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

* OXIDOREDUCTASE 27-SEP-05 2C29 *

CA distance fluctuations for 2406271141311183625

--- normal mode 8 ---

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 216 0.11 GLU 6 -0.10 LYS 305

ASN 216 0.13 THR 7 -0.08 LYS 305

ASN 216 0.14 VAL 8 -0.08 LYS 305

GLY 282 0.17 CYS 9 -0.06 LYS 305

GLY 282 0.19 VAL 10 -0.06 LYS 305

GLY 282 0.24 THR 11 -0.09 SER 201

PRO 204 0.32 GLY 12 -0.16 PRO 102

PRO 204 0.28 ALA 13 -0.12 PRO 102

PRO 204 0.34 SER 14 -0.18 GLU 98

PRO 204 0.41 GLY 15 -0.36 PRO 87

GLY 15 0.23 PHE 16 -0.37 PRO 87

SER 205 0.17 ILE 17 -0.25 THR 86

SER 205 0.21 GLY 18 -0.21 THR 86

ASN 216 0.21 SER 19 -0.19 PRO 87

ASN 216 0.15 TRP 20 -0.19 PRO 87

ASN 216 0.13 LEU 21 -0.13 THR 86

ASN 216 0.17 VAL 22 -0.09 LYS 305

ILE 198 0.16 MET 23 -0.12 LYS 305

LYS 322 0.14 ARG 24 -0.14 LYS 305

LYS 322 0.12 LEU 25 -0.13 LYS 305

LYS 322 0.15 LEU 26 -0.15 LYS 305

LYS 322 0.19 GLU 27 -0.19 LYS 305

LYS 322 0.15 ARG 28 -0.19 LYS 305

LYS 322 0.14 GLY 29 -0.16 LYS 305

LYS 322 0.12 TYR 30 -0.13 LYS 305

ASN 216 0.15 THR 31 -0.10 LYS 305

ASN 216 0.18 VAL 32 -0.09 LYS 305

ASN 216 0.20 ARG 33 -0.07 LYS 305

ASN 216 0.23 ALA 34 -0.06 LYS 305

ASN 216 0.26 THR 35 -0.05 TRP 20

PRO 204 0.33 VAL 36 -0.07 SER 200

GLY 282 0.36 ARG 37 -0.14 SER 200

ASN 216 0.41 ASP 38 -0.08 ALA 321

ASN 216 0.36 PRO 39 -0.06 ALA 54

ASN 216 0.40 THR 40 -0.09 LEU 49

ASN 216 0.45 ASN 41 -0.10 ASN 97

ASN 216 0.38 VAL 42 -0.13 ASN 97

ASN 216 0.41 LYS 43 -0.21 GLU 98

ASN 216 0.40 LYS 44 -0.18 GLU 98

ASN 216 0.33 VAL 45 -0.12 GLU 98

ASN 216 0.29 LYS 46 -0.14 GLU 98

SER 200 0.26 HIS 47 -0.17 GLU 98

ASN 216 0.24 LEU 48 -0.11 GLU 98

ASN 216 0.24 LEU 49 -0.10 ASP 310

SER 200 0.26 ASP 50 -0.12 ASP 310

SER 200 0.22 LEU 51 -0.14 ASP 310

LYS 322 0.23 PRO 52 -0.15 LYS 305

LYS 322 0.18 LYS 53 -0.14 LYS 305

ASN 216 0.19 ALA 54 -0.12 LYS 305

ASN 216 0.19 GLU 55 -0.11 LYS 305

ASN 216 0.17 THR 56 -0.12 LYS 305

ASN 216 0.17 HIS 57 -0.12 LYS 305

ASN 216 0.20 LEU 58 -0.10 LYS 305

ASN 216 0.22 THR 59 -0.08 LYS 305

ASN 216 0.26 LEU 60 -0.06 LYS 305

ASN 216 0.26 TRP 61 -0.05 LYS 305

GLY 282 0.30 LYS 62 -0.06 ASP 72

GLY 282 0.31 ALA 63 -0.09 SER 200

GLY 282 0.34 ASP 64 -0.18 SER 201

GLY 282 0.31 LEU 65 -0.23 SER 201

GLY 282 0.34 ALA 66 -0.24 SER 201

GLY 282 0.31 ASP 67 -0.18 SER 201

GLY 282 0.28 GLU 68 -0.15 SER 201

GLY 282 0.25 GLY 69 -0.11 SER 201

GLY 282 0.27 SER 70 -0.10 SER 201

GLY 282 0.24 PHE 71 -0.09 SER 201

GLY 282 0.21 ASP 72 -0.07 SER 201

GLY 282 0.21 GLU 73 -0.05 LYS 62

GLY 282 0.21 ALA 74 -0.05 LYS 305

GLY 282 0.18 ILE 75 -0.05 ARG 122

GLY 282 0.16 LYS 76 -0.06 PRO 245

GLY 282 0.14 GLY 77 -0.07 PRO 245

GLY 282 0.13 CYS 78 -0.06 PRO 245

ASN 216 0.11 THR 79 -0.08 PRO 245

GLY 282 0.11 GLY 80 -0.06 TYR 240

GLY 282 0.14 VAL 81 -0.05 LYS 305

GLY 282 0.15 PHE 82 -0.07 SER 201

GLY 282 0.20 HIS 83 -0.13 SER 201

GLY 282 0.23 VAL 84 -0.14 SER 201

GLY 282 0.29 ALA 85 -0.24 GLY 15

GLY 282 0.30 THR 86 -0.38 SER 201

GLY 282 0.36 PRO 87 -0.51 SER 201

GLY 282 0.37 MET 88 -0.52 PRO 203

GLY 282 0.41 ASP 89 -0.60 MET 202

GLY 282 0.47 PHE 90 -0.48 LEU 324

GLY 282 0.51 GLU 91 -0.55 LEU 324

GLY 282 0.46 SER 92 -0.52 LEU 324

GLY 282 0.48 LYS 93 -0.49 GLY 323

GLY 282 0.42 ASP 94 -0.44 GLY 323

GLY 282 0.41 PRO 95 -0.41 SER 201

GLY 282 0.36 GLU 96 -0.38 SER 201

GLY 282 0.34 ASN 97 -0.41 SER 201

GLY 282 0.36 GLU 98 -0.49 SER 201

GLY 282 0.36 VAL 99 -0.44 SER 201

GLY 282 0.33 ILE 100 -0.36 SER 201

GLY 282 0.30 LYS 101 -0.34 SER 201

GLY 282 0.30 PRO 102 -0.36 SER 201

GLY 282 0.29 THR 103 -0.33 SER 201

GLY 282 0.25 ILE 104 -0.27 SER 201

GLY 282 0.25 GLU 105 -0.25 SER 201

GLY 282 0.26 GLY 106 -0.24 SER 201

GLY 282 0.22 MET 107 -0.21 SER 201

GLY 282 0.20 LEU 108 -0.18 SER 201

GLY 282 0.22 GLY 109 -0.17 SER 201

GLY 282 0.20 ILE 110 -0.14 SER 201

GLY 282 0.17 MET 111 -0.12 SER 201

GLY 282 0.17 LYS 112 -0.12 SER 201

GLY 282 0.18 SER 113 -0.09 SER 201

GLY 282 0.15 CYS 114 -0.08 SER 201

GLY 282 0.13 ALA 115 -0.08 ASP 184

GLY 282 0.15 ALA 116 -0.07 ASP 184

GLY 282 0.14 ALA 117 -0.07 ASP 184

GLY 282 0.11 LYS 118 -0.09 ASP 184

GLY 282 0.10 THR 119 -0.08 PRO 245

GLY 282 0.11 VAL 120 -0.07 ARG 122

ILE 183 0.09 ARG 121 -0.09 PRO 245

GLY 282 0.08 ARG 122 -0.08 LYS 118

GLY 282 0.11 LEU 123 -0.07 SER 201

GLY 282 0.11 VAL 124 -0.08 SER 201

GLY 282 0.15 PHE 125 -0.13 SER 201

GLY 282 0.17 THR 126 -0.14 SER 201

GLY 282 0.17 SER 127 -0.17 PRO 203

GLY 282 0.19 SER 128 -0.20 PRO 203

GLY 282 0.15 ALA 129 -0.17 PRO 203

GLY 282 0.23 GLY 130 -0.22 PRO 203

GLY 282 0.18 THR 131 -0.19 PRO 203

LEU 287 0.11 VAL 132 -0.15 LEU 324

LEU 287 0.17 ASN 133 -0.24 SER 221

LEU 287 0.29 ILE 134 -0.24 ALA 218

LEU 287 0.30 GLN 135 -0.29 SER 221

LEU 287 0.38 GLU 136 -0.38 SER 221

ASN 286 0.28 HIS 137 -0.42 SER 221

LEU 287 0.19 GLN 138 -0.39 SER 221

MET 266 0.10 LEU 139 -0.28 SER 221

MET 266 0.15 PRO 140 -0.20 SER 221

HIS 256 0.15 VAL 141 -0.17 SER 221

HIS 256 0.10 TYR 142 -0.19 SER 221

SER 307 0.11 ASP 143 -0.14 SER 221

SER 307 0.08 GLU 144 -0.13 ASP 143

SER 307 0.08 SER 145 -0.13 SER 221

HIS 256 0.07 CYS 146 -0.16 SER 221

LEU 287 0.11 TRP 147 -0.15 LEU 324

LEU 287 0.19 SER 148 -0.18 LEU 324

LEU 287 0.24 ASP 149 -0.19 LEU 324

LEU 287 0.26 MET 150 -0.22 LEU 324

LEU 287 0.30 GLU 151 -0.22 LEU 324

LEU 287 0.36 PHE 152 -0.22 ALA 218

GLY 282 0.38 CYS 153 -0.24 LEU 324

GLY 282 0.41 ARG 154 -0.27 LEU 324

GLY 282 0.45 ALA 155 -0.25 PRO 326

GLY 282 0.54 LYS 156 -0.27 ALA 218

GLY 282 0.59 LYS 157 -0.30 PRO 326

GLY 282 0.66 MET 158 -0.27 PRO 326

GLY 282 0.60 THR 159 -0.33 PRO 326

GLY 282 0.48 ALA 160 -0.35 LEU 324

GLY 282 0.47 TRP 161 -0.31 LEU 324

GLY 282 0.43 MET 162 -0.34 LEU 324

GLY 282 0.38 TYR 163 -0.35 MET 202

GLY 282 0.33 PHE 164 -0.27 PRO 203

GLY 282 0.32 VAL 165 -0.27 LEU 324

GLY 282 0.31 SER 166 -0.30 SER 201

GLY 282 0.26 LYS 167 -0.26 PRO 203

GLY 282 0.22 THR 168 -0.21 PRO 203

GLY 282 0.22 LEU 169 -0.23 SER 201

GLY 282 0.22 ALA 170 -0.23 SER 201

GLY 282 0.17 GLU 171 -0.19 SER 201

GLY 282 0.14 GLN 172 -0.18 SER 201

GLY 282 0.16 ALA 173 -0.19 SER 201

GLY 282 0.15 ALA 174 -0.16 SER 201

GLY 282 0.10 TRP 175 -0.14 SER 201

GLY 282 0.10 LYS 176 -0.15 SER 201

GLY 282 0.12 TYR 177 -0.14 SER 201

GLY 282 0.09 ALA 178 -0.11 SER 201

LYS 246 0.07 LYS 179 -0.11 SER 201

GLY 282 0.07 GLU 180 -0.11 SER 201

ARG 121 0.09 ASN 181 -0.10 SER 201

ARG 121 0.09 ASN 182 -0.10 SER 145

ARG 121 0.09 ILE 183 -0.09 SER 145

LYS 179 0.06 ASP 184 -0.09 LYS 118

GLY 282 0.08 PHE 185 -0.08 SER 201

GLY 282 0.07 ILE 186 -0.08 ASP 143

GLY 282 0.09 THR 187 -0.10 SER 201

GLY 282 0.08 ILE 188 -0.09 SER 201

GLY 282 0.09 ILE 189 -0.12 PRO 203

GLY 282 0.10 PRO 190 -0.10 PRO 203

ASP 38 0.13 THR 191 -0.11 LEU 192

GLY 15 0.18 LEU 192 -0.11 THR 191

GLY 15 0.16 VAL 193 -0.16 ASP 89

GLY 15 0.14 VAL 194 -0.20 ASP 89

GLY 282 0.07 GLY 195 -0.23 ASP 89

THR 318 0.13 PRO 196 -0.26 ASP 89

THR 214 0.13 PHE 197 -0.29 ASP 89

MET 23 0.16 ILE 198 -0.28 PRO 87

ASN 216 0.23 MET 199 -0.35 PRO 87

HIS 47 0.26 SER 200 -0.41 PRO 87

THR 214 0.35 SER 201 -0.54 ASP 89

LYS 43 0.35 MET 202 -0.60 ASP 89

LYS 44 0.32 PRO 203 -0.52 MET 88

GLY 15 0.41 PRO 204 -0.44 ASP 89

GLY 15 0.36 SER 205 -0.27 ALA 160

GLY 15 0.29 LEU 206 -0.32 PHE 90

LYS 44 0.36 ILE 207 -0.34 PHE 90

ASN 41 0.32 THR 208 -0.28 THR 159

GLY 15 0.25 ALA 209 -0.16 THR 159

ASN 41 0.26 LEU 210 -0.22 THR 159

ASN 41 0.34 SER 211 -0.22 THR 159

ASN 41 0.29 PRO 212 -0.18 HIS 137

ASN 41 0.27 ILE 213 -0.19 THR 159

LYS 43 0.36 THR 214 -0.27 THR 159

ASN 41 0.38 GLY 215 -0.24 HIS 137

ASN 41 0.45 ASN 216 -0.28 GLU 136

ASN 41 0.40 GLU 217 -0.33 HIS 137

GLY 282 0.40 ALA 218 -0.35 GLU 136

ASP 38 0.37 HIS 219 -0.30 GLU 136

ASN 41 0.33 TYR 220 -0.32 HIS 137

GLY 282 0.44 SER 221 -0.42 HIS 137

ASP 38 0.29 ILE 222 -0.30 GLN 138

ASP 38 0.25 ILE 223 -0.21 GLN 138

MET 158 0.33 ARG 224 -0.16 GLN 138

MET 158 0.26 GLN 225 -0.17 VAL 290

ASP 38 0.19 GLY 226 -0.12 ILE 223

ASP 38 0.14 GLN 227 -0.11 THR 298

ASP 38 0.12 PHE 228 -0.10 CYS 258

GLY 15 0.08 VAL 229 -0.11 ASN 286

GLY 15 0.07 HIS 230 -0.14 ASP 89

GLY 282 0.08 LEU 231 -0.17 MET 88

ALA 321 0.12 ASP 232 -0.14 PRO 87

ALA 321 0.10 ASP 233 -0.16 ASN 286

ALA 321 0.06 LEU 234 -0.11 ASN 286

ASN 216 0.08 CYS 235 -0.11 PRO 87

ALA 321 0.11 ASN 236 -0.14 ASN 286

ALA 321 0.08 ALA 237 -0.15 ASN 286

GLY 282 0.06 HIS 238 -0.10 ASN 286

ALA 321 0.09 ILE 239 -0.12 ASN 286

ALA 321 0.10 TYR 240 -0.16 ASN 286

ALA 321 0.07 LEU 241 -0.13 ASN 286

ALA 321 0.07 PHE 242 -0.11 ASN 286

ALA 321 0.09 GLU 243 -0.14 ASN 286

ALA 321 0.09 ASN 244 -0.16 ASN 286

ALA 321 0.08 PRO 245 -0.15 ASN 286

LYS 179 0.07 LYS 246 -0.17 ASN 286

LYS 179 0.07 ALA 247 -0.15 ASN 286

LEU 300 0.07 GLU 248 -0.12 VAL 141

LEU 300 0.07 GLY 249 -0.12 ASP 143

ASP 299 0.05 ARG 250 -0.10 ASP 143

TYR 306 0.06 TYR 251 -0.11 CYS 291

SER 307 0.07 ILE 252 -0.10 ASN 286

SER 307 0.07 CYS 253 -0.13 ASN 286

SER 307 0.08 SER 254 -0.15 ASN 286

SER 293 0.14 SER 255 -0.21 ASN 286

CYS 291 0.16 HIS 256 -0.22 CYS 258

MET 266 0.17 ASP 257 -0.21 CYS 258

SER 289 0.17 CYS 258 -0.22 HIS 256

MET 158 0.24 ILE 259 -0.16 THR 298

ASP 38 0.22 ILE 260 -0.14 SER 307

MET 158 0.21 LEU 261 -0.19 SER 307

LYS 156 0.18 ASP 262 -0.24 SER 307

ASP 38 0.15 LEU 263 -0.19 SER 307

ASN 41 0.18 ALA 264 -0.14 SER 307

LYS 288 0.14 LYS 265 -0.18 SER 307

SER 289 0.17 MET 266 -0.17 LYS 265

ASN 41 0.12 LEU 267 -0.10 GLU 91

ASN 41 0.13 ARG 268 -0.08 GLU 91

SER 289 0.15 GLU 269 -0.12 LYS 270

ASP 257 0.15 LYS 270 -0.14 GLU 91

ASP 257 0.10 TYR 271 -0.18 GLU 91

SER 289 0.09 PRO 272 -0.16 GLU 91

SER 201 0.10 GLU 273 -0.22 GLU 91

SER 201 0.16 TYR 274 -0.22 GLU 91

ASN 41 0.22 ASN 275 -0.15 ASN 216

ASN 41 0.23 ILE 276 -0.12 HIS 137

ASN 41 0.25 PRO 277 -0.11 HIS 137

ASN 41 0.22 THR 278 -0.13 SER 307

ASN 41 0.26 GLU 279 -0.12 SER 307

ASN 41 0.30 PHE 280 -0.13 GLN 138

THR 159 0.41 LYS 281 -0.17 HIS 137

MET 158 0.66 GLY 282 -0.18 PRO 140

MET 158 0.53 VAL 283 -0.15 LYS 295

LYS 156 0.47 ASP 284 -0.18 ASP 299

LYS 156 0.38 GLU 285 -0.24 GLU 303

LYS 156 0.45 ASN 286 -0.28 ASP 299

LYS 156 0.48 LEU 287 -0.23 LYS 295

LYS 156 0.31 LYS 288 -0.23 LYS 295

LYS 156 0.24 SER 289 -0.24 LYS 295

LYS 156 0.16 VAL 290 -0.17 LYS 295

HIS 256 0.16 CYS 291 -0.23 LYS 295

HIS 256 0.13 PHE 292 -0.15 SER 221

SER 307 0.14 SER 293 -0.21 CYS 291

SER 307 0.10 SER 294 -0.22 ASN 286

TYR 306 0.10 LYS 295 -0.28 ASN 286

TYR 306 0.08 LYS 296 -0.22 ASN 286

TYR 306 0.08 LEU 297 -0.21 ASN 286

ALA 321 0.08 THR 298 -0.28 ASN 286

ALA 321 0.08 ASP 299 -0.28 ASN 286

ALA 321 0.08 LEU 300 -0.24 ASN 286

ALA 321 0.11 GLY 301 -0.26 ASN 286

ALA 321 0.11 PHE 302 -0.24 ASN 286

ALA 321 0.12 GLU 303 -0.27 ASN 286

ALA 321 0.11 PHE 304 -0.24 ASN 286

ALA 321 0.15 LYS 305 -0.23 ASN 286

GLY 314 0.13 TYR 306 -0.20 ASN 286

SER 293 0.14 SER 307 -0.24 ASP 262

CYS 291 0.14 LEU 308 -0.20 SER 307

CYS 291 0.11 GLU 309 -0.16 ASP 262

SER 307 0.11 ASP 310 -0.15 ASP 89

SER 293 0.08 MET 311 -0.17 ASP 89

ASP 257 0.09 PHE 312 -0.19 ASP 89

LYS 305 0.10 THR 313 -0.21 ASP 89

LYS 305 0.10 THR 313 -0.21 ASP 89

LYS 305 0.14 GLY 314 -0.24 ASP 89

LYS 305 0.08 ALA 315 -0.29 ASP 89

LYS 305 0.09 VAL 316 -0.31 GLU 91

LYS 305 0.14 ASP 317 -0.30 ASP 89

PRO 196 0.13 THR 318 -0.34 ASP 89

PRO 52 0.13 CYS 319 -0.41 ASP 89

PRO 52 0.13 ARG 320 -0.41 GLU 91

GLU 27 0.17 ALA 321 -0.38 SER 92

PRO 52 0.23 LYS 322 -0.44 ASP 89

ASP 50 0.21 GLY 323 -0.52 GLU 91

ASP 50 0.22 LEU 324 -0.55 GLU 91

ASP 50 0.16 LEU 325 -0.50 GLU 91

ASP 50 0.16 PRO 326 -0.48 GLU 91

LYS 305 0.10 PRO 327 -0.39 GLU 91

SER 201 0.11 SER 328 -0.33 GLU 91

ASN 41 0.17 HIS 329 -0.31 GLU 91

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 8 ---

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

* OXIDOREDUCTASE 27-SEP-05 2C29 *