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
0.0000
ASP 36
ARG 37
-0.0053
ARG 37
VAL 38
-0.0004
VAL 38
ASP 39
0.0017
ASP 39
TRP 40
-0.0002
TRP 40
ILE 41
-0.0035
ILE 41
ASN 42
-0.0001
ASN 42
ARG 43
-0.0122
ARG 43
PHE 44
-0.0000
PHE 44
LEU 45
-0.0246
LEU 45
GLU 46
0.0001
GLU 46
TYR 47
-0.0231
TYR 47
MET 48
0.0000
MET 48
TRP 49
-0.0404
TRP 49
PRO 50
-0.0003
PRO 50
TYR 51
0.0045
TYR 51
LEU 52
0.0001
LEU 52
ASP 53
0.0038
ASP 53
LYS 54
0.0002
LYS 54
ALA 55
0.0222
ALA 55
ILE 56
-0.0003
ILE 56
CYS 57
0.0658
CYS 57
LYS 58
0.0001
LYS 58
THR 59
-0.0459
THR 59
ALA 60
0.0000
ALA 60
LYS 61
-0.0060
LYS 61
ASN 62
-0.0002
ASN 62
ILE 63
0.0282
ILE 63
ALA 64
-0.0001
ALA 64
LYS 65
-0.0146
LYS 65
PRO 66
-0.0003
PRO 66
ILE 67
0.0176
ILE 67
ILE 68
0.0005
ILE 68
GLU 69
-0.0238
GLU 69
GLU 70
0.0001
GLU 70
GLN 71
0.0107
GLN 71
ILE 72
0.0002
ILE 72
PRO 73
0.0284
PRO 73
LYS 74
0.0000
LYS 74
TYR 75
-0.0072
TYR 75
LYS 76
0.0001
LYS 76
ILE 77
0.0105
ILE 77
ASP 78
-0.0002
ASP 78
SER 79
0.0657
SER 79
VAL 80
0.0001
VAL 80
GLU 81
0.0400
GLU 81
PHE 82
-0.0001
PHE 82
GLU 83
0.0251
GLU 83
THR 84
0.0001
THR 84
LEU 85
-0.0084
LEU 85
THR 86
0.0001
THR 86
LEU 87
0.0071
LEU 87
GLY 88
0.0002
GLY 88
SER 89
-0.0182
SER 89
LEU 90
0.0001
LEU 90
PRO 91
-0.0128
PRO 91
PRO 92
-0.0001
PRO 92
THR 93
0.0016
THR 93
PHE 94
0.0001
PHE 94
GLN 95
0.0009
GLN 95
GLY 96
-0.0002
GLY 96
MET 97
-0.0099
MET 97
LYS 98
-0.0002
LYS 98
VAL 99
-0.0016
VAL 99
TYR 100
-0.0001
TYR 100
LEU 101
-0.0197
LEU 101
THR 102
-0.0004
THR 102
ASP 103
0.0007
ASP 103
GLU 104
0.0003
GLU 104
LYS 105
0.0018
LYS 105
GLU 106
-0.0003
GLU 106
LEU 107
0.0011
LEU 107
ILE 108
0.0001
ILE 108
MET 109
-0.0018
MET 109
GLU 110
0.0003
GLU 110
PRO 111
-0.0002
PRO 111
CYS 112
-0.0001
CYS 112
LEU 113
0.0103
LEU 113
LYS 114
0.0003
LYS 114
TRP 115
-0.0031
TRP 115
ALA 116
0.0000
ALA 116
ALA 117
0.0128
ALA 117
ASN 118
0.0000
ASN 118
PRO 119
-0.0099
PRO 119
ASN 120
0.0000
ASN 120
ILE 121
-0.0417
ILE 121
LEU 122
0.0000
LEU 122
VAL 123
-0.0373
VAL 123
ALA 124
0.0006
ALA 124
ILE 125
-0.0067
ILE 125
LYS 126
-0.0001
LYS 126
ALA 127
-0.0113
ALA 127
PHE 128
0.0001
PHE 128
GLY 129
0.0626
GLY 129
LEU 130
-0.0004
LEU 130
LYS 131
0.0097
LYS 131
ALA 132
-0.0001
ALA 132
THR 133
-0.0423
THR 133
VAL 134
0.0002
VAL 134
GLN 135
-0.0692
GLN 135
VAL 136
-0.0002
VAL 136
VAL 137
-0.0387
VAL 137
ASP 138
0.0001
ASP 138
LEU 139
-0.0053
LEU 139
GLN 140
0.0003
GLN 140
VAL 141
0.0156
VAL 141
PHE 142
0.0003
PHE 142
ALA 143
0.0103
ALA 143
GLN 144
-0.0002
GLN 144
PRO 145
0.0026
PRO 145
ARG 146
-0.0001
ARG 146
ILE 147
-0.0003
ILE 147
THR 148
-0.0004
THR 148
LEU 149
-0.0009
LEU 149
LYS 150
-0.0000
LYS 150
PRO 151
0.0061
PRO 151
LEU 152
-0.0003
LEU 152
VAL 153
-0.0158
VAL 153
PRO 154
0.0001
PRO 154
SER 155
-0.0041
SER 155
PHE 156
-0.0003
PHE 156
PRO 157
-0.0342
PRO 157
CYS 158
-0.0002
CYS 158
PHE 159
-0.0050
PHE 159
ALA 160
0.0003
ALA 160
ASN 161
-0.0061
ASN 161
ILE 162
0.0001
ILE 162
TYR 163
-0.0112
TYR 163
VAL 164
0.0000
VAL 164
SER 165
-0.0010
SER 165
LEU 166
-0.0002
LEU 166
MET 167
-0.0110
MET 167
GLU 168
0.0004
GLU 168
LYS 169
0.0439
LYS 169
PRO 170
0.0004
PRO 170
HIS 171
-0.0092
HIS 171
VAL 172
-0.0001
VAL 172
ASP 173
0.0112
ASP 173
PHE 174
0.0001
PHE 174
GLY 175
-0.0071
GLY 175
LEU 176
-0.0003
LEU 176
LYS 177
0.0426
LYS 177
LEU 178
0.0001
LEU 178
GLY 179
0.0081
GLY 179
GLY 180
-0.0003
GLY 180
ALA 181
0.0508
ALA 181
ASP 182
-0.0002
ASP 182
LEU 183
0.0383
LEU 183
MET 184
0.0003
MET 184
SER 185
-0.0104
SER 185
ILE 186
0.0000
ILE 186
PRO 187
-0.0240
PRO 187
GLY 188
-0.0003
GLY 188
LEU 189
-0.0209
LEU 189
TYR 190
-0.0000
TYR 190
ARG 191
-0.0055
ARG 191
PHE 192
0.0001
PHE 192
VAL 193
-0.0255
VAL 193
GLN 194
0.0001
GLN 194
GLU 195
0.0122
GLU 195
GLN 196
-0.0002
GLN 196
ILE 197
-0.0243
ILE 197
LYS 198
0.0000
LYS 198
ASP 199
-0.0023
ASP 199
GLN 200
-0.0005
GLN 200
VAL 201
-0.0233
VAL 201
ALA 202
-0.0000
ALA 202
ASN 203
-0.0083
ASN 203
MET 204
0.0003
MET 204
TYR 205
-0.0198
TYR 205
LEU 206
0.0000
LEU 206
TRP 207
0.0056
TRP 207
PRO 208
0.0004
PRO 208
LYS 209
0.0031
LYS 209
THR 210
-0.0000
THR 210
LEU 211
-0.0269
LEU 211
VAL 212
0.0003
VAL 212
VAL 213
-0.0194
VAL 213
PRO 214
-0.0002
PRO 214
ILE 215
-0.0184
ILE 215
LEU 216
-0.0002
LEU 216
ASP 217
0.0049
ASP 217
PRO 218
-0.0003
PRO 218
ALA 219
0.0008
ALA 219
LYS 220
-0.0002
LYS 220
ALA 221
0.0004
ALA 221
PHE 222
-0.0000
PHE 222
ASP 34
0.0120
ASP 34
PHE 35
-0.0000
PHE 35
ASP 36
-0.0008
ASP 36
ARG 37
0.0002
ARG 37
VAL 38
0.0035
VAL 38
ASP 39
-0.0003
ASP 39
TRP 40
0.0014
TRP 40
ILE 41
-0.0000
ILE 41
ASN 42
0.0053
ASN 42
ARG 43
-0.0002
ARG 43
PHE 44
-0.0041
PHE 44
LEU 45
-0.0001
LEU 45
GLU 46
0.0054
GLU 46
TYR 47
-0.0000
TYR 47
MET 48
-0.0073
MET 48
TRP 49
0.0001
TRP 49
PRO 50
-0.0021
PRO 50
TYR 51
-0.0003
TYR 51
LEU 52
0.0205
LEU 52
ASP 53
-0.0001
ASP 53
LYS 54
-0.0190
LYS 54
ALA 55
0.0002
ALA 55
ILE 56
0.0075
ILE 56
CYS 57
-0.0002
CYS 57
LYS 58
-0.0060
LYS 58
THR 59
-0.0001
THR 59
ALA 60
-0.0313
ALA 60
LYS 61
0.0004
LYS 61
ASN 62
0.0734
ASN 62
ILE 63
-0.0001
ILE 63
ALA 64
-0.0532
ALA 64
LYS 65
-0.0002
LYS 65
PRO 66
-0.0101
PRO 66
ILE 67
-0.0001
ILE 67
ILE 68
0.0216
ILE 68
GLU 69
0.0000
GLU 69
GLU 70
-0.0447
GLU 70
GLN 71
-0.0001
GLN 71
ILE 72
0.0035
ILE 72
PRO 73
-0.0002
PRO 73
LYS 74
-0.0342
LYS 74
TYR 75
-0.0000
TYR 75
LYS 76
-0.0506
LYS 76
ILE 77
0.0000
ILE 77
ASP 78
-0.0334
ASP 78
SER 79
-0.0000
SER 79
VAL 80
-0.0000
VAL 80
GLU 81
-0.0001
GLU 81
PHE 82
-0.0935
PHE 82
GLU 83
0.0000
GLU 83
THR 84
-0.0862
THR 84
LEU 85
-0.0004
LEU 85
THR 86
-0.0171
THR 86
LEU 87
-0.0004
LEU 87
GLY 88
0.0111
GLY 88
SER 89
-0.0000
SER 89
LEU 90
-0.0149
LEU 90
PRO 91
-0.0001
PRO 91
PRO 92
-0.0055
PRO 92
THR 93
0.0001
THR 93
PHE 94
0.0028
PHE 94
GLN 95
-0.0001
GLN 95
GLY 96
0.0163
GLY 96
MET 97
-0.0002
MET 97
LYS 98
0.0144
LYS 98
VAL 99
-0.0000
VAL 99
TYR 100
0.0231
TYR 100
LEU 101
0.0001
LEU 101
THR 102
-0.0030
THR 102
ASP 103
0.0001
ASP 103
GLU 104
0.0015
GLU 104
LYS 105
0.0003
LYS 105
GLU 106
-0.0078
GLU 106
LEU 107
-0.0002
LEU 107
ILE 108
-0.0083
ILE 108
MET 109
-0.0002
MET 109
GLU 110
-0.0035
GLU 110
PRO 111
-0.0003
PRO 111
CYS 112
-0.0015
CYS 112
LEU 113
-0.0000
LEU 113
LYS 114
-0.0114
LYS 114
TRP 115
0.0001
TRP 115
ALA 116
-0.0008
ALA 116
ALA 117
-0.0002
ALA 117
ASN 118
-0.0176
ASN 118
PRO 119
0.0000
PRO 119
ASN 120
-0.0281
ASN 120
ILE 121
-0.0001
ILE 121
LEU 122
0.0126
LEU 122
VAL 123
-0.0001
VAL 123
ALA 124
0.0036
ALA 124
ILE 125
-0.0000
ILE 125
LYS 126
0.0503
LYS 126
ALA 127
0.0000
ALA 127
PHE 128
0.0653
PHE 128
GLY 129
-0.0003
GLY 129
LEU 130
-0.0350
LEU 130
LYS 131
0.0002
LYS 131
ALA 132
0.0358
ALA 132
THR 133
-0.0000
THR 133
VAL 134
-0.0033
VAL 134
GLN 135
-0.0000
GLN 135
VAL 136
0.0052
VAL 136
VAL 137
-0.0004
VAL 137
ASP 138
0.0194
ASP 138
LEU 139
-0.0001
LEU 139
GLN 140
-0.0060
GLN 140
VAL 141
-0.0001
VAL 141
PHE 142
-0.0159
PHE 142
ALA 143
0.0001
ALA 143
GLN 144
-0.0311
GLN 144
PRO 145
-0.0003
PRO 145
ARG 146
-0.0191
ARG 146
ILE 147
0.0000
ILE 147
THR 148
-0.0067
THR 148
LEU 149
0.0001
LEU 149
LYS 150
0.0008
LYS 150
PRO 151
-0.0000
PRO 151
LEU 152
-0.0158
LEU 152
VAL 153
0.0001
VAL 153
PRO 154
0.0109
PRO 154
SER 155
0.0001
SER 155
PHE 156
-0.0210
PHE 156
PRO 157
-0.0001
PRO 157
CYS 158
-0.0056
CYS 158
PHE 159
0.0004
PHE 159
ALA 160
-0.0091
ALA 160
ASN 161
0.0001
ASN 161
ILE 162
-0.0037
ILE 162
TYR 163
-0.0000
TYR 163
VAL 164
-0.0010
VAL 164
SER 165
0.0002
SER 165
LEU 166
-0.0061
LEU 166
MET 167
0.0000
MET 167
GLU 168
-0.0252
GLU 168
LYS 169
0.0000
LYS 169
PRO 170
0.0211
PRO 170
HIS 171
0.0003
HIS 171
VAL 172
-0.0128
VAL 172
ASP 173
0.0000
ASP 173
PHE 174
0.0068
PHE 174
GLY 175
0.0000
GLY 175
LEU 176
0.0563
LEU 176
LYS 177
-0.0003
LYS 177
LEU 178
-0.0060
LEU 178
GLY 179
0.0001
GLY 179
GLY 180
-0.0052
GLY 180
ALA 181
-0.0001
ALA 181
ASP 182
-0.0040
ASP 182
LEU 183
-0.0002
LEU 183
MET 184
0.0235
MET 184
SER 185
0.0001
SER 185
ILE 186
-0.0186
ILE 186
PRO 187
0.0001
PRO 187
GLY 188
0.0044
GLY 188
LEU 189
0.0003
LEU 189
TYR 190
0.0148
TYR 190
ARG 191
0.0001
ARG 191
PHE 192
-0.0044
PHE 192
VAL 193
-0.0000
VAL 193
GLN 194
0.0071
GLN 194
GLU 195
-0.0003
GLU 195
GLN 196
0.0110
GLN 196
ILE 197
-0.0003
ILE 197
LYS 198
-0.0247
LYS 198
ASP 199
-0.0001
ASP 199
GLN 200
0.0283
GLN 200
VAL 201
-0.0003
VAL 201
ALA 202
-0.0075
ALA 202
ASN 203
0.0001
ASN 203
MET 204
0.0432
MET 204
TYR 205
0.0003
TYR 205
LEU 206
0.0323
LEU 206
TRP 207
0.0001
TRP 207
PRO 208
-0.0060
PRO 208
LYS 209
-0.0000
LYS 209
THR 210
0.0062
THR 210
LEU 211
0.0000
LEU 211
VAL 212
0.0096
VAL 212
VAL 213
0.0003
VAL 213
PRO 214
0.0060
PRO 214
ILE 215
0.0002
ILE 215
LEU 216
0.0053
LEU 216
ASP 217
0.0003
ASP 217
PRO 218
-0.0012
PRO 218
ALA 219
0.0000
ALA 219
LYS 220
0.0080
LYS 220
ALA 221
-0.0003
ALA 221
PHE 222
0.0030
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.