Should you encounter any unexpected behaviour,
please let us know.

* *

CA strain for 22022413193125998

--- normal mode 8 ---

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
ARG 79 PRO 80 0.0000

PRO 80 GLU 81 0.1504

GLU 81 ASP 82 -0.0001

ASP 82 LEU 83 0.0723

LEU 83 GLY 84 0.0000

GLY 84 THR 85 0.1984

THR 85 GLY 86 -0.0000

GLY 86 LEU 87 0.1563

LEU 87 LEU 88 -0.0004

LEU 88 GLU 89 0.2415

GLU 89 ALA 90 -0.0002

ALA 90 LEU 91 -0.0950

LEU 91 LEU 92 0.0003

LEU 92 ARG 93 0.0117

ARG 93 GLY 94 0.0000

GLY 94 ASP 95 -0.1517

ASP 95 LEU 96 -0.0002

LEU 96 ALA 97 -0.1272

ALA 97 GLY 98 0.0000

GLY 98 ALA 99 -0.0243

ALA 99 GLU 100 -0.0003

GLU 100 ALA 101 0.1675

ALA 101 LEU 102 0.0001

LEU 102 PHE 103 -0.0060

PHE 103 ARG 104 -0.0001

ARG 104 ARG 105 0.5671

ARG 105 GLY 106 0.0001

GLY 106 LEU 107 -0.1492

LEU 107 ARG 108 0.0003

ARG 108 PHE 109 0.0290

PHE 109 TRP 110 0.0001

TRP 110 GLY 111 0.1645

GLY 111 PRO 112 -0.0004

PRO 112 GLU 113 0.0003

GLU 113 GLY 114 -0.0004

GLY 114 VAL 115 0.0133

VAL 115 LEU 116 -0.0000

LEU 116 GLU 117 0.0360

GLU 117 HIS 118 -0.0000

HIS 118 LEU 119 0.1731

LEU 119 LEU 120 0.0001

LEU 120 LEU 121 0.0295

LEU 121 PRO 122 0.0003

PRO 122 VAL 123 0.1180

VAL 123 LEU 124 0.0001

LEU 124 ARG 125 0.1452

ARG 125 GLU 126 0.0004

GLU 126 VAL 127 -0.1355

VAL 127 GLY 128 -0.0001

GLY 128 GLU 129 0.0363

GLU 129 ALA 130 -0.0002

ALA 130 TRP 131 -0.0710

TRP 131 HIS 132 -0.0002

HIS 132 ARG 133 0.0054

ARG 133 GLY 134 0.0000

GLY 134 GLU 135 0.1073

GLU 135 ILE 136 -0.0001

ILE 136 GLY 137 -0.4280

GLY 137 VAL 138 0.0002

VAL 138 ALA 139 0.0025

ALA 139 GLU 140 0.0005

GLU 140 GLU 141 0.1030

GLU 141 HIS 142 0.0003

HIS 142 LEU 143 0.0336

LEU 143 ALA 144 -0.0001

ALA 144 SER 145 0.1400

SER 145 THR 146 -0.0003

THR 146 PHE 147 0.1001

PHE 147 LEU 148 -0.0002

LEU 148 ARG 149 -0.0267

ARG 149 ALA 150 -0.0001

ALA 150 ARG 151 0.1863

ARG 151 LEU 152 0.0002

LEU 152 GLN 153 0.2123

GLN 153 GLU 154 -0.0003

GLU 154 LEU 155 0.3082

LEU 155 LEU 156 0.0000

LEU 156 ASP 157 0.4387

ASP 157 LEU 158 -0.0000

LEU 158 ALA 159 0.1021

ALA 159 GLY 160 0.0003

GLY 160 PHE 161 0.1419

PHE 161 PRO 162 0.0000

PRO 162 PRO 163 -0.0782

PRO 163 GLY 164 0.0004

GLY 164 PRO 165 0.0397

PRO 165 PRO 166 -0.0002

PRO 166 VAL 167 0.0422

VAL 167 LEU 168 -0.0002

LEU 168 VAL 169 0.0071

VAL 169 THR 170 0.0001

THR 170 THR 171 0.0379

THR 171 PRO 172 0.0004

PRO 172 PRO 173 0.0257

PRO 173 GLY 174 -0.0003

GLY 174 GLU 175 0.0984

GLU 175 ARG 176 -0.0000

ARG 176 HIS 177 -0.0457

HIS 177 GLU 178 -0.0000

GLU 178 ILE 179 -0.0464

ILE 179 GLY 180 -0.0001

GLY 180 ALA 181 0.0118

ALA 181 MET 182 0.0002

MET 182 LEU 183 -0.0327

LEU 183 ALA 184 -0.0001

ALA 184 ALA 185 0.0688

ALA 185 TYR 186 0.0001

TYR 186 HIS 187 0.0834

HIS 187 LEU 188 -0.0001

LEU 188 ARG 189 0.1135

ARG 189 ARG 190 -0.0002

ARG 190 LYS 191 0.0149

LYS 191 GLY 192 0.0002

GLY 192 VAL 193 -0.0051

VAL 193 PRO 194 -0.0001

PRO 194 ALA 195 -0.0379

ALA 195 LEU 196 -0.0002

LEU 196 TYR 197 -0.0363

TYR 197 LEU 198 -0.0003

LEU 198 GLY 199 0.0268

GLY 199 PRO 200 0.0002

PRO 200 ASP 201 0.0419

ASP 201 THR 202 -0.0000

THR 202 PRO 203 0.0922

PRO 203 LEU 204 -0.0002

LEU 204 PRO 205 -0.0357

PRO 205 ASP 206 -0.0001

ASP 206 LEU 207 -0.0841

LEU 207 ARG 208 0.0001

ARG 208 ALA 209 -0.1600

ALA 209 LEU 210 0.0000

LEU 210 ALA 211 -0.0555

ALA 211 ARG 212 -0.0002

ARG 212 ARG 213 -0.1242

ARG 213 LEU 214 0.0001

LEU 214 GLY 215 0.0364

GLY 215 ALA 216 0.0000

ALA 216 GLY 217 0.0246

GLY 217 ALA 218 0.0000

ALA 218 VAL 219 0.0020

VAL 219 VAL 220 0.0000

VAL 220 LEU 221 0.0319

LEU 221 SER 222 0.0003

SER 222 ALA 223 0.1142

ALA 223 VAL 224 -0.0001

VAL 224 LEU 225 0.0856

LEU 225 SER 226 -0.0000

SER 226 GLU 227 -0.0412

GLU 227 PRO 228 -0.0002

PRO 228 LEU 229 -0.0622

LEU 229 ARG 230 -0.0002

ARG 230 ALA 231 -0.0142

ALA 231 LEU 232 -0.0000

LEU 232 PRO 233 -0.0606

PRO 233 ASP 234 0.0002

ASP 234 GLY 235 -0.0351

GLY 235 ALA 236 -0.0001

ALA 236 LEU 237 0.0485

LEU 237 LYS 238 -0.0002

LYS 238 ASP 239 0.0030

ASP 239 LEU 240 0.0001

LEU 240 ALA 241 -0.0164

ALA 241 PRO 242 0.0003

PRO 242 ARG 243 -0.0146

ARG 243 VAL 244 0.0001

VAL 244 PHE 245 -0.0358

PHE 245 LEU 246 -0.0001

LEU 246 GLY 247 0.0223

GLY 247 GLY 248 -0.0001

GLY 248 GLN 249 -0.0052

GLN 249 GLY 250 -0.0004

GLY 250 ALA 251 -0.0001

ALA 251 GLY 252 0.0001

GLY 252 PRO 253 -0.0694

PRO 253 GLU 254 0.0003

GLU 254 GLU 255 -0.0887

GLU 255 ALA 256 0.0001

ALA 256 ARG 257 0.0402

ARG 257 ARG 258 0.0002

ARG 258 LEU 259 -0.0612

LEU 259 GLY 260 -0.0002

GLY 260 ALA 261 0.0540

ALA 261 GLU 262 -0.0001

GLU 262 TYR 263 -0.0494

TYR 263 MET 264 -0.0000

MET 264 GLU 265 -0.0796

GLU 265 ASP 266 0.0002

ASP 266 LEU 267 0.1479

LEU 267 LYS 268 -0.0002

LYS 268 GLY 269 -0.0547

GLY 269 LEU 270 -0.0001

LEU 270 ALA 271 0.0902

ALA 271 GLU 272 0.0001

GLU 272 ALA 273 0.0031

ALA 273 LEU 274 0.0002

LEU 274 ASP 82 0.0764

ASP 82 LEU 83 -0.0002

LEU 83 GLY 84 0.0120

GLY 84 THR 85 -0.0004

THR 85 GLY 86 0.0785

GLY 86 LEU 87 0.0003

LEU 87 LEU 88 -0.0586

LEU 88 GLU 89 0.0002

GLU 89 ALA 90 0.1428

ALA 90 LEU 91 -0.0003

LEU 91 LEU 92 -0.0440

LEU 92 ARG 93 -0.0005

ARG 93 GLY 94 0.0656

GLY 94 ASP 95 0.0000

ASP 95 LEU 96 -0.0223

LEU 96 ALA 97 0.0004

ALA 97 GLY 98 0.2446

GLY 98 ALA 99 0.0000

ALA 99 GLU 100 -0.0434

GLU 100 ALA 101 0.0001

ALA 101 LEU 102 0.1404

LEU 102 PHE 103 -0.0003

PHE 103 ARG 104 -0.0663

ARG 104 ARG 105 0.0000

ARG 105 GLY 106 0.0242

GLY 106 LEU 107 0.0000

LEU 107 ARG 108 0.0265

ARG 108 PHE 109 -0.0000

PHE 109 TRP 110 -0.0348

TRP 110 GLY 111 -0.0002

GLY 111 PRO 112 0.0912

PRO 112 GLU 113 0.0000

GLU 113 GLY 114 -0.0322

GLY 114 VAL 115 0.0004

VAL 115 LEU 116 -0.0343

LEU 116 GLU 117 0.0000

GLU 117 HIS 118 0.0561

HIS 118 LEU 119 0.0001

LEU 119 LEU 120 0.0144

LEU 120 LEU 121 -0.0001

LEU 121 PRO 122 0.0650

PRO 122 VAL 123 0.0001

VAL 123 LEU 124 0.0304

LEU 124 ARG 125 0.0003

ARG 125 GLU 126 0.0385

GLU 126 VAL 127 0.0002

VAL 127 GLY 128 0.0878

GLY 128 GLU 129 -0.0001

GLU 129 ALA 130 -0.0193

ALA 130 TRP 131 0.0002

TRP 131 HIS 132 -0.0489

HIS 132 ARG 133 -0.0002

ARG 133 GLY 134 0.0639

GLY 134 GLU 135 -0.0001

GLU 135 ILE 136 -0.0819

ILE 136 GLY 137 -0.0001

GLY 137 VAL 138 -0.1378

VAL 138 ALA 139 -0.0001

ALA 139 GLU 140 -0.1470

GLU 140 GLU 141 0.0001

GLU 141 HIS 142 -0.0934

HIS 142 LEU 143 0.0004

LEU 143 ALA 144 -0.0106

ALA 144 SER 145 0.0001

SER 145 THR 146 0.0587

THR 146 PHE 147 0.0003

PHE 147 LEU 148 0.0132

LEU 148 ARG 149 0.0005

ARG 149 ALA 150 0.1751

ALA 150 ARG 151 0.0001

ARG 151 LEU 152 0.0418

LEU 152 GLN 153 -0.0001

GLN 153 GLU 154 -0.0270

GLU 154 LEU 155 -0.0002

LEU 155 LEU 156 -0.0689

LEU 156 ASP 157 0.0001

ASP 157 LEU 158 0.3436

LEU 158 ALA 159 -0.0000

ALA 159 GLY 160 0.0754

GLY 160 PHE 161 -0.0002

PHE 161 PRO 162 -0.0192

PRO 162 PRO 163 0.0002

PRO 163 GLY 164 0.0071

GLY 164 PRO 165 -0.0002

PRO 165 PRO 166 0.0800

PRO 166 VAL 167 0.0001

VAL 167 LEU 168 -0.0350

LEU 168 VAL 169 0.0001

VAL 169 THR 170 0.0101

THR 170 THR 171 -0.0001

THR 171 PRO 172 -0.0014

PRO 172 PRO 173 0.0000

PRO 173 GLY 174 0.1490

GLY 174 GLU 175 -0.0001

GLU 175 ARG 176 -0.1486

ARG 176 HIS 177 -0.0002

HIS 177 GLU 178 0.0004

GLU 178 ILE 179 0.0003

ILE 179 GLY 180 0.0499

GLY 180 ALA 181 -0.0004

ALA 181 MET 182 0.0303

MET 182 LEU 183 0.0001

LEU 183 ALA 184 -0.0093

ALA 184 ALA 185 -0.0003

ALA 185 TYR 186 -0.0733

TYR 186 HIS 187 -0.0000

HIS 187 LEU 188 -0.0534

LEU 188 ARG 189 -0.0002

ARG 189 ARG 190 -0.0010

ARG 190 LYS 191 -0.0001

LYS 191 GLY 192 0.1309

GLY 192 VAL 193 -0.0003

VAL 193 PRO 194 0.0947

PRO 194 ALA 195 -0.0002

ALA 195 LEU 196 0.0318

LEU 196 TYR 197 0.0003

TYR 197 LEU 198 -0.0103

LEU 198 GLY 199 -0.0002

GLY 199 PRO 200 -0.0230

PRO 200 ASP 201 0.0003

ASP 201 THR 202 0.2452

THR 202 PRO 203 0.0002

PRO 203 LEU 204 -0.2477

LEU 204 PRO 205 -0.0003

PRO 205 ASP 206 -0.2853

ASP 206 LEU 207 -0.0001

LEU 207 ARG 208 0.0485

ARG 208 ALA 209 -0.0003

ALA 209 LEU 210 -0.1534

LEU 210 ALA 211 -0.0000

ALA 211 ARG 212 0.0366

ARG 212 ARG 213 -0.0001

ARG 213 LEU 214 0.0584

LEU 214 GLY 215 0.0002

GLY 215 ALA 216 0.0220

ALA 216 GLY 217 -0.0001

GLY 217 ALA 218 0.0193

ALA 218 VAL 219 0.0000

VAL 219 VAL 220 0.0059

VAL 220 LEU 221 -0.0004

LEU 221 SER 222 0.1096

SER 222 ALA 223 0.0002

ALA 223 VAL 224 0.0800

VAL 224 LEU 225 0.0003

LEU 225 SER 226 0.0790

SER 226 GLU 227 -0.0001

GLU 227 PRO 228 -0.0944

PRO 228 LEU 229 0.0002

LEU 229 ARG 230 -0.0370

ARG 230 ALA 231 -0.0001

ALA 231 LEU 232 0.0485

LEU 232 PRO 233 0.0001

PRO 233 ASP 234 0.0209

ASP 234 GLY 235 0.0002

GLY 235 ALA 236 -0.1695

ALA 236 LEU 237 0.0002

LEU 237 LYS 238 0.0924

LYS 238 ASP 239 -0.0001

ASP 239 LEU 240 -0.0224

LEU 240 ALA 241 -0.0000

ALA 241 PRO 242 -0.0657

PRO 242 ARG 243 -0.0000

ARG 243 VAL 244 0.0253

VAL 244 PHE 245 0.0000

PHE 245 LEU 246 0.0441

LEU 246 GLY 247 -0.0002

GLY 247 GLY 248 -0.0077

GLY 248 GLN 249 0.0001

GLN 249 GLY 250 0.1920

GLY 250 ALA 251 -0.0000

ALA 251 GLY 252 -0.0904

GLY 252 PRO 253 -0.0002

PRO 253 GLU 254 0.0419

GLU 254 GLU 255 0.0001

GLU 255 ALA 256 0.0640

ALA 256 ARG 257 -0.0001

ARG 257 ARG 258 0.0053

ARG 258 LEU 259 0.0001

LEU 259 GLY 260 0.0886

GLY 260 ALA 261 0.0002

ALA 261 GLU 262 -0.0118

GLU 262 TYR 263 0.0001

TYR 263 MET 264 0.1279

MET 264 GLU 265 0.0003

GLU 265 ASP 266 0.2392

ASP 266 LEU 267 0.0001

LEU 267 LYS 268 -0.1518

LYS 268 GLY 269 0.0001

GLY 269 LEU 270 0.0261

LEU 270 ALA 271 0.0002

ALA 271 GLU 272 0.1237

GLU 272 ALA 273 0.0001

ALA 273 LEU 274 0.0300

LEU 274 ALA 275 -0.0001

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).
Last modification: October 18th, 2018.

Should you encounter any unexpected behaviour, please let us know.

*** ***

CA strain for 22022413193125998

--- normal mode 8 ---

Should you encounter any unexpected behaviour,
please let us know.

* *