Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* *

CA strain for 2607171153561942151

--- normal mode 14 ---

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 0.0001

SER 2 ARG 3 0.0001

ARG 3 ILE 4 -0.0003

ILE 4 GLU 5 0.0800

GLU 5 LYS 6 0.0003

LYS 6 MET 7 -0.0002

MET 7 SER 8 -0.0001

SER 8 ILE 9 -0.1185

ILE 9 LEU 10 0.0000

LEU 10 GLY 11 0.0002

GLY 11 VAL 12 -0.0002

VAL 12 ARG 13 0.0012

ARG 13 SER 14 -0.0001

SER 14 PHE 15 0.0001

PHE 15 GLY 16 -0.0002

GLY 16 ILE 17 0.0092

ILE 17 GLU 18 0.0002

GLU 18 ASP 19 -0.0000

ASP 19 LYS 20 0.0000

LYS 20 ASP 21 0.0122

ASP 21 LYS 22 -0.0001

LYS 22 GLN 23 0.0000

GLN 23 ILE 24 0.0001

ILE 24 ILE 25 0.1062

ILE 25 THR 26 0.0002

THR 26 PHE 27 -0.0001

PHE 27 PHE 28 0.0002

PHE 28 SER 29 0.0685

SER 29 PRO 30 0.0000

PRO 30 LEU 31 -0.0003

LEU 31 THR 32 -0.0001

THR 32 ILE 33 -0.0102

ILE 33 LEU 34 0.0003

LEU 34 VAL 35 0.0003

VAL 35 GLY 36 -0.0002

GLY 36 PRO 37 -0.0103

PRO 37 ASN 38 -0.0002

ASN 38 GLY 39 -0.0004

GLY 39 ALA 40 0.0000

ALA 40 GLY 41 0.0229

GLY 41 LYS 42 0.0004

LYS 42 THR 43 -0.0001

THR 43 THR 44 -0.0001

THR 44 ILE 45 -0.0295

ILE 45 ILE 46 -0.0003

ILE 46 GLU 47 -0.0002

GLU 47 CYS 48 0.0000

CYS 48 LEU 49 -0.0309

LEU 49 LYS 50 -0.0004

LYS 50 TYR 51 0.0001

TYR 51 ILE 52 0.0003

ILE 52 CYS 53 -0.0118

CYS 53 THR 54 0.0003

THR 54 GLY 55 -0.0001

GLY 55 ASP 56 0.0002

ASP 56 PHE 57 0.0060

PHE 57 PRO 58 0.0002

PRO 58 PRO 59 -0.0000

PRO 59 GLY 60 0.0001

GLY 60 THR 61 -0.2580

THR 61 LYS 62 0.0002

LYS 62 GLY 63 -0.0003

GLY 63 ASN 64 0.0003

ASN 64 THR 65 -0.0063

THR 65 PHE 66 -0.0001

PHE 66 VAL 67 -0.0001

VAL 67 HIS 68 0.0001

HIS 68 ASP 69 -0.0867

ASP 69 PRO 70 0.0004

PRO 70 LYS 71 0.0001

LYS 71 VAL 72 -0.0002

VAL 72 ALA 73 0.0219

ALA 73 GLN 74 -0.0002

GLN 74 GLU 75 -0.0002

GLU 75 THR 76 -0.0000

THR 76 ASP 77 0.0486

ASP 77 VAL 78 0.0004

VAL 78 ARG 79 -0.0004

ARG 79 ALA 80 0.0003

ALA 80 GLN 81 0.0186

GLN 81 ILE 82 -0.0001

ILE 82 HIS 83 0.0002

HIS 83 LEU 84 -0.0001

LEU 84 GLN 85 0.0060

GLN 85 PHE 86 0.0001

PHE 86 ARG 87 0.0002

ARG 87 ASP 88 0.0004

ASP 88 VAL 89 -0.0362

VAL 89 ASN 90 -0.0004

ASN 90 GLY 91 0.0001

GLY 91 GLU 92 0.0003

GLU 92 LEU 93 0.1072

LEU 93 ILE 94 -0.0000

ILE 94 ALA 95 0.0003

ALA 95 VAL 96 -0.0000

VAL 96 GLN 97 0.0836

GLN 97 ARG 98 -0.0000

ARG 98 SER 99 -0.0005

SER 99 MET 100 0.0002

MET 100 VAL 101 0.1928

VAL 101 CYS 102 0.0000

CYS 102 THR 103 0.0001

THR 103 GLN 104 -0.0001

GLN 104 LYS 105 0.0392

LYS 105 SER 106 -0.0001

SER 106 LYS 107 0.0001

LYS 107 LYS 108 -0.0000

LYS 108 THR 109 -0.1150

THR 109 GLU 110 0.0001

GLU 110 PHE 111 -0.0002

PHE 111 LYS 112 -0.0001

LYS 112 THR 113 0.1401

THR 113 LEU 114 -0.0001

LEU 114 GLU 115 -0.0004

GLU 115 GLY 116 -0.0002

GLY 116 VAL 117 0.1333

VAL 117 ILE 118 -0.0002

ILE 118 THR 119 0.0000

THR 119 ARG 120 0.0000

ARG 120 THR 121 0.0294

THR 121 LYS 122 0.0002

LYS 122 HIS 123 -0.0000

HIS 123 GLY 124 -0.0005

GLY 124 GLU 125 -0.0021

GLU 125 LYS 126 -0.0001

LYS 126 VAL 127 -0.0001

VAL 127 SER 128 -0.0002

SER 128 LEU 129 -0.0632

LEU 129 SER 130 -0.0000

SER 130 SER 131 -0.0002

SER 131 LYS 132 0.0001

LYS 132 CYS 133 -0.0234

CYS 133 ALA 134 0.0001

ALA 134 GLU 135 -0.0001

GLU 135 ILE 136 0.0002

ILE 136 ASP 137 -0.0332

ASP 137 ARG 138 0.0000

ARG 138 GLU 139 0.0005

GLU 139 MET 140 -0.0002

MET 140 ILE 141 -0.0192

ILE 141 SER 142 -0.0004

SER 142 SER 143 -0.0003

SER 143 LEU 144 -0.0001

LEU 144 GLY 145 -0.0098

GLY 145 VAL 146 0.0002

VAL 146 SER 147 0.0000

SER 147 LYS 148 -0.0001

LYS 148 ALA 149 0.0287

ALA 149 VAL 150 -0.0002

VAL 150 LEU 151 -0.0002

LEU 151 ASN 152 -0.0004

ASN 152 ASN 153 -0.0254

ASN 153 VAL 154 -0.0004

VAL 154 ILE 155 -0.0001

ILE 155 PHE 156 0.0001

PHE 156 CYS 157 0.0285

CYS 157 HIS 158 0.0001

HIS 158 GLN 159 -0.0001

GLN 159 GLU 160 0.0000

GLU 160 ASP 161 0.0143

ASP 161 SER 162 0.0005

SER 162 ASN 163 -0.0002

ASN 163 TRP 164 -0.0003

TRP 164 PRO 165 -0.0602

PRO 165 LEU 166 0.0001

LEU 166 SER 1202 -0.0200

SER 1202 ALA 1203 -0.0004

ALA 1203 GLY 1204 0.0001

GLY 1204 GLN 1205 0.0001

GLN 1205 LYS 1206 -0.0300

LYS 1206 VAL 1207 0.0000

VAL 1207 LEU 1208 -0.0002

LEU 1208 ALA 1209 0.0004

ALA 1209 SER 1210 -0.0323

SER 1210 LEU 1211 0.0001

LEU 1211 ILE 1212 -0.0001

ILE 1212 ILE 1213 0.0000

ILE 1213 ARG 1214 0.0322

ARG 1214 LEU 1215 -0.0002

LEU 1215 ALA 1216 0.0002

ALA 1216 LEU 1217 0.0002

LEU 1217 ALA 1218 0.0737

ALA 1218 GLU 1219 0.0001

GLU 1219 THR 1220 -0.0002

THR 1220 PHE 1221 0.0002

PHE 1221 CYS 1222 0.0495

CYS 1222 LEU 1223 0.0004

LEU 1223 ASN 1224 0.0002

ASN 1224 CYS 1225 0.0001

CYS 1225 GLY 1226 -0.1001

GLY 1226 ILE 1227 -0.0001

ILE 1227 ILE 1228 0.0004

ILE 1228 ALA 1229 -0.0003

ALA 1229 LEU 1230 0.0123

LEU 1230 ASP 1231 -0.0005

ASP 1231 GLU 1232 -0.0000

GLU 1232 PRO 1233 -0.0002

PRO 1233 THR 1234 0.0128

THR 1234 THR 1235 0.0002

THR 1235 ASN 1236 -0.0000

ASN 1236 LEU 1237 -0.0000

LEU 1237 ASP 1238 0.1608

ASP 1238 ARG 1239 0.0001

ARG 1239 GLU 1240 0.0000

GLU 1240 ASN 1241 -0.0004

ASN 1241 ILE 1242 -0.0238

ILE 1242 GLU 1243 -0.0002

GLU 1243 SER 1244 -0.0000

SER 1244 LEU 1245 0.0004

LEU 1245 ALA 1246 0.0536

ALA 1246 HIS 1247 0.0000

HIS 1247 ALA 1248 0.0003

ALA 1248 LEU 1249 -0.0000

LEU 1249 VAL 1250 0.0551

VAL 1250 GLU 1251 0.0001

GLU 1251 ILE 1252 0.0003

ILE 1252 ILE 1253 0.0002

ILE 1253 LYS 1254 0.0464

LYS 1254 SER 1255 0.0000

SER 1255 ARG 1256 -0.0001

ARG 1256 SER 1257 -0.0001

SER 1257 GLN 1258 0.0145

GLN 1258 GLN 1259 -0.0002

GLN 1259 ARG 1260 -0.0002

ARG 1260 ASN 1261 0.0003

ASN 1261 PHE 1262 -0.0218

PHE 1262 GLN 1263 0.0002

GLN 1263 LEU 1264 -0.0002

LEU 1264 LEU 1265 0.0003

LEU 1265 VAL 1266 -0.0095

VAL 1266 ILE 1267 0.0001

ILE 1267 THR 1268 -0.0003

THR 1268 HIS 1269 0.0000

HIS 1269 ASP 1270 0.0592

ASP 1270 GLU 1271 -0.0001

GLU 1271 ASP 1272 0.0000

ASP 1272 PHE 1273 0.0001

PHE 1273 VAL 1274 -0.0133

VAL 1274 GLU 1275 0.0001

GLU 1275 LEU 1276 0.0001

LEU 1276 LEU 1277 -0.0002

LEU 1277 GLY 1278 0.0657

GLY 1278 ARG 1279 0.0005

ARG 1279 SER 1280 0.0005

SER 1280 GLU 1281 0.0001

GLU 1281 TYR 1282 0.0168

TYR 1282 VAL 1283 -0.0003

VAL 1283 GLU 1284 -0.0001

GLU 1284 LYS 1285 0.0001

LYS 1285 PHE 1286 -0.0585

PHE 1286 TYR 1287 0.0001

TYR 1287 ARG 1288 -0.0004

ARG 1288 ILE 1289 0.0001

ILE 1289 LYS 1290 -0.0138

LYS 1290 LYS 1291 0.0001

LYS 1291 ASN 1292 -0.0000

ASN 1292 ILE 1293 -0.0002

ILE 1293 ASP 1294 -0.0025

ASP 1294 GLN 1295 0.0001

GLN 1295 CYS 1296 -0.0001

CYS 1296 SER 1297 -0.0001

SER 1297 GLU 1298 0.0177

GLU 1298 ILE 1299 0.0000

ILE 1299 VAL 1300 -0.0000

VAL 1300 LYS 1301 0.0004

LYS 1301 CYS 1302 -0.0114

CYS 1302 SER 1303 -0.0000

SER 1303 VAL 1304 -0.0004

VAL 1304 SER 1305 0.0001

SER 1305 SER 1306 0.0255

SER 1306 GLU 10 -0.0034

GLU 10 ASN 11 0.0001

ASN 11 THR 12 -0.0000

THR 12 PHE 13 0.0004

PHE 13 LYS 14 -0.0535

LYS 14 ILE 15 -0.0003

ILE 15 LEU 16 0.0001

LEU 16 VAL 17 -0.0004

VAL 17 ALA 18 0.0005

ALA 18 THR 19 0.0001

THR 19 ASP 20 0.0001

ASP 20 ILE 21 0.0001

ILE 21 HIS 22 0.0191

HIS 22 LEU 23 -0.0000

LEU 23 GLY 24 0.0001

GLY 24 PHE 25 -0.0004

PHE 25 MET 26 0.0354

MET 26 GLU 27 0.0003

GLU 27 LYS 28 0.0001

LYS 28 ASP 29 -0.0003

ASP 29 ALA 30 0.0469

ALA 30 VAL 31 -0.0002

VAL 31 ARG 32 0.0003

ARG 32 GLY 33 0.0000

GLY 33 ASN 34 0.0407

ASN 34 ASP 35 -0.0003

ASP 35 THR 36 -0.0002

THR 36 PHE 37 -0.0001

PHE 37 VAL 38 -0.0265

VAL 38 THR 39 -0.0002

THR 39 LEU 40 0.0001

LEU 40 ASP 41 -0.0001

ASP 41 GLU 42 -0.0136

GLU 42 ILE 43 -0.0006

ILE 43 LEU 44 0.0001

LEU 44 ARG 45 0.0002

ARG 45 LEU 46 -0.0002

LEU 46 ALA 47 0.0000

ALA 47 GLN 48 -0.0003

GLN 48 GLU 49 0.0002

GLU 49 ASN 50 -0.0222

ASN 50 GLU 51 -0.0001

GLU 51 VAL 52 0.0001

VAL 52 ASP 53 -0.0003

ASP 53 PHE 54 0.0039

PHE 54 ILE 55 0.0003

ILE 55 LEU 56 0.0001

LEU 56 LEU 57 0.0001

LEU 57 GLY 58 0.0591

GLY 58 GLY 59 -0.0002

GLY 59 ASP 60 0.0003

ASP 60 LEU 61 0.0003

LEU 61 PHE 62 0.0220

PHE 62 HIS 63 -0.0004

HIS 63 GLU 64 -0.0001

GLU 64 ASN 65 0.0002

ASN 65 LYS 66 0.0065

LYS 66 PRO 67 0.0003

PRO 67 SER 68 -0.0001

SER 68 ARG 69 0.0001

ARG 69 LYS 70 -0.0583

LYS 70 THR 71 -0.0004

THR 71 LEU 72 -0.0000

LEU 72 HIS 73 0.0002

HIS 73 THR 74 -0.0321

THR 74 CYS 75 -0.0002

CYS 75 LEU 76 0.0003

LEU 76 GLU 77 0.0001

GLU 77 LEU 78 -0.0199

LEU 78 LEU 79 -0.0002

LEU 79 ARG 80 -0.0001

ARG 80 LYS 81 -0.0000

LYS 81 TYR 82 0.0067

TYR 82 CYS 83 -0.0003

CYS 83 MET 84 0.0002

MET 84 GLY 85 -0.0000

GLY 85 ASP 86 0.0582

ASP 86 ARG 87 0.0003

ARG 87 PRO 88 0.0001

PRO 88 VAL 89 0.0002

VAL 89 GLN 90 0.0167

GLN 90 PHE 91 0.0002

PHE 91 GLU 92 0.0001

GLU 92 ILE 93 -0.0001

ILE 93 LEU 94 -0.0704

LEU 94 SER 95 -0.0003

SER 95 ASP 96 -0.0001

ASP 96 GLN 97 -0.0000

GLN 97 SER 98 0.0203

SER 98 VAL 99 0.0001

VAL 99 ASN 100 -0.0002

ASN 100 PHE 101 -0.0003

PHE 101 GLY 102 -0.0637

GLY 102 PHE 103 -0.0002

PHE 103 SER 104 -0.0001

SER 104 LYS 105 0.0000

LYS 105 PHE 106 -0.0380

PHE 106 PRO 107 -0.0001

PRO 107 TRP 108 0.0001

TRP 108 VAL 109 -0.0002

VAL 109 ASN 110 -0.0333

ASN 110 TYR 111 -0.0002

TYR 111 GLN 112 0.0000

GLN 112 ASP 113 -0.0002

ASP 113 GLY 114 -0.0592

GLY 114 ASN 115 0.0004

ASN 115 LEU 116 0.0005

LEU 116 ASN 117 -0.0003

ASN 117 ILE 118 0.0357

ILE 118 SER 119 0.0000

SER 119 ILE 120 -0.0001

ILE 120 PRO 121 0.0005

PRO 121 VAL 122 -0.0071

VAL 122 PHE 123 -0.0003

PHE 123 SER 124 -0.0002

SER 124 ILE 125 0.0004

ILE 125 HIS 126 0.0443

HIS 126 GLY 127 -0.0000

GLY 127 ASN 128 -0.0002

ASN 128 HIS 129 0.0002

HIS 129 ASP 130 0.0045

ASP 130 ASP 131 -0.0000

ASP 131 PRO 132 -0.0004

PRO 132 THR 133 0.0002

THR 133 GLY 134 0.0212

GLY 134 ALA 135 0.0001

ALA 135 ASP 136 -0.0001

ASP 136 ALA 137 0.0000

ALA 137 LEU 138 -0.0712

LEU 138 CYS 139 -0.0002

CYS 139 ALA 140 0.0000

ALA 140 LEU 141 0.0000

LEU 141 ASP 142 0.0542

ASP 142 ILE 143 -0.0005

ILE 143 LEU 144 0.0003

LEU 144 SER 145 -0.0000

SER 145 CYS 146 0.0258

CYS 146 ALA 147 -0.0001

ALA 147 GLY 148 0.0004

GLY 148 PHE 149 0.0000

PHE 149 VAL 150 -0.0474

VAL 150 ASN 151 0.0002

ASN 151 HIS 152 -0.0001

HIS 152 PHE 153 -0.0001

PHE 153 GLY 154 -0.1312

GLY 154 ARG 155 0.0001

ARG 155 SER 156 0.0000

SER 156 MET 157 -0.0001

MET 157 SER 158 -0.4567

SER 158 VAL 159 -0.0002

VAL 159 GLU 160 0.0002

GLU 160 LYS 161 -0.0000

LYS 161 ILE 162 -0.0066

ILE 162 ASP 163 -0.0002

ASP 163 ILE 164 -0.0001

ILE 164 SER 165 -0.0000

SER 165 PRO 166 -0.1972

PRO 166 VAL 167 0.0001

VAL 167 LEU 168 0.0001

LEU 168 LEU 169 -0.0003

LEU 169 GLN 170 -0.0404

GLN 170 LYS 171 -0.0001

LYS 171 GLY 172 -0.0001

GLY 172 SER 173 -0.0001

SER 173 THR 174 0.0074

THR 174 LYS 175 0.0000

LYS 175 ILE 176 -0.0000

ILE 176 ALA 177 0.0000

ALA 177 LEU 178 0.0449

LEU 178 TYR 179 -0.0001

TYR 179 GLY 180 -0.0000

GLY 180 LEU 181 0.0000

LEU 181 GLY 182 0.0950

GLY 182 SER 183 -0.0001

SER 183 ILE 184 -0.0001

ILE 184 PRO 185 0.0002

PRO 185 ASP 186 -0.0120

ASP 186 GLU 187 0.0004

GLU 187 ARG 188 0.0003

ARG 188 LEU 189 -0.0000

LEU 189 TYR 190 -0.0210

TYR 190 ARG 191 -0.0003

ARG 191 MET 192 0.0001

MET 192 PHE 193 0.0001

PHE 193 VAL 194 -0.0919

VAL 194 ASN 195 0.0002

ASN 195 LYS 196 0.0000

LYS 196 LYS 197 -0.0002

LYS 197 VAL 198 -0.1042

VAL 198 THR 199 0.0004

THR 199 MET 200 -0.0003

MET 200 LEU 201 -0.0001

LEU 201 ARG 202 -0.0060

ARG 202 PRO 203 0.0000

PRO 203 LYS 204 0.0002

LYS 204 GLU 205 -0.0004

GLU 205 ASP 206 -0.0107

ASP 206 GLU 207 0.0000

GLU 207 ASN 208 0.0004

ASN 208 SER 209 -0.0001

SER 209 TRP 210 -0.0008

TRP 210 PHE 211 -0.0001

PHE 211 ASN 212 0.0004

ASN 212 LEU 213 -0.0001

LEU 213 PHE 214 0.0457

PHE 214 VAL 215 -0.0005

VAL 215 ILE 216 0.0003

ILE 216 HIS 217 0.0001

HIS 217 GLN 218 0.0202

GLN 218 ASN 219 0.0000

ASN 219 ARG 220 0.0004

ARG 220 SER 221 -0.0002

SER 221 LYS 222 0.0696

LYS 222 HIS 223 0.0002

HIS 223 GLY 224 0.0000

GLY 224 SER 225 0.0004

SER 225 THR 226 0.1065

THR 226 ASN 227 0.0001

ASN 227 PHE 228 -0.0001

PHE 228 ILE 229 0.0000

ILE 229 PRO 230 -0.0618

PRO 230 GLU 231 -0.0004

GLU 231 GLN 232 -0.0001

GLN 232 PHE 233 0.0002

PHE 233 LEU 234 -0.0666

LEU 234 ASP 235 0.0000

ASP 235 ASP 236 -0.0002

ASP 236 PHE 237 -0.0002

PHE 237 ILE 238 -0.0181

ILE 238 ASP 239 0.0002

ASP 239 LEU 240 -0.0001

LEU 240 VAL 241 -0.0005

VAL 241 ILE 242 -0.0271

ILE 242 TRP 243 -0.0002

TRP 243 GLY 244 0.0003

GLY 244 HIS 245 0.0001

HIS 245 GLU 246 -0.0073

GLU 246 HIS 247 0.0003

HIS 247 GLU 248 -0.0004

GLU 248 CYS 249 0.0002

CYS 249 LYS 250 -0.0075

LYS 250 ILE 251 -0.0003

ILE 251 ALA 252 -0.0000

ALA 252 PRO 253 -0.0002

PRO 253 THR 254 0.2102

THR 254 LYS 255 0.0001

LYS 255 ASN 256 -0.0002

ASN 256 GLU 257 0.0002

GLU 257 GLN 258 0.0514

GLN 258 GLN 259 -0.0000

GLN 259 LEU 260 0.0001

LEU 260 PHE 261 0.0002

PHE 261 TYR 262 -0.0329

TYR 262 ILE 263 0.0004

ILE 263 SER 264 0.0001

SER 264 GLN 265 -0.0005

GLN 265 PRO 266 0.0970

PRO 266 GLY 267 0.0001

GLY 267 SER 268 0.0000

SER 268 SER 269 -0.0001

SER 269 VAL 270 0.0023

VAL 270 VAL 271 -0.0001

VAL 271 THR 272 0.0003

THR 272 SER 273 0.0001

SER 273 LEU 274 -0.0063

LEU 274 SER 275 0.0000

SER 275 PRO 276 0.0001

PRO 276 GLY 277 0.0001

GLY 277 GLU 278 -0.0097

GLU 278 ALA 279 -0.0002

ALA 279 VAL 280 -0.0003

VAL 280 LYS 281 -0.0001

LYS 281 LYS 282 -0.0391

LYS 282 HIS 283 0.0001

HIS 283 VAL 284 -0.0005

VAL 284 GLY 285 0.0000

GLY 285 LEU 286 -0.0380

LEU 286 LEU 287 0.0001

LEU 287 ARG 288 -0.0001

ARG 288 ILE 289 -0.0001

ILE 289 LYS 290 -0.0237

LYS 290 GLY 291 0.0002

GLY 291 ARG 292 0.0003

ARG 292 LYS 293 0.0002

LYS 293 MET 294 -0.0580

MET 294 ASN 295 -0.0002

ASN 295 MET 296 0.0001

MET 296 HIS 297 -0.0001

HIS 297 LYS 298 -0.0799

LYS 298 ILE 299 0.0004

ILE 299 PRO 300 -0.0001

PRO 300 LEU 301 -0.0003

LEU 301 HIS 302 -0.0192

HIS 302 THR 303 0.0000

THR 303 VAL 304 -0.0000

VAL 304 ARG 305 0.0002

ARG 305 LYS 690 0.0187

LYS 690 VAL 691 0.0003

VAL 691 THR 692 0.0000

THR 692 TYR 693 -0.0003

TYR 693 PRO 694 -0.0347

PRO 694 GLY 695 0.0001

GLY 695 ALA 696 0.0003

ALA 696 GLY 697 0.0001

GLY 697 LYS 698 0.1097

LYS 698 LEU 699 -0.0001

LEU 699 PRO 700 -0.0001

PRO 700 HIS 701 0.0000

HIS 701 ILE 702 -0.0127

ILE 702 ILE 703 -0.0004

ILE 703 GLY 704 -0.0004

GLY 704 GLY 705 0.0000

GLY 705 SER 706 -0.0433

SER 706 ASP 707 -0.0000

ASP 707 LEU 708 0.0002

LEU 708 ILE 709 0.0002

ILE 709 ALA 710 -0.0358

ALA 710 HIS 711 -0.0001

HIS 711 HIS 712 -0.0003

HIS 712 ALA 713 0.0003

ALA 713 ARG 714 0.2807

ARG 714 LYS 715 -0.0001

LYS 715 ASN 716 -0.0002

ASN 716 THR 717 0.0001

THR 717 GLU 718 -0.0995

GLU 718 LEU 719 0.0003

LEU 719 GLU 720 -0.0000

GLU 720 GLU 721 0.0002

GLU 721 TRP 722 0.0077

TRP 722 LEU 723 0.0002

LEU 723 ARG 724 0.0000

ARG 724 GLN 725 -0.0000

GLN 725 GLU 726 -0.0948

GLU 726 MET 727 -0.0002

MET 727 GLU 728 -0.0001

GLU 728 VAL 729 0.0002

VAL 729 GLN 730 -0.0394

GLN 730 ASN 731 0.0001

ASN 731 GLN 732 0.0001

GLN 732 HIS 733 -0.0003

HIS 733 ALA 734 -0.0960

ALA 734 LYS 735 0.0002

LYS 735 GLU 736 -0.0001

GLU 736 GLU 737 0.0001

GLU 737 SER 738 0.0956

SER 738 LEU 739 -0.0004

LEU 739 ALA 740 -0.0002

ALA 740 ASP 741 0.0000

ASP 741 ASP 742 0.0916

ASP 742 LEU 743 0.0002

LEU 743 PHE 744 0.0001

PHE 744 ARG 745 -0.0002

ARG 745 TYR 746 0.0415

TYR 746 ASN 747 0.0002

ASN 747 PRO 748 0.0001

PRO 748 TYR 749 -0.0002

TYR 749 LEU 750 0.0000

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** ***

CA strain for 2607171153561942151

--- normal mode 14 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* *