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
GLU 2
-0.0003
GLU 2
LEU 3
-0.0218
LEU 3
ARG 4
-0.0000
ARG 4
HIS 5
0.0074
HIS 5
THR 6
0.0001
THR 6
PRO 7
0.0384
PRO 7
ALA 8
-0.0000
ALA 8
ARG 9
-0.0178
ARG 9
ASP 10
-0.0001
ASP 10
LEU 11
0.0137
LEU 11
ASP 12
-0.0003
ASP 12
LYS 13
0.0495
LYS 13
PHE 14
0.0002
PHE 14
ILE 15
0.0229
ILE 15
GLU 16
-0.0003
GLU 16
ASP 17
0.0077
ASP 17
HIS 18
0.0002
HIS 18
LEU 19
-0.0095
LEU 19
LEU 20
-0.0004
LEU 20
PRO 21
0.0291
PRO 21
ASN 22
-0.0000
ASN 22
THR 23
0.0033
THR 23
CYS 24
-0.0001
CYS 24
PHE 25
-0.0315
PHE 25
ARG 26
-0.0001
ARG 26
THR 27
0.0246
THR 27
GLN 28
0.0002
GLN 28
VAL 29
-0.0042
VAL 29
LYS 30
-0.0002
LYS 30
GLU 31
-0.0168
GLU 31
ALA 32
0.0000
ALA 32
ILE 33
-0.0127
ILE 33
ASP 34
-0.0003
ASP 34
ILE 35
-0.0596
ILE 35
VAL 36
-0.0001
VAL 36
CYS 37
-0.0085
CYS 37
ARG 38
0.0001
ARG 38
PHE 39
-0.1086
PHE 39
LEU 40
-0.0000
LEU 40
LYS 41
-0.0114
LYS 41
GLU 42
-0.0001
GLU 42
ARG 43
-0.1514
ARG 43
CYS 44
-0.0004
CYS 44
PHE 45
0.0021
PHE 45
GLN 46
-0.0000
GLN 46
GLY 47
-0.0030
GLY 47
THR 48
0.0000
THR 48
ALA 49
0.0061
ALA 49
ASP 50
-0.0000
ASP 50
PRO 51
-0.0036
PRO 51
VAL 52
0.0003
VAL 52
ARG 53
-0.0040
ARG 53
VAL 54
0.0001
VAL 54
SER 55
-0.0363
SER 55
LYS 56
-0.0001
LYS 56
VAL 57
0.0137
VAL 57
VAL 58
0.0000
VAL 58
LYS 59
0.0352
LYS 59
GLY 60
-0.0001
GLY 60
GLY 61
0.1028
GLY 61
SER 62
0.0001
SER 62
SER 63
0.0527
SER 63
GLY 64
-0.0002
GLY 64
LYS 65
0.0010
LYS 65
GLY 66
-0.0002
GLY 66
THR 67
0.0496
THR 67
THR 68
0.0003
THR 68
LEU 69
0.0245
LEU 69
ARG 70
0.0002
ARG 70
GLY 71
0.0718
GLY 71
ARG 72
-0.0002
ARG 72
SER 73
0.2245
SER 73
ASP 74
0.0002
ASP 74
ALA 75
-0.0064
ALA 75
ASP 76
-0.0002
ASP 76
LEU 77
0.0167
LEU 77
VAL 78
-0.0003
VAL 78
VAL 79
0.0316
VAL 79
PHE 80
0.0003
PHE 80
LEU 81
0.0047
LEU 81
THR 82
-0.0001
THR 82
LYS 83
0.0107
LYS 83
LEU 84
-0.0000
LEU 84
THR 85
-0.0088
THR 85
SER 86
0.0002
SER 86
PHE 87
0.0088
PHE 87
GLU 88
-0.0004
GLU 88
ASP 89
0.0360
ASP 89
GLN 90
0.0001
GLN 90
LEU 91
-0.0090
LEU 91
ARG 92
-0.0000
ARG 92
ARG 93
0.0262
ARG 93
ARG 94
0.0001
ARG 94
GLY 95
-0.0051
GLY 95
GLU 96
-0.0004
GLU 96
PHE 97
-0.0163
PHE 97
ILE 98
0.0001
ILE 98
GLN 99
0.0243
GLN 99
GLU 100
-0.0001
GLU 100
ILE 101
0.0103
ILE 101
ARG 102
-0.0001
ARG 102
ARG 103
-0.0026
ARG 103
GLN 104
-0.0000
GLN 104
LEU 105
0.0186
LEU 105
GLU 106
0.0002
GLU 106
ALA 107
-0.0053
ALA 107
CYS 108
-0.0001
CYS 108
GLN 109
-0.0132
GLN 109
ARG 110
0.0000
ARG 110
GLU 111
0.0167
GLU 111
GLN 112
-0.0003
GLN 112
LYS 113
-0.0160
LYS 113
PHE 114
0.0001
PHE 114
LYS 115
-0.0062
LYS 115
VAL 116
-0.0002
VAL 116
THR 117
-0.0374
THR 117
PHE 118
-0.0002
PHE 118
GLU 119
-0.0572
GLU 119
VAL 120
0.0003
VAL 120
GLN 121
-0.0224
GLN 121
SER 122
-0.0002
SER 122
PRO 123
-0.0472
PRO 123
ARG 124
0.0000
ARG 124
ARG 125
-0.0673
ARG 125
GLU 126
-0.0002
GLU 126
ASN 127
0.0727
ASN 127
PRO 128
0.0004
PRO 128
ARG 129
0.0684
ARG 129
ALA 130
0.0001
ALA 130
LEU 131
-0.0336
LEU 131
SER 132
0.0002
SER 132
PHE 133
-0.0547
PHE 133
VAL 134
-0.0001
VAL 134
LEU 135
-0.0265
LEU 135
SER 136
-0.0001
SER 136
SER 137
-0.0251
SER 137
PRO 138
0.0000
PRO 138
GLN 139
-0.0208
GLN 139
LEU 140
0.0005
LEU 140
GLN 141
0.0088
GLN 141
GLN 142
-0.0001
GLN 142
GLU 143
-0.0688
GLU 143
VAL 144
-0.0003
VAL 144
GLU 145
-0.0624
GLU 145
PHE 146
-0.0004
PHE 146
ASP 147
-0.0542
ASP 147
VAL 148
0.0001
VAL 148
LEU 149
-0.0338
LEU 149
PRO 150
-0.0005
PRO 150
ALA 151
-0.0168
ALA 151
PHE 152
-0.0002
PHE 152
ASP 153
-0.0010
ASP 153
ALA 154
0.0002
ALA 154
LEU 155
-0.0132
LEU 155
GLY 156
-0.0001
GLY 156
GLN 157
0.0487
GLN 157
TRP 158
-0.0001
TRP 158
THR 159
-0.0222
THR 159
PRO 160
-0.0001
PRO 160
GLY 161
-0.0065
GLY 161
TYR 162
0.0001
TYR 162
LYS 163
0.0044
LYS 163
PRO 164
0.0002
PRO 164
ASN 165
0.0262
ASN 165
PRO 166
0.0000
PRO 166
GLU 167
-0.0202
GLU 167
ILE 168
0.0000
ILE 168
TYR 169
-0.0001
TYR 169
VAL 170
-0.0001
VAL 170
GLN 171
-0.0780
GLN 171
LEU 172
-0.0001
LEU 172
ILE 173
-0.0093
ILE 173
LYS 174
0.0000
LYS 174
GLU 175
-0.0205
GLU 175
CYS 176
0.0002
CYS 176
LYS 177
0.0174
LYS 177
SER 178
0.0001
SER 178
ARG 179
-0.0170
ARG 179
GLY 180
-0.0001
GLY 180
LYS 181
-0.0221
LYS 181
GLU 182
0.0000
GLU 182
GLY 183
-0.0124
GLY 183
GLU 184
0.0000
GLU 184
PHE 185
-0.0195
PHE 185
SER 186
-0.0002
SER 186
THR 187
0.0491
THR 187
CYS 188
-0.0005
CYS 188
PHE 189
0.0050
PHE 189
THR 190
-0.0004
THR 190
GLU 191
0.0264
GLU 191
LEU 192
0.0003
LEU 192
GLN 193
0.0244
GLN 193
ARG 194
-0.0002
ARG 194
ASP 195
0.0121
ASP 195
PHE 196
-0.0001
PHE 196
LEU 197
0.0263
LEU 197
ARG 198
0.0003
ARG 198
ASN 199
-0.0236
ASN 199
ARG 200
0.0002
ARG 200
PRO 201
0.0428
PRO 201
THR 202
0.0001
THR 202
LYS 203
-0.0576
LYS 203
LEU 204
-0.0000
LEU 204
LYS 205
0.0014
LYS 205
SER 206
0.0004
SER 206
LEU 207
0.0033
LEU 207
ILE 208
-0.0002
ILE 208
ARG 209
-0.0078
ARG 209
LEU 210
-0.0001
LEU 210
VAL 211
-0.0260
VAL 211
LYS 212
0.0001
LYS 212
HIS 213
-0.0015
HIS 213
TRP 214
0.0002
TRP 214
TYR 215
-0.0390
TYR 215
GLN 216
0.0001
GLN 216
THR 217
0.0727
THR 217
CYS 218
0.0001
CYS 218
LYS 219
-0.0249
LYS 219
LYS 220
-0.0001
LYS 220
THR 221
0.0035
THR 221
HIS 222
-0.0004
HIS 222
GLY 223
-0.0082
GLY 223
ASN 224
-0.0001
ASN 224
LYS 225
-0.0232
LYS 225
LEU 226
0.0001
LEU 226
PRO 227
0.0272
PRO 227
PRO 228
-0.0002
PRO 228
GLN 229
-0.0467
GLN 229
TYR 230
-0.0001
TYR 230
ALA 231
0.0207
ALA 231
LEU 232
0.0003
LEU 232
GLU 233
0.0262
GLU 233
LEU 234
-0.0002
LEU 234
LEU 235
0.0162
LEU 235
THR 236
-0.0001
THR 236
VAL 237
-0.0278
VAL 237
TYR 238
0.0000
TYR 238
ALA 239
-0.0211
ALA 239
TRP 240
-0.0002
TRP 240
GLU 241
0.0124
GLU 241
GLN 242
-0.0001
GLN 242
GLY 243
-0.0117
GLY 243
SER 244
0.0000
SER 244
ARG 245
-0.0410
ARG 245
LYS 246
0.0000
LYS 246
THR 247
-0.0100
THR 247
ASP 248
0.0002
ASP 248
PHE 249
-0.1428
PHE 249
SER 250
-0.0005
SER 250
THR 251
0.0197
THR 251
ALA 252
-0.0001
ALA 252
GLN 253
0.0374
GLN 253
GLY 254
0.0003
GLY 254
PHE 255
-0.0278
PHE 255
GLN 256
-0.0001
GLN 256
THR 257
-0.0009
THR 257
VAL 258
-0.0002
VAL 258
LEU 259
-0.0206
LEU 259
GLU 260
0.0001
GLU 260
LEU 261
0.0035
LEU 261
VAL 262
-0.0002
VAL 262
LEU 263
0.0065
LEU 263
LYS 264
-0.0001
LYS 264
HIS 265
0.0197
HIS 265
GLN 266
0.0004
GLN 266
LYS 267
-0.0305
LYS 267
LEU 268
0.0004
LEU 268
CYS 269
-0.0830
CYS 269
ILE 270
0.0002
ILE 270
PHE 271
-0.1035
PHE 271
TRP 272
0.0000
TRP 272
GLU 273
-0.0881
GLU 273
ALA 274
-0.0002
ALA 274
TYR 275
-0.0344
TYR 275
TYR 276
0.0001
TYR 276
ASP 277
0.0182
ASP 277
PHE 278
0.0000
PHE 278
THR 279
-0.0374
THR 279
ASN 280
-0.0000
ASN 280
PRO 281
0.0029
PRO 281
VAL 282
0.0002
VAL 282
VAL 283
0.0107
VAL 283
GLY 284
0.0000
GLY 284
ARG 285
0.0303
ARG 285
CYS 286
-0.0003
CYS 286
MET 287
0.0137
MET 287
LEU 288
0.0002
LEU 288
GLN 289
-0.0064
GLN 289
GLN 290
-0.0001
GLN 290
LEU 291
0.0610
LEU 291
LYS 292
-0.0001
LYS 292
LYS 293
-0.0596
LYS 293
PRO 294
0.0001
PRO 294
ARG 295
0.0306
ARG 295
PRO 296
-0.0002
PRO 296
VAL 297
-0.0094
VAL 297
ILE 298
-0.0001
ILE 298
LEU 299
0.0133
LEU 299
ASP 300
-0.0001
ASP 300
PRO 301
0.0075
PRO 301
ALA 302
-0.0001
ALA 302
ASP 303
-0.0056
ASP 303
PRO 304
-0.0004
PRO 304
THR 305
0.0170
THR 305
GLY 306
-0.0001
GLY 306
ASN 307
0.1876
ASN 307
VAL 308
0.0000
VAL 308
GLY 309
0.0807
GLY 309
GLY 310
0.0003
GLY 310
GLY 311
-0.0575
GLY 311
ASP 312
-0.0002
ASP 312
THR 313
0.0203
THR 313
HIS 314
0.0001
HIS 314
SER 315
0.0126
SER 315
TRP 316
0.0001
TRP 316
GLN 317
0.0134
GLN 317
ARG 318
0.0003
ARG 318
LEU 319
-0.0044
LEU 319
ALA 320
-0.0001
ALA 320
GLN 321
-0.0019
GLN 321
GLU 322
0.0000
GLU 322
ALA 323
-0.0211
ALA 323
ARG 324
-0.0002
ARG 324
VAL 325
0.0056
VAL 325
TRP 326
-0.0002
TRP 326
LEU 327
0.0055
LEU 327
GLY 328
-0.0005
GLY 328
TYR 329
0.0022
TYR 329
PRO 330
-0.0003
PRO 330
CYS 331
0.0043
CYS 331
CYS 332
0.0001
CYS 332
LYS 333
0.0029
LYS 333
ASN 334
-0.0004
ASN 334
LEU 335
-0.0106
LEU 335
ASP 336
-0.0000
ASP 336
GLY 337
0.0239
GLY 337
SER 338
-0.0002
SER 338
LEU 339
-0.0109
LEU 339
VAL 340
0.0001
VAL 340
GLY 341
0.0040
GLY 341
ALA 342
0.0003
ALA 342
TRP 343
-0.0301
TRP 343
THR 344
-0.0001
THR 344
MET 345
0.0093
MET 345
LEU 346
0.0003
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 8th, 2025.