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
GLU 26
MET 27
0.0000
MET 27
THR 28
0.0423
THR 28
ARG 29
0.0000
ARG 29
ILE 30
0.0205
ILE 30
GLY 31
0.0000
GLY 31
VAL 32
-0.0066
VAL 32
VAL 33
0.0000
VAL 33
ARG 34
0.0012
ARG 34
ASN 35
-0.0002
ASN 35
PRO 36
0.0083
PRO 36
LYS 37
0.0002
LYS 37
SER 38
-0.0422
SER 38
HIS 39
-0.0003
HIS 39
GLY 40
0.0328
GLY 40
ASN 41
0.0001
ASN 41
ARG 42
-0.0082
ARG 42
ILE 43
-0.0003
ILE 43
ARG 44
0.0217
ARG 44
PRO 45
-0.0001
PRO 45
PRO 46
-0.0098
PRO 46
GLY 47
0.0003
GLY 47
PRO 48
0.0281
PRO 48
ALA 49
-0.0003
ALA 49
PRO 50
-0.0279
PRO 50
GLU 51
0.0001
GLU 51
ASP 52
-0.0038
ASP 52
VAL 53
0.0001
VAL 53
ARG 54
-0.0449
ARG 54
LEU 55
0.0002
LEU 55
VAL 56
-0.0507
VAL 56
GLU 57
-0.0001
GLU 57
PRO 58
-0.0279
PRO 58
ILE 59
-0.0002
ILE 59
GLY 60
-0.0293
GLY 60
ARG 61
-0.0002
ARG 61
GLU 62
-0.0564
GLU 62
ALA 63
-0.0001
ALA 63
LEU 64
-0.0038
LEU 64
LYS 65
-0.0000
LYS 65
ALA 66
-0.0385
ALA 66
ALA 67
-0.0002
ALA 67
LEU 68
0.0040
LEU 68
ASP 69
-0.0000
ASP 69
ASP 70
-0.0399
ASP 70
PHE 71
-0.0001
PHE 71
ALA 72
-0.0110
ALA 72
ARG 73
0.0001
ARG 73
THR 74
-0.0198
THR 74
GLY 75
0.0000
GLY 75
LEU 76
0.0764
LEU 76
ASP 77
0.0004
ASP 77
LEU 78
0.0302
LEU 78
LEU 79
0.0004
LEU 79
VAL 80
0.0127
VAL 80
ILE 81
0.0001
ILE 81
ASP 82
-0.0028
ASP 82
GLY 83
0.0001
GLY 83
GLY 84
0.0334
GLY 84
ASP 85
0.0003
ASP 85
GLY 86
-0.0553
GLY 86
THR 87
0.0002
THR 87
VAL 88
0.0408
VAL 88
ARG 89
0.0002
ARG 89
ASP 90
-0.0308
ASP 90
VAL 91
0.0002
VAL 91
ILE 92
-0.0153
ILE 92
SER 93
0.0001
SER 93
LEU 94
-0.1245
LEU 94
LEU 95
0.0001
LEU 95
PRO 96
-0.0303
PRO 96
HIS 97
0.0000
HIS 97
THR 98
-0.2205
THR 98
PHE 99
-0.0002
PHE 99
GLY 100
0.0133
GLY 100
GLU 101
0.0001
GLU 101
ALA 102
-0.0643
ALA 102
THR 103
-0.0001
THR 103
PRO 104
-0.0815
PRO 104
LEU 105
0.0005
LEU 105
LEU 106
-0.0401
LEU 106
ALA 107
-0.0004
ALA 107
VAL 108
0.0365
VAL 108
LEU 109
-0.0005
LEU 109
PRO 110
0.0363
PRO 110
SER 111
0.0004
SER 111
GLY 112
0.0955
GLY 112
LYS 113
-0.0001
LYS 113
THR 114
0.0761
THR 114
ASN 115
-0.0003
ASN 115
VAL 116
0.1273
VAL 116
LEU 117
-0.0002
LEU 117
ALA 118
0.0988
ALA 118
ILE 119
-0.0002
ILE 119
ASP 120
-0.0113
ASP 120
LEU 121
0.0001
LEU 121
GLY 122
-0.0390
GLY 122
THR 123
0.0003
THR 123
SER 124
-0.0271
SER 124
GLU 125
-0.0000
GLU 125
GLY 126
0.0316
GLY 126
TRP 127
-0.0001
TRP 127
ARG 128
0.0626
ARG 128
LEU 129
-0.0003
LEU 129
GLU 130
-0.0424
GLU 130
ASP 131
0.0001
ASP 131
ALA 132
-0.0184
ALA 132
LEU 133
-0.0002
LEU 133
ARG 134
-0.0606
ARG 134
ALA 135
-0.0003
ALA 135
ALA 136
0.0342
ALA 136
ARG 137
0.0001
ARG 137
ARG 138
-0.0780
ARG 138
GLU 139
-0.0001
GLU 139
ASN 140
0.0139
ASN 140
PRO 141
0.0001
PRO 141
THR 142
0.1085
THR 142
ILE 143
0.0001
ILE 143
LYS 144
0.1239
LYS 144
SER 145
-0.0003
SER 145
ARG 146
0.0211
ARG 146
PRO 147
-0.0002
PRO 147
PRO 148
-0.0058
PRO 148
LEU 149
0.0002
LEU 149
ARG 150
0.0255
ARG 150
VAL 151
-0.0002
VAL 151
SER 152
0.0689
SER 152
TRP 153
0.0002
TRP 153
ALA 154
0.0132
ALA 154
ASP 155
0.0003
ASP 155
ASP 156
-0.0446
ASP 156
LYS 157
-0.0002
LYS 157
PRO 158
-0.1361
PRO 158
CYS 159
-0.0002
CYS 159
LEU 160
0.0602
LEU 160
GLN 161
-0.0004
GLN 161
GLY 162
0.0042
GLY 162
PHE 163
0.0003
PHE 163
PHE 164
0.0222
PHE 164
PHE 165
-0.0001
PHE 165
GLY 166
-0.0075
GLY 166
ILE 167
0.0002
ILE 167
GLY 168
0.0020
GLY 168
ALA 169
0.0002
ALA 169
PRO 170
-0.0239
PRO 170
VAL 171
-0.0001
VAL 171
LYS 172
-0.0920
LYS 172
ALA 173
-0.0004
ALA 173
THR 174
-0.0211
THR 174
ASN 175
0.0001
ASN 175
LEU 176
0.0650
LEU 176
ALA 177
-0.0001
ALA 177
GLN 178
-0.0833
GLN 178
ARG 179
0.0003
ARG 179
VAL 180
-0.0387
VAL 180
HIS 181
0.0002
HIS 181
LYS 182
0.1697
LYS 182
VAL 183
-0.0001
VAL 183
GLY 184
-0.1306
GLY 184
PHE 185
-0.0000
PHE 185
PHE 186
0.1018
PHE 186
HIS 187
0.0000
HIS 187
ASN 188
-0.0170
ASN 188
PHE 189
0.0001
PHE 189
ALA 190
-0.0659
ALA 190
VAL 191
-0.0001
VAL 191
ALA 192
0.0002
ALA 192
LEU 193
-0.0001
LEU 193
THR 194
0.2035
THR 194
ILE 195
0.0001
ILE 195
GLY 196
0.0249
GLY 196
THR 197
-0.0001
THR 197
ALA 198
0.0636
ALA 198
ALA 199
0.0002
ALA 199
LEU 200
0.0490
LEU 200
GLY 201
-0.0000
GLY 201
ALA 202
-0.0115
ALA 202
LEU 203
-0.0001
LEU 203
PHE 204
-0.0276
PHE 204
GLY 205
-0.0004
GLY 205
GLY 206
0.0661
GLY 206
SER 207
-0.0004
SER 207
ARG 208
0.0790
ARG 208
ASP 209
-0.0000
ASP 209
GLU 210
-0.0729
GLU 210
TRP 211
0.0001
TRP 211
ARG 212
0.0663
ARG 212
GLU 213
0.0001
GLU 213
GLY 214
-0.0814
GLY 214
VAL 215
0.0001
VAL 215
PRO 216
0.0928
PRO 216
ALA 217
-0.0001
ALA 217
ARG 218
0.0747
ARG 218
LEU 219
0.0000
LEU 219
VAL 220
0.0264
VAL 220
LEU 221
0.0002
LEU 221
ASP 222
-0.0105
ASP 222
GLY 223
-0.0002
GLY 223
GLU 224
-0.0099
GLU 224
ALA 225
0.0002
ALA 225
GLN 226
-0.0094
GLN 226
GLY 227
0.0004
GLY 227
GLU 228
0.0406
GLU 228
GLY 229
0.0001
GLY 229
HIS 230
0.1013
HIS 230
ARG 231
-0.0000
ARG 231
PHE 232
0.0112
PHE 232
ALA 233
-0.0000
ALA 233
VAL 234
0.0019
VAL 234
ILE 235
-0.0001
ILE 235
ALA 236
0.0107
ALA 236
THR 237
-0.0001
THR 237
ALA 238
0.0304
ALA 238
LEU 239
-0.0002
LEU 239
LYS 240
-0.0502
LYS 240
ARG 241
-0.0002
ARG 241
LEU 242
-0.1277
LEU 242
PRO 243
-0.0001
PRO 243
PHE 244
0.0402
PHE 244
GLY 245
-0.0003
GLY 245
LEU 246
-0.0097
LEU 246
LYS 247
0.0002
LYS 247
PRO 248
-0.0369
PRO 248
PHE 249
0.0001
PHE 249
GLY 250
-0.0146
GLY 250
ALA 251
0.0003
ALA 251
PRO 252
0.1473
PRO 252
ARG 253
0.0001
ARG 253
GLU 254
0.0532
GLU 254
GLY 255
-0.0003
GLY 255
LEU 256
0.0274
LEU 256
LYS 257
0.0001
LYS 257
LEU 258
0.0918
LEU 258
LEU 259
-0.0003
LEU 259
ASP 260
0.0709
ASP 260
VAL 261
0.0000
VAL 261
ASP 262
0.0326
ASP 262
ALA 263
-0.0001
ALA 263
PRO 264
0.0448
PRO 264
PRO 265
-0.0001
PRO 265
ARG 266
-0.0387
ARG 266
ARG 267
0.0005
ARG 267
LEU 268
0.0163
LEU 268
HIS 269
-0.0000
HIS 269
LYS 270
-0.0487
LYS 270
ALA 271
-0.0002
ALA 271
LEU 272
0.0188
LEU 272
PRO 273
0.0001
PRO 273
LEU 274
-0.0949
LEU 274
MET 275
-0.0000
MET 275
LEU 276
0.0982
LEU 276
SER 277
-0.0002
SER 277
GLY 278
-0.0141
GLY 278
LYS 279
0.0000
LYS 279
VAL 280
0.0807
VAL 280
VAL 281
0.0004
VAL 281
PRO 282
0.0271
PRO 282
ALA 283
0.0001
ALA 283
LEU 284
0.0022
LEU 284
GLU 285
0.0002
GLU 285
GLY 286
0.0118
GLY 286
LEU 287
-0.0002
LEU 287
GLY 288
-0.0239
GLY 288
TYR 289
-0.0000
TYR 289
ARG 290
-0.0245
ARG 290
ARG 291
-0.0001
ARG 291
ARG 292
-0.0867
ARG 292
ASP 293
0.0000
ASP 293
PRO 294
-0.0033
PRO 294
ARG 295
-0.0001
ARG 295
SER 296
0.0315
SER 296
VAL 297
-0.0000
VAL 297
LYS 298
0.0511
LYS 298
LEU 299
0.0003
LEU 299
SER 300
0.0607
SER 300
GLY 301
0.0001
GLY 301
GLY 302
-0.0027
GLY 302
ALA 303
-0.0002
ALA 303
PRO 304
-0.0385
PRO 304
PHE 305
0.0002
PHE 305
VAL 306
0.0284
VAL 306
LEU 307
0.0004
LEU 307
ASP 308
0.0479
ASP 308
GLY 309
0.0000
GLY 309
GLU 310
0.0205
GLU 310
VAL 311
-0.0000
VAL 311
TYR 312
0.0537
TYR 312
GLU 313
-0.0002
GLU 313
GLY 314
-0.0149
GLY 314
GLY 315
-0.0000
GLY 315
ASP 316
0.0643
ASP 316
LEU 317
-0.0002
LEU 317
THR 318
0.0568
THR 318
ILE 319
0.0002
ILE 319
GLN 320
0.0246
GLN 320
LEU 321
0.0004
LEU 321
GLY 322
-0.0818
GLY 322
PRO 323
-0.0001
PRO 323
ALA 324
-0.0374
ALA 324
LEU 325
-0.0003
LEU 325
ARG 326
-0.1067
ARG 326
PHE 327
0.0005
PHE 327
LEU 328
-0.0520
LEU 328
VAL 329
0.0001
VAL 329
GLY 330
-0.0252
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 25th, 2023.