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

* 4qg6 *

CA strain for 2407051322282258162

--- normal mode 7 ---

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
ASP 24 THR 25 -0.0005

THR 25 PHE 26 0.0005

PHE 26 LEU 27 0.0020

LEU 27 GLU 28 0.0002

GLU 28 HIS 29 -0.0000

HIS 29 MET 30 -0.0013

MET 30 CYS 31 -0.0003

CYS 31 ARG 32 0.0000

ARG 32 LEU 33 0.0007

LEU 33 ASP 34 -0.0000

ASP 34 ILE 35 -0.0001

ILE 35 ASP 36 -0.0008

ASP 36 SER 37 -0.0003

SER 37 PRO 38 0.0003

PRO 38 PRO 39 0.0070

PRO 39 ILE 40 0.0001

ILE 40 THR 41 -0.0003

THR 41 ALA 42 -0.0073

ALA 42 ARG 43 -0.0003

ARG 43 ASN 44 0.0001

ASN 44 THR 45 0.0161

THR 45 GLY 46 -0.0001

GLY 46 ILE 47 0.0004

ILE 47 ILE 48 0.0079

ILE 48 CYS 49 -0.0002

CYS 49 THR 50 0.0003

THR 50 ILE 51 -0.0155

ILE 51 GLY 52 -0.0003

GLY 52 PRO 53 0.0000

PRO 53 ALA 54 0.0226

ALA 54 SER 55 -0.0000

SER 55 ARG 56 0.0002

ARG 56 SER 57 0.0154

SER 57 VAL 58 -0.0001

VAL 58 GLU 59 0.0004

GLU 59 THR 60 -0.0073

THR 60 LEU 61 -0.0000

LEU 61 LYS 62 0.0004

LYS 62 GLU 63 -0.0030

GLU 63 MET 64 0.0003

MET 64 ILE 65 0.0004

ILE 65 LYS 66 0.0009

LYS 66 SER 67 0.0003

SER 67 GLY 68 0.0003

GLY 68 MET 69 0.0023

MET 69 ASN 70 -0.0001

ASN 70 VAL 71 -0.0005

VAL 71 ALA 72 0.0195

ALA 72 ARG 73 0.0000

ARG 73 LEU 74 -0.0001

LEU 74 ASN 75 0.0646

ASN 75 PHE 76 -0.0001

PHE 76 SER 77 -0.0001

SER 77 HIS 78 0.0419

HIS 78 GLY 79 0.0000

GLY 79 THR 80 -0.0001

THR 80 HIS 81 -0.0011

HIS 81 GLU 82 0.0002

GLU 82 TYR 83 -0.0002

TYR 83 HIS 84 -0.0068

HIS 84 ALA 85 0.0001

ALA 85 GLU 86 0.0002

GLU 86 THR 87 -0.0200

THR 87 ILE 88 0.0000

ILE 88 LYS 89 -0.0002

LYS 89 ASN 90 -0.0042

ASN 90 VAL 91 -0.0000

VAL 91 ARG 92 -0.0000

ARG 92 THR 93 -0.0215

THR 93 ALA 94 -0.0001

ALA 94 THR 95 -0.0001

THR 95 GLU 96 0.0008

GLU 96 SER 97 0.0001

SER 97 PHE 98 -0.0001

PHE 98 ALA 99 0.0087

ALA 99 SER 100 0.0000

SER 100 ASP 101 0.0000

ASP 101 PRO 102 0.0105

PRO 102 ILE 103 0.0004

ILE 103 LEU 104 -0.0002

LEU 104 GLU 105 -0.0125

GLU 105 ARG 106 0.0002

ARG 106 PRO 107 -0.0001

PRO 107 VAL 108 0.0243

VAL 108 ALA 109 -0.0003

ALA 109 VAL 110 -0.0000

VAL 110 ALA 111 0.0276

ALA 111 LEU 112 -0.0001

LEU 112 ASP 113 -0.0002

ASP 113 THR 114 0.0448

THR 114 LYS 115 -0.0002

LYS 115 GLY 116 0.0001

GLY 116 PRO 117 0.1197

PRO 117 GLU 118 -0.0001

GLU 118 ILE 119 0.0003

ILE 119 ARG 120 0.0096

ARG 120 THR 121 0.0003

THR 121 GLY 122 -0.0000

GLY 122 LEU 123 0.0049

LEU 123 ILE 124 0.0002

ILE 124 LYS 125 0.0000

LYS 125 ALA 130 -0.0061

ALA 130 GLU 131 -0.0000

GLU 131 VAL 132 0.0004

VAL 132 GLU 133 -0.0132

GLU 133 LYS 136 -0.0159

LYS 136 GLY 137 0.0003

GLY 137 ALA 138 -0.0002

ALA 138 THR 139 0.0028

THR 139 LEU 140 -0.0000

LEU 140 LYS 141 0.0001

LYS 141 ILE 142 0.0070

ILE 142 THR 143 -0.0000

THR 143 LEU 144 -0.0003

LEU 144 ASP 145 -0.0209

ASP 145 ASN 146 0.0002

ASN 146 ALA 147 0.0002

ALA 147 TYR 148 0.0013

TYR 148 MET 149 0.0002

MET 149 GLU 150 0.0001

GLU 150 LYS 151 -0.0031

LYS 151 CYS 152 -0.0002

CYS 152 ASP 153 0.0002

ASP 153 GLU 154 -0.0003

GLU 154 ASN 155 0.0001

ASN 155 ILE 156 0.0003

ILE 156 LEU 157 0.0215

LEU 157 TRP 158 -0.0004

TRP 158 LEU 159 0.0004

LEU 159 ASP 160 0.0099

ASP 160 TYR 161 -0.0000

TYR 161 LYS 162 -0.0004

LYS 162 ASN 163 0.0018

ASN 163 ILE 164 0.0001

ILE 164 CYS 165 0.0003

CYS 165 LYS 166 -0.0245

LYS 166 VAL 167 0.0004

VAL 167 VAL 168 -0.0001

VAL 168 GLU 169 -0.0253

GLU 169 VAL 170 -0.0000

VAL 170 GLY 171 -0.0001

GLY 171 SER 172 -0.0104

SER 172 LYS 173 0.0000

LYS 173 ILE 174 -0.0003

ILE 174 TYR 175 0.0304

TYR 175 VAL 176 -0.0001

VAL 176 ASP 177 0.0001

ASP 177 ASP 178 0.0671

ASP 178 GLY 179 -0.0001

GLY 179 LEU 180 -0.0002

LEU 180 ILE 181 0.0168

ILE 181 SER 182 -0.0001

SER 182 LEU 183 -0.0002

LEU 183 GLN 184 0.0186

GLN 184 VAL 185 0.0001

VAL 185 LYS 186 -0.0001

LYS 186 GLN 187 0.0072

GLN 187 LYS 188 0.0001

LYS 188 GLY 189 -0.0001

GLY 189 ALA 190 0.0205

ALA 190 ASP 191 0.0003

ASP 191 PHE 192 -0.0002

PHE 192 LEU 193 0.0015

LEU 193 VAL 194 -0.0001

VAL 194 THR 195 -0.0000

THR 195 GLU 196 0.0008

GLU 196 VAL 197 0.0001

VAL 197 GLU 198 -0.0004

GLU 198 ASN 199 -0.0010

ASN 199 GLY 200 -0.0001

GLY 200 GLY 201 0.0003

GLY 201 SER 202 -0.0251

SER 202 LEU 203 0.0004

LEU 203 GLY 204 -0.0002

GLY 204 SER 205 -0.0257

SER 205 LYS 206 -0.0000

LYS 206 LYS 207 0.0002

LYS 207 GLY 208 0.0330

GLY 208 VAL 209 -0.0001

VAL 209 ASN 210 0.0002

ASN 210 LEU 211 0.0016

LEU 211 PRO 212 0.0000

PRO 212 GLY 213 0.0007

GLY 213 ALA 214 0.0055

ALA 214 ALA 215 -0.0003

ALA 215 VAL 216 0.0000

VAL 216 ASP 217 0.0389

ASP 217 LEU 218 0.0001

LEU 218 PRO 219 -0.0003

PRO 219 ALA 220 -0.0161

ALA 220 VAL 221 0.0001

VAL 221 SER 222 -0.0002

SER 222 GLU 223 0.0047

GLU 223 LYS 224 -0.0003

LYS 224 ASP 225 -0.0001

ASP 225 ILE 226 0.0020

ILE 226 GLN 227 -0.0003

GLN 227 ASP 228 -0.0004

ASP 228 LEU 229 0.0117

LEU 229 LYS 230 -0.0001

LYS 230 PHE 231 -0.0001

PHE 231 GLY 232 -0.0070

GLY 232 VAL 233 0.0003

VAL 233 GLU 234 0.0000

GLU 234 GLN 235 -0.0188

GLN 235 ASP 236 0.0002

ASP 236 VAL 237 0.0003

VAL 237 ASP 238 -0.0008

ASP 238 MET 239 -0.0001

MET 239 VAL 240 0.0001

VAL 240 PHE 241 -0.0103

PHE 241 ALA 242 -0.0001

ALA 242 SER 243 -0.0003

SER 243 PHE 244 0.0210

PHE 244 ILE 245 -0.0000

ILE 245 ARG 246 0.0004

ARG 246 LYS 247 0.0230

LYS 247 ALA 248 0.0001

ALA 248 SER 249 -0.0000

SER 249 ASP 250 0.0210

ASP 250 VAL 251 -0.0000

VAL 251 HIS 252 -0.0001

HIS 252 GLU 253 0.0301

GLU 253 VAL 254 -0.0002

VAL 254 ARG 255 0.0000

ARG 255 LYS 256 0.0246

LYS 256 VAL 257 -0.0002

VAL 257 LEU 258 -0.0005

LEU 258 GLY 259 0.0135

GLY 259 GLU 260 0.0000

GLU 260 LYS 261 -0.0003

LYS 261 GLY 262 -0.0072

GLY 262 LYS 263 -0.0005

LYS 263 ASN 264 0.0002

ASN 264 ILE 265 0.0176

ILE 265 LYS 266 -0.0000

LYS 266 ILE 267 0.0002

ILE 267 ILE 268 0.0013

ILE 268 SER 269 -0.0001

SER 269 LYS 270 0.0001

LYS 270 ILE 271 -0.0289

ILE 271 GLU 272 0.0001

GLU 272 ASN 273 -0.0005

ASN 273 HIS 274 0.0062

HIS 274 GLU 275 -0.0003

GLU 275 GLY 276 -0.0002

GLY 276 VAL 277 -0.0327

VAL 277 ARG 278 -0.0001

ARG 278 ARG 279 0.0005

ARG 279 PHE 280 -0.0824

PHE 280 ASP 281 0.0002

ASP 281 GLU 282 0.0003

GLU 282 ILE 283 0.0120

ILE 283 LEU 284 0.0000

LEU 284 GLU 285 -0.0002

GLU 285 ALA 286 0.0166

ALA 286 SER 287 -0.0001

SER 287 ASP 288 -0.0002

ASP 288 GLY 289 0.0021

GLY 289 ILE 290 -0.0001

ILE 290 MET 291 0.0000

MET 291 VAL 292 0.0086

VAL 292 ALA 293 -0.0001

ALA 293 ARG 294 0.0003

ARG 294 GLY 295 0.1085

GLY 295 ASP 296 -0.0002

ASP 296 LEU 297 -0.0000

LEU 297 GLY 298 -0.0075

GLY 298 ILE 299 -0.0004

ILE 299 GLU 300 0.0001

GLU 300 ILE 301 0.0068

ILE 301 PRO 302 -0.0004

PRO 302 ALA 303 0.0001

ALA 303 GLU 304 0.0186

GLU 304 LYS 305 -0.0001

LYS 305 VAL 306 0.0001

VAL 306 PHE 307 0.0238

PHE 307 LEU 308 -0.0002

LEU 308 ALA 309 0.0001

ALA 309 GLN 310 0.0054

GLN 310 LYS 311 -0.0003

LYS 311 MET 312 -0.0003

MET 312 MET 313 0.0060

MET 313 ILE 314 0.0002

ILE 314 GLY 315 -0.0000

GLY 315 ARG 316 0.0039

ARG 316 CYS 317 0.0000

CYS 317 ASN 318 0.0002

ASN 318 ARG 319 -0.0047

ARG 319 ALA 320 -0.0002

ALA 320 GLY 321 -0.0003

GLY 321 LYS 322 -0.0483

LYS 322 PRO 323 -0.0001

PRO 323 VAL 324 -0.0001

VAL 324 ILE 325 0.0003

ILE 325 CYS 326 -0.0000

CYS 326 ALA 327 0.0003

ALA 327 THR 328 0.0003

THR 328 GLN 329 -0.0004

GLN 329 MET 330 0.0000

MET 330 LEU 331 0.0387

LEU 331 GLU 332 0.0001

GLU 332 SER 333 0.0000

SER 333 MET 334 0.0040

MET 334 ILE 335 -0.0001

ILE 335 LYS 336 0.0004

LYS 336 LYS 337 -0.0056

LYS 337 PRO 338 -0.0003

PRO 338 ARG 339 0.0002

ARG 339 PRO 340 -0.0012

PRO 340 THR 341 -0.0000

THR 341 ARG 342 0.0002

ARG 342 ALA 343 0.0013

ALA 343 GLU 344 0.0005

GLU 344 GLY 345 -0.0001

GLY 345 SER 346 -0.0027

SER 346 ASP 347 0.0000

ASP 347 VAL 348 0.0003

VAL 348 ALA 349 0.0240

ALA 349 ASN 350 -0.0001

ASN 350 ALA 351 -0.0003

ALA 351 VAL 352 0.0283

VAL 352 LEU 353 0.0002

LEU 353 ASP 354 0.0003

ASP 354 GLY 355 0.0090

GLY 355 ALA 356 -0.0001

ALA 356 ASP 357 0.0001

ASP 357 CYS 358 -0.0124

CYS 358 ILE 359 0.0004

ILE 359 MET 360 0.0001

MET 360 LEU 361 -0.0043

LEU 361 SER 362 0.0002

SER 362 GLY 363 -0.0003

GLY 363 GLU 364 0.0075

GLU 364 THR 365 -0.0003

THR 365 ALA 366 -0.0004

ALA 366 LYS 367 0.0062

LYS 367 GLY 368 -0.0001

GLY 368 ASP 369 0.0002

ASP 369 TYR 370 -0.0017

TYR 370 PRO 371 0.0003

PRO 371 LEU 372 -0.0001

LEU 372 GLU 373 0.0011

GLU 373 ALA 374 0.0003

ALA 374 VAL 375 0.0000

VAL 375 ARG 376 0.0016

ARG 376 MET 377 -0.0000

MET 377 GLN 378 -0.0001

GLN 378 HIS 379 0.0096

HIS 379 LEU 380 0.0000

LEU 380 ILE 381 0.0003

ILE 381 ALA 382 -0.0098

ALA 382 ARG 383 -0.0001

ARG 383 GLU 384 0.0001

GLU 384 ALA 385 0.0076

ALA 385 GLU 386 -0.0002

GLU 386 ALA 387 0.0001

ALA 387 ALA 388 -0.0105

ALA 388 ILE 389 0.0000

ILE 389 TYR 390 -0.0002

TYR 390 HIS 391 0.0104

HIS 391 LEU 392 0.0003

LEU 392 GLN 393 0.0002

GLN 393 LEU 394 -0.0034

LEU 394 PHE 395 0.0000

PHE 395 GLU 396 0.0002

GLU 396 GLU 397 0.0023

GLU 397 LEU 398 0.0005

LEU 398 ARG 399 -0.0003

ARG 399 ARG 400 0.0019

ARG 400 LEU 401 -0.0000

LEU 401 ALA 402 -0.0002

ALA 402 PRO 403 -0.0068

PRO 403 ILE 404 -0.0003

ILE 404 THR 405 0.0001

THR 405 SER 406 0.0044

SER 406 ASP 407 -0.0003

ASP 407 PRO 408 0.0005

PRO 408 THR 409 -0.0017

THR 409 GLU 410 -0.0001

GLU 410 ALA 411 -0.0000

ALA 411 THR 412 0.0028

THR 412 ALA 413 -0.0003

ALA 413 VAL 414 0.0001

VAL 414 GLY 415 -0.0143

GLY 415 ALA 416 -0.0002

ALA 416 VAL 417 0.0001

VAL 417 GLU 418 -0.0076

GLU 418 ALA 419 0.0002

ALA 419 SER 420 -0.0001

SER 420 PHE 421 0.0032

PHE 421 LYS 422 -0.0000

LYS 422 CYS 423 -0.0002

CYS 423 CYS 424 0.0067

CYS 424 SER 425 0.0001

SER 425 GLY 426 -0.0000

GLY 426 ALA 427 -0.0053

ALA 427 ILE 428 -0.0002

ILE 428 ILE 429 0.0002

ILE 429 VAL 430 -0.0069

VAL 430 LEU 431 0.0000

LEU 431 THR 432 0.0003

THR 432 LYS 433 -0.0021

LYS 433 SER 434 0.0000

SER 434 GLY 435 -0.0001

GLY 435 ARG 436 0.0049

ARG 436 SER 437 -0.0000

SER 437 ALA 438 -0.0003

ALA 438 HIS 439 -0.0160

HIS 439 GLN 440 -0.0001

GLN 440 VAL 441 -0.0001

VAL 441 ALA 442 -0.0129

ALA 442 ARG 443 -0.0002

ARG 443 TYR 444 -0.0005

TYR 444 ARG 445 0.0012

ARG 445 PRO 446 0.0002

PRO 446 ARG 447 0.0001

ARG 447 ALA 448 -0.0111

ALA 448 PRO 449 0.0005

PRO 449 ILE 450 0.0001

ILE 450 ILE 451 -0.0036

ILE 451 ALA 452 0.0002

ALA 452 VAL 453 -0.0001

VAL 453 THR 454 -0.0081

THR 454 ARG 455 0.0006

ARG 455 ASN 456 0.0000

ASN 456 PRO 457 0.0123

PRO 457 GLN 458 -0.0004

GLN 458 THR 459 -0.0001

THR 459 ALA 460 0.0121

ALA 460 ARG 461 0.0003

ARG 461 GLN 462 0.0001

GLN 462 ALA 463 0.0022

ALA 463 HIS 464 -0.0001

HIS 464 LEU 465 0.0001

LEU 465 TYR 466 -0.0032

TYR 466 ARG 467 0.0002

ARG 467 GLY 468 0.0001

GLY 468 ILE 469 0.0208

ILE 469 PHE 470 0.0003

PHE 470 PRO 471 -0.0001

PRO 471 VAL 472 0.0032

VAL 472 LEU 473 0.0000

LEU 473 CYS 474 -0.0001

CYS 474 LYS 475 0.0065

LYS 475 ASP 476 0.0001

ASP 476 PRO 477 -0.0000

PRO 477 VAL 478 0.0062

VAL 478 GLN 479 0.0001

GLN 479 GLU 480 -0.0004

GLU 480 ALA 481 0.0033

ALA 481 TRP 482 0.0004

TRP 482 ALA 483 0.0000

ALA 483 GLU 484 -0.0014

GLU 484 ASP 485 -0.0001

ASP 485 VAL 486 -0.0003

VAL 486 ASP 487 0.0048

ASP 487 LEU 488 0.0002

LEU 488 ARG 489 -0.0000

ARG 489 VAL 490 -0.0126

VAL 490 ASN 491 0.0000

ASN 491 PHE 492 0.0001

PHE 492 ALA 493 0.0000

ALA 493 MET 494 -0.0002

MET 494 ASN 495 -0.0002

ASN 495 VAL 496 0.0097

VAL 496 GLY 497 -0.0002

GLY 497 LYS 498 -0.0000

LYS 498 ALA 499 0.0191

ALA 499 ARG 500 0.0003

ARG 500 GLY 501 0.0004

GLY 501 PHE 502 -0.0011

PHE 502 PHE 503 0.0004

PHE 503 LYS 504 -0.0003

LYS 504 LYS 505 0.0059

LYS 505 GLY 506 0.0000

GLY 506 ASP 507 0.0004

ASP 507 VAL 508 -0.0053

VAL 508 VAL 509 -0.0000

VAL 509 ILE 510 -0.0001

ILE 510 VAL 511 0.0005

VAL 511 LEU 512 0.0004

LEU 512 THR 513 -0.0003

THR 513 GLY 514 0.0029

GLY 514 TRP 515 -0.0000

TRP 515 ARG 516 0.0003

ARG 516 PRO 517 -0.0015

PRO 517 GLY 518 0.0003

GLY 518 SER 519 0.0003

SER 519 GLY 520 0.0000

GLY 520 PHE 521 -0.0002

PHE 521 THR 522 0.0004

THR 522 ASN 523 0.0046

ASN 523 THR 524 -0.0001

THR 524 MET 525 -0.0002

MET 525 ARG 526 -0.0017

ARG 526 VAL 527 -0.0002

VAL 527 VAL 528 0.0001

VAL 528 PRO 529 -0.0027

PRO 529 VAL 530 -0.0005

VAL 530 PRO 531 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.

*** 4qg6 ***

CA strain for 2407051322282258162

--- normal mode 7 ---

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

* 4qg6 *