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

* 2V7Y copy *

CA strain for 2402070142291776838

--- normal mode 16 ---

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
MET 1 SER 2 0.0000

SER 2 LYS 3 -0.0004

LYS 3 ILE 4 -0.0102

ILE 4 ILE 5 0.0002

ILE 5 GLY 6 -0.0003

GLY 6 ILE 7 -0.0093

ILE 7 ASP 8 0.0001

ASP 8 LEU 9 -0.0000

LEU 9 GLY 10 -0.0214

GLY 10 THR 11 0.0004

THR 11 THR 12 0.0004

THR 12 ASN 13 0.0329

ASN 13 SER 14 -0.0000

SER 14 CYS 15 0.0004

CYS 15 VAL 16 0.0256

VAL 16 ALA 17 0.0001

ALA 17 VAL 18 -0.0002

VAL 18 LEU 19 -0.0058

LEU 19 GLU 20 -0.0001

GLU 20 GLY 21 0.0002

GLY 21 GLY 22 0.0270

GLY 22 GLU 23 0.0002

GLU 23 VAL 24 0.0001

VAL 24 LYS 25 -0.0439

LYS 25 VAL 26 0.0001

VAL 26 ILE 27 0.0000

ILE 27 PRO 28 -0.0661

PRO 28 ASN 29 -0.0001

ASN 29 PRO 30 0.0001

PRO 30 GLU 31 0.0016

GLU 31 GLY 32 0.0001

GLY 32 ASN 33 -0.0001

ASN 33 ARG 34 -0.0507

ARG 34 THR 35 0.0001

THR 35 THR 36 -0.0002

THR 36 PRO 37 0.0104

PRO 37 SER 38 0.0003

SER 38 VAL 39 -0.0002

VAL 39 VAL 40 -0.0103

VAL 40 ALA 41 -0.0001

ALA 41 PHE 42 0.0003

PHE 42 LYS 43 0.0516

LYS 43 ASN 44 -0.0001

ASN 44 GLY 45 -0.0001

GLY 45 GLU 46 0.0312

GLU 46 ARG 47 0.0002

ARG 47 LEU 48 -0.0003

LEU 48 VAL 49 -0.0729

VAL 49 GLY 50 0.0001

GLY 50 GLU 51 -0.0002

GLU 51 VAL 52 -0.0543

VAL 52 ALA 53 -0.0003

ALA 53 LYS 54 0.0000

LYS 54 ARG 55 0.0192

ARG 55 GLN 56 0.0001

GLN 56 ALA 57 0.0000

ALA 57 ILE 58 -0.0049

ILE 58 THR 59 -0.0001

THR 59 ASN 60 0.0003

ASN 60 PRO 61 0.0338

PRO 61 ASN 62 0.0000

ASN 62 THR 63 -0.0001

THR 63 ILE 64 0.0830

ILE 64 ILE 65 0.0003

ILE 65 SER 66 -0.0001

SER 66 ILE 67 -0.0295

ILE 67 LYS 68 -0.0000

LYS 68 ARG 69 0.0001

ARG 69 HIS 70 -0.1576

HIS 70 MET 71 0.0000

MET 71 GLY 72 0.0003

GLY 72 THR 73 0.0686

THR 73 ASP 74 0.0003

ASP 74 TYR 75 0.0000

TYR 75 LYS 76 0.0559

LYS 76 VAL 77 -0.0003

VAL 77 GLU 78 0.0002

GLU 78 ILE 79 0.0564

ILE 79 GLU 80 -0.0001

GLU 80 GLY 81 -0.0002

GLY 81 LYS 82 0.0127

LYS 82 GLN 83 -0.0002

GLN 83 TYR 84 0.0003

TYR 84 THR 85 0.0351

THR 85 PRO 86 0.0001

PRO 86 GLN 87 0.0001

GLN 87 GLU 88 0.0081

GLU 88 ILE 89 0.0003

ILE 89 SER 90 -0.0002

SER 90 ALA 91 -0.0297

ALA 91 ILE 92 0.0001

ILE 92 ILE 93 -0.0002

ILE 93 LEU 94 -0.0022

LEU 94 GLN 95 0.0000

GLN 95 TYR 96 -0.0000

TYR 96 LEU 97 -0.0332

LEU 97 LYS 98 0.0002

LYS 98 SER 99 -0.0000

SER 99 TYR 100 0.0004

TYR 100 ALA 101 0.0001

ALA 101 GLU 102 0.0005

GLU 102 ASP 103 -0.0042

ASP 103 TYR 104 -0.0004

TYR 104 LEU 105 -0.0001

LEU 105 GLY 106 0.0115

GLY 106 GLU 107 0.0002

GLU 107 PRO 108 -0.0003

PRO 108 VAL 109 -0.0119

VAL 109 THR 110 0.0002

THR 110 ARG 111 -0.0004

ARG 111 ALA 112 -0.0284

ALA 112 VAL 113 -0.0001

VAL 113 ILE 114 0.0004

ILE 114 THR 115 -0.0469

THR 115 VAL 116 0.0002

VAL 116 PRO 117 -0.0000

PRO 117 ALA 118 0.0151

ALA 118 TYR 119 0.0001

TYR 119 PHE 120 -0.0000

PHE 120 ASN 121 -0.0176

ASN 121 ASP 122 0.0000

ASP 122 ALA 123 -0.0004

ALA 123 GLN 124 -0.0039

GLN 124 ARG 125 -0.0003

ARG 125 GLN 126 0.0001

GLN 126 ALA 127 -0.0116

ALA 127 THR 128 -0.0001

THR 128 LYS 129 0.0003

LYS 129 ASP 130 0.0386

ASP 130 ALA 131 -0.0002

ALA 131 GLY 132 -0.0002

GLY 132 ARG 133 -0.0002

ARG 133 ILE 134 -0.0002

ILE 134 ALA 135 0.0001

ALA 135 GLY 136 -0.0007

GLY 136 LEU 137 -0.0001

LEU 137 GLU 138 0.0000

GLU 138 VAL 139 -0.0071

VAL 139 GLU 140 0.0001

GLU 140 ARG 141 0.0000

ARG 141 ILE 142 -0.0487

ILE 142 ILE 143 -0.0002

ILE 143 ASN 144 0.0000

ASN 144 GLU 145 -0.0226

GLU 145 PRO 146 -0.0000

PRO 146 THR 147 -0.0002

THR 147 ALA 148 -0.0931

ALA 148 ALA 149 -0.0004

ALA 149 ALA 150 0.0002

ALA 150 LEU 151 -0.0640

LEU 151 ALA 152 0.0001

ALA 152 TYR 153 -0.0002

TYR 153 GLY 154 -0.1008

GLY 154 LEU 155 0.0000

LEU 155 ASP 156 0.0002

ASP 156 LYS 157 0.0085

LYS 157 GLU 158 0.0001

GLU 158 GLU 159 -0.0003

GLU 159 ASP 160 0.0093

ASP 160 GLN 161 -0.0002

GLN 161 THR 162 0.0003

THR 162 ILE 163 -0.0062

ILE 163 LEU 164 -0.0001

LEU 164 VAL 165 0.0005

VAL 165 TYR 166 0.0150

TYR 166 ASP 167 -0.0002

ASP 167 LEU 168 0.0002

LEU 168 GLY 169 0.0041

GLY 169 GLY 170 0.0001

GLY 170 GLY 171 -0.0001

GLY 171 THR 172 0.1031

THR 172 PHE 173 -0.0001

PHE 173 ASP 174 0.0003

ASP 174 VAL 175 0.0945

VAL 175 SER 176 0.0000

SER 176 ILE 177 0.0001

ILE 177 LEU 178 0.0166

LEU 178 GLU 179 -0.0000

GLU 179 LEU 180 0.0002

LEU 180 GLY 181 0.0237

GLY 181 ASP 182 -0.0001

ASP 182 GLY 183 -0.0001

GLY 183 VAL 184 0.0188

VAL 184 PHE 185 -0.0002

PHE 185 GLU 186 0.0002

GLU 186 VAL 187 0.0445

VAL 187 LYS 188 -0.0001

LYS 188 ALA 189 0.0001

ALA 189 THR 190 0.0890

THR 190 ALA 191 -0.0003

ALA 191 GLY 192 -0.0000

GLY 192 ASP 193 0.1227

ASP 193 ASN 194 -0.0002

ASN 194 HIS 195 -0.0002

HIS 195 LEU 196 -0.0769

LEU 196 GLY 197 -0.0001

GLY 197 GLY 198 -0.0001

GLY 198 ASP 199 -0.0037

ASP 199 ASP 200 -0.0001

ASP 200 PHE 201 0.0002

PHE 201 ASP 202 0.0642

ASP 202 GLN 203 0.0000

GLN 203 VAL 204 0.0002

VAL 204 ILE 205 0.0506

ILE 205 ILE 206 -0.0002

ILE 206 ASP 207 0.0002

ASP 207 TYR 208 -0.0843

TYR 208 LEU 209 -0.0002

LEU 209 VAL 210 -0.0001

VAL 210 ASN 211 -0.0821

ASN 211 GLN 212 0.0000

GLN 212 PHE 213 0.0000

PHE 213 LYS 214 -0.0225

LYS 214 GLN 215 -0.0001

GLN 215 GLU 216 -0.0004

GLU 216 HIS 217 0.0049

HIS 217 GLY 218 -0.0002

GLY 218 ILE 219 0.0000

ILE 219 ASP 220 -0.0073

ASP 220 LEU 221 0.0000

LEU 221 SER 222 -0.0001

SER 222 LYS 223 0.0488

LYS 223 ASP 224 0.0000

ASP 224 LYS 225 0.0002

LYS 225 MET 226 -0.0306

MET 226 ALA 227 -0.0000

ALA 227 LEU 228 0.0001

LEU 228 GLN 229 0.0050

GLN 229 ARG 230 -0.0003

ARG 230 LEU 231 0.0002

LEU 231 LYS 232 0.0552

LYS 232 ASP 233 -0.0003

ASP 233 ALA 234 0.0001

ALA 234 ALA 235 0.0779

ALA 235 GLU 236 -0.0001

GLU 236 LYS 237 -0.0002

LYS 237 ALA 238 0.0471

ALA 238 LYS 239 -0.0000

LYS 239 LYS 240 -0.0001

LYS 240 GLU 241 0.1154

GLU 241 LEU 242 0.0002

LEU 242 SER 243 -0.0001

SER 243 GLY 244 -0.0169

GLY 244 VAL 245 -0.0001

VAL 245 THR 246 -0.0000

THR 246 GLN 247 -0.0830

GLN 247 THR 248 0.0001

THR 248 GLN 249 -0.0000

GLN 249 ILE 250 -0.0361

ILE 250 SER 251 -0.0003

SER 251 LEU 252 -0.0002

LEU 252 PRO 253 -0.0706

PRO 253 PHE 254 -0.0002

PHE 254 ILE 255 -0.0000

ILE 255 SER 256 0.0149

SER 256 ALA 257 0.0002

ALA 257 ASN 258 -0.0003

ASN 258 GLU 259 0.0469

GLU 259 ASN 260 0.0001

ASN 260 GLY 261 0.0003

GLY 261 PRO 262 -0.0532

PRO 262 LEU 263 0.0003

LEU 263 HIS 264 -0.0001

HIS 264 LEU 265 -0.0356

LEU 265 GLU 266 -0.0000

GLU 266 MET 267 -0.0001

MET 267 THR 268 -0.1185

THR 268 LEU 269 -0.0001

LEU 269 THR 270 0.0000

THR 270 ARG 271 -0.0881

ARG 271 ALA 272 0.0001

ALA 272 LYS 273 -0.0000

LYS 273 PHE 274 -0.0241

PHE 274 GLU 275 0.0003

GLU 275 GLU 276 -0.0001

GLU 276 LEU 277 0.0016

LEU 277 SER 278 0.0002

SER 278 ALA 279 0.0001

ALA 279 HIS 280 -0.1487

HIS 280 LEU 281 -0.0001

LEU 281 VAL 282 0.0003

VAL 282 GLU 283 0.0077

GLU 283 ARG 284 0.0001

ARG 284 THR 285 -0.0002

THR 285 MET 286 0.0454

MET 286 GLY 287 -0.0001

GLY 287 PRO 288 0.0001

PRO 288 VAL 289 0.0248

VAL 289 ARG 290 0.0001

ARG 290 GLN 291 -0.0000

GLN 291 ALA 292 -0.0258

ALA 292 LEU 293 -0.0002

LEU 293 GLN 294 -0.0002

GLN 294 ASP 295 -0.0115

ASP 295 ALA 296 -0.0002

ALA 296 GLY 297 0.0000

GLY 297 LEU 298 -0.0157

LEU 298 THR 299 -0.0001

THR 299 PRO 300 -0.0002

PRO 300 ALA 301 -0.0037

ALA 301 ASP 302 -0.0001

ASP 302 ILE 303 0.0000

ILE 303 ASP 304 0.0061

ASP 304 LYS 305 -0.0001

LYS 305 VAL 306 -0.0000

VAL 306 ILE 307 -0.0110

ILE 307 LEU 308 -0.0000

LEU 308 VAL 309 0.0003

VAL 309 GLY 310 -0.0000

GLY 310 GLY 311 -0.0002

GLY 311 SER 312 0.0002

SER 312 THR 313 -0.0175

THR 313 ARG 314 0.0000

ARG 314 ILE 315 0.0000

ILE 315 PRO 316 0.1133

PRO 316 ALA 317 0.0000

ALA 317 VAL 318 0.0005

VAL 318 GLN 319 0.0787

GLN 319 GLU 320 -0.0000

GLU 320 ALA 321 0.0002

ALA 321 ILE 322 0.0221

ILE 322 LYS 323 -0.0000

LYS 323 ARG 324 -0.0001

ARG 324 GLU 325 -0.0465

GLU 325 LEU 326 -0.0004

LEU 326 GLY 327 0.0001

GLY 327 LYS 328 0.0391

LYS 328 GLU 329 0.0002

GLU 329 PRO 330 -0.0001

PRO 330 HIS 331 0.0618

HIS 331 LYS 332 -0.0002

LYS 332 GLY 333 0.0000

GLY 333 VAL 334 0.0204

VAL 334 ASN 335 -0.0002

ASN 335 PRO 336 0.0001

PRO 336 ASP 337 -0.0766

ASP 337 GLU 338 -0.0000

GLU 338 VAL 339 0.0001

VAL 339 VAL 340 0.0169

VAL 340 ALA 341 0.0005

ALA 341 ILE 342 -0.0002

ILE 342 GLY 343 -0.0237

GLY 343 ALA 344 -0.0000

ALA 344 ALA 345 -0.0002

ALA 345 ILE 346 -0.0592

ILE 346 GLN 347 0.0002

GLN 347 GLY 348 -0.0001

GLY 348 GLY 349 -0.0145

GLY 349 VAL 350 -0.0000

VAL 350 ILE 351 0.0001

ILE 351 ALA 352 0.0464

ALA 352 GLY 353 0.0003

GLY 353 GLU 354 -0.0000

GLU 354 VAL 355 0.0753

VAL 355 LYS 356 -0.0000

LYS 356 ASP 357 0.0002

ASP 357 VAL 358 0.1199

VAL 358 VAL 359 -0.0002

VAL 359 LEU 360 0.0000

LEU 360 LEU 361 0.1094

LEU 361 ASP 362 -0.0004

ASP 362 VAL 363 0.0003

VAL 363 THR 364 0.0301

THR 364 PRO 365 -0.0000

PRO 365 LEU 366 -0.0001

LEU 366 SER 367 0.0043

SER 367 LEU 368 -0.0003

LEU 368 GLY 369 0.0000

GLY 369 ILE 370 0.0054

ILE 370 GLU 371 0.0002

GLU 371 THR 372 0.0000

THR 372 MET 373 0.0056

MET 373 GLY 374 0.0002

GLY 374 GLY 375 0.0001

GLY 375 VAL 376 -0.0048

VAL 376 PHE 377 -0.0002

PHE 377 THR 378 -0.0002

THR 378 LYS 379 -0.0063

LYS 379 LEU 380 -0.0001

LEU 380 ILE 381 0.0000

ILE 381 GLU 382 0.0057

GLU 382 ARG 383 -0.0002

ARG 383 ASN 384 0.0002

ASN 384 THR 385 -0.0004

THR 385 THR 386 0.0002

THR 386 ILE 387 0.0003

ILE 387 PRO 388 0.0050

PRO 388 THR 389 -0.0001

THR 389 SER 390 -0.0000

SER 390 LYS 391 -0.0003

LYS 391 SER 392 0.0004

SER 392 GLN 393 -0.0004

GLN 393 VAL 394 0.0045

VAL 394 PHE 395 -0.0000

PHE 395 THR 396 -0.0002

THR 396 THR 397 0.0021

THR 397 ALA 398 0.0000

ALA 398 ALA 399 0.0001

ALA 399 ASP 400 -0.0003

ASP 400 ASN 401 -0.0001

ASN 401 GLN 402 0.0003

GLN 402 THR 403 0.0016

THR 403 THR 404 -0.0003

THR 404 VAL 405 -0.0001

VAL 405 ASP 406 -0.0052

ASP 406 ILE 407 -0.0002

ILE 407 HIS 408 -0.0001

HIS 408 VAL 409 0.0004

VAL 409 LEU 410 0.0001

LEU 410 GLN 411 -0.0001

GLN 411 GLY 412 -0.0017

GLY 412 GLU 413 -0.0001

GLU 413 ARG 414 -0.0001

ARG 414 PRO 415 -0.0054

PRO 415 MET 416 -0.0005

MET 416 ALA 417 -0.0000

ALA 417 ALA 418 -0.0039

ALA 418 ASP 419 -0.0002

ASP 419 ASN 420 -0.0003

ASN 420 LYS 421 0.0035

LYS 421 SER 422 -0.0002

SER 422 LEU 423 0.0004

LEU 423 GLY 424 -0.0069

GLY 424 ARG 425 -0.0001

ARG 425 PHE 426 0.0000

PHE 426 GLN 427 -0.0034

GLN 427 LEU 428 0.0002

LEU 428 THR 429 0.0001

THR 429 GLY 430 0.0003

GLY 430 ILE 431 -0.0002

ILE 431 PRO 432 0.0000

PRO 432 PRO 433 0.0011

PRO 433 ALA 434 0.0001

ALA 434 PRO 435 0.0001

PRO 435 ARG 436 -0.0009

ARG 436 GLY 437 -0.0000

GLY 437 VAL 438 0.0002

VAL 438 PRO 439 0.0001

PRO 439 GLN 440 0.0004

GLN 440 ILE 441 -0.0002

ILE 441 GLU 442 0.0047

GLU 442 VAL 443 -0.0003

VAL 443 THR 444 0.0003

THR 444 PHE 445 0.0065

PHE 445 ASP 446 0.0000

ASP 446 ILE 447 0.0001

ILE 447 ASP 448 -0.0011

ASP 448 ALA 449 -0.0000

ALA 449 ASN 450 0.0003

ASN 450 GLY 451 -0.0047

GLY 451 ILE 452 -0.0003

ILE 452 VAL 453 0.0004

VAL 453 HIS 454 0.0028

HIS 454 VAL 455 0.0000

VAL 455 ARG 456 0.0002

ARG 456 ALA 457 0.0053

ALA 457 LYS 458 -0.0002

LYS 458 ASP 459 0.0003

ASP 459 LEU 460 -0.0010

LEU 460 GLY 461 0.0004

GLY 461 THR 462 0.0003

THR 462 ASN 463 0.0002

ASN 463 LYS 464 0.0002

LYS 464 GLU 465 0.0001

GLU 465 GLN 466 -0.0012

GLN 466 SER 467 -0.0003

SER 467 ILE 468 0.0003

ILE 468 THR 469 0.0036

THR 469 ILE 470 0.0004

ILE 470 LYS 471 0.0004

LYS 471 SER 472 -0.0078

SER 472 SER 473 -0.0002

SER 473 SER 474 -0.0001

SER 474 GLY 475 -0.0047

GLY 475 LEU 476 0.0001

LEU 476 SER 477 0.0002

SER 477 GLU 478 -0.0048

GLU 478 GLU 479 -0.0002

GLU 479 GLU 480 0.0002

GLU 480 ILE 481 0.0057

ILE 481 GLN 482 0.0001

GLN 482 ARG 483 0.0001

ARG 483 MET 484 -0.0061

MET 484 ILE 485 -0.0000

ILE 485 LYS 486 -0.0001

LYS 486 GLU 487 -0.0016

GLU 487 ALA 488 0.0002

ALA 488 GLU 489 -0.0000

GLU 489 GLU 490 -0.0002

GLU 490 ASN 491 0.0004

ASN 491 ALA 492 0.0003

ALA 492 GLU 493 -0.0022

GLU 493 ALA 494 0.0000

ALA 494 ASP 495 0.0002

ASP 495 ARG 496 -0.0099

ARG 496 LYS 497 0.0003

LYS 497 ARG 498 -0.0000

ARG 498 LYS 499 -0.0033

LYS 499 GLU 500 -0.0003

GLU 500 ALA 501 -0.0002

ALA 501 ALA 502 0.0060

ALA 502 GLU 503 0.0004

GLU 503 LEU 504 -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.

*** 2V7Y copy ***

CA strain for 2402070142291776838

--- normal mode 16 ---

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

* 2V7Y copy *