NMR Restraints Grid |
Result table
image | mrblock_id | pdb_id | cing | stage | position | program | type |
20118 | 2f3j | cing | 1-original | 1 | unknown | sequence |
; NMR constraints data for REF2-I(1-155), ; entry ID RCSB035407, PDB id 2F3J ;Authors: 'Golovanov, A.P.' 'Hautbergue, G.M.' 'Wilson, S.A.' 'Lian, L.Y.' ; ; Format of constraints is that of ARIA/CNS which were used for ; NMR structure calculation. ; ; The polypeptide sequence of REF2-I(1-155) used in the study contains ; additional 14-residue N-terminal T7-tag, and C-terminal ; LEHHHHHH tag. The N-terminal tag was omitted in PDB ; deposition as it was unstructured, however, it was ; partially assigned and was included during NMR structure ; calculations. Therefore note that the numbering ; of REF2-I amino acid residues in the PDB file (PDB id 2F3J, RCSB035407) ; differs from the one used here. ; ; The actual sequence used for the structure calculation: MASMTGGQQMGRDPMADKMDMSLDDIIKLNRNQRRVNRGG GPRRNRPAIARGGRNRPAPYSRPKPLPDKWQHDLFDSGCG GGEGVETGAKLLVSNLDFGVSDADIQELFAEFGTLKKAAV DYDRSGRSLGTADVHFERRADALKAMKQYKGVPLDGRPMD IQLVASQIDLEH ; 1 1 MET 2 2 ALA 3 3 SER 4 4 MET 5 5 THR 6 6 GLY 7 7 GLY 8 8 GLN 9 9 GLN 10 10 MET 11 11 GLY 12 12 ARG 13 13 ASP 14 14 PRO 15 15 MET 16 16 ALA 17 17 ASP 18 18 LYS 19 19 MET 20 20 ASP 21 21 MET 22 22 SER 23 23 LEU 24 24 ASP 25 25 ASP 26 26 ILE 27 27 ILE 28 28 LYS 29 29 LEU 30 30 ASN 31 31 ARG 32 32 ASN 33 33 GLN 34 34 ARG 35 35 ARG 36 36 VAL 37 37 ASN 38 38 ARG 39 39 GLY 40 40 GLY 41 41 GLY 42 42 PRO 43 43 ARG 44 44 ARG 45 45 ASN 46 46 ARG 47 47 PRO 48 48 ALA 49 49 ILE 50 50 ALA 51 51 ARG 52 52 GLY 53 53 GLY 54 54 ARG 55 55 ASN 56 56 ARG 57 57 PRO 58 58 ALA 59 59 PRO 60 60 TYR 61 61 SER 62 62 ARG 63 63 PRO 64 64 LYS 65 65 PRO 66 66 LEU 67 67 PRO 68 68 ASP 69 69 LYS 70 70 TRP 71 71 GLN 72 72 HIS 73 73 ASP 74 74 LEU 75 75 PHE 76 76 ASP 77 77 SER 78 78 GLY 79 79 CYS 80 80 GLY 81 81 GLY 82 82 GLY 83 83 GLU 84 84 GLY 85 85 VAL 86 86 GLU 87 87 THR 88 88 GLY 89 89 ALA 90 90 LYS 91 91 LEU 92 92 LEU 93 93 VAL 94 94 SER 95 95 ASN 96 96 LEU 97 97 ASP 98 98 PHE 99 99 GLY 100 100 VAL 101 101 SER 102 102 ASP 103 103 ALA 104 104 ASP 105 105 ILE 106 106 GLN 107 107 GLU 108 108 LEU 109 109 PHE 110 110 ALA 111 111 GLU 112 112 PHE 113 113 GLY 114 114 THR 115 115 LEU 116 116 LYS 117 117 LYS 118 118 ALA 119 119 ALA 120 120 VAL 121 121 ASP 122 122 TYR 123 123 ASP 124 124 ARG 125 125 SER 126 126 GLY 127 127 ARG 128 128 SER 129 129 LEU 130 130 GLY 131 131 THR 132 132 ALA 133 133 ASP 134 134 VAL 135 135 HIS 136 136 PHE 137 137 GLU 138 138 ARG 139 139 ARG 140 140 ALA 141 141 ASP 142 142 ALA 143 143 LEU 144 144 LYS 145 145 ALA 146 146 MET 147 147 LYS 148 148 GLN 149 149 TYR 150 150 LYS 151 151 GLY 152 152 VAL 153 153 PRO 154 154 LEU 155 155 ASP 156 156 GLY 157 157 ARG 158 158 PRO 159 159 MET 160 160 ASP 161 161 ILE 162 162 GLN 163 163 LEU 164 164 VAL 165 165 ALA 166 166 SER 167 167 GLN 168 168 ILE 169 169 ASP 170 170 LEU 171 171 GLU 172 172 HIS
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