Should you encounter any unexpected behaviour,
please let us know. elNémo has been relocated.
**Some cleaning from time to time**
Sorry for the inconvenience.
***  9I43 Structure of anti-EV71 human monoclonal antibody 16-2-9D Fab  ***
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
GLN 1
VAL 2
0.0003
VAL 2
GLN 3
-0.0003
GLN 3
LEU 4
-0.0090
LEU 4
GLN 5
-0.0001
GLN 5
GLU 6
-0.0001
GLU 6
SER 7
-0.0206
SER 7
GLY 8
0.0001
GLY 8
PRO 9
0.0001
PRO 9
GLY 10
-0.0019
GLY 10
LEU 11
0.0001
LEU 11
VAL 12
-0.0003
VAL 12
VAL 12
-0.0000
VAL 12
LYS 13
-0.0238
LYS 13
PRO 14
0.0002
PRO 14
SER 15
-0.0000
SER 15
SER 15
0.0125
SER 15
GLU 16
0.0053
GLU 16
THR 17
0.0002
THR 17
THR 17
-0.0035
THR 17
LEU 18
0.0003
LEU 18
SER 19
0.0176
SER 19
SER 19
-0.0809
SER 19
LEU 20
-0.0000
LEU 20
THR 21
-0.0002
THR 21
CYS 22
0.0153
CYS 22
SER 23
0.0001
SER 23
VAL 24
-0.0004
VAL 24
SER 25
0.0045
SER 25
GLY 26
-0.0003
GLY 26
VAL 27
-0.0002
VAL 27
SER 28
0.0028
SER 28
ILE 29
-0.0002
ILE 29
SER 30
0.0002
SER 30
SER 30
-0.0353
SER 30
SER 31
0.0001
SER 31
ARG 32
-0.0002
ARG 32
THR 33
-0.0001
THR 33
TYR 34
-0.0015
TYR 34
TYR 35
-0.0002
TYR 35
TRP 36
-0.0002
TRP 36
GLY 37
0.0070
GLY 37
TRP 38
-0.0003
TRP 38
ILE 39
-0.0002
ILE 39
ARG 40
0.0144
ARG 40
GLN 41
-0.0001
GLN 41
PRO 42
-0.0002
PRO 42
PRO 43
0.0050
PRO 43
GLY 44
0.0001
GLY 44
LYS 45
-0.0002
LYS 45
GLY 46
0.0029
GLY 46
LEU 47
0.0002
LEU 47
GLU 48
-0.0000
GLU 48
TRP 49
0.0083
TRP 49
ILE 50
0.0001
ILE 50
GLY 51
-0.0001
GLY 51
THR 52
0.0081
THR 52
ILE 53
0.0002
ILE 53
TYR 54
-0.0001
TYR 54
TYR 55
0.0019
TYR 55
SER 56
-0.0002
SER 56
GLY 57
0.0000
GLY 57
ILE 58
-0.0032
ILE 58
ILE 58
0.0026
ILE 58
THR 59
0.0000
THR 59
HIS 60
-0.0001
HIS 60
TYR 61
0.0186
TYR 61
SER 62
0.0001
SER 62
PRO 63
-0.0000
PRO 63
SER 64
0.0004
SER 64
LEU 65
0.0002
LEU 65
LYS 66
-0.0004
LYS 66
SER 67
0.0286
SER 67
PRO 68
-0.0000
PRO 68
VAL 69
-0.0000
VAL 69
THR 70
0.0307
THR 70
ILE 71
-0.0001
ILE 71
SER 72
0.0002
SER 72
VAL 73
0.0396
VAL 73
ASP 74
0.0004
ASP 74
LYS 75
-0.0001
LYS 75
SER 76
0.0051
SER 76
LYS 77
0.0004
LYS 77
ASN 78
-0.0002
ASN 78
GLN 79
0.0062
GLN 79
PHE 80
0.0000
PHE 80
SER 81
-0.0001
SER 81
LEU 82
0.0327
LEU 82
GLU 83
-0.0002
GLU 83
LEU 84
0.0000
LEU 84
THR 85
-0.0070
THR 85
SER 86
0.0000
SER 86
VAL 87
0.0000
VAL 87
VAL 87
-0.0076
VAL 87
THR 88
-0.0078
THR 88
ALA 89
0.0003
ALA 89
ALA 90
-0.0000
ALA 90
ASP 91
-0.0133
ASP 91
THR 92
0.0002
THR 92
ALA 93
0.0000
ALA 93
MET 94
-0.0203
MET 94
TYR 95
0.0001
TYR 95
TYR 96
-0.0005
TYR 96
CYS 97
-0.0048
CYS 97
ALA 98
0.0002
ALA 98
ARG 99
0.0002
ARG 99
HIS 100
-0.0152
HIS 100
SER 101
-0.0003
SER 101
SER 102
0.0002
SER 102
PRO 103
-0.0038
PRO 103
GLN 104
0.0001
GLN 104
GLN 104
0.0244
GLN 104
CYS 105
-0.0001
CYS 105
SER 106
0.0054
SER 106
PRO 107
-0.0002
PRO 107
THR 108
-0.0000
THR 108
SER 109
0.0039
SER 109
CYS 110
0.0002
CYS 110
TYR 111
0.0003
TYR 111
GLU 112
0.0068
GLU 112
GLY 113
-0.0004
GLY 113
PRO 114
-0.0000
PRO 114
TYR 115
-0.0082
TYR 115
THR 116
0.0003
THR 116
ARG 117
-0.0002
ARG 117
ASP 118
-0.0043
ASP 118
TRP 119
0.0002
TRP 119
TYR 120
-0.0001
TYR 120
VAL 121
-0.0085
VAL 121
ASP 122
0.0001
ASP 122
TYR 123
-0.0002
TYR 123
TRP 124
-0.0173
TRP 124
GLY 125
0.0002
GLY 125
GLN 126
0.0003
GLN 126
GLY 127
-0.0240
GLY 127
VAL 128
0.0000
VAL 128
VAL 128
-0.0237
VAL 128
LEU 129
-0.0002
LEU 129
VAL 130
-0.0387
VAL 130
THR 131
-0.0001
THR 131
VAL 132
0.0001
VAL 132
SER 133
0.0237
SER 133
SER 134
-0.0002
SER 134
ALA 135
-0.0002
ALA 135
SER 136
0.0349
SER 136
THR 137
0.0001
THR 137
THR 137
0.0007
THR 137
LYS 138
-0.0003
LYS 138
GLY 139
0.0391
GLY 139
PRO 140
0.0003
PRO 140
SER 141
-0.0001
SER 141
VAL 142
0.0729
VAL 142
PHE 143
0.0005
PHE 143
PRO 144
-0.0000
PRO 144
LEU 145
0.0043
LEU 145
ALA 146
0.0000
ALA 146
PRO 147
0.0001
PRO 147
SER 148
-0.0030
SER 148
SER 149
-0.0002
SER 149
LYS 150
-0.0000
LYS 150
SER 151
0.0008
SER 151
THR 152
-0.0001
THR 152
SER 153
0.0003
SER 153
GLY 154
0.0042
GLY 154
GLY 155
-0.0002
GLY 155
THR 156
0.0000
THR 156
ALA 157
0.0018
ALA 157
ALA 158
0.0000
ALA 158
LEU 159
-0.0003
LEU 159
GLY 160
0.0112
GLY 160
CYS 161
0.0002
CYS 161
CYS 161
0.0059
CYS 161
LEU 162
0.0000
LEU 162
VAL 163
0.0107
VAL 163
LYS 164
-0.0002
LYS 164
ASP 165
0.0000
ASP 165
TYR 166
0.0524
TYR 166
PHE 167
-0.0002
PHE 167
PRO 168
0.0004
PRO 168
GLU 169
-0.0466
GLU 169
PRO 170
0.0002
PRO 170
VAL 171
-0.0002
VAL 171
THR 172
-0.0592
THR 172
VAL 173
-0.0000
VAL 173
SER 174
0.0001
SER 174
TRP 175
-0.0470
TRP 175
ASN 176
0.0001
ASN 176
SER 177
-0.0003
SER 177
GLY 178
0.0016
GLY 178
ALA 179
-0.0001
ALA 179
LEU 180
-0.0002
LEU 180
THR 181
0.0038
THR 181
SER 182
0.0002
SER 182
GLY 183
0.0001
GLY 183
VAL 184
-0.0160
VAL 184
HIS 185
-0.0004
HIS 185
THR 186
0.0000
THR 186
PHE 187
-0.0179
PHE 187
PRO 188
0.0001
PRO 188
ALA 189
-0.0002
ALA 189
VAL 190
-0.0142
VAL 190
LEU 191
-0.0001
LEU 191
GLN 192
0.0001
GLN 192
SER 193
-0.0179
SER 193
SER 194
-0.0003
SER 194
GLY 195
0.0000
GLY 195
LEU 196
-0.0037
LEU 196
TYR 197
-0.0001
TYR 197
SER 198
-0.0001
SER 198
LEU 199
0.0119
LEU 199
SER 200
0.0004
SER 200
SER 201
-0.0005
SER 201
VAL 202
-0.0056
VAL 202
VAL 203
-0.0000
VAL 203
THR 204
-0.0002
THR 204
VAL 205
-0.0117
VAL 205
PRO 206
0.0001
PRO 206
SER 207
0.0002
SER 207
SER 208
-0.0025
SER 208
SER 209
-0.0003
SER 209
LEU 210
0.0002
LEU 210
GLY 211
0.0037
GLY 211
THR 212
-0.0002
THR 212
GLN 213
0.0001
GLN 213
THR 214
0.0009
THR 214
TYR 215
-0.0004
TYR 215
ILE 216
0.0002
ILE 216
CYS 217
-0.0153
CYS 217
CYS 217
-0.0009
CYS 217
ASN 218
0.0000
ASN 218
VAL 219
-0.0002
VAL 219
ASN 220
-0.1657
ASN 220
HIS 221
0.0003
HIS 221
LYS 222
-0.0003
LYS 222
PRO 223
-0.0055
PRO 223
SER 224
0.0000
SER 224
ASN 225
0.0002
ASN 225
THR 226
-0.0154
THR 226
LYS 227
0.0003
LYS 227
VAL 228
0.0002
VAL 228
ASP 229
0.0028
ASP 229
LYS 230
0.0001
LYS 230
LYS 230
-0.1115
LYS 230
LYS 231
-0.0002
LYS 231
VAL 232
-0.0092
VAL 232
GLU 233
-0.0002
GLU 233
PRO 234
-0.0002
PRO 234
LYS 235
0.0072
LYS 235
ALA 3
-0.0054
ALA 3
LEU 4
0.0002
LEU 4
THR 5
-0.0002
THR 5
GLN 6
0.0171
GLN 6
PRO 7
0.0000
PRO 7
PRO 8
-0.0001
PRO 8
SER 9
0.0055
SER 9
SER 9
-0.0015
SER 9
ALA 10
-0.0000
ALA 10
SER 11
-0.0004
SER 11
GLY 12
-0.0366
GLY 12
THR 13
-0.0001
THR 13
PRO 14
0.0001
PRO 14
GLY 15
-0.0195
GLY 15
GLN 16
-0.0000
GLN 16
ARG 17
0.0003
ARG 17
VAL 18
-0.0142
VAL 18
THR 19
-0.0004
THR 19
ILE 20
0.0000
ILE 20
ILE 20
0.0085
ILE 20
SER 21
0.0014
SER 21
CYS 22
0.0002
CYS 22
SER 23
0.0003
SER 23
SER 23
-0.0494
SER 23
GLY 24
0.0094
GLY 24
SER 25
0.0001
SER 25
SER 26
0.0002
SER 26
SER 27
-0.0007
SER 27
ASN 28
-0.0002
ASN 28
ILE 29
-0.0003
ILE 29
ARG 30
0.0008
ARG 30
SER 31
-0.0000
SER 31
SER 31
0.0405
SER 31
ASN 32
0.0002
ASN 32
THR 33
-0.0070
THR 33
VAL 34
-0.0003
VAL 34
ASN 35
0.0003
ASN 35
TRP 36
-0.0066
TRP 36
TYR 37
-0.0000
TYR 37
GLN 38
0.0004
GLN 38
LYS 39
-0.0067
LYS 39
LEU 40
-0.0004
LEU 40
PRO 41
0.0001
PRO 41
GLY 42
-0.0168
GLY 42
ALA 43
-0.0002
ALA 43
ALA 44
0.0000
ALA 44
PRO 45
-0.0014
PRO 45
THR 46
0.0004
THR 46
LEU 47
-0.0000
LEU 47
LEU 48
0.0146
LEU 48
ILE 49
0.0001
ILE 49
TYR 50
-0.0003
TYR 50
THR 51
-0.0020
THR 51
ASN 52
-0.0000
ASN 52
ASN 53
-0.0003
ASN 53
GLN 54
-0.0031
GLN 54
ARG 55
-0.0005
ARG 55
PRO 56
-0.0000
PRO 56
SER 57
-0.0006
SER 57
GLY 58
0.0002
GLY 58
VAL 59
0.0002
VAL 59
PRO 60
0.0032
PRO 60
ASP 61
0.0002
ASP 61
ASP 61
0.0000
ASP 61
ARG 62
0.0002
ARG 62
PHE 63
-0.0017
PHE 63
SER 64
-0.0002
SER 64
GLY 65
0.0001
GLY 65
SER 66
-0.0315
SER 66
LYS 67
0.0002
LYS 67
SER 68
-0.0005
SER 68
GLY 69
-0.0096
GLY 69
THR 70
-0.0002
THR 70
SER 71
0.0001
SER 71
SER 71
-0.0022
SER 71
ALA 72
-0.0065
ALA 72
SER 73
-0.0001
SER 73
SER 73
-0.0070
SER 73
SER 73
-0.0206
SER 73
LEU 74
-0.0001
LEU 74
ALA 75
-0.0087
ALA 75
ILE 76
-0.0003
ILE 76
SER 77
0.0002
SER 77
SER 77
0.0272
SER 77
GLY 78
-0.0124
GLY 78
LEU 79
0.0001
LEU 79
GLN 80
-0.0004
GLN 80
GLN 80
0.0060
GLN 80
SER 81
-0.0532
SER 81
GLU 82
-0.0004
GLU 82
ASP 83
0.0001
ASP 83
GLU 84
0.0456
GLU 84
ALA 85
-0.0001
ALA 85
ASP 86
0.0000
ASP 86
TYR 87
0.0140
TYR 87
PHE 88
-0.0002
PHE 88
CYS 89
0.0000
CYS 89
ALA 90
0.0055
ALA 90
ALA 91
0.0001
ALA 91
TRP 92
0.0001
TRP 92
ASP 93
-0.0011
ASP 93
GLY 94
-0.0003
GLY 94
SER 95
-0.0000
SER 95
LEU 96
0.0011
LEU 96
ASN 97
-0.0000
ASN 97
ALA 98
0.0002
ALA 98
VAL 99
-0.0003
VAL 99
VAL 100
-0.0000
VAL 100
PHE 101
0.0004
PHE 101
GLY 102
0.0048
GLY 102
GLY 103
-0.0003
GLY 103
GLY 104
-0.0002
GLY 104
THR 105
0.0055
THR 105
LYS 106
-0.0000
LYS 106
LEU 107
-0.0001
LEU 107
THR 108
0.0402
THR 108
VAL 109
-0.0002
VAL 109
LEU 110
-0.0002
LEU 110
GLY 111
-0.0088
GLY 111
GLN 112
-0.0001
GLN 112
GLN 112
0.0778
GLN 112
PRO 113
0.0002
PRO 113
LYS 114
0.0079
LYS 114
ALA 115
-0.0002
ALA 115
ASN 116
0.0002
ASN 116
PRO 117
0.0144
PRO 117
THR 118
-0.0002
THR 118
VAL 119
0.0001
VAL 119
THR 120
0.0145
THR 120
LEU 121
0.0005
LEU 121
PHE 122
0.0001
PHE 122
PRO 123
-0.0052
PRO 123
PRO 124
0.0004
PRO 124
SER 125
-0.0002
SER 125
SER 126
-0.0062
SER 126
GLU 127
-0.0002
GLU 127
GLU 128
0.0002
GLU 128
LEU 129
-0.0113
LEU 129
GLN 130
-0.0001
GLN 130
ALA 131
0.0001
ALA 131
ASN 132
-0.0052
ASN 132
LYS 133
0.0001
LYS 133
ALA 134
-0.0003
ALA 134
THR 135
0.0059
THR 135
LEU 136
-0.0001
LEU 136
VAL 137
-0.0002
VAL 137
CYS 138
-0.0094
CYS 138
LEU 139
0.0003
LEU 139
ILE 140
-0.0002
ILE 140
SER 141
-0.0371
SER 141
ASP 142
-0.0001
ASP 142
PHE 143
0.0000
PHE 143
TYR 144
0.0271
TYR 144
PRO 145
0.0000
PRO 145
GLY 146
-0.0001
GLY 146
ALA 147
0.0403
ALA 147
VAL 148
-0.0004
VAL 148
VAL 148
-0.0112
VAL 148
THR 149
-0.0000
THR 149
THR 149
-0.0014
THR 149
VAL 150
0.0128
VAL 150
ALA 151
-0.0003
ALA 151
TRP 152
0.0002
TRP 152
LYS 153
0.0137
LYS 153
ALA 154
-0.0004
ALA 154
ASP 155
0.0001
ASP 155
SER 156
-0.0040
SER 156
SER 157
-0.0002
SER 157
PRO 158
0.0001
PRO 158
VAL 159
0.0029
VAL 159
LYS 160
0.0000
LYS 160
ALA 161
0.0001
ALA 161
GLY 162
0.0090
GLY 162
VAL 163
-0.0000
VAL 163
GLU 164
0.0001
GLU 164
THR 165
0.0206
THR 165
THR 166
0.0001
THR 166
THR 167
-0.0001
THR 167
THR 167
-0.0236
THR 167
PRO 168
0.0184
PRO 168
SER 169
0.0001
SER 169
LYS 170
0.0005
LYS 170
LYS 170
-0.0310
LYS 170
GLN 171
0.0145
GLN 171
SER 172
-0.0003
SER 172
ASN 173
-0.0002
ASN 173
ASN 174
0.0174
ASN 174
LYS 175
-0.0004
LYS 175
TYR 176
-0.0001
TYR 176
ALA 177
-0.0103
ALA 177
ALA 178
0.0001
ALA 178
SER 179
0.0002
SER 179
SER 179
-0.0043
SER 179
SER 180
0.0026
SER 180
TYR 181
-0.0000
TYR 181
LEU 182
0.0001
LEU 182
SER 183
0.0034
SER 183
LEU 184
-0.0001
LEU 184
THR 185
0.0002
THR 185
PRO 186
0.0057
PRO 186
GLU 187
0.0004
GLU 187
GLN 188
0.0001
GLN 188
TRP 189
-0.0010
TRP 189
LYS 190
0.0000
LYS 190
SER 191
-0.0001
SER 191
HIS 192
-0.0006
HIS 192
ARG 193
-0.0000
ARG 193
SER 194
0.0003
SER 194
TYR 195
0.0036
TYR 195
SER 196
-0.0001
SER 196
CYS 197
-0.0000
CYS 197
GLN 198
0.0053
GLN 198
VAL 199
-0.0003
VAL 199
THR 200
-0.0001
THR 200
HIS 201
0.0076
HIS 201
GLU 202
-0.0001
GLU 202
GLY 203
-0.0002
GLY 203
SER 204
0.0106
SER 204
THR 205
0.0003
THR 205
VAL 206
0.0002
VAL 206
GLU 207
0.0069
GLU 207
LYS 208
-0.0001
LYS 208
THR 209
0.0001
THR 209
VAL 210
0.0086
VAL 210
ALA 211
-0.0001
ALA 211
PRO 212
-0.0003
PRO 212
THR 213
-0.0026
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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.