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CA distance fluctuations for 260612085305979267

---  normal mode 9  ---

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
ASP 183 0.18 MET 1 -1.22 ALA 211
ALA 82 0.22 GLU 2 -1.35 PHE 142
ASN 154 0.19 GLN 3 -1.22 PHE 142
ASN 154 0.20 PHE 4 -1.28 ALA 141
PRO 221 0.25 ASP 5 -1.12 ALA 141
PRO 221 0.36 PHE 6 -1.04 ALA 141
PRO 221 0.46 ASP 7 -0.89 LYS 166
PRO 221 0.53 VAL 8 -0.87 LYS 166
ARG 202 0.50 VAL 9 -0.90 ALA 141
ARG 202 0.62 ILE 10 -0.79 LYS 166
ARG 202 0.63 VAL 11 -0.68 ALA 141
PRO 176 0.70 GLY 12 -0.68 VAL 163
PRO 176 0.67 GLY 13 -0.86 VAL 163
PRO 176 0.89 GLY 14 -0.65 VAL 163
PRO 176 0.91 PRO 15 -0.63 LYS 166
ARG 202 0.94 ALA 16 -0.60 LYS 166
ARG 202 0.78 GLY 17 -0.74 LYS 166
PRO 221 0.71 CYS 18 -0.88 LYS 166
PRO 221 0.83 THR 19 -0.78 LYS 166
PRO 221 0.80 CYS 20 -0.77 LYS 166
PRO 221 0.65 ALA 21 -0.95 LYS 166
PRO 221 0.67 LEU 22 -0.95 LYS 166
PRO 221 0.73 TYR 23 -0.83 LYS 166
PRO 221 0.65 THR 24 -0.88 LYS 166
PRO 221 0.54 ALA 25 -1.02 LYS 166
GLY 222 0.60 ARG 26 -0.93 LYS 166
GLY 222 0.62 SER 27 -0.85 LYS 166
GLY 222 0.50 GLU 28 -0.95 LYS 166
PRO 221 0.50 LEU 29 -0.94 LYS 166
PRO 221 0.41 LYS 30 -1.07 LYS 166
PRO 221 0.46 THR 31 -1.08 LYS 166
PRO 221 0.40 VAL 32 -1.16 LYS 166
PRO 176 0.46 ILE 33 -1.05 LYS 166
PRO 176 0.40 LEU 34 -1.03 ALA 141
PRO 176 0.42 ASP 35 -0.96 VAL 163
ASN 154 0.39 LYS 36 -0.94 THR 137
ASN 154 0.48 ASN 37 -0.78 VAL 163
ASN 154 0.51 PRO 38 -0.79 VAL 163
ASN 154 0.60 ALA 39 -0.50 VAL 163
ASN 154 0.78 ALA 40 -0.38 GLY 41
PRO 176 0.93 GLY 41 -0.38 ALA 40
PRO 176 1.29 ALA 42 -0.30 ASN 281
PRO 176 1.19 LEU 43 -0.44 LYS 285
LYS 177 0.88 ALA 44 -0.47 GLU 188
LYS 177 1.05 ILE 45 -0.30 LYS 285
LYS 177 1.35 THR 46 -0.42 LYS 285
THR 181 1.20 HIS 47 -0.35 PRO 283
LYS 177 1.22 LYS 48 -0.37 LYS 285
LYS 177 1.26 ILE 49 -0.33 PHE 284
PRO 221 1.13 ALA 50 -0.31 GLU 188
PRO 221 1.33 ASN 51 -0.29 GLU 264
PRO 221 1.24 TYR 52 -0.38 GLU 188
PRO 221 1.26 PRO 53 -0.42 LYS 166
PRO 221 1.08 GLY 54 -0.53 LYS 166
PRO 221 0.99 VAL 55 -0.57 GLU 188
PRO 221 1.00 PRO 56 -0.51 GLU 188
PRO 221 0.94 GLY 57 -0.47 GLU 188
LYS 177 0.94 GLU 58 -0.43 GLU 188
LYS 177 0.87 MET 59 -0.57 GLU 188
LYS 177 0.91 SER 60 -0.52 GLU 188
LYS 177 1.03 GLY 61 -0.49 GLU 188
LYS 177 0.73 ASP 62 -0.71 GLU 188
LYS 177 0.60 HIS 63 -0.94 GLU 188
PRO 176 0.77 LEU 64 -0.77 GLU 188
PRO 176 0.76 LEU 65 -0.78 GLU 188
PRO 176 0.49 GLU 66 -1.08 GLU 188
PRO 221 0.57 VAL 67 -0.99 GLU 188
PRO 221 0.69 MET 68 -0.88 LYS 166
PRO 221 0.54 ARG 69 -1.05 LYS 166
PRO 221 0.43 ASP 70 -1.17 LYS 166
PRO 221 0.55 GLN 71 -1.06 LYS 166
PRO 221 0.55 ALA 72 -1.11 LYS 166
PRO 221 0.37 VAL 73 -1.32 LYS 166
PRO 221 0.38 GLU 74 -1.21 LYS 166
PRO 221 0.47 PHE 75 -1.11 LYS 166
PRO 221 0.37 GLY 76 -1.23 LYS 166
PRO 221 0.41 THR 77 -1.25 LYS 166
PRO 221 0.30 VAL 78 -1.42 LYS 166
PRO 176 0.32 TYR 79 -1.41 LYS 166
GLU 2 0.21 ARG 80 -1.34 LYS 166
ASN 154 0.36 ARG 81 -1.36 VAL 163
GLU 100 0.33 ALA 82 -1.50 THR 137
ASN 154 0.40 GLN 83 -0.81 CYS 138
ASN 154 0.39 VAL 84 -0.56 CYS 138
ASN 154 0.32 TYR 85 -0.49 LYS 242
ARG 202 0.38 GLY 86 -0.41 LYS 242
ALA 125 0.55 LEU 87 -0.37 ALA 141
ALA 125 0.57 ASP 88 -0.37 ALA 141
ALA 125 0.76 LEU 89 -0.35 ALA 141
ALA 125 0.72 SER 90 -0.28 ALA 141
ALA 125 0.58 GLU 91 -0.44 ALA 141
ALA 125 0.57 PRO 92 -0.52 ALA 141
ALA 119 0.47 VAL 93 -0.66 ALA 141
ALA 119 0.53 LYS 94 -0.63 ALA 141
ALA 119 0.39 LYS 95 -0.71 ALA 141
ARG 202 0.38 VAL 96 -0.76 ALA 141
ASN 154 0.28 TYR 97 -0.73 ALA 141
ALA 82 0.29 THR 98 -1.05 ASP 139
PRO 155 0.22 PRO 99 -1.36 ASP 139
ALA 82 0.33 GLU 100 -1.47 PHE 142
ALA 82 0.32 GLY 101 -1.34 PHE 142
ALA 82 0.29 ILE 102 -1.07 ALA 141
ARG 202 0.26 PHE 103 -1.14 ALA 141
ALA 119 0.34 THR 104 -0.95 ALA 141
PRO 221 0.43 GLY 105 -0.87 ALA 141
PRO 221 0.51 ARG 106 -0.72 ALA 141
SER 120 0.61 ALA 107 -0.67 ALA 141
ALA 119 0.67 LEU 108 -0.64 ALA 141
ARG 202 0.75 VAL 109 -0.59 LYS 166
ALA 119 0.91 LEU 110 -0.46 LYS 166
ARG 202 0.88 ALA 111 -0.53 VAL 163
ARG 202 0.90 THR 112 -0.45 VAL 163
ARG 202 1.06 GLY 113 -0.40 VAL 163
ARG 202 1.30 ALA 114 -0.32 CYS 138
PRO 176 1.20 MET 115 -0.35 CYS 138
ARG 202 1.09 GLY 116 -0.37 CYS 138
PRO 243 1.62 ARG 117 -0.47 GLY 240
PRO 243 1.32 ILE 118 -0.29 GLY 240
VAL 260 1.32 ALA 119 -0.21 LEU 153
GLY 259 1.76 SER 120 -0.37 LEU 153
GLY 258 1.96 ILE 121 -0.43 PRO 176
PRO 256 1.85 PRO 122 -0.47 PRO 176
PRO 256 1.58 GLY 123 -0.44 MET 1
GLY 258 1.38 GLU 124 -0.39 MET 1
GLY 250 1.51 ALA 125 -0.28 MET 1
MET 254 1.40 GLU 126 -0.45 MET 1
GLY 250 1.13 TYR 127 -0.65 MET 1
GLY 250 1.26 LEU 128 -0.53 PRO 99
GLY 250 0.82 GLY 129 -0.85 PRO 99
GLY 250 0.79 ARG 130 -0.97 MET 1
PRO 256 0.77 GLY 131 -0.91 MET 1
GLY 250 0.95 VAL 132 -0.68 PRO 99
ALA 249 0.84 SER 133 -0.62 PRO 99
ASP 246 0.90 TYR 134 -0.44 ALA 82
ALA 249 0.52 CYS 135 -0.74 ALA 82
ALA 249 0.44 ALA 136 -1.11 ALA 82
ALA 249 0.27 THR 137 -1.50 ALA 82
ALA 249 0.30 CYS 138 -1.15 ALA 82
ALA 249 0.41 ASP 139 -1.36 PRO 99
ALA 249 0.35 GLY 140 -1.24 GLU 100
PRO 256 0.21 ALA 141 -1.45 GLU 100
PRO 256 0.38 PHE 142 -1.47 GLU 100
PRO 256 0.46 TYR 143 -1.22 GLU 100
PRO 256 0.35 ARG 144 -1.16 PHE 4
PRO 256 0.43 ASN 145 -1.04 GLU 2
PRO 256 0.58 ARG 146 -1.01 GLU 2
PRO 256 0.68 GLU 147 -0.88 GLU 2
PRO 256 0.71 VAL 148 -0.81 GLU 100
GLY 258 0.81 VAL 149 -0.59 GLU 100
GLY 258 0.70 VAL 150 -0.48 ALA 82
GLN 239 0.85 VAL 151 -0.37 GLY 123
GLN 239 1.02 GLY 152 -0.38 ILE 121
ILE 45 0.93 LEU 153 -0.39 ILE 121
ALA 40 0.78 ASN 154 -0.27 SER 120
GLN 83 0.29 PRO 155 -0.27 HIS 63
PHE 247 0.35 GLU 156 -0.31 GLN 239
ASP 246 0.50 ALA 157 -0.24 GLU 66
ASP 246 0.37 VAL 158 -0.49 GLU 66
ASP 246 0.31 GLU 159 -0.64 GLU 66
ASP 246 0.38 GLU 160 -0.62 ARG 80
ASP 246 0.44 ALA 161 -0.78 ARG 80
ALA 249 0.24 GLN 162 -1.04 ARG 80
ALA 249 0.22 VAL 163 -1.36 ARG 81
ALA 249 0.33 LEU 164 -1.19 ARG 80
PRO 256 0.30 THR 165 -1.15 ARG 80
PRO 256 0.16 LYS 166 -1.42 VAL 78
PRO 256 0.27 PHE 167 -1.28 VAL 78
PRO 256 0.44 ALA 168 -1.04 ARG 80
PRO 256 0.47 SER 169 -0.96 VAL 78
PRO 256 0.56 THR 170 -0.82 ARG 80
PRO 256 0.58 VAL 171 -0.81 ARG 80
PRO 256 0.73 HIS 172 -0.58 ARG 80
GLY 258 0.68 TRP 173 -0.49 ARG 80
SER 241 0.98 ILE 174 -0.32 MET 1
GLY 240 1.17 THR 175 -0.38 PRO 122
SER 241 1.48 PRO 176 -0.47 PRO 122
THR 46 1.35 LYS 177 -0.41 PRO 122
THR 46 1.11 ASP 178 -0.30 PRO 122
HIS 47 0.87 PRO 179 -0.30 ILE 121
HIS 47 0.81 HIS 180 -0.26 ILE 121
HIS 47 1.20 THR 181 -0.35 ILE 121
HIS 47 0.54 LEU 182 -0.30 ILE 121
GLU 100 0.24 ASP 183 -0.27 SER 120
ASP 246 0.18 GLY 184 -0.58 HIS 63
ASP 246 0.19 HIS 185 -0.73 HIS 63
ASP 246 0.27 ALA 186 -0.59 GLU 66
ASP 246 0.21 ASP 187 -0.78 GLU 66
ASP 246 0.15 GLU 188 -1.08 GLU 66
ASP 246 0.26 LEU 189 -0.86 ASP 70
PRO 256 0.36 LEU 190 -0.69 ASP 70
PRO 256 0.28 ALA 191 -0.91 ASP 70
PRO 256 0.29 HIS 192 -1.00 VAL 73
PRO 256 0.37 PRO 193 -0.97 GLU 74
PRO 256 0.44 SER 194 -0.91 VAL 73
PRO 256 0.49 VAL 195 -0.76 ARG 80
PRO 256 0.63 LYS 196 -0.59 ARG 80
ASP 257 0.67 LEU 197 -0.46 ARG 80
SER 241 0.89 TRP 198 -0.37 MET 1
SER 241 1.01 GLU 199 -0.26 MET 1
SER 241 1.28 LYS 200 -0.24 PRO 122
SER 241 1.34 THR 201 -0.20 MET 1
SER 241 1.57 ARG 202 -0.23 ILE 204
GLY 258 1.41 LEU 203 -0.37 PRO 176
ASP 257 1.63 ILE 204 -0.26 PRO 176
ASP 257 1.65 ARG 205 -0.40 MET 1
PRO 256 1.42 ILE 206 -0.55 MET 1
PRO 256 1.37 LYS 207 -0.66 MET 1
PRO 256 1.16 GLY 208 -0.84 MET 1
PRO 256 1.09 GLU 209 -0.89 MET 1
PRO 256 0.95 GLU 210 -0.99 MET 1
PRO 256 0.78 ALA 211 -1.22 MET 1
PRO 256 0.90 GLY 212 -1.06 MET 1
PRO 256 1.02 VAL 213 -0.91 MET 1
PRO 256 1.00 THR 214 -0.89 MET 1
PRO 256 1.09 ALA 215 -0.75 MET 1
PRO 256 1.24 VAL 216 -0.59 MET 1
ASP 257 1.33 GLU 217 -0.48 MET 1
ASP 257 1.31 VAL 218 -0.38 MET 1
PRO 283 1.44 ARG 219 -0.27 MET 1
PRO 283 1.38 HIS 220 -0.24 MET 1
PHE 284 1.54 PRO 221 -0.11 GLN 227
PHE 284 1.33 GLY 222 -0.12 LYS 196
PRO 283 1.28 GLU 223 -0.19 MET 1
PRO 283 1.26 SER 224 -0.16 MET 1
PRO 283 1.24 ASP 225 -0.28 MET 1
PRO 283 1.28 SER 226 -0.35 MET 1
ASP 257 1.11 GLN 227 -0.46 MET 1
PRO 256 1.11 GLU 228 -0.56 MET 1
PRO 256 1.02 LEU 229 -0.63 MET 1
PRO 256 0.94 LEU 230 -0.76 GLU 2
PRO 256 0.88 ALA 231 -0.81 GLU 2
PRO 256 0.82 GLU 232 -0.96 MET 1
PRO 256 0.75 GLY 233 -0.89 GLU 100
GLY 258 0.89 VAL 234 -0.63 MET 1
ASP 246 0.77 PHE 235 -0.54 ALA 82
ASP 246 0.95 VAL 236 -0.26 GLU 124
ASP 246 0.76 TYR 237 -0.22 SER 120
GLY 116 1.01 LEU 238 -0.24 SER 120
THR 175 1.05 GLN 239 -0.32 ARG 117
PRO 176 1.39 GLY 240 -0.47 ARG 117
ARG 202 1.57 SER 241 -0.36 ASP 246
ARG 202 1.55 LYS 242 -0.61 ILE 244
ARG 117 1.62 PRO 243 -0.30 ALA 114
ARG 117 1.22 ILE 244 -0.61 LYS 242
ALA 119 1.27 THR 245 -0.53 LYS 242
VAL 236 0.95 ASP 246 -0.58 LYS 242
TYR 134 0.70 PHE 247 -0.47 LYS 242
ALA 125 1.00 VAL 248 -0.34 LYS 242
LEU 128 1.11 ALA 249 -0.37 LYS 242
ALA 125 1.51 GLY 250 -0.25 GLY 258
ALA 125 1.28 GLN 251 -0.15 GLY 258
ALA 125 1.38 VAL 252 -0.12 VAL 289
ALA 125 1.41 GLU 253 -0.14 VAL 289
PRO 122 1.52 MET 254 -0.17 THR 282
PRO 122 1.68 LYS 255 -0.16 LYS 48
PRO 122 1.85 PRO 256 -0.14 THR 46
PRO 122 1.72 ASP 257 -0.18 THR 46
ILE 121 1.96 GLY 258 -0.25 GLY 250
SER 120 1.76 GLY 259 -0.18 PRO 38
SER 120 1.50 VAL 260 -0.15 PRO 38
SER 120 1.36 TRP 261 -0.21 VAL 289
SER 120 1.17 VAL 262 -0.25 VAL 289
ILE 204 1.07 ASP 263 -0.25 LYS 166
SER 224 1.10 GLU 264 -0.32 PRO 53
GLY 222 0.98 MET 265 -0.41 LYS 166
ILE 204 1.00 MET 266 -0.39 LYS 166
SER 120 0.98 GLN 267 -0.37 LYS 166
SER 120 1.11 THR 268 -0.25 LYS 166
ALA 125 1.09 SER 269 -0.17 LYS 166
ALA 125 1.00 VAL 270 -0.24 LYS 166
ALA 125 0.83 PRO 271 -0.35 LYS 166
SER 120 0.75 GLY 272 -0.48 LYS 166
SER 120 0.86 VAL 273 -0.43 LYS 166
SER 120 0.95 TRP 274 -0.44 LYS 166
SER 120 1.07 GLY 275 -0.38 LYS 166
ARG 202 1.03 ILE 276 -0.44 LYS 166
ARG 202 1.12 GLY 277 -0.43 VAL 163
ARG 202 1.31 ASP 278 -0.35 PRO 38
SER 120 1.24 ILE 279 -0.27 VAL 163
SER 120 1.35 ARG 280 -0.24 PRO 38
ILE 204 1.46 ASN 281 -0.30 ALA 42
ILE 204 1.41 THR 282 -0.34 THR 46
PRO 221 1.50 PRO 283 -0.38 THR 46
PRO 221 1.54 PHE 284 -0.37 LYS 48
ARG 202 1.43 LYS 285 -0.44 LEU 43
PRO 221 1.38 GLN 286 -0.33 LYS 48
PRO 221 1.20 ALA 287 -0.39 GLU 188
PRO 221 1.25 VAL 288 -0.42 LYS 166
PRO 221 1.30 VAL 289 -0.38 LYS 166
PRO 221 1.16 ALA 290 -0.45 LYS 166
PRO 221 1.06 ALA 291 -0.56 LYS 166
PRO 221 1.14 GLY 292 -0.50 LYS 166
PRO 221 1.10 ASP 293 -0.48 LYS 166
PRO 221 0.95 GLY 294 -0.61 LYS 166
PRO 221 0.95 CYS 295 -0.63 LYS 166
PRO 221 1.00 ILE 296 -0.53 LYS 166
PRO 221 0.91 ALA 297 -0.57 LYS 166
PRO 221 0.81 ALA 298 -0.69 LYS 166
GLY 222 0.85 MET 299 -0.63 LYS 166
GLY 222 0.86 ALA 300 -0.55 LYS 166
PRO 221 0.75 ILE 301 -0.64 LYS 166
GLY 222 0.72 ASP 302 -0.70 LYS 166
GLY 222 0.77 ARG 303 -0.59 LYS 166
GLY 222 0.73 PHE 304 -0.57 LYS 166
GLY 222 0.63 LEU 305 -0.67 LYS 166
GLY 222 0.63 ASN 306 -0.67 LYS 166
GLY 222 0.68 SER 307 -0.58 LYS 166

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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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.