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
SER 7
VAL 8
0.0001
VAL 8
TYR 9
-0.0294
TYR 9
ILE 10
-0.0001
ILE 10
THR 11
0.0001
THR 11
VAL 12
0.0001
VAL 12
GLU 13
-0.0181
GLU 13
LEU 14
0.0001
LEU 14
ALA 15
-0.0414
ALA 15
ILE 16
0.0003
ILE 16
ALA 17
-0.0029
ALA 17
VAL 18
-0.0001
VAL 18
LEU 19
-0.0741
LEU 19
ALA 20
0.0003
ALA 20
ILE 21
0.0008
ILE 21
LEU 22
0.0003
LEU 22
GLY 23
-0.0953
GLY 23
ASN 24
-0.0001
ASN 24
VAL 25
-0.0052
VAL 25
LEU 26
0.0002
LEU 26
VAL 27
0.0369
VAL 27
CYS 28
0.0003
CYS 28
TRP 29
-0.1559
TRP 29
ALA 30
-0.0001
ALA 30
VAL 31
0.0068
VAL 31
TRP 32
0.0001
TRP 32
LEU 33
-0.0183
LEU 33
ASN 34
-0.0003
ASN 34
SER 35
-0.0199
SER 35
ASN 36
0.0000
ASN 36
LEU 37
-0.0107
LEU 37
GLN 38
0.0001
GLN 38
ASN 39
0.1670
ASN 39
VAL 40
0.0002
VAL 40
THR 41
-0.0322
THR 41
ASN 42
-0.0001
ASN 42
TYR 43
-0.0297
TYR 43
PHE 44
-0.0000
PHE 44
VAL 45
0.0349
VAL 45
VAL 46
0.0002
VAL 46
SER 47
-0.1716
SER 47
LEU 48
0.0000
LEU 48
ALA 49
-0.0557
ALA 49
ALA 50
-0.0003
ALA 50
ALA 51
-0.0669
ALA 51
ASP 52
0.0001
ASP 52
ILE 53
-0.0267
ILE 53
LEU 54
0.0003
LEU 54
VAL 55
0.0139
VAL 55
GLY 56
0.0002
GLY 56
VAL 57
-0.0313
VAL 57
LEU 58
0.0001
LEU 58
ALA 59
0.0020
ALA 59
ILE 60
-0.0002
ILE 60
PRO 61
-0.0268
PRO 61
PHE 62
0.0000
PHE 62
ALA 63
-0.0099
ALA 63
ILE 64
0.0001
ILE 64
THR 65
-0.0556
THR 65
ILE 66
0.0001
ILE 66
SER 67
-0.0085
SER 67
THR 68
-0.0003
THR 68
GLY 69
-0.0023
GLY 69
PHE 70
-0.0000
PHE 70
CYS 71
-0.0531
CYS 71
ALA 72
0.0003
ALA 72
ALA 73
0.0221
ALA 73
CYS 74
-0.0001
CYS 74
HIS 75
-0.0058
HIS 75
GLY 76
0.0002
GLY 76
CYS 77
0.0030
CYS 77
LEU 78
0.0000
LEU 78
PHE 79
-0.0446
PHE 79
ILE 80
0.0002
ILE 80
ALA 81
0.0024
ALA 81
CYS 82
0.0002
CYS 82
PHE 83
-0.0497
PHE 83
VAL 84
-0.0002
VAL 84
LEU 85
0.0063
LEU 85
VAL 86
-0.0001
VAL 86
LEU 87
-0.0373
LEU 87
ALA 88
0.0000
ALA 88
GLN 89
0.0028
GLN 89
SER 90
-0.0001
SER 90
SER 91
0.0200
SER 91
ILE 92
-0.0003
ILE 92
PHE 93
-0.0717
PHE 93
SER 94
-0.0001
SER 94
LEU 95
0.0125
LEU 95
LEU 96
0.0000
LEU 96
ALA 97
-0.1145
ALA 97
ILE 98
-0.0001
ILE 98
ALA 99
0.0293
ALA 99
ILE 100
0.0003
ILE 100
ASP 101
-0.0638
ASP 101
ARG 102
-0.0003
ARG 102
TYR 103
0.0394
TYR 103
ILE 104
0.0001
ILE 104
ALA 105
-0.0450
ALA 105
ILE 106
-0.0001
ILE 106
ALA 107
-0.0108
ALA 107
ILE 108
0.0002
ILE 108
PRO 109
-0.0090
PRO 109
LEU 110
0.0000
LEU 110
ARG 111
0.0073
ARG 111
TYR 112
0.0001
TYR 112
ASN 113
-0.0245
ASN 113
GLY 114
-0.0002
GLY 114
LEU 115
-0.0089
LEU 115
VAL 116
0.0001
VAL 116
THR 117
-0.0249
THR 117
GLY 118
-0.0002
GLY 118
THR 119
-0.0119
THR 119
ARG 120
0.0000
ARG 120
ALA 121
-0.0110
ALA 121
ALA 122
-0.0003
ALA 122
GLY 123
-0.0933
GLY 123
ILE 124
-0.0001
ILE 124
ILE 125
0.0250
ILE 125
ALA 126
0.0002
ALA 126
ILE 127
-0.0250
ILE 127
CYS 128
-0.0002
CYS 128
TRP 129
0.0243
TRP 129
VAL 130
0.0001
VAL 130
LEU 131
0.0040
LEU 131
SER 132
-0.0000
SER 132
PHE 133
0.0341
PHE 133
ALA 134
-0.0003
ALA 134
ILE 135
0.0077
ILE 135
GLY 136
-0.0004
GLY 136
LEU 137
0.0136
LEU 137
THR 138
-0.0000
THR 138
PRO 139
-0.0056
PRO 139
MET 140
-0.0001
MET 140
LEU 141
-0.0038
LEU 141
GLY 142
0.0003
GLY 142
TRP 143
0.0222
TRP 143
ASN 144
-0.0000
ASN 144
ASN 145
0.0023
ASN 145
CYS 146
-0.0002
CYS 146
GLY 147
-0.0148
GLY 147
GLN 148
0.0004
GLN 148
PRO 149
-0.0185
PRO 149
GLY 158
0.0587
GLY 158
CYS 159
0.0001
CYS 159
GLY 160
-0.0810
GLY 160
GLU 161
-0.0000
GLU 161
GLY 162
0.0131
GLY 162
GLN 163
-0.0002
GLN 163
VAL 164
0.0197
VAL 164
ALA 165
0.0001
ALA 165
CYS 166
-0.0031
CYS 166
LEU 167
-0.0001
LEU 167
PHE 168
-0.0397
PHE 168
GLU 169
-0.0000
GLU 169
ASP 170
0.0133
ASP 170
VAL 171
0.0000
VAL 171
VAL 172
0.0008
VAL 172
PRO 173
0.0000
PRO 173
MET 174
-0.0022
MET 174
ASN 175
0.0002
ASN 175
TYR 176
-0.0293
TYR 176
MET 177
-0.0001
MET 177
VAL 178
-0.0061
VAL 178
TYR 179
0.0001
TYR 179
PHE 180
-0.0651
PHE 180
ASN 181
0.0000
ASN 181
PHE 182
-0.0060
PHE 182
PHE 183
-0.0002
PHE 183
ALA 184
-0.0383
ALA 184
CYS 185
0.0000
CYS 185
VAL 186
0.0244
VAL 186
LEU 187
-0.0003
LEU 187
VAL 188
-0.0656
VAL 188
PRO 189
-0.0001
PRO 189
LEU 190
0.0082
LEU 190
LEU 191
-0.0003
LEU 191
LEU 192
-0.0989
LEU 192
MET 193
-0.0004
MET 193
LEU 194
-0.0172
LEU 194
GLY 195
-0.0002
GLY 195
VAL 196
-0.0392
VAL 196
TYR 197
-0.0002
TYR 197
LEU 198
-0.0712
LEU 198
ARG 199
-0.0002
ARG 199
ILE 200
0.0127
ILE 200
PHE 201
-0.0003
PHE 201
ALA 202
-0.0783
ALA 202
ALA 203
0.0003
ALA 203
ALA 204
0.0186
ALA 204
ARG 205
0.0002
ARG 205
ARG 206
-0.0142
ARG 206
GLN 207
0.0002
GLN 207
LEU 208
-0.0262
LEU 208
LYS 209
0.0002
LYS 209
GLN 210
0.0652
GLN 210
MET 211
0.0001
MET 211
GLU 212
-0.0519
GLU 212
SER 213
-0.0003
SER 213
GLN 214
0.0433
GLN 214
PRO 215
-0.0001
PRO 215
LEU 216
0.0243
LEU 216
PRO 217
-0.0002
PRO 217
GLY 218
-0.0761
GLY 218
GLU 219
0.0000
GLU 219
ARG 220
-0.0140
ARG 220
ALA 221
-0.0002
ALA 221
ARG 222
0.0354
ARG 222
SER 223
0.0002
SER 223
THR 224
-0.0890
THR 224
LEU 225
-0.0003
LEU 225
GLN 226
-0.0581
GLN 226
LYS 227
0.0002
LYS 227
GLU 228
0.0044
GLU 228
VAL 229
0.0000
VAL 229
HIS 230
-0.0034
HIS 230
ALA 231
0.0005
ALA 231
ALA 232
0.0245
ALA 232
LYS 233
-0.0000
LYS 233
SER 234
-0.0555
SER 234
ALA 235
-0.0000
ALA 235
ALA 236
0.0058
ALA 236
ILE 237
-0.0002
ILE 237
ILE 238
-0.0229
ILE 238
ALA 239
-0.0002
ALA 239
GLY 240
-0.0675
GLY 240
LEU 241
0.0005
LEU 241
PHE 242
0.0773
PHE 242
ALA 243
0.0001
ALA 243
LEU 244
-0.0707
LEU 244
CYS 245
-0.0001
CYS 245
TRP 246
0.0564
TRP 246
LEU 247
-0.0003
LEU 247
PRO 248
-0.0752
PRO 248
LEU 249
0.0002
LEU 249
HIS 250
0.0067
HIS 250
ILE 251
-0.0000
ILE 251
ILE 252
-0.0601
ILE 252
ASN 253
0.0002
ASN 253
CYS 254
-0.0206
CYS 254
PHE 255
-0.0001
PHE 255
THR 256
-0.0186
THR 256
PHE 257
0.0000
PHE 257
PHE 258
-0.0106
PHE 258
CYS 259
-0.0000
CYS 259
PRO 260
0.0076
PRO 260
ASP 261
-0.0001
ASP 261
CYS 262
0.0222
CYS 262
SER 263
0.0001
SER 263
HIS 264
0.0125
HIS 264
ALA 265
0.0002
ALA 265
PRO 266
-0.0401
PRO 266
LEU 267
0.0001
LEU 267
TRP 268
0.0047
TRP 268
LEU 269
0.0001
LEU 269
MET 270
-0.0168
MET 270
TYR 271
-0.0003
TYR 271
LEU 272
-0.0037
LEU 272
ALA 273
0.0000
ALA 273
ILE 274
-0.0255
ILE 274
VAL 275
-0.0002
VAL 275
LEU 276
-0.1090
LEU 276
ALA 277
-0.0001
ALA 277
HIS 278
0.0051
HIS 278
THR 279
-0.0001
THR 279
ASN 280
-0.1022
ASN 280
SER 281
-0.0002
SER 281
VAL 282
0.0215
VAL 282
VAL 283
0.0002
VAL 283
ASN 284
0.0151
ASN 284
PRO 285
0.0001
PRO 285
PHE 286
-0.0294
PHE 286
ILE 287
-0.0003
ILE 287
TYR 288
0.0784
TYR 288
ALA 289
0.0001
ALA 289
TYR 290
-0.0452
TYR 290
ARG 291
-0.0001
ARG 291
ILE 292
0.0212
ILE 292
ARG 293
0.0005
ARG 293
GLU 294
-0.0556
GLU 294
PHE 295
0.0003
PHE 295
ARG 296
-0.0250
ARG 296
GLN 297
0.0000
GLN 297
THR 298
0.0204
THR 298
PHE 299
-0.0001
PHE 299
ARG 300
-0.0122
ARG 300
LYS 301
0.0004
LYS 301
ILE 302
-0.0095
ILE 302
ILE 303
0.0002
ILE 303
ARG 304
0.0110
ARG 304
SER 305
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).
Last modification: April 8th, 2025.