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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
MET 1
ARG 2
-0.0001
ARG 2
VAL 3
-0.0100
VAL 3
VAL 4
0.0000
VAL 4
LEU 5
-0.0222
LEU 5
SER 6
0.0000
SER 6
GLY 7
0.0079
GLY 7
GLY 8
0.0001
GLY 8
GLY 9
0.0613
GLY 9
THR 10
0.0000
THR 10
GLY 11
-0.0443
GLY 11
GLY 12
-0.0004
GLY 12
HIS 13
-0.0176
HIS 13
VAL 14
0.0001
VAL 14
TYR 15
-0.0530
TYR 15
PRO 16
-0.0001
PRO 16
ALA 17
-0.0425
ALA 17
LEU 18
0.0002
LEU 18
ALA 19
-0.0475
ALA 19
VAL 20
-0.0002
VAL 20
ALA 21
-0.0062
ALA 21
GLU 22
-0.0003
GLU 22
GLN 23
-0.0051
GLN 23
CYS 24
0.0002
CYS 24
LEU 25
0.0045
LEU 25
GLN 26
0.0002
GLN 26
VAL 27
-0.0101
VAL 27
ASP 28
-0.0001
ASP 28
THR 29
-0.0042
THR 29
ASP 30
0.0002
ASP 30
SER 31
0.0049
SER 31
GLN 32
-0.0004
GLN 32
PHE 33
0.0173
PHE 33
LEU 34
-0.0000
LEU 34
TYR 35
-0.0012
TYR 35
ILE 36
-0.0001
ILE 36
GLY 37
0.0154
GLY 37
THR 38
0.0002
THR 38
ASN 39
0.0108
ASN 39
SER 40
-0.0000
SER 40
GLY 41
-0.0399
GLY 41
LEU 42
-0.0001
LEU 42
GLU 43
0.0578
GLU 43
ARG 44
-0.0001
ARG 44
ASP 45
-0.0019
ASP 45
ILE 46
0.0002
ILE 46
VAL 47
0.0069
VAL 47
GLU 48
-0.0002
GLU 48
LYS 49
0.0105
LYS 49
SER 50
-0.0001
SER 50
LYS 51
0.0025
LYS 51
LEU 52
0.0001
LEU 52
GLU 53
-0.0083
GLU 53
MET 54
-0.0001
MET 54
PRO 55
0.0079
PRO 55
PHE 56
-0.0000
PHE 56
GLU 57
0.0147
GLU 57
ALA 58
-0.0001
ALA 58
ILE 59
0.0312
ILE 59
ASP 60
-0.0002
ASP 60
ILE 61
0.0304
ILE 61
ARG 62
0.0002
ARG 62
GLY 63
0.0730
GLY 63
PHE 64
-0.0001
PHE 64
ARG 65
0.0097
ARG 65
ARG 66
-0.0003
ARG 66
LYS 67
-0.2096
LYS 67
LEU 68
0.0001
LEU 68
VAL 69
-0.0364
VAL 69
SER 70
-0.0003
SER 70
LEU 71
-0.0593
LEU 71
ASP 72
-0.0000
ASP 72
ASN 73
0.0168
ASN 73
ILE 74
0.0001
ILE 74
LYS 75
-0.0323
LYS 75
THR 76
-0.0002
THR 76
VAL 77
-0.0245
VAL 77
MET 78
0.0003
MET 78
LYS 79
-0.0733
LYS 79
PHE 80
0.0003
PHE 80
LEU 81
-0.0336
LEU 81
LYS 82
0.0001
LYS 82
GLY 83
-0.0263
GLY 83
VAL 84
-0.0004
VAL 84
ASN 85
-0.0438
ASN 85
ARG 86
0.0003
ARG 86
SER 87
-0.0129
SER 87
LYS 88
0.0000
LYS 88
GLU 89
-0.0305
GLU 89
LEU 90
-0.0001
LEU 90
LEU 91
0.0018
LEU 91
ARG 92
-0.0000
ARG 92
ASN 93
-0.0100
ASN 93
PHE 94
-0.0000
PHE 94
LYS 95
-0.0056
LYS 95
PRO 96
0.0001
PRO 96
ASP 97
0.0272
ASP 97
ILE 98
-0.0002
ILE 98
VAL 99
0.0036
VAL 99
ILE 100
0.0002
ILE 100
GLY 101
-0.0143
GLY 101
THR 102
-0.0002
THR 102
GLY 103
-0.0569
GLY 103
GLY 104
-0.0003
GLY 104
TYR 105
-0.1479
TYR 105
VAL 106
0.0000
VAL 106
CYS 107
-0.0049
CYS 107
GLY 108
0.0002
GLY 108
PRO 109
-0.0443
PRO 109
VAL 110
0.0001
VAL 110
LEU 111
0.0013
LEU 111
TYR 112
-0.0001
TYR 112
ALA 113
-0.0225
ALA 113
ALA 114
0.0001
ALA 114
ALA 115
0.0013
ALA 115
LYS 116
0.0002
LYS 116
LEU 117
-0.0140
LEU 117
GLY 118
-0.0002
GLY 118
VAL 119
-0.0234
VAL 119
PRO 120
-0.0003
PRO 120
THR 121
0.0099
THR 121
LEU 122
-0.0003
LEU 122
ILE 123
0.0002
ILE 123
HIS 124
-0.0002
HIS 124
GLU 125
0.0269
GLU 125
GLN 126
0.0001
GLN 126
ASN 127
0.0098
ASN 127
ALA 128
-0.0003
ALA 128
ILE 129
-0.0458
ILE 129
ALA 130
-0.0004
ALA 130
GLY 131
-0.0462
GLY 131
LEU 132
0.0004
LEU 132
THR 133
0.0333
THR 133
ASN 134
0.0001
ASN 134
LYS 135
0.0095
LYS 135
PHE 136
-0.0001
PHE 136
LEU 137
0.0062
LEU 137
SER 138
-0.0002
SER 138
ARG 139
-0.0003
ARG 139
TYR 140
0.0002
TYR 140
ALA 141
-0.0107
ALA 141
ASN 142
0.0001
ASN 142
SER 143
0.0197
SER 143
VAL 144
-0.0003
VAL 144
LEU 145
-0.0067
LEU 145
VAL 146
-0.0000
VAL 146
SER 147
0.0271
SER 147
PHE 148
0.0003
PHE 148
LYS 149
0.0050
LYS 149
GLY 150
0.0001
GLY 150
THR 151
-0.0451
THR 151
GLU 152
-0.0002
GLU 152
SER 153
-0.0060
SER 153
ILE 154
-0.0001
ILE 154
PHE 155
0.0213
PHE 155
SER 156
-0.0003
SER 156
LYS 157
-0.0088
LYS 157
ALA 158
0.0001
ALA 158
GLY 159
0.0015
GLY 159
SER 160
-0.0003
SER 160
HIS 161
-0.0098
HIS 161
VAL 162
0.0003
VAL 162
LEU 163
-0.0279
LEU 163
TYR 164
-0.0000
TYR 164
SER 165
-0.0069
SER 165
GLY 166
0.0001
GLY 166
ASN 167
-0.0008
ASN 167
PRO 168
0.0001
PRO 168
ARG 169
0.0011
ARG 169
ALA 170
-0.0002
ALA 170
THR 171
-0.0012
THR 171
SER 172
-0.0002
SER 172
VAL 173
-0.0685
VAL 173
VAL 174
0.0002
VAL 174
ASN 175
0.0360
ASN 175
ALA 176
-0.0003
ALA 176
ASP 177
-0.0683
ASP 177
PRO 178
-0.0002
PRO 178
GLU 179
-0.0019
GLU 179
GLU 180
-0.0001
GLU 180
GLY 181
0.0044
GLY 181
TYR 182
-0.0001
TYR 182
GLN 183
0.0399
GLN 183
SER 184
-0.0001
SER 184
LEU 185
-0.0124
LEU 185
GLY 186
0.0001
GLY 186
ILE 187
0.0252
ILE 187
ARG 188
-0.0002
ARG 188
PRO 189
-0.0235
PRO 189
GLY 190
0.0001
GLY 190
THR 191
-0.0070
THR 191
GLN 192
-0.0002
GLN 192
ILE 193
0.0008
ILE 193
VAL 194
-0.0000
VAL 194
LEU 195
0.0004
LEU 195
VAL 196
0.0003
VAL 196
VAL 197
-0.0044
VAL 197
GLY 198
0.0001
GLY 198
GLY 199
-0.0189
GLY 199
SER 200
0.0001
SER 200
ARG 201
-0.0222
ARG 201
GLY 202
-0.0005
GLY 202
ALA 203
-0.0566
ALA 203
LYS 204
-0.0002
LYS 204
ALA 205
-0.0447
ALA 205
ILE 206
-0.0002
ILE 206
ASN 207
0.0245
ASN 207
ARG 208
-0.0004
ARG 208
ALA 209
-0.0284
ALA 209
MET 210
0.0002
MET 210
ILE 211
0.0038
ILE 211
GLU 212
-0.0001
GLU 212
MET 213
-0.0098
MET 213
ALA 214
0.0000
ALA 214
SER 215
0.0062
SER 215
LEU 216
0.0001
LEU 216
VAL 217
0.0019
VAL 217
ASN 218
0.0003
ASN 218
LYS 219
-0.0383
LYS 219
LEU 220
-0.0001
LEU 220
SER 221
-0.0072
SER 221
ASP 222
0.0002
ASP 222
ILE 223
-0.0032
ILE 223
GLN 224
-0.0004
GLN 224
PHE 225
0.0055
PHE 225
ILE 226
0.0000
ILE 226
PHE 227
-0.0301
PHE 227
VAL 228
0.0000
VAL 228
THR 229
-0.0002
THR 229
GLY 230
0.0002
GLY 230
ALA 231
0.0027
ALA 231
PRO 232
-0.0001
PRO 232
TYR 233
-0.0019
TYR 233
TYR 234
0.0002
TYR 234
GLU 235
0.0208
GLU 235
GLU 236
-0.0002
GLU 236
THR 237
-0.0221
THR 237
ARG 238
0.0000
ARG 238
ASP 239
0.0033
ASP 239
ALA 240
-0.0001
ALA 240
ILE 241
-0.0148
ILE 241
SER 242
0.0001
SER 242
ALA 243
-0.0044
ALA 243
PHE 244
-0.0002
PHE 244
SER 245
-0.0049
SER 245
PRO 246
0.0001
PRO 246
ASP 247
-0.0077
ASP 247
ILE 248
-0.0001
ILE 248
PRO 249
-0.0005
PRO 249
ASN 250
-0.0002
ASN 250
LEU 251
0.0077
LEU 251
ALA 252
-0.0001
ALA 252
VAL 253
-0.0141
VAL 253
LEU 254
-0.0002
LEU 254
PRO 255
-0.0145
PRO 255
TYR 256
0.0003
TYR 256
VAL 257
0.0099
VAL 257
HIS 258
-0.0000
HIS 258
ASN 259
0.0101
ASN 259
MET 260
-0.0001
MET 260
PRO 261
0.0798
PRO 261
GLU 262
0.0003
GLU 262
VAL 263
-0.0032
VAL 263
LEU 264
-0.0001
LEU 264
ALA 265
0.0034
ALA 265
ALA 266
-0.0002
ALA 266
THR 267
0.0262
THR 267
SER 268
-0.0002
SER 268
LEU 269
0.0330
LEU 269
ILE 270
0.0001
ILE 270
VAL 271
-0.0022
VAL 271
ILE 272
-0.0005
ILE 272
ASN 273
-0.0085
ASN 273
ARG 274
-0.0005
ARG 274
ALA 275
0.1506
ALA 275
GLY 276
-0.0002
GLY 276
ALA 277
0.1205
ALA 277
SER 278
-0.0004
SER 278
THR 279
0.0039
THR 279
ILE 280
-0.0000
ILE 280
ALA 281
0.0448
ALA 281
GLU 282
-0.0002
GLU 282
LEU 283
-0.0375
LEU 283
THR 284
0.0002
THR 284
ALA 285
0.0167
ALA 285
LEU 286
0.0001
LEU 286
GLY 287
0.0242
GLY 287
LEU 288
0.0001
LEU 288
PRO 289
-0.0129
PRO 289
SER 290
-0.0001
SER 290
ILE 291
-0.0063
ILE 291
LEU 292
-0.0001
LEU 292
ILE 293
0.0044
ILE 293
PRO 294
-0.0001
PRO 294
SER 295
-0.0218
SER 295
PRO 296
0.0001
PRO 296
ASN 297
-0.0017
ASN 297
VAL 298
0.0001
VAL 298
THR 299
0.0577
THR 299
GLY 300
-0.0000
GLY 300
ASN 301
-0.0923
ASN 301
HIS 302
0.0001
HIS 302
GLN 303
0.0275
GLN 303
GLU 304
0.0000
GLU 304
TYR 305
0.0531
TYR 305
ASN 306
-0.0001
ASN 306
ALA 307
-0.0084
ALA 307
ARG 308
-0.0000
ARG 308
GLN 309
0.0373
GLN 309
LEU 310
-0.0001
LEU 310
SER 311
-0.0082
SER 311
ASP 312
0.0001
ASP 312
GLN 313
0.0051
GLN 313
GLY 314
-0.0002
GLY 314
ALA 315
0.0075
ALA 315
ALA 316
0.0004
ALA 316
GLU 317
-0.0174
GLU 317
LEU 318
-0.0004
LEU 318
ILE 319
-0.0020
ILE 319
LEU 320
-0.0003
LEU 320
GLU 321
-0.0123
GLU 321
LYS 322
0.0002
LYS 322
ASP 323
0.0445
ASP 323
LEU 324
0.0001
LEU 324
SER 325
0.0395
SER 325
GLY 326
-0.0001
GLY 326
ALA 327
-0.0200
ALA 327
SER 328
0.0004
SER 328
LEU 329
-0.0083
LEU 329
PHE 330
0.0003
PHE 330
GLU 331
-0.0154
GLU 331
LYS 332
0.0004
LYS 332
ILE 333
0.0142
ILE 333
SER 334
0.0001
SER 334
ASP 335
-0.0376
ASP 335
ILE 336
0.0001
ILE 336
MET 337
0.0163
MET 337
GLN 338
0.0002
GLN 338
ASN 339
-0.0570
ASN 339
PRO 340
0.0003
PRO 340
ILE 341
-0.0075
ILE 341
ARG 342
0.0001
ARG 342
ALA 343
0.0407
ALA 343
GLU 344
0.0003
GLU 344
HIS 345
0.0079
HIS 345
MET 346
-0.0001
MET 346
SER 347
-0.0085
SER 347
ILE 348
-0.0001
ILE 348
GLN 349
0.0040
GLN 349
ALA 350
-0.0002
ALA 350
LYS 351
0.0078
LYS 351
LYS 352
-0.0002
LYS 352
LEU 353
-0.0397
LEU 353
GLY 354
-0.0002
GLY 354
GLU 355
-0.0174
GLU 355
PRO 356
0.0003
PRO 356
GLU 357
-0.0137
GLU 357
SER 358
0.0001
SER 358
ALA 359
-0.0007
ALA 359
MET 360
0.0003
MET 360
LEU 361
0.0022
LEU 361
ILE 362
0.0002
ILE 362
VAL 363
0.0149
VAL 363
LYS 364
-0.0000
LYS 364
GLU 365
-0.0126
GLU 365
MET 366
0.0001
MET 366
GLN 367
-0.0009
GLN 367
ARG 368
0.0001
ARG 368
LEU 369
-0.0004
LEU 369
LEU 370
0.0001
LEU 370
LYS 371
0.0239
LYS 371
ASN 372
-0.0000
ASN 372
SER 373
0.0184
SER 373
PHE 374
0.0001
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.