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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
0.0000
ARG 2
VAL 3
0.0013
VAL 3
VAL 4
0.0002
VAL 4
LEU 5
-0.0060
LEU 5
SER 6
0.0003
SER 6
GLY 7
-0.0004
GLY 7
GLY 8
-0.0003
GLY 8
GLY 9
0.0008
GLY 9
THR 10
0.0004
THR 10
GLY 11
0.0166
GLY 11
GLY 12
-0.0003
GLY 12
HIS 13
0.0027
HIS 13
VAL 14
0.0003
VAL 14
TYR 15
0.0182
TYR 15
PRO 16
-0.0002
PRO 16
ALA 17
-0.0018
ALA 17
LEU 18
0.0000
LEU 18
ALA 19
0.0157
ALA 19
VAL 20
0.0002
VAL 20
ALA 21
-0.0065
ALA 21
GLU 22
0.0003
GLU 22
GLN 23
0.0275
GLN 23
CYS 24
-0.0003
CYS 24
LEU 25
0.0093
LEU 25
GLN 26
0.0000
GLN 26
VAL 27
-0.0084
VAL 27
ASP 28
-0.0002
ASP 28
THR 29
0.0222
THR 29
ASP 30
0.0004
ASP 30
SER 31
-0.0015
SER 31
GLN 32
-0.0001
GLN 32
PHE 33
-0.0286
PHE 33
LEU 34
0.0000
LEU 34
TYR 35
-0.0153
TYR 35
ILE 36
0.0001
ILE 36
GLY 37
-0.0204
GLY 37
THR 38
-0.0000
THR 38
ASN 39
0.0131
ASN 39
SER 40
0.0004
SER 40
GLY 41
0.0047
GLY 41
LEU 42
0.0002
LEU 42
GLU 43
-0.0070
GLU 43
ARG 44
0.0001
ARG 44
ASP 45
-0.0049
ASP 45
ILE 46
0.0001
ILE 46
VAL 47
-0.0007
VAL 47
GLU 48
0.0003
GLU 48
LYS 49
0.0052
LYS 49
SER 50
-0.0004
SER 50
LYS 51
-0.0294
LYS 51
LEU 52
-0.0003
LEU 52
GLU 53
0.0032
GLU 53
MET 54
0.0003
MET 54
PRO 55
-0.0115
PRO 55
PHE 56
-0.0000
PHE 56
GLU 57
-0.0014
GLU 57
ALA 58
0.0001
ALA 58
ILE 59
-0.0691
ILE 59
ASP 60
-0.0001
ASP 60
ILE 61
0.0071
ILE 61
ARG 62
0.0002
ARG 62
GLY 63
0.0190
GLY 63
PHE 64
0.0001
PHE 64
ARG 65
0.0216
ARG 65
ARG 66
0.0002
ARG 66
LYS 67
0.1643
LYS 67
LEU 68
-0.0002
LEU 68
VAL 69
-0.0197
VAL 69
SER 70
-0.0002
SER 70
LEU 71
-0.0361
LEU 71
ASP 72
-0.0001
ASP 72
ASN 73
0.0363
ASN 73
ILE 74
0.0001
ILE 74
LYS 75
-0.0130
LYS 75
THR 76
-0.0000
THR 76
VAL 77
-0.0745
VAL 77
MET 78
-0.0002
MET 78
LYS 79
0.0060
LYS 79
PHE 80
-0.0001
PHE 80
LEU 81
-0.0562
LEU 81
LYS 82
-0.0003
LYS 82
GLY 83
0.0079
GLY 83
VAL 84
-0.0001
VAL 84
ASN 85
0.0008
ASN 85
ARG 86
-0.0002
ARG 86
SER 87
-0.0107
SER 87
LYS 88
0.0002
LYS 88
GLU 89
-0.0021
GLU 89
LEU 90
-0.0002
LEU 90
LEU 91
-0.0123
LEU 91
ARG 92
0.0000
ARG 92
ASN 93
0.0124
ASN 93
PHE 94
-0.0001
PHE 94
LYS 95
-0.0102
LYS 95
PRO 96
-0.0001
PRO 96
ASP 97
-0.0241
ASP 97
ILE 98
-0.0000
ILE 98
VAL 99
0.0023
VAL 99
ILE 100
0.0001
ILE 100
GLY 101
0.0096
GLY 101
THR 102
-0.0004
THR 102
GLY 103
0.0200
GLY 103
GLY 104
0.0000
GLY 104
TYR 105
0.0462
TYR 105
VAL 106
-0.0001
VAL 106
CYS 107
-0.0035
CYS 107
GLY 108
0.0001
GLY 108
PRO 109
-0.0005
PRO 109
VAL 110
0.0001
VAL 110
LEU 111
-0.0120
LEU 111
TYR 112
0.0002
TYR 112
ALA 113
-0.0072
ALA 113
ALA 114
-0.0002
ALA 114
ALA 115
-0.0100
ALA 115
LYS 116
0.0000
LYS 116
LEU 117
0.0136
LEU 117
GLY 118
-0.0001
GLY 118
VAL 119
0.0121
VAL 119
PRO 120
-0.0000
PRO 120
THR 121
0.0133
THR 121
LEU 122
0.0000
LEU 122
ILE 123
0.0218
ILE 123
HIS 124
-0.0002
HIS 124
GLU 125
0.0269
GLU 125
GLN 126
-0.0001
GLN 126
ASN 127
0.0047
ASN 127
ALA 128
0.0000
ALA 128
ILE 129
0.0121
ILE 129
ALA 130
-0.0002
ALA 130
GLY 131
0.0159
GLY 131
LEU 132
0.0004
LEU 132
THR 133
-0.0147
THR 133
ASN 134
0.0004
ASN 134
LYS 135
-0.0300
LYS 135
PHE 136
0.0002
PHE 136
LEU 137
0.0152
LEU 137
SER 138
0.0002
SER 138
ARG 139
-0.0106
ARG 139
TYR 140
-0.0002
TYR 140
ALA 141
-0.0022
ALA 141
ASN 142
0.0004
ASN 142
SER 143
-0.0095
SER 143
VAL 144
0.0002
VAL 144
LEU 145
-0.0148
LEU 145
VAL 146
0.0000
VAL 146
SER 147
0.0009
SER 147
PHE 148
-0.0002
PHE 148
LYS 149
0.0010
LYS 149
GLY 150
0.0003
GLY 150
THR 151
-0.0279
THR 151
GLU 152
0.0001
GLU 152
SER 153
-0.0068
SER 153
ILE 154
-0.0004
ILE 154
PHE 155
0.0148
PHE 155
SER 156
-0.0003
SER 156
LYS 157
-0.0226
LYS 157
ALA 158
0.0000
ALA 158
GLY 159
0.0099
GLY 159
SER 160
-0.0001
SER 160
HIS 161
-0.0123
HIS 161
VAL 162
0.0000
VAL 162
LEU 163
-0.0506
LEU 163
TYR 164
-0.0002
TYR 164
SER 165
-0.0108
SER 165
GLY 166
0.0001
GLY 166
ASN 167
-0.0024
ASN 167
PRO 168
-0.0002
PRO 168
ARG 169
-0.0217
ARG 169
ALA 170
0.0001
ALA 170
THR 171
-0.0322
THR 171
SER 172
0.0002
SER 172
VAL 173
-0.0753
VAL 173
VAL 174
0.0000
VAL 174
ASN 175
-0.0206
ASN 175
ALA 176
-0.0001
ALA 176
ASP 177
-0.0429
ASP 177
PRO 178
0.0002
PRO 178
GLU 179
-0.0014
GLU 179
GLU 180
0.0002
GLU 180
GLY 181
-0.0010
GLY 181
TYR 182
-0.0002
TYR 182
GLN 183
0.0080
GLN 183
SER 184
0.0003
SER 184
LEU 185
-0.0091
LEU 185
GLY 186
0.0004
GLY 186
ILE 187
0.0064
ILE 187
ARG 188
-0.0002
ARG 188
PRO 189
-0.0025
PRO 189
GLY 190
0.0001
GLY 190
THR 191
-0.0010
THR 191
GLN 192
-0.0001
GLN 192
ILE 193
0.0122
ILE 193
VAL 194
0.0002
VAL 194
LEU 195
0.0026
LEU 195
VAL 196
0.0001
VAL 196
VAL 197
0.0111
VAL 197
GLY 198
-0.0003
GLY 198
GLY 199
-0.0014
GLY 199
SER 200
0.0004
SER 200
ARG 201
0.0010
ARG 201
GLY 202
-0.0002
GLY 202
ALA 203
0.0140
ALA 203
LYS 204
0.0002
LYS 204
ALA 205
-0.0071
ALA 205
ILE 206
-0.0000
ILE 206
ASN 207
0.0148
ASN 207
ARG 208
-0.0001
ARG 208
ALA 209
-0.0100
ALA 209
MET 210
0.0001
MET 210
ILE 211
0.0032
ILE 211
GLU 212
0.0001
GLU 212
MET 213
-0.0067
MET 213
ALA 214
0.0002
ALA 214
SER 215
0.0008
SER 215
LEU 216
0.0001
LEU 216
VAL 217
-0.0102
VAL 217
ASN 218
-0.0001
ASN 218
LYS 219
0.0042
LYS 219
LEU 220
-0.0000
LEU 220
SER 221
0.0077
SER 221
ASP 222
0.0002
ASP 222
ILE 223
0.0045
ILE 223
GLN 224
0.0002
GLN 224
PHE 225
0.0075
PHE 225
ILE 226
-0.0001
ILE 226
PHE 227
0.0056
PHE 227
VAL 228
0.0002
VAL 228
THR 229
-0.0011
THR 229
GLY 230
0.0001
GLY 230
ALA 231
-0.0012
ALA 231
PRO 232
0.0001
PRO 232
TYR 233
-0.0017
TYR 233
TYR 234
-0.0000
TYR 234
GLU 235
-0.0011
GLU 235
GLU 236
-0.0002
GLU 236
THR 237
-0.0010
THR 237
ARG 238
0.0001
ARG 238
ASP 239
-0.0063
ASP 239
ALA 240
-0.0000
ALA 240
ILE 241
-0.0053
ILE 241
SER 242
0.0004
SER 242
ALA 243
-0.0010
ALA 243
PHE 244
0.0002
PHE 244
SER 245
-0.0027
SER 245
PRO 246
-0.0002
PRO 246
ASP 247
-0.0069
ASP 247
ILE 248
0.0003
ILE 248
PRO 249
-0.0054
PRO 249
ASN 250
-0.0002
ASN 250
LEU 251
0.0139
LEU 251
ALA 252
0.0004
ALA 252
VAL 253
0.0076
VAL 253
LEU 254
-0.0000
LEU 254
PRO 255
0.0119
PRO 255
TYR 256
-0.0003
TYR 256
VAL 257
-0.0255
VAL 257
HIS 258
-0.0001
HIS 258
ASN 259
-0.0073
ASN 259
MET 260
0.0003
MET 260
PRO 261
-0.0500
PRO 261
GLU 262
-0.0001
GLU 262
VAL 263
-0.0238
VAL 263
LEU 264
0.0002
LEU 264
ALA 265
0.0083
ALA 265
ALA 266
-0.0004
ALA 266
THR 267
0.0084
THR 267
SER 268
-0.0001
SER 268
LEU 269
0.0197
LEU 269
ILE 270
-0.0004
ILE 270
VAL 271
0.0012
VAL 271
ILE 272
0.0003
ILE 272
ASN 273
0.0002
ASN 273
ARG 274
0.0001
ARG 274
ALA 275
0.0143
ALA 275
GLY 276
0.0001
GLY 276
ALA 277
0.0002
ALA 277
SER 278
-0.0002
SER 278
THR 279
-0.0051
THR 279
ILE 280
-0.0003
ILE 280
ALA 281
-0.0282
ALA 281
GLU 282
0.0001
GLU 282
LEU 283
-0.0317
LEU 283
THR 284
0.0000
THR 284
ALA 285
-0.0147
ALA 285
LEU 286
0.0001
LEU 286
GLY 287
0.0084
GLY 287
LEU 288
0.0001
LEU 288
PRO 289
-0.0041
PRO 289
SER 290
-0.0002
SER 290
ILE 291
-0.0128
ILE 291
LEU 292
0.0002
LEU 292
ILE 293
-0.0061
ILE 293
PRO 294
0.0000
PRO 294
SER 295
-0.0058
SER 295
PRO 296
-0.0003
PRO 296
ASN 297
0.0039
ASN 297
VAL 298
-0.0003
VAL 298
THR 299
0.0395
THR 299
GLY 300
-0.0001
GLY 300
ASN 301
0.0622
ASN 301
HIS 302
0.0000
HIS 302
GLN 303
0.0330
GLN 303
GLU 304
-0.0002
GLU 304
TYR 305
0.0303
TYR 305
ASN 306
0.0000
ASN 306
ALA 307
0.0268
ALA 307
ARG 308
-0.0000
ARG 308
GLN 309
0.0307
GLN 309
LEU 310
0.0001
LEU 310
SER 311
0.0013
SER 311
ASP 312
-0.0002
ASP 312
GLN 313
0.0001
GLN 313
GLY 314
-0.0001
GLY 314
ALA 315
-0.0030
ALA 315
ALA 316
-0.0004
ALA 316
GLU 317
-0.0046
GLU 317
LEU 318
0.0001
LEU 318
ILE 319
0.0140
ILE 319
LEU 320
0.0003
LEU 320
GLU 321
0.0060
GLU 321
LYS 322
-0.0001
LYS 322
ASP 323
0.0066
ASP 323
LEU 324
0.0002
LEU 324
SER 325
0.0249
SER 325
GLY 326
-0.0002
GLY 326
ALA 327
-0.0055
ALA 327
SER 328
-0.0001
SER 328
LEU 329
-0.0105
LEU 329
PHE 330
0.0002
PHE 330
GLU 331
0.0032
GLU 331
LYS 332
0.0005
LYS 332
ILE 333
0.0008
ILE 333
SER 334
-0.0000
SER 334
ASP 335
0.0007
ASP 335
ILE 336
0.0001
ILE 336
MET 337
0.0078
MET 337
GLN 338
-0.0001
GLN 338
ASN 339
-0.0013
ASN 339
PRO 340
0.0002
PRO 340
ILE 341
0.0015
ILE 341
ARG 342
0.0000
ARG 342
ALA 343
0.0028
ALA 343
GLU 344
0.0002
GLU 344
HIS 345
-0.0016
HIS 345
MET 346
0.0001
MET 346
SER 347
-0.0010
SER 347
ILE 348
-0.0000
ILE 348
GLN 349
-0.0021
GLN 349
ALA 350
0.0002
ALA 350
LYS 351
0.0042
LYS 351
LYS 352
0.0003
LYS 352
LEU 353
-0.0079
LEU 353
GLY 354
-0.0003
GLY 354
GLU 355
-0.0052
GLU 355
PRO 356
-0.0002
PRO 356
GLU 357
-0.0499
GLU 357
SER 358
-0.0000
SER 358
ALA 359
0.0231
ALA 359
MET 360
-0.0000
MET 360
LEU 361
0.0401
LEU 361
ILE 362
-0.0002
ILE 362
VAL 363
0.0179
VAL 363
LYS 364
-0.0003
LYS 364
GLU 365
0.0098
GLU 365
MET 366
0.0002
MET 366
GLN 367
0.0137
GLN 367
ARG 368
0.0001
ARG 368
LEU 369
-0.0077
LEU 369
LEU 370
0.0003
LEU 370
LYS 371
0.0216
LYS 371
ASN 372
0.0001
ASN 372
SER 373
0.0130
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.