------------------------------------------------ PDB || UniProt -------------------------||--------------------- PDB Chn SeqNo Res ResNo||Accession Res Number ------------------------------------------------ 3s5p A 1 PRO -2 3s5p A 2 GLY -1 3s5p A 3 SER 0 3s5p A 4 MET 1 A8B2K2 M 1 3s5p A 5 LYS 2 A8B2K2 K 2 3s5p A 6 VAL 3 A8B2K2 V 3 3s5p A 7 ALA 4 A8B2K2 A 4 3s5p A 8 PHE 5 A8B2K2 F 5 3s5p A 9 ALA 6 A8B2K2 A 6 3s5p A 10 SER 7 A8B2K2 S 7 3s5p A 11 ASP 8 A8B2K2 D 8 3s5p A 12 HIS 9 A8B2K2 H 9 3s5p A 13 GLY 10 A8B2K2 G 10 3s5p A 14 GLY 11 A8B2K2 G 11 3s5p A 15 ARG 12 A8B2K2 R 12 3s5p A 16 ASP 13 A8B2K2 D 13 3s5p A 17 LEU 14 A8B2K2 L 14 3s5p A 18 ARG 15 A8B2K2 R 15 3s5p A 19 MET 16 A8B2K2 M 16 3s5p A 20 PHE 17 A8B2K2 F 17 3s5p A 21 LEU 18 A8B2K2 L 18 3s5p A 22 GLN 19 A8B2K2 Q 19 3s5p A 23 GLN 20 A8B2K2 Q 20 3s5p A 24 ARG 21 A8B2K2 R 21 3s5p A 25 ALA 22 A8B2K2 A 22 3s5p A 26 SER 23 A8B2K2 S 23 3s5p A 27 ALA 24 A8B2K2 A 24 3s5p A 28 HIS 25 A8B2K2 H 25 3s5p A 29 GLY 26 A8B2K2 G 26 3s5p A 30 TYR 27 A8B2K2 Y 27 3s5p A 31 GLU 28 A8B2K2 E 28 3s5p A 32 VAL 29 A8B2K2 V 29 3s5p A 33 MET 30 A8B2K2 M 30 3s5p A 34 ASP 31 A8B2K2 D 31 3s5p A 35 LEU 32 A8B2K2 L 32 3s5p A 36 GLY 33 A8B2K2 G 33 3s5p A 37 THR 34 A8B2K2 T 34 3s5p A 38 PRO 43 A8B2K2 P 43 3s5p A 39 ASP 44 A8B2K2 D 44 3s5p A 40 PHE 45 A8B2K2 F 45 3s5p A 41 ALA 46 A8B2K2 A 46 3s5p A 42 LYS 47 A8B2K2 K 47 3s5p A 43 ILE 48 A8B2K2 I 48 3s5p A 44 GLY 49 A8B2K2 G 49 3s5p A 45 CYS 50 A8B2K2 C 50 3s5p A 46 GLU 51 A8B2K2 E 51 3s5p A 47 ALA 52 A8B2K2 A 52 3s5p A 48 VAL 53 A8B2K2 V 53 3s5p A 49 THR 54 A8B2K2 T 54 3s5p A 50 SER 55 A8B2K2 S 55 3s5p A 51 GLY 56 A8B2K2 G 56 3s5p A 52 ARG 57 A8B2K2 R 57 3s5p A 53 ALA 58 A8B2K2 A 58 3s5p A 54 ASP 59 A8B2K2 D 59 3s5p A 55 CYS 60 A8B2K2 C 60 3s5p A 56 CYS 61 A8B2K2 C 61 3s5p A 57 ILE 62 A8B2K2 I 62 3s5p A 58 LEU 63 A8B2K2 L 63 3s5p A 59 VAL 64 A8B2K2 V 64 3s5p A 60 CYS 65 A8B2K2 C 65 3s5p A 61 GLY 66 A8B2K2 G 66 3s5p A 62 THR 67 A8B2K2 T 67 3s5p A 63 GLY 68 A8B2K2 G 68 3s5p A 64 ILE 69 A8B2K2 I 69 3s5p A 65 GLY 70 A8B2K2 G 70 3s5p A 66 ILE 71 A8B2K2 I 71 3s5p A 67 SER 72 A8B2K2 S 72 3s5p A 68 ILE 73 A8B2K2 I 73 3s5p A 69 ALA 74 A8B2K2 A 74 3s5p A 70 ALA 75 A8B2K2 A 75 3s5p A 71 ASN 76 A8B2K2 N 76 3s5p A 72 LYS 77 A8B2K2 K 77 3s5p A 73 MET 78 A8B2K2 M 78 3s5p A 74 LYS 79 A8B2K2 K 79 3s5p A 75 GLY 80 A8B2K2 G 80 3s5p A 76 ILE 81 A8B2K2 I 81 3s5p A 77 ARG 82 A8B2K2 R 82 3s5p A 78 CYS 83 A8B2K2 C 83 3s5p A 79 ALA 84 A8B2K2 A 84 3s5p A 80 LEU 85 A8B2K2 L 85 3s5p A 81 CYS 86 A8B2K2 C 86 3s5p A 82 SER 87 A8B2K2 S 87 3s5p A 83 THR 88 A8B2K2 T 88 3s5p A 84 GLU 89 A8B2K2 E 89 3s5p A 85 TYR 90 A8B2K2 Y 90 3s5p A 86 ASP 91 A8B2K2 D 91 3s5p A 87 ALA 92 A8B2K2 A 92 3s5p A 88 GLU 93 A8B2K2 E 93 3s5p A 89 MET 94 A8B2K2 M 94 3s5p A 90 ALA 95 A8B2K2 A 95 3s5p A 91 ARG 96 A8B2K2 R 96 3s5p A 92 LYS 97 A8B2K2 K 97 3s5p A 93 HIS 98 A8B2K2 H 98 3s5p A 94 ASN 99 A8B2K2 N 99 3s5p A 95 ASN 100 A8B2K2 N 100 3s5p A 96 ALA 101 A8B2K2 A 101 3s5p A 97 ASN 102 A8B2K2 N 102 3s5p A 98 ALA 103 A8B2K2 A 103 3s5p A 99 LEU 104 A8B2K2 L 104 3s5p A 100 ALA 105 A8B2K2 A 105 3s5p A 101 LEU 106 A8B2K2 L 106 3s5p A 102 GLY 107 A8B2K2 G 107 3s5p A 103 GLY 108 A8B2K2 G 108 3s5p A 104 ARG 109 A8B2K2 R 109 3s5p A 105 THR 110 A8B2K2 T 110 3s5p A 106 THR 111 A8B2K2 T 111 3s5p A 107 GLY 112 A8B2K2 G 112 3s5p A 108 PRO 113 A8B2K2 P 113 3s5p A 109 GLU 114 A8B2K2 E 114 3s5p A 110 VAL 115 A8B2K2 V 115 3s5p A 111 ALA 116 A8B2K2 A 116 3s5p A 112 ALA 117 A8B2K2 A 117 3s5p A 113 SER 118 A8B2K2 S 118 3s5p A 114 ILE 119 A8B2K2 I 119 3s5p A 115 LEU 120 A8B2K2 L 120 3s5p A 116 SER 121 A8B2K2 S 121 3s5p A 117 ARG 122 A8B2K2 R 122 3s5p A 118 PHE 123 A8B2K2 F 123 3s5p A 119 LEU 124 A8B2K2 L 124 3s5p A 120 SER 125 A8B2K2 S 125 3s5p A 121 THR 126 A8B2K2 T 126 3s5p A 122 ASN 127 A8B2K2 N 127 3s5p A 123 PHE 128 A8B2K2 F 128 3s5p A 124 GLU 129 A8B2K2 E 129 3s5p A 125 GLY 130 A8B2K2 G 130 3s5p A 126 GLY 131 A8B2K2 G 131 3s5p A 127 ARG 132 A8B2K2 R 132 3s5p A 128 HIS 133 A8B2K2 H 133 3s5p A 129 ALA 134 A8B2K2 A 134 3s5p A 130 ALA 135 A8B2K2 A 135 3s5p A 131 ARG 136 A8B2K2 R 136 3s5p A 132 ILE 137 A8B2K2 I 137 3s5p A 133 ALA 138 A8B2K2 A 138 3s5p A 134 LYS 139 A8B2K2 K 139
A total of 134 residues were displayed (of which 131 were aligned with UniProt) for 1 chains.