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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
LYS 1
ILE 2
-0.0003
ILE 2
GLU 3
0.0001
GLU 3
GLU 4
-0.0001
GLU 4
GLY 5
0.0604
GLY 5
LYS 6
-0.0000
LYS 6
LEU 7
0.0002
LEU 7
VAL 8
0.0003
VAL 8
ILE 9
-0.0202
ILE 9
TRP 10
-0.0004
TRP 10
ILE 11
0.0001
ILE 11
ASN 12
-0.0002
ASN 12
GLY 13
-0.0189
GLY 13
ASP 14
0.0002
ASP 14
LYS 15
0.0001
LYS 15
GLY 16
0.0000
GLY 16
TYR 17
-0.0201
TYR 17
ASN 18
0.0001
ASN 18
GLY 19
-0.0001
GLY 19
LEU 20
0.0005
LEU 20
ALA 21
0.0233
ALA 21
GLU 22
-0.0002
GLU 22
VAL 23
0.0003
VAL 23
GLY 24
0.0002
GLY 24
LYS 25
0.0670
LYS 25
LYS 26
-0.0003
LYS 26
PHE 27
-0.0000
PHE 27
GLU 28
0.0002
GLU 28
LYS 29
-0.0503
LYS 29
ASP 30
0.0003
ASP 30
THR 31
-0.0003
THR 31
GLY 32
-0.0001
GLY 32
ILE 33
-0.0732
ILE 33
LYS 34
-0.0005
LYS 34
VAL 35
-0.0001
VAL 35
THR 36
-0.0001
THR 36
VAL 37
0.0797
VAL 37
GLU 38
0.0001
GLU 38
HIS 39
0.0001
HIS 39
PRO 40
-0.0003
PRO 40
ASP 41
0.0326
ASP 41
LYS 42
0.0003
LYS 42
LEU 43
0.0002
LEU 43
GLU 44
-0.0001
GLU 44
GLU 45
0.0390
GLU 45
LYS 46
-0.0001
LYS 46
PHE 47
0.0001
PHE 47
PRO 48
-0.0003
PRO 48
GLN 49
0.0071
GLN 49
VAL 50
0.0004
VAL 50
ALA 51
-0.0000
ALA 51
ALA 52
-0.0000
ALA 52
THR 53
0.0313
THR 53
GLY 54
0.0000
GLY 54
ASP 55
0.0003
ASP 55
GLY 56
-0.0002
GLY 56
PRO 57
0.0040
PRO 57
ASP 58
0.0000
ASP 58
ILE 59
0.0004
ILE 59
ILE 60
0.0000
ILE 60
PHE 61
0.0008
PHE 61
TRP 62
0.0001
TRP 62
ALA 63
0.0000
ALA 63
HIS 64
0.0000
HIS 64
ASP 65
-0.1022
ASP 65
ARG 66
-0.0001
ARG 66
PHE 67
-0.0002
PHE 67
GLY 68
-0.0000
GLY 68
GLY 69
0.0114
GLY 69
TYR 70
0.0001
TYR 70
ALA 71
0.0003
ALA 71
GLN 72
0.0002
GLN 72
SER 73
0.0229
SER 73
GLY 74
0.0004
GLY 74
LEU 75
-0.0001
LEU 75
LEU 76
-0.0000
LEU 76
ALA 77
-0.0203
ALA 77
GLU 78
0.0001
GLU 78
ILE 79
-0.0003
ILE 79
THR 80
-0.0001
THR 80
PRO 81
-0.0952
PRO 81
ASP 82
-0.0003
ASP 82
LYS 83
0.0004
LYS 83
ALA 84
-0.0001
ALA 84
PHE 85
-0.3416
PHE 85
GLN 86
-0.0002
GLN 86
ASP 87
-0.0002
ASP 87
LYS 88
-0.0001
LYS 88
LEU 89
-0.2513
LEU 89
TYR 90
-0.0004
TYR 90
PRO 91
-0.0002
PRO 91
PHE 92
0.0002
PHE 92
THR 93
0.0427
THR 93
TRP 94
0.0001
TRP 94
ASP 95
-0.0002
ASP 95
ALA 96
-0.0002
ALA 96
VAL 97
0.0383
VAL 97
ARG 98
-0.0003
ARG 98
TYR 99
-0.0001
TYR 99
ASN 100
-0.0002
ASN 100
GLY 101
-0.0554
GLY 101
LYS 102
-0.0001
LYS 102
LEU 103
0.0001
LEU 103
ILE 104
-0.0003
ILE 104
ALA 105
0.0322
ALA 105
TYR 106
0.0002
TYR 106
PRO 107
-0.0002
PRO 107
ILE 108
0.0002
ILE 108
ALA 109
-0.0125
ALA 109
VAL 110
0.0000
VAL 110
GLU 111
0.0000
GLU 111
ALA 112
-0.0004
ALA 112
LEU 113
0.1024
LEU 113
SER 114
-0.0001
SER 114
LEU 115
0.0001
LEU 115
ILE 116
-0.0003
ILE 116
TYR 117
0.0828
TYR 117
ASN 118
0.0000
ASN 118
LYS 119
-0.0000
LYS 119
ASP 120
-0.0004
ASP 120
LEU 121
0.0055
LEU 121
LEU 122
0.0003
LEU 122
PRO 123
0.0003
PRO 123
ASN 124
-0.0002
ASN 124
PRO 125
0.0139
PRO 125
PRO 126
-0.0005
PRO 126
LYS 127
0.0001
LYS 127
THR 128
0.0000
THR 128
TRP 129
-0.0067
TRP 129
GLU 130
0.0000
GLU 130
GLU 131
-0.0000
GLU 131
ILE 132
0.0003
ILE 132
PRO 133
0.0408
PRO 133
ALA 134
0.0004
ALA 134
LEU 135
-0.0001
LEU 135
ASP 136
0.0003
ASP 136
LYS 137
0.0285
LYS 137
GLU 138
0.0000
GLU 138
LEU 139
-0.0003
LEU 139
LYS 140
-0.0000
LYS 140
ALA 141
0.1365
ALA 141
LYS 142
0.0006
LYS 142
GLY 143
0.0004
GLY 143
LYS 144
-0.0002
LYS 144
SER 145
0.0702
SER 145
ALA 146
-0.0002
ALA 146
LEU 147
-0.0004
LEU 147
MET 148
-0.0002
MET 148
PHE 149
0.0840
PHE 149
ASN 150
0.0002
ASN 150
LEU 151
-0.0002
LEU 151
GLN 152
-0.0000
GLN 152
GLU 153
0.0047
GLU 153
PRO 154
-0.0001
PRO 154
TYR 155
0.0002
TYR 155
PHE 156
0.0004
PHE 156
THR 157
-0.0942
THR 157
TRP 158
-0.0000
TRP 158
PRO 159
0.0001
PRO 159
LEU 160
0.0003
LEU 160
ILE 161
0.0137
ILE 161
ALA 162
0.0003
ALA 162
ALA 163
-0.0001
ALA 163
ASP 164
0.0005
ASP 164
GLY 165
-0.0159
GLY 165
GLY 166
0.0002
GLY 166
TYR 167
0.0002
TYR 167
ALA 168
-0.0002
ALA 168
PHE 169
0.0251
PHE 169
LYS 170
0.0000
LYS 170
TYR 171
-0.0001
TYR 171
GLU 172
-0.0004
GLU 172
ASN 173
0.1308
ASN 173
GLY 174
-0.0002
GLY 174
LYS 175
0.0004
LYS 175
TYR 176
0.0000
TYR 176
ASP 177
0.0048
ASP 177
ILE 178
-0.0003
ILE 178
LYS 179
-0.0002
LYS 179
ASP 180
-0.0003
ASP 180
VAL 181
0.0329
VAL 181
GLY 182
-0.0002
GLY 182
VAL 183
0.0002
VAL 183
ASP 184
0.0001
ASP 184
ASN 185
-0.0124
ASN 185
ALA 186
0.0003
ALA 186
GLY 187
0.0004
GLY 187
ALA 188
0.0003
ALA 188
LYS 189
0.0017
LYS 189
ALA 190
-0.0001
ALA 190
GLY 191
0.0001
GLY 191
LEU 192
-0.0004
LEU 192
THR 193
-0.0583
THR 193
PHE 194
0.0002
PHE 194
LEU 195
-0.0003
LEU 195
VAL 196
0.0001
VAL 196
ASP 197
-0.0478
ASP 197
LEU 198
-0.0000
LEU 198
ILE 199
-0.0003
ILE 199
LYS 200
-0.0000
LYS 200
ASN 201
0.0444
ASN 201
LYS 202
-0.0002
LYS 202
HIS 203
0.0002
HIS 203
MET 204
0.0001
MET 204
ASN 205
0.0768
ASN 205
ALA 206
-0.0004
ALA 206
ASP 207
-0.0001
ASP 207
THR 208
0.0001
THR 208
ASP 209
-0.0449
ASP 209
TYR 210
0.0000
TYR 210
SER 211
0.0003
SER 211
ILE 212
-0.0002
ILE 212
ALA 213
0.0212
ALA 213
GLU 214
-0.0000
GLU 214
ALA 215
-0.0002
ALA 215
ALA 216
0.0001
ALA 216
PHE 217
0.0065
PHE 217
ASN 218
0.0001
ASN 218
LYS 219
-0.0001
LYS 219
GLY 220
-0.0003
GLY 220
GLU 221
0.0586
GLU 221
THR 222
0.0001
THR 222
ALA 223
-0.0003
ALA 223
MET 224
-0.0002
MET 224
THR 225
0.0136
THR 225
ILE 226
-0.0000
ILE 226
ASN 227
0.0001
ASN 227
GLY 228
0.0000
GLY 228
PRO 229
-0.0385
PRO 229
TRP 230
-0.0002
TRP 230
ALA 231
0.0002
ALA 231
TRP 232
0.0003
TRP 232
SER 233
-0.1423
SER 233
ASN 234
0.0002
ASN 234
ILE 235
0.0000
ILE 235
ASP 236
0.0003
ASP 236
THR 237
-0.0064
THR 237
SER 238
-0.0001
SER 238
LYS 239
0.0002
LYS 239
VAL 240
0.0000
VAL 240
ASN 241
-0.0181
ASN 241
TYR 242
-0.0002
TYR 242
GLY 243
-0.0001
GLY 243
VAL 244
-0.0001
VAL 244
THR 245
-0.0099
THR 245
VAL 246
-0.0004
VAL 246
LEU 247
0.0001
LEU 247
PRO 248
-0.0005
PRO 248
THR 249
-0.0078
THR 249
PHE 250
0.0001
PHE 250
LYS 251
0.0001
LYS 251
GLY 252
-0.0000
GLY 252
GLN 253
-0.0376
GLN 253
PRO 254
-0.0001
PRO 254
SER 255
0.0005
SER 255
LYS 256
-0.0003
LYS 256
PRO 257
-0.0075
PRO 257
PHE 258
-0.0006
PHE 258
VAL 259
-0.0000
VAL 259
GLY 260
0.0002
GLY 260
VAL 261
-0.0121
VAL 261
LEU 262
0.0000
LEU 262
SER 263
0.0004
SER 263
ALA 264
-0.0000
ALA 264
GLY 265
0.0334
GLY 265
ILE 266
0.0002
ILE 266
ASN 267
-0.0003
ASN 267
ALA 268
0.0002
ALA 268
ALA 269
0.0173
ALA 269
SER 270
0.0001
SER 270
PRO 271
0.0003
PRO 271
ASN 272
0.0004
ASN 272
LYS 273
-0.0001
LYS 273
GLU 274
0.0002
GLU 274
LEU 275
0.0004
LEU 275
ALA 276
-0.0002
ALA 276
LYS 277
-0.0883
LYS 277
GLU 278
0.0001
GLU 278
PHE 279
0.0002
PHE 279
LEU 280
-0.0000
LEU 280
GLU 281
-0.1020
GLU 281
ASN 282
-0.0001
ASN 282
TYR 283
0.0000
TYR 283
LEU 284
-0.0004
LEU 284
LEU 285
-0.1410
LEU 285
THR 286
0.0002
THR 286
ASP 287
0.0003
ASP 287
GLU 288
-0.0002
GLU 288
GLY 289
0.0427
GLY 289
LEU 290
0.0000
LEU 290
GLU 291
-0.0001
GLU 291
ALA 292
0.0000
ALA 292
VAL 293
-0.0657
VAL 293
ASN 294
0.0003
ASN 294
LYS 295
0.0003
LYS 295
ASP 296
0.0002
ASP 296
LYS 297
-0.0213
LYS 297
PRO 298
0.0000
PRO 298
LEU 299
-0.0001
LEU 299
GLY 300
0.0002
GLY 300
ALA 301
0.0300
ALA 301
VAL 302
0.0001
VAL 302
ALA 303
-0.0000
ALA 303
LEU 304
0.0001
LEU 304
LYS 305
-0.0345
LYS 305
SER 306
0.0000
SER 306
TYR 307
0.0001
TYR 307
GLU 308
0.0001
GLU 308
GLU 309
-0.0499
GLU 309
GLU 310
-0.0001
GLU 310
LEU 311
0.0000
LEU 311
ALA 312
0.0001
ALA 312
LYS 313
-0.0330
LYS 313
ASP 314
-0.0001
ASP 314
PRO 315
0.0000
PRO 315
ARG 316
0.0000
ARG 316
ILE 317
0.0259
ILE 317
ALA 318
-0.0000
ALA 318
ALA 319
0.0004
ALA 319
THR 320
-0.0001
THR 320
MET 321
0.0123
MET 321
GLU 322
-0.0001
GLU 322
ASN 323
0.0002
ASN 323
ALA 324
0.0003
ALA 324
GLN 325
-0.0145
GLN 325
LYS 326
0.0001
LYS 326
GLY 327
-0.0002
GLY 327
GLU 328
-0.0001
GLU 328
ILE 329
-0.0091
ILE 329
MET 330
-0.0001
MET 330
PRO 331
0.0003
PRO 331
ASN 332
-0.0001
ASN 332
ILE 333
0.0573
ILE 333
PRO 334
-0.0000
PRO 334
GLN 335
0.0000
GLN 335
MET 336
0.0002
MET 336
SER 337
0.0354
SER 337
ALA 338
-0.0002
ALA 338
PHE 339
-0.0001
PHE 339
TRP 340
-0.0001
TRP 340
TYR 341
0.0505
TYR 341
ALA 342
0.0000
ALA 342
VAL 343
-0.0000
VAL 343
ARG 344
-0.0004
ARG 344
THR 345
0.0091
THR 345
ALA 346
-0.0000
ALA 346
VAL 347
0.0002
VAL 347
ILE 348
0.0002
ILE 348
ASN 349
-0.0388
ASN 349
ALA 350
0.0001
ALA 350
ALA 351
-0.0003
ALA 351
SER 352
0.0001
SER 352
GLY 353
-0.0441
GLY 353
ARG 354
0.0000
ARG 354
GLN 355
-0.0003
GLN 355
THR 356
0.0002
THR 356
VAL 357
0.0377
VAL 357
ASP 358
0.0003
ASP 358
GLU 359
0.0000
GLU 359
ALA 360
-0.0001
ALA 360
LEU 361
0.0065
LEU 361
LYS 362
0.0002
LYS 362
ASP 363
0.0000
ASP 363
ALA 364
0.0005
ALA 364
GLN 365
0.0109
GLN 365
THR 366
-0.0002
THR 366
ARG 367
0.0003
ARG 367
ILE 368
0.0002
ILE 368
THR 369
-0.0002
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.