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 11 ---

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
VAL 33 0.38 ALA 1 -0.25 LYS 423

VAL 33 0.34 SER 2 -0.22 PRO 422

VAL 33 0.31 SER 3 -0.20 PRO 422

VAL 33 0.28 THR 4 -0.20 PRO 422

VAL 33 0.28 ASN 5 -0.18 PRO 422

VAL 33 0.30 LEU 6 -0.20 PRO 422

VAL 33 0.28 LYS 7 -0.15 PRO 422

VAL 33 0.30 ASP 8 -0.13 PRO 422

VAL 33 0.34 VAL 9 -0.17 PRO 422

VAL 33 0.35 LEU 10 -0.17 PRO 422

VAL 33 0.32 ALA 11 -0.11 PRO 422

VAL 33 0.35 SER 12 -0.13 PRO 422

VAL 33 0.42 LEU 13 -0.16 LYS 423

VAL 33 0.39 ILE 14 -0.14 ARG 421

VAL 33 0.35 PRO 15 -0.20 LYS 423

VAL 33 0.39 LYS 16 -0.33 LYS 423

VAL 33 0.47 GLU 17 -0.32 GLY 99

VAL 33 0.41 GLN 18 -0.31 GLU 54

ALA 32 0.38 ALA 19 -0.43 LYS 423

THR 31 0.47 ARG 20 -0.59 LYS 423

VAL 33 0.50 ILE 21 -0.63 GLU 54

THR 31 0.42 LYS 22 -0.42 LYS 423

ASN 30 0.45 THR 23 -0.80 LYS 423

THR 31 0.54 PHE 24 -0.87 LYS 423

THR 31 0.53 ARG 25 -0.96 ILE 52

ASN 30 0.45 GLN 26 -0.81 ARG 421

ASN 30 0.52 GLN 27 -0.89 LYS 423

ASN 30 0.59 HIS 28 -1.05 ARG 421

ASN 30 0.63 GLY 29 -1.40 ARG 421

GLY 29 0.63 ASN 30 -1.27 ARG 421

GLY 29 0.60 THR 31 -0.91 LEU 430

VAL 33 0.82 ALA 32 -0.88 LEU 430

ALA 32 0.82 VAL 33 -0.43 LYS 423

VAL 57 0.45 GLY 34 -0.23 LEU 430

GLY 50 0.46 GLN 35 -0.18 GLY 312

GLY 50 0.44 ILE 36 -0.32 ALA 32

LYS 432 0.53 THR 37 -0.30 VAL 38

LEU 430 0.81 VAL 38 -0.32 LEU 135

LYS 432 0.74 ASP 39 -0.42 LEU 135

SER 426 0.67 MET 40 -0.40 ASN 267

SER 426 0.80 SER 41 -0.45 ASN 30

THR 427 0.88 TYR 42 -0.45 ALA 147

LYS 368 0.90 GLY 43 -0.51 ALA 143

SER 426 0.94 GLY 44 -0.75 ASN 267

SER 426 0.70 MET 45 -0.52 ASN 30

VAL 322 0.67 ARG 46 -0.48 GLY 271

PRO 60 0.65 GLY 47 -0.47 PRO 422

ASP 59 0.46 MET 48 -0.41 PRO 422

VAL 57 0.47 LYS 49 -0.74 PRO 422

GLN 35 0.46 GLY 50 -1.11 GLY 29

SER 426 0.46 LEU 51 -0.97 GLY 29

VAL 33 0.51 ILE 52 -0.96 ARG 25

VAL 33 0.46 TYR 53 -0.66 ARG 25

VAL 33 0.51 GLU 54 -0.63 ILE 21

VAL 33 0.42 THR 55 -0.55 PRO 422

VAL 33 0.42 SER 56 -0.70 PRO 422

GLY 47 0.53 VAL 57 -0.82 PRO 422

GLY 47 0.57 LEU 58 -0.95 PRO 422

GLY 47 0.64 ASP 59 -0.90 PRO 422

GLY 47 0.65 PRO 60 -0.95 PRO 422

GLY 43 0.60 ASP 61 -0.78 PRO 422

GLY 43 0.51 GLU 62 -0.73 PRO 422

GLY 43 0.47 GLY 63 -0.79 PRO 422

SER 426 0.45 ILE 64 -0.77 PRO 422

GLY 47 0.44 ARG 65 -0.67 PRO 422

VAL 33 0.38 PHE 66 -0.60 PRO 422

VAL 33 0.45 ARG 67 -0.51 PRO 422

VAL 33 0.47 GLY 68 -0.53 PRO 422

VAL 33 0.39 PHE 69 -0.53 PRO 422

SER 426 0.37 SER 70 -0.57 PRO 422

SER 426 0.38 ILE 71 -0.55 PRO 422

SER 426 0.36 PRO 72 -0.49 PRO 422

SER 426 0.33 GLU 73 -0.47 PRO 422

SER 426 0.33 CYS 74 -0.47 PRO 422

SER 426 0.33 GLN 75 -0.45 PRO 422

SER 426 0.31 LYS 76 -0.41 PRO 422

VAL 33 0.30 LEU 77 -0.39 PRO 422

VAL 33 0.29 LEU 78 -0.38 PRO 422

SER 426 0.26 PRO 79 -0.34 PRO 422

SER 426 0.27 LYS 80 -0.34 PRO 422

SER 426 0.26 ALA 81 -0.31 PRO 422

SER 426 0.24 GLY 82 -0.28 PRO 422

SER 426 0.28 GLY 84 -0.33 PRO 422

SER 426 0.30 GLU 85 -0.36 PRO 422

SER 426 0.32 GLU 86 -0.39 PRO 422

SER 426 0.31 PRO 87 -0.39 PRO 422

SER 426 0.30 LEU 88 -0.37 PRO 422

SER 426 0.31 PRO 89 -0.39 PRO 422

SER 426 0.27 GLU 90 -0.34 PRO 422

VAL 33 0.28 GLY 91 -0.36 PRO 422

SER 426 0.30 LEU 92 -0.42 PRO 422

VAL 33 0.29 PHE 93 -0.38 PRO 422

VAL 33 0.32 TRP 94 -0.34 PRO 422

VAL 33 0.36 LEU 95 -0.39 PRO 422

VAL 33 0.37 LEU 96 -0.44 PRO 422

VAL 33 0.36 VAL 97 -0.34 PRO 422

VAL 33 0.39 THR 98 -0.31 PRO 422

VAL 33 0.43 GLY 99 -0.38 PRO 422

VAL 33 0.40 GLN 100 -0.34 PRO 422

VAL 33 0.36 ILE 101 -0.35 PRO 422

VAL 33 0.32 PRO 102 -0.31 PRO 422

VAL 33 0.30 THR 103 -0.28 PRO 422

VAL 33 0.26 PRO 104 -0.28 PRO 422

VAL 33 0.26 GLU 105 -0.24 PRO 422

VAL 33 0.28 GLN 106 -0.25 PRO 422

VAL 33 0.26 VAL 107 -0.28 PRO 422

VAL 33 0.23 SER 108 -0.25 PRO 422

VAL 33 0.24 TRP 109 -0.22 PRO 422

VAL 33 0.24 VAL 110 -0.25 PRO 422

SER 426 0.22 SER 111 -0.25 PRO 422

VAL 33 0.20 LYS 112 -0.21 PRO 422

VAL 33 0.21 GLU 113 -0.19 PRO 422

SER 426 0.21 TRP 114 -0.21 PRO 422

SER 426 0.20 ALA 115 -0.20 PRO 422

VAL 33 0.17 LYS 116 -0.19 GLY 44

SER 426 0.17 ARG 117 -0.22 GLY 44

SER 426 0.19 ALA 118 -0.24 GLY 44

LYS 423 0.19 ALA 119 -0.28 GLY 44

LYS 423 0.23 LEU 120 -0.33 GLY 44

LYS 423 0.27 PRO 121 -0.35 GLY 44

LYS 423 0.28 SER 122 -0.36 GLY 44

LYS 423 0.32 HIS 123 -0.41 GLY 44

LYS 423 0.31 VAL 124 -0.42 GLY 44

LYS 423 0.27 VAL 125 -0.38 GLY 44

LYS 423 0.30 THR 126 -0.40 GLY 44

LYS 423 0.33 MET 127 -0.45 GLY 44

LYS 423 0.28 LEU 128 -0.42 GLY 44

LYS 423 0.26 ASP 129 -0.39 GLY 44

LYS 423 0.30 ASN 130 -0.43 GLY 43

LYS 423 0.31 PHE 131 -0.46 GLY 44

ALA 428 0.32 PRO 132 -0.45 GLY 43

ALA 428 0.34 THR 133 -0.39 GLY 44

ALA 428 0.38 ASN 134 -0.43 GLY 43

ALA 428 0.38 LEU 135 -0.49 GLY 44

SER 426 0.42 HIS 136 -0.46 GLY 44

SER 426 0.40 PRO 137 -0.42 GLY 44

SER 426 0.43 MET 138 -0.48 GLY 44

SER 426 0.40 SER 139 -0.59 GLY 44

SER 426 0.34 GLN 140 -0.51 GLY 44

SER 426 0.35 LEU 141 -0.47 GLY 44

SER 426 0.36 SER 142 -0.58 GLY 44

LYS 423 0.39 ALA 143 -0.60 GLY 44

LYS 423 0.33 ALA 144 -0.50 GLY 44

LYS 423 0.33 ILE 145 -0.49 GLY 44

LYS 423 0.42 THR 146 -0.57 GLY 44

LYS 423 0.40 ALA 147 -0.51 GLY 44

LYS 423 0.34 LEU 148 -0.44 GLY 44

LYS 423 0.39 ASN 149 -0.45 GLY 44

LYS 423 0.38 SER 150 -0.42 GLY 44

LYS 423 0.33 GLU 151 -0.36 GLY 44

LYS 423 0.34 SER 152 -0.35 GLY 44

LYS 423 0.31 ASN 153 -0.29 ASN 30

LYS 423 0.34 PHE 154 -0.33 ASN 30

LYS 423 0.42 ALA 155 -0.39 ASN 30

LYS 423 0.39 ARG 156 -0.35 TYR 42

LYS 423 0.35 ALA 157 -0.30 ASN 30

LYS 423 0.42 TYR 158 -0.36 ASN 30

LYS 423 0.46 ALA 159 -0.39 TYR 42

LYS 423 0.39 GLU 160 -0.34 TYR 42

LYS 423 0.40 GLY 161 -0.30 ASN 30

LYS 423 0.34 ILE 162 -0.25 ASN 30

LYS 423 0.31 ASN 163 -0.20 ASN 30

LYS 423 0.31 ARG 164 -0.22 ASN 30

ALA 19 0.33 THR 165 -0.15 LYS 432

ALA 19 0.27 LYS 166 -0.15 ASN 30

LYS 423 0.27 TYR 167 -0.24 ASN 30

VAL 33 0.28 TRP 168 -0.19 GLY 29

VAL 33 0.26 GLU 169 -0.16 ASN 30

LYS 423 0.23 PHE 170 -0.23 ASN 30

LYS 423 0.23 VAL 171 -0.27 GLY 29

VAL 33 0.25 TYR 172 -0.21 GLY 29

VAL 33 0.21 GLU 173 -0.21 GLY 29

LYS 423 0.23 ASP 174 -0.27 GLY 29

SER 426 0.22 ALA 175 -0.29 GLY 29

VAL 33 0.21 MET 176 -0.23 GLY 29

SER 426 0.19 ASP 177 -0.26 GLY 44

SER 426 0.24 LEU 178 -0.30 GLY 29

SER 426 0.26 ILE 179 -0.28 GLY 29

SER 426 0.23 ALA 180 -0.24 GLY 29

SER 426 0.24 LYS 181 -0.29 GLY 44

SER 426 0.28 LEU 182 -0.30 GLY 44

SER 426 0.29 PRO 183 -0.27 GLY 29

SER 426 0.26 CYS 184 -0.28 GLY 44

SER 426 0.28 VAL 185 -0.34 GLY 44

SER 426 0.32 ALA 186 -0.32 GLY 44

SER 426 0.30 ALA 187 -0.28 GLY 44

SER 426 0.28 LYS 188 -0.32 GLY 44

SER 426 0.31 ILE 189 -0.35 GLY 44

SER 426 0.33 TYR 190 -0.29 GLY 44

SER 426 0.29 ARG 191 -0.28 GLY 44

ALA 428 0.29 ASN 192 -0.32 GLY 44

ALA 428 0.33 LEU 193 -0.32 GLY 44

ALA 428 0.33 TYR 194 -0.26 GLY 44

ALA 428 0.30 ARG 195 -0.25 GLY 44

ALA 428 0.28 ALA 196 -0.27 GLY 44

ALA 428 0.27 GLY 197 -0.29 GLY 44

ALA 428 0.25 SER 198 -0.26 GLY 44

ALA 428 0.23 SER 199 -0.26 GLY 44

SER 426 0.24 ILE 200 -0.25 GLY 44

SER 426 0.22 GLY 201 -0.22 GLY 44

SER 426 0.20 ALA 202 -0.21 GLY 44

SER 426 0.21 ILE 203 -0.19 GLY 44

SER 426 0.20 ASP 204 -0.20 PRO 422

SER 426 0.19 SER 205 -0.19 PRO 422

SER 426 0.20 LYS 206 -0.21 PRO 422

SER 426 0.23 LEU 207 -0.24 PRO 422

SER 426 0.25 ASP 208 -0.27 PRO 422

SER 426 0.26 TRP 209 -0.28 PRO 422

SER 426 0.29 SER 210 -0.32 PRO 422

SER 426 0.27 HIS 211 -0.29 PRO 422

SER 426 0.25 ASN 212 -0.25 PRO 422

SER 426 0.28 PHE 213 -0.28 PRO 422

SER 426 0.30 THR 214 -0.28 PRO 422

SER 426 0.27 ASN 215 -0.25 PRO 422

SER 426 0.27 MET 216 -0.23 PRO 422

SER 426 0.30 LEU 217 -0.26 PRO 422

SER 426 0.28 GLY 218 -0.24 PRO 422

SER 426 0.30 TYR 219 -0.27 PRO 422

SER 426 0.28 THR 220 -0.26 PRO 422

SER 426 0.30 ASP 221 -0.29 PRO 422

SER 426 0.30 PRO 222 -0.30 PRO 422

SER 426 0.32 GLN 223 -0.32 PRO 422

SER 426 0.33 PHE 224 -0.33 PRO 422

SER 426 0.31 THR 225 -0.32 PRO 422

SER 426 0.32 GLU 226 -0.35 PRO 422

SER 426 0.35 LEU 227 -0.38 PRO 422

SER 426 0.35 MET 228 -0.38 PRO 422

SER 426 0.33 ARG 229 -0.38 PRO 422

SER 426 0.36 LEU 230 -0.43 PRO 422

SER 426 0.39 TYR 231 -0.46 PRO 422

SER 426 0.37 LEU 232 -0.44 PRO 422

SER 426 0.36 THR 233 -0.47 PRO 422

SER 426 0.40 ILE 234 -0.54 PRO 422

SER 426 0.43 HIS 235 -0.57 PRO 422

SER 426 0.40 SER 236 -0.55 PRO 422

SER 426 0.43 ASP 237 -0.66 PRO 422

SER 426 0.48 HIS 238 -0.83 PRO 422

SER 426 0.47 GLU 239 -0.92 PRO 422

SER 426 0.49 GLY 240 -0.94 PRO 422

SER 426 0.60 GLY 241 -1.28 PRO 422

SER 426 0.61 ASN 242 -1.03 PRO 422

SER 426 0.63 VAL 243 -0.75 PRO 422

SER 426 0.53 SER 244 -0.59 PRO 422

SER 426 0.49 ALA 245 -0.67 PRO 422

SER 426 0.53 HIS 246 -0.72 GLY 29

SER 426 0.51 THR 247 -0.68 GLY 29

SER 426 0.40 SER 248 -0.60 GLY 29

SER 426 0.39 HIS 249 -0.70 GLY 29

LYS 423 0.55 LEU 250 -0.82 GLY 29

LYS 423 0.58 VAL 251 -0.67 ASN 30

LYS 423 0.46 GLY 252 -0.57 GLY 29

LYS 423 0.53 SER 253 -0.64 GLY 29

LYS 423 0.66 ALA 254 -0.72 ASN 30

LYS 423 0.54 LEU 255 -0.55 ASN 30

LYS 423 0.54 SER 256 -0.55 ASN 30

LYS 423 0.42 ASP 257 -0.44 ASN 30

LYS 423 0.33 PRO 258 -0.40 GLY 29

LYS 423 0.36 TYR 259 -0.44 GLY 44

LYS 423 0.45 LEU 260 -0.55 GLY 44

LYS 423 0.42 SER 261 -0.51 GLY 29

SER 426 0.35 PHE 262 -0.46 GLY 29

LYS 423 0.38 ALA 263 -0.58 GLY 44

LYS 423 0.46 ALA 264 -0.72 GLY 44

SER 426 0.46 ALA 265 -0.53 GLY 44

SER 426 0.45 MET 266 -0.54 GLY 44

SER 426 0.50 ASN 267 -0.75 GLY 44

SER 426 0.59 GLY 268 -0.61 GLY 44

SER 426 0.55 LEU 269 -0.48 PRO 422

SER 426 0.55 ALA 270 -0.47 GLY 44

SER 426 0.64 GLY 271 -0.48 ARG 46

SER 426 0.66 PRO 272 -0.41 PRO 422

SER 426 0.72 LEU 273 -0.51 PRO 422

SER 426 0.64 HIS 274 -0.60 PRO 422

SER 426 0.56 GLY 275 -0.54 PRO 422

SER 426 0.57 LEU 276 -0.44 PRO 422

SER 426 0.59 ALA 277 -0.49 PRO 422

SER 426 0.53 ASN 278 -0.47 PRO 422

SER 426 0.52 GLN 279 -0.40 PRO 422

SER 426 0.56 GLU 280 -0.39 PRO 422

SER 426 0.55 VAL 281 -0.43 PRO 422

SER 426 0.50 LEU 282 -0.38 PRO 422

SER 426 0.52 LEU 283 -0.33 PRO 422

SER 426 0.55 TRP 284 -0.35 PRO 422

SER 426 0.51 LEU 285 -0.37 PRO 422

SER 426 0.49 SER 286 -0.32 PRO 422

ALA 428 0.51 GLN 287 -0.30 PRO 422

ALA 428 0.51 LEU 288 -0.33 PRO 422

ALA 428 0.47 GLN 289 -0.31 PRO 422

ALA 428 0.47 LYS 290 -0.28 PRO 422

ALA 428 0.50 ASP 291 -0.27 PRO 422

ALA 428 0.44 ASP 295 -0.30 PRO 422

ALA 428 0.47 ALA 296 -0.31 PRO 422

ALA 428 0.48 SER 297 -0.31 PRO 422

ALA 428 0.50 ASP 298 -0.33 PRO 422

ALA 428 0.52 GLU 299 -0.30 PRO 422

ALA 428 0.53 LYS 300 -0.29 PRO 422

ALA 428 0.53 LEU 301 -0.33 PRO 422

ALA 428 0.56 ARG 302 -0.33 PRO 422

ALA 428 0.58 ASP 303 -0.29 PRO 422

ALA 428 0.58 TYR 304 -0.29 PRO 422

SER 426 0.61 ILE 305 -0.33 PRO 422

ALA 428 0.64 TRP 306 -0.30 PRO 422

ALA 428 0.64 ASN 307 -0.26 PRO 422

ALA 428 0.66 THR 308 -0.29 PRO 422

ALA 428 0.71 LEU 309 -0.30 PRO 422

ALA 428 0.72 ASN 310 -0.24 PRO 422

ALA 428 0.72 SER 311 -0.23 GLN 27

ALA 428 0.78 GLY 312 -0.25 HIS 28

SER 426 0.74 ARG 313 -0.28 PRO 422

SER 426 0.73 VAL 314 -0.37 PRO 422

SER 426 0.66 VAL 315 -0.41 PRO 422

SER 426 0.62 PRO 316 -0.47 PRO 422

SER 426 0.59 GLY 317 -0.55 PRO 422

SER 426 0.62 TYR 318 -0.57 PRO 422

SER 426 0.66 GLY 319 -0.66 PRO 422

SER 426 0.66 HIS 320 -0.81 PRO 422

GLY 43 0.74 ALA 321 -0.92 PRO 422

GLY 43 0.73 VAL 322 -1.11 PRO 422

GLY 43 0.64 LEU 323 -0.93 PRO 422

GLY 43 0.70 ARG 324 -0.80 PRO 422

GLY 43 0.58 LYS 325 -0.71 PRO 422

SER 426 0.51 THR 326 -0.66 PRO 422

SER 426 0.50 ASP 327 -0.70 PRO 422

SER 426 0.45 PRO 328 -0.64 PRO 422

SER 426 0.45 ARG 329 -0.62 PRO 422

SER 426 0.48 TYR 330 -0.58 PRO 422

SER 426 0.44 THR 331 -0.55 PRO 422

SER 426 0.41 CYS 332 -0.53 PRO 422

SER 426 0.42 GLN 333 -0.50 PRO 422

SER 426 0.43 ARG 334 -0.47 PRO 422

SER 426 0.39 GLU 335 -0.45 PRO 422

SER 426 0.38 PHE 336 -0.43 PRO 422

SER 426 0.39 ALA 337 -0.41 PRO 422

SER 426 0.39 LEU 338 -0.40 PRO 422

SER 426 0.36 LYS 339 -0.39 PRO 422

SER 426 0.36 HIS 340 -0.37 PRO 422

SER 426 0.37 LEU 341 -0.36 PRO 422

SER 426 0.38 PRO 342 -0.36 PRO 422

SER 426 0.39 SER 343 -0.34 PRO 422

SER 426 0.40 ASP 344 -0.35 PRO 422

SER 426 0.42 PRO 345 -0.34 PRO 422

SER 426 0.44 MET 346 -0.36 PRO 422

SER 426 0.44 PHE 347 -0.39 PRO 422

SER 426 0.44 LYS 348 -0.38 PRO 422

SER 426 0.47 LEU 349 -0.38 PRO 422

SER 426 0.48 VAL 350 -0.43 PRO 422

SER 426 0.47 ALA 351 -0.43 PRO 422

SER 426 0.48 GLN 352 -0.40 PRO 422

SER 426 0.52 LEU 353 -0.42 PRO 422

SER 426 0.51 TYR 354 -0.47 PRO 422

SER 426 0.50 LYS 355 -0.44 PRO 422

SER 426 0.54 ILE 356 -0.41 PRO 422

SER 426 0.58 VAL 357 -0.44 PRO 422

SER 426 0.58 PRO 358 -0.49 PRO 422

SER 426 0.57 ASN 359 -0.43 PRO 422

SER 426 0.61 VAL 360 -0.39 PRO 422

SER 426 0.65 LEU 361 -0.44 PRO 422

TYR 42 0.67 LEU 362 -0.44 PRO 422

TYR 42 0.65 GLU 363 -0.37 PRO 422

THR 427 0.70 GLN 364 -0.34 PRO 422

TYR 42 0.79 GLY 365 -0.38 PRO 422

TYR 42 0.85 LYS 366 -0.39 PRO 422

TYR 42 0.81 ALA 367 -0.50 PRO 422

GLY 43 0.90 LYS 368 -0.61 PRO 422

GLY 43 0.73 ASN 369 -0.66 PRO 422

TYR 42 0.63 PRO 370 -0.57 PRO 422

SER 426 0.57 TRP 371 -0.61 PRO 422

SER 426 0.56 PRO 372 -0.61 PRO 422

SER 426 0.55 ASN 373 -0.67 PRO 422

SER 426 0.51 VAL 374 -0.63 PRO 422

SER 426 0.53 ASP 375 -0.56 PRO 422

SER 426 0.53 ALA 376 -0.53 PRO 422

SER 426 0.48 HIS 377 -0.50 PRO 422

SER 426 0.46 SER 378 -0.48 PRO 422

SER 426 0.46 GLY 379 -0.42 PRO 422

SER 426 0.44 VAL 380 -0.41 PRO 422

SER 426 0.41 LEU 381 -0.40 PRO 422

SER 426 0.40 LEU 382 -0.37 PRO 422

SER 426 0.40 GLN 383 -0.35 PRO 422

SER 426 0.39 TYR 384 -0.34 PRO 422

SER 426 0.36 TYR 385 -0.32 PRO 422

SER 426 0.36 GLY 386 -0.30 PRO 422

SER 426 0.38 MET 387 -0.32 PRO 422

SER 426 0.40 THR 388 -0.31 PRO 422

SER 426 0.41 GLU 389 -0.30 PRO 422

SER 426 0.45 MET 390 -0.33 PRO 422

SER 426 0.45 ASN 391 -0.31 GLY 29

SER 426 0.42 TYR 392 -0.32 PRO 422

SER 426 0.45 TYR 393 -0.38 PRO 422

SER 426 0.47 THR 394 -0.41 PRO 422

SER 426 0.41 VAL 395 -0.35 PRO 422

SER 426 0.40 LEU 396 -0.39 PRO 422

SER 426 0.44 PHE 397 -0.47 PRO 422

SER 426 0.42 GLY 398 -0.42 PRO 422

SER 426 0.37 VAL 399 -0.37 PRO 422

SER 426 0.38 SER 400 -0.45 PRO 422

SER 426 0.41 ARG 401 -0.51 PRO 422

SER 426 0.35 ALA 402 -0.39 PRO 422

SER 426 0.33 LEU 403 -0.42 PRO 422

SER 426 0.37 GLY 404 -0.52 PRO 422

SER 426 0.37 VAL 405 -0.46 PRO 422

SER 426 0.30 LEU 406 -0.36 GLY 29

VAL 33 0.30 ALA 407 -0.36 PRO 422

VAL 33 0.33 GLN 408 -0.38 PRO 422

VAL 33 0.28 LEU 409 -0.41 GLY 29

VAL 33 0.31 ILE 410 -0.28 GLY 29

VAL 33 0.38 TRP 411 -0.25 GLY 29

VAL 33 0.35 SER 412 -0.39 GLY 29

VAL 33 0.31 ARG 413 -0.29 GLY 29

VAL 33 0.36 ALA 414 -0.15 GLY 29

VAL 33 0.43 LEU 415 -0.16 ARG 421

VAL 33 0.35 GLY 416 -0.20 GLY 29

VAL 33 0.35 PHE 417 -0.44 GLY 29

LYS 423 0.51 PRO 418 -0.48 ASN 30

LYS 423 0.69 LEU 419 -0.82 ASN 30

LYS 423 0.71 GLU 420 -1.04 GLY 29

PRO 422 1.05 ARG 421 -1.40 GLY 29

SER 424 1.08 PRO 422 -1.28 GLY 241

SER 424 1.27 LYS 423 -0.89 GLN 27

LYS 423 1.27 SER 424 -0.70 ASN 30

LYS 423 1.13 MET 425 -0.69 THR 31

LYS 423 1.07 SER 426 -0.35 THR 31

TYR 42 0.88 THR 427 -0.44 THR 31

LYS 423 0.88 ALA 428 -0.37 THR 31

LYS 423 0.90 GLY 429 -0.55 THR 31

VAL 38 0.81 LEU 430 -0.91 THR 31

TYR 42 0.81 GLU 431 -0.70 THR 31

GLU 431 0.81 LYS 432 -0.62 THR 31

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 11 ---

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 *