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

* CHAPERONE 1SVT *

CA strain for 2404010833281775939

--- normal mode 14 ---

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 0.0002

ALA 3 LYS 4 -0.0001

LYS 4 ASP 5 0.0119

ASP 5 VAL 6 0.0000

VAL 6 LYS 7 -0.0002

LYS 7 PHE 8 0.0265

PHE 8 GLY 9 -0.0001

GLY 9 ASN 10 -0.0004

ASN 10 ASP 11 -0.0303

ASP 11 ALA 12 0.0001

ALA 12 ARG 13 0.0000

ARG 13 VAL 14 0.0175

VAL 14 LYS 15 -0.0000

LYS 15 MET 16 0.0002

MET 16 LEU 17 -0.0040

LEU 17 ARG 18 -0.0001

ARG 18 GLY 19 -0.0003

GLY 19 VAL 20 -0.0044

VAL 20 ASN 21 -0.0002

ASN 21 VAL 22 0.0002

VAL 22 LEU 23 0.0077

LEU 23 ALA 24 0.0004

ALA 24 ASP 25 0.0002

ASP 25 ALA 26 -0.0246

ALA 26 VAL 27 0.0002

VAL 27 LYS 28 0.0004

LYS 28 VAL 29 0.0164

VAL 29 THR 30 0.0002

THR 30 LEU 31 0.0005

LEU 31 GLY 32 -0.0564

GLY 32 PRO 33 0.0002

PRO 33 LYS 34 -0.0002

LYS 34 GLY 35 0.0579

GLY 35 ARG 36 0.0000

ARG 36 ASN 37 -0.0002

ASN 37 VAL 38 -0.0368

VAL 38 VAL 39 0.0000

VAL 39 LEU 40 0.0002

LEU 40 ASP 41 -0.0666

ASP 41 LYS 42 0.0003

LYS 42 SER 43 -0.0002

SER 43 PHE 44 -0.0478

PHE 44 GLY 45 0.0000

GLY 45 ALA 46 0.0002

ALA 46 PRO 47 0.0517

PRO 47 THR 48 0.0003

THR 48 ILE 49 -0.0003

ILE 49 THR 50 0.0962

THR 50 LYS 51 -0.0002

LYS 51 ASP 52 0.0001

ASP 52 GLY 53 -0.1042

GLY 53 VAL 54 0.0002

VAL 54 SER 55 0.0003

SER 55 VAL 56 -0.0154

VAL 56 ALA 57 -0.0004

ALA 57 ARG 58 -0.0000

ARG 58 GLU 59 -0.1333

GLU 59 ILE 60 -0.0001

ILE 60 GLU 61 -0.0000

GLU 61 LEU 62 -0.1314

LEU 62 GLU 63 0.0002

GLU 63 ASP 64 0.0003

ASP 64 LYS 65 0.0218

LYS 65 PHE 66 0.0002

PHE 66 GLU 67 -0.0001

GLU 67 ASN 68 -0.0417

ASN 68 MET 69 0.0000

MET 69 GLY 70 0.0003

GLY 70 ALA 71 -0.0769

ALA 71 GLN 72 -0.0003

GLN 72 MET 73 0.0000

MET 73 VAL 74 0.0560

VAL 74 LYS 75 -0.0000

LYS 75 GLU 76 0.0001

GLU 76 VAL 77 0.0636

VAL 77 ALA 78 -0.0002

ALA 78 SER 79 -0.0001

SER 79 LYS 80 0.0138

LYS 80 ALA 81 0.0002

ALA 81 ASN 82 -0.0002

ASN 82 ASP 83 0.0087

ASP 83 ALA 84 -0.0001

ALA 84 ALA 85 -0.0002

ALA 85 GLY 86 -0.0208

GLY 86 ASP 87 0.0001

ASP 87 GLY 88 -0.0000

GLY 88 THR 89 -0.0394

THR 89 THR 90 0.0002

THR 90 THR 91 -0.0001

THR 91 ALA 92 0.0205

ALA 92 THR 93 0.0002

THR 93 VAL 94 -0.0001

VAL 94 LEU 95 -0.0094

LEU 95 ALA 96 0.0001

ALA 96 GLN 97 -0.0001

GLN 97 ALA 98 -0.0742

ALA 98 ILE 99 0.0001

ILE 99 ILE 100 -0.0003

ILE 100 THR 101 -0.0089

THR 101 GLU 102 0.0000

GLU 102 GLY 103 -0.0001

GLY 103 LEU 104 0.0413

LEU 104 LYS 105 -0.0003

LYS 105 ALA 106 0.0004

ALA 106 VAL 107 0.0825

VAL 107 ALA 108 0.0003

ALA 108 ALA 109 0.0003

ALA 109 GLY 110 -0.0403

GLY 110 MET 111 -0.0000

MET 111 ASN 112 -0.0002

ASN 112 PRO 113 -0.0016

PRO 113 MET 114 -0.0001

MET 114 ASP 115 -0.0003

ASP 115 LEU 116 -0.0233

LEU 116 LYS 117 0.0000

LYS 117 ARG 118 0.0001

ARG 118 GLY 119 0.0318

GLY 119 ILE 120 0.0001

ILE 120 ASP 121 -0.0001

ASP 121 LYS 122 0.0151

LYS 122 ALA 123 0.0002

ALA 123 VAL 124 -0.0001

VAL 124 THR 125 0.0021

THR 125 ALA 126 0.0000

ALA 126 ALA 127 0.0002

ALA 127 VAL 128 0.0063

VAL 128 GLU 129 0.0000

GLU 129 GLU 130 0.0000

GLU 130 LEU 131 0.0330

LEU 131 LYS 132 -0.0004

LYS 132 ALA 133 -0.0001

ALA 133 LEU 134 -0.0261

LEU 134 SER 135 0.0002

SER 135 VAL 136 -0.0003

VAL 136 PRO 137 0.0819

PRO 137 CYS 138 -0.0001

CYS 138 SER 139 0.0001

SER 139 ASP 140 0.0487

ASP 140 SER 141 -0.0002

SER 141 LYS 142 0.0002

LYS 142 ALA 143 -0.0082

ALA 143 ILE 144 -0.0000

ILE 144 ALA 145 0.0002

ALA 145 GLN 146 0.0669

GLN 146 VAL 147 0.0001

VAL 147 GLY 148 -0.0001

GLY 148 THR 149 0.0146

THR 149 ILE 150 0.0000

ILE 150 SER 151 0.0004

SER 151 ALA 152 0.0386

ALA 152 ASN 153 -0.0000

ASN 153 SER 154 -0.0001

SER 154 ASP 155 -0.0095

ASP 155 GLU 156 0.0002

GLU 156 THR 157 -0.0000

THR 157 VAL 158 -0.0560

VAL 158 GLY 159 -0.0001

GLY 159 LYS 160 -0.0001

LYS 160 LEU 161 0.0639

LEU 161 ILE 162 0.0001

ILE 162 ALA 163 0.0001

ALA 163 GLU 164 -0.0208

GLU 164 ALA 165 0.0001

ALA 165 MET 166 -0.0001

MET 166 ASP 167 -0.0134

ASP 167 LYS 168 -0.0002

LYS 168 VAL 169 0.0003

VAL 169 GLY 170 0.0991

GLY 170 LYS 171 0.0003

LYS 171 GLU 172 0.0004

GLU 172 GLY 173 -0.1438

GLY 173 VAL 174 -0.0004

VAL 174 ILE 175 0.0002

ILE 175 THR 176 -0.1316

THR 176 VAL 177 -0.0001

VAL 177 GLU 178 0.0001

GLU 178 ASP 179 -0.1575

ASP 179 GLY 180 0.0000

GLY 180 THR 181 -0.0002

THR 181 GLY 182 -0.0461

GLY 182 LEU 183 0.0000

LEU 183 GLN 184 0.0001

GLN 184 ASP 185 0.0483

ASP 185 GLU 186 0.0001

GLU 186 LEU 187 0.0002

LEU 187 ASP 188 -0.1859

ASP 188 VAL 189 0.0001

VAL 189 VAL 190 -0.0003

VAL 190 GLU 191 -0.1124

GLU 191 GLY 192 0.0001

GLY 192 MET 193 0.0003

MET 193 GLN 194 0.0648

GLN 194 PHE 195 -0.0002

PHE 195 ASP 196 0.0004

ASP 196 ARG 197 0.0645

ARG 197 GLY 198 -0.0002

GLY 198 TYR 199 0.0003

TYR 199 LEU 200 0.0105

LEU 200 SER 201 0.0000

SER 201 PRO 202 0.0004

PRO 202 TYR 203 0.0046

TYR 203 PHE 204 0.0004

PHE 204 ILE 205 0.0002

ILE 205 ASN 206 0.0003

ASN 206 LYS 207 -0.0001

LYS 207 PRO 208 -0.0002

PRO 208 GLU 209 -0.0113

GLU 209 THR 210 -0.0000

THR 210 GLY 211 0.0001

GLY 211 ALA 212 0.0014

ALA 212 VAL 213 -0.0002

VAL 213 GLU 214 -0.0001

GLU 214 LEU 215 0.0004

LEU 215 GLU 216 -0.0002

GLU 216 SER 217 0.0002

SER 217 PRO 218 0.0082

PRO 218 PHE 219 -0.0000

PHE 219 ILE 220 -0.0002

ILE 220 LEU 221 0.0153

LEU 221 LEU 222 -0.0000

LEU 222 ALA 223 -0.0000

ALA 223 ASP 224 0.0237

ASP 224 LYS 225 0.0000

LYS 225 LYS 226 0.0000

LYS 226 ILE 227 -0.0010

ILE 227 SER 228 -0.0001

SER 228 ASN 229 -0.0000

ASN 229 ILE 230 0.0037

ILE 230 ARG 231 -0.0002

ARG 231 GLU 232 0.0002

GLU 232 MET 233 0.0007

MET 233 LEU 234 -0.0000

LEU 234 PRO 235 0.0002

PRO 235 VAL 236 -0.0102

VAL 236 LEU 237 0.0001

LEU 237 GLU 238 0.0000

GLU 238 ALA 239 -0.0102

ALA 239 VAL 240 0.0001

VAL 240 ALA 241 -0.0002

ALA 241 LYS 242 0.0040

LYS 242 ALA 243 -0.0000

ALA 243 GLY 244 -0.0004

GLY 244 LYS 245 0.0064

LYS 245 PRO 246 0.0003

PRO 246 LEU 247 -0.0002

LEU 247 LEU 248 0.0052

LEU 248 ILE 249 -0.0001

ILE 249 ILE 250 -0.0003

ILE 250 ALA 251 0.0012

ALA 251 GLU 252 -0.0000

GLU 252 ASP 253 0.0002

ASP 253 VAL 254 0.0033

VAL 254 GLU 255 -0.0000

GLU 255 GLY 256 0.0003

GLY 256 GLU 257 0.0018

GLU 257 ALA 258 0.0004

ALA 258 LEU 259 -0.0000

LEU 259 ALA 260 0.0034

ALA 260 THR 261 -0.0000

THR 261 LEU 262 0.0004

LEU 262 VAL 263 -0.0014

VAL 263 VAL 264 0.0004

VAL 264 ASN 265 0.0000

ASN 265 THR 266 0.0037

THR 266 MET 267 -0.0003

MET 267 ARG 268 -0.0000

ARG 268 GLY 269 -0.0008

GLY 269 ILE 270 0.0000

ILE 270 VAL 271 -0.0004

VAL 271 LYS 272 0.0107

LYS 272 VAL 273 -0.0001

VAL 273 ALA 274 0.0003

ALA 274 ALA 275 0.0143

ALA 275 VAL 276 0.0001

VAL 276 LYS 277 -0.0001

LYS 277 ALA 278 0.0174

ALA 278 PRO 279 -0.0001

PRO 279 GLY 280 -0.0002

GLY 280 PHE 281 -0.0418

PHE 281 GLY 282 0.0002

GLY 282 ASP 283 -0.0002

ASP 283 ARG 284 -0.0029

ARG 284 ARG 285 0.0002

ARG 285 LYS 286 0.0000

LYS 286 ALA 287 -0.0249

ALA 287 MET 288 -0.0002

MET 288 LEU 289 0.0002

LEU 289 GLN 290 0.0163

GLN 290 ASP 291 0.0001

ASP 291 ILE 292 -0.0003

ILE 292 ALA 293 -0.0354

ALA 293 THR 294 -0.0002

THR 294 LEU 295 0.0003

LEU 295 THR 296 -0.0435

THR 296 GLY 297 -0.0001

GLY 297 GLY 298 0.0001

GLY 298 THR 299 0.0274

THR 299 VAL 300 -0.0002

VAL 300 ILE 301 -0.0001

ILE 301 SER 302 0.0304

SER 302 GLU 303 -0.0002

GLU 303 GLU 304 0.0003

GLU 304 ILE 305 -0.0100

ILE 305 GLY 306 -0.0001

GLY 306 MET 307 -0.0001

MET 307 GLU 308 0.0030

GLU 308 LEU 309 -0.0002

LEU 309 GLU 310 0.0000

GLU 310 LYS 311 0.0104

LYS 311 ALA 312 0.0000

ALA 312 THR 313 -0.0000

THR 313 LEU 314 0.0233

LEU 314 GLU 315 -0.0001

GLU 315 ASP 316 -0.0002

ASP 316 LEU 317 0.0080

LEU 317 GLY 318 -0.0004

GLY 318 GLN 319 0.0003

GLN 319 ALA 320 0.0021

ALA 320 LYS 321 0.0002

LYS 321 ARG 322 -0.0003

ARG 322 VAL 323 -0.0135

VAL 323 VAL 324 -0.0001

VAL 324 ILE 325 0.0002

ILE 325 ASN 326 -0.0283

ASN 326 LYS 327 -0.0001

LYS 327 ASP 328 -0.0004

ASP 328 THR 329 0.0229

THR 329 THR 330 0.0001

THR 330 THR 331 -0.0000

THR 331 ILE 332 -0.0151

ILE 332 ILE 333 -0.0001

ILE 333 ASP 334 0.0001

ASP 334 GLY 335 -0.0074

GLY 335 VAL 336 -0.0000

VAL 336 GLY 337 0.0001

GLY 337 GLU 338 -0.0024

GLU 338 GLU 339 -0.0003

GLU 339 ALA 340 -0.0001

ALA 340 ALA 341 0.0457

ALA 341 ILE 342 0.0001

ILE 342 GLN 343 -0.0002

GLN 343 GLY 344 0.0424

GLY 344 ARG 345 0.0002

ARG 345 VAL 346 0.0001

VAL 346 ALA 347 0.0024

ALA 347 GLN 348 -0.0001

GLN 348 ILE 349 -0.0000

ILE 349 ARG 350 -0.0004

ARG 350 GLN 351 -0.0003

GLN 351 GLN 352 0.0002

GLN 352 ILE 353 0.0006

ILE 353 GLU 354 0.0000

GLU 354 GLU 355 -0.0002

GLU 355 ALA 356 0.0073

ALA 356 THR 357 -0.0001

THR 357 SER 358 0.0002

SER 358 ASP 359 -0.0044

ASP 359 TYR 360 -0.0001

TYR 360 ASP 361 -0.0003

ASP 361 ARG 362 -0.0044

ARG 362 GLU 363 0.0001

GLU 363 LYS 364 -0.0001

LYS 364 LEU 365 0.0353

LEU 365 GLN 366 -0.0001

GLN 366 GLU 367 0.0001

GLU 367 ARG 368 -0.0666

ARG 368 VAL 369 -0.0000

VAL 369 ALA 370 0.0003

ALA 370 LYS 371 0.0464

LYS 371 LEU 372 -0.0002

LEU 372 ALA 373 0.0002

ALA 373 GLY 374 -0.0362

GLY 374 GLY 375 -0.0000

GLY 375 VAL 376 0.0001

VAL 376 ALA 377 -0.2480

ALA 377 VAL 378 -0.0002

VAL 378 ILE 379 0.0002

ILE 379 LYS 380 -0.0581

LYS 380 VAL 381 0.0001

VAL 381 GLY 382 -0.0002

GLY 382 ALA 383 -0.1286

ALA 383 ALA 384 -0.0001

ALA 384 THR 385 0.0002

THR 385 GLU 386 -0.0755

GLU 386 VAL 387 -0.0001

VAL 387 GLU 388 -0.0003

GLU 388 MET 389 -0.0237

MET 389 LYS 390 -0.0000

LYS 390 GLU 391 0.0002

GLU 391 LYS 392 -0.0929

LYS 392 LYS 393 -0.0002

LYS 393 ALA 394 0.0001

ALA 394 ARG 395 0.0187

ARG 395 VAL 396 0.0002

VAL 396 GLU 397 -0.0001

GLU 397 ASP 398 -0.0501

ASP 398 ALA 399 -0.0001

ALA 399 LEU 400 -0.0002

LEU 400 HIS 401 -0.0079

HIS 401 ALA 402 0.0000

ALA 402 THR 403 -0.0001

THR 403 ARG 404 -0.0000

ARG 404 ALA 405 -0.0001

ALA 405 ALA 406 -0.0002

ALA 406 VAL 407 -0.0269

VAL 407 GLU 408 0.0000

GLU 408 GLU 409 -0.0002

GLU 409 GLY 410 -0.0417

GLY 410 VAL 411 -0.0002

VAL 411 VAL 412 -0.0000

VAL 412 ALA 413 -0.0870

ALA 413 GLY 414 0.0000

GLY 414 GLY 415 -0.0003

GLY 415 GLY 416 0.0305

GLY 416 VAL 417 0.0001

VAL 417 ALA 418 0.0001

ALA 418 LEU 419 0.0565

LEU 419 ILE 420 -0.0000

ILE 420 ARG 421 0.0002

ARG 421 VAL 422 0.0127

VAL 422 ALA 423 0.0003

ALA 423 SER 424 -0.0001

SER 424 LYS 425 -0.0279

LYS 425 LEU 426 -0.0002

LEU 426 ALA 427 0.0002

ALA 427 ASP 428 0.0161

ASP 428 LEU 429 -0.0000

LEU 429 ARG 430 -0.0001

ARG 430 GLY 431 0.0685

GLY 431 GLN 432 -0.0003

GLN 432 ASN 433 0.0002

ASN 433 GLU 434 -0.0125

GLU 434 ASP 435 0.0000

ASP 435 GLN 436 -0.0000

GLN 436 ASN 437 0.0315

ASN 437 VAL 438 0.0003

VAL 438 GLY 439 0.0004

GLY 439 ILE 440 0.0394

ILE 440 LYS 441 0.0003

LYS 441 VAL 442 0.0003

VAL 442 ALA 443 0.0436

ALA 443 LEU 444 0.0004

LEU 444 ARG 445 0.0001

ARG 445 ALA 446 -0.0839

ALA 446 MET 447 0.0002

MET 447 GLU 448 0.0003

GLU 448 ALA 449 -0.0281

ALA 449 PRO 450 0.0004

PRO 450 LEU 451 -0.0002

LEU 451 ARG 452 -0.0353

ARG 452 GLN 453 0.0002

GLN 453 ILE 454 0.0002

ILE 454 VAL 455 -0.0014

VAL 455 LEU 456 -0.0002

LEU 456 ASN 457 0.0002

ASN 457 CYS 458 -0.0143

CYS 458 GLY 459 0.0000

GLY 459 GLU 460 0.0002

GLU 460 GLU 461 -0.0048

GLU 461 PRO 462 -0.0003

PRO 462 SER 463 0.0003

SER 463 VAL 464 0.0010

VAL 464 VAL 465 0.0000

VAL 465 ALA 466 0.0003

ALA 466 ASN 467 0.0025

ASN 467 THR 468 -0.0000

THR 468 VAL 469 0.0001

VAL 469 LYS 470 0.0068

LYS 470 GLY 471 -0.0000

GLY 471 GLY 472 0.0001

GLY 472 ASP 473 0.0058

ASP 473 GLY 474 -0.0003

GLY 474 ASN 475 -0.0001

ASN 475 TYR 476 -0.0442

TYR 476 GLY 477 -0.0001

GLY 477 TYR 478 0.0000

TYR 478 ASN 479 0.0152

ASN 479 ALA 480 -0.0003

ALA 480 ALA 481 -0.0002

ALA 481 THR 482 0.0212

THR 482 GLU 483 -0.0003

GLU 483 GLU 484 0.0004

GLU 484 TYR 485 0.0058

TYR 485 GLY 486 0.0001

GLY 486 ASN 487 -0.0004

ASN 487 MET 488 -0.0045

MET 488 ILE 489 -0.0003

ILE 489 ASP 490 0.0001

ASP 490 MET 491 -0.0182

MET 491 GLY 492 -0.0005

GLY 492 ILE 493 0.0004

ILE 493 LEU 494 -0.0605

LEU 494 ASP 495 -0.0003

ASP 495 PRO 496 0.0003

PRO 496 THR 497 0.0698

THR 497 LYS 498 0.0001

LYS 498 VAL 499 -0.0001

VAL 499 THR 500 0.0064

THR 500 ARG 501 0.0003

ARG 501 SER 502 0.0001

SER 502 ALA 503 0.0198

ALA 503 LEU 504 0.0000

LEU 504 GLN 505 0.0002

GLN 505 TYR 506 0.0264

TYR 506 ALA 507 0.0000

ALA 507 ALA 508 0.0000

ALA 508 SER 509 0.0164

SER 509 VAL 510 -0.0001

VAL 510 ALA 511 0.0002

ALA 511 GLY 512 -0.0516

GLY 512 LEU 513 -0.0000

LEU 513 MET 514 -0.0003

MET 514 ILE 515 -0.1010

ILE 515 THR 516 -0.0003

THR 516 THR 517 -0.0001

THR 517 GLU 518 0.0054

GLU 518 CYS 519 -0.0000

CYS 519 MET 520 -0.0002

MET 520 VAL 521 0.2599

VAL 521 THR 522 -0.0002

THR 522 ASP 523 -0.0002

ASP 523 LEU 524 0.0642

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 14 ---

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

* CHAPERONE 1SVT *