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***  444  ***

CA distance fluctuations for 240323171349264498

---  normal mode 11  ---

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
SER 167 0.31 GLY 5 -0.27 PRO 182
SER 167 0.29 ILE 6 -0.28 PRO 182
SER 167 0.32 ARG 7 -0.25 ALA 211
SER 167 0.30 ALA 8 -0.27 ALA 211
SER 167 0.30 ALA 9 -0.25 ALA 211
SER 167 0.32 THR 10 -0.21 ALA 211
SER 167 0.26 SER 11 -0.23 ALA 211
SER 167 0.29 GLN 12 -0.17 ALA 211
SER 167 0.29 GLU 13 -0.18 ALA 211
SER 167 0.22 ILE 14 -0.23 ALA 211
SER 167 0.18 ASN 15 -0.19 PRO 210
SER 167 0.18 GLU 16 -0.14 PRO 210
SER 167 0.15 LEU 17 -0.16 PRO 210
SER 228 0.16 THR 18 -0.19 PRO 210
HIS 42 0.15 TYR 19 -0.15 PRO 210
SER 228 0.12 TYR 20 -0.12 PRO 210
SER 24 0.13 THR 21 -0.19 GLY 175
SER 228 0.13 THR 22 -0.16 PRO 210
PRO 100 0.15 LEU 23 -0.11 ALA 67
THR 21 0.13 SER 24 -0.11 PRO 210
SER 228 0.14 ALA 25 -0.18 LEU 92
LEU 58 0.16 ASN 26 -0.14 ALA 67
LEU 58 0.16 SER 27 -0.21 ALA 67
LEU 58 0.19 TYR 28 -0.17 ALA 67
LEU 58 0.20 CYS 29 -0.16 ALA 67
LEU 58 0.29 ARG 30 -0.20 ILE 52
LEU 58 0.27 THR 31 -0.19 LYS 50
LEU 58 0.24 VAL 32 -0.23 LYS 50
LEU 58 0.25 ILE 33 -0.25 ILE 52
THR 57 0.34 PRO 34 -0.30 ILE 52
LEU 58 0.31 GLY 35 -0.22 GLN 132
TRP 55 0.31 ALA 36 -0.28 LYS 50
PRO 100 0.26 THR 37 -0.22 LYS 50
PRO 100 0.22 TRP 38 -0.14 LYS 50
LEU 58 0.21 ASP 39 -0.11 LYS 50
LEU 58 0.18 CYS 40 -0.16 LEU 92
LEU 58 0.15 ILE 41 -0.19 LEU 258
TYR 19 0.15 HIS 42 -0.19 ASN 264
LEU 58 0.16 CYS 43 -0.16 ASN 264
PRO 100 0.17 ASP 44 -0.19 ILE 263
PRO 100 0.15 ALA 45 -0.19 ILE 263
PRO 100 0.21 THR 46 -0.13 ILE 263
PRO 100 0.24 GLU 47 -0.14 ILE 263
PRO 100 0.27 ASP 48 -0.11 ILE 263
PRO 100 0.30 LEU 49 -0.14 ALA 36
PRO 100 0.35 LYS 50 -0.28 ALA 36
PRO 100 0.34 ILE 51 -0.26 ALA 36
PRO 100 0.42 ILE 52 -0.30 PRO 34
PRO 100 0.39 LYS 53 -0.33 GLN 129
PRO 100 0.32 THR 54 -0.25 ASP 128
ALA 36 0.31 TRP 55 -0.27 ASP 128
THR 57 0.39 SER 56 -0.28 SER 84
SER 56 0.39 THR 57 -0.41 ASN 120
PRO 34 0.34 LEU 58 -0.40 ASN 120
PRO 34 0.24 ILE 59 -0.31 ASN 120
THR 93 0.20 TYR 60 -0.24 GLU 162
TYR 60 0.17 ASP 61 -0.25 GLU 162
PRO 34 0.19 THR 62 -0.25 GLU 162
SER 114 0.20 ASN 63 -0.22 GLU 162
TYR 115 0.25 ALA 64 -0.23 GLU 162
PRO 100 0.33 MET 65 -0.17 ILE 33
PRO 100 0.40 VAL 66 -0.20 GLN 129
PRO 100 0.37 ALA 67 -0.23 ILE 33
PRO 100 0.38 ARG 68 -0.20 ALA 36
PRO 100 0.31 GLY 69 -0.15 ALA 36
PRO 101 0.33 ASP 70 -0.16 ALA 36
PRO 101 0.27 SER 71 -0.10 ALA 36
PRO 101 0.25 GLU 72 -0.09 ALA 36
PRO 101 0.32 LYS 73 -0.13 ALA 36
PRO 101 0.33 THR 74 -0.13 PRO 34
PRO 101 0.39 ILE 75 -0.16 PRO 34
PRO 100 0.33 TYR 76 -0.12 SER 27
PRO 100 0.32 ILE 77 -0.15 LEU 164
PRO 100 0.23 VAL 78 -0.13 GLU 162
PRO 100 0.15 PHE 79 -0.18 GLU 162
HIS 143 0.13 ARG 80 -0.15 GLU 162
GLN 174 0.16 GLY 81 -0.18 LEU 267
GLY 175 0.21 SER 82 -0.22 LEU 267
LEU 258 0.30 SER 83 -0.20 SER 56
VAL 254 0.27 SER 84 -0.28 SER 56
VAL 205 0.28 ILE 85 -0.21 SER 56
PRO 209 0.22 ARG 86 -0.19 GLU 162
PRO 209 0.22 ASN 87 -0.15 GLU 162
PRO 209 0.30 TRP 88 -0.25 LEU 267
PRO 209 0.29 ILE 89 -0.20 LEU 267
PRO 209 0.19 ALA 90 -0.21 GLY 110
PRO 209 0.30 ASP 91 -0.33 LEU 267
PRO 209 0.34 LEU 92 -0.35 LEU 267
GLU 117 0.25 THR 93 -0.43 PRO 250
GLY 116 0.25 PHE 94 -0.57 PRO 250
ASN 120 0.31 VAL 95 -0.64 PRO 250
ASN 120 0.36 PRO 96 -0.62 PRO 250
ASN 120 0.46 VAL 97 -0.53 PRO 250
ASN 120 0.52 SER 98 -0.47 PRO 250
LEU 127 0.49 TYR 99 -0.40 PRO 250
LEU 127 0.66 PRO 100 -0.34 PRO 250
ARG 160 0.78 PRO 101 -0.27 PRO 250
GLU 161 0.67 VAL 102 -0.31 PRO 250
GLU 161 0.65 SER 103 -0.39 PRO 250
GLU 161 0.56 GLY 104 -0.46 PRO 250
GLU 161 0.50 THR 105 -0.44 PRO 250
LEU 127 0.39 LYS 106 -0.51 PRO 250
ASN 120 0.35 VAL 107 -0.46 PRO 250
GLN 119 0.29 HIS 108 -0.48 PRO 250
GLY 116 0.36 LYS 109 -0.42 PRO 250
GLU 117 0.25 GLY 110 -0.32 PRO 250
GLN 119 0.21 PHE 111 -0.26 PRO 250
GLN 119 0.43 LEU 112 -0.27 PRO 250
GLU 117 0.41 ASP 113 -0.23 PRO 250
TRP 55 0.24 SER 114 -0.19 ASP 156
LEU 112 0.30 TYR 115 -0.21 ASP 156
LEU 112 0.40 GLY 116 -0.28 ASP 156
ASP 113 0.41 GLU 117 -0.34 GLN 119
LEU 112 0.32 VAL 118 -0.41 GLN 119
PRO 100 0.51 GLN 119 -0.41 VAL 118
PRO 100 0.65 ASN 120 -0.41 THR 57
PRO 100 0.53 GLU 121 -0.40 THR 57
PRO 100 0.50 LEU 122 -0.34 GLU 162
PRO 100 0.65 VAL 123 -0.41 GLU 162
PRO 100 0.64 ALA 124 -0.40 GLU 162
PRO 100 0.57 THR 125 -0.26 THR 57
PRO 100 0.56 VAL 126 -0.25 GLY 163
PRO 101 0.69 LEU 127 -0.26 THR 57
PRO 101 0.60 ASP 128 -0.32 LYS 53
PRO 101 0.54 GLN 129 -0.33 LYS 53
PRO 101 0.57 PHE 130 -0.23 LYS 53
PRO 101 0.64 LYS 131 -0.25 LYS 53
PRO 101 0.53 GLN 132 -0.29 LYS 53
PRO 101 0.49 TYR 133 -0.23 LYS 53
PRO 101 0.51 PRO 134 -0.21 LYS 53
PRO 101 0.40 SER 135 -0.17 LYS 53
PRO 101 0.38 TYR 136 -0.16 LYS 53
PRO 101 0.33 LYS 137 -0.13 THR 57
PRO 101 0.35 VAL 138 -0.15 ILE 77
PRO 100 0.25 ALA 139 -0.08 THR 57
PRO 100 0.24 VAL 140 -0.10 LEU 169
PRO 100 0.15 THR 141 -0.07 GLU 162
ARG 80 0.10 GLY 142 -0.08 GLU 162
SER 83 0.17 HIS 143 -0.16 PHE 94
SER 82 0.21 SER 144 -0.26 PHE 94
ASN 87 0.14 LEU 145 -0.19 LEU 267
ASN 63 0.11 GLY 146 -0.12 GLU 162
TRP 88 0.11 GLY 147 -0.09 LEU 267
TRP 88 0.12 ALA 148 -0.14 PRO 250
GLY 214 0.18 THR 149 -0.13 SER 165
GLY 214 0.15 ALA 150 -0.14 SER 165
GLY 214 0.18 LEU 151 -0.12 SER 190
CYS 153 0.31 LEU 152 -0.16 THR 191
PRO 100 0.33 CYS 153 -0.25 GLU 117
ILE 75 0.26 ALA 154 -0.22 SER 165
LEU 127 0.33 LEU 155 -0.25 GLU 117
PRO 100 0.47 ASP 156 -0.33 GLU 117
PRO 101 0.53 LEU 157 -0.33 GLU 117
VAL 102 0.41 TYR 158 -0.28 GLU 117
VAL 102 0.57 GLN 159 -0.31 GLU 117
PRO 101 0.78 ARG 160 -0.31 GLU 117
VAL 102 0.67 GLU 161 -0.31 GLU 117
PRO 101 0.57 GLU 162 -0.41 VAL 123
SER 103 0.45 GLY 163 -0.35 ALA 124
VAL 102 0.41 LEU 164 -0.33 VAL 123
PRO 134 0.30 SER 165 -0.29 GLU 117
THR 236 0.32 SER 166 -0.23 GLU 117
THR 236 0.33 SER 167 -0.21 VAL 123
THR 10 0.27 ASN 168 -0.20 VAL 123
PRO 101 0.25 LEU 169 -0.18 GLU 117
GLU 13 0.22 PHE 170 -0.13 GLU 117
LEU 155 0.17 LEU 171 -0.08 PRO 194
VAL 234 0.11 TYR 172 -0.07 VAL 189
SER 83 0.13 THR 173 -0.09 PHE 94
SER 83 0.19 GLN 174 -0.19 PRO 210
SER 83 0.22 GLY 175 -0.23 PHE 94
TRP 88 0.21 GLN 176 -0.20 VAL 179
TRP 88 0.28 PRO 177 -0.25 HIS 108
TRP 88 0.23 ARG 178 -0.32 VAL 179
LEU 127 0.20 VAL 179 -0.35 PRO 250
LEU 127 0.28 GLY 180 -0.44 PRO 250
GLY 214 0.35 ASN 181 -0.53 PRO 250
GLY 214 0.34 PRO 182 -0.48 SER 242
GLU 161 0.39 ALA 183 -0.38 PRO 250
GLU 161 0.37 PHE 184 -0.34 PRO 250
GLU 161 0.27 ALA 185 -0.25 PRO 250
GLU 161 0.30 ASN 186 -0.21 SER 103
GLU 161 0.36 TYR 187 -0.19 VAL 102
GLU 161 0.27 VAL 188 -0.14 ASP 113
PRO 134 0.22 VAL 189 -0.12 ASP 113
PRO 134 0.26 SER 190 -0.17 GLU 117
PRO 134 0.30 THR 191 -0.22 GLU 117
THR 236 0.31 GLY 192 -0.19 GLU 117
THR 236 0.27 ILE 193 -0.17 GLU 117
THR 236 0.34 PRO 194 -0.13 GLU 117
PRO 194 0.20 TYR 195 -0.08 VAL 189
GLU 221 0.19 ARG 196 -0.10 ALA 183
PRO 194 0.16 ARG 197 -0.15 PRO 182
SER 83 0.18 THR 198 -0.20 ALA 211
SER 83 0.21 VAL 199 -0.33 ALA 211
SER 83 0.22 ASN 200 -0.38 PRO 210
SER 83 0.20 GLU 201 -0.49 PRO 210
SER 83 0.19 ARG 202 -0.62 PRO 210
ILE 85 0.23 ASP 203 -0.48 PRO 210
ILE 85 0.23 ILE 204 -0.59 PRO 210
ILE 85 0.28 VAL 205 -0.40 PHE 94
TRP 88 0.24 PRO 206 -0.32 PRO 210
TRP 88 0.22 HIS 207 -0.62 PRO 210
TRP 88 0.22 LEU 208 -0.75 PRO 209
LEU 92 0.34 PRO 209 -0.75 LEU 208
LEU 92 0.27 PRO 210 -1.04 PRO 250
LEU 92 0.27 ALA 211 -0.94 VAL 249
GLU 161 0.26 ALA 212 -1.12 PRO 250
GLU 161 0.25 PHE 213 -0.97 PRO 250
ASN 181 0.35 GLY 214 -0.78 PRO 250
LEU 92 0.24 PHE 215 -0.62 PRO 250
GLU 161 0.23 LEU 216 -0.46 ASN 246
TRP 88 0.19 HIS 217 -0.28 ASN 181
PRO 134 0.19 ALA 218 -0.20 ALA 183
ILE 193 0.17 GLY 219 -0.17 ALA 183
PRO 194 0.29 SER 220 -0.17 PRO 182
PRO 194 0.25 GLU 221 -0.28 PRO 182
PRO 194 0.22 TYR 222 -0.26 ALA 211
PRO 194 0.19 TRP 223 -0.40 ALA 211
SER 167 0.18 ILE 224 -0.37 ALA 211
SER 167 0.17 THR 225 -0.47 ALA 212
SER 167 0.17 ASP 226 -0.43 ALA 212
SER 83 0.16 ASN 227 -0.38 ALA 212
ILE 263 0.20 SER 228 -0.36 ALA 212
SER 167 0.19 PRO 229 -0.33 ALA 212
SER 167 0.19 GLU 230 -0.32 ALA 212
SER 167 0.22 THR 231 -0.34 ALA 212
SER 167 0.23 VAL 232 -0.33 ALA 211
SER 167 0.24 GLN 233 -0.34 ALA 211
SER 167 0.28 VAL 234 -0.28 ALA 211
PRO 194 0.27 CYS 235 -0.31 PRO 182
PRO 194 0.34 THR 236 -0.23 PRO 182
GLY 192 0.25 SER 237 -0.24 PRO 182
GLY 192 0.28 ASP 238 -0.21 ALA 183
GLY 192 0.21 LEU 239 -0.29 ALA 183
TRP 88 0.19 GLU 240 -0.38 PRO 182
PRO 194 0.19 THR 241 -0.48 PRO 182
ILE 85 0.17 SER 242 -0.52 ALA 211
SER 167 0.21 ASP 243 -0.47 ALA 212
PRO 194 0.20 CYS 244 -0.51 ALA 211
ILE 85 0.19 SER 245 -0.59 ALA 211
ILE 85 0.19 ASN 246 -0.79 ALA 211
SER 167 0.16 SER 247 -0.79 ALA 212
ILE 85 0.16 ILE 248 -0.80 ALA 212
ILE 85 0.14 VAL 249 -1.04 ALA 212
ILE 248 0.10 PRO 250 -1.12 ALA 212
SER 84 0.13 PHE 251 -0.86 ALA 212
ILE 85 0.18 THR 252 -0.75 PRO 210
ILE 85 0.22 SER 253 -0.53 PRO 210
SER 84 0.27 VAL 254 -0.41 PRO 210
SER 83 0.26 LEU 255 -0.37 PRO 210
SER 83 0.25 ASP 256 -0.41 PRO 210
SER 83 0.27 HIS 257 -0.37 PRO 210
SER 83 0.30 LEU 258 -0.29 PRO 210
SER 83 0.23 SER 259 -0.30 PRO 210
SER 83 0.20 TYR 260 -0.28 PRO 210
SER 83 0.17 PHE 261 -0.27 PRO 210
ILE 263 0.22 GLY 262 -0.28 PRO 210
GLY 262 0.22 ILE 263 -0.26 PRO 210
GLY 262 0.18 ASN 264 -0.27 PRO 210
SER 83 0.19 THR 265 -0.24 PHE 94
SER 83 0.25 GLY 266 -0.30 LEU 92
GLY 262 0.16 LEU 267 -0.35 LEU 92
SER 228 0.16 CYS 268 -0.25 LEU 92
SER 228 0.18 THR 269 -0.29 LEU 92

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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.