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
LYS 2
-0.0001
LYS 2
ASN 3
0.0001
ASN 3
GLY 4
0.0678
GLY 4
PHE 5
0.0001
PHE 5
TYR 6
0.0002
TYR 6
ALA 7
0.0087
ALA 7
THR 8
-0.0001
THR 8
TYR 9
0.0003
TYR 9
ARG 10
0.0132
ARG 10
SER 11
-0.0003
SER 11
LYS 12
0.0003
LYS 12
ASN 13
0.0144
ASN 13
LYS 14
-0.0002
LYS 14
GLY 15
-0.0001
GLY 15
LYS 16
0.0241
LYS 16
ASP 17
-0.0002
ASP 17
LYS 18
0.0004
LYS 18
ARG 19
-0.0513
ARG 19
SER 20
0.0002
SER 20
ILE 21
-0.0003
ILE 21
ASN 22
-0.0181
ASN 22
LEU 23
-0.0000
LEU 23
SER 24
-0.0002
SER 24
VAL 25
0.0552
VAL 25
PHE 26
-0.0003
PHE 26
LEU 27
0.0001
LEU 27
ASN 28
0.0028
ASN 28
SER 29
-0.0002
SER 29
LEU 30
-0.0001
LEU 30
ASN 34
-0.0218
ASN 34
HIS 35
0.0002
HIS 35
HIS 36
0.0000
HIS 36
LEU 37
0.0045
LEU 37
GLN 38
0.0001
GLN 38
VAL 39
-0.0004
VAL 39
GLY 40
0.0067
GLY 40
SER 41
0.0001
SER 41
ASN 42
-0.0001
ASN 42
TYR 43
0.0091
TYR 43
LEU 44
0.0002
LEU 44
TYR 45
-0.0004
TYR 45
ILE 46
0.0393
ILE 46
HIS 47
0.0005
HIS 47
LYS 48
-0.0003
LYS 48
ILE 49
0.0116
ILE 49
ASP 50
-0.0002
ASP 50
GLY 51
0.0004
GLY 51
LYS 52
-0.0342
LYS 52
THR 53
-0.0000
THR 53
PHE 54
0.0002
PHE 54
LEU 55
0.0006
LEU 55
PHE 56
0.0002
PHE 56
THR 57
-0.0004
THR 57
LYS 58
0.0115
LYS 58
THR 59
0.0002
THR 59
ASN 60
-0.0001
ASN 60
ASP 61
-0.0043
ASP 61
LYS 62
0.0002
LYS 62
SER 63
-0.0004
SER 63
LEU 64
0.0013
LEU 64
VAL 65
0.0000
VAL 65
GLN 66
0.0001
GLN 66
LYS 67
0.0038
LYS 67
ILE 68
-0.0000
ILE 68
ASN 69
0.0000
ASN 69
ARG 70
-0.0175
ARG 70
SER 71
-0.0001
SER 71
LYS 72
0.0002
LYS 72
ALA 73
0.0276
ALA 73
SER 74
-0.0002
SER 74
VAL 75
0.0001
VAL 75
GLU 76
-0.0087
GLU 76
ASP 77
0.0001
ASP 77
ILE 78
0.0002
ILE 78
LYS 79
0.0159
LYS 79
ASN 80
-0.0001
ASN 80
SER 81
-0.0001
SER 81
LEU 82
-0.0193
LEU 82
ALA 83
0.0000
ALA 83
ASP 84
0.0004
ASP 84
ASP 85
-0.0079
ASP 85
GLU 86
0.0003
GLU 86
SER 87
0.0000
SER 87
LEU 88
-0.0060
LEU 88
GLY 89
0.0001
GLY 89
PHE 90
0.0000
PHE 90
PRO 91
0.0075
PRO 91
SER 92
0.0003
SER 92
PHE 93
-0.0002
PHE 93
LEU 94
-0.0048
LEU 94
PHE 95
-0.0001
PHE 95
VAL 96
-0.0003
VAL 96
GLU 97
-0.0173
GLU 97
GLY 98
-0.0000
GLY 98
ASP 99
-0.0001
ASP 99
THR 100
0.0350
THR 100
ILE 101
0.0003
ILE 101
GLY 102
-0.0003
GLY 102
PHE 103
0.0277
PHE 103
ALA 104
-0.0002
ALA 104
ARG 105
0.0002
ARG 105
THR 106
0.0218
THR 106
VAL 107
0.0002
VAL 107
PHE 108
-0.0001
PHE 108
GLY 109
0.0125
GLY 109
PRO 110
0.0002
PRO 110
THR 111
0.0000
THR 111
THR 112
0.0308
THR 112
SER 113
0.0001
SER 113
ASP 114
0.0000
ASP 114
LEU 115
0.0133
LEU 115
THR 116
0.0001
THR 116
ASP 117
0.0001
ASP 117
PHE 118
-0.0039
PHE 118
LEU 119
-0.0002
LEU 119
ILE 120
-0.0000
ILE 120
GLY 121
-0.0027
GLY 121
LYS 122
-0.0001
LYS 122
GLY 123
0.0001
GLY 123
MET 124
-0.0535
MET 124
SER 125
0.0002
SER 125
LEU 126
-0.0001
LEU 126
SER 127
0.0221
SER 127
SER 128
-0.0001
SER 128
GLY 129
-0.0003
GLY 129
GLU 130
-0.0057
GLU 130
ARG 131
-0.0005
ARG 131
VAL 132
0.0001
VAL 132
GLN 133
-0.0837
GLN 133
ILE 134
-0.0001
ILE 134
GLU 135
0.0000
GLU 135
PRO 136
-0.1351
PRO 136
LEU 137
-0.0002
LEU 137
MET 138
0.0000
MET 138
ARG 139
0.0663
ARG 139
GLY 140
0.0002
GLY 140
THR 141
-0.0000
THR 141
THR 142
-0.0401
THR 142
LYS 143
0.0000
LYS 143
ASP 144
0.0003
ASP 144
ASP 145
0.0133
ASP 145
VAL 146
-0.0003
VAL 146
MET 147
0.0004
MET 147
HIS 148
-0.0027
HIS 148
MET 149
0.0001
MET 149
HIS 150
-0.0001
HIS 150
PHE 151
0.0358
PHE 151
ILE 152
0.0005
ILE 152
GLY 153
0.0001
GLY 153
ARG 154
0.1082
ARG 154
THR 155
-0.0001
THR 155
THR 156
0.0003
THR 156
VAL 157
-0.0434
VAL 157
LYS 158
-0.0004
LYS 158
VAL 159
0.0000
VAL 159
GLU 160
-0.0174
GLU 160
ALA 161
-0.0001
ALA 161
LYS 162
0.0001
LYS 162
LEU 163
-0.0290
LEU 163
PRO 164
-0.0001
PRO 164
VAL 165
-0.0001
VAL 165
PHE 166
-0.0901
PHE 166
GLY 167
0.0001
GLY 167
ASP 168
0.0001
ASP 168
ILE 169
0.0290
ILE 169
LEU 170
0.0001
LEU 170
LYS 171
0.0002
LYS 171
VAL 172
-0.0140
VAL 172
LEU 173
-0.0000
LEU 173
GLY 174
-0.0000
GLY 174
ALA 175
0.0048
ALA 175
THR 176
-0.0002
THR 176
ASP 177
0.0002
ASP 177
ILE 178
0.0205
ILE 178
GLU 179
-0.0003
GLU 179
GLY 180
0.0001
GLY 180
GLU 181
-0.0084
GLU 181
LEU 182
0.0002
LEU 182
PHE 183
0.0002
PHE 183
ASP 184
0.1458
ASP 184
SER 185
0.0000
SER 185
LEU 186
-0.0001
LEU 186
ASP 187
0.0213
ASP 187
ILE 188
-0.0000
ILE 188
VAL 189
-0.0000
VAL 189
ILE 190
0.0555
ILE 190
LYS 191
0.0000
LYS 191
PRO 192
-0.0002
PRO 192
LYS 193
0.0187
LYS 193
PHE 194
-0.0003
PHE 194
LYS 195
0.0001
LYS 195
ARG 196
-0.0120
ARG 196
ASP 197
0.0003
ASP 197
ILE 198
0.0001
ILE 198
LYS 199
0.0418
LYS 199
LYS 200
-0.0003
LYS 200
VAL 201
-0.0001
VAL 201
ALA 202
-0.0077
ALA 202
LYS 203
0.0001
LYS 203
ASP 204
-0.0003
ASP 204
ILE 205
0.0177
ILE 205
ILE 206
0.0001
ILE 206
PHE 207
-0.0001
PHE 207
ASN 208
-0.0411
ASN 208
PRO 209
-0.0004
PRO 209
SER 210
-0.0001
SER 210
PRO 211
0.0063
PRO 211
GLN 212
0.0003
GLN 212
PHE 213
0.0001
PHE 213
SER 214
0.1175
SER 214
ASP 215
0.0001
ASP 215
ILE 216
0.0000
ILE 216
SER 217
0.0004
SER 217
LEU 218
0.0004
LEU 218
ARG 219
-0.0003
ARG 219
ALA 220
0.0632
ALA 220
LYS 221
-0.0002
LYS 221
ASP 222
0.0002
ASP 222
GLU 223
-0.0118
GLU 223
ALA 224
-0.0003
ALA 224
GLY 225
0.0002
GLY 225
ASP 226
0.0008
ASP 226
LEU 228
0.0406
LEU 228
THR 229
0.0001
THR 229
GLU 230
0.0003
GLU 230
HIS 231
0.0226
HIS 231
TYR 232
0.0001
TYR 232
LEU 233
0.0004
LEU 233
SER 234
0.0109
SER 234
GLU 235
0.0002
GLU 235
LYS 236
-0.0001
LYS 236
GLY 237
-0.0389
GLY 237
HIS 238
-0.0002
HIS 238
LEU 239
-0.0001
LEU 239
SER 240
0.0048
SER 240
ALA 241
0.0001
ALA 241
PRO 242
0.0003
PRO 242
LEU 243
-0.0351
LEU 243
ASN 244
-0.0001
ASN 244
LYS 245
-0.0001
LYS 245
VAL 246
-0.0151
VAL 246
THR 247
-0.0000
THR 247
ASN 248
0.0000
ASN 248
ALA 249
0.0014
ALA 249
GLU 250
-0.0002
GLU 250
ILE 251
0.0002
ILE 251
ALA 252
-0.0363
ALA 252
GLU 253
-0.0005
GLU 253
GLU 254
-0.0003
GLU 254
MET 255
-0.0134
MET 255
ALA 256
-0.0002
ALA 256
TYR 257
-0.0003
TYR 257
CYS 258
-0.0308
CYS 258
TYR 259
0.0002
TYR 259
ALA 260
0.0003
ALA 260
ARG 261
0.1047
ARG 261
MET 262
-0.0001
MET 262
LYS 263
0.0000
LYS 263
SER 264
0.0247
SER 264
ASP 265
-0.0003
ASP 265
ILE 266
0.0001
ILE 266
LEU 267
-0.0397
LEU 267
GLU 268
0.0001
GLU 268
CYS 269
-0.0002
CYS 269
PHE 270
0.0563
PHE 270
LYS 271
-0.0002
LYS 271
ARG 272
-0.0003
ARG 272
GLN 273
-0.0813
GLN 273
VAL 274
-0.0000
VAL 274
GLY 275
-0.0000
GLY 275
LYS 276
0.1929
LYS 276
VAL 277
-0.0001
VAL 277
LYS 278
-0.0000
LYS 278
ASP 279
-0.1820
ASP 279
MET 1
0.0716
MET 1
LYS 2
-0.0002
LYS 2
ASN 3
0.0005
ASN 3
GLY 4
0.0618
GLY 4
PHE 5
0.0002
PHE 5
TYR 6
0.0000
TYR 6
ALA 7
0.0098
ALA 7
THR 8
0.0001
THR 8
TYR 9
0.0003
TYR 9
ARG 10
0.0136
ARG 10
SER 11
0.0000
SER 11
LYS 12
-0.0002
LYS 12
ASN 13
0.0115
ASN 13
LYS 14
0.0002
LYS 14
GLY 15
-0.0002
GLY 15
LYS 16
-0.0104
LYS 16
ASP 17
-0.0003
ASP 17
LYS 18
0.0004
LYS 18
ARG 19
-0.0410
ARG 19
SER 20
-0.0001
SER 20
ILE 21
0.0005
ILE 21
ASN 22
-0.0143
ASN 22
LEU 23
-0.0002
LEU 23
SER 24
0.0003
SER 24
VAL 25
0.0369
VAL 25
PHE 26
-0.0001
PHE 26
LEU 27
0.0003
LEU 27
ASN 28
0.0015
ASN 28
SER 29
0.0001
SER 29
LEU 30
-0.0001
LEU 30
LEU 31
-0.0099
LEU 31
ALA 32
-0.0002
ALA 32
ASP 33
-0.0001
ASP 33
ASN 34
-0.0083
ASN 34
HIS 35
0.0000
HIS 35
HIS 36
-0.0001
HIS 36
LEU 37
0.0067
LEU 37
GLN 38
0.0005
GLN 38
VAL 39
-0.0003
VAL 39
GLY 40
0.0133
GLY 40
SER 41
-0.0000
SER 41
ASN 42
-0.0002
ASN 42
TYR 43
0.0077
TYR 43
LEU 44
-0.0000
LEU 44
TYR 45
-0.0004
TYR 45
ILE 46
0.0363
ILE 46
HIS 47
0.0001
HIS 47
LYS 48
0.0002
LYS 48
ILE 49
0.0438
ILE 49
ASP 50
-0.0001
ASP 50
GLY 51
0.0003
GLY 51
LYS 52
-0.0139
LYS 52
THR 53
0.0001
THR 53
PHE 54
0.0001
PHE 54
LEU 55
-0.0060
LEU 55
PHE 56
-0.0001
PHE 56
THR 57
0.0003
THR 57
LYS 58
0.0082
LYS 58
THR 59
0.0003
THR 59
ASN 60
-0.0002
ASN 60
ASP 61
0.0032
ASP 61
LYS 62
-0.0000
LYS 62
SER 63
0.0000
SER 63
LEU 64
-0.0024
LEU 64
VAL 65
-0.0001
VAL 65
GLN 66
-0.0001
GLN 66
LYS 67
0.0028
LYS 67
ILE 68
0.0002
ILE 68
ASN 69
-0.0000
ASN 69
ARG 70
-0.0108
ARG 70
SER 71
0.0000
SER 71
LYS 72
-0.0000
LYS 72
ALA 73
0.0194
ALA 73
SER 74
-0.0001
SER 74
VAL 75
-0.0003
VAL 75
GLU 76
-0.0015
GLU 76
ASP 77
0.0003
ASP 77
ILE 78
0.0002
ILE 78
LYS 79
0.0373
LYS 79
ASN 80
-0.0000
ASN 80
SER 81
-0.0002
SER 81
LEU 82
-0.0003
LEU 82
ALA 83
0.0001
ALA 83
ASP 84
-0.0001
ASP 84
ASP 85
0.0006
ASP 85
GLU 86
-0.0002
GLU 86
SER 87
-0.0001
SER 87
LEU 88
-0.0018
LEU 88
GLY 89
-0.0001
GLY 89
PHE 90
0.0001
PHE 90
PRO 91
0.0020
PRO 91
SER 92
-0.0001
SER 92
PHE 93
0.0000
PHE 93
LEU 94
-0.0079
LEU 94
PHE 95
-0.0006
PHE 95
VAL 96
-0.0001
VAL 96
GLU 97
-0.0151
GLU 97
GLY 98
0.0001
GLY 98
ASP 99
-0.0001
ASP 99
THR 100
0.0749
THR 100
ILE 101
-0.0002
ILE 101
GLY 102
0.0002
GLY 102
PHE 103
0.0123
PHE 103
ALA 104
-0.0003
ALA 104
ARG 105
-0.0001
ARG 105
THR 106
0.0237
THR 106
VAL 107
-0.0000
VAL 107
PHE 108
-0.0002
PHE 108
GLY 109
0.0119
GLY 109
PRO 110
0.0004
PRO 110
THR 111
-0.0004
THR 111
THR 112
0.0438
THR 112
SER 113
-0.0002
SER 113
ASP 114
-0.0000
ASP 114
LEU 115
0.0122
LEU 115
THR 116
-0.0000
THR 116
ASP 117
0.0000
ASP 117
PHE 118
0.0001
PHE 118
LEU 119
-0.0003
LEU 119
ILE 120
0.0002
ILE 120
GLY 121
0.0056
GLY 121
LYS 122
0.0002
LYS 122
GLY 123
0.0000
GLY 123
MET 124
-0.0450
MET 124
SER 125
-0.0001
SER 125
LEU 126
0.0002
LEU 126
SER 127
0.0122
SER 127
SER 128
0.0001
SER 128
GLY 129
-0.0002
GLY 129
GLU 130
-0.0045
GLU 130
ARG 131
-0.0001
ARG 131
VAL 132
-0.0001
VAL 132
GLN 133
-0.0816
GLN 133
ILE 134
0.0000
ILE 134
GLU 135
0.0000
GLU 135
PRO 136
-0.2233
PRO 136
LEU 137
0.0000
LEU 137
MET 138
0.0003
MET 138
ARG 139
0.0673
ARG 139
GLY 140
0.0002
GLY 140
THR 141
-0.0002
THR 141
THR 142
-0.0249
THR 142
LYS 143
0.0004
LYS 143
ASP 144
0.0001
ASP 144
ASP 145
-0.0102
ASP 145
VAL 146
0.0002
VAL 146
MET 147
-0.0002
MET 147
HIS 148
-0.0138
HIS 148
MET 149
0.0004
MET 149
HIS 150
0.0001
HIS 150
PHE 151
0.0373
PHE 151
ILE 152
0.0002
ILE 152
GLY 153
0.0004
GLY 153
ARG 154
0.1096
ARG 154
THR 155
0.0001
THR 155
THR 156
-0.0001
THR 156
VAL 157
-0.0179
VAL 157
LYS 158
-0.0003
LYS 158
VAL 159
-0.0002
VAL 159
GLU 160
-0.0081
GLU 160
ALA 161
0.0002
ALA 161
LYS 162
0.0005
LYS 162
LEU 163
-0.0533
LEU 163
PRO 164
-0.0001
PRO 164
VAL 165
-0.0001
VAL 165
PHE 166
-0.0895
PHE 166
GLY 167
-0.0001
GLY 167
ASP 168
-0.0003
ASP 168
ILE 169
0.0337
ILE 169
LEU 170
0.0000
LEU 170
LYS 171
-0.0001
LYS 171
VAL 172
-0.0026
VAL 172
LEU 173
-0.0001
LEU 173
GLY 174
-0.0001
GLY 174
ALA 175
0.0093
ALA 175
THR 176
-0.0003
THR 176
ASP 177
-0.0001
ASP 177
ILE 178
0.0213
ILE 178
GLU 179
0.0001
GLU 179
GLY 180
-0.0004
GLY 180
GLU 181
-0.0127
GLU 181
LEU 182
0.0002
LEU 182
PHE 183
-0.0000
PHE 183
ASP 184
0.0896
ASP 184
SER 185
0.0001
SER 185
LEU 186
0.0000
LEU 186
ASP 187
0.0502
ASP 187
ILE 188
-0.0005
ILE 188
VAL 189
0.0000
VAL 189
ILE 190
0.0310
ILE 190
LYS 191
-0.0001
LYS 191
PRO 192
-0.0001
PRO 192
LYS 193
-0.0155
LYS 193
PHE 194
-0.0003
PHE 194
LYS 195
-0.0001
LYS 195
ARG 196
-0.0060
ARG 196
ASP 197
-0.0001
ASP 197
ILE 198
0.0000
ILE 198
LYS 199
0.0559
LYS 199
LYS 200
0.0001
LYS 200
VAL 201
0.0000
VAL 201
ALA 202
-0.0112
ALA 202
LYS 203
-0.0003
LYS 203
ASP 204
-0.0001
ASP 204
ILE 205
0.0158
ILE 205
ILE 206
0.0002
ILE 206
PHE 207
-0.0001
PHE 207
ASN 208
-0.0605
ASN 208
PRO 209
0.0001
PRO 209
SER 210
-0.0000
SER 210
PRO 211
-0.0019
PRO 211
GLN 212
-0.0002
GLN 212
PHE 213
-0.0001
PHE 213
SER 214
0.1458
SER 214
ASP 215
0.0005
ASP 215
ILE 216
-0.0000
ILE 216
SER 217
-0.0100
SER 217
LEU 218
0.0001
LEU 218
ARG 219
0.0002
ARG 219
ALA 220
0.0654
ALA 220
LYS 221
-0.0004
LYS 221
ASP 222
-0.0001
ASP 222
GLU 223
-0.0064
GLU 223
ALA 224
0.0003
ALA 224
GLY 225
0.0002
GLY 225
ASP 226
-0.0128
ASP 226
ILE 227
0.0004
ILE 227
LEU 228
-0.0001
LEU 228
THR 229
-0.0661
THR 229
GLU 230
0.0002
GLU 230
HIS 231
0.0002
HIS 231
TYR 232
-0.0102
TYR 232
LEU 233
0.0001
LEU 233
SER 234
0.0003
SER 234
GLU 235
-0.0234
GLU 235
LYS 236
0.0003
LYS 236
GLY 237
0.0001
GLY 237
HIS 238
0.0604
HIS 238
LEU 239
-0.0002
LEU 239
SER 240
0.0000
SER 240
ALA 241
0.0541
ALA 241
PRO 242
0.0002
PRO 242
LEU 243
-0.0002
LEU 243
ASN 244
0.0199
ASN 244
LYS 245
-0.0001
LYS 245
VAL 246
-0.0002
VAL 246
THR 247
0.0010
THR 247
ASN 248
-0.0003
ASN 248
ALA 249
-0.0003
ALA 249
GLU 250
0.0250
GLU 250
ILE 251
-0.0001
ILE 251
ALA 252
0.0002
ALA 252
GLU 253
0.0365
GLU 253
GLU 254
0.0001
GLU 254
MET 255
0.0001
MET 255
ALA 256
-0.0365
ALA 256
TYR 257
0.0001
TYR 257
CYS 258
0.0000
CYS 258
TYR 259
-0.0950
TYR 259
ALA 260
-0.0002
ALA 260
ARG 261
-0.0002
ARG 261
MET 262
-0.1006
MET 262
LYS 263
-0.0001
LYS 263
SER 264
0.0003
SER 264
ASP 265
0.0282
ASP 265
ILE 266
-0.0002
ILE 266
LEU 267
0.0001
LEU 267
GLU 268
-0.0456
GLU 268
CYS 269
-0.0001
CYS 269
PHE 270
0.0002
PHE 270
LYS 271
-0.0806
LYS 271
ARG 272
0.0003
ARG 272
GLN 273
-0.0001
GLN 273
VAL 274
-0.1537
VAL 274
GLY 275
-0.0003
GLY 275
LYS 276
-0.0002
LYS 276
VAL 277
-0.2211
VAL 277
LYS 278
-0.0001
LYS 278
ASP 279
-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.