CNRS Nantes University US2B US2B
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***  AF-1F0N_recycle_12  ***

CA distance fluctuations for 2402070206021787280

---  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
GLY 29 0.20 SER 1 -0.49 ASN 222
VAL 7 0.38 ARG 2 -0.54 ASN 222
GLU 8 0.75 PRO 3 -0.49 ASN 222
GLU 8 0.44 GLY 4 -0.46 LEU 218
GLY 29 0.39 LEU 5 -0.41 ASN 222
ASN 30 0.47 PRO 6 -0.36 ASN 222
PRO 3 0.71 VAL 7 -0.32 ASN 222
PRO 3 0.75 GLU 8 -0.29 ASN 222
PRO 3 0.61 TYR 9 -0.28 ILE 223
PRO 3 0.50 LEU 10 -0.26 PRO 224
PRO 3 0.39 GLN 11 -0.23 PRO 224
PRO 3 0.35 VAL 12 -0.24 PRO 224
PRO 3 0.30 PRO 13 -0.21 PRO 224
PRO 3 0.24 SER 14 -0.22 PRO 224
PRO 3 0.21 PRO 15 -0.19 PRO 224
PRO 3 0.17 SER 16 -0.22 ASP 184
TYR 137 0.18 MET 17 -0.21 PRO 224
PRO 3 0.17 GLY 18 -0.18 PRO 224
PRO 3 0.20 ARG 19 -0.19 ILE 223
PRO 3 0.26 ASP 20 -0.20 ILE 223
PRO 3 0.27 ILE 21 -0.25 PRO 224
PRO 3 0.32 LYS 22 -0.28 PRO 224
PRO 3 0.37 VAL 23 -0.31 PRO 224
PRO 3 0.41 GLN 24 -0.34 PRO 224
PRO 3 0.46 PHE 25 -0.31 PRO 224
PRO 3 0.40 GLN 26 -0.30 ASN 222
PRO 3 0.38 SER 27 -0.30 ASN 250
PRO 3 0.26 GLY 28 -0.36 ASN 250
PRO 6 0.46 GLY 29 -0.39 ASN 250
PRO 6 0.47 ASN 30 -0.46 ASN 203
PRO 6 0.33 ASN 31 -0.50 ASN 203
PRO 3 0.25 SER 32 -0.46 ASN 250
PRO 3 0.16 PRO 33 -0.43 ASN 250
PRO 3 0.18 ALA 34 -0.32 ASN 250
GLN 278 0.17 VAL 35 -0.32 PRO 224
GLN 278 0.14 TYR 36 -0.35 PRO 224
LYS 274 0.18 LEU 37 -0.40 PRO 224
LYS 274 0.16 LEU 38 -0.43 PRO 224
LYS 274 0.17 ASP 39 -0.53 PRO 224
ALA 170 0.21 GLY 40 -0.63 PRO 224
ALA 150 0.25 LEU 41 -0.62 PRO 224
SER 149 0.18 ARG 42 -0.60 PRO 224
ARG 42 0.17 ALA 43 -0.52 PRO 224
ASP 20 0.14 GLN 44 -0.42 PRO 224
ASP 20 0.18 ASP 45 -0.35 ILE 223
GLN 11 0.16 ASP 46 -0.35 ILE 223
PRO 3 0.16 TYR 47 -0.38 ILE 223
ARG 42 0.12 ASN 48 -0.43 PRO 224
ASP 169 0.13 GLY 49 -0.55 PRO 224
ASP 169 0.14 TRP 50 -0.48 PRO 224
GLY 29 0.11 ASP 51 -0.46 ASN 222
ASP 169 0.11 ILE 52 -0.51 ASN 222
ASP 169 0.14 ASN 53 -0.61 ASN 222
ASP 169 0.13 THR 54 -0.53 ASN 222
GLY 29 0.13 PRO 55 -0.49 ASN 222
TRP 59 0.13 ALA 56 -0.43 ASN 222
GLY 29 0.17 PHE 57 -0.39 ASN 222
GLY 29 0.19 GLU 58 -0.41 ASN 222
ALA 56 0.13 TRP 59 -0.36 GLY 4
ASP 169 0.12 TYR 60 -0.31 ASN 222
GLY 29 0.25 TYR 61 -0.32 ASN 222
GLY 29 0.25 GLN 62 -0.29 ASN 250
ALA 166 0.11 SER 63 -0.34 ASN 250
GLN 62 0.16 GLY 64 -0.38 ASN 250
PRO 3 0.11 LEU 65 -0.38 ASN 250
PRO 3 0.23 SER 66 -0.32 ASN 250
PRO 3 0.20 ILE 67 -0.33 PRO 224
PRO 3 0.24 VAL 68 -0.34 PRO 224
PRO 3 0.20 MET 69 -0.38 PRO 224
PRO 3 0.22 PRO 70 -0.36 PRO 224
PRO 3 0.19 VAL 71 -0.36 PRO 224
ASP 20 0.15 GLY 72 -0.37 PRO 224
ALA 246 0.16 GLY 73 -0.39 PRO 224
TYR 243 0.19 GLN 74 -0.41 PRO 224
ALA 150 0.29 SER 75 -0.37 PRO 224
TYR 243 0.26 SER 76 -0.34 PRO 224
TYR 243 0.27 PHE 77 -0.36 PRO 224
ILE 133 0.22 TYR 78 -0.34 PRO 224
ILE 133 0.39 SER 79 -0.33 ALA 186
LYS 198 0.34 ASP 80 -0.31 TRP 179
GLN 195 0.45 TRP 81 -0.26 LYS 95
GLN 195 0.44 TYR 82 -0.21 SER 16
ALA 246 0.41 SER 83 -0.18 LEU 165
GLN 195 0.35 PRO 84 -0.16 PRO 224
ASP 191 0.36 ALA 85 -0.17 ILE 223
ALA 245 0.35 CYS 86 -0.17 ASP 45
ALA 242 0.34 GLY 87 -0.14 ILE 223
ALA 245 0.28 LYS 88 -0.20 ILE 223
ALA 245 0.23 ALA 89 -0.27 ILE 223
ALA 245 0.27 GLY 90 -0.29 ASP 45
ALA 246 0.30 CYS 91 -0.23 ASP 45
GLN 195 0.27 GLN 92 -0.23 ASP 45
GLN 195 0.28 THR 93 -0.20 PRO 224
GLN 195 0.29 TYR 94 -0.24 PRO 224
TYR 137 0.27 LYS 95 -0.26 TRP 81
GLU 97 0.25 TRP 96 -0.30 PRO 224
TRP 96 0.25 GLU 97 -0.42 ALA 186
GLN 140 0.18 THR 98 -0.39 ALA 186
PRO 3 0.20 PHE 99 -0.32 ALA 186
PRO 3 0.19 LEU 100 -0.34 ALA 186
THR 117 0.22 THR 101 -0.39 ALA 186
PRO 3 0.23 SER 102 -0.38 ALA 186
PRO 3 0.26 GLU 103 -0.31 ALA 186
PRO 3 0.30 LEU 104 -0.30 ALA 186
PRO 3 0.30 PRO 105 -0.31 ALA 186
PRO 3 0.33 GLN 106 -0.30 PRO 185
PRO 3 0.37 TRP 107 -0.27 ALA 186
PRO 3 0.40 LEU 108 -0.29 ASN 203
PRO 3 0.38 SER 109 -0.34 ASN 203
PRO 3 0.40 ALA 110 -0.29 ASN 203
PRO 3 0.46 ASN 111 -0.29 ASN 203
PRO 3 0.48 ARG 112 -0.33 ASN 203
PRO 3 0.42 ALA 113 -0.37 ASN 203
PRO 3 0.35 VAL 114 -0.39 ASN 203
PRO 3 0.28 LYS 115 -0.41 ASN 203
PRO 3 0.26 PRO 116 -0.37 GLN 141
THR 101 0.22 THR 117 -0.41 ASN 202
THR 101 0.18 GLY 118 -0.52 ASN 203
LEU 281 0.22 SER 119 -0.34 THR 204
SER 279 0.18 ALA 120 -0.29 PRO 224
LEU 277 0.18 ALA 121 -0.32 PRO 224
ALA 166 0.20 ILE 122 -0.36 PRO 224
ALA 166 0.24 GLY 123 -0.40 PRO 224
ALA 166 0.31 LEU 124 -0.49 PRO 224
ALA 166 0.46 SER 125 -0.51 PRO 224
ALA 166 0.35 MET 126 -0.46 PRO 224
LEU 41 0.24 ALA 127 -0.42 PRO 224
SER 147 0.36 GLY 128 -0.37 PRO 224
ALA 166 0.28 SER 129 -0.31 PRO 224
MET 132 0.26 SER 130 -0.31 PRO 224
SER 79 0.21 ALA 131 -0.32 PRO 224
SER 79 0.31 MET 132 -0.25 PRO 224
SER 79 0.39 ILE 133 -0.28 ASP 191
SER 79 0.30 LEU 134 -0.26 PRO 224
SER 79 0.27 ALA 135 -0.25 ASN 31
TRP 81 0.33 ALA 136 -0.26 GLN 195
ASP 80 0.33 TYR 137 -0.22 GLN 194
ASP 80 0.22 HIS 138 -0.31 PRO 116
ASP 80 0.18 PRO 139 -0.32 LYS 198
THR 98 0.18 GLN 140 -0.35 ASN 202
SER 280 0.16 GLN 141 -0.37 PRO 116
SER 280 0.19 PHE 142 -0.28 LEU 199
SER 79 0.17 ILE 143 -0.43 THR 204
SER 79 0.19 TYR 144 -0.34 SER 32
ALA 166 0.22 ALA 145 -0.26 PRO 224
ALA 166 0.26 GLY 146 -0.29 PRO 224
ALA 166 0.36 SER 147 -0.27 PRO 224
ALA 166 0.39 LEU 148 -0.33 PRO 224
ALA 166 0.54 SER 149 -0.26 PRO 224
ALA 166 0.57 ALA 150 -0.27 PRO 224
ALA 166 0.56 LEU 151 -0.18 PRO 224
ALA 166 0.42 LEU 152 -0.18 ASN 31
ALA 242 0.54 ASP 153 -0.22 ILE 133
LYS 174 0.49 PRO 154 -0.23 SER 129
ALA 245 0.57 SER 155 -0.25 ASN 190
ALA 242 0.64 GLN 156 -0.21 THR 101
ALA 245 0.54 GLY 157 -0.20 THR 101
ALA 245 0.44 MET 158 -0.24 MET 126
ALA 242 0.48 GLY 159 -0.28 MET 126
LYS 174 0.45 PRO 160 -0.22 PHE 77
LYS 174 0.42 SER 161 -0.16 THR 101
SER 235 0.42 LEU 162 -0.24 LEU 41
LEU 151 0.53 ILE 163 -0.16 LEU 41
ALA 245 0.38 GLY 164 -0.26 ALA 175
LEU 228 0.63 LEU 165 -0.34 ALA 175
ALA 150 0.57 ALA 166 -0.15 ALA 175
LEU 151 0.47 MET 167 -0.13 ASP 177
LEU 151 0.41 GLY 168 -0.18 LYS 174
HIS 261 0.49 ASP 169 -0.15 LYS 174
HIS 261 0.34 ALA 170 -0.28 ILE 223
ALA 150 0.29 GLY 171 -0.24 ILE 223
GLY 164 0.37 GLY 172 -0.12 SER 83
LEU 151 0.39 TYR 173 -0.15 SER 83
ALA 175 0.55 LYS 174 -0.18 GLY 168
LYS 174 0.55 ALA 175 -0.34 LEU 165
ALA 245 0.46 ALA 176 -0.30 LEU 165
ALA 245 0.43 ASP 177 -0.23 LEU 165
ASP 191 0.46 MET 178 -0.22 LEU 165
ALA 246 0.46 TRP 179 -0.31 ASP 80
ALA 245 0.48 GLY 180 -0.28 LEU 165
ALA 245 0.49 PRO 181 -0.27 LEU 165
ALA 245 0.54 SER 182 -0.26 GLU 97
ALA 245 0.60 SER 183 -0.28 SER 102
ALA 245 0.56 ASP 184 -0.34 THR 98
ALA 246 0.61 PRO 185 -0.36 SER 102
ALA 246 0.52 ALA 186 -0.42 GLU 97
ALA 246 0.51 TRP 187 -0.29 THR 101
ALA 246 0.63 GLU 188 -0.35 ARG 189
GLN 195 0.47 ARG 189 -0.35 GLU 188
GLN 195 0.43 ASN 190 -0.26 THR 101
MET 178 0.46 ASP 191 -0.28 ILE 133
MET 178 0.38 PRO 192 -0.21 ASN 31
TYR 243 0.53 THR 193 -0.21 ASN 31
ALA 246 0.61 GLN 194 -0.23 ALA 136
ARG 189 0.47 GLN 195 -0.26 PRO 139
GLY 248 0.43 ILE 196 -0.29 ASN 31
GLU 188 0.46 PRO 197 -0.30 ASN 31
TRP 81 0.40 LYS 198 -0.32 PRO 139
TRP 81 0.36 LEU 199 -0.37 GLY 118
GLU 188 0.35 VAL 200 -0.41 GLY 118
TYR 82 0.35 ALA 201 -0.38 ASN 31
TRP 81 0.29 ASN 202 -0.47 GLY 118
TRP 81 0.28 ASN 203 -0.52 GLY 118
TRP 81 0.25 THR 204 -0.47 GLY 118
ALA 166 0.23 ARG 205 -0.42 LEU 281
ALA 166 0.28 LEU 206 -0.32 SER 32
ALA 166 0.30 TRP 207 -0.26 SER 32
ALA 166 0.36 VAL 208 -0.21 SER 32
ALA 166 0.40 TYR 209 -0.22 ARG 2
ALA 166 0.44 CYS 210 -0.22 ARG 2
ALA 166 0.40 GLY 211 -0.25 ARG 2
LEU 165 0.38 ASN 212 -0.25 ARG 2
LEU 165 0.40 GLY 213 -0.30 ARG 2
LEU 165 0.34 THR 214 -0.33 ARG 2
LEU 165 0.35 PRO 215 -0.40 ARG 2
LEU 165 0.31 ASN 216 -0.40 PRO 3
LEU 165 0.32 GLU 217 -0.48 PRO 3
LEU 165 0.32 LEU 218 -0.50 ARG 2
LEU 165 0.35 GLY 219 -0.49 ARG 2
LEU 165 0.41 GLY 220 -0.47 ARG 2
LEU 165 0.30 ALA 221 -0.49 ARG 2
LEU 165 0.30 ASN 222 -0.61 ASN 53
ASN 230 0.23 ILE 223 -0.54 ASN 53
LEU 165 0.30 PRO 224 -0.63 GLY 40
LEU 165 0.47 ALA 225 -0.39 TRP 263
LEU 165 0.43 GLU 226 -0.33 ARG 2
LEU 165 0.47 PHE 227 -0.30 ARG 2
LEU 165 0.63 LEU 228 -0.30 SER 125
LEU 165 0.54 GLU 229 -0.25 ARG 2
LEU 165 0.47 ASN 230 -0.23 ARG 2
LEU 165 0.52 PHE 231 -0.19 ARG 2
LEU 165 0.55 VAL 232 -0.18 ARG 2
LEU 165 0.46 ARG 233 -0.20 ARG 2
LEU 165 0.44 SER 234 -0.18 ASN 31
ILE 163 0.47 SER 235 -0.18 ASN 31
ALA 166 0.44 ASN 236 -0.20 ASN 31
LEU 165 0.39 LEU 237 -0.21 ASN 31
GLN 156 0.48 LYS 238 -0.26 PHE 239
ASP 153 0.53 PHE 239 -0.26 LYS 238
ALA 166 0.35 GLN 240 -0.27 ASN 31
GLN 156 0.51 ASP 241 -0.29 ASN 31
GLN 156 0.64 ALA 242 -0.31 ASN 31
THR 193 0.53 TYR 243 -0.33 ASN 31
GLN 156 0.45 ASN 244 -0.34 ASN 31
GLN 156 0.63 ALA 245 -0.36 SER 280
GLU 188 0.63 ALA 246 -0.37 ASN 31
GLU 188 0.51 GLY 247 -0.41 SER 280
GLU 188 0.46 GLY 248 -0.47 SER 280
GLU 188 0.39 HIS 249 -0.49 SER 280
GLU 188 0.29 ASN 250 -0.63 SER 280
ALA 166 0.31 ALA 251 -0.38 SER 280
ALA 166 0.31 VAL 252 -0.29 MET 273
ALA 166 0.35 PHE 253 -0.23 SER 32
ALA 166 0.35 ASN 254 -0.25 ARG 2
ALA 166 0.36 PHE 255 -0.23 ARG 2
LEU 165 0.32 PRO 256 -0.24 ARG 2
LEU 165 0.31 PRO 257 -0.24 ARG 2
LEU 165 0.34 ASN 258 -0.29 ARG 2
LEU 165 0.38 GLY 259 -0.31 ARG 2
LEU 165 0.44 THR 260 -0.33 ARG 2
ALA 166 0.52 HIS 261 -0.37 ALA 225
ASP 169 0.44 SER 262 -0.49 ASN 222
ASP 169 0.31 TRP 263 -0.60 ASN 222
ASP 169 0.30 GLU 264 -0.46 ARG 2
ALA 166 0.33 TYR 265 -0.37 ARG 2
ALA 166 0.33 TRP 266 -0.33 PRO 224
ASP 169 0.24 GLY 267 -0.38 ASN 222
ALA 166 0.25 ALA 268 -0.36 LEU 218
ALA 166 0.29 GLN 269 -0.29 LEU 218
ALA 166 0.24 LEU 270 -0.31 ASN 222
ALA 166 0.23 ASN 271 -0.37 LEU 218
ALA 166 0.25 ALA 272 -0.34 LEU 218
ALA 166 0.24 MET 273 -0.29 VAL 252
ALA 166 0.21 LYS 274 -0.30 ASN 250
ALA 166 0.22 GLY 275 -0.31 ASN 250
ALA 166 0.22 ASP 276 -0.40 ASN 250
ALA 166 0.20 LEU 277 -0.44 ASN 250
SER 119 0.18 GLN 278 -0.44 ASN 250
ALA 166 0.19 SER 279 -0.53 ASN 250
PHE 142 0.19 SER 280 -0.63 ASN 250
SER 119 0.22 LEU 281 -0.55 ASN 250
SER 119 0.15 GLY 282 -0.51 ASN 250
SER 119 0.14 ALA 283 -0.43 ASN 250
ALA 166 0.13 GLY 284 -0.36 ASN 250

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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.