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

* CHAPERONE 1SVT *

CA strain for 2404010833281775939

--- normal mode 22 ---

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
ALA 2 ALA 3 -0.0004

ALA 3 LYS 4 0.0002

LYS 4 ASP 5 -0.1597

ASP 5 VAL 6 0.0001

VAL 6 LYS 7 -0.0003

LYS 7 PHE 8 -0.0771

PHE 8 GLY 9 -0.0000

GLY 9 ASN 10 -0.0001

ASN 10 ASP 11 -0.0287

ASP 11 ALA 12 0.0001

ALA 12 ARG 13 -0.0002

ARG 13 VAL 14 -0.0841

VAL 14 LYS 15 -0.0002

LYS 15 MET 16 0.0002

MET 16 LEU 17 0.0539

LEU 17 ARG 18 -0.0003

ARG 18 GLY 19 0.0003

GLY 19 VAL 20 0.0263

VAL 20 ASN 21 0.0003

ASN 21 VAL 22 0.0003

VAL 22 LEU 23 0.0778

LEU 23 ALA 24 0.0002

ALA 24 ASP 25 -0.0006

ASP 25 ALA 26 0.0071

ALA 26 VAL 27 0.0005

VAL 27 LYS 28 -0.0004

LYS 28 VAL 29 0.0045

VAL 29 THR 30 -0.0001

THR 30 LEU 31 -0.0001

LEU 31 GLY 32 0.0210

GLY 32 PRO 33 0.0001

PRO 33 LYS 34 0.0002

LYS 34 GLY 35 0.2739

GLY 35 ARG 36 0.0000

ARG 36 ASN 37 -0.0002

ASN 37 VAL 38 -0.0178

VAL 38 VAL 39 0.0003

VAL 39 LEU 40 -0.0001

LEU 40 ASP 41 -0.3097

ASP 41 LYS 42 0.0004

LYS 42 SER 43 -0.0001

SER 43 PHE 44 -0.1037

PHE 44 GLY 45 0.0001

GLY 45 ALA 46 -0.0000

ALA 46 PRO 47 0.0073

PRO 47 THR 48 -0.0001

THR 48 ILE 49 0.0001

ILE 49 THR 50 -0.0199

THR 50 LYS 51 0.0003

LYS 51 ASP 52 -0.0002

ASP 52 GLY 53 0.0455

GLY 53 VAL 54 -0.0001

VAL 54 SER 55 0.0004

SER 55 VAL 56 0.0647

VAL 56 ALA 57 -0.0000

ALA 57 ARG 58 -0.0001

ARG 58 GLU 59 -0.1813

GLU 59 ILE 60 -0.0002

ILE 60 GLU 61 -0.0000

GLU 61 LEU 62 0.0438

LEU 62 GLU 63 -0.0000

GLU 63 ASP 64 0.0003

ASP 64 LYS 65 -0.0429

LYS 65 PHE 66 0.0001

PHE 66 GLU 67 -0.0004

GLU 67 ASN 68 -0.0447

ASN 68 MET 69 0.0001

MET 69 GLY 70 -0.0002

GLY 70 ALA 71 0.0074

ALA 71 GLN 72 -0.0001

GLN 72 MET 73 0.0002

MET 73 VAL 74 0.0297

VAL 74 LYS 75 0.0004

LYS 75 GLU 76 0.0000

GLU 76 VAL 77 -0.0077

VAL 77 ALA 78 0.0000

ALA 78 SER 79 -0.0001

SER 79 LYS 80 -0.0669

LYS 80 ALA 81 0.0001

ALA 81 ASN 82 -0.0001

ASN 82 ASP 83 0.0011

ASP 83 ALA 84 0.0001

ALA 84 ALA 85 0.0003

ALA 85 GLY 86 -0.0361

GLY 86 ASP 87 0.0004

ASP 87 GLY 88 -0.0001

GLY 88 THR 89 0.0327

THR 89 THR 90 0.0003

THR 90 THR 91 -0.0000

THR 91 ALA 92 0.0188

ALA 92 THR 93 0.0002

THR 93 VAL 94 -0.0003

VAL 94 LEU 95 -0.0348

LEU 95 ALA 96 0.0000

ALA 96 GLN 97 0.0000

GLN 97 ALA 98 -0.0942

ALA 98 ILE 99 -0.0003

ILE 99 ILE 100 -0.0004

ILE 100 THR 101 0.0318

THR 101 GLU 102 -0.0000

GLU 102 GLY 103 0.0002

GLY 103 LEU 104 0.0096

LEU 104 LYS 105 -0.0004

LYS 105 ALA 106 -0.0002

ALA 106 VAL 107 0.0826

VAL 107 ALA 108 -0.0000

ALA 108 ALA 109 0.0003

ALA 109 GLY 110 -0.0547

GLY 110 MET 111 -0.0002

MET 111 ASN 112 -0.0001

ASN 112 PRO 113 0.0712

PRO 113 MET 114 -0.0003

MET 114 ASP 115 -0.0002

ASP 115 LEU 116 -0.0186

LEU 116 LYS 117 -0.0000

LYS 117 ARG 118 -0.0001

ARG 118 GLY 119 -0.1234

GLY 119 ILE 120 -0.0001

ILE 120 ASP 121 -0.0002

ASP 121 LYS 122 -0.1018

LYS 122 ALA 123 -0.0002

ALA 123 VAL 124 0.0001

VAL 124 THR 125 -0.0548

THR 125 ALA 126 -0.0003

ALA 126 ALA 127 0.0001

ALA 127 VAL 128 0.0206

VAL 128 GLU 129 -0.0002

GLU 129 GLU 130 -0.0001

GLU 130 LEU 131 0.0096

LEU 131 LYS 132 -0.0002

LYS 132 ALA 133 0.0002

ALA 133 LEU 134 0.0429

LEU 134 SER 135 -0.0002

SER 135 VAL 136 0.0001

VAL 136 PRO 137 -0.0659

PRO 137 CYS 138 0.0002

CYS 138 SER 139 -0.0003

SER 139 ASP 140 0.0007

ASP 140 SER 141 -0.0001

SER 141 LYS 142 0.0000

LYS 142 ALA 143 0.0155

ALA 143 ILE 144 0.0001

ILE 144 ALA 145 0.0001

ALA 145 GLN 146 -0.0221

GLN 146 VAL 147 -0.0001

VAL 147 GLY 148 0.0002

GLY 148 THR 149 0.0066

THR 149 ILE 150 -0.0000

ILE 150 SER 151 0.0001

SER 151 ALA 152 0.0130

ALA 152 ASN 153 -0.0003

ASN 153 SER 154 0.0000

SER 154 ASP 155 0.0254

ASP 155 GLU 156 0.0001

GLU 156 THR 157 0.0002

THR 157 VAL 158 -0.0063

VAL 158 GLY 159 0.0001

GLY 159 LYS 160 0.0001

LYS 160 LEU 161 -0.0563

LEU 161 ILE 162 0.0001

ILE 162 ALA 163 0.0001

ALA 163 GLU 164 -0.0421

GLU 164 ALA 165 -0.0001

ALA 165 MET 166 0.0003

MET 166 ASP 167 -0.0449

ASP 167 LYS 168 0.0001

LYS 168 VAL 169 0.0001

VAL 169 GLY 170 -0.0180

GLY 170 LYS 171 -0.0000

LYS 171 GLU 172 0.0001

GLU 172 GLY 173 0.1111

GLY 173 VAL 174 0.0003

VAL 174 ILE 175 -0.0003

ILE 175 THR 176 -0.0086

THR 176 VAL 177 0.0003

VAL 177 GLU 178 -0.0004

GLU 178 ASP 179 -0.1152

ASP 179 GLY 180 0.0004

GLY 180 THR 181 0.0001

THR 181 GLY 182 0.0232

GLY 182 LEU 183 0.0002

LEU 183 GLN 184 0.0000

GLN 184 ASP 185 0.0982

ASP 185 GLU 186 -0.0001

GLU 186 LEU 187 0.0001

LEU 187 ASP 188 0.2185

ASP 188 VAL 189 0.0000

VAL 189 VAL 190 -0.0001

VAL 190 GLU 191 -0.0218

GLU 191 GLY 192 0.0000

GLY 192 MET 193 0.0004

MET 193 GLN 194 0.1186

GLN 194 PHE 195 -0.0001

PHE 195 ASP 196 0.0001

ASP 196 ARG 197 0.1727

ARG 197 GLY 198 -0.0001

GLY 198 TYR 199 0.0002

TYR 199 LEU 200 0.0261

LEU 200 SER 201 -0.0001

SER 201 PRO 202 -0.0000

PRO 202 TYR 203 0.0024

TYR 203 PHE 204 -0.0001

PHE 204 ILE 205 -0.0000

ILE 205 ASN 206 0.0040

ASN 206 LYS 207 0.0001

LYS 207 PRO 208 0.0004

PRO 208 GLU 209 0.0162

GLU 209 THR 210 0.0000

THR 210 GLY 211 -0.0000

GLY 211 ALA 212 0.0755

ALA 212 VAL 213 -0.0001

VAL 213 GLU 214 0.0001

GLU 214 LEU 215 0.0897

LEU 215 GLU 216 0.0003

GLU 216 SER 217 -0.0003

SER 217 PRO 218 0.0296

PRO 218 PHE 219 -0.0004

PHE 219 ILE 220 0.0003

ILE 220 LEU 221 0.0500

LEU 221 LEU 222 -0.0000

LEU 222 ALA 223 -0.0004

ALA 223 ASP 224 0.0475

ASP 224 LYS 225 -0.0001

LYS 225 LYS 226 0.0002

LYS 226 ILE 227 0.0623

ILE 227 SER 228 0.0000

SER 228 ASN 229 0.0004

ASN 229 ILE 230 0.0125

ILE 230 ARG 231 0.0001

ARG 231 GLU 232 0.0001

GLU 232 MET 233 -0.0076

MET 233 LEU 234 0.0001

LEU 234 PRO 235 -0.0002

PRO 235 VAL 236 -0.0410

VAL 236 LEU 237 0.0000

LEU 237 GLU 238 -0.0001

GLU 238 ALA 239 -0.0558

ALA 239 VAL 240 -0.0002

VAL 240 ALA 241 -0.0002

ALA 241 LYS 242 0.0441

LYS 242 ALA 243 -0.0005

ALA 243 GLY 244 0.0002

GLY 244 LYS 245 0.0143

LYS 245 PRO 246 0.0000

PRO 246 LEU 247 0.0002

LEU 247 LEU 248 0.0113

LEU 248 ILE 249 -0.0000

ILE 249 ILE 250 -0.0001

ILE 250 ALA 251 0.0156

ALA 251 GLU 252 -0.0003

GLU 252 ASP 253 -0.0002

ASP 253 VAL 254 0.0375

VAL 254 GLU 255 0.0002

GLU 255 GLY 256 -0.0001

GLY 256 GLU 257 0.0039

GLU 257 ALA 258 0.0002

ALA 258 LEU 259 0.0002

LEU 259 ALA 260 0.0309

ALA 260 THR 261 0.0000

THR 261 LEU 262 -0.0002

LEU 262 VAL 263 0.0188

VAL 263 VAL 264 0.0000

VAL 264 ASN 265 0.0002

ASN 265 THR 266 0.0241

THR 266 MET 267 -0.0002

MET 267 ARG 268 0.0001

ARG 268 GLY 269 0.0082

GLY 269 ILE 270 -0.0001

ILE 270 VAL 271 -0.0002

VAL 271 LYS 272 0.0733

LYS 272 VAL 273 0.0000

VAL 273 ALA 274 -0.0003

ALA 274 ALA 275 0.0152

ALA 275 VAL 276 -0.0001

VAL 276 LYS 277 -0.0000

LYS 277 ALA 278 -0.0515

ALA 278 PRO 279 -0.0002

PRO 279 GLY 280 -0.0002

GLY 280 PHE 281 -0.0308

PHE 281 GLY 282 -0.0001

GLY 282 ASP 283 0.0000

ASP 283 ARG 284 -0.0046

ARG 284 ARG 285 0.0001

ARG 285 LYS 286 -0.0003

LYS 286 ALA 287 0.0034

ALA 287 MET 288 -0.0000

MET 288 LEU 289 -0.0001

LEU 289 GLN 290 -0.0770

GLN 290 ASP 291 -0.0003

ASP 291 ILE 292 -0.0003

ILE 292 ALA 293 -0.0887

ALA 293 THR 294 0.0004

THR 294 LEU 295 0.0001

LEU 295 THR 296 -0.0936

THR 296 GLY 297 0.0004

GLY 297 GLY 298 0.0001

GLY 298 THR 299 0.0093

THR 299 VAL 300 -0.0000

VAL 300 ILE 301 0.0003

ILE 301 SER 302 0.0694

SER 302 GLU 303 -0.0002

GLU 303 GLU 304 -0.0003

GLU 304 ILE 305 -0.0189

ILE 305 GLY 306 0.0000

GLY 306 MET 307 -0.0001

MET 307 GLU 308 0.0124

GLU 308 LEU 309 -0.0001

LEU 309 GLU 310 0.0002

GLU 310 LYS 311 0.0061

LYS 311 ALA 312 0.0000

ALA 312 THR 313 0.0001

THR 313 LEU 314 0.0886

LEU 314 GLU 315 -0.0003

GLU 315 ASP 316 0.0003

ASP 316 LEU 317 0.0476

LEU 317 GLY 318 0.0000

GLY 318 GLN 319 -0.0002

GLN 319 ALA 320 0.0286

ALA 320 LYS 321 0.0004

LYS 321 ARG 322 -0.0003

ARG 322 VAL 323 0.0496

VAL 323 VAL 324 0.0003

VAL 324 ILE 325 0.0001

ILE 325 ASN 326 0.0555

ASN 326 LYS 327 0.0002

LYS 327 ASP 328 -0.0000

ASP 328 THR 329 0.1064

THR 329 THR 330 0.0004

THR 330 THR 331 0.0001

THR 331 ILE 332 0.1514

ILE 332 ILE 333 0.0001

ILE 333 ASP 334 0.0001

ASP 334 GLY 335 0.0534

GLY 335 VAL 336 0.0002

VAL 336 GLY 337 -0.0000

GLY 337 GLU 338 -0.1533

GLU 338 GLU 339 -0.0002

GLU 339 ALA 340 -0.0001

ALA 340 ALA 341 -0.3520

ALA 341 ILE 342 0.0000

ILE 342 GLN 343 0.0004

GLN 343 GLY 344 -0.2657

GLY 344 ARG 345 -0.0001

ARG 345 VAL 346 0.0004

VAL 346 ALA 347 0.0138

ALA 347 GLN 348 -0.0000

GLN 348 ILE 349 0.0003

ILE 349 ARG 350 -0.1910

ARG 350 GLN 351 -0.0001

GLN 351 GLN 352 -0.0001

GLN 352 ILE 353 -0.1811

ILE 353 GLU 354 0.0001

GLU 354 GLU 355 0.0001

GLU 355 ALA 356 0.0884

ALA 356 THR 357 0.0002

THR 357 SER 358 0.0001

SER 358 ASP 359 0.0428

ASP 359 TYR 360 0.0002

TYR 360 ASP 361 -0.0003

ASP 361 ARG 362 -0.0174

ARG 362 GLU 363 -0.0002

GLU 363 LYS 364 0.0001

LYS 364 LEU 365 0.1063

LEU 365 GLN 366 -0.0004

GLN 366 GLU 367 -0.0004

GLU 367 ARG 368 0.0374

ARG 368 VAL 369 0.0003

VAL 369 ALA 370 0.0002

ALA 370 LYS 371 0.0190

LYS 371 LEU 372 0.0002

LEU 372 ALA 373 -0.0001

ALA 373 GLY 374 0.2972

GLY 374 GLY 375 -0.0001

GLY 375 VAL 376 0.0002

VAL 376 ALA 377 0.3121

ALA 377 VAL 378 0.0005

VAL 378 ILE 379 -0.0001

ILE 379 LYS 380 0.0833

LYS 380 VAL 381 0.0004

VAL 381 GLY 382 -0.0002

GLY 382 ALA 383 0.1535

ALA 383 ALA 384 0.0001

ALA 384 THR 385 0.0001

THR 385 GLU 386 0.0530

GLU 386 VAL 387 0.0001

VAL 387 GLU 388 -0.0001

GLU 388 MET 389 -0.0564

MET 389 LYS 390 0.0000

LYS 390 GLU 391 -0.0000

GLU 391 LYS 392 0.0643

LYS 392 LYS 393 -0.0003

LYS 393 ALA 394 -0.0000

ALA 394 ARG 395 0.0226

ARG 395 VAL 396 -0.0002

VAL 396 GLU 397 -0.0001

GLU 397 ASP 398 -0.0115

ASP 398 ALA 399 -0.0000

ALA 399 LEU 400 0.0002

LEU 400 HIS 401 -0.0076

HIS 401 ALA 402 -0.0000

ALA 402 THR 403 -0.0001

THR 403 ARG 404 0.0913

ARG 404 ALA 405 -0.0001

ALA 405 ALA 406 0.0004

ALA 406 VAL 407 0.0414

VAL 407 GLU 408 0.0003

GLU 408 GLU 409 0.0001

GLU 409 GLY 410 -0.0007

GLY 410 VAL 411 0.0001

VAL 411 VAL 412 -0.0002

VAL 412 ALA 413 -0.0047

ALA 413 GLY 414 0.0001

GLY 414 GLY 415 -0.0001

GLY 415 GLY 416 -0.0318

GLY 416 VAL 417 0.0001

VAL 417 ALA 418 -0.0002

ALA 418 LEU 419 -0.0349

LEU 419 ILE 420 0.0002

ILE 420 ARG 421 -0.0002

ARG 421 VAL 422 -0.0638

VAL 422 ALA 423 -0.0002

ALA 423 SER 424 -0.0001

SER 424 LYS 425 -0.0517

LYS 425 LEU 426 0.0001

LEU 426 ALA 427 -0.0001

ALA 427 ASP 428 -0.1262

ASP 428 LEU 429 -0.0002

LEU 429 ARG 430 -0.0002

ARG 430 GLY 431 -0.1900

GLY 431 GLN 432 -0.0001

GLN 432 ASN 433 0.0001

ASN 433 GLU 434 -0.0323

GLU 434 ASP 435 -0.0002

ASP 435 GLN 436 -0.0002

GLN 436 ASN 437 -0.0167

ASN 437 VAL 438 0.0000

VAL 438 GLY 439 0.0001

GLY 439 ILE 440 0.0035

ILE 440 LYS 441 -0.0002

LYS 441 VAL 442 -0.0002

VAL 442 ALA 443 0.0141

ALA 443 LEU 444 -0.0002

LEU 444 ARG 445 -0.0003

ARG 445 ALA 446 -0.0793

ALA 446 MET 447 -0.0002

MET 447 GLU 448 -0.0002

GLU 448 ALA 449 0.0322

ALA 449 PRO 450 -0.0001

PRO 450 LEU 451 0.0001

LEU 451 ARG 452 0.0386

ARG 452 GLN 453 -0.0003

GLN 453 ILE 454 -0.0003

ILE 454 VAL 455 -0.0026

VAL 455 LEU 456 -0.0003

LEU 456 ASN 457 0.0001

ASN 457 CYS 458 0.0382

CYS 458 GLY 459 0.0002

GLY 459 GLU 460 0.0000

GLU 460 GLU 461 0.0015

GLU 461 PRO 462 0.0002

PRO 462 SER 463 -0.0002

SER 463 VAL 464 -0.0206

VAL 464 VAL 465 -0.0000

VAL 465 ALA 466 -0.0001

ALA 466 ASN 467 0.0199

ASN 467 THR 468 -0.0002

THR 468 VAL 469 -0.0000

VAL 469 LYS 470 -0.0277

LYS 470 GLY 471 0.0001

GLY 471 GLY 472 0.0002

GLY 472 ASP 473 0.0141

ASP 473 GLY 474 -0.0003

GLY 474 ASN 475 0.0003

ASN 475 TYR 476 0.0390

TYR 476 GLY 477 0.0005

GLY 477 TYR 478 -0.0002

TYR 478 ASN 479 -0.0074

ASN 479 ALA 480 -0.0001

ALA 480 ALA 481 -0.0000

ALA 481 THR 482 0.0670

THR 482 GLU 483 0.0000

GLU 483 GLU 484 -0.0005

GLU 484 TYR 485 -0.0011

TYR 485 GLY 486 -0.0000

GLY 486 ASN 487 0.0002

ASN 487 MET 488 0.0050

MET 488 ILE 489 0.0003

ILE 489 ASP 490 -0.0003

ASP 490 MET 491 0.0220

MET 491 GLY 492 0.0002

GLY 492 ILE 493 -0.0002

ILE 493 LEU 494 0.0320

LEU 494 ASP 495 0.0002

ASP 495 PRO 496 -0.0001

PRO 496 THR 497 -0.0036

THR 497 LYS 498 0.0002

LYS 498 VAL 499 -0.0007

VAL 499 THR 500 -0.0344

THR 500 ARG 501 0.0005

ARG 501 SER 502 -0.0001

SER 502 ALA 503 -0.0236

ALA 503 LEU 504 0.0001

LEU 504 GLN 505 0.0001

GLN 505 TYR 506 -0.0528

TYR 506 ALA 507 0.0005

ALA 507 ALA 508 0.0001

ALA 508 SER 509 -0.0636

SER 509 VAL 510 -0.0001

VAL 510 ALA 511 0.0001

ALA 511 GLY 512 0.0067

GLY 512 LEU 513 0.0002

LEU 513 MET 514 0.0002

MET 514 ILE 515 -0.0327

ILE 515 THR 516 0.0000

THR 516 THR 517 0.0000

THR 517 GLU 518 -0.1738

GLU 518 CYS 519 -0.0000

CYS 519 MET 520 -0.0002

MET 520 VAL 521 0.2925

VAL 521 THR 522 -0.0000

THR 522 ASP 523 -0.0000

ASP 523 LEU 524 0.0435

LEU 524 PRO 525 -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.

*** CHAPERONE 1SVT ***

CA strain for 2404010833281775939

--- normal mode 22 ---

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

* CHAPERONE 1SVT *