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CA distance fluctuations for 250309214143438028

---  normal mode 27  ---

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
VAL 172 0.92 VAL 97 -0.89 ILE 254
PRO 151 0.91 PRO 98 -1.19 ILE 254
LYS 164 1.32 SER 99 -0.58 GLU 224
LEU 252 1.81 GLN 100 -0.73 PRO 222
GLU 271 1.55 LYS 101 -0.86 PRO 222
PRO 151 1.11 THR 102 -1.10 PRO 222
PRO 152 0.98 TYR 103 -1.26 PRO 222
PRO 152 1.01 GLN 104 -1.20 PRO 222
PRO 152 1.22 GLY 105 -1.06 PRO 222
PRO 152 1.02 SER 106 -1.07 LEU 201
PRO 152 1.02 SER 106 -1.07 LEU 201
SER 227 1.05 TYR 107 -1.24 THR 155
SER 227 0.99 GLY 108 -1.51 GLU 221
PRO 152 0.94 PHE 109 -1.38 GLU 221
PRO 151 1.08 ARG 110 -1.30 GLU 221
THR 150 1.28 LEU 111 -0.96 ASN 131
THR 150 1.21 GLY 112 -1.37 PRO 128
THR 150 1.43 PHE 113 -1.26 PRO 128
THR 150 1.29 LEU 114 -1.02 CYS 229
THR 150 1.23 HIS 115 -1.07 CYS 229
THR 150 1.22 SER 116 -0.93 ASP 228
GLY 226 1.14 VAL 122 -1.10 ASP 228
THR 150 1.24 THR 123 -0.91 ASP 228
THR 150 1.36 CYS 124 -0.82 ASP 228
THR 150 1.22 THR 125 -0.83 ASP 228
THR 150 1.22 THR 125 -0.83 ASP 228
THR 150 1.20 TYR 126 -1.05 GLU 286
GLY 226 1.10 SER 127 -1.61 GLU 286
GLY 226 0.91 PRO 128 -1.37 GLY 112
GLY 226 1.08 ALA 129 -1.24 GLY 112
GLU 285 1.21 LEU 130 -1.05 GLY 112
GLU 285 0.99 ASN 131 -1.41 VAL 143
GLU 285 1.00 ASN 131 -1.40 GLN 144
LYS 101 1.08 LYS 132 -1.14 VAL 143
THR 150 1.10 MET 133 -0.99 PRO 142
THR 150 1.18 PHE 134 -0.69 ASP 228
THR 150 1.31 CYS 135 -0.71 ASP 228
THR 150 1.23 GLN 136 -0.75 ASP 228
THR 150 1.20 LEU 137 -0.77 PRO 191
THR 150 1.26 ALA 138 -0.97 PRO 191
LEU 188 1.39 LYS 139 -0.76 PRO 191
LEU 188 1.39 LYS 139 -0.77 PRO 191
LEU 188 1.53 THR 140 -0.71 GLY 262
THR 150 1.66 CYS 141 -0.83 MET 133
THR 150 1.66 CYS 141 -0.82 MET 133
THR 150 1.53 PRO 142 -0.99 MET 133
THR 150 1.57 VAL 143 -1.41 ASN 131
THR 150 1.20 GLN 144 -1.40 ASN 131
PRO 151 1.13 LEU 145 -1.08 ASN 200
SER 149 1.24 TRP 146 -1.36 PRO 223
SER 227 1.10 VAL 147 -1.38 THR 155
SER 227 1.40 ASP 148 -1.51 GLU 221
TRP 146 1.24 SER 149 -1.26 LEU 201
CYS 141 1.66 THR 150 -0.83 LEU 201
THR 256 1.61 PRO 151 -1.09 LEU 201
LEU 265 1.41 PRO 152 -1.04 LEU 201
LEU 265 1.41 PRO 152 -1.06 LEU 201
CYS 229 0.96 PRO 153 -1.09 GLU 224
CYS 229 1.15 PRO 153 -1.23 GLU 224
CYS 229 0.89 GLY 154 -1.66 GLU 224
CYS 229 0.91 GLY 154 -1.69 GLU 224
CYS 182 1.01 THR 155 -1.39 GLU 224
CYS 182 1.01 ARG 156 -1.51 GLU 224
CYS 182 1.11 VAL 157 -1.07 GLU 224
CYS 182 1.18 ARG 158 -1.11 GLY 262
THR 150 1.35 ALA 159 -1.07 GLY 262
PRO 151 1.26 MET 160 -0.89 GLY 262
PRO 151 1.18 ALA 161 -0.73 GLY 262
SER 99 1.20 ILE 162 -0.64 THR 170
SER 99 1.25 TYR 163 -0.54 THR 211
SER 99 1.32 LYS 164 -0.50 GLU 286
LYS 101 1.09 GLN 165 -0.58 THR 211
ARG 249 0.68 SER 166 -0.85 SER 269
ARG 248 1.35 GLN 167 -0.84 ASN 210
ARG 248 1.35 GLN 167 -0.84 ASN 210
MET 246 1.20 HIS 168 -0.87 ASN 210
PRO 151 0.79 MET 169 -0.80 ASN 210
PRO 151 0.65 THR 170 -1.21 THR 211
PRO 151 0.87 GLU 171 -0.99 THR 211
PRO 151 1.00 VAL 172 -0.78 PRO 177
PRO 151 0.98 VAL 173 -0.63 SER 261
THR 150 0.95 ARG 174 -0.80 SER 261
THR 150 0.97 ARG 175 -0.80 SER 261
THR 150 0.97 ARG 175 -0.80 SER 261
THR 150 0.93 CYS 176 -0.74 SER 261
THR 150 0.82 PRO 177 -0.98 SER 261
THR 150 1.12 HIS 178 -0.68 GLY 244
ALA 189 1.24 HIS 179 -0.64 GLY 244
THR 150 0.86 GLU 180 -0.80 SER 261
LEU 201 0.98 ARG 181 -0.83 SER 261
VAL 197 1.59 CYS 182 -0.48 MET 243
VAL 197 1.59 CYS 182 -0.48 MET 243
ASN 200 1.42 GLY 187 -1.13 SER 261
THR 140 1.53 LEU 188 -1.14 SER 261
CYS 182 1.27 ALA 189 -1.71 SER 261
CYS 182 1.04 PRO 190 -1.40 SER 261
ASP 207 0.81 PRO 191 -1.19 MET 237
THR 150 0.87 GLN 192 -0.94 SER 261
THR 150 0.99 HIS 193 -1.07 SER 261
THR 150 1.12 LEU 194 -0.85 SER 261
THR 150 1.25 ILE 195 -0.92 GLY 262
CYS 182 1.41 ARG 196 -1.08 SER 261
CYS 182 1.59 VAL 197 -1.08 GLY 262
CYS 182 1.45 GLU 198 -1.02 GLY 262
CYS 182 1.39 GLY 199 -0.91 VAL 147
GLY 187 1.42 ASN 200 -1.46 PRO 219
ARG 181 0.98 LEU 201 -1.26 SER 149
CYS 182 1.38 ARG 202 -1.55 GLU 224
CYS 182 1.50 VAL 203 -1.18 GLU 224
CYS 182 1.34 GLU 204 -1.54 GLY 262
CYS 182 1.46 TYR 205 -1.54 SER 261
CYS 182 1.22 LEU 206 -1.21 SER 261
CYS 182 0.96 ASP 207 -1.06 SER 261
CYS 182 0.77 ASP 208 -1.10 THR 170
PRO 191 0.73 ARG 209 -0.93 THR 170
THR 155 0.76 ASN 210 -1.08 THR 170
PRO 151 0.82 THR 211 -1.21 THR 170
PRO 151 0.81 PHE 212 -0.79 PRO 177
PRO 151 0.97 ARG 213 -0.73 THR 170
PRO 151 0.96 HIS 214 -0.99 SER 261
CYS 182 1.02 SER 215 -1.11 GLY 262
CYS 182 1.02 SER 215 -1.11 GLY 262
CYS 182 1.32 VAL 216 -1.50 GLY 262
CYS 182 1.34 VAL 217 -1.62 GLY 262
CYS 182 1.33 VAL 218 -1.27 GLY 262
CYS 182 0.98 PRO 219 -1.46 ASN 200
CYS 182 1.08 TYR 220 -1.37 PHE 109
CYS 182 1.15 GLU 221 -1.51 GLY 108
CYS 182 0.86 PRO 222 -1.26 TYR 103
CYS 182 0.98 PRO 223 -1.36 TRP 146
CYS 182 0.41 GLU 224 -1.69 GLY 154
ASP 148 0.31 VAL 225 -0.96 GLY 187
GLY 279 1.27 GLY 226 -0.99 LEU 201
ASP 148 1.40 SER 227 -0.80 GLY 199
PRO 153 0.92 ASP 228 -1.10 VAL 122
PRO 153 1.15 CYS 229 -1.07 HIS 115
CYS 182 0.89 THR 230 -1.00 ASN 131
THR 150 1.19 THR 231 -0.95 ASN 200
THR 150 1.34 ILE 232 -0.97 ASN 131
THR 150 1.42 HIS 233 -0.90 GLY 262
THR 150 1.63 TYR 234 -0.91 VAL 272
THR 150 1.49 ASN 235 -0.85 PRO 191
THR 150 1.38 TYR 236 -0.93 PRO 191
THR 150 1.23 MET 237 -1.19 PRO 191
THR 150 1.14 CYS 238 -0.68 SER 261
THR 150 1.14 CYS 238 -0.68 SER 261
THR 150 1.07 ASN 239 -0.62 SER 261
GLN 100 1.07 SER 240 -0.59 SER 261
GLN 167 1.06 SER 241 -0.56 ASP 228
GLN 167 1.00 CYS 242 -0.57 SER 261
GLN 167 1.09 MET 243 -0.63 HIS 179
GLN 167 0.92 GLY 244 -0.68 HIS 178
HIS 168 0.91 GLY 245 -0.61 SER 261
HIS 168 1.20 MET 246 -0.54 SER 261
GLN 167 1.34 ASN 247 -0.48 SER 261
GLN 167 1.35 ARG 248 -0.53 ASP 228
GLN 167 1.20 ARG 249 -0.45 SER 261
LYS 101 1.19 PRO 250 -0.50 VAL 143
GLN 100 1.48 ILE 251 -0.55 SER 261
GLN 100 1.81 LEU 252 -0.58 GLY 262
GLN 100 1.81 LEU 252 -0.58 GLY 262
THR 150 1.30 THR 253 -0.81 GLY 262
THR 150 1.44 ILE 254 -1.18 PRO 98
THR 150 1.44 ILE 254 -1.19 PRO 98
PRO 151 1.50 ILE 255 -0.79 PRO 98
PRO 151 1.61 THR 256 -0.74 GLU 224
PRO 151 1.61 THR 256 -0.74 GLU 224
PRO 151 1.14 LEU 257 -1.00 GLU 224
CYS 182 0.90 GLU 258 -1.29 GLU 224
CYS 182 0.90 GLU 258 -1.28 GLU 224
PRO 152 1.01 ASP 259 -1.28 GLU 224
ASP 228 0.70 SER 260 -1.44 GLU 224
ASP 228 0.88 SER 261 -1.71 ALA 189
PRO 152 0.60 GLY 262 -1.62 VAL 217
PRO 152 1.20 ASN 263 -1.16 LEU 206
PRO 152 1.26 LEU 264 -0.92 GLU 224
PRO 152 1.41 LEU 265 -0.82 GLU 224
PRO 151 1.22 GLY 266 -0.81 PRO 222
PRO 151 1.48 ARG 267 -0.86 PRO 222
PRO 151 1.54 ASN 268 -0.84 PRO 222
THR 150 1.37 SER 269 -0.85 SER 166
LYS 101 1.35 PHE 270 -1.07 VAL 143
LYS 101 1.55 GLU 271 -0.89 VAL 143
LYS 101 1.55 GLU 271 -0.89 VAL 143
LYS 101 1.22 VAL 272 -0.91 ILE 195
LYS 101 1.07 ARG 273 -0.63 SER 261
THR 150 1.15 VAL 274 -0.60 ASP 228
THR 150 1.07 CYS 275 -0.74 ASP 228
THR 150 1.04 ALA 276 -0.84 ASP 228
GLY 226 1.08 CYS 277 -0.96 ASP 228
THR 150 1.10 PRO 278 -0.89 ASP 228
GLY 226 1.27 GLY 279 -1.05 ASP 228
GLY 226 1.23 ARG 280 -1.07 ASP 228
GLY 226 1.11 ASP 281 -0.89 ASP 228
GLY 226 1.22 ARG 282 -0.83 ASP 228
GLY 226 1.16 ARG 283 -1.08 ASP 228
GLY 226 0.99 THR 284 -1.04 ASP 228
LEU 130 1.21 GLU 285 -0.77 ASP 228
GLY 226 1.08 GLU 286 -1.61 SER 127

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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 8th, 2025.