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

* CHAPERONE 1SVT *

CA strain for 2404010833281775939

--- normal mode 21 ---

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 -0.0003

LYS 4 ASP 5 -0.2138

ASP 5 VAL 6 0.0003

VAL 6 LYS 7 -0.0002

LYS 7 PHE 8 -0.0761

PHE 8 GLY 9 0.0001

GLY 9 ASN 10 0.0004

ASN 10 ASP 11 -0.0212

ASP 11 ALA 12 -0.0001

ALA 12 ARG 13 0.0003

ARG 13 VAL 14 -0.0625

VAL 14 LYS 15 0.0002

LYS 15 MET 16 0.0004

MET 16 LEU 17 0.0175

LEU 17 ARG 18 -0.0002

ARG 18 GLY 19 0.0003

GLY 19 VAL 20 -0.0233

VAL 20 ASN 21 -0.0005

ASN 21 VAL 22 0.0000

VAL 22 LEU 23 -0.0020

LEU 23 ALA 24 0.0003

ALA 24 ASP 25 -0.0002

ASP 25 ALA 26 0.0371

ALA 26 VAL 27 0.0002

VAL 27 LYS 28 0.0003

LYS 28 VAL 29 -0.0111

VAL 29 THR 30 -0.0001

THR 30 LEU 31 -0.0004

LEU 31 GLY 32 0.0925

GLY 32 PRO 33 -0.0002

PRO 33 LYS 34 -0.0004

LYS 34 GLY 35 -0.0686

GLY 35 ARG 36 0.0000

ARG 36 ASN 37 -0.0001

ASN 37 VAL 38 0.0795

VAL 38 VAL 39 -0.0002

VAL 39 LEU 40 0.0001

LEU 40 ASP 41 0.3874

ASP 41 LYS 42 0.0001

LYS 42 SER 43 0.0002

SER 43 PHE 44 0.1705

PHE 44 GLY 45 0.0000

GLY 45 ALA 46 0.0002

ALA 46 PRO 47 0.0599

PRO 47 THR 48 0.0004

THR 48 ILE 49 0.0000

ILE 49 THR 50 -0.0302

THR 50 LYS 51 -0.0002

LYS 51 ASP 52 -0.0003

ASP 52 GLY 53 0.0637

GLY 53 VAL 54 -0.0001

VAL 54 SER 55 -0.0002

SER 55 VAL 56 -0.0244

VAL 56 ALA 57 -0.0000

ALA 57 ARG 58 0.0001

ARG 58 GLU 59 0.1822

GLU 59 ILE 60 -0.0002

ILE 60 GLU 61 -0.0001

GLU 61 LEU 62 0.1467

LEU 62 GLU 63 -0.0002

GLU 63 ASP 64 -0.0000

ASP 64 LYS 65 -0.0622

LYS 65 PHE 66 -0.0001

PHE 66 GLU 67 0.0002

GLU 67 ASN 68 0.0039

ASN 68 MET 69 0.0002

MET 69 GLY 70 -0.0002

GLY 70 ALA 71 0.0527

ALA 71 GLN 72 0.0001

GLN 72 MET 73 -0.0000

MET 73 VAL 74 -0.0491

VAL 74 LYS 75 0.0001

LYS 75 GLU 76 0.0005

GLU 76 VAL 77 -0.0280

VAL 77 ALA 78 0.0000

ALA 78 SER 79 0.0002

SER 79 LYS 80 0.0531

LYS 80 ALA 81 0.0004

ALA 81 ASN 82 -0.0002

ASN 82 ASP 83 -0.0047

ASP 83 ALA 84 -0.0004

ALA 84 ALA 85 0.0002

ALA 85 GLY 86 0.0358

GLY 86 ASP 87 -0.0003

ASP 87 GLY 88 0.0003

GLY 88 THR 89 0.0065

THR 89 THR 90 0.0002

THR 90 THR 91 -0.0002

THR 91 ALA 92 0.0295

ALA 92 THR 93 -0.0002

THR 93 VAL 94 -0.0001

VAL 94 LEU 95 -0.0033

LEU 95 ALA 96 -0.0000

ALA 96 GLN 97 -0.0000

GLN 97 ALA 98 -0.0344

ALA 98 ILE 99 -0.0001

ILE 99 ILE 100 -0.0002

ILE 100 THR 101 0.0365

THR 101 GLU 102 0.0004

GLU 102 GLY 103 0.0004

GLY 103 LEU 104 0.0040

LEU 104 LYS 105 0.0002

LYS 105 ALA 106 0.0002

ALA 106 VAL 107 0.0767

VAL 107 ALA 108 -0.0001

ALA 108 ALA 109 0.0000

ALA 109 GLY 110 -0.0816

GLY 110 MET 111 -0.0001

MET 111 ASN 112 -0.0003

ASN 112 PRO 113 0.1052

PRO 113 MET 114 0.0002

MET 114 ASP 115 0.0001

ASP 115 LEU 116 -0.0356

LEU 116 LYS 117 0.0002

LYS 117 ARG 118 0.0001

ARG 118 GLY 119 -0.1588

GLY 119 ILE 120 0.0004

ILE 120 ASP 121 0.0002

ASP 121 LYS 122 -0.0575

LYS 122 ALA 123 -0.0005

ALA 123 VAL 124 -0.0003

VAL 124 THR 125 -0.0567

THR 125 ALA 126 0.0002

ALA 126 ALA 127 0.0001

ALA 127 VAL 128 0.0184

VAL 128 GLU 129 -0.0004

GLU 129 GLU 130 -0.0003

GLU 130 LEU 131 0.0451

LEU 131 LYS 132 0.0004

LYS 132 ALA 133 0.0004

ALA 133 LEU 134 0.0396

LEU 134 SER 135 0.0002

SER 135 VAL 136 0.0002

VAL 136 PRO 137 -0.0668

PRO 137 CYS 138 -0.0002

CYS 138 SER 139 -0.0000

SER 139 ASP 140 0.0163

ASP 140 SER 141 -0.0001

SER 141 LYS 142 0.0003

LYS 142 ALA 143 0.0015

ALA 143 ILE 144 0.0003

ILE 144 ALA 145 -0.0000

ALA 145 GLN 146 0.0982

GLN 146 VAL 147 -0.0001

VAL 147 GLY 148 -0.0002

GLY 148 THR 149 0.0135

THR 149 ILE 150 0.0000

ILE 150 SER 151 -0.0004

SER 151 ALA 152 -0.0011

ALA 152 ASN 153 0.0000

ASN 153 SER 154 0.0001

SER 154 ASP 155 0.2214

ASP 155 GLU 156 -0.0001

GLU 156 THR 157 -0.0001

THR 157 VAL 158 -0.0829

VAL 158 GLY 159 0.0005

GLY 159 LYS 160 -0.0001

LYS 160 LEU 161 0.0458

LEU 161 ILE 162 -0.0003

ILE 162 ALA 163 -0.0002

ALA 163 GLU 164 -0.0179

GLU 164 ALA 165 0.0001

ALA 165 MET 166 -0.0000

MET 166 ASP 167 0.0037

ASP 167 LYS 168 -0.0004

LYS 168 VAL 169 0.0001

VAL 169 GLY 170 -0.0100

GLY 170 LYS 171 0.0001

LYS 171 GLU 172 -0.0001

GLU 172 GLY 173 0.0760

GLY 173 VAL 174 -0.0001

VAL 174 ILE 175 0.0001

ILE 175 THR 176 0.0810

THR 176 VAL 177 -0.0001

VAL 177 GLU 178 0.0003

GLU 178 ASP 179 0.0158

ASP 179 GLY 180 0.0001

GLY 180 THR 181 0.0001

THR 181 GLY 182 -0.1178

GLY 182 LEU 183 0.0002

LEU 183 GLN 184 -0.0003

GLN 184 ASP 185 -0.0299

ASP 185 GLU 186 -0.0003

GLU 186 LEU 187 0.0000

LEU 187 ASP 188 -0.2532

ASP 188 VAL 189 -0.0002

VAL 189 VAL 190 0.0002

VAL 190 GLU 191 -0.1169

GLU 191 GLY 192 0.0001

GLY 192 MET 193 -0.0001

MET 193 GLN 194 0.0947

GLN 194 PHE 195 -0.0005

PHE 195 ASP 196 0.0004

ASP 196 ARG 197 0.0533

ARG 197 GLY 198 -0.0002

GLY 198 TYR 199 -0.0001

TYR 199 LEU 200 0.0402

LEU 200 SER 201 0.0003

SER 201 PRO 202 -0.0000

PRO 202 TYR 203 -0.0005

TYR 203 PHE 204 -0.0001

PHE 204 ILE 205 0.0003

ILE 205 ASN 206 0.0080

ASN 206 LYS 207 -0.0001

LYS 207 PRO 208 -0.0002

PRO 208 GLU 209 -0.0272

GLU 209 THR 210 0.0003

THR 210 GLY 211 0.0002

GLY 211 ALA 212 0.0012

ALA 212 VAL 213 -0.0000

VAL 213 GLU 214 -0.0001

GLU 214 LEU 215 -0.0202

LEU 215 GLU 216 -0.0001

GLU 216 SER 217 -0.0003

SER 217 PRO 218 -0.0090

PRO 218 PHE 219 0.0004

PHE 219 ILE 220 0.0001

ILE 220 LEU 221 0.0177

LEU 221 LEU 222 -0.0000

LEU 222 ALA 223 0.0004

ALA 223 ASP 224 0.0715

ASP 224 LYS 225 0.0000

LYS 225 LYS 226 0.0002

LYS 226 ILE 227 -0.0289

ILE 227 SER 228 0.0001

SER 228 ASN 229 -0.0005

ASN 229 ILE 230 0.0003

ILE 230 ARG 231 -0.0000

ARG 231 GLU 232 -0.0001

GLU 232 MET 233 0.0011

MET 233 LEU 234 -0.0000

LEU 234 PRO 235 0.0002

PRO 235 VAL 236 -0.0247

VAL 236 LEU 237 -0.0002

LEU 237 GLU 238 -0.0001

GLU 238 ALA 239 -0.0137

ALA 239 VAL 240 0.0001

VAL 240 ALA 241 0.0006

ALA 241 LYS 242 -0.0119

LYS 242 ALA 243 0.0001

ALA 243 GLY 244 -0.0000

GLY 244 LYS 245 -0.0126

LYS 245 PRO 246 0.0000

PRO 246 LEU 247 -0.0003

LEU 247 LEU 248 -0.0024

LEU 248 ILE 249 0.0004

ILE 249 ILE 250 -0.0000

ILE 250 ALA 251 0.0084

ALA 251 GLU 252 0.0003

GLU 252 ASP 253 -0.0002

ASP 253 VAL 254 -0.0302

VAL 254 GLU 255 0.0002

GLU 255 GLY 256 0.0001

GLY 256 GLU 257 -0.0116

GLU 257 ALA 258 -0.0003

ALA 258 LEU 259 -0.0002

LEU 259 ALA 260 -0.0108

ALA 260 THR 261 -0.0004

THR 261 LEU 262 0.0003

LEU 262 VAL 263 0.0005

VAL 263 VAL 264 0.0001

VAL 264 ASN 265 -0.0002

ASN 265 THR 266 -0.0031

THR 266 MET 267 -0.0004

MET 267 ARG 268 -0.0003

ARG 268 GLY 269 0.0072

GLY 269 ILE 270 -0.0000

ILE 270 VAL 271 -0.0003

VAL 271 LYS 272 -0.0131

LYS 272 VAL 273 -0.0001

VAL 273 ALA 274 -0.0001

ALA 274 ALA 275 0.0154

ALA 275 VAL 276 0.0001

VAL 276 LYS 277 -0.0001

LYS 277 ALA 278 -0.0234

ALA 278 PRO 279 0.0001

PRO 279 GLY 280 -0.0003

GLY 280 PHE 281 -0.0502

PHE 281 GLY 282 0.0003

GLY 282 ASP 283 0.0003

ASP 283 ARG 284 -0.0007

ARG 284 ARG 285 0.0001

ARG 285 LYS 286 0.0000

LYS 286 ALA 287 -0.1011

ALA 287 MET 288 -0.0001

MET 288 LEU 289 -0.0002

LEU 289 GLN 290 -0.0231

GLN 290 ASP 291 0.0001

ASP 291 ILE 292 0.0001

ILE 292 ALA 293 -0.0784

ALA 293 THR 294 -0.0002

THR 294 LEU 295 -0.0003

LEU 295 THR 296 -0.0104

THR 296 GLY 297 -0.0003

GLY 297 GLY 298 -0.0002

GLY 298 THR 299 -0.1117

THR 299 VAL 300 -0.0004

VAL 300 ILE 301 -0.0002

ILE 301 SER 302 -0.0171

SER 302 GLU 303 0.0001

GLU 303 GLU 304 0.0001

GLU 304 ILE 305 0.0009

ILE 305 GLY 306 -0.0001

GLY 306 MET 307 -0.0002

MET 307 GLU 308 0.0018

GLU 308 LEU 309 -0.0000

LEU 309 GLU 310 0.0002

GLU 310 LYS 311 0.0138

LYS 311 ALA 312 -0.0001

ALA 312 THR 313 0.0004

THR 313 LEU 314 0.0013

LEU 314 GLU 315 0.0001

GLU 315 ASP 316 -0.0001

ASP 316 LEU 317 -0.0188

LEU 317 GLY 318 0.0000

GLY 318 GLN 319 -0.0002

GLN 319 ALA 320 -0.0404

ALA 320 LYS 321 -0.0000

LYS 321 ARG 322 -0.0003

ARG 322 VAL 323 -0.0104

VAL 323 VAL 324 -0.0003

VAL 324 ILE 325 0.0000

ILE 325 ASN 326 -0.0495

ASN 326 LYS 327 0.0003

LYS 327 ASP 328 -0.0002

ASP 328 THR 329 0.0223

THR 329 THR 330 0.0001

THR 330 THR 331 0.0001

THR 331 ILE 332 -0.0054

ILE 332 ILE 333 -0.0001

ILE 333 ASP 334 0.0004

ASP 334 GLY 335 -0.0129

GLY 335 VAL 336 -0.0000

VAL 336 GLY 337 -0.0001

GLY 337 GLU 338 -0.1202

GLU 338 GLU 339 -0.0001

GLU 339 ALA 340 0.0002

ALA 340 ALA 341 -0.2998

ALA 341 ILE 342 -0.0002

ILE 342 GLN 343 -0.0000

GLN 343 GLY 344 -0.1169

GLY 344 ARG 345 0.0002

ARG 345 VAL 346 -0.0003

VAL 346 ALA 347 0.0253

ALA 347 GLN 348 -0.0002

GLN 348 ILE 349 -0.0002

ILE 349 ARG 350 -0.0094

ARG 350 GLN 351 0.0002

GLN 351 GLN 352 -0.0004

GLN 352 ILE 353 0.0456

ILE 353 GLU 354 0.0005

GLU 354 GLU 355 0.0001

GLU 355 ALA 356 -0.0236

ALA 356 THR 357 0.0004

THR 357 SER 358 -0.0002

SER 358 ASP 359 -0.0225

ASP 359 TYR 360 0.0003

TYR 360 ASP 361 0.0000

ASP 361 ARG 362 0.0004

ARG 362 GLU 363 0.0004

GLU 363 LYS 364 0.0003

LYS 364 LEU 365 -0.0139

LEU 365 GLN 366 0.0001

GLN 366 GLU 367 0.0000

GLU 367 ARG 368 -0.1225

ARG 368 VAL 369 0.0004

VAL 369 ALA 370 -0.0001

ALA 370 LYS 371 0.0286

LYS 371 LEU 372 0.0000

LEU 372 ALA 373 0.0003

ALA 373 GLY 374 0.1516

GLY 374 GLY 375 -0.0002

GLY 375 VAL 376 0.0003

VAL 376 ALA 377 -0.1367

ALA 377 VAL 378 0.0001

VAL 378 ILE 379 0.0000

ILE 379 LYS 380 -0.0906

LYS 380 VAL 381 0.0002

VAL 381 GLY 382 0.0000

GLY 382 ALA 383 -0.2194

ALA 383 ALA 384 0.0002

ALA 384 THR 385 -0.0001

THR 385 GLU 386 -0.1101

GLU 386 VAL 387 -0.0002

VAL 387 GLU 388 0.0001

GLU 388 MET 389 -0.0220

MET 389 LYS 390 -0.0001

LYS 390 GLU 391 -0.0002

GLU 391 LYS 392 -0.0055

LYS 392 LYS 393 -0.0001

LYS 393 ALA 394 -0.0001

ALA 394 ARG 395 -0.1154

ARG 395 VAL 396 -0.0001

VAL 396 GLU 397 -0.0002

GLU 397 ASP 398 -0.0361

ASP 398 ALA 399 0.0002

ALA 399 LEU 400 -0.0000

LEU 400 HIS 401 -0.0659

HIS 401 ALA 402 -0.0003

ALA 402 THR 403 -0.0002

THR 403 ARG 404 0.0729

ARG 404 ALA 405 0.0003

ALA 405 ALA 406 0.0005

ALA 406 VAL 407 0.0361

VAL 407 GLU 408 0.0003

GLU 408 GLU 409 0.0002

GLU 409 GLY 410 0.0151

GLY 410 VAL 411 0.0003

VAL 411 VAL 412 -0.0003

VAL 412 ALA 413 -0.0488

ALA 413 GLY 414 -0.0003

GLY 414 GLY 415 0.0001

GLY 415 GLY 416 -0.0040

GLY 416 VAL 417 0.0005

VAL 417 ALA 418 -0.0001

ALA 418 LEU 419 -0.0251

LEU 419 ILE 420 0.0000

ILE 420 ARG 421 -0.0000

ARG 421 VAL 422 -0.0899

VAL 422 ALA 423 -0.0004

ALA 423 SER 424 0.0004

SER 424 LYS 425 -0.1136

LYS 425 LEU 426 0.0001

LEU 426 ALA 427 0.0001

ALA 427 ASP 428 -0.1398

ASP 428 LEU 429 0.0000

LEU 429 ARG 430 0.0001

ARG 430 GLY 431 -0.1723

GLY 431 GLN 432 -0.0002

GLN 432 ASN 433 0.0001

ASN 433 GLU 434 -0.0506

GLU 434 ASP 435 -0.0004

ASP 435 GLN 436 -0.0002

GLN 436 ASN 437 -0.0020

ASN 437 VAL 438 0.0001

VAL 438 GLY 439 -0.0000

GLY 439 ILE 440 0.0105

ILE 440 LYS 441 -0.0002

LYS 441 VAL 442 0.0004

VAL 442 ALA 443 0.0211

ALA 443 LEU 444 -0.0001

LEU 444 ARG 445 0.0000

ARG 445 ALA 446 -0.0817

ALA 446 MET 447 0.0004

MET 447 GLU 448 -0.0000

GLU 448 ALA 449 0.0600

ALA 449 PRO 450 -0.0001

PRO 450 LEU 451 -0.0003

LEU 451 ARG 452 0.0200

ARG 452 GLN 453 -0.0000

GLN 453 ILE 454 0.0000

ILE 454 VAL 455 0.0459

VAL 455 LEU 456 -0.0001

LEU 456 ASN 457 0.0002

ASN 457 CYS 458 -0.0351

CYS 458 GLY 459 -0.0002

GLY 459 GLU 460 0.0002

GLU 460 GLU 461 0.0275

GLU 461 PRO 462 0.0003

PRO 462 SER 463 0.0003

SER 463 VAL 464 0.0055

VAL 464 VAL 465 0.0002

VAL 465 ALA 466 0.0003

ALA 466 ASN 467 0.0125

ASN 467 THR 468 0.0003

THR 468 VAL 469 0.0001

VAL 469 LYS 470 -0.0503

LYS 470 GLY 471 0.0001

GLY 471 GLY 472 0.0001

GLY 472 ASP 473 0.0323

ASP 473 GLY 474 -0.0001

GLY 474 ASN 475 0.0004

ASN 475 TYR 476 0.0044

TYR 476 GLY 477 0.0003

GLY 477 TYR 478 -0.0002

TYR 478 ASN 479 -0.0083

ASN 479 ALA 480 -0.0001

ALA 480 ALA 481 0.0002

ALA 481 THR 482 0.0214

THR 482 GLU 483 -0.0002

GLU 483 GLU 484 0.0002

GLU 484 TYR 485 -0.0509

TYR 485 GLY 486 0.0002

GLY 486 ASN 487 -0.0001

ASN 487 MET 488 0.0087

MET 488 ILE 489 -0.0001

ILE 489 ASP 490 0.0002

ASP 490 MET 491 -0.0230

MET 491 GLY 492 0.0004

GLY 492 ILE 493 -0.0001

ILE 493 LEU 494 0.0989

LEU 494 ASP 495 -0.0002

ASP 495 PRO 496 0.0000

PRO 496 THR 497 0.0708

THR 497 LYS 498 0.0005

LYS 498 VAL 499 -0.0002

VAL 499 THR 500 -0.0208

THR 500 ARG 501 0.0002

ARG 501 SER 502 0.0003

SER 502 ALA 503 -0.0411

ALA 503 LEU 504 -0.0002

LEU 504 GLN 505 0.0002

GLN 505 TYR 506 0.0342

TYR 506 ALA 507 0.0003

ALA 507 ALA 508 0.0001

ALA 508 SER 509 -0.0110

SER 509 VAL 510 -0.0002

VAL 510 ALA 511 0.0001

ALA 511 GLY 512 0.0330

GLY 512 LEU 513 0.0001

LEU 513 MET 514 0.0001

MET 514 ILE 515 0.0231

ILE 515 THR 516 0.0001

THR 516 THR 517 0.0002

THR 517 GLU 518 -0.1990

GLU 518 CYS 519 -0.0001

CYS 519 MET 520 0.0002

MET 520 VAL 521 0.3859

VAL 521 THR 522 0.0002

THR 522 ASP 523 -0.0004

ASP 523 LEU 524 0.0697

LEU 524 PRO 525 -0.0004

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 21 ---

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

* CHAPERONE 1SVT *