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
PHE 35
ASP 36
0.0002
ASP 36
ARG 37
0.0035
ARG 37
VAL 38
0.0001
VAL 38
ASP 39
-0.0017
ASP 39
TRP 40
0.0003
TRP 40
ILE 41
0.0052
ILE 41
ASN 42
0.0002
ASN 42
ARG 43
0.0051
ARG 43
PHE 44
-0.0001
PHE 44
LEU 45
0.0258
LEU 45
GLU 46
-0.0000
GLU 46
TYR 47
0.0141
TYR 47
MET 48
0.0000
MET 48
TRP 49
0.0414
TRP 49
PRO 50
-0.0004
PRO 50
TYR 51
-0.0228
TYR 51
LEU 52
-0.0000
LEU 52
ASP 53
0.0165
ASP 53
LYS 54
0.0000
LYS 54
ALA 55
-0.0274
ALA 55
ILE 56
-0.0004
ILE 56
CYS 57
-0.0384
CYS 57
LYS 58
0.0002
LYS 58
THR 59
0.0095
THR 59
ALA 60
-0.0001
ALA 60
LYS 61
-0.0151
LYS 61
ASN 62
-0.0003
ASN 62
ILE 63
-0.0001
ILE 63
ALA 64
0.0001
ALA 64
LYS 65
-0.0094
LYS 65
PRO 66
-0.0002
PRO 66
ILE 67
0.0005
ILE 67
ILE 68
-0.0000
ILE 68
GLU 69
0.0016
GLU 69
GLU 70
0.0002
GLU 70
GLN 71
0.0071
GLN 71
ILE 72
-0.0004
ILE 72
PRO 73
0.0028
PRO 73
LYS 74
-0.0002
LYS 74
TYR 75
0.0038
TYR 75
LYS 76
0.0002
LYS 76
ILE 77
0.0020
ILE 77
ASP 78
-0.0001
ASP 78
SER 79
0.0271
SER 79
VAL 80
0.0002
VAL 80
GLU 81
0.0100
GLU 81
PHE 82
-0.0000
PHE 82
GLU 83
-0.0096
GLU 83
THR 84
0.0001
THR 84
LEU 85
0.0111
LEU 85
THR 86
0.0001
THR 86
LEU 87
0.0146
LEU 87
GLY 88
-0.0000
GLY 88
SER 89
0.0299
SER 89
LEU 90
-0.0000
LEU 90
PRO 91
0.0187
PRO 91
PRO 92
0.0001
PRO 92
THR 93
-0.0003
THR 93
PHE 94
0.0001
PHE 94
GLN 95
0.0026
GLN 95
GLY 96
-0.0000
GLY 96
MET 97
0.0028
MET 97
LYS 98
-0.0004
LYS 98
VAL 99
-0.0031
VAL 99
TYR 100
-0.0000
TYR 100
LEU 101
0.0149
LEU 101
THR 102
-0.0002
THR 102
ASP 103
-0.0011
ASP 103
GLU 104
-0.0001
GLU 104
LYS 105
-0.0050
LYS 105
GLU 106
0.0002
GLU 106
LEU 107
0.0037
LEU 107
ILE 108
0.0000
ILE 108
MET 109
-0.0015
MET 109
GLU 110
-0.0000
GLU 110
PRO 111
-0.0022
PRO 111
CYS 112
-0.0003
CYS 112
LEU 113
-0.0142
LEU 113
LYS 114
0.0001
LYS 114
TRP 115
0.0037
TRP 115
ALA 116
0.0001
ALA 116
ALA 117
0.0161
ALA 117
ASN 118
-0.0005
ASN 118
PRO 119
0.0205
PRO 119
ASN 120
-0.0002
ASN 120
ILE 121
0.0104
ILE 121
LEU 122
0.0001
LEU 122
VAL 123
0.0109
VAL 123
ALA 124
0.0000
ALA 124
ILE 125
0.0158
ILE 125
LYS 126
-0.0002
LYS 126
ALA 127
0.0105
ALA 127
PHE 128
0.0001
PHE 128
GLY 129
0.0023
GLY 129
LEU 130
0.0002
LEU 130
LYS 131
0.0344
LYS 131
ALA 132
-0.0001
ALA 132
THR 133
0.0055
THR 133
VAL 134
-0.0002
VAL 134
GLN 135
-0.0034
GLN 135
VAL 136
-0.0002
VAL 136
VAL 137
-0.0078
VAL 137
ASP 138
-0.0002
ASP 138
LEU 139
0.0103
LEU 139
GLN 140
-0.0000
GLN 140
VAL 141
-0.0145
VAL 141
PHE 142
0.0002
PHE 142
ALA 143
-0.0078
ALA 143
GLN 144
-0.0001
GLN 144
PRO 145
-0.0037
PRO 145
ARG 146
0.0003
ARG 146
ILE 147
-0.0004
ILE 147
THR 148
0.0002
THR 148
LEU 149
-0.0062
LEU 149
LYS 150
0.0000
LYS 150
PRO 151
-0.0249
PRO 151
LEU 152
-0.0003
LEU 152
VAL 153
-0.0161
VAL 153
PRO 154
0.0001
PRO 154
SER 155
0.0072
SER 155
PHE 156
-0.0002
PHE 156
PRO 157
0.0470
PRO 157
CYS 158
0.0002
CYS 158
PHE 159
0.0048
PHE 159
ALA 160
-0.0000
ALA 160
ASN 161
0.0021
ASN 161
ILE 162
-0.0003
ILE 162
TYR 163
0.0148
TYR 163
VAL 164
-0.0003
VAL 164
SER 165
0.0097
SER 165
LEU 166
0.0000
LEU 166
MET 167
-0.0000
MET 167
GLU 168
0.0002
GLU 168
LYS 169
-0.0371
LYS 169
PRO 170
-0.0002
PRO 170
HIS 171
0.0070
HIS 171
VAL 172
0.0002
VAL 172
ASP 173
-0.0081
ASP 173
PHE 174
-0.0003
PHE 174
GLY 175
0.0046
GLY 175
LEU 176
0.0001
LEU 176
LYS 177
-0.0451
LYS 177
LEU 178
0.0001
LEU 178
GLY 179
-0.0201
GLY 179
GLY 180
-0.0001
GLY 180
ALA 181
0.0052
ALA 181
ASP 182
0.0000
ASP 182
LEU 183
-0.0221
LEU 183
MET 184
0.0001
MET 184
SER 185
-0.0098
SER 185
ILE 186
-0.0001
ILE 186
PRO 187
0.0177
PRO 187
GLY 188
-0.0002
GLY 188
LEU 189
-0.0002
LEU 189
TYR 190
-0.0001
TYR 190
ARG 191
0.0029
ARG 191
PHE 192
-0.0003
PHE 192
VAL 193
0.0053
VAL 193
GLN 194
0.0001
GLN 194
GLU 195
-0.0076
GLU 195
GLN 196
0.0001
GLN 196
ILE 197
0.0104
ILE 197
LYS 198
0.0003
LYS 198
ASP 199
0.0095
ASP 199
GLN 200
0.0001
GLN 200
VAL 201
0.0094
VAL 201
ALA 202
-0.0000
ALA 202
ASN 203
0.0158
ASN 203
MET 204
-0.0001
MET 204
TYR 205
-0.0160
TYR 205
LEU 206
0.0003
LEU 206
TRP 207
-0.0106
TRP 207
PRO 208
0.0001
PRO 208
LYS 209
-0.0056
LYS 209
THR 210
0.0004
THR 210
LEU 211
0.0330
LEU 211
VAL 212
0.0001
VAL 212
VAL 213
0.0261
VAL 213
PRO 214
0.0001
PRO 214
ILE 215
0.0209
ILE 215
LEU 216
-0.0000
LEU 216
ASP 217
-0.0057
ASP 217
PRO 218
-0.0003
PRO 218
ALA 219
-0.0011
ALA 219
LYS 220
-0.0002
LYS 220
ALA 221
-0.0019
ALA 221
PHE 222
0.0002
PHE 222
ASP 34
-0.0065
ASP 34
PHE 35
-0.0002
PHE 35
ASP 36
-0.0033
ASP 36
ARG 37
-0.0003
ARG 37
VAL 38
-0.0040
VAL 38
ASP 39
-0.0002
ASP 39
TRP 40
0.0006
TRP 40
ILE 41
-0.0002
ILE 41
ASN 42
-0.0061
ASN 42
ARG 43
-0.0003
ARG 43
PHE 44
0.0068
PHE 44
LEU 45
0.0001
LEU 45
GLU 46
-0.0025
GLU 46
TYR 47
0.0003
TYR 47
MET 48
0.0043
MET 48
TRP 49
-0.0002
TRP 49
PRO 50
0.0042
PRO 50
TYR 51
-0.0001
TYR 51
LEU 52
-0.0082
LEU 52
ASP 53
0.0001
ASP 53
LYS 54
0.0274
LYS 54
ALA 55
0.0000
ALA 55
ILE 56
-0.0153
ILE 56
CYS 57
-0.0000
CYS 57
LYS 58
0.0230
LYS 58
THR 59
0.0001
THR 59
ALA 60
-0.0019
ALA 60
LYS 61
0.0002
LYS 61
ASN 62
0.0185
ASN 62
ILE 63
-0.0000
ILE 63
ALA 64
-0.0124
ALA 64
LYS 65
-0.0002
LYS 65
PRO 66
-0.0143
PRO 66
ILE 67
-0.0001
ILE 67
ILE 68
0.0053
ILE 68
GLU 69
-0.0003
GLU 69
GLU 70
-0.0301
GLU 70
GLN 71
0.0005
GLN 71
ILE 72
0.0101
ILE 72
PRO 73
0.0001
PRO 73
LYS 74
-0.0057
LYS 74
TYR 75
0.0001
TYR 75
LYS 76
-0.0026
LYS 76
ILE 77
0.0001
ILE 77
ASP 78
-0.0202
ASP 78
SER 79
0.0001
SER 79
VAL 80
-0.0111
VAL 80
GLU 81
0.0003
GLU 81
PHE 82
-0.0346
PHE 82
GLU 83
0.0001
GLU 83
THR 84
-0.0925
THR 84
LEU 85
-0.0005
LEU 85
THR 86
-0.0588
THR 86
LEU 87
0.0004
LEU 87
GLY 88
-0.0148
GLY 88
SER 89
0.0003
SER 89
LEU 90
-0.0091
LEU 90
PRO 91
0.0000
PRO 91
PRO 92
-0.0029
PRO 92
THR 93
0.0004
THR 93
PHE 94
-0.0075
PHE 94
GLN 95
0.0000
GLN 95
GLY 96
-0.0045
GLY 96
MET 97
-0.0000
MET 97
LYS 98
-0.0097
LYS 98
VAL 99
0.0001
VAL 99
TYR 100
-0.0227
TYR 100
LEU 101
-0.0000
LEU 101
THR 102
-0.0026
THR 102
ASP 103
-0.0000
ASP 103
GLU 104
0.0012
GLU 104
LYS 105
-0.0002
LYS 105
GLU 106
0.0070
GLU 106
LEU 107
-0.0000
LEU 107
ILE 108
0.0167
ILE 108
MET 109
-0.0001
MET 109
GLU 110
0.0076
GLU 110
PRO 111
-0.0000
PRO 111
CYS 112
0.0051
CYS 112
LEU 113
-0.0005
LEU 113
LYS 114
0.0070
LYS 114
TRP 115
-0.0001
TRP 115
ALA 116
-0.0100
ALA 116
ALA 117
0.0004
ALA 117
ASN 118
-0.0193
ASN 118
PRO 119
-0.0000
PRO 119
ASN 120
-0.0473
ASN 120
ILE 121
-0.0003
ILE 121
LEU 122
-0.0030
LEU 122
VAL 123
0.0000
VAL 123
ALA 124
-0.0025
ALA 124
ILE 125
0.0001
ILE 125
LYS 126
0.0203
LYS 126
ALA 127
0.0002
ALA 127
PHE 128
0.0144
PHE 128
GLY 129
-0.0002
GLY 129
LEU 130
0.0067
LEU 130
LYS 131
0.0000
LYS 131
ALA 132
0.0624
ALA 132
THR 133
-0.0002
THR 133
VAL 134
0.0719
VAL 134
GLN 135
0.0003
GLN 135
VAL 136
0.0496
VAL 136
VAL 137
0.0000
VAL 137
ASP 138
-0.0127
ASP 138
LEU 139
0.0001
LEU 139
GLN 140
0.0110
GLN 140
VAL 141
-0.0001
VAL 141
PHE 142
0.0211
PHE 142
ALA 143
-0.0001
ALA 143
GLN 144
0.0374
GLN 144
PRO 145
0.0002
PRO 145
ARG 146
0.0172
ARG 146
ILE 147
-0.0000
ILE 147
THR 148
0.0110
THR 148
LEU 149
0.0000
LEU 149
LYS 150
0.0013
LYS 150
PRO 151
-0.0002
PRO 151
LEU 152
0.0182
LEU 152
VAL 153
-0.0001
VAL 153
PRO 154
0.0170
PRO 154
SER 155
-0.0000
SER 155
PHE 156
0.0194
PHE 156
PRO 157
0.0003
PRO 157
CYS 158
0.0050
CYS 158
PHE 159
-0.0001
PHE 159
ALA 160
0.0061
ALA 160
ASN 161
-0.0001
ASN 161
ILE 162
0.0026
ILE 162
TYR 163
0.0003
TYR 163
VAL 164
0.0031
VAL 164
SER 165
-0.0000
SER 165
LEU 166
-0.0051
LEU 166
MET 167
0.0002
MET 167
GLU 168
0.0269
GLU 168
LYS 169
0.0001
LYS 169
PRO 170
-0.0250
PRO 170
HIS 171
-0.0001
HIS 171
VAL 172
0.0169
VAL 172
ASP 173
0.0003
ASP 173
PHE 174
0.0227
PHE 174
GLY 175
-0.0002
GLY 175
LEU 176
-0.0153
LEU 176
LYS 177
-0.0001
LYS 177
LEU 178
0.0040
LEU 178
GLY 179
-0.0003
GLY 179
GLY 180
-0.0257
GLY 180
ALA 181
-0.0002
ALA 181
ASP 182
-0.0341
ASP 182
LEU 183
-0.0001
LEU 183
MET 184
-0.0049
MET 184
SER 185
-0.0002
SER 185
ILE 186
0.0131
ILE 186
PRO 187
-0.0001
PRO 187
GLY 188
-0.0251
GLY 188
LEU 189
-0.0000
LEU 189
TYR 190
-0.0114
TYR 190
ARG 191
0.0003
ARG 191
PHE 192
-0.0054
PHE 192
VAL 193
0.0000
VAL 193
GLN 194
0.0045
GLN 194
GLU 195
-0.0004
GLU 195
GLN 196
-0.0149
GLN 196
ILE 197
-0.0001
ILE 197
LYS 198
0.0203
LYS 198
ASP 199
0.0000
ASP 199
GLN 200
-0.0143
GLN 200
VAL 201
0.0001
VAL 201
ALA 202
0.0005
ALA 202
ASN 203
-0.0001
ASN 203
MET 204
-0.0161
MET 204
TYR 205
-0.0000
TYR 205
LEU 206
0.0090
LEU 206
TRP 207
-0.0002
TRP 207
PRO 208
-0.0061
PRO 208
LYS 209
0.0002
LYS 209
THR 210
-0.0157
THR 210
LEU 211
-0.0001
LEU 211
VAL 212
-0.0211
VAL 212
VAL 213
0.0000
VAL 213
PRO 214
-0.0135
PRO 214
ILE 215
-0.0002
ILE 215
LEU 216
-0.0149
LEU 216
ASP 217
-0.0000
ASP 217
PRO 218
-0.0038
PRO 218
ALA 219
0.0001
ALA 219
LYS 220
0.0025
LYS 220
ALA 221
-0.0001
ALA 221
PHE 222
0.0033
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.