Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
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* close cutoff 10 melek *

CA distance fluctuations for 260522120726406031

--- normal mode 10 ---

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
LYS 423 0.94 ALA 1 -0.10 SER 424

LYS 423 0.90 SER 2 -0.10 SER 424

LYS 423 0.85 SER 3 -0.09 SER 424

LYS 423 0.83 THR 4 -0.10 SER 424

LYS 423 0.82 ASN 5 -0.11 SER 424

LYS 423 0.90 LEU 6 -0.11 SER 424

LYS 423 0.86 LYS 7 -0.12 SER 424

LYS 423 0.83 ASP 8 -0.12 SER 424

LYS 423 0.90 VAL 9 -0.12 SER 424

LYS 423 0.94 LEU 10 -0.13 SER 424

LYS 423 0.88 ALA 11 -0.14 SER 424

LYS 423 0.89 SER 12 -0.13 SER 424

LYS 423 0.97 LEU 13 -0.13 SER 424

LYS 423 0.98 ILE 14 -0.15 SER 424

LYS 423 0.95 PRO 15 -0.15 SER 424

LYS 423 0.99 LYS 16 -0.15 SER 424

LYS 423 1.08 GLU 17 -0.16 SER 424

LYS 423 1.05 GLN 18 -0.18 SER 424

LYS 423 1.02 ALA 19 -0.17 SER 424

LYS 423 1.10 ARG 20 -0.19 SER 424

LYS 423 1.17 ILE 21 -0.21 SER 424

LYS 423 1.09 LYS 22 -0.20 SER 424

LYS 423 1.09 THR 23 -0.21 SER 424

LYS 423 1.18 PHE 24 -0.26 SER 424

LYS 423 1.19 ARG 25 -0.29 SER 424

LYS 423 1.10 GLN 26 -0.26 SER 424

LYS 423 1.14 GLN 27 -0.29 SER 424

LYS 423 1.24 HIS 28 -0.35 SER 424

LYS 423 1.26 GLY 29 -0.39 SER 424

LYS 423 1.26 ASN 30 -0.48 SER 424

LYS 423 1.33 THR 31 -0.43 SER 424

LYS 423 1.44 ALA 32 -0.51 SER 424

LYS 423 1.56 VAL 33 -0.32 SER 424

LYS 423 1.66 GLY 34 -0.32 LEU 430

LYS 423 1.70 GLN 35 -0.29 LEU 430

LYS 423 1.72 ILE 36 -0.29 LEU 430

LYS 423 1.68 THR 37 -0.11 GLY 271

LYS 423 1.60 VAL 38 -0.12 GLY 271

LYS 423 1.66 ASP 39 -0.16 GLY 271

LYS 423 1.79 MET 40 -0.16 GLY 271

LYS 423 1.66 SER 41 -0.14 GLY 271

LYS 423 1.57 TYR 42 -0.16 GLY 271

LYS 423 1.66 GLY 43 -0.21 GLY 271

PRO 422 1.70 GLY 44 -0.24 GLY 271

LYS 423 1.78 MET 45 -0.16 GLY 268

LYS 423 1.82 ARG 46 -0.17 LEU 273

LYS 423 1.88 GLY 47 -0.14 VAL 243

LYS 423 1.89 MET 48 -0.25 SER 424

LYS 423 1.74 LYS 49 -0.31 SER 424

LYS 423 1.65 GLY 50 -0.37 SER 424

LYS 423 1.54 LEU 51 -0.30 SER 424

LYS 423 1.44 ILE 52 -0.23 SER 424

LYS 423 1.39 TYR 53 -0.19 SER 424

LYS 423 1.31 GLU 54 -0.16 SER 424

LYS 423 1.27 THR 55 -0.14 SER 424

LYS 423 1.35 SER 56 -0.12 SER 424

LYS 423 1.44 VAL 57 -0.12 PHE 24

LYS 423 1.48 LEU 58 -0.11 PHE 24

LYS 423 1.50 ASP 59 -0.11 PHE 24

LYS 423 1.54 PRO 60 -0.11 PHE 24

LYS 423 1.46 ASP 61 -0.10 PHE 24

LYS 423 1.39 GLU 62 -0.09 ARG 20

LYS 423 1.40 GLY 63 -0.09 PHE 24

LYS 423 1.38 ILE 64 -0.09 ARG 20

LYS 423 1.33 ARG 65 -0.10 ARG 20

LYS 423 1.27 PHE 66 -0.10 SER 424

LYS 423 1.24 ARG 67 -0.11 SER 424

LYS 423 1.27 GLY 68 -0.11 ARG 20

LYS 423 1.23 PHE 69 -0.09 ARG 20

LYS 423 1.25 SER 70 -0.08 ARG 20

LYS 423 1.21 ILE 71 -0.07 ARG 20

LYS 423 1.16 PRO 72 -0.06 ARG 20

LYS 423 1.15 GLU 73 -0.07 ARG 20

LYS 423 1.13 CYS 74 -0.07 SER 424

LYS 423 1.10 GLN 75 -0.06 SER 424

LYS 423 1.06 LYS 76 -0.06 SER 424

LYS 423 1.05 LEU 77 -0.07 SER 424

LYS 423 1.03 LEU 78 -0.07 SER 424

LYS 423 0.97 PRO 79 -0.07 SER 424

LYS 423 0.95 LYS 80 -0.06 SER 424

LYS 423 0.90 ALA 81 -0.06 SER 424

LYS 423 0.85 GLY 82 -0.06 SER 424

LYS 423 0.92 GLY 84 -0.05 LYS 339

LYS 423 0.97 GLU 85 -0.06 LYS 339

LYS 423 1.01 GLU 86 -0.05 SER 424

LYS 423 1.03 PRO 87 -0.06 SER 424

LYS 423 0.99 LEU 88 -0.07 SER 424

LYS 423 1.03 PRO 89 -0.08 SER 424

LYS 423 0.98 GLU 90 -0.09 SER 424

LYS 423 1.01 GLY 91 -0.09 SER 424

LYS 423 1.09 LEU 92 -0.09 SER 424

LYS 423 1.07 PHE 93 -0.11 SER 424

LYS 423 1.03 TRP 94 -0.11 SER 424

LYS 423 1.09 LEU 95 -0.10 SER 424

LYS 423 1.15 LEU 96 -0.12 SER 424

LYS 423 1.09 VAL 97 -0.13 SER 424

LYS 423 1.06 THR 98 -0.12 SER 424

LYS 423 1.13 GLY 99 -0.12 SER 424

LYS 423 1.07 GLN 100 -0.10 SER 424

LYS 423 1.05 ILE 101 -0.09 SER 424

LYS 423 0.98 PRO 102 -0.09 SER 424

LYS 423 0.93 THR 103 -0.08 SER 424

LYS 423 0.89 PRO 104 -0.08 SER 424

LYS 423 0.85 GLU 105 -0.08 SER 424

LYS 423 0.89 GLN 106 -0.09 SER 424

LYS 423 0.91 VAL 107 -0.09 SER 424

LYS 423 0.85 SER 108 -0.08 SER 424

LYS 423 0.83 TRP 109 -0.09 SER 424

LYS 423 0.88 VAL 110 -0.09 SER 424

PRO 422 0.86 SER 111 -0.08 SER 424

PRO 422 0.80 LYS 112 -0.08 SER 424

PRO 422 0.82 GLU 113 -0.09 SER 424

PRO 422 0.88 TRP 114 -0.09 SER 424

PRO 422 0.83 ALA 115 -0.08 SER 424

PRO 422 0.78 LYS 116 -0.09 SER 424

PRO 422 0.83 ARG 117 -0.09 SER 424

PRO 422 0.86 ALA 118 -0.08 SER 424

PRO 422 0.83 ALA 119 -0.08 SER 424

PRO 422 0.86 LEU 120 -0.08 ASN 30

PRO 422 0.81 PRO 121 -0.08 ASN 30

PRO 422 0.78 SER 122 -0.09 ARG 421

PRO 422 0.81 HIS 123 -0.11 ARG 421

PRO 422 0.88 VAL 124 -0.09 ASN 30

PRO 422 0.86 VAL 125 -0.09 TYR 42

PRO 422 0.82 THR 126 -0.09 TYR 42

PRO 422 0.88 MET 127 -0.11 TYR 42

PRO 422 0.92 LEU 128 -0.10 TYR 42

PRO 422 0.87 ASP 129 -0.10 TYR 42

PRO 422 0.86 ASN 130 -0.11 TYR 42

PRO 422 0.93 PHE 131 -0.12 TYR 42

PRO 422 0.93 PRO 132 -0.12 TYR 42

PRO 422 0.96 THR 133 -0.12 GLY 43

PRO 422 1.00 ASN 134 -0.13 GLY 43

PRO 422 1.04 LEU 135 -0.14 GLY 43

PRO 422 1.11 HIS 136 -0.14 GLY 43

PRO 422 1.11 PRO 137 -0.13 GLY 44

PRO 422 1.19 MET 138 -0.14 GLY 44

PRO 422 1.15 SER 139 -0.15 GLY 44

PRO 422 1.08 GLN 140 -0.13 GLY 44

PRO 422 1.12 LEU 141 -0.12 GLY 44

PRO 422 1.17 SER 142 -0.13 GLY 44

PRO 422 1.08 ALA 143 -0.13 TYR 42

PRO 422 1.03 ALA 144 -0.11 GLY 44

PRO 422 1.07 ILE 145 -0.11 ASN 30

PRO 422 1.06 THR 146 -0.12 ASN 30

PRO 422 0.96 ALA 147 -0.11 ASN 30

PRO 422 0.94 LEU 148 -0.10 ASN 30

PRO 422 0.94 ASN 149 -0.12 ARG 421

PRO 422 0.84 SER 150 -0.17 ARG 421

PRO 422 0.83 GLU 151 -0.12 ARG 421

PRO 422 0.87 SER 152 -0.12 ARG 421

PRO 422 0.80 ASN 153 -0.12 LEU 419

PRO 422 0.84 PHE 154 -0.14 LEU 419

PRO 422 0.83 ALA 155 -0.20 ARG 421

PRO 422 0.72 ARG 156 -0.21 ARG 421

PRO 422 0.69 ALA 157 -0.19 ARG 421

PRO 422 0.72 TYR 158 -0.25 ARG 421

PRO 422 0.65 ALA 159 -0.32 ARG 421

PRO 422 0.56 GLU 160 -0.27 ARG 421

LYS 423 0.57 GLY 161 -0.28 ARG 421

LYS 423 0.65 ILE 162 -0.20 ARG 421

LYS 423 0.70 ASN 163 -0.19 LEU 419

LYS 423 0.81 ARG 164 -0.23 LEU 419

LYS 423 0.82 THR 165 -0.16 LEU 419

LYS 423 0.79 LYS 166 -0.16 LEU 419

LYS 423 0.85 TYR 167 -0.19 LEU 419

LYS 423 0.92 TRP 168 -0.16 SER 424

LYS 423 0.84 GLU 169 -0.14 SER 424

PRO 422 0.82 PHE 170 -0.14 SER 424

PRO 422 0.94 VAL 171 -0.15 SER 424

PRO 422 0.91 TYR 172 -0.14 SER 424

PRO 422 0.86 GLU 173 -0.12 SER 424

PRO 422 0.93 ASP 174 -0.12 SER 424

PRO 422 1.01 ALA 175 -0.13 SER 424

PRO 422 0.94 MET 176 -0.11 SER 424

PRO 422 0.92 ASP 177 -0.11 SER 424

PRO 422 1.01 LEU 178 -0.11 SER 424

PRO 422 1.03 ILE 179 -0.10 SER 424

PRO 422 0.95 ALA 180 -0.09 SER 424

PRO 422 0.95 LYS 181 -0.08 SER 424

PRO 422 1.03 LEU 182 -0.08 SER 424

PRO 422 1.00 PRO 183 -0.07 GLY 44

PRO 422 0.94 CYS 184 -0.07 GLY 44

PRO 422 0.99 VAL 185 -0.09 GLY 44

PRO 422 1.04 ALA 186 -0.09 GLY 44

PRO 422 0.97 ALA 187 -0.08 GLY 44

PRO 422 0.94 LYS 188 -0.09 GLY 44

PRO 422 0.99 ILE 189 -0.10 GLY 44

PRO 422 0.99 TYR 190 -0.09 GLY 44

PRO 422 0.92 ARG 191 -0.08 GLY 44

PRO 422 0.91 ASN 192 -0.09 GLY 43

PRO 422 0.95 LEU 193 -0.10 GLY 43

PRO 422 0.94 TYR 194 -0.09 GLY 44

PRO 422 0.89 ARG 195 -0.08 GLY 44

PRO 422 0.85 ALA 196 -0.08 GLY 43

PRO 422 0.85 GLY 197 -0.08 GLY 43

PRO 422 0.83 SER 198 -0.07 GLY 44

PRO 422 0.82 SER 199 -0.07 GLY 44

PRO 422 0.85 ILE 200 -0.07 GLY 44

PRO 422 0.81 GLY 201 -0.06 GLY 44

PRO 422 0.80 ALA 202 -0.06 SER 424

PRO 422 0.82 ILE 203 -0.06 SER 424

PRO 422 0.79 ASP 204 -0.06 SER 424

PRO 422 0.77 SER 205 -0.07 SER 424

PRO 422 0.77 LYS 206 -0.07 SER 424

PRO 422 0.82 LEU 207 -0.06 SER 424

PRO 422 0.88 ASP 208 -0.07 SER 424

PRO 422 0.93 TRP 209 -0.07 SER 424

PRO 422 0.96 SER 210 -0.06 SER 424

PRO 422 0.90 HIS 211 -0.06 SER 424

PRO 422 0.89 ASN 212 -0.06 SER 424

PRO 422 0.95 PHE 213 -0.06 SER 424

PRO 422 0.94 THR 214 -0.05 GLY 44

PRO 422 0.88 ASN 215 -0.05 GLY 44

PRO 422 0.89 MET 216 -0.06 GLY 44

PRO 422 0.94 LEU 217 -0.06 GLY 44

PRO 422 0.89 GLY 218 -0.06 GLY 44

PRO 422 0.90 TYR 219 -0.05 GLY 44

PRO 422 0.86 THR 220 -0.04 GLY 44

PRO 422 0.88 ASP 221 -0.04 GLY 44

PRO 422 0.88 PRO 222 -0.04 SER 424

PRO 422 0.91 GLN 223 -0.03 LEU 341

PRO 422 0.95 PHE 224 -0.04 GLY 44

PRO 422 0.94 THR 225 -0.05 SER 424

LYS 423 0.95 GLU 226 -0.05 SER 424

PRO 422 1.00 LEU 227 -0.04 SER 424

PRO 422 1.02 MET 228 -0.05 SER 424

PRO 422 1.01 ARG 229 -0.06 SER 424

LYS 423 1.06 LEU 230 -0.05 SER 424

PRO 422 1.11 TYR 231 -0.05 GLY 29

PRO 422 1.11 LEU 232 -0.07 SER 424

LYS 423 1.11 THR 233 -0.07 SER 424

LYS 423 1.17 ILE 234 -0.06 SER 424

PRO 422 1.24 HIS 235 -0.07 GLY 29

PRO 422 1.22 SER 236 -0.09 SER 424

PRO 422 1.30 ASP 237 -0.10 SER 424

LYS 423 1.38 HIS 238 -0.10 PHE 24

LYS 423 1.43 GLU 239 -0.12 PHE 24

PRO 422 1.49 GLY 240 -0.15 SER 424

PRO 422 1.64 GLY 241 -0.13 GLY 29

PRO 422 1.63 ASN 242 -0.13 GLY 29

PRO 422 1.67 VAL 243 -0.18 GLY 44

PRO 422 1.53 SER 244 -0.14 GLY 44

PRO 422 1.49 ALA 245 -0.15 SER 424

PRO 422 1.61 HIS 246 -0.18 SER 424

PRO 422 1.56 THR 247 -0.17 SER 424

PRO 422 1.40 SER 248 -0.18 SER 424

PRO 422 1.41 HIS 249 -0.25 SER 424

PRO 422 1.44 LEU 250 -0.30 SER 424

PRO 422 1.32 VAL 251 -0.22 SER 424

PRO 422 1.22 GLY 252 -0.21 SER 424

PRO 422 1.20 SER 253 -0.24 SER 424

PRO 422 1.13 ALA 254 -0.32 LEU 255

PRO 422 1.02 LEU 255 -0.32 ALA 254

PRO 422 1.07 SER 256 -0.16 SER 424

PRO 422 1.03 ASP 257 -0.14 SER 424

PRO 422 1.10 PRO 258 -0.14 SER 424

PRO 422 1.08 TYR 259 -0.12 SER 424

PRO 422 1.14 LEU 260 -0.14 ASN 30

PRO 422 1.25 SER 261 -0.15 SER 424

PRO 422 1.25 PHE 262 -0.13 SER 424

PRO 422 1.23 ALA 263 -0.13 ASN 30

PRO 422 1.34 ALA 264 -0.15 ASN 30

PRO 422 1.41 ALA 265 -0.15 GLY 44

PRO 422 1.34 MET 266 -0.15 GLY 44

PRO 422 1.37 ASN 267 -0.19 GLY 44

PRO 422 1.51 GLY 268 -0.22 GLY 44

PRO 422 1.43 LEU 269 -0.18 GLY 44

PRO 422 1.36 ALA 270 -0.19 GLY 44

PRO 422 1.43 GLY 271 -0.24 GLY 44

PRO 422 1.38 PRO 272 -0.20 GLY 44

PRO 422 1.47 LEU 273 -0.19 GLY 44

PRO 422 1.48 HIS 274 -0.17 GLY 44

PRO 422 1.39 GLY 275 -0.14 GLY 44

PRO 422 1.33 LEU 276 -0.15 GLY 44

PRO 422 1.32 ALA 277 -0.12 GLY 44

PRO 422 1.25 ASN 278 -0.09 GLY 44

PRO 422 1.20 GLN 279 -0.11 GLY 44

PRO 422 1.22 GLU 280 -0.11 ASP 39

PRO 422 1.20 VAL 281 -0.08 ASP 39

PRO 422 1.13 LEU 282 -0.08 ASP 39

PRO 422 1.12 LEU 283 -0.09 ASP 39

PRO 422 1.13 TRP 284 -0.08 ASP 39

PRO 422 1.09 LEU 285 -0.07 ASP 39

PRO 422 1.04 SER 286 -0.07 ASP 39

PRO 422 1.04 GLN 287 -0.08 ASP 39

PRO 422 1.03 LEU 288 -0.07 ASP 39

PRO 422 0.99 GLN 289 -0.06 ASP 39

PRO 422 0.97 LYS 290 -0.07 ASP 39

PRO 422 0.96 ASP 291 -0.06 ASP 39

LYS 423 0.95 ASP 295 -0.04 PHE 24

LYS 423 0.98 ALA 296 -0.04 PHE 24

LYS 423 1.00 SER 297 -0.04 PHE 24

LYS 423 1.05 ASP 298 -0.05 PHE 24

LYS 423 1.04 GLU 299 -0.05 PHE 24

LYS 423 1.02 LYS 300 -0.04 PHE 24

LYS 423 1.07 LEU 301 -0.05 PHE 24

LYS 423 1.11 ARG 302 -0.05 PHE 24

LYS 423 1.07 ASP 303 -0.05 PHE 24

LYS 423 1.07 TYR 304 -0.05 PHE 24

LYS 423 1.14 ILE 305 -0.05 PHE 24

LYS 423 1.13 TRP 306 -0.05 PHE 24

LYS 423 1.09 ASN 307 -0.05 ASP 39

LYS 423 1.13 THR 308 -0.07 ASP 39

LYS 423 1.19 LEU 309 -0.06 ASP 39

LYS 423 1.13 ASN 310 -0.07 ASP 39

PRO 422 1.11 SER 311 -0.09 ASP 39

PRO 422 1.17 GLY 312 -0.11 ASP 39

PRO 422 1.22 ARG 313 -0.11 ASP 39

PRO 422 1.26 VAL 314 -0.09 ASP 39

LYS 423 1.23 VAL 315 -0.06 PHE 24

PRO 422 1.26 PRO 316 -0.08 ASP 39

PRO 422 1.28 GLY 317 -0.07 PHE 24

LYS 423 1.32 TYR 318 -0.07 PHE 24

LYS 423 1.41 GLY 319 -0.07 PHE 24

LYS 423 1.48 HIS 320 -0.08 PHE 24

LYS 423 1.59 ALA 321 -0.09 PHE 24

LYS 423 1.61 VAL 322 -0.11 PHE 24

LYS 423 1.51 LEU 323 -0.09 PHE 24

LYS 423 1.50 ARG 324 -0.09 PHE 24

LYS 423 1.41 LYS 325 -0.08 PHE 24

LYS 423 1.34 THR 326 -0.07 PHE 24

LYS 423 1.34 ASP 327 -0.07 PHE 24

LYS 423 1.29 PRO 328 -0.07 ARG 20

LYS 423 1.25 ARG 329 -0.06 ARG 20

LYS 423 1.23 TYR 330 -0.06 PHE 24

LYS 423 1.20 THR 331 -0.06 ARG 20

LYS 423 1.17 CYS 332 -0.06 ARG 20

LYS 423 1.13 GLN 333 -0.05 ARG 20

LYS 423 1.12 ARG 334 -0.05 ARG 20

LYS 423 1.09 GLU 335 -0.05 ARG 20

LYS 423 1.05 PHE 336 -0.05 GLU 85

LYS 423 1.04 ALA 337 -0.05 ARG 20

LYS 423 1.03 LEU 338 -0.05 GLU 85

LYS 423 1.00 LYS 339 -0.06 GLU 85

LYS 423 0.97 HIS 340 -0.04 GLU 85

LYS 423 0.97 LEU 341 -0.04 ARG 20

LYS 423 0.98 PRO 342 -0.04 ARG 20

LYS 423 0.95 SER 343 -0.04 ARG 20

LYS 423 0.96 ASP 344 -0.04 PHE 24

LYS 423 0.96 PRO 345 -0.04 PHE 24

PRO 422 1.01 MET 346 -0.04 PHE 24

LYS 423 1.03 PHE 347 -0.04 PHE 24

LYS 423 1.03 LYS 348 -0.04 PHE 24

LYS 423 1.05 LEU 349 -0.05 PHE 24

LYS 423 1.10 VAL 350 -0.05 PHE 24

LYS 423 1.11 ALA 351 -0.05 PHE 24

LYS 423 1.10 GLN 352 -0.05 PHE 24

LYS 423 1.14 LEU 353 -0.05 PHE 24

LYS 423 1.18 TYR 354 -0.06 PHE 24

LYS 423 1.16 LYS 355 -0.06 PHE 24

LYS 423 1.17 ILE 356 -0.05 PHE 24

LYS 423 1.22 VAL 357 -0.06 PHE 24

LYS 423 1.27 PRO 358 -0.06 PHE 24

LYS 423 1.24 ASN 359 -0.06 PHE 24

LYS 423 1.23 VAL 360 -0.06 PHE 24

LYS 423 1.30 LEU 361 -0.06 PHE 24

LYS 423 1.32 LEU 362 -0.06 PHE 24

LYS 423 1.26 GLU 363 -0.06 PHE 24

LYS 423 1.28 GLN 364 -0.06 PHE 24

LYS 423 1.35 GLY 365 -0.06 PHE 24

LYS 423 1.40 LYS 366 -0.06 GLN 27

LYS 423 1.44 ALA 367 -0.07 PHE 24

LYS 423 1.52 LYS 368 -0.08 PHE 24

LYS 423 1.46 ASN 369 -0.08 PHE 24

LYS 423 1.37 PRO 370 -0.07 PHE 24

LYS 423 1.34 TRP 371 -0.07 PHE 24

LYS 423 1.30 PRO 372 -0.07 PHE 24

LYS 423 1.32 ASN 373 -0.07 PHE 24

LYS 423 1.26 VAL 374 -0.07 PHE 24

PRO 422 1.27 ASP 375 -0.07 PHE 24

PRO 422 1.21 ALA 376 -0.06 PHE 24

LYS 423 1.15 HIS 377 -0.06 PHE 24

PRO 422 1.15 SER 378 -0.05 PHE 24

PRO 422 1.13 GLY 379 -0.06 GLY 44

PRO 422 1.07 VAL 380 -0.05 PHE 24

PRO 422 1.05 LEU 381 -0.04 PHE 24

PRO 422 1.05 LEU 382 -0.05 GLY 44

PRO 422 1.02 GLN 383 -0.06 GLY 44

PRO 422 0.98 TYR 384 -0.04 GLY 44

PRO 422 0.96 TYR 385 -0.05 GLY 44

PRO 422 0.95 GLY 386 -0.06 GLY 44

PRO 422 1.00 MET 387 -0.07 GLY 44

PRO 422 1.01 THR 388 -0.07 GLY 44

PRO 422 1.04 GLU 389 -0.09 GLY 44

PRO 422 1.10 MET 390 -0.09 GLY 44

PRO 422 1.13 ASN 391 -0.12 GLY 44

PRO 422 1.12 TYR 392 -0.11 GLY 44

PRO 422 1.16 TYR 393 -0.10 GLY 44

PRO 422 1.24 THR 394 -0.11 GLY 44

PRO 422 1.18 VAL 395 -0.11 GLY 44

PRO 422 1.15 LEU 396 -0.09 GLY 44

PRO 422 1.24 PHE 397 -0.09 GLY 44

PRO 422 1.25 GLY 398 -0.10 GLY 44

PRO 422 1.16 VAL 399 -0.08 GLY 44

PRO 422 1.18 SER 400 -0.08 SER 424

PRO 422 1.27 ARG 401 -0.09 SER 424

PRO 422 1.21 ALA 402 -0.11 SER 424

PRO 422 1.16 LEU 403 -0.11 SER 424

PRO 422 1.23 GLY 404 -0.12 SER 424

PRO 422 1.29 VAL 405 -0.14 SER 424

PRO 422 1.16 LEU 406 -0.14 SER 424

PRO 422 1.12 ALA 407 -0.14 SER 424

LYS 423 1.19 GLN 408 -0.17 SER 424

PRO 422 1.16 LEU 409 -0.18 SER 424

LYS 423 1.05 ILE 410 -0.17 SER 424

LYS 423 1.12 TRP 411 -0.18 SER 424

LYS 423 1.16 SER 412 -0.21 SER 424

LYS 423 1.04 ARG 413 -0.19 SER 424

LYS 423 1.02 ALA 414 -0.18 SER 424

LYS 423 1.09 LEU 415 -0.19 SER 424

LYS 423 1.06 GLY 416 -0.20 SER 424

LYS 423 1.17 PHE 417 -0.27 SER 424

LYS 423 1.13 PRO 418 -0.26 SER 424

LYS 423 1.15 LEU 419 -0.23 ARG 164

PRO 422 1.31 GLU 420 -0.64 SER 424

PRO 422 1.29 ARG 421 -0.32 ALA 159

GLY 44 1.70 PRO 422 0.00 ALA 1

MET 48 1.89 LYS 423 0.00 ALA 1

LYS 423 1.32 SER 424 -0.64 GLU 420

LYS 423 1.29 MET 425 -0.48 ALA 32

LYS 423 1.19 SER 426 -0.39 ALA 32

LYS 423 1.21 THR 427 -0.34 ALA 32

LYS 423 1.08 ALA 428 -0.36 ALA 32

LYS 423 1.12 GLY 429 -0.48 ALA 32

LYS 423 1.27 LEU 430 -0.49 ALA 32

LYS 423 1.19 GLU 431 -0.40 ALA 32

LYS 423 1.09 LYS 432 -0.48 ALA 32

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.

*** close cutoff 10 melek ***

CA distance fluctuations for 260522120726406031

--- normal mode 10 ---

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

* close cutoff 10 melek *