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 cutoff 10 melek new *

CA distance fluctuations for 260522120818411546

--- normal mode 15 ---

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 0.31 ALA 1 -0.09 ASN 153

LYS 423 0.37 SER 2 -0.08 ASP 61

LYS 423 0.42 SER 3 -0.08 ASP 61

LYS 423 0.47 THR 4 -0.09 ASP 61

LYS 423 0.48 ASN 5 -0.11 GLN 100

LYS 423 0.53 LEU 6 -0.10 ASN 5

LYS 423 0.53 LYS 7 -0.10 LEU 33

LYS 423 0.53 ASP 8 -0.11 GLY 312

LYS 423 0.59 VAL 9 -0.13 GLY 312

LYS 423 0.64 LEU 10 -0.14 GLY 312

LYS 423 0.61 ALA 11 -0.15 GLY 312

LYS 423 0.64 ALA 12 -0.17 GLY 312

LYS 423 0.70 LEU 13 -0.23 ILE 14

LYS 423 0.75 ILE 14 -0.23 LEU 13

LYS 423 0.74 PRO 15 -0.23 THR 165

LYS 423 0.78 LYS 16 -0.18 GLY 312

LYS 423 0.86 GLU 17 -0.19 GLY 312

LYS 423 0.87 GLN 18 -0.22 THR 165

LYS 423 0.85 ALA 19 -0.28 THR 165

LYS 423 0.95 ARG 20 -0.17 PHE 24

LYS 423 1.03 ILE 21 -0.21 GLY 312

LYS 423 0.95 LYS 22 -0.35 GLN 35

LYS 423 0.97 THR 23 -0.21 LEU 163

LYS 423 1.12 PHE 24 -0.17 ARG 20

LYS 423 1.17 ARG 25 -0.31 GLY 312

LYS 423 1.03 GLN 26 -0.43 GLN 35

LYS 423 1.12 GLN 27 -0.19 GLY 312

LYS 423 1.31 HIS 28 -0.19 GLY 312

LYS 423 1.32 GLY 29 -0.38 GLY 312

LYS 423 1.47 GLY 30 -0.48 GLY 312

LYS 423 1.51 THR 31 -0.45 GLY 312

LYS 423 1.67 ALA 32 -0.46 GLY 312

LYS 423 1.49 LEU 33 -0.59 GLY 312

LYS 423 1.42 GLY 34 -0.37 PRO 418

LYS 423 1.26 GLN 35 -0.90 PRO 422

LYS 423 1.47 ILE 36 -0.43 MET 425

LYS 423 1.36 THR 37 -0.38 GLY 312

LYS 423 1.31 VAL 38 -0.48 GLY 312

LYS 423 1.19 ASP 39 -0.51 GLY 312

LYS 423 1.25 MET 40 -0.41 ARG 313

LYS 423 1.28 SER 41 -0.41 SER 311

LYS 423 1.09 TYR 42 -0.39 SER 311

LYS 423 1.08 GLY 43 -0.46 SER 311

LYS 423 1.07 GLY 44 -0.39 SER 311

LYS 423 1.24 MET 45 -0.39 ARG 313

LYS 423 1.15 ARG 46 -0.46 ARG 313

LYS 423 1.19 GLY 47 -0.48 ARG 313

LYS 423 1.34 MET 48 -0.38 ARG 313

LYS 423 1.34 LYS 49 -0.40 ARG 313

LYS 423 1.35 GLY 50 -0.47 GLU 420

LYS 423 1.24 LEU 51 -0.33 ARG 313

LYS 423 1.17 VAL 52 -0.36 LEU 33

LYS 423 1.05 TYR 53 -0.32 LEU 33

LYS 423 0.98 GLU 54 -0.26 ARG 313

LYS 423 0.89 THR 55 -0.21 LEU 33

LYS 423 0.93 SER 56 -0.23 VAL 314

LYS 423 1.00 VAL 57 -0.28 VAL 314

LYS 423 1.00 LEU 58 -0.28 VAL 314

LYS 423 0.99 ASP 59 -0.25 THR 31

LYS 423 1.01 PRO 60 -0.28 ALA 32

LYS 423 0.94 ASP 61 -0.24 ALA 32

LYS 423 0.87 GLU 62 -0.21 ALA 32

LYS 423 0.87 GLY 63 -0.19 THR 31

LYS 423 0.87 ILE 64 -0.18 VAL 314

LYS 423 0.87 ARG 65 -0.17 THR 31

LYS 423 0.82 PHE 66 -0.16 THR 31

LYS 423 0.86 ARG 67 -0.20 THR 31

LYS 423 0.87 GLY 68 -0.22 THR 31

LYS 423 0.80 PHE 69 -0.20 THR 31

LYS 423 0.79 SER 70 -0.18 THR 31

LYS 423 0.73 ILE 71 -0.15 THR 31

LYS 423 0.70 PRO 72 -0.15 THR 31

LYS 423 0.70 GLU 73 -0.22 ASP 61

LYS 423 0.68 CYS 74 -0.15 THR 31

LYS 423 0.62 GLN 75 -0.13 ASP 61

LYS 423 0.61 LYS 76 -0.16 ASP 61

LYS 423 0.62 LEU 77 -0.16 ASP 61

LYS 423 0.60 LEU 78 -0.13 THR 31

LYS 423 0.53 PRO 79 -0.11 ASP 61

LYS 423 0.49 LYS 80 -0.11 GLY 81

LYS 423 0.43 GLY 81 -0.11 LYS 80

LYS 423 0.41 GLY 82 -0.09 ASP 61

LYS 423 0.42 GLY 84 -0.09 THR 31

LYS 423 0.48 GLY 85 -0.11 THR 31

LYS 423 0.50 GLU 86 -0.11 THR 31

LYS 423 0.53 PRO 87 -0.10 THR 31

LYS 423 0.50 LEU 88 -0.10 LEU 33

LYS 423 0.53 PRO 89 -0.12 LEU 33

LYS 423 0.51 GLU 90 -0.11 LEU 33

LYS 423 0.56 GLY 91 -0.10 LEU 33

LYS 423 0.62 LEU 92 -0.12 LEU 33

LYS 423 0.61 PHE 93 -0.13 LEU 33

LYS 423 0.61 TRP 94 -0.11 LEU 33

LYS 423 0.68 LEU 95 -0.11 THR 31

LYS 423 0.73 LEU 96 -0.14 LEU 33

LYS 423 0.71 VAL 97 -0.13 LEU 33

LYS 423 0.71 THR 98 -0.13 GLY 312

LYS 423 0.77 GLY 99 -0.14 THR 31

LYS 423 0.70 GLN 100 -0.14 THR 31

LYS 423 0.65 ILE 101 -0.14 THR 31

LYS 423 0.58 PRO 102 -0.11 THR 31

LYS 423 0.54 THR 103 -0.12 ASP 61

LYS 423 0.48 GLY 104 -0.10 ASP 61

LYS 423 0.44 ALA 105 -0.08 ASP 61

LYS 423 0.49 GLN 106 -0.09 ASP 61

LYS 423 0.48 VAL 107 -0.08 LEU 33

LYS 423 0.41 SER 108 -0.08 LEU 33

LYS 423 0.41 TRP 109 -0.08 LEU 33

LYS 423 0.43 LEU 110 -0.09 LEU 33

LYS 423 0.38 SER 111 -0.08 LEU 33

LYS 423 0.33 LYS 112 -0.08 LEU 33

LYS 423 0.35 GLU 113 -0.08 LEU 33

LYS 423 0.34 TRP 114 -0.09 LEU 33

LYS 423 0.28 ALA 115 -0.12 SER 424

LYS 423 0.25 LYS 116 -0.11 SER 424

LYS 423 0.27 ARG 117 -0.11 SER 424

LYS 423 0.23 ALA 118 -0.18 SER 424

SER 426 0.21 ALA 119 -0.23 SER 424

SER 426 0.23 LEU 120 -0.29 SER 424

SER 426 0.22 PRO 121 -0.31 SER 424

SER 426 0.22 SER 122 -0.37 SER 424

SER 426 0.23 HIS 123 -0.42 SER 424

SER 426 0.24 VAL 124 -0.43 SER 424

SER 426 0.23 VAL 125 -0.45 SER 424

SER 426 0.23 THR 126 -0.51 SER 424

SER 426 0.24 MET 127 -0.58 SER 424

SER 426 0.25 LEU 128 -0.57 SER 424

SER 426 0.23 ASP 129 -0.59 SER 424

SER 426 0.23 ASN 130 -0.67 SER 424

SER 426 0.25 PHE 131 -0.73 SER 424

SER 426 0.24 PRO 132 -0.83 SER 424

SER 426 0.24 THR 133 -0.80 SER 424

SER 426 0.25 ASN 134 -0.92 SER 424

SER 426 0.27 LEU 135 -0.90 SER 424

SER 426 0.28 HIS 136 -0.81 SER 424

SER 426 0.28 PRO 137 -0.65 SER 424

SER 426 0.30 MET 138 -0.60 SER 424

SER 426 0.31 SER 139 -0.71 SER 424

SER 426 0.29 GLN 140 -0.65 SER 424

SER 426 0.29 LEU 141 -0.50 SER 424

SER 426 0.32 SER 142 -0.48 SER 424

SER 426 0.30 ALA 143 -0.55 SER 424

SER 426 0.28 ALA 144 -0.45 SER 424

SER 426 0.29 ILE 145 -0.32 SER 424

SER 426 0.30 THR 146 -0.34 SER 424

SER 426 0.28 ALA 147 -0.38 SER 424

SER 426 0.27 LEU 148 -0.28 SER 424

SER 426 0.28 ASN 149 -0.19 SER 424

SER 426 0.25 SER 150 -0.21 GLN 35

SER 426 0.24 GLU 151 -0.19 GLN 35

LYS 423 0.26 SER 152 -0.21 GLN 35

LYS 423 0.29 ASN 153 -0.23 GLN 35

LYS 423 0.37 PHE 154 -0.27 GLN 35

LYS 423 0.28 ALA 155 -0.31 GLN 35

GLY 30 0.23 ARG 156 -0.31 GLN 35

LYS 423 0.29 ALA 157 -0.33 GLN 35

LYS 423 0.31 TYR 158 -0.38 GLN 35

ALA 32 0.26 ALA 159 -0.39 GLN 35

GLY 30 0.24 GLU 160 -0.38 GLN 35

LYS 423 0.29 GLY 161 -0.43 GLN 35

LYS 423 0.38 ILE 162 -0.39 GLN 35

LYS 423 0.48 LEU 163 -0.43 GLN 35

LYS 423 0.61 ARG 164 -0.44 GLN 35

LYS 423 0.63 THR 165 -0.36 GLN 35

LYS 423 0.54 LYS 166 -0.32 GLN 35

LYS 423 0.58 TYR 167 -0.31 GLN 35

LYS 423 0.61 TRP 168 -0.22 GLN 35

LYS 423 0.52 GLU 169 -0.21 GLN 35

LYS 423 0.46 MET 170 -0.21 GLN 35

LYS 423 0.52 VAL 171 -0.19 GLN 35

LYS 423 0.52 TYR 172 -0.13 GLN 35

LYS 423 0.41 GLU 173 -0.14 GLN 35

LYS 423 0.40 SER 174 -0.15 GLN 35

LYS 423 0.49 ALA 175 -0.12 LEU 33

LYS 423 0.43 MET 176 -0.11 LEU 33

LYS 423 0.34 ASP 177 -0.11 LEU 33

LYS 423 0.37 LEU 178 -0.12 LEU 33

LYS 423 0.42 ILE 179 -0.12 LEU 33

LYS 423 0.34 ALA 180 -0.13 SER 424

LYS 423 0.27 LYS 181 -0.22 SER 424

LYS 423 0.32 LEU 182 -0.24 SER 424

LYS 423 0.29 PRO 183 -0.27 SER 424

SER 426 0.24 CYS 184 -0.32 SER 424

SER 426 0.25 VAL 185 -0.38 SER 424

SER 426 0.26 ALA 186 -0.39 SER 424

SER 426 0.24 ALA 187 -0.39 SER 424

SER 426 0.23 LYS 188 -0.46 SER 424

SER 426 0.25 ILE 189 -0.53 SER 424

SER 426 0.24 TYR 190 -0.51 SER 424

SER 426 0.22 ARG 191 -0.50 SER 424

SER 426 0.22 ASN 192 -0.57 SER 424

SER 426 0.23 LEU 193 -0.63 SER 424

GLY 312 0.22 TYR 194 -0.58 SER 424

GLY 312 0.21 ARG 195 -0.52 SER 424

GLY 312 0.21 ALA 196 -0.57 SER 424

SER 426 0.21 GLY 197 -0.56 SER 424

SER 426 0.20 SER 198 -0.49 SER 424

SER 426 0.20 SER 199 -0.44 SER 424

SER 426 0.21 ILE 200 -0.39 SER 424

SER 426 0.20 GLY 201 -0.34 SER 424

SER 426 0.20 ALA 202 -0.28 SER 424

SER 426 0.20 ILE 203 -0.23 SER 424

LYS 423 0.21 ASP 204 -0.19 SER 424

LYS 423 0.25 SER 205 -0.14 SER 424

LYS 423 0.27 LYS 206 -0.12 SER 424

LYS 423 0.30 LEU 207 -0.14 SER 424

LYS 423 0.36 ASP 208 -0.10 SER 424

LYS 423 0.38 TRP 209 -0.12 SER 424

LYS 423 0.39 SER 210 -0.15 SER 424

LYS 423 0.33 HIS 211 -0.18 SER 424

LYS 423 0.28 ASN 212 -0.21 SER 424

LYS 423 0.30 PHE 213 -0.24 SER 424

LYS 423 0.28 THR 214 -0.27 SER 424

LYS 423 0.23 ASN 215 -0.28 SER 424

SER 426 0.22 MET 216 -0.32 SER 424

SER 426 0.22 LEU 217 -0.35 SER 424

SER 426 0.21 GLY 218 -0.35 SER 424

LYS 423 0.22 TYR 219 -0.34 SER 424

LYS 423 0.23 THR 220 -0.29 SER 424

LYS 423 0.27 ASP 221 -0.28 SER 424

LYS 423 0.31 ALA 222 -0.22 SER 424

LYS 423 0.35 GLN 223 -0.21 PHE 336

LYS 423 0.33 PHE 224 -0.26 SER 424

LYS 423 0.35 THR 225 -0.20 SER 424

LYS 423 0.41 GLU 226 -0.15 SER 424

LYS 423 0.43 LEU 227 -0.18 SER 424

LYS 423 0.41 MET 228 -0.19 SER 424

LYS 423 0.46 ARG 229 -0.12 LEU 33

LYS 423 0.52 LEU 230 -0.12 LEU 33

LYS 423 0.51 TYR 231 -0.14 LEU 33

LYS 423 0.52 LEU 232 -0.14 LEU 33

LYS 423 0.59 THR 233 -0.14 LEU 33

LYS 423 0.64 ILE 234 -0.15 LEU 33

LYS 423 0.64 HIS 235 -0.17 LEU 33

LYS 423 0.66 SER 236 -0.18 LEU 33

LYS 423 0.77 ASP 237 -0.21 LEU 33

LYS 423 0.86 HIS 238 -0.26 ALA 277

LYS 423 0.97 GLU 239 -0.31 LEU 33

LYS 423 1.01 GLY 240 -0.30 LEU 33

LYS 423 1.05 GLY 241 -0.36 ARG 313

LYS 423 0.91 ASN 242 -0.30 ALA 277

LYS 423 0.80 VAL 243 -0.24 LEU 33

LYS 423 0.72 SER 244 -0.21 LEU 33

LYS 423 0.83 ALA 245 -0.23 LEU 33

LYS 423 0.94 HIS 246 -0.24 ARG 313

LYS 423 0.79 THR 247 -0.29 GLY 50

LYS 423 0.72 SER 248 -0.20 GLY 50

LYS 423 0.86 HIS 249 -0.25 GLY 50

LYS 423 0.88 LEU 250 -0.44 GLY 50

LYS 423 0.68 VAL 251 -0.35 GLY 50

LYS 423 0.69 GLY 252 -0.26 GLY 50

LYS 423 0.82 SER 253 -0.32 GLY 50

LYS 423 0.67 ALA 254 -0.40 GLN 35

LYS 423 0.59 LEU 255 -0.38 GLN 35

LYS 423 0.49 SER 256 -0.30 GLN 35

LYS 423 0.44 ASP 257 -0.24 GLN 35

LYS 423 0.50 PRO 258 -0.16 GLN 35

LYS 423 0.38 TYR 259 -0.14 GLY 50

LYS 423 0.39 LEU 260 -0.20 GLY 50

LYS 423 0.54 SER 261 -0.21 GLY 50

LYS 423 0.51 PHE 262 -0.15 GLY 50

LYS 423 0.39 ALA 263 -0.27 SER 424

LYS 423 0.48 ALA 264 -0.23 GLY 50

LYS 423 0.59 ALA 265 -0.18 GLY 50

LYS 423 0.47 MET 266 -0.31 SER 424

LYS 423 0.42 ASN 267 -0.44 SER 424

LYS 423 0.58 GLY 268 -0.26 SER 424

LYS 423 0.55 LEU 269 -0.29 SER 424

LYS 423 0.43 ALA 270 -0.51 SER 424

LYS 423 0.50 GLY 271 -0.49 SER 424

LYS 423 0.48 PRO 272 -0.52 SER 424

LYS 423 0.60 LEU 273 -0.33 SER 424

LYS 423 0.62 HIS 274 -0.27 SER 424

LYS 423 0.51 GLY 275 -0.37 SER 424

LYS 423 0.47 LEU 276 -0.40 SER 424

LYS 423 0.54 ALA 277 -0.32 LEU 33

LYS 423 0.50 ASN 278 -0.28 SER 424

LYS 423 0.41 GLN 279 -0.43 SER 424

LYS 423 0.44 GLU 280 -0.40 SER 424

LYS 423 0.46 VAL 281 -0.32 SER 424

LYS 423 0.38 LEU 282 -0.42 SER 424

ARG 313 0.37 GLY 283 -0.54 SER 424

ARG 313 0.49 TRP 284 -0.44 SER 424

ARG 313 0.47 LEU 285 -0.41 SER 424

ARG 313 0.44 ALA 286 -0.53 SER 424

ARG 313 0.53 GLN 287 -0.57 SER 424

ARG 313 0.57 LEU 288 -0.46 SER 424

ARG 313 0.48 GLN 289 -0.50 SER 424

ARG 313 0.46 LYS 290 -0.62 GLY 296

GLY 312 0.51 ALA 291 -0.66 SER 300

GLY 296 0.60 ALA 295 -0.37 SER 424

ALA 295 0.60 GLY 296 -0.62 LYS 290

ALA 351 0.34 ALA 297 -0.36 ALA 291

LYS 423 0.40 ASP 298 -0.24 SER 424

ASN 359 0.37 ALA 299 -0.34 ALA 291

ARG 302 0.38 SER 300 -0.66 ALA 291

GLY 312 0.35 LEU 301 -0.36 SER 424

LYS 423 0.42 ARG 302 -0.25 SER 424

GLY 312 0.38 ASP 303 -0.33 SER 424

GLY 312 0.41 TYR 304 -0.42 SER 424

LYS 423 0.42 ILE 305 -0.29 SER 424

LYS 423 0.45 TRP 306 -0.26 LEU 33

GLY 312 0.42 ASN 307 -0.33 LEU 33

GLY 312 0.46 THR 308 -0.38 LEU 33

LYS 423 0.52 LEU 309 -0.40 LEU 33

LYS 423 0.48 ASN 310 -0.40 LEU 33

ALA 291 0.50 SER 311 -0.49 ASP 39

LEU 288 0.53 GLY 312 -0.59 LEU 33

LEU 288 0.57 ARG 313 -0.57 LEU 33

LYS 423 0.53 VAL 314 -0.50 LEU 33

LYS 423 0.54 VAL 315 -0.34 LEU 33

LYS 423 0.56 PRO 316 -0.32 LEU 33

LYS 423 0.63 GLY 317 -0.28 LEU 33

LYS 423 0.70 TYR 318 -0.23 LEU 33

LYS 423 0.81 GLY 319 -0.23 ALA 32

LYS 423 0.90 HIS 320 -0.24 ALA 32

LYS 423 1.01 ALA 321 -0.30 ALA 32

LYS 423 1.05 VAL 322 -0.32 ALA 32

LYS 423 0.95 LEU 323 -0.24 ALA 32

LYS 423 0.93 ARG 324 -0.24 ALA 32

LYS 423 0.84 LYS 325 -0.20 ALA 32

LYS 423 0.77 THR 326 -0.17 ALA 32

LYS 423 0.78 ASP 327 -0.15 THR 31

LYS 423 0.73 PRO 328 -0.14 THR 31

LYS 423 0.69 ARG 329 -0.12 THR 31

LYS 423 0.64 TYR 330 -0.13 THR 31

LYS 423 0.64 THR 331 -0.14 GLN 223

LYS 423 0.61 CYS 332 -0.16 GLN 223

LYS 423 0.55 GLN 333 -0.14 GLN 223

LYS 423 0.54 ARG 334 -0.10 THR 31

LYS 423 0.55 GLU 335 -0.16 GLN 223

LYS 423 0.49 PHE 336 -0.21 GLN 223

LYS 423 0.45 ALA 337 -0.17 SER 424

LYS 423 0.45 LEU 338 -0.15 SER 424

GLY 85 0.46 LYS 339 -0.12 SER 424

LYS 423 0.40 HIS 340 -0.19 SER 424

LYS 423 0.37 LEU 341 -0.24 SER 424

LYS 423 0.39 PRO 342 -0.22 SER 424

GLY 296 0.40 GLY 343 -0.26 SER 424

LYS 423 0.33 ASP 344 -0.31 SER 424

ARG 313 0.34 PRO 345 -0.36 SER 424

ARG 313 0.35 MET 346 -0.37 SER 424

LYS 423 0.40 PHE 347 -0.28 SER 424

GLY 296 0.45 LYS 348 -0.25 SER 424

LYS 423 0.40 LEU 349 -0.29 SER 424

LYS 423 0.46 VAL 350 -0.23 SER 424

LYS 423 0.49 ALA 351 -0.16 SER 424

LYS 423 0.47 GLN 352 -0.19 SER 424

LYS 423 0.51 LEU 353 -0.17 SER 424

LYS 423 0.58 TYR 354 -0.09 ALA 32

LYS 423 0.58 LYS 355 -0.08 GLY 343

LYS 423 0.54 ILE 356 -0.10 SER 424

LYS 423 0.58 VAL 357 -0.16 ALA 32

LYS 423 0.68 PRO 358 -0.15 ALA 32

LYS 423 0.66 ASN 359 -0.14 ALA 32

LYS 423 0.61 VAL 360 -0.18 ALA 32

LYS 423 0.69 LEU 361 -0.24 ALA 32

LYS 423 0.75 LEU 362 -0.22 ALA 32

LYS 423 0.70 GLU 363 -0.21 ALA 32

LYS 423 0.68 GLN 364 -0.28 ALA 32

LYS 423 0.78 GLY 365 -0.32 ALA 32

LYS 423 0.79 ALA 366 -0.35 ALA 32

LYS 423 0.85 ALA 367 -0.28 ALA 32

LYS 423 0.93 ALA 368 -0.26 ALA 32

LYS 423 0.89 ASN 369 -0.23 ALA 32

LYS 423 0.79 PRO 370 -0.21 ALA 32

LYS 423 0.76 TRP 371 -0.17 ALA 32

LYS 423 0.71 PRO 372 -0.15 ALA 32

LYS 423 0.72 ASN 373 -0.18 LEU 33

LYS 423 0.65 VAL 374 -0.19 LEU 33

LYS 423 0.60 ASP 375 -0.24 LEU 33

LYS 423 0.57 ALA 376 -0.20 LEU 33

LYS 423 0.54 HIS 377 -0.16 LEU 33

LYS 423 0.49 SER 378 -0.22 SER 424

LYS 423 0.42 GLY 379 -0.33 SER 424

LYS 423 0.39 VAL 380 -0.33 SER 424

LYS 423 0.40 LEU 381 -0.29 SER 424

LYS 423 0.36 LEU 382 -0.34 SER 424

LYS 423 0.30 GLN 383 -0.41 SER 424

LYS 423 0.30 TYR 384 -0.36 SER 424

LYS 423 0.28 TYR 385 -0.36 SER 424

ARG 313 0.25 GLY 386 -0.43 SER 424

LYS 423 0.26 MET 387 -0.45 SER 424

GLY 312 0.28 THR 388 -0.51 SER 424

GLY 312 0.25 GLU 389 -0.59 SER 424

LYS 423 0.27 MET 390 -0.57 SER 424

LYS 423 0.25 ASN 391 -0.65 SER 424

LYS 423 0.27 TYR 392 -0.55 SER 424

LYS 423 0.36 TYR 393 -0.44 SER 424

LYS 423 0.41 THR 394 -0.42 SER 424

LYS 423 0.37 VAL 395 -0.39 SER 424

LYS 423 0.41 LEU 396 -0.30 SER 424

LYS 423 0.51 PHE 397 -0.23 SER 424

LYS 423 0.49 GLY 398 -0.23 SER 424

LYS 423 0.45 VAL 399 -0.20 SER 424

LYS 423 0.54 SER 400 -0.16 LEU 33

LYS 423 0.63 ARG 401 -0.19 LEU 33

LYS 423 0.57 ALA 402 -0.16 LEU 33

LYS 423 0.61 LEU 403 -0.16 LEU 33

LYS 423 0.72 GLY 404 -0.19 LEU 33

LYS 423 0.72 VAL 405 -0.20 LEU 33

LYS 423 0.65 LEU 406 -0.16 LEU 33

LYS 423 0.70 ALA 407 -0.16 LEU 33

LYS 423 0.81 GLN 408 -0.19 LEU 33

LYS 423 0.75 LEU 409 -0.17 ARG 313

LYS 423 0.70 ILE 410 -0.15 ARG 313

LYS 423 0.81 TRP 411 -0.19 ARG 313

LYS 423 0.88 SER 412 -0.23 ARG 313

LYS 423 0.76 ARG 413 -0.23 GLN 35

LYS 423 0.76 ALA 414 -0.20 GLN 35

LYS 423 0.88 LEU 415 -0.23 GLY 312

LYS 423 0.85 GLY 416 -0.35 GLN 35

LYS 423 0.98 PHE 417 -0.32 GLN 35

LYS 423 1.00 PRO 418 -0.51 GLN 35

LYS 423 0.96 LEU 419 -0.52 GLN 35

LYS 423 1.08 GLU 420 -0.47 GLY 50

LYS 423 1.16 ARG 421 -0.38 GLN 35

LYS 423 1.31 PRO 422 -0.90 GLN 35

ALA 32 1.67 LYS 423 -0.14 ASN 130

MET 425 1.30 SER 424 -0.92 ASN 134

SER 424 1.30 MET 425 -0.43 ILE 36

SER 424 1.12 SER 426 -0.21 ILE 36

LYS 423 0.98 THR 427 -0.24 SER 311

SER 424 1.01 ASP 428 -0.21 SER 311

SER 424 1.25 GLY 429 -0.27 SER 311

SER 424 1.24 LEU 430 -0.33 SER 311

LYS 423 1.08 ILE 431 -0.35 SER 311

SER 424 1.17 ALA 432 -0.34 SER 311

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 cutoff 10 melek new ***

CA distance fluctuations for 260522120818411546

--- normal mode 15 ---

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 cutoff 10 melek new *