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

* Xhaly *

CA strain for 22042218234111840

--- normal mode 8 ---

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
HIS 11 MET 12 -0.0005

MET 12 ARG 13 -0.0002

ARG 13 TYR 14 0.0006

TYR 14 SER 15 -0.0002

SER 15 GLU 16 0.0004

GLU 16 LEU 17 -0.0030

LEU 17 ALA 18 0.0002

ALA 18 GLU 19 0.0000

GLU 19 LEU 20 -0.0028

LEU 20 TYR 21 0.0001

TYR 21 ARG 22 -0.0001

ARG 22 ARG 23 0.0021

ARG 23 LEU 24 0.0000

LEU 24 GLU 25 0.0001

GLU 25 LYS 26 -0.0041

LYS 26 THR 27 -0.0002

THR 27 THR 28 0.0003

THR 28 LEU 29 0.0033

LEU 29 LYS 30 -0.0002

LYS 30 THR 31 0.0005

THR 31 LEU 32 -0.0001

LEU 32 LYS 33 -0.0000

LYS 33 THR 34 -0.0001

THR 34 LYS 35 -0.0082

LYS 35 PHE 36 -0.0001

PHE 36 VAL 37 -0.0003

VAL 37 ALA 38 0.0071

ALA 38 ASP 39 0.0003

ASP 39 PHE 40 -0.0005

PHE 40 LEU 41 0.0017

LEU 41 LYS 42 0.0001

LYS 42 LYS 43 0.0000

LYS 43 THR 44 0.0036

THR 44 PRO 45 0.0000

PRO 45 ASP 46 0.0000

ASP 46 ASP 47 -0.0054

ASP 47 LEU 48 0.0002

LEU 48 LEU 49 -0.0002

LEU 49 GLU 50 0.0130

GLU 50 ILE 51 0.0003

ILE 51 VAL 52 -0.0004

VAL 52 PRO 53 -0.0102

PRO 53 TYR 54 -0.0002

TYR 54 LEU 55 0.0001

LEU 55 ILE 56 0.0016

ILE 56 LEU 57 -0.0004

LEU 57 GLY 58 -0.0002

GLY 58 LYS 59 -0.0194

LYS 59 VAL 60 -0.0001

VAL 60 PHE 61 0.0001

PHE 61 PRO 62 -0.0064

PRO 62 ASP 63 0.0003

ASP 63 TRP 64 0.0005

TRP 64 ASP 65 -0.0073

ASP 65 GLU 66 -0.0000

GLU 66 ARG 67 -0.0002

ARG 67 GLU 68 -0.0507

GLU 68 LEU 69 -0.0003

LEU 69 GLY 70 0.0003

GLY 70 VAL 71 -0.0218

VAL 71 GLY 72 0.0004

GLY 72 GLU 73 -0.0000

GLU 73 LYS 74 0.0011

LYS 74 LEU 75 0.0002

LEU 75 LEU 76 0.0002

LEU 76 ILE 77 -0.0026

ILE 77 LYS 78 -0.0002

LYS 78 ALA 79 -0.0003

ALA 79 VAL 80 0.0008

VAL 80 SER 81 0.0001

SER 81 MET 82 -0.0002

MET 82 ALA 83 -0.0026

ALA 83 THR 84 -0.0002

THR 84 GLY 85 0.0001

GLY 85 VAL 86 -0.0007

VAL 86 PRO 87 -0.0001

PRO 87 GLU 88 0.0004

GLU 88 LYS 89 -0.0012

LYS 89 GLU 90 0.0001

GLU 90 ILE 91 0.0001

ILE 91 GLU 92 0.0003

GLU 92 ASN 93 0.0002

ASN 93 SER 94 0.0003

SER 94 ILE 95 0.0001

ILE 95 LYS 96 0.0004

LYS 96 ASP 97 0.0003

ASP 97 THR 98 0.0002

THR 98 GLY 99 0.0001

GLY 99 ASP 100 -0.0000

ASP 100 LEU 101 -0.0023

LEU 101 GLY 102 0.0000

GLY 102 GLU 103 -0.0004

GLU 103 SER 104 0.0050

SER 104 VAL 105 0.0001

VAL 105 ALA 106 0.0004

ALA 106 LEU 107 0.0000

LEU 107 ALA 108 0.0000

ALA 108 LEU 109 -0.0000

LEU 109 LYS 110 0.0001

LYS 110 LYS 111 0.0002

LYS 111 ARG 112 -0.0003

ARG 112 ARG 113 0.0007

ARG 113 GLN 114 -0.0000

GLN 114 LYS 115 0.0002

LYS 115 SER 116 -0.0069

SER 116 PHE 117 0.0004

PHE 117 PHE 118 0.0003

PHE 118 SER 119 -0.0166

SER 119 GLN 120 0.0002

GLN 120 PRO 121 -0.0000

PRO 121 LEU 122 -0.0072

LEU 122 THR 123 -0.0001

THR 123 ILE 124 -0.0001

ILE 124 LYS 125 0.0081

LYS 125 ARG 126 -0.0003

ARG 126 VAL 127 -0.0001

VAL 127 TYR 128 0.0229

TYR 128 ASN 129 0.0001

ASN 129 THR 130 0.0001

THR 130 PHE 131 0.0155

PHE 131 VAL 132 -0.0000

VAL 132 LYS 133 -0.0001

LYS 133 VAL 134 -0.0041

VAL 134 ALA 135 0.0003

ALA 135 GLU 136 -0.0002

GLU 136 ALA 137 0.0020

ALA 137 SER 138 0.0001

SER 138 GLY 139 -0.0001

GLY 139 GLU 140 0.0014

GLU 140 GLY 141 -0.0003

GLY 141 SER 142 0.0001

SER 142 GLN 143 0.0014

GLN 143 ASP 144 0.0000

ASP 144 ARG 145 -0.0002

ARG 145 LYS 146 -0.0009

LYS 146 MET 147 -0.0001

MET 147 LYS 148 0.0003

LYS 148 TYR 149 -0.0030

TYR 149 LEU 150 0.0000

LEU 150 ALA 151 -0.0004

ALA 151 ASN 152 -0.0101

ASN 152 LEU 153 0.0002

LEU 153 PHE 154 0.0001

PHE 154 MET 155 0.0019

MET 155 ASP 156 0.0004

ASP 156 ALA 157 -0.0003

ALA 157 GLY 158 0.0043

GLY 158 PRO 159 0.0002

PRO 159 GLU 160 -0.0001

GLU 160 GLU 161 -0.0010

GLU 161 GLY 162 -0.0003

GLY 162 LYS 163 -0.0003

LYS 163 TYR 164 0.0014

TYR 164 ILE 165 0.0000

ILE 165 ALA 166 -0.0004

ALA 166 ARG 167 0.0018

ARG 167 THR 168 -0.0001

THR 168 VAL 169 -0.0000

VAL 169 LEU 170 -0.0007

LEU 170 GLY 171 0.0001

GLY 171 THR 172 -0.0004

THR 172 MET 173 0.0124

MET 173 ARG 174 -0.0004

ARG 174 THR 175 0.0001

THR 175 GLY 176 0.0086

GLY 176 VAL 177 -0.0002

VAL 177 ALA 178 -0.0002

ALA 178 GLU 179 -0.0030

GLU 179 GLY 180 0.0002

GLY 180 ILE 181 0.0001

ILE 181 LEU 182 -0.0008

LEU 182 ARG 183 -0.0001

ARG 183 ASP 184 0.0002

ASP 184 ALA 185 -0.0124

ALA 185 ILE 186 0.0002

ILE 186 ALA 187 0.0000

ALA 187 GLU 188 -0.0057

GLU 188 ALA 189 -0.0002

ALA 189 PHE 190 0.0001

PHE 190 LYS 191 -0.0135

LYS 191 VAL 192 -0.0000

VAL 192 LYS 193 0.0002

LYS 193 VAL 194 -0.0049

VAL 194 GLU 195 -0.0001

GLU 195 LEU 196 -0.0001

LEU 196 VAL 197 0.0062

VAL 197 GLU 198 0.0001

GLU 198 ARG 199 0.0002

ARG 199 ALA 200 0.0290

ALA 200 TYR 201 0.0003

TYR 201 MET 202 0.0001

MET 202 LEU 203 0.0216

LEU 203 THR 204 -0.0005

THR 204 SER 205 -0.0004

SER 205 ASP 206 -0.0141

ASP 206 PHE 207 0.0002

PHE 207 GLY 208 -0.0000

GLY 208 TYR 209 -0.0108

TYR 209 VAL 210 -0.0000

VAL 210 ALA 211 -0.0003

ALA 211 LYS 212 -0.0175

LYS 212 ILE 213 0.0000

ILE 213 ALA 214 0.0001

ALA 214 LYS 215 -0.0124

LYS 215 LEU 216 0.0003

LEU 216 GLU 217 -0.0001

GLU 217 GLY 218 -0.0064

GLY 218 ASN 219 0.0003

ASN 219 GLU 220 0.0003

GLU 220 GLY 221 0.0039

GLY 221 LEU 222 0.0005

LEU 222 SER 223 -0.0001

SER 223 LYS 224 0.0285

LYS 224 VAL 225 0.0002

VAL 225 SER 226 -0.0001

SER 226 ILE 227 0.0491

ILE 227 GLN 228 0.0000

GLN 228 ILE 229 0.0004

ILE 229 GLY 230 0.0005

GLY 230 LYS 231 -0.0002

LYS 231 PRO 232 0.0003

PRO 232 ILE 233 -0.0129

ILE 233 ARG 234 -0.0001

ARG 234 PRO 235 -0.0002

PRO 235 MET 236 -0.0382

MET 236 LEU 237 -0.0002

LEU 237 ALA 238 0.0004

ALA 238 GLN 239 -0.0198

GLN 239 ASN 240 0.0001

ASN 240 ALA 241 -0.0004

ALA 241 ALA 242 -0.0024

ALA 242 SER 243 -0.0002

SER 243 VAL 244 -0.0003

VAL 244 LYS 245 0.0261

LYS 245 ASP 246 -0.0001

ASP 246 ALA 247 -0.0002

ALA 247 LEU 248 -0.0027

LEU 248 ILE 249 0.0001

ILE 249 GLU 250 0.0004

GLU 250 MET 251 -0.0348

MET 251 GLY 252 0.0002

GLY 252 GLY 253 -0.0001

GLY 253 GLU 254 -0.0054

GLU 254 ALA 255 0.0003

ALA 255 ALA 256 0.0001

ALA 256 PHE 257 -0.0031

PHE 257 GLU 258 -0.0003

GLU 258 ILE 259 0.0002

ILE 259 LYS 260 -0.0043

LYS 260 TYR 261 -0.0001

TYR 261 ASP 262 -0.0001

ASP 262 GLY 263 0.0123

GLY 263 ALA 264 0.0002

ALA 264 ARG 265 -0.0001

ARG 265 VAL 266 0.0116

VAL 266 GLN 267 0.0001

GLN 267 VAL 268 -0.0001

VAL 268 HIS 269 0.0144

HIS 269 ARG 270 -0.0003

ARG 270 ASP 271 -0.0000

ASP 271 GLY 272 0.0082

GLY 272 ASP 273 0.0004

ASP 273 LYS 274 -0.0005

LYS 274 VAL 275 -0.0078

VAL 275 ILE 276 0.0001

ILE 276 ILE 277 0.0002

ILE 277 TYR 278 -0.0207

TYR 278 SER 279 0.0002

SER 279 ARG 280 0.0001

ARG 280 ARG 281 -0.0046

ARG 281 LEU 282 0.0001

LEU 282 GLU 283 -0.0002

GLU 283 ASN 284 0.0064

ASN 284 VAL 285 -0.0003

VAL 285 THR 286 0.0001

THR 286 ARG 287 -0.0133

ARG 287 SER 288 -0.0003

SER 288 ILE 289 0.0002

ILE 289 PRO 290 -0.0142

PRO 290 GLU 291 0.0003

GLU 291 ILE 292 0.0004

ILE 292 VAL 293 0.0110

VAL 293 GLU 294 0.0002

GLU 294 ALA 295 -0.0001

ALA 295 VAL 296 0.0014

VAL 296 LYS 297 0.0000

LYS 297 ALA 298 0.0001

ALA 298 SER 299 -0.0026

SER 299 LEU 300 -0.0003

LEU 300 LYS 301 0.0004

LYS 301 PRO 302 0.0135

PRO 302 SER 303 0.0001

SER 303 LYS 304 0.0002

LYS 304 VAL 305 -0.0043

VAL 305 ILE 306 -0.0000

ILE 306 VAL 307 -0.0006

VAL 307 GLU 308 0.0032

GLU 308 GLY 309 -0.0003

GLY 309 GLU 310 0.0002

GLU 310 LEU 311 -0.0068

LEU 311 VAL 312 0.0003

VAL 312 ALA 313 0.0000

ALA 313 VAL 314 -0.0103

VAL 314 GLY 315 -0.0001

GLY 315 GLU 316 -0.0001

GLU 316 ASN 317 -0.0005

ASN 317 GLY 318 0.0001

GLY 318 ARG 319 0.0002

ARG 319 PRO 320 -0.0092

PRO 320 ARG 321 0.0001

ARG 321 PRO 322 0.0002

PRO 322 PHE 323 -0.0019

PHE 323 GLN 324 0.0002

GLN 324 TYR 325 -0.0000

TYR 325 VAL 326 -0.0030

VAL 326 LEU 327 0.0001

LEU 327 ARG 328 0.0004

ARG 328 ARG 329 0.0023

ARG 329 PHE 330 0.0001

PHE 330 ARG 331 0.0003

ARG 331 ARG 332 -0.0023

ARG 332 LYS 333 0.0002

LYS 333 TYR 334 0.0001

TYR 334 ASN 335 -0.0017

ASN 335 ILE 336 0.0000

ILE 336 GLU 337 -0.0000

GLU 337 GLU 338 0.0000

GLU 338 MET 339 -0.0000

MET 339 ILE 340 -0.0003

ILE 340 GLU 341 0.0015

GLU 341 LYS 342 0.0001

LYS 342 ILE 343 -0.0003

ILE 343 PRO 344 -0.0106

PRO 344 LEU 345 0.0000

LEU 345 GLU 346 0.0002

GLU 346 LEU 347 -0.0105

LEU 347 ASN 348 -0.0001

ASN 348 LEU 349 0.0001

LEU 349 PHE 350 -0.0172

PHE 350 ASP 351 -0.0001

ASP 351 ILE 352 0.0000

ILE 352 LEU 353 0.0030

LEU 353 TYR 354 -0.0001

TYR 354 VAL 355 -0.0001

VAL 355 ASN 356 -0.0075

ASN 356 GLY 357 0.0004

GLY 357 GLU 358 -0.0002

GLU 358 SER 359 -0.0112

SER 359 LEU 360 0.0001

LEU 360 ILE 361 0.0001

ILE 361 ASP 362 0.0005

ASP 362 THR 363 0.0004

THR 363 LYS 364 0.0001

LYS 364 PHE 365 0.0054

PHE 365 THR 366 -0.0000

THR 366 GLU 367 0.0002

GLU 367 ARG 368 -0.0004

ARG 368 ARG 369 -0.0001

ARG 369 LYS 370 0.0000

LYS 370 ARG 371 0.0058

ARG 371 LEU 372 -0.0004

LEU 372 GLU 373 0.0002

GLU 373 GLU 374 0.0022

GLU 374 SER 375 -0.0000

SER 375 VAL 376 0.0002

VAL 376 GLU 377 -0.0072

GLU 377 GLU 378 0.0001

GLU 378 SER 379 -0.0002

SER 379 ASP 380 0.0017

ASP 380 LYS 381 -0.0002

LYS 381 ILE 382 -0.0003

ILE 382 LYS 383 0.0089

LYS 383 LEU 384 0.0004

LEU 384 ALA 385 -0.0004

ALA 385 GLU 386 0.0000

GLU 386 GLN 387 -0.0002

GLN 387 LEU 388 -0.0001

LEU 388 VAL 389 -0.0006

VAL 389 THR 390 -0.0001

THR 390 LYS 391 -0.0001

LYS 391 LYS 392 -0.0022

LYS 392 VAL 393 -0.0001

VAL 393 ASP 394 -0.0002

ASP 394 GLU 395 0.0039

GLU 395 ALA 396 0.0001

ALA 396 GLU 397 -0.0002

GLU 397 GLU 398 0.0171

GLU 398 PHE 399 -0.0003

PHE 399 TYR 400 0.0001

TYR 400 LYS 401 0.0000

LYS 401 ARG 402 0.0002

ARG 402 ALA 403 -0.0002

ALA 403 LEU 404 -0.0041

LEU 404 GLU 405 0.0001

GLU 405 LEU 406 0.0001

LEU 406 GLY 407 -0.0040

GLY 407 HIS 408 -0.0003

HIS 408 GLU 409 0.0004

GLU 409 GLY 410 0.0157

GLY 410 LEU 411 0.0001

LEU 411 MET 412 0.0000

MET 412 ALA 413 0.0077

ALA 413 LYS 414 0.0000

LYS 414 ARG 415 0.0001

ARG 415 LEU 416 -0.0063

LEU 416 ASP 417 0.0001

ASP 417 ALA 418 -0.0000

ALA 418 ILE 419 -0.0107

ILE 419 TYR 420 -0.0001

TYR 420 GLU 421 0.0004

GLU 421 PRO 422 -0.0158

PRO 422 GLY 423 0.0001

GLY 423 ASN 424 -0.0002

ASN 424 ARG 425 -0.0801

ARG 425 GLY 426 0.0004

GLY 426 LYS 427 -0.0005

LYS 427 LYS 428 -0.0496

LYS 428 TRP 429 0.0003

TRP 429 LEU 430 0.0001

LEU 430 LYS 431 0.0035

LYS 431 ILE 432 0.0003

ILE 432 LYS 433 -0.0000

LYS 433 PRO 434 -0.0399

PRO 434 THR 435 0.0002

THR 435 MET 436 0.0001

MET 436 GLU 437 0.1177

GLU 437 ASN 438 0.0001

ASN 438 LEU 439 0.0001

LEU 439 ASP 440 0.0527

ASP 440 LEU 441 -0.0001

LEU 441 VAL 442 0.0001

VAL 442 ILE 443 0.0150

ILE 443 ILE 444 -0.0000

ILE 444 GLY 445 0.0003

GLY 445 ALA 446 0.0132

ALA 446 GLU 447 0.0002

GLU 447 TRP 448 0.0000

TRP 448 GLY 449 0.0033

GLY 449 GLU 450 -0.0000

GLU 450 GLY 451 0.0000

GLY 451 ARG 452 -0.0092

ARG 452 ARG 453 0.0002

ARG 453 ALA 454 -0.0001

ALA 454 HIS 455 0.0023

HIS 455 LEU 456 0.0001

LEU 456 LEU 457 -0.0002

LEU 457 GLY 458 -0.0255

GLY 458 SER 459 -0.0002

SER 459 PHE 460 -0.0000

PHE 460 LEU 461 0.0047

LEU 461 VAL 462 0.0002

VAL 462 GLY 463 0.0002

GLY 463 ALA 464 -0.0023

ALA 464 TYR 465 -0.0003

TYR 465 ASP 466 0.0001

ASP 466 PRO 467 -0.0042

PRO 467 GLU 468 -0.0001

GLU 468 SER 469 -0.0001

SER 469 GLY 470 0.0026

GLY 470 GLU 471 0.0000

GLU 471 PHE 472 -0.0001

PHE 472 VAL 473 -0.0155

VAL 473 PRO 474 -0.0002

PRO 474 VAL 475 -0.0001

VAL 475 GLY 476 -0.0044

GLY 476 LYS 477 0.0002

LYS 477 VAL 478 -0.0000

VAL 478 GLY 479 0.0114

GLY 479 SER 480 -0.0003

SER 480 GLY 481 0.0001

GLY 481 PHE 482 -0.0570

PHE 482 THR 483 -0.0000

THR 483 ASP 484 0.0001

ASP 484 GLU 485 -0.0044

GLU 485 ASP 486 -0.0002

ASP 486 LEU 487 0.0003

LEU 487 VAL 488 -0.0120

VAL 488 GLU 489 0.0002

GLU 489 PHE 490 0.0002

PHE 490 THR 491 0.0043

THR 491 LYS 492 -0.0001

LYS 492 MET 493 -0.0000

MET 493 LEU 494 -0.0043

LEU 494 LYS 495 -0.0003

LYS 495 PRO 496 0.0002

PRO 496 LEU 497 0.0070

LEU 497 ILE 498 -0.0002

ILE 498 ILE 499 -0.0002

ILE 499 ARG 500 0.0066

ARG 500 GLU 501 -0.0001

GLU 501 GLU 502 -0.0002

GLU 502 GLY 503 0.0039

GLY 503 LYS 504 0.0001

LYS 504 PHE 505 0.0003

PHE 505 VAL 506 0.0054

VAL 506 GLU 507 -0.0003

GLU 507 ILE 508 0.0002

ILE 508 GLU 509 0.0037

GLU 509 PRO 510 -0.0003

PRO 510 LYS 511 -0.0002

LYS 511 VAL 512 0.0074

VAL 512 VAL 513 -0.0005

VAL 513 ILE 514 -0.0000

ILE 514 GLU 515 0.0381

GLU 515 VAL 516 -0.0002

VAL 516 THR 517 0.0001

THR 517 TYR 518 0.0265

TYR 518 GLN 519 -0.0003

GLN 519 GLU 520 -0.0007

GLU 520 ILE 521 0.0063

ILE 521 GLN 522 -0.0001

GLN 522 LYS 523 -0.0003

LYS 523 SER 524 -0.0070

SER 524 PRO 525 -0.0004

PRO 525 LYS 526 0.0001

LYS 526 TYR 527 -0.0029

TYR 527 LYS 528 0.0002

LYS 528 SER 529 -0.0001

SER 529 GLY 530 0.0015

GLY 530 PHE 531 -0.0001

PHE 531 ALA 532 0.0003

ALA 532 LEU 533 -0.0116

LEU 533 ARG 534 -0.0002

ARG 534 PHE 535 0.0003

PHE 535 PRO 536 0.0000

PRO 536 ARG 537 0.0001

ARG 537 TYR 538 -0.0001

TYR 538 VAL 539 0.0405

VAL 539 ALA 540 -0.0003

ALA 540 LEU 541 0.0003

LEU 541 ARG 542 -0.0116

ARG 542 GLU 543 0.0003

GLU 543 ASN 544 -0.0000

ASN 544 LYS 545 -0.0014

LYS 545 SER 546 0.0001

SER 546 PRO 547 -0.0003

PRO 547 GLU 548 0.0001

GLU 548 GLU 549 0.0001

GLU 549 ALA 550 -0.0003

ALA 550 ASP 551 0.0146

ASP 551 THR 552 0.0003

THR 552 ILE 553 0.0000

ILE 553 GLU 554 0.0005

GLU 554 ARG 555 -0.0002

ARG 555 VAL 556 0.0004

VAL 556 ALA 557 -0.0041

ALA 557 GLN 558 -0.0002

GLN 558 LEU 559 -0.0004

LEU 559 TYR 560 -0.0026

TYR 560 GLU 561 -0.0003

GLU 561 LEU 562 -0.0003

LEU 562 GLN 563 0.0132

GLN 563 GLU 564 0.0002

GLU 564 ARG 565 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: October 18th, 2018.

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

*** Xhaly ***

CA strain for 22042218234111840

--- normal mode 8 ---

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

* Xhaly *