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
-0.0073
GLU 3
GLU 4
-0.0001
GLU 4
GLY 5
0.0112
GLY 5
LYS 6
0.0001
LYS 6
LEU 7
-0.0140
LEU 7
VAL 8
0.0001
VAL 8
ILE 9
-0.0227
ILE 9
TRP 10
-0.0001
TRP 10
ILE 11
-0.0854
ILE 11
ASN 12
0.0001
ASN 12
GLY 13
-0.0192
GLY 13
ASP 14
0.0003
ASP 14
LYS 15
-0.0466
LYS 15
GLY 16
-0.0002
GLY 16
TYR 17
-0.0688
TYR 17
ASN 18
0.0003
ASN 18
GLY 19
0.0629
GLY 19
LEU 20
0.0003
LEU 20
ALA 21
-0.0014
ALA 21
GLU 22
-0.0000
GLU 22
VAL 23
0.0155
VAL 23
GLY 24
-0.0002
GLY 24
LYS 25
0.0492
LYS 25
LYS 26
0.0002
LYS 26
PHE 27
0.0215
PHE 27
GLU 28
0.0003
GLU 28
LYS 29
0.0724
LYS 29
ASP 30
0.0002
ASP 30
THR 31
0.0349
THR 31
GLY 32
-0.0002
GLY 32
ILE 33
0.0397
ILE 33
LYS 34
-0.0001
LYS 34
VAL 35
-0.0288
VAL 35
THR 36
0.0000
THR 36
VAL 37
-0.0844
VAL 37
GLU 38
-0.0001
GLU 38
HIS 39
-0.0178
HIS 39
PRO 40
-0.0001
PRO 40
ASP 41
0.0140
ASP 41
LYS 42
-0.0000
LYS 42
LEU 43
-0.0124
LEU 43
GLU 44
-0.0001
GLU 44
GLU 45
0.0135
GLU 45
LYS 46
-0.0001
LYS 46
PHE 47
-0.0214
PHE 47
PRO 48
0.0001
PRO 48
GLN 49
-0.0196
GLN 49
VAL 50
0.0000
VAL 50
ALA 51
-0.0165
ALA 51
ALA 52
0.0004
ALA 52
THR 53
-0.0035
THR 53
GLY 54
-0.0000
GLY 54
ASP 55
-0.0185
ASP 55
GLY 56
0.0002
GLY 56
PRO 57
-0.0076
PRO 57
ASP 58
0.0002
ASP 58
ILE 59
-0.0021
ILE 59
ILE 60
0.0002
ILE 60
PHE 61
0.0057
PHE 61
TRP 62
0.0000
TRP 62
ALA 63
0.0750
ALA 63
HIS 64
0.0001
HIS 64
ASP 65
0.0768
ASP 65
ARG 66
0.0003
ARG 66
PHE 67
0.1241
PHE 67
GLY 68
0.0000
GLY 68
GLY 69
0.0270
GLY 69
TYR 70
-0.0003
TYR 70
ALA 71
-0.0951
ALA 71
GLN 72
0.0003
GLN 72
SER 73
-0.0419
SER 73
GLY 74
0.0003
GLY 74
LEU 75
-0.0003
LEU 75
LEU 76
-0.0002
LEU 76
ALA 77
-0.0004
ALA 77
GLU 78
-0.0003
GLU 78
ILE 79
-0.0429
ILE 79
THR 80
0.0001
THR 80
PRO 81
-0.0394
PRO 81
ASP 82
0.0001
ASP 82
LYS 83
-0.0126
LYS 83
ALA 84
0.0004
ALA 84
PHE 85
-0.0251
PHE 85
GLN 86
0.0000
GLN 86
ASP 87
-0.0178
ASP 87
LYS 88
-0.0003
LYS 88
LEU 89
0.0187
LEU 89
TYR 90
0.0005
TYR 90
PRO 91
-0.0025
PRO 91
PHE 92
0.0001
PHE 92
THR 93
-0.0081
THR 93
TRP 94
-0.0001
TRP 94
ASP 95
0.0657
ASP 95
ALA 96
-0.0003
ALA 96
VAL 97
0.0419
VAL 97
ARG 98
-0.0002
ARG 98
TYR 99
-0.0517
TYR 99
ASN 100
0.0002
ASN 100
GLY 101
-0.0152
GLY 101
LYS 102
0.0001
LYS 102
LEU 103
-0.0162
LEU 103
ILE 104
0.0002
ILE 104
ALA 105
0.0166
ALA 105
TYR 106
-0.0000
TYR 106
PRO 107
-0.0347
PRO 107
ILE 108
-0.0002
ILE 108
ALA 109
-0.0720
ALA 109
VAL 110
-0.0001
VAL 110
GLU 111
-0.0017
GLU 111
ALA 112
0.0002
ALA 112
LEU 113
0.0376
LEU 113
SER 114
0.0001
SER 114
LEU 115
0.0297
LEU 115
ILE 116
-0.0001
ILE 116
TYR 117
-0.0123
TYR 117
ASN 118
0.0002
ASN 118
LYS 119
0.0358
LYS 119
ASP 120
-0.0000
ASP 120
LEU 121
-0.0553
LEU 121
LEU 122
-0.0003
LEU 122
PRO 123
-0.0120
PRO 123
ASN 124
-0.0001
ASN 124
PRO 125
0.0143
PRO 125
PRO 126
-0.0001
PRO 126
LYS 127
0.0464
LYS 127
THR 128
0.0002
THR 128
TRP 129
-0.0128
TRP 129
GLU 130
0.0000
GLU 130
GLU 131
0.0821
GLU 131
ILE 132
-0.0001
ILE 132
PRO 133
-0.0460
PRO 133
ALA 134
0.0001
ALA 134
LEU 135
-0.0783
LEU 135
ASP 136
0.0001
ASP 136
LYS 137
-0.0307
LYS 137
GLU 138
-0.0000
GLU 138
LEU 139
-0.0539
LEU 139
LYS 140
-0.0001
LYS 140
ALA 141
-0.0117
ALA 141
LYS 142
-0.0004
LYS 142
GLY 143
-0.0139
GLY 143
LYS 144
0.0002
LYS 144
SER 145
0.0251
SER 145
ALA 146
0.0004
ALA 146
LEU 147
0.0056
LEU 147
MET 148
0.0001
MET 148
PHE 149
-0.0082
PHE 149
ASN 150
0.0002
ASN 150
LEU 151
-0.0492
LEU 151
GLN 152
-0.0002
GLN 152
GLU 153
0.0398
GLU 153
PRO 154
-0.0000
PRO 154
TYR 155
-0.0145
TYR 155
PHE 156
-0.0001
PHE 156
THR 157
-0.0425
THR 157
TRP 158
-0.0000
TRP 158
PRO 159
0.0136
PRO 159
LEU 160
0.0001
LEU 160
ILE 161
0.0253
ILE 161
ALA 162
-0.0002
ALA 162
ALA 163
0.0822
ALA 163
ASP 164
0.0002
ASP 164
GLY 165
0.2260
GLY 165
GLY 166
-0.0002
GLY 166
TYR 167
0.1669
TYR 167
ALA 168
-0.0000
ALA 168
PHE 169
0.0731
PHE 169
LYS 170
0.0000
LYS 170
TYR 171
0.0279
TYR 171
GLU 172
0.0001
GLU 172
ASN 173
-0.0190
ASN 173
GLY 174
-0.0001
GLY 174
LYS 175
-0.0118
LYS 175
TYR 176
0.0002
TYR 176
ASP 177
0.0292
ASP 177
ILE 178
-0.0001
ILE 178
LYS 179
0.0758
LYS 179
ASP 180
0.0003
ASP 180
VAL 181
-0.0104
VAL 181
GLY 182
0.0001
GLY 182
VAL 183
-0.0238
VAL 183
ASP 184
-0.0000
ASP 184
ASN 185
-0.0163
ASN 185
ALA 186
-0.0000
ALA 186
GLY 187
-0.0363
GLY 187
ALA 188
-0.0004
ALA 188
LYS 189
0.0050
LYS 189
ALA 190
-0.0001
ALA 190
GLY 191
-0.0227
GLY 191
LEU 192
-0.0001
LEU 192
THR 193
0.0170
THR 193
PHE 194
-0.0002
PHE 194
LEU 195
-0.0205
LEU 195
VAL 196
-0.0001
VAL 196
ASP 197
0.0052
ASP 197
LEU 198
-0.0001
LEU 198
ILE 199
-0.0186
ILE 199
LYS 200
0.0001
LYS 200
ASN 201
-0.0092
ASN 201
LYS 202
0.0001
LYS 202
HIS 203
-0.0232
HIS 203
MET 204
0.0002
MET 204
ASN 205
-0.0205
ASN 205
ALA 206
-0.0001
ALA 206
ASP 207
-0.0106
ASP 207
THR 208
-0.0000
THR 208
ASP 209
0.0101
ASP 209
TYR 210
0.0000
TYR 210
SER 211
-0.0279
SER 211
ILE 212
0.0001
ILE 212
ALA 213
0.0168
ALA 213
GLU 214
0.0001
GLU 214
ALA 215
-0.0261
ALA 215
ALA 216
0.0001
ALA 216
PHE 217
0.0110
PHE 217
ASN 218
-0.0004
ASN 218
LYS 219
-0.0683
LYS 219
GLY 220
-0.0002
GLY 220
GLU 221
-0.0080
GLU 221
THR 222
-0.0005
THR 222
ALA 223
0.0339
ALA 223
MET 224
-0.0001
MET 224
THR 225
-0.0182
THR 225
ILE 226
-0.0001
ILE 226
ASN 227
-0.1404
ASN 227
GLY 228
-0.0002
GLY 228
PRO 229
-0.0928
PRO 229
TRP 230
-0.0006
TRP 230
ALA 231
-0.0898
ALA 231
TRP 232
-0.0001
TRP 232
SER 233
-0.0571
SER 233
ASN 234
0.0000
ASN 234
ILE 235
-0.1339
ILE 235
ASP 236
-0.0001
ASP 236
THR 237
0.0543
THR 237
SER 238
0.0001
SER 238
LYS 239
-0.0237
LYS 239
VAL 240
0.0001
VAL 240
ASN 241
0.0350
ASN 241
TYR 242
-0.0003
TYR 242
GLY 243
0.0936
GLY 243
VAL 244
-0.0000
VAL 244
THR 245
-0.0025
THR 245
VAL 246
-0.0004
VAL 246
LEU 247
-0.0865
LEU 247
PRO 248
0.0002
PRO 248
THR 249
-0.0680
THR 249
PHE 250
-0.0002
PHE 250
LYS 251
-0.0236
LYS 251
GLY 252
-0.0001
GLY 252
GLN 253
0.0181
GLN 253
PRO 254
-0.0003
PRO 254
SER 255
-0.0022
SER 255
LYS 256
-0.0000
LYS 256
PRO 257
0.0134
PRO 257
PHE 258
0.0001
PHE 258
VAL 259
0.0179
VAL 259
GLY 260
-0.0003
GLY 260
VAL 261
0.0474
VAL 261
LEU 262
0.0001
LEU 262
SER 263
-0.0511
SER 263
ALA 264
-0.0000
ALA 264
GLY 265
-0.0284
GLY 265
ILE 266
0.0004
ILE 266
ASN 267
-0.0622
ASN 267
ALA 268
-0.0000
ALA 268
ALA 269
0.0258
ALA 269
SER 270
-0.0003
SER 270
PRO 271
0.0230
PRO 271
ASN 272
-0.0001
ASN 272
LYS 273
0.0213
LYS 273
GLU 274
-0.0003
GLU 274
LEU 275
0.0436
LEU 275
ALA 276
0.0002
ALA 276
LYS 277
-0.0289
LYS 277
GLU 278
0.0002
GLU 278
PHE 279
-0.0242
PHE 279
LEU 280
-0.0003
LEU 280
GLU 281
-0.0023
GLU 281
ASN 282
0.0004
ASN 282
TYR 283
0.0391
TYR 283
LEU 284
0.0000
LEU 284
LEU 285
0.0307
LEU 285
THR 286
-0.0001
THR 286
ASP 287
-0.0799
ASP 287
GLU 288
0.0001
GLU 288
GLY 289
0.0214
GLY 289
LEU 290
-0.0000
LEU 290
GLU 291
-0.0232
GLU 291
ALA 292
0.0001
ALA 292
VAL 293
0.0441
VAL 293
ASN 294
-0.0001
ASN 294
LYS 295
-0.0029
LYS 295
ASP 296
0.0002
ASP 296
LYS 297
-0.0960
LYS 297
PRO 298
0.0001
PRO 298
LEU 299
-0.1807
LEU 299
GLY 300
-0.0002
GLY 300
ALA 301
-0.0722
ALA 301
VAL 302
-0.0001
VAL 302
ALA 303
-0.0574
ALA 303
LEU 304
-0.0000
LEU 304
LYS 305
0.0141
LYS 305
SER 306
0.0004
SER 306
TYR 307
0.0154
TYR 307
GLU 308
-0.0000
GLU 308
GLU 309
0.0189
GLU 309
GLU 310
0.0002
GLU 310
LEU 311
-0.0186
LEU 311
ALA 312
0.0000
ALA 312
LYS 313
0.0062
LYS 313
ASP 314
-0.0001
ASP 314
PRO 315
-0.1565
PRO 315
ARG 316
-0.0002
ARG 316
ILE 317
-0.0898
ILE 317
ALA 318
0.0006
ALA 318
ALA 319
-0.1179
ALA 319
THR 320
-0.0001
THR 320
MET 321
0.0155
MET 321
GLU 322
-0.0000
GLU 322
ASN 323
-0.0193
ASN 323
ALA 324
0.0002
ALA 324
GLN 325
-0.0306
GLN 325
LYS 326
-0.0001
LYS 326
GLY 327
0.1172
GLY 327
GLU 328
0.0001
GLU 328
ILE 329
0.1130
ILE 329
MET 330
0.0003
MET 330
PRO 331
0.0190
PRO 331
ASN 332
-0.0000
ASN 332
ILE 333
0.0494
ILE 333
PRO 334
-0.0002
PRO 334
GLN 335
0.3782
GLN 335
MET 336
-0.0000
MET 336
SER 337
-0.0290
SER 337
ALA 338
0.0001
ALA 338
PHE 339
-0.0117
PHE 339
TRP 340
0.0001
TRP 340
TYR 341
0.0048
TYR 341
ALA 342
0.0001
ALA 342
VAL 343
-0.0513
VAL 343
ARG 344
-0.0000
ARG 344
THR 345
0.0169
THR 345
ALA 346
-0.0001
ALA 346
VAL 347
-0.0735
VAL 347
ILE 348
-0.0001
ILE 348
ASN 349
-0.0152
ASN 349
ALA 350
-0.0001
ALA 350
ALA 351
-0.0418
ALA 351
SER 352
0.0000
SER 352
GLY 353
-0.0120
GLY 353
ARG 354
0.0000
ARG 354
GLN 355
-0.0275
GLN 355
THR 356
-0.0002
THR 356
VAL 357
-0.0346
VAL 357
ASP 358
-0.0002
ASP 358
GLU 359
-0.0226
GLU 359
ALA 360
-0.0003
ALA 360
LEU 361
-0.0194
LEU 361
LYS 362
-0.0002
LYS 362
ASP 363
0.0282
ASP 363
ALA 364
-0.0001
ALA 364
GLN 365
-0.0603
GLN 365
THR 366
-0.0000
THR 366
ARG 367
0.0673
ARG 367
ILE 368
0.0003
ILE 368
THR 369
-0.0537
THR 369
LYS 370
0.0000
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.