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

* *

CA strain for EXAMPLE4

--- normal mode 7 ---

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
ASP 7 SER 8 -0.0001

SER 8 GLY 9 0.0002

GLY 9 VAL 10 0.1537

VAL 10 ASP 11 0.0002

ASP 11 SER 12 0.0001

SER 12 GLY 13 -0.1254

GLY 13 ARG 14 0.0000

ARG 14 PRO 15 0.0002

PRO 15 ILE 16 0.0508

ILE 16 GLY 17 0.0002

GLY 17 VAL 18 -0.0001

VAL 18 VAL 19 0.0709

VAL 19 PRO 20 -0.0000

PRO 20 PHE 21 0.0001

PHE 21 GLN 22 0.0659

GLN 22 TRP 23 0.0002

TRP 23 ALA 24 -0.0002

ALA 24 GLY 25 0.0003

GLY 25 PRO 26 -0.0001

PRO 26 GLY 27 -0.0001

GLY 27 ALA 28 0.0442

ALA 28 ALA 29 -0.0000

ALA 29 PRO 30 0.0004

PRO 30 GLU 31 0.0661

GLU 31 ASP 32 -0.0001

ASP 32 ILE 33 -0.0001

ILE 33 GLY 34 0.0258

GLY 34 GLY 35 -0.0004

GLY 35 ILE 36 -0.0001

ILE 36 VAL 37 -0.0032

VAL 37 ALA 38 0.0001

ALA 38 ALA 39 0.0002

ALA 39 ASP 40 0.0102

ASP 40 LEU 41 0.0000

LEU 41 ARG 42 0.0002

ARG 42 ASN 43 -0.0022

ASN 43 SER 44 -0.0001

SER 44 GLY 45 0.0002

GLY 45 LYS 46 -0.0273

LYS 46 PHE 47 -0.0002

PHE 47 ASN 48 0.0002

ASN 48 PRO 49 0.0984

PRO 49 LEU 50 -0.0002

LEU 50 ASP 51 -0.0001

ASP 51 ARG 52 0.0879

ARG 52 ALA 53 0.0000

ALA 53 ARG 54 0.0003

ARG 54 LEU 55 0.0222

LEU 55 PRO 56 -0.0002

PRO 56 GLN 57 0.0002

GLN 57 GLN 58 -0.0059

GLN 58 PRO 59 -0.0003

PRO 59 GLY 60 -0.0000

GLY 60 SER 61 0.0096

SER 61 ALA 62 -0.0001

ALA 62 GLN 63 0.0001

GLN 63 GLU 64 0.0005

GLU 64 VAL 65 0.0001

VAL 65 GLN 66 -0.0002

GLN 66 PRO 67 0.0010

PRO 67 ALA 68 -0.0000

ALA 68 ALA 69 0.0001

ALA 69 TRP 70 0.0006

TRP 70 SER 71 0.0002

SER 71 ALA 72 0.0002

ALA 72 LEU 73 0.0003

LEU 73 GLY 74 -0.0001

GLY 74 ILE 75 0.0001

ILE 75 ASP 76 -0.0060

ASP 76 ALA 77 0.0003

ALA 77 VAL 78 -0.0002

VAL 78 VAL 79 -0.0048

VAL 79 VAL 80 -0.0000

VAL 80 GLY 81 -0.0000

GLY 81 GLN 82 0.0329

GLN 82 VAL 83 0.0001

VAL 83 THR 84 0.0001

THR 84 PRO 85 0.0307

PRO 85 ASN 86 -0.0002

ASN 86 PRO 87 -0.0003

PRO 87 ASP 88 0.0141

ASP 88 GLY 89 0.0000

GLY 89 SER 90 -0.0002

SER 90 TYR 91 0.0114

TYR 91 ASN 92 -0.0005

ASN 92 VAL 93 -0.0000

VAL 93 ALA 94 0.0309

ALA 94 TYR 95 -0.0000

TYR 95 GLN 96 0.0000

GLN 96 LEU 97 0.0060

LEU 97 VAL 98 0.0003

VAL 98 ASP 99 -0.0004

ASP 99 THR 100 -0.0024

THR 100 GLY 101 0.0001

GLY 101 GLY 102 -0.0001

GLY 102 ALA 103 -0.0040

ALA 103 PRO 104 -0.0002

PRO 104 GLY 105 -0.0000

GLY 105 THR 106 -0.0164

THR 106 VAL 107 0.0000

VAL 107 LEU 108 -0.0001

LEU 108 ALA 109 0.0005

ALA 109 GLN 110 0.0003

GLN 110 ASN 111 -0.0001

ASN 111 SER 112 0.0118

SER 112 TYR 113 0.0000

TYR 113 LYS 114 0.0002

LYS 114 VAL 115 0.0546

VAL 115 ASN 116 0.0001

ASN 116 LYS 117 0.0002

LYS 117 GLN 118 0.0026

GLN 118 TRP 119 -0.0002

TRP 119 LEU 120 -0.0001

LEU 120 ARG 121 0.0661

ARG 121 TYR 122 0.0001

TYR 122 ALA 123 -0.0002

ALA 123 GLY 124 -0.0114

GLY 124 HIS 125 0.0003

HIS 125 THR 126 0.0002

THR 126 ALA 127 0.0446

ALA 127 SER 128 0.0001

SER 128 ASP 129 0.0001

ASP 129 GLU 130 0.0288

GLU 130 VAL 131 -0.0000

VAL 131 PHE 132 -0.0002

PHE 132 GLU 133 -0.0102

GLU 133 LYS 134 -0.0002

LYS 134 LEU 135 -0.0001

LEU 135 THR 136 -0.0126

THR 136 GLY 137 0.0001

GLY 137 ILE 138 -0.0002

ILE 138 LYS 139 0.1013

LYS 139 GLY 140 0.0001

GLY 140 ALA 141 0.0001

ALA 141 PHE 142 -0.0117

PHE 142 ARG 143 -0.0003

ARG 143 THR 144 -0.0001

THR 144 ARG 145 -0.0178

ARG 145 ILE 146 -0.0002

ILE 146 ALA 147 0.0001

ALA 147 TYR 148 -0.0363

TYR 148 VAL 149 0.0001

VAL 149 VAL 150 -0.0001

VAL 150 GLN 151 0.0228

GLN 151 THR 152 -0.0002

THR 152 ASN 153 -0.0001

ASN 153 GLY 154 -0.0380

GLY 154 GLY 155 -0.0002

GLY 155 GLN 156 0.0003

GLN 156 PHE 157 0.0096

PHE 157 PRO 158 -0.0000

PRO 158 TYR 159 -0.0003

TYR 159 GLU 160 0.0266

GLU 160 LEU 161 -0.0001

LEU 161 ARG 162 0.0000

ARG 162 VAL 163 -0.0165

VAL 163 SER 164 0.0000

SER 164 ASP 165 -0.0001

ASP 165 TYR 166 0.0160

TYR 166 ASP 167 -0.0000

ASP 167 GLY 168 0.0001

GLY 168 TYR 169 0.0197

TYR 169 ASN 170 -0.0001

ASN 170 GLN 171 0.0000

GLN 171 PHE 172 -0.0645

PHE 172 VAL 173 0.0000

VAL 173 VAL 174 -0.0001

VAL 174 HIS 175 -0.0210

HIS 175 ARG 176 -0.0004

ARG 176 SER 177 -0.0000

SER 177 PRO 178 0.0047

PRO 178 GLN 179 0.0001

GLN 179 PRO 180 0.0002

PRO 180 LEU 181 -0.0159

LEU 181 MSE 182 -0.0000

MSE 182 SER 183 -0.0002

SER 183 PRO 184 -0.0058

PRO 184 ALA 185 -0.0004

ALA 185 TRP 186 0.0004

TRP 186 SER 187 0.0123

SER 187 PRO 188 0.0001

PRO 188 ASP 189 0.0000

ASP 189 GLY 190 -0.0143

GLY 190 SER 191 -0.0000

SER 191 LYS 192 0.0000

LYS 192 LEU 193 -0.0031

LEU 193 ALA 194 -0.0003

ALA 194 TYR 195 -0.0002

TYR 195 VAL 196 -0.0247

VAL 196 THR 197 -0.0004

THR 197 PHE 198 -0.0000

PHE 198 GLU 199 -0.0139

GLU 199 SER 200 -0.0000

SER 200 GLY 201 -0.0000

GLY 201 ARG 202 0.0093

ARG 202 SER 203 -0.0002

SER 203 ALA 204 -0.0003

ALA 204 LEU 205 -0.0097

LEU 205 VAL 206 -0.0002

VAL 206 ILE 207 0.0001

ILE 207 GLN 208 -0.0254

GLN 208 THR 209 -0.0002

THR 209 LEU 210 -0.0002

LEU 210 ALA 211 -0.0155

ALA 211 ASN 212 -0.0002

ASN 212 GLY 213 0.0000

GLY 213 ALA 214 0.0030

ALA 214 VAL 215 -0.0002

VAL 215 ARG 216 -0.0002

ARG 216 GLN 217 -0.0136

GLN 217 VAL 218 -0.0001

VAL 218 ALA 219 0.0003

ALA 219 SER 220 0.0049

SER 220 PHE 221 0.0001

PHE 221 PRO 222 -0.0002

PRO 222 ARG 223 0.0133

ARG 223 HIS 224 -0.0000

HIS 224 ASN 225 0.0004

ASN 225 GLY 226 -0.0049

GLY 226 ALA 227 0.0000

ALA 227 PRO 228 -0.0002

PRO 228 ALA 229 0.0115

ALA 229 PHE 230 -0.0000

PHE 230 SER 231 0.0001

SER 231 PRO 232 0.0145

PRO 232 ASP 233 -0.0003

ASP 233 GLY 234 -0.0001

GLY 234 SER 235 -0.0648

SER 235 LYS 236 -0.0005

LYS 236 LEU 237 0.0003

LEU 237 ALA 238 -0.0081

ALA 238 PHE 239 0.0000

PHE 239 ALA 240 0.0001

ALA 240 LEU 241 -0.0093

LEU 241 SER 242 0.0004

SER 242 LYS 243 -0.0003

LYS 243 THR 244 0.0022

THR 244 GLY 245 0.0001

GLY 245 SER 246 -0.0002

SER 246 LEU 247 0.0065

LEU 247 ASN 248 0.0000

ASN 248 LEU 249 0.0001

LEU 249 TYR 250 0.0063

TYR 250 VAL 251 0.0001

VAL 251 MSE 252 0.0000

MSE 252 ASP 253 0.0152

ASP 253 LEU 254 0.0000

LEU 254 ALA 255 -0.0002

ALA 255 SER 256 -0.0017

SER 256 GLY 257 -0.0001

GLY 257 GLN 258 -0.0001

GLN 258 ILE 259 0.0125

ILE 259 ARG 260 0.0002

ARG 260 GLN 261 0.0001

GLN 261 VAL 262 0.0156

VAL 262 THR 263 -0.0001

THR 263 ASP 264 -0.0001

ASP 264 GLY 265 -0.0408

GLY 265 ARG 266 -0.0000

ARG 266 SER 267 -0.0001

SER 267 ASN 268 0.0074

ASN 268 ASN 269 -0.0000

ASN 269 THR 270 0.0000

THR 270 GLU 271 0.0143

GLU 271 PRO 272 0.0002

PRO 272 THR 273 -0.0002

THR 273 TRP 274 0.0006

TRP 274 PHE 275 0.0003

PHE 275 PRO 276 -0.0000

PRO 276 ASP 277 -0.0241

ASP 277 SER 278 -0.0000

SER 278 GLN 279 -0.0004

GLN 279 ASN 280 0.0081

ASN 280 LEU 281 -0.0004

LEU 281 ALA 282 0.0002

ALA 282 PHE 283 -0.0076

PHE 283 THR 284 -0.0002

THR 284 SER 285 0.0000

SER 285 ASP 286 -0.0086

ASP 286 GLN 287 0.0004

GLN 287 ALA 288 0.0001

ALA 288 GLY 289 0.0256

GLY 289 ARG 290 0.0001

ARG 290 PRO 291 0.0001

PRO 291 GLN 292 -0.0080

GLN 292 VAL 293 -0.0001

VAL 293 TYR 294 -0.0001

TYR 294 LYS 295 0.0192

LYS 295 VAL 296 -0.0000

VAL 296 ASN 297 0.0001

ASN 297 ILE 298 0.0220

ILE 298 ASN 299 0.0004

ASN 299 GLY 300 -0.0002

GLY 300 GLY 301 0.0199

GLY 301 ALA 302 -0.0001

ALA 302 PRO 303 -0.0002

PRO 303 GLN 304 0.0107

GLN 304 ARG 305 -0.0001

ARG 305 ILE 306 -0.0003

ILE 306 THR 307 0.0232

THR 307 TRP 308 -0.0004

TRP 308 GLU 309 0.0001

GLU 309 GLY 310 -0.0050

GLY 310 SER 311 -0.0003

SER 311 GLN 312 0.0003

GLN 312 ASN 313 -0.0288

ASN 313 GLN 314 -0.0001

GLN 314 ASP 315 0.0001

ASP 315 ALA 316 -0.0135

ALA 316 ASP 317 -0.0000

ASP 317 VAL 318 0.0002

VAL 318 SER 319 -0.0660

SER 319 SER 320 -0.0003

SER 320 ASP 321 0.0001

ASP 321 GLY 322 -0.0878

GLY 322 LYS 323 -0.0001

LYS 323 PHE 324 0.0003

PHE 324 MSE 325 0.0097

MSE 325 VAL 326 0.0003

VAL 326 MSE 327 -0.0000

MSE 327 VAL 328 -0.0255

VAL 328 SER 329 -0.0001

SER 329 SER 330 -0.0000

SER 330 ASN 331 -0.0318

ASN 331 GLY 332 0.0001

GLY 332 GLY 333 -0.0002

GLY 333 GLN 334 0.0308

GLN 334 GLN 335 -0.0001

GLN 335 HIS 336 0.0003

HIS 336 ILE 337 -0.0352

ILE 337 ALA 338 -0.0002

ALA 338 LYS 339 -0.0002

LYS 339 GLN 340 0.0317

GLN 340 ASP 341 0.0002

ASP 341 LEU 342 -0.0002

LEU 342 ALA 343 0.0112

ALA 343 THR 344 -0.0001

THR 344 GLY 345 0.0003

GLY 345 GLY 346 0.0220

GLY 346 VAL 347 0.0002

VAL 347 GLN 348 -0.0001

GLN 348 VAL 349 -0.0136

VAL 349 LEU 350 0.0000

LEU 350 SER 351 -0.0003

SER 351 SER 352 -0.0629

SER 352 THR 353 -0.0004

THR 353 PHE 354 -0.0000

PHE 354 LEU 355 0.0035

LEU 355 ASP 356 -0.0002

ASP 356 GLU 357 0.0004

GLU 357 THR 358 -0.0334

THR 358 PRO 359 -0.0000

PRO 359 SER 360 -0.0001

SER 360 LEU 361 -0.0551

LEU 361 ALA 362 0.0003

ALA 362 PRO 363 -0.0001

PRO 363 ASN 364 0.0194

ASN 364 GLY 365 -0.0002

GLY 365 THR 366 0.0000

THR 366 MSE 367 -0.0619

MSE 367 VAL 368 -0.0001

VAL 368 ILE 369 0.0000

ILE 369 TYR 370 -0.0142

TYR 370 SER 371 -0.0002

SER 371 SER 372 0.0001

SER 372 SER 373 -0.0138

SER 373 GLN 374 0.0001

GLN 374 GLY 375 0.0003

GLY 375 MSE 376 0.0077

MSE 376 GLY 377 -0.0001

GLY 377 SER 378 0.0002

SER 378 VAL 379 0.0331

VAL 379 LEU 380 0.0002

LEU 380 ASN 381 -0.0002

ASN 381 LEU 382 -0.0166

LEU 382 VAL 383 0.0003

VAL 383 SER 384 -0.0002

SER 384 THR 385 0.0100

THR 385 ASP 386 -0.0003

ASP 386 GLY 387 -0.0003

GLY 387 ARG 388 0.0938

ARG 388 PHE 389 -0.0004

PHE 389 LYS 390 -0.0001

LYS 390 ALA 391 -0.1528

ALA 391 ARG 392 0.0005

ARG 392 LEU 393 0.0004

LEU 393 PRO 394 -0.0191

PRO 394 ALA 395 -0.0002

ALA 395 THR 396 0.0003

THR 396 ASP 397 0.0321

ASP 397 GLY 398 0.0001

GLY 398 GLN 399 0.0003

GLN 399 VAL 400 0.0009

VAL 400 LYS 401 0.0000

LYS 401 PHE 402 -0.0000

PHE 402 PRO 403 -0.0235

PRO 403 ALA 404 -0.0005

ALA 404 TRP 405 0.0002

TRP 405 SER 406 0.0035

SER 406 PRO 407 0.0001

PRO 407 TYR 408 0.0002

TYR 408 LEU 409 -0.0402

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: April 25th, 2023.

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

*** ***

CA strain for EXAMPLE4

--- normal mode 7 ---

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

* *