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
0.0001
ILE 2
GLU 3
-0.0096
GLU 3
GLU 4
0.0003
GLU 4
GLY 5
-0.0069
GLY 5
LYS 6
-0.0000
LYS 6
LEU 7
-0.0007
LEU 7
VAL 8
0.0000
VAL 8
ILE 9
-0.0214
ILE 9
TRP 10
-0.0004
TRP 10
ILE 11
-0.0735
ILE 11
ASN 12
-0.0002
ASN 12
GLY 13
0.0328
GLY 13
ASP 14
0.0001
ASP 14
LYS 15
0.0057
LYS 15
GLY 16
-0.0003
GLY 16
TYR 17
0.0035
TYR 17
ASN 18
-0.0003
ASN 18
GLY 19
-0.0205
GLY 19
LEU 20
-0.0001
LEU 20
ALA 21
0.0091
ALA 21
GLU 22
-0.0004
GLU 22
VAL 23
-0.0185
VAL 23
GLY 24
-0.0001
GLY 24
LYS 25
-0.0118
LYS 25
LYS 26
-0.0003
LYS 26
PHE 27
-0.0126
PHE 27
GLU 28
0.0001
GLU 28
LYS 29
-0.0494
LYS 29
ASP 30
0.0001
ASP 30
THR 31
-0.0237
THR 31
GLY 32
-0.0001
GLY 32
ILE 33
-0.0422
ILE 33
LYS 34
-0.0001
LYS 34
VAL 35
-0.0060
VAL 35
THR 36
-0.0001
THR 36
VAL 37
-0.0233
VAL 37
GLU 38
-0.0002
GLU 38
HIS 39
-0.0383
HIS 39
PRO 40
-0.0001
PRO 40
ASP 41
0.0123
ASP 41
LYS 42
-0.0003
LYS 42
LEU 43
0.0591
LEU 43
GLU 44
-0.0002
GLU 44
GLU 45
-0.0209
GLU 45
LYS 46
0.0003
LYS 46
PHE 47
0.0409
PHE 47
PRO 48
-0.0002
PRO 48
GLN 49
-0.0152
GLN 49
VAL 50
0.0002
VAL 50
ALA 51
0.0315
ALA 51
ALA 52
-0.0001
ALA 52
THR 53
-0.0175
THR 53
GLY 54
0.0000
GLY 54
ASP 55
0.0146
ASP 55
GLY 56
-0.0002
GLY 56
PRO 57
0.0066
PRO 57
ASP 58
0.0001
ASP 58
ILE 59
-0.0132
ILE 59
ILE 60
0.0001
ILE 60
PHE 61
-0.0443
PHE 61
TRP 62
-0.0001
TRP 62
ALA 63
-0.0037
ALA 63
HIS 64
0.0002
HIS 64
ASP 65
-0.0002
ASP 65
ARG 66
0.0003
ARG 66
PHE 67
-0.0346
PHE 67
GLY 68
-0.0001
GLY 68
GLY 69
-0.0147
GLY 69
TYR 70
0.0000
TYR 70
ALA 71
0.1160
ALA 71
GLN 72
0.0000
GLN 72
SER 73
0.0029
SER 73
GLY 74
0.0001
GLY 74
LEU 75
-0.0005
LEU 75
LEU 76
0.0003
LEU 76
ALA 77
0.0124
ALA 77
GLU 78
0.0001
GLU 78
ILE 79
0.0271
ILE 79
THR 80
-0.0004
THR 80
PRO 81
0.0401
PRO 81
ASP 82
0.0001
ASP 82
LYS 83
0.0279
LYS 83
ALA 84
0.0001
ALA 84
PHE 85
-0.0269
PHE 85
GLN 86
0.0003
GLN 86
ASP 87
0.0244
ASP 87
LYS 88
-0.0003
LYS 88
LEU 89
0.0095
LEU 89
TYR 90
0.0003
TYR 90
PRO 91
0.0101
PRO 91
PHE 92
0.0001
PHE 92
THR 93
-0.0112
THR 93
TRP 94
-0.0001
TRP 94
ASP 95
-0.0139
ASP 95
ALA 96
0.0002
ALA 96
VAL 97
-0.0439
VAL 97
ARG 98
0.0003
ARG 98
TYR 99
0.1134
TYR 99
ASN 100
0.0003
ASN 100
GLY 101
0.0514
GLY 101
LYS 102
0.0000
LYS 102
LEU 103
0.0161
LEU 103
ILE 104
-0.0004
ILE 104
ALA 105
-0.0123
ALA 105
TYR 106
-0.0000
TYR 106
PRO 107
0.0053
PRO 107
ILE 108
0.0000
ILE 108
ALA 109
0.0238
ALA 109
VAL 110
-0.0005
VAL 110
GLU 111
-0.0333
GLU 111
ALA 112
-0.0001
ALA 112
LEU 113
-0.0308
LEU 113
SER 114
-0.0001
SER 114
LEU 115
0.0250
LEU 115
ILE 116
0.0000
ILE 116
TYR 117
-0.0012
TYR 117
ASN 118
0.0000
ASN 118
LYS 119
-0.0322
LYS 119
ASP 120
-0.0003
ASP 120
LEU 121
-0.0079
LEU 121
LEU 122
-0.0000
LEU 122
PRO 123
-0.0415
PRO 123
ASN 124
0.0004
ASN 124
PRO 125
0.0084
PRO 125
PRO 126
-0.0000
PRO 126
LYS 127
0.0359
LYS 127
THR 128
-0.0000
THR 128
TRP 129
-0.0432
TRP 129
GLU 130
-0.0001
GLU 130
GLU 131
0.0645
GLU 131
ILE 132
0.0002
ILE 132
PRO 133
-0.0153
PRO 133
ALA 134
0.0002
ALA 134
LEU 135
-0.0552
LEU 135
ASP 136
0.0001
ASP 136
LYS 137
0.0016
LYS 137
GLU 138
0.0001
GLU 138
LEU 139
-0.0243
LEU 139
LYS 140
0.0005
LYS 140
ALA 141
-0.0665
ALA 141
LYS 142
-0.0000
LYS 142
GLY 143
-0.0065
GLY 143
LYS 144
0.0001
LYS 144
SER 145
-0.0482
SER 145
ALA 146
-0.0003
ALA 146
LEU 147
-0.0498
LEU 147
MET 148
-0.0001
MET 148
PHE 149
-0.1256
PHE 149
ASN 150
0.0002
ASN 150
LEU 151
-0.0118
LEU 151
GLN 152
0.0002
GLN 152
GLU 153
-0.0472
GLU 153
PRO 154
0.0000
PRO 154
TYR 155
0.0885
TYR 155
PHE 156
0.0001
PHE 156
THR 157
0.0468
THR 157
TRP 158
-0.0003
TRP 158
PRO 159
0.0200
PRO 159
LEU 160
0.0002
LEU 160
ILE 161
0.0692
ILE 161
ALA 162
-0.0003
ALA 162
ALA 163
0.0546
ALA 163
ASP 164
-0.0002
ASP 164
GLY 165
0.2859
GLY 165
GLY 166
0.0002
GLY 166
TYR 167
0.1015
TYR 167
ALA 168
0.0004
ALA 168
PHE 169
0.2020
PHE 169
LYS 170
-0.0000
LYS 170
TYR 171
0.1725
TYR 171
GLU 172
-0.0001
GLU 172
ASN 173
0.0473
ASN 173
GLY 174
0.0001
GLY 174
LYS 175
-0.0528
LYS 175
TYR 176
0.0001
TYR 176
ASP 177
0.1624
ASP 177
ILE 178
0.0003
ILE 178
LYS 179
-0.0222
LYS 179
ASP 180
0.0002
ASP 180
VAL 181
0.0180
VAL 181
GLY 182
-0.0002
GLY 182
VAL 183
0.0467
VAL 183
ASP 184
0.0001
ASP 184
ASN 185
0.0425
ASN 185
ALA 186
0.0003
ALA 186
GLY 187
-0.0032
GLY 187
ALA 188
0.0001
ALA 188
LYS 189
0.0243
LYS 189
ALA 190
0.0001
ALA 190
GLY 191
-0.0108
GLY 191
LEU 192
-0.0003
LEU 192
THR 193
-0.0090
THR 193
PHE 194
-0.0003
PHE 194
LEU 195
-0.0173
LEU 195
VAL 196
-0.0000
VAL 196
ASP 197
-0.0568
ASP 197
LEU 198
0.0001
LEU 198
ILE 199
-0.0151
ILE 199
LYS 200
-0.0001
LYS 200
ASN 201
-0.1115
ASN 201
LYS 202
0.0001
LYS 202
HIS 203
0.0310
HIS 203
MET 204
-0.0003
MET 204
ASN 205
-0.0850
ASN 205
ALA 206
-0.0004
ALA 206
ASP 207
-0.0088
ASP 207
THR 208
-0.0001
THR 208
ASP 209
0.0822
ASP 209
TYR 210
-0.0001
TYR 210
SER 211
-0.0358
SER 211
ILE 212
0.0002
ILE 212
ALA 213
0.0257
ALA 213
GLU 214
0.0003
GLU 214
ALA 215
-0.0057
ALA 215
ALA 216
-0.0001
ALA 216
PHE 217
-0.0026
PHE 217
ASN 218
0.0001
ASN 218
LYS 219
0.0277
LYS 219
GLY 220
0.0003
GLY 220
GLU 221
0.0016
GLU 221
THR 222
0.0002
THR 222
ALA 223
0.0093
ALA 223
MET 224
-0.0001
MET 224
THR 225
-0.0513
THR 225
ILE 226
-0.0003
ILE 226
ASN 227
-0.0047
ASN 227
GLY 228
-0.0004
GLY 228
PRO 229
0.0475
PRO 229
TRP 230
-0.0000
TRP 230
ALA 231
-0.0062
ALA 231
TRP 232
0.0002
TRP 232
SER 233
0.0309
SER 233
ASN 234
0.0004
ASN 234
ILE 235
-0.0174
ILE 235
ASP 236
0.0003
ASP 236
THR 237
0.0199
THR 237
SER 238
-0.0003
SER 238
LYS 239
-0.0140
LYS 239
VAL 240
-0.0001
VAL 240
ASN 241
-0.0158
ASN 241
TYR 242
-0.0000
TYR 242
GLY 243
0.0814
GLY 243
VAL 244
0.0002
VAL 244
THR 245
0.0245
THR 245
VAL 246
0.0001
VAL 246
LEU 247
0.0247
LEU 247
PRO 248
0.0001
PRO 248
THR 249
0.0284
THR 249
PHE 250
0.0001
PHE 250
LYS 251
-0.0129
LYS 251
GLY 252
0.0003
GLY 252
GLN 253
-0.0085
GLN 253
PRO 254
-0.0001
PRO 254
SER 255
-0.0382
SER 255
LYS 256
-0.0003
LYS 256
PRO 257
-0.0676
PRO 257
PHE 258
0.0003
PHE 258
VAL 259
-0.0013
VAL 259
GLY 260
-0.0001
GLY 260
VAL 261
-0.0989
VAL 261
LEU 262
-0.0001
LEU 262
SER 263
-0.0446
SER 263
ALA 264
0.0001
ALA 264
GLY 265
-0.0070
GLY 265
ILE 266
-0.0005
ILE 266
ASN 267
0.0615
ASN 267
ALA 268
0.0002
ALA 268
ALA 269
-0.0255
ALA 269
SER 270
0.0000
SER 270
PRO 271
-0.0303
PRO 271
ASN 272
-0.0003
ASN 272
LYS 273
-0.0025
LYS 273
GLU 274
-0.0001
GLU 274
LEU 275
-0.0398
LEU 275
ALA 276
0.0000
ALA 276
LYS 277
0.0320
LYS 277
GLU 278
-0.0002
GLU 278
PHE 279
-0.0127
PHE 279
LEU 280
-0.0002
LEU 280
GLU 281
0.0020
GLU 281
ASN 282
-0.0000
ASN 282
TYR 283
-0.0376
TYR 283
LEU 284
-0.0002
LEU 284
LEU 285
0.0096
LEU 285
THR 286
-0.0001
THR 286
ASP 287
0.0834
ASP 287
GLU 288
0.0001
GLU 288
GLY 289
-0.0034
GLY 289
LEU 290
-0.0000
LEU 290
GLU 291
0.0128
GLU 291
ALA 292
0.0002
ALA 292
VAL 293
-0.0176
VAL 293
ASN 294
-0.0002
ASN 294
LYS 295
-0.0024
LYS 295
ASP 296
-0.0001
ASP 296
LYS 297
0.0620
LYS 297
PRO 298
-0.0001
PRO 298
LEU 299
0.0569
LEU 299
GLY 300
0.0001
GLY 300
ALA 301
-0.0016
ALA 301
VAL 302
0.0001
VAL 302
ALA 303
0.0016
ALA 303
LEU 304
-0.0004
LEU 304
LYS 305
0.0066
LYS 305
SER 306
-0.0001
SER 306
TYR 307
-0.0370
TYR 307
GLU 308
-0.0001
GLU 308
GLU 309
-0.0100
GLU 309
GLU 310
-0.0002
GLU 310
LEU 311
0.0179
LEU 311
ALA 312
-0.0004
ALA 312
LYS 313
-0.0123
LYS 313
ASP 314
0.0002
ASP 314
PRO 315
0.0961
PRO 315
ARG 316
0.0002
ARG 316
ILE 317
0.0723
ILE 317
ALA 318
-0.0004
ALA 318
ALA 319
0.0599
ALA 319
THR 320
-0.0000
THR 320
MET 321
-0.0191
MET 321
GLU 322
0.0000
GLU 322
ASN 323
0.0135
ASN 323
ALA 324
0.0001
ALA 324
GLN 325
-0.0594
GLN 325
LYS 326
0.0000
LYS 326
GLY 327
0.1055
GLY 327
GLU 328
-0.0004
GLU 328
ILE 329
-0.1465
ILE 329
MET 330
0.0001
MET 330
PRO 331
-0.0150
PRO 331
ASN 332
-0.0000
ASN 332
ILE 333
0.0830
ILE 333
PRO 334
0.0002
PRO 334
GLN 335
-0.1217
GLN 335
MET 336
0.0000
MET 336
SER 337
0.0497
SER 337
ALA 338
-0.0002
ALA 338
PHE 339
0.0805
PHE 339
TRP 340
-0.0003
TRP 340
TYR 341
0.0618
TYR 341
ALA 342
-0.0005
ALA 342
VAL 343
0.0159
VAL 343
ARG 344
-0.0002
ARG 344
THR 345
0.0185
THR 345
ALA 346
0.0000
ALA 346
VAL 347
-0.0490
VAL 347
ILE 348
0.0002
ILE 348
ASN 349
0.0336
ASN 349
ALA 350
0.0001
ALA 350
ALA 351
-0.0592
ALA 351
SER 352
0.0005
SER 352
GLY 353
-0.0067
GLY 353
ARG 354
0.0001
ARG 354
GLN 355
-0.0095
GLN 355
THR 356
-0.0001
THR 356
VAL 357
0.0375
VAL 357
ASP 358
-0.0004
ASP 358
GLU 359
0.0000
GLU 359
ALA 360
0.0002
ALA 360
LEU 361
0.0118
LEU 361
LYS 362
0.0003
LYS 362
ASP 363
0.0769
ASP 363
ALA 364
-0.0002
ALA 364
GLN 365
-0.0782
GLN 365
THR 366
-0.0000
THR 366
ARG 367
0.0792
ARG 367
ILE 368
0.0001
ILE 368
THR 369
-0.0688
THR 369
LYS 370
-0.0004
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).
Last modification: April 8th, 2025.