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CA distance fluctuations for 2404111220353637058

---  normal mode 14  ---

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
ASN 263 0.65 SER 96 -1.08 GLU 285
ASN 263 0.84 VAL 97 -1.19 GLU 285
GLY 105 0.67 PRO 98 -1.59 ILE 251
GLN 167 1.00 SER 99 -1.73 ALA 159
MET 169 0.68 GLN 100 -1.53 GLU 285
SER 166 0.77 LYS 101 -1.44 GLU 285
SER 166 0.48 THR 102 -1.70 GLU 285
PRO 98 0.57 TYR 103 -1.60 GLU 286
PRO 98 0.45 GLN 104 -1.75 LEU 130
PRO 98 0.67 GLY 105 -1.84 LEU 130
PRO 98 0.63 SER 106 -1.62 LEU 130
THR 211 0.45 TYR 107 -1.77 ALA 129
PRO 98 0.34 GLY 108 -1.71 ALA 129
SER 166 0.34 PHE 109 -1.54 ASN 131
PRO 223 0.40 ARG 110 -1.57 ASN 131
CYS 229 0.49 LEU 111 -1.42 SER 127
ILE 255 0.63 GLY 112 -1.26 SER 127
PHE 270 1.34 PHE 113 -0.67 PRO 128
PHE 270 0.82 LEU 114 -0.42 ASP 184
ASP 228 0.80 HIS 115 -0.40 THR 150
SER 227 0.91 SER 116 -0.47 PRO 98
GLY 226 0.78 GLY 117 -0.62 PRO 98
GLY 226 0.67 THR 118 -0.76 PRO 98
GLY 226 0.82 ALA 119 -0.66 PRO 98
GLY 226 0.75 LYS 120 -0.69 PRO 98
GLY 199 0.96 SER 121 -0.58 PRO 98
GLY 226 0.87 VAL 122 -0.59 PRO 98
THR 140 0.97 THR 123 -0.59 PRO 98
SER 227 0.66 CYS 124 -0.63 PRO 98
GLY 226 0.50 THR 125 -0.69 PRO 98
ARG 248 0.29 TYR 126 -1.11 LEU 111
ARG 248 0.46 SER 127 -1.50 ARG 110
ARG 248 0.49 PRO 128 -1.78 TRP 146
ARG 248 0.64 ALA 129 -1.77 TYR 107
SER 241 0.78 LEU 130 -1.84 GLY 105
ARG 248 0.66 ASN 131 -1.57 ARG 110
ARG 248 0.51 LYS 132 -0.93 ARG 282
PHE 113 0.50 MET 133 -0.93 PRO 98
LEU 130 0.38 PHE 134 -1.01 PRO 98
GLY 262 0.45 CYS 135 -0.88 PRO 98
GLY 262 0.59 GLN 136 -0.83 PRO 98
GLY 262 0.65 LEU 137 -0.87 PRO 98
GLY 262 0.75 ALA 138 -0.76 PRO 98
GLY 262 0.70 LYS 139 -0.66 PRO 98
THR 123 0.97 THR 140 -0.76 ASP 184
ALA 159 0.82 CYS 141 -0.60 TYR 126
ILE 255 0.89 PRO 142 -0.62 PRO 128
ILE 255 1.23 VAL 143 -0.95 TYR 126
ILE 255 0.93 GLN 144 -1.19 PRO 128
ILE 255 0.74 LEU 145 -1.51 PRO 128
PRO 223 0.52 TRP 146 -1.78 PRO 128
PRO 222 0.59 VAL 147 -1.70 ALA 129
PRO 222 0.51 ASP 148 -1.77 ALA 129
TYR 220 0.36 SER 149 -1.75 ALA 129
THR 211 0.32 THR 150 -1.59 ALA 129
TYR 220 0.45 PRO 151 -1.45 ALA 129
THR 211 0.55 PRO 152 -1.28 ALA 129
THR 211 0.49 PRO 153 -1.23 PRO 128
ASP 208 0.57 GLY 154 -1.01 PRO 128
THR 211 0.51 THR 155 -1.10 PRO 128
ILE 232 0.63 ARG 156 -1.02 SER 99
ILE 232 1.04 VAL 157 -1.36 SER 99
ILE 232 1.22 ARG 158 -1.39 SER 99
TYR 234 1.07 ALA 159 -1.73 SER 99
GLY 262 0.70 MET 160 -1.17 SER 99
GLY 262 0.66 ALA 161 -1.31 PRO 98
PHE 113 0.67 ILE 162 -1.29 PRO 98
PHE 113 0.63 TYR 163 -1.32 PRO 98
PHE 113 0.73 LYS 164 -1.04 PRO 98
PHE 113 0.64 GLN 165 -0.88 THR 284
SER 99 1.00 SER 166 -0.86 THR 284
SER 99 1.00 GLN 167 -0.72 THR 284
SER 99 0.59 HIS 168 -0.67 THR 284
GLN 100 0.68 MET 169 -0.76 THR 284
ASN 263 0.62 THR 170 -0.77 THR 211
ASN 263 0.70 GLU 171 -0.64 PRO 98
ASN 263 0.87 VAL 172 -0.78 PRO 98
GLY 262 0.83 VAL 173 -1.21 PRO 98
GLY 262 0.90 ARG 174 -1.01 PRO 98
GLY 262 0.85 ARG 175 -0.93 PRO 98
GLY 262 0.76 CYS 176 -0.80 PRO 98
SER 261 0.75 PRO 177 -0.63 PRO 98
SER 261 0.70 HIS 178 -0.65 PRO 98
GLY 262 0.74 HIS 179 -0.74 PRO 98
SER 261 0.83 GLU 180 -0.69 PRO 98
SER 261 0.79 ARG 181 -0.57 PRO 98
SER 261 0.71 CYS 182 -0.65 PRO 98
SER 261 0.70 SER 183 -0.65 THR 140
SER 261 0.59 ASP 184 -0.86 GLU 198
SER 261 0.73 SER 185 -0.76 GLU 198
SER 261 0.62 ASP 186 -0.84 GLY 199
SER 261 0.77 GLY 187 -0.68 SER 99
GLY 262 0.82 LEU 188 -0.74 SER 99
GLY 262 0.91 ALA 189 -0.85 SER 99
GLY 262 1.09 PRO 190 -0.72 SER 99
SER 261 0.96 PRO 191 -0.67 PRO 98
GLY 262 1.01 GLN 192 -0.76 PRO 98
GLY 262 1.09 HIS 193 -0.89 PRO 98
GLY 262 0.92 LEU 194 -1.11 PRO 98
GLY 262 0.92 ILE 195 -1.04 PRO 98
GLY 262 0.88 ARG 196 -0.96 SER 99
VAL 217 0.75 VAL 197 -0.96 SER 99
THR 123 0.74 GLU 198 -0.86 ASP 184
SER 121 0.96 GLY 199 -0.84 ASP 186
SER 121 0.76 ASN 200 -0.95 SER 99
SER 121 0.73 LEU 201 -0.86 SER 99
SER 121 0.62 ARG 202 -0.94 SER 99
GLY 262 0.63 VAL 203 -1.07 SER 99
GLY 262 0.91 GLU 204 -1.00 SER 99
GLY 262 1.20 TYR 205 -0.96 SER 99
GLY 262 1.55 LEU 206 -0.95 SER 99
GLY 262 1.43 ASP 207 -0.73 SER 99
GLY 262 1.46 ASP 208 -0.78 ASN 288
SER 261 1.49 ARG 209 -0.79 ASN 288
ASN 263 1.25 ASN 210 -0.87 ASN 288
ASN 263 1.39 THR 211 -0.80 GLU 285
ASN 263 1.21 PHE 212 -0.63 ASN 288
ASN 263 1.17 ARG 213 -0.66 GLU 285
GLY 262 1.23 HIS 214 -0.70 SER 99
GLY 262 1.14 SER 215 -1.07 SER 99
GLY 262 1.03 VAL 216 -1.25 SER 99
HIS 233 0.85 VAL 217 -1.26 SER 99
THR 123 0.66 VAL 218 -1.19 SER 99
THR 123 0.58 PRO 219 -1.04 SER 99
VAL 147 0.49 TYR 220 -1.13 ASN 131
VAL 147 0.54 GLU 221 -0.99 PRO 128
VAL 147 0.59 PRO 222 -1.07 PRO 128
TRP 146 0.52 PRO 223 -0.97 PRO 128
SER 121 0.52 GLU 224 -0.79 PRO 128
SER 121 0.60 VAL 225 -1.00 PRO 153
SER 116 0.88 GLY 226 -0.92 PRO 153
SER 116 0.91 SER 227 -0.90 PRO 153
SER 116 0.83 ASP 228 -1.16 PRO 153
GLY 112 0.55 CYS 229 -1.32 PRO 128
THR 123 0.51 THR 230 -1.24 PRO 128
ARG 158 0.82 THR 231 -1.03 PRO 128
ARG 158 1.22 ILE 232 -0.90 PRO 128
ARG 158 1.09 HIS 233 -0.76 ASP 184
ALA 159 1.07 TYR 234 -0.72 ASP 184
GLY 262 0.76 ASN 235 -0.85 ASP 184
GLY 262 0.75 TYR 236 -0.92 PRO 98
GLY 262 0.77 MET 237 -0.94 PRO 98
GLY 262 0.71 CYS 238 -1.01 PRO 98
GLY 262 0.59 ASN 239 -1.07 PRO 98
LEU 130 0.60 SER 240 -1.14 PRO 98
LEU 130 0.78 SER 241 -0.93 PRO 98
LEU 130 0.64 CYS 242 -0.89 PRO 98
LEU 130 0.67 MET 243 -0.76 PRO 98
GLY 262 0.65 GLY 244 -0.70 PRO 98
GLY 262 0.69 GLY 245 -0.88 PRO 98
GLY 262 0.65 MET 246 -1.07 PRO 98
LEU 130 0.66 ASN 247 -0.91 PRO 98
LEU 130 0.77 ARG 248 -0.99 PRO 98
ASN 131 0.59 ARG 249 -1.12 PRO 98
PHE 113 0.63 PRO 250 -1.29 PRO 98
PHE 113 0.70 ILE 251 -1.59 PRO 98
PHE 113 0.91 LEU 252 -1.35 PRO 98
PHE 113 0.94 THR 253 -1.19 PRO 98
VAL 143 1.10 ILE 254 -1.15 SER 99
VAL 143 1.23 ILE 255 -1.53 SER 99
VAL 143 0.78 THR 256 -1.13 SER 99
SER 215 0.44 LEU 257 -1.14 ASN 131
SER 215 0.72 GLU 258 -1.07 ASN 288
ASP 208 0.86 ASP 259 -1.04 ASN 288
ASP 208 1.05 SER 260 -0.92 ASN 288
ARG 209 1.49 SER 261 -0.93 ASN 288
LEU 206 1.55 GLY 262 -0.97 ASN 288
ASP 208 1.41 ASN 263 -1.16 ASN 288
THR 211 1.04 LEU 264 -1.26 ASN 288
THR 211 0.73 LEU 265 -1.41 LEU 130
ARG 213 0.56 GLY 266 -1.46 LEU 130
VAL 143 0.48 ARG 267 -1.33 GLU 285
PHE 113 0.58 ASN 268 -1.33 GLU 285
PHE 113 0.98 SER 269 -1.21 GLU 285
PHE 113 1.34 PHE 270 -0.99 PRO 98
PHE 113 1.01 GLU 271 -1.08 PRO 98
PHE 113 0.73 VAL 272 -1.23 PRO 98
PHE 113 0.44 ARG 273 -1.16 PRO 98
GLY 262 0.47 VAL 274 -1.15 PRO 98
LEU 130 0.59 CYS 275 -1.04 PRO 98
LEU 130 0.54 ALA 276 -0.89 PRO 98
GLY 199 0.60 CYS 277 -0.90 PRO 98
GLY 226 0.51 PRO 278 -0.97 PRO 98
GLY 226 0.59 GLY 279 -0.87 PRO 98
GLY 226 0.50 ARG 280 -0.93 PRO 98
ALA 276 0.43 ASP 281 -1.10 PRO 98
LEU 130 0.38 ARG 282 -1.05 PRO 98
GLY 226 0.34 ARG 283 -0.94 THR 102
ALA 276 0.26 THR 284 -1.14 THR 102
ALA 276 0.21 GLU 285 -1.70 THR 102
GLU 285 0.19 GLU 286 -1.60 TYR 103
ALA 276 0.19 GLU 287 -1.30 THR 102
ALA 276 0.13 ASN 288 -1.28 TYR 103

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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.