Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* open cutoff8 melek *

CA distance fluctuations for 260522120615405517

--- normal mode 8 ---

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 increase ref largest decrease
SER 2 0.73 ALA 1 -0.13 ALA 12

ALA 1 0.73 SER 2 -0.03 PRO 422

ALA 1 0.35 SER 3 -0.02 PRO 422

ARG 421 0.13 THR 4 -0.00 SER 41

ARG 421 0.16 ASN 5 -0.02 ALA 1

ARG 421 0.19 LEU 6 -0.00 ILE 36

ARG 421 0.22 LYS 7 -0.00 LEU 33

ARG 421 0.15 ASP 8 -0.10 ALA 1

SER 424 0.13 VAL 9 -0.06 ALA 1

ARG 421 0.15 LEU 10 -0.02 ALA 1

PRO 422 0.18 ALA 11 -0.09 ALA 1

PRO 422 0.18 ALA 12 -0.13 ALA 1

PRO 422 0.18 LEU 13 -0.07 ALA 1

PRO 422 0.24 ILE 14 -0.06 ALA 1

PRO 422 0.30 PRO 15 -0.10 ALA 1

PRO 422 0.26 LYS 16 -0.14 ARG 421

PRO 422 0.28 GLU 17 -0.10 ARG 421

PRO 422 0.37 GLN 18 -0.09 ARG 421

PRO 422 0.37 ALA 19 -0.27 ARG 421

PRO 422 0.35 ARG 20 -0.35 ARG 421

PRO 422 0.42 ILE 21 -0.30 ARG 421

PRO 422 0.49 LYS 22 -0.39 ARG 421

PRO 422 0.44 THR 23 -0.59 ARG 421

PRO 422 0.44 PHE 24 -0.64 ARG 421

PRO 422 0.56 ARG 25 -0.63 ARG 421

PRO 422 0.55 GLN 26 -0.77 ARG 421

PRO 422 0.50 GLN 27 -1.03 ARG 421

PRO 422 0.49 HIS 28 -1.10 ARG 421

PRO 422 0.61 GLY 29 -0.88 ARG 421

PRO 422 0.67 GLY 30 -1.06 ARG 421

PRO 422 0.54 THR 31 -1.16 ARG 421

PRO 422 0.51 ALA 32 -0.90 ARG 421

PRO 422 0.42 LEU 33 -0.56 ARG 421

PRO 422 0.38 GLY 34 -0.55 LYS 423

PRO 422 0.38 GLN 35 -0.67 LYS 423

THR 427 0.42 ILE 36 -0.90 LYS 423

THR 427 0.46 THR 37 -1.04 LYS 423

THR 427 0.57 VAL 38 -0.84 LYS 423

THR 427 0.47 ASP 39 -1.06 LYS 423

THR 427 0.45 MET 40 -1.60 LYS 423

ARG 421 0.58 SER 41 -1.05 LYS 423

ARG 421 0.59 TYR 42 -0.84 LYS 423

ARG 421 0.54 GLY 43 -1.04 LYS 423

ARG 421 0.71 GLY 44 -0.86 LYS 423

ARG 421 0.61 MET 45 -1.13 LYS 423

ARG 421 0.42 ARG 46 -1.18 LYS 423

THR 427 0.32 GLY 47 -1.02 LYS 423

THR 427 0.35 MET 48 -0.97 LYS 423

THR 427 0.30 LYS 49 -0.58 LYS 423

PRO 422 0.43 GLY 50 -0.31 LYS 423

ARG 421 0.37 LEU 51 -0.22 LYS 423

PRO 422 0.28 VAL 52 -0.12 LYS 423

ARG 421 0.32 TYR 53 -0.15 LYS 423

ARG 421 0.17 GLU 54 -0.14 LYS 423

ARG 421 0.22 THR 55 -0.17 LYS 423

ARG 421 0.18 SER 56 -0.27 LYS 423

THR 427 0.16 VAL 57 -0.37 LYS 423

THR 427 0.15 LEU 58 -0.46 LYS 423

THR 427 0.14 ASP 59 -0.45 LYS 423

THR 427 0.13 PRO 60 -0.52 LYS 423

THR 427 0.12 ASP 61 -0.44 LYS 423

ALA 1 0.11 GLU 62 -0.40 LYS 423

ALA 1 0.12 GLY 63 -0.42 LYS 423

ARG 421 0.13 ILE 64 -0.38 LYS 423

THR 427 0.13 ARG 65 -0.31 LYS 423

THR 427 0.13 PHE 66 -0.23 LYS 423

THR 427 0.14 ARG 67 -0.21 LYS 423

THR 427 0.13 GLY 68 -0.25 LYS 423

THR 427 0.12 PHE 69 -0.24 LYS 423

ALA 1 0.13 SER 70 -0.29 LYS 423

ALA 1 0.16 ILE 71 -0.29 LYS 423

ALA 1 0.17 PRO 72 -0.27 LYS 423

ALA 1 0.16 GLU 73 -0.24 LYS 423

ALA 1 0.18 CYS 74 -0.21 LYS 423

ALA 1 0.21 GLN 75 -0.23 PRO 422

ALA 1 0.21 LYS 76 -0.20 LYS 423

ALA 1 0.20 LEU 77 -0.17 LYS 423

ALA 1 0.24 LEU 78 -0.16 PRO 422

ALA 1 0.31 PRO 79 -0.16 PRO 422

ALA 1 0.34 LYS 80 -0.19 PRO 422

ALA 1 0.39 GLY 81 -0.21 PRO 422

ALA 1 0.42 GLY 82 -0.18 PRO 422

ALA 1 0.33 GLY 84 -0.23 PRO 422

ALA 1 0.29 GLY 85 -0.24 PRO 422

ALA 1 0.28 GLU 86 -0.27 PRO 422

ALA 1 0.29 PRO 87 -0.24 PRO 422

ALA 1 0.32 LEU 88 -0.23 PRO 422

ARG 421 0.28 PRO 89 -0.25 PRO 422

ALA 1 0.31 GLU 90 -0.18 PRO 422

ALA 1 0.28 GLY 91 -0.15 PRO 422

ALA 1 0.23 LEU 92 -0.18 PRO 422

ARG 421 0.28 PHE 93 -0.15 PRO 422

ARG 421 0.21 TRP 94 -0.08 PRO 422

ALA 1 0.16 LEU 95 -0.11 LYS 423

ARG 421 0.21 LEU 96 -0.11 LYS 423

ARG 421 0.23 VAL 97 -0.04 LYS 423

THR 427 0.13 THR 98 -0.05 LYS 423

THR 427 0.13 GLY 99 -0.10 LYS 423

THR 427 0.12 GLN 100 -0.10 LYS 423

ALA 1 0.16 ILE 101 -0.11 LYS 423

ALA 1 0.22 PRO 102 -0.08 LYS 423

ALA 1 0.26 THR 103 -0.08 LYS 423

ALA 1 0.41 GLY 104 -0.09 PRO 422

ALA 1 0.52 ALA 105 -0.07 PRO 422

ALA 1 0.34 GLN 106 -0.06 PRO 422

ALA 1 0.40 VAL 107 -0.11 PRO 422

ALA 1 0.57 SER 108 -0.11 PRO 422

ALA 1 0.51 TRP 109 -0.07 PRO 422

ALA 1 0.40 LEU 110 -0.10 PRO 422

ALA 1 0.47 SER 111 -0.14 PRO 422

ALA 1 0.55 LYS 112 -0.11 PRO 422

ALA 1 0.38 GLU 113 -0.08 PRO 422

ARG 421 0.35 TRP 114 -0.13 PRO 422

ALA 1 0.41 ALA 115 -0.15 PRO 422

ARG 421 0.35 LYS 116 -0.10 PRO 422

ARG 421 0.40 ARG 117 -0.10 PRO 422

ARG 421 0.42 ALA 118 -0.16 PRO 422

ARG 421 0.45 ALA 119 -0.15 PRO 422

ARG 421 0.50 LEU 120 -0.18 PRO 422

ARG 421 0.52 PRO 121 -0.15 PRO 422

ARG 421 0.51 SER 122 -0.16 PRO 422

ARG 421 0.56 HIS 123 -0.17 PRO 422

ARG 421 0.58 VAL 124 -0.22 PRO 422

ARG 421 0.52 VAL 125 -0.24 PRO 422

ARG 421 0.54 THR 126 -0.23 PRO 422

ARG 421 0.58 MET 127 -0.27 PRO 422

ARG 421 0.56 LEU 128 -0.32 PRO 422

ARG 421 0.52 ASP 129 -0.30 PRO 422

ARG 421 0.54 ASN 130 -0.30 PRO 422

ARG 421 0.58 PHE 131 -0.36 PRO 422

ARG 421 0.56 PRO 132 -0.39 PRO 422

ARG 421 0.53 THR 133 -0.44 PRO 422

ARG 421 0.56 ASN 134 -0.48 PRO 422

ARG 421 0.60 LEU 135 -0.50 PRO 422

ARG 421 0.60 HIS 136 -0.57 PRO 422

ARG 421 0.58 PRO 137 -0.54 PRO 422

ARG 421 0.63 MET 138 -0.61 PRO 422

ARG 421 0.68 SER 139 -0.55 PRO 422

ARG 421 0.64 GLN 140 -0.45 PRO 422

ARG 421 0.64 LEU 141 -0.44 PRO 422

ARG 421 0.72 SER 142 -0.45 PRO 422

ARG 421 0.72 ALA 143 -0.36 PRO 422

ARG 421 0.65 ALA 144 -0.30 PRO 422

ARG 421 0.68 ILE 145 -0.27 PRO 422

ARG 421 0.75 THR 146 -0.23 PRO 422

ARG 421 0.69 ALA 147 -0.19 PRO 422

ARG 421 0.64 LEU 148 -0.16 PRO 422

ARG 421 0.69 ASN 149 -0.09 PRO 422

ARG 421 0.64 SER 150 -0.05 PRO 422

ARG 421 0.58 GLU 151 -0.04 PRO 422

ARG 421 0.61 SER 152 -0.00 LEU 33

ARG 421 0.53 ASN 153 -0.00 LEU 33

ARG 421 0.58 PHE 154 -0.00 LEU 33

ARG 421 0.66 ALA 155 -0.00 LEU 33

ARG 421 0.58 ARG 156 -0.00 LEU 33

ARG 421 0.52 ALA 157 -0.01 ALA 1

ARG 421 0.60 TYR 158 -0.00 LEU 33

ARG 421 0.59 ALA 159 -0.00 ALA 1

ARG 421 0.50 GLU 160 -0.03 ALA 1

ARG 421 0.48 GLY 161 -0.04 ALA 1

ARG 421 0.43 ILE 162 -0.05 ALA 1

ARG 421 0.37 LEU 163 -0.07 ALA 1

PRO 422 0.42 ARG 164 -0.05 ALA 1

PRO 422 0.37 THR 165 -0.07 ALA 1

ARG 421 0.33 LYS 166 -0.06 ALA 1

ARG 421 0.44 TYR 167 -0.02 ALA 1

ARG 421 0.40 TRP 168 -0.01 LEU 33

ARG 421 0.35 GLU 169 -0.02 ALA 1

ARG 421 0.45 MET 170 -0.00 LEU 33

ARG 421 0.52 VAL 171 -0.00 LEU 33

ARG 421 0.43 TYR 172 -0.00 LEU 33

ARG 421 0.44 GLU 173 -0.00 LEU 33

ARG 421 0.53 SER 174 -0.01 PRO 422

ARG 421 0.50 ALA 175 -0.05 PRO 422

ARG 421 0.43 MET 176 -0.08 PRO 422

ARG 421 0.47 ASP 177 -0.10 PRO 422

ARG 421 0.53 LEU 178 -0.17 PRO 422

ARG 421 0.47 ILE 179 -0.21 PRO 422

ARG 421 0.43 ALA 180 -0.18 PRO 422

ARG 421 0.48 LYS 181 -0.22 PRO 422

ARG 421 0.51 LEU 182 -0.29 PRO 422

ARG 421 0.46 PRO 183 -0.31 PRO 422

ARG 421 0.47 CYS 184 -0.28 PRO 422

ARG 421 0.53 VAL 185 -0.32 PRO 422

ARG 421 0.51 ALA 186 -0.39 PRO 422

ARG 421 0.46 ALA 187 -0.35 PRO 422

ARG 421 0.48 LYS 188 -0.34 PRO 422

ARG 421 0.52 ILE 189 -0.40 PRO 422

ARG 421 0.47 TYR 190 -0.42 PRO 422

ARG 421 0.45 ARG 191 -0.37 PRO 422

ARG 421 0.48 ASN 192 -0.37 PRO 422

ARG 421 0.49 LEU 193 -0.43 PRO 422

ARG 421 0.44 TYR 194 -0.42 PRO 422

ARG 421 0.42 ARG 195 -0.38 PRO 422

ARG 421 0.43 ALA 196 -0.36 PRO 422

ARG 421 0.45 GLY 197 -0.34 PRO 422

ARG 421 0.42 SER 198 -0.31 PRO 422

ARG 421 0.41 SER 199 -0.28 PRO 422

ARG 421 0.42 ILE 200 -0.29 PRO 422

ARG 421 0.38 GLY 201 -0.25 PRO 422

ARG 421 0.37 ALA 202 -0.21 PRO 422

ALA 1 0.36 ILE 203 -0.20 PRO 422

ALA 1 0.43 ASP 204 -0.18 PRO 422

ALA 1 0.51 SER 205 -0.15 PRO 422

ALA 1 0.57 LYS 206 -0.15 PRO 422

ALA 1 0.48 LEU 207 -0.19 PRO 422

ALA 1 0.45 ASP 208 -0.20 PRO 422

ALA 1 0.37 TRP 209 -0.23 PRO 422

ALA 1 0.34 SER 210 -0.28 PRO 422

ALA 1 0.37 HIS 211 -0.27 PRO 422

ALA 1 0.36 ASN 212 -0.25 PRO 422

ARG 421 0.38 PHE 213 -0.31 PRO 422

ARG 421 0.35 THR 214 -0.33 PRO 422

ARG 421 0.34 ASN 215 -0.29 PRO 422

ARG 421 0.38 MET 216 -0.30 PRO 422

ARG 421 0.40 LEU 217 -0.35 PRO 422

ARG 421 0.36 GLY 218 -0.33 PRO 422

ARG 421 0.33 TYR 219 -0.34 PRO 422

ALA 1 0.30 THR 220 -0.31 PRO 422

ALA 1 0.29 ASP 221 -0.32 PRO 422

ALA 1 0.32 ALA 222 -0.29 PRO 422

ALA 1 0.29 GLN 223 -0.32 PRO 422

ALA 1 0.28 PHE 224 -0.35 PRO 422

ALA 1 0.32 THR 225 -0.32 PRO 422

ALA 1 0.31 GLU 226 -0.31 PRO 422

ARG 421 0.27 LEU 227 -0.36 PRO 422

ARG 421 0.31 MET 228 -0.36 PRO 422

ALA 1 0.30 ARG 229 -0.31 PRO 422

ALA 1 0.26 LEU 230 -0.34 PRO 422

ARG 421 0.31 TYR 231 -0.41 PRO 422

ARG 421 0.35 LEU 232 -0.38 PRO 422

ARG 421 0.29 THR 233 -0.32 PRO 422

ARG 421 0.28 ILE 234 -0.39 PRO 422

ARG 421 0.37 HIS 235 -0.48 PRO 422

ARG 421 0.38 SER 236 -0.38 PRO 422

ARG 421 0.37 ASP 237 -0.35 PRO 422

ARG 421 0.34 HIS 238 -0.41 PRO 422

ARG 421 0.34 GLU 239 -0.35 LYS 423

ARG 421 0.49 GLY 240 -0.27 LYS 423

ARG 421 0.55 GLY 241 -0.43 LYS 423

ARG 421 0.60 ASN 242 -0.71 PRO 422

ARG 421 0.74 VAL 243 -0.92 PRO 422

ARG 421 0.72 SER 244 -0.67 PRO 422

ARG 421 0.68 ALA 245 -0.41 PRO 422

ARG 421 0.81 HIS 246 -0.34 PRO 422

ARG 421 0.95 THR 247 -0.39 PRO 422

ARG 421 0.85 SER 248 -0.21 PRO 422

ARG 421 0.88 HIS 249 -0.01 ILE 36

ARG 421 1.16 LEU 250 -0.01 ILE 36

ARG 421 1.13 VAL 251 -0.01 GLN 35

ARG 421 0.94 GLY 252 -0.01 LEU 33

ARG 421 1.00 SER 253 -0.01 LEU 33

ARG 421 1.10 ALA 254 -0.01 LEU 33

ARG 421 0.87 LEU 255 -0.01 LEU 33

ARG 421 0.90 SER 256 -0.00 LEU 33

ARG 421 0.76 ASP 257 -0.00 LEU 33

ARG 421 0.70 PRO 258 -0.03 PRO 422

ARG 421 0.72 TYR 259 -0.13 PRO 422

ARG 421 0.84 LEU 260 -0.12 PRO 422

ARG 421 0.87 SER 261 -0.15 PRO 422

ARG 421 0.76 PHE 262 -0.29 PRO 422

ARG 421 0.79 ALA 263 -0.37 PRO 422

ARG 421 0.91 ALA 264 -0.43 PRO 422

ARG 421 0.82 ALA 265 -0.51 PRO 422

ARG 421 0.75 MET 266 -0.62 PRO 422

ARG 421 0.82 ASN 267 -0.71 PRO 422

ARG 421 0.82 GLY 268 -0.90 PRO 422

ARG 421 0.69 LEU 269 -0.87 PRO 422

ARG 421 0.69 ALA 270 -0.86 PRO 422

ARG 421 0.70 GLY 271 -1.10 PRO 422

ARG 421 0.61 PRO 272 -1.09 PRO 422

ARG 421 0.59 LEU 273 -1.25 PRO 422

ARG 421 0.60 HIS 274 -1.12 PRO 422

ARG 421 0.58 GLY 275 -0.92 PRO 422

ARG 421 0.51 LEU 276 -0.86 PRO 422

ARG 421 0.43 ALA 277 -0.81 PRO 422

ARG 421 0.40 ASN 278 -0.69 PRO 422

ARG 421 0.42 GLN 279 -0.70 PRO 422

ARG 421 0.41 GLU 280 -0.74 PRO 422

ARG 421 0.35 VAL 281 -0.66 PRO 422

ARG 421 0.35 LEU 282 -0.61 PRO 422

ARG 421 0.36 GLY 283 -0.63 PRO 422

ARG 421 0.33 TRP 284 -0.61 PRO 422

ARG 421 0.29 LEU 285 -0.56 PRO 422

ARG 421 0.31 ALA 286 -0.54 PRO 422

ARG 421 0.31 GLN 287 -0.54 PRO 422

ARG 421 0.27 LEU 288 -0.51 PRO 422

ARG 421 0.27 GLN 289 -0.49 PRO 422

ARG 421 0.27 LYS 290 -0.47 PRO 422

ARG 421 0.26 ALA 291 -0.47 PRO 422

ARG 421 0.19 ALA 295 -0.40 PRO 422

ARG 421 0.17 GLY 296 -0.40 PRO 422

ARG 421 0.15 ALA 297 -0.39 PRO 422

ALA 1 0.14 ASP 298 -0.38 PRO 422

ARG 421 0.13 ALA 299 -0.38 PRO 422

ARG 421 0.16 SER 300 -0.41 PRO 422

ARG 421 0.18 LEU 301 -0.44 PRO 422

ARG 421 0.15 ARG 302 -0.42 PRO 422

ARG 421 0.16 ASP 303 -0.42 PRO 422

ARG 421 0.20 TYR 304 -0.46 PRO 422

ARG 421 0.19 ILE 305 -0.49 PRO 422

ARG 421 0.16 TRP 306 -0.45 PRO 422

ARG 421 0.19 ASN 307 -0.47 PRO 422

ARG 421 0.22 THR 308 -0.52 PRO 422

ARG 421 0.20 LEU 309 -0.51 PRO 422

ARG 421 0.18 ASN 310 -0.47 PRO 422

ARG 421 0.22 SER 311 -0.50 PRO 422

ARG 421 0.24 GLY 312 -0.54 PRO 422

ARG 421 0.27 ARG 313 -0.59 PRO 422

ARG 421 0.26 VAL 314 -0.62 PRO 422

ARG 421 0.26 VAL 315 -0.61 PRO 422

ARG 421 0.31 PRO 316 -0.68 PRO 422

ARG 421 0.28 GLY 317 -0.64 PRO 422

ARG 421 0.22 TYR 318 -0.58 PRO 422

ARG 421 0.19 GLY 319 -0.56 PRO 422

ARG 421 0.18 HIS 320 -0.59 LYS 423

ARG 421 0.15 ALA 321 -0.70 LYS 423

THR 427 0.13 VAL 322 -0.65 LYS 423

THR 427 0.11 LEU 323 -0.55 LYS 423

ALA 1 0.10 ARG 324 -0.51 LYS 423

ALA 1 0.12 LYS 325 -0.45 LYS 423

ALA 1 0.14 THR 326 -0.42 LYS 423

ARG 421 0.15 ASP 327 -0.42 PRO 422

ALA 1 0.16 PRO 328 -0.37 PRO 422

ARG 421 0.20 ARG 329 -0.42 PRO 422

ARG 421 0.20 TYR 330 -0.45 PRO 422

ALA 1 0.17 THR 331 -0.39 PRO 422

ALA 1 0.20 CYS 332 -0.37 PRO 422

ARG 421 0.21 GLN 333 -0.41 PRO 422

ALA 1 0.19 ARG 334 -0.39 PRO 422

ALA 1 0.20 GLU 335 -0.34 PRO 422

ALA 1 0.22 PHE 336 -0.36 PRO 422

ALA 1 0.21 ALA 337 -0.38 PRO 422

ALA 1 0.20 LEU 338 -0.34 PRO 422

ALA 1 0.22 LYS 339 -0.32 PRO 422

ALA 1 0.23 HIS 340 -0.34 PRO 422

ALA 1 0.22 LEU 341 -0.37 PRO 422

ALA 1 0.20 PRO 342 -0.36 PRO 422

ALA 1 0.19 GLY 343 -0.36 PRO 422

ARG 421 0.22 ASP 344 -0.40 PRO 422

ARG 421 0.22 PRO 345 -0.41 PRO 422

ARG 421 0.25 MET 346 -0.46 PRO 422

ARG 421 0.22 PHE 347 -0.44 PRO 422

ARG 421 0.19 LYS 348 -0.41 PRO 422

ARG 421 0.21 LEU 349 -0.45 PRO 422

ARG 421 0.22 VAL 350 -0.48 PRO 422

ARG 421 0.17 ALA 351 -0.43 PRO 422

ARG 421 0.16 GLN 352 -0.43 PRO 422

ARG 421 0.18 LEU 353 -0.47 PRO 422

ALA 1 0.15 TYR 354 -0.43 PRO 422

ALA 1 0.14 LYS 355 -0.39 PRO 422

ALA 1 0.13 ILE 356 -0.42 PRO 422

ARG 421 0.15 VAL 357 -0.46 PRO 422

ALA 1 0.12 PRO 358 -0.43 LYS 423

ALA 1 0.12 ASN 359 -0.42 LYS 423

ALA 1 0.12 VAL 360 -0.42 LYS 423

ARG 421 0.12 LEU 361 -0.47 LYS 423

ALA 1 0.11 LEU 362 -0.48 LYS 423

ALA 1 0.10 GLU 363 -0.45 LYS 423

ALA 1 0.10 GLN 364 -0.46 LYS 423

ALA 1 0.10 GLY 365 -0.51 LYS 423

ARG 421 0.12 ALA 366 -0.55 LYS 423

ALA 1 0.10 ALA 367 -0.55 LYS 423

ALA 1 0.10 ALA 368 -0.57 LYS 423

ALA 1 0.11 ASN 369 -0.54 LYS 423

ALA 1 0.12 PRO 370 -0.50 LYS 423

ALA 1 0.13 TRP 371 -0.46 LYS 423

ARG 421 0.19 PRO 372 -0.52 PRO 422

ARG 421 0.23 ASN 373 -0.54 PRO 422

ARG 421 0.27 VAL 374 -0.54 PRO 422

ARG 421 0.33 ASP 375 -0.64 PRO 422

ARG 421 0.28 ALA 376 -0.58 PRO 422

ARG 421 0.26 HIS 377 -0.51 PRO 422

ARG 421 0.31 SER 378 -0.52 PRO 422

ARG 421 0.34 GLY 379 -0.56 PRO 422

ARG 421 0.30 VAL 380 -0.50 PRO 422

ARG 421 0.29 LEU 381 -0.46 PRO 422

ARG 421 0.34 LEU 382 -0.48 PRO 422

ARG 421 0.33 GLN 383 -0.48 PRO 422

ARG 421 0.29 TYR 384 -0.43 PRO 422

ARG 421 0.30 TYR 385 -0.41 PRO 422

ARG 421 0.33 GLY 386 -0.42 PRO 422

ARG 421 0.37 MET 387 -0.46 PRO 422

ARG 421 0.38 THR 388 -0.50 PRO 422

ARG 421 0.43 GLU 389 -0.52 PRO 422

ARG 421 0.44 MET 390 -0.59 PRO 422

ARG 421 0.50 ASN 391 -0.63 PRO 422

ARG 421 0.49 TYR 392 -0.57 PRO 422

ARG 421 0.46 TYR 393 -0.60 PRO 422

ARG 421 0.53 THR 394 -0.67 PRO 422

ARG 421 0.53 VAL 395 -0.55 PRO 422

ARG 421 0.47 LEU 396 -0.51 PRO 422

ARG 421 0.48 PHE 397 -0.58 PRO 422

ARG 421 0.55 GLY 398 -0.54 PRO 422

ARG 421 0.50 VAL 399 -0.42 PRO 422

ARG 421 0.44 SER 400 -0.41 PRO 422

ARG 421 0.49 ARG 401 -0.44 PRO 422

ARG 421 0.52 ALA 402 -0.33 PRO 422

ARG 421 0.42 LEU 403 -0.25 PRO 422

ARG 421 0.42 GLY 404 -0.24 PRO 422

ARG 421 0.56 VAL 405 -0.23 PRO 422

ARG 421 0.53 LEU 406 -0.11 PRO 422

ARG 421 0.40 ALA 407 -0.06 PRO 422

ARG 421 0.42 GLN 408 -0.01 ILE 36

ARG 421 0.56 LEU 409 -0.01 ILE 36

ARG 421 0.45 ILE 410 -0.01 LEU 33

ARG 421 0.34 TRP 411 -0.01 LEU 33

ARG 421 0.47 SER 412 -0.01 LEU 33

ARG 421 0.49 ARG 413 -0.01 LEU 33

ARG 421 0.30 ALA 414 -0.01 ALA 1

PRO 422 0.39 LEU 415 -0.02 ALA 1

PRO 422 0.48 GLY 416 -0.02 ALA 1

PRO 422 0.58 PHE 417 -0.02 LEU 33

PRO 422 0.76 PRO 418 -0.01 LEU 33

ARG 421 1.08 LEU 419 -0.01 LEU 33

ARG 421 1.20 GLU 420 -0.01 LEU 33

PRO 422 1.27 ARG 421 -1.16 THR 31

ARG 421 1.27 PRO 422 -1.25 LEU 273

ARG 421 1.04 LYS 423 -1.60 MET 40

ARG 421 1.18 SER 424 -0.18 GLY 429

ARG 421 0.99 MET 425 -0.17 GLY 312

ARG 421 0.89 SER 426 -0.07 GLY 312

ARG 421 0.77 THR 427 -0.05 SER 311

ARG 421 0.64 ASP 428 -0.06 SER 424

ARG 421 0.59 GLY 429 -0.18 SER 424

ARG 421 0.59 LEU 430 -0.18 GLY 312

ARG 421 0.51 ILE 431 -0.11 GLY 312

ARG 421 0.36 ALA 432 -0.14 GLY 312

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** open cutoff8 melek ***

CA distance fluctuations for 260522120615405517

--- normal mode 8 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* open cutoff8 melek *