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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 19
PRO 20
0.0003
PRO 20
PRO 21
-0.0001
PRO 21
MET 22
-0.0033
MET 22
LYS 23
-0.0001
LYS 23
ASP 24
0.0000
ASP 24
TYR 25
0.0027
TYR 25
MET 26
-0.0003
MET 26
ILE 27
0.0000
ILE 27
LEU 28
0.0065
LEU 28
SER 29
-0.0002
SER 29
GLY 30
-0.0001
GLY 30
PRO 31
0.0042
PRO 31
GLN 32
-0.0001
GLN 32
LYS 33
0.0001
LYS 33
THR 34
0.0054
THR 34
ALA 35
-0.0001
ALA 35
VAL 36
-0.0000
VAL 36
ALA 37
0.0030
ALA 37
VAL 38
-0.0002
VAL 38
LEU 39
0.0000
LEU 39
CYS 40
0.0011
CYS 40
THR 41
0.0003
THR 41
LEU 42
-0.0000
LEU 42
LEU 43
-0.0196
LEU 43
GLY 44
-0.0002
GLY 44
LEU 45
0.0000
LEU 45
LEU 46
-0.0264
LEU 46
SER 47
0.0002
SER 47
ALA 48
-0.0002
ALA 48
LEU 49
-0.0225
LEU 49
GLU 50
-0.0002
GLU 50
ASN 51
-0.0003
ASN 51
VAL 52
0.0340
VAL 52
ALA 53
-0.0000
ALA 53
VAL 54
0.0000
VAL 54
LEU 55
-0.0326
LEU 55
TYR 56
0.0000
TYR 56
LEU 57
0.0003
LEU 57
ILE 58
0.0358
ILE 58
LEU 59
0.0003
LEU 59
SER 60
-0.0002
SER 60
SER 61
0.0405
SER 61
HIS 62
0.0001
HIS 62
GLN 63
0.0003
GLN 63
LEU 64
-0.0268
LEU 64
ARG 65
-0.0000
ARG 65
ARG 66
0.0003
ARG 66
LYS 67
-0.0049
LYS 67
PRO 68
0.0002
PRO 68
SER 69
-0.0002
SER 69
TYR 70
0.0120
TYR 70
LEU 71
0.0002
LEU 71
PHE 72
0.0001
PHE 72
ILE 73
0.0376
ILE 73
GLY 74
-0.0001
GLY 74
SER 75
-0.0004
SER 75
LEU 76
0.0041
LEU 76
ALA 77
-0.0001
ALA 77
LEU 78
0.0002
LEU 78
ALA 79
-0.0071
ALA 79
ASP 80
0.0004
ASP 80
PHE 81
-0.0002
PHE 81
LEU 82
-0.0182
LEU 82
ALA 83
-0.0001
ALA 83
SER 84
0.0003
SER 84
VAL 85
-0.0245
VAL 85
VAL 86
-0.0002
VAL 86
PHE 87
-0.0002
PHE 87
ALA 88
0.0032
ALA 88
CYS 89
-0.0000
CYS 89
SER 90
0.0002
SER 90
PHE 91
-0.0014
PHE 91
VAL 92
0.0002
VAL 92
ASN 93
0.0002
ASN 93
PHE 94
0.0037
PHE 94
HIS 95
0.0000
HIS 95
VAL 96
0.0004
VAL 96
PHE 97
-0.0004
PHE 97
HIS 98
-0.0002
HIS 98
GLY 99
0.0000
GLY 99
VAL 100
-0.0123
VAL 100
ASP 101
-0.0004
ASP 101
SER 102
0.0002
SER 102
LYS 103
-0.0024
LYS 103
ALA 104
-0.0000
ALA 104
VAL 105
0.0001
VAL 105
PHE 106
-0.0025
PHE 106
LEU 107
-0.0002
LEU 107
LEU 108
0.0000
LEU 108
LYS 109
-0.0122
LYS 109
ILE 110
0.0001
ILE 110
GLY 111
-0.0001
GLY 111
SER 112
-0.0208
SER 112
VAL 113
0.0001
VAL 113
THR 114
0.0003
THR 114
MET 115
0.0008
MET 115
THR 116
-0.0000
THR 116
PHE 117
-0.0003
PHE 117
THR 118
-0.0036
THR 118
ALA 119
-0.0000
ALA 119
SER 120
-0.0001
SER 120
VAL 121
0.0127
VAL 121
GLY 122
0.0001
GLY 122
SER 123
-0.0002
SER 123
LEU 124
0.0215
LEU 124
LEU 125
-0.0003
LEU 125
LEU 126
0.0001
LEU 126
ALA 127
0.0239
ALA 127
ALA 128
-0.0000
ALA 128
ILE 129
0.0003
ILE 129
ASP 130
-0.0390
ASP 130
ARG 131
0.0002
ARG 131
TYR 132
-0.0001
TYR 132
LEU 133
-0.0234
LEU 133
CYS 134
-0.0000
CYS 134
LEU 135
0.0003
LEU 135
ARG 136
-0.0058
ARG 136
TYR 137
-0.0000
TYR 137
PRO 138
0.0001
PRO 138
PRO 139
0.0100
PRO 139
SER 140
-0.0001
SER 140
TYR 141
0.0002
TYR 141
LYS 142
-0.0125
LYS 142
ALA 143
-0.0002
ALA 143
LEU 144
0.0001
LEU 144
LEU 145
-0.0013
LEU 145
THR 146
0.0004
THR 146
ARG 147
0.0000
ARG 147
GLY 148
-0.0265
GLY 148
ARG 149
0.0001
ARG 149
ALA 150
-0.0002
ALA 150
LEU 151
0.0129
LEU 151
VAL 152
0.0004
VAL 152
LEU 153
0.0003
LEU 153
LEU 154
0.0308
LEU 154
GLY 155
0.0002
GLY 155
ILE 156
0.0001
ILE 156
MET 157
-0.0198
MET 157
TRP 158
-0.0002
TRP 158
VAL 159
0.0004
VAL 159
LEU 160
-0.0227
LEU 160
SER 161
0.0001
SER 161
ALA 162
-0.0003
ALA 162
LEU 163
0.0033
LEU 163
VAL 164
0.0001
VAL 164
SER 165
-0.0001
SER 165
TYR 166
0.0221
TYR 166
LEU 167
-0.0004
LEU 167
PRO 168
0.0000
PRO 168
LEU 169
0.0024
LEU 169
MET 170
0.0000
MET 170
GLY 171
-0.0004
GLY 171
TRP 172
0.0149
TRP 172
THR 173
0.0001
THR 173
CYS 174
0.0001
CYS 174
CYS 175
0.0011
CYS 175
PRO 176
-0.0004
PRO 176
ARG 177
0.0001
ARG 177
PRO 178
-0.0001
PRO 178
CYS 179
0.0001
CYS 179
SER 180
-0.0000
SER 180
GLU 181
-0.0011
GLU 181
LEU 182
0.0003
LEU 182
PHE 183
-0.0000
PHE 183
PRO 184
0.0017
PRO 184
LEU 185
-0.0000
LEU 185
ILE 186
0.0003
ILE 186
PRO 187
0.0012
PRO 187
ASN 188
0.0000
ASN 188
ASP 189
0.0003
ASP 189
TYR 190
-0.0111
TYR 190
LEU 191
0.0001
LEU 191
LEU 192
-0.0001
LEU 192
SER 193
-0.0230
SER 193
TRP 194
-0.0001
TRP 194
LEU 195
0.0001
LEU 195
LEU 196
-0.0200
LEU 196
PHE 197
-0.0001
PHE 197
ILE 198
0.0001
ILE 198
ALA 199
0.0150
ALA 199
PHE 200
0.0001
PHE 200
PHE 200
-0.0028
PHE 200
LEU 201
-0.0004
LEU 201
PHE 202
0.0172
PHE 202
SER 203
0.0000
SER 203
GLY 204
0.0001
GLY 204
ILE 205
0.0231
ILE 205
ILE 206
0.0003
ILE 206
TYR 207
0.0001
TYR 207
THR 208
-0.0358
THR 208
TYR 209
0.0001
TYR 209
GLY 210
0.0000
GLY 210
HIS 211
-0.0096
HIS 211
VAL 212
-0.0001
VAL 212
LEU 213
-0.0000
LEU 213
TRP 214
-0.0290
TRP 214
LYS 215
0.0002
LYS 215
ALA 216
-0.0004
ALA 216
HIS 217
-0.0218
HIS 217
GLN 218
-0.0003
GLN 218
HIS 219
0.0000
HIS 219
VAL 220
0.0468
VAL 220
ALA 221
0.0005
ALA 221
SER 222
-0.0003
SER 222
ASN 1001
-0.0233
ASN 1001
ILE 1002
-0.0001
ILE 1002
PHE 1003
0.0001
PHE 1003
GLU 1004
-0.0125
GLU 1004
MET 1005
0.0002
MET 1005
LEU 1006
-0.0004
LEU 1006
ARG 1007
0.0087
ARG 1007
ILE 1008
-0.0001
ILE 1008
ASP 1009
-0.0001
ASP 1009
GLU 1010
0.0160
GLU 1010
GLY 1011
-0.0002
GLY 1011
LEU 1012
-0.0001
LEU 1012
ARG 1013
0.0147
ARG 1013
LEU 1014
0.0001
LEU 1014
LYS 1015
-0.0000
LYS 1015
ILE 1016
0.0235
ILE 1016
TYR 1017
-0.0002
TYR 1017
LYS 1018
-0.0001
LYS 1018
ASP 1019
-0.0067
ASP 1019
THR 1020
-0.0000
THR 1020
GLU 1021
-0.0001
GLU 1021
GLY 1022
-0.0269
GLY 1022
TYR 1023
-0.0003
TYR 1023
TYR 1024
0.0002
TYR 1024
THR 1025
-0.0007
THR 1025
ILE 1026
-0.0002
ILE 1026
GLY 1027
-0.0001
GLY 1027
ILE 1028
-0.0141
ILE 1028
GLY 1029
0.0001
GLY 1029
HIS 1030
0.0002
HIS 1030
LEU 1031
-0.0255
LEU 1031
LEU 1032
0.0004
LEU 1032
THR 1033
-0.0001
THR 1033
LYS 1034
-0.0066
LYS 1034
SER 1035
0.0003
SER 1035
PRO 1036
-0.0001
PRO 1036
SER 1037
0.0019
SER 1037
LEU 1038
0.0001
LEU 1038
ASN 1039
0.0001
ASN 1039
ALA 1040
-0.0089
ALA 1040
ALA 1041
0.0001
ALA 1041
LYS 1042
0.0000
LYS 1042
SER 1043
0.0009
SER 1043
GLU 1044
0.0004
GLU 1044
LEU 1045
-0.0001
LEU 1045
ASP 1046
0.0010
ASP 1046
LYS 1047
0.0003
LYS 1047
ALA 1048
-0.0000
ALA 1048
ILE 1049
-0.0020
ILE 1049
GLY 1050
-0.0002
GLY 1050
ARG 1051
0.0001
ARG 1051
ASN 1052
-0.0019
ASN 1052
THR 1053
-0.0004
THR 1053
ASN 1054
0.0000
ASN 1054
GLY 1055
-0.0096
GLY 1055
VAL 1056
0.0002
VAL 1056
ILE 1057
0.0003
ILE 1057
THR 1058
0.0233
THR 1058
LYS 1059
0.0002
LYS 1059
ASP 1060
-0.0003
ASP 1060
GLU 1061
-0.0170
GLU 1061
ALA 1062
-0.0003
ALA 1062
GLU 1063
0.0001
GLU 1063
LYS 1064
-0.0081
LYS 1064
LEU 1065
0.0001
LEU 1065
PHE 1066
0.0002
PHE 1066
ASN 1067
0.0019
ASN 1067
GLN 1068
0.0003
GLN 1068
ASP 1069
-0.0000
ASP 1069
VAL 1070
-0.0357
VAL 1070
ASP 1071
0.0002
ASP 1071
ALA 1072
-0.0001
ALA 1072
ALA 1073
0.0008
ALA 1073
VAL 1074
0.0002
VAL 1074
ARG 1075
0.0003
ARG 1075
GLY 1076
0.0115
GLY 1076
ILE 1077
-0.0002
ILE 1077
LEU 1078
-0.0001
LEU 1078
ARG 1079
-0.0001
ARG 1079
ASN 1080
-0.0001
ASN 1080
ALA 1081
-0.0003
ALA 1081
LYS 1082
0.0043
LYS 1082
LEU 1083
-0.0000
LEU 1083
LYS 1084
-0.0000
LYS 1084
PRO 1085
-0.0045
PRO 1085
VAL 1086
0.0001
VAL 1086
TYR 1087
-0.0002
TYR 1087
ASP 1088
-0.0045
ASP 1088
SER 1089
0.0003
SER 1089
LEU 1090
-0.0000
LEU 1090
ASP 1091
0.0054
ASP 1091
ALA 1092
-0.0003
ALA 1092
VAL 1093
-0.0000
VAL 1093
ARG 1094
0.0057
ARG 1094
ARG 1095
0.0004
ARG 1095
ALA 1096
0.0001
ALA 1096
ALA 1097
0.0093
ALA 1097
LEU 1098
0.0002
LEU 1098
ILE 1099
-0.0003
ILE 1099
ASN 1100
-0.0014
ASN 1100
MET 1101
-0.0003
MET 1101
VAL 1102
0.0001
VAL 1102
PHE 1103
-0.0313
PHE 1103
GLN 1104
0.0000
GLN 1104
MET 1105
-0.0002
MET 1105
GLY 1106
0.0166
GLY 1106
GLU 1107
0.0003
GLU 1107
THR 1108
-0.0002
THR 1108
GLY 1109
0.0086
GLY 1109
VAL 1110
0.0002
VAL 1110
ALA 1111
-0.0002
ALA 1111
GLY 1112
0.0078
GLY 1112
PHE 1113
-0.0001
PHE 1113
THR 1114
-0.0003
THR 1114
ASN 1115
0.0014
ASN 1115
SER 1116
0.0002
SER 1116
LEU 1117
-0.0003
LEU 1117
ARG 1118
-0.0106
ARG 1118
MET 1119
-0.0001
MET 1119
LEU 1120
-0.0002
LEU 1120
GLN 1121
0.0020
GLN 1121
GLN 1122
-0.0002
GLN 1122
LYS 1123
-0.0002
LYS 1123
ARG 1124
-0.0065
ARG 1124
TRP 1125
-0.0000
TRP 1125
ASP 1126
0.0002
ASP 1126
GLU 1127
0.0055
GLU 1127
ALA 1128
0.0001
ALA 1128
ALA 1129
0.0002
ALA 1129
VAL 1130
0.0099
VAL 1130
ASN 1131
0.0001
ASN 1131
LEU 1132
0.0002
LEU 1132
ALA 1133
0.0017
ALA 1133
LYS 1134
-0.0001
LYS 1134
SER 1135
0.0000
SER 1135
ARG 1136
-0.0048
ARG 1136
TRP 1137
0.0001
TRP 1137
TYR 1138
0.0003
TYR 1138
ASN 1139
0.0049
ASN 1139
GLN 1140
0.0004
GLN 1140
THR 1141
-0.0001
THR 1141
PRO 1142
0.0160
PRO 1142
ASN 1143
0.0000
ASN 1143
ARG 1144
0.0001
ARG 1144
ALA 1145
-0.0418
ALA 1145
LYS 1146
-0.0005
LYS 1146
ARG 1147
0.0001
ARG 1147
VAL 1148
0.0202
VAL 1148
ILE 1149
-0.0003
ILE 1149
THR 1150
-0.0000
THR 1150
THR 1151
-0.0035
THR 1151
PHE 1152
-0.0001
PHE 1152
ARG 1153
-0.0004
ARG 1153
THR 1154
0.0236
THR 1154
GLY 1155
0.0002
GLY 1155
THR 1156
-0.0001
THR 1156
TRP 1157
0.0261
TRP 1157
ASP 1158
-0.0002
ASP 1158
ALA 1159
-0.0001
ALA 1159
TYR 1160
0.0091
TYR 1160
ALA 235
0.0866
ALA 235
ARG 236
-0.0002
ARG 236
MET 237
-0.0002
MET 237
ARG 238
0.0016
ARG 238
LEU 239
0.0000
LEU 239
ASP 240
0.0001
ASP 240
VAL 241
-0.0236
VAL 241
GLU 242
-0.0000
GLU 242
LEU 243
-0.0001
LEU 243
ALA 244
0.0169
ALA 244
LYS 245
-0.0001
LYS 245
THR 246
0.0001
THR 246
LEU 247
0.0368
LEU 247
GLY 248
0.0001
GLY 248
LEU 249
-0.0003
LEU 249
VAL 250
-0.0113
VAL 250
LEU 251
-0.0004
LEU 251
ALA 252
0.0000
ALA 252
VAL 253
-0.0580
VAL 253
LEU 254
0.0002
LEU 254
LEU 255
0.0003
LEU 255
ILE 256
-0.0583
ILE 256
CYS 257
-0.0001
CYS 257
TRP 258
0.0004
TRP 258
PHE 259
-0.0014
PHE 259
PRO 260
-0.0003
PRO 260
VAL 261
0.0002
VAL 261
LEU 262
-0.0077
LEU 262
ALA 263
-0.0002
ALA 263
LEU 264
0.0001
LEU 264
MET 265
0.0051
MET 265
ALA 266
0.0002
ALA 266
HIS 267
0.0002
HIS 267
SER 268
0.0028
SER 268
LEU 269
0.0001
LEU 269
ALA 270
-0.0003
ALA 270
THR 271
-0.0098
THR 271
THR 272
0.0002
THR 272
LEU 273
-0.0002
LEU 273
SER 274
-0.0136
SER 274
ASP 275
0.0000
ASP 275
GLN 276
0.0003
GLN 276
VAL 277
-0.0064
VAL 277
LYS 278
-0.0003
LYS 278
LYS 279
0.0001
LYS 279
ALA 280
-0.0118
ALA 280
PHE 281
-0.0002
PHE 281
ALA 282
-0.0000
ALA 282
PHE 283
0.0018
PHE 283
CYS 284
0.0003
CYS 284
SER 285
0.0002
SER 285
MET 286
0.0289
MET 286
LEU 287
-0.0000
LEU 287
CYS 288
0.0001
CYS 288
LEU 289
0.0151
LEU 289
ILE 290
0.0000
ILE 290
ASN 291
0.0001
ASN 291
SER 292
0.0194
SER 292
MET 293
-0.0001
MET 293
VAL 294
0.0001
VAL 294
ASN 295
-0.0099
ASN 295
PRO 296
0.0003
PRO 296
VAL 297
-0.0004
VAL 297
ILE 298
-0.0770
ILE 298
TYR 299
0.0000
TYR 299
ALA 300
-0.0001
ALA 300
LEU 301
-0.0091
LEU 301
ARG 302
0.0001
ARG 302
SER 303
0.0000
SER 303
GLU 304
0.0003
GLU 304
GLU 305
-0.0002
GLU 305
ILE 306
0.0001
ILE 306
ARG 307
-0.0153
ARG 307
SER 308
-0.0002
SER 308
SER 309
0.0003
SER 309
ALA 310
-0.1215
ALA 310
HIS 311
-0.0001
HIS 311
HIS 311
0.0225
HIS 311
HIS 312
-0.0001
HIS 312
CYS 313
0.1820
CYS 313
LEU 314
0.0000
LEU 314
ALA 315
0.0001
ALA 315
HIS 316
0.1420
HIS 316
TRP 317
0.0001
TRP 317
LYS 318
0.0000
LYS 318
LYS 319
0.0514
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.