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 260712001235660292

--- normal mode 10 ---

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
THR 109 GLU 110 -0.0002

GLU 110 ARG 111 -0.0695

ARG 111 ALA 112 -0.0003

ALA 112 THR 113 -0.0844

THR 113 ARG 114 0.0002

ARG 114 HIS 115 -0.0462

HIS 115 ARG 116 0.0002

ARG 116 TYR 117 -0.1923

TYR 117 ASN 118 -0.0003

ASN 118 ALA 119 -0.0661

ALA 119 VAL 120 -0.0004

VAL 120 THR 121 0.0198

THR 121 GLY 122 -0.0000

GLY 122 GLU 123 0.0142

GLU 123 TRP 124 0.0002

TRP 124 LEU 125 -0.0511

LEU 125 ASP 126 0.0000

ASP 126 ASP 127 -0.0335

ASP 127 GLU 128 0.0000

GLU 128 VAL 129 -0.1025

VAL 129 LEU 130 -0.0003

LEU 130 ILE 131 0.0494

ILE 131 LYS 132 -0.0001

LYS 132 MET 133 0.2127

MET 133 ALA 134 0.0002

ALA 134 SER 135 0.0446

SER 135 GLN 136 -0.0002

GLN 136 PRO 137 0.0058

PRO 137 PHE 138 -0.0003

PHE 138 GLY 139 -0.0115

GLY 139 ARG 140 0.0004

ARG 140 GLY 141 0.0092

GLY 141 ALA 142 0.0000

ALA 142 MET 143 0.0098

MET 143 ARG 144 0.0000

ARG 144 GLU 145 0.0124

GLU 145 CYS 146 0.0001

CYS 146 PHE 147 0.0048

PHE 147 ARG 148 -0.0003

ARG 148 THR 149 0.0689

THR 149 LYS 150 -0.0003

LYS 150 LYS 151 0.0771

LYS 151 LEU 152 -0.0001

LEU 152 SER 153 -0.1634

SER 153 ASN 154 -0.0003

ASN 154 PHE 155 0.1413

PHE 155 LEU 156 0.0003

LEU 156 HIS 157 -0.0807

HIS 157 ALA 158 0.0008

ALA 158 GLN 159 -0.0566

GLN 159 GLN 160 -0.0002

GLN 160 TRP 161 0.2418

TRP 161 LYS 162 0.0002

LYS 162 GLY 163 -0.1609

GLY 163 ALA 164 0.0003

ALA 164 SER 165 -0.1504

SER 165 ASN 166 0.0004

ASN 166 TYR 167 -0.0278

TYR 167 VAL 168 0.0005

VAL 168 ALA 169 0.0106

ALA 169 LYS 170 -0.0002

LYS 170 ARG 171 -0.0036

ARG 171 TYR 172 -0.0002

TYR 172 ILE 173 0.0218

ILE 173 GLU 174 -0.0005

GLU 174 PRO 175 -0.0122

PRO 175 VAL 176 0.0001

VAL 176 ASP 177 -0.0056

ASP 177 ARG 178 0.0000

ARG 178 ASP 179 0.0027

ASP 179 VAL 180 0.0002

VAL 180 TYR 181 -0.0402

TYR 181 PHE 182 0.0001

PHE 182 GLU 183 -0.1955

GLU 183 ASP 184 -0.0003

ASP 184 VAL 185 -0.0474

VAL 185 ARG 186 0.0003

ARG 186 LEU 187 -0.1200

LEU 187 GLN 188 -0.0003

GLN 188 MET 189 -0.0120

MET 189 GLU 190 0.0000

GLU 190 ALA 191 -0.0140

ALA 191 LYS 192 0.0002

LYS 192 LEU 193 -0.0067

LEU 193 TRP 194 0.0001

TRP 194 GLY 195 -0.0083

GLY 195 GLU 196 -0.0003

GLU 196 GLU 197 0.0024

GLU 197 TYR 198 0.0000

TYR 198 ASN 199 -0.0090

ASN 199 ARG 200 -0.0002

ARG 200 HIS 201 0.0263

HIS 201 LYS 202 -0.0002

LYS 202 PRO 203 -0.0077

PRO 203 PRO 204 -0.0003

PRO 204 LYS 205 0.0153

LYS 205 GLN 206 -0.0001

GLN 206 VAL 207 0.0436

VAL 207 ASP 208 0.0000

ASP 208 ILE 209 0.0351

ILE 209 MET 210 -0.0003

MET 210 GLN 211 0.0473

GLN 211 MET 212 0.0001

MET 212 CYS 213 -0.0433

CYS 213 ILE 214 -0.0002

ILE 214 ILE 215 -0.0724

ILE 215 GLU 216 -0.0001

GLU 216 LEU 217 -0.0306

LEU 217 LYS 218 0.0000

LYS 218 ASP 219 -0.0304

ASP 219 ARG 220 0.0001

ARG 220 PRO 221 0.0178

PRO 221 GLY 222 0.0001

GLY 222 LYS 223 -0.0085

LYS 223 PRO 224 0.0000

PRO 224 LEU 225 -0.0159

LEU 225 PHE 226 -0.0000

PHE 226 HIS 227 0.0104

HIS 227 LEU 228 0.0002

LEU 228 GLU 229 0.0393

GLU 229 HIS 230 -0.0004

HIS 230 TYR 231 0.0237

TYR 231 ILE 232 0.0000

ILE 232 GLU 233 -0.0072

GLU 233 GLY 234 0.0001

GLY 234 LYS 235 0.0313

LYS 235 TYR 236 -0.0000

TYR 236 ILE 237 -0.0428

ILE 237 LYS 238 0.0003

LYS 238 TYR 239 -0.0234

TYR 239 ASN 240 -0.0001

ASN 240 SER 241 0.0395

SER 241 ASN 242 -0.0001

ASN 242 SER 243 -0.0774

SER 243 GLY 244 -0.0000

GLY 244 PHE 245 -0.0026

PHE 245 VAL 246 0.0002

VAL 246 ARG 247 0.0247

ARG 247 ASP 248 -0.0000

ASP 248 ASP 249 0.0131

ASP 249 ASN 250 -0.0001

ASN 250 ILE 251 -0.0043

ILE 251 ARG 252 0.0001

ARG 252 LEU 253 -0.0084

LEU 253 THR 254 0.0001

THR 254 PRO 255 -0.0056

PRO 255 GLN 256 0.0003

GLN 256 ALA 257 -0.0054

ALA 257 PHE 258 0.0002

PHE 258 SER 259 -0.0156

SER 259 HIS 260 -0.0002

HIS 260 PHE 261 0.0293

PHE 261 THR 262 0.0001

THR 262 PHE 263 -0.0209

PHE 263 GLU 264 0.0004

GLU 264 ARG 265 0.0356

ARG 265 SER 266 -0.0000

SER 266 GLY 267 -0.0299

GLY 267 HIS 268 0.0003

HIS 268 GLN 269 -0.0185

GLN 269 LEU 270 0.0001

LEU 270 ILE 271 -0.0003

ILE 271 VAL 272 0.0000

VAL 272 VAL 273 -0.0026

VAL 273 ASP 274 0.0004

ASP 274 ILE 275 -0.0046

ILE 275 GLN 276 0.0000

GLN 276 GLY 277 -0.0240

GLY 277 VAL 278 -0.0001

VAL 278 GLY 279 -0.0192

GLY 279 ASP 280 0.0002

ASP 280 LEU 281 0.0411

LEU 281 TYR 282 -0.0001

TYR 282 THR 283 0.0141

THR 283 ASP 284 0.0002

ASP 284 PRO 285 -0.0835

PRO 285 GLN 286 0.0002

GLN 286 ILE 287 -0.0178

ILE 287 HIS 288 -0.0003

HIS 288 THR 289 0.0340

THR 289 GLU 290 -0.0003

GLU 290 THR 291 -0.0549

THR 291 GLY 292 -0.0002

GLY 292 THR 293 -0.0342

THR 293 ASP 294 0.0000

ASP 294 PHE 295 -0.0208

PHE 295 GLY 296 -0.0003

GLY 296 ASP 297 0.0198

ASP 297 GLY 298 -0.0003

GLY 298 ASN 299 0.0374

ASN 299 LEU 300 0.0004

LEU 300 GLY 301 -0.0094

GLY 301 VAL 302 -0.0002

VAL 302 ARG 303 -0.0133

ARG 303 GLY 304 -0.0000

GLY 304 MET 305 0.0231

MET 305 ALA 306 -0.0001

ALA 306 LEU 307 -0.0010

LEU 307 PHE 308 -0.0003

PHE 308 PHE 309 -0.0494

PHE 309 TYR 310 0.0003

TYR 310 SER 311 0.0071

SER 311 HIS 312 -0.0002

HIS 312 ALA 313 0.0247

ALA 313 CYS 314 0.0001

CYS 314 ASN 315 0.0318

ASN 315 ARG 316 0.0000

ARG 316 ILE 317 0.0016

ILE 317 CYS 318 -0.0002

CYS 318 GLU 319 -0.0031

GLU 319 SER 320 0.0003

SER 320 MET 321 -0.0011

MET 321 GLY 322 0.0001

GLY 322 LEU 323 0.0308

LEU 323 ALA 324 0.0003

ALA 324 PRO 325 0.0678

PRO 325 PHE 326 0.0000

PHE 326 ASP 327 0.0247

ASP 327 LEU 328 0.0000

LEU 328 SER 329 0.0221

SER 329 PRO 330 0.0001

PRO 330 ARG 331 0.0301

ARG 331 GLU 332 0.0001

GLU 332 ARG 333 0.0194

ARG 333 ASP 334 0.0003

ASP 334 ALA 335 -0.0347

ALA 335 VAL 336 0.0000

VAL 336 ASN 337 -0.0102

ASN 337 GLN 338 -0.0003

GLN 338 ASN 339 -0.0110

ASN 339 THR 340 -0.0001

THR 340 LYS 341 -0.0058

LYS 341 LEU 342 0.0002

LEU 342 LEU 343 -0.0152

LEU 343 GLN 344 0.0000

GLN 344 SER 345 -0.0008

SER 345 ALA 346 -0.0001

ALA 346 LYS 347 0.0188

LYS 347 ILE 349 -0.0187

ILE 349 LEU 350 -0.0000

LEU 350 ARG 351 0.0087

ARG 351 GLY 352 0.0001

GLY 352 THR 353 -0.0041

THR 353 GLU 354 0.0003

GLU 354 GLU 355 -0.0220

GLU 355 LYS 356 0.0002

LYS 356 CYS 357 -0.0222

CYS 357 HIS 495 -0.0138

HIS 495 LEU 496 -0.0001

LEU 496 PRO 497 0.0178

PRO 497 ARG 498 0.0003

ARG 498 ALA 499 0.0382

ALA 499 SER 500 0.0002

SER 500 ALA 501 0.0182

ALA 501 VAL 502 -0.0002

VAL 502 ALA 503 -0.0155

ALA 503 LEU 504 -0.0001

LEU 504 GLU 505 -0.0125

GLU 505 VAL 506 0.0003

VAL 506 GLN 507 -0.0011

GLN 507 ARG 508 -0.0000

ARG 508 LEU 509 0.0110

LEU 509 ASN 510 0.0003

ASN 510 ALA 511 0.0309

ALA 511 LEU 512 0.0003

LEU 512 ASP 513 -0.1763

ASP 513 LEU 514 0.0002

LEU 514 GLU 515 -0.0166

GLU 515 LYS 517 -0.0240

LYS 517 ILE 518 0.0000

ILE 518 GLY 519 -0.0157

GLY 519 LYS 520 -0.0003

LYS 520 SER 521 -0.0720

SER 521 ILE 522 -0.0001

ILE 522 LEU 523 -0.0305

LEU 523 GLY 524 -0.0000

GLY 524 LYS 525 -0.0127

LYS 525 VAL 526 -0.0001

VAL 526 HIS 527 -0.0641

HIS 527 LEU 528 0.0001

LEU 528 ALA 529 -0.0301

ALA 529 MET 530 0.0001

MET 530 VAL 531 -0.0304

VAL 531 ARG 532 -0.0004

ARG 532 TYR 533 0.0180

TYR 533 HIS 534 -0.0001

HIS 534 GLU 535 0.0260

GLU 535 GLY 536 0.0001

GLY 536 GLY 537 -0.0465

GLY 537 ARG 538 -0.0000

ARG 538 PHE 539 -0.0171

PHE 539 CYS 540 -0.0000

CYS 540 GLU 541 0.0951

GLU 541 LYS 542 -0.0001

LYS 542 GLU 544 0.0509

GLU 544 GLU 545 0.0001

GLU 545 TRP 546 -0.0148

TRP 546 ASP 547 -0.0003

ASP 547 GLN 548 0.0161

GLN 548 GLU 549 0.0002

GLU 549 SER 550 -0.0161

SER 550 ALA 551 0.0001

ALA 551 VAL 552 -0.0160

VAL 552 PHE 553 -0.0002

PHE 553 HIS 554 -0.0200

HIS 554 LEU 555 0.0000

LEU 555 GLU 556 -0.0289

GLU 556 HIS 557 -0.0001

HIS 557 ALA 558 -0.0082

ALA 558 ALA 559 -0.0002

ALA 559 ASN 560 -0.0051

ASN 560 LEU 561 0.0002

LEU 561 GLY 562 0.0157

GLY 562 GLU 563 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).
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 260712001235660292

--- normal mode 10 ---

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

* *