Should you encounter any unexpected behaviour,
please let us know. elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.
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
THR 20
THR 21
-0.0002
THR 21
MET 22
0.0025
MET 22
ALA 23
-0.0004
ALA 23
SER 24
-0.0510
SER 24
PRO 25
0.0001
PRO 25
GLN 26
0.0036
GLN 26
LEU 27
-0.0001
LEU 27
MET 28
-0.0101
MET 28
PRO 29
-0.0001
PRO 29
LEU 30
0.0008
LEU 30
VAL 31
0.0000
VAL 31
VAL 32
0.0572
VAL 32
VAL 33
-0.0000
VAL 33
LEU 34
-0.0175
LEU 34
SER 35
-0.0001
SER 35
THR 36
-0.0352
THR 36
ILE 37
0.0001
ILE 37
CYS 38
0.0376
CYS 38
LEU 39
0.0004
LEU 39
VAL 40
-0.1132
VAL 40
THR 41
0.0001
THR 41
VAL 42
0.0297
VAL 42
GLY 43
-0.0001
GLY 43
LEU 44
-0.0663
LEU 44
ASN 45
-0.0002
ASN 45
LEU 46
0.0593
LEU 46
LEU 47
-0.0001
LEU 47
VAL 48
0.0299
VAL 48
LEU 49
-0.0002
LEU 49
TYR 50
-0.0251
TYR 50
ALA 51
-0.0005
ALA 51
VAL 52
0.0062
VAL 52
ARG 53
0.0001
ARG 53
SER 54
-0.0187
SER 54
GLU 55
-0.0004
GLU 55
ARG 56
-0.0139
ARG 56
LYS 57
0.0007
LYS 57
LEU 58
-0.0018
LEU 58
HIS 59
-0.0001
HIS 59
THR 60
-0.0321
THR 60
VAL 61
0.0001
VAL 61
GLY 62
0.0221
GLY 62
ASN 63
0.0002
ASN 63
LEU 64
0.0169
LEU 64
TYR 65
-0.0001
TYR 65
ILE 66
0.0055
ILE 66
VAL 67
-0.0003
VAL 67
SER 68
-0.0291
SER 68
LEU 69
0.0002
LEU 69
SER 70
0.0242
SER 70
VAL 71
0.0001
VAL 71
ALA 72
-0.0523
ALA 72
ASP 73
0.0002
ASP 73
LEU 74
0.0279
LEU 74
ILE 75
0.0002
ILE 75
VAL 76
-0.0254
VAL 76
GLY 77
-0.0003
GLY 77
ALA 78
0.0222
ALA 78
VAL 79
-0.0001
VAL 79
VAL 80
0.0070
VAL 80
MET 81
-0.0002
MET 81
PRO 82
-0.0166
PRO 82
MET 83
0.0004
MET 83
ASN 84
0.0657
ASN 84
ILE 85
0.0002
ILE 85
LEU 86
-0.0029
LEU 86
TYR 87
0.0002
TYR 87
LEU 88
0.0335
LEU 88
LEU 89
0.0003
LEU 89
MET 90
0.0067
MET 90
SER 91
-0.0000
SER 91
LYS 92
-0.0519
LYS 92
TRP 93
-0.0001
TRP 93
SER 94
-0.0131
SER 94
LEU 95
0.0003
LEU 95
GLY 96
-0.0166
GLY 96
ARG 97
-0.0002
ARG 97
PRO 98
-0.0234
PRO 98
LEU 99
0.0002
LEU 99
CYS 100
0.0305
CYS 100
LEU 101
0.0003
LEU 101
PHE 102
-0.0815
PHE 102
TRP 103
-0.0002
TRP 103
LEU 104
-0.0195
LEU 104
SER 105
-0.0003
SER 105
MET 106
-0.0762
MET 106
ASP 107
0.0002
ASP 107
TYR 108
-0.0264
TYR 108
VAL 109
-0.0000
VAL 109
ALA 110
-0.0233
ALA 110
SER 111
0.0001
SER 111
THR 112
0.0015
THR 112
ALA 113
-0.0000
ALA 113
SER 114
0.0049
SER 114
ILE 115
0.0003
ILE 115
PHE 116
-0.0147
PHE 116
SER 117
0.0002
SER 117
VAL 118
-0.0022
VAL 118
PHE 119
0.0001
PHE 119
ILE 120
-0.0086
ILE 120
LEU 121
0.0000
LEU 121
CYS 122
-0.0091
CYS 122
ILE 123
0.0001
ILE 123
ASP 124
0.0210
ASP 124
ARG 125
0.0002
ARG 125
TYR 126
-0.0215
TYR 126
ARG 127
-0.0000
ARG 127
SER 128
0.0106
SER 128
VAL 129
0.0001
VAL 129
GLN 130
-0.1001
GLN 130
GLN 131
-0.0001
GLN 131
PRO 132
0.0281
PRO 132
LEU 133
-0.0000
LEU 133
ARG 134
0.0145
ARG 134
TYR 135
-0.0003
TYR 135
LEU 136
-0.0098
LEU 136
LYS 137
0.0001
LYS 137
TYR 138
-0.0065
TYR 138
ARG 139
0.0002
ARG 139
THR 140
0.0254
THR 140
LYS 141
-0.0001
LYS 141
THR 142
0.0189
THR 142
ARG 143
-0.0002
ARG 143
ALA 144
0.0108
ALA 144
SER 145
0.0001
SER 145
ALA 146
0.0102
ALA 146
THR 147
0.0002
THR 147
ILE 148
0.0396
ILE 148
LEU 149
-0.0001
LEU 149
GLY 150
-0.0027
GLY 150
ALA 151
-0.0001
ALA 151
TRP 152
0.0265
TRP 152
PHE 153
0.0000
PHE 153
LEU 154
-0.0188
LEU 154
SER 155
0.0005
SER 155
PHE 156
0.0410
PHE 156
LEU 157
0.0002
LEU 157
TRP 158
-0.0495
TRP 158
VAL 159
0.0001
VAL 159
ILE 160
-0.0129
ILE 160
PRO 161
-0.0003
PRO 161
ILE 162
-0.0098
ILE 162
LEU 163
0.0003
LEU 163
GLY 164
-0.0605
GLY 164
TRP 165
-0.0003
TRP 165
ASN 166
0.0454
ASN 166
HIS 167
0.0000
HIS 167
PHE 168
0.0050
PHE 168
MET 169
-0.0004
MET 169
GLN 170
0.0601
GLN 170
GLN 171
0.0001
GLN 171
VAL 174
-0.0720
VAL 174
ARG 175
0.0001
ARG 175
ARG 176
-0.0134
ARG 176
GLU 177
-0.0000
GLU 177
ASP 178
-0.0178
ASP 178
LYS 179
-0.0001
LYS 179
CYS 180
0.0207
CYS 180
GLU 181
-0.0004
GLU 181
THR 182
0.0480
THR 182
ASP 183
-0.0003
ASP 183
PHE 184
0.0591
PHE 184
TYR 185
0.0001
TYR 185
ASP 186
-0.0569
ASP 186
VAL 187
0.0001
VAL 187
THR 188
0.0214
THR 188
TRP 189
0.0001
TRP 189
PHE 190
-0.0924
PHE 190
LYS 191
0.0002
LYS 191
VAL 192
0.0759
VAL 192
MET 193
-0.0003
MET 193
THR 194
-0.0926
THR 194
ALA 195
-0.0001
ALA 195
ILE 196
0.0274
ILE 196
ILE 197
-0.0001
ILE 197
ASN 198
-0.0521
ASN 198
PHE 199
-0.0001
PHE 199
TYR 200
-0.0146
TYR 200
LEU 201
0.0001
LEU 201
PRO 202
0.0188
PRO 202
THR 203
-0.0004
THR 203
LEU 204
-0.0580
LEU 204
LEU 205
-0.0001
LEU 205
MET 206
-0.0009
MET 206
LEU 207
0.0000
LEU 207
TRP 208
-0.0145
TRP 208
PHE 209
-0.0003
PHE 209
TYR 210
-0.0242
TYR 210
ALA 211
-0.0000
ALA 211
LYS 212
-0.0231
LYS 212
ILE 213
-0.0002
ILE 213
TYR 214
-0.0287
TYR 214
LYS 215
-0.0001
LYS 215
ALA 216
-0.0343
ALA 216
VAL 217
-0.0001
VAL 217
LYS 218
-0.0290
LYS 218
ARG 219
0.0001
ARG 219
GLN 220
-0.0106
GLN 220
LEU 221
-0.0002
LEU 221
ASN 408
-0.0290
ASN 408
ARG 409
0.0003
ARG 409
GLU 410
-0.0030
GLU 410
ARG 411
-0.0000
ARG 411
LYS 412
-0.0886
LYS 412
ALA 413
0.0004
ALA 413
ALA 414
0.0030
ALA 414
LYS 415
0.0003
LYS 415
GLN 416
-0.0203
GLN 416
LEU 417
-0.0001
LEU 417
GLY 418
0.0236
GLY 418
PHE 419
-0.0002
PHE 419
ILE 420
0.0100
ILE 420
MET 421
0.0002
MET 421
ALA 422
-0.0099
ALA 422
ALA 423
0.0001
ALA 423
PHE 424
0.0311
PHE 424
ILE 425
-0.0003
ILE 425
LEU 426
-0.0435
LEU 426
CYS 427
0.0003
CYS 427
TRP 428
-0.0018
TRP 428
ILE 429
0.0001
ILE 429
PRO 430
0.0400
PRO 430
TYR 431
-0.0000
TYR 431
PHE 432
0.0119
PHE 432
ILE 433
0.0000
ILE 433
PHE 434
0.0553
PHE 434
PHE 435
-0.0002
PHE 435
MET 436
-0.0009
MET 436
VAL 437
-0.0002
VAL 437
ILE 438
0.0327
ILE 438
ALA 439
0.0001
ALA 439
PHE 440
-0.0077
PHE 440
CYS 441
-0.0002
CYS 441
LYS 442
0.0127
LYS 442
ASN 443
-0.0001
ASN 443
CYS 444
0.0033
CYS 444
CYS 445
-0.0003
CYS 445
ASN 446
-0.0216
ASN 446
GLU 447
0.0001
GLU 447
HIS 448
-0.0014
HIS 448
LEU 449
0.0001
LEU 449
HIS 450
-0.0150
HIS 450
MET 451
0.0002
MET 451
PHE 452
0.0428
PHE 452
THR 453
-0.0001
THR 453
ILE 454
-0.0010
ILE 454
TRP 455
0.0001
TRP 455
LEU 456
0.0551
LEU 456
GLY 457
0.0002
GLY 457
TYR 458
-0.0048
TYR 458
ILE 459
0.0002
ILE 459
ASN 460
-0.0246
ASN 460
SER 461
0.0002
SER 461
THR 462
0.0057
THR 462
LEU 463
-0.0002
LEU 463
ASN 464
-0.0094
ASN 464
PRO 465
-0.0002
PRO 465
LEU 466
0.0088
LEU 466
ILE 467
-0.0003
ILE 467
TYR 468
0.0731
TYR 468
PRO 469
-0.0002
PRO 469
LEU 470
-0.0280
LEU 470
CYS 471
-0.0002
CYS 471
ASN 472
0.0909
ASN 472
GLU 473
-0.0001
GLU 473
ASN 474
-0.0078
ASN 474
PHE 475
-0.0001
PHE 475
LYS 476
-0.0012
LYS 476
LYS 477
0.0003
LYS 477
THR 478
-0.0450
THR 478
PHE 479
0.0000
PHE 479
LYS 480
-0.0364
LYS 480
ARG 481
-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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: december 26th, 2025.