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***  7D9Z Crystal structure of anti-basigin Fab fragment  ***
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
ALA 1
ASP 2
0.0001
ASP 2
VAL 3
0.0004
VAL 3
VAL 4
-0.0707
VAL 4
MET 5
0.0001
MET 5
THR 6
0.0001
THR 6
GLN 7
-0.0766
GLN 7
THR 8
0.0005
THR 8
PRO 9
-0.0003
PRO 9
SER 10
0.0150
SER 10
SER 10
0.0123
SER 10
SER 11
0.0000
SER 11
VAL 12
-0.0000
VAL 12
VAL 12
-0.0082
VAL 12
SER 13
-0.0645
SER 13
SER 13
0.0067
SER 13
ALA 14
0.0001
ALA 14
ALA 15
-0.0003
ALA 15
VAL 16
-0.0342
VAL 16
GLY 17
-0.0002
GLY 17
GLY 18
0.0001
GLY 18
THR 19
-0.0424
THR 19
VAL 20
-0.0005
VAL 20
THR 21
0.0005
THR 21
THR 21
-0.0004
THR 21
ILE 22
-0.0244
ILE 22
ASN 23
-0.0001
ASN 23
CYS 24
0.0002
CYS 24
CYS 24
-0.0012
CYS 24
GLN 25
-0.0209
GLN 25
GLN 25
0.0041
GLN 25
ALA 26
0.0002
ALA 26
SER 27
-0.0001
SER 27
GLN 28
-0.0254
GLN 28
SER 29
-0.0000
SER 29
ILE 30
0.0002
ILE 30
SER 31
0.0152
SER 31
SER 31
-0.0148
SER 31
ALA 32
-0.0003
ALA 32
TYR 33
-0.0002
TYR 33
LEU 34
-0.0012
LEU 34
ALA 35
0.0003
ALA 35
TRP 36
-0.0004
TRP 36
TYR 37
-0.0010
TYR 37
GLN 38
0.0002
GLN 38
GLN 39
0.0001
GLN 39
LYS 40
0.0195
LYS 40
PRO 41
0.0002
PRO 41
GLY 42
-0.0003
GLY 42
GLN 43
0.0281
GLN 43
PRO 44
-0.0002
PRO 44
PRO 45
0.0003
PRO 45
LYS 46
-0.0756
LYS 46
LEU 47
-0.0001
LEU 47
LEU 48
-0.0005
LEU 48
ILE 49
-0.0163
ILE 49
ILE 49
0.0196
ILE 49
TYR 50
-0.0000
TYR 50
ASP 51
0.0001
ASP 51
ALA 52
-0.0243
ALA 52
SER 53
0.0000
SER 53
ASP 54
-0.0003
ASP 54
LEU 55
0.0142
LEU 55
ALA 56
0.0001
ALA 56
SER 57
-0.0001
SER 57
SER 57
-0.0561
SER 57
GLY 58
0.0249
GLY 58
VAL 59
-0.0001
VAL 59
SER 60
0.0002
SER 60
SER 61
-0.0195
SER 61
ARG 62
-0.0001
ARG 62
PHE 63
-0.0001
PHE 63
LYS 64
0.0071
LYS 64
GLY 65
-0.0002
GLY 65
SER 66
-0.0001
SER 66
GLY 67
0.0107
GLY 67
SER 68
0.0004
SER 68
GLY 69
-0.0005
GLY 69
THR 70
-0.0059
THR 70
GLN 71
0.0002
GLN 71
PHE 72
0.0002
PHE 72
THR 73
-0.0235
THR 73
LEU 74
0.0001
LEU 74
THR 75
0.0000
THR 75
ILE 76
-0.0096
ILE 76
SER 77
-0.0001
SER 77
SER 77
-0.0604
SER 77
ASP 78
-0.0004
ASP 78
LEU 79
-0.0169
LEU 79
GLU 80
-0.0002
GLU 80
CYS 81
0.0001
CYS 81
ALA 82
0.0510
ALA 82
ASP 83
0.0002
ASP 83
ALA 84
-0.0001
ALA 84
ALA 85
-0.0153
ALA 85
THR 86
0.0002
THR 86
TYR 87
-0.0002
TYR 87
TYR 88
-0.0171
TYR 88
CYS 89
0.0001
CYS 89
CYS 89
-0.0035
CYS 89
GLN 90
0.0002
GLN 90
THR 91
-0.0027
THR 91
TYR 92
-0.0000
TYR 92
TYR 93
0.0000
TYR 93
ALA 94
0.0085
ALA 94
ILE 95
-0.0001
ILE 95
ILE 96
-0.0004
ILE 96
THR 97
-0.0521
THR 97
TYR 98
0.0003
TYR 98
GLY 99
0.0003
GLY 99
ALA 100
0.0142
ALA 100
ALA 101
0.0000
ALA 101
PHE 102
0.0002
PHE 102
GLY 103
-0.0569
GLY 103
GLY 104
-0.0000
GLY 104
GLY 105
-0.0001
GLY 105
THR 106
-0.0497
THR 106
GLU 107
-0.0001
GLU 107
GLU 107
-0.0517
GLU 107
VAL 108
0.0001
VAL 108
VAL 109
-0.0210
VAL 109
VAL 110
0.0002
VAL 110
LYS 111
-0.0002
LYS 111
ARG 112
-0.1689
ARG 112
THR 113
0.0002
THR 113
VAL 114
-0.0001
VAL 114
ALA 115
-0.0408
ALA 115
ALA 116
-0.0000
ALA 116
PRO 117
-0.0004
PRO 117
SER 118
-0.0208
SER 118
SER 118
-0.0147
SER 118
VAL 119
0.0000
VAL 119
PHE 120
-0.0002
PHE 120
ILE 121
-0.0306
ILE 121
PHE 122
0.0002
PHE 122
PRO 123
-0.0003
PRO 123
PRO 124
-0.0006
PRO 124
SER 125
0.0002
SER 125
ASP 126
-0.0001
ASP 126
GLU 127
0.0069
GLU 127
GLN 128
0.0004
GLN 128
LEU 129
-0.0001
LEU 129
LYS 130
0.0051
LYS 130
SER 131
-0.0002
SER 131
GLY 132
-0.0002
GLY 132
THR 133
0.0152
THR 133
ALA 134
-0.0002
ALA 134
SER 135
0.0000
SER 135
VAL 136
-0.0127
VAL 136
VAL 137
-0.0001
VAL 137
CYS 138
-0.0001
CYS 138
LEU 139
-0.0075
LEU 139
LEU 140
-0.0000
LEU 140
ASN 141
0.0002
ASN 141
ASN 142
-0.0433
ASN 142
ASN 142
0.0079
ASN 142
PHE 143
-0.0001
PHE 143
TYR 144
0.0001
TYR 144
PRO 145
0.0332
PRO 145
ARG 146
-0.0001
ARG 146
GLU 147
-0.0001
GLU 147
ALA 148
0.0808
ALA 148
LYS 149
0.0004
LYS 149
VAL 150
0.0000
VAL 150
GLN 151
0.0829
GLN 151
TRP 152
0.0001
TRP 152
LYS 153
0.0001
LYS 153
VAL 154
0.0302
VAL 154
ASP 155
-0.0000
ASP 155
ASN 156
0.0004
ASN 156
ALA 157
-0.0126
ALA 157
LEU 158
-0.0001
LEU 158
GLN 159
0.0001
GLN 159
SER 160
-0.0149
SER 160
GLY 161
0.0003
GLY 161
ASN 162
-0.0001
ASN 162
SER 163
0.0434
SER 163
GLN 164
-0.0001
GLN 164
GLU 165
-0.0001
GLU 165
SER 166
0.0217
SER 166
SER 166
0.0049
SER 166
VAL 167
-0.0001
VAL 167
VAL 167
-0.0085
VAL 167
THR 168
-0.0002
THR 168
GLU 169
0.0145
GLU 169
GLU 169
-0.0031
GLU 169
GLN 170
-0.0003
GLN 170
ASP 171
-0.0002
ASP 171
SER 172
-0.0771
SER 172
LYS 173
-0.0002
LYS 173
ASP 174
-0.0001
ASP 174
CYS 175
-0.0638
CYS 175
THR 176
0.0001
THR 176
TYR 177
-0.0001
TYR 177
SER 178
-0.0096
SER 178
LEU 179
-0.0000
LEU 179
SER 180
0.0001
SER 180
SER 181
0.0087
SER 181
THR 182
-0.0002
THR 182
LEU 183
-0.0002
LEU 183
THR 184
0.0075
THR 184
LEU 185
-0.0002
LEU 185
SER 186
0.0001
SER 186
LYS 187
0.0172
LYS 187
ALA 188
0.0002
ALA 188
ASP 189
-0.0001
ASP 189
TYR 190
0.0013
TYR 190
GLU 191
-0.0003
GLU 191
LYS 192
-0.0004
LYS 192
HIS 193
0.0068
HIS 193
LYS 194
-0.0001
LYS 194
LYS 194
-0.0034
LYS 194
VAL 195
0.0001
VAL 195
TYR 196
0.0039
TYR 196
ALA 197
0.0001
ALA 197
CYS 198
-0.0001
CYS 198
CYS 198
0.0033
CYS 198
GLU 199
0.0301
GLU 199
VAL 200
0.0000
VAL 200
THR 201
-0.0003
THR 201
HIS 202
0.0900
HIS 202
GLN 203
-0.0000
GLN 203
GLY 204
0.0001
GLY 204
LEU 205
0.0133
LEU 205
SER 206
-0.0001
SER 206
SER 207
-0.0002
SER 207
PRO 208
0.0025
PRO 208
VAL 209
0.0004
VAL 209
THR 210
-0.0003
THR 210
LYS 211
0.0221
LYS 211
SER 212
-0.0002
SER 212
PHE 213
0.0004
PHE 213
ASN 214
-0.0090
ASN 214
ARG 215
0.0000
ARG 215
GLY 216
-0.0001
GLY 216
GLU 217
-0.0086
GLU 217
SER 2
0.0162
SER 2
VAL 3
0.0001
VAL 3
GLU 4
0.0001
GLU 4
GLU 5
-0.0637
GLU 5
SER 6
0.0001
SER 6
GLY 7
-0.0002
GLY 7
GLY 8
-0.0655
GLY 8
ARG 9
-0.0002
ARG 9
LEU 10
0.0001
LEU 10
VAL 11
0.0539
VAL 11
THR 12
0.0001
THR 12
PRO 13
-0.0001
PRO 13
GLY 14
0.0088
GLY 14
THR 15
-0.0001
THR 15
PRO 16
0.0005
PRO 16
LEU 17
-0.0049
LEU 17
THR 18
-0.0001
THR 18
LEU 19
0.0001
LEU 19
THR 20
-0.0605
THR 20
CYS 21
-0.0002
CYS 21
THR 22
0.0001
THR 22
VAL 23
-0.0448
VAL 23
SER 24
-0.0003
SER 24
GLY 25
-0.0003
GLY 25
PHE 26
-0.0085
PHE 26
SER 27
-0.0001
SER 27
LEU 28
-0.0002
LEU 28
SER 29
-0.0003
SER 29
SER 29
-0.0102
SER 29
ASP 30
0.0002
ASP 30
TYR 31
0.0001
TYR 31
ALA 32
-0.0041
ALA 32
MET 33
-0.0001
MET 33
SER 34
0.0005
SER 34
TRP 35
0.0024
TRP 35
VAL 36
-0.0001
VAL 36
ARG 37
-0.0001
ARG 37
GLN 38
-0.0158
GLN 38
ALA 39
-0.0002
ALA 39
PRO 40
0.0004
PRO 40
GLY 41
0.0270
GLY 41
LYS 42
-0.0000
LYS 42
GLY 43
-0.0001
GLY 43
LEU 44
0.0179
LEU 44
GLU 45
-0.0001
GLU 45
TRP 46
0.0003
TRP 46
ILE 47
-0.0221
ILE 47
GLY 48
0.0005
GLY 48
ILE 49
-0.0002
ILE 49
ILE 50
-0.0068
ILE 50
TYR 51
-0.0000
TYR 51
ALA 52
-0.0003
ALA 52
SER 53
0.0077
SER 53
GLY 54
0.0000
GLY 54
SER 55
-0.0001
SER 55
THR 56
-0.0005
THR 56
THR 56
0.0250
THR 56
TYR 57
-0.0001
TYR 57
TYR 58
-0.0002
TYR 58
ALA 59
0.0008
ALA 59
SER 60
0.0002
SER 60
TRP 61
0.0001
TRP 61
ALA 62
0.0079
ALA 62
LYS 63
0.0002
LYS 63
GLY 64
-0.0004
GLY 64
ARG 65
0.0048
ARG 65
PHE 66
0.0001
PHE 66
THR 67
0.0003
THR 67
ILE 68
0.0200
ILE 68
SER 69
-0.0000
SER 69
LYS 70
-0.0000
LYS 70
THR 71
-0.0054
THR 71
SER 72
-0.0004
SER 72
THR 73
-0.0001
THR 73
THR 74
-0.0145
THR 74
VAL 75
-0.0001
VAL 75
ASP 76
-0.0001
ASP 76
LEU 77
-0.0010
LEU 77
LYS 78
-0.0001
LYS 78
ILE 79
0.0000
ILE 79
THR 80
-0.0107
THR 80
SER 81
-0.0000
SER 81
PRO 82
-0.0000
PRO 82
THR 83
-0.0291
THR 83
THR 84
-0.0005
THR 84
GLU 85
-0.0000
GLU 85
ASP 86
-0.0369
ASP 86
THR 87
-0.0001
THR 87
ALA 88
-0.0002
ALA 88
THR 89
-0.0549
THR 89
TYR 90
-0.0003
TYR 90
PHE 91
0.0003
PHE 91
CYS 92
-0.0228
CYS 92
CYS 92
-0.0051
CYS 92
ALA 93
-0.0000
ALA 93
ARG 94
-0.0000
ARG 94
TYR 95
-0.0374
TYR 95
TYR 96
0.0002
TYR 96
TYR 96
-0.0153
TYR 96
ALA 97
-0.0001
ALA 97
GLY 98
-0.0119
GLY 98
SER 99
-0.0004
SER 99
ASP 100
0.0002
ASP 100
ILE 101
-0.0273
ILE 101
ILE 101
0.0159
ILE 101
TRP 102
-0.0001
TRP 102
GLY 103
-0.0000
GLY 103
PRO 104
-0.0572
PRO 104
GLY 105
0.0005
GLY 105
THR 106
-0.0002
THR 106
LEU 107
-0.0830
LEU 107
LEU 107
-0.0234
LEU 107
VAL 108
0.0000
VAL 108
THR 109
0.0002
THR 109
VAL 110
-0.0271
VAL 110
SER 111
-0.0001
SER 111
SER 112
-0.0001
SER 112
ALA 113
0.0102
ALA 113
SER 114
-0.0001
SER 114
THR 115
0.0001
THR 115
LYS 116
0.0146
LYS 116
GLY 117
0.0001
GLY 117
PRO 118
0.0001
PRO 118
SER 119
0.0081
SER 119
VAL 120
0.0004
VAL 120
PHE 121
-0.0001
PHE 121
PRO 122
-0.0012
PRO 122
LEU 123
-0.0000
LEU 123
ALA 124
-0.0002
ALA 124
PRO 125
-0.0146
PRO 125
SER 126
-0.0002
SER 126
GLY 133
-0.0094
GLY 133
THR 134
-0.0002
THR 134
THR 134
-0.0150
THR 134
ALA 135
-0.0001
ALA 135
ALA 136
0.0051
ALA 136
LEU 137
0.0002
LEU 137
GLY 138
-0.0004
GLY 138
CYS 139
0.0005
CYS 139
CYS 139
-0.0113
CYS 139
LEU 140
-0.0000
LEU 140
VAL 141
-0.0001
VAL 141
LYS 142
-0.0047
LYS 142
ASP 143
0.0001
ASP 143
TYR 144
-0.0002
TYR 144
PHE 145
-0.0483
PHE 145
PRO 146
-0.0003
PRO 146
GLU 147
0.0002
GLU 147
GLU 147
0.0024
GLU 147
PRO 148
0.0306
PRO 148
VAL 149
0.0002
VAL 149
THR 150
-0.0001
THR 150
VAL 151
0.0979
VAL 151
SER 152
-0.0000
SER 152
TRP 153
-0.0001
TRP 153
ASN 154
0.0052
ASN 154
SER 155
0.0003
SER 155
GLY 156
0.0001
GLY 156
ALA 157
0.0140
ALA 157
LEU 158
-0.0003
LEU 158
THR 159
-0.0002
THR 159
SER 160
-0.0170
SER 160
SER 160
-0.0327
SER 160
GLY 161
-0.0002
GLY 161
VAL 162
-0.0000
VAL 162
HIS 163
-0.0037
HIS 163
THR 164
0.0002
THR 164
PHE 165
-0.0000
PHE 165
PRO 166
0.0136
PRO 166
ALA 167
0.0003
ALA 167
VAL 168
-0.0000
VAL 168
VAL 168
0.0127
VAL 168
LEU 169
0.0084
LEU 169
GLN 170
-0.0002
GLN 170
SER 171
-0.0001
SER 171
SER 172
-0.0058
SER 172
GLY 173
0.0001
GLY 173
LEU 174
-0.0000
LEU 174
TYR 175
0.0045
TYR 175
SER 176
-0.0001
SER 176
SER 176
-0.0071
SER 176
LEU 177
-0.0002
LEU 177
SER 178
-0.0260
SER 178
SER 178
-0.0158
SER 178
SER 179
0.0001
SER 179
VAL 180
-0.0001
VAL 180
VAL 181
-0.0048
VAL 181
THR 182
0.0001
THR 182
VAL 183
-0.0001
VAL 183
PRO 184
-0.0072
PRO 184
SER 185
0.0002
SER 185
SER 185
0.0049
SER 185
SER 186
-0.0004
SER 186
SER 187
0.0127
SER 187
LEU 188
-0.0002
LEU 188
GLY 189
0.0001
GLY 189
THR 190
-0.0017
THR 190
GLN 191
0.0001
GLN 191
GLN 191
0.0278
GLN 191
THR 192
-0.0001
THR 192
TYR 193
0.0127
TYR 193
ILE 194
-0.0001
ILE 194
CYS 195
0.0002
CYS 195
CYS 195
-0.0011
CYS 195
ASN 196
0.0515
ASN 196
VAL 197
0.0000
VAL 197
ASN 198
0.0002
ASN 198
ASN 198
-0.0024
ASN 198
HIS 199
0.0667
HIS 199
LYS 200
0.0002
LYS 200
PRO 201
-0.0002
PRO 201
SER 202
0.0045
SER 202
ASN 203
0.0001
ASN 203
THR 204
0.0001
THR 204
LYS 205
0.0433
LYS 205
VAL 206
0.0002
VAL 206
ASP 207
-0.0000
ASP 207
LYS 208
0.0516
LYS 208
LYS 209
-0.0002
LYS 209
VAL 210
0.0003
VAL 210
GLU 211
0.0159
GLU 211
PRO 212
-0.0000
PRO 212
LYS 213
-0.0002
LYS 213
SER 214
-0.0006
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.