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CA distance fluctuations for 240414155710142639

---  normal mode 16  ---

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
LEU 206 0.90 SER 94 -1.06 PRO 98
LEU 206 0.81 SER 95 -0.81 GLY 244
LEU 206 0.80 SER 96 -0.74 VAL 172
PHE 270 0.57 VAL 97 -1.18 VAL 172
ILE 254 1.26 PRO 98 -1.06 SER 94
THR 256 1.08 SER 99 -1.14 SER 166
PRO 128 0.53 GLN 100 -1.11 ILE 162
PRO 128 0.63 LYS 101 -0.94 SER 166
TYR 126 0.65 THR 102 -0.81 GLN 165
TYR 126 0.56 TYR 103 -0.64 GLN 165
PRO 223 0.53 GLN 104 -0.58 GLN 165
PRO 223 0.71 GLY 105 -0.62 ASN 210
PRO 223 0.85 SER 106 -0.67 ASN 210
PRO 223 0.94 TYR 107 -0.74 ASN 210
PRO 223 0.65 GLY 108 -0.61 ASN 210
PRO 223 0.60 PHE 109 -0.58 GLN 165
THR 155 0.55 ARG 110 -0.61 GLN 165
TYR 220 0.66 LEU 111 -0.79 PHE 270
PRO 153 0.49 GLY 112 -1.11 ASN 131
CYS 124 0.57 PHE 113 -1.40 ASN 131
THR 123 0.63 LEU 114 -1.76 ASP 228
THR 102 0.49 HIS 115 -1.46 ASP 228
ARG 290 0.50 SER 116 -1.63 SER 227
GLU 287 0.65 GLY 117 -1.49 GLY 226
GLU 287 0.49 THR 118 -1.54 ASP 186
GLU 287 0.49 ALA 119 -1.62 GLY 226
TYR 220 0.31 LYS 120 -1.61 ASP 186
LEU 114 0.43 SER 121 -1.61 GLY 187
LEU 114 0.54 VAL 122 -1.47 GLY 226
LEU 114 0.63 THR 123 -1.43 LEU 188
PHE 113 0.57 CYS 124 -1.54 SER 227
THR 102 0.45 THR 125 -1.65 SER 227
THR 102 0.65 TYR 126 -1.42 SER 227
THR 102 0.50 SER 127 -1.25 SER 227
THR 102 0.64 PRO 128 -1.29 ASP 228
LYS 101 0.45 ALA 129 -1.13 ASP 186
ASP 281 0.53 LEU 130 -1.10 ASP 228
VAL 97 0.52 ASN 131 -1.40 PHE 113
PRO 98 0.47 LYS 132 -1.17 SER 227
PRO 98 0.51 MET 133 -1.32 SER 227
PRO 98 0.41 PHE 134 -1.32 SER 227
TYR 220 0.45 CYS 135 -1.34 SER 185
TYR 220 0.46 GLN 136 -1.38 SER 185
TYR 220 0.49 LEU 137 -1.18 SER 185
TYR 220 0.53 ALA 138 -1.29 ALA 189
TYR 220 0.54 LYS 139 -1.27 LEU 188
TYR 220 0.62 THR 140 -1.22 SER 227
TYR 220 0.68 CYS 141 -1.28 SER 227
TYR 220 0.70 PRO 142 -1.07 SER 227
TYR 220 0.82 VAL 143 -1.58 PHE 270
PRO 153 0.59 GLN 144 -1.34 PHE 270
PRO 153 0.72 LEU 145 -1.31 ILE 255
PRO 153 0.62 TRP 146 -0.75 ILE 255
PRO 223 0.62 VAL 147 -0.78 ASN 210
ASP 228 0.58 ASP 148 -0.86 GLU 221
ASP 228 0.93 SER 149 -0.92 GLU 221
ASP 228 1.24 THR 150 -1.43 TYR 220
PRO 223 1.51 PRO 151 -0.99 ASN 210
PRO 223 1.53 PRO 152 -1.01 ASN 210
GLU 224 1.60 PRO 153 -1.04 ASN 210
GLU 224 1.46 GLY 154 -1.23 ASN 210
GLU 224 1.09 THR 155 -1.21 ASN 210
SER 99 0.72 ARG 156 -0.98 ASN 210
SER 99 0.76 VAL 157 -1.19 THR 230
PRO 98 0.80 ARG 158 -1.27 THR 230
PRO 98 0.96 ALA 159 -1.23 THR 230
PRO 98 0.80 MET 160 -1.00 THR 230
PRO 98 0.43 ALA 161 -0.84 THR 230
ARG 213 0.49 ILE 162 -1.11 GLN 100
ARG 213 0.47 TYR 163 -0.93 GLN 100
THR 211 0.40 LYS 164 -0.89 LEU 289
THR 211 0.60 GLN 165 -1.00 LEU 289
THR 211 0.69 SER 166 -1.14 SER 99
THR 211 1.07 GLN 167 -1.13 LYS 291
THR 211 1.12 HIS 168 -1.04 LEU 289
THR 211 0.87 MET 169 -1.12 SER 99
ASP 208 1.22 THR 170 -0.99 SER 99
THR 211 1.19 GLU 171 -0.85 SER 99
ARG 249 0.57 VAL 172 -1.18 VAL 97
ARG 249 0.47 VAL 173 -0.81 GLY 262
LEU 201 0.44 ARG 174 -0.74 VAL 97
LEU 201 0.56 ARG 175 -0.69 ASN 288
LEU 201 0.57 CYS 176 -0.74 ASN 288
LEU 201 0.67 PRO 177 -0.72 VAL 97
LEU 201 0.78 HIS 178 -0.67 ASN 288
LEU 201 0.89 HIS 179 -0.69 ASN 288
LEU 201 0.93 GLU 180 -0.61 ASN 288
LEU 201 0.97 ARG 181 -0.59 ASN 288
LEU 201 1.24 CYS 182 -0.55 ASN 288
LEU 201 1.15 SER 183 -0.82 LEU 137
LEU 201 1.13 ASP 184 -1.29 ALA 276
LEU 201 0.68 SER 185 -1.73 ALA 276
LEU 201 0.39 ASP 186 -1.86 ARG 280
SER 94 0.45 GLY 187 -1.61 SER 121
SER 94 0.60 LEU 188 -1.43 THR 123
VAL 203 1.32 ALA 189 -1.29 ALA 138
VAL 203 0.85 PRO 190 -0.84 ALA 138
LEU 201 1.09 PRO 191 -0.57 ASN 288
LEU 201 0.73 GLN 192 -0.58 SER 227
VAL 203 0.73 HIS 193 -0.61 SER 227
VAL 218 0.47 LEU 194 -0.73 SER 227
VAL 218 0.55 ILE 195 -0.76 SER 227
VAL 218 0.70 ARG 196 -0.98 TYR 205
TYR 220 0.93 VAL 197 -1.28 TYR 205
CYS 182 0.86 GLU 198 -1.10 TYR 205
CYS 182 0.94 GLY 199 -1.00 PRO 223
CYS 182 0.94 ASN 200 -0.92 PRO 223
CYS 182 1.24 LEU 201 -1.01 PRO 223
ALA 189 1.29 ARG 202 -0.64 THR 150
ALA 189 1.32 VAL 203 -0.73 THR 230
ALA 189 0.83 GLU 204 -0.80 GLU 198
SER 94 0.67 TYR 205 -1.28 VAL 197
SER 94 0.90 LEU 206 -0.77 ARG 196
THR 170 0.89 ASP 207 -0.64 THR 230
THR 170 1.22 ASP 208 -0.98 SER 261
THR 170 0.96 ARG 209 -1.15 SER 261
GLN 167 0.90 ASN 210 -1.71 SER 260
GLU 171 1.19 THR 211 -1.76 SER 261
GLU 171 1.12 PHE 212 -1.35 SER 261
THR 170 1.21 ARG 213 -1.08 GLY 262
THR 170 0.75 HIS 214 -0.80 THR 230
PRO 98 0.66 SER 215 -0.90 THR 230
PRO 190 0.70 VAL 216 -0.98 THR 230
SER 99 0.62 VAL 217 -0.90 THR 230
VAL 197 0.83 VAL 218 -0.85 THR 230
VAL 197 0.77 PRO 219 -1.02 THR 150
ILE 232 0.97 TYR 220 -1.43 THR 150
GLY 154 0.88 GLU 221 -0.94 THR 150
GLY 154 1.05 PRO 222 -1.08 LEU 114
PRO 152 1.53 PRO 223 -1.01 LEU 201
PRO 153 1.60 GLU 224 -0.67 HIS 115
PRO 153 0.78 VAL 225 -1.03 ALA 129
PRO 152 0.71 GLY 226 -1.62 ALA 119
PRO 152 0.86 SER 227 -1.65 THR 125
THR 150 1.24 ASP 228 -1.76 LEU 114
PRO 153 0.70 CYS 229 -0.96 ILE 255
PRO 153 0.61 THR 230 -1.38 ILE 255
PRO 153 0.66 THR 231 -1.07 PHE 270
TYR 220 0.97 ILE 232 -1.23 ALA 159
TYR 220 0.86 HIS 233 -0.99 SER 227
TYR 220 0.85 TYR 234 -0.93 SER 227
TYR 220 0.68 ASN 235 -0.98 SER 227
TYR 220 0.56 TYR 236 -0.91 SER 227
TYR 220 0.54 MET 237 -0.97 ALA 189
LEU 201 0.42 CYS 238 -0.92 SER 185
TYR 220 0.37 ASN 239 -1.21 SER 185
VAL 172 0.29 SER 240 -1.15 SER 185
LEU 201 0.26 SER 241 -1.12 SER 185
LEU 201 0.39 CYS 242 -1.01 ASP 184
LEU 201 0.40 MET 243 -0.89 ASN 288
LEU 201 0.44 GLY 244 -0.82 LYS 291
LEU 201 0.41 GLY 245 -0.85 ASN 288
VAL 172 0.36 MET 246 -0.95 LEU 289
VAL 172 0.31 ASN 247 -1.05 ASN 288
VAL 172 0.38 ARG 248 -1.28 ASN 288
VAL 172 0.57 ARG 249 -1.28 LEU 289
VAL 172 0.38 PRO 250 -1.26 LEU 289
ARG 213 0.26 ILE 251 -0.90 LEU 289
PRO 98 0.58 LEU 252 -1.06 VAL 143
PRO 98 0.82 THR 253 -1.13 VAL 143
PRO 98 1.26 ILE 254 -1.11 LEU 145
PRO 98 1.08 ILE 255 -1.38 THR 230
SER 99 1.08 THR 256 -1.09 THR 230
SER 99 0.92 LEU 257 -0.80 ASN 210
SER 99 0.89 GLU 258 -1.05 ASN 210
PRO 223 1.08 ASP 259 -1.37 ASN 210
GLU 224 1.08 SER 260 -1.71 ASN 210
PRO 222 0.92 SER 261 -1.76 THR 211
GLU 224 0.69 GLY 262 -1.51 THR 211
PRO 223 0.83 ASN 263 -1.27 THR 211
SER 99 1.03 LEU 264 -0.91 THR 211
PRO 223 0.86 LEU 265 -0.85 ASN 210
SER 99 0.88 GLY 266 -0.69 ASN 210
SER 99 0.83 ARG 267 -0.68 THR 230
TYR 126 0.60 ASN 268 -0.77 LEU 145
PRO 98 0.74 SER 269 -1.06 LEU 145
PRO 98 0.69 PHE 270 -1.58 VAL 143
PRO 98 0.52 GLU 271 -1.23 VAL 143
PRO 98 0.47 VAL 272 -1.09 SER 227
PRO 98 0.35 ARG 273 -1.26 SER 185
TYR 220 0.38 VAL 274 -1.37 SER 185
TYR 220 0.36 CYS 275 -1.68 SER 185
TYR 220 0.38 ALA 276 -1.73 SER 185
TYR 220 0.34 CYS 277 -1.65 SER 185
PRO 98 0.35 PRO 278 -1.55 SER 185
PRO 98 0.32 GLY 279 -1.64 ASP 186
LEU 130 0.29 ARG 280 -1.86 ASP 186
LEU 130 0.53 ASP 281 -1.67 ASP 186
LEU 130 0.43 ARG 282 -1.57 ASP 186
GLY 117 0.43 ARG 283 -1.63 ASP 186
GLY 117 0.31 THR 284 -1.62 ASP 186
LEU 130 0.28 GLU 285 -1.51 SER 185
GLY 117 0.58 GLU 286 -1.40 ASP 186
GLY 117 0.65 GLU 287 -1.38 ASP 186
GLY 117 0.41 ASN 288 -1.36 SER 185
GLY 117 0.45 LEU 289 -1.28 ARG 249
GLY 117 0.60 ARG 290 -1.16 ASP 186
GLY 117 0.49 LYS 291 -1.15 ASP 186

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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.