CNRS Nantes University US2B US2B
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CA distance fluctuations for 2402180042123244403

---  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
SER 261 1.22 VAL 97 -1.46 THR 284
LEU 264 0.97 PRO 98 -1.03 ILE 254
GLN 167 1.37 SER 99 -1.71 THR 150
LYS 164 1.02 GLN 100 -1.18 GLU 285
SER 166 1.16 LYS 101 -1.16 GLU 285
SER 166 0.86 THR 102 -1.53 GLU 285
SER 166 0.90 TYR 103 -1.54 LEU 130
SER 166 0.70 GLN 104 -1.72 LEU 130
PRO 153 0.76 GLY 105 -1.51 LEU 130
PRO 153 1.15 SER 106 -1.41 ALA 129
PRO 153 1.14 SER 106 -1.42 ALA 129
PRO 153 1.21 TYR 107 -1.51 ALA 129
SER 166 0.66 GLY 108 -1.74 ALA 129
SER 166 0.61 PHE 109 -1.71 PRO 128
PRO 152 0.65 ARG 110 -1.49 ASN 131
PRO 152 0.85 LEU 111 -1.18 ASN 131
PRO 152 0.99 GLY 112 -1.15 TYR 126
PHE 270 1.36 PHE 113 -1.34 CYS 229
PRO 152 1.04 LEU 114 -0.85 SER 227
PRO 152 1.04 HIS 115 -0.74 ASP 228
PRO 151 1.21 SER 116 -0.51 GLY 226
PRO 151 1.28 VAL 122 -0.49 ALA 276
PRO 151 1.19 THR 123 -0.40 CYS 182
PRO 151 1.01 CYS 124 -0.52 ASP 228
PRO 151 0.88 THR 125 -0.77 ASP 228
PRO 151 0.88 THR 125 -0.77 ASP 228
PRO 151 0.63 TYR 126 -1.17 LEU 111
ARG 248 0.49 SER 127 -1.29 ARG 110
ARG 248 0.45 PRO 128 -1.71 PHE 109
ARG 248 0.62 ALA 129 -1.74 GLY 108
ARG 248 0.80 LEU 130 -1.72 GLN 104
ARG 248 0.57 ASN 131 -1.49 ARG 110
ARG 248 0.58 ASN 131 -1.48 ARG 110
PHE 113 0.61 LYS 132 -0.91 ARG 282
PRO 151 0.66 MET 133 -0.76 LEU 111
PRO 151 0.73 PHE 134 -0.72 LEU 111
PRO 151 0.89 CYS 135 -0.46 LEU 111
PRO 151 0.98 GLN 136 -0.33 CYS 182
PRO 151 0.91 LEU 137 -0.42 CYS 182
PRO 151 0.95 ALA 138 -0.74 CYS 182
PRO 151 1.08 LYS 139 -0.69 CYS 182
PRO 151 1.08 LYS 139 -0.69 CYS 182
PRO 151 1.06 THR 140 -0.70 CYS 182
THR 253 1.10 CYS 141 -0.54 PRO 191
THR 253 1.10 CYS 141 -0.54 PRO 191
ILE 254 1.22 PRO 142 -0.63 LEU 188
ILE 255 1.35 VAL 143 -0.83 TYR 126
PRO 152 1.19 GLN 144 -0.97 PRO 128
PRO 152 0.99 LEU 145 -1.22 PRO 128
PRO 152 0.94 TRP 146 -1.54 PRO 128
PRO 152 0.62 VAL 147 -1.61 GLU 221
SER 166 0.61 ASP 148 -1.40 PRO 222
SER 166 0.38 SER 149 -1.44 PRO 153
GLY 226 0.90 THR 150 -1.71 SER 99
VAL 122 1.28 PRO 151 -0.77 SER 261
SER 227 1.44 PRO 152 -1.14 SER 261
SER 227 1.43 PRO 152 -1.23 SER 261
TYR 107 1.21 PRO 153 -1.29 SER 99
GLY 226 0.58 PRO 153 -1.44 SER 149
SER 106 1.08 GLY 154 -1.52 SER 99
SER 106 0.91 GLY 154 -1.54 SER 99
ASN 210 0.75 THR 155 -1.54 SER 99
GLU 224 0.70 ARG 156 -1.63 SER 99
GLU 224 1.03 VAL 157 -1.31 SER 99
ILE 232 1.35 ARG 158 -1.09 THR 150
TYR 234 1.42 ALA 159 -0.86 THR 150
TYR 234 1.03 MET 160 -0.72 THR 150
GLY 262 0.84 ALA 161 -0.67 THR 170
GLN 100 0.95 ILE 162 -0.74 THR 170
GLN 100 0.92 TYR 163 -0.73 THR 284
GLN 100 1.02 LYS 164 -0.91 THR 284
LYS 101 1.09 GLN 165 -0.75 THR 284
LYS 101 1.16 SER 166 -0.76 THR 284
SER 99 1.37 GLN 167 -0.56 THR 284
SER 99 1.37 GLN 167 -0.56 THR 284
SER 99 0.98 ARG 168 -0.80 VAL 172
ASN 263 0.91 MET 169 -0.81 THR 284
ASN 263 0.73 THR 170 -0.82 ILE 254
ASN 263 0.81 GLU 171 -1.22 THR 211
ASN 263 1.26 VAL 172 -0.80 ARG 168
GLY 262 1.03 VAL 173 -0.57 ARG 168
GLY 262 1.07 ARG 174 -0.57 THR 150
GLY 262 0.98 ARG 175 -0.55 THR 150
GLY 262 0.98 ARG 175 -0.55 THR 150
GLY 262 0.87 CYS 176 -0.48 THR 150
SER 261 0.83 PRO 177 -0.51 THR 150
GLY 262 0.77 HIS 178 -0.47 THR 150
GLY 262 0.86 HIS 179 -0.50 THR 150
SER 261 0.90 GLU 180 -0.61 GLU 198
SER 261 0.80 ARG 181 -0.68 GLY 199
GLY 187 0.85 CYS 182 -0.74 GLU 198
GLY 187 0.85 CYS 182 -0.75 GLU 198
CYS 182 0.85 GLY 187 -1.50 ASN 200
SER 261 0.51 LEU 188 -1.36 ASN 200
GLY 262 0.70 ALA 189 -1.37 VAL 203
SER 261 1.16 PRO 190 -1.00 ASN 200
SER 261 1.03 PRO 191 -1.09 GLU 198
GLY 262 1.11 GLN 192 -0.69 THR 150
GLY 262 1.23 HIS 193 -0.73 THR 150
GLY 262 1.11 LEU 194 -0.62 THR 150
GLY 262 1.08 ILE 195 -0.91 PHE 270
TYR 205 1.26 ARG 196 -0.76 LEU 111
GLU 224 0.97 VAL 197 -0.94 LEU 188
GLU 224 1.14 GLU 198 -1.09 PRO 191
PRO 151 1.19 GLY 199 -1.37 GLY 187
GLU 224 1.59 ASN 200 -1.50 GLY 187
VAL 225 1.76 LEU 201 -1.29 GLY 187
VAL 225 1.36 ARG 202 -1.27 SER 99
GLU 224 1.24 VAL 203 -1.37 ALA 189
GLU 224 1.00 GLU 204 -1.22 THR 150
ARG 196 1.26 TYR 205 -1.04 THR 150
GLY 262 1.14 LEU 206 -1.08 THR 150
GLY 262 1.59 ASP 207 -0.87 THR 150
SER 261 1.55 ASP 208 -0.81 GLU 171
SER 261 1.69 ARG 209 -0.70 GLU 171
ASN 263 1.49 ASN 210 -0.86 GLU 171
ASN 263 1.87 THR 211 -1.22 GLU 171
ASN 263 1.65 PHE 212 -0.85 GLU 171
GLY 262 1.46 ARG 213 -0.84 GLU 171
GLY 262 1.51 HIS 214 -0.72 THR 150
GLY 262 1.30 SER 215 -0.83 THR 150
GLY 262 1.30 SER 215 -0.84 THR 150
GLY 262 1.04 VAL 216 -0.90 THR 150
GLU 224 1.10 VAL 217 -1.20 SER 99
GLU 224 1.13 VAL 218 -1.30 SER 99
ASN 210 0.63 PRO 219 -1.34 SER 99
GLU 224 0.64 TYR 220 -1.40 PRO 128
PRO 152 0.74 GLU 221 -1.61 VAL 147
PRO 152 0.94 PRO 222 -1.40 ASP 148
PRO 152 1.29 PRO 223 -1.23 PRO 128
ASN 200 1.59 GLU 224 -1.03 ASP 148
LEU 201 1.76 VAL 225 -0.91 ALA 129
PRO 152 1.18 GLY 226 -0.94 PHE 113
PRO 152 1.44 SER 227 -1.19 PHE 113
PRO 152 1.20 ASP 228 -1.19 PHE 113
PRO 152 1.38 CYS 229 -1.34 PHE 113
PRO 152 1.18 THR 230 -1.00 PRO 128
PRO 152 1.29 THR 231 -0.80 PRO 128
ILE 255 1.67 ILE 232 -0.89 GLY 187
ALA 159 1.27 HIS 233 -0.76 GLY 187
ALA 159 1.42 TYR 234 -0.67 PRO 191
GLY 262 0.92 ASN 235 -0.79 PRO 191
GLY 262 0.93 TYR 236 -0.53 PRO 191
GLY 262 0.90 MET 237 -0.53 PRO 191
GLY 262 0.84 CYS 238 -0.45 THR 150
GLY 262 0.84 CYS 238 -0.45 THR 150
GLY 262 0.75 ASN 239 -0.36 THR 150
GLY 262 0.72 SER 240 -0.32 THR 150
LEU 130 0.78 SER 241 -0.31 GLN 167
GLY 262 0.74 CYS 242 -0.36 THR 150
GLY 262 0.70 MET 243 -0.40 GLN 167
ASN 263 0.78 GLY 244 -0.41 THR 150
GLY 262 0.83 GLY 245 -0.43 THR 150
GLY 262 0.77 MET 246 -0.40 GLN 167
GLY 262 0.68 ASN 247 -0.46 GLN 167
LEU 130 0.80 ARG 248 -0.37 GLN 167
ASN 263 0.64 SER 249 -0.53 ASP 281
PHE 113 0.69 PRO 250 -0.75 ASP 281
PHE 113 0.80 ILE 251 -0.70 ASP 281
PHE 113 1.04 LEU 252 -0.81 GLU 285
PHE 113 1.04 LEU 252 -0.81 GLU 285
CYS 141 1.10 THR 253 -0.79 GLU 285
VAL 143 1.31 ILE 254 -1.03 PRO 98
VAL 143 1.31 ILE 254 -1.03 PRO 98
ILE 232 1.67 ILE 255 -0.94 GLU 285
ILE 232 1.43 THR 256 -0.96 GLU 285
ILE 232 1.43 THR 256 -0.96 GLU 285
THR 230 0.97 LEU 257 -1.16 SER 99
THR 211 0.86 GLU 258 -1.26 SER 99
THR 211 0.86 GLU 258 -1.25 SER 99
ASN 210 1.24 ASP 259 -1.20 SER 99
ASN 210 1.17 SER 260 -1.39 SER 99
ARG 209 1.69 SER 261 -1.23 PRO 152
ASP 207 1.59 GLY 262 -0.94 THR 150
THR 211 1.87 ASN 263 -0.84 THR 150
THR 211 1.32 LEU 264 -0.88 THR 150
THR 211 0.91 LEU 265 -1.21 ALA 129
SER 166 0.73 GLY 266 -1.22 LEU 130
ILE 232 0.86 ARG 267 -1.21 GLU 285
VAL 143 0.89 ASN 268 -1.25 GLU 285
PHE 113 1.32 SER 269 -1.16 GLU 285
PHE 113 1.36 PHE 270 -0.91 ILE 195
PHE 113 1.13 GLU 271 -0.92 ASP 281
PHE 113 1.13 GLU 271 -0.92 ASP 281
PHE 113 0.80 VAL 272 -0.67 ILE 195
PRO 151 0.63 ARG 273 -0.51 ILE 195
PRO 151 0.75 VAL 274 -0.36 LEU 111
PRO 151 0.81 CYS 275 -0.38 ASP 228
PRO 151 0.90 ALA 276 -0.49 VAL 122
PRO 151 1.01 CYS 277 -0.53 PRO 250
PRO 151 0.93 PRO 278 -0.56 ASP 228
PRO 151 1.00 GLY 279 -0.63 ASP 228
PRO 151 0.92 ARG 280 -0.80 VAL 97
PRO 151 0.69 ASP 281 -0.92 GLU 271
PRO 151 0.63 ARG 282 -0.91 LYS 132
PRO 151 0.67 ARG 283 -1.06 VAL 97
PRO 151 0.43 THR 284 -1.46 VAL 97
ALA 276 0.21 GLU 285 -1.53 THR 102
SER 241 0.31 GLU 286 -1.28 GLN 104

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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.