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This graph displays the distance variation between successive pairs of CA atoms
in the two extreme conformations that were computed for this mode (DQMIN/DQMAX).
Large distance variations can be an indicator for residue pairs that support the
important strain in that particular normal mode movement.
Note that residue pairs between chain breaks or at flexible ends of the protein
may also exhibit large CA-CA distance variations.
If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations
between CA atoms in the same block will be very low.
This feature is still experimental and will be further developped in the future.
CA i
CA i+1
vari
SER 1
THR 2
0.0004
THR 2
ALA 3
0.0002
ALA 3
GLY 4
-0.0001
GLY 4
LYS 5
-0.0456
LYS 5
VAL 6
0.0004
VAL 6
ILE 7
0.0002
ILE 7
LYS 8
-0.0005
LYS 8
CYS 9
-0.0415
CYS 9
LYS 10
-0.0001
LYS 10
ALA 11
0.0004
ALA 11
ALA 12
-0.0005
ALA 12
VAL 13
-0.0055
VAL 13
LEU 14
-0.0001
LEU 14
TRP 15
-0.0002
TRP 15
GLU 16
-0.0001
GLU 16
GLU 17
-0.0464
GLU 17
LYS 18
-0.0002
LYS 18
LYS 19
-0.0001
LYS 19
PRO 20
-0.0001
PRO 20
PHE 21
-0.0216
PHE 21
SER 22
0.0000
SER 22
ILE 23
-0.0003
ILE 23
GLU 24
0.0002
GLU 24
GLU 25
-0.1071
GLU 25
VAL 26
0.0001
VAL 26
GLU 27
0.0000
GLU 27
VAL 28
-0.0002
VAL 28
ALA 29
-0.0462
ALA 29
PRO 30
-0.0001
PRO 30
PRO 31
0.0002
PRO 31
LYS 32
-0.0003
LYS 32
ALA 33
-0.0300
ALA 33
HIS 34
0.0003
HIS 34
GLU 35
-0.0000
GLU 35
VAL 36
0.0001
VAL 36
ARG 37
-0.0498
ARG 37
ILE 38
-0.0001
ILE 38
LYS 39
0.0001
LYS 39
MET 40
0.0001
MET 40
VAL 41
-0.0251
VAL 41
ALA 42
-0.0000
ALA 42
THR 43
0.0000
THR 43
GLY 44
0.0001
GLY 44
ILE 45
0.0472
ILE 45
CYS 46
-0.0000
CYS 46
ARG 47
-0.0002
ARG 47
SER 48
0.0001
SER 48
ASP 49
0.0167
ASP 49
ASP 50
0.0003
ASP 50
HIS 51
0.0002
HIS 51
VAL 52
0.0002
VAL 52
VAL 53
-0.0320
VAL 53
SER 54
-0.0003
SER 54
GLY 55
-0.0002
GLY 55
THR 56
0.0001
THR 56
LEU 57
0.0330
LEU 57
VAL 58
0.0000
VAL 58
THR 59
-0.0000
THR 59
PRO 60
0.0002
PRO 60
LEU 61
-0.0324
LEU 61
PRO 62
-0.0005
PRO 62
VAL 63
0.0001
VAL 63
ILE 64
-0.0002
ILE 64
ALA 65
0.0214
ALA 65
GLY 66
0.0004
GLY 66
HIS 67
-0.0003
HIS 67
GLU 68
-0.0000
GLU 68
ALA 69
-0.0605
ALA 69
ALA 70
0.0004
ALA 70
GLY 71
-0.0002
GLY 71
ILE 72
-0.0003
ILE 72
VAL 73
-0.1481
VAL 73
GLU 74
-0.0000
GLU 74
SER 75
-0.0000
SER 75
ILE 76
-0.0002
ILE 76
GLY 77
-0.1464
GLY 77
GLU 78
0.0001
GLU 78
GLY 79
0.0005
GLY 79
VAL 80
0.0001
VAL 80
THR 81
0.0212
THR 81
THR 82
0.0000
THR 82
VAL 83
-0.0002
VAL 83
ARG 84
0.0000
ARG 84
PRO 85
0.0618
PRO 85
GLY 86
-0.0002
GLY 86
ASP 87
-0.0002
ASP 87
LYS 88
0.0003
LYS 88
VAL 89
-0.0273
VAL 89
ILE 90
-0.0002
ILE 90
PRO 91
-0.0002
PRO 91
LEU 92
0.0000
LEU 92
PHE 93
-0.0835
PHE 93
THR 94
0.0001
THR 94
PRO 95
0.0001
PRO 95
GLN 96
0.0001
GLN 96
CYS 97
-0.0644
CYS 97
GLY 98
0.0001
GLY 98
LYS 99
-0.0002
LYS 99
CYS 100
0.0001
CYS 100
ARG 101
-0.0001
ARG 101
VAL 102
-0.0000
VAL 102
CYS 103
0.0002
CYS 103
LYS 104
0.0001
LYS 104
HIS 105
0.1399
HIS 105
PRO 106
-0.0005
PRO 106
GLU 107
-0.0004
GLU 107
GLY 108
0.0001
GLY 108
ASN 109
-0.0334
ASN 109
PHE 110
0.0001
PHE 110
CYS 111
-0.0001
CYS 111
LEU 112
0.0000
LEU 112
LYS 113
-0.1592
LYS 113
ASN 114
0.0001
ASN 114
ASP 115
-0.0002
ASP 115
LEU 116
0.0001
LEU 116
SER 117
-0.0976
SER 117
MET 118
0.0002
MET 118
PRO 119
0.0002
PRO 119
ARG 120
0.0003
ARG 120
GLY 121
-0.0274
GLY 121
THR 122
0.0003
THR 122
MET 123
-0.0001
MET 123
GLN 124
-0.0003
GLN 124
ASP 125
-0.0119
ASP 125
GLY 126
-0.0000
GLY 126
THR 127
-0.0002
THR 127
SER 128
-0.0001
SER 128
ARG 129
0.0638
ARG 129
PHE 130
-0.0002
PHE 130
THR 131
-0.0000
THR 131
CYS 132
0.0002
CYS 132
ARG 133
0.0109
ARG 133
GLY 134
0.0001
GLY 134
LYS 135
-0.0000
LYS 135
PRO 136
-0.0001
PRO 136
ILE 137
-0.0109
ILE 137
HIS 138
-0.0001
HIS 138
HIS 139
0.0002
HIS 139
PHE 140
-0.0003
PHE 140
LEU 141
-0.0593
LEU 141
GLY 142
-0.0001
GLY 142
THR 143
-0.0002
THR 143
SER 144
0.0002
SER 144
THR 145
-0.0117
THR 145
PHE 146
0.0001
PHE 146
SER 147
-0.0000
SER 147
GLN 148
0.0003
GLN 148
TYR 149
-0.0627
TYR 149
THR 150
-0.0001
THR 150
VAL 151
0.0004
VAL 151
VAL 152
-0.0003
VAL 152
ASP 153
0.0230
ASP 153
GLU 154
-0.0001
GLU 154
ILE 155
0.0003
ILE 155
SER 156
-0.0001
SER 156
VAL 157
-0.0452
VAL 157
ALA 158
0.0001
ALA 158
LYS 159
0.0003
LYS 159
ILE 160
-0.0004
ILE 160
ASP 161
-0.0689
ASP 161
ALA 162
-0.0003
ALA 162
ALA 163
-0.0002
ALA 163
SER 164
-0.0001
SER 164
PRO 165
0.0006
PRO 165
LEU 166
0.0001
LEU 166
GLU 167
0.0002
GLU 167
LYS 168
0.0001
LYS 168
VAL 169
0.0219
VAL 169
CYS 170
0.0005
CYS 170
LEU 171
-0.0001
LEU 171
ILE 172
0.0001
ILE 172
GLY 173
0.0225
GLY 173
CYS 174
-0.0000
CYS 174
GLY 175
-0.0000
GLY 175
PHE 176
-0.0001
PHE 176
SER 177
0.0832
SER 177
THR 178
-0.0002
THR 178
GLY 179
-0.0000
GLY 179
TYR 180
0.0002
TYR 180
GLY 181
-0.0124
GLY 181
SER 182
0.0001
SER 182
ALA 183
-0.0001
ALA 183
VAL 184
-0.0001
VAL 184
LYS 185
0.0230
LYS 185
VAL 186
-0.0002
VAL 186
ALA 187
-0.0002
ALA 187
LYS 188
0.0001
LYS 188
VAL 189
-0.0076
VAL 189
THR 190
-0.0004
THR 190
GLN 191
0.0002
GLN 191
GLY 192
-0.0001
GLY 192
SER 193
-0.0065
SER 193
THR 194
0.0001
THR 194
CYS 195
-0.0002
CYS 195
ALA 196
0.0001
ALA 196
VAL 197
0.0071
VAL 197
PHE 198
0.0000
PHE 198
GLY 199
-0.0002
GLY 199
LEU 200
0.0002
LEU 200
GLY 201
0.0692
GLY 201
GLY 202
-0.0000
GLY 202
VAL 203
0.0001
VAL 203
GLY 204
0.0001
GLY 204
LEU 205
0.0736
LEU 205
SER 206
-0.0001
SER 206
VAL 207
-0.0004
VAL 207
ILE 208
0.0001
ILE 208
MET 209
-0.0089
MET 209
GLY 210
-0.0001
GLY 210
CYS 211
0.0004
CYS 211
LYS 212
0.0003
LYS 212
ALA 213
0.0657
ALA 213
ALA 214
0.0002
ALA 214
GLY 215
0.0000
GLY 215
ALA 216
-0.0004
ALA 216
ALA 217
-0.0194
ALA 217
ARG 218
0.0004
ARG 218
ILE 219
-0.0004
ILE 219
ILE 220
0.0003
ILE 220
GLY 221
0.0068
GLY 221
VAL 222
0.0000
VAL 222
ASP 223
0.0003
ASP 223
ILE 224
-0.0001
ILE 224
ASN 225
-0.0218
ASN 225
LYS 226
-0.0001
LYS 226
ASP 227
-0.0001
ASP 227
LYS 228
0.0004
LYS 228
PHE 229
-0.0537
PHE 229
ALA 230
-0.0002
ALA 230
LYS 231
-0.0001
LYS 231
ALA 232
0.0002
ALA 232
LYS 233
0.0234
LYS 233
GLU 234
0.0001
GLU 234
VAL 235
-0.0000
VAL 235
GLY 236
-0.0002
GLY 236
ALA 237
-0.0001
ALA 237
THR 238
-0.0001
THR 238
GLU 239
0.0003
GLU 239
CYS 240
-0.0001
CYS 240
VAL 241
0.0764
VAL 241
ASN 242
-0.0000
ASN 242
PRO 243
-0.0001
PRO 243
GLN 244
-0.0002
GLN 244
ASP 245
-0.0909
ASP 245
TYR 246
0.0001
TYR 246
LYS 247
-0.0002
LYS 247
LYS 248
-0.0001
LYS 248
PRO 249
-0.1413
PRO 249
ILE 250
0.0000
ILE 250
GLN 251
0.0001
GLN 251
GLU 252
-0.0002
GLU 252
VAL 253
-0.0232
VAL 253
LEU 254
0.0002
LEU 254
THR 255
-0.0002
THR 255
GLU 256
-0.0002
GLU 256
MET 257
-0.0426
MET 257
SER 258
0.0003
SER 258
ASN 259
-0.0001
ASN 259
GLY 260
-0.0003
GLY 260
GLY 261
-0.0249
GLY 261
VAL 262
-0.0000
VAL 262
ASP 263
0.0002
ASP 263
PHE 264
-0.0001
PHE 264
SER 265
-0.0366
SER 265
PHE 266
-0.0000
PHE 266
GLU 267
-0.0001
GLU 267
VAL 268
0.0002
VAL 268
ILE 269
0.0500
ILE 269
GLY 270
0.0003
GLY 270
ARG 271
-0.0001
ARG 271
LEU 272
-0.0001
LEU 272
ASP 273
-0.1010
ASP 273
THR 274
0.0003
THR 274
MET 275
0.0001
MET 275
VAL 276
0.0002
VAL 276
THR 277
-0.0265
THR 277
ALA 278
-0.0001
ALA 278
LEU 279
-0.0003
LEU 279
SER 280
-0.0004
SER 280
CYS 281
-0.0551
CYS 281
CYS 282
0.0000
CYS 282
GLN 283
0.0001
GLN 283
GLU 284
0.0001
GLU 284
ALA 285
0.0451
ALA 285
TYR 286
0.0002
TYR 286
GLY 287
-0.0004
GLY 287
VAL 288
0.0000
VAL 288
SER 289
-0.0382
SER 289
VAL 290
0.0003
VAL 290
ILE 291
-0.0004
ILE 291
VAL 292
-0.0001
VAL 292
GLY 293
-0.1218
GLY 293
VAL 294
0.0003
VAL 294
PRO 295
-0.0005
PRO 295
PRO 296
0.0005
PRO 296
ASP 297
0.0613
ASP 297
SER 298
0.0001
SER 298
GLN 299
0.0002
GLN 299
ASN 300
-0.0002
ASN 300
LEU 301
-0.0298
LEU 301
SER 302
0.0000
SER 302
MET 303
-0.0002
MET 303
ASN 304
0.0002
ASN 304
PRO 305
-0.1158
PRO 305
MET 306
-0.0001
MET 306
LEU 307
-0.0001
LEU 307
LEU 308
0.0000
LEU 308
LEU 309
-0.0097
LEU 309
SER 310
-0.0004
SER 310
GLY 311
0.0002
GLY 311
ARG 312
0.0000
ARG 312
THR 313
0.0340
THR 313
TRP 314
0.0002
TRP 314
LYS 315
-0.0003
LYS 315
GLY 316
0.0001
GLY 316
ALA 317
0.1664
ALA 317
ILE 318
-0.0002
ILE 318
PHE 319
-0.0002
PHE 319
GLY 320
0.0000
GLY 320
GLY 321
0.0131
GLY 321
PHE 322
-0.0002
PHE 322
LYS 323
0.0001
LYS 323
SER 324
-0.0003
SER 324
LYS 325
-0.0052
LYS 325
ASP 326
0.0001
ASP 326
SER 327
-0.0000
SER 327
VAL 328
-0.0002
VAL 328
PRO 329
0.0270
PRO 329
LYS 330
0.0004
LYS 330
LEU 331
0.0003
LEU 331
VAL 332
0.0001
VAL 332
ALA 333
0.0620
ALA 333
ASP 334
0.0003
ASP 334
PHE 335
-0.0000
PHE 335
MET 336
0.0001
MET 336
ALA 337
0.0614
ALA 337
LYS 338
-0.0002
LYS 338
LYS 339
-0.0000
LYS 339
PHE 340
-0.0001
PHE 340
ALA 341
-0.1128
ALA 341
LEU 342
-0.0002
LEU 342
ASP 343
0.0000
ASP 343
PRO 344
-0.0001
PRO 344
LEU 345
-0.0049
LEU 345
ILE 346
-0.0000
ILE 346
THR 347
0.0002
THR 347
HIS 348
-0.0001
HIS 348
VAL 349
-0.0987
VAL 349
LEU 350
-0.0001
LEU 350
PRO 351
0.0003
PRO 351
PHE 352
-0.0002
PHE 352
GLU 353
0.0004
GLU 353
LYS 354
-0.0001
LYS 354
ILE 355
0.0001
ILE 355
ASN 356
0.0001
ASN 356
GLU 357
-0.0015
GLU 357
GLY 358
-0.0000
GLY 358
PHE 359
0.0001
PHE 359
ASP 360
0.0002
ASP 360
LEU 361
0.0425
LEU 361
LEU 362
0.0002
LEU 362
ARG 363
-0.0001
ARG 363
SER 364
0.0002
SER 364
GLY 365
-0.0854
GLY 365
GLU 366
0.0000
GLU 366
SER 367
-0.0005
SER 367
ILE 368
0.0002
ILE 368
ARG 369
0.0198
ARG 369
THR 370
0.0000
THR 370
ILE 371
0.0003
ILE 371
LEU 372
0.0001
LEU 372
THR 373
-0.0003
If you find results from this site helpful for your research, please cite one of our papers:
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.