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

* CHAPERONE 1SVT *

CA strain for 2404010822081770164

--- normal mode 13 ---

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 -0.0000

ALA 3 LYS 4 0.0001

LYS 4 ASP 5 -0.1742

ASP 5 VAL 6 -0.0004

VAL 6 LYS 7 0.0002

LYS 7 PHE 8 -0.0309

PHE 8 GLY 9 0.0004

GLY 9 ASN 10 -0.0005

ASN 10 ASP 11 0.0004

ASP 11 ALA 12 0.0001

ALA 12 ARG 13 0.0001

ARG 13 VAL 14 0.0816

VAL 14 LYS 15 0.0002

LYS 15 MET 16 0.0002

MET 16 LEU 17 -0.0609

LEU 17 ARG 18 -0.0000

ARG 18 GLY 19 0.0001

GLY 19 VAL 20 -0.0478

VAL 20 ASN 21 0.0002

ASN 21 VAL 22 -0.0001

VAL 22 LEU 23 0.0150

LEU 23 ALA 24 0.0002

ALA 24 ASP 25 -0.0001

ASP 25 ALA 26 0.1012

ALA 26 VAL 27 -0.0000

VAL 27 LYS 28 0.0002

LYS 28 VAL 29 0.0371

VAL 29 THR 30 0.0000

THR 30 LEU 31 -0.0002

LEU 31 GLY 32 0.0128

GLY 32 PRO 33 0.0003

PRO 33 LYS 34 -0.0001

LYS 34 GLY 35 -0.0545

GLY 35 ARG 36 -0.0002

ARG 36 ASN 37 -0.0001

ASN 37 VAL 38 0.0293

VAL 38 VAL 39 -0.0001

VAL 39 LEU 40 0.0003

LEU 40 ASP 41 0.0786

ASP 41 LYS 42 0.0001

LYS 42 SER 43 0.0000

SER 43 PHE 44 0.0589

PHE 44 GLY 45 -0.0003

GLY 45 ALA 46 0.0000

ALA 46 PRO 47 0.0289

PRO 47 THR 48 -0.0001

THR 48 ILE 49 -0.0001

ILE 49 THR 50 0.0012

THR 50 LYS 51 0.0003

LYS 51 ASP 52 0.0000

ASP 52 GLY 53 0.0213

GLY 53 VAL 54 0.0003

VAL 54 SER 55 -0.0001

SER 55 VAL 56 0.0227

VAL 56 ALA 57 -0.0000

ALA 57 ARG 58 0.0000

ARG 58 GLU 59 0.0261

GLU 59 ILE 60 0.0002

ILE 60 GLU 61 -0.0003

GLU 61 LEU 62 0.1025

LEU 62 GLU 63 0.0000

GLU 63 ASP 64 -0.0003

ASP 64 LYS 65 -0.0625

LYS 65 PHE 66 -0.0000

PHE 66 GLU 67 -0.0002

GLU 67 ASN 68 0.0393

ASN 68 MET 69 -0.0002

MET 69 GLY 70 0.0000

GLY 70 ALA 71 0.0375

ALA 71 GLN 72 0.0000

GLN 72 MET 73 -0.0002

MET 73 VAL 74 0.0835

VAL 74 LYS 75 -0.0001

LYS 75 GLU 76 0.0001

GLU 76 VAL 77 0.0875

VAL 77 ALA 78 0.0000

ALA 78 SER 79 -0.0001

SER 79 LYS 80 -0.0031

LYS 80 ALA 81 0.0004

ALA 81 ASN 82 -0.0002

ASN 82 ASP 83 -0.0121

ASP 83 ALA 84 -0.0003

ALA 84 ALA 85 0.0001

ALA 85 GLY 86 -0.0134

GLY 86 ASP 87 -0.0001

ASP 87 GLY 88 0.0003

GLY 88 THR 89 0.0043

THR 89 THR 90 0.0003

THR 90 THR 91 0.0002

THR 91 ALA 92 0.0200

ALA 92 THR 93 0.0002

THR 93 VAL 94 -0.0002

VAL 94 LEU 95 0.0654

LEU 95 ALA 96 -0.0006

ALA 96 GLN 97 0.0001

GLN 97 ALA 98 0.0089

ALA 98 ILE 99 -0.0004

ILE 99 ILE 100 -0.0003

ILE 100 THR 101 -0.0191

THR 101 GLU 102 0.0001

GLU 102 GLY 103 -0.0000

GLY 103 LEU 104 -0.0718

LEU 104 LYS 105 -0.0001

LYS 105 ALA 106 -0.0002

ALA 106 VAL 107 -0.0414

VAL 107 ALA 108 -0.0001

ALA 108 ALA 109 0.0002

ALA 109 GLY 110 0.0632

GLY 110 MET 111 -0.0001

MET 111 ASN 112 -0.0001

ASN 112 PRO 113 -0.0235

PRO 113 MET 114 0.0002

MET 114 ASP 115 0.0001

ASP 115 LEU 116 -0.0031

LEU 116 LYS 117 -0.0003

LYS 117 ARG 118 -0.0003

ARG 118 GLY 119 0.0768

GLY 119 ILE 120 -0.0005

ILE 120 ASP 121 -0.0001

ASP 121 LYS 122 0.0958

LYS 122 ALA 123 -0.0002

ALA 123 VAL 124 -0.0002

VAL 124 THR 125 0.0274

THR 125 ALA 126 0.0006

ALA 126 ALA 127 0.0001

ALA 127 VAL 128 -0.0369

VAL 128 GLU 129 0.0002

GLU 129 GLU 130 -0.0002

GLU 130 LEU 131 -0.0357

LEU 131 LYS 132 0.0003

LYS 132 ALA 133 -0.0002

ALA 133 LEU 134 -0.0052

LEU 134 SER 135 -0.0004

SER 135 VAL 136 0.0001

VAL 136 PRO 137 -0.0192

PRO 137 CYS 138 0.0002

CYS 138 SER 139 0.0001

SER 139 ASP 140 0.0738

ASP 140 SER 141 -0.0003

SER 141 LYS 142 0.0000

LYS 142 ALA 143 -0.0353

ALA 143 ILE 144 0.0003

ILE 144 ALA 145 -0.0001

ALA 145 GLN 146 0.1112

GLN 146 VAL 147 -0.0002

VAL 147 GLY 148 -0.0002

GLY 148 THR 149 -0.0251

THR 149 ILE 150 -0.0002

ILE 150 SER 151 0.0001

SER 151 ALA 152 -0.0157

ALA 152 ASN 153 0.0003

ASN 153 SER 154 0.0001

SER 154 ASP 155 0.0943

ASP 155 GLU 156 -0.0002

GLU 156 THR 157 0.0004

THR 157 VAL 158 -0.0109

VAL 158 GLY 159 0.0003

GLY 159 LYS 160 0.0001

LYS 160 LEU 161 -0.0291

LEU 161 ILE 162 0.0002

ILE 162 ALA 163 0.0000

ALA 163 GLU 164 0.0370

GLU 164 ALA 165 -0.0000

ALA 165 MET 166 -0.0001

MET 166 ASP 167 -0.1324

ASP 167 LYS 168 0.0003

LYS 168 VAL 169 -0.0002

VAL 169 GLY 170 -0.0485

GLY 170 LYS 171 -0.0000

LYS 171 GLU 172 -0.0003

GLU 172 GLY 173 -0.0760

GLY 173 VAL 174 0.0001

VAL 174 ILE 175 0.0001

ILE 175 THR 176 -0.0761

THR 176 VAL 177 -0.0002

VAL 177 GLU 178 -0.0002

GLU 178 ASP 179 -0.0334

ASP 179 GLY 180 -0.0002

GLY 180 THR 181 0.0001

THR 181 GLY 182 0.0037

GLY 182 LEU 183 -0.0003

LEU 183 GLN 184 0.0002

GLN 184 ASP 185 -0.0069

ASP 185 GLU 186 -0.0001

GLU 186 LEU 187 0.0001

LEU 187 ASP 188 0.0440

ASP 188 VAL 189 0.0001

VAL 189 VAL 190 -0.0002

VAL 190 GLU 191 -0.0676

GLU 191 GLY 192 0.0000

GLY 192 MET 193 -0.0000

MET 193 GLN 194 0.0518

GLN 194 PHE 195 -0.0000

PHE 195 ASP 196 0.0001

ASP 196 ARG 197 0.0480

ARG 197 GLY 198 0.0002

GLY 198 TYR 199 -0.0002

TYR 199 LEU 200 0.0179

LEU 200 SER 201 -0.0001

SER 201 PRO 202 0.0000

PRO 202 TYR 203 -0.0025

TYR 203 PHE 204 -0.0002

PHE 204 ILE 205 -0.0001

ILE 205 ASN 206 -0.0031

ASN 206 LYS 207 -0.0001

LYS 207 PRO 208 0.0002

PRO 208 GLU 209 -0.0014

GLU 209 THR 210 0.0005

THR 210 GLY 211 0.0005

GLY 211 ALA 212 0.0063

ALA 212 VAL 213 0.0001

VAL 213 GLU 214 -0.0003

GLU 214 LEU 215 -0.0012

LEU 215 GLU 216 0.0004

GLU 216 SER 217 -0.0004

SER 217 PRO 218 -0.0091

PRO 218 PHE 219 -0.0001

PHE 219 ILE 220 0.0001

ILE 220 LEU 221 -0.0064

LEU 221 LEU 222 -0.0003

LEU 222 ALA 223 -0.0001

ALA 223 ASP 224 -0.0057

ASP 224 LYS 225 -0.0000

LYS 225 LYS 226 -0.0005

LYS 226 ILE 227 0.0067

ILE 227 SER 228 0.0001

SER 228 ASN 229 0.0002

ASN 229 ILE 230 -0.0006

ILE 230 ARG 231 0.0000

ARG 231 GLU 232 0.0002

GLU 232 MET 233 -0.0011

MET 233 LEU 234 -0.0002

LEU 234 PRO 235 -0.0001

PRO 235 VAL 236 0.0033

VAL 236 LEU 237 -0.0001

LEU 237 GLU 238 -0.0000

GLU 238 ALA 239 0.0011

ALA 239 VAL 240 -0.0001

VAL 240 ALA 241 -0.0001

ALA 241 LYS 242 -0.0014

LYS 242 ALA 243 -0.0000

ALA 243 GLY 244 0.0002

GLY 244 LYS 245 -0.0053

LYS 245 PRO 246 -0.0001

PRO 246 LEU 247 0.0001

LEU 247 LEU 248 -0.0052

LEU 248 ILE 249 0.0003

ILE 249 ILE 250 0.0000

ILE 250 ALA 251 0.0018

ALA 251 GLU 252 0.0001

GLU 252 ASP 253 -0.0000

ASP 253 VAL 254 0.0020

VAL 254 GLU 255 0.0001

GLU 255 GLY 256 0.0000

GLY 256 GLU 257 -0.0056

GLU 257 ALA 258 0.0002

ALA 258 LEU 259 -0.0005

LEU 259 ALA 260 0.0037

ALA 260 THR 261 -0.0003

THR 261 LEU 262 0.0001

LEU 262 VAL 263 -0.0024

VAL 263 VAL 264 0.0004

VAL 264 ASN 265 -0.0004

ASN 265 THR 266 -0.0004

THR 266 MET 267 0.0000

MET 267 ARG 268 -0.0001

ARG 268 GLY 269 0.0013

GLY 269 ILE 270 -0.0001

ILE 270 VAL 271 -0.0000

VAL 271 LYS 272 -0.0028

LYS 272 VAL 273 -0.0001

VAL 273 ALA 274 0.0000

ALA 274 ALA 275 -0.0086

ALA 275 VAL 276 -0.0001

VAL 276 LYS 277 0.0000

LYS 277 ALA 278 -0.0280

ALA 278 PRO 279 -0.0002

PRO 279 GLY 280 0.0002

GLY 280 PHE 281 0.0161

PHE 281 GLY 282 -0.0001

GLY 282 ASP 283 0.0001

ASP 283 ARG 284 0.0179

ARG 284 ARG 285 -0.0003

ARG 285 LYS 286 0.0001

LYS 286 ALA 287 0.0043

ALA 287 MET 288 -0.0002

MET 288 LEU 289 -0.0003

LEU 289 GLN 290 -0.0233

GLN 290 ASP 291 -0.0001

ASP 291 ILE 292 0.0002

ILE 292 ALA 293 0.0057

ALA 293 THR 294 -0.0002

THR 294 LEU 295 -0.0001

LEU 295 THR 296 0.0271

THR 296 GLY 297 0.0002

GLY 297 GLY 298 0.0001

GLY 298 THR 299 -0.0278

THR 299 VAL 300 0.0001

VAL 300 ILE 301 0.0001

ILE 301 SER 302 -0.0201

SER 302 GLU 303 -0.0002

GLU 303 GLU 304 0.0001

GLU 304 ILE 305 0.0097

ILE 305 GLY 306 0.0002

GLY 306 MET 307 -0.0001

MET 307 GLU 308 -0.0090

GLU 308 LEU 309 0.0002

LEU 309 GLU 310 0.0001

GLU 310 LYS 311 -0.0086

LYS 311 ALA 312 -0.0000

ALA 312 THR 313 -0.0002

THR 313 LEU 314 -0.0118

LEU 314 GLU 315 0.0002

GLU 315 ASP 316 0.0000

ASP 316 LEU 317 -0.0073

LEU 317 GLY 318 -0.0001

GLY 318 GLN 319 0.0004

GLN 319 ALA 320 -0.0077

ALA 320 LYS 321 -0.0002

LYS 321 ARG 322 -0.0001

ARG 322 VAL 323 -0.0037

VAL 323 VAL 324 0.0000

VAL 324 ILE 325 -0.0001

ILE 325 ASN 326 -0.0002

ASN 326 LYS 327 -0.0004

LYS 327 ASP 328 0.0002

ASP 328 THR 329 0.0227

THR 329 THR 330 0.0001

THR 330 THR 331 -0.0004

THR 331 ILE 332 0.0079

ILE 332 ILE 333 -0.0002

ILE 333 ASP 334 -0.0002

ASP 334 GLY 335 -0.0027

GLY 335 VAL 336 -0.0001

VAL 336 GLY 337 -0.0000

GLY 337 GLU 338 -0.0110

GLU 338 GLU 339 0.0001

GLU 339 ALA 340 -0.0003

ALA 340 ALA 341 -0.0351

ALA 341 ILE 342 0.0002

ILE 342 GLN 343 -0.0002

GLN 343 GLY 344 -0.0229

GLY 344 ARG 345 0.0002

ARG 345 VAL 346 -0.0001

VAL 346 ALA 347 0.0038

ALA 347 GLN 348 0.0001

GLN 348 ILE 349 -0.0002

ILE 349 ARG 350 -0.0144

ARG 350 GLN 351 0.0000

GLN 351 GLN 352 0.0003

GLN 352 ILE 353 0.0005

ILE 353 GLU 354 -0.0001

GLU 354 GLU 355 -0.0002

GLU 355 ALA 356 -0.0030

ALA 356 THR 357 0.0000

THR 357 SER 358 -0.0000

SER 358 ASP 359 0.0110

ASP 359 TYR 360 0.0001

TYR 360 ASP 361 0.0000

ASP 361 ARG 362 0.0057

ARG 362 GLU 363 -0.0000

GLU 363 LYS 364 -0.0002

LYS 364 LEU 365 -0.0027

LEU 365 GLN 366 0.0001

GLN 366 GLU 367 0.0000

GLU 367 ARG 368 0.0380

ARG 368 VAL 369 0.0001

VAL 369 ALA 370 -0.0000

ALA 370 LYS 371 0.0570

LYS 371 LEU 372 0.0000

LEU 372 ALA 373 -0.0001

ALA 373 GLY 374 0.0032

GLY 374 GLY 375 -0.0001

GLY 375 VAL 376 0.0003

VAL 376 ALA 377 0.0339

ALA 377 VAL 378 -0.0001

VAL 378 ILE 379 0.0004

ILE 379 LYS 380 -0.0031

LYS 380 VAL 381 -0.0004

VAL 381 GLY 382 0.0000

GLY 382 ALA 383 0.0208

ALA 383 ALA 384 -0.0001

ALA 384 THR 385 0.0001

THR 385 GLU 386 0.0270

GLU 386 VAL 387 -0.0000

VAL 387 GLU 388 -0.0000

GLU 388 MET 389 -0.0340

MET 389 LYS 390 0.0000

LYS 390 GLU 391 0.0004

GLU 391 LYS 392 0.0135

LYS 392 LYS 393 -0.0003

LYS 393 ALA 394 0.0002

ALA 394 ARG 395 -0.0178

ARG 395 VAL 396 -0.0000

VAL 396 GLU 397 0.0004

GLU 397 ASP 398 -0.0014

ASP 398 ALA 399 -0.0002

ALA 399 LEU 400 -0.0001

LEU 400 HIS 401 -0.0479

HIS 401 ALA 402 0.0002

ALA 402 THR 403 -0.0005

THR 403 ARG 404 0.0466

ARG 404 ALA 405 -0.0004

ALA 405 ALA 406 0.0005

ALA 406 VAL 407 -0.0034

VAL 407 GLU 408 -0.0001

GLU 408 GLU 409 -0.0002

GLU 409 GLY 410 0.0548

GLY 410 VAL 411 0.0001

VAL 411 VAL 412 0.0002

VAL 412 ALA 413 0.0348

ALA 413 GLY 414 0.0000

GLY 414 GLY 415 0.0001

GLY 415 GLY 416 0.0175

GLY 416 VAL 417 0.0001

VAL 417 ALA 418 -0.0002

ALA 418 LEU 419 0.0054

LEU 419 ILE 420 -0.0004

ILE 420 ARG 421 -0.0000

ARG 421 VAL 422 0.0401

VAL 422 ALA 423 0.0003

ALA 423 SER 424 -0.0003

SER 424 LYS 425 0.0395

LYS 425 LEU 426 0.0003

LEU 426 ALA 427 0.0002

ALA 427 ASP 428 0.0738

ASP 428 LEU 429 0.0000

LEU 429 ARG 430 -0.0001

ARG 430 GLY 431 0.1034

GLY 431 GLN 432 0.0001

GLN 432 ASN 433 0.0003

ASN 433 GLU 434 0.0028

GLU 434 ASP 435 0.0001

ASP 435 GLN 436 0.0003

GLN 436 ASN 437 0.0110

ASN 437 VAL 438 0.0004

VAL 438 GLY 439 0.0003

GLY 439 ILE 440 0.0049

ILE 440 LYS 441 0.0001

LYS 441 VAL 442 -0.0003

VAL 442 ALA 443 -0.0442

ALA 443 LEU 444 0.0000

LEU 444 ARG 445 -0.0002

ARG 445 ALA 446 0.1117

ALA 446 MET 447 -0.0001

MET 447 GLU 448 -0.0002

GLU 448 ALA 449 -0.0109

ALA 449 PRO 450 -0.0002

PRO 450 LEU 451 -0.0002

LEU 451 ARG 452 -0.0471

ARG 452 GLN 453 0.0001

GLN 453 ILE 454 -0.0001

ILE 454 VAL 455 -0.0050

VAL 455 LEU 456 0.0001

LEU 456 ASN 457 0.0001

ASN 457 CYS 458 -0.0679

CYS 458 GLY 459 -0.0002

GLY 459 GLU 460 -0.0001

GLU 460 GLU 461 0.0394

GLU 461 PRO 462 -0.0002

PRO 462 SER 463 -0.0001

SER 463 VAL 464 0.0009

VAL 464 VAL 465 0.0002

VAL 465 ALA 466 0.0001

ALA 466 ASN 467 -0.0199

ASN 467 THR 468 0.0000

THR 468 VAL 469 0.0001

VAL 469 LYS 470 0.0135

LYS 470 GLY 471 0.0001

GLY 471 GLY 472 -0.0004

GLY 472 ASP 473 -0.0017

ASP 473 GLY 474 0.0000

GLY 474 ASN 475 -0.0001

ASN 475 TYR 476 -0.0108

TYR 476 GLY 477 -0.0001

GLY 477 TYR 478 -0.0002

TYR 478 ASN 479 0.0105

ASN 479 ALA 480 -0.0003

ALA 480 ALA 481 0.0001

ALA 481 THR 482 -0.0039

THR 482 GLU 483 0.0002

GLU 483 GLU 484 0.0003

GLU 484 TYR 485 -0.0109

TYR 485 GLY 486 -0.0002

GLY 486 ASN 487 0.0001

ASN 487 MET 488 0.0118

MET 488 ILE 489 -0.0001

ILE 489 ASP 490 -0.0003

ASP 490 MET 491 -0.0306

MET 491 GLY 492 0.0001

GLY 492 ILE 493 0.0003

ILE 493 LEU 494 0.0361

LEU 494 ASP 495 0.0002

ASP 495 PRO 496 -0.0004

PRO 496 THR 497 -0.0526

THR 497 LYS 498 0.0000

LYS 498 VAL 499 -0.0002

VAL 499 THR 500 -0.0259

THR 500 ARG 501 -0.0001

ARG 501 SER 502 -0.0002

SER 502 ALA 503 -0.0094

ALA 503 LEU 504 0.0001

LEU 504 GLN 505 -0.0001

GLN 505 TYR 506 0.0440

TYR 506 ALA 507 -0.0001

ALA 507 ALA 508 0.0000

ALA 508 SER 509 0.0582

SER 509 VAL 510 -0.0003

VAL 510 ALA 511 -0.0001

ALA 511 GLY 512 -0.0339

GLY 512 LEU 513 0.0002

LEU 513 MET 514 -0.0002

MET 514 ILE 515 -0.0198

ILE 515 THR 516 -0.0000

THR 516 THR 517 -0.0001

THR 517 GLU 518 0.1298

GLU 518 CYS 519 0.0002

CYS 519 MET 520 -0.0001

MET 520 VAL 521 0.1706

VAL 521 THR 522 0.0003

THR 522 ASP 523 0.0001

ASP 523 LEU 524 0.0346

LEU 524 PRO 525 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).
Last modification: April 25th, 2023.

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

*** CHAPERONE 1SVT ***

CA strain for 2404010822081770164

--- normal mode 13 ---

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

* CHAPERONE 1SVT *