Should you encounter any unexpected behaviour,
please let us know. elNémo has been relocated.
**Some cleaning from time to time**
Sorry for the inconvenience.
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
MET 1
SER 2
0.0002
SER 2
ARG 3
-0.0003
ARG 3
ILE 4
0.0001
ILE 4
GLU 5
-0.0356
GLU 5
LYS 6
-0.0004
LYS 6
MET 7
0.0002
MET 7
SER 8
-0.0000
SER 8
ILE 9
0.1829
ILE 9
LEU 10
0.0000
LEU 10
GLY 11
-0.0002
GLY 11
VAL 12
0.0003
VAL 12
ARG 13
-0.0020
ARG 13
SER 14
0.0003
SER 14
PHE 15
-0.0002
PHE 15
GLY 16
-0.0001
GLY 16
ILE 17
0.1353
ILE 17
GLU 18
-0.0000
GLU 18
ASP 19
0.0001
ASP 19
LYS 20
-0.0003
LYS 20
ASP 21
-0.0695
ASP 21
LYS 22
0.0004
LYS 22
GLN 23
-0.0001
GLN 23
ILE 24
0.0002
ILE 24
ILE 25
0.1143
ILE 25
THR 26
-0.0001
THR 26
PHE 27
0.0004
PHE 27
PHE 28
0.0000
PHE 28
SER 29
0.0584
SER 29
PRO 30
0.0004
PRO 30
LEU 31
-0.0003
LEU 31
THR 32
0.0001
THR 32
ILE 33
-0.0273
ILE 33
LEU 34
0.0003
LEU 34
VAL 35
0.0004
VAL 35
GLY 36
0.0000
GLY 36
PRO 37
0.0440
PRO 37
ASN 38
-0.0000
ASN 38
GLY 39
-0.0000
GLY 39
ALA 40
-0.0002
ALA 40
GLY 41
0.0614
GLY 41
LYS 42
-0.0000
LYS 42
THR 43
-0.0000
THR 43
THR 44
-0.0003
THR 44
ILE 45
0.0370
ILE 45
ILE 46
0.0000
ILE 46
GLU 47
-0.0002
GLU 47
CYS 48
-0.0001
CYS 48
LEU 49
0.1473
LEU 49
LYS 50
-0.0000
LYS 50
TYR 51
0.0001
TYR 51
ILE 52
0.0002
ILE 52
CYS 53
0.0749
CYS 53
THR 54
-0.0001
THR 54
GLY 55
0.0003
GLY 55
ASP 56
-0.0001
ASP 56
PHE 57
0.1027
PHE 57
PRO 58
0.0002
PRO 58
PRO 59
-0.0003
PRO 59
GLY 60
-0.0001
GLY 60
THR 61
0.0874
THR 61
LYS 62
0.0001
LYS 62
GLY 63
-0.0003
GLY 63
ASN 64
0.0004
ASN 64
THR 65
-0.0771
THR 65
PHE 66
-0.0001
PHE 66
VAL 67
0.0002
VAL 67
HIS 68
-0.0001
HIS 68
ASP 69
0.1835
ASP 69
PRO 70
-0.0001
PRO 70
LYS 71
0.0001
LYS 71
VAL 72
0.0000
VAL 72
ALA 73
-0.0233
ALA 73
GLN 74
-0.0000
GLN 74
GLU 75
0.0002
GLU 75
THR 76
0.0003
THR 76
ASP 77
-0.0228
ASP 77
VAL 78
-0.0002
VAL 78
ARG 79
0.0000
ARG 79
ALA 80
0.0004
ALA 80
GLN 81
0.2056
GLN 81
ILE 82
-0.0003
ILE 82
HIS 83
-0.0001
HIS 83
LEU 84
-0.0000
LEU 84
GLN 85
0.0745
GLN 85
PHE 86
-0.0000
PHE 86
ARG 87
-0.0000
ARG 87
ASP 88
0.0001
ASP 88
VAL 89
0.0939
VAL 89
ASN 90
0.0000
ASN 90
GLY 91
0.0002
GLY 91
GLU 92
-0.0000
GLU 92
LEU 93
-0.0047
LEU 93
ILE 94
0.0001
ILE 94
ALA 95
0.0001
ALA 95
VAL 96
-0.0004
VAL 96
GLN 97
0.1557
GLN 97
ARG 98
0.0001
ARG 98
SER 99
0.0004
SER 99
MET 100
0.0001
MET 100
VAL 101
-0.0975
VAL 101
CYS 102
0.0001
CYS 102
THR 103
0.0001
THR 103
GLN 104
0.0002
GLN 104
LYS 105
0.0833
LYS 105
SER 106
-0.0001
SER 106
LYS 107
0.0002
LYS 107
LYS 108
-0.0000
LYS 108
THR 109
0.1470
THR 109
GLU 110
-0.0000
GLU 110
PHE 111
0.0000
PHE 111
LYS 112
-0.0000
LYS 112
THR 113
-0.0078
THR 113
LEU 114
0.0001
LEU 114
GLU 115
0.0001
GLU 115
GLY 116
-0.0001
GLY 116
VAL 117
0.1330
VAL 117
ILE 118
0.0002
ILE 118
THR 119
0.0000
THR 119
ARG 120
-0.0001
ARG 120
THR 121
0.0272
THR 121
LYS 122
0.0001
LYS 122
HIS 123
0.0002
HIS 123
GLY 124
0.0000
GLY 124
GLU 125
0.0982
GLU 125
LYS 126
0.0001
LYS 126
VAL 127
-0.0002
VAL 127
SER 128
-0.0002
SER 128
LEU 129
0.0035
LEU 129
SER 130
-0.0002
SER 130
SER 131
-0.0001
SER 131
LYS 132
0.0003
LYS 132
CYS 133
0.0653
CYS 133
ALA 134
0.0000
ALA 134
GLU 135
0.0001
GLU 135
ILE 136
-0.0001
ILE 136
ASP 137
0.0354
ASP 137
ARG 138
0.0000
ARG 138
GLU 139
-0.0001
GLU 139
MET 140
-0.0000
MET 140
ILE 141
-0.0206
ILE 141
SER 142
0.0004
SER 142
SER 143
-0.0000
SER 143
LEU 144
-0.0001
LEU 144
GLY 145
0.0710
GLY 145
VAL 146
-0.0000
VAL 146
SER 147
0.0001
SER 147
LYS 148
-0.0002
LYS 148
ALA 149
-0.0676
ALA 149
VAL 150
-0.0002
VAL 150
LEU 151
-0.0002
LEU 151
ASN 152
0.0002
ASN 152
ASN 153
-0.0242
ASN 153
VAL 154
-0.0001
VAL 154
ILE 155
-0.0002
ILE 155
PHE 156
-0.0001
PHE 156
CYS 157
-0.2025
CYS 157
HIS 158
-0.0002
HIS 158
GLN 159
0.0001
GLN 159
GLU 160
0.0001
GLU 160
ASP 161
0.3329
ASP 161
SER 162
-0.0001
SER 162
ASN 163
0.0001
ASN 163
TRP 164
0.0003
TRP 164
PRO 165
0.1725
PRO 165
LEU 166
0.0003
LEU 166
SER 1202
-0.0551
SER 1202
ALA 1203
-0.0001
ALA 1203
GLY 1204
0.0001
GLY 1204
GLN 1205
-0.0001
GLN 1205
LYS 1206
-0.0653
LYS 1206
VAL 1207
0.0001
VAL 1207
LEU 1208
-0.0002
LEU 1208
ALA 1209
-0.0001
ALA 1209
SER 1210
0.0109
SER 1210
LEU 1211
-0.0002
LEU 1211
ILE 1212
-0.0001
ILE 1212
ILE 1213
-0.0001
ILE 1213
ARG 1214
-0.0006
ARG 1214
LEU 1215
0.0002
LEU 1215
ALA 1216
0.0003
ALA 1216
LEU 1217
-0.0001
LEU 1217
ALA 1218
-0.1097
ALA 1218
GLU 1219
0.0001
GLU 1219
THR 1220
0.0000
THR 1220
PHE 1221
0.0001
PHE 1221
CYS 1222
-0.0906
CYS 1222
LEU 1223
-0.0001
LEU 1223
ASN 1224
-0.0001
ASN 1224
CYS 1225
0.0001
CYS 1225
GLY 1226
0.1914
GLY 1226
ILE 1227
-0.0001
ILE 1227
ILE 1228
-0.0001
ILE 1228
ALA 1229
0.0001
ALA 1229
LEU 1230
-0.1828
LEU 1230
ASP 1231
0.0002
ASP 1231
GLU 1232
0.0000
GLU 1232
PRO 1233
0.0000
PRO 1233
THR 1234
-0.1557
THR 1234
THR 1235
-0.0004
THR 1235
ASN 1236
-0.0001
ASN 1236
LEU 1237
-0.0001
LEU 1237
ASP 1238
0.0458
ASP 1238
ARG 1239
0.0001
ARG 1239
GLU 1240
0.0000
GLU 1240
ASN 1241
0.0002
ASN 1241
ILE 1242
-0.1301
ILE 1242
GLU 1243
0.0001
GLU 1243
SER 1244
-0.0001
SER 1244
LEU 1245
-0.0001
LEU 1245
ALA 1246
-0.0245
ALA 1246
HIS 1247
-0.0001
HIS 1247
ALA 1248
0.0001
ALA 1248
LEU 1249
-0.0001
LEU 1249
VAL 1250
-0.0817
VAL 1250
GLU 1251
-0.0000
GLU 1251
ILE 1252
0.0000
ILE 1252
ILE 1253
0.0001
ILE 1253
LYS 1254
-0.1215
LYS 1254
SER 1255
0.0001
SER 1255
ARG 1256
0.0004
ARG 1256
SER 1257
-0.0000
SER 1257
GLN 1258
-0.0415
GLN 1258
GLN 1259
-0.0000
GLN 1259
ARG 1260
0.0000
ARG 1260
ASN 1261
-0.0001
ASN 1261
PHE 1262
0.0031
PHE 1262
GLN 1263
0.0001
GLN 1263
LEU 1264
0.0001
LEU 1264
LEU 1265
0.0000
LEU 1265
VAL 1266
-0.1540
VAL 1266
ILE 1267
-0.0003
ILE 1267
THR 1268
0.0002
THR 1268
HIS 1269
-0.0002
HIS 1269
ASP 1270
-0.2479
ASP 1270
GLU 1271
-0.0002
GLU 1271
ASP 1272
0.0000
ASP 1272
PHE 1273
-0.0001
PHE 1273
VAL 1274
-0.1070
VAL 1274
GLU 1275
0.0001
GLU 1275
LEU 1276
0.0004
LEU 1276
LEU 1277
-0.0004
LEU 1277
GLY 1278
-0.0621
GLY 1278
ARG 1279
-0.0000
ARG 1279
SER 1280
-0.0001
SER 1280
GLU 1281
-0.0004
GLU 1281
TYR 1282
-0.0202
TYR 1282
VAL 1283
0.0000
VAL 1283
GLU 1284
0.0001
GLU 1284
LYS 1285
-0.0004
LYS 1285
PHE 1286
-0.0670
PHE 1286
TYR 1287
-0.0001
TYR 1287
ARG 1288
0.0003
ARG 1288
ILE 1289
-0.0001
ILE 1289
LYS 1290
0.0792
LYS 1290
LYS 1291
0.0003
LYS 1291
ASN 1292
-0.0002
ASN 1292
ILE 1293
-0.0001
ILE 1293
ASP 1294
0.0210
ASP 1294
GLN 1295
0.0003
GLN 1295
CYS 1296
-0.0002
CYS 1296
SER 1297
0.0000
SER 1297
GLU 1298
0.0617
GLU 1298
ILE 1299
0.0003
ILE 1299
VAL 1300
-0.0003
VAL 1300
LYS 1301
0.0001
LYS 1301
CYS 1302
-0.0081
CYS 1302
SER 1303
0.0001
SER 1303
VAL 1304
0.0001
VAL 1304
SER 1305
-0.0004
SER 1305
SER 1306
-0.0102
SER 1306
GLU 10
0.0008
GLU 10
ASN 11
0.0001
ASN 11
THR 12
-0.0002
THR 12
PHE 13
0.0001
PHE 13
LYS 14
-0.0349
LYS 14
ILE 15
0.0003
ILE 15
LEU 16
-0.0001
LEU 16
VAL 17
0.0004
VAL 17
ALA 18
0.0655
ALA 18
THR 19
-0.0002
THR 19
ASP 20
-0.0001
ASP 20
ILE 21
-0.0001
ILE 21
HIS 22
0.0099
HIS 22
LEU 23
0.0003
LEU 23
GLY 24
-0.0001
GLY 24
PHE 25
0.0002
PHE 25
MET 26
-0.0306
MET 26
GLU 27
-0.0004
GLU 27
LYS 28
-0.0001
LYS 28
ASP 29
0.0001
ASP 29
ALA 30
0.0166
ALA 30
VAL 31
0.0003
VAL 31
ARG 32
0.0002
ARG 32
GLY 33
0.0001
GLY 33
ASN 34
0.0849
ASN 34
ASP 35
-0.0003
ASP 35
THR 36
0.0000
THR 36
PHE 37
0.0001
PHE 37
VAL 38
0.0529
VAL 38
THR 39
0.0001
THR 39
LEU 40
-0.0002
LEU 40
ASP 41
0.0000
ASP 41
GLU 42
0.0721
GLU 42
ILE 43
-0.0002
ILE 43
LEU 44
0.0002
LEU 44
ARG 45
0.0003
ARG 45
LEU 46
0.0969
LEU 46
ALA 47
-0.0004
ALA 47
GLN 48
-0.0000
GLN 48
GLU 49
-0.0004
GLU 49
ASN 50
0.1787
ASN 50
GLU 51
-0.0000
GLU 51
VAL 52
0.0002
VAL 52
ASP 53
0.0001
ASP 53
PHE 54
0.0319
PHE 54
ILE 55
-0.0003
ILE 55
LEU 56
0.0002
LEU 56
LEU 57
0.0001
LEU 57
GLY 58
-0.0310
GLY 58
GLY 59
0.0002
GLY 59
ASP 60
-0.0002
ASP 60
LEU 61
0.0001
LEU 61
PHE 62
-0.0515
PHE 62
HIS 63
-0.0001
HIS 63
GLU 64
0.0002
GLU 64
ASN 65
-0.0001
ASN 65
LYS 66
-0.0172
LYS 66
PRO 67
-0.0002
PRO 67
SER 68
0.0002
SER 68
ARG 69
0.0000
ARG 69
LYS 70
-0.0777
LYS 70
THR 71
0.0003
THR 71
LEU 72
-0.0002
LEU 72
HIS 73
0.0000
HIS 73
THR 74
0.0206
THR 74
CYS 75
-0.0000
CYS 75
LEU 76
0.0000
LEU 76
GLU 77
-0.0000
GLU 77
LEU 78
0.0439
LEU 78
LEU 79
0.0000
LEU 79
ARG 80
0.0002
ARG 80
LYS 81
0.0000
LYS 81
TYR 82
0.0765
TYR 82
CYS 83
0.0001
CYS 83
MET 84
-0.0001
MET 84
GLY 85
-0.0001
GLY 85
ASP 86
-0.3025
ASP 86
ARG 87
-0.0003
ARG 87
PRO 88
0.0001
PRO 88
VAL 89
-0.0001
VAL 89
GLN 90
0.1705
GLN 90
PHE 91
-0.0002
PHE 91
GLU 92
0.0001
GLU 92
ILE 93
0.0000
ILE 93
LEU 94
-0.0475
LEU 94
SER 95
-0.0000
SER 95
ASP 96
0.0003
ASP 96
GLN 97
0.0004
GLN 97
SER 98
-0.0006
SER 98
VAL 99
0.0001
VAL 99
ASN 100
0.0001
ASN 100
PHE 101
-0.0000
PHE 101
GLY 102
-0.0267
GLY 102
PHE 103
0.0004
PHE 103
SER 104
0.0002
SER 104
LYS 105
0.0001
LYS 105
PHE 106
0.0165
PHE 106
PRO 107
-0.0000
PRO 107
TRP 108
-0.0000
TRP 108
VAL 109
0.0001
VAL 109
ASN 110
-0.0387
ASN 110
TYR 111
0.0003
TYR 111
GLN 112
0.0002
GLN 112
ASP 113
0.0000
ASP 113
GLY 114
0.0383
GLY 114
ASN 115
0.0002
ASN 115
LEU 116
0.0001
LEU 116
ASN 117
-0.0002
ASN 117
ILE 118
0.0067
ILE 118
SER 119
-0.0003
SER 119
ILE 120
-0.0001
ILE 120
PRO 121
-0.0002
PRO 121
VAL 122
-0.0635
VAL 122
PHE 123
0.0001
PHE 123
SER 124
0.0005
SER 124
ILE 125
0.0001
ILE 125
HIS 126
-0.0121
HIS 126
GLY 127
-0.0001
GLY 127
ASN 128
-0.0002
ASN 128
HIS 129
-0.0003
HIS 129
ASP 130
0.0375
ASP 130
ASP 131
-0.0001
ASP 131
PRO 132
0.0002
PRO 132
THR 133
0.0001
THR 133
GLY 134
0.1065
GLY 134
ALA 135
-0.0003
ALA 135
ASP 136
0.0001
ASP 136
ALA 137
0.0001
ALA 137
LEU 138
0.0041
LEU 138
CYS 139
-0.0000
CYS 139
ALA 140
-0.0002
ALA 140
LEU 141
0.0003
LEU 141
ASP 142
0.0281
ASP 142
ILE 143
0.0001
ILE 143
LEU 144
-0.0002
LEU 144
SER 145
-0.0003
SER 145
CYS 146
0.0071
CYS 146
ALA 147
-0.0001
ALA 147
GLY 148
-0.0002
GLY 148
PHE 149
-0.0002
PHE 149
VAL 150
-0.0341
VAL 150
ASN 151
0.0001
ASN 151
HIS 152
0.0002
HIS 152
PHE 153
0.0001
PHE 153
GLY 154
-0.0302
GLY 154
ARG 155
-0.0001
ARG 155
SER 156
0.0004
SER 156
MET 157
-0.0001
MET 157
SER 158
-0.0085
SER 158
VAL 159
-0.0003
VAL 159
GLU 160
0.0001
GLU 160
LYS 161
0.0002
LYS 161
ILE 162
-0.0236
ILE 162
ASP 163
0.0000
ASP 163
ILE 164
-0.0001
ILE 164
SER 165
0.0003
SER 165
PRO 166
-0.1008
PRO 166
VAL 167
0.0003
VAL 167
LEU 168
-0.0001
LEU 168
LEU 169
0.0001
LEU 169
GLN 170
-0.1100
GLN 170
LYS 171
0.0003
LYS 171
GLY 172
0.0001
GLY 172
SER 173
0.0004
SER 173
THR 174
-0.0658
THR 174
LYS 175
0.0000
LYS 175
ILE 176
-0.0003
ILE 176
ALA 177
-0.0000
ALA 177
LEU 178
-0.0397
LEU 178
TYR 179
0.0001
TYR 179
GLY 180
-0.0001
GLY 180
LEU 181
0.0001
LEU 181
GLY 182
-0.0520
GLY 182
SER 183
0.0000
SER 183
ILE 184
-0.0001
ILE 184
PRO 185
-0.0001
PRO 185
ASP 186
-0.1025
ASP 186
GLU 187
-0.0001
GLU 187
ARG 188
0.0002
ARG 188
LEU 189
-0.0003
LEU 189
TYR 190
-0.1031
TYR 190
ARG 191
-0.0000
ARG 191
MET 192
-0.0004
MET 192
PHE 193
0.0002
PHE 193
VAL 194
-0.1209
VAL 194
ASN 195
-0.0002
ASN 195
LYS 196
-0.0002
LYS 196
LYS 197
-0.0004
LYS 197
VAL 198
-0.1812
VAL 198
THR 199
-0.0000
THR 199
MET 200
0.0002
MET 200
LEU 201
0.0000
LEU 201
ARG 202
-0.2397
ARG 202
PRO 203
-0.0004
PRO 203
LYS 204
-0.0001
LYS 204
GLU 205
-0.0002
GLU 205
ASP 206
-0.0543
ASP 206
GLU 207
-0.0003
GLU 207
ASN 208
0.0003
ASN 208
SER 209
-0.0003
SER 209
TRP 210
0.0148
TRP 210
PHE 211
0.0002
PHE 211
ASN 212
-0.0000
ASN 212
LEU 213
-0.0006
LEU 213
PHE 214
-0.0514
PHE 214
VAL 215
-0.0002
VAL 215
ILE 216
0.0003
ILE 216
HIS 217
0.0003
HIS 217
GLN 218
-0.0814
GLN 218
ASN 219
0.0001
ASN 219
ARG 220
0.0001
ARG 220
SER 221
-0.0003
SER 221
LYS 222
-0.2146
LYS 222
HIS 223
0.0000
HIS 223
GLY 224
-0.0003
GLY 224
SER 225
0.0002
SER 225
THR 226
-0.0115
THR 226
ASN 227
-0.0002
ASN 227
PHE 228
-0.0004
PHE 228
ILE 229
0.0004
ILE 229
PRO 230
-0.2578
PRO 230
GLU 231
-0.0000
GLU 231
GLN 232
-0.0002
GLN 232
PHE 233
0.0002
PHE 233
LEU 234
-0.1013
LEU 234
ASP 235
0.0005
ASP 235
ASP 236
0.0001
ASP 236
PHE 237
0.0002
PHE 237
ILE 238
-0.1344
ILE 238
ASP 239
-0.0002
ASP 239
LEU 240
0.0000
LEU 240
VAL 241
-0.0001
VAL 241
ILE 242
-0.0004
ILE 242
TRP 243
-0.0001
TRP 243
GLY 244
-0.0002
GLY 244
HIS 245
0.0001
HIS 245
GLU 246
0.2159
GLU 246
HIS 247
0.0002
HIS 247
GLU 248
-0.0001
GLU 248
CYS 249
0.0003
CYS 249
LYS 250
-0.1122
LYS 250
ILE 251
0.0000
ILE 251
ALA 252
0.0003
ALA 252
PRO 253
0.0001
PRO 253
THR 254
0.0644
THR 254
LYS 255
0.0002
LYS 255
ASN 256
0.0002
ASN 256
GLU 257
0.0000
GLU 257
GLN 258
-0.1008
GLN 258
GLN 259
-0.0001
GLN 259
LEU 260
-0.0003
LEU 260
PHE 261
0.0001
PHE 261
TYR 262
-0.1517
TYR 262
ILE 263
0.0003
ILE 263
SER 264
-0.0003
SER 264
GLN 265
0.0001
GLN 265
PRO 266
-0.0547
PRO 266
GLY 267
-0.0001
GLY 267
SER 268
-0.0003
SER 268
SER 269
-0.0000
SER 269
VAL 270
-0.0414
VAL 270
VAL 271
0.0000
VAL 271
THR 272
0.0001
THR 272
SER 273
0.0001
SER 273
LEU 274
0.3447
LEU 274
SER 275
-0.0004
SER 275
PRO 276
0.0002
PRO 276
GLY 277
0.0002
GLY 277
GLU 278
0.0006
GLU 278
ALA 279
-0.0001
ALA 279
VAL 280
-0.0003
VAL 280
LYS 281
-0.0001
LYS 281
LYS 282
-0.0746
LYS 282
HIS 283
-0.0003
HIS 283
VAL 284
0.0001
VAL 284
GLY 285
0.0001
GLY 285
LEU 286
-0.1799
LEU 286
LEU 287
-0.0001
LEU 287
ARG 288
-0.0000
ARG 288
ILE 289
0.0001
ILE 289
LYS 290
-0.0184
LYS 290
GLY 291
-0.0002
GLY 291
ARG 292
-0.0001
ARG 292
LYS 293
-0.0001
LYS 293
MET 294
-0.0305
MET 294
ASN 295
0.0002
ASN 295
MET 296
0.0003
MET 296
HIS 297
-0.0002
HIS 297
LYS 298
-0.0765
LYS 298
ILE 299
0.0000
ILE 299
PRO 300
0.0001
PRO 300
LEU 301
-0.0002
LEU 301
HIS 302
0.0696
HIS 302
THR 303
0.0002
THR 303
VAL 304
0.0000
VAL 304
ARG 305
0.0001
ARG 305
LYS 690
-0.0780
LYS 690
VAL 691
0.0001
VAL 691
THR 692
0.0002
THR 692
TYR 693
-0.0002
TYR 693
PRO 694
0.1212
PRO 694
GLY 695
0.0002
GLY 695
ALA 696
-0.0000
ALA 696
GLY 697
0.0001
GLY 697
LYS 698
-0.0988
LYS 698
LEU 699
-0.0002
LEU 699
PRO 700
0.0002
PRO 700
HIS 701
-0.0001
HIS 701
ILE 702
0.1380
ILE 702
ILE 703
-0.0001
ILE 703
GLY 704
0.0000
GLY 704
GLY 705
0.0001
GLY 705
SER 706
-0.0374
SER 706
ASP 707
0.0001
ASP 707
LEU 708
-0.0001
LEU 708
ILE 709
-0.0000
ILE 709
ALA 710
0.1920
ALA 710
HIS 711
-0.0003
HIS 711
HIS 712
0.0002
HIS 712
ALA 713
0.0001
ALA 713
ARG 714
0.2437
ARG 714
LYS 715
0.0000
LYS 715
ASN 716
-0.0003
ASN 716
THR 717
-0.0001
THR 717
GLU 718
-0.0262
GLU 718
LEU 719
-0.0001
LEU 719
GLU 720
-0.0001
GLU 720
GLU 721
-0.0000
GLU 721
TRP 722
-0.2013
TRP 722
LEU 723
0.0001
LEU 723
ARG 724
0.0002
ARG 724
GLN 725
-0.0001
GLN 725
GLU 726
-0.0449
GLU 726
MET 727
0.0001
MET 727
GLU 728
0.0002
GLU 728
VAL 729
-0.0001
VAL 729
GLN 730
-0.0882
GLN 730
ASN 731
0.0003
ASN 731
GLN 732
-0.0001
GLN 732
HIS 733
0.0000
HIS 733
ALA 734
-0.2613
ALA 734
LYS 735
-0.0002
LYS 735
GLU 736
-0.0006
GLU 736
GLU 737
-0.0001
GLU 737
SER 738
-0.0956
SER 738
LEU 739
-0.0001
LEU 739
ALA 740
-0.0001
ALA 740
ASP 741
0.0002
ASP 741
ASP 742
-0.1305
ASP 742
LEU 743
-0.0003
LEU 743
PHE 744
-0.0002
PHE 744
ARG 745
0.0002
ARG 745
TYR 746
-0.1665
TYR 746
ASN 747
0.0000
ASN 747
PRO 748
0.0002
PRO 748
TYR 749
-0.0000
TYR 749
LEU 750
-0.1245
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.