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
GLY 11
MET 12
-0.0001
MET 12
PRO 13
0.0717
PRO 13
PRO 14
-0.0001
PRO 14
PHE 15
-0.0219
PHE 15
VAL 16
-0.0002
VAL 16
VAL 17
-0.0187
VAL 17
ASP 18
-0.0001
ASP 18
PHE 19
-0.0018
PHE 19
LEU 20
-0.0001
LEU 20
MET 21
-0.0067
MET 21
GLY 22
-0.0003
GLY 22
GLY 23
0.0072
GLY 23
VAL 24
-0.0000
VAL 24
SER 25
0.0118
SER 25
ALA 26
0.0001
ALA 26
ALA 27
-0.0015
ALA 27
VAL 28
-0.0000
VAL 28
SER 29
-0.0061
SER 29
LYS 30
-0.0001
LYS 30
THR 31
-0.0280
THR 31
ALA 32
0.0000
ALA 32
ALA 33
-0.0236
ALA 33
ALA 34
0.0002
ALA 34
PRO 35
0.0611
PRO 35
ILE 36
-0.0002
ILE 36
GLU 37
0.0105
GLU 37
ARG 38
0.0003
ARG 38
ILE 39
0.0805
ILE 39
LYS 40
0.0000
LYS 40
LEU 41
-0.0098
LEU 41
LEU 42
-0.0002
LEU 42
VAL 43
-0.0473
VAL 43
GLN 44
-0.0001
GLN 44
ASN 45
0.0661
ASN 45
GLN 46
0.0001
GLN 46
ASP 47
-0.0245
ASP 47
GLU 48
-0.0003
GLU 48
MET 49
-0.0338
MET 49
ILE 50
0.0001
ILE 50
LYS 51
-0.0243
LYS 51
ALA 52
0.0000
ALA 52
GLY 53
-0.0470
GLY 53
ARG 54
0.0003
ARG 54
LEU 55
0.0434
LEU 55
ASP 56
0.0002
ASP 56
ARG 57
0.0599
ARG 57
ARG 58
0.0003
ARG 58
TYR 59
0.0567
TYR 59
ASN 60
-0.0001
ASN 60
GLY 61
0.1071
GLY 61
ILE 62
0.0002
ILE 62
ILE 63
-0.0052
ILE 63
ASP 64
-0.0005
ASP 64
CYS 65
0.0017
CYS 65
PHE 66
0.0001
PHE 66
ARG 67
0.0146
ARG 67
ARG 68
-0.0003
ARG 68
THR 69
-0.0405
THR 69
THR 70
-0.0001
THR 70
ALA 71
0.0066
ALA 71
ASP 72
0.0003
ASP 72
GLU 73
-0.0212
GLU 73
GLY 74
-0.0003
GLY 74
LEU 75
0.0006
LEU 75
MET 76
-0.0001
MET 76
ALA 77
-0.0133
ALA 77
LEU 78
-0.0003
LEU 78
TRP 79
0.0134
TRP 79
ARG 80
-0.0002
ARG 80
GLY 81
0.1146
GLY 81
ASN 82
-0.0002
ASN 82
THR 83
0.0576
THR 83
ALA 84
0.0003
ALA 84
ASN 85
0.0088
ASN 85
VAL 86
-0.0001
VAL 86
ILE 87
0.0641
ILE 87
ARG 88
0.0002
ARG 88
TYR 89
0.0157
TYR 89
PHE 90
0.0000
PHE 90
PRO 91
0.0250
PRO 91
THR 92
-0.0002
THR 92
GLN 93
0.0118
GLN 93
ALA 94
-0.0002
ALA 94
LEU 95
0.0076
LEU 95
ASN 96
-0.0002
ASN 96
PHE 97
-0.0006
PHE 97
ALA 98
0.0001
ALA 98
PHE 99
0.0154
PHE 99
ARG 100
0.0001
ARG 100
ASP 101
0.0075
ASP 101
LYS 102
-0.0000
LYS 102
PHE 103
0.1259
PHE 103
LYS 104
-0.0000
LYS 104
ALA 105
-0.1347
ALA 105
MET 106
0.0004
MET 106
PHE 107
0.0942
PHE 107
GLY 108
0.0004
GLY 108
TYR 109
0.1409
TYR 109
LYS 110
-0.0000
LYS 110
LYS 111
-0.0403
LYS 111
ASP 112
-0.0001
ASP 112
LYS 113
0.1181
LYS 113
ASP 114
0.0002
ASP 114
GLY 115
-0.0174
GLY 115
TYR 116
-0.0001
TYR 116
ALA 117
-0.0313
ALA 117
LYS 118
-0.0003
LYS 118
TRP 119
0.0835
TRP 119
MET 120
0.0002
MET 120
ALA 121
0.0368
ALA 121
GLY 122
-0.0000
GLY 122
ASN 123
-0.0204
ASN 123
LEU 124
0.0003
LEU 124
ALA 125
0.0362
ALA 125
SER 126
-0.0002
SER 126
GLY 127
-0.0114
GLY 127
GLY 128
-0.0001
GLY 128
ALA 129
0.0306
ALA 129
ALA 130
-0.0001
ALA 130
GLY 131
0.0075
GLY 131
ALA 132
0.0001
ALA 132
THR 133
0.0502
THR 133
SER 134
0.0001
SER 134
LEU 135
-0.0296
LEU 135
LEU 136
-0.0001
LEU 136
PHE 137
0.0261
PHE 137
VAL 138
0.0001
VAL 138
TYR 139
-0.0397
TYR 139
SER 140
-0.0001
SER 140
LEU 141
0.0518
LEU 141
ASP 142
-0.0001
ASP 142
TYR 143
-0.0741
TYR 143
ALA 144
0.0003
ALA 144
ARG 145
0.0954
ARG 145
THR 146
-0.0003
THR 146
ARG 147
-0.1408
ARG 147
LEU 148
-0.0001
LEU 148
ALA 149
0.1296
ALA 149
ASN 150
0.0002
ASN 150
ASP 151
-0.0542
ASP 151
ALA 152
0.0000
ALA 152
LYS 153
0.0865
LYS 153
SER 154
0.0002
SER 154
ALA 155
0.0443
ALA 155
LYS 156
0.0003
LYS 156
GLY 157
-0.0573
GLY 157
GLY 158
-0.0003
GLY 158
GLY 159
0.0502
GLY 159
ALA 160
0.0001
ALA 160
ARG 161
-0.0261
ARG 161
GLN 162
0.0001
GLN 162
PHE 163
-0.0343
PHE 163
ASN 164
0.0001
ASN 164
GLY 165
-0.0324
GLY 165
LEU 166
-0.0000
LEU 166
ILE 167
0.0819
ILE 167
ASP 168
0.0000
ASP 168
VAL 169
-0.0473
VAL 169
TYR 170
-0.0000
TYR 170
ARG 171
0.0960
ARG 171
LYS 172
-0.0004
LYS 172
THR 173
-0.0613
THR 173
LEU 174
0.0000
LEU 174
ALA 175
0.0448
ALA 175
SER 176
0.0002
SER 176
ASP 177
-0.0299
ASP 177
GLY 178
-0.0002
GLY 178
ILE 179
0.0604
ILE 179
ALA 180
-0.0000
ALA 180
GLY 181
0.0448
GLY 181
LEU 182
0.0000
LEU 182
TYR 183
-0.1105
TYR 183
ARG 184
0.0001
ARG 184
GLY 185
-0.2352
GLY 185
PHE 186
-0.0001
PHE 186
GLY 187
-0.0700
GLY 187
PRO 188
-0.0002
PRO 188
SER 189
-0.0037
SER 189
VAL 190
-0.0002
VAL 190
ALA 191
-0.0129
ALA 191
GLY 192
0.0001
GLY 192
ILE 193
0.0199
ILE 193
VAL 194
-0.0001
VAL 194
VAL 195
-0.0148
VAL 195
TYR 196
0.0000
TYR 196
ARG 197
0.0116
ARG 197
GLY 198
0.0001
GLY 198
LEU 199
0.0109
LEU 199
TYR 200
0.0003
TYR 200
PHE 201
0.0312
PHE 201
GLY 202
0.0002
GLY 202
MET 203
0.0097
MET 203
TYR 204
0.0001
TYR 204
ASP 205
0.0774
ASP 205
SER 206
-0.0001
SER 206
ILE 207
-0.0461
ILE 207
LYS 208
-0.0001
LYS 208
PRO 209
0.1357
PRO 209
VAL 210
0.0002
VAL 210
VAL 211
-0.0087
VAL 211
LEU 212
0.0002
LEU 212
VAL 213
-0.0019
VAL 213
GLY 214
-0.0000
GLY 214
PRO 215
0.0221
PRO 215
LEU 216
0.0001
LEU 216
ALA 217
-0.0071
ALA 217
ASN 218
-0.0003
ASN 218
ASN 219
-0.0128
ASN 219
PHE 220
-0.0000
PHE 220
LEU 221
-0.0175
LEU 221
ALA 222
0.0002
ALA 222
SER 223
-0.0101
SER 223
PHE 224
0.0001
PHE 224
LEU 225
-0.0131
LEU 225
LEU 226
-0.0001
LEU 226
GLY 227
0.0227
GLY 227
TRP 228
0.0001
TRP 228
CYS 229
-0.0251
CYS 229
VAL 230
-0.0003
VAL 230
THR 231
-0.0138
THR 231
THR 232
0.0001
THR 232
GLY 233
-0.0555
GLY 233
ALA 234
-0.0002
ALA 234
GLY 235
-0.0466
GLY 235
ILE 236
-0.0000
ILE 236
ALA 237
-0.0393
ALA 237
SER 238
0.0003
SER 238
TYR 239
-0.0196
TYR 239
PRO 240
0.0002
PRO 240
LEU 241
-0.0463
LEU 241
ASP 242
-0.0001
ASP 242
THR 243
-0.0183
THR 243
VAL 244
0.0001
VAL 244
ARG 245
-0.0457
ARG 245
ARG 246
-0.0000
ARG 246
ARG 247
-0.0398
ARG 247
MET 248
-0.0001
MET 248
MET 249
-0.1279
MET 249
MET 250
0.0002
MET 250
THR 251
0.1029
THR 251
SER 252
0.0003
SER 252
LYS 257
-0.1929
LYS 257
TYR 258
0.0002
TYR 258
LYS 259
0.0309
LYS 259
SER 260
0.0001
SER 260
SER 261
0.0330
SER 261
ILE 262
-0.0002
ILE 262
ASP 263
-0.0003
ASP 263
ALA 264
-0.0000
ALA 264
PHE 265
-0.0030
PHE 265
ARG 266
0.0001
ARG 266
GLN 267
0.0032
GLN 267
ILE 268
-0.0004
ILE 268
ILE 269
-0.0195
ILE 269
ALA 270
0.0002
ALA 270
LYS 271
0.0073
LYS 271
GLU 272
0.0001
GLU 272
GLY 273
0.0315
GLY 273
VAL 274
0.0003
VAL 274
LYS 275
-0.0177
LYS 275
SER 276
0.0002
SER 276
LEU 277
-0.0073
LEU 277
PHE 278
-0.0002
PHE 278
LYS 279
-0.0019
LYS 279
GLY 280
0.0001
GLY 280
ALA 281
-0.0457
ALA 281
GLY 282
-0.0003
GLY 282
ALA 283
0.0234
ALA 283
ASN 284
0.0001
ASN 284
ILE 285
-0.0007
ILE 285
LEU 286
0.0001
LEU 286
ARG 287
0.0284
ARG 287
GLY 288
-0.0000
GLY 288
VAL 289
-0.0156
VAL 289
ALA 290
0.0002
ALA 290
GLY 291
-0.0062
GLY 291
ALA 292
0.0001
ALA 292
GLY 293
-0.0136
GLY 293
VAL 294
0.0000
VAL 294
LEU 295
0.0209
LEU 295
SER 296
0.0002
SER 296
ILE 297
0.0216
ILE 297
TYR 298
0.0001
TYR 298
ASP 299
-0.0164
ASP 299
GLN 300
-0.0002
GLN 300
LEU 301
0.0093
LEU 301
LYS 302
-0.0004
LYS 302
ILE 303
-0.0410
ILE 303
LEU 304
0.0000
LEU 304
LEU 305
-0.0106
LEU 305
PHE 306
-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).
Last modification: October 18th, 2018.