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
GLY 1
LYS 2
0.0004
LYS 2
LEU 3
-0.0346
LEU 3
THR 4
-0.0001
THR 4
ALA 5
0.0080
ALA 5
VAL 6
-0.0000
VAL 6
ASP 7
-0.0451
ASP 7
PRO 8
0.0003
PRO 8
GLU 9
0.0017
GLU 9
THR 10
0.0001
THR 10
ASN 11
-0.0173
ASN 11
MET 12
0.0005
MET 12
ASN 13
0.0025
ASN 13
VAL 14
-0.0002
VAL 14
SER 15
0.0098
SER 15
GLU 16
0.0001
GLU 16
ILE 17
-0.0049
ILE 17
ILE 18
-0.0000
ILE 18
SER 19
0.0044
SER 19
TYR 20
0.0001
TYR 20
TRP 21
-0.0051
TRP 21
GLY 22
0.0001
GLY 22
PHE 23
-0.0094
PHE 23
PRO 24
0.0002
PRO 24
SER 25
-0.0118
SER 25
GLU 26
-0.0003
GLU 26
GLU 27
-0.0308
GLU 27
TYR 28
-0.0004
TYR 28
LEU 29
-0.0634
LEU 29
VAL 30
-0.0000
VAL 30
GLU 31
-0.0648
GLU 31
THR 32
-0.0001
THR 32
GLU 33
-0.0297
GLU 33
ASP 34
-0.0001
ASP 34
GLY 35
0.0052
GLY 35
TYR 36
-0.0001
TYR 36
ILE 37
-0.0240
ILE 37
LEU 38
0.0000
LEU 38
CYS 39
-0.0479
CYS 39
LEU 40
-0.0004
LEU 40
ASN 41
-0.0521
ASN 41
ARG 42
-0.0001
ARG 42
ILE 43
-0.0135
ILE 43
PRO 44
0.0002
PRO 44
HIS 45
-0.0181
HIS 45
GLY 46
-0.0000
GLY 46
ARG 47
-0.0175
ARG 47
LYS 48
-0.0003
LYS 48
ASN 49
0.0027
ASN 49
HIS 50
-0.0002
HIS 50
SER 51
-0.0051
SER 51
ASP 52
-0.0001
ASP 52
LYS 53
0.0030
LYS 53
GLY 54
-0.0002
GLY 54
PRO 55
-0.0019
PRO 55
LYS 56
0.0000
LYS 56
PRO 57
-0.0264
PRO 57
VAL 58
0.0003
VAL 58
VAL 59
0.0095
VAL 59
PHE 60
-0.0000
PHE 60
LEU 61
0.0039
LEU 61
GLN 62
-0.0002
GLN 62
HIS 63
0.0238
HIS 63
GLY 64
-0.0000
GLY 64
LEU 65
0.0373
LEU 65
LEU 66
0.0001
LEU 66
ALA 67
0.0760
ALA 67
ASP 68
-0.0001
ASP 68
SER 69
0.0373
SER 69
SER 70
0.0004
SER 70
ASN 71
-0.0116
ASN 71
TRP 72
0.0003
TRP 72
VAL 73
-0.0121
VAL 73
THR 74
-0.0005
THR 74
ASN 75
0.0072
ASN 75
LEU 76
-0.0001
LEU 76
ALA 77
0.0123
ALA 77
ASN 78
-0.0003
ASN 78
SER 79
0.0276
SER 79
SER 80
-0.0001
SER 80
LEU 81
-0.0278
LEU 81
GLY 82
-0.0002
GLY 82
PHE 83
-0.0075
PHE 83
ILE 84
0.0002
ILE 84
LEU 85
-0.0114
LEU 85
ALA 86
-0.0001
ALA 86
ASP 87
-0.0123
ASP 87
ALA 88
-0.0003
ALA 88
GLY 89
0.0018
GLY 89
PHE 90
0.0002
PHE 90
ASP 91
0.0103
ASP 91
VAL 92
0.0000
VAL 92
TRP 93
-0.0052
TRP 93
MET 94
-0.0001
MET 94
GLY 95
-0.0198
GLY 95
ASN 96
-0.0003
ASN 96
SER 97
-0.0361
SER 97
ARG 98
-0.0003
ARG 98
GLY 99
0.0136
GLY 99
ASN 100
0.0000
ASN 100
THR 101
0.0315
THR 101
TRP 102
0.0001
TRP 102
SER 103
-0.0273
SER 103
ARG 104
0.0003
ARG 104
LYS 105
-0.0116
LYS 105
HIS 106
-0.0004
HIS 106
LYS 107
-0.0128
LYS 107
THR 108
0.0001
THR 108
LEU 109
-0.0202
LEU 109
SER 110
-0.0005
SER 110
VAL 111
-0.0199
VAL 111
SER 112
-0.0003
SER 112
GLN 113
0.0171
GLN 113
ASP 114
0.0000
ASP 114
GLU 115
-0.0323
GLU 115
PHE 116
-0.0001
PHE 116
TRP 117
-0.0208
TRP 117
ALA 118
-0.0001
ALA 118
PHE 119
0.0392
PHE 119
SER 120
-0.0000
SER 120
TYR 121
0.0436
TYR 121
ASP 122
0.0001
ASP 122
GLU 123
-0.0242
GLU 123
MET 124
0.0001
MET 124
ALA 125
0.0557
ALA 125
LYS 126
-0.0001
LYS 126
TYR 127
-0.0119
TYR 127
ASP 128
-0.0001
ASP 128
LEU 129
0.0264
LEU 129
PRO 130
0.0001
PRO 130
ALA 131
0.0571
ALA 131
SER 132
-0.0003
SER 132
ILE 133
0.0292
ILE 133
ASN 134
-0.0000
ASN 134
PHE 135
0.0236
PHE 135
ILE 136
0.0002
ILE 136
LEU 137
0.0241
LEU 137
ASN 138
0.0000
ASN 138
LYS 139
0.0063
LYS 139
THR 140
0.0002
THR 140
GLY 141
0.0065
GLY 141
GLN 142
0.0002
GLN 142
GLU 143
-0.0431
GLU 143
GLN 144
-0.0000
GLN 144
VAL 145
0.0052
VAL 145
TYR 146
-0.0003
TYR 146
TYR 147
-0.0115
TYR 147
VAL 148
-0.0001
VAL 148
GLY 149
0.0168
GLY 149
HIS 150
0.0000
HIS 150
SER 151
0.0215
SER 151
GLN 152
-0.0003
GLN 152
GLY 153
0.0029
GLY 153
THR 154
-0.0000
THR 154
THR 155
-0.0280
THR 155
ILE 156
0.0003
ILE 156
GLY 157
0.0070
GLY 157
PHE 158
-0.0001
PHE 158
ILE 159
-0.0302
ILE 159
ALA 160
0.0001
ALA 160
PHE 161
-0.0340
PHE 161
SER 162
-0.0000
SER 162
GLN 163
-0.0310
GLN 163
ILE 164
-0.0000
ILE 164
PRO 165
-0.0453
PRO 165
GLU 166
-0.0001
GLU 166
LEU 167
0.0311
LEU 167
ALA 168
0.0002
ALA 168
LYS 169
-0.0221
LYS 169
ARG 170
0.0001
ARG 170
ILE 171
0.0241
ILE 171
LYS 172
0.0001
LYS 172
MET 173
0.0333
MET 173
PHE 174
-0.0000
PHE 174
PHE 175
-0.0126
PHE 175
ALA 176
0.0002
ALA 176
LEU 177
-0.0144
LEU 177
GLY 178
0.0000
GLY 178
PRO 179
-0.0075
PRO 179
VAL 180
0.0004
VAL 180
ALA 181
-0.0083
ALA 181
SER 182
-0.0000
SER 182
VAL 183
-0.0352
VAL 183
ALA 184
-0.0001
ALA 184
PHE 185
0.0593
PHE 185
CYS 186
-0.0001
CYS 186
THR 187
0.0290
THR 187
SER 188
0.0001
SER 188
PRO 189
-0.0217
PRO 189
MET 190
-0.0000
MET 190
ALA 191
0.0180
ALA 191
LYS 192
0.0002
LYS 192
LEU 193
-0.0425
LEU 193
GLY 194
-0.0000
GLY 194
ARG 195
0.0092
ARG 195
LEU 196
-0.0001
LEU 196
PRO 197
0.0829
PRO 197
ASP 198
-0.0002
ASP 198
HIS 199
-0.0016
HIS 199
LEU 200
-0.0001
LEU 200
ILE 201
0.0154
ILE 201
LYS 202
0.0000
LYS 202
ASP 203
0.0185
ASP 203
LEU 204
0.0001
LEU 204
PHE 205
-0.0345
PHE 205
GLY 206
-0.0000
GLY 206
ASP 207
-0.0801
ASP 207
LYS 208
0.0002
LYS 208
GLU 209
0.0291
GLU 209
PHE 210
-0.0002
PHE 210
LEU 211
0.0399
LEU 211
PRO 212
0.0001
PRO 212
GLN 213
0.0296
GLN 213
SER 214
0.0000
SER 214
ALA 215
0.0109
ALA 215
PHE 216
0.0000
PHE 216
LEU 217
0.0250
LEU 217
LYS 218
-0.0004
LYS 218
TRP 219
-0.0009
TRP 219
LEU 220
0.0003
LEU 220
GLY 221
0.0364
GLY 221
THR 222
0.0000
THR 222
HIS 223
-0.0297
HIS 223
VAL 224
-0.0001
VAL 224
CYS 225
-0.0021
CYS 225
THR 226
0.0000
THR 226
HIS 227
-0.0058
HIS 227
VAL 228
-0.0001
VAL 228
ILE 229
-0.0055
ILE 229
LEU 230
0.0000
LEU 230
LYS 231
-0.0258
LYS 231
GLU 232
0.0005
GLU 232
LEU 233
-0.0112
LEU 233
CYS 234
0.0000
CYS 234
GLY 235
0.0404
GLY 235
ASN 236
-0.0001
ASN 236
LEU 237
0.0744
LEU 237
CYS 238
-0.0001
CYS 238
PHE 239
-0.0211
PHE 239
LEU 240
-0.0001
LEU 240
LEU 241
0.0496
LEU 241
CYS 242
0.0002
CYS 242
GLY 243
0.0454
GLY 243
PHE 244
-0.0000
PHE 244
ASN 245
0.0281
ASN 245
GLU 246
0.0001
GLU 246
ARG 247
0.0124
ARG 247
ASN 248
-0.0001
ASN 248
LEU 249
-0.0274
LEU 249
ASN 250
0.0005
ASN 250
MET 251
-0.0454
MET 251
SER 252
0.0001
SER 252
ARG 253
-0.0186
ARG 253
VAL 254
0.0002
VAL 254
ASP 255
-0.0055
ASP 255
VAL 256
-0.0000
VAL 256
TYR 257
0.0351
TYR 257
THR 258
-0.0001
THR 258
THR 259
-0.0156
THR 259
HIS 260
0.0004
HIS 260
SER 261
0.0619
SER 261
PRO 262
0.0001
PRO 262
ALA 263
-0.0321
ALA 263
GLY 264
0.0001
GLY 264
THR 265
0.0648
THR 265
SER 266
-0.0002
SER 266
VAL 267
-0.0153
VAL 267
GLN 268
-0.0001
GLN 268
ASN 269
0.0326
ASN 269
MET 270
0.0000
MET 270
LEU 271
0.1219
LEU 271
HIS 272
0.0001
HIS 272
TRP 273
0.0551
TRP 273
SER 274
0.0003
SER 274
GLN 275
0.1396
GLN 275
ALA 276
-0.0001
ALA 276
VAL 277
0.0089
VAL 277
LYS 278
-0.0001
LYS 278
PHE 279
0.0738
PHE 279
GLN 280
0.0000
GLN 280
LYS 281
-0.1031
LYS 281
PHE 282
0.0004
PHE 282
GLN 283
-0.1036
GLN 283
ALA 284
0.0003
ALA 284
PHE 285
0.0169
PHE 285
ASP 286
0.0000
ASP 286
TRP 287
-0.0663
TRP 287
GLY 288
-0.0001
GLY 288
SER 289
0.2435
SER 289
SER 290
0.0003
SER 290
ALA 291
0.0064
ALA 291
LYS 292
0.0003
LYS 292
ASN 293
-0.0203
ASN 293
TYR 294
-0.0004
TYR 294
PHE 295
-0.0952
PHE 295
HIS 296
-0.0000
HIS 296
TYR 297
0.1754
TYR 297
ASN 298
-0.0000
ASN 298
GLN 299
0.0891
GLN 299
SER 300
-0.0002
SER 300
TYR 301
0.1089
TYR 301
PRO 302
-0.0001
PRO 302
PRO 303
-0.1807
PRO 303
THR 304
-0.0003
THR 304
TYR 305
-0.2869
TYR 305
ASN 306
0.0004
ASN 306
VAL 307
-0.1246
VAL 307
LYS 308
0.0001
LYS 308
ASP 309
0.0422
ASP 309
MET 310
0.0002
MET 310
LEU 311
-0.0396
LEU 311
VAL 312
-0.0001
VAL 312
PRO 313
-0.0218
PRO 313
THR 314
0.0001
THR 314
ALA 315
-0.0244
ALA 315
VAL 316
-0.0000
VAL 316
TRP 317
-0.0285
TRP 317
SER 318
0.0002
SER 318
GLY 319
-0.0094
GLY 319
GLY 320
-0.0001
GLY 320
HIS 321
-0.0058
HIS 321
ASP 322
0.0001
ASP 322
TRP 323
0.0324
TRP 323
LEU 324
-0.0005
LEU 324
ALA 325
-0.0178
ALA 325
ASP 326
0.0001
ASP 326
VAL 327
-0.0043
VAL 327
TYR 328
-0.0001
TYR 328
ASP 329
-0.0038
ASP 329
VAL 330
-0.0001
VAL 330
ASN 331
-0.0041
ASN 331
ILE 332
0.0000
ILE 332
LEU 333
0.0045
LEU 333
LEU 334
0.0000
LEU 334
THR 335
-0.0087
THR 335
GLN 336
-0.0001
GLN 336
ILE 337
0.0056
ILE 337
THR 338
-0.0001
THR 338
ASN 339
-0.0358
ASN 339
LEU 340
-0.0001
LEU 340
VAL 341
-0.0295
VAL 341
PHE 342
-0.0004
PHE 342
HIS 343
0.0114
HIS 343
GLU 344
0.0000
GLU 344
SER 345
0.0121
SER 345
ILE 346
-0.0003
ILE 346
PRO 347
-0.0038
PRO 347
GLU 348
0.0002
GLU 348
TRP 349
0.0032
TRP 349
GLU 350
-0.0001
GLU 350
HIS 351
-0.0037
HIS 351
LEU 352
0.0003
LEU 352
ASP 353
0.0163
ASP 353
PHE 354
0.0002
PHE 354
ILE 355
-0.0025
ILE 355
TRP 356
0.0001
TRP 356
GLY 357
-0.0044
GLY 357
LEU 358
-0.0000
LEU 358
ASP 359
-0.0231
ASP 359
ALA 360
-0.0004
ALA 360
PRO 361
0.0166
PRO 361
TRP 362
0.0001
TRP 362
ARG 363
0.0013
ARG 363
LEU 364
-0.0001
LEU 364
TYR 365
0.0213
TYR 365
ASN 366
0.0002
ASN 366
LYS 367
-0.0241
LYS 367
ILE 368
-0.0002
ILE 368
ILE 369
0.0104
ILE 369
ASN 370
0.0004
ASN 370
LEU 371
-0.0246
LEU 371
MET 372
-0.0001
MET 372
ARG 373
-0.0165
ARG 373
LYS 374
-0.0000
LYS 374
TYR 375
-0.0211
TYR 375
GLN 376
-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).
Last modification: October 18th, 2018.