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CA distance fluctuations for 250309214534470056

---  normal mode 29  ---

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
PRO 190 1.41 VAL 97 -1.39 ILE 254
PRO 190 1.02 PRO 98 -1.81 PHE 270
VAL 172 1.02 SER 99 -1.51 ASN 268
HIS 214 1.43 GLN 100 -0.96 ASN 131
VAL 172 1.34 LYS 101 -0.81 ASN 131
VAL 172 1.02 THR 102 -0.95 ASN 131
VAL 172 0.90 TYR 103 -0.97 SER 127
CYS 182 0.87 GLN 104 -1.08 SER 127
CYS 182 0.79 GLY 105 -1.08 PRO 128
CYS 182 0.68 SER 106 -1.35 PRO 128
CYS 182 0.68 SER 106 -1.35 PRO 128
CYS 182 0.78 TYR 107 -1.45 PRO 128
CYS 182 0.81 GLY 108 -1.29 SER 127
CYS 182 0.90 PHE 109 -1.18 SER 127
CYS 182 0.89 ARG 110 -1.12 SER 127
CYS 182 1.02 LEU 111 -1.04 SER 127
CYS 182 1.12 GLY 112 -1.12 SER 127
GLU 271 1.55 PHE 113 -0.77 SER 127
CYS 182 1.12 LEU 114 -0.66 LEU 188
CYS 182 0.97 HIS 115 -0.80 PRO 98
CYS 182 1.10 SER 116 -0.69 PRO 98
CYS 182 0.77 VAL 122 -0.77 PRO 191
CYS 182 1.03 THR 123 -0.75 PRO 98
CYS 182 1.10 CYS 124 -0.82 PRO 98
CYS 182 0.90 THR 125 -1.03 PRO 98
CYS 182 0.90 THR 125 -1.03 PRO 98
ARG 282 1.14 TYR 126 -1.35 VAL 218
SER 240 1.08 SER 127 -1.51 ASP 148
THR 284 0.71 PRO 128 -1.69 THR 150
MET 243 0.83 ALA 129 -1.15 SER 149
MET 243 1.69 LEU 130 -0.68 ASP 148
ARG 283 1.27 ASN 131 -1.57 ASN 268
ARG 282 1.25 ASN 131 -1.53 ASN 268
PHE 113 1.54 LYS 132 -1.20 PRO 98
PHE 113 1.31 MET 133 -1.24 PRO 98
HIS 178 0.96 PHE 134 -1.13 PRO 98
HIS 178 1.10 CYS 135 -0.99 PRO 98
HIS 178 1.31 GLN 136 -0.78 PRO 98
HIS 178 1.50 LEU 137 -0.89 PRO 191
ARG 181 1.52 ALA 138 -1.02 PRO 191
HIS 178 1.38 LYS 139 -0.85 PRO 191
HIS 178 1.38 LYS 139 -0.85 PRO 191
CYS 182 1.64 THR 140 -0.74 LEU 188
CYS 182 1.57 CYS 141 -0.98 TYR 126
CYS 182 1.57 CYS 141 -0.98 TYR 126
CYS 182 1.48 PRO 142 -0.98 TYR 126
CYS 182 1.37 VAL 143 -1.13 TYR 126
CYS 182 1.21 GLN 144 -1.16 ASN 200
CYS 182 1.07 LEU 145 -1.54 TYR 220
CYS 182 0.96 TRP 146 -1.34 SER 127
CYS 182 0.90 VAL 147 -1.40 SER 127
CYS 182 0.83 ASP 148 -1.51 SER 127
PRO 223 0.86 SER 149 -1.54 PRO 128
CYS 182 0.91 THR 150 -1.69 PRO 128
LEU 265 1.03 PRO 151 -1.62 PRO 128
ASN 263 0.79 PRO 152 -1.72 GLU 221
ASN 263 0.75 PRO 152 -1.75 GLU 221
CYS 182 0.50 PRO 153 -1.41 ARG 202
CYS 182 0.50 PRO 153 -1.56 ARG 202
CYS 182 0.57 GLY 154 -1.37 ARG 202
CYS 182 0.57 GLY 154 -1.43 ARG 202
CYS 182 0.74 THR 155 -1.32 PRO 128
CYS 182 0.78 ARG 156 -1.17 PRO 128
CYS 182 0.95 VAL 157 -1.10 TYR 126
CYS 182 1.08 ARG 158 -1.05 GLY 262
CYS 182 1.22 ALA 159 -0.99 THR 170
CYS 182 1.12 MET 160 -1.31 THR 170
LEU 194 1.30 ALA 161 -1.14 THR 170
LYS 101 1.15 ILE 162 -1.38 GLU 171
CYS 238 1.07 TYR 163 -1.22 THR 211
CYS 238 1.08 LYS 164 -0.89 ASN 210
CYS 238 1.06 GLN 165 -0.81 ASN 210
CYS 238 0.97 SER 166 -0.73 ASN 210
LEU 130 1.19 GLN 167 -0.78 ASN 210
LEU 130 1.19 GLN 167 -0.78 ASN 210
ARG 174 1.37 HIS 168 -0.98 ASN 210
VAL 173 1.24 MET 169 -1.03 ASN 210
LEU 130 0.78 THR 170 -1.62 ASN 210
GLN 192 1.13 GLU 171 -1.50 THR 211
LYS 101 1.34 VAL 172 -1.53 MET 246
MET 169 1.24 VAL 173 -1.42 ARG 213
HIS 168 1.37 ARG 174 -0.99 LEU 206
HIS 168 1.18 ARG 175 -0.77 ARG 213
HIS 168 1.18 ARG 175 -0.77 ARG 213
LEU 130 1.25 CYS 176 -0.99 ARG 213
LEU 130 1.13 PRO 177 -0.87 PHE 212
LEU 137 1.50 HIS 178 -0.54 ASP 244
ALA 138 1.44 HIS 179 -0.62 MET 243
ALA 161 1.06 GLU 180 -0.32 ARG 213
ALA 138 1.52 ARG 181 -0.31 MET 243
HIS 233 1.69 CYS 182 -0.39 MET 243
HIS 233 1.69 CYS 182 -0.39 MET 243
ARG 181 0.97 GLY 187 -0.55 PRO 190
ARG 209 1.33 LEU 188 -0.83 PRO 223
GLN 100 1.00 ALA 189 -0.66 GLU 198
PHE 212 1.52 PRO 190 -0.65 MET 237
VAL 97 1.04 PRO 191 -1.02 ALA 138
GLU 171 1.13 GLN 192 -0.60 MET 237
GLN 100 1.09 HIS 193 -0.73 MET 237
ALA 161 1.30 LEU 194 -1.19 SER 240
CYS 182 1.10 ILE 195 -0.99 SER 240
CYS 182 1.24 ARG 196 -1.13 TYR 205
CYS 182 1.47 VAL 197 -0.89 TYR 205
CYS 182 1.58 GLU 198 -0.81 PRO 153
CYS 182 1.39 GLY 199 -1.05 PRO 223
CYS 182 1.11 ASN 200 -1.81 THR 230
CYS 182 0.97 LEU 201 -1.68 PRO 152
CYS 182 1.01 ARG 202 -1.56 PRO 153
CYS 182 1.02 VAL 203 -1.02 PRO 153
CYS 182 0.75 GLU 204 -0.90 PRO 128
GLN 100 0.87 TYR 205 -1.13 ARG 196
GLN 100 1.13 LEU 206 -1.10 SER 240
GLN 100 1.10 ASP 207 -1.06 SER 240
PRO 190 1.08 ASP 208 -1.33 THR 170
LEU 188 1.33 ARG 209 -1.34 THR 170
PRO 190 1.03 ASN 210 -1.62 THR 170
PRO 190 1.06 THR 211 -1.50 GLU 171
PRO 190 1.52 PHE 212 -1.13 SER 240
GLN 100 1.29 ARG 213 -1.52 SER 240
GLN 100 1.43 HIS 214 -1.39 SER 240
GLN 100 1.21 SER 215 -0.91 SER 240
GLN 100 1.23 SER 215 -0.91 SER 240
CYS 182 0.93 VAL 216 -1.00 TYR 126
CYS 182 0.91 VAL 217 -1.00 TYR 126
CYS 182 0.78 VAL 218 -1.35 TYR 126
CYS 182 0.76 PRO 219 -1.23 ASN 200
CYS 182 0.87 TYR 220 -1.54 LEU 145
CYS 182 1.29 GLU 221 -1.75 PRO 152
CYS 182 0.99 PRO 222 -1.57 LEU 201
SER 149 0.86 PRO 223 -1.28 LEU 201
CYS 182 0.96 GLU 224 -0.96 LEU 201
CYS 182 0.91 VAL 225 -0.91 PRO 128
CYS 182 0.94 GLY 226 -1.07 SER 127
CYS 182 1.01 SER 227 -1.17 SER 127
CYS 182 0.95 ASP 228 -1.36 LEU 201
CYS 182 1.01 CYS 229 -1.34 LEU 201
CYS 182 1.08 THR 230 -1.81 ASN 200
CYS 182 1.26 THR 231 -1.34 ASN 200
CYS 182 1.40 ILE 232 -1.31 VAL 218
CYS 182 1.69 HIS 233 -1.01 TYR 126
CYS 182 1.67 TYR 234 -1.04 TYR 126
CYS 182 1.58 ASN 235 -0.83 TYR 126
HIS 179 1.44 TYR 236 -0.98 ASN 239
HIS 179 1.20 MET 237 -0.92 PRO 191
PRO 250 1.51 CYS 238 -0.86 PRO 191
PRO 250 1.51 CYS 238 -0.87 PRO 191
LEU 130 1.11 ASN 239 -1.08 ARG 213
THR 284 1.35 SER 240 -1.52 ARG 213
LEU 130 1.44 SER 241 -1.09 ARG 213
LEU 130 1.46 CYS 242 -1.05 ARG 213
LEU 130 1.69 MET 243 -0.88 ARG 213
LEU 130 1.49 ASP 244 -0.88 VAL 172
LEU 130 1.43 GLY 245 -1.22 ARG 213
CYS 238 1.37 MET 246 -1.53 VAL 172
LEU 130 1.57 ASN 247 -0.98 VAL 172
LEU 130 1.43 ARG 248 -0.96 ARG 213
LEU 130 1.18 ARG 249 -1.05 THR 211
CYS 238 1.51 PRO 250 -0.95 THR 211
CYS 238 1.42 ILE 251 -0.99 PRO 98
PHE 113 1.22 LEU 252 -1.28 PRO 98
PHE 113 1.22 LEU 252 -1.28 PRO 98
CYS 182 1.22 THR 253 -1.42 PRO 98
CYS 182 1.22 ILE 254 -1.39 VAL 97
CYS 182 1.22 ILE 254 -1.39 VAL 97
CYS 182 1.14 ILE 255 -1.41 SER 99
CYS 182 1.00 THR 256 -1.22 SER 99
CYS 182 1.00 THR 256 -1.22 SER 99
CYS 182 0.91 LEU 257 -1.04 PRO 128
CYS 182 0.76 GLU 258 -1.11 PRO 128
CYS 182 0.76 GLU 258 -1.12 PRO 128
PRO 152 0.69 ASP 259 -1.17 PRO 128
GLN 100 0.46 SER 260 -1.11 PRO 128
PRO 152 0.62 SER 261 -0.98 PRO 128
PRO 152 0.52 GLY 262 -1.05 ARG 158
PRO 152 0.79 ASN 263 -0.98 PRO 128
PRO 151 0.78 LEU 264 -0.96 PRO 128
PRO 151 1.03 LEU 265 -1.08 PRO 128
PRO 222 0.91 GLY 266 -0.94 PRO 128
CYS 182 0.90 ARG 267 -1.12 ASN 131
CYS 182 0.93 ASN 268 -1.57 ASN 131
CYS 182 0.95 SER 269 -1.53 PRO 98
PHE 113 1.21 PHE 270 -1.81 PRO 98
PHE 113 1.55 GLU 271 -1.47 PRO 98
PHE 113 1.55 GLU 271 -1.47 PRO 98
PHE 113 1.33 VAL 272 -1.33 PRO 98
GLU 285 1.14 ARG 273 -1.09 PRO 98
ASP 281 1.04 VAL 274 -1.07 HIS 214
HIS 178 0.91 CYS 275 -0.96 ARG 213
HIS 178 0.90 ALA 276 -0.88 ARG 248
HIS 178 0.77 CYS 277 -0.84 PRO 98
HIS 178 0.87 PRO 278 -0.94 PRO 98
TYR 126 0.89 GLY 279 -0.85 PRO 98
TYR 126 0.96 ARG 280 -0.71 PRO 98
ARG 273 1.10 ASP 281 -0.71 PRO 98
ASN 131 1.25 ARG 282 -0.80 PRO 98
ASN 131 1.27 ARG 283 -0.59 PRO 98
SER 240 1.35 THR 284 -0.41 PRO 98
CYS 238 1.39 GLU 285 -0.33 PRO 98
ASN 131 1.25 GLU 286 -0.33 PRO 98

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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.