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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
GLN 40
VAL 41
0.0001
VAL 41
GLY 42
-0.0009
GLY 42
GLN 43
0.0001
GLN 43
ALA 44
0.0469
ALA 44
PRO 45
-0.0000
PRO 45
THR 46
-0.0565
THR 46
ALA 47
-0.0001
ALA 47
ALA 48
0.0140
ALA 48
ASN 49
-0.0001
ASN 49
ILE 50
0.0415
ILE 50
THR 51
-0.0002
THR 51
GLY 52
0.1201
GLY 52
ASP 53
-0.0003
ASP 53
GLY 54
0.1097
GLY 54
SER 55
0.0005
SER 55
PHE 56
0.0373
PHE 56
ALA 57
-0.0003
ALA 57
THR 58
0.0249
THR 58
ALA 59
-0.0003
ALA 59
SER 60
0.0553
SER 60
ALA 61
0.0005
ALA 61
PRO 62
0.0648
PRO 62
ILE 63
0.0002
ILE 63
THR 64
-0.0417
THR 64
ASN 65
-0.0001
ASN 65
GLN 66
-0.0625
GLN 66
THR 67
-0.0000
THR 67
GLY 68
-0.1798
GLY 68
PHE 69
-0.0001
PHE 69
GLY 70
0.0645
GLY 70
GLY 71
0.0004
GLY 71
GLY 72
0.0991
GLY 72
THR 73
0.0002
THR 73
VAL 74
-0.0269
VAL 74
TYR 75
0.0002
TYR 75
TYR 76
0.0519
TYR 76
PRO 77
-0.0001
PRO 77
THR 78
0.0011
THR 78
ALA 79
0.0001
ALA 79
ALA 80
0.0735
ALA 80
GLY 81
0.0000
GLY 81
THR 82
-0.0803
THR 82
TYR 83
-0.0002
TYR 83
PRO 84
-0.0825
PRO 84
VAL 85
0.0003
VAL 85
VAL 86
-0.0066
VAL 86
ALA 87
-0.0002
ALA 87
VAL 88
-0.0416
VAL 88
VAL 89
0.0003
VAL 89
PRO 90
-0.0107
PRO 90
GLY 91
-0.0002
GLY 91
PHE 92
-0.0259
PHE 92
VAL 93
0.0000
VAL 93
SER 94
0.1228
SER 94
THR 95
0.0004
THR 95
TRP 96
0.0369
TRP 96
SER 97
0.0002
SER 97
GLN 98
-0.1192
GLN 98
ILE 99
0.0002
ILE 99
SER 100
0.0568
SER 100
TRP 101
-0.0003
TRP 101
LEU 102
-0.0236
LEU 102
GLY 103
-0.0000
GLY 103
PRO 104
0.0544
PRO 104
ARG 105
0.0001
ARG 105
VAL 106
-0.0068
VAL 106
ALA 107
-0.0001
ALA 107
SER 108
0.0099
SER 108
TRP 109
0.0002
TRP 109
GLY 110
0.1159
GLY 110
PHE 111
-0.0003
PHE 111
VAL 112
-0.0230
VAL 112
VAL 113
0.0001
VAL 113
VAL 114
-0.0265
VAL 114
GLY 115
0.0005
GLY 115
ALA 116
0.0953
ALA 116
ASP 117
0.0000
ASP 117
THR 118
0.1449
THR 118
THR 119
0.0000
THR 119
SER 120
-0.2107
SER 120
GLY 121
0.0003
GLY 121
PHE 122
0.0682
PHE 122
ASP 123
-0.0001
ASP 123
SER 124
-0.0830
SER 124
PRO 125
0.0001
PRO 125
SER 126
-0.0296
SER 126
GLN 127
0.0000
GLN 127
ARG 128
0.0483
ARG 128
ALA 129
0.0001
ALA 129
ASP 130
0.0093
ASP 130
GLU 131
0.0001
GLU 131
LEU 132
-0.0538
LEU 132
LEU 133
-0.0000
LEU 133
ALA 134
0.1714
ALA 134
ALA 135
-0.0004
ALA 135
LEU 136
-0.0465
LEU 136
ASN 137
0.0002
ASN 137
TRP 138
0.1173
TRP 138
ALA 139
0.0001
ALA 139
VAL 140
0.0414
VAL 140
ASN 141
0.0001
ASN 141
SER 142
0.0716
SER 142
ALA 143
0.0001
ALA 143
PRO 144
0.0168
PRO 144
ALA 145
0.0001
ALA 145
ALA 146
-0.0463
ALA 146
VAL 147
0.0000
VAL 147
ARG 148
-0.0152
ARG 148
GLY 149
0.0000
GLY 149
LYS 150
0.0362
LYS 150
VAL 151
0.0003
VAL 151
ASP 152
0.0437
ASP 152
GLY 153
0.0001
GLY 153
THR 154
0.0461
THR 154
ARG 155
-0.0001
ARG 155
ARG 156
-0.0385
ARG 156
GLY 157
0.0001
GLY 157
VAL 158
-0.0575
VAL 158
ALA 159
0.0001
ALA 159
GLY 160
-0.0493
GLY 160
TRP 161
0.0003
TRP 161
SER 162
0.0075
SER 162
MET 163
-0.0001
MET 163
GLY 164
-0.0318
GLY 164
GLY 165
-0.0000
GLY 165
GLY 166
0.0118
GLY 166
GLY 167
0.0003
GLY 167
THR 168
-0.0485
THR 168
LEU 169
0.0001
LEU 169
GLU 170
0.0226
GLU 170
ALA 171
-0.0002
ALA 171
LEU 172
-0.0706
LEU 172
ALA 173
0.0003
ALA 173
LYS 174
-0.0022
LYS 174
ASP 175
-0.0003
ASP 175
THR 176
0.1091
THR 176
THR 177
0.0000
THR 177
GLY 178
-0.1093
GLY 178
THR 179
0.0000
THR 179
VAL 180
-0.0151
VAL 180
LYS 181
-0.0001
LYS 181
ALA 182
0.0524
ALA 182
GLY 183
-0.0004
GLY 183
VAL 184
0.0529
VAL 184
PRO 185
0.0004
PRO 185
LEU 186
-0.0358
LEU 186
ALA 187
0.0003
ALA 187
PRO 188
0.0609
PRO 188
TRP 189
-0.0002
TRP 189
ASP 190
0.0470
ASP 190
ILE 191
0.0003
ILE 191
PHE 195
-0.0545
PHE 195
SER 196
0.0005
SER 196
LYS 197
0.0135
LYS 197
VAL 198
-0.0001
VAL 198
THR 199
-0.0743
THR 199
LYS 200
0.0001
LYS 200
PRO 201
-0.0697
PRO 201
VAL 202
-0.0001
VAL 202
PHE 203
0.0059
PHE 203
ILE 204
0.0002
ILE 204
VAL 205
-0.0162
VAL 205
GLY 206
0.0003
GLY 206
ALA 207
-0.0205
ALA 207
GLN 208
0.0002
GLN 208
ASN 209
0.1341
ASN 209
ASP 210
0.0000
ASP 210
THR 211
0.0696
THR 211
ILE 212
0.0000
ILE 212
ALA 213
0.0405
ALA 213
PRO 214
0.0003
PRO 214
PRO 215
0.1455
PRO 215
ALA 216
-0.0000
ALA 216
GLN 217
-0.0186
GLN 217
HIS 218
0.0001
HIS 218
ALA 219
0.0655
ALA 219
VAL 220
-0.0002
VAL 220
PRO 221
-0.0617
PRO 221
PHE 222
-0.0001
PHE 222
TYR 223
0.0605
TYR 223
ASN 224
-0.0004
ASN 224
ALA 225
-0.0315
ALA 225
ALA 226
0.0000
ALA 226
ALA 227
0.0298
ALA 227
GLY 228
-0.0001
GLY 228
PRO 229
-0.1025
PRO 229
LYS 230
-0.0003
LYS 230
SER 231
-0.0065
SER 231
TYR 232
-0.0003
TYR 232
LEU 233
-0.0165
LEU 233
GLU 234
0.0001
GLU 234
LEU 235
0.0271
LEU 235
ALA 236
0.0003
ALA 236
GLY 237
0.0421
GLY 237
ALA 238
0.0002
ALA 238
ASP 239
-0.0632
ASP 239
HIS 240
0.0002
HIS 240
PHE 241
0.1003
PHE 241
PHE 242
0.0002
PHE 242
PRO 243
0.0438
PRO 243
THR 244
-0.0001
THR 244
THR 245
0.0253
THR 245
ALA 246
-0.0003
ALA 246
ASN 247
0.0055
ASN 247
PRO 248
-0.0001
PRO 248
THR 249
0.0765
THR 249
VAL 250
-0.0001
VAL 250
SER 251
0.2898
SER 251
ARG 252
0.0001
ARG 252
ALA 253
0.0018
ALA 253
MET 254
-0.0000
MET 254
VAL 255
0.1140
VAL 255
SER 256
0.0004
SER 256
TRP 257
-0.0675
TRP 257
LEU 258
0.0004
LEU 258
LYS 259
0.0290
LYS 259
ARG 260
-0.0002
ARG 260
PHE 261
-0.1592
PHE 261
VAL 262
-0.0002
VAL 262
SER 263
-0.0925
SER 263
SER 264
0.0001
SER 264
ASP 265
-0.0731
ASP 265
ASP 266
0.0002
ASP 266
ARG 267
-0.0222
ARG 267
PHE 268
-0.0002
PHE 268
THR 269
-0.1173
THR 269
PRO 270
-0.0002
PRO 270
PHE 271
-0.0650
PHE 271
THR 272
-0.0003
THR 272
CYS 273
0.1119
CYS 273
GLY 274
0.0003
GLY 274
PHE 275
0.2641
PHE 275
ALA 276
0.0000
ALA 276
GLY 277
0.0581
GLY 277
ALA 278
-0.0001
ALA 278
ALA 279
0.3567
ALA 279
VAL 280
-0.0001
VAL 280
SER 281
0.1772
SER 281
ALA 282
-0.0003
ALA 282
PHE 283
0.3312
PHE 283
ARG 284
-0.0002
ARG 284
SER 285
0.2616
SER 285
THR 286
-0.0000
THR 286
ALA 287
0.1848
ALA 287
CYS 288
0.0000
CYS 288
LEU 289
0.0087
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.