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

* 2htv_monomer *

CA strain for 2404132040384056527

--- normal mode 1 ---

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
VAL 82 ILE 83 0.0001

ILE 83 HIS 84 0.0003

HIS 84 TYR 85 -0.0002

TYR 85 SER 86 0.0001

SER 86 SER 87 -0.0002

SER 87 GLY 88 0.0003

GLY 88 LYS 89 0.0002

LYS 89 ASP 90 -0.0002

ASP 90 LEU 91 -0.0002

LEU 91 CYS 92 0.0003

CYS 92 PRO 93 -0.0005

PRO 93 VAL 94 0.0001

VAL 94 LYS 95 -0.0001

LYS 95 GLY 96 0.0001

GLY 96 TRP 97 0.0004

TRP 97 ALA 98 -0.0002

ALA 98 PRO 99 0.0001

PRO 99 LEU 100 -0.0002

LEU 100 SER 101 -0.0000

SER 101 LYS 102 0.0001

LYS 102 ASP 103 -0.0001

ASP 103 ASN 104 -0.0002

ASN 104 GLY 105 -0.0002

GLY 105 ILE 106 -0.0000

ILE 106 ARG 107 -0.0003

ARG 107 ILE 108 0.0004

ILE 108 GLY 109 0.0005

GLY 109 SER 110 -0.0001

SER 110 ARG 111 -0.0001

ARG 111 GLY 112 -0.0000

GLY 112 GLU 113 0.0001

GLU 113 VAL 114 0.0002

VAL 114 PHE 115 -0.0001

PHE 115 VAL 116 -0.0001

VAL 116 ILE 117 -0.0004

ILE 117 ARG 118 0.0002

ARG 118 GLU 119 -0.0001

GLU 119 PRO 120 0.0001

PRO 120 PHE 121 -0.0002

PHE 121 ILE 122 -0.0000

ILE 122 SER 123 0.0001

SER 123 CYS 124 0.0004

CYS 124 SER 125 -0.0007

SER 125 ILE 126 -0.0000

ILE 126 ASN 127 0.0001

ASN 127 GLU 128 -0.0000

GLU 128 CYS 129 -0.0003

CYS 129 ARG 130 -0.0002

ARG 130 THR 131 0.0002

THR 131 PHE 132 -0.0000

PHE 132 PHE 133 0.0002

PHE 133 LEU 134 0.0001

LEU 134 THR 135 -0.0004

THR 135 GLN 136 0.0002

GLN 136 GLY 137 0.0001

GLY 137 ALA 138 0.0002

ALA 138 LEU 139 -0.0001

LEU 139 LEU 140 0.0001

LEU 140 ASN 141 0.0002

ASN 141 ASP 142 -0.0000

ASP 142 LYS 143 0.0002

LYS 143 HIS 144 0.0004

HIS 144 SER 145 -0.0000

SER 145 ASN 146 0.0003

ASN 146 GLY 147 -0.0006

GLY 147 THR 148 -0.0002

THR 148 VAL 149 0.0003

VAL 149 LYS 150 -0.0004

LYS 150 ASP 151 0.0001

ASP 151 ARG 152 -0.0000

ARG 152 SER 153 -0.0002

SER 153 PRO 154 0.0001

PRO 154 PHE 155 -0.0003

PHE 155 ARG 156 0.0004

ARG 156 THR 157 -0.0000

THR 157 LEU 158 0.0004

LEU 158 MET 159 0.0000

MET 159 SER 160 -0.0001

SER 160 CYS 161 0.0001

CYS 161 PRO 162 -0.0001

PRO 162 ILE 163 0.0002

ILE 163 GLY 164 0.0005

GLY 164 VAL 165 -0.0002

VAL 165 ALA 166 0.0002

ALA 166 PRO 167 -0.0003

PRO 167 SER 168 0.0002

SER 168 PRO 169 0.0002

PRO 169 SER 169 0.0002

SER 169 ASN 170 0.0000

ASN 170 SER 171 0.0001

SER 171 ARG 172 0.0000

ARG 172 PHE 173 -0.0002

PHE 173 GLU 174 0.0003

GLU 174 SER 175 -0.0002

SER 175 VAL 176 -0.0001

VAL 176 ALA 177 0.0003

ALA 177 TRP 178 0.0000

TRP 178 SER 179 -0.0004

SER 179 ALA 180 0.0001

ALA 180 THR 181 -0.0001

THR 181 ALA 182 0.0001

ALA 182 CYS 183 0.0001

CYS 183 SER 184 -0.0001

SER 184 ASP 185 0.0001

ASP 185 GLY 186 -0.0002

GLY 186 PRO 187 0.0001

PRO 187 GLY 188 -0.0006

GLY 188 TRP 189 -0.0000

TRP 189 LEU 190 0.0001

LEU 190 THR 191 -0.0002

THR 191 ILE 192 0.0002

ILE 192 GLY 193 -0.0004

GLY 193 ILE 194 -0.0002

ILE 194 THR 195 -0.0000

THR 195 GLY 196 0.0001

GLY 196 PRO 197 -0.0001

PRO 197 ASP 198 0.0002

ASP 198 ALA 199 0.0000

ALA 199 THR 200 -0.0004

THR 200 ALA 201 -0.0001

ALA 201 VAL 202 0.0003

VAL 202 ALA 203 -0.0002

ALA 203 VAL 204 0.0002

VAL 204 LEU 205 0.0003

LEU 205 LYS 206 0.0002

LYS 206 TYR 207 0.0000

TYR 207 ASN 208 0.0001

ASN 208 GLY 209 0.0003

GLY 209 ILE 210 -0.0003

ILE 210 ILE 211 0.0003

ILE 211 THR 212 -0.0000

THR 212 ASP 213 0.0002

ASP 213 THR 214 -0.0000

THR 214 LEU 215 0.0002

LEU 215 LYS 216 0.0002

LYS 216 SER 217 -0.0002

SER 217 TRP 218 -0.0005

TRP 218 LYS 219 -0.0001

LYS 219 GLY 220 0.0000

GLY 220 ASN 221 -0.0002

ASN 221 ILE 222 -0.0001

ILE 222 MET 223 0.0000

MET 223 ARG 224 0.0001

ARG 224 THR 225 -0.0003

THR 225 GLN 226 0.0005

GLN 226 GLU 227 -0.0001

GLU 227 SER 228 -0.0004

SER 228 GLU 229 -0.0002

GLU 229 CYS 230 0.0005

CYS 230 VAL 231 -0.0002

VAL 231 CYS 232 0.0001

CYS 232 GLN 233 -0.0001

GLN 233 ASP 234 -0.0003

ASP 234 GLU 235 0.0001

GLU 235 PHE 236 -0.0003

PHE 236 CYS 237 -0.0001

CYS 237 TYR 238 0.0001

TYR 238 THR 239 -0.0001

THR 239 LEU 240 -0.0000

LEU 240 ILE 241 -0.0001

ILE 241 THR 242 -0.0001

THR 242 ASP 243 0.0003

ASP 243 GLY 244 -0.0004

GLY 244 PRO 245 0.0003

PRO 245 SER 246 -0.0002

SER 246 ASP 247 -0.0000

ASP 247 ALA 248 -0.0000

ALA 248 GLN 249 0.0002

GLN 249 ALA 250 -0.0001

ALA 250 PHE 251 -0.0000

PHE 251 TYR 252 -0.0001

TYR 252 LYS 253 0.0003

LYS 253 ILE 254 -0.0005

ILE 254 LEU 255 0.0002

LEU 255 LYS 256 -0.0004

LYS 256 ILE 257 0.0003

ILE 257 LYS 258 0.0002

LYS 258 LYS 259 -0.0000

LYS 259 GLY 260 -0.0001

GLY 260 LYS 261 0.0004

LYS 261 ILE 262 -0.0003

ILE 262 VAL 263 0.0001

VAL 263 SER 264 -0.0000

SER 264 VAL 265 0.0000

VAL 265 LYS 266 0.0002

LYS 266 ASP 267 -0.0001

ASP 267 VAL 268 -0.0000

VAL 268 ASP 269 0.0000

ASP 269 ALA 270 0.0000

ALA 270 PRO 271 0.0000

PRO 271 GLY 272 -0.0001

GLY 272 PHE 273 -0.0003

PHE 273 HIS 274 0.0001

HIS 274 PHE 275 0.0005

PHE 275 GLU 276 -0.0001

GLU 276 GLU 277 -0.0000

GLU 277 CYS 278 0.0000

CYS 278 SER 279 -0.0001

SER 279 CYS 280 0.0003

CYS 280 TYR 281 -0.0002

TYR 281 PRO 282 -0.0004

PRO 282 SER 283 -0.0000

SER 283 GLY 284 -0.0003

GLY 284 GLU 285 -0.0002

GLU 285 ASN 286 0.0003

ASN 286 VAL 287 -0.0001

VAL 287 GLU 288 0.0002

GLU 288 CYS 289 -0.0001

CYS 289 VAL 290 -0.0002

VAL 290 CYS 291 -0.0002

CYS 291 ARG 292 0.0004

ARG 292 ASP 293 0.0001

ASP 293 ASN 294 -0.0001

ASN 294 TRP 295 -0.0001

TRP 295 ARG 296 0.0001

ARG 296 GLY 297 -0.0000

GLY 297 SER 298 0.0003

SER 298 ASN 299 -0.0002

ASN 299 ARG 300 -0.0002

ARG 300 PRO 301 0.0001

PRO 301 TRP 302 -0.0002

TRP 302 ILE 303 0.0001

ILE 303 ARG 304 -0.0002

ARG 304 PHE 305 0.0001

PHE 305 ASN 306 -0.0000

ASN 306 SER 308 -0.0001

SER 308 ASP 309 0.0003

ASP 309 LEU 310 0.0000

LEU 310 ASP 311 -0.0000

ASP 311 TYR 312 -0.0000

TYR 312 GLN 313 -0.0002

GLN 313 ILE 314 -0.0002

ILE 314 GLY 315 0.0003

GLY 315 TYR 316 0.0001

TYR 316 VAL 317 -0.0004

VAL 317 CYS 318 0.0003

CYS 318 SER 319 0.0001

SER 319 GLY 320 -0.0004

GLY 320 VAL 321 -0.0000

VAL 321 PHE 322 -0.0004

PHE 322 GLY 323 -0.0001

GLY 323 ASP 324 0.0000

ASP 324 ASN 325 0.0001

ASN 325 PRO 326 0.0001

PRO 326 ARG 327 0.0005

ARG 327 PRO 328 -0.0002

PRO 328 MET 329 0.0003

MET 329 ASP 330 0.0000

ASP 330 SER 332 -0.0005

SER 332 THR 333 0.0002

THR 333 GLY 335 0.0001

GLY 335 SER 336 0.0001

SER 336 CYS 337 -0.0000

CYS 337 ASN 338 -0.0001

ASN 338 SER 339 0.0000

SER 339 PRO 340 0.0002

PRO 340 ILE 341 -0.0000

ILE 341 ASN 342 0.0002

ASN 342 ASN 342 0.0001

ASN 342 GLY 343 0.0002

GLY 343 LYS 344 -0.0002

LYS 344 GLY 345 -0.0002

GLY 345 ARG 346 -0.0000

ARG 346 TYR 347 -0.0000

TYR 347 GLY 348 0.0001

GLY 348 VAL 349 0.0001

VAL 349 LYS 350 0.0001

LYS 350 GLY 351 -0.0002

GLY 351 PHE 352 0.0002

PHE 352 SER 353 -0.0001

SER 353 PHE 354 -0.0001

PHE 354 ARG 355 0.0001

ARG 355 TYR 356 0.0001

TYR 356 GLY 357 -0.0000

GLY 357 ASP 358 0.0002

ASP 358 GLY 359 0.0001

GLY 359 VAL 360 0.0001

VAL 360 TRP 361 0.0001

TRP 361 ILE 362 -0.0001

ILE 362 GLY 363 0.0004

GLY 363 ARG 364 0.0001

ARG 364 THR 365 -0.0002

THR 365 LYS 366 0.0000

LYS 366 SER 367 -0.0002

SER 367 LEU 368 -0.0001

LEU 368 GLU 369 0.0002

GLU 369 SER 370 -0.0001

SER 370 ARG 371 0.0001

ARG 371 SER 372 0.0002

SER 372 GLY 373 -0.0002

GLY 373 PHE 374 0.0003

PHE 374 GLU 375 -0.0001

GLU 375 MET 376 0.0002

MET 376 VAL 377 -0.0003

VAL 377 TRP 378 0.0002

TRP 378 ASP 379 -0.0002

ASP 379 ALA 380 -0.0001

ALA 380 ASN 381 -0.0001

ASN 381 GLY 382 0.0002

GLY 382 TRP 383 -0.0002

TRP 383 VAL 384 -0.0002

VAL 384 SER 385 0.0001

SER 385 THR 386 -0.0000

THR 386 ASP 387 -0.0001

ASP 387 LYS 388 0.0000

LYS 388 ASP 389 -0.0001

ASP 389 SER 390 -0.0002

SER 390 ASN 391 -0.0000

ASN 391 GLY 392 -0.0002

GLY 392 VAL 394 0.0003

VAL 394 GLN 395 -0.0002

GLN 395 ASP 396 -0.0002

ASP 396 ILE 397 -0.0002

ILE 397 ILE 398 0.0000

ILE 398 ASP 399 0.0002

ASP 399 ASN 400 -0.0003

ASN 400 ASP 401 -0.0002

ASP 401 ASN 402 0.0001

ASN 402 TRP 403 -0.0000

TRP 403 SER 404 -0.0002

SER 404 GLY 405 0.0000

GLY 405 TYR 406 -0.0002

TYR 406 SER 407 0.0002

SER 407 GLY 408 -0.0002

GLY 408 SER 409 0.0004

SER 409 PHE 410 0.0002

PHE 410 SER 411 -0.0005

SER 411 ILE 412 0.0003

ILE 412 ARG 412 -0.0002

ARG 412 GLY 412 -0.0001

GLY 412 GLU 412 0.0003

GLU 412 THR 412 0.0003

THR 412 THR 413 0.0002

THR 413 GLY 414 -0.0002

GLY 414 ARG 415 0.0001

ARG 415 ASN 416 0.0002

ASN 416 CYS 417 0.0002

CYS 417 THR 418 -0.0003

THR 418 VAL 419 -0.0000

VAL 419 PRO 420 0.0002

PRO 420 CYS 421 0.0001

CYS 421 PHE 422 0.0001

PHE 422 TRP 423 -0.0003

TRP 423 VAL 424 -0.0001

VAL 424 GLU 425 -0.0002

GLU 425 MET 426 0.0003

MET 426 ILE 427 -0.0004

ILE 427 ARG 428 0.0003

ARG 428 GLY 429 -0.0003

GLY 429 GLN 430 -0.0003

GLN 430 PRO 431 0.0004

PRO 431 LYS 432 -0.0002

LYS 432 GLU 433 0.0003

GLU 433 LYS 435 0.0002

LYS 435 THR 436 0.0000

THR 436 ILE 437 0.0001

ILE 437 TRP 438 -0.0003

TRP 438 THR 439 0.0000

THR 439 SER 440 0.0001

SER 440 GLY 441 -0.0001

GLY 441 SER 442 0.0002

SER 442 SER 443 -0.0003

SER 443 ILE 444 0.0002

ILE 444 ALA 445 -0.0000

ALA 445 PHE 446 -0.0001

PHE 446 CYS 447 0.0002

CYS 447 GLY 448 -0.0003

GLY 448 VAL 449 -0.0001

VAL 449 ASN 450 -0.0004

ASN 450 SER 451 -0.0001

SER 451 ASP 452 -0.0001

ASP 452 THR 453 0.0002

THR 453 THR 454 -0.0000

THR 454 GLY 455 -0.0001

GLY 455 TRP 456 0.0002

TRP 456 SER 457 0.0000

SER 457 TRP 458 -0.0001

TRP 458 PRO 459 -0.0002

PRO 459 ASP 460 0.0003

ASP 460 GLY 461 0.0001

GLY 461 ALA 462 0.0002

ALA 462 LEU 463 -0.0002

LEU 463 LEU 464 -0.0001

LEU 464 PRO 465 0.0001

PRO 465 PHE 466 0.0001

PHE 466 ASP 467 -0.0001

ASP 467 ILE 468 -0.0003

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.

*** 2htv_monomer ***

CA strain for 2404132040384056527

--- normal mode 1 ---

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

* 2htv_monomer *