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
ARG 1
CYS 2
0.0001
CYS 2
THR 3
0.0325
THR 3
HIS 4
-0.0001
HIS 4
LEU 5
-0.0571
LEU 5
GLU 6
-0.0001
GLU 6
ASN 7
-0.0225
ASN 7
ARG 8
0.0001
ARG 8
ASP 9
0.0029
ASP 9
PHE 10
0.0001
PHE 10
VAL 11
-0.1019
VAL 11
THR 12
0.0000
THR 12
GLY 13
-0.0467
GLY 13
THR 14
0.0005
THR 14
GLN 15
-0.0099
GLN 15
GLY 16
-0.0002
GLY 16
THR 17
0.0199
THR 17
THR 18
0.0002
THR 18
ARG 19
0.0315
ARG 19
VAL 20
-0.0003
VAL 20
THR 21
0.0522
THR 21
LEU 22
0.0003
LEU 22
VAL 23
0.0526
VAL 23
LEU 24
0.0001
LEU 24
GLU 25
0.0401
GLU 25
LEU 26
0.0000
LEU 26
GLY 27
0.0026
GLY 27
GLY 28
0.0000
GLY 28
CYS 29
0.0091
CYS 29
VAL 30
-0.0002
VAL 30
THR 31
0.0023
THR 31
ILE 32
-0.0002
ILE 32
THR 33
0.0221
THR 33
ALA 34
0.0005
ALA 34
GLU 35
0.0005
GLU 35
GLY 36
0.0001
GLY 36
LYS 37
0.0157
LYS 37
PRO 38
-0.0000
PRO 38
SER 39
0.0118
SER 39
MET 40
0.0001
MET 40
ASP 41
0.0107
ASP 41
VAL 42
0.0001
VAL 42
TRP 43
0.0318
TRP 43
LEU 44
-0.0003
LEU 44
ASP 45
0.0292
ASP 45
ALA 46
-0.0001
ALA 46
ILE 47
0.0279
ILE 47
TYR 48
0.0002
TYR 48
GLN 49
0.0601
GLN 49
GLU 50
-0.0002
GLU 50
ASN 51
0.0810
ASN 51
PRO 52
0.0000
PRO 52
ALA 53
0.0374
ALA 53
LYS 54
-0.0003
LYS 54
THR 55
-0.0120
THR 55
ARG 56
-0.0004
ARG 56
GLU 57
0.0398
GLU 57
TYR 58
-0.0001
TYR 58
CYS 59
0.0105
CYS 59
LEU 60
0.0003
LEU 60
HIS 61
-0.0160
HIS 61
ALA 62
-0.0003
ALA 62
LYS 63
-0.0904
LYS 63
LEU 64
0.0001
LEU 64
SER 65
-0.2054
SER 65
ASP 66
0.0001
ASP 66
THR 67
0.0267
THR 67
LYS 68
0.0002
LYS 68
VAL 69
-0.1374
VAL 69
ALA 70
-0.0000
ALA 70
ALA 71
-0.1055
ALA 71
ARG 72
-0.0001
ARG 72
CYS 73
-0.0115
CYS 73
PRO 74
0.0002
PRO 74
THR 75
0.0126
THR 75
MET 76
0.0000
MET 76
GLY 77
0.0281
GLY 77
PRO 78
0.0002
PRO 78
ALA 79
-0.0462
ALA 79
THR 80
-0.0001
THR 80
LEU 81
-0.1292
LEU 81
ALA 82
-0.0002
ALA 82
GLU 83
-0.0336
GLU 83
GLU 84
0.0004
GLU 84
HIS 85
0.0121
HIS 85
GLN 86
0.0003
GLN 86
GLY 87
0.0522
GLY 87
GLY 88
-0.0003
GLY 88
THR 89
-0.0106
THR 89
VAL 90
0.0000
VAL 90
CYS 91
0.1065
CYS 91
LYS 92
0.0002
LYS 92
ARG 93
0.1824
ARG 93
ASP 94
-0.0002
ASP 94
GLN 95
0.0175
GLN 95
SER 96
0.0002
SER 96
ASP 97
-0.0207
ASP 97
ARG 98
-0.0000
ARG 98
GLY 99
0.0215
GLY 99
TRP 100
-0.0003
TRP 100
GLY 101
0.0010
GLY 101
ASN 102
-0.0001
ASN 102
HIS 103
-0.0203
HIS 103
CYS 104
0.0001
CYS 104
GLY 105
-0.0161
GLY 105
LEU 106
-0.0001
LEU 106
PHE 107
0.0171
PHE 107
GLY 108
0.0003
GLY 108
LYS 109
-0.0034
LYS 109
GLY 110
0.0001
GLY 110
SER 111
-0.0648
SER 111
ILE 112
0.0000
ILE 112
VAL 113
0.0122
VAL 113
ALA 114
-0.0004
ALA 114
CYS 115
-0.0102
CYS 115
VAL 116
-0.0003
VAL 116
LYS 117
-0.0507
LYS 117
ALA 118
0.0002
ALA 118
ALA 119
-0.0886
ALA 119
CYS 120
-0.0003
CYS 120
GLU 121
-0.0484
GLU 121
ALA 122
0.0001
ALA 122
LYS 123
-0.0147
LYS 123
LYS 124
0.0002
LYS 124
LYS 125
0.0813
LYS 125
ALA 126
-0.0002
ALA 126
THR 127
0.1156
THR 127
GLY 128
-0.0002
GLY 128
HIS 129
0.0644
HIS 129
VAL 130
0.0001
VAL 130
TYR 131
0.0889
TYR 131
ASP 132
-0.0002
ASP 132
ALA 133
0.0197
ALA 133
ASN 134
-0.0000
ASN 134
LYS 135
-0.0506
LYS 135
ILE 136
0.0005
ILE 136
VAL 137
0.0812
VAL 137
TYR 138
0.0002
TYR 138
THR 139
0.0355
THR 139
VAL 140
-0.0001
VAL 140
LYS 141
0.0261
LYS 141
VAL 142
0.0001
VAL 142
GLU 143
0.0185
GLU 143
PRO 144
-0.0003
PRO 144
HIS 145
0.0003
HIS 145
THR 146
-0.0002
THR 146
ARG 147
-0.0492
ARG 147
LYS 148
-0.0002
LYS 148
THR 149
0.0136
THR 149
ALA 150
-0.0002
ALA 150
SER 151
0.0754
SER 151
PHE 152
0.0003
PHE 152
THR 153
0.0651
THR 153
ILE 154
-0.0002
ILE 154
SER 155
-0.0151
SER 155
SER 156
0.0001
SER 156
GLU 157
-0.0043
GLU 157
LYS 158
0.0002
LYS 158
THR 159
0.0334
THR 159
ILE 160
0.0000
ILE 160
LEU 161
0.0237
LEU 161
THR 162
0.0000
THR 162
MET 163
0.0188
MET 163
GLY 164
0.0002
GLY 164
GLU 165
-0.0441
GLU 165
TYR 166
-0.0004
TYR 166
GLY 167
0.0458
GLY 167
ASP 168
0.0002
ASP 168
VAL 169
0.0046
VAL 169
SER 170
-0.0001
SER 170
LEU 171
0.0400
LEU 171
LEU 172
0.0002
LEU 172
CYS 173
0.0205
CYS 173
ARG 174
-0.0000
ARG 174
VAL 175
0.0242
VAL 175
ALA 176
-0.0002
ALA 176
SER 177
0.0256
SER 177
GLY 178
0.0002
GLY 178
VAL 179
-0.0390
VAL 179
ASP 180
0.0001
ASP 180
LEU 181
-0.0195
LEU 181
ALA 182
0.0002
ALA 182
GLN 183
0.0296
GLN 183
THR 184
0.0000
THR 184
VAL 185
0.0046
VAL 185
ILE 186
-0.0002
ILE 186
LEU 187
0.0308
LEU 187
GLU 188
-0.0004
GLU 188
LEU 189
0.0905
LEU 189
ASP 190
0.0001
ASP 190
PRO 191
0.0768
PRO 191
THR 192
0.0001
THR 192
ALA 193
-0.0072
ALA 193
TRP 194
-0.0002
TRP 194
GLN 195
0.0304
GLN 195
VAL 196
0.0003
VAL 196
HIS 197
0.0068
HIS 197
ARG 198
-0.0002
ARG 198
ASP 199
0.0067
ASP 199
TRP 200
0.0001
TRP 200
PHE 201
0.0124
PHE 201
ASN 202
0.0000
ASN 202
ASP 203
0.0144
ASP 203
LEU 204
-0.0003
LEU 204
ALA 205
0.0673
ALA 205
LEU 206
-0.0003
LEU 206
PRO 207
0.0007
PRO 207
TRP 208
-0.0002
TRP 208
LYS 209
-0.0179
LYS 209
HIS 210
0.0002
HIS 210
GLU 211
-0.0283
GLU 211
GLY 212
-0.0004
GLY 212
ALA 213
0.0107
ALA 213
GLN 214
-0.0002
GLN 214
ASN 215
0.0021
ASN 215
TRP 216
0.0002
TRP 216
ASN 217
0.0285
ASN 217
ASN 218
0.0001
ASN 218
ALA 219
0.0425
ALA 219
GLU 220
-0.0005
GLU 220
ARG 221
0.2002
ARG 221
LEU 222
-0.0001
LEU 222
VAL 223
0.1140
VAL 223
GLU 224
0.0002
GLU 224
PHE 225
0.2073
PHE 225
GLY 226
-0.0002
GLY 226
ALA 227
0.1835
ALA 227
PRO 228
0.0003
PRO 228
HIS 229
-0.0439
HIS 229
ALA 230
0.0001
ALA 230
VAL 231
0.0450
VAL 231
LYS 232
-0.0000
LYS 232
MET 233
-0.0234
MET 233
ASP 234
0.0003
ASP 234
VAL 235
0.0141
VAL 235
TYR 236
-0.0000
TYR 236
ASN 237
0.1216
ASN 237
LEU 238
-0.0000
LEU 238
GLY 239
0.1838
GLY 239
ASP 240
-0.0001
ASP 240
GLN 241
-0.0499
GLN 241
THR 242
0.0002
THR 242
GLY 243
-0.0489
GLY 243
VAL 244
0.0000
VAL 244
LEU 245
0.0222
LEU 245
LEU 246
0.0003
LEU 246
LYS 247
-0.0055
LYS 247
ALA 248
0.0002
ALA 248
LEU 249
-0.0000
LEU 249
ALA 250
-0.0001
ALA 250
GLY 251
-0.0159
GLY 251
VAL 252
0.0003
VAL 252
PRO 253
-0.0774
PRO 253
VAL 254
-0.0000
VAL 254
ALA 255
-0.0556
ALA 255
HIS 256
-0.0001
HIS 256
ILE 257
-0.0147
ILE 257
GLU 258
-0.0001
GLU 258
GLY 259
0.0008
GLY 259
THR 260
-0.0002
THR 260
LYS 261
0.0070
LYS 261
TYR 262
0.0001
TYR 262
HIS 263
0.0300
HIS 263
LEU 264
-0.0001
LEU 264
LYS 265
-0.0319
LYS 265
SER 266
-0.0003
SER 266
GLY 267
0.1606
GLY 267
HIS 268
-0.0000
HIS 268
VAL 269
0.0275
VAL 269
THR 270
0.0001
THR 270
CYS 271
0.0255
CYS 271
GLU 272
0.0002
GLU 272
VAL 273
0.0111
VAL 273
GLY 274
-0.0002
GLY 274
LEU 275
0.0352
LEU 275
GLU 276
-0.0003
GLU 276
LYS 277
0.0053
LYS 277
LEU 278
-0.0001
LEU 278
LYS 279
0.0705
LYS 279
MET 280
-0.0002
MET 280
LYS 281
0.1074
LYS 281
GLY 282
-0.0002
GLY 282
LEU 283
-0.0338
LEU 283
THR 284
-0.0002
THR 284
TYR 285
0.0227
TYR 285
THR 286
0.0002
THR 286
MET 287
-0.0097
MET 287
CYS 288
0.0003
CYS 288
ASP 289
0.0080
ASP 289
LYS 290
0.0002
LYS 290
THR 291
0.0024
THR 291
LYS 292
0.0002
LYS 292
PHE 293
-0.0181
PHE 293
THR 294
-0.0002
THR 294
TRP 295
-0.0059
TRP 295
LYS 296
0.0002
LYS 296
ARG 297
-0.0054
ARG 297
ALA 298
-0.0004
ALA 298
PRO 299
0.0041
PRO 299
THR 300
0.0002
THR 300
ASP 301
-0.0147
ASP 301
SER 302
-0.0003
SER 302
GLY 303
-0.0338
GLY 303
HIS 304
-0.0002
HIS 304
ASP 305
0.1301
ASP 305
THR 306
-0.0000
THR 306
VAL 307
-0.0096
VAL 307
VAL 308
-0.0001
VAL 308
MET 309
-0.0353
MET 309
GLU 310
-0.0001
GLU 310
VAL 311
-0.0194
VAL 311
THR 312
0.0001
THR 312
PHE 313
-0.0109
PHE 313
SER 314
0.0001
SER 314
GLY 315
-0.0065
GLY 315
THR 316
0.0002
THR 316
LYS 317
0.0042
LYS 317
PRO 318
0.0000
PRO 318
CYS 319
-0.0060
CYS 319
ARG 320
0.0003
ARG 320
ILE 321
-0.0200
ILE 321
PRO 322
-0.0002
PRO 322
VAL 323
-0.0284
VAL 323
ARG 324
-0.0001
ARG 324
ALA 325
-0.0359
ALA 325
VAL 326
-0.0002
VAL 326
ALA 327
-0.0168
ALA 327
HIS 328
-0.0001
HIS 328
GLY 329
0.0044
GLY 329
SER 330
-0.0003
SER 330
PRO 331
-0.0054
PRO 331
ASP 332
0.0004
ASP 332
VAL 333
0.0077
VAL 333
ASN 334
0.0004
ASN 334
VAL 335
-0.0006
VAL 335
ALA 336
-0.0003
ALA 336
MET 337
0.0087
MET 337
LEU 338
-0.0003
LEU 338
ILE 339
0.0389
ILE 339
THR 340
0.0000
THR 340
PRO 341
0.0028
PRO 341
ASN 342
0.0001
ASN 342
PRO 343
0.0091
PRO 343
THR 344
0.0001
THR 344
ILE 345
-0.0101
ILE 345
GLU 346
0.0004
GLU 346
ASN 347
0.0135
ASN 347
ASN 348
-0.0001
ASN 348
GLY 349
-0.0140
GLY 349
GLY 350
0.0000
GLY 350
GLY 351
-0.0352
GLY 351
PHE 352
-0.0003
PHE 352
ILE 353
-0.0162
ILE 353
GLU 354
-0.0001
GLU 354
MET 355
-0.0172
MET 355
GLN 356
0.0001
GLN 356
LEU 357
-0.0044
LEU 357
PRO 358
0.0001
PRO 358
PRO 359
-0.0800
PRO 359
GLY 360
-0.0000
GLY 360
ASP 361
-0.0130
ASP 361
ASN 362
-0.0001
ASN 362
ILE 363
-0.0027
ILE 363
ILE 364
0.0002
ILE 364
TYR 365
0.0019
TYR 365
VAL 366
0.0001
VAL 366
GLY 367
-0.0019
GLY 367
GLU 368
0.0002
GLU 368
LEU 369
-0.0137
LEU 369
SER 370
-0.0001
SER 370
HIS 371
0.0138
HIS 371
GLN 372
-0.0002
GLN 372
TRP 373
0.0154
TRP 373
PHE 374
-0.0004
PHE 374
GLN 375
0.0104
GLN 375
LYS 376
0.0004
LYS 376
GLY 377
0.1728
GLY 377
SER 378
0.0000
SER 378
SER 379
0.0472
SER 379
ILE 380
-0.0001
ILE 380
GLY 381
-0.0538
GLY 381
ARG 382
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).
Last modification: April 25th, 2023.