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
0.0001
VAL 2
GLN 3
-0.0002
GLN 3
LEU 4
-0.0227
LEU 4
GLN 5
-0.0004
GLN 5
GLU 6
-0.0001
GLU 6
SER 7
-0.0589
SER 7
GLY 8
0.0002
GLY 8
PRO 9
-0.0004
PRO 9
GLY 10
-0.0527
GLY 10
LEU 11
0.0001
LEU 11
VAL 12
0.0001
VAL 12
VAL 12
-0.0340
VAL 12
LYS 13
-0.0002
LYS 13
PRO 14
0.0002
PRO 14
SER 15
0.0001
SER 15
SER 15
-0.0460
SER 15
GLU 16
0.0021
GLU 16
THR 17
-0.0002
THR 17
THR 17
-0.0194
THR 17
LEU 18
0.0003
LEU 18
SER 19
-0.0530
SER 19
SER 19
0.0809
SER 19
LEU 20
-0.0001
LEU 20
THR 21
0.0001
THR 21
CYS 22
-0.0422
CYS 22
SER 23
0.0000
SER 23
VAL 24
-0.0000
VAL 24
SER 25
-0.0231
SER 25
GLY 26
-0.0002
GLY 26
VAL 27
-0.0001
VAL 27
SER 28
0.0153
SER 28
ILE 29
0.0001
ILE 29
SER 30
0.0000
SER 30
SER 30
0.0047
SER 30
SER 31
-0.0168
SER 31
ARG 32
0.0002
ARG 32
THR 33
0.0004
THR 33
TYR 34
-0.0009
TYR 34
TYR 35
-0.0001
TYR 35
TRP 36
-0.0002
TRP 36
GLY 37
0.0028
GLY 37
TRP 38
-0.0002
TRP 38
ILE 39
-0.0001
ILE 39
ARG 40
0.0078
ARG 40
GLN 41
0.0002
GLN 41
PRO 42
0.0000
PRO 42
PRO 43
-0.0102
PRO 43
GLY 44
-0.0002
GLY 44
LYS 45
-0.0000
LYS 45
GLY 46
0.0260
GLY 46
LEU 47
0.0001
LEU 47
GLU 48
0.0000
GLU 48
TRP 49
-0.0078
TRP 49
ILE 50
0.0002
ILE 50
GLY 51
-0.0003
GLY 51
THR 52
-0.0147
THR 52
ILE 53
0.0002
ILE 53
TYR 54
-0.0001
TYR 54
TYR 55
-0.0036
TYR 55
SER 56
0.0003
SER 56
GLY 57
0.0001
GLY 57
ILE 58
-0.0065
ILE 58
ILE 58
-0.0128
ILE 58
THR 59
0.0000
THR 59
HIS 60
-0.0003
HIS 60
TYR 61
-0.0018
TYR 61
SER 62
0.0001
SER 62
PRO 63
-0.0001
PRO 63
SER 64
-0.0021
SER 64
LEU 65
0.0002
LEU 65
LYS 66
0.0003
LYS 66
SER 67
0.0669
SER 67
PRO 68
-0.0001
PRO 68
VAL 69
0.0002
VAL 69
THR 70
-0.0039
THR 70
ILE 71
0.0003
ILE 71
SER 72
-0.0003
SER 72
VAL 73
-0.0140
VAL 73
ASP 74
-0.0002
ASP 74
LYS 75
-0.0000
LYS 75
SER 76
-0.0075
SER 76
LYS 77
-0.0003
LYS 77
ASN 78
-0.0001
ASN 78
GLN 79
-0.0156
GLN 79
PHE 80
-0.0001
PHE 80
SER 81
0.0000
SER 81
LEU 82
-0.0195
LEU 82
GLU 83
-0.0003
GLU 83
LEU 84
0.0002
LEU 84
THR 85
-0.0075
THR 85
SER 86
0.0004
SER 86
VAL 87
-0.0002
VAL 87
VAL 87
0.0017
VAL 87
THR 88
-0.0165
THR 88
ALA 89
0.0001
ALA 89
ALA 90
-0.0001
ALA 90
ASP 91
-0.0254
ASP 91
THR 92
-0.0001
THR 92
ALA 93
0.0000
ALA 93
MET 94
-0.0220
MET 94
TYR 95
0.0004
TYR 95
TYR 96
0.0001
TYR 96
CYS 97
-0.0046
CYS 97
ALA 98
0.0000
ALA 98
ARG 99
0.0004
ARG 99
HIS 100
-0.0295
HIS 100
SER 101
-0.0001
SER 101
SER 102
-0.0000
SER 102
PRO 103
-0.0049
PRO 103
GLN 104
-0.0003
GLN 104
GLN 104
0.0294
GLN 104
CYS 105
0.0000
CYS 105
SER 106
-0.0006
SER 106
PRO 107
-0.0003
PRO 107
THR 108
-0.0001
THR 108
SER 109
-0.0044
SER 109
CYS 110
0.0002
CYS 110
TYR 111
-0.0001
TYR 111
GLU 112
-0.0064
GLU 112
GLY 113
-0.0001
GLY 113
PRO 114
-0.0003
PRO 114
TYR 115
-0.0156
TYR 115
THR 116
-0.0004
THR 116
ARG 117
-0.0001
ARG 117
ASP 118
0.0169
ASP 118
TRP 119
-0.0000
TRP 119
TYR 120
-0.0001
TYR 120
VAL 121
-0.0025
VAL 121
ASP 122
0.0000
ASP 122
TYR 123
0.0001
TYR 123
TRP 124
-0.0175
TRP 124
GLY 125
-0.0003
GLY 125
GLN 126
0.0001
GLN 126
GLY 127
-0.0282
GLY 127
VAL 128
-0.0001
VAL 128
VAL 128
-0.0063
VAL 128
LEU 129
-0.0001
LEU 129
VAL 130
-0.0276
VAL 130
THR 131
-0.0003
THR 131
VAL 132
0.0000
VAL 132
SER 133
0.1016
SER 133
SER 134
-0.0003
SER 134
ALA 135
-0.0000
ALA 135
SER 136
0.1250
SER 136
THR 137
-0.0003
THR 137
THR 137
0.0028
THR 137
LYS 138
0.0003
LYS 138
GLY 139
0.0710
GLY 139
PRO 140
-0.0000
PRO 140
SER 141
-0.0001
SER 141
VAL 142
0.0359
VAL 142
PHE 143
0.0001
PHE 143
PRO 144
0.0002
PRO 144
LEU 145
0.0096
LEU 145
ALA 146
-0.0001
ALA 146
PRO 147
-0.0002
PRO 147
SER 148
0.0184
SER 148
SER 149
-0.0001
SER 149
LYS 150
-0.0002
LYS 150
SER 151
0.0002
SER 151
THR 152
-0.0001
THR 152
SER 153
0.0001
SER 153
GLY 154
-0.0016
GLY 154
GLY 155
-0.0000
GLY 155
THR 156
0.0003
THR 156
ALA 157
0.0015
ALA 157
ALA 158
-0.0002
ALA 158
LEU 159
0.0002
LEU 159
GLY 160
0.0053
GLY 160
CYS 161
-0.0000
CYS 161
CYS 161
-0.0073
CYS 161
LEU 162
-0.0001
LEU 162
VAL 163
0.0078
VAL 163
LYS 164
-0.0002
LYS 164
ASP 165
0.0002
ASP 165
TYR 166
-0.0348
TYR 166
PHE 167
0.0001
PHE 167
PRO 168
-0.0004
PRO 168
GLU 169
-0.0074
GLU 169
PRO 170
0.0000
PRO 170
VAL 171
0.0000
VAL 171
THR 172
0.0117
THR 172
VAL 173
0.0001
VAL 173
SER 174
0.0002
SER 174
TRP 175
0.0337
TRP 175
ASN 176
0.0001
ASN 176
SER 177
0.0000
SER 177
GLY 178
0.0058
GLY 178
ALA 179
0.0002
ALA 179
LEU 180
-0.0004
LEU 180
THR 181
-0.0172
THR 181
SER 182
0.0004
SER 182
GLY 183
0.0001
GLY 183
VAL 184
0.0164
VAL 184
HIS 185
-0.0003
HIS 185
THR 186
0.0000
THR 186
PHE 187
-0.0167
PHE 187
PRO 188
-0.0001
PRO 188
ALA 189
0.0003
ALA 189
VAL 190
0.0053
VAL 190
LEU 191
-0.0003
LEU 191
GLN 192
0.0002
GLN 192
SER 193
0.0436
SER 193
SER 194
0.0004
SER 194
GLY 195
0.0001
GLY 195
LEU 196
0.0034
LEU 196
TYR 197
0.0001
TYR 197
SER 198
-0.0000
SER 198
LEU 199
-0.0336
LEU 199
SER 200
0.0001
SER 200
SER 201
-0.0003
SER 201
VAL 202
0.0039
VAL 202
VAL 203
0.0001
VAL 203
THR 204
0.0000
THR 204
VAL 205
-0.0531
VAL 205
PRO 206
0.0000
PRO 206
SER 207
-0.0002
SER 207
SER 208
-0.0090
SER 208
SER 209
0.0001
SER 209
LEU 210
-0.0002
LEU 210
GLY 211
-0.0137
GLY 211
THR 212
-0.0002
THR 212
GLN 213
-0.0003
GLN 213
THR 214
0.0361
THR 214
TYR 215
-0.0002
TYR 215
ILE 216
0.0001
ILE 216
CYS 217
0.0236
CYS 217
CYS 217
0.0651
CYS 217
ASN 218
-0.0001
ASN 218
VAL 219
0.0000
VAL 219
ASN 220
0.0933
ASN 220
HIS 221
-0.0004
HIS 221
LYS 222
0.0001
LYS 222
PRO 223
0.0557
PRO 223
SER 224
0.0005
SER 224
ASN 225
-0.0002
ASN 225
THR 226
0.0512
THR 226
LYS 227
-0.0002
LYS 227
VAL 228
0.0002
VAL 228
ASP 229
0.0763
ASP 229
LYS 230
-0.0001
LYS 230
LYS 230
-0.1115
LYS 230
LYS 231
-0.0001
LYS 231
VAL 232
0.0187
VAL 232
GLU 233
0.0003
GLU 233
PRO 234
-0.0001
PRO 234
LYS 235
0.0230
LYS 235
ALA 3
-0.0309
ALA 3
LEU 4
-0.0002
LEU 4
THR 5
0.0001
THR 5
GLN 6
-0.0719
GLN 6
PRO 7
-0.0003
PRO 7
PRO 8
0.0000
PRO 8
SER 9
-0.0345
SER 9
SER 9
0.0055
SER 9
ALA 10
0.0001
ALA 10
SER 11
0.0001
SER 11
GLY 12
0.0216
GLY 12
THR 13
0.0000
THR 13
PRO 14
0.0001
PRO 14
GLY 15
0.0677
GLY 15
GLN 16
-0.0001
GLN 16
ARG 17
0.0001
ARG 17
VAL 18
-0.0042
VAL 18
THR 19
-0.0001
THR 19
ILE 20
0.0001
ILE 20
ILE 20
0.0027
ILE 20
SER 21
-0.0534
SER 21
CYS 22
0.0002
CYS 22
SER 23
0.0002
SER 23
SER 23
-0.0227
SER 23
GLY 24
-0.0547
GLY 24
SER 25
-0.0006
SER 25
SER 26
0.0005
SER 26
SER 27
0.0024
SER 27
ASN 28
-0.0004
ASN 28
ILE 29
0.0001
ILE 29
ARG 30
0.0088
ARG 30
SER 31
0.0000
SER 31
SER 31
0.0178
SER 31
ASN 32
-0.0004
ASN 32
THR 33
0.0169
THR 33
VAL 34
-0.0001
VAL 34
ASN 35
0.0003
ASN 35
TRP 36
0.0177
TRP 36
TYR 37
-0.0002
TYR 37
GLN 38
0.0002
GLN 38
LYS 39
-0.0320
LYS 39
LEU 40
-0.0002
LEU 40
PRO 41
0.0001
PRO 41
GLY 42
0.0586
GLY 42
ALA 43
0.0003
ALA 43
ALA 44
-0.0003
ALA 44
PRO 45
-0.0166
PRO 45
THR 46
0.0003
THR 46
LEU 47
-0.0001
LEU 47
LEU 48
-0.0167
LEU 48
ILE 49
-0.0002
ILE 49
TYR 50
0.0003
TYR 50
THR 51
0.0107
THR 51
ASN 52
0.0001
ASN 52
ASN 53
-0.0000
ASN 53
GLN 54
-0.0003
GLN 54
ARG 55
-0.0003
ARG 55
PRO 56
-0.0001
PRO 56
SER 57
0.0104
SER 57
GLY 58
-0.0001
GLY 58
VAL 59
-0.0001
VAL 59
PRO 60
0.0174
PRO 60
ASP 61
0.0004
ASP 61
ASP 61
-0.0077
ASP 61
ARG 62
0.0002
ARG 62
PHE 63
0.0088
PHE 63
SER 64
0.0000
SER 64
GLY 65
-0.0003
GLY 65
SER 66
0.0325
SER 66
LYS 67
-0.0000
LYS 67
SER 68
0.0003
SER 68
GLY 69
0.0095
GLY 69
THR 70
-0.0002
THR 70
SER 71
-0.0001
SER 71
SER 71
-0.0035
SER 71
ALA 72
-0.0017
ALA 72
SER 73
0.0002
SER 73
SER 73
0.0064
SER 73
SER 73
0.0091
SER 73
LEU 74
-0.0001
LEU 74
ALA 75
0.0068
ALA 75
ILE 76
-0.0002
ILE 76
SER 77
0.0001
SER 77
SER 77
0.0156
SER 77
GLY 78
-0.0094
GLY 78
LEU 79
-0.0000
LEU 79
GLN 80
0.0001
GLN 80
GLN 80
0.0086
GLN 80
SER 81
-0.0128
SER 81
GLU 82
0.0003
GLU 82
ASP 83
-0.0002
ASP 83
GLU 84
-0.0070
GLU 84
ALA 85
0.0000
ALA 85
ASP 86
-0.0002
ASP 86
TYR 87
-0.0251
TYR 87
PHE 88
-0.0000
PHE 88
CYS 89
0.0003
CYS 89
ALA 90
-0.0291
ALA 90
ALA 91
-0.0001
ALA 91
TRP 92
0.0004
TRP 92
ASP 93
-0.0105
ASP 93
GLY 94
-0.0001
GLY 94
SER 95
-0.0002
SER 95
LEU 96
0.0266
LEU 96
ASN 97
-0.0003
ASN 97
ALA 98
-0.0004
ALA 98
VAL 99
-0.0226
VAL 99
VAL 100
0.0001
VAL 100
PHE 101
-0.0000
PHE 101
GLY 102
-0.0544
GLY 102
GLY 103
-0.0000
GLY 103
GLY 104
0.0002
GLY 104
THR 105
-0.0390
THR 105
LYS 106
0.0002
LYS 106
LEU 107
0.0001
LEU 107
THR 108
-0.0601
THR 108
VAL 109
-0.0006
VAL 109
LEU 110
-0.0000
LEU 110
GLY 111
-0.1466
GLY 111
GLN 112
-0.0003
GLN 112
GLN 112
-0.0028
GLN 112
PRO 113
0.0000
PRO 113
LYS 114
0.0397
LYS 114
ALA 115
-0.0002
ALA 115
ASN 116
0.0003
ASN 116
PRO 117
-0.0366
PRO 117
THR 118
-0.0000
THR 118
VAL 119
0.0000
VAL 119
THR 120
-0.1070
THR 120
LEU 121
0.0001
LEU 121
PHE 122
0.0001
PHE 122
PRO 123
-0.0434
PRO 123
PRO 124
-0.0001
PRO 124
SER 125
-0.0001
SER 125
SER 126
-0.0172
SER 126
GLU 127
-0.0002
GLU 127
GLU 128
-0.0000
GLU 128
LEU 129
0.0047
LEU 129
GLN 130
-0.0001
GLN 130
ALA 131
0.0002
ALA 131
ASN 132
0.0014
ASN 132
LYS 133
-0.0003
LYS 133
ALA 134
0.0000
ALA 134
THR 135
-0.0091
THR 135
LEU 136
-0.0002
LEU 136
VAL 137
-0.0001
VAL 137
CYS 138
-0.0312
CYS 138
LEU 139
0.0001
LEU 139
ILE 140
-0.0003
ILE 140
SER 141
-0.0855
SER 141
ASP 142
-0.0000
ASP 142
PHE 143
0.0001
PHE 143
TYR 144
-0.0574
TYR 144
PRO 145
-0.0000
PRO 145
GLY 146
-0.0001
GLY 146
ALA 147
0.1600
ALA 147
VAL 148
0.0001
VAL 148
VAL 148
0.0125
VAL 148
THR 149
-0.0001
THR 149
THR 149
-0.0067
THR 149
VAL 150
0.1068
VAL 150
ALA 151
0.0004
ALA 151
TRP 152
-0.0004
TRP 152
LYS 153
0.0171
LYS 153
ALA 154
0.0003
ALA 154
ASP 155
0.0001
ASP 155
SER 156
-0.0035
SER 156
SER 157
0.0000
SER 157
PRO 158
-0.0002
PRO 158
VAL 159
-0.0180
VAL 159
LYS 160
-0.0000
LYS 160
ALA 161
0.0002
ALA 161
GLY 162
-0.0294
GLY 162
VAL 163
0.0000
VAL 163
GLU 164
0.0002
GLU 164
THR 165
0.0572
THR 165
THR 166
0.0002
THR 166
THR 167
-0.0000
THR 167
THR 167
0.0165
THR 167
PRO 168
0.0632
PRO 168
SER 169
-0.0003
SER 169
LYS 170
0.0003
LYS 170
LYS 170
0.0047
LYS 170
GLN 171
-0.0563
GLN 171
SER 172
-0.0002
SER 172
ASN 173
0.0001
ASN 173
ASN 174
0.0001
ASN 174
LYS 175
0.0001
LYS 175
TYR 176
-0.0003
TYR 176
ALA 177
-0.0686
ALA 177
ALA 178
0.0004
ALA 178
SER 179
-0.0002
SER 179
SER 179
0.0035
SER 179
SER 180
-0.0099
SER 180
TYR 181
-0.0001
TYR 181
LEU 182
0.0002
LEU 182
SER 183
0.0176
SER 183
LEU 184
-0.0002
LEU 184
THR 185
-0.0000
THR 185
PRO 186
0.0128
PRO 186
GLU 187
0.0002
GLU 187
GLN 188
0.0003
GLN 188
TRP 189
0.0006
TRP 189
LYS 190
0.0004
LYS 190
SER 191
0.0003
SER 191
HIS 192
0.0001
HIS 192
ARG 193
-0.0003
ARG 193
SER 194
-0.0001
SER 194
TYR 195
-0.0032
TYR 195
SER 196
-0.0000
SER 196
CYS 197
0.0001
CYS 197
GLN 198
0.0378
GLN 198
VAL 199
0.0000
VAL 199
THR 200
-0.0002
THR 200
HIS 201
0.1078
HIS 201
GLU 202
0.0004
GLU 202
GLY 203
0.0001
GLY 203
SER 204
0.0042
SER 204
THR 205
0.0001
THR 205
VAL 206
-0.0003
VAL 206
GLU 207
0.0090
GLU 207
LYS 208
0.0001
LYS 208
THR 209
-0.0002
THR 209
VAL 210
-0.0032
VAL 210
ALA 211
-0.0003
ALA 211
PRO 212
0.0002
PRO 212
THR 213
0.0293
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.