42	52	83
   14	300040 ARG A, 300088 SER A	1.51	31.47	-2.45	-0.61	27.69	83
   15	300040 ARG A, 300088 SER A, 300091 SER A	2.16	32.2	-1.77	-0.67	19.59	83
   16	300040 ARG A, 300088 SER A, 300091 SER A	2.32	32.39	-1.9	-0.73	19.02	100
   17	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.48	32.62	-1.83	-0.57	14.66	86
   18	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.71	33.23	-1.73	-0.53	15.09	70
   19	300040 ARG A, 300088 SER A, 300041 PRO A	3.01	35.82	-2.17	-0.44	18.99	70
   20	300040 ARG A, 300041 PRO A, 300088 SER A	4.49	37.87	-2.3	-0.49	18.42	86
   21	300041 PRO A, 300088 SER A	4.81	39.01	-1.2	-0.53	1.63	87
   22	300091 SER A, 300041 PRO A, 300088 SER A	4.57	39.81	-1.07	-0.68	1.64	97
   23	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.53	40.44	0.15	-0.22	1.26	86
   24	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.56	40.66	0.02	0.3	1.25	69
   25	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.34	40.99	0.23	0.08	1.27	84
   26	300091 SER A, 300088 SER A, 300180 TYR A	4.07	41.15	-0.97	-0.28	1.65	94
   27	300091 SER A, 300088 SER A	4.13	41.29	-0.8	-0.97	1.67	117
   28	300091 SER A, 300088 SER A, 300180 TYR A	4.3	41.6	-0.97	-0.28	1.65	94
   29	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.4	42.11	0.23	0.08	1.27	84
   30	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.35	42.78	-0.06	0.08	1.67	69
   31	300041 PRO A, 300175 LEU A, 300180 TYR A	4.04	47.08	0.3	0.72	1.11	54
   32	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.46	47.42	0.13	0.34	1.68	54
   33	300041 PRO A, 300175 LEU A, 300180 TYR A	4.37	48.05	0.3	0.72	1.11	54
   34	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.44	48.64	0.13	0.34	1.68	54
   35	300041 PRO A, 300180 TYR A, 300173 ALA A	3.47	50.97	-1.1	0.07	2.19	54
   36	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.28	52.87	-1.7	-0.23	14.12	61
   37	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.35	55.01	-1.78	-0.53	14.11	64
   38	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.38	55.73	-2.55	-0.52	14.11	74
   39	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.47	56.22	-2.55	-0.52	14.11	74
   40	300153 GLU A, 300172 PRO A, 300041 ASN B	3.11	56.87	-2.87	-0.67	18.29	79
   41	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.27	60.27	-2.25	-0.7	14.56	79
   42	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.44	60.7	-1.95	-0.88	15.01	90
   43	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A	2.62	61.04	-1.64	-0.86	12.68	90
   44	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.74	61.28	-0.8	-0.47	12.03	78
   45	300153 GLU A, 300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A	2.62	61.48	-0.8	-0.47	12.03	78
   46	300041 ASN B, 300172 PRO A, 300171 PHE A, 300182 LEU A	2.58	62.31	-0.13	-0.31	2.57	79
   47	300041 ASN B, 300171 PHE A, 300182 LEU A	2.75	62.63	-0.03	-0.14	2.3	79
   48	300041 ASN B, 300182 LEU A, 300170 THR A	2.76	62.87	-0.13	-0.13	1.72	88
   49	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.61	64.04	-0.2	-0.3	2.14	88
   50	300041 ASN B, 300170 THR A, 300155 VAL A	2.5	68.13	-1.53	-0.78	2.81	105
   51	300041 ASN B, 300156 THR A, 300157 VAL A	3.14	68.5	-1.53	-0.78	2.81	105
   52	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.22	68.76	-1.33	-0.78	2.52	106
   53	300041 ASN B, 300170 THR A, 300157 VAL A	3.23	68.84	-1.53	-0.78	2.81	105
   54	300041 ASN B, 300170 THR A, 300155 VAL A	3.17	69.01	-1.53	-0.78	2.81	105
   55	300041 ASN B, 300170 THR A, 300157 VAL A	3.23	69.23	-1.53	-0.78	2.81	105
   56	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.19	69.65	-1.33	-0.78	2.52	106
   57	300170 THR A, 300156 THR A, 300157 VAL A	3.23	69.79	-0.6	-0.78	2.23	107
   58	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.29	70.38	-1.33	-0.78	2.52	106
   59	300041 ASN B, 300156 THR A, 300157 VAL A	3.31	72.4	-1.53	-0.78	2.81	105
   60	300041 ASN B, 300156 THR A, 300157 VAL A, 300040 THR B	3.79	72.99	-1.25	-0.79	2.95	105

   pore with bottle neck

   pore with local minimum

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

    Unique lining residues set - all

    100046 GLU A, 100061 ASN A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100064 ILE A, 300020 SER B, 100063 LYS A, 300018 ARG B, 100040 ARG A, 100088 SER A, 100091 SER A, 100041 PRO A, 100091 SER A, 100088 SER A, 100175 LEU A, 100180 TYR A, 100173 ALA A, 100153 GLU A, 100172 PRO A, 100041 ASN B, 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

    100046 GLU A, 100061 ASN A, 100063 LYS A, 100003 LEU B, 100064 ILE A, 300020 SER B, 300018 ARG B, 100040 ARG A, 100041 PRO A, 100091 SER A, 100088 SER A, 100175 LEU A, 100180 TYR A, 100153 GLU A, 100172 PRO A, 100041 ASN B, 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: 0 (4-4)
    Hydropathy: -1.2
    Hydrophobicity: -0.39
    Polarity: 13.61
    Mutability: 89
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100046 GLU A, 100061 ASN A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.26	1.35	-1.5	-0.4	21.26	76
    2	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.45	2.62	-1	-0.3	25.73	67
    3	100046 GLU A, 100063 LYS A, 100003 LEU B, 100064 ILE A	4.67	5.14	0.23	0.35	24.92	76
    4	100046 GLU A, 100063 LYS A, 100003 LEU B, 300020 SER B	5.72	5.83	-1.1	-0.35	25.3	80
    5	100046 GLU A, 100063 LYS A, 100003 LEU B, 100064 ILE A	5.65	6.5	0.23	0.35	24.92	76
    6	100046 GLU A, 100063 LYS A, 100064 ILE A	2.93	11.08	-0.97	0.09	33.18	84
    7	100046 GLU A, 100064 ILE A, 100063 LYS A	3.39	11.87	0.2	-0.04	17.8	90
    8	100046 GLU A, 100064 ILE A, 100063 LYS A, 300018 ARG B	3.63	14.99	-0.98	-0.14	26.35	87
    9	100046 GLU A, 100064 ILE A, 300018 ARG B, 100040 ARG A	3.53	18.28	-2	-0.04	38.51	86
    10	100046 GLU A, 300018 ARG B, 100040 ARG A	4.05	20.58	-4.17	-0.66	51.3	81
    11	100046 GLU A, 100064 ILE A, 100040 ARG A	4.2	21.65	-1.17	0.08	34.01	87
    12	100046 GLU A, 100040 ARG A	2.18	24.04	-4	-0.78	50.95	80
    13	100040 ARG A	0.49	30.43	-4.5	-0.42	52	83
    14	100040 ARG A, 100088 SER A	1.51	31.39	-2.45	-0.61	27.69	83
    15	100040 ARG A, 100088 SER A, 100091 SER A	1.91	32.22	-1.77	-0.67	19.59	83
    16	100040 ARG A, 100088 SER A, 100041 PRO A, 100091 SER A	2.39	32.46	-1.83	-0.57	14.66	86
    17	100040 ARG A, 100088 SER A, 100091 SER A, 100041 PRO A	2.56	33.15	-1.73	-0.53	15.09	70
    18	100040 ARG A, 100088 SER A, 100041 PRO A	2.96	35.6	-2.17	-0.44	18.99	70
    19	100040 ARG A, 100041 PRO A, 100088 SER A	4.34	37.84	-2.3	-0.49	18.42	86
    20	100041 PRO A, 100088 SER A	4.73	39.22	-1.2	-0.53	1.63	87
    21	100041 PRO A, 100091 SER A, 100088 SER A	4.66	39.69	-1.07	-0.68	1.64	97
    22	100041 PRO A, 100091 SER A, 100088 SER A, 100175 LEU A	4.58	40.44	0.15	-0.22	1.26	86
    23	100041 PRO A, 100088 SER A, 100175 LEU A, 100180 TYR A	4.45	40.68	0.02	0.3	1.25	69
    24	100091 SER A, 100088 SER A, 100175 LEU A, 100180 TYR A	4.28	40.88	0.23	0.08	1.27	84
    25	100091 SER A, 100088 SER A, 100180 TYR A	4.16	41.09	-0.97	-0.28	1.65	94
    26	100091 SER A, 100088 SER A	4.32	41.28	-0.8	-0.97	1.67	117
    27	100091 SER A, 100088 SER A, 100180 TYR A	4.5	41.71	-0.97	-0.28	1.65	94
    28	100041 PRO A, 100088 SER A, 100175 LEU A, 100180 TYR A	4.55	42.42	0.02	0.3	1.25	69
    29	100088 SER A, 100041 PRO A, 100091 SER A, 100175 LEU A, 100180 TYR A	4.42	43.32	-0.06	0.08	1.67	69
    30	100041 PRO A, 100175 LEU A, 100180 TYR A	4.05	46.98	0.3	0.72	1.11	54
    31	100041 PRO A, 100175 LEU A, 100180 TYR A, 100173 ALA A	4.45	47.41	0.13	0.34	1.68	54
    32	100041 PRO A, 100175 LEU A, 100180 TYR A	4.38	47.99	0.3	0.72	1.11	54
    33	100041 PRO A, 100175 LEU A, 100180 TYR A, 100173 ALA A	4.48	48.52	0.13	0.34	1.68	54
    34	100041 PRO A, 100180 TYR A, 100173 ALA A	3.57	50.73	-1.1	0.07	2.19	54
    35	100041 PRO A, 100180 TYR A, 100173 ALA A, 100153 GLU A	3.4	53.01	-1.7	-0.23	14.12	61
    36	100041 PRO A, 100173 ALA A, 100153 GLU A, 100172 PRO A	3.39	55.14	-1.78	-0.53	14.11	64
    37	100041 PRO A, 100153 GLU A, 100172 PRO A, 100041 ASN B	3.42	55.69	-2.55	-0.52	14.11	74
    38	100041 PRO A, 100153 GLU A, 100172 PRO A, 100041 ASN B	3.36	56.31	-2.55	-0.52	14.11	74
    39	100153 GLU A, 100172 PRO A, 100041 ASN B	3.24	56.7	-2.87	-0.67	18.29	79
    40	100173 ALA A, 100153 GLU A, 100172 PRO A, 100041 ASN B	2.3	60.14	-2.25	-0.7	14.56	79
    41	100173 ALA A, 100153 GLU A, 100041 ASN B, 100172 PRO A	2.4	60.66	-1.95	-0.88	15.01	90
    42	100173 ALA A, 100153 GLU A, 100041 ASN B, 100172 PRO A, 100171 PHE A	2.55	61.05	-1.64	-0.86	12.68	90
    43	100153 GLU A, 100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A	2.68	61.45	-0.8	-0.47	12.03	78
    44	100041 ASN B, 100172 PRO A, 100171 PHE A, 100182 LEU A	2.63	62.36	-0.13	-0.31	2.57	79
    45	100041 ASN B, 100171 PHE A, 100182 LEU A	2.76	62.55	-0.03	-0.14	2.3	79
    46	100041 ASN B, 100182 LEU A, 100170 THR A	2.79	62.83	-0.13	-0.13	1.72	88
    47	100041 ASN B, 100182 LEU A, 100170 THR A, 100155 VAL A	2.64	64.49	-0.2	-0.3	2.14	88
    48	100041 ASN B, 100170 THR A, 100155 VAL A	2.59	68.02	-1.53	-0.78	2.81	105
    49	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.16	68.21	-1.33	-0.78	2.52	106
    50	100041 ASN B, 100156 THR A, 100157 VAL A	3.23	68.48	-1.53	-0.78	2.81	105
    51	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.19	68.63	-1.33	-0.78	2.52	106
    52	100041 ASN B, 100170 THR A, 100157 VAL A	3.18	68.73	-1.53	-0.78	2.81	105
    53	100041 ASN B, 100170 THR A, 100155 VAL A	3.18	68.87	-1.53	-0.78	2.81	105
    54	100041 ASN B, 100170 THR A, 100157 VAL A	3.23	69.07	-1.53	-0.78	2.81	105
    55	100041 ASN B, 100170 THR A, 100156 THR A, 100157 VAL A	3.27	69.53	-1.33	-0.78	2.52	106
    56	100041 ASN B, 100170 THR A, 100157 VAL A	3.27	72.67	-1.53	-0.78	2.81	105
    57	100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B	4.12	73.42	-1.25	-0.79	2.95	105
    58	100041 ASN B, 100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A	4.55	73.56	-1.08	-0.79	3.04	105
    59	100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A	4.61	73.77	0.68	-0.31	2.14	102
    60	100170 THR A, 100157 VAL A, 100040 THR B, 100168 VAL A, 100169 LYS B	4.56	73.92	-1.16	-0.72	12.26	89
    61	100170 THR A, 100157 VAL A, 100168 VAL A, 100169 LYS B	4.45	74.65	-0.2	-0.21	13.67	92
    62	100157 VAL A, 100168 VAL A, 100169 LYS B, 100165 SER A	4.08	75.44	-0.13	-0.22	14.1	85
    63	100168 VAL A, 100169 LYS B, 100165 SER A	2.14	79.13	-0.03	-0.03	17.67	85
    64	100168 VAL A, 100169 LYS B, 100165 SER A	1.44	81.38	-1.57	-0.67	18.75	72
    65	100168 VAL A, 100169 LYS B, 100165 SER A, 100167 GLY A	1.54	82.53	-1.28	-0.7	14.91	72
    66	100168 VAL A, 100169 LYS B, 100167 GLY A	1.71	83.69	-1.57	-0.67	18.75	72
    67	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.84	83.86	-1.98	-0.44	26.97	81
    68	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.9	84.07	-1.98	-0.44	26.97	81
    69	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.97	84.09	-1.98	-0.44	26.97	81
    70	100168 VAL A, 100169 LYS B, 100167 GLY A, 100169 HIS A	1.85	84.48	-1.98	-0.44	26.97	81
    71	100168 VAL A, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.86	84.62	-1.88	-0.6	27.02	88
    72	100169 LYS B, 100167 GLY A, 100169 HIS A, 100167 ASP B	1.83	85.21	-2.75	-0.5	38.55	83
    73	100169 LYS B, 100167 GLY A, 100167 ASP B	1.64	86.43	-2.6	-0.75	34.19	79
    74	100169 LYS B, 100167 GLY A	1.61	87.12	-2.15	-0.61	26.44	72
    75	100169 LYS B, 100167 GLY A, 100166 SER A	1.68	88.64	-1.57	-0.67	18.75	72
    76	100169 LYS B, 100167 GLY A, 100166 SER A	1.83	88.93	-1.7	-0.73	18.18	94
    77	100169 LYS B, 100166 SER A	1.83	89.15	-2.35	-0.69	25.59	94
    78	100169 LYS B, 100167 GLY A, 100166 SER A	1.91	92.26	-1.7	-0.73	18.18	94
    79	100169 LYS B, 100167 GLY A, 100166 SER A, 100170 ASP B	3.47	93.64	-2.15	-0.81	26.06	91
    80	100167 GLY A, 100166 SER A, 100170 ASP B, 100169 LYS B	4.21	94.07	-1.28	-0.9	14.53	101
    81	100167 GLY A, 100166 SER A, 100170 ASP B	4.45	95.19	-1.57	-0.94	18.25	101
    82	100167 GLY A, 100166 SER A, 100170 ASP B, 100140 MET A	5.04	96.01	-0.7	-0.45	14.05	98
    83	100167 GLY A, 100170 ASP B, 100140 MET A	4.21	97.74	-0.67	-0.28	18.17	89
    84	100167 GLY A, 100170 ASP B, 100140 MET A, 100138 ASN B	3.9	98.88	-1.38	-0.4	14.47	94
    85	100170 ASP B, 100140 MET A, 100138 ASN B	3.94	100.39	-1.7	-0.27	18.17	94
    86	100140 MET A, 100138 ASN B, 100187 THR A	3.51	102.45	-0.77	-0.18	2.16	101
    87	100140 MET A, 100138 ASN B, 100187 THR A, 100114 THR B	2.77	104.12	-0.75	-0.33	2.03	102
    88	100140 MET A, 100187 THR A, 100114 THR B	2.56	105.75	0.17	-0.18	1.58	102
    89	100140 MET A, 100114 THR B	2.7	107.05	0.6	0.12	1.55	100
    90	100140 MET A, 100114 THR B, 100138 ASN A	3.05	107.55	-0.77	-0.18	2.16	101
    91	100140 MET A, 100114 THR B, 100138 ASN A, 100139 SER A	2.84	108.61	-0.78	-0.38	2.04	105
    92	100140 MET A, 100114 THR B, 100138 ASN A	2.77	109.41	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 98 PHE B, 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, 171 PHE A, 182 LEU 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

    46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 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: 0 (4-4)
    Hydropathy: -1.2
    Hydrophobicity: -0.39
    Polarity: 13.61
    Mutability: 89
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 98 PHE B	4.26	1.35	-1.5	-0.4	21.26	76
    2	46 GLU A, 63 LYS A, 3 LEU B, 98 PHE B	4.45	2.62	-1	-0.3	25.73	67
    3	46 GLU A, 63 LYS A, 3 LEU B, 64 ILE A	4.67	5.14	0.23	0.35	24.92	76
    4	46 GLU A, 63 LYS A, 3 LEU B, 200020 SER B	5.72	5.83	-1.1	-0.35	25.3	80
    5	46 GLU A, 63 LYS A, 3 LEU B, 64 ILE A	5.65	6.5	0.23	0.35	24.92	76
    6	46 GLU A, 63 LYS A, 64 ILE A	2.93	11.08	-0.97	0.09	33.18	84
    7	46 GLU A, 64 ILE A, 63 LYS A	3.39	11.87	0.2	-0.04	17.8	90
    8	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.63	14.99	-0.98	-0.14	26.35	87
    9	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.53	18.28	-2	-0.04	38.51	86
    10	46 GLU A, 200018 ARG B, 40 ARG A	4.05	20.58	-4.17	-0.66	51.3	81
    11	46 GLU A, 64 ILE A, 40 ARG A	4.2	21.65	-1.17	0.08	34.01	87
    12	46 GLU A, 40 ARG A	2.18	24.04	-4	-0.78	50.95	80
    13	40 ARG A	0.49	30.43	-4.5	-0.42	52	83
    14	40 ARG A, 88 SER A	1.51	31.39	-2.45	-0.61	27.69	83
    15	40 ARG A, 88 SER A, 91 SER A	1.91	32.22	-1.77	-0.67	19.59	83
    16	40 ARG A, 88 SER A, 41 PRO A, 91 SER A	2.39	32.46	-1.83	-0.57	14.66	86
    17	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.56	33.15	-1.73	-0.53	15.09	70
    18	40 ARG A, 88 SER A, 41 PRO A	2.96	35.6	-2.17	-0.44	18.99	70
    19	40 ARG A, 41 PRO A, 88 SER A	4.34	37.84	-2.3	-0.49	18.42	86
    20	41 PRO A, 88 SER A	4.73	39.22	-1.2	-0.53	1.63	87
    21	41 PRO A, 91 SER A, 88 SER A	4.66	39.69	-1.07	-0.68	1.64	97
    22	41 PRO A, 91 SER A, 88 SER A, 175 LEU A	4.58	40.44	0.15	-0.22	1.26	86
    23	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.45	40.68	0.02	0.3	1.25	69
    24	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.28	40.88	0.23	0.08	1.27	84
    25	91 SER A, 88 SER A, 180 TYR A	4.16	41.09	-0.97	-0.28	1.65	94
    26	91 SER A, 88 SER A	4.32	41.28	-0.8	-0.97	1.67	117
    27	91 SER A, 88 SER A, 180 TYR A	4.5	41.71	-0.97	-0.28	1.65	94
    28	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.55	42.42	0.02	0.3	1.25	69
    29	88 SER A, 41 PRO A, 91 SER A, 175 LEU A, 180 TYR A	4.42	43.32	-0.06	0.08	1.67	69
    30	41 PRO A, 175 LEU A, 180 TYR A	4.05	46.98	0.3	0.72	1.11	54
    31	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.45	47.41	0.13	0.34	1.68	54
    32	41 PRO A, 175 LEU A, 180 TYR A	4.38	47.99	0.3	0.72	1.11	54
    33	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.48	48.53	0.13	0.34	1.68	54
    34	41 PRO A, 180 TYR A, 173 ALA A	3.57	50.73	-1.1	0.07	2.19	54
    35	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.4	53.01	-1.7	-0.23	14.12	61
    36	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.39	55.14	-1.78	-0.53	14.11	64
    37	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.42	55.69	-2.55	-0.52	14.11	74
    38	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.36	56.31	-2.55	-0.52	14.11	74
    39	153 GLU A, 172 PRO A, 41 ASN B	3.24	56.7	-2.87	-0.67	18.29	79
    40	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.3	60.14	-2.25	-0.7	14.56	79
    41	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.4	60.66	-1.95	-0.88	15.01	90
    42	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 171 PHE A	2.55	61.05	-1.64	-0.86	12.68	90
    43	153 GLU A, 41 ASN B, 172 PRO A, 171 PHE A, 182 LEU A	2.68	61.45	-0.8	-0.47	12.03	78
    44	41 ASN B, 172 PRO A, 171 PHE A, 182 LEU A	2.63	62.37	-0.13	-0.31	2.57	79
    45	41 ASN B, 171 PHE A, 182 LEU A	2.76	62.55	-0.03	-0.14	2.3	79
    46	41 ASN B, 182 LEU A, 170 THR A	2.79	62.83	-0.13	-0.13	1.72	88
    47	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.64	64.49	-0.2	-0.3	2.14	88
    48	41 ASN B, 170 THR A, 155 VAL A	2.59	68.02	-1.53	-0.78	2.81	105
    49	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.16	68.21	-1.33	-0.78	2.52	106
    50	41 ASN B, 156 THR A, 157 VAL A	3.23	68.48	-1.53	-0.78	2.81	105
    51	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.19	68.64	-1.33	-0.78	2.52	106
    52	41 ASN B, 170 THR A, 157 VAL A	3.18	68.73	-1.53	-0.78	2.81	105
    53	41 ASN B, 170 THR A, 155 VAL A	3.18	68.87	-1.53	-0.78	2.81	105
    54	41 ASN B, 170 THR A, 157 VAL A	3.23	69.08	-1.53	-0.78	2.81	105
    55	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.27	69.53	-1.33	-0.78	2.52	106
    56	41 ASN B, 170 THR A, 157 VAL A	3.27	72.67	-1.53	-0.78	2.81	105
    57	41 ASN B, 170 THR A, 157 VAL A, 40 THR B	4.12	73.42	-1.25	-0.79	2.95	105
    58	41 ASN B, 170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.55	73.57	-1.08	-0.79	3.04	105
    59	170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.61	73.77	0.68	-0.31	2.14	102
    60	170 THR A, 157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.56	73.92	-1.16	-0.72	12.26	89
    61	170 THR A, 157 VAL A, 168 VAL A, 169 LYS B	4.45	74.65	-0.2	-0.21	13.67	92
    62	157 VAL A, 168 VAL A, 169 LYS B, 165 SER A	4.08	75.44	-0.13	-0.22	14.1	85
    63	168 VAL A, 169 LYS B, 165 SER A	2.14	79.14	-0.03	-0.03	17.67	85
    64	168 VAL A, 169 LYS B, 165 SER A	1.44	81.38	-1.57	-0.67	18.75	72
    65	168 VAL A, 169 LYS B, 165 SER A, 167 GLY A	1.54	82.53	-1.28	-0.7	14.91	72
    66	168 VAL A, 169 LYS B, 167 GLY A	1.71	83.7	-1.57	-0.67	18.75	72
    67	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.84	83.86	-1.98	-0.44	26.97	81
    68	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.9	84.07	-1.98	-0.44	26.97	81
    69	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.97	84.09	-1.98	-0.44	26.97	81
    70	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.85	84.48	-1.98	-0.44	26.97	81
    71	168 VAL A, 167 GLY A, 169 HIS A, 167 ASP B	1.86	84.62	-1.88	-0.6	27.02	88
    72	169 LYS B, 167 GLY A, 169 HIS A, 167 ASP B	1.83	85.22	-2.75	-0.5	38.55	83
    73	169 LYS B, 167 GLY A, 167 ASP B	1.64	86.43	-2.6	-0.75	34.19	79
    74	169 LYS B, 167 GLY A	1.61	87.12	-2.15	-0.61	26.44	72
    75	169 LYS B, 167 GLY A, 166 SER A	1.68	88.64	-1.57	-0.67	18.75	72
    76	169 LYS B, 167 GLY A, 166 SER A	1.83	88.93	-1.7	-0.73	18.18	94
    77	169 LYS B, 166 SER A	1.83	89.15	-2.35	-0.69	25.59	94
    78	169 LYS B, 167 GLY A, 166 SER A	1.91	92.26	-1.7	-0.73	18.18	94
    79	169 LYS B, 167 GLY A, 166 SER A, 170 ASP B	3.47	93.64	-2.15	-0.81	26.06	91
    80	167 GLY A, 166 SER A, 170 ASP B, 169 LYS B	4.21	94.07	-1.28	-0.9	14.53	101
    81	167 GLY A, 166 SER A, 170 ASP B	4.45	95.2	-1.57	-0.94	18.25	101
    82	167 GLY A, 166 SER A, 170 ASP B, 140 MET A	5.04	96.01	-0.7	-0.45	14.05	98
    83	167 GLY A, 170 ASP B, 140 MET A	4.21	97.74	-0.67	-0.28	18.17	89
    84	167 GLY A, 170 ASP B, 140 MET A, 138 ASN B	3.9	98.88	-1.38	-0.4	14.47	94
    85	170 ASP B, 140 MET A, 138 ASN B	3.94	100.39	-1.7	-0.27	18.17	94
    86	140 MET A, 138 ASN B, 187 THR A	3.51	102.45	-0.77	-0.18	2.16	101
    87	140 MET A, 138 ASN B, 187 THR A, 114 THR B	2.77	104.13	-0.75	-0.33	2.03	102
    88	140 MET A, 187 THR A, 114 THR B	2.56	105.75	0.17	-0.18	1.58	102
    89	140 MET A, 114 THR B	2.7	107.05	0.6	0.12	1.55	100
    90	140 MET A, 114 THR B, 138 ASN A	3.05	107.55	-0.77	-0.18	2.16	101
    91	140 MET A, 114 THR B, 138 ASN A, 139 SER A	2.84	108.61	-0.78	-0.38	2.04	105
    92	140 MET A, 114 THR B, 138 ASN A	2.77	109.41	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    200046 GLU A, 200061 ASN A, 200063 LYS A, 200003 LEU B, 200098 PHE B, 200064 ILE A, 100020 SER B, 200063 LYS A, 100018 ARG B, 200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A, 200091 SER 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

    200046 GLU A, 200061 ASN A, 200063 LYS A, 200003 LEU B, 200064 ILE A, 100020 SER B, 100018 ARG B, 200040 ARG A, 200041 PRO A, 200091 SER 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: 0 (4-4)
    Hydropathy: -1.2
    Hydrophobicity: -0.39
    Polarity: 13.61
    Mutability: 89
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	200046 GLU A, 200061 ASN A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.26	1.35	-1.5	-0.4	21.26	76
    2	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.45	2.62	-1	-0.3	25.73	67
    3	200046 GLU A, 200063 LYS A, 200003 LEU B, 200064 ILE A	4.67	5.14	0.23	0.35	24.92	76
    4	200046 GLU A, 200063 LYS A, 200003 LEU B, 100020 SER B	5.72	5.83	-1.1	-0.35	25.3	80
    5	200046 GLU A, 200063 LYS A, 200003 LEU B, 200064 ILE A	5.65	6.5	0.23	0.35	24.92	76
    6	200046 GLU A, 200063 LYS A, 200064 ILE A	2.93	11.08	-0.97	0.09	33.18	84
    7	200046 GLU A, 200064 ILE A, 200063 LYS A	3.39	11.87	0.2	-0.04	17.8	90
    8	200046 GLU A, 200064 ILE A, 200063 LYS A, 100018 ARG B	3.63	14.99	-0.98	-0.14	26.35	87
    9	200046 GLU A, 200064 ILE A, 100018 ARG B, 200040 ARG A	3.53	18.28	-2	-0.04	38.51	86
    10	200046 GLU A, 100018 ARG B, 200040 ARG A	4.05	20.58	-4.17	-0.66	51.3	81
    11	200046 GLU A, 200064 ILE A, 200040 ARG A	4.2	21.65	-1.17	0.08	34.01	87
    12	200046 GLU A, 200040 ARG A	2.18	24.04	-4	-0.78	50.95	80
    13	200040 ARG A	0.49	30.43	-4.5	-0.42	52	83
    14	200040 ARG A, 200088 SER A	1.51	31.39	-2.45	-0.61	27.69	83
    15	200040 ARG A, 200088 SER A, 200091 SER A	1.91	32.22	-1.77	-0.67	19.59	83
    16	200040 ARG A, 200088 SER A, 200041 PRO A, 200091 SER A	2.39	32.46	-1.83	-0.57	14.66	86
    17	200040 ARG A, 200088 SER A, 200091 SER A, 200041 PRO A	2.56	33.15	-1.73	-0.53	15.09	70
    18	200040 ARG A, 200088 SER A, 200041 PRO A	2.96	35.6	-2.17	-0.44	18.99	70
    19	200040 ARG A, 200041 PRO A, 200088 SER A	4.34	37.84	-2.3	-0.49	18.42	86
    20	200041 PRO A, 200088 SER A	4.73	39.22	-1.2	-0.53	1.63	87
    21	200041 PRO A, 200091 SER A, 200088 SER A	4.66	39.69	-1.07	-0.68	1.64	97
    22	200041 PRO A, 200091 SER A, 200088 SER A, 200175 LEU A	4.58	40.44	0.15	-0.22	1.26	86
    23	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.45	40.68	0.02	0.3	1.25	69
    24	200091 SER A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.28	40.88	0.23	0.08	1.27	84
    25	200091 SER A, 200088 SER A, 200180 TYR A	4.16	41.09	-0.97	-0.28	1.65	94
    26	200091 SER A, 200088 SER A	4.32	41.28	-0.8	-0.97	1.67	117
    27	200091 SER A, 200088 SER A, 200180 TYR A	4.5	41.71	-0.97	-0.28	1.65	94
    28	200041 PRO A, 200088 SER A, 200175 LEU A, 200180 TYR A	4.55	42.42	0.02	0.3	1.25	69
    29	200088 SER A, 200041 PRO A, 200091 SER A, 200175 LEU A, 200180 TYR A	4.42	43.32	-0.06	0.08	1.67	69
    30	200041 PRO A, 200175 LEU A, 200180 TYR A	4.05	46.98	0.3	0.72	1.11	54
    31	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.45	47.41	0.13	0.34	1.68	54
    32	200041 PRO A, 200175 LEU A, 200180 TYR A	4.38	47.99	0.3	0.72	1.11	54
    33	200041 PRO A, 200175 LEU A, 200180 TYR A, 200173 ALA A	4.48	48.52	0.13	0.34	1.68	54
    34	200041 PRO A, 200180 TYR A, 200173 ALA A	3.57	50.73	-1.1	0.07	2.19	54
    35	200041 PRO A, 200180 TYR A, 200173 ALA A, 200153 GLU A	3.4	53.01	-1.7	-0.23	14.12	61
    36	200041 PRO A, 200173 ALA A, 200153 GLU A, 200172 PRO A	3.39	55.14	-1.78	-0.53	14.11	64
    37	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.42	55.69	-2.55	-0.52	14.11	74
    38	200041 PRO A, 200153 GLU A, 200172 PRO A, 200041 ASN B	3.36	56.31	-2.55	-0.52	14.11	74
    39	200153 GLU A, 200172 PRO A, 200041 ASN B	3.24	56.7	-2.87	-0.67	18.29	79
    40	200173 ALA A, 200153 GLU A, 200172 PRO A, 200041 ASN B	2.3	60.14	-2.25	-0.7	14.56	79
    41	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A	2.4	60.66	-1.95	-0.88	15.01	90
    42	200173 ALA A, 200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A	2.55	61.05	-1.64	-0.86	12.68	90
    43	200153 GLU A, 200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.68	61.45	-0.8	-0.47	12.03	78
    44	200041 ASN B, 200172 PRO A, 200171 PHE A, 200182 LEU A	2.63	62.36	-0.13	-0.31	2.57	79
    45	200041 ASN B, 200171 PHE A, 200182 LEU A	2.76	62.55	-0.03	-0.14	2.3	79
    46	200041 ASN B, 200182 LEU A, 200170 THR A	2.79	62.83	-0.13	-0.13	1.72	88
    47	200041 ASN B, 200182 LEU A, 200170 THR A, 200155 VAL A	2.64	64.49	-0.2	-0.3	2.14	88
    48	200041 ASN B, 200170 THR A, 200155 VAL A	2.59	68.02	-1.53	-0.78	2.81	105
    49	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.16	68.21	-1.33	-0.78	2.52	106
    50	200041 ASN B, 200156 THR A, 200157 VAL A	3.23	68.48	-1.53	-0.78	2.81	105
    51	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.19	68.63	-1.33	-0.78	2.52	106
    52	200041 ASN B, 200170 THR A, 200157 VAL A	3.18	68.73	-1.53	-0.78	2.81	105
    53	200041 ASN B, 200170 THR A, 200155 VAL A	3.18	68.87	-1.53	-0.78	2.81	105
    54	200041 ASN B, 200170 THR A, 200157 VAL A	3.23	69.08	-1.53	-0.78	2.81	105
    55	200041 ASN B, 200170 THR A, 200156 THR A, 200157 VAL A	3.27	69.53	-1.33	-0.78	2.52	106
    56	200041 ASN B, 200170 THR A, 200157 VAL A	3.27	72.67	-1.53	-0.78	2.81	105
    57	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B	4.12	73.42	-1.25	-0.79	2.95	105
    58	200041 ASN B, 200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.55	73.56	-1.08	-0.79	3.04	105
    59	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A	4.61	73.77	0.68	-0.31	2.14	102
    60	200170 THR A, 200157 VAL A, 200040 THR B, 200168 VAL A, 200169 LYS B	4.56	73.92	-1.16	-0.72	12.26	89
    61	200170 THR A, 200157 VAL A, 200168 VAL A, 200169 LYS B	4.45	74.65	-0.2	-0.21	13.67	92
    62	200157 VAL A, 200168 VAL A, 200169 LYS B, 200165 SER A	4.08	75.44	-0.13	-0.22	14.1	85
    63	200168 VAL A, 200169 LYS B, 200165 SER A	2.14	79.14	-0.03	-0.03	17.67	85
    64	200168 VAL A, 200169 LYS B, 200165 SER A	1.44	81.38	-1.57	-0.67	18.75	72
    65	200168 VAL A, 200169 LYS B, 200165 SER A, 200167 GLY A	1.54	82.53	-1.28	-0.7	14.91	72
    66	200168 VAL A, 200169 LYS B, 200167 GLY A	1.71	83.69	-1.57	-0.67	18.75	72
    67	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.84	83.86	-1.98	-0.44	26.97	81
    68	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.9	84.07	-1.98	-0.44	26.97	81
    69	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.97	84.09	-1.98	-0.44	26.97	81
    70	200168 VAL A, 200169 LYS B, 200167 GLY A, 200169 HIS A	1.85	84.48	-1.98	-0.44	26.97	81
    71	200168 VAL A, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.86	84.62	-1.88	-0.6	27.02	88
    72	200169 LYS B, 200167 GLY A, 200169 HIS A, 200167 ASP B	1.83	85.21	-2.75	-0.5	38.55	83
    73	200169 LYS B, 200167 GLY A, 200167 ASP B	1.64	86.43	-2.6	-0.75	34.19	79
    74	200169 LYS B, 200167 GLY A	1.61	87.12	-2.15	-0.61	26.44	72
    75	200169 LYS B, 200167 GLY A, 200166 SER A	1.68	88.64	-1.57	-0.67	18.75	72
    76	200169 LYS B, 200167 GLY A, 200166 SER A	1.83	88.93	-1.7	-0.73	18.18	94
    77	200169 LYS B, 200166 SER A	1.83	89.15	-2.35	-0.69	25.59	94
    78	200169 LYS B, 200167 GLY A, 200166 SER A	1.91	92.26	-1.7	-0.73	18.18	94
    79	200169 LYS B, 200167 GLY A, 200166 SER A, 200170 ASP B	3.47	93.64	-2.15	-0.81	26.06	91
    80	200167 GLY A, 200166 SER A, 200170 ASP B, 200169 LYS B	4.21	94.07	-1.28	-0.9	14.53	101
    81	200167 GLY A, 200166 SER A, 200170 ASP B	4.45	95.2	-1.57	-0.94	18.25	101
    82	200167 GLY A, 200166 SER A, 200170 ASP B, 200140 MET A	5.04	96.01	-0.7	-0.45	14.05	98
    83	200167 GLY A, 200170 ASP B, 200140 MET A	4.21	97.74	-0.67	-0.28	18.17	89
    84	200167 GLY A, 200170 ASP B, 200140 MET A, 200138 ASN B	3.9	98.88	-1.38	-0.4	14.47	94
    85	200170 ASP B, 200140 MET A, 200138 ASN B	3.94	100.39	-1.7	-0.27	18.17	94
    86	200140 MET A, 200138 ASN B, 200187 THR A	3.51	102.45	-0.77	-0.18	2.16	101
    87	200140 MET A, 200138 ASN B, 200187 THR A, 200114 THR B	2.77	104.12	-0.75	-0.33	2.03	102
    88	200140 MET A, 200187 THR A, 200114 THR B	2.56	105.75	0.17	-0.18	1.58	102
    89	200140 MET A, 200114 THR B	2.7	107.05	0.6	0.12	1.55	100
    90	200140 MET A, 200114 THR B, 200138 ASN A	3.05	107.55	-0.77	-0.18	2.16	101
    91	200140 MET A, 200114 THR B, 200138 ASN A, 200139 SER A	2.84	108.61	-0.78	-0.38	2.04	105
    92	200140 MET A, 200114 THR B, 200138 ASN A	2.77	109.41	-0.77	-0.18	2.16	101

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    200042 GLY A, 200040 THR B, 200085 ASN B, 200165 ASP B, 200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A, 200173 ALA A, 200180 TYR A, 200175 LEU A, 200088 SER A, 200091 SER A, 200088 SER A, 200040 ARG A, 200091 SER A, 200043 HIS A, 200046 GLU A, 100018 ARG B, 200064 ILE A, 200063 LYS A, 200063 LYS A, 100020 SER B, 200003 LEU B, 200098 PHE B, 200061 ASN A, 200097 THR B, 200001 ASP B, 100072 THR B, 100070 ASP B, 200001 ASP B, 200026 SER B, 100024 ARG B, 200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B, 100028 SER B, 100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B, 27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B, 200028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 100058 GLN 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, 100050 TYR B, 100053 GLU B, 200085 THR C, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A

    Unique lining residues set - sidechains

    200040 THR B, 200085 ASN B, 200165 ASP B, 200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A, 200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A, 200040 ARG A, 200043 HIS A, 200046 GLU A, 100018 ARG B, 200064 ILE A, 200063 LYS A, 100020 SER B, 200003 LEU B, 200061 ASN A, 200097 THR B, 200001 ASP B, 100072 THR B, 100070 ASP B, 200026 SER B, 100024 ARG B, 100069 THR B, 100028 SER B, 200027 GLN B, 100027 GLN B, 27 GLN B, 28 SER B, 300027 GLN B, 200028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 100058 GLN C, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B, 100050 TYR B, 100053 GLU B, 200085 THR C, 200054 ALA C, 200057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 1 (8-7)
    Hydropathy: -1.4
    Hydrophobicity: -0.42
    Polarity: 15.82
    Mutability: 89
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	200042 GLY A, 200040 THR B, 200085 ASN B, 200165 ASP B	3.3	0.13	-2.03	-0.85	14.53	99
    2	200042 GLY A, 200040 THR B, 200165 ASP B	3.16	1.85	-1.53	-0.87	18.25	96
    3	200042 GLY A, 200040 THR B, 200165 ASP B, 200041 ASN B	3.19	3.92	-2.03	-0.85	14.53	99
    4	200042 GLY A, 200040 THR B, 200165 ASP B, 200041 ASN B, 200172 PRO A	3.67	4.14	-1.94	-0.69	11.94	88
    5	200042 GLY A, 200165 ASP B, 200041 ASN B, 200172 PRO A	3.68	4.73	-2.25	-0.68	14.51	82
    6	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.69	5.03	-1.78	-0.44	2.48	73
    7	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.71	5.26	-1.78	-0.44	2.48	73
    8	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.63	6.24	-1.78	-0.44	2.48	73
    9	200041 ASN B, 200172 PRO A, 200041 PRO A	3.58	6.55	-2.23	-0.32	2.18	73
    10	200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A	3.48	7.07	-2.55	-0.52	14.11	74
    11	200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A	3.42	7.91	-2.55	-0.52	14.11	74
    12	200172 PRO A, 200041 PRO A, 200153 GLU A, 200173 ALA A	3.43	9.94	-1.78	-0.53	14.11	64
    13	200041 PRO A, 200153 GLU A, 200173 ALA A, 200180 TYR A	3.28	12.14	-1.7	-0.23	14.12	61
    14	200041 PRO A, 200173 ALA A, 200180 TYR A	3.46	14.12	-1.1	0.07	2.19	54
    15	200041 PRO A, 200173 ALA A, 200180 TYR A, 200175 LEU A	4.43	14.65	0.13	0.34	1.68	54
    16	200041 PRO A, 200180 TYR A, 200175 LEU A	4.38	15.3	0.3	0.72	1.11	54
    17	200041 PRO A, 200173 ALA A, 200180 TYR A, 200175 LEU A	4.43	15.84	0.13	0.34	1.68	54
    18	200041 PRO A, 200180 TYR A, 200175 LEU A	4.09	20.47	0.3	0.72	1.11	54
    19	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A, 200091 SER A	4.51	21.03	-0.06	0.08	1.67	69
    20	200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A	4.57	21.35	0.23	0.08	1.27	84
    21	200180 TYR A, 200091 SER A, 200088 SER A	4.53	21.48	-0.97	-0.28	1.65	94
    22	200091 SER A, 200088 SER A	4.43	21.55	-0.8	-0.97	1.67	117
    23	200180 TYR A, 200091 SER A, 200088 SER A	4.24	21.87	-0.97	-0.28	1.65	94
    24	200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A	4.24	22.09	0.23	0.08	1.27	84
    25	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A	4.3	22.75	0.02	0.3	1.25	69
    26	200041 PRO A, 200175 LEU A, 200091 SER A, 200088 SER A	4.52	23.17	0.15	-0.22	1.26	86
    27	200041 PRO A, 200091 SER A, 200088 SER A	4.64	24.08	-1.07	-0.68	1.64	97
    28	200041 PRO A, 200088 SER A	4.87	25.13	-1.2	-0.53	1.63	87
    29	200041 PRO A, 200088 SER A, 200040 ARG A	4.4	27.48	-2.3	-0.49	18.42	86
    30	200041 PRO A, 200088 SER A, 200040 ARG A	3.1	29.6	-2.17	-0.44	18.99	70
    31	200041 PRO A, 200088 SER A, 200040 ARG A, 200091 SER A	2.78	30.24	-1.73	-0.53	15.09	70
    32	200088 SER A, 200040 ARG A, 200091 SER A	1.76	31.21	-1.77	-0.67	19.59	83
    33	200088 SER A, 200040 ARG A	0.42	33.11	-2.45	-0.61	27.69	83
    34	200040 ARG A	0.03	38.61	-4.5	-0.42	52	83
    35	200040 ARG A, 200043 HIS A	2.46	39.68	-3.85	-0.08	51.8	87
    36	200040 ARG A, 200046 GLU A	3.24	43.59	-4	-0.78	50.95	80
    37	200040 ARG A, 200046 GLU A, 100018 ARG B	3.9	46.1	-4.17	-0.66	51.3	81
    38	200040 ARG A, 200046 GLU A, 100018 ARG B, 200064 ILE A	3.5	49.53	-2	-0.04	38.51	86
    39	200046 GLU A, 100018 ARG B, 200064 ILE A	3.7	50.08	-1.17	0.08	34.01	87
    40	200046 GLU A, 100018 ARG B, 200064 ILE A, 200063 LYS A	3.5	53.31	-0.98	-0.14	26.35	87
    41	200046 GLU A, 200064 ILE A, 200063 LYS A	2.87	58.21	-0.97	0.09	33.18	84
    42	200046 GLU A, 200064 ILE A, 200063 LYS A, 100020 SER B	5.6	58.61	-0.93	-0.18	25.3	92
    43	200046 GLU A, 200063 LYS A, 100020 SER B, 200003 LEU B	5.96	59.5	-1.1	-0.35	25.3	80
    44	200046 GLU A, 200064 ILE A, 200063 LYS A, 200003 LEU B	4.63	62.51	0.23	0.35	24.92	76
    45	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.19	63.47	-1	-0.3	25.73	67
    46	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B, 200061 ASN A	3.84	64.6	-1.5	-0.4	21.26	76
    47	200046 GLU A, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200097 THR B	3.86	64.74	-2.4	-0.78	21.56	90
    48	200046 GLU A, 200098 PHE B, 200061 ASN A, 200097 THR B	3.94	64.93	-2.03	-0.87	14.58	96
    49	200046 GLU A, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200097 THR B	4.15	65.13	-2.4	-0.78	21.56	90
    50	200063 LYS A, 200003 LEU B, 200098 PHE B, 200061 ASN A, 200097 THR B	4.08	65.93	-0.94	-0.32	11.61	84
    51	200063 LYS A, 200003 LEU B, 200098 PHE B, 200097 THR B	3.91	66.31	-0.3	-0.21	13.67	77
    52	200063 LYS A, 200003 LEU B, 200061 ASN A, 200097 THR B	3.72	66.71	-1.08	-0.2	13.67	84
    53	200063 LYS A, 200003 LEU B, 200097 THR B, 200001 ASP B	3.41	68.56	-1.08	-0.27	25.25	79
    54	200063 LYS A, 200003 LEU B, 200001 ASP B	3.52	70.23	-1.2	-0.1	33.11	70
    55	200063 LYS A, 200003 LEU B, 200001 ASP B, 100072 THR B	3.99	71.21	-1.08	-0.27	25.25	79
    56	200063 LYS A, 200003 LEU B, 200001 ASP B, 100072 THR B, 100070 ASP B	4.15	71.6	-1.56	-0.42	30.14	81
    57	200003 LEU B, 200001 ASP B, 100072 THR B, 100070 ASP B	4.01	72.37	-0.98	-0.43	25.3	83
    58	200003 LEU B, 100072 THR B, 100070 ASP B, 200001 ASP B	3.94	72.52	-0.2	-0.37	13.72	82
    59	200003 LEU B, 100070 ASP B, 200001 ASP B	3.11	74.46	-0.03	-0.23	17.74	70
    60	200003 LEU B, 100070 ASP B	2.2	77.35	0.15	0.05	24.92	70
    61	200003 LEU B, 100070 ASP B, 200026 SER B	2.16	80.12	-0.17	-0.29	17.17	85
    62	200003 LEU B, 100070 ASP B, 200026 SER B, 100024 ARG B	2.48	82.17	-1.25	-0.32	25.88	85
    63	100070 ASP B, 200026 SER B, 100024 ARG B	3.29	83.71	-2.93	-0.81	34.46	95
    64	100070 ASP B, 100024 ARG B, 200026 SER B	3.64	84.79	-2.8	-0.75	35.03	84
    65	100070 ASP B, 100024 ARG B, 200026 SER B, 100069 THR B	3.73	86.2	-2.28	-0.76	26.69	92
    66	100024 ARG B, 200026 SER B, 100069 THR B	4.27	87.7	-1.87	-0.66	19.01	95
    67	100024 ARG B, 200026 SER B, 100069 THR B, 100026 SER B	4.87	88.73	-1.5	-0.7	15.11	95
    68	200026 SER B, 100069 THR B, 100026 SER B	4.45	91.48	-0.5	-0.79	2.81	107
    69	200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B	4.46	92.37	-0.48	-0.79	2.95	107
    70	200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B, 100028 SER B	4.54	94.55	-0.46	-0.79	3.04	107
    71	200026 SER B, 100027 GLN B, 100028 SER B, 200027 GLN B	5.13	94.83	-1.28	-0.92	2.99	100
    72	200026 SER B, 100069 THR B, 100028 SER B, 200027 GLN B	4.17	97.73	-1.35	-0.91	2.56	102
    73	200026 SER B, 100028 SER B, 200027 GLN B	5.13	98.36	-1.57	-0.96	2.86	100
    74	100027 GLN B, 100028 SER B, 200027 GLN B	5.59	98.97	-1.57	-0.96	2.86	100
    75	100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B	6.05	99.91	-2.05	-0.99	3.03	95
    76	27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B	6.14	101.09	-2.05	-0.99	3.03	95
    77	100028 SER B, 200027 GLN B, 200028 SER B	5.03	104.5	-1.7	-1.01	2.29	106
    78	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.85	104.83	-2.4	-0.87	14.72	100
    79	200027 GLN B, 200028 SER B, 200093 ARG B	4.8	105.38	-2.93	-0.83	19.07	94
    80	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.65	105.81	-2.4	-0.87	14.72	100
    81	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.41	106.4	-2.3	-0.82	15.15	94
    82	100028 SER B, 200027 GLN B, 200093 ARG B	2.44	111.27	-2.93	-0.83	19.07	94
    83	100028 SER B, 200093 ARG B	2.92	111.96	-2.65	-0.7	26.84	100
    84	100028 SER B, 200093 ARG B, 200082 TYR C	3.2	113.48	-2.2	-0.09	18.43	83
    85	100028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B	3.91	113.8	-2.78	-0.18	26.82	83
    86	100028 SER B, 200082 TYR C, 100093 ARG B	4	114.09	-2.2	-0.09	18.43	83
    87	100028 SER B, 200082 TYR C, 100093 ARG B, 100058 GLN C	3.83	115.21	-2.53	-0.35	14.7	83
    88	100028 SER B, 200082 TYR C, 100058 GLN C	3.17	117.88	-1.87	-0.32	2.27	83
    89	100028 SER B, 200082 TYR C, 100058 GLN C, 100030 GLY B	3.11	118.77	-1.5	-0.44	2.55	83
    90	200082 TYR C, 100058 GLN C, 100030 GLY B, 100092 ASN B	3.14	120.71	-2.18	-0.39	2.98	79
    91	200082 TYR C, 100030 GLY B, 100092 ASN B	3.25	121.04	-1.73	-0.15	2.79	77
    92	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C	3.32	121.8	-0.25	0.17	2.13	84
    93	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C	3.26	122.07	-1.1	0.05	12.1	83
    94	100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B	3.05	123.4	-1.54	-0.38	21.72	92
    95	100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B	3	124.33	-1.05	-0.28	26.3	89
    96	100030 GLY B, 200084 VAL C, 100064 ARG C	2.97	124.47	-0.23	-0.03	18.5	90
    97	100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B	2.94	124.57	-0.35	-0.22	14.29	96
    98	100030 GLY B, 100064 ARG C, 100031 THR B	2.94	124.59	-1.87	-0.66	19.01	95
    99	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	2.96	124.65	-2.2	-0.77	27.12	84
    100	100030 GLY B, 100064 ARG C, 100031 THR B	3.01	124.72	-1.87	-0.66	19.01	95
    101	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.91	124.98	-1.13	-0.28	25.87	93
    102	200084 VAL C, 100064 ARG C, 100031 THR B	2.82	125.19	-0.33	-0.02	17.93	96
    103	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.71	125.46	-1.13	-0.28	25.87	93
    104	200084 VAL C, 100064 ARG C, 100031 THR B	2.49	126.29	-0.33	-0.02	17.93	96
    105	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.38	128.2	-1.13	-0.28	25.87	93
    106	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C	2.52	128.87	-2.28	-0.76	26.69	92
    107	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 100050 TYR B	2.67	129.96	-2.08	-0.38	21.67	81
    108	100064 ARG C, 100031 THR B, 200084 VAL C, 100050 TYR B	2.91	130.5	-1.73	-0.22	14.66	80
    109	100064 ARG C, 100031 THR B, 100050 TYR B	2.88	130.6	-2.17	-0.03	18.42	80
    110	100031 THR B, 100050 TYR B, 100053 GLU B	2.82	130.68	-1.83	-0.27	17.72	78
    111	100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B	2.79	132.21	-1.48	-0.4	14.14	78
    112	100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B, 200085 THR C	3.11	132.63	-1.26	-0.48	11.99	78
    113	100031 THR B, 200084 VAL C, 100053 GLU B, 200085 THR C	3.09	133.52	-1.33	-0.87	14.15	97
    114	100031 THR B, 200084 VAL C, 100053 GLU B, 200085 THR C, 200054 ALA C	2.91	134.72	-0.7	-0.69	11.32	97
    115	100031 THR B, 100053 GLU B, 200085 THR C, 200054 ALA C	2.87	135.28	-0.78	-0.67	13.31	97
    116	100053 GLU B, 200085 THR C, 200054 ALA C	2.89	136.51	-0.8	-0.63	17.19	94
    117	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C	3.07	138.38	-0.7	-0.67	13.74	94
    118	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A	3.55	138.96	-1.46	-0.62	21.39	91
    119	100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A	3.77	139.41	-2.28	-0.78	26.74	89
    120	100053 GLU B, 200053 GLY C, 200057 ARG A	3.83	140.31	-2.8	-0.79	35.09	80

    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, 300058 GLN C, 300030 GLY B, 300092 ASN B, 100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B, 300031 THR B, 100084 VAL C, 300050 TYR B, 300053 GLU B, 100085 THR C, 100054 ALA C, 100053 GLY C, 100057 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, 100028 SER B, 27 GLN B, 200027 GLN B, 200028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300058 GLN C, 300092 ASN B, 100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B, 300050 TYR B, 300053 GLU B, 100085 THR C, 100054 ALA C, 100057 ARG A

    Physicochemical properties of lining side-chains

    Charge: 2 (8-6)
    Hydropathy: -1.4
    Hydrophobicity: -0.44
    Polarity: 14.93
    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	0.25	-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	3.21	0.71	-1.53	-0.78	2.81	105
    4	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.22	1.01	-1.33	-0.78	2.52	106
    5	100156 THR A, 100157 VAL A, 100041 ASN B	3.04	1.41	-1.53	-0.78	2.81	105
    6	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	2.92	1.92	-1.14	-0.78	2.69	106
    7	100170 THR A, 100041 ASN B, 100155 VAL A	2.62	5.6	-1.53	-0.78	2.81	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.67	6.6	-0.2	-0.3	2.14	88
    9	100170 THR A, 100041 ASN B, 100182 LEU A	2.76	6.95	-0.13	-0.13	1.72	88
    10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.75	7.13	-0.03	-0.14	2.3	79
    11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.66	7.98	-0.13	-0.31	2.57	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.51	8.51	-0.8	-0.47	12.03	78
    13	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.43	8.98	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.36	9.54	-1.95	-0.88	15.01	90
    15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.33	12.81	-2.25	-0.7	14.56	79
    16	100041 ASN B, 100153 GLU A, 100172 PRO A	3.11	13.46	-2.87	-0.67	18.29	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.47	13.99	-2.55	-0.52	14.11	74
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.52	14.61	-2.55	-0.52	14.11	74
    19	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.37	16.81	-1.78	-0.53	14.11	64
    20	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.32	18.64	-1.7	-0.23	14.12	61
    21	100173 ALA A, 100041 PRO A, 100180 TYR A	3.52	21.08	-1.1	0.07	2.19	54
    22	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.41	21.42	0.13	0.34	1.68	54
    23	100041 PRO A, 100180 TYR A, 100175 LEU A	4.39	22.11	0.3	0.72	1.11	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.48	22.49	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.02	27.24	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	27.82	-0.06	0.08	1.67	69
    27	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.13	28.13	0.23	0.08	1.27	84
    28	100180 TYR A, 100091 SER A, 100088 SER A	4.21	28.25	-0.97	-0.28	1.65	94
    29	100091 SER A, 100088 SER A	4.29	28.34	-0.8	-0.97	1.67	117
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.37	28.5	-0.97	-0.28	1.65	94
    31	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	28.96	0.23	0.08	1.27	84
    32	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.52	29.3	0.02	0.3	1.25	69
    33	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.54	29.73	0.15	-0.22	1.26	86
    34	100041 PRO A, 100091 SER A, 100088 SER A	4.57	30.68	-1.07	-0.68	1.64	97
    35	100041 PRO A, 100088 SER A	4.75	31.84	-1.2	-0.53	1.63	87
    36	100041 PRO A, 100088 SER A, 100040 ARG A	4.42	34.37	-2.3	-0.49	18.42	86
    37	100041 PRO A, 100088 SER A, 100040 ARG A	2.94	36.52	-2.17	-0.44	18.99	70
    38	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.78	36.86	-1.73	-0.53	15.09	70
    39	100088 SER A, 100040 ARG A, 100091 SER A	1.14	38.5	-1.77	-0.67	19.59	83
    40	100088 SER A, 100040 ARG A	0.6	39.61	-2.45	-0.61	27.69	83
    41	100040 ARG A	0.31	45.39	-4.5	-0.42	52	83
    42	100040 ARG A, 100043 HIS A	2.56	46.51	-3.85	-0.08	51.8	87
    43	100040 ARG A, 100046 GLU A	3.28	50.56	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	3.82	52.63	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.58	56.39	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.37	59.68	-0.98	-0.14	26.35	87
    47	100046 GLU A, 100064 ILE A, 100063 LYS A	3.24	60.46	0.2	-0.04	17.8	90
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.01	64.93	-0.97	0.09	33.18	84
    49	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.66	65.36	-0.93	-0.18	25.3	92
    50	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.69	66.34	-1.1	-0.35	25.3	80
    51	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.41	69.56	0.23	0.35	24.92	76
    52	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.13	70.51	-1	-0.3	25.73	67
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	3.98	71.14	-1.5	-0.4	21.26	76
    54	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.93	71.43	-2.4	-0.78	21.56	90
    55	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	3.96	71.79	-2.03	-0.87	14.58	96
    56	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.19	72.01	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4.11	72.59	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.95	72.99	-0.3	-0.21	13.67	77
    59	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.75	73.42	-1.08	-0.2	13.67	84
    60	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.41	75.38	-1.08	-0.27	25.25	79
    61	100063 LYS A, 100003 LEU B, 100001 ASP B	3.5	77.12	-1.2	-0.1	33.11	70
    62	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.9	78.04	-1.08	-0.27	25.25	79
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.14	78.24	-1.56	-0.42	30.14	81
    64	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.97	79.12	-0.98	-0.43	25.3	83
    65	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	3.92	79.28	-0.2	-0.37	13.72	82
    66	100003 LEU B, 300070 ASP B, 100001 ASP B	2.93	81.61	-0.03	-0.23	17.74	70
    67	100003 LEU B, 300070 ASP B	2.21	84.21	0.15	0.05	24.92	70
    68	100003 LEU B, 300070 ASP B, 100026 SER B	2.16	87.12	-0.17	-0.29	17.17	85
    69	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.6	88.83	-1.25	-0.32	25.88	85
    70	300070 ASP B, 100026 SER B, 300024 ARG B	3.23	90.45	-2.93	-0.81	34.46	95
    71	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	91.4	-2.8	-0.75	35.03	84
    72	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.7	93.41	-2.28	-0.76	26.69	92
    73	300024 ARG B, 100026 SER B, 300069 THR B	4.41	94.42	-1.87	-0.66	19.01	95
    74	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.91	95.58	-1.5	-0.7	15.11	95
    75	100026 SER B, 300069 THR B, 300026 SER B	4.38	98.7	-0.5	-0.79	2.81	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.41	99.61	-0.48	-0.79	2.95	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.56	101.23	-0.46	-0.79	3.04	107
    78	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.15	101.39	-0.58	-0.84	2.52	112
    79	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.19	101.54	-1.28	-0.92	2.99	100
    80	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.16	104.78	-1.35	-0.91	2.56	102
    81	300027 GLN B, 300028 SER B, 100027 GLN B	5.29	105.45	-1.57	-0.96	2.86	100
    82	300028 SER B, 100027 GLN B, 300027 GLN B	5.59	106.05	-2.6	-1.06	2.91	95
    83	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	5.88	106.53	-2.05	-0.99	3.03	95
    84	300028 SER B, 100027 GLN B, 100028 SER B	6.13	106.84	-1.7	-1.01	2.29	106
    85	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.36	107.83	-2.05	-0.99	3.03	95
    86	300028 SER B, 100027 GLN B, 100028 SER B	4.84	111.33	-1.7	-1.01	2.29	106
    87	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.78	111.61	-2.4	-0.87	14.72	100
    88	100027 GLN B, 100028 SER B, 100093 ARG B	4.86	112.02	-2.93	-0.83	19.07	94
    89	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.69	112.99	-2.4	-0.87	14.72	100
    90	300028 SER B, 100027 GLN B, 100093 ARG B	2.42	118.16	-2.93	-0.83	19.07	94
    91	300028 SER B, 100093 ARG B	2.91	118.88	-2.65	-0.7	26.84	100
    92	300028 SER B, 100093 ARG B, 100082 TYR C	3.23	120.36	-2.2	-0.09	18.43	83
    93	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.01	120.68	-2.78	-0.18	26.82	83
    94	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.73	122.31	-2.53	-0.35	14.7	83
    95	300028 SER B, 100082 TYR C, 300058 GLN C	3.21	124.59	-1.87	-0.32	2.27	83
    96	300028 SER B, 100082 TYR C, 300058 GLN C, 300030 GLY B	3.12	125.31	-1.5	-0.44	2.55	83
    97	100082 TYR C, 300058 GLN C, 300030 GLY B, 300092 ASN B	3.11	127.4	-2.18	-0.39	2.98	79
    98	100082 TYR C, 300030 GLY B, 300092 ASN B	3.22	127.75	-1.73	-0.15	2.79	77
    99	100082 TYR C, 300030 GLY B, 300092 ASN B, 100084 VAL C	3.23	128.41	-0.25	0.17	2.13	84
    100	100082 TYR C, 300030 GLY B, 300092 ASN B, 100084 VAL C, 300064 ARG C	3.24	128.68	-1.1	0.05	12.1	83
    101	300030 GLY B, 300092 ASN B, 100084 VAL C, 300064 ARG C, 300032 ASP B	3.11	129.97	-1.54	-0.38	21.72	92
    102	300030 GLY B, 100084 VAL C, 300064 ARG C, 300032 ASP B	2.96	131.02	-1.05	-0.28	26.3	89
    103	300030 GLY B, 100084 VAL C, 300064 ARG C	2.94	131.19	-0.23	-0.03	18.5	90
    104	300030 GLY B, 100084 VAL C, 300064 ARG C, 300031 THR B	2.94	131.3	-0.35	-0.22	14.29	96
    105	300030 GLY B, 300064 ARG C, 300031 THR B	2.96	131.32	-1.87	-0.66	19.01	95
    106	300030 GLY B, 300064 ARG C, 300032 ASP B, 300031 THR B	2.98	131.35	-2.2	-0.77	27.12	84
    107	300030 GLY B, 300064 ARG C, 300032 ASP B, 300031 THR B	3.02	131.39	-2.28	-0.76	26.69	92
    108	300030 GLY B, 300064 ARG C, 300031 THR B	3	131.48	-1.87	-0.66	19.01	95
    109	100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B	2.95	131.61	-1.13	-0.28	25.87	93
    110	100084 VAL C, 300064 ARG C, 300031 THR B	2.76	132.05	-0.33	-0.02	17.93	96
    111	100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B	2.65	132.39	-1.13	-0.28	25.87	93
    112	100084 VAL C, 300064 ARG C, 300031 THR B	2.55	132.84	-0.33	-0.02	17.93	96
    113	100084 VAL C, 300064 ARG C, 300032 ASP B, 300031 THR B	2.4	134.81	-1.13	-0.28	25.87	93
    114	300064 ARG C, 300032 ASP B, 300031 THR B, 100084 VAL C	2.42	136.17	-2.28	-0.76	26.69	92
    115	300064 ARG C, 300032 ASP B, 300031 THR B, 100084 VAL C, 300050 TYR B	2.58	136.69	-2.08	-0.38	21.67	81
    116	300064 ARG C, 300031 THR B, 100084 VAL C, 300050 TYR B	2.68	137.24	-1.73	-0.22	14.66	80
    117	300064 ARG C, 300031 THR B, 300050 TYR B	2.84	137.34	-2.17	-0.03	18.42	80
    118	300031 THR B, 300050 TYR B, 300053 GLU B	2.88	137.43	-1.83	-0.27	17.72	78
    119	300031 THR B, 100084 VAL C, 300050 TYR B, 300053 GLU B	2.92	139.15	-1.48	-0.4	14.14	78
    120	300031 THR B, 100084 VAL C, 300053 GLU B, 100085 THR C	3.09	140.19	-1.33	-0.87	14.15	97
    121	300031 THR B, 100084 VAL C, 300053 GLU B, 100085 THR C, 100054 ALA C	3	141.49	-0.7	-0.69	11.32	97
    122	300031 THR B, 300053 GLU B, 100085 THR C, 100054 ALA C	3	142.09	-0.78	-0.67	13.31	97
    123	300053 GLU B, 100085 THR C, 100054 ALA C	2.99	143.38	-0.8	-0.63	17.19	94
    124	300053 GLU B, 100085 THR C, 100054 ALA C, 100053 GLY C	3.04	145	-0.7	-0.67	13.74	94
    125	300053 GLU B, 100085 THR C, 100054 ALA C, 100053 GLY C, 100057 ARG A	3.5	145.64	-1.46	-0.62	21.39	91
    126	300053 GLU B, 100085 THR C, 100053 GLY C, 100057 ARG A	3.79	146.09	-2.28	-0.78	26.74	89
    127	300053 GLU B, 100053 GLY C, 100057 ARG A	3.83	147.03	-2.8	-0.79	35.09	80

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    300046 GLU A, 300061 ASN A, 300063 LYS A, 300003 LEU B, 300098 PHE B, 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, 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, 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

    300046 GLU A, 300061 ASN A, 300063 LYS A, 300003 LEU B, 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: 3 (7-4)
    Hydropathy: -1
    Hydrophobicity: -0.37
    Polarity: 11.83
    Mutability: 86
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	300046 GLU A, 300061 ASN A, 300063 LYS A, 300003 LEU B, 300098 PHE B	4.26	1.42	-1.5	-0.4	21.26	76
    2	300046 GLU A, 300063 LYS A, 300003 LEU B, 300098 PHE B	4.73	2.74	-1	-0.3	25.73	67
    3	300046 GLU A, 300063 LYS A, 300003 LEU B, 300064 ILE A	5.15	5.23	0.23	0.35	24.92	76
    4	300046 GLU A, 300063 LYS A, 300003 LEU B, 20 SER B	5.38	6.05	-1.1	-0.35	25.3	80
    5	300046 GLU A, 300063 LYS A, 300064 ILE A	2.92	10.86	-0.97	0.09	33.18	84
    6	300046 GLU A, 300064 ILE A, 300063 LYS A	3.05	11.69	0.2	-0.04	17.8	90
    7	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.31	15.01	-0.98	-0.14	26.35	87
    8	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.53	18	-2	-0.04	38.51	86
    9	300046 GLU A, 18 ARG B, 300040 ARG A	3.92	20.52	-4.17	-0.66	51.3	81
    10	300046 GLU A, 300064 ILE A, 300040 ARG A	4.05	21.59	-1.17	0.08	34.01	87
    11	300046 GLU A, 300040 ARG A	2.98	24.09	-4	-0.78	50.95	80
    12	300040 ARG A	1.23	30.7	-4.5	-0.42	52	83
    13	300040 ARG A, 300088 SER A	1.25	31.59	-2.45	-0.61	27.69	83
    14	300040 ARG A, 300088 SER A, 300091 SER A	1.51	32.05	-1.77	-0.67	19.59	83
    15	300040 ARG A, 300088 SER A, 300091 SER A	1.91	32.31	-1.9	-0.73	19.02	100
    16	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.35	32.59	-1.83	-0.57	14.66	86
    17	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.74	33.41	-1.73	-0.53	15.09	70
    18	300040 ARG A, 300088 SER A, 300041 PRO A	3.23	36.07	-2.17	-0.44	18.99	70
    19	300040 ARG A, 300041 PRO A, 300088 SER A	4.55	37.86	-2.3	-0.49	18.42	86
    20	300041 PRO A, 300088 SER A	4.79	39.33	-1.2	-0.53	1.63	87
    21	300091 SER A, 300041 PRO A, 300088 SER A	4.69	39.81	-1.07	-0.68	1.64	97
    22	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.6	40.23	0.15	-0.22	1.26	86
    23	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.5	40.53	0.02	0.3	1.25	69
    24	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.27	40.95	0.23	0.08	1.27	84
    25	300091 SER A, 300088 SER A, 300180 TYR A	4.02	41.52	-0.97	-0.28	1.65	94
    26	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.01	42.17	0.23	0.08	1.27	84
    27	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.02	43.08	-0.06	0.08	1.67	69
    28	300041 PRO A, 300175 LEU A, 300180 TYR A	4.07	46.98	0.3	0.72	1.11	54
    29	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.48	47.3	0.13	0.34	1.68	54
    30	300041 PRO A, 300175 LEU A, 300180 TYR A	4.38	48.04	0.3	0.72	1.11	54
    31	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.21	48.9	0.13	0.34	1.68	54
    32	300041 PRO A, 300180 TYR A, 300173 ALA A	3.72	50.72	-1.1	0.07	2.19	54
    33	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.4	52.67	-1.7	-0.23	14.12	61
    34	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.43	54.99	-1.78	-0.53	14.11	64
    35	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.38	55.59	-2.55	-0.52	14.11	74
    36	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.32	56.21	-2.55	-0.52	14.11	74
    37	300153 GLU A, 300172 PRO A, 300041 ASN B	3.06	57.08	-2.87	-0.67	18.29	79
    38	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.3	60.19	-2.25	-0.7	14.56	79
    39	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.43	60.72	-1.95	-0.88	15.01	90
    40	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.57	61.1	-0.8	-0.47	12.03	78
    41	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.7	61.41	-0.8	-0.47	12.03	78
    42	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.67	62.33	-0.13	-0.31	2.57	79
    43	300041 ASN B, 300182 LEU A, 300171 PHE A	2.76	62.53	-0.03	-0.14	2.3	79
    44	300041 ASN B, 300182 LEU A, 300170 THR A	2.76	62.82	-0.13	-0.13	1.72	88
    45	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.71	64.03	-0.2	-0.3	2.14	88
    46	300041 ASN B, 300170 THR A, 300155 VAL A	2.79	67.89	-1.53	-0.78	2.81	105
    47	300041 ASN B, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A	2.99	68.17	-1.14	-0.78	2.69	106
    48	300041 ASN B, 300156 THR A, 300157 VAL A	3.06	68.47	-1.53	-0.78	2.81	105
    49	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.18	68.64	-1.33	-0.78	2.52	106
    50	300041 ASN B, 300170 THR A, 300157 VAL A	3.19	68.75	-1.53	-0.78	2.81	105
    51	300041 ASN B, 300170 THR A, 300155 VAL A	3.18	68.91	-1.53	-0.78	2.81	105
    52	300041 ASN B, 300170 THR A, 300157 VAL A	3.23	69.12	-1.53	-0.78	2.81	105
    53	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.26	69.53	-1.33	-0.78	2.52	106
    54	300041 ASN B, 300170 THR A, 300157 VAL A	3.26	72.79	-1.53	-0.78	2.81	105
    55	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B	4.21	73.51	-1.25	-0.79	2.95	105
    56	300041 ASN B, 300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.57	73.64	-1.08	-0.79	3.04	105
    57	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A	4.62	73.78	0.68	-0.31	2.14	102
    58	300170 THR A, 300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.53	73.94	-1.16	-0.72	12.26	89
    59	300157 VAL A, 300040 THR B, 300168 VAL A, 300169 LYS B	4.52	73.99	-0.13	-0.22	14.1	85
    60	300170 THR A, 300157 VAL A, 300168 VAL A, 300169 LYS B	4.39	74.75	-0.2	-0.21	13.67	92
    61	300157 VAL A, 300168 VAL A, 300169 LYS B, 300165 SER A	4.26	75.12	-0.13	-0.22	14.1	85
    62	300168 VAL A, 300169 LYS B, 300165 SER A	1.97	79.73	-0.03	-0.03	17.67	85
    63	300168 VAL A, 300169 LYS B, 300165 SER A	1.32	81.39	-1.57	-0.67	18.75	72
    64	300168 VAL A, 300169 LYS B, 300165 SER A, 300167 GLY A	1.52	82.59	-1.28	-0.7	14.91	72
    65	300168 VAL A, 300169 LYS B, 300167 GLY A	1.66	83.77	-1.57	-0.67	18.75	72
    66	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.84	84.06	-1.98	-0.44	26.97	81
    67	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	2	84.16	-1.98	-0.44	26.97	81
    68	300168 VAL A, 300169 LYS B, 300167 GLY A, 300169 HIS A	1.86	84.6	-1.98	-0.44	26.97	81
    69	300169 LYS B, 300167 GLY A, 300169 HIS A, 300167 ASP B	1.71	85.15	-2.75	-0.5	38.55	83
    70	300169 LYS B, 300167 GLY A, 300167 ASP B	1.59	86.4	-2.6	-0.75	34.19	79
    71	300169 LYS B, 300167 GLY A	1.57	87.13	-2.15	-0.61	26.44	72
    72	300169 LYS B, 300167 GLY A, 300166 SER A	1.58	88.69	-1.57	-0.67	18.75	72
    73	300169 LYS B, 300167 GLY A, 300166 SER A	1.77	92.1	-1.7	-0.73	18.18	94
    74	300169 LYS B, 300167 GLY A, 300166 SER A, 300170 ASP B	3.44	93.66	-2.15	-0.81	26.06	91
    75	300167 GLY A, 300166 SER A, 300170 ASP B, 300169 LYS B	4.28	94.11	-1.28	-0.9	14.53	101
    76	300167 GLY A, 300166 SER A, 300170 ASP B	4.45	95.25	-1.57	-0.94	18.25	101
    77	300167 GLY A, 300166 SER A, 300170 ASP B, 300140 MET A	4.93	96.14	-0.7	-0.45	14.05	98
    78	300167 GLY A, 300170 ASP B, 300140 MET A	4.22	97.72	-0.67	-0.28	18.17	89
    79	300167 GLY A, 300170 ASP B, 300140 MET A, 300138 ASN B	3.89	98.92	-1.38	-0.4	14.47	94
    80	300170 ASP B, 300140 MET A, 300138 ASN B	3.95	100.48	-1.7	-0.27	18.17	94
    81	300140 MET A, 300138 ASN B, 300187 THR A	3.57	102.42	-0.77	-0.18	2.16	101
    82	300140 MET A, 300138 ASN B, 300187 THR A, 300114 THR B	2.84	103.86	-0.75	-0.33	2.03	102
    83	300140 MET A, 300187 THR A, 300114 THR B	2.63	106.15	0.17	-0.18	1.58	102
    84	300140 MET A, 300114 THR B	2.77	106.87	0.6	0.12	1.55	100
    85	300140 MET A, 300114 THR B, 300138 ASN A	2.91	107.43	-0.77	-0.18	2.16	101
    86	300140 MET A, 300114 THR B, 300138 ASN A, 300139 SER A	2.92	108.72	-0.78	-0.38	2.04	105
    87	300140 MET A, 300114 THR B, 300138 ASN A	2.61	111.28	-0.77	-0.18	2.16	101
    88	300114 THR B, 300138 ASN A	3.16	114.63	-2.1	-0.77	2.52	105
    89	300114 THR B, 300138 ASN A, 300113 PRO B	3.78	115.19	-1.53	-0.78	2.81	105
    90	300114 THR B, 300138 ASN A, 300113 PRO B, 300207 LYS B	3.67	115.74	-2.13	-0.69	14.48	94
    91	300114 THR B, 300138 ASN A, 300207 LYS B	3.24	117.55	-2.7	-0.65	18.18	94
    92	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B	3.05	118.55	-2.13	-0.69	14.48	94
    93	300114 THR B, 300138 ASN A, 300207 LYS B, 300136 GLN A	2.93	119.37	-2.13	-0.69	14.48	94
    94	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.76	120.34	-1.78	-0.71	12.26	94
    95	300114 THR B, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.71	120.71	-1.35	-0.7	14.48	89
    96	300114 THR B, 300138 ASN A, 300207 LYS B, 300115 VAL B, 300136 GLN A	2.67	121.29	-1.78	-0.71	12.26	94
    97	300114 THR B, 300138 ASN A, 300115 VAL B, 300136 GLN A, 300116 SER B	2.65	121.64	-1.16	-0.82	2.69	109
    98	300114 THR B, 300115 VAL B, 300136 GLN A, 300116 SER B, 300140 MET A	2.61	123.16	-0.54	-0.83	2.69	112
    99	300207 LYS B, 300115 VAL B, 300136 GLN A, 300116 SER B	2.59	123.79	-1.38	-0.75	14.48	94
    100	300115 VAL B, 300136 GLN A, 300116 SER B	2.49	124.9	-0.53	-0.86	2.81	117
    101	300115 VAL B, 300136 GLN A, 300116 SER B, 300135 ALA A	2.28	125.6	0.05	-0.64	2.11	108
    102	300115 VAL B, 300116 SER B, 300135 ALA A	2.25	126.65	0.2	-0.58	1.68	108
    103	300116 SER B, 300135 ALA A, 300117 ILE B	1.96	129.35	0.2	-0.58	1.68	108
    104	300135 ALA A, 300117 ILE B, 300116 SER B	1.88	129.82	0.33	-0.53	2.25	100
    105	300135 ALA A, 300116 SER B, 300117 ILE B	1.72	130.75	1.97	0.34	1.17	101
    106	300135 ALA A, 300117 ILE B	1.67	131.82	3.15	0.92	0.07	101
    107	300135 ALA A, 300117 ILE B, 300208 SER B	1.7	132.36	1.97	0.34	1.17	101
    108	300135 ALA A, 300117 ILE B, 300208 SER B, 300132 GLY A	1.75	133.22	1.38	0.06	1.72	101
    109	300135 ALA A, 300117 ILE B, 300132 GLY A	1.85	133.71	1.97	0.34	1.17	101
    110	300117 ILE B, 300132 GLY A, 300209 PHE B	1.58	135.13	2.3	0.79	1.29	77
    111	300117 ILE B, 300132 GLY A, 300209 PHE B, 300119 PRO B	1.56	135.57	0.1	-0.09	2.17	54
    112	300117 ILE B, 300132 GLY A, 300119 PRO B	1.56	135.71	-0.8	-0.56	2.78	58
    113	300117 ILE B, 300132 GLY A, 300119 PRO B	1.49	135.89	0.83	0.31	1.7	80
    114	300117 ILE B, 300132 GLY A, 300119 PRO B	1.46	136.27	-0.8	-0.56	2.78	58
    115	300132 GLY A, 300209 PHE B, 300119 PRO B	1.45	140.29	0.27	0.15	1.77	54
    116	300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B	1.96	140.78	0.1	-0.09	2.17	54
    117	300132 GLY A, 300209 PHE B, 300119 PRO B, 300210 ASN B, 300133 SER A	2.08	141.35	0	-0.23	2.41	54
    118	300132 GLY A, 300119 PRO B, 300210 ASN B, 300133 SER A, 300218 ARG A	2.22	142.36	-1.46	-0.58	12.74	70
    119	300132 GLY A, 300119 PRO B, 300210 ASN B, 300218 ARG A	2.34	142.61	-1.73	-0.53	15.09	70
    120	300119 PRO B, 300210 ASN B, 300218 ARG A	2.06	144.02	-2.17	-0.44	18.99	70
    121	300209 PHE B, 300119 PRO B, 300210 ASN B, 300218 ARG A	2.05	144.49	-0.93	0.01	14.33	64
    122	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B	1.99	145.18	-1.73	-0.53	15.09	70
    123	300119 PRO B, 300210 ASN B, 300218 ARG A, 300211 ARG B, 300186 TYR B	1.96	145.33	-1.64	-0.2	12.39	63
    124	300119 PRO B, 300218 ARG A, 300211 ARG B, 300186 TYR B	1.93	146.63	-1.95	-0.05	14.64	63
    125	300218 ARG A, 300211 ARG B, 300186 TYR B	2.04	147.3	-2.07	-0.04	19	66
    126	300218 ARG A, 300186 TYR B, 300211 ARG B	2.15	148.79	-3.43	0.09	35.2	72
    127	300218 ARG A, 300186 TYR B, 300211 ARG B, 300125 LEU B	2.41	148.79	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 98 PHE B, 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, 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, 113 PRO B, 207 LYS B, 115 VAL B, 136 GLN A, 116 SER B, 140 MET A, 135 ALA A, 117 ILE B, 116 SER B, 117 ILE B, 208 SER B, 132 GLY A, 209 PHE B, 119 PRO B, 210 ASN B, 133 SER A, 218 ARG A, 211 ARG B, 186 TYR B, 211 ARG B, 125 LEU B

    Unique lining residues set - sidechains

    46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 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, 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, 207 LYS B, 116 SER B, 135 ALA A, 117 ILE B, 209 PHE B, 119 PRO B, 218 ARG A, 186 TYR B, 211 ARG B, 125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 3 (7-4)
    Hydropathy: -1
    Hydrophobicity: -0.37
    Polarity: 11.83
    Mutability: 86
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	46 GLU A, 61 ASN A, 63 LYS A, 3 LEU B, 98 PHE B	4.26	1.42	-1.5	-0.4	21.26	76
    2	46 GLU A, 63 LYS A, 3 LEU B, 98 PHE B	4.73	2.74	-1	-0.3	25.73	67
    3	46 GLU A, 63 LYS A, 3 LEU B, 64 ILE A	5.15	5.23	0.23	0.35	24.92	76
    4	46 GLU A, 63 LYS A, 3 LEU B, 200020 SER B	5.38	6.05	-1.1	-0.35	25.3	80
    5	46 GLU A, 63 LYS A, 64 ILE A	2.92	10.86	-0.97	0.09	33.18	84
    6	46 GLU A, 64 ILE A, 63 LYS A	3.05	11.69	0.2	-0.04	17.8	90
    7	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.31	15.01	-0.98	-0.14	26.35	87
    8	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.53	18	-2	-0.04	38.51	86
    9	46 GLU A, 200018 ARG B, 40 ARG A	3.92	20.52	-4.17	-0.66	51.3	81
    10	46 GLU A, 64 ILE A, 40 ARG A	4.05	21.59	-1.17	0.08	34.01	87
    11	46 GLU A, 40 ARG A	2.98	24.09	-4	-0.78	50.95	80
    12	40 ARG A	1.23	30.7	-4.5	-0.42	52	83
    13	40 ARG A, 88 SER A	1.25	31.59	-2.45	-0.61	27.69	83
    14	40 ARG A, 88 SER A, 91 SER A	1.51	32.05	-1.77	-0.67	19.59	83
    15	40 ARG A, 88 SER A, 91 SER A	1.91	32.31	-1.9	-0.73	19.02	100
    16	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.35	32.59	-1.83	-0.57	14.66	86
    17	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.74	33.41	-1.73	-0.53	15.09	70
    18	40 ARG A, 88 SER A, 41 PRO A	3.23	36.07	-2.17	-0.44	18.99	70
    19	40 ARG A, 41 PRO A, 88 SER A	4.55	37.86	-2.3	-0.49	18.42	86
    20	41 PRO A, 88 SER A	4.79	39.33	-1.2	-0.53	1.63	87
    21	91 SER A, 41 PRO A, 88 SER A	4.69	39.81	-1.07	-0.68	1.64	97
    22	91 SER A, 41 PRO A, 88 SER A, 175 LEU A	4.6	40.23	0.15	-0.22	1.26	86
    23	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.5	40.53	0.02	0.3	1.25	69
    24	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.27	40.95	0.23	0.08	1.27	84
    25	91 SER A, 88 SER A, 180 TYR A	4.02	41.52	-0.97	-0.28	1.65	94
    26	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.01	42.17	0.23	0.08	1.27	84
    27	88 SER A, 91 SER A, 41 PRO A, 175 LEU A, 180 TYR A	4.02	43.08	-0.06	0.08	1.67	69
    28	41 PRO A, 175 LEU A, 180 TYR A	4.07	46.98	0.3	0.72	1.11	54
    29	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.48	47.3	0.13	0.34	1.68	54
    30	41 PRO A, 175 LEU A, 180 TYR A	4.38	48.04	0.3	0.72	1.11	54
    31	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.21	48.9	0.13	0.34	1.68	54
    32	41 PRO A, 180 TYR A, 173 ALA A	3.72	50.72	-1.1	0.07	2.19	54
    33	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.4	52.67	-1.7	-0.23	14.12	61
    34	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.43	54.99	-1.78	-0.53	14.11	64
    35	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.38	55.59	-2.55	-0.52	14.11	74
    36	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.32	56.21	-2.55	-0.52	14.11	74
    37	153 GLU A, 172 PRO A, 41 ASN B	3.06	57.08	-2.87	-0.67	18.29	79
    38	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.3	60.19	-2.25	-0.7	14.56	79
    39	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.43	60.72	-1.95	-0.88	15.01	90
    40	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.57	61.1	-0.8	-0.47	12.03	78
    41	153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.7	61.41	-0.8	-0.47	12.03	78
    42	41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.67	62.33	-0.13	-0.31	2.57	79
    43	41 ASN B, 182 LEU A, 171 PHE A	2.76	62.53	-0.03	-0.14	2.3	79
    44	41 ASN B, 182 LEU A, 170 THR A	2.76	62.82	-0.13	-0.13	1.72	88
    45	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.71	64.03	-0.2	-0.3	2.14	88
    46	41 ASN B, 170 THR A, 155 VAL A	2.79	67.89	-1.53	-0.78	2.81	105
    47	41 ASN B, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A	2.99	68.17	-1.14	-0.78	2.69	106
    48	41 ASN B, 156 THR A, 157 VAL A	3.06	68.48	-1.53	-0.78	2.81	105
    49	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.19	68.64	-1.33	-0.78	2.52	106
    50	41 ASN B, 170 THR A, 157 VAL A	3.19	68.75	-1.53	-0.78	2.81	105
    51	41 ASN B, 170 THR A, 155 VAL A	3.18	68.9	-1.53	-0.78	2.81	105
    52	41 ASN B, 170 THR A, 157 VAL A	3.23	69.12	-1.53	-0.78	2.81	105
    53	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.26	69.53	-1.33	-0.78	2.52	106
    54	41 ASN B, 170 THR A, 157 VAL A	3.26	72.79	-1.53	-0.78	2.81	105
    55	41 ASN B, 170 THR A, 157 VAL A, 40 THR B	4.21	73.51	-1.25	-0.79	2.95	105
    56	41 ASN B, 170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.57	73.64	-1.08	-0.79	3.04	105
    57	170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.62	73.78	0.68	-0.31	2.14	102
    58	170 THR A, 157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.53	73.94	-1.16	-0.72	12.26	89
    59	157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.52	73.99	-0.13	-0.22	14.1	85
    60	170 THR A, 157 VAL A, 168 VAL A, 169 LYS B	4.39	74.75	-0.2	-0.21	13.67	92
    61	157 VAL A, 168 VAL A, 169 LYS B, 165 SER A	4.26	75.12	-0.13	-0.22	14.1	85
    62	168 VAL A, 169 LYS B, 165 SER A	1.97	79.73	-0.03	-0.03	17.67	85
    63	168 VAL A, 169 LYS B, 165 SER A	1.32	81.39	-1.57	-0.67	18.75	72
    64	168 VAL A, 169 LYS B, 165 SER A, 167 GLY A	1.52	82.59	-1.28	-0.7	14.91	72
    65	168 VAL A, 169 LYS B, 167 GLY A	1.66	83.77	-1.57	-0.67	18.75	72
    66	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.84	84.06	-1.98	-0.44	26.97	81
    67	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	2	84.16	-1.98	-0.44	26.97	81
    68	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.86	84.6	-1.98	-0.44	26.97	81
    69	169 LYS B, 167 GLY A, 169 HIS A, 167 ASP B	1.71	85.15	-2.75	-0.5	38.55	83
    70	169 LYS B, 167 GLY A, 167 ASP B	1.59	86.4	-2.6	-0.75	34.19	79
    71	169 LYS B, 167 GLY A	1.57	87.13	-2.15	-0.61	26.44	72
    72	169 LYS B, 167 GLY A, 166 SER A	1.58	88.69	-1.57	-0.67	18.75	72
    73	169 LYS B, 167 GLY A, 166 SER A	1.77	92.09	-1.7	-0.73	18.18	94
    74	169 LYS B, 167 GLY A, 166 SER A, 170 ASP B	3.44	93.66	-2.15	-0.81	26.06	91
    75	167 GLY A, 166 SER A, 170 ASP B, 169 LYS B	4.28	94.11	-1.28	-0.9	14.53	101
    76	167 GLY A, 166 SER A, 170 ASP B	4.45	95.25	-1.57	-0.94	18.25	101
    77	167 GLY A, 166 SER A, 170 ASP B, 140 MET A	4.93	96.14	-0.7	-0.45	14.05	98
    78	167 GLY A, 170 ASP B, 140 MET A	4.22	97.72	-0.67	-0.28	18.17	89
    79	167 GLY A, 170 ASP B, 140 MET A, 138 ASN B	3.89	98.92	-1.38	-0.4	14.47	94
    80	170 ASP B, 140 MET A, 138 ASN B	3.95	100.48	-1.7	-0.27	18.17	94
    81	140 MET A, 138 ASN B, 187 THR A	3.57	102.42	-0.77	-0.18	2.16	101
    82	140 MET A, 138 ASN B, 187 THR A, 114 THR B	2.84	103.86	-0.75	-0.33	2.03	102
    83	140 MET A, 187 THR A, 114 THR B	2.63	106.15	0.17	-0.18	1.58	102
    84	140 MET A, 114 THR B	2.77	106.87	0.6	0.12	1.55	100
    85	140 MET A, 114 THR B, 138 ASN A	2.91	107.43	-0.77	-0.18	2.16	101
    86	140 MET A, 114 THR B, 138 ASN A, 139 SER A	2.92	108.71	-0.78	-0.38	2.04	105
    87	140 MET A, 114 THR B, 138 ASN A	2.61	111.28	-0.77	-0.18	2.16	101
    88	114 THR B, 138 ASN A	3.16	114.63	-2.1	-0.77	2.52	105
    89	114 THR B, 138 ASN A, 113 PRO B	3.78	115.19	-1.53	-0.78	2.81	105
    90	114 THR B, 138 ASN A, 113 PRO B, 207 LYS B	3.67	115.74	-2.13	-0.69	14.48	94
    91	114 THR B, 138 ASN A, 207 LYS B	3.24	117.55	-2.7	-0.65	18.18	94
    92	114 THR B, 138 ASN A, 207 LYS B, 115 VAL B	3.05	118.54	-2.13	-0.69	14.48	94
    93	114 THR B, 138 ASN A, 207 LYS B, 136 GLN A	2.93	119.36	-2.13	-0.69	14.48	94
    94	114 THR B, 138 ASN A, 207 LYS B, 115 VAL B, 136 GLN A	2.76	120.34	-1.78	-0.71	12.26	94
    95	114 THR B, 207 LYS B, 115 VAL B, 136 GLN A	2.71	120.71	-1.35	-0.7	14.48	89
    96	114 THR B, 138 ASN A, 207 LYS B, 115 VAL B, 136 GLN A	2.67	121.29	-1.78	-0.71	12.26	94
    97	114 THR B, 138 ASN A, 115 VAL B, 136 GLN A, 116 SER B	2.65	121.64	-1.16	-0.82	2.69	109
    98	114 THR B, 115 VAL B, 136 GLN A, 116 SER B, 140 MET A	2.61	123.15	-0.54	-0.83	2.69	112
    99	207 LYS B, 115 VAL B, 136 GLN A, 116 SER B	2.59	123.79	-1.38	-0.75	14.48	94
    100	115 VAL B, 136 GLN A, 116 SER B	2.49	124.9	-0.53	-0.86	2.81	117
    101	115 VAL B, 136 GLN A, 116 SER B, 135 ALA A	2.28	125.6	0.05	-0.64	2.11	108
    102	115 VAL B, 116 SER B, 135 ALA A	2.25	126.65	0.2	-0.58	1.68	108
    103	116 SER B, 135 ALA A, 117 ILE B	1.96	129.35	0.2	-0.58	1.68	108
    104	135 ALA A, 117 ILE B, 116 SER B	1.88	129.81	0.33	-0.53	2.25	100
    105	135 ALA A, 116 SER B, 117 ILE B	1.72	130.75	1.97	0.34	1.17	101
    106	135 ALA A, 117 ILE B	1.67	131.82	3.15	0.92	0.07	101
    107	135 ALA A, 117 ILE B, 208 SER B	1.7	132.36	1.97	0.34	1.17	101
    108	135 ALA A, 117 ILE B, 208 SER B, 132 GLY A	1.75	133.22	1.38	0.06	1.72	101
    109	135 ALA A, 117 ILE B, 132 GLY A	1.85	133.71	1.97	0.34	1.17	101
    110	117 ILE B, 132 GLY A, 209 PHE B	1.58	135.13	2.3	0.79	1.29	77
    111	117 ILE B, 132 GLY A, 209 PHE B, 119 PRO B	1.56	135.57	0.1	-0.09	2.17	54
    112	117 ILE B, 132 GLY A, 119 PRO B	1.56	135.7	-0.8	-0.56	2.78	58
    113	117 ILE B, 132 GLY A, 119 PRO B	1.49	135.89	0.83	0.31	1.7	80
    114	117 ILE B, 132 GLY A, 119 PRO B	1.46	136.27	-0.8	-0.56	2.78	58
    115	132 GLY A, 209 PHE B, 119 PRO B	1.45	140.29	0.27	0.15	1.77	54
    116	132 GLY A, 209 PHE B, 119 PRO B, 210 ASN B	1.96	140.78	0.1	-0.09	2.17	54
    117	132 GLY A, 209 PHE B, 119 PRO B, 210 ASN B, 133 SER A	2.08	141.35	0	-0.23	2.41	54
    118	132 GLY A, 119 PRO B, 210 ASN B, 133 SER A, 218 ARG A	2.22	142.36	-1.46	-0.58	12.74	70
    119	132 GLY A, 119 PRO B, 210 ASN B, 218 ARG A	2.34	142.61	-1.73	-0.53	15.09	70
    120	119 PRO B, 210 ASN B, 218 ARG A	2.05	144.02	-2.17	-0.44	18.99	70
    121	209 PHE B, 119 PRO B, 210 ASN B, 218 ARG A	2.05	144.49	-0.93	0.01	14.33	64
    122	119 PRO B, 210 ASN B, 218 ARG A, 211 ARG B	1.99	145.18	-1.73	-0.53	15.09	70
    123	119 PRO B, 210 ASN B, 218 ARG A, 211 ARG B, 186 TYR B	1.96	145.33	-1.64	-0.2	12.39	63
    124	119 PRO B, 218 ARG A, 211 ARG B, 186 TYR B	1.93	146.63	-1.95	-0.05	14.64	63
    125	218 ARG A, 211 ARG B, 186 TYR B	2.04	147.3	-2.07	-0.04	19	66
    126	218 ARG A, 186 TYR B, 211 ARG B	2.15	148.79	-3.43	0.09	35.2	72
    127	218 ARG A, 186 TYR B, 211 ARG B, 125 LEU B	2.41	148.79	-1.63	0.35	26.44	67

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    200042 GLY A, 200040 THR B, 200085 ASN B, 200165 ASP B, 200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A, 200173 ALA A, 200180 TYR A, 200175 LEU A, 200088 SER A, 200091 SER A, 200088 SER A, 200040 ARG A, 200091 SER A, 200043 HIS A, 200046 GLU A, 100018 ARG B, 200064 ILE A, 200063 LYS A, 200063 LYS A, 100020 SER B, 200003 LEU B, 200098 PHE B, 200061 ASN A, 200097 THR B, 200001 ASP B, 100072 THR B, 100070 ASP B, 200001 ASP B, 200026 SER B, 100024 ARG B, 200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B, 100028 SER B, 100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B, 200028 SER B, 27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C, 200079 GLY C, 300093 ARG B, 79 GLY C, 100082 TYR C, 300079 GLY C, 300082 TYR C, 93 ARG B, 82 TYR C, 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, 200050 TYR B, 200053 GLU B, 85 THR C, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A

    Unique lining residues set - sidechains

    200040 THR B, 200085 ASN B, 200165 ASP B, 200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A, 200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A, 200040 ARG A, 200043 HIS A, 200046 GLU A, 100018 ARG B, 200064 ILE A, 200063 LYS A, 100020 SER B, 200003 LEU B, 200061 ASN A, 200097 THR B, 200001 ASP B, 100072 THR B, 100070 ASP B, 200026 SER B, 100024 ARG B, 100069 THR B, 100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B, 27 GLN B, 28 SER B, 300027 GLN B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 300093 ARG B, 100082 TYR C, 300082 TYR C, 93 ARG B, 82 TYR C, 200058 GLN C, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200050 TYR B, 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: -0.4
    Polarity: 16.06
    Mutability: 86
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	200042 GLY A, 200040 THR B, 200085 ASN B, 200165 ASP B	3.31	0.14	-2.03	-0.85	14.53	99
    2	200042 GLY A, 200040 THR B, 200165 ASP B	3.13	1.96	-1.53	-0.87	18.25	96
    3	200042 GLY A, 200040 THR B, 200165 ASP B, 200041 ASN B	3.19	4.02	-2.03	-0.85	14.53	99
    4	200042 GLY A, 200040 THR B, 200165 ASP B, 200041 ASN B, 200172 PRO A	3.69	4.22	-1.94	-0.69	11.94	88
    5	200042 GLY A, 200165 ASP B, 200041 ASN B, 200172 PRO A	3.73	4.79	-2.25	-0.68	14.51	82
    6	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.71	4.95	-1.78	-0.44	2.48	73
    7	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.64	5.45	-1.78	-0.44	2.48	73
    8	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.55	6.46	-1.78	-0.44	2.48	73
    9	200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A	3.52	7.01	-2.55	-0.52	14.11	74
    10	200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A	3.49	7.85	-2.55	-0.52	14.11	74
    11	200172 PRO A, 200041 PRO A, 200153 GLU A, 200173 ALA A	3.36	9.93	-1.78	-0.53	14.11	64
    12	200041 PRO A, 200153 GLU A, 200173 ALA A, 200180 TYR A	3.31	12.2	-1.7	-0.23	14.12	61
    13	200041 PRO A, 200173 ALA A, 200180 TYR A	3.48	14.18	-1.1	0.07	2.19	54
    14	200041 PRO A, 200173 ALA A, 200180 TYR A, 200175 LEU A	4.38	14.69	0.13	0.34	1.68	54
    15	200041 PRO A, 200180 TYR A, 200175 LEU A	4.37	15.36	0.3	0.72	1.11	54
    16	200041 PRO A, 200173 ALA A, 200180 TYR A, 200175 LEU A	4.44	15.72	0.13	0.34	1.68	54
    17	200041 PRO A, 200180 TYR A, 200175 LEU A	4.33	20.33	0.3	0.72	1.11	54
    18	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A, 200091 SER A	4.29	20.95	-0.06	0.08	1.67	69
    19	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A	4.23	21.32	0.02	0.3	1.25	69
    20	200180 TYR A, 200091 SER A, 200088 SER A	4.18	21.47	-0.97	-0.28	1.65	94
    21	200091 SER A, 200088 SER A	4.14	21.54	-0.8	-0.97	1.67	117
    22	200180 TYR A, 200091 SER A, 200088 SER A	4.12	21.86	-0.97	-0.28	1.65	94
    23	200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A	4.23	22.08	0.23	0.08	1.27	84
    24	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A	4.33	22.76	0.02	0.3	1.25	69
    25	200041 PRO A, 200175 LEU A, 200091 SER A, 200088 SER A	4.56	23.19	0.15	-0.22	1.26	86
    26	200041 PRO A, 200091 SER A, 200088 SER A	4.66	24.12	-1.07	-0.68	1.64	97
    27	200041 PRO A, 200088 SER A	4.88	24.9	-1.2	-0.53	1.63	87
    28	200041 PRO A, 200088 SER A, 200040 ARG A	4.22	27.7	-2.3	-0.49	18.42	86
    29	200041 PRO A, 200088 SER A, 200040 ARG A	2.96	29.76	-2.17	-0.44	18.99	70
    30	200041 PRO A, 200088 SER A, 200040 ARG A, 200091 SER A	2.78	30.09	-1.73	-0.53	15.09	70
    31	200088 SER A, 200040 ARG A, 200091 SER A	2.27	31.61	-1.77	-0.67	19.59	83
    32	200088 SER A, 200040 ARG A	1.97	32.63	-2.45	-0.61	27.69	83
    33	200040 ARG A	0.8	38.25	-4.5	-0.42	52	83
    34	200040 ARG A, 200043 HIS A	1.11	39.41	-3.85	-0.08	51.8	87
    35	200040 ARG A, 200046 GLU A	1.7	43.5	-4	-0.78	50.95	80
    36	200040 ARG A, 200046 GLU A, 100018 ARG B	4.03	46.08	-4.17	-0.66	51.3	81
    37	200040 ARG A, 200046 GLU A, 100018 ARG B, 200064 ILE A	3.53	49.67	-2	-0.04	38.51	86
    38	200046 GLU A, 100018 ARG B, 200064 ILE A, 200063 LYS A	3.66	52.85	-0.98	-0.14	26.35	87
    39	200046 GLU A, 200064 ILE A, 200063 LYS A	3.42	53.61	0.2	-0.04	17.8	90
    40	200046 GLU A, 200064 ILE A, 200063 LYS A	2.96	57.97	-0.97	0.09	33.18	84
    41	200046 GLU A, 200064 ILE A, 200063 LYS A, 100020 SER B	5.25	58.49	-0.93	-0.18	25.3	92
    42	200046 GLU A, 200063 LYS A, 100020 SER B, 200003 LEU B	5.42	59.26	-1.1	-0.35	25.3	80
    43	200046 GLU A, 200064 ILE A, 200063 LYS A, 200003 LEU B	4.65	63.26	0.23	0.35	24.92	76
    44	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.45	64.07	-1	-0.3	25.73	67
    45	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B, 200061 ASN A	4.3	64.54	-1.5	-0.4	21.26	76
    46	200046 GLU A, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200097 THR B	4.21	64.74	-2.4	-0.78	21.56	90
    47	200046 GLU A, 200098 PHE B, 200061 ASN A, 200097 THR B	4.17	64.9	-2.03	-0.87	14.58	96
    48	200046 GLU A, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200097 THR B	4.17	65.1	-2.4	-0.78	21.56	90
    49	200063 LYS A, 200003 LEU B, 200098 PHE B, 200061 ASN A, 200097 THR B	3.95	65.91	-0.94	-0.32	11.61	84
    50	200063 LYS A, 200003 LEU B, 200098 PHE B, 200097 THR B	3.82	66.3	-0.3	-0.21	13.67	77
    51	200063 LYS A, 200003 LEU B, 200061 ASN A, 200097 THR B	3.7	66.71	-1.08	-0.2	13.67	84
    52	200063 LYS A, 200003 LEU B, 200097 THR B, 200001 ASP B	3.47	68.62	-1.08	-0.27	25.25	79
    53	200063 LYS A, 200003 LEU B, 200001 ASP B	3.56	70.32	-1.2	-0.1	33.11	70
    54	200063 LYS A, 200003 LEU B, 200001 ASP B, 100072 THR B	4.02	71.25	-1.08	-0.27	25.25	79
    55	200063 LYS A, 200003 LEU B, 200001 ASP B, 100072 THR B, 100070 ASP B	4.2	71.45	-1.56	-0.42	30.14	81
    56	200003 LEU B, 200001 ASP B, 100072 THR B, 100070 ASP B	3.96	72.44	-0.98	-0.43	25.3	83
    57	200003 LEU B, 100070 ASP B, 200001 ASP B	2.95	74.86	-0.03	-0.23	17.74	70
    58	200003 LEU B, 100070 ASP B	2.22	77.39	0.15	0.05	24.92	70
    59	200003 LEU B, 100070 ASP B, 200026 SER B	2.13	80.22	-0.17	-0.29	17.17	85
    60	200003 LEU B, 100070 ASP B, 200026 SER B, 100024 ARG B	2.51	81.89	-1.25	-0.32	25.88	85
    61	100070 ASP B, 200026 SER B, 100024 ARG B	3.17	83.69	-2.93	-0.81	34.46	95
    62	100070 ASP B, 100024 ARG B, 200026 SER B	3.64	84.68	-2.8	-0.75	35.03	84
    63	100070 ASP B, 100024 ARG B, 200026 SER B, 100069 THR B	3.71	86.65	-2.28	-0.76	26.69	92
    64	100024 ARG B, 200026 SER B, 100069 THR B	4.4	87.96	-1.87	-0.66	19.01	95
    65	100024 ARG B, 200026 SER B, 100069 THR B, 100026 SER B	4.97	88.73	-1.5	-0.7	15.11	95
    66	200026 SER B, 100069 THR B, 100026 SER B	4.4	91.59	-0.5	-0.79	2.81	107
    67	200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B	4.39	92.49	-0.48	-0.79	2.95	107
    68	200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B, 100028 SER B	4.48	94.57	-0.46	-0.79	3.04	107
    69	200026 SER B, 100027 GLN B, 100028 SER B, 200027 GLN B	5.17	94.87	-1.28	-0.92	2.99	100
    70	200026 SER B, 100069 THR B, 100028 SER B, 200027 GLN B	4.16	98.08	-1.35	-0.91	2.56	102
    71	100027 GLN B, 100028 SER B, 200027 GLN B	5.34	98.73	-1.57	-0.96	2.86	100
    72	100028 SER B, 200027 GLN B, 100027 GLN B	5.62	99.31	-2.6	-1.06	2.91	95
    73	100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B	5.85	99.78	-2.05	-0.99	3.03	95
    74	100028 SER B, 200027 GLN B, 200028 SER B	6.05	100.08	-1.7	-1.01	2.29	106
    75	27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B	6.23	100.99	-2.05	-0.99	3.03	95
    76	100028 SER B, 200027 GLN B, 200028 SER B	4.89	104.47	-1.7	-1.01	2.29	106
    77	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.78	104.81	-2.4	-0.87	14.72	100
    78	200027 GLN B, 200028 SER B, 200093 ARG B	4.82	105.39	-2.93	-0.83	19.07	94
    79	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.75	105.84	-2.4	-0.87	14.72	100
    80	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.51	106.45	-2.3	-0.82	15.15	94
    81	100028 SER B, 200027 GLN B, 200093 ARG B	2.47	111.62	-2.93	-0.83	19.07	94
    82	100028 SER B, 200093 ARG B	3.06	112.3	-2.65	-0.7	26.84	100
    83	100028 SER B, 200093 ARG B, 200082 TYR C	3.37	113.38	-2.2	-0.09	18.43	83
    84	100028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B	4.01	116.3	-2.78	-0.18	26.82	83
    85	100028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C	5.99	117.1	-2.3	-0.3	22.13	83
    86	200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C, 200079 GLY C	6.52	118.03	-2.22	-0.27	22.47	72
    87	300093 ARG B, 79 GLY C, 100082 TYR C, 300079 GLY C, 300082 TYR C	6.73	118.25	-1.58	0.04	12.4	61
    88	300093 ARG B, 100082 TYR C, 300079 GLY C, 300082 TYR C, 93 ARG B	6.42	118.61	-2.4	0.12	22.12	66
    89	100093 ARG B, 300093 ARG B, 100082 TYR C, 300079 GLY C, 300082 TYR C	6.3	119.03	-2.4	0.12	22.12	66
    90	200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C, 200079 GLY C	6.15	119.71	-2.22	-0.27	22.47	72
    91	200093 ARG B, 200082 TYR C, 100079 GLY C, 200079 GLY C, 82 TYR C	5.57	121.53	-1.58	0.04	12.4	61
    92	200093 ARG B, 200082 TYR C, 200079 GLY C, 82 TYR C	5.07	122.47	-1.88	0.25	14.65	61
    93	200093 ARG B, 200082 TYR C, 200079 GLY C, 200058 GLN C	3.24	124.79	-2.43	-0.3	15.13	72
    94	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3.37	125.49	-2.2	-0.78	15.57	83
    95	200093 ARG B, 200079 GLY C, 82 TYR C, 200058 GLN C	3.75	126.58	-2.43	-0.3	15.13	72
    96	200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C	3.67	126.78	-2.43	-0.3	15.13	72
    97	200093 ARG B, 82 TYR C, 200058 GLN C	3.55	127.81	-3.1	-0.14	19.05	72
    98	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.63	128.03	-2.43	-0.3	15.13	72
    99	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.69	128.41	-2.53	-0.35	14.7	83
    100	200028 SER B, 200093 ARG B, 82 TYR C	3.84	128.48	-2.2	-0.09	18.43	83
    101	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.67	129.25	-2.53	-0.35	14.7	83
    102	200028 SER B, 82 TYR C, 200058 GLN C	3.23	131.52	-1.87	-0.32	2.27	83
    103	200028 SER B, 82 TYR C, 200058 GLN C, 200030 GLY B	3.11	132.57	-1.5	-0.44	2.55	83
    104	82 TYR C, 200058 GLN C, 200030 GLY B, 200092 ASN B	3.11	134.62	-2.18	-0.39	2.98	79
    105	82 TYR C, 200030 GLY B, 200092 ASN B	3.18	134.94	-1.73	-0.15	2.79	77
    106	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C	3.21	135.56	-0.25	0.17	2.13	84
    107	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C	3.28	135.82	-1.1	0.05	12.1	83
    108	200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B	3.1	137.07	-1.54	-0.38	21.72	92
    109	200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B	2.94	138.24	-1.05	-0.28	26.3	89
    110	200030 GLY B, 84 VAL C, 200064 ARG C	2.94	138.31	-0.23	-0.03	18.5	90
    111	200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B	2.94	138.42	-0.35	-0.22	14.29	96
    112	200030 GLY B, 200064 ARG C, 200031 THR B	2.98	138.45	-1.87	-0.66	19.01	95
    113	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	3	138.46	-2.28	-0.76	26.69	92
    114	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	3.01	138.5	-2.2	-0.77	27.12	84
    115	200030 GLY B, 200064 ARG C, 200031 THR B	3	138.56	-1.87	-0.66	19.01	95
    116	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.88	138.81	-1.13	-0.28	25.87	93
    117	84 VAL C, 200064 ARG C, 200031 THR B	2.8	139.01	-0.33	-0.02	17.93	96
    118	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.6	139.64	-1.13	-0.28	25.87	93
    119	84 VAL C, 200064 ARG C, 200031 THR B	2.51	140.11	-0.33	-0.02	17.93	96
    120	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.4	142.07	-1.13	-0.28	25.87	93
    121	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C	2.46	142.75	-2.28	-0.76	26.69	92
    122	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 200050 TYR B	2.56	143.85	-2.08	-0.38	21.67	81
    123	200064 ARG C, 200031 THR B, 84 VAL C, 200050 TYR B	2.78	144.37	-1.73	-0.22	14.66	80
    124	200064 ARG C, 200031 THR B, 200050 TYR B	2.88	144.47	-2.17	-0.03	18.42	80
    125	200031 THR B, 200050 TYR B, 200053 GLU B	2.89	144.56	-1.83	-0.27	17.72	78
    126	200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B	2.89	146.2	-1.48	-0.4	14.14	78
    127	200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B, 85 THR C	3.08	146.63	-1.26	-0.48	11.99	78
    128	200031 THR B, 84 VAL C, 200053 GLU B, 85 THR C	3.08	147.27	-1.33	-0.87	14.15	97
    129	200031 THR B, 84 VAL C, 200053 GLU B, 85 THR C, 54 ALA C	3	148.37	-0.7	-0.69	11.32	97
    130	200031 THR B, 200053 GLU B, 85 THR C, 54 ALA C	3.02	148.9	-0.78	-0.67	13.31	97
    131	200053 GLU B, 85 THR C, 54 ALA C	2.99	150.15	-0.8	-0.63	17.19	94
    132	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C	3	152.19	-0.7	-0.67	13.74	94
    133	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A	3.54	152.8	-1.46	-0.62	21.39	91
    134	200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A	3.79	153.25	-2.28	-0.78	26.74	89
    135	200053 GLU B, 53 GLY C, 57 ARG A	3.83	154.16	-2.8	-0.79	35.09	80

    pore with bottle neck

    pore with local minimum

18. 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, 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, 100050 TYR B, 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, 100050 TYR B, 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: -0.4
    Polarity: 15.51
    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	3.28	0.26	-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	0.62	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.21	0.76	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.24	1.04	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.31	1.57	-1.53	-0.78	2.81	105
    7	100170 THR A, 100041 ASN B, 100155 VAL A	2.53	5.78	-1.53	-0.78	2.81	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.51	6.68	-0.2	-0.3	2.14	88
    9	100170 THR A, 100041 ASN B, 100182 LEU A	2.77	6.86	-0.13	-0.13	1.72	88
    10	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.22	-0.03	-0.14	2.3	79
    11	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.7	7.95	-0.13	-0.31	2.57	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.55	8.45	-0.8	-0.47	12.03	78
    13	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.44	8.91	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.28	10.1	-1.95	-0.88	15.01	90
    15	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.29	12.8	-2.25	-0.7	14.56	79
    16	100041 ASN B, 100153 GLU A, 100172 PRO A	3.06	13.46	-2.87	-0.67	18.29	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.3	13.73	-2.55	-0.52	14.11	74
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.38	14.63	-2.55	-0.52	14.11	74
    19	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.36	16.89	-1.78	-0.53	14.11	64
    20	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.32	18.79	-1.7	-0.23	14.12	61
    21	100173 ALA A, 100041 PRO A, 100180 TYR A	3.55	20.9	-1.1	0.07	2.19	54
    22	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.22	21.34	0.13	0.34	1.68	54
    23	100041 PRO A, 100180 TYR A, 100175 LEU A	4.38	22.05	0.3	0.72	1.11	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.49	22.37	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.03	27.04	0.3	0.72	1.11	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	3.99	27.69	-0.06	0.08	1.67	69
    27	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	3.99	28.07	0.02	0.3	1.25	69
    28	100180 TYR A, 100091 SER A, 100088 SER A	4.02	28.22	-0.97	-0.28	1.65	94
    29	100091 SER A, 100088 SER A	4.07	28.29	-0.8	-0.97	1.67	117
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.15	28.65	-0.97	-0.28	1.65	94
    31	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.36	28.9	0.23	0.08	1.27	84
    32	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.47	29.24	0.02	0.3	1.25	69
    33	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.56	30.14	0.15	-0.22	1.26	86
    34	100041 PRO A, 100091 SER A, 100088 SER A	4.72	30.63	-1.07	-0.68	1.64	97
    35	100041 PRO A, 100088 SER A	4.82	31.82	-1.2	-0.53	1.63	87
    36	100041 PRO A, 100088 SER A, 100040 ARG A	4.21	34.42	-2.3	-0.49	18.42	86
    37	100041 PRO A, 100088 SER A, 100040 ARG A	3	36.56	-2.17	-0.44	18.99	70
    38	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.75	36.89	-1.73	-0.53	15.09	70
    39	100088 SER A, 100040 ARG A, 100091 SER A	1.71	37.9	-1.77	-0.67	19.59	83
    40	100088 SER A, 100040 ARG A	1.21	39.95	-2.45	-0.61	27.69	83
    41	100040 ARG A	1.21	45.78	-4.5	-0.42	52	83
    42	100040 ARG A, 100043 HIS A	2.68	46.83	-3.85	-0.08	51.8	87
    43	100040 ARG A, 100046 GLU A	3.18	50.17	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	3.74	52.89	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.52	56.19	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A	3.87	56.78	-1.17	0.08	34.01	87
    47	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.59	59.48	-0.98	-0.14	26.35	87
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.26	60.28	0.2	-0.04	17.8	90
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	2.87	64.86	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	5.17	65.32	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.31	66.29	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.78	69.55	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.52	70.51	-1	-0.3	25.73	67
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.3	71.14	-1.5	-0.4	21.26	76
    55	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.15	71.42	-2.4	-0.78	21.56	90
    56	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.1	71.79	-2.03	-0.87	14.58	96
    57	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.2	72.01	-2.4	-0.78	21.56	90
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4.04	72.62	-0.94	-0.32	11.61	84
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.87	73.04	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.69	73.47	-1.08	-0.2	13.67	84
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.44	75.51	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B	3.54	77.23	-1.2	-0.1	33.11	70
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.86	78.09	-1.08	-0.27	25.25	79
    64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.07	78.29	-1.56	-0.42	30.14	81
    65	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.95	79.18	-0.98	-0.43	25.3	83
    66	100003 LEU B, 300070 ASP B, 100001 ASP B	3.04	81.49	-0.03	-0.23	17.74	70
    67	100003 LEU B, 300070 ASP B	2.22	84.12	0.15	0.05	24.92	70
    68	100003 LEU B, 300070 ASP B, 100026 SER B	2.12	87.09	-0.17	-0.29	17.17	85
    69	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.58	88.82	-1.25	-0.32	25.88	85
    70	300070 ASP B, 100026 SER B, 300024 ARG B	3.24	90.42	-2.93	-0.81	34.46	95
    71	300070 ASP B, 300024 ARG B, 100026 SER B	3.63	91.47	-2.8	-0.75	35.03	84
    72	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.72	93	-2.28	-0.76	26.69	92
    73	300024 ARG B, 100026 SER B, 300069 THR B	4.32	94.53	-1.87	-0.66	19.01	95
    74	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.92	95.36	-1.5	-0.7	15.11	95
    75	100026 SER B, 300069 THR B, 300026 SER B	4.32	98.25	-0.5	-0.79	2.81	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.44	99.2	-0.48	-0.79	2.95	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.65	101.31	-0.46	-0.79	3.04	107
    78	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.24	101.45	-1.28	-0.92	2.99	100
    79	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.16	104.65	-1.35	-0.91	2.56	102
    80	100026 SER B, 100027 GLN B, 300028 SER B	5.25	105.33	-1.57	-0.96	2.86	100
    81	100027 GLN B, 300028 SER B, 300027 GLN B	5.54	105.95	-2.6	-1.06	2.91	95
    82	100027 GLN B, 300028 SER B, 300027 GLN B, 100028 SER B	5.79	106.79	-2.05	-0.99	3.03	95
    83	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.18	107.8	-2.05	-0.99	3.03	95
    84	100027 GLN B, 300028 SER B, 100028 SER B	4.89	111.32	-1.7	-1.01	2.29	106
    85	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.82	111.59	-2.4	-0.87	14.72	100
    86	100027 GLN B, 100028 SER B, 100093 ARG B	4.82	112.02	-2.93	-0.83	19.07	94
    87	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.63	112.45	-2.4	-0.87	14.72	100
    88	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.36	113.06	-2.3	-0.82	15.15	94
    89	100027 GLN B, 300028 SER B, 100093 ARG B	2.42	118.49	-2.93	-0.83	19.07	94
    90	300028 SER B, 100093 ARG B, 100082 TYR C	3.16	120.25	-2.2	-0.09	18.43	83
    91	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.35	123.31	-2.78	-0.18	26.82	83
    92	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.14	123.73	-2.3	-0.3	22.13	83
    93	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.35	124.72	-2.22	-0.27	22.47	72
    94	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
    95	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.49	125.36	-2.4	0.12	22.12	66
    96	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.48	125.83	-2.4	0.12	22.12	66
    97	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	6.08	127.53	-1.58	0.04	12.4	61
    98	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	5.6	128.53	-1.88	0.25	14.65	61
    99	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.23	131.7	-2.43	-0.3	15.13	72
    100	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.48	132.08	-2.2	-0.78	15.57	83
    101	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.69	133.27	-2.43	-0.3	15.13	72
    102	100093 ARG B, 200082 TYR C, 100058 GLN C, 100080 ASP C	3.71	133.48	-2.43	-0.3	15.13	72
    103	100093 ARG B, 200082 TYR C, 100058 GLN C	3.57	134.56	-3.1	-0.14	19.05	72
    104	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.59	134.78	-2.43	-0.3	15.13	72
    105	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.62	135.15	-2.53	-0.35	14.7	83
    106	100028 SER B, 100093 ARG B, 200082 TYR C	3.76	135.2	-2.2	-0.09	18.43	83
    107	100028 SER B, 100093 ARG B, 200082 TYR C, 100058 GLN C	3.77	135.77	-2.53	-0.35	14.7	83
    108	100028 SER B, 200082 TYR C, 100058 GLN C	3.38	138.1	-1.87	-0.32	2.27	83
    109	100028 SER B, 200082 TYR C, 100058 GLN C, 100030 GLY B	3.15	139.26	-1.5	-0.44	2.55	83
    110	200082 TYR C, 100058 GLN C, 100030 GLY B, 100092 ASN B	3.13	141.16	-2.18	-0.39	2.98	79
    111	200082 TYR C, 100030 GLY B, 100092 ASN B	3.22	141.52	-1.73	-0.15	2.79	77
    112	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C	3.28	142.37	-0.25	0.17	2.13	84
    113	200082 TYR C, 100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C	3.34	142.5	-1.1	0.05	12.1	83
    114	100030 GLY B, 100092 ASN B, 200084 VAL C, 100064 ARG C, 100032 ASP B	3.07	143.8	-1.54	-0.38	21.72	92
    115	100030 GLY B, 200084 VAL C, 100064 ARG C, 100032 ASP B	2.95	144.87	-1.05	-0.28	26.3	89
    116	100030 GLY B, 200084 VAL C, 100064 ARG C	2.94	145.03	-0.23	-0.03	18.5	90
    117	100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B	2.94	145.11	-0.35	-0.22	14.29	96
    118	100030 GLY B, 100064 ARG C, 100031 THR B	2.95	145.14	-1.87	-0.66	19.01	95
    119	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	2.97	145.16	-2.28	-0.76	26.69	92
    120	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	3	145.19	-2.2	-0.77	27.12	84
    121	100030 GLY B, 100064 ARG C, 100032 ASP B, 100031 THR B	3.02	145.25	-2.28	-0.76	26.69	92
    122	100030 GLY B, 200084 VAL C, 100064 ARG C, 100031 THR B	3	145.34	-0.35	-0.22	14.29	96
    123	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.93	145.49	-1.13	-0.28	25.87	93
    124	200084 VAL C, 100064 ARG C, 100031 THR B	2.84	145.7	-0.33	-0.02	17.93	96
    125	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.63	146.35	-1.13	-0.28	25.87	93
    126	200084 VAL C, 100064 ARG C, 100031 THR B	2.55	146.84	-0.33	-0.02	17.93	96
    127	200084 VAL C, 100064 ARG C, 100032 ASP B, 100031 THR B	2.49	148.91	-1.13	-0.28	25.87	93
    128	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C	2.51	149.62	-2.28	-0.76	26.69	92
    129	100064 ARG C, 100032 ASP B, 100031 THR B, 200084 VAL C, 100050 TYR B	2.54	150.69	-2.08	-0.38	21.67	81
    130	100064 ARG C, 100031 THR B, 200084 VAL C, 100050 TYR B	2.6	151.13	-1.73	-0.22	14.66	80
    131	100031 THR B, 100050 TYR B, 100053 GLU B	2.73	151.35	-1.83	-0.27	17.72	78
    132	100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B	2.92	152.79	-1.48	-0.4	14.14	78
    133	100031 THR B, 200084 VAL C, 100050 TYR B, 100053 GLU B, 200085 THR C	3.13	153.24	-1.26	-0.48	11.99	78
    134	100031 THR B, 200084 VAL C, 100053 GLU B, 200085 THR C	3.08	154.12	-1.33	-0.87	14.15	97
    135	100031 THR B, 200084 VAL C, 100053 GLU B, 200085 THR C, 200054 ALA C	3	155.18	-0.7	-0.69	11.32	97
    136	100031 THR B, 100053 GLU B, 200085 THR C, 200054 ALA C	2.93	155.76	-0.78	-0.67	13.31	97
    137	100053 GLU B, 200085 THR C, 200054 ALA C	2.88	157.08	-0.8	-0.63	17.19	94
    138	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C	2.94	158.8	-0.7	-0.67	13.74	94
    139	100053 GLU B, 200085 THR C, 200054 ALA C, 200053 GLY C, 200057 ARG A	3.53	159.46	-1.46	-0.62	21.39	91
    140	100053 GLU B, 200085 THR C, 200053 GLY C, 200057 ARG A	3.8	159.91	-2.28	-0.78	26.74	89
    141	100053 GLU B, 200053 GLY C, 200057 ARG A	3.83	160.86	-2.8	-0.79	35.09	80

    pore with bottle neck

    pore with local minimum

19. 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, 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, 200079 GLY C, 200082 TYR C, 100058 GLN C, 100080 ASP C, 28 SER B, 200058 GLN C, 200080 ASP C, 200028 SER B, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B, 200031 THR B, 84 VAL C, 200050 TYR B, 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, 200050 TYR B, 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: -0.39
    Polarity: 15.95
    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	3.29	0.25	-1.33	-0.78	2.52	106
    2	100157 VAL A, 100170 THR A, 100041 ASN B	3.23	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	3.2	0.85	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.19	0.99	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.09	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	3.03	1.8	-1.14	-0.78	2.69	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.78	5.48	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.73	6.55	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.76	6.87	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.75	7.23	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.62	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	2.59	8.33	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100182 LEU A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.57	8.74	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.51	9.85	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.48	12.98	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.2	13.3	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.39	13.83	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.58	14.41	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100172 PRO A, 100041 PRO A	3.54	14.74	-2.23	-0.44	17.69	64
    21	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.28	16.97	-1.78	-0.53	14.11	64
    22	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.28	18.83	-1.7	-0.23	14.12	61
    23	100173 ALA A, 100041 PRO A, 100180 TYR A	3.48	20.89	-1.1	0.07	2.19	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.25	21.43	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.39	22.12	0.3	0.72	1.11	54
    26	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.47	22.55	0.13	0.34	1.68	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A	4.05	27.33	0.3	0.72	1.11	54
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A, 100091 SER A	4.02	27.87	-0.06	0.08	1.67	69
    29	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.02	28.14	0.23	0.08	1.27	84
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.03	28.5	-0.97	-0.28	1.65	94
    31	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.21	28.97	0.23	0.08	1.27	84
    32	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.4	29.32	0.02	0.3	1.25	69
    33	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.5	29.74	0.15	-0.22	1.26	86
    34	100041 PRO A, 100091 SER A, 100088 SER A	4.61	30.69	-1.07	-0.68	1.64	97
    35	100041 PRO A, 100088 SER A	4.84	31.84	-1.2	-0.53	1.63	87
    36	100041 PRO A, 100088 SER A, 100040 ARG A	4.42	34.34	-2.3	-0.49	18.42	86
    37	100041 PRO A, 100088 SER A, 100040 ARG A	2.94	36.48	-2.17	-0.44	18.99	70
    38	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.77	36.82	-1.73	-0.53	15.09	70
    39	100088 SER A, 100040 ARG A, 100091 SER A	1.44	38.4	-1.77	-0.67	19.59	83
    40	100088 SER A, 100040 ARG A	0.84	39.46	-2.45	-0.61	27.69	83
    41	100040 ARG A	0.02	45.19	-4.5	-0.42	52	83
    42	100040 ARG A, 100043 HIS A	1.16	46.34	-3.85	-0.08	51.8	87
    43	100040 ARG A, 100046 GLU A	1.98	50.43	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	4.19	52.49	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.57	56.2	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A	3.75	56.77	-1.17	0.08	34.01	87
    47	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.23	59.38	-0.98	-0.14	26.35	87
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.08	60.17	0.2	-0.04	17.8	90
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3	64.66	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.9	65.2	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	5.25	65.99	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.86	70.07	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.53	70.87	-1	-0.3	25.73	67
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.27	71.31	-1.5	-0.4	21.26	76
    55	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.14	71.47	-2.4	-0.78	21.56	90
    56	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.11	71.68	-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	71.89	-2.4	-0.78	21.56	90
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.94	72.76	-0.94	-0.32	11.61	84
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.78	73.17	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.63	73.6	-0.3	-0.21	13.67	77
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.46	75.62	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B	3.56	77.28	-1.2	-0.1	33.11	70
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.84	78.11	-1.08	-0.27	25.25	79
    64	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
    65	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.99	79.15	-0.98	-0.43	25.3	83
    66	100003 LEU B, 300070 ASP B, 100001 ASP B	3.08	81.22	-0.03	-0.23	17.74	70
    67	100003 LEU B, 300070 ASP B	2.12	84.26	0.15	0.05	24.92	70
    68	100003 LEU B, 300070 ASP B, 100026 SER B	2.01	87.14	-0.17	-0.29	17.17	85
    69	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.69	88.83	-1.25	-0.32	25.88	85
    70	300070 ASP B, 100026 SER B, 300024 ARG B	3.41	90.44	-2.93	-0.81	34.46	95
    71	300070 ASP B, 300024 ARG B, 100026 SER B	3.64	91.37	-2.8	-0.75	35.03	84
    72	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.71	93.33	-2.28	-0.76	26.69	92
    73	300024 ARG B, 100026 SER B, 300069 THR B	4.37	94.69	-1.87	-0.66	19.01	95
    74	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.79	95.5	-1.5	-0.7	15.11	95
    75	100026 SER B, 300069 THR B, 300026 SER B	4.45	98.48	-0.5	-0.79	2.81	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.64	99.39	-0.48	-0.79	2.95	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.8	101.17	-0.46	-0.79	3.04	107
    78	100026 SER B, 300069 THR B, 300027 GLN B, 300028 SER B	5.15	101.35	-0.58	-0.84	2.52	112
    79	100026 SER B, 300027 GLN B, 300028 SER B, 100027 GLN B	5.16	101.49	-1.28	-0.92	2.99	100
    80	100026 SER B, 300069 THR B, 300028 SER B, 100027 GLN B	4.16	104.53	-1.35	-0.91	2.56	102
    81	100026 SER B, 300028 SER B, 100027 GLN B	5.18	105.19	-1.57	-0.96	2.86	100
    82	300028 SER B, 100027 GLN B, 300027 GLN B	5.46	105.82	-2.6	-1.06	2.91	95
    83	300028 SER B, 100027 GLN B, 300027 GLN B, 100028 SER B	5.71	106.73	-2.05	-0.99	3.03	95
    84	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.11	107.63	-2.05	-0.99	3.03	95
    85	300028 SER B, 100027 GLN B, 100028 SER B	5.05	111.19	-1.7	-1.01	2.29	106
    86	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.87	111.55	-2.4	-0.87	14.72	100
    87	100027 GLN B, 100028 SER B, 100093 ARG B	4.88	112.15	-2.93	-0.83	19.07	94
    88	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.63	112.61	-2.4	-0.87	14.72	100
    89	300028 SER B, 100027 GLN B, 100028 SER B, 100093 ARG B	4.26	113.24	-2.3	-0.82	15.15	94
    90	300028 SER B, 100027 GLN B, 100093 ARG B	2.52	117.81	-2.93	-0.83	19.07	94
    91	300028 SER B, 100093 ARG B	2.73	118.54	-2.65	-0.7	26.84	100
    92	300028 SER B, 100093 ARG B, 100082 TYR C	3	120.26	-2.2	-0.09	18.43	83
    93	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.09	123.25	-2.78	-0.18	26.82	83
    94	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	6.08	124.04	-2.3	-0.3	22.13	83
    95	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.6	124.66	-2.22	-0.27	22.47	72
    96	300079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.98	124.9	-1.58	0.04	12.4	61
    97	93 ARG B, 79 GLY C, 82 TYR C, 200093 ARG B, 200079 GLY C	7.08	125.06	-2.22	-0.27	22.47	72
    98	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	7.02	125.24	-2.4	0.12	22.12	66
    99	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.83	125.57	-2.4	0.12	22.12	66
    100	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.5	126.15	-2.22	-0.27	22.47	72
    101	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.53	127.86	-1.58	0.04	12.4	61
    102	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C	4.97	128.81	-1.88	0.25	14.65	61
    103	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.1	131.45	-2.43	-0.3	15.13	72
    104	100093 ARG B, 100079 GLY C, 100058 GLN C	2.89	131.77	-2.8	-0.77	19.64	83
    105	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	2.83	133.11	-2.2	-0.78	15.57	83
    106	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.62	134.67	-2.43	-0.3	15.13	72
    107	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.57	135.57	-2.2	-0.02	12.43	66
    108	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.05	137.25	-2.4	0.12	22.12	66
    109	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.92	138.34	-2.22	-0.27	22.47	72
    110	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.63	138.72	-2.22	-0.27	22.47	72
    111	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	7.12	138.85	-2.3	-0.3	22.13	83
    112	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	7.19	139.16	-2.22	-0.27	22.47	72
    113	100093 ARG B, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	7.09	139.71	-3.04	-0.19	32.2	74
    114	100079 GLY C, 82 TYR C, 200093 ARG B, 200079 GLY C, 200082 TYR C	6.24	141.42	-1.58	0.04	12.4	61
    115	82 TYR C, 200093 ARG B, 200079 GLY C, 200082 TYR C	5.54	142.39	-1.88	0.25	14.65	61
    116	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.27	145.49	-2.43	-0.3	15.13	72
    117	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3.48	146.18	-2.2	-0.78	15.57	83
    118	82 TYR C, 200093 ARG B, 200079 GLY C, 200058 GLN C	3.73	147.23	-2.43	-0.3	15.13	72
    119	82 TYR C, 200093 ARG B, 200058 GLN C	3.56	148.26	-3.1	-0.14	19.05	72
    120	82 TYR C, 200093 ARG B, 200058 GLN C, 200028 SER B	3.57	148.51	-2.43	-0.3	15.13	72
    121	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.6	149.73	-2.53	-0.35	14.7	83
    122	200028 SER B, 82 TYR C, 200058 GLN C	3.39	152.05	-1.87	-0.32	2.27	83
    123	200028 SER B, 82 TYR C, 200058 GLN C, 200030 GLY B	3.19	153.12	-1.5	-0.44	2.55	83
    124	82 TYR C, 200058 GLN C, 200030 GLY B, 200092 ASN B	3.16	154.92	-2.18	-0.39	2.98	79
    125	82 TYR C, 200030 GLY B, 200092 ASN B	3.16	155.59	-1.73	-0.15	2.79	77
    126	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C	3.21	156.15	-0.25	0.17	2.13	84
    127	82 TYR C, 200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C	3.25	156.43	-1.1	0.05	12.1	83
    128	200030 GLY B, 200092 ASN B, 84 VAL C, 200064 ARG C, 200032 ASP B	3.09	157.81	-1.54	-0.38	21.72	92
    129	200030 GLY B, 84 VAL C, 200064 ARG C, 200032 ASP B	2.98	158.74	-1.05	-0.28	26.3	89
    130	200030 GLY B, 84 VAL C, 200064 ARG C	2.97	158.83	-0.23	-0.03	18.5	90
    131	200030 GLY B, 84 VAL C, 200064 ARG C, 200031 THR B	2.96	158.95	-0.35	-0.22	14.29	96
    132	200030 GLY B, 200064 ARG C, 200031 THR B	2.97	158.97	-1.87	-0.66	19.01	95
    133	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	2.96	158.99	-2.28	-0.76	26.69	92
    134	200030 GLY B, 200064 ARG C, 200032 ASP B, 200031 THR B	2.94	159.02	-2.2	-0.77	27.12	84
    135	200030 GLY B, 200064 ARG C, 200031 THR B	2.92	159.08	-1.87	-0.66	19.01	95
    136	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.84	159.34	-1.13	-0.28	25.87	93
    137	84 VAL C, 200064 ARG C, 200031 THR B	2.78	159.54	-0.33	-0.02	17.93	96
    138	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.62	160.19	-1.13	-0.28	25.87	93
    139	84 VAL C, 200064 ARG C, 200031 THR B	2.54	160.68	-0.33	-0.02	17.93	96
    140	84 VAL C, 200064 ARG C, 200032 ASP B, 200031 THR B	2.43	162.7	-1.13	-0.28	25.87	93
    141	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C	2.49	163.39	-2.28	-0.76	26.69	92
    142	200064 ARG C, 200032 ASP B, 200031 THR B, 84 VAL C, 200050 TYR B	2.57	164.47	-2.08	-0.38	21.67	81
    143	200064 ARG C, 200031 THR B, 84 VAL C, 200050 TYR B	2.76	164.94	-1.73	-0.22	14.66	80
    144	200064 ARG C, 200031 THR B, 200050 TYR B	2.9	165.02	-2.17	-0.03	18.42	80
    145	200031 THR B, 200050 TYR B, 200053 GLU B	2.95	165.13	-1.83	-0.27	17.72	78
    146	200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B	2.98	166.46	-1.48	-0.4	14.14	78
    147	200031 THR B, 84 VAL C, 200050 TYR B, 200053 GLU B, 85 THR C	3.11	166.91	-1.26	-0.48	11.99	78
    148	200031 THR B, 84 VAL C, 200053 GLU B, 85 THR C	3.13	167.88	-1.33	-0.87	14.15	97
    149	200031 THR B, 84 VAL C, 200053 GLU B, 85 THR C, 54 ALA C	2.88	169.22	-0.7	-0.69	11.32	97
    150	200031 THR B, 200053 GLU B, 85 THR C, 54 ALA C	2.84	169.83	-0.78	-0.67	13.31	97
    151	200053 GLU B, 85 THR C, 54 ALA C	2.85	171.11	-0.8	-0.63	17.19	94
    152	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C	3.02	172.67	-0.7	-0.67	13.74	94
    153	200053 GLU B, 85 THR C, 54 ALA C, 53 GLY C, 57 ARG A	3.58	173.31	-1.46	-0.62	21.39	91
    154	200053 GLU B, 85 THR C, 53 GLY C, 57 ARG A	3.81	173.76	-2.28	-0.78	26.74	89
    155	200053 GLU B, 53 GLY C, 57 ARG A	3.84	174.69	-2.8	-0.79	35.09	80

    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, 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, 300079 GLY C, 300080 ASP C, 300082 TYR C, 79 GLY C, 93 ARG B, 200079 GLY C, 200093 ARG B, 82 TYR 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, 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, 300042 GLY A, 300165 ASP B, 300040 THR B, 300085 ASN B, 300103 LYS B, 300010 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, 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, 300165 ASP B, 300040 THR B, 300085 ASN B, 300103 LYS B, 300010 ILE B

    Physicochemical properties of lining side-chains

    Charge: 4 (13-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.43
    Polarity: 15.04
    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	0.75	-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	1.52	-1.53	-0.78	2.81	105
    7	100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	2.89	2.1	-1.25	-0.79	2.95	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.51	5.74	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.52	6.67	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.78	7.03	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.76	7.21	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.56	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	2.4	8.36	-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	8.79	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.31	9.93	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.38	12.69	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.13	13.39	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.37	13.92	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.48	14.53	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.31	16.74	-1.78	-0.53	14.11	64
    21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.3	19.15	-1.7	-0.23	14.12	61
    22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.77	21.07	-1.1	0.07	2.19	54
    23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.44	21.42	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	4.45	22.54	0.13	0.34	1.68	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.21	27.38	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	27.91	-0.06	0.08	1.67	69
    28	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.21	28.17	0.23	0.08	1.27	84
    29	100091 SER A, 100088 SER A	4.23	28.26	-0.8	-0.97	1.67	117
    30	100180 TYR A, 100091 SER A, 100088 SER A	4.28	28.55	-0.97	-0.28	1.65	94
    31	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.42	29.05	0.23	0.08	1.27	84
    32	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.62	29.42	0.02	0.3	1.25	69
    33	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.73	29.87	0.15	-0.22	1.26	86
    34	100041 PRO A, 100091 SER A, 100088 SER A	4.83	30.84	-1.07	-0.68	1.64	97
    35	100041 PRO A, 100088 SER A	5.01	31.65	-1.2	-0.53	1.63	87
    36	100041 PRO A, 100088 SER A, 100040 ARG A	4.52	34	-2.3	-0.49	18.42	86
    37	100041 PRO A, 100088 SER A, 100040 ARG A	3.55	36.32	-2.17	-0.44	18.99	70
    38	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.83	37.01	-1.73	-0.53	15.09	70
    39	100088 SER A, 100040 ARG A, 100091 SER A	1.4	38.13	-1.77	-0.67	19.59	83
    40	100088 SER A, 100040 ARG A	0.93	39.08	-2.45	-0.61	27.69	83
    41	100040 ARG A	0.22	44.87	-4.5	-0.42	52	83
    42	100040 ARG A, 100043 HIS A	0.79	46.11	-3.85	-0.08	51.8	87
    43	100040 ARG A, 100046 GLU A	1.4	50.36	-4	-0.78	50.95	80
    44	100040 ARG A, 100046 GLU A, 300018 ARG B	4.62	52.47	-4.17	-0.66	51.3	81
    45	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.53	56.3	-2	-0.04	38.51	86
    46	100046 GLU A, 300018 ARG B, 100064 ILE A	3.49	56.89	-1.17	0.08	34.01	87
    47	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.15	59.6	-0.98	-0.14	26.35	87
    48	100046 GLU A, 100064 ILE A, 100063 LYS A	3.21	60.39	0.2	-0.04	17.8	90
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.37	64.93	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.97	65.36	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.8	66.36	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.32	69.62	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.21	70.57	-1	-0.3	25.73	67
    54	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.15	71.17	-1.5	-0.4	21.26	76
    55	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.14	71.44	-2.4	-0.78	21.56	90
    56	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.16	71.6	-2.03	-0.87	14.58	96
    57	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.2	72.03	-2.4	-0.78	21.56	90
    58	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	4.07	72.64	-0.94	-0.32	11.61	84
    59	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.97	73.05	-0.3	-0.21	13.67	77
    60	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.84	73.49	-1.08	-0.2	13.67	84
    61	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.56	75.51	-1.08	-0.27	25.25	79
    62	100063 LYS A, 100003 LEU B, 100001 ASP B	3.6	77.23	-1.2	-0.1	33.11	70
    63	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.86	78.09	-1.08	-0.27	25.25	79
    64	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.11	78.29	-1.56	-0.42	30.14	81
    65	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.83	79.17	-0.98	-0.43	25.3	83
    66	100003 LEU B, 300070 ASP B, 100001 ASP B	3.04	81.41	-0.03	-0.23	17.74	70
    67	100003 LEU B, 300070 ASP B	2.18	84.53	0.15	0.05	24.92	70
    68	100003 LEU B, 300070 ASP B, 100026 SER B	2.09	86.98	-0.17	-0.29	17.17	85
    69	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.46	88.72	-1.25	-0.32	25.88	85
    70	300070 ASP B, 100026 SER B, 300024 ARG B	3.22	90.43	-2.93	-0.81	34.46	95
    71	300070 ASP B, 300024 ARG B, 100026 SER B	3.57	91.37	-2.8	-0.75	35.03	84
    72	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.73	93.39	-2.28	-0.76	26.69	92
    73	300024 ARG B, 100026 SER B, 300069 THR B	4.66	94.41	-1.87	-0.66	19.01	95
    74	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.62	95.6	-1.5	-0.7	15.11	95
    75	100026 SER B, 300069 THR B, 300026 SER B	4.47	98.81	-0.5	-0.79	2.81	107
    76	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.76	99.71	-0.48	-0.79	2.95	107
    77	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.92	101.25	-0.46	-0.79	3.04	107
    78	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	5.07	101.56	-1.28	-0.92	2.99	100
    79	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.24	104.32	-1.35	-0.91	2.56	102
    80	100026 SER B, 100027 GLN B, 300028 SER B	5.26	104.99	-1.57	-0.96	2.86	100
    81	300027 GLN B, 100027 GLN B, 300028 SER B	5.55	105.65	-1.57	-0.96	2.86	100
    82	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.83	106.64	-2.05	-0.99	3.03	95
    83	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.29	107.56	-2.05	-0.99	3.03	95
    84	100027 GLN B, 300028 SER B, 100028 SER B	5.1	111.17	-1.7	-1.01	2.29	106
    85	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.81	111.54	-2.4	-0.87	14.72	100
    86	100027 GLN B, 100028 SER B, 100093 ARG B	4.71	112.2	-2.93	-0.83	19.07	94
    87	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.62	112.72	-2.4	-0.87	14.72	100
    88	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.44	113.4	-2.3	-0.82	15.15	94
    89	100027 GLN B, 300028 SER B, 100093 ARG B	2.48	118.63	-2.93	-0.83	19.07	94
    90	300028 SER B, 100093 ARG B, 100082 TYR C	2.7	120.24	-2.2	-0.09	18.43	83
    91	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	3.48	120.61	-2.78	-0.18	26.82	83
    92	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.71	121.64	-2.53	-0.35	14.7	83
    93	300028 SER B, 300093 ARG B, 300058 GLN C	3.64	121.92	-2.93	-0.83	19.07	94
    94	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.52	122.52	-2.53	-0.35	14.7	83
    95	300028 SER B, 100082 TYR C, 300093 ARG B, 300058 GLN C	3.52	122.79	-2.43	-0.3	15.13	72
    96	100082 TYR C, 300093 ARG B, 300058 GLN C	3.54	123.69	-3.1	-0.14	19.05	72
    97	100082 TYR C, 300093 ARG B, 300058 GLN C, 300079 GLY C	3.71	124.95	-2.43	-0.3	15.13	72
    98	300093 ARG B, 300058 GLN C, 300079 GLY C, 300080 ASP C	3.73	125.64	-2.2	-0.78	15.57	83
    99	300093 ARG B, 300058 GLN C, 300079 GLY C, 300082 TYR C	3.69	128.65	-2.43	-0.3	15.13	72
    100	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	4.43	129.65	-1.88	0.25	14.65	61
    101	100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C	4.81	131.23	-1.58	0.04	12.4	61
    102	300093 ARG B, 300079 GLY C, 79 GLY C, 93 ARG B, 200079 GLY C	5.65	131.63	-2.04	-0.65	22.83	83
    103	93 ARG B, 200079 GLY C, 200093 ARG B, 82 TYR C, 200082 TYR C	6.03	131.78	-2.4	0.12	22.12	66
    104	100093 ARG B, 200079 GLY C, 200093 ARG B, 82 TYR C, 200082 TYR C	6.34	132.25	-2.4	0.12	22.12	66
    105	200079 GLY C, 200093 ARG B, 82 TYR C, 200082 TYR C, 100079 GLY C	6.63	132.55	-1.58	0.04	12.4	61
    106	300093 ARG B, 300079 GLY C, 300082 TYR C, 79 GLY C, 93 ARG B	6.41	133.28	-2.22	-0.27	22.47	72
    107	300093 ARG B, 300082 TYR C, 79 GLY C, 93 ARG B, 28 SER B	6.01	134.13	-2.3	-0.3	22.13	83
    108	300093 ARG B, 300082 TYR C, 93 ARG B, 28 SER B	4.17	137.23	-2.78	-0.18	26.82	83
    109	300093 ARG B, 300082 TYR C, 28 SER B	3.44	138.54	-2.2	-0.09	18.43	83
    110	300093 ARG B, 28 SER B	3.08	139.29	-2.65	-0.7	26.84	100
    111	300027 GLN B, 300093 ARG B, 28 SER B	2.47	144.53	-2.93	-0.83	19.07	94
    112	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	4.34	145.11	-2.4	-0.87	14.72	100
    113	300028 SER B, 300027 GLN B, 300093 ARG B	4.97	145.45	-2.93	-0.83	19.07	94
    114	300028 SER B, 300027 GLN B, 300093 ARG B, 28 SER B	5.1	145.96	-2.4	-0.87	14.72	100
    115	300028 SER B, 300027 GLN B, 28 SER B	5.07	149.55	-1.7	-1.01	2.29	106
    116	100027 GLN B, 200027 GLN B, 100028 SER B, 200028 SER B	6	150.46	-2.05	-0.99	3.03	95
    117	300028 SER B, 300027 GLN B, 27 GLN B, 28 SER B	5.6	151.59	-2.05	-0.99	3.03	95
    118	300027 GLN B, 27 GLN B, 28 SER B	5.33	152.27	-2.6	-1.06	2.91	95
    119	300026 SER B, 300027 GLN B, 28 SER B	5.07	152.92	-1.57	-0.96	2.86	100
    120	300026 SER B, 300027 GLN B, 28 SER B, 69 THR B	4.51	155.59	-1.35	-0.91	2.56	102
    121	300026 SER B, 300027 GLN B, 28 SER B, 27 GLN B	4.85	155.78	-1.28	-0.92	2.99	100
    122	300026 SER B, 28 SER B, 69 THR B, 27 GLN B	4.9	156.17	-0.58	-0.84	2.52	112
    123	300026 SER B, 28 SER B, 69 THR B, 27 GLN B, 26 SER B	4.94	158.58	-0.46	-0.79	3.04	107
    124	300026 SER B, 69 THR B, 27 GLN B, 26 SER B	5	159.52	-0.48	-0.79	2.95	107
    125	300026 SER B, 69 THR B, 26 SER B	4.96	161.8	-0.5	-0.79	2.81	107
    126	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.71	162.73	-1.5	-0.7	15.11	95
    127	300026 SER B, 69 THR B, 24 ARG B	4.39	164.41	-1.87	-0.66	19.01	95
    128	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.96	165.7	-2.28	-0.76	26.69	92
    129	300026 SER B, 24 ARG B, 70 ASP B	3.63	166.56	-2.8	-0.75	35.03	84
    130	24 ARG B, 70 ASP B, 300026 SER B	3.49	168.42	-2.93	-0.81	34.46	95
    131	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.63	170.68	-1.25	-0.32	25.88	85
    132	70 ASP B, 300026 SER B, 300003 LEU B	2.09	173.15	-0.17	-0.29	17.17	85
    133	70 ASP B, 300003 LEU B	2.15	176.15	0.15	0.05	24.92	70
    134	70 ASP B, 300003 LEU B, 300001 ASP B	3.06	177.83	-0.03	-0.23	17.74	70
    135	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.92	177.96	-0.2	-0.37	13.72	82
    136	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.95	178.93	-0.98	-0.43	25.3	83
    137	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	4.09	179.16	-1.56	-0.42	30.14	81
    138	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.99	180.48	-1.08	-0.27	25.25	79
    139	300003 LEU B, 300001 ASP B, 300063 LYS A	3.75	182.27	-1.2	-0.1	33.11	70
    140	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.52	183.65	-1.08	-0.27	25.25	79
    141	300003 LEU B, 300063 LYS A, 300097 THR B, 300002 ILE B	3.49	184.08	-0.3	-0.21	13.67	77
    142	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.49	184.46	-1.08	-0.2	13.67	84
    143	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	3.51	185.22	-0.94	-0.32	11.61	84
    144	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	3.8	185.4	-2.4	-0.78	21.56	90
    145	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	3.96	185.6	-2.03	-0.87	14.58	96
    146	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.39	186.02	-2.4	-0.78	21.56	90
    147	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.61	187.86	-1.5	-0.4	21.26	76
    148	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	4.87	191.46	0.23	0.35	24.92	76
    149	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	4.42	192.33	-1.1	-0.35	25.3	80
    150	300063 LYS A, 300046 GLU A, 300064 ILE A	3.54	197.74	-0.97	0.09	33.18	84
    151	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.83	200.93	-0.98	-0.14	26.35	87
    152	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.53	204.72	-2	-0.04	38.51	86
    153	300046 GLU A, 18 ARG B, 300040 ARG A	4.1	206.92	-4.17	-0.66	51.3	81
    154	300046 GLU A, 300064 ILE A, 300040 ARG A	4.17	207.39	-1.17	0.08	34.01	87
    155	300046 GLU A, 300040 ARG A	2.11	210.69	-4	-0.78	50.95	80
    156	300040 ARG A	-0.04	216.9	-4.5	-0.42	52	83
    157	300040 ARG A, 300088 SER A	0.02	217.75	-2.45	-0.61	27.69	83
    158	300040 ARG A, 300088 SER A, 300091 SER A	0.31	218.22	-1.77	-0.67	19.59	83
    159	300040 ARG A, 300088 SER A, 300091 SER A	0.78	218.48	-1.9	-0.73	19.02	100
    160	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	1.37	218.72	-1.83	-0.57	14.66	86
    161	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.01	219.43	-1.73	-0.53	15.09	70
    162	300040 ARG A, 300088 SER A, 300041 PRO A	3.26	221.88	-2.17	-0.44	18.99	70
    163	300040 ARG A, 300041 PRO A, 300088 SER A	4.87	224.06	-2.3	-0.49	18.42	86
    164	300041 PRO A, 300088 SER A	4.74	225.42	-1.2	-0.53	1.63	87
    165	300091 SER A, 300041 PRO A, 300088 SER A	4.62	225.89	-1.07	-0.68	1.64	97
    166	300091 SER A, 300041 PRO A, 300088 SER A, 300175 LEU A	4.41	226.64	0.15	-0.22	1.26	86
    167	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.32	226.88	0.02	0.3	1.25	69
    168	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.25	227.08	0.23	0.08	1.27	84
    169	300091 SER A, 300088 SER A, 300180 TYR A	4.13	227.3	-0.97	-0.28	1.65	94
    170	300091 SER A, 300088 SER A	4.08	227.46	-0.8	-0.97	1.67	117
    171	300091 SER A, 300088 SER A, 300180 TYR A	4.05	227.84	-0.97	-0.28	1.65	94
    172	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.03	228.51	0.02	0.3	1.25	69
    173	300088 SER A, 300091 SER A, 300041 PRO A, 300175 LEU A, 300180 TYR A	4.02	229.37	-0.06	0.08	1.67	69
    174	300041 PRO A, 300175 LEU A, 300180 TYR A	4.02	233.31	0.3	0.72	1.11	54
    175	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.34	233.59	0.13	0.34	1.68	54
    176	300041 PRO A, 300175 LEU A, 300180 TYR A	4.43	234.26	0.3	0.72	1.11	54
    177	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.29	234.99	0.13	0.34	1.68	54
    178	300041 PRO A, 300180 TYR A, 300173 ALA A	3.81	237.23	-1.1	0.07	2.19	54
    179	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.31	239.02	-1.7	-0.23	14.12	61
    180	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.24	241.44	-1.78	-0.53	14.11	64
    181	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.43	241.96	-2.55	-0.52	14.11	74
    182	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.49	242.6	-2.55	-0.52	14.11	74
    183	300041 PRO A, 300172 PRO A, 300041 ASN B, 300042 GLY A	3.55	243.61	-1.78	-0.44	2.48	73
    184	300041 PRO A, 300172 PRO A, 300041 ASN B, 300042 GLY A	3.65	243.83	-1.78	-0.44	2.48	73
    185	300041 PRO A, 300172 PRO A, 300041 ASN B, 300042 GLY A	3.68	244.1	-1.78	-0.44	2.48	73
    186	300172 PRO A, 300041 ASN B, 300042 GLY A, 300165 ASP B	3.62	244.84	-2.25	-0.68	14.51	82
    187	300172 PRO A, 300041 ASN B, 300042 GLY A, 300165 ASP B, 300040 THR B	3.55	245.11	-1.94	-0.69	11.94	88
    188	300041 ASN B, 300042 GLY A, 300165 ASP B, 300040 THR B	3.22	247.5	-2.03	-0.85	14.53	99
    189	300042 GLY A, 300165 ASP B, 300040 THR B	3.21	248.73	-1.53	-0.87	18.25	96
    190	300042 GLY A, 300165 ASP B, 300085 ASN B	3.27	248.8	-2.47	-0.87	18.82	95
    191	300042 GLY A, 300165 ASP B, 300040 THR B, 300085 ASN B	3.23	249.12	-2.03	-0.85	14.53	99
    192	300165 ASP B, 300040 THR B, 300085 ASN B	2.9	249.63	-2.57	-0.86	18.25	99
    193	300042 GLY A, 300165 ASP B, 300085 ASN B	2.67	254.89	-2.47	-0.87	18.82	95
    194	300042 GLY A, 300165 ASP B, 300085 ASN B, 300103 LYS B	3.54	255.95	-2.83	-0.76	26.49	87
    195	300042 GLY A, 300165 ASP B, 300103 LYS B, 300010 ILE B	3.93	256.15	-0.83	-0.11	25.68	87

    pore with bottle neck

    pore with local minimum

21. 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

22. 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

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, 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

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, 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, 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, 200093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR 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, 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, 42 GLY A, 165 ASP B, 40 THR B, 85 ASN B, 103 LYS B, 10 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, 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, 200093 ARG B, 82 TYR C, 300082 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, 91 SER A, 41 PRO A, 88 SER A, 175 LEU A, 180 TYR A, 153 GLU A, 172 PRO A, 41 ASN B, 165 ASP B, 40 THR B, 85 ASN B, 103 LYS B, 10 ILE B

    Physicochemical properties of lining side-chains

    Charge: 4 (13-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.41
    Polarity: 15.58
    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	0.25	-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	3.19	0.68	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.83	-1.53	-0.78	2.81	105
    5	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.2	0.98	-1.33	-0.78	2.52	106
    6	100156 THR A, 100157 VAL A, 100041 ASN B	3.11	1.3	-1.53	-0.78	2.81	105
    7	100156 THR A, 100157 VAL A, 100170 THR A, 100041 ASN B	3.05	1.73	-1.33	-0.78	2.52	106
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.69	5.4	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.65	6.67	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.8	6.84	-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	2.62	7.91	-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	8.64	-0.8	-0.47	12.03	78
    14	100041 ASN B, 100171 PHE A, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.34	9.13	-1.64	-0.86	12.68	90
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.29	9.71	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.27	12.88	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	3.09	13.22	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.29	13.76	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.58	14.64	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.44	16.83	-1.78	-0.53	14.11	64
    21	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.41	18.64	-1.7	-0.23	14.12	61
    22	100173 ALA A, 100041 PRO A, 100180 TYR A	3.52	21.06	-1.1	0.07	2.19	54
    23	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.1	21.4	0.13	0.34	1.68	54
    24	100041 PRO A, 100180 TYR A, 100175 LEU A	4.4	22.08	0.3	0.72	1.11	54
    25	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.37	22.41	0.13	0.34	1.68	54
    26	100041 PRO A, 100180 TYR A, 100175 LEU A	4.19	27	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	27.66	-0.06	0.08	1.67	69
    28	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.11	28.05	0.02	0.3	1.25	69
    29	100180 TYR A, 100091 SER A, 100088 SER A	4.09	28.21	-0.97	-0.28	1.65	94
    30	100091 SER A, 100088 SER A	4.08	28.28	-0.8	-0.97	1.67	117
    31	100180 TYR A, 100091 SER A, 100088 SER A	4.08	28.6	-0.97	-0.28	1.65	94
    32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.16	28.84	0.23	0.08	1.27	84
    33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.23	29.53	0.02	0.3	1.25	69
    34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	29.98	0.15	-0.22	1.26	86
    35	100041 PRO A, 100091 SER A, 100088 SER A	4.57	30.45	-1.07	-0.68	1.64	97
    36	100041 PRO A, 100088 SER A	4.73	31.69	-1.2	-0.53	1.63	87
    37	100041 PRO A, 100088 SER A, 100040 ARG A	4.86	33.98	-2.3	-0.49	18.42	86
    38	100041 PRO A, 100088 SER A, 100040 ARG A	3.32	36.27	-2.17	-0.44	18.99	70
    39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.33	36.95	-1.73	-0.53	15.09	70
    40	100088 SER A, 100040 ARG A, 100091 SER A	1.02	37.96	-1.77	-0.67	19.59	83
    41	100088 SER A, 100040 ARG A	0.63	39.99	-2.45	-0.61	27.69	83
    42	100040 ARG A	0.67	45.68	-4.5	-0.42	52	83
    43	100040 ARG A, 100043 HIS A	2.2	46.73	-3.85	-0.08	51.8	87
    44	100040 ARG A, 100043 HIS A, 100046 GLU A	2.7	47.61	-3.73	-0.43	51.17	83
    45	100040 ARG A, 100046 GLU A	3.16	50.01	-4	-0.78	50.95	80
    46	100040 ARG A, 100046 GLU A, 100064 ILE A	3.91	50.65	-1.17	0.08	34.01	87
    47	100040 ARG A, 100046 GLU A, 300018 ARG B	3.76	52.69	-4.17	-0.66	51.3	81
    48	100040 ARG A, 100046 GLU A, 100064 ILE A, 300018 ARG B	3.56	56.38	-2	-0.04	38.51	86
    49	100046 GLU A, 100064 ILE A, 300018 ARG B, 100063 LYS A	3.69	59.61	-0.98	-0.14	26.35	87
    50	100046 GLU A, 100064 ILE A, 100063 LYS A	3.79	60.38	0.2	-0.04	17.8	90
    51	100046 GLU A, 100064 ILE A, 100063 LYS A	3.83	64.82	-0.97	0.09	33.18	84
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	4.26	65.29	-0.93	-0.18	25.3	92
    53	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	4.32	66.16	-1.1	-0.35	25.3	80
    54	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.42	69.28	0.23	0.35	24.92	76
    55	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B	4.48	70.27	-1	-0.3	25.73	67
    56	100046 GLU A, 100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A	4.46	70.99	-1.5	-0.4	21.26	76
    57	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.42	71.37	-2.4	-0.78	21.56	90
    58	100046 GLU A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.24	71.73	-2.03	-0.87	14.58	96
    59	100046 GLU A, 100063 LYS A, 100098 PHE B, 100061 ASN A, 100097 THR B	4.15	71.94	-2.4	-0.78	21.56	90
    60	100063 LYS A, 100003 LEU B, 100098 PHE B, 100061 ASN A, 100097 THR B	3.85	72.84	-0.94	-0.32	11.61	84
    61	100063 LYS A, 100003 LEU B, 100098 PHE B, 100097 THR B	3.76	73.25	-0.3	-0.21	13.67	77
    62	100063 LYS A, 100003 LEU B, 100097 THR B, 100002 ILE B	3.68	73.68	-0.3	-0.21	13.67	77
    63	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.59	75.13	-1.08	-0.27	25.25	79
    64	100063 LYS A, 100003 LEU B, 100001 ASP B	3.64	77.35	-1.2	-0.1	33.11	70
    65	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.96	78.14	-1.08	-0.27	25.25	79
    66	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.14	78.34	-1.56	-0.42	30.14	81
    67	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	3.82	79.17	-0.98	-0.43	25.3	83
    68	100003 LEU B, 300070 ASP B, 100001 ASP B	3.1	81.24	-0.03	-0.23	17.74	70
    69	100003 LEU B, 300070 ASP B	2.22	84.27	0.15	0.05	24.92	70
    70	100003 LEU B, 300070 ASP B, 100026 SER B	2.11	87.14	-0.17	-0.29	17.17	85
    71	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.49	88.82	-1.25	-0.32	25.88	85
    72	300070 ASP B, 100026 SER B, 300024 ARG B	3.21	90.45	-2.93	-0.81	34.46	95
    73	300070 ASP B, 300024 ARG B, 100026 SER B	3.67	91.34	-2.8	-0.75	35.03	84
    74	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	3.7	93.27	-2.28	-0.76	26.69	92
    75	300024 ARG B, 100026 SER B, 300069 THR B	4.36	94.66	-1.87	-0.66	19.01	95
    76	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.91	95.45	-1.5	-0.7	15.11	95
    77	100026 SER B, 300069 THR B, 300026 SER B	4.34	98.33	-0.5	-0.79	2.81	107
    78	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.32	99.25	-0.48	-0.79	2.95	107
    79	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.38	101.33	-0.46	-0.79	3.04	107
    80	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.92	101.65	-1.28	-0.92	2.99	100
    81	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.23	104.38	-1.35	-0.91	2.56	102
    82	100026 SER B, 100027 GLN B, 300028 SER B	5.09	105.04	-1.57	-0.96	2.86	100
    83	300027 GLN B, 100027 GLN B, 300028 SER B	5.47	105.68	-1.57	-0.96	2.86	100
    84	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.84	106.66	-2.05	-0.99	3.03	95
    85	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.32	107.52	-2.05	-0.99	3.03	95
    86	200027 GLN B, 200028 SER B, 100028 SER B	6.14	107.98	-1.7	-1.01	2.29	106
    87	100027 GLN B, 300028 SER B, 100028 SER B	5.37	111.37	-1.7	-1.01	2.29	106
    88	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	5.17	111.63	-2.4	-0.87	14.72	100
    89	100027 GLN B, 100028 SER B, 100093 ARG B	4.5	112.04	-2.93	-0.83	19.07	94
    90	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	3.83	113.02	-2.4	-0.87	14.72	100
    91	100027 GLN B, 300028 SER B, 100093 ARG B	2.76	118.27	-2.93	-0.83	19.07	94
    92	300028 SER B, 100093 ARG B	3.34	118.98	-2.65	-0.7	26.84	100
    93	300028 SER B, 100093 ARG B, 100082 TYR C	3.6	120.09	-2.2	-0.09	18.43	83
    94	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.15	123.08	-2.78	-0.18	26.82	83
    95	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	5.93	123.89	-2.3	-0.3	22.13	83
    96	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.33	124.81	-2.22	-0.27	22.47	72
    97	93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C	6.62	125	-2.22	-0.27	22.47	72
    98	93 ARG B, 200093 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.25	125.39	-2.4	0.12	22.12	66
    99	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	5.97	125.85	-2.4	0.12	22.12	66
    100	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	4.92	128.37	-1.58	0.04	12.4	61
    101	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	3.42	131.62	-2.43	-0.3	15.13	72
    102	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.29	132.8	-2.2	-0.78	15.57	83
    103	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.63	135.1	-2.43	-0.3	15.13	72
    104	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	5	135.99	-2.2	-0.02	12.43	66
    105	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	5.54	136.84	-2.4	0.12	22.12	66
    106	100093 ARG B, 100079 GLY C, 200093 ARG B, 200079 GLY C, 200082 TYR C	6.05	138.12	-2.22	-0.27	22.47	72
    107	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	6.8	138.67	-2.22	-0.27	22.47	72
    108	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	6.89	138.96	-2.3	-0.3	22.13	83
    109	100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	6.69	139.37	-2.4	0.12	22.12	66
    110	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	6.41	140.02	-2.4	0.12	22.12	66
    111	100079 GLY C, 200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.7	141.84	-1.58	0.04	12.4	61
    112	200093 ARG B, 82 TYR C, 200079 GLY C, 200082 TYR C	5.31	142.8	-1.88	0.25	14.65	61
    113	200093 ARG B, 200079 GLY C, 200082 TYR C, 200058 GLN C	3.63	145.28	-2.43	-0.3	15.13	72
    114	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	3.33	145.98	-2.2	-0.78	15.57	83
    115	200093 ARG B, 82 TYR C, 200079 GLY C, 200058 GLN C	3.29	147.11	-2.43	-0.3	15.13	72
    116	200093 ARG B, 82 TYR C, 200058 GLN C, 200080 ASP C	3.76	147.29	-2.43	-0.3	15.13	72
    117	200093 ARG B, 82 TYR C, 200058 GLN C	3.8	148.27	-3.1	-0.14	19.05	72
    118	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.78	148.83	-2.53	-0.35	14.7	83
    119	200028 SER B, 200093 ARG B, 200058 GLN C	3.83	149.24	-2.93	-0.83	19.07	94
    120	200028 SER B, 200093 ARG B, 82 TYR C, 200058 GLN C	3.54	150.47	-2.53	-0.35	14.7	83
    121	200028 SER B, 93 ARG B, 200093 ARG B, 82 TYR C	3.35	150.88	-2.78	-0.18	26.82	83
    122	200028 SER B, 93 ARG B, 82 TYR C	2.86	152.75	-2.2	-0.09	18.43	83
    123	200028 SER B, 93 ARG B	2.79	153.47	-2.65	-0.7	26.84	100
    124	27 GLN B, 200028 SER B, 93 ARG B	2.81	158.38	-2.93	-0.83	19.07	94
    125	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	4.21	158.91	-2.4	-0.87	14.72	100
    126	27 GLN B, 93 ARG B, 28 SER B	4.39	159.25	-2.93	-0.83	19.07	94
    127	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	4.72	159.76	-2.4	-0.87	14.72	100
    128	27 GLN B, 200028 SER B, 28 SER B	5.14	163.3	-1.7	-1.01	2.29	106
    129	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	6.28	164.61	-2.05	-0.99	3.03	95
    130	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	6.07	165.19	-2.05	-0.99	3.03	95
    131	27 GLN B, 200027 GLN B, 200028 SER B	5.82	165.84	-2.6	-1.06	2.91	95
    132	27 GLN B, 200028 SER B, 200027 GLN B	5.54	166.49	-1.57	-0.96	2.86	100
    133	27 GLN B, 200028 SER B, 26 SER B	5.25	167.08	-1.57	-0.96	2.86	100
    134	27 GLN B, 200028 SER B, 26 SER B, 200069 THR B	4.25	169.31	-1.35	-0.91	2.56	102
    135	27 GLN B, 200028 SER B, 200027 GLN B, 26 SER B	5.01	169.69	-1.28	-0.92	2.99	100
    136	200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B, 200028 SER B	4.95	172.61	-0.46	-0.79	3.04	107
    137	200027 GLN B, 26 SER B, 200069 THR B, 200026 SER B	4.83	173.52	-0.48	-0.79	2.95	107
    138	26 SER B, 200069 THR B, 200026 SER B	4.58	175.62	-0.5	-0.79	2.81	107
    139	26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B	4.65	176.53	-1.5	-0.7	15.11	95
    140	26 SER B, 200069 THR B, 200024 ARG B	4.58	178.17	-1.87	-0.66	19.01	95
    141	26 SER B, 200069 THR B, 200024 ARG B, 200070 ASP B	3.96	179.46	-2.28	-0.76	26.69	92
    142	26 SER B, 200024 ARG B, 200070 ASP B	3.57	180.34	-2.8	-0.75	35.03	84
    143	200024 ARG B, 200070 ASP B, 26 SER B	3.38	182.43	-2.93	-0.81	34.46	95
    144	200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B	2.67	184.18	-1.25	-0.32	25.88	85
    145	200070 ASP B, 26 SER B, 3 LEU B	2.11	187.1	-0.17	-0.29	17.17	85
    146	200070 ASP B, 3 LEU B	2.22	189.6	0.15	0.05	24.92	70
    147	200070 ASP B, 3 LEU B, 1 ASP B	2.93	191.6	-0.03	-0.23	17.74	70
    148	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B	3.93	191.74	-0.2	-0.37	13.72	82
    149	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B	3.97	192.64	-0.98	-0.43	25.3	83
    150	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.97	192.85	-1.56	-0.42	30.14	81
    151	3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.89	193.97	-1.08	-0.27	25.25	79
    152	3 LEU B, 1 ASP B, 63 LYS A	3.82	195.73	-1.2	-0.1	33.11	70
    153	3 LEU B, 1 ASP B, 63 LYS A, 97 THR B	3.7	197.58	-1.08	-0.27	25.25	79
    154	3 LEU B, 63 LYS A, 97 THR B, 2 ILE B	3.65	197.99	-0.3	-0.21	13.67	77
    155	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B	3.59	198.35	-0.3	-0.21	13.67	77
    156	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B, 61 ASN A	3.51	199.06	-0.94	-0.32	11.61	84
    157	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	3.57	199.22	-2.4	-0.78	21.56	90
    158	97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	3.69	199.42	-2.03	-0.87	14.58	96
    159	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.18	199.86	-2.4	-0.78	21.56	90
    160	3 LEU B, 63 LYS A, 98 PHE B, 61 ASN A, 46 GLU A	4.53	200.65	-1.5	-0.4	21.26	76
    161	3 LEU B, 63 LYS A, 98 PHE B, 46 GLU A	4.91	201.69	-1	-0.3	25.73	67
    162	3 LEU B, 63 LYS A, 46 GLU A, 64 ILE A	5.26	205.24	0.23	0.35	24.92	76
    163	3 LEU B, 63 LYS A, 46 GLU A, 200020 SER B	5.37	206.05	-1.1	-0.35	25.3	80
    164	63 LYS A, 46 GLU A, 64 ILE A, 200020 SER B	4.96	206.78	-0.93	-0.18	25.3	92
    165	63 LYS A, 46 GLU A, 64 ILE A	2.89	211.29	-0.97	0.09	33.18	84
    166	46 GLU A, 64 ILE A, 63 LYS A	3.06	212.05	0.2	-0.04	17.8	90
    167	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	3.24	214.48	-0.98	-0.14	26.35	87
    168	46 GLU A, 64 ILE A, 200018 ARG B	3.75	215.04	-1.17	0.08	34.01	87
    169	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3.51	218.12	-2	-0.04	38.51	86
    170	46 GLU A, 200018 ARG B, 40 ARG A	4.17	220.76	-4.17	-0.66	51.3	81
    171	46 GLU A, 64 ILE A, 40 ARG A	3.99	221.25	-1.17	0.08	34.01	87
    172	46 GLU A, 40 ARG A	3.28	224.56	-4	-0.78	50.95	80
    173	40 ARG A	2.35	230.64	-4.5	-0.42	52	83
    174	40 ARG A, 88 SER A	2.21	231.5	-2.45	-0.61	27.69	83
    175	40 ARG A, 88 SER A, 91 SER A	2.14	231.98	-1.77	-0.67	19.59	83
    176	40 ARG A, 88 SER A, 91 SER A	2.15	232.24	-1.9	-0.73	19.02	100
    177	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.23	232.47	-1.83	-0.57	14.66	86
    178	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	2.39	233.14	-1.73	-0.53	15.09	70
    179	40 ARG A, 88 SER A, 41 PRO A	2.87	235.49	-2.17	-0.44	18.99	70
    180	40 ARG A, 41 PRO A, 88 SER A	4.09	237.69	-2.3	-0.49	18.42	86
    181	41 PRO A, 88 SER A	5.08	238.95	-1.2	-0.53	1.63	87
    182	91 SER A, 41 PRO A, 88 SER A	4.81	239.87	-1.07	-0.68	1.64	97
    183	91 SER A, 41 PRO A, 88 SER A, 175 LEU A	4.67	240.24	0.15	-0.22	1.26	86
    184	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.46	240.75	0.02	0.3	1.25	69
    185	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.41	240.93	0.23	0.08	1.27	84
    186	91 SER A, 88 SER A, 180 TYR A	4.37	241.12	-0.97	-0.28	1.65	94
    187	91 SER A, 88 SER A	4.38	241.32	-0.8	-0.97	1.67	117
    188	91 SER A, 88 SER A, 180 TYR A	4.39	241.77	-0.97	-0.28	1.65	94
    189	88 SER A, 91 SER A, 41 PRO A, 175 LEU A, 180 TYR A	4.41	242.47	-0.06	0.08	1.67	69
    190	91 SER A, 41 PRO A, 175 LEU A, 180 TYR A	4.44	243.34	0.02	0.3	1.25	69
    191	41 PRO A, 175 LEU A, 180 TYR A	4.45	246.95	0.3	0.72	1.11	54
    192	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.41	247.38	0.13	0.34	1.68	54
    193	41 PRO A, 175 LEU A, 180 TYR A	4.36	248.03	0.3	0.72	1.11	54
    194	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.39	248.64	0.13	0.34	1.68	54
    195	41 PRO A, 180 TYR A, 173 ALA A	3.75	250.8	-1.1	0.07	2.19	54
    196	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.28	253	-1.7	-0.23	14.12	61
    197	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.28	255.02	-1.78	-0.53	14.11	64
    198	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.44	255.56	-2.55	-0.52	14.11	74
    199	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.48	256.47	-2.55	-0.52	14.11	74
    200	41 PRO A, 172 PRO A, 41 ASN B, 42 GLY A	3.55	257.44	-1.78	-0.44	2.48	73
    201	41 PRO A, 172 PRO A, 41 ASN B, 42 GLY A	3.64	257.65	-1.78	-0.44	2.48	73
    202	41 PRO A, 172 PRO A, 41 ASN B, 42 GLY A	3.66	257.9	-1.78	-0.44	2.48	73
    203	172 PRO A, 41 ASN B, 42 GLY A, 165 ASP B	3.61	258.61	-2.25	-0.68	14.51	82
    204	172 PRO A, 41 ASN B, 42 GLY A, 165 ASP B, 40 THR B	3.57	258.88	-1.94	-0.69	11.94	88
    205	41 ASN B, 42 GLY A, 165 ASP B, 40 THR B	3.33	261.2	-2.03	-0.85	14.53	99
    206	42 GLY A, 165 ASP B, 40 THR B	3.26	262.5	-1.53	-0.87	18.25	96
    207	42 GLY A, 165 ASP B, 85 ASN B	3.26	262.63	-2.47	-0.87	18.82	95
    208	42 GLY A, 165 ASP B, 40 THR B, 85 ASN B	3.24	262.85	-2.03	-0.85	14.53	99
    209	165 ASP B, 40 THR B, 85 ASN B	2.94	263.25	-2.57	-0.86	18.25	99
    210	42 GLY A, 165 ASP B, 40 THR B, 85 ASN B	2.85	263.63	-2.03	-0.85	14.53	99
    211	42 GLY A, 165 ASP B, 85 ASN B	2.7	268.77	-2.47	-0.87	18.82	95
    212	42 GLY A, 165 ASP B, 85 ASN B, 103 LYS B	3.58	269.77	-2.83	-0.76	26.49	87
    213	42 GLY A, 165 ASP B, 103 LYS B, 10 ILE B	3.93	269.96	-0.83	-0.11	25.68	87

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    200042 GLY A, 200040 THR B, 200085 ASN B, 200165 ASP B, 200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A, 200173 ALA A, 200180 TYR A, 200175 LEU A, 200088 SER A, 200091 SER A, 200088 SER A, 200040 ARG A, 200091 SER A, 200043 HIS A, 200046 GLU A, 200064 ILE A, 100018 ARG B, 200063 LYS A, 200063 LYS A, 100020 SER B, 200003 LEU B, 200098 PHE B, 200061 ASN A, 200097 THR B, 200002 ILE B, 200001 ASP B, 100072 THR B, 100070 ASP B, 200001 ASP B, 200026 SER B, 100024 ARG B, 200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B, 100028 SER B, 100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B, 200028 SER B, 27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C, 200079 GLY C, 300093 ARG B, 100082 TYR C, 300079 GLY C, 300082 TYR C, 93 ARG B, 79 GLY C, 82 TYR C, 200058 GLN C, 200080 ASP C, 300028 SER B, 58 GLN C, 80 ASP C, 300026 SER B, 69 THR B, 27 GLN 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, 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, 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

    Unique lining residues set - sidechains

    200040 THR B, 200085 ASN B, 200165 ASP B, 200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A, 200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A, 200040 ARG A, 200043 HIS A, 200046 GLU A, 200064 ILE A, 100018 ARG B, 200063 LYS A, 100020 SER B, 200003 LEU B, 200061 ASN A, 200097 THR B, 200001 ASP B, 100072 THR B, 100070 ASP B, 200026 SER B, 100024 ARG B, 100069 THR B, 100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B, 27 GLN B, 28 SER B, 300027 GLN B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 300093 ARG B, 100082 TYR C, 300082 TYR C, 93 ARG B, 82 TYR C, 200058 GLN C, 300028 SER B, 58 GLN C, 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,

    Physicochemical properties of lining side-chains

    Charge: 3 (12-9)
    Hydropathy: -1.5
    Hydrophobicity: -0.41
    Polarity: 15.09
    Mutability: 87
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	200042 GLY A, 200040 THR B, 200085 ASN B, 200165 ASP B	3.23	0.13	-2.03	-0.85	14.53	99
    2	200042 GLY A, 200040 THR B, 200165 ASP B	3.18	1.91	-1.53	-0.87	18.25	96
    3	200042 GLY A, 200040 THR B, 200165 ASP B, 200041 ASN B	3.29	3.97	-2.03	-0.85	14.53	99
    4	200042 GLY A, 200040 THR B, 200165 ASP B, 200041 ASN B, 200172 PRO A	3.6	4.19	-1.94	-0.69	11.94	88
    5	200042 GLY A, 200165 ASP B, 200041 ASN B, 200172 PRO A	3.64	4.76	-2.25	-0.68	14.51	82
    6	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.68	5.1	-1.78	-0.44	2.48	73
    7	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.66	5.36	-1.78	-0.44	2.48	73
    8	200042 GLY A, 200041 ASN B, 200172 PRO A, 200041 PRO A	3.58	6.36	-1.78	-0.44	2.48	73
    9	200041 ASN B, 200172 PRO A, 200041 PRO A	3.56	6.67	-2.23	-0.32	2.18	73
    10	200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A	3.54	7.17	-2.55	-0.52	14.11	74
    11	200041 ASN B, 200172 PRO A, 200041 PRO A, 200153 GLU A	3.53	7.73	-2.55	-0.52	14.11	74
    12	200172 PRO A, 200041 PRO A, 200153 GLU A, 200173 ALA A	3.33	10.16	-1.78	-0.53	14.11	64
    13	200041 PRO A, 200153 GLU A, 200173 ALA A, 200180 TYR A	3.29	11.93	-1.7	-0.23	14.12	61
    14	200041 PRO A, 200173 ALA A, 200180 TYR A	3.46	14.3	-1.1	0.07	2.19	54
    15	200041 PRO A, 200173 ALA A, 200180 TYR A, 200175 LEU A	4.3	14.63	0.13	0.34	1.68	54
    16	200041 PRO A, 200180 TYR A, 200175 LEU A	4.35	15.29	0.3	0.72	1.11	54
    17	200041 PRO A, 200173 ALA A, 200180 TYR A, 200175 LEU A	4.38	15.82	0.13	0.34	1.68	54
    18	200041 PRO A, 200180 TYR A, 200175 LEU A	4.48	20.47	0.3	0.72	1.11	54
    19	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A, 200091 SER A	4.47	21.04	-0.06	0.08	1.67	69
    20	200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A	4.45	21.36	0.23	0.08	1.27	84
    21	200180 TYR A, 200091 SER A, 200088 SER A	4.43	21.49	-0.97	-0.28	1.65	94
    22	200091 SER A, 200088 SER A	4.41	21.56	-0.8	-0.97	1.67	117
    23	200180 TYR A, 200091 SER A, 200088 SER A	4.4	21.89	-0.97	-0.28	1.65	94
    24	200180 TYR A, 200175 LEU A, 200091 SER A, 200088 SER A	4.44	22.12	0.23	0.08	1.27	84
    25	200041 PRO A, 200180 TYR A, 200175 LEU A, 200088 SER A	4.49	22.42	0.02	0.3	1.25	69
    26	200041 PRO A, 200175 LEU A, 200091 SER A, 200088 SER A	4.58	23.24	0.15	-0.22	1.26	86
    27	200041 PRO A, 200091 SER A, 200088 SER A	4.82	23.7	-1.07	-0.68	1.64	97
    28	200041 PRO A, 200088 SER A	4.96	24.91	-1.2	-0.53	1.63	87
    29	200041 PRO A, 200088 SER A, 200040 ARG A	4.13	27.67	-2.3	-0.49	18.42	86
    30	200041 PRO A, 200088 SER A, 200040 ARG A	2.99	29.74	-2.17	-0.44	18.99	70
    31	200041 PRO A, 200088 SER A, 200040 ARG A, 200091 SER A	2.73	30.06	-1.73	-0.53	15.09	70
    32	200088 SER A, 200040 ARG A, 200091 SER A	1.91	31.5	-1.77	-0.67	19.59	83
    33	200088 SER A, 200040 ARG A	1.79	32.45	-2.45	-0.61	27.69	83
    34	200040 ARG A	1.73	39.19	-4.5	-0.42	52	83
    35	200040 ARG A, 200043 HIS A	2.39	40.16	-3.85	-0.08	51.8	87
    36	200040 ARG A, 200046 GLU A	2.74	43.32	-4	-0.78	50.95	80
    37	200040 ARG A, 200046 GLU A, 200064 ILE A	4.21	43.94	-1.17	0.08	34.01	87
    38	200040 ARG A, 200046 GLU A, 100018 ARG B	4.44	45.91	-4.17	-0.66	51.3	81
    39	200040 ARG A, 200046 GLU A, 200064 ILE A, 100018 ARG B	3.49	49.41	-2	-0.04	38.51	86
    40	200046 GLU A, 200064 ILE A, 100018 ARG B	3.62	49.97	-1.17	0.08	34.01	87
    41	200046 GLU A, 200064 ILE A, 100018 ARG B, 200063 LYS A	2.78	53.21	-0.98	-0.14	26.35	87
    42	200046 GLU A, 200064 ILE A, 200063 LYS A	2.73	58.2	-0.97	0.09	33.18	84
    43	200046 GLU A, 200064 ILE A, 200063 LYS A, 100020 SER B	5.72	58.61	-0.93	-0.18	25.3	92
    44	200046 GLU A, 200063 LYS A, 100020 SER B, 200003 LEU B	5.88	59.52	-1.1	-0.35	25.3	80
    45	200046 GLU A, 200064 ILE A, 200063 LYS A, 200003 LEU B	5.15	62.58	0.23	0.35	24.92	76
    46	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B	4.81	63.54	-1	-0.3	25.73	67
    47	200046 GLU A, 200063 LYS A, 200003 LEU B, 200098 PHE B, 200061 ASN A	4.24	64.62	-1.5	-0.4	21.26	76
    48	200046 GLU A, 200098 PHE B, 200061 ASN A, 200097 THR B	3.95	64.97	-2.03	-0.87	14.58	96
    49	200046 GLU A, 200063 LYS A, 200098 PHE B, 200061 ASN A, 200097 THR B	3.96	65.17	-2.4	-0.78	21.56	90
    50	200063 LYS A, 200003 LEU B, 200098 PHE B, 200061 ASN A, 200097 THR B	3.99	66	-0.94	-0.32	11.61	84
    51	200063 LYS A, 200003 LEU B, 200098 PHE B, 200097 THR B	3.99	66.4	-0.3	-0.21	13.67	77
    52	200063 LYS A, 200003 LEU B, 200097 THR B, 200002 ILE B	3.93	66.81	-0.3	-0.21	13.67	77
    53	200063 LYS A, 200003 LEU B, 200097 THR B, 200001 ASP B	3.61	68.73	-1.08	-0.27	25.25	79
    54	200063 LYS A, 200003 LEU B, 200001 ASP B	3.56	70.39	-1.2	-0.1	33.11	70
    55	200063 LYS A, 200003 LEU B, 200001 ASP B, 100072 THR B	3.66	71.29	-1.08	-0.27	25.25	79
    56	200063 LYS A, 200003 LEU B, 200001 ASP B, 100072 THR B, 100070 ASP B	3.93	71.48	-1.56	-0.42	30.14	81
    57	200003 LEU B, 200001 ASP B, 100072 THR B, 100070 ASP B	3.91	72.45	-0.98	-0.43	25.3	83
    58	200003 LEU B, 100070 ASP B, 200001 ASP B	3.02	74.78	-0.03	-0.23	17.74	70
    59	200003 LEU B, 100070 ASP B	2.11	77.75	0.15	0.05	24.92	70
    60	200003 LEU B, 100070 ASP B, 200026 SER B	2.08	80.08	-0.17	-0.29	17.17	85
    61	200003 LEU B, 100070 ASP B, 200026 SER B, 100024 ARG B	2.44	82.16	-1.25	-0.32	25.88	85
    62	100070 ASP B, 200026 SER B, 100024 ARG B	3.27	83.72	-2.93	-0.81	34.46	95
    63	100070 ASP B, 100024 ARG B, 200026 SER B	3.71	84.85	-2.8	-0.75	35.03	84
    64	100070 ASP B, 100024 ARG B, 200026 SER B, 100069 THR B	3.79	86.32	-2.28	-0.76	26.69	92
    65	100024 ARG B, 200026 SER B, 100069 THR B	4.21	87.79	-1.87	-0.66	19.01	95
    66	100024 ARG B, 200026 SER B, 100069 THR B, 100026 SER B	4.8	88.87	-1.5	-0.7	15.11	95
    67	200026 SER B, 100069 THR B, 100026 SER B	4.41	91.84	-0.5	-0.79	2.81	107
    68	200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B	4.38	92.72	-0.48	-0.79	2.95	107
    69	200026 SER B, 100069 THR B, 100026 SER B, 100027 GLN B, 100028 SER B	4.42	94.43	-0.46	-0.79	3.04	107
    70	200026 SER B, 100069 THR B, 100027 GLN B, 100028 SER B	4.77	94.62	-0.58	-0.84	2.52	112
    71	200026 SER B, 100027 GLN B, 100028 SER B, 200027 GLN B	4.89	94.75	-1.28	-0.92	2.99	100
    72	200026 SER B, 100069 THR B, 100028 SER B, 200027 GLN B	4.26	97.51	-1.35	-0.91	2.56	102
    73	200026 SER B, 100028 SER B, 200027 GLN B	5	98.14	-1.57	-0.96	2.86	100
    74	100027 GLN B, 100028 SER B, 200027 GLN B	5.37	98.77	-1.57	-0.96	2.86	100
    75	100028 SER B, 200027 GLN B, 100027 GLN B	5.74	99.35	-2.6	-1.06	2.91	95
    76	100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B	6.08	99.8	-2.05	-0.99	3.03	95
    77	100028 SER B, 200027 GLN B, 200028 SER B	6.36	100.1	-1.7	-1.01	2.29	106
    78	27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B	6.29	100.99	-2.05	-0.99	3.03	95
    79	100028 SER B, 200027 GLN B, 200028 SER B	5.42	104.46	-1.7	-1.01	2.29	106
    80	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	5.06	104.93	-2.4	-0.87	14.72	100
    81	200027 GLN B, 200028 SER B, 200093 ARG B	4.37	105.35	-2.93	-0.83	19.07	94
    82	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	4.08	105.76	-2.4	-0.87	14.72	100
    83	100028 SER B, 200027 GLN B, 200028 SER B, 200093 ARG B	3.78	106.34	-2.3	-0.82	15.15	94
    84	100028 SER B, 200027 GLN B, 200093 ARG B	2.91	111.43	-2.93	-0.83	19.07	94
    85	100028 SER B, 200093 ARG B	3.27	112.12	-2.65	-0.7	26.84	100
    86	100028 SER B, 200093 ARG B, 200082 TYR C	3.47	113.68	-2.2	-0.09	18.43	83
    87	100028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B	4.21	116.57	-2.78	-0.18	26.82	83
    88	100028 SER B, 200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C	6.09	117.33	-2.3	-0.3	22.13	83
    89	200093 ARG B, 200082 TYR C, 100093 ARG B, 100079 GLY C, 200079 GLY C	6.46	117.93	-2.22	-0.27	22.47	72
    90	100079 GLY C, 300093 ARG B, 100082 TYR C, 300079 GLY C, 300082 TYR C	6.67	118.16	-1.58	0.04	12.4	61
    91	300093 ARG B, 300079 GLY C, 300082 TYR C, 93 ARG B, 79 GLY C	6.71	118.33	-2.22	-0.27	22.47	72
    92	300093 ARG B, 100082 TYR C, 300079 GLY C, 300082 TYR C, 93 ARG B	6.45	118.76	-2.4	0.12	22.12	66
    93	100093 ARG B, 300093 ARG B, 100082 TYR C, 300079 GLY C, 300082 TYR C	6.25	119.27	-2.4	0.12	22.12	66
    94	200093 ARG B, 200082 TYR C, 100079 GLY C, 200079 GLY C, 82 TYR C	5.67	120.86	-1.58	0.04	12.4	61
    95	200093 ARG B, 200082 TYR C, 200079 GLY C, 82 TYR C	5.3	121.78	-1.88	0.25	14.65	61
    96	200093 ARG B, 200082 TYR C, 200079 GLY C, 200058 GLN C	3.23	124.9	-2.43	-0.3	15.13	72
    97	200093 ARG B, 200079 GLY C, 200058 GLN C, 200080 ASP C	2.95	126.04	-2.2	-0.78	15.57	83
    98	200093 ARG B, 200079 GLY C, 82 TYR C, 200058 GLN C	3.36	128.23	-2.43	-0.3	15.13	72
    99	200093 ARG B, 200082 TYR C, 200079 GLY C, 82 TYR C, 200058 GLN C	4.91	129.1	-2.2	-0.02	12.43	66
    100	200093 ARG B, 200082 TYR C, 200079 GLY C, 93 ARG B, 82 TYR C	5.5	130.68	-2.4	0.12	22.12	66
    101	200093 ARG B, 200079 GLY C, 93 ARG B, 79 GLY C, 82 TYR C	6.54	131.27	-2.22	-0.27	22.47	72
    102	200093 ARG B, 100093 ARG B, 300093 ARG B, 300079 GLY C, 93 ARG B	6.93	131.67	-3.68	-0.5	42.28	83
    103	100093 ARG B, 100079 GLY C, 300093 ARG B, 100082 TYR C, 300079 GLY C	7.2	131.91	-2.22	-0.27	22.47	72
    104	100093 ARG B, 100079 GLY C, 300093 ARG B, 100082 TYR C, 300028 SER B	7.37	132.14	-2.3	-0.3	22.13	83
    105	100093 ARG B, 100079 GLY C, 300093 ARG B, 100082 TYR C, 300079 GLY C	7.34	132.45	-2.22	-0.27	22.47	72
    106	200093 ARG B, 100093 ARG B, 100079 GLY C, 300093 ARG B, 100082 TYR C	7.14	132.98	-3.04	-0.19	32.2	74
    107	200079 GLY C, 300082 TYR C, 93 ARG B, 79 GLY C, 82 TYR C	5.81	135.56	-1.58	0.04	12.4	61
    108	93 ARG B, 79 GLY C, 82 TYR C, 58 GLN C	3.05	138.66	-2.43	-0.3	15.13	72
    109	93 ARG B, 79 GLY C, 58 GLN C, 80 ASP C	3	139.34	-2.2	-0.78	15.57	83
    110	300082 TYR C, 93 ARG B, 79 GLY C, 58 GLN C	3.2	140.4	-2.43	-0.3	15.13	72
    111	300082 TYR C, 93 ARG B, 58 GLN C, 80 ASP C	3.97	140.58	-2.43	-0.3	15.13	72
    112	300082 TYR C, 93 ARG B, 58 GLN C	3.75	141.54	-3.1	-0.14	19.05	72
    113	28 SER B, 300082 TYR C, 93 ARG B, 58 GLN C	3.55	142.19	-2.53	-0.35	14.7	83
    114	28 SER B, 93 ARG B, 58 GLN C	3.54	142.47	-2.93	-0.83	19.07	94
    115	28 SER B, 300082 TYR C, 93 ARG B, 58 GLN C	3.74	143.6	-2.53	-0.35	14.7	83
    116	28 SER B, 300093 ARG B, 300082 TYR C, 93 ARG B	4.04	143.97	-2.78	-0.18	26.82	83
    117	28 SER B, 300093 ARG B, 300082 TYR C	3.78	145.63	-2.2	-0.09	18.43	83
    118	28 SER B, 300093 ARG B	3.56	146.34	-2.65	-0.7	26.84	100
    119	28 SER B, 300027 GLN B, 300093 ARG B	2.69	151.21	-2.93	-0.83	19.07	94
    120	28 SER B, 300027 GLN B, 300028 SER B, 300093 ARG B	3.66	151.74	-2.3	-0.82	15.15	94
    121	28 SER B, 300027 GLN B, 300093 ARG B, 300028 SER B	4.04	152.21	-2.4	-0.87	14.72	100
    122	300027 GLN B, 300093 ARG B, 300028 SER B	4.73	152.54	-2.93	-0.83	19.07	94
    123	28 SER B, 300027 GLN B, 300093 ARG B, 300028 SER B	5.22	153.03	-2.4	-0.87	14.72	100
    124	28 SER B, 300027 GLN B, 300028 SER B	5.29	156.51	-1.7	-1.01	2.29	106
    125	100028 SER B, 300027 GLN B, 300028 SER B	5.99	156.8	-1.7	-1.01	2.29	106
    126	100028 SER B, 200027 GLN B, 100027 GLN B, 200028 SER B	6.15	157.71	-2.05	-0.99	3.03	95
    127	27 GLN B, 28 SER B, 300027 GLN B, 300028 SER B	5.64	158.84	-2.05	-0.99	3.03	95
    128	27 GLN B, 28 SER B, 300027 GLN B	5.33	159.48	-2.6	-1.06	2.91	95
    129	28 SER B, 300027 GLN B, 300026 SER B	5.02	160.09	-1.57	-0.96	2.86	100
    130	28 SER B, 300027 GLN B, 300026 SER B, 69 THR B	4.41	162.63	-1.35	-0.91	2.56	102
    131	28 SER B, 300027 GLN B, 300026 SER B, 27 GLN B	4.74	163.03	-1.28	-0.92	2.99	100
    132	300026 SER B, 69 THR B, 27 GLN B, 26 SER B, 28 SER B	4.57	165.91	-0.46	-0.79	3.04	107
    133	300026 SER B, 69 THR B, 27 GLN B, 26 SER B	4.62	166.79	-0.48	-0.79	2.95	107
    134	300026 SER B, 69 THR B, 26 SER B	4.7	168.89	-0.5	-0.79	2.81	107
    135	300026 SER B, 69 THR B, 26 SER B, 24 ARG B	4.76	169.7	-1.5	-0.7	15.11	95
    136	300026 SER B, 69 THR B, 24 ARG B	4.28	171.26	-1.87	-0.66	19.01	95
    137	300026 SER B, 69 THR B, 24 ARG B, 70 ASP B	3.84	172.9	-2.28	-0.76	26.69	92
    138	300026 SER B, 24 ARG B, 70 ASP B	3.73	173.65	-2.8	-0.75	35.03	84
    139	24 ARG B, 70 ASP B, 300026 SER B	3.23	175.76	-2.93	-0.81	34.46	95
    140	24 ARG B, 70 ASP B, 300026 SER B, 300003 LEU B	2.56	177.46	-1.25	-0.32	25.88	85
    141	70 ASP B, 300026 SER B, 300003 LEU B	2.06	180.28	-0.17	-0.29	17.17	85
    142	70 ASP B, 300003 LEU B	2.12	183.15	0.15	0.05	24.92	70
    143	70 ASP B, 300003 LEU B, 300001 ASP B	3.1	184.93	-0.03	-0.23	17.74	70
    144	70 ASP B, 300003 LEU B, 300001 ASP B, 72 THR B	3.93	185.06	-0.2	-0.37	13.72	82
    145	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B	3.99	185.92	-0.98	-0.43	25.3	83
    146	70 ASP B, 300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.97	186.12	-1.56	-0.42	30.14	81
    147	300003 LEU B, 72 THR B, 300001 ASP B, 300063 LYS A	3.68	187.7	-1.08	-0.27	25.25	79
    148	300003 LEU B, 300001 ASP B, 300063 LYS A	3.65	189.39	-1.2	-0.1	33.11	70
    149	300003 LEU B, 300001 ASP B, 300063 LYS A, 300097 THR B	3.73	190.7	-1.08	-0.27	25.25	79
    150	300003 LEU B, 300063 LYS A, 300097 THR B, 300002 ILE B	3.87	191.11	-0.3	-0.21	13.67	77
    151	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A	3.88	191.48	-1.08	-0.2	13.67	84
    152	300003 LEU B, 300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B	3.75	192.24	-0.94	-0.32	11.61	84
    153	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	3.71	192.43	-2.4	-0.78	21.56	90
    154	300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	3.7	192.81	-2.03	-0.87	14.58	96
    155	300063 LYS A, 300097 THR B, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.12	193.34	-2.4	-0.78	21.56	90
    156	300003 LEU B, 300063 LYS A, 300061 ASN A, 300098 PHE B, 300046 GLU A	4.45	194.19	-1.5	-0.4	21.26	76
    157	300003 LEU B, 300063 LYS A, 300098 PHE B, 300046 GLU A	4.84	195.23	-1	-0.3	25.73	67
    158	300003 LEU B, 300063 LYS A, 300046 GLU A, 300064 ILE A	5.24	198.56	0.23	0.35	24.92	76
    159	300003 LEU B, 300063 LYS A, 300046 GLU A, 20 SER B	5.79	199.37	-1.1	-0.35	25.3	80
    160	300063 LYS A, 300046 GLU A, 300064 ILE A, 20 SER B	5.4	200.08	-0.93	-0.18	25.3	92
    161	300063 LYS A, 300046 GLU A, 300064 ILE A	2.75	204.45	-0.97	0.09	33.18	84
    162	300046 GLU A, 300064 ILE A, 300063 LYS A	2.84	205.19	0.2	-0.04	17.8	90
    163	300046 GLU A, 300064 ILE A, 300063 LYS A, 18 ARG B	3.01	208.14	-0.98	-0.14	26.35	87
    164	300046 GLU A, 300064 ILE A, 18 ARG B, 300040 ARG A	3.52	211.61	-2	-0.04	38.51	86
    165	300046 GLU A, 18 ARG B, 300040 ARG A	4.24	214.12	-4.17	-0.66	51.3	81
    166	300046 GLU A, 300064 ILE A, 300040 ARG A	4.07	214.62	-1.17	0.08	34.01	87
    167	300046 GLU A, 300040 ARG A	3.37	217.88	-4	-0.78	50.95	80
    168	300040 ARG A	2.37	223.83	-4.5	-0.42	52	83
    169	300040 ARG A, 300088 SER A	2.21	224.71	-2.45	-0.61	27.69	83
    170	300040 ARG A, 300088 SER A, 300091 SER A	2.09	225.51	-1.77	-0.67	19.59	83
    171	300040 ARG A, 300088 SER A, 300041 PRO A, 300091 SER A	2.15	225.72	-1.83	-0.57	14.66	86
    172	300040 ARG A, 300088 SER A, 300091 SER A, 300041 PRO A	2.29	226.76	-1.73	-0.53	15.09	70
    173	300040 ARG A, 300088 SER A, 300041 PRO A	3	229.15	-2.17	-0.44	18.99	70
    174	300040 ARG A, 300041 PRO A, 300088 SER A	4.3	231.13	-2.3	-0.49	18.42	86
    175	300041 PRO A, 300088 SER A	4.98	232.4	-1.2	-0.53	1.63	87
    176	300041 PRO A, 300091 SER A, 300088 SER A	4.66	233.27	-1.07	-0.68	1.64	97
    177	300041 PRO A, 300091 SER A, 300088 SER A, 300175 LEU A	4.52	233.61	0.15	-0.22	1.26	86
    178	300041 PRO A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.43	233.88	0.02	0.3	1.25	69
    179	300091 SER A, 300088 SER A, 300175 LEU A, 300180 TYR A	4.33	234.25	0.23	0.08	1.27	84
    180	300091 SER A, 300088 SER A, 300180 TYR A	4.33	234.43	-0.97	-0.28	1.65	94
    181	300091 SER A, 300088 SER A	4.35	234.64	-0.8	-0.97	1.67	117
    182	300091 SER A, 300088 SER A, 300180 TYR A	4.38	235.08	-0.97	-0.28	1.65	94
    183	300088 SER A, 300041 PRO A, 300091 SER A, 300175 LEU A, 300180 TYR A	4.4	235.76	-0.06	0.08	1.67	69
    184	300041 PRO A, 300091 SER A, 300175 LEU A, 300180 TYR A	4.43	236.6	0.02	0.3	1.25	69
    185	300041 PRO A, 300175 LEU A, 300180 TYR A	4.44	240.39	0.3	0.72	1.11	54
    186	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.38	240.65	0.13	0.34	1.68	54
    187	300041 PRO A, 300175 LEU A, 300180 TYR A	4.36	241.29	0.3	0.72	1.11	54
    188	300041 PRO A, 300175 LEU A, 300180 TYR A, 300173 ALA A	4.1	242.05	0.13	0.34	1.68	54
    189	300041 PRO A, 300180 TYR A, 300173 ALA A	3.49	244.18	-1.1	0.07	2.19	54
    190	300041 PRO A, 300180 TYR A, 300173 ALA A, 300153 GLU A	3.33	246.3	-1.7	-0.23	14.12	61
    191	300041 PRO A, 300173 ALA A, 300153 GLU A, 300172 PRO A	3.41	248.31	-1.78	-0.53	14.11	64
    192	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.6	249.1	-2.55	-0.52	14.11	74
    193	300041 PRO A, 300153 GLU A, 300172 PRO A, 300041 ASN B	3.34	249.71	-2.55	-0.52	14.11	74
    194	300153 GLU A, 300172 PRO A, 300041 ASN B	3.15	250.09	-2.87	-0.67	18.29	79
    195	300173 ALA A, 300153 GLU A, 300172 PRO A, 300041 ASN B	2.25	253.33	-2.25	-0.7	14.56	79
    196	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A	2.26	254.24	-1.95	-0.88	15.01	90
    197	300173 ALA A, 300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A	2.36	254.52	-0.8	-0.47	12.03	78
    198	300153 GLU A, 300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.44	254.74	-0.8	-0.47	12.03	78
    199	300041 ASN B, 300172 PRO A, 300182 LEU A, 300171 PHE A	2.6	255.64	-0.13	-0.31	2.57	79
    200	300041 ASN B, 300182 LEU A, 300171 PHE A	2.76	255.82	-0.03	-0.14	2.3	79
    201	300041 ASN B, 300182 LEU A, 300170 THR A	2.78	256.11	-0.13	-0.13	1.72	88
    202	300041 ASN B, 300182 LEU A, 300170 THR A, 300155 VAL A	2.72	257.79	-0.2	-0.3	2.14	88
    203	300041 ASN B, 300170 THR A, 300155 VAL A	2.78	261.24	-1.53	-0.78	2.81	105
    204	300041 ASN B, 300170 THR A, 300155 VAL A, 300156 THR A, 300157 VAL A	3.1	261.49	-1.14	-0.78	2.69	106
    205	300041 ASN B, 300156 THR A, 300157 VAL A	3.15	261.74	-1.53	-0.78	2.81	105
    206	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.19	262.03	-1.33	-0.78	2.52	106
    207	300041 ASN B, 300170 THR A, 300155 VAL A	3.17	262.33	-1.53	-0.78	2.81	105
    208	300041 ASN B, 300170 THR A, 300157 VAL A	3.24	262.49	-1.53	-0.78	2.81	105
    209	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.18	262.91	-1.33	-0.78	2.52	106
    210	300170 THR A, 300156 THR A, 300157 VAL A	3.23	263.1	-0.6	-0.78	2.23	107
    211	300041 ASN B, 300170 THR A, 300156 THR A, 300157 VAL A	3.29	263.41	-1.33	-0.78	2.52	106
    212	300041 ASN B, 300156 THR A, 300157 VAL A	3.38	266.24	-1.53	-0.78	2.81	105
    213	300041 ASN B, 300156 THR A, 300157 VAL A, 300040 THR B	4.05	266.24	-1.25	-0.79	2.95	105

    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, 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

27. 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

28. 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

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, 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, 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, 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, 207 LYS B, 115 VAL B, 136 GLN A, 116 SER B, 140 MET A, 135 ALA A, 117 ILE B, 116 SER B, 117 ILE B, 208 SER B, 132 GLY A, 209 PHE B, 119 PRO B, 210 ASN B, 133 SER A, 218 ARG A, 211 ARG B, 186 TYR B, 211 ARG B, 125 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, 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, 207 LYS B, 116 SER B, 135 ALA A, 117 ILE B, 209 PHE B, 119 PRO B, 218 ARG A, 186 TYR B, 211 ARG B, 125 LEU B

    Physicochemical properties of lining side-chains

    Charge: 6 (16-10)
    Hydropathy: -1.3
    Hydrophobicity: -0.41
    Polarity: 13.87
    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	3.27	0.43	-1.53	-0.78	2.81	105
    3	100170 THR A, 100041 ASN B, 100155 VAL A	3.25	0.64	-1.53	-0.78	2.81	105
    4	100157 VAL A, 100170 THR A, 100041 ASN B	3.23	0.82	-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	3.05	1.56	-1.53	-0.78	2.81	105
    7	100157 VAL A, 100170 THR A, 100041 ASN B, 100155 VAL A	2.98	2.26	-1.25	-0.79	2.95	105
    8	100170 THR A, 100041 ASN B, 100155 VAL A	2.71	5.67	-1.53	-0.78	2.81	105
    9	100170 THR A, 100041 ASN B, 100155 VAL A, 100182 LEU A	2.63	6.65	-0.2	-0.3	2.14	88
    10	100170 THR A, 100041 ASN B, 100182 LEU A	2.71	7.07	-0.13	-0.13	1.72	88
    11	100041 ASN B, 100182 LEU A, 100171 PHE A	2.74	7.26	-0.03	-0.14	2.3	79
    12	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A	2.6	8.03	-0.13	-0.31	2.57	79
    13	100041 ASN B, 100182 LEU A, 100171 PHE A, 100172 PRO A, 100153 GLU A	2.6	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	2.61	8.8	-0.8	-0.47	12.03	78
    15	100041 ASN B, 100172 PRO A, 100153 GLU A, 100173 ALA A	2.63	10.14	-1.95	-0.88	15.01	90
    16	100041 ASN B, 100153 GLU A, 100173 ALA A, 100172 PRO A	2.7	12.67	-2.25	-0.7	14.56	79
    17	100041 ASN B, 100153 GLU A, 100172 PRO A	2.91	13.46	-2.87	-0.67	18.29	79
    18	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.04	13.76	-2.55	-0.52	14.11	74
    19	100041 ASN B, 100153 GLU A, 100172 PRO A, 100041 PRO A	3.12	14.44	-2.55	-0.52	14.11	74
    20	100153 GLU A, 100172 PRO A, 100041 PRO A	3.27	14.82	-2.23	-0.44	17.69	64
    21	100153 GLU A, 100173 ALA A, 100172 PRO A, 100041 PRO A	3.34	17.02	-1.78	-0.53	14.11	64
    22	100153 GLU A, 100173 ALA A, 100041 PRO A, 100180 TYR A	3.72	18.63	-1.7	-0.23	14.12	61
    23	100173 ALA A, 100041 PRO A, 100180 TYR A	3.93	20.99	-1.1	0.07	2.19	54
    24	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.16	21.44	0.13	0.34	1.68	54
    25	100041 PRO A, 100180 TYR A, 100175 LEU A	4.32	22.04	0.3	0.72	1.11	54
    26	100173 ALA A, 100041 PRO A, 100180 TYR A, 100175 LEU A	4.32	22.47	0.13	0.34	1.68	54
    27	100041 PRO A, 100180 TYR A, 100175 LEU A	4.19	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	4.17	27.8	-0.06	0.08	1.67	69
    29	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.18	28.14	0.23	0.08	1.27	84
    30	100091 SER A, 100088 SER A	4.2	28.24	-0.8	-0.97	1.67	117
    31	100180 TYR A, 100091 SER A, 100088 SER A	4.25	28.6	-0.97	-0.28	1.65	94
    32	100180 TYR A, 100175 LEU A, 100091 SER A, 100088 SER A	4.44	28.88	0.23	0.08	1.27	84
    33	100041 PRO A, 100180 TYR A, 100175 LEU A, 100088 SER A	4.59	29.27	0.02	0.3	1.25	69
    34	100041 PRO A, 100175 LEU A, 100091 SER A, 100088 SER A	4.77	29.77	0.15	-0.22	1.26	86
    35	100041 PRO A, 100091 SER A, 100088 SER A	4.96	30.88	-1.07	-0.68	1.64	97
    36	100041 PRO A, 100088 SER A	5.29	31.77	-1.2	-0.53	1.63	87
    37	100041 PRO A, 100088 SER A, 100040 ARG A	4.39	34.23	-2.3	-0.49	18.42	86
    38	100041 PRO A, 100088 SER A, 100040 ARG A	2.88	36.66	-2.17	-0.44	18.99	70
    39	100041 PRO A, 100088 SER A, 100040 ARG A, 100091 SER A	2.62	37.02	-1.73	-0.53	15.09	70
    40	100088 SER A, 100040 ARG A, 100091 SER A	2.37	38.62	-1.77	-0.67	19.59	83
    41	100088 SER A, 100040 ARG A	2.43	40.01	-2.45	-0.61	27.69	83
    42	100040 ARG A	2.54	45.13	-4.5	-0.42	52	83
    43	100040 ARG A, 100043 HIS A	3.01	46.46	-3.85	-0.08	51.8	87
    44	100040 ARG A, 100046 GLU A	3.16	50.3	-4	-0.78	50.95	80
    45	100040 ARG A, 100046 GLU A, 300018 ARG B	3.52	52.76	-4.17	-0.66	51.3	81
    46	100040 ARG A, 100046 GLU A, 300018 ARG B, 100064 ILE A	3.62	56.24	-2	-0.04	38.51	86
    47	100046 GLU A, 300018 ARG B, 100064 ILE A	3.61	56.92	-1.17	0.08	34.01	87
    48	100046 GLU A, 300018 ARG B, 100064 ILE A, 100063 LYS A	3.55	60.14	-0.98	-0.14	26.35	87
    49	100046 GLU A, 100064 ILE A, 100063 LYS A	3.54	64.66	-0.97	0.09	33.18	84
    50	100046 GLU A, 100064 ILE A, 100063 LYS A, 300020 SER B	3.84	65.24	-0.93	-0.18	25.3	92
    51	100046 GLU A, 100063 LYS A, 300020 SER B, 100003 LEU B	3.93	66.39	-1.1	-0.35	25.3	80
    52	100046 GLU A, 100064 ILE A, 100063 LYS A, 100003 LEU B	4.1	70.13	0.23	0.35	24.92	76
    53	100046 GLU A, 100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B	4.21	70.97	-1.5	-0.4	21.26	76
    54	100046 GLU A, 100063 LYS A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.19	71.34	-2.4	-0.78	21.56	90
    55	100046 GLU A, 100061 ASN A, 100098 PHE B, 100097 THR B	4.05	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	3.95	71.79	-2.4	-0.78	21.56	90
    57	100063 LYS A, 100003 LEU B, 100061 ASN A, 100098 PHE B, 100097 THR B	3.67	72.88	-0.94	-0.32	11.61	84
    58	100063 LYS A, 100003 LEU B, 100061 ASN A, 100097 THR B	3.61	73.38	-1.08	-0.2	13.67	84
    59	100063 LYS A, 100003 LEU B, 100097 THR B, 100001 ASP B	3.58	75.07	-1.08	-0.27	25.25	79
    60	100063 LYS A, 100003 LEU B, 100001 ASP B	3.67	77.08	-1.2	-0.1	33.11	70
    61	100063 LYS A, 100003 LEU B, 100001 ASP B, 300072 THR B	3.89	78.06	-1.08	-0.27	25.25	79
    62	100003 LEU B, 100001 ASP B, 300072 THR B, 300070 ASP B	4.01	79.03	-0.98	-0.43	25.3	83
    63	100003 LEU B, 300072 THR B, 300070 ASP B, 100001 ASP B	4	79.22	-0.2	-0.37	13.72	82
    64	100003 LEU B, 300070 ASP B, 100001 ASP B	2.9	81.11	-0.03	-0.23	17.74	70
    65	100003 LEU B, 300070 ASP B	2.14	84.09	0.15	0.05	24.92	70
    66	100003 LEU B, 300070 ASP B, 100026 SER B	2.14	86.92	-0.17	-0.29	17.17	85
    67	100003 LEU B, 300070 ASP B, 100026 SER B, 300024 ARG B	2.74	88.92	-1.25	-0.32	25.88	85
    68	300070 ASP B, 100026 SER B, 300024 ARG B	3.3	90.31	-2.93	-0.81	34.46	95
    69	300070 ASP B, 300024 ARG B, 100026 SER B	3.62	91.45	-2.8	-0.75	35.03	84
    70	300070 ASP B, 300024 ARG B, 100026 SER B, 300069 THR B	4.34	93.28	-2.28	-0.76	26.69	92
    71	300024 ARG B, 100026 SER B, 300069 THR B	4.62	94.42	-1.87	-0.66	19.01	95
    72	300024 ARG B, 100026 SER B, 300069 THR B, 300026 SER B	4.5	95.53	-1.5	-0.7	15.11	95
    73	100026 SER B, 300069 THR B, 300026 SER B	4.31	98.26	-0.5	-0.79	2.81	107
    74	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B	4.26	99.33	-0.48	-0.79	2.95	107
    75	100026 SER B, 300069 THR B, 300026 SER B, 300027 GLN B, 300028 SER B	4.22	101.17	-0.46	-0.79	3.04	107
    76	100026 SER B, 300027 GLN B, 100027 GLN B, 300028 SER B	4.25	101.54	-1.28	-0.92	2.99	100
    77	100026 SER B, 300069 THR B, 100027 GLN B, 300028 SER B	4.39	104.75	-1.35	-0.91	2.56	102
    78	300027 GLN B, 100027 GLN B, 300028 SER B	6	105.52	-1.57	-0.96	2.86	100
    79	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	6.11	106.61	-2.05	-0.99	3.03	95
    80	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.88	107.39	-2.05	-0.99	3.03	95
    81	100027 GLN B, 300028 SER B, 200028 SER B, 100028 SER B	5.75	107.95	-1.48	-1	2.14	108
    82	100027 GLN B, 300028 SER B, 100028 SER B	5.07	111.25	-1.7	-1.01	2.29	106
    83	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.97	111.4	-2.4	-0.87	14.72	100
    84	100027 GLN B, 100028 SER B, 100093 ARG B	4.67	111.85	-2.93	-0.83	19.07	94
    85	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.55	112.3	-2.4	-0.87	14.72	100
    86	100027 GLN B, 300028 SER B, 100028 SER B, 100093 ARG B	4.43	113.01	-2.3	-0.82	15.15	94
    87	100027 GLN B, 300028 SER B, 100093 ARG B	3.61	118.46	-2.93	-0.83	19.07	94
    88	300028 SER B, 100093 ARG B, 100082 TYR C	3.65	120.36	-2.2	-0.09	18.43	83
    89	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B	4.25	122.88	-2.78	-0.18	26.82	83
    90	300028 SER B, 100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C	5.99	123.83	-2.3	-0.3	22.13	83
    91	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 100079 GLY C	6.45	124.55	-2.22	-0.27	22.47	72
    92	93 ARG B, 79 GLY C, 82 TYR C, 200079 GLY C, 300082 TYR C	6.58	124.81	-1.58	0.04	12.4	61
    93	93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C, 200093 ARG B	6.27	125.36	-2.4	0.12	22.12	66
    94	300093 ARG B, 93 ARG B, 79 GLY C, 82 TYR C, 300082 TYR C	6.06	126.05	-2.4	0.12	22.12	66
    95	100093 ARG B, 100082 TYR C, 300079 GLY C, 100079 GLY C, 200082 TYR C	5.54	128.13	-1.58	0.04	12.4	61
    96	100093 ARG B, 100082 TYR C, 100079 GLY C, 100058 GLN C	4.38	131.33	-2.43	-0.3	15.13	72
    97	100093 ARG B, 100079 GLY C, 100058 GLN C	4.17	131.7	-2.8	-0.77	19.64	83
    98	100093 ARG B, 100079 GLY C, 100058 GLN C, 100080 ASP C	3.95	132.74	-2.2	-0.78	15.57	83
    99	100093 ARG B, 100079 GLY C, 200082 TYR C, 100058 GLN C	3.97	134.53	-2.43	-0.3	15.13	72
    100	100093 ARG B, 100082 TYR C, 100079 GLY C, 200082 TYR C, 100058 GLN C	4.38	135.59	-2.2	-0.02	12.43	66
    101	100093 ARG B, 100082 TYR C, 100079 GLY C, 200093 ARG B, 200082 TYR C	4.73	137.46	-2.4	0.12	22.12	66
    102	100093 ARG B, 100079 GLY C, 200079 GLY C, 200093 ARG B, 200082 TYR C	5.53	138.06	-2.22	-0.27	22.47	72
    103	300093 ARG B, 300079 GLY C, 93 ARG B, 79 GLY C, 300082 TYR C	5.92	138.53	-2.22	-0.27	22.47	72
    104	300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C, 28 SER B	6.49	138.72	-2.3	-0.3	22.13	83
    105	100082 TYR C, 300093 ARG B, 300079 GLY C, 93 ARG B, 300082 TYR C	6.59	139.19	-2.4	0.12	22.12	66
    106	100093 ARG B, 100082 TYR C, 300093 ARG B, 300079 GLY C, 300082 TYR C	6.53	139.99	-2.4	0.12	22.12	66
    107	100079 GLY C, 82 TYR C, 200079 GLY C, 200093 ARG B, 200082 TYR C	5.97	142.19	-1.58	0.04	12.4	61
    108	200079 GLY C, 200093 ARG B, 200082 TYR C, 200058 GLN C	3.66	145.24	-2.43	-0.3	15.13	72
    109	200079 GLY C, 200093 ARG B, 200058 GLN C, 200080 ASP C	3.11	146.03	-2.2	-0.78	15.57	83
    110	82 TYR C, 200079 GLY C, 200093 ARG B, 200058 GLN C	2.96	147.04	-2.43	-0.3	15.13	72
    111	82 TYR C, 200093 ARG B, 200058 GLN C	3.37	148.19	-3.1	-0.14	19.05	72
    112	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.88	148.72	-2.53	-0.35	14.7	83
    113	200028 SER B, 200093 ARG B, 200058 GLN C	3.86	148.96	-2.93	-0.83	19.07	94
    114	200028 SER B, 82 TYR C, 200093 ARG B, 200058 GLN C	3.17	150.38	-2.53	-0.35	14.7	83
    115	200028 SER B, 93 ARG B, 82 TYR C, 200093 ARG B	2.96	150.9	-2.78	-0.18	26.82	83
    116	200028 SER B, 93 ARG B, 82 TYR C	2.6	152.41	-2.2	-0.09	18.43	83
    117	200028 SER B, 93 ARG B	2.49	153.27	-2.65	-0.7	26.84	100
    118	27 GLN B, 200028 SER B, 93 ARG B	2.45	157.65	-2.93	-0.83	19.07	94
    119	27 GLN B, 28 SER B, 200028 SER B, 93 ARG B	3.68	158.29	-2.3	-0.82	15.15	94
    120	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	4.04	158.62	-2.4	-0.87	14.72	100
    121	27 GLN B, 93 ARG B, 28 SER B	4.42	159.03	-2.93	-0.83	19.07	94
    122	27 GLN B, 200028 SER B, 93 ARG B, 28 SER B	5.5	159.71	-2.4	-0.87	14.72	100
    123	27 GLN B, 200028 SER B, 28 SER B	6.08	163.16	-1.7	-1.01	2.29	106
    124	100027 GLN B, 300028 SER B, 100028 SER B, 300027 GLN B	5.66	164.48	-2.05	-0.99	3.03	95
    125	27 GLN B, 28 SER B, 200027 GLN B, 200028 SER B	5.38	165.2	-2.05	-0.99	3.03	95
    126	27 GLN B, 200027 GLN B, 200028 SER B	5.11	165.97	-2.6	-1.06	2.91	95
    127	27 GLN B, 200028 SER B, 26 SER B	4.87	166.7	-1.57	-0.96	2.86	100
    128	27 GLN B, 200028 SER B, 26 SER B, 200069 THR B	4.52	169.13	-1.35	-0.91	2.56	102
    129	27 GLN B, 200028 SER B, 26 SER B, 200027 GLN B	5.12	169.32	-1.28	-0.92	2.99	100
    130	200028 SER B, 26 SER B, 200069 THR B, 200027 GLN B	5.2	169.76	-0.58	-0.84	2.52	112
    131	26 SER B, 200069 THR B, 200027 GLN B, 200026 SER B, 200028 SER B	5.25	172.62	-0.46	-0.79	3.04	107
    132	26 SER B, 200069 THR B, 200026 SER B	5	175.39	-0.5	-0.79	2.81	107
    133	26 SER B, 200069 THR B, 200026 SER B, 200024 ARG B	4.42	176.17	-1.5	-0.7	15.11	95
    134	26 SER B, 200069 THR B, 200024 ARG B	4	178.08	-1.87	-0.66	19.01	95
    135	26 SER B, 200069 THR B, 200024 ARG B, 200070 ASP B	3.8	179.43	-2.28	-0.76	26.69	92
    136	26 SER B, 200024 ARG B, 200070 ASP B	3.81	180.1	-2.8	-0.75	35.03	84
    137	200024 ARG B, 200070 ASP B, 26 SER B	3.1	182.18	-2.93	-0.81	34.46	95
    138	200024 ARG B, 200070 ASP B, 26 SER B, 3 LEU B	2.43	184.29	-1.25	-0.32	25.88	85
    139	200070 ASP B, 26 SER B, 3 LEU B	2.3	186.56	-0.17	-0.29	17.17	85
    140	200070 ASP B, 3 LEU B	2.39	189.5	0.15	0.05	24.92	70
    141	200070 ASP B, 3 LEU B, 1 ASP B	2.88	191.43	-0.03	-0.23	17.74	70
    142	200070 ASP B, 3 LEU B, 1 ASP B, 200072 THR B	3.93	191.57	-0.2	-0.37	13.72	82
    143	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B	3.95	192.42	-0.98	-0.43	25.3	83
    144	200070 ASP B, 3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.91	192.68	-1.56	-0.42	30.14	81
    145	3 LEU B, 200072 THR B, 1 ASP B, 63 LYS A	3.8	194.21	-1.08	-0.27	25.25	79
    146	3 LEU B, 1 ASP B, 63 LYS A	3.75	195.61	-1.2	-0.1	33.11	70
    147	3 LEU B, 1 ASP B, 63 LYS A, 97 THR B	3.75	197.23	-1.08	-0.27	25.25	79
    148	3 LEU B, 63 LYS A, 97 THR B, 2 ILE B	3.85	197.71	-0.3	-0.21	13.67	77
    149	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B	3.93	198.13	-0.3	-0.21	13.67	77
    150	3 LEU B, 63 LYS A, 97 THR B, 98 PHE B, 61 ASN A	4.05	198.7	-0.94	-0.32	11.61	84
    151	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.37	198.92	-2.4	-0.78	21.56	90
    152	97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.58	199.18	-2.03	-0.87	14.58	96
    153	63 LYS A, 97 THR B, 98 PHE B, 61 ASN A, 46 GLU A	4.98	199.76	-2.4	-0.78	21.56	90
    154	3 LEU B, 63 LYS A, 98 PHE B, 61 ASN A, 46 GLU A	5.15	200.8	-1.5	-0.4	21.26	76
    155	3 LEU B, 63 LYS A, 98 PHE B, 46 GLU A	5.27	202.09	-1	-0.3	25.73	67
    156	3 LEU B, 63 LYS A, 46 GLU A, 64 ILE A	5.23	205.02	0.23	0.35	24.92	76
    157	3 LEU B, 63 LYS A, 46 GLU A, 200020 SER B	5.05	205.4	-1.1	-0.35	25.3	80
    158	63 LYS A, 46 GLU A, 64 ILE A, 200020 SER B	4.79	206.13	-0.93	-0.18	25.3	92
    159	63 LYS A, 46 GLU A, 64 ILE A	2.96	210.7	-0.97	0.09	33.18	84
    160	46 GLU A, 64 ILE A, 63 LYS A	2.8	211.61	0.2	-0.04	17.8	90
    161	46 GLU A, 64 ILE A, 63 LYS A, 200018 ARG B	2.7	214.49	-0.98	-0.14	26.35	87
    162	46 GLU A, 64 ILE A, 200018 ARG B, 40 ARG A	3	217.92	-2	-0.04	38.51	86
    163	46 GLU A, 200018 ARG B, 40 ARG A	3.1	220.57	-4.17	-0.66	51.3	81
    164	46 GLU A, 64 ILE A, 40 ARG A	2.42	221.23	-1.17	0.08	34.01	87
    165	46 GLU A, 40 ARG A	1.11	223.89	-4	-0.78	50.95	80
    166	40 ARG A	-0.01	230.82	-4.5	-0.42	52	83
    167	40 ARG A, 88 SER A	0.2	231.57	-2.45	-0.61	27.69	83
    168	40 ARG A, 88 SER A, 91 SER A	0.55	231.93	-1.77	-0.67	19.59	83
    169	40 ARG A, 88 SER A, 41 PRO A, 91 SER A	1.01	232.2	-1.83	-0.57	14.66	86
    170	40 ARG A, 88 SER A, 91 SER A, 41 PRO A	1.55	233.02	-1.73	-0.53	15.09	70
    171	40 ARG A, 88 SER A, 41 PRO A	2.69	235.86	-2.17	-0.44	18.99	70
    172	40 ARG A, 41 PRO A, 88 SER A	4.4	237.41	-2.3	-0.49	18.42	86
    173	41 PRO A, 88 SER A	4.92	238.93	-1.2	-0.53	1.63	87
    174	41 PRO A, 91 SER A, 88 SER A	4.82	239.47	-1.07	-0.68	1.64	97
    175	41 PRO A, 91 SER A, 88 SER A, 175 LEU A	4.71	239.93	0.15	-0.22	1.26	86
    176	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.58	240.27	0.02	0.3	1.25	69
    177	91 SER A, 88 SER A, 175 LEU A, 180 TYR A	4.34	240.71	0.23	0.08	1.27	84
    178	91 SER A, 88 SER A, 180 TYR A	4.23	240.8	-0.97	-0.28	1.65	94
    179	91 SER A, 88 SER A	4.15	240.98	-0.8	-0.97	1.67	117
    180	91 SER A, 88 SER A, 180 TYR A	4.1	241.48	-0.97	-0.28	1.65	94
    181	41 PRO A, 88 SER A, 175 LEU A, 180 TYR A	4.08	242.33	0.02	0.3	1.25	69
    182	41 PRO A, 91 SER A, 175 LEU A, 180 TYR A	4.09	243.39	0.02	0.3	1.25	69
    183	41 PRO A, 175 LEU A, 180 TYR A	4.13	246.68	0.3	0.72	1.11	54
    184	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	4.39	247.05	0.13	0.34	1.68	54
    185	41 PRO A, 175 LEU A, 180 TYR A	4.43	247.75	0.3	0.72	1.11	54
    186	41 PRO A, 175 LEU A, 180 TYR A, 173 ALA A	3.87	248.71	0.13	0.34	1.68	54
    187	41 PRO A, 180 TYR A, 173 ALA A	3.49	250.68	-1.1	0.07	2.19	54
    188	41 PRO A, 180 TYR A, 173 ALA A, 153 GLU A	3.36	252.72	-1.7	-0.23	14.12	61
    189	41 PRO A, 173 ALA A, 153 GLU A, 172 PRO A	3.4	254.75	-1.78	-0.53	14.11	64
    190	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	3.27	255.4	-2.55	-0.52	14.11	74
    191	41 PRO A, 153 GLU A, 172 PRO A, 41 ASN B	2.99	256.1	-2.55	-0.52	14.11	74
    192	153 GLU A, 172 PRO A, 41 ASN B	2.83	256.58	-2.87	-0.67	18.29	79
    193	173 ALA A, 153 GLU A, 172 PRO A, 41 ASN B	2.26	259.89	-2.25	-0.7	14.56	79
    194	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A	2.25	260.46	-1.95	-0.88	15.01	90
    195	173 ALA A, 153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A	2.27	260.86	-0.8	-0.47	12.03	78
    196	153 GLU A, 41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.33	261.15	-0.8	-0.47	12.03	78
    197	41 ASN B, 172 PRO A, 182 LEU A, 171 PHE A	2.48	262.05	-0.13	-0.31	2.57	79
    198	41 ASN B, 182 LEU A, 171 PHE A	2.87	262.27	-0.03	-0.14	2.3	79
    199	41 ASN B, 182 LEU A, 170 THR A	2.81	262.56	-0.13	-0.13	1.72	88
    200	41 ASN B, 182 LEU A, 170 THR A, 155 VAL A	2.5	264.37	-0.2	-0.3	2.14	88
    201	41 ASN B, 170 THR A, 155 VAL A	2.5	267.67	-1.53	-0.78	2.81	105
    202	41 ASN B, 170 THR A, 155 VAL A, 156 THR A, 157 VAL A	2.69	267.92	-1.14	-0.78	2.69	106
    203	41 ASN B, 156 THR A, 157 VAL A	2.78	268.06	-1.53	-0.78	2.81	105
    204	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	2.97	268.4	-1.33	-0.78	2.52	106
    205	41 ASN B, 170 THR A, 155 VAL A	3.15	268.58	-1.53	-0.78	2.81	105
    206	41 ASN B, 170 THR A, 157 VAL A	3.34	268.81	-1.53	-0.78	2.81	105
    207	41 ASN B, 170 THR A, 156 THR A, 157 VAL A	3.14	269.19	-1.33	-0.78	2.52	106
    208	41 ASN B, 170 THR A, 157 VAL A	3.16	272.3	-1.53	-0.78	2.81	105
    209	41 ASN B, 170 THR A, 157 VAL A, 40 THR B	4.21	273.16	-1.25	-0.79	2.95	105
    210	41 ASN B, 170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.55	273.31	-1.08	-0.79	3.04	105
    211	170 THR A, 157 VAL A, 40 THR B, 168 VAL A	4.61	273.46	0.68	-0.31	2.14	102
    212	170 THR A, 157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.58	273.6	-1.16	-0.72	12.26	89
    213	157 VAL A, 40 THR B, 168 VAL A, 169 LYS B	4.59	273.65	-0.13	-0.22	14.1	85
    214	170 THR A, 157 VAL A, 168 VAL A, 169 LYS B	4.38	274.45	-0.2	-0.21	13.67	92
    215	157 VAL A, 168 VAL A, 169 LYS B, 165 SER A	4.21	274.89	-0.13	-0.22	14.1	85
    216	168 VAL A, 169 LYS B, 165 SER A	3.01	278.94	-0.03	-0.03	17.67	85
    217	168 VAL A, 169 LYS B, 165 SER A	1.72	281.05	-1.57	-0.67	18.75	72
    218	168 VAL A, 169 LYS B, 165 SER A, 167 GLY A	1.35	282.39	-1.28	-0.7	14.91	72
    219	168 VAL A, 169 LYS B, 167 GLY A	1.5	283.29	-1.57	-0.67	18.75	72
    220	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.73	283.54	-1.98	-0.44	26.97	81
    221	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	1.84	283.77	-1.98	-0.44	26.97	81
    222	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	2.08	283.83	-1.98	-0.44	26.97	81
    223	168 VAL A, 169 LYS B, 167 GLY A, 169 HIS A	2.06	284.3	-1.98	-0.44	26.97	81
    224	169 LYS B, 167 GLY A, 169 HIS A, 167 ASP B	1.97	284.99	-2.75	-0.5	38.55	83
    225	169 LYS B, 167 GLY A, 167 ASP B	1.85	286.43	-2.6	-0.75	34.19	79
    226	169 LYS B, 167 GLY A	1.79	287.2	-2.15	-0.61	26.44	72
    227	169 LYS B, 167 GLY A, 166 SER A	1.7	288.5	-1.57	-0.67	18.75	72
    228	169 LYS B, 167 GLY A, 166 SER A	1.72	291.99	-1.7	-0.73	18.18	94
    229	169 LYS B, 167 GLY A, 166 SER A, 170 ASP B	3.26	293.36	-2.15	-0.81	26.06	91
    230	167 GLY A, 166 SER A, 170 ASP B, 169 LYS B	4.76	293.85	-1.28	-0.9	14.53	101
    231	167 GLY A, 166 SER A, 170 ASP B	4.88	294.75	-1.57	-0.94	18.25	101
    232	167 GLY A, 166 SER A, 170 ASP B, 140 MET A	4.88	295.81	-0.7	-0.45	14.05	98
    233	167 GLY A, 170 ASP B, 140 MET A	4.48	297.52	-0.67	-0.28	18.17	89
    234	167 GLY A, 170 ASP B, 140 MET A, 138 ASN B	4.19	298.81	-1.38	-0.4	14.47	94
    235	170 ASP B, 140 MET A, 138 ASN B	3.87	300.2	-1.7	-0.27	18.17	94
    236	140 MET A, 138 ASN B, 187 THR A	3.47	301.99	-0.77	-0.18	2.16	101
    237	140 MET A, 138 ASN B, 187 THR A, 114 THR B	2.96	303.55	-0.75	-0.33	2.03	102
    238	140 MET A, 187 THR A, 114 THR B	2.65	305.3	0.17	-0.18	1.58	102
    239	140 MET A, 114 THR B	2.47	306.84	0.6	0.12	1.55	100
    240	140 MET A, 114 THR B, 138 ASN A	2.4	307.32	-0.77	-0.18	2.16	101
    241	140 MET A, 114 THR B, 138 ASN A, 139 SER A	2.33	308.31	-0.78	-0.38	2.04	105
    242	140 MET A, 114 THR B, 138 ASN A	2.37	311.11	-0.77	-0.18	2.16	101
    243	114 THR B, 138 ASN A	2.85	314.54	-2.1	-0.77	2.52	105
    244	114 THR B, 138 ASN A, 207 LYS B	3.27	316.82	-2.7	-0.65	18.18	94
    245	114 THR B, 138 ASN A, 207 LYS B, 115 VAL B	3.44	317.92	-2.13	-0.69	14.48	94
    246	114 THR B, 138 ASN A, 207 LYS B, 136 GLN A	3.4	318.87	-2.13	-0.69	14.48	94
    247	114 THR B, 138 ASN A, 207 LYS B, 115 VAL B, 136 GLN A	2.99	320	-1.78	-0.71	12.26	94
    248	114 THR B, 207 LYS B, 115 VAL B, 136 GLN A	2.68	320.45	-1.35	-0.7	14.48	89
    249	114 THR B, 138 ASN A, 207 LYS B, 115 VAL B, 136 GLN A	2.63	320.76	-1.78	-0.71	12.26	94
    250	114 THR B, 207 LYS B, 115 VAL B, 136 GLN A, 116 SER B	2.59	321.12	-1.24	-0.75	11.92	98
    251	114 THR B, 115 VAL B, 136 GLN A, 116 SER B, 140 MET A	2.57	322.66	-0.54	-0.83	2.69	112
    252	207 LYS B, 115 VAL B, 136 GLN A, 116 SER B	2.59	323.35	-1.38	-0.75	14.48	94
    253	115 VAL B, 136 GLN A, 116 SER B	2.59	324.56	-0.53	-0.86	2.81	117
    254	115 VAL B, 136 GLN A, 116 SER B, 135 ALA A	2.54	325.27	0.05	-0.64	2.11	108
    255	115 VAL B, 116 SER B, 135 ALA A	2.26	326.48	0.2	-0.58	1.68	108
    256	116 SER B, 135 ALA A, 117 ILE B	1.98	328.95	0.2	-0.58	1.68	108
    257	135 ALA A, 117 ILE B, 116 SER B	1.94	329.45	0.33	-0.53	2.25	100
    258	135 ALA A, 116 SER B, 117 ILE B	1.91	329.95	1.97	0.34	1.17	101
    259	135 ALA A, 117 ILE B	1.87	331.64	3.15	0.92	0.07	101
    260	135 ALA A, 117 ILE B, 208 SER B	1.87	332.2	1.97	0.34	1.17	101
    261	135 ALA A, 117 ILE B, 208 SER B, 132 GLY A	1.87	332.68	1.38	0.06	1.72	101
    262	135 ALA A, 117 ILE B, 132 GLY A	1.86	333.28	1.97	0.34	1.17	101
    263	117 ILE B, 208 SER B, 132 GLY A	1.85	333.48	1.23	0.07	2.3	103
    264	117 ILE B, 132 GLY A, 209 PHE B	1.63	334.61	2.3	0.79	1.29	77
    265	117 ILE B, 132 GLY A, 209 PHE B, 119 PRO B	1.5	335.1	0.1	-0.09	2.17	54
    266	117 ILE B, 132 GLY A, 119 PRO B	1.48	335.38	-0.8	-0.56	2.78	58
    267	117 ILE B, 132 GLY A, 119 PRO B	1.52	335.76	0.83	0.31	1.7	80
    268	117 ILE B, 132 GLY A, 209 PHE B, 119 PRO B	1.65	336.41	0.1	-0.09	2.17	54
    269	132 GLY A, 209 PHE B, 119 PRO B	1.74	340	0.27	0.15	1.77	54
    270	132 GLY A, 209 PHE B, 119 PRO B, 210 ASN B	2.11	340.49	0.1	-0.09	2.17	54
    271	132 GLY A, 209 PHE B, 119 PRO B, 210 ASN B, 133 SER A	2.19	341.04	0	-0.23	2.41	54
    272	132 GLY A, 119 PRO B, 210 ASN B, 133 SER A, 218 ARG A	2.29	342.02	-1.46	-0.58	12.74	70
    273	132 GLY A, 119 PRO B, 210 ASN B, 218 ARG A	2.26	342.29	-1.73	-0.53	15.09	70
    274	119 PRO B, 210 ASN B, 218 ARG A	2.04	343.62	-2.17	-0.44	18.99	70
    275	209 PHE B, 119 PRO B, 210 ASN B, 218 ARG A	2.01	344.12	-0.93	0.01	14.33	64
    276	119 PRO B, 210 ASN B, 218 ARG A, 211 ARG B	2.01	344.76	-1.73	-0.53	15.09	70
    277	119 PRO B, 210 ASN B, 218 ARG A, 211 ARG B, 186 TYR B	2.08	345.11	-1.64	-0.2	12.39	63
    278	119 PRO B, 218 ARG A, 211 ARG B, 186 TYR B	2.16	346.81	-1.95	-0.05	14.64	63
    279	218 ARG A, 186 TYR B, 211 ARG B	2.31	348.42	-3.43	0.09	35.2	72
    280	218 ARG A, 186 TYR B, 211 ARG B, 125 LEU B	2.41	348.42	-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

    100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU 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

    Unique lining residues set - sidechains

    300106 VAL C, 300107 THR C, 300110 LEU C, 100100 ILE C, 100103 PHE C, 200100 ILE C, 100107 THR C, 100106 VAL C, 100110 LEU C, 200101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.1
    Hydrophobicity: 0.02
    Polarity: 1.81
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU C	1.85	0.66	1.73	0.18	1.33	86
    2	100101 THR C, 300106 VAL C, 300107 THR C	1.83	0.94	1.03	-0.15	1.72	102
    3	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C	1.85	1.53	0.68	-0.31	2.14	102
    4	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.96	1.68	0.46	-0.41	2.39	102
    5	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.94	1.79	-0.48	-0.79	2.95	107
    6	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.91	2.57	0.75	-0.14	2.14	105
    7	300107 THR C, 300103 PHE C, 100100 ILE C	1.52	4.16	1.13	0.08	1.72	105
    8	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.44	5.18	0.75	-0.14	2.14	105
    9	300107 THR C, 100100 ILE C, 100104 GLY C	1.65	8.26	1.13	0.08	1.72	105
    10	100100 ILE C, 100104 GLY C, 100103 PHE C	3.3	8.97	2.3	0.79	1.29	77
    11	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.42	9.17	1.63	0.39	1.81	77
    12	100104 GLY C, 100103 PHE C, 200100 ILE C	3.31	9.4	2.3	0.79	1.29	77
    13	100104 GLY C, 100103 PHE C, 200100 ILE C, 100107 THR C	2.74	10.42	1.55	0.4	1.38	87
    14	100103 PHE C, 200100 ILE C, 100107 THR C	1.39	14.66	2.2	0.8	0.71	87
    15	200100 ILE C, 100107 THR C, 100103 PHE C	1.7	15.07	1.13	0.08	1.72	105
    16	200100 ILE C, 100107 THR C, 100103 PHE C, 200101 THR C	1.86	15.74	0.75	-0.14	2.14	105
    17	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.98	15.91	0.46	-0.41	2.39	102
    18	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.87	16.74	0.68	-0.31	2.14	102
    19	100107 THR C, 200101 THR C, 100106 VAL C	1.84	17.05	1.03	-0.15	1.72	102
    20	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.77	17.81	1.73	0.18	1.33	86
    21	100106 VAL C, 100110 LEU C, 200101 THR C	1.22	22.08	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    100106 VAL C, 100107 THR C, 100110 LEU 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, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C, 200110 LEU C, 101 THR C

    Unique lining residues set - sidechains

    100106 VAL C, 100107 THR C, 100110 LEU C, 200100 ILE C, 200103 PHE C, 100 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: 1.1
    Hydrophobicity: 0.02
    Polarity: 1.81
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100106 VAL C, 100107 THR C, 100110 LEU C, 200101 THR C	1.85	0.65	1.73	0.18	1.33	86
    2	100106 VAL C, 100107 THR C, 200101 THR C	1.83	0.94	1.03	-0.15	1.72	102
    3	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C	1.85	1.53	0.68	-0.31	2.14	102
    4	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.96	1.68	0.46	-0.41	2.39	102
    5	100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.94	1.79	-0.48	-0.79	2.95	107
    6	100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.91	2.57	0.75	-0.14	2.14	105
    7	100107 THR C, 100103 PHE C, 200100 ILE C	1.52	4.16	1.13	0.08	1.72	105
    8	100107 THR C, 100103 PHE C, 200100 ILE C, 200104 GLY C	1.44	5.18	0.75	-0.14	2.14	105
    9	100107 THR C, 200100 ILE C, 200104 GLY C	1.65	8.26	1.13	0.08	1.72	105
    10	200100 ILE C, 200104 GLY C, 200103 PHE C	3.3	8.97	2.3	0.79	1.29	77
    11	200100 ILE C, 200104 GLY C, 200103 PHE C, 100 ILE C	3.42	9.17	1.63	0.39	1.81	77
    12	200104 GLY C, 200103 PHE C, 100 ILE C	3.31	9.4	2.3	0.79	1.29	77
    13	200104 GLY C, 200103 PHE C, 100 ILE C, 200107 THR C	2.74	10.42	1.55	0.4	1.38	87
    14	200103 PHE C, 100 ILE C, 200107 THR C	1.39	14.66	2.2	0.8	0.71	87
    15	100 ILE C, 200107 THR C, 200103 PHE C	1.7	15.07	1.13	0.08	1.72	105
    16	100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C	1.86	15.74	0.75	-0.14	2.14	105
    17	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.98	15.91	0.46	-0.41	2.39	102
    18	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.87	16.74	0.68	-0.31	2.14	102
    19	200107 THR C, 101 THR C, 200106 VAL C	1.84	17.05	1.03	-0.15	1.72	102
    20	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.77	17.81	1.73	0.18	1.33	86
    21	200106 VAL C, 200110 LEU C, 101 THR C	1.22	22.08	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    106 VAL C, 107 THR C, 110 LEU C, 300101 THR C, 103 PHE C, 300100 ILE C, 300100 ILE C, 103 PHE C, 104 GLY C, 100 ILE C, 100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C, 200110 LEU C, 101 THR C

    Unique lining residues set - sidechains

    106 VAL C, 107 THR C, 110 LEU C, 300100 ILE C, 103 PHE C, 100 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: 1.2
    Hydrophobicity: 0.05
    Polarity: 1.75
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	106 VAL C, 107 THR C, 110 LEU C, 300101 THR C	1.86	0.64	1.73	0.18	1.33	86
    2	106 VAL C, 107 THR C, 300101 THR C	1.84	0.92	1.03	-0.15	1.72	102
    3	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C	1.86	1.52	0.68	-0.31	2.14	102
    4	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.97	1.79	0.46	-0.41	2.39	102
    5	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.84	2.45	0.75	-0.14	2.14	105
    6	107 THR C, 103 PHE C, 300100 ILE C	1.55	3.85	1.13	0.08	1.72	105
    7	107 THR C, 300100 ILE C, 103 PHE C	1.38	6.59	2.2	0.8	0.71	87
    8	107 THR C, 103 PHE C, 104 GLY C	2.25	7.88	0.57	-0.07	1.8	79
    9	300100 ILE C, 103 PHE C, 104 GLY C	3.01	8.32	2.3	0.79	1.29	77
    10	300100 ILE C, 103 PHE C, 104 GLY C, 100 ILE C	3.31	8.63	1.63	0.39	1.81	77
    11	103 PHE C, 104 GLY C, 100 ILE C	3.27	9.73	2.3	0.79	1.29	77
    12	104 GLY C, 100 ILE C, 200107 THR C	1.59	13.63	1.13	0.08	1.72	105
    13	100 ILE C, 200107 THR C, 200103 PHE C	1.43	15.48	1.13	0.08	1.72	105
    14	100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C	1.91	16.09	0.75	-0.14	2.14	105
    15	100 ILE C, 200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.96	16.26	0.46	-0.41	2.39	102
    16	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.85	17.1	0.68	-0.31	2.14	102
    17	200107 THR C, 101 THR C, 200106 VAL C	1.83	17.4	1.03	-0.15	1.72	102
    18	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.75	18.15	1.73	0.18	1.33	86
    19	200106 VAL C, 200110 LEU C, 101 THR C	1.22	22.4	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU C, 300103 PHE C, 100100 ILE C, 100100 ILE C, 300103 PHE C, 300104 GLY C, 300100 ILE C, 300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 110 LEU C, 300101 THR C

    Unique lining residues set - sidechains

    300106 VAL C, 300107 THR C, 300110 LEU C, 100100 ILE C, 300103 PHE C, 300100 ILE C, 107 THR C, 106 VAL C, 110 LEU C, 300101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.2
    Hydrophobicity: 0.05
    Polarity: 1.75
    Mutability: 88
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU C	1.86	0.64	1.73	0.18	1.33	86
    2	100101 THR C, 300106 VAL C, 300107 THR C	1.84	0.92	1.03	-0.15	1.72	102
    3	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C	1.86	1.52	0.68	-0.31	2.14	102
    4	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.97	1.79	0.46	-0.41	2.39	102
    5	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.84	2.45	0.75	-0.14	2.14	105
    6	300107 THR C, 300103 PHE C, 100100 ILE C	1.55	3.85	1.13	0.08	1.72	105
    7	300107 THR C, 100100 ILE C, 300103 PHE C	1.38	6.59	2.2	0.8	0.71	87
    8	300107 THR C, 300103 PHE C, 300104 GLY C	2.25	7.88	0.57	-0.07	1.8	79
    9	100100 ILE C, 300103 PHE C, 300104 GLY C	3	8.32	2.3	0.79	1.29	77
    10	100100 ILE C, 300103 PHE C, 300104 GLY C, 300100 ILE C	3.31	8.63	1.63	0.39	1.81	77
    11	300103 PHE C, 300104 GLY C, 300100 ILE C	3.27	9.73	2.3	0.79	1.29	77
    12	300104 GLY C, 300100 ILE C, 107 THR C	1.59	13.63	1.13	0.08	1.72	105
    13	300100 ILE C, 107 THR C, 103 PHE C	1.43	15.48	1.13	0.08	1.72	105
    14	300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C	1.91	16.09	0.75	-0.14	2.14	105
    15	300100 ILE C, 107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.96	16.26	0.46	-0.41	2.39	102
    16	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.85	17.1	0.68	-0.31	2.14	102
    17	107 THR C, 300101 THR C, 106 VAL C	1.83	17.4	1.03	-0.15	1.72	102
    18	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.75	18.15	1.73	0.18	1.33	86
    19	106 VAL C, 110 LEU C, 300101 THR C	1.22	22.4	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU 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

    Unique lining residues set - sidechains

    300106 VAL C, 300107 THR C, 300110 LEU 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

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.2
    Polarity: 1.51
    Mutability: 90
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU C	1.92	0.44	1.73	0.18	1.33	86
    2	100101 THR C, 300106 VAL C, 300107 THR C	1.84	0.84	1.03	-0.15	1.72	102
    3	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C	1.84	1.62	0.68	-0.31	2.14	102
    4	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.95	1.79	0.46	-0.41	2.39	102
    5	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.91	2.67	0.75	-0.14	2.14	105
    6	300107 THR C, 300103 PHE C, 100100 ILE C	1.44	5	1.13	0.08	1.72	105
    7	300107 THR C, 100100 ILE C, 100104 GLY C	1.6	8.28	1.13	0.08	1.72	105
    8	100100 ILE C, 100104 GLY C, 100103 PHE C	3.32	8.82	2.3	0.79	1.29	77
    9	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.59	9.28	2.85	1.04	1	85
    10	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.82	9.56	1.98	0.51	1.33	104
    11	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.02	10.62	1.44	0.26	1.39	105
    12	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.66	10.79	1.38	0.26	1.05	105
    13	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.61	10.97	1.38	0.26	1.05	105
    14	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.62	11.18	1.38	0.26	1.05	105
    15	100100 ILE C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.66	11.45	2.42	0.78	0.74	104
    16	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.53	11.82	1.38	0.26	1.05	105
    17	200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C	4.09	12.51	1.44	0.26	1.39	105
    18	100 ILE C, 107 THR C, 300100 ILE C, 104 GLY C	3.88	12.74	1.98	0.51	1.33	104
    19	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.55	13.14	2.85	1.04	1	85
    20	100 ILE C, 104 GLY C, 103 PHE C	3.17	14.36	2.3	0.79	1.29	77
    21	200107 THR C, 100 ILE C, 104 GLY C	1.76	17.77	1.13	0.08	1.72	105
    22	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.43	18.92	0.75	-0.14	2.14	105
    23	200107 THR C, 100 ILE C, 200103 PHE C	1.59	19.61	1.13	0.08	1.72	105
    24	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.9	20.37	0.75	-0.14	2.14	105
    25	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.97	20.63	0.46	-0.41	2.39	102
    26	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.85	21.43	0.68	-0.31	2.14	102
    27	200107 THR C, 101 THR C, 200106 VAL C	1.83	21.79	1.03	-0.15	1.72	102
    28	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.85	22.22	1.73	0.18	1.33	86
    29	200106 VAL C, 200110 LEU C, 101 THR C	1.22	26.63	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    106 VAL C, 107 THR C, 110 LEU 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

    Unique lining residues set - sidechains

    106 VAL C, 107 THR C, 110 LEU 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

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.3
    Hydrophobicity: 0.16
    Polarity: 1.54
    Mutability: 90
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	106 VAL C, 107 THR C, 110 LEU C, 300101 THR C	1.92	0.48	1.73	0.18	1.33	86
    2	106 VAL C, 107 THR C, 300101 THR C	1.83	0.9	1.03	-0.15	1.72	102
    3	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C	1.85	1.48	0.68	-0.31	2.14	102
    4	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.97	1.7	0.46	-0.41	2.39	102
    5	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.94	1.84	-0.48	-0.79	2.95	107
    6	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.91	2.49	0.75	-0.14	2.14	105
    7	107 THR C, 103 PHE C, 300100 ILE C	1.47	4.89	1.13	0.08	1.72	105
    8	107 THR C, 103 PHE C, 300100 ILE C, 300104 GLY C	1.56	6.29	0.75	-0.14	2.14	105
    9	107 THR C, 300100 ILE C, 300104 GLY C	2.19	8.34	1.13	0.08	1.72	105
    10	300100 ILE C, 300104 GLY C, 300103 PHE C	3.36	8.82	2.3	0.79	1.29	77
    11	300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C	3.59	9.34	2.85	1.04	1	85
    12	300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	3.87	9.68	1.98	0.51	1.33	104
    13	107 THR C, 300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	4.09	10.48	1.44	0.26	1.39	105
    14	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.57	10.74	1.38	0.26	1.05	105
    15	107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C	4.62	10.92	1.38	0.26	1.05	105
    16	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.68	10.98	1.38	0.26	1.05	105
    17	107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C	4.68	11.04	1.38	0.26	1.05	105
    18	107 THR C, 100100 ILE C, 100107 THR C, 100 ILE C, 200107 THR C	4.69	11.11	1.38	0.26	1.05	105
    19	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.62	11.52	1.38	0.26	1.05	105
    20	107 THR C, 100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C	4.54	11.92	1.38	0.26	1.05	105
    21	100107 THR C, 100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C	4.06	12.65	1.44	0.26	1.39	105
    22	100 ILE C, 200100 ILE C, 200107 THR C, 200104 GLY C	3.84	12.88	1.98	0.51	1.33	104
    23	100 ILE C, 200100 ILE C, 200104 GLY C, 200103 PHE C	3.58	13.2	2.85	1.04	1	85
    24	200100 ILE C, 200104 GLY C, 200103 PHE C	3.33	14.05	2.3	0.79	1.29	77
    25	100107 THR C, 200100 ILE C, 200104 GLY C	2.07	17.29	1.13	0.08	1.72	105
    26	100107 THR C, 200100 ILE C, 200104 GLY C, 100103 PHE C	1.51	18.65	0.75	-0.14	2.14	105
    27	100107 THR C, 200100 ILE C, 100103 PHE C	1.5	19.56	1.13	0.08	1.72	105
    28	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.84	20.48	0.75	-0.14	2.14	105
    29	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.97	20.78	0.46	-0.41	2.39	102
    30	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.83	21.66	0.68	-0.31	2.14	102
    31	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.78	22.51	1.73	0.18	1.33	86
    32	100106 VAL C, 100110 LEU C, 200101 THR C	1.25	26.7	2.43	0.5	0.64	86

    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, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 103 PHE C, 300101 THR C, 300100 ILE C, 106 VAL C, 110 LEU C, 300101 THR 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, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.4
    Hydrophobicity: 0.12
    Polarity: 1.16
    Mutability: 94
    

    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	2.9	1.42	-3.5	-1.1	3.53	84
    4	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.4	3.1	2.66	0.68	0.81	95
    5	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.71	10.88	4.2	1.13	0.13	98
    6	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.29	11.46	3.72	0.91	0.1	98
    7	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.26	12.12	2.28	0.24	0.03	99
    8	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.37	12.64	2.28	0.24	0.03	99
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.18	13.95	3.72	0.91	0.1	98
    10	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	14.86	2.28	0.24	0.03	99
    11	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.73	18.07	1.8	0.02	0	100
    12	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.22	18.85	1.3	-0.14	0.33	101
    13	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.16	20.44	-0.2	-0.61	1.33	105
    14	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.18	22.13	1.3	-0.14	0.33	101
    15	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.43	23.27	-0.2	-0.61	1.33	105
    16	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.44	32.69	-0.7	-0.77	1.66	107
    17	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	4.18	33.28	-0.64	-0.78	2	107
    18	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300100 ILE C	4.55	33.72	0.34	-0.25	1.35	106
    19	200107 THR C, 300100 ILE C, 100 ILE C, 100100 ILE C, 200100 ILE C	4.58	34.36	3.46	1.29	0.44	103
    20	100107 THR C, 200107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C	4.66	34.54	2.42	0.78	0.74	104
    21	107 THR C, 100107 THR C, 300107 THR C, 300100 ILE C, 100100 ILE C	4.64	34.74	1.38	0.26	1.05	105
    22	107 THR C, 300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	4.09	35.65	1.44	0.26	1.39	105
    23	300107 THR C, 300104 GLY C, 300100 ILE C, 100100 ILE C	3.84	35.97	1.98	0.51	1.33	104
    24	300104 GLY C, 300100 ILE C, 100100 ILE C, 300103 PHE C	3.58	36.33	2.85	1.04	1	85
    25	300104 GLY C, 300100 ILE C, 300103 PHE C	3.15	37.4	2.3	0.79	1.29	77
    26	107 THR C, 300104 GLY C, 300100 ILE C	1.65	40.78	1.13	0.08	1.72	105
    27	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.45	41.57	0.75	-0.14	2.14	105
    28	107 THR C, 300100 ILE C, 103 PHE C	1.46	42.7	1.13	0.08	1.72	105
    29	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.82	43.43	0.75	-0.14	2.14	105
    30	107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C	1.94	43.55	-0.48	-0.79	2.95	107
    31	107 THR C, 103 PHE C, 300101 THR C, 300100 ILE C, 106 VAL C	1.96	43.69	0.46	-0.41	2.39	102
    32	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.84	44.61	0.68	-0.31	2.14	102
    33	107 THR C, 300101 THR C, 106 VAL C	1.83	44.86	1.03	-0.15	1.72	102
    34	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.81	45.47	1.73	0.18	1.33	86
    35	106 VAL C, 110 LEU C, 300101 THR C	1.21	49.89	2.43	0.5	0.64	86

    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, 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

    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

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.14
    Polarity: 1.08
    Mutability: 94
    

    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	0.46	2.66	0.68	0.81	95
    3	119 GLN C, 100119 GLN C, 300119 GLN C, 200119 GLN C	2.9	1.71	-3.5	-1.1	3.53	84
    4	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.2	3.56	2.66	0.68	0.81	95
    5	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.71	10.89	4.2	1.13	0.13	98
    6	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.28	11.47	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	11.96	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	12.41	2.28	0.24	0.03	99
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 111 ALA C	2.41	12.93	3.72	0.91	0.1	98
    10	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 300111 ALA C	2.19	14.37	3.72	0.91	0.1	98
    11	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	15.42	2.28	0.24	0.03	99
    12	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.75	17.69	1.8	0.02	0	100
    13	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.07	18.6	1.36	-0.14	0.68	100
    14	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.39	19.19	1.3	-0.14	0.33	101
    15	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.17	20.34	-0.2	-0.61	1.33	105
    16	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.2	22.1	1.3	-0.14	0.33	101
    17	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.27	23.31	-0.2	-0.61	1.33	105
    18	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.44	32.38	-0.7	-0.77	1.66	107
    19	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.06	33.53	-0.64	-0.78	2	107
    20	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.74	33.8	0.34	-0.25	1.35	106
    21	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.62	34.26	3.46	1.29	0.44	103
    22	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.69	34.3	0.34	-0.25	1.35	106
    23	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.63	34.56	1.38	0.26	1.05	105
    24	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.65	34.75	1.38	0.26	1.05	105
    25	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.08	35.7	1.44	0.26	1.39	105
    26	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.82	36.02	1.98	0.51	1.33	104
    27	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.57	36.4	2.85	1.04	1	85
    28	100 ILE C, 104 GLY C, 103 PHE C	3.18	37.4	2.3	0.79	1.29	77
    29	200107 THR C, 100 ILE C, 104 GLY C	1.67	40.84	1.13	0.08	1.72	105
    30	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.45	41.65	0.75	-0.14	2.14	105
    31	200107 THR C, 100 ILE C, 200103 PHE C	1.46	42.79	1.13	0.08	1.72	105
    32	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.84	43.53	0.75	-0.14	2.14	105
    33	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.95	43.82	0.46	-0.41	2.39	102
    34	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.87	44.54	0.68	-0.31	2.14	102
    35	200107 THR C, 101 THR C, 200106 VAL C	1.82	44.82	1.03	-0.15	1.72	102
    36	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.74	45.67	1.73	0.18	1.33	86
    37	200106 VAL C, 200110 LEU C, 101 THR C	1.22	49.94	2.43	0.5	0.64	86

    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, 300108 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE 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

    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, 100103 PHE C, 300106 VAL C, 300110 LEU C, 100101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.14
    Polarity: 1.08
    Mutability: 94
    

    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	0.46	2.66	0.68	0.81	95
    3	119 GLN C, 100119 GLN C, 300119 GLN C, 200119 GLN C	2.9	1.71	-3.5	-1.1	3.53	84
    4	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.2	3.56	2.66	0.68	0.81	95
    5	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.71	10.89	4.2	1.13	0.13	98
    6	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.28	11.47	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	11.96	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	12.41	2.28	0.24	0.03	99
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 111 ALA C	2.41	12.93	3.72	0.91	0.1	98
    10	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 300111 ALA C	2.19	14.37	3.72	0.91	0.1	98
    11	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	15.42	2.28	0.24	0.03	99
    12	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.75	17.69	1.8	0.02	0	100
    13	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.07	18.6	1.36	-0.14	0.68	100
    14	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.39	19.19	1.3	-0.14	0.33	101
    15	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.17	20.34	-0.2	-0.61	1.33	105
    16	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.2	22.1	1.3	-0.14	0.33	101
    17	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.27	23.31	-0.2	-0.61	1.33	105
    18	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.44	32.38	-0.7	-0.77	1.66	107
    19	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 104 GLY C	4.06	33.53	-0.64	-0.78	2	107
    20	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.74	33.8	0.34	-0.25	1.35	106
    21	100107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.62	34.26	3.46	1.29	0.44	103
    22	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.69	34.3	0.34	-0.25	1.35	106
    23	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.63	34.56	1.38	0.26	1.05	105
    24	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.65	34.75	1.38	0.26	1.05	105
    25	100107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C, 100104 GLY C	4.08	35.7	1.44	0.26	1.39	105
    26	100107 THR C, 100100 ILE C, 200100 ILE C, 100104 GLY C	3.82	36.02	1.98	0.51	1.33	104
    27	100100 ILE C, 200100 ILE C, 100104 GLY C, 100103 PHE C	3.57	36.4	2.85	1.04	1	85
    28	100100 ILE C, 100104 GLY C, 100103 PHE C	3.18	37.4	2.3	0.79	1.29	77
    29	300107 THR C, 100100 ILE C, 100104 GLY C	1.67	40.84	1.13	0.08	1.72	105
    30	300107 THR C, 100100 ILE C, 100104 GLY C, 300103 PHE C	1.45	41.65	0.75	-0.14	2.14	105
    31	300107 THR C, 100100 ILE C, 300103 PHE C	1.46	42.79	1.13	0.08	1.72	105
    32	300107 THR C, 100100 ILE C, 300103 PHE C, 100101 THR C	1.84	43.53	0.75	-0.14	2.14	105
    33	300107 THR C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C	1.95	43.82	0.46	-0.41	2.39	102
    34	300107 THR C, 300103 PHE C, 100101 THR C, 300106 VAL C	1.87	44.54	0.68	-0.31	2.14	102
    35	300107 THR C, 100101 THR C, 300106 VAL C	1.82	44.82	1.03	-0.15	1.72	102
    36	300107 THR C, 100101 THR C, 300106 VAL C, 300110 LEU C	1.74	45.67	1.73	0.18	1.33	86
    37	300106 VAL C, 300110 LEU C, 100101 THR C	1.22	49.94	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

40. 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, 200104 GLY C, 100100 ILE C, 100 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

    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, 200103 PHE C, 100106 VAL C, 100110 LEU C, 200101 THR C

    Physicochemical properties of lining side-chains

    Charge: 0 (0-0)
    Hydropathy: 1.5
    Hydrophobicity: 0.16
    Polarity: 1.02
    Mutability: 94
    

    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	0.08	-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	0.3	2.66	0.68	0.81	95
    3	119 GLN C, 100119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C	2.98	0.49	-0.42	-0.21	2.17	89
    4	119 GLN C, 100119 GLN C, 300119 GLN C, 200119 GLN C	2.91	1.25	-3.5	-1.1	3.53	84
    5	119 GLN C, 200115 VAL C, 300115 VAL C, 300119 GLN C, 115 VAL C	2.89	1.96	1.12	0.24	1.49	92
    6	119 GLN C, 200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	2.57	2.91	2.66	0.68	0.81	95
    7	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.73	5.64	4.2	1.13	0.13	98
    8	200115 VAL C, 300115 VAL C, 115 VAL C	1.86	6.06	4.2	1.13	0.13	98
    9	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.74	7.73	4.2	1.13	0.13	98
    10	300115 VAL C, 115 VAL C, 100115 VAL C	1.81	8.36	4.2	1.13	0.13	98
    11	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C	1.7	10.83	4.2	1.13	0.13	98
    12	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C	2.19	11.47	3.72	0.91	0.1	98
    13	300115 VAL C, 115 VAL C, 100115 VAL C, 100111 ALA C, 111 ALA C	2.44	11.84	3.24	0.69	0.08	98
    14	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.25	12.03	2.28	0.24	0.03	99
    15	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.28	12.48	2.28	0.24	0.03	99
    16	300115 VAL C, 115 VAL C, 100111 ALA C, 111 ALA C, 300111 ALA C	2.52	12.78	2.76	0.46	0.05	99
    17	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 111 ALA C	2.39	13.01	3.72	0.91	0.1	98
    18	200115 VAL C, 300115 VAL C, 115 VAL C, 100115 VAL C, 300111 ALA C	2.21	13.73	3.72	0.91	0.1	98
    19	300115 VAL C, 115 VAL C, 100111 ALA C, 111 ALA C, 300111 ALA C	2.34	14.57	2.76	0.46	0.05	99
    20	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.11	15.68	2.28	0.24	0.03	99
    21	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.78	17.98	1.8	0.02	0	100
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.15	19.36	1.3	-0.14	0.33	101
    23	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.18	20.23	-0.2	-0.61	1.33	105
    24	100111 ALA C, 300111 ALA C, 107 THR C, 100107 THR C, 300107 THR C	2.63	20.61	0.3	-0.45	1	104
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.19	21.21	1.3	-0.14	0.33	101
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.39	21.81	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.37	22.88	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.52	29.64	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 300107 THR C	2.96	29.92	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.61	30.6	-0.7	-0.77	1.66	107
    31	107 THR C, 100107 THR C, 300107 THR C	2.95	31.16	-0.7	-0.77	1.66	107
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	3.3	32.58	-0.7	-0.77	1.66	107
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	4.08	33.75	-0.64	-0.78	2	107
    34	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.69	34.01	0.34	-0.25	1.35	106
    35	300107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.65	34.4	3.46	1.29	0.44	103
    36	107 THR C, 100107 THR C, 200107 THR C, 100100 ILE C, 100 ILE C	4.7	34.47	1.38	0.26	1.05	105
    37	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.71	34.5	0.34	-0.25	1.35	106
    38	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200100 ILE C	4.69	34.6	0.34	-0.25	1.35	106
    39	107 THR C, 100107 THR C, 200107 THR C, 100100 ILE C, 100 ILE C	4.7	34.64	1.38	0.26	1.05	105
    40	107 THR C, 300107 THR C, 100100 ILE C, 100 ILE C, 300100 ILE C	4.62	34.82	2.42	0.78	0.74	104
    41	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.6	35.21	1.38	0.26	1.05	105
    42	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	4.02	36.16	1.44	0.26	1.39	105
    43	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.88	36.32	1.98	0.51	1.33	104
    44	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.55	36.77	2.85	1.04	1	85
    45	200104 GLY C, 200100 ILE C, 200103 PHE C	3.17	37.8	2.3	0.79	1.29	77
    46	100107 THR C, 200104 GLY C, 200100 ILE C	1.6	41.41	1.13	0.08	1.72	105
    47	100107 THR C, 200104 GLY C, 200100 ILE C, 100103 PHE C	1.43	42.22	0.75	-0.14	2.14	105
    48	100107 THR C, 200100 ILE C, 100103 PHE C	1.5	43.26	1.13	0.08	1.72	105
    49	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.89	43.96	0.75	-0.14	2.14	105
    50	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C, 200100 ILE C	1.96	44.11	0.46	-0.41	2.39	102
    51	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.83	45.09	0.68	-0.31	2.14	102
    52	100107 THR C, 200101 THR C, 100106 VAL C	1.84	45.35	1.03	-0.15	1.72	102
    53	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.76	45.98	1.73	0.18	1.33	86
    54	100106 VAL C, 100110 LEU C, 200101 THR C	1.22	50.3	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    106 VAL C, 107 THR C, 110 LEU 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, 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

    106 VAL C, 107 THR C, 110 LEU 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, 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: 0.3
    Hydrophobicity: -0.04
    Polarity: 6.27
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	106 VAL C, 107 THR C, 110 LEU C, 300101 THR C	1.86	0.59	1.73	0.18	1.33	86
    2	106 VAL C, 107 THR C, 300101 THR C	1.83	0.85	1.03	-0.15	1.72	102
    3	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C	1.84	1.57	0.68	-0.31	2.14	102
    4	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.96	1.7	0.46	-0.41	2.39	102
    5	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.94	1.8	-0.48	-0.79	2.95	107
    6	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.87	2.77	0.75	-0.14	2.14	105
    7	107 THR C, 103 PHE C, 300100 ILE C	1.47	4.29	1.13	0.08	1.72	105
    8	107 THR C, 103 PHE C, 300100 ILE C, 300104 GLY C	1.45	5.19	0.75	-0.14	2.14	105
    9	107 THR C, 300100 ILE C, 300104 GLY C	1.67	8.13	1.13	0.08	1.72	105
    10	300100 ILE C, 300104 GLY C, 300103 PHE C	3.21	8.81	2.3	0.79	1.29	77
    11	300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C	3.56	9.28	2.85	1.04	1	85
    12	300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	3.84	9.69	1.98	0.51	1.33	104
    13	107 THR C, 300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	4.09	10.44	1.44	0.26	1.39	105
    14	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.55	10.83	1.38	0.26	1.05	105
    15	300100 ILE C, 100100 ILE C, 100 ILE C, 200100 ILE C, 200107 THR C	4.58	11.73	3.46	1.29	0.44	103
    16	107 THR C, 300100 ILE C, 300107 THR C, 100107 THR C, 200107 THR C	4.57	12.36	0.34	-0.25	1.35	106
    17	107 THR C, 300104 GLY C, 300107 THR C, 100107 THR C, 200107 THR C	4.27	13.08	-0.64	-0.78	2	107
    18	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C	1.44	23.19	-0.7	-0.77	1.66	107
    19	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C, 100111 ALA C	2.49	23.88	-0.2	-0.61	1.33	105
    20	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.18	24.87	1.3	-0.14	0.33	101
    21	300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.54	25.24	1.3	-0.14	0.33	101
    22	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C, 100111 ALA C	2.21	27.11	-0.2	-0.61	1.33	105
    23	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.18	28.22	1.3	-0.14	0.33	101
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.76	30.55	1.8	0.02	0	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.15	31.9	2.28	0.24	0.03	99
    26	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.18	32.69	3.72	0.91	0.1	98
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.43	33.14	2.28	0.24	0.03	99
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	33.73	2.28	0.24	0.03	99
    29	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.18	35.22	3.72	0.91	0.1	98
    30	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	42.51	4.2	1.13	0.13	98
    31	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.19	44.04	2.66	0.68	0.81	95
    32	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.9	44.86	-3.5	-1.1	3.53	84
    33	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.93	44.97	2.66	0.68	0.81	95
    34	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.9	45.16	2.66	0.68	0.81	95
    35	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.25	-1.96	-0.65	2.85	86
    36	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.65	51.14	-3.5	-1.1	3.53	84
    37	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C	3.53	52.85	-3.44	-0.83	13.14	85
    38	200119 GLN C, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C	4.4	53.18	-3.26	-0.01	41.99	89
    39	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.33	53.51	-3.38	-0.56	22.76	86
    40	119 GLN C, 100119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	4.12	54.67	-3.38	-0.56	22.76	86
    41	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.11	55.49	-3.38	-0.56	22.76	86
    42	100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	2.99	57.42	-3.35	-0.42	27.57	87
    43	300119 GLN C, 100124 HIS C, 300124 HIS C	2.41	60.56	-3.3	-0.19	35.58	88
    44	300119 GLN C, 300124 HIS C, 100124 HIS C, 300122 ARG C	2.25	61.49	-2.9	-0.52	27.63	86
    45	300124 HIS C, 100124 HIS C, 300122 ARG C	2.25	62.08	-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

    106 VAL C, 107 THR C, 110 LEU 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, 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

    106 VAL C, 107 THR C, 110 LEU 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
    Hydrophobicity: -0.09
    Polarity: 7.09
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	106 VAL C, 107 THR C, 110 LEU C, 300101 THR C	1.86	0.6	1.73	0.18	1.33	86
    2	106 VAL C, 107 THR C, 300101 THR C	1.83	0.87	1.03	-0.15	1.72	102
    3	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C	1.84	1.59	0.68	-0.31	2.14	102
    4	106 VAL C, 107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.96	1.72	0.46	-0.41	2.39	102
    5	107 THR C, 300101 THR C, 103 PHE C, 300100 ILE C	1.91	2.43	0.75	-0.14	2.14	105
    6	107 THR C, 103 PHE C, 300100 ILE C	1.44	4.61	1.13	0.08	1.72	105
    7	107 THR C, 103 PHE C, 300100 ILE C, 300104 GLY C	1.5	5.54	0.75	-0.14	2.14	105
    8	107 THR C, 300100 ILE C, 300104 GLY C	1.81	8.24	1.13	0.08	1.72	105
    9	300100 ILE C, 300104 GLY C, 300103 PHE C	3.29	8.79	2.3	0.79	1.29	77
    10	300100 ILE C, 300104 GLY C, 300103 PHE C, 100100 ILE C	3.56	9.26	2.85	1.04	1	85
    11	300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	3.83	9.67	1.98	0.51	1.33	104
    12	107 THR C, 300100 ILE C, 300104 GLY C, 100100 ILE C, 300107 THR C	4.08	10.43	1.44	0.26	1.39	105
    13	107 THR C, 300100 ILE C, 100100 ILE C, 300107 THR C, 100107 THR C	4.56	10.83	1.38	0.26	1.05	105
    14	300100 ILE C, 100100 ILE C, 100 ILE C, 200100 ILE C, 200107 THR C	4.57	11.82	3.46	1.29	0.44	103
    15	107 THR C, 300100 ILE C, 300107 THR C, 100107 THR C, 200107 THR C	4.6	12.48	0.34	-0.25	1.35	106
    16	107 THR C, 300104 GLY C, 300107 THR C, 100107 THR C, 200107 THR C	4.18	13.22	-0.64	-0.78	2	107
    17	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C	1.5	22.72	-0.7	-0.77	1.66	107
    18	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C, 100111 ALA C	2.31	23.65	-0.2	-0.61	1.33	105
    19	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.16	25.12	1.3	-0.14	0.33	101
    20	107 THR C, 300107 THR C, 100107 THR C, 200107 THR C, 100111 ALA C	2.19	26.87	-0.2	-0.61	1.33	105
    21	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.18	27.97	1.3	-0.14	0.33	101
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	30.36	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2	31.85	2.28	0.24	0.03	99
    24	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.22	32.65	3.72	0.91	0.1	98
    25	100111 ALA C, 111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C	2.44	32.93	2.76	0.46	0.05	99
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.39	33.12	2.28	0.24	0.03	99
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	33.74	2.28	0.24	0.03	99
    28	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.12	35.29	3.72	0.91	0.1	98
    29	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	42.91	4.2	1.13	0.13	98
    30	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.43	44.18	2.66	0.68	0.81	95
    31	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.92	44.79	-3.5	-1.1	3.53	84
    32	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	3	44.91	-1.96	-0.65	2.85	86
    33	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	45.12	2.66	0.68	0.81	95
    34	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.21	-1.96	-0.65	2.85	86
    35	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.65	51.23	-3.5	-1.1	3.53	84
    36	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.59	52.68	-3.44	-0.83	13.14	85
    37	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 124 HIS C	4.4	52.86	-3.44	-0.83	13.14	85
    38	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.42	53.11	-3.26	-0.01	41.99	89
    39	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.4	53.17	-3.44	-0.83	13.14	85
    40	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.38	53.24	-3.38	-0.56	22.76	86
    41	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.34	53.49	-3.38	-0.56	22.76	86
    42	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.15	54.5	-3.38	-0.56	22.76	86
    43	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.12	55.27	-3.38	-0.56	22.76	86
    44	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	3.13	57.22	-3.35	-0.42	27.57	87
    45	100119 GLN C, 100124 HIS C, 200124 HIS C	2.4	60.83	-3.3	-0.19	35.58	88
    46	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.25	61.51	-2.9	-0.52	27.63	86
    47	100124 HIS C, 100122 ARG C, 200124 HIS C	2.25	62.11	-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

    100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU 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

    300106 VAL C, 300107 THR C, 300110 LEU 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: 6.05
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU C	1.86	0.6	1.73	0.18	1.33	86
    2	100101 THR C, 300106 VAL C, 300107 THR C	1.83	0.87	1.03	-0.15	1.72	102
    3	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C	1.84	1.59	0.68	-0.31	2.14	102
    4	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.96	1.72	0.46	-0.41	2.39	102
    5	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.91	2.43	0.75	-0.14	2.14	105
    6	300107 THR C, 300103 PHE C, 100100 ILE C	1.44	4.61	1.13	0.08	1.72	105
    7	300107 THR C, 300103 PHE C, 100100 ILE C, 100104 GLY C	1.5	5.54	0.75	-0.14	2.14	105
    8	300107 THR C, 100100 ILE C, 100104 GLY C	1.81	8.24	1.13	0.08	1.72	105
    9	100100 ILE C, 100104 GLY C, 100103 PHE C	3.29	8.8	2.3	0.79	1.29	77
    10	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.56	9.27	2.85	1.04	1	85
    11	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.81	9.68	1.98	0.51	1.33	104
    12	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.08	10.46	1.44	0.26	1.39	105
    13	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.54	10.77	1.38	0.26	1.05	105
    14	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	10.95	1.38	0.26	1.05	105
    15	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.69	11.07	0.34	-0.25	1.35	106
    16	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.64	12.06	3.46	1.29	0.44	103
    17	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.13	13.49	-0.64	-0.78	2	107
    18	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.55	23.05	-0.7	-0.77	1.66	107
    19	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	2.1	23.91	-0.2	-0.61	1.33	105
    20	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.21	25.29	1.3	-0.14	0.33	101
    21	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.16	27.15	-0.2	-0.61	1.33	105
    22	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.3	28.28	1.3	-0.14	0.33	101
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.79	30.66	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.1	31.54	2.28	0.24	0.03	99
    25	100111 ALA C, 111 ALA C, 300111 ALA C, 300115 VAL C, 115 VAL C	2.28	32.02	2.76	0.46	0.05	99
    26	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.22	32.53	3.72	0.91	0.1	98
    27	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.44	32.83	3.72	0.91	0.1	98
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.27	33.28	2.28	0.24	0.03	99
    29	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.27	33.95	2.28	0.24	0.03	99
    30	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.12	35.54	3.72	0.91	0.1	98
    31	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.71	43.17	4.2	1.13	0.13	98
    32	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.54	44.33	2.66	0.68	0.81	95
    33	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.89	44.92	-3.5	-1.1	3.53	84
    34	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.94	45.06	2.66	0.68	0.81	95
    35	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.9	45.24	2.66	0.68	0.81	95
    36	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.34	-1.96	-0.65	2.85	86
    37	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.66	51.46	-3.5	-1.1	3.53	84
    38	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C	3.64	52.85	-3.44	-0.83	13.14	85
    39	200119 GLN C, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C	4.42	53.26	-3.26	-0.01	41.99	89
    40	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.33	53.55	-3.38	-0.56	22.76	86
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	4.15	54.57	-3.38	-0.56	22.76	86
    42	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.12	55.34	-3.38	-0.56	22.76	86
    43	100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	3.13	57.29	-3.35	-0.42	27.57	87
    44	300119 GLN C, 100124 HIS C, 300124 HIS C	2.4	60.9	-3.3	-0.19	35.58	88
    45	300119 GLN C, 300124 HIS C, 100124 HIS C, 300122 ARG C	2.25	61.58	-2.9	-0.52	27.63	86
    46	300124 HIS C, 100124 HIS C, 300122 ARG C	2.25	62.17	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU 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, 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

    300106 VAL C, 300107 THR C, 300110 LEU 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: 0.1
    Hydrophobicity: -0.06
    Polarity: 7.43
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100101 THR C, 300106 VAL C, 300107 THR C, 300110 LEU C	1.86	0.61	1.73	0.18	1.33	86
    2	100101 THR C, 300106 VAL C, 300107 THR C	1.83	0.88	1.03	-0.15	1.72	102
    3	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C	1.85	1.47	0.68	-0.31	2.14	102
    4	100101 THR C, 300106 VAL C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.96	1.74	0.46	-0.41	2.39	102
    5	100101 THR C, 300107 THR C, 300103 PHE C, 100100 ILE C	1.91	2.6	0.75	-0.14	2.14	105
    6	300107 THR C, 300103 PHE C, 100100 ILE C	1.44	5.03	1.13	0.08	1.72	105
    7	300107 THR C, 100100 ILE C, 100104 GLY C	1.61	8.14	1.13	0.08	1.72	105
    8	100100 ILE C, 100104 GLY C, 100103 PHE C	3.22	8.8	2.3	0.79	1.29	77
    9	100100 ILE C, 100104 GLY C, 100103 PHE C, 200100 ILE C	3.56	9.29	2.85	1.04	1	85
    10	100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	3.81	9.72	1.98	0.51	1.33	104
    11	300107 THR C, 100100 ILE C, 100104 GLY C, 200100 ILE C, 100107 THR C	4.1	10.51	1.44	0.26	1.39	105
    12	300107 THR C, 100100 ILE C, 200100 ILE C, 100107 THR C, 200107 THR C	4.58	10.79	1.38	0.26	1.05	105
    13	300107 THR C, 200107 THR C, 100 ILE C, 107 THR C, 300100 ILE C	4.64	10.91	1.38	0.26	1.05	105
    14	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.68	10.99	0.34	-0.25	1.35	106
    15	100100 ILE C, 200100 ILE C, 100107 THR C, 100 ILE C, 300100 ILE C	4.64	11.8	3.46	1.29	0.44	103
    16	300107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 107 THR C	4.61	12.41	0.34	-0.25	1.35	106
    17	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 104 GLY C	4.34	13.16	-0.64	-0.78	2	107
    18	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C	1.56	23.02	-0.7	-0.77	1.66	107
    19	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 100111 ALA C	2.08	23.9	-0.2	-0.61	1.33	105
    20	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.22	25.34	1.3	-0.14	0.33	101
    21	300107 THR C, 100107 THR C, 200107 THR C, 107 THR C, 300111 ALA C	2.18	26.47	-0.2	-0.61	1.33	105
    22	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.41	27.43	1.3	-0.14	0.33	101
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.17	28.64	1.36	-0.14	0.68	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.76	31	1.8	0.02	0	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.29	31.76	2.28	0.24	0.03	99
    26	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.2	32.33	3.72	0.91	0.1	98
    27	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.31	32.93	3.72	0.91	0.1	98
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.33	33.25	2.28	0.24	0.03	99
    29	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	34.38	2.28	0.24	0.03	99
    30	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.16	35.24	3.72	0.91	0.1	98
    31	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	43.25	4.2	1.13	0.13	98
    32	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.55	44	2.66	0.68	0.81	95
    33	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.84	44.37	-1.96	-0.65	2.85	86
    34	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.92	44.95	-3.5	-1.1	3.53	84
    35	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	45.27	2.66	0.68	0.81	95
    36	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.37	-1.96	-0.65	2.85	86
    37	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.67	51.39	-3.5	-1.1	3.53	84
    38	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.61	52.84	-3.44	-0.83	13.14	85
    39	200119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.44	53	-3.26	-0.01	41.99	89
    40	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.42	53.25	-3.26	-0.01	41.99	89
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	53.29	-3.44	-0.83	13.14	85
    42	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.38	53.37	-3.38	-0.56	22.76	86
    43	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.33	53.69	-3.38	-0.56	22.76	86
    44	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.18	54.42	-3.38	-0.56	22.76	86
    45	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	3.86	56.05	-3.38	-0.56	22.76	86
    46	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	2.83	58.08	-3.35	-0.42	27.57	87
    47	100119 GLN C, 100124 HIS C, 200124 HIS C	2.39	60.94	-3.3	-0.19	35.58	88
    48	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.26	61.64	-2.9	-0.52	27.63	86
    49	100124 HIS C, 100122 ARG C, 200124 HIS C	2.24	62.25	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    101 THR C, 200106 VAL C, 200107 THR C, 200110 LEU 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, 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

    200106 VAL C, 200107 THR C, 200110 LEU 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: 0.1
    Hydrophobicity: -0.06
    Polarity: 7.43
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	101 THR C, 200106 VAL C, 200107 THR C, 200110 LEU C	1.86	0.61	1.73	0.18	1.33	86
    2	101 THR C, 200106 VAL C, 200107 THR C	1.83	0.88	1.03	-0.15	1.72	102
    3	101 THR C, 200106 VAL C, 200107 THR C, 200103 PHE C	1.85	1.47	0.68	-0.31	2.14	102
    4	101 THR C, 200106 VAL C, 200107 THR C, 200103 PHE C, 100 ILE C	1.96	1.74	0.46	-0.41	2.39	102
    5	101 THR C, 200107 THR C, 200103 PHE C, 100 ILE C	1.91	2.6	0.75	-0.14	2.14	105
    6	200107 THR C, 200103 PHE C, 100 ILE C	1.44	5.03	1.13	0.08	1.72	105
    7	200107 THR C, 100 ILE C, 104 GLY C	1.61	8.14	1.13	0.08	1.72	105
    8	100 ILE C, 104 GLY C, 103 PHE C	3.22	8.8	2.3	0.79	1.29	77
    9	100 ILE C, 104 GLY C, 103 PHE C, 300100 ILE C	3.56	9.29	2.85	1.04	1	85
    10	100 ILE C, 104 GLY C, 300100 ILE C, 107 THR C	3.81	9.72	1.98	0.51	1.33	104
    11	200107 THR C, 100 ILE C, 104 GLY C, 300100 ILE C, 107 THR C	4.1	10.51	1.44	0.26	1.39	105
    12	200107 THR C, 100 ILE C, 300100 ILE C, 107 THR C, 300107 THR C	4.58	10.79	1.38	0.26	1.05	105
    13	200107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C, 200100 ILE C	4.64	10.91	1.38	0.26	1.05	105
    14	200107 THR C, 107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C	4.68	10.99	0.34	-0.25	1.35	106
    15	100 ILE C, 300100 ILE C, 107 THR C, 100100 ILE C, 200100 ILE C	4.64	11.8	3.46	1.29	0.44	103
    16	200107 THR C, 107 THR C, 300107 THR C, 100100 ILE C, 100107 THR C	4.61	12.41	0.34	-0.25	1.35	106
    17	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C, 100104 GLY C	4.34	13.16	-0.64	-0.78	2	107
    18	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C	1.56	23.02	-0.7	-0.77	1.66	107
    19	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C, 100111 ALA C	2.08	23.9	-0.2	-0.61	1.33	105
    20	300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.22	25.34	1.3	-0.14	0.33	101
    21	200107 THR C, 107 THR C, 300107 THR C, 100107 THR C, 300111 ALA C	2.18	26.47	-0.2	-0.61	1.33	105
    22	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.41	27.43	1.3	-0.14	0.33	101
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.17	28.64	1.36	-0.14	0.68	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.76	31	1.8	0.02	0	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.29	31.76	2.28	0.24	0.03	99
    26	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.2	32.33	3.72	0.91	0.1	98
    27	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.31	32.93	3.72	0.91	0.1	98
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.33	33.25	2.28	0.24	0.03	99
    29	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.28	34.38	2.28	0.24	0.03	99
    30	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.16	35.24	3.72	0.91	0.1	98
    31	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.7	43.25	4.2	1.13	0.13	98
    32	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.55	44	2.66	0.68	0.81	95
    33	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.84	44.37	-1.96	-0.65	2.85	86
    34	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.92	44.95	-3.5	-1.1	3.53	84
    35	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	45.27	2.66	0.68	0.81	95
    36	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.37	-1.96	-0.65	2.85	86
    37	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.67	51.39	-3.5	-1.1	3.53	84
    38	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.61	52.84	-3.44	-0.83	13.14	85
    39	200119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.44	53	-3.26	-0.01	41.99	89
    40	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.42	53.25	-3.26	-0.01	41.99	89
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	53.29	-3.44	-0.83	13.14	85
    42	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.38	53.37	-3.38	-0.56	22.76	86
    43	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.33	53.69	-3.38	-0.56	22.76	86
    44	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.18	54.42	-3.38	-0.56	22.76	86
    45	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	3.86	56.05	-3.38	-0.56	22.76	86
    46	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	2.83	58.08	-3.35	-0.42	27.57	87
    47	100119 GLN C, 100124 HIS C, 200124 HIS C	2.39	60.94	-3.3	-0.19	35.58	88
    48	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.26	61.64	-2.9	-0.52	27.63	86
    49	100124 HIS C, 100122 ARG C, 200124 HIS C	2.24	62.25	-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

    100106 VAL C, 100107 THR C, 100110 LEU 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, 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, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C, 100124 HIS C, 300122 ARG C

    Unique lining residues set - sidechains

    100106 VAL C, 100107 THR C, 100110 LEU 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, 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
    Polarity: 5.61
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100106 VAL C, 100107 THR C, 100110 LEU C, 200101 THR C	1.86	0.61	1.73	0.18	1.33	86
    2	100106 VAL C, 100107 THR C, 200101 THR C	1.83	0.88	1.03	-0.15	1.72	102
    3	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C	1.85	1.47	0.68	-0.31	2.14	102
    4	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.96	1.74	0.46	-0.41	2.39	102
    5	100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.91	2.6	0.75	-0.14	2.14	105
    6	100107 THR C, 100103 PHE C, 200100 ILE C	1.44	5.03	1.13	0.08	1.72	105
    7	100107 THR C, 200100 ILE C, 200104 GLY C	1.61	8.14	1.13	0.08	1.72	105
    8	200100 ILE C, 200104 GLY C, 200103 PHE C	3.22	8.8	2.3	0.79	1.29	77
    9	200100 ILE C, 200104 GLY C, 200103 PHE C, 100 ILE C	3.56	9.29	2.85	1.04	1	85
    10	200100 ILE C, 200104 GLY C, 100 ILE C, 200107 THR C	3.82	9.71	1.98	0.51	1.33	104
    11	100107 THR C, 200100 ILE C, 200104 GLY C, 100 ILE C, 200107 THR C	4.1	10.5	1.44	0.26	1.39	105
    12	100107 THR C, 200100 ILE C, 100 ILE C, 200107 THR C, 107 THR C	4.58	10.79	1.38	0.26	1.05	105
    13	100 ILE C, 107 THR C, 100100 ILE C, 300100 ILE C, 300107 THR C	4.62	10.95	2.42	0.78	0.74	104
    14	100107 THR C, 200100 ILE C, 100 ILE C, 200107 THR C, 107 THR C	4.7	10.99	1.38	0.26	1.05	105
    15	100107 THR C, 200100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.7	11.08	0.34	-0.25	1.35	106
    16	100107 THR C, 100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.71	11.18	0.34	-0.25	1.35	106
    17	200100 ILE C, 100 ILE C, 100100 ILE C, 300100 ILE C, 300107 THR C	4.63	12.09	3.46	1.29	0.44	103
    18	100107 THR C, 100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.55	12.75	0.34	-0.25	1.35	106
    19	100107 THR C, 200104 GLY C, 200107 THR C, 107 THR C, 300107 THR C	4.16	13.52	-0.64	-0.78	2	107
    20	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C	1.44	23.44	-0.7	-0.77	1.66	107
    21	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C, 100111 ALA C	2.47	24.17	-0.2	-0.61	1.33	105
    22	100107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.4	24.42	1.3	-0.14	0.33	101
    23	300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.18	25.24	1.3	-0.14	0.33	101
    24	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C, 300111 ALA C	2.21	26.84	-0.2	-0.61	1.33	105
    25	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	27.89	1.3	-0.14	0.33	101
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	1.95	29.13	1.36	-0.14	0.68	100
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.79	31.39	1.8	0.02	0	100
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.23	32.04	2.28	0.24	0.03	99
    29	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.22	32.56	3.72	0.91	0.1	98
    30	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.37	33.16	3.72	0.91	0.1	98
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.28	33.4	2.28	0.24	0.03	99
    32	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.26	34.02	2.28	0.24	0.03	99
    33	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.15	35.63	3.72	0.91	0.1	98
    34	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.72	42.66	4.2	1.13	0.13	98
    35	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.16	44.26	2.66	0.68	0.81	95
    36	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.89	44.91	-3.5	-1.1	3.53	84
    37	300115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.97	45.07	-1.96	-0.65	2.85	86
    38	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.94	45.14	2.66	0.68	0.81	95
    39	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.91	45.37	2.66	0.68	0.81	95
    40	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.47	-1.96	-0.65	2.85	86
    41	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.65	51.64	-3.5	-1.1	3.53	84
    42	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C	3.73	52.96	-3.44	-0.83	13.14	85
    43	200119 GLN C, 100124 HIS C, 124 HIS C, 200124 HIS C, 300124 HIS C	4.4	53.33	-3.26	-0.01	41.99	89
    44	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	4.32	53.69	-3.38	-0.56	22.76	86
    45	119 GLN C, 100119 GLN C, 200119 GLN C, 124 HIS C, 200124 HIS C	4.18	54.42	-3.38	-0.56	22.76	86
    46	119 GLN C, 100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	3.86	56.04	-3.38	-0.56	22.76	86
    47	100119 GLN C, 300119 GLN C, 100124 HIS C, 300124 HIS C	2.82	58.07	-3.35	-0.42	27.57	87
    48	300119 GLN C, 100124 HIS C, 300124 HIS C	2.39	60.94	-3.3	-0.19	35.58	88
    49	300119 GLN C, 300124 HIS C, 100124 HIS C, 300122 ARG C	2.26	61.63	-2.9	-0.52	27.63	86
    50	300124 HIS C, 100124 HIS C, 300122 ARG C	2.24	62.24	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

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

    Unique lining residues set - all

    100106 VAL C, 100107 THR C, 100110 LEU 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, 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

    100106 VAL C, 100107 THR C, 100110 LEU 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: -0.03
    Polarity: 6.36
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100106 VAL C, 100107 THR C, 100110 LEU C, 200101 THR C	1.86	0.63	1.73	0.18	1.33	86
    2	100106 VAL C, 100107 THR C, 200101 THR C	1.83	0.9	1.03	-0.15	1.72	102
    3	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C	1.85	1.48	0.68	-0.31	2.14	102
    4	100106 VAL C, 100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.95	1.76	0.46	-0.41	2.39	102
    5	100107 THR C, 200101 THR C, 100103 PHE C, 200100 ILE C	1.88	2.75	0.75	-0.14	2.14	105
    6	100107 THR C, 100103 PHE C, 200100 ILE C	1.47	4.38	1.13	0.08	1.72	105
    7	100107 THR C, 100103 PHE C, 200100 ILE C, 200104 GLY C	1.47	5.35	0.75	-0.14	2.14	105
    8	100107 THR C, 200100 ILE C, 200104 GLY C	1.72	8.25	1.13	0.08	1.72	105
    9	200100 ILE C, 200104 GLY C, 200103 PHE C	3.29	8.83	2.3	0.79	1.29	77
    10	200100 ILE C, 200104 GLY C, 200103 PHE C, 100 ILE C	3.58	9.25	2.85	1.04	1	85
    11	200100 ILE C, 200104 GLY C, 100 ILE C, 200107 THR C	3.8	9.67	1.98	0.51	1.33	104
    12	100107 THR C, 200100 ILE C, 200104 GLY C, 100 ILE C, 200107 THR C	4.07	10.48	1.44	0.26	1.39	105
    13	100107 THR C, 200100 ILE C, 100 ILE C, 200107 THR C, 107 THR C	4.55	10.79	1.38	0.26	1.05	105
    14	100 ILE C, 107 THR C, 100100 ILE C, 300100 ILE C, 300107 THR C	4.63	10.94	2.42	0.78	0.74	104
    15	100107 THR C, 200100 ILE C, 100 ILE C, 200107 THR C, 107 THR C	4.69	10.99	1.38	0.26	1.05	105
    16	100107 THR C, 200100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.69	11.08	0.34	-0.25	1.35	106
    17	100107 THR C, 100 ILE C, 200107 THR C, 107 THR C, 300107 THR C	4.7	11.2	0.34	-0.25	1.35	106
    18	200100 ILE C, 100 ILE C, 100100 ILE C, 300100 ILE C, 300107 THR C	4.65	12.23	3.46	1.29	0.44	103
    19	100107 THR C, 200104 GLY C, 200107 THR C, 107 THR C, 300107 THR C	4.09	13.74	-0.64	-0.78	2	107
    20	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C	1.54	23.03	-0.7	-0.77	1.66	107
    21	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C, 100111 ALA C	2.3	24	-0.2	-0.61	1.33	105
    22	100107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	24.46	1.3	-0.14	0.33	101
    23	300107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.17	25.52	1.3	-0.14	0.33	101
    24	100107 THR C, 200107 THR C, 107 THR C, 300107 THR C, 300111 ALA C	2.19	26.7	-0.2	-0.61	1.33	105
    25	107 THR C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.57	27.7	1.3	-0.14	0.33	101
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.09	28.94	1.36	-0.14	0.68	100
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.75	31.31	1.8	0.02	0	100
    28	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.19	32.03	2.28	0.24	0.03	99
    29	300111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.23	32.57	3.72	0.91	0.1	98
    30	111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.37	33.18	3.72	0.91	0.1	98
    31	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300115 VAL C	2.29	33.43	2.28	0.24	0.03	99
    32	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 115 VAL C	2.29	34.08	2.28	0.24	0.03	99
    33	100111 ALA C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.09	35.74	3.72	0.91	0.1	98
    34	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.69	43.08	4.2	1.13	0.13	98
    35	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 119 GLN C	2.4	44.44	2.66	0.68	0.81	95
    36	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.91	45.07	-3.5	-1.1	3.53	84
    37	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300119 GLN C	2.9	45.42	2.66	0.68	0.81	95
    38	200115 VAL C, 119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.99	45.52	-1.96	-0.65	2.85	86
    39	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C	2.65	51.73	-3.5	-1.1	3.53	84
    40	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	3.74	53.06	-3.44	-0.83	13.14	85
    41	100119 GLN C, 300124 HIS C, 124 HIS C, 100124 HIS C, 200124 HIS C	4.41	53.39	-3.26	-0.01	41.99	89
    42	119 GLN C, 100119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C	4.39	53.43	-3.44	-0.83	13.14	85
    43	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.38	53.48	-3.38	-0.56	22.76	86
    44	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.34	53.76	-3.38	-0.56	22.76	86
    45	119 GLN C, 200119 GLN C, 300119 GLN C, 300124 HIS C, 124 HIS C	4.16	55.02	-3.38	-0.56	22.76	86
    46	100119 GLN C, 200119 GLN C, 300119 GLN C, 100124 HIS C, 200124 HIS C	4.01	55.92	-3.38	-0.56	22.76	86
    47	100119 GLN C, 200119 GLN C, 100124 HIS C, 200124 HIS C	2.91	57.99	-3.35	-0.42	27.57	87
    48	100119 GLN C, 100124 HIS C, 200124 HIS C	2.39	61.02	-3.3	-0.19	35.58	88
    49	100119 GLN C, 100124 HIS C, 100122 ARG C, 200124 HIS C	2.26	61.73	-2.9	-0.52	27.63	86
    50	100124 HIS C, 100122 ARG C, 200124 HIS C	2.24	62.36	-2.7	-0.32	35.66	87

    pore with bottle neck

    pore with local minimum

48. 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, 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

    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, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: -0.02
    Polarity: 5.5
    Mutability: 93
    

    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	0.79	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.24	1.71	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.39	5.77	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	3.05	7.4	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	4.11	7.95	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.31	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	4.16	9.11	-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	10.63	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.65	16.45	-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	16.53	-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	16.82	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	-1.96	-0.65	2.85	86
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.88	18.22	-3.5	-1.1	3.53	84
    14	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.25	20.01	2.66	0.68	0.81	95
    15	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.71	27.05	4.2	1.13	0.13	98
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.1	28.19	3.72	0.91	0.1	98
    17	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.24	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	29.05	2.28	0.24	0.03	99
    19	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 111 ALA C	2.49	29.33	3.72	0.91	0.1	98
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.23	30.97	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.14	31.99	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.74	34.19	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.1	35.1	1.36	-0.14	0.68	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.49	35.71	1.3	-0.14	0.33	101
    25	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.16	36.84	-0.2	-0.61	1.33	105
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.22	38.32	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.25	39.34	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.54	48.97	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	4.05	50.1	-0.64	-0.78	2	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.76	50.4	0.34	-0.25	1.35	106
    31	200107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.56	50.98	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 300107 THR C, 100100 ILE C, 300100 ILE C	4.56	51.41	1.38	0.26	1.05	105
    33	107 THR C, 300107 THR C, 300104 GLY C, 100100 ILE C, 300100 ILE C	3.99	52.28	1.44	0.26	1.39	105
    34	300107 THR C, 300104 GLY C, 100100 ILE C, 300100 ILE C	3.87	52.43	1.98	0.51	1.33	104
    35	300104 GLY C, 100100 ILE C, 300100 ILE C, 300103 PHE C	3.55	52.85	2.85	1.04	1	85
    36	300104 GLY C, 300100 ILE C, 300103 PHE C	3.17	53.84	2.3	0.79	1.29	77
    37	107 THR C, 300104 GLY C, 300100 ILE C	1.7	57.17	1.13	0.08	1.72	105
    38	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.47	57.97	0.75	-0.14	2.14	105
    39	107 THR C, 300100 ILE C, 103 PHE C	1.45	59.44	1.13	0.08	1.72	105
    40	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.91	60.04	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	60.18	0.46	-0.41	2.39	102
    42	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.84	61.09	0.68	-0.31	2.14	102
    43	107 THR C, 300101 THR C, 106 VAL C	1.83	61.35	1.03	-0.15	1.72	102
    44	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.8	61.96	1.73	0.18	1.33	86
    45	106 VAL C, 110 LEU C, 300101 THR C	1.22	66.38	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

49. 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, 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

    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

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.4
    Hydrophobicity: -0.03
    Polarity: 5.23
    Mutability: 93
    

    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	0.81	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.24	1.76	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.38	5.09	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	2.79	6.9	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	3.7	8.09	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.27	8.38	-3.38	-0.56	22.76	86
    7	124 HIS C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.18	8.93	-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	10.99	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.62	16.45	-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	2.9	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	3	17.03	-1.96	-0.65	2.85	86
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.91	17.75	-3.5	-1.1	3.53	84
    14	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.88	18.43	-1.96	-0.65	2.85	86
    15	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.6	19.33	2.66	0.68	0.81	95
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.72	27.5	4.2	1.13	0.13	98
    17	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.35	28.05	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.25	28.52	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	28.98	2.28	0.24	0.03	99
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 111 ALA C	2.39	29.49	3.72	0.91	0.1	98
    21	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300111 ALA C	2.23	30.9	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.1	31.93	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	34.18	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.02	35.1	1.36	-0.14	0.68	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.43	35.71	1.3	-0.14	0.33	101
    26	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.17	36.86	-0.2	-0.61	1.33	105
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.18	38.48	1.3	-0.14	0.33	101
    28	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.35	39.61	-0.2	-0.61	1.33	105
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.49	49.41	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.38	49.97	-0.64	-0.78	2	107
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.62	50.32	0.34	-0.25	1.35	106
    32	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.64	50.8	3.46	1.29	0.44	103
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.69	50.86	0.34	-0.25	1.35	106
    34	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.63	51.06	1.38	0.26	1.05	105
    35	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.59	51.44	1.38	0.26	1.05	105
    36	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.01	52.36	1.44	0.26	1.39	105
    37	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.78	52.65	1.98	0.51	1.33	104
    38	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.56	52.98	2.85	1.04	1	85
    39	100 ILE C, 104 GLY C, 103 PHE C	3.29	53.75	2.3	0.79	1.29	77
    40	200107 THR C, 100 ILE C, 104 GLY C	1.6	57.62	1.13	0.08	1.72	105
    41	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.43	58.41	0.75	-0.14	2.14	105
    42	200107 THR C, 100 ILE C, 200103 PHE C	1.49	59.44	1.13	0.08	1.72	105
    43	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.87	60.13	0.75	-0.14	2.14	105
    44	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.95	60.42	0.46	-0.41	2.39	102
    45	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.85	61.15	0.68	-0.31	2.14	102
    46	200107 THR C, 101 THR C, 200106 VAL C	1.83	61.42	1.03	-0.15	1.72	102
    47	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.74	62.26	1.73	0.18	1.33	86
    48	200106 VAL C, 200110 LEU C, 101 THR C	1.23	66.52	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

50. 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, 104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE 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

    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, 100103 PHE C, 300106 VAL C, 300110 LEU C, 100101 THR C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.4
    Hydrophobicity: -0.03
    Polarity: 5.23
    Mutability: 93
    

    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	0.81	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.24	1.76	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.38	5.09	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	2.79	6.9	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	3.7	8.09	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.27	8.38	-3.38	-0.56	22.76	86
    7	124 HIS C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.18	8.93	-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	10.99	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.62	16.45	-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	2.9	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	3	17.03	-1.96	-0.65	2.85	86
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.91	17.75	-3.5	-1.1	3.53	84
    14	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.88	18.43	-1.96	-0.65	2.85	86
    15	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.6	19.33	2.66	0.68	0.81	95
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.72	27.5	4.2	1.13	0.13	98
    17	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.35	28.05	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.25	28.52	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	28.98	2.28	0.24	0.03	99
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 111 ALA C	2.39	29.49	3.72	0.91	0.1	98
    21	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300111 ALA C	2.23	30.9	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.1	31.93	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	34.18	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	2.02	35.1	1.36	-0.14	0.68	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.43	35.71	1.3	-0.14	0.33	101
    26	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.17	36.86	-0.2	-0.61	1.33	105
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.18	38.48	1.3	-0.14	0.33	101
    28	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.35	39.61	-0.2	-0.61	1.33	105
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.49	49.41	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 104 GLY C	4.38	49.97	-0.64	-0.78	2	107
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.62	50.32	0.34	-0.25	1.35	106
    32	100107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.64	50.8	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	50.86	0.34	-0.25	1.35	106
    34	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.63	51.06	1.38	0.26	1.05	105
    35	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.59	51.44	1.38	0.26	1.05	105
    36	100107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C, 100104 GLY C	4.01	52.36	1.44	0.26	1.39	105
    37	100107 THR C, 100100 ILE C, 200100 ILE C, 100104 GLY C	3.78	52.65	1.98	0.51	1.33	104
    38	100100 ILE C, 200100 ILE C, 100104 GLY C, 100103 PHE C	3.56	52.98	2.85	1.04	1	85
    39	100100 ILE C, 100104 GLY C, 100103 PHE C	3.29	53.75	2.3	0.79	1.29	77
    40	300107 THR C, 100100 ILE C, 100104 GLY C	1.6	57.62	1.13	0.08	1.72	105
    41	300107 THR C, 100100 ILE C, 100104 GLY C, 300103 PHE C	1.43	58.41	0.75	-0.14	2.14	105
    42	300107 THR C, 100100 ILE C, 300103 PHE C	1.49	59.44	1.13	0.08	1.72	105
    43	300107 THR C, 100100 ILE C, 300103 PHE C, 100101 THR C	1.87	60.13	0.75	-0.14	2.14	105
    44	300107 THR C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C	1.95	60.42	0.46	-0.41	2.39	102
    45	300107 THR C, 300103 PHE C, 100101 THR C, 300106 VAL C	1.85	61.15	0.68	-0.31	2.14	102
    46	300107 THR C, 100101 THR C, 300106 VAL C	1.83	61.42	1.03	-0.15	1.72	102
    47	300107 THR C, 100101 THR C, 300106 VAL C, 300110 LEU C	1.74	62.26	1.73	0.18	1.33	86
    48	300106 VAL C, 300110 LEU C, 100101 THR C	1.23	66.52	2.43	0.5	0.64	86

    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, 200104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C, 200103 PHE C, 100103 PHE C, 200101 THR C, 200100 ILE C, 100106 VAL C, 100110 LEU C, 200101 THR 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

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: -0.01
    Polarity: 5.13
    Mutability: 93
    

    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	0.82	-2.7	-0.32	35.66	87
    2	122 ARG C, 124 HIS C, 300124 HIS C, 119 GLN C	2.25	1.83	-2.9	-0.52	27.63	86
    3	124 HIS C, 119 GLN C, 300124 HIS C	2.37	5.39	-3.3	-0.19	35.58	88
    4	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C	2.9	7.18	-3.35	-0.42	27.57	87
    5	124 HIS C, 119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C	3.88	8.21	-3.38	-0.56	22.76	86
    6	300119 GLN C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.24	8.36	-3.38	-0.56	22.76	86
    7	124 HIS C, 200119 GLN C, 100119 GLN C, 100124 HIS C, 200124 HIS C	4.21	9.11	-3.32	-0.28	32.37	88
    8	119 GLN C, 300124 HIS C, 300119 GLN C, 200119 GLN C, 100119 GLN C	3.7	10.74	-3.44	-0.83	13.14	85
    9	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.64	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	16.55	-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	16.9	2.66	0.68	0.81	95
    12	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C, 300115 VAL C	2.97	17.1	-1.96	-0.65	2.85	86
    13	119 GLN C, 300119 GLN C, 200119 GLN C, 100119 GLN C	2.89	18	-3.5	-1.1	3.53	84
    14	119 GLN C, 300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	2.35	19.81	2.66	0.68	0.81	95
    15	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C	1.73	27.44	4.2	1.13	0.13	98
    16	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 100111 ALA C	2.35	28.01	3.72	0.91	0.1	98
    17	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.25	28.49	2.28	0.24	0.03	99
    18	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.3	28.98	2.28	0.24	0.03	99
    19	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 111 ALA C	2.36	29.48	3.72	0.91	0.1	98
    20	300115 VAL C, 115 VAL C, 100115 VAL C, 200115 VAL C, 300111 ALA C	2.22	30.25	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.01	32.23	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.79	34.5	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.11	35.34	1.3	-0.14	0.33	101
    24	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.23	36.67	-0.2	-0.61	1.33	105
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.18	37.64	1.3	-0.14	0.33	101
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.31	39.27	1.3	-0.14	0.33	101
    27	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.55	48.87	-0.7	-0.77	1.66	107
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	4	50.09	-0.64	-0.78	2	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.63	50.41	0.34	-0.25	1.35	106
    30	300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.64	50.9	3.46	1.29	0.44	103
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.71	50.93	0.34	-0.25	1.35	106
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200100 ILE C	4.69	51.02	0.34	-0.25	1.35	106
    33	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.7	51.07	1.38	0.26	1.05	105
    34	107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 300100 ILE C	4.63	51.35	2.42	0.78	0.74	104
    35	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.63	51.55	1.38	0.26	1.05	105
    36	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	4.09	52.51	1.44	0.26	1.39	105
    37	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.82	52.83	1.98	0.51	1.33	104
    38	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.57	53.19	2.85	1.04	1	85
    39	200104 GLY C, 200100 ILE C, 200103 PHE C	3.27	54.01	2.3	0.79	1.29	77
    40	100107 THR C, 200104 GLY C, 200100 ILE C	1.86	57.21	1.13	0.08	1.72	105
    41	100107 THR C, 200104 GLY C, 200100 ILE C, 100103 PHE C	1.53	58.08	0.75	-0.14	2.14	105
    42	100107 THR C, 200100 ILE C, 100103 PHE C	1.43	59.76	1.13	0.08	1.72	105
    43	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.91	60.29	0.75	-0.14	2.14	105
    44	100107 THR C, 100103 PHE C, 200101 THR C, 200100 ILE C	1.94	60.42	-0.48	-0.79	2.95	107
    45	100107 THR C, 100103 PHE C, 200101 THR C, 200100 ILE C, 100106 VAL C	1.97	60.57	0.46	-0.41	2.39	102
    46	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.83	61.56	0.68	-0.31	2.14	102
    47	100107 THR C, 200101 THR C, 100106 VAL C	1.84	61.81	1.03	-0.15	1.72	102
    48	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.76	62.44	1.73	0.18	1.33	86
    49	100106 VAL C, 100110 LEU C, 200101 THR C	1.24	66.74	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

52. 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, 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

    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, 300103 PHE C, 106 VAL C, 110 LEU C, 300101 THR C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.3
    Hydrophobicity: -0.02
    Polarity: 6.06
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.25	0.82	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.25	1.81	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.37	5.34	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	2.88	7.13	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	3.86	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	4.18	8.77	-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	4.41	9.5	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.87	11.02	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.65	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	3	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	2.91	17.29	2.66	0.68	0.81	95
    13	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 300115 VAL C	2.97	17.48	-1.96	-0.65	2.85	86
    14	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.9	18.23	-3.5	-1.1	3.53	84
    15	119 GLN C, 300119 GLN C, 200115 VAL C, 115 VAL C, 300115 VAL C	3.01	18.93	1.12	0.24	1.49	92
    16	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.58	19.86	2.66	0.68	0.81	95
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.71	27.59	4.2	1.13	0.13	98
    18	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.15	28.73	3.72	0.91	0.1	98
    19	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.26	29.08	2.28	0.24	0.03	99
    20	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.35	29.61	2.28	0.24	0.03	99
    21	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.21	31.05	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.18	32.04	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.79	34.34	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300108 ALA C	1.93	35.35	1.36	-0.14	0.68	100
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.24	36.05	1.3	-0.14	0.33	101
    26	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.19	37.28	-0.2	-0.61	1.33	105
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.19	38.95	1.3	-0.14	0.33	101
    28	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.44	40.11	-0.2	-0.61	1.33	105
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.44	49.43	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 300104 GLY C	4.06	50.58	-0.64	-0.78	2	107
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.7	50.85	0.34	-0.25	1.35	106
    32	200107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.57	51.3	3.46	1.29	0.44	103
    33	100107 THR C, 200107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C	4.65	51.49	2.42	0.78	0.74	104
    34	107 THR C, 100107 THR C, 300107 THR C, 100100 ILE C, 300100 ILE C	4.62	51.7	1.38	0.26	1.05	105
    35	107 THR C, 300107 THR C, 300104 GLY C, 100100 ILE C, 300100 ILE C	4.05	52.64	1.44	0.26	1.39	105
    36	300107 THR C, 300104 GLY C, 100100 ILE C, 300100 ILE C	3.81	52.95	1.98	0.51	1.33	104
    37	300104 GLY C, 100100 ILE C, 300100 ILE C, 300103 PHE C	3.56	53.28	2.85	1.04	1	85
    38	300104 GLY C, 300100 ILE C, 300103 PHE C	3.25	54.13	2.3	0.79	1.29	77
    39	107 THR C, 300104 GLY C, 300100 ILE C	1.8	57.41	1.13	0.08	1.72	105
    40	107 THR C, 300104 GLY C, 300100 ILE C, 103 PHE C	1.5	58.27	0.75	-0.14	2.14	105
    41	107 THR C, 300100 ILE C, 103 PHE C	1.44	59.86	1.13	0.08	1.72	105
    42	107 THR C, 300100 ILE C, 103 PHE C, 300101 THR C	1.91	60.37	0.75	-0.14	2.14	105
    43	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C, 300100 ILE C	1.95	60.65	0.46	-0.41	2.39	102
    44	107 THR C, 103 PHE C, 300101 THR C, 106 VAL C	1.87	61.37	0.68	-0.31	2.14	102
    45	107 THR C, 300101 THR C, 106 VAL C	1.83	61.89	1.03	-0.15	1.72	102
    46	107 THR C, 300101 THR C, 106 VAL C, 110 LEU C	1.75	62.52	1.73	0.18	1.33	86
    47	106 VAL C, 110 LEU C, 300101 THR C	1.24	66.81	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

53. 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

    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

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.4
    Hydrophobicity: -0.01
    Polarity: 6.13
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.25	0.83	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.25	1.89	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.37	5.63	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	3	7.4	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.04	7.97	-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	8.72	-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	8.97	-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	9.43	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.54	11.64	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.67	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	2.9	17.38	2.66	0.68	0.81	95
    13	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.91	18.62	-3.5	-1.1	3.53	84
    14	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.2	20.54	2.66	0.68	0.81	95
    15	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.7	27.63	4.2	1.13	0.13	98
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.19	28.72	3.72	0.91	0.1	98
    17	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	28.91	2.28	0.24	0.03	99
    18	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	29.65	2.28	0.24	0.03	99
    19	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.39	29.9	3.72	0.91	0.1	98
    20	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.2	31.44	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	32.54	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	34.87	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.15	36.27	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	37.15	-0.2	-0.61	1.33	105
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.24	38.8	1.3	-0.14	0.33	101
    26	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.18	39.92	-0.2	-0.61	1.33	105
    27	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.6	49.65	-0.7	-0.77	1.66	107
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.25	50.28	-0.64	-0.78	2	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.62	50.72	0.34	-0.25	1.35	106
    30	107 THR C, 100100 ILE C, 100 ILE C, 200100 ILE C, 300100 ILE C	4.62	51.27	3.46	1.29	0.44	103
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.7	51.32	0.34	-0.25	1.35	106
    32	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.65	51.55	1.38	0.26	1.05	105
    33	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.54	51.98	1.38	0.26	1.05	105
    34	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.09	52.73	1.44	0.26	1.39	105
    35	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.83	53.06	1.98	0.51	1.33	104
    36	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.57	53.44	2.85	1.04	1	85
    37	100 ILE C, 104 GLY C, 103 PHE C	3.22	54.36	2.3	0.79	1.29	77
    38	200107 THR C, 100 ILE C, 104 GLY C	1.68	57.86	1.13	0.08	1.72	105
    39	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.47	58.7	0.75	-0.14	2.14	105
    40	200107 THR C, 100 ILE C, 200103 PHE C	1.46	59.86	1.13	0.08	1.72	105
    41	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.85	60.62	0.75	-0.14	2.14	105
    42	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.96	60.76	0.46	-0.41	2.39	102
    43	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.84	61.74	0.68	-0.31	2.14	102
    44	200107 THR C, 101 THR C, 200106 VAL C	1.83	62	1.03	-0.15	1.72	102
    45	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.77	62.65	1.73	0.18	1.33	86
    46	200106 VAL C, 200110 LEU C, 101 THR C	1.24	66.98	2.43	0.5	0.64	86

    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, 104 GLY C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE 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

    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, 100103 PHE C, 300106 VAL C, 300110 LEU C, 100101 THR C

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.4
    Hydrophobicity: -0.01
    Polarity: 6.13
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.25	0.83	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.25	1.89	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.37	5.63	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	3	7.4	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.04	7.97	-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	8.72	-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	8.97	-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	9.43	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.54	11.64	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.67	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	2.9	17.38	2.66	0.68	0.81	95
    13	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.91	18.62	-3.5	-1.1	3.53	84
    14	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.2	20.54	2.66	0.68	0.81	95
    15	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.7	27.63	4.2	1.13	0.13	98
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.19	28.72	3.72	0.91	0.1	98
    17	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	28.91	2.28	0.24	0.03	99
    18	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	29.65	2.28	0.24	0.03	99
    19	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.39	29.9	3.72	0.91	0.1	98
    20	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.2	31.44	3.72	0.91	0.1	98
    21	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	32.54	2.28	0.24	0.03	99
    22	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	34.87	1.8	0.02	0	100
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.15	36.27	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	37.15	-0.2	-0.61	1.33	105
    25	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.24	38.8	1.3	-0.14	0.33	101
    26	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.18	39.92	-0.2	-0.61	1.33	105
    27	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.6	49.65	-0.7	-0.77	1.66	107
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 104 GLY C	4.25	50.28	-0.64	-0.78	2	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.62	50.72	0.34	-0.25	1.35	106
    30	100107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.62	51.27	3.46	1.29	0.44	103
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.7	51.32	0.34	-0.25	1.35	106
    32	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.65	51.55	1.38	0.26	1.05	105
    33	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.54	51.98	1.38	0.26	1.05	105
    34	100107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C, 100104 GLY C	4.09	52.73	1.44	0.26	1.39	105
    35	100107 THR C, 100100 ILE C, 200100 ILE C, 100104 GLY C	3.83	53.06	1.98	0.51	1.33	104
    36	100100 ILE C, 200100 ILE C, 100104 GLY C, 100103 PHE C	3.57	53.44	2.85	1.04	1	85
    37	100100 ILE C, 100104 GLY C, 100103 PHE C	3.22	54.36	2.3	0.79	1.29	77
    38	300107 THR C, 100100 ILE C, 100104 GLY C	1.68	57.86	1.13	0.08	1.72	105
    39	300107 THR C, 100100 ILE C, 100104 GLY C, 300103 PHE C	1.47	58.7	0.75	-0.14	2.14	105
    40	300107 THR C, 100100 ILE C, 300103 PHE C	1.46	59.86	1.13	0.08	1.72	105
    41	300107 THR C, 100100 ILE C, 300103 PHE C, 100101 THR C	1.85	60.62	0.75	-0.14	2.14	105
    42	300107 THR C, 300103 PHE C, 100101 THR C, 100100 ILE C, 300106 VAL C	1.96	60.76	0.46	-0.41	2.39	102
    43	300107 THR C, 300103 PHE C, 100101 THR C, 300106 VAL C	1.84	61.74	0.68	-0.31	2.14	102
    44	300107 THR C, 100101 THR C, 300106 VAL C	1.83	62	1.03	-0.15	1.72	102
    45	300107 THR C, 100101 THR C, 300106 VAL C, 300110 LEU C	1.77	62.65	1.73	0.18	1.33	86
    46	300106 VAL C, 300110 LEU C, 100101 THR C	1.24	66.98	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

55. 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

    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

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.5
    Hydrophobicity: 0.01
    Polarity: 6
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	100124 HIS C, 300122 ARG C, 300124 HIS C	2.25	0.83	-2.7	-0.32	35.66	87
    2	100124 HIS C, 300122 ARG C, 300124 HIS C, 300119 GLN C	2.25	1.89	-2.9	-0.52	27.63	86
    3	300124 HIS C, 300119 GLN C, 100124 HIS C	2.37	5.63	-3.3	-0.19	35.58	88
    4	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C	3	7.4	-3.35	-0.42	27.57	87
    5	300124 HIS C, 300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C	4.04	7.97	-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	8.72	-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	8.97	-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	9.43	-3.26	-0.01	41.99	89
    9	300119 GLN C, 100124 HIS C, 100119 GLN C, 119 GLN C, 200119 GLN C	3.54	11.64	-3.44	-0.83	13.14	85
    10	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.67	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	2.9	17.22	2.66	0.68	0.81	95
    13	300119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.96	17.38	2.66	0.68	0.81	95
    14	300119 GLN C, 100119 GLN C, 119 GLN C, 200119 GLN C	2.91	18.62	-3.5	-1.1	3.53	84
    15	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.2	20.54	2.66	0.68	0.81	95
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.7	27.63	4.2	1.13	0.13	98
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.19	28.72	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	28.91	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	29.65	2.28	0.24	0.03	99
    20	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.39	29.9	3.72	0.91	0.1	98
    21	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.2	31.44	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.15	32.54	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.77	34.87	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.15	36.27	1.3	-0.14	0.33	101
    25	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.21	37.15	-0.2	-0.61	1.33	105
    26	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 300107 THR C	2.24	38.8	1.3	-0.14	0.33	101
    27	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.18	39.92	-0.2	-0.61	1.33	105
    28	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.6	49.65	-0.7	-0.77	1.66	107
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100104 GLY C	4.25	50.28	-0.64	-0.78	2	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.62	50.72	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	51.27	3.46	1.29	0.44	103
    32	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C	4.7	51.32	0.34	-0.25	1.35	106
    33	100107 THR C, 200107 THR C, 300107 THR C, 100100 ILE C, 200100 ILE C	4.65	51.55	1.38	0.26	1.05	105
    34	107 THR C, 200107 THR C, 300107 THR C, 100 ILE C, 300100 ILE C	4.54	51.98	1.38	0.26	1.05	105
    35	107 THR C, 200107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	4.09	52.73	1.44	0.26	1.39	105
    36	107 THR C, 100 ILE C, 300100 ILE C, 104 GLY C	3.83	53.06	1.98	0.51	1.33	104
    37	100 ILE C, 300100 ILE C, 104 GLY C, 103 PHE C	3.57	53.44	2.85	1.04	1	85
    38	100 ILE C, 104 GLY C, 103 PHE C	3.22	54.36	2.3	0.79	1.29	77
    39	200107 THR C, 100 ILE C, 104 GLY C	1.68	57.86	1.13	0.08	1.72	105
    40	200107 THR C, 100 ILE C, 104 GLY C, 200103 PHE C	1.47	58.7	0.75	-0.14	2.14	105
    41	200107 THR C, 100 ILE C, 200103 PHE C	1.46	59.86	1.13	0.08	1.72	105
    42	200107 THR C, 100 ILE C, 200103 PHE C, 101 THR C	1.85	60.62	0.75	-0.14	2.14	105
    43	200107 THR C, 200103 PHE C, 101 THR C, 100 ILE C, 200106 VAL C	1.96	60.76	0.46	-0.41	2.39	102
    44	200107 THR C, 200103 PHE C, 101 THR C, 200106 VAL C	1.84	61.74	0.68	-0.31	2.14	102
    45	200107 THR C, 101 THR C, 200106 VAL C	1.83	62	1.03	-0.15	1.72	102
    46	200107 THR C, 101 THR C, 200106 VAL C, 200110 LEU C	1.77	62.65	1.73	0.18	1.33	86
    47	200106 VAL C, 200110 LEU C, 101 THR C	1.24	66.98	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum

56. 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, 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

    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

    Physicochemical properties of lining side-chains

    Charge: 1 (1-0)
    Hydropathy: 0.4
    Hydrophobicity: -0.01
    Polarity: 5.76
    Mutability: 93
    

    Lining residues

    show all | hide all

    #	Res	Btn	Dist	Hpa	Hpb	Pol	Mut
    1	124 HIS C, 200122 ARG C, 200124 HIS C	2.25	0.85	-2.7	-0.32	35.66	87
    2	124 HIS C, 200122 ARG C, 200124 HIS C, 200119 GLN C	2.26	1.57	-2.9	-0.52	27.63	86
    3	200124 HIS C, 200119 GLN C, 124 HIS C	2.38	5.92	-3.3	-0.19	35.58	88
    4	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C	3.14	7.63	-3.35	-0.42	27.57	87
    5	200124 HIS C, 200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C	4.21	8.11	-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	8.75	-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	9.01	-3.38	-0.56	22.76	86
    8	200124 HIS C, 124 HIS C, 100124 HIS C, 300119 GLN C, 300124 HIS C	4.42	9.35	-3.26	-0.01	41.99	89
    9	200119 GLN C, 124 HIS C, 119 GLN C, 100119 GLN C, 300119 GLN C	3.61	11.5	-3.44	-0.83	13.14	85
    10	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.65	16.93	-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	17.02	-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	17.27	2.66	0.68	0.81	95
    13	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C, 300115 VAL C	3.01	17.47	-1.96	-0.65	2.85	86
    14	200119 GLN C, 119 GLN C, 100119 GLN C, 300119 GLN C	2.92	18.34	-3.5	-1.1	3.53	84
    15	119 GLN C, 200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	2.41	20.17	2.66	0.68	0.81	95
    16	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C	1.7	27.66	4.2	1.13	0.13	98
    17	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 100111 ALA C	2.2	28.75	3.72	0.91	0.1	98
    18	115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.27	28.95	2.28	0.24	0.03	99
    19	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.29	29.43	2.28	0.24	0.03	99
    20	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 111 ALA C	2.36	29.97	3.72	0.91	0.1	98
    21	200115 VAL C, 115 VAL C, 100115 VAL C, 300115 VAL C, 300111 ALA C	2.21	30.82	3.72	0.91	0.1	98
    22	300115 VAL C, 100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	2.44	31.79	2.28	0.24	0.03	99
    23	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C	1.72	35.28	1.8	0.02	0	100
    24	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 107 THR C	2.35	36.03	1.3	-0.14	0.33	101
    25	300111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.2	37.36	-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	1.3	-0.14	0.33	101
    27	100111 ALA C, 111 ALA C, 200111 ALA C, 300111 ALA C, 100107 THR C	2.43	39.49	1.3	-0.14	0.33	101
    28	100111 ALA C, 107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	2.03	40.87	-0.2	-0.61	1.33	105
    29	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C	1.54	49.7	-0.7	-0.77	1.66	107
    30	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 200104 GLY C	4.24	50.33	-0.64	-0.78	2	107
    31	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.53	50.74	0.34	-0.25	1.35	106
    32	300107 THR C, 100 ILE C, 100100 ILE C, 200100 ILE C, 300100 ILE C	4.65	51.28	3.46	1.29	0.44	103
    33	107 THR C, 100107 THR C, 200107 THR C, 300107 THR C, 100 ILE C	4.7	51.32	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	51.41	0.34	-0.25	1.35	106
    35	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.69	51.46	1.38	0.26	1.05	105
    36	107 THR C, 300107 THR C, 100 ILE C, 100100 ILE C, 300100 ILE C	4.62	51.81	2.42	0.78	0.74	104
    37	107 THR C, 100107 THR C, 200107 THR C, 100 ILE C, 200100 ILE C	4.61	52.03	1.38	0.26	1.05	105
    38	100107 THR C, 200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	4	53.01	1.44	0.26	1.39	105
    39	200107 THR C, 200104 GLY C, 100 ILE C, 200100 ILE C	3.86	53.17	1.98	0.51	1.33	104
    40	200104 GLY C, 100 ILE C, 200100 ILE C, 200103 PHE C	3.58	53.58	2.85	1.04	1	85
    41	200104 GLY C, 200100 ILE C, 200103 PHE C	3.19	54.59	2.3	0.79	1.29	77
    42	100107 THR C, 200104 GLY C, 200100 ILE C	1.6	58.31	1.13	0.08	1.72	105
    43	100107 THR C, 200100 ILE C, 100103 PHE C	1.43	60.13	1.13	0.08	1.72	105
    44	100107 THR C, 200100 ILE C, 100103 PHE C, 200101 THR C	1.9	60.7	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	61.01	0.46	-0.41	2.39	102
    46	100107 THR C, 100103 PHE C, 200101 THR C, 100106 VAL C	1.86	61.79	0.68	-0.31	2.14	102
    47	100107 THR C, 200101 THR C, 100106 VAL C	1.83	62.08	1.03	-0.15	1.72	102
    48	100107 THR C, 200101 THR C, 100106 VAL C, 100110 LEU C	1.79	62.76	1.73	0.18	1.33	86
    49	100106 VAL C, 100110 LEU C, 200101 THR C	1.24	67.12	2.43	0.5	0.64	86

    pore with bottle neck

    pore with local minimum