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***  2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000  ***

CA distance fluctuations for 240220090021146876

---  normal mode 13  ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok
largest increasereflargest decrease
ARG 209 0.22 GLY 1 -0.69 GLY 226
ARG 209 0.18 GLU 2 -0.72 GLY 226
LYS 208 0.20 GLU 3 -0.85 GLY 226
LYS 208 0.26 LEU 4 -0.69 GLY 226
ARG 209 0.20 PHE 5 -0.59 GLY 226
ARG 209 0.18 THR 6 -0.68 GLY 226
ARG 209 0.17 GLY 7 -0.57 GLY 226
ARG 209 0.20 VAL 8 -0.45 GLY 226
LYS 208 0.27 VAL 9 -0.43 GLY 226
LYS 208 0.38 PRO 10 -0.35 GLY 226
ARG 209 0.33 ILE 11 -0.24 GLY 226
ARG 209 0.43 LEU 12 -0.19 GLY 226
ARG 209 0.35 VAL 13 -0.10 GLY 226
ARG 209 0.40 GLU 14 -0.07 GLU 166
ARG 116 0.33 LEU 15 -0.10 GLU 166
ARG 116 0.25 ASP 16 -0.11 GLU 166
ASP 184 0.22 GLY 17 -0.11 GLU 166
PRO 205 0.27 ASP 18 -0.09 PRO 69
PRO 205 0.30 VAL 19 -0.12 THR 91
PRO 205 0.33 ASN 20 -0.15 THR 91
PRO 205 0.37 GLY 21 -0.13 GLN 151
PRO 205 0.44 HIS 22 -0.14 HIS 133
PRO 205 0.37 LYS 23 -0.15 GLU 166
PRO 205 0.37 PHE 24 -0.19 GLU 166
ARG 116 0.31 SER 25 -0.20 GLU 166
GLU 14 0.37 VAL 26 -0.19 GLU 166
ARG 209 0.41 SER 27 -0.17 GLU 166
PHE 43 0.33 GLY 28 -0.15 GLU 166
GLU 207 0.39 GLU 29 -0.15 GLU 166
GLU 31 0.28 GLY 30 -0.29 PRO 205
GLY 30 0.28 GLU 31 -0.34 PRO 205
ARG 209 0.16 GLY 32 -0.39 PRO 205
GLY 30 0.14 ASP 33 -0.43 PRO 205
GLY 28 0.13 ALA 34 -0.39 HIS 225
GLY 28 0.11 THR 35 -0.52 ASP 70
ILE 223 0.10 TYR 36 -0.50 PRO 205
ILE 223 0.18 GLY 37 -0.43 PRO 205
ILE 223 0.18 LYS 38 -0.49 PRO 205
ILE 223 0.19 LEU 39 -0.43 PRO 205
ILE 223 0.17 THR 40 -0.47 PRO 205
ILE 223 0.21 LEU 41 -0.34 PRO 205
ILE 223 0.19 LYS 42 -0.22 GLU 166
GLY 28 0.33 PHE 43 -0.26 GLU 166
SER 27 0.38 ILE 44 -0.33 GLU 166
GLU 14 0.35 CYS 45 -0.35 GLU 166
LYS 208 0.42 THR 46 -0.33 GLU 166
PRO 205 0.41 THR 47 -0.32 GLU 166
PRO 205 0.58 GLY 48 -0.41 GLU 166
PRO 205 0.66 LYS 49 -0.42 GLU 166
PRO 205 0.48 LEU 50 -0.34 GLU 166
PRO 205 0.48 PRO 51 -0.21 GLU 166
PRO 205 0.34 VAL 52 -0.21 LYS 208
PRO 205 0.23 PRO 53 -0.41 LYS 208
THR 224 0.20 TRP 54 -0.34 LYS 208
THR 224 0.23 PRO 55 -0.42 LYS 208
THR 224 0.22 THR 56 -0.29 LYS 208
THR 224 0.21 LEU 57 -0.16 LYS 208
THR 224 0.23 VAL 58 -0.19 LYS 208
THR 224 0.25 THR 59 -0.16 ARG 67
ILE 223 0.22 THR 60 -0.12 LEU 214
ILE 223 0.24 PHE 61 -0.12 LEU 214
ILE 223 0.24 VAL 62 -0.17 PRO 205
ILE 223 0.24 GLN 63 -0.21 PRO 205
SER 27 0.18 CYS 64 -0.24 GLY 226
ILE 223 0.17 PHE 65 -0.31 PRO 205
ILE 223 0.24 SER 66 -0.33 PRO 205
ILE 223 0.17 ARG 67 -0.40 PRO 205
ILE 223 0.12 TYR 68 -0.36 PRO 69
ILE 223 0.14 PRO 69 -0.43 PRO 205
ASP 191 0.22 ASP 70 -0.69 HIS 225
ASP 191 0.31 HIS 71 -0.72 HIS 225
ASP 191 0.23 MET 72 -0.38 HIS 225
LYS 150 0.12 LYS 73 -0.56 HIS 225
LYS 150 0.17 ARG 74 -0.55 GLY 226
PRO 190 0.19 HIS 75 -0.29 GLY 226
SER 27 0.13 ASP 76 -0.34 GLY 226
SER 27 0.15 PHE 77 -0.29 GLY 226
SER 27 0.18 PHE 78 -0.28 GLY 226
SER 27 0.18 LYS 79 -0.46 GLY 226
THR 46 0.18 SER 80 -0.55 GLY 226
THR 46 0.21 ALA 81 -0.48 GLY 183
LYS 208 0.25 MET 82 -0.53 GLY 226
LYS 208 0.30 PRO 83 -0.55 GLY 226
LYS 208 0.32 GLU 84 -0.47 GLY 226
THR 46 0.26 GLY 85 -0.36 GLY 226
THR 46 0.23 TYR 86 -0.23 GLY 226
ASP 184 0.25 VAL 87 -0.12 GLY 226
ASP 184 0.18 GLN 88 -0.08 PRO 69
ASP 184 0.25 GLU 89 -0.10 LYS 120
LEU 172 0.20 ARG 90 -0.19 LYS 101
ARG 103 0.21 THR 91 -0.18 ILE 122
GLY 226 0.23 ILE 92 -0.21 ASN 99
GLY 226 0.28 PHE 93 -0.22 GLY 98
GLY 226 0.28 PHE 94 -0.27 LYS 208
GLY 226 0.32 LYS 95 -0.31 LYS 208
GLY 226 0.30 ASP 96 -0.29 LYS 208
ASP 167 0.25 ASP 97 -0.24 LYS 208
GLY 226 0.21 GLY 98 -0.22 PHE 93
LYS 95 0.27 ASN 99 -0.21 TYR 176
LYS 95 0.19 TYR 100 -0.15 THR 91
LYS 95 0.22 LYS 101 -0.19 ARG 90
ASP 184 0.22 THR 102 -0.11 LYS 120
ASP 184 0.25 ARG 103 -0.09 VAL 62
ILE 182 0.22 ALA 104 -0.10 VAL 62
THR 46 0.28 GLU 105 -0.16 GLY 226
ARG 209 0.27 VAL 106 -0.22 GLY 226
LYS 208 0.33 LYS 107 -0.34 GLY 226
LYS 208 0.39 PHE 108 -0.43 GLY 226
LYS 208 0.50 GLU 109 -0.42 GLY 226
LYS 208 0.53 GLY 110 -0.51 GLY 226
LYS 208 0.47 ASP 111 -0.53 GLY 226
LYS 208 0.47 THR 112 -0.40 GLY 226
LYS 208 0.35 LEU 113 -0.33 GLY 226
LYS 208 0.39 VAL 114 -0.25 GLY 226
ARG 209 0.31 ASN 115 -0.15 GLY 226
THR 46 0.34 ARG 116 -0.11 GLY 226
GLU 105 0.24 ILE 117 -0.08 LEU 214
ASP 184 0.25 GLU 118 -0.08 LEU 214
ASP 184 0.22 LEU 119 -0.10 PRO 69
ASP 184 0.20 LYS 120 -0.12 ARG 90
PRO 205 0.19 GLY 121 -0.16 THR 91
PRO 205 0.21 ILE 122 -0.19 TYR 176
PRO 205 0.23 ASP 123 -0.21 TYR 176
PRO 205 0.25 PHE 124 -0.19 PHE 93
PRO 205 0.29 LYS 125 -0.18 PHE 93
PRO 205 0.40 GLU 126 -0.14 LYS 208
PRO 205 0.36 ASP 127 -0.26 LYS 208
GLY 226 0.23 GLY 128 -0.33 LYS 208
GLY 226 0.27 ASN 129 -0.47 LYS 208
GLY 226 0.22 ILE 130 -0.35 LYS 208
PRO 205 0.37 LEU 131 -0.24 LYS 208
PRO 205 0.37 GLY 132 -0.37 LYS 208
TYR 137 0.38 HIS 133 -0.53 LYS 208
GLY 226 0.28 LYS 134 -0.69 LYS 208
GLY 226 0.28 LEU 135 -0.76 LYS 208
GLY 226 0.27 GLU 136 -0.94 LYS 208
HIS 133 0.38 TYR 137 -0.80 LYS 208
HIS 133 0.26 ASN 138 -0.65 LYS 208
THR 224 0.28 TYR 139 -0.51 LYS 208
THR 224 0.34 ASN 140 -0.47 LYS 208
THR 224 0.38 SER 141 -0.35 LYS 208
THR 224 0.43 HIS 142 -0.28 LYS 208
THR 224 0.47 ASN 143 -0.23 LYS 95
THR 224 0.37 VAL 144 -0.23 PHE 159
ILE 223 0.42 TYR 145 -0.17 ASP 123
ILE 223 0.36 ILE 146 -0.15 ASP 123
ILE 223 0.30 MET 147 -0.17 ASP 123
HIS 225 0.21 ALA 148 -0.15 ASP 123
HIS 225 0.22 ASP 149 -0.18 ASP 123
HIS 71 0.22 LYS 150 -0.16 ASP 123
ASP 184 0.22 GLN 151 -0.16 ASP 123
ASP 184 0.29 LYS 152 -0.12 ASP 123
ASP 184 0.22 ASN 153 -0.14 GLY 226
ASP 184 0.16 GLY 154 -0.10 ASP 123
ILE 223 0.20 ILE 155 -0.14 ASP 123
ILE 223 0.26 LYS 156 -0.19 ASP 123
ILE 223 0.28 VAL 157 -0.18 ASP 123
GLY 226 0.36 ASN 158 -0.21 ASP 123
GLY 226 0.39 PHE 159 -0.23 VAL 144
GLY 226 0.42 LYS 160 -0.28 LYS 208
GLY 226 0.37 ILE 161 -0.35 LYS 208
GLY 226 0.41 ARG 162 -0.46 LYS 208
GLY 226 0.35 HIS 163 -0.57 LYS 208
GLY 226 0.37 ASN 164 -0.73 LYS 208
GLY 226 0.37 ILE 165 -0.84 LYS 208
GLY 226 0.35 GLU 166 -1.07 LYS 208
GLY 226 0.40 ASP 167 -1.01 LYS 208
GLY 226 0.45 GLY 168 -0.95 LYS 208
GLY 226 0.47 SER 169 -0.77 LYS 208
GLY 226 0.46 VAL 170 -0.65 LYS 208
GLY 226 0.38 GLN 171 -0.51 LYS 208
GLY 226 0.39 LEU 172 -0.42 LYS 208
GLY 226 0.34 ALA 173 -0.31 LYS 208
GLY 226 0.36 ASP 174 -0.24 LYS 208
GLY 226 0.29 HIS 175 -0.21 ASN 99
GLY 226 0.27 TYR 176 -0.21 ASP 123
ILE 223 0.22 GLN 177 -0.17 ASP 123
ASP 184 0.20 GLN 178 -0.14 ASP 123
ILE 223 0.18 ASN 179 -0.08 ASP 123
ASP 184 0.28 THR 180 -0.12 GLY 226
GLY 185 0.26 PRO 181 -0.28 GLY 226
GLY 185 0.30 ILE 182 -0.32 GLY 226
THR 46 0.27 GLY 183 -0.54 GLY 226
LYS 152 0.29 ASP 184 -0.55 GLY 226
ILE 182 0.30 GLY 185 -0.70 GLY 226
THR 46 0.23 PRO 186 -0.66 GLY 226
THR 46 0.18 VAL 187 -0.48 GLY 226
THR 46 0.14 LEU 188 -0.44 GLY 226
ASP 70 0.16 LEU 189 -0.22 PRO 186
HIS 71 0.22 PRO 190 -0.21 PRO 186
HIS 71 0.31 ASP 191 -0.22 PRO 186
HIS 225 0.42 ASN 192 -0.16 PRO 205
ILE 223 0.60 HIS 193 -0.18 PRO 205
ILE 223 0.52 TYR 194 -0.19 PRO 205
ILE 223 0.42 LEU 195 -0.24 PRO 205
THR 224 0.43 SER 196 -0.28 PRO 205
THR 224 0.35 THR 197 -0.31 PRO 205
THR 224 0.32 GLN 198 -0.40 PRO 205
THR 224 0.25 VAL 199 -0.40 PRO 205
THR 224 0.21 ALA 200 -0.50 PRO 205
HIS 133 0.18 LEU 201 -0.43 LYS 208
HIS 133 0.23 SER 202 -0.60 LYS 203
LYS 49 0.29 LYS 203 -0.60 SER 202
LYS 49 0.29 ASP 204 -0.35 GLY 168
LYS 49 0.66 PRO 205 -0.52 LEU 215
ASP 210 0.33 ASN 206 -0.47 GLY 168
GLY 110 0.39 GLU 207 -0.67 GLU 166
GLY 110 0.53 LYS 208 -1.07 GLU 166
LEU 12 0.43 ARG 209 -0.67 GLU 166
PRO 205 0.57 ASP 210 -0.69 GLU 136
PRO 205 0.24 HIS 211 -0.47 GLU 136
PRO 51 0.16 MET 212 -0.37 GLU 136
THR 224 0.14 VAL 213 -0.27 PRO 205
THR 224 0.16 LEU 214 -0.33 PRO 205
THR 224 0.18 LEU 215 -0.52 PRO 205
THR 224 0.21 GLU 216 -0.43 PRO 205
THR 224 0.24 PHE 217 -0.46 PRO 205
ILE 223 0.29 VAL 218 -0.36 PRO 205
ILE 223 0.28 THR 219 -0.35 PRO 205
ILE 223 0.37 ALA 220 -0.29 PRO 205
ILE 223 0.52 ALA 221 -0.24 PRO 205
THR 224 0.59 GLY 222 -0.18 ARG 74
HIS 193 0.60 ILE 223 -0.23 ARG 74
GLY 222 0.59 THR 224 -0.44 ARG 74
ASN 192 0.42 HIS 225 -0.72 HIS 71
SER 169 0.47 GLY 226 -0.85 GLU 3

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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: April 25th, 2023.