Should you encounter any unexpected behaviour,
please let us know.

* OXIDOREDUCTASE 27-SEP-05 2C29 *

CA distance fluctuations for 2406271141311183625

--- normal mode 14 ---

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
ASN 286 0.16 GLU 6 -0.15 LYS 270

ASP 143 0.13 THR 7 -0.17 LYS 270

ASP 143 0.13 VAL 8 -0.18 LYS 270

ARG 250 0.12 CYS 9 -0.22 ASP 317

ILE 188 0.15 VAL 10 -0.23 ASP 317

VAL 36 0.23 THR 11 -0.32 PHE 16

LYS 44 0.29 GLY 12 -0.39 SER 201

LYS 44 0.20 ALA 13 -0.31 ALA 321

LYS 44 0.27 SER 14 -0.43 MET 199

LYS 43 0.29 GLY 15 -0.45 ASP 64

LYS 43 0.32 PHE 16 -0.45 ALA 85

GLY 15 0.29 ILE 17 -0.35 VAL 84

LYS 44 0.23 GLY 18 -0.27 PHE 197

ASN 286 0.14 SER 19 -0.29 PHE 197

ASN 286 0.18 TRP 20 -0.28 GLY 314

ASN 286 0.18 LEU 21 -0.22 LYS 270

ASN 286 0.16 VAL 22 -0.22 GLY 314

ASN 286 0.17 MET 23 -0.24 LYS 270

ASN 286 0.20 ARG 24 -0.24 LYS 270

ASN 286 0.19 LEU 25 -0.21 LYS 270

ASN 286 0.18 LEU 26 -0.20 LYS 270

ASN 286 0.20 GLU 27 -0.21 LYS 270

ASN 286 0.22 ARG 28 -0.19 LYS 270

ASN 286 0.19 GLY 29 -0.17 LYS 270

ASN 286 0.17 TYR 30 -0.17 LYS 270

ASN 286 0.14 THR 31 -0.17 LYS 270

ASN 286 0.13 VAL 32 -0.18 LYS 270

GLU 55 0.12 ARG 33 -0.23 ALA 321

THR 126 0.14 ALA 34 -0.28 ALA 321

THR 11 0.18 THR 35 -0.34 SER 201

ALA 85 0.31 VAL 36 -0.45 SER 201

ASP 38 0.44 ARG 37 -0.60 SER 201

ARG 37 0.44 ASP 38 -0.48 ALA 321

THR 86 0.23 PRO 39 -0.38 ALA 321

PRO 87 0.33 THR 40 -0.37 ALA 321

PRO 87 0.46 ASN 41 -0.47 ALA 321

PRO 204 0.37 VAL 42 -0.45 ALA 321

PRO 204 0.47 LYS 43 -0.58 ALA 321

THR 86 0.36 LYS 44 -0.55 ALA 321

THR 86 0.25 VAL 45 -0.41 ALA 321

PRO 204 0.23 LYS 46 -0.44 ALA 321

SER 200 0.23 HIS 47 -0.38 ALA 321

PRO 204 0.15 LEU 48 -0.30 ASP 317

LYS 62 0.16 LEU 49 -0.27 ASP 317

SER 200 0.28 ASP 50 -0.28 ASP 317

SER 200 0.26 LEU 51 -0.24 LYS 270

SER 200 0.26 PRO 52 -0.20 LYS 270

SER 200 0.16 LYS 53 -0.18 LYS 270

ASN 286 0.13 ALA 54 -0.19 LYS 270

THR 59 0.20 GLU 55 -0.21 VAL 42

ASN 286 0.13 THR 56 -0.21 THR 40

ASN 286 0.14 HIS 57 -0.19 THR 40

GLU 55 0.13 LEU 58 -0.21 THR 40

GLU 55 0.20 THR 59 -0.28 THR 40

GLU 55 0.17 LEU 60 -0.29 ALA 321

GLY 109 0.17 TRP 61 -0.33 ALA 321

GLU 55 0.18 LYS 62 -0.39 SER 201

GLY 109 0.22 ALA 63 -0.48 SER 201

ASP 38 0.31 ASP 64 -0.59 SER 201

GLY 106 0.33 LEU 65 -0.52 GLU 98

GLU 105 0.26 ALA 66 -0.92 GLU 98

GLY 109 0.30 ASP 67 -0.71 GLU 98

GLU 180 0.22 GLU 68 -0.66 GLU 98

GLU 180 0.15 GLY 69 -0.52 GLU 98

GLY 109 0.17 SER 70 -0.47 GLU 98

TRP 61 0.16 PHE 71 -0.37 GLU 98

GLU 55 0.13 ASP 72 -0.37 GLU 98

GLU 55 0.15 GLU 73 -0.34 GLU 98

GLU 55 0.16 ALA 74 -0.29 SER 201

ARG 122 0.14 ILE 75 -0.26 SER 201

PRO 245 0.15 LYS 76 -0.27 GLU 98

PRO 245 0.17 GLY 77 -0.22 GLU 98

PRO 245 0.15 CYS 78 -0.19 GLU 98

PRO 245 0.19 THR 79 -0.16 LYS 270

ASP 143 0.15 GLY 80 -0.18 LYS 270

ARG 250 0.12 VAL 81 -0.21 ILE 17

ASP 38 0.16 PHE 82 -0.24 ILE 17

ASP 38 0.23 HIS 83 -0.30 ILE 17

LYS 44 0.28 VAL 84 -0.35 ILE 17

ASN 41 0.36 ALA 85 -0.45 PHE 16

ASN 41 0.43 THR 86 -0.46 PRO 203

ASN 41 0.46 PRO 87 -0.51 ALA 66

ASN 41 0.39 MET 88 -0.53 PRO 203

ASN 41 0.29 ASP 89 -0.55 MET 202

ALA 218 0.31 PHE 90 -0.51 GLY 323

ALA 218 0.37 GLU 91 -0.56 GLY 323

ALA 218 0.26 SER 92 -0.60 ALA 66

ALA 218 0.25 LYS 93 -0.55 ALA 66

ASN 41 0.18 ASP 94 -0.56 ALA 66

ASN 41 0.24 PRO 95 -0.51 ALA 66

ASN 41 0.27 GLU 96 -0.43 GLU 68

ASN 41 0.30 ASN 97 -0.61 GLU 68

ASN 41 0.31 GLU 98 -0.92 ALA 66

ASN 41 0.35 VAL 99 -0.62 ALA 66

ASN 41 0.33 ILE 100 -0.35 GLU 68

ASN 41 0.34 LYS 101 -0.42 GLU 68

ASN 41 0.39 PRO 102 -0.49 GLU 68

ASN 41 0.37 THR 103 -0.33 PRO 203

ASN 41 0.31 ILE 104 -0.28 PRO 203

ASP 38 0.28 GLU 105 -0.34 GLY 109

LEU 65 0.33 GLY 106 -0.33 SER 201

ASP 38 0.28 MET 107 -0.30 PRO 203

ASP 38 0.25 LEU 108 -0.26 PRO 203

ASP 67 0.30 GLY 109 -0.34 GLU 105

ASP 38 0.22 ILE 110 -0.28 SER 201

ASP 38 0.18 MET 111 -0.24 PRO 203

GLU 68 0.20 LYS 112 -0.26 GLU 98

ASP 184 0.14 SER 113 -0.32 GLU 98

ASP 184 0.19 CYS 114 -0.24 GLU 98

ASP 184 0.23 ALA 115 -0.23 GLU 98

ASP 184 0.21 ALA 116 -0.30 GLU 98

ASP 184 0.19 ALA 117 -0.27 GLU 98

ASP 184 0.27 LYS 118 -0.23 GLU 98

PRO 245 0.23 THR 119 -0.20 GLU 98

ARG 122 0.19 VAL 120 -0.18 GLU 98

PRO 245 0.26 ARG 121 -0.25 ILE 183

LYS 118 0.22 ARG 122 -0.24 ILE 183

ASP 38 0.15 LEU 123 -0.20 LYS 270

ASP 38 0.17 VAL 124 -0.21 LYS 270

ASN 41 0.21 PHE 125 -0.23 GLY 195

ASN 41 0.26 THR 126 -0.24 GLY 195

ASN 41 0.26 SER 127 -0.25 VAL 193

ASN 41 0.27 SER 128 -0.27 VAL 193

ASN 41 0.24 ALA 129 -0.25 LEU 192

ASN 41 0.23 GLY 130 -0.28 SER 205

ASN 41 0.23 THR 131 -0.23 LEU 324

ASN 41 0.21 VAL 132 -0.19 LEU 324

LYS 156 0.23 ASN 133 -0.22 LEU 287

LYS 156 0.23 ILE 134 -0.31 LEU 287

LYS 156 0.23 GLN 135 -0.42 LEU 287

SER 145 0.25 GLU 136 -0.65 LEU 287

LYS 295 0.22 HIS 137 -0.60 LEU 287

LYS 295 0.20 GLN 138 -0.35 LEU 287

LYS 295 0.28 LEU 139 -0.18 GLU 285

LYS 295 0.28 PRO 140 -0.14 THR 278

LYS 295 0.36 VAL 141 -0.19 LYS 265

LYS 295 0.31 TYR 142 -0.19 LYS 265

LYS 296 0.33 ASP 143 -0.20 LYS 265

CYS 146 0.26 GLU 144 -0.19 MET 266

GLU 136 0.25 SER 145 -0.17 MET 266

GLU 144 0.26 CYS 146 -0.17 CYS 258

SER 148 0.33 TRP 147 -0.19 LEU 324

TRP 147 0.33 SER 148 -0.26 LEU 287

TRP 147 0.28 ASP 149 -0.34 LEU 287

LYS 176 0.21 MET 150 -0.31 LEU 287

LYS 179 0.23 GLU 151 -0.36 ASN 286

TRP 147 0.23 PHE 152 -0.40 LEU 287

TRP 147 0.21 CYS 153 -0.35 LEU 324

ASN 41 0.16 ARG 154 -0.35 GLY 323

TRP 147 0.17 ALA 155 -0.35 GLY 323

ILE 134 0.23 LYS 156 -0.38 GLY 323

ASN 133 0.21 LYS 157 -0.41 GLY 323

ASN 133 0.20 MET 158 -0.41 LEU 324

ASN 133 0.18 THR 159 -0.49 LEU 324

ASN 41 0.20 ALA 160 -0.46 LEU 324

ASN 41 0.20 TRP 161 -0.40 LEU 324

ASN 41 0.24 MET 162 -0.39 GLY 323

ASN 41 0.28 TYR 163 -0.38 MET 202

ASN 41 0.26 PHE 164 -0.32 LEU 324

ASN 41 0.26 VAL 165 -0.30 GLY 323

ASN 41 0.31 SER 166 -0.30 PRO 203

ASN 41 0.30 LYS 167 -0.30 PRO 203

ASN 41 0.26 THR 168 -0.24 PRO 203

ASN 41 0.27 LEU 169 -0.24 GLY 323

ASN 41 0.29 ALA 170 -0.25 PRO 203

ASN 41 0.26 GLU 171 -0.22 PRO 203

ASN 41 0.23 GLN 172 -0.20 PRO 203

ASN 41 0.24 ALA 173 -0.20 PRO 203

ASP 38 0.23 ALA 174 -0.22 PRO 203

ASP 38 0.20 TRP 175 -0.22 LYS 176

GLU 151 0.22 LYS 176 -0.22 TRP 175

ASP 67 0.22 TYR 177 -0.19 PRO 203

ASP 67 0.16 ALA 178 -0.19 PRO 203

GLU 151 0.23 LYS 179 -0.25 GLU 248

ASP 67 0.22 GLU 180 -0.21 ASP 184

GLU 68 0.20 ASN 181 -0.25 ARG 121

ASP 149 0.18 ASN 182 -0.24 ARG 121

ALA 115 0.22 ILE 183 -0.25 ARG 121

LYS 118 0.27 ASP 184 -0.23 LYS 179

LYS 118 0.18 PHE 185 -0.21 LYS 179

ASP 38 0.17 ILE 186 -0.22 LYS 179

ASN 41 0.20 THR 187 -0.21 LYS 270

LYS 44 0.21 ILE 188 -0.22 LYS 270

ASN 41 0.23 ILE 189 -0.21 LYS 270

LYS 43 0.24 PRO 190 -0.22 LYS 270

LYS 43 0.24 THR 191 -0.20 MET 266

LYS 43 0.24 LEU 192 -0.26 SER 128

LYS 43 0.22 VAL 193 -0.27 SER 128

ASN 286 0.23 VAL 194 -0.28 ALA 66

ASN 286 0.27 GLY 195 -0.32 ASP 64

ASN 286 0.23 PRO 196 -0.39 GLY 314

ASN 286 0.19 PHE 197 -0.38 ASP 64

PRO 52 0.22 ILE 198 -0.41 ASP 317

PRO 52 0.19 MET 199 -0.43 SER 14

ASP 50 0.28 SER 200 -0.51 ARG 37

ASP 50 0.21 SER 201 -0.60 ARG 37

LYS 43 0.28 MET 202 -0.55 ASP 89

LYS 43 0.38 PRO 203 -0.53 MET 88

LYS 43 0.47 PRO 204 -0.42 ALA 160

LYS 43 0.36 SER 205 -0.34 ALA 160

LYS 43 0.25 LEU 206 -0.33 ALA 66

LYS 43 0.30 ILE 207 -0.44 LEU 324

LYS 43 0.26 THR 208 -0.34 LEU 324

LYS 43 0.20 ALA 209 -0.28 GLU 136

LYS 43 0.17 LEU 210 -0.28 GLU 136

LYS 43 0.22 SER 211 -0.38 GLY 282

LYS 43 0.18 PRO 212 -0.32 GLY 282

MET 202 0.19 ILE 213 -0.29 GLY 282

LYS 43 0.21 THR 214 -0.42 PRO 326

LYS 43 0.23 GLY 215 -0.48 GLY 282

LYS 43 0.24 ASN 216 -0.50 GLY 282

GLU 91 0.29 GLU 217 -0.67 GLY 282

GLU 91 0.37 ALA 218 -0.63 GLY 282

LYS 43 0.24 HIS 219 -0.48 GLY 282

LYS 43 0.19 TYR 220 -0.48 GLY 282

LYS 281 0.20 SER 221 -0.45 GLU 136

LYS 43 0.19 ILE 222 -0.38 GLU 136

LYS 43 0.18 ILE 223 -0.35 GLU 136

LYS 281 0.26 ARG 224 -0.39 GLU 136

LYS 281 0.18 GLN 225 -0.38 GLU 136

LYS 43 0.17 GLY 226 -0.26 GLU 136

ASN 286 0.21 GLN 227 -0.24 LYS 265

ASN 286 0.27 PHE 228 -0.25 MET 266

ASN 286 0.28 VAL 229 -0.27 LYS 270

ASN 286 0.31 HIS 230 -0.29 LYS 270

ASN 286 0.24 LEU 231 -0.25 LYS 270

ASN 286 0.27 ASP 232 -0.30 LYS 270

ASN 286 0.30 ASP 233 -0.29 LYS 270

ASN 286 0.24 LEU 234 -0.25 LYS 270

ASN 286 0.21 CYS 235 -0.25 LYS 270

ASN 286 0.25 ASN 236 -0.26 LYS 270

ASN 286 0.24 ALA 237 -0.24 LYS 270

ASN 286 0.19 HIS 238 -0.22 LYS 270

ASN 286 0.20 ILE 239 -0.22 LYS 270

ASN 286 0.22 TYR 240 -0.23 LYS 270

PHE 242 0.23 LEU 241 -0.21 LYS 270

LEU 241 0.23 PHE 242 -0.19 LYS 270

ASN 286 0.20 GLU 243 -0.18 LYS 270

ASN 286 0.20 ASN 244 -0.20 LYS 270

ARG 121 0.26 PRO 245 -0.20 LYS 179

LYS 118 0.23 LYS 246 -0.19 LYS 179

ASP 143 0.22 ALA 247 -0.22 LYS 179

LYS 118 0.21 GLU 248 -0.25 LYS 179

CYS 146 0.23 GLY 249 -0.23 LYS 179

ASN 41 0.19 ARG 250 -0.19 LYS 270

ASP 143 0.20 TYR 251 -0.22 GLU 269

ASN 41 0.20 ILE 252 -0.21 GLU 269

ASN 286 0.20 CYS 253 -0.24 GLU 269

ASN 286 0.25 SER 254 -0.25 GLU 269

ASN 286 0.37 SER 255 -0.31 GLU 269

ASN 286 0.42 HIS 256 -0.34 LYS 265

ASN 286 0.40 ASP 257 -0.33 LYS 265

ASN 286 0.41 CYS 258 -0.26 VAL 290

ASN 286 0.25 ILE 259 -0.33 GLU 136

LYS 43 0.15 ILE 260 -0.32 GLU 136

LYS 265 0.25 LEU 261 -0.29 GLU 136

GLU 285 0.48 ASP 262 -0.32 THR 278

ASN 286 0.31 LEU 263 -0.31 ASP 257

GLU 285 0.21 ALA 264 -0.24 ASP 257

GLU 285 0.42 LYS 265 -0.34 HIS 256

GLU 285 0.48 MET 266 -0.33 HIS 256

GLU 285 0.31 LEU 267 -0.27 GLU 309

GLU 285 0.27 ARG 268 -0.31 GLU 309

GLU 285 0.40 GLU 269 -0.45 GLU 309

ASN 286 0.39 LYS 270 -0.50 GLU 309

ASN 286 0.26 TYR 271 -0.32 PRO 272

GLU 285 0.24 PRO 272 -0.32 TYR 271

ASN 286 0.14 GLU 273 -0.24 ASP 310

MET 202 0.16 TYR 274 -0.22 GLU 136

MET 202 0.19 ASN 275 -0.24 LYS 281

GLU 91 0.15 ILE 276 -0.22 GLU 136

GLU 91 0.21 PRO 277 -0.23 ASP 262

GLU 91 0.19 THR 278 -0.32 ASP 262

PHE 280 0.24 GLU 279 -0.25 GLU 285

GLU 279 0.24 PHE 280 -0.34 ASP 284

ARG 224 0.26 LYS 281 -0.38 ASP 284

GLU 279 0.18 GLY 282 -0.67 GLU 217

LYS 265 0.25 VAL 283 -0.46 GLU 136

LYS 265 0.28 ASP 284 -0.49 GLU 136

MET 266 0.48 GLU 285 -0.46 GLU 136

GLU 309 0.52 ASN 286 -0.58 GLU 136

LEU 308 0.35 LEU 287 -0.65 GLU 136

GLU 303 0.21 LYS 288 -0.32 GLU 136

ASP 257 0.32 SER 289 -0.27 GLU 136

GLU 303 0.17 VAL 290 -0.26 CYS 258

GLU 303 0.21 CYS 291 -0.24 LYS 265

LYS 43 0.19 PHE 292 -0.22 LYS 265

SER 294 0.29 SER 293 -0.23 LYS 265

SER 293 0.29 SER 294 -0.25 GLU 269

VAL 141 0.36 LYS 295 -0.24 GLU 269

ASP 143 0.33 LYS 296 -0.22 GLU 269

ASP 143 0.25 LEU 297 -0.24 GLU 269

ASN 286 0.31 THR 298 -0.26 GLU 269

ASN 286 0.28 ASP 299 -0.23 GLU 269

ASN 286 0.25 LEU 300 -0.22 GLU 269

ASN 286 0.30 GLY 301 -0.24 GLU 269

ASN 286 0.31 PHE 302 -0.25 GLU 269

ASN 286 0.37 GLU 303 -0.29 GLU 269

ASN 286 0.39 PHE 304 -0.32 GLU 269

ASN 286 0.42 LYS 305 -0.35 GLU 269

ASN 286 0.44 TYR 306 -0.36 LYS 270

ASN 286 0.51 SER 307 -0.42 GLU 269

ASN 286 0.52 LEU 308 -0.36 GLU 269

ASN 286 0.52 GLU 309 -0.50 LYS 270

ASN 286 0.44 ASP 310 -0.47 LYS 270

ASN 286 0.36 MET 311 -0.33 LYS 270

ASN 286 0.35 PHE 312 -0.28 ASP 64

ASN 286 0.38 THR 313 -0.30 ASP 64

ASN 286 0.37 THR 313 -0.30 ASP 64

ASN 286 0.32 GLY 314 -0.39 PRO 196

ASN 286 0.24 ALA 315 -0.35 ASP 64

ASN 286 0.22 VAL 316 -0.34 ASP 64

ASN 286 0.26 ASP 317 -0.41 ILE 198

ASN 286 0.20 THR 318 -0.40 ARG 37

ASN 286 0.12 CYS 319 -0.41 ASP 64

GLY 323 0.17 ARG 320 -0.40 ARG 37

ASP 317 0.20 ALA 321 -0.58 LYS 43

PRO 52 0.21 LYS 322 -0.48 ARG 37

PRO 52 0.19 GLY 323 -0.56 GLU 91

PRO 52 0.18 LEU 324 -0.52 GLU 91

TYR 271 0.14 LEU 325 -0.45 ASN 216

TYR 271 0.12 PRO 326 -0.42 THR 214

TYR 271 0.17 PRO 327 -0.32 ASP 64

GLU 273 0.12 SER 328 -0.23 ASP 64

MET 202 0.20 HIS 329 -0.29 LYS 281

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).
Last modification: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** OXIDOREDUCTASE 27-SEP-05 2C29 ***

CA distance fluctuations for 2406271141311183625

--- normal mode 14 ---

Should you encounter any unexpected behaviour,
please let us know.

* OXIDOREDUCTASE 27-SEP-05 2C29 *