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

* *

CA distance fluctuations for 2604262204102534339

--- normal mode 16 ---

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
CYS 9 0.20 SER 1 -0.11 ASP 125

CYS 9 0.20 THR 2 -0.10 ASP 125

PRO 106 0.18 ALA 3 -0.15 ASP 125

PRO 106 0.18 GLY 4 -0.19 ASP 125

PRO 106 0.16 LYS 5 -0.15 ASP 125

LYS 99 0.15 VAL 6 -0.12 ASP 125

LYS 99 0.12 ILE 7 -0.12 GLU 74

LYS 99 0.11 LYS 8 -0.12 LYS 39

THR 2 0.20 CYS 9 -0.09 GLU 25

SER 1 0.17 LYS 10 -0.08 VAL 41

SER 1 0.14 ALA 11 -0.11 LYS 135

SER 1 0.12 ALA 12 -0.13 LYS 135

CYS 97 0.13 VAL 13 -0.16 LYS 135

CYS 97 0.12 LEU 14 -0.14 LYS 135

CYS 97 0.13 TRP 15 -0.17 LYS 135

CYS 97 0.11 GLU 16 -0.13 LYS 135

CYS 97 0.09 GLU 17 -0.13 GLU 107

SER 117 0.07 LYS 18 -0.15 GLU 107

SER 1 0.08 LYS 19 -0.12 GLU 107

SER 1 0.09 PRO 20 -0.12 LYS 135

SER 1 0.10 PHE 21 -0.14 LYS 135

SER 1 0.11 SER 22 -0.16 LYS 135

SER 1 0.14 ILE 23 -0.13 LYS 135

SER 1 0.12 GLU 24 -0.16 ARG 133

LYS 99 0.12 GLU 25 -0.09 CYS 9

LYS 99 0.15 VAL 26 -0.07 GLN 148

LYS 99 0.17 GLU 27 -0.07 LYS 39

LYS 99 0.17 VAL 28 -0.08 LEU 301

LYS 99 0.19 ALA 29 -0.14 ASP 125

GLY 98 0.19 PRO 30 -0.19 ASP 125

GLY 98 0.22 PRO 31 -0.23 ASP 125

GLY 98 0.27 LYS 32 -0.39 ASP 125

GLY 98 0.32 ALA 33 -0.30 ASP 125

GLY 98 0.35 HIS 34 -0.19 LEU 301

GLY 98 0.26 GLU 35 -0.18 ASP 125

PRO 106 0.22 VAL 36 -0.15 LEU 301

PRO 106 0.18 ARG 37 -0.12 LEU 301

PRO 106 0.16 ILE 38 -0.11 LEU 301

SER 1 0.16 LYS 39 -0.12 LYS 8

SER 1 0.14 MET 40 -0.09 LYS 8

SER 1 0.15 VAL 41 -0.09 LYS 8

SER 1 0.12 ALA 42 -0.08 LYS 10

PRO 305 0.11 THR 43 -0.06 GLY 321

ASN 300 0.12 GLY 44 -0.08 GLY 108

PRO 305 0.11 ILE 45 -0.11 GLY 108

ASN 300 0.14 CYS 46 -0.16 GLU 107

SER 117 0.15 ARG 47 -0.21 GLU 107

SER 117 0.17 SER 48 -0.22 GLU 107

SER 117 0.14 ASP 49 -0.16 GLY 108

SER 117 0.11 ASP 50 -0.18 GLU 107

SER 117 0.12 HIS 51 -0.22 GLU 107

PRO 305 0.12 VAL 52 -0.17 GLY 108

PRO 305 0.09 VAL 53 -0.16 GLU 107

PRO 305 0.08 SER 54 -0.20 GLU 107

PRO 305 0.11 GLY 55 -0.19 GLU 107

PRO 305 0.12 THR 56 -0.24 GLU 107

PRO 305 0.16 LEU 57 -0.23 GLY 108

PRO 305 0.16 VAL 58 -0.18 GLY 108

PRO 305 0.16 THR 59 -0.13 LYS 32

CYS 97 0.17 PRO 60 -0.11 LYS 32

CYS 97 0.16 LEU 61 -0.09 LYS 135

CYS 97 0.16 PRO 62 -0.13 LYS 135

CYS 97 0.16 VAL 63 -0.09 LYS 135

CYS 97 0.14 ILE 64 -0.08 LYS 135

PRO 305 0.12 ALA 65 -0.10 GLY 108

PRO 305 0.12 GLY 66 -0.10 GLY 108

PRO 305 0.14 HIS 67 -0.11 LEU 301

ASN 300 0.13 GLU 68 -0.10 LEU 301

PRO 305 0.12 ALA 69 -0.09 LEU 301

PRO 305 0.12 ALA 70 -0.09 LEU 301

PRO 106 0.13 GLY 71 -0.09 LEU 301

PRO 106 0.16 ILE 72 -0.10 LYS 8

PRO 106 0.20 VAL 73 -0.10 LEU 301

PRO 106 0.19 GLU 74 -0.12 ILE 7

PRO 106 0.21 SER 75 -0.14 ASP 125

PRO 106 0.24 ILE 76 -0.15 ASP 125

PRO 106 0.24 GLY 77 -0.23 ASP 125

PRO 106 0.27 GLU 78 -0.22 ASP 125

PRO 106 0.32 GLY 79 -0.18 LEU 301

PRO 106 0.34 VAL 80 -0.17 LEU 301

PRO 106 0.38 THR 81 -0.17 LEU 301

PRO 106 0.38 THR 82 -0.16 LEU 301

PRO 106 0.30 VAL 83 -0.14 LEU 301

PRO 106 0.27 ARG 84 -0.13 LEU 301

PRO 106 0.23 PRO 85 -0.11 LEU 301

PRO 106 0.20 GLY 86 -0.10 LYS 8

PRO 106 0.22 ASP 87 -0.11 LEU 301

PRO 106 0.19 LYS 88 -0.10 LEU 301

PRO 106 0.19 VAL 89 -0.12 LEU 301

PRO 106 0.14 ILE 90 -0.13 LEU 301

PRO 106 0.14 PRO 91 -0.15 LEU 301

PRO 305 0.15 LEU 92 -0.19 LEU 301

PRO 305 0.16 PHE 93 -0.19 LEU 301

PRO 305 0.17 THR 94 -0.26 LEU 301

GLN 124 0.16 PRO 95 -0.25 LEU 301

PRO 106 0.29 GLN 96 -0.31 CYS 97

GLN 124 0.56 CYS 97 -0.31 GLN 96

GLN 124 0.44 GLY 98 -0.51 LYS 323

ASP 125 0.50 LYS 99 -0.34 LYS 185

ASP 125 0.37 CYS 100 -0.33 LEU 301

ASP 125 0.27 ARG 101 -0.42 LEU 301

ASP 125 0.21 VAL 102 -0.46 LEU 301

GLN 124 0.32 CYS 103 -0.41 LEU 301

ASP 125 0.33 LYS 104 -0.45 LEU 301

THR 81 0.29 HIS 105 -0.59 LEU 301

ASP 326 0.40 PRO 106 -0.66 VAL 186

ASP 326 0.39 GLU 107 -0.79 VAL 186

ASP 326 0.22 GLY 108 -0.61 LEU 301

PRO 305 0.15 ASN 109 -0.40 LEU 301

PRO 305 0.21 PHE 110 -0.38 LEU 301

PRO 305 0.19 CYS 111 -0.32 LEU 301

PRO 305 0.20 LEU 112 -0.30 LEU 301

CYS 97 0.23 LYS 113 -0.23 LEU 301

PRO 305 0.21 ASN 114 -0.22 LEU 301

PRO 305 0.21 ASP 115 -0.18 LYS 32

PRO 305 0.23 LEU 116 -0.19 LEU 301

PRO 305 0.27 SER 117 -0.21 GLY 108

PRO 305 0.24 MET 118 -0.16 LEU 301

PRO 305 0.20 PRO 119 -0.15 LYS 32

CYS 97 0.26 ARG 120 -0.17 LYS 32

CYS 97 0.26 GLY 121 -0.14 LYS 32

CYS 97 0.32 THR 122 -0.18 LYS 32

CYS 97 0.40 MET 123 -0.24 LYS 32

CYS 97 0.56 GLN 124 -0.23 LYS 32

LYS 99 0.50 ASP 125 -0.39 LYS 32

LYS 99 0.39 GLY 126 -0.25 LYS 32

LYS 99 0.36 THR 127 -0.20 LYS 32

CYS 97 0.30 SER 128 -0.11 LEU 301

CYS 97 0.27 ARG 129 -0.12 ALA 29

CYS 97 0.22 PHE 130 -0.08 LEU 301

LYS 99 0.21 THR 131 -0.06 LEU 301

LYS 99 0.17 CYS 132 -0.10 ARG 133

LYS 99 0.19 ARG 133 -0.16 GLU 24

LYS 99 0.24 GLY 134 -0.12 SER 22

LYS 99 0.22 LYS 135 -0.17 TRP 15

LYS 99 0.24 PRO 136 -0.06 LEU 301

CYS 97 0.20 ILE 137 -0.07 LEU 301

CYS 97 0.22 HIS 138 -0.10 LYS 32

CYS 97 0.22 HIS 139 -0.11 LYS 32

CYS 97 0.17 PHE 140 -0.12 LEU 301

CYS 97 0.18 LEU 141 -0.17 LEU 301

CYS 97 0.25 GLY 142 -0.17 LEU 301

CYS 97 0.15 THR 143 -0.14 LEU 301

CYS 97 0.14 SER 144 -0.11 LEU 301

PRO 305 0.11 THR 145 -0.09 LEU 301

SER 1 0.12 PHE 146 -0.08 LYS 135

SER 1 0.14 SER 147 -0.08 LYS 135

SER 1 0.19 GLN 148 -0.08 GLU 25

THR 2 0.19 TYR 149 -0.08 LEU 301

THR 2 0.13 THR 150 -0.11 LEU 301

CYS 97 0.17 VAL 151 -0.13 LEU 301

CYS 97 0.20 VAL 152 -0.16 LEU 301

GLY 98 0.26 ASP 153 -0.19 LEU 301

PRO 106 0.28 GLU 154 -0.19 LEU 301

PRO 106 0.29 ILE 155 -0.22 LEU 301

PRO 106 0.19 SER 156 -0.20 LEU 301

PRO 106 0.23 VAL 157 -0.17 LEU 301

PRO 106 0.26 ALA 158 -0.16 LEU 301

PRO 106 0.27 LYS 159 -0.14 LEU 301

PRO 106 0.22 ILE 160 -0.12 GLY 98

PRO 106 0.21 ASP 161 -0.11 GLY 98

PRO 106 0.20 ALA 162 -0.09 LEU 301

PRO 106 0.16 ALA 163 -0.09 LYS 8

PRO 106 0.13 SER 164 -0.10 GLY 98

ASN 300 0.12 PRO 165 -0.09 MET 336

ASN 300 0.11 LEU 166 -0.07 LYS 8

ASN 300 0.11 GLU 167 -0.07 LYS 10

ASN 300 0.14 LYS 168 -0.10 GLY 98

ASN 300 0.15 VAL 169 -0.12 GLY 98

ASN 300 0.14 CYS 170 -0.09 GLY 98

ASN 300 0.16 LEU 171 -0.12 GLY 98

ASN 300 0.18 ILE 172 -0.16 GLY 98

ASN 300 0.16 GLY 173 -0.13 LEU 301

ASN 300 0.19 CYS 174 -0.13 LEU 301

ASN 300 0.20 GLY 175 -0.16 GLU 107

ASN 300 0.20 PHE 176 -0.18 GLY 98

ASN 300 0.20 SER 177 -0.22 GLY 98

ASN 300 0.24 THR 178 -0.23 GLU 107

ASN 300 0.24 GLY 179 -0.29 GLU 107

ASN 300 0.21 TYR 180 -0.26 GLY 98

ASN 300 0.21 GLY 181 -0.30 GLY 98

ASN 300 0.25 SER 182 -0.46 GLU 107

ASN 300 0.23 ALA 183 -0.43 PRO 106

ASN 300 0.20 VAL 184 -0.42 PRO 106

ASN 300 0.20 LYS 185 -0.54 PRO 106

ASN 300 0.24 VAL 186 -0.79 GLU 107

ASN 300 0.24 ALA 187 -0.66 GLU 107

ASN 300 0.21 LYS 188 -0.63 PRO 106

ASN 300 0.21 VAL 189 -0.52 PRO 106

ASN 300 0.18 THR 190 -0.47 PRO 106

ASN 300 0.17 GLN 191 -0.38 PRO 106

ASN 300 0.17 GLY 192 -0.36 PRO 106

ASN 300 0.18 SER 193 -0.41 PRO 106

ASN 300 0.19 THR 194 -0.39 PRO 106

ASN 300 0.21 CYS 195 -0.40 PRO 106

ASN 300 0.23 ALA 196 -0.37 GLU 107

ASN 300 0.24 VAL 197 -0.35 GLU 107

THR 274 0.27 PHE 198 -0.33 GLU 107

ASN 300 0.22 GLY 199 -0.29 GLU 107

ASN 300 0.19 LEU 200 -0.25 GLU 107

ASN 300 0.18 GLY 201 -0.23 GLU 107

ASN 300 0.18 GLY 202 -0.20 GLU 107

ASN 300 0.21 VAL 203 -0.25 GLU 107

ASN 300 0.22 GLY 204 -0.28 GLU 107

ASN 300 0.20 LEU 205 -0.22 GLU 107

ASN 300 0.20 SER 206 -0.22 GLU 107

ASN 300 0.23 VAL 207 -0.31 GLU 107

ASN 300 0.21 ILE 208 -0.27 PRO 106

ASN 300 0.19 MET 209 -0.23 PRO 106

ASN 300 0.20 GLY 210 -0.29 PRO 106

ASN 300 0.21 CYS 211 -0.34 PRO 106

ASN 300 0.19 LYS 212 -0.28 PRO 106

ASN 300 0.18 ALA 213 -0.28 GLY 98

ASN 300 0.18 ALA 214 -0.34 PRO 106

ASN 300 0.17 GLY 215 -0.32 PRO 106

ASN 300 0.18 ALA 216 -0.36 PRO 106

ASN 300 0.16 ALA 217 -0.33 PRO 106

ASN 300 0.17 ARG 218 -0.32 PRO 106

ASN 300 0.19 ILE 219 -0.32 PRO 106

ASN 300 0.19 ILE 220 -0.31 PRO 106

THR 274 0.20 GLY 221 -0.28 GLU 107

THR 274 0.30 VAL 222 -0.28 GLU 107

ASP 273 0.34 ASP 223 -0.25 GLU 107

ASP 273 0.39 ILE 224 -0.23 GLU 107

ASP 273 0.30 ASN 225 -0.20 GLU 107

ASP 273 0.26 LYS 226 -0.20 GLU 107

ASP 273 0.22 ASP 227 -0.18 GLU 107

ASP 273 0.21 LYS 228 -0.20 GLU 107

ASP 273 0.20 PHE 229 -0.21 GLU 107

ASP 273 0.16 ALA 230 -0.18 GLU 107

ASN 300 0.16 LYS 231 -0.18 GLU 107

ASN 300 0.17 ALA 232 -0.22 GLU 107

ASN 300 0.16 LYS 233 -0.21 PRO 106

ASN 300 0.15 GLU 234 -0.17 PRO 106

ASN 300 0.17 VAL 235 -0.19 PRO 106

ASN 300 0.17 GLY 236 -0.23 PRO 106

ASN 300 0.18 ALA 237 -0.26 PRO 106

ASN 300 0.16 THR 238 -0.26 PRO 106

ASN 300 0.16 GLU 239 -0.26 PRO 106

ASP 273 0.20 CYS 240 -0.25 PRO 106

ASP 273 0.26 VAL 241 -0.25 PRO 106

ASP 273 0.34 ASN 242 -0.23 GLU 107

ASP 273 0.39 PRO 243 -0.24 GLU 107

ASP 273 0.39 GLN 244 -0.22 GLU 107

LEU 301 0.29 ASP 245 -0.21 GLU 107

LEU 301 0.24 TYR 246 -0.23 PRO 106

LEU 301 0.23 LYS 247 -0.24 PRO 106

SER 302 0.20 LYS 248 -0.29 ASN 304

SER 302 0.25 PRO 249 -0.30 GLU 107

SER 302 0.19 ILE 250 -0.31 GLU 107

SER 302 0.16 GLN 251 -0.34 PRO 106

SER 302 0.15 GLU 252 -0.31 PRO 106

SER 302 0.13 VAL 253 -0.29 PRO 106

ASN 300 0.14 LEU 254 -0.32 PRO 106

ASN 300 0.15 THR 255 -0.34 PRO 106

ASN 300 0.12 GLU 256 -0.30 PRO 106

ASN 300 0.12 MET 257 -0.30 PRO 106

ASN 300 0.15 SER 258 -0.33 PRO 106

ASN 300 0.14 ASN 259 -0.32 PRO 106

ASN 300 0.16 GLY 260 -0.34 PRO 106

ASN 300 0.18 GLY 261 -0.38 PRO 106

ASN 300 0.20 VAL 262 -0.40 PRO 106

ASN 300 0.21 ASP 263 -0.46 PRO 106

ASN 300 0.24 PHE 264 -0.49 PRO 106

ASN 300 0.27 SER 265 -0.44 GLU 107

ASN 300 0.30 PHE 266 -0.44 GLU 107

ASN 300 0.33 GLU 267 -0.41 GLU 107

ASN 300 0.29 VAL 268 -0.36 GLU 107

ASN 300 0.21 ILE 269 -0.31 GLU 107

ASN 300 0.31 GLY 270 -0.37 GLU 107

ILE 224 0.28 ARG 271 -0.39 GLU 107

ILE 224 0.30 LEU 272 -0.46 GLU 107

GLN 244 0.39 ASP 273 -0.40 GLU 107

ASP 223 0.31 THR 274 -0.36 GLU 107

ASN 300 0.42 MET 275 -0.46 GLU 107

ASN 300 0.33 VAL 276 -0.46 GLU 107

ASN 300 0.21 THR 277 -0.38 GLU 107

ASN 300 0.27 ALA 278 -0.41 GLU 107

ASN 300 0.34 LEU 279 -0.44 GLU 107

ASN 300 0.25 SER 280 -0.38 PRO 106

ASN 300 0.21 CYS 281 -0.38 PRO 106

ASN 300 0.23 CYS 282 -0.43 PRO 106

ASN 300 0.21 GLN 283 -0.43 PRO 106

ASN 300 0.23 GLU 284 -0.41 PRO 106

ASN 300 0.20 ALA 285 -0.44 PRO 106

ASN 300 0.21 TYR 286 -0.51 PRO 106

ASN 300 0.24 GLY 287 -0.51 PRO 106

ASN 300 0.26 VAL 288 -0.57 PRO 106

ASN 300 0.33 SER 289 -0.56 GLU 107

ASN 300 0.36 VAL 290 -0.60 GLU 107

ASN 300 0.42 ILE 291 -0.53 GLU 107

ASN 300 0.34 VAL 292 -0.45 GLU 107

ASN 300 0.42 GLY 293 -0.39 GLU 107

ASN 300 0.43 VAL 294 -0.44 GLU 107

ASN 300 0.18 PRO 295 -0.35 GLU 107

ASN 300 0.20 PRO 296 -0.35 GLU 107

PRO 305 0.14 ASP 297 -0.34 GLU 107

ILE 224 0.24 SER 298 -0.42 GLU 107

PRO 305 0.28 GLN 299 -0.26 ASP 273

MET 303 0.46 ASN 300 -0.19 SER 302

GLN 244 0.37 LEU 301 -0.68 GLU 107

GLN 244 0.32 SER 302 -0.52 GLU 107

ASN 300 0.46 MET 303 -0.36 GLU 107

ASN 300 0.43 ASN 304 -0.30 GLU 252

ASN 300 0.45 PRO 305 -0.24 SER 302

ASN 300 0.38 MET 306 -0.26 PRO 106

ASN 300 0.36 LEU 307 -0.33 PRO 106

ASN 300 0.27 LEU 308 -0.40 LEU 301

ASN 300 0.24 LEU 309 -0.35 PRO 106

ASN 300 0.23 SER 310 -0.39 PRO 106

ASN 300 0.21 GLY 311 -0.47 PRO 106

ASN 300 0.24 ARG 312 -0.49 PRO 106

ASN 300 0.25 THR 313 -0.56 PRO 106

ASN 300 0.32 TRP 314 -0.63 LEU 301

ASN 300 0.33 LYS 315 -0.72 GLU 107

ASN 300 0.35 GLY 316 -0.67 GLU 107

ASN 300 0.27 ALA 317 -0.55 GLU 107

ASN 300 0.23 ILE 318 -0.36 LEU 301

ASN 300 0.20 PHE 319 -0.28 LEU 301

ASN 300 0.22 GLY 320 -0.31 GLU 107

PRO 305 0.19 GLY 321 -0.36 LEU 301

ASN 300 0.18 PHE 322 -0.36 GLY 98

GLU 107 0.27 LYS 323 -0.51 GLY 98

ASN 300 0.17 SER 324 -0.37 GLY 98

PRO 106 0.33 LYS 325 -0.31 GLY 98

PRO 106 0.40 ASP 326 -0.45 GLY 98

GLU 107 0.26 SER 327 -0.35 GLY 98

PRO 106 0.17 VAL 328 -0.24 GLY 98

PRO 106 0.24 PRO 329 -0.23 GLY 98

GLU 107 0.24 LYS 330 -0.27 GLY 98

ASN 300 0.18 LEU 331 -0.23 GLY 98

ASN 300 0.16 VAL 332 -0.18 GLY 98

GLU 107 0.19 ALA 333 -0.19 GLY 98

ASN 300 0.18 ASP 334 -0.21 GLY 98

ASN 300 0.17 PHE 335 -0.17 GLY 98

ASN 300 0.15 MET 336 -0.15 GLY 98

ASN 300 0.16 ALA 337 -0.16 GLY 98

ASN 300 0.15 LYS 338 -0.16 GLY 98

ASN 300 0.17 LYS 339 -0.20 GLY 98

ASN 300 0.17 PHE 340 -0.21 GLY 98

ASN 300 0.15 ALA 341 -0.17 GLY 98

ASN 300 0.15 LEU 342 -0.15 GLY 98

ASN 300 0.13 ASP 343 -0.12 GLY 98

ASN 300 0.14 PRO 344 -0.13 GLY 98

ASN 300 0.15 LEU 345 -0.13 GLU 107

ASN 300 0.13 ILE 346 -0.10 GLY 98

ASN 300 0.11 THR 347 -0.11 GLU 107

SER 1 0.11 HIS 348 -0.09 GLU 107

SER 1 0.13 VAL 349 -0.07 GLY 108

SER 1 0.14 LEU 350 -0.07 LYS 135

SER 1 0.16 PRO 351 -0.08 ARG 133

SER 1 0.17 PHE 352 -0.09 LYS 135

SER 1 0.18 GLU 353 -0.09 ARG 133

SER 1 0.15 LYS 354 -0.09 LYS 135

SER 1 0.13 ILE 355 -0.09 LYS 135

SER 1 0.12 ASN 356 -0.10 GLU 107

SER 1 0.12 GLU 357 -0.10 GLU 107

SER 1 0.12 GLY 358 -0.11 GLU 107

SER 1 0.10 PHE 359 -0.13 GLU 107

SER 298 0.11 ASP 360 -0.14 GLU 107

SER 298 0.11 LEU 361 -0.14 GLU 107

SER 298 0.12 LEU 362 -0.17 GLU 107

SER 298 0.15 ARG 363 -0.18 GLU 107

SER 298 0.16 SER 364 -0.18 GLU 107

SER 298 0.17 GLY 365 -0.17 GLU 107

SER 298 0.15 GLU 366 -0.17 GLU 107

SER 298 0.12 SER 367 -0.15 GLU 107

ASN 300 0.14 ILE 368 -0.16 GLU 107

ASN 300 0.13 ARG 369 -0.13 GLU 107

ASN 300 0.11 THR 370 -0.10 GLU 107

SER 1 0.11 ILE 371 -0.07 GLY 108

SER 1 0.13 LEU 372 -0.08 LYS 135

SER 1 0.16 THR 373 -0.08 GLU 25

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.

*** ***

CA distance fluctuations for 2604262204102534339

--- normal mode 16 ---

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

* *