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

* YejA NMA *

CA strain for 240125141212352800

--- normal mode 11 ---

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 GLN 2 0.0001

GLN 2 ALA 3 0.0000

ALA 3 ILE 4 -0.0256

ILE 4 LYS 5 0.0001

LYS 5 GLU 6 0.0002

GLU 6 SER 7 -0.1767

SER 7 TYR 8 -0.0002

TYR 8 ALA 9 0.0001

ALA 9 PHE 10 0.0373

PHE 10 ALA 11 0.0001

ALA 11 VAL 12 -0.0004

VAL 12 LEU 13 0.0002

LEU 13 GLY 14 -0.0003

GLY 14 GLU 15 0.0003

GLU 15 PRO 16 -0.0447

PRO 16 ARG 17 -0.0002

ARG 17 TYR 18 -0.0001

TYR 18 ALA 19 -0.0048

ALA 19 PHE 20 -0.0001

PHE 20 ASN 21 -0.0001

ASN 21 PHE 22 0.0042

PHE 22 ASN 23 -0.0004

ASN 23 HIS 24 0.0002

HIS 24 PHE 25 0.0176

PHE 25 ASP 26 0.0001

ASP 26 TYR 27 0.0001

TYR 27 VAL 28 -0.0056

VAL 28 ASN 29 -0.0000

ASN 29 PRO 30 0.0001

PRO 30 ALA 31 -0.0244

ALA 31 ALA 32 0.0001

ALA 32 PRO 33 0.0001

PRO 33 LYS 34 0.0071

LYS 34 GLY 35 -0.0000

GLY 35 GLY 36 0.0000

GLY 36 GLN 37 -0.0014

GLN 37 ILE 38 0.0002

ILE 38 THR 39 0.0001

THR 39 LEU 40 -0.0015

LEU 40 SER 41 0.0004

SER 41 ALA 42 -0.0004

ALA 42 LEU 43 0.0223

LEU 43 GLY 44 0.0001

GLY 44 THR 45 -0.0000

THR 45 PHE 46 -0.0093

PHE 46 ASP 47 0.0003

ASP 47 ASN 48 0.0001

ASN 48 PHE 49 -0.0040

PHE 49 ASN 50 0.0001

ASN 50 ARG 51 -0.0002

ARG 51 TYR 52 -0.0003

TYR 52 ALA 53 0.0001

ALA 53 LEU 54 0.0002

LEU 54 ARG 55 0.0054

ARG 55 ARG 55 -0.0036

ARG 55 GLY 56 0.0003

GLY 56 ASN 57 0.0000

ASN 57 PRO 58 0.0258

PRO 58 GLY 59 0.0002

GLY 59 ALA 60 0.0001

ALA 60 ARG 61 0.0111

ARG 61 THR 62 -0.0001

THR 62 GLU 63 0.0001

GLU 63 GLN 64 0.0340

GLN 64 LEU 65 -0.0001

LEU 65 TYR 66 -0.0001

TYR 66 ASP 67 -0.0192

ASP 67 THR 68 0.0001

THR 68 LEU 69 0.0000

LEU 69 PHE 70 0.0095

PHE 70 THR 71 -0.0001

THR 71 THR 72 -0.0002

THR 72 SER 73 0.0489

SER 73 ASP 74 -0.0001

ASP 74 ASP 75 0.0004

ASP 75 GLU 76 -0.0538

GLU 76 PRO 77 -0.0003

PRO 77 GLY 78 0.0001

GLY 78 SER 79 0.0036

SER 79 TYR 80 -0.0001

TYR 80 TYR 81 -0.0002

TYR 81 PRO 82 0.0211

PRO 82 LEU 83 0.0001

LEU 83 ILE 84 0.0002

ILE 84 ALA 85 -0.0302

ALA 85 GLU 86 0.0002

GLU 86 SER 87 -0.0000

SER 87 ALA 88 -0.0144

ALA 88 ARG 89 0.0003

ARG 89 TYR 90 -0.0001

TYR 90 ALA 91 0.0145

ALA 91 ASP 92 -0.0003

ASP 92 ASP 93 -0.0002

ASP 93 TYR 94 -0.0259

TYR 94 SER 95 -0.0001

SER 95 TRP 96 0.0001

TRP 96 VAL 97 0.0049

VAL 97 GLU 98 -0.0002

GLU 98 VAL 99 0.0003

VAL 99 ALA 100 0.0091

ALA 100 ILE 101 0.0001

ILE 101 ASN 102 -0.0002

ASN 102 PRO 103 0.0123

PRO 103 ARG 104 0.0001

ARG 104 ALA 105 0.0003

ALA 105 ARG 106 -0.0099

ARG 106 PHE 107 0.0001

PHE 107 HIS 108 -0.0002

HIS 108 ASP 109 0.0042

ASP 109 GLY 110 0.0003

GLY 110 SER 111 -0.0003

SER 111 PRO 112 0.0105

PRO 112 ILE 113 -0.0001

ILE 113 THR 114 -0.0002

THR 114 ALA 115 0.0151

ALA 115 ARG 116 0.0001

ARG 116 ASP 117 -0.0000

ASP 117 VAL 118 0.0044

VAL 118 GLU 119 -0.0001

GLU 119 PHE 120 -0.0001

PHE 120 THR 121 0.0016

THR 121 PHE 122 -0.0003

PHE 122 GLN 123 0.0000

GLN 123 LYS 124 0.0118

LYS 124 PHE 125 0.0002

PHE 125 MET 126 -0.0001

MET 126 THR 127 0.0030

THR 127 GLU 128 0.0001

GLU 128 GLY 129 0.0001

GLY 129 VAL 130 0.0232

VAL 130 PRO 131 0.0001

PRO 131 GLN 132 0.0001

GLN 132 PHE 133 0.0364

PHE 133 ARG 134 -0.0001

ARG 134 LEU 135 0.0000

LEU 135 VAL 136 -0.0058

VAL 136 TYR 137 0.0004

TYR 137 LYS 138 -0.0002

LYS 138 GLY 139 0.0342

GLY 139 THR 140 -0.0002

THR 140 THR 141 0.0002

THR 141 VAL 142 -0.0037

VAL 142 LYS 143 -0.0003

LYS 143 ALA 144 -0.0000

ALA 144 ILE 145 0.0153

ILE 145 ALA 146 -0.0000

ALA 146 PRO 147 -0.0001

PRO 147 LEU 148 0.0021

LEU 148 THR 149 -0.0003

THR 149 VAL 150 0.0001

VAL 150 ARG 151 0.0170

ARG 151 ILE 152 -0.0002

ILE 152 GLU 153 0.0003

GLU 153 LEU 154 0.0048

LEU 154 ALA 155 -0.0003

ALA 155 LYS 156 -0.0001

LYS 156 PRO 157 -0.0172

PRO 157 GLY 158 -0.0001

GLY 158 LYS 159 0.0005

LYS 159 GLU 160 0.0014

GLU 160 ASP 161 0.0004

ASP 161 MET 162 -0.0004

MET 162 MET 162 -0.0021

MET 162 LEU 163 0.0062

LEU 163 SER 164 0.0000

SER 164 LEU 165 -0.0000

LEU 165 PHE 166 0.0093

PHE 166 SER 167 -0.0003

SER 167 LEU 168 0.0003

LEU 168 PRO 169 -0.0192

PRO 169 VAL 170 -0.0005

VAL 170 PHE 171 0.0002

PHE 171 PRO 172 -0.0012

PRO 172 GLU 173 -0.0003

GLU 173 LYS 174 0.0002

LYS 174 TYR 175 -0.0024

TYR 175 TRP 176 0.0005

TRP 176 LYS 177 0.0001

LYS 177 ASP 178 -0.0004

ASP 178 HIS 179 -0.0001

HIS 179 LYS 180 0.0002

LYS 180 LEU 181 -0.0014

LEU 181 SER 182 -0.0004

SER 182 ASP 183 -0.0002

ASP 183 PRO 184 0.0106

PRO 184 LEU 185 -0.0001

LEU 185 ALA 186 -0.0000

ALA 186 THR 187 0.0081

THR 187 PRO 188 -0.0000

PRO 188 PRO 189 -0.0000

PRO 189 LEU 190 -0.0104

LEU 190 ALA 191 -0.0004

ALA 191 SER 192 0.0004

SER 192 GLY 193 -0.0101

GLY 193 PRO 194 -0.0001

PRO 194 TYR 195 0.0001

TYR 195 ARG 196 0.0187

ARG 196 VAL 197 -0.0002

VAL 197 THR 198 0.0004

THR 198 SER 199 -0.0244

SER 199 TRP 200 -0.0002

TRP 200 LYS 201 0.0001

LYS 201 MET 202 -0.0027

MET 202 GLY 203 0.0001

GLY 203 GLN 204 -0.0003

GLN 204 ASN 205 -0.0038

ASN 205 ILE 206 -0.0002

ILE 206 VAL 207 -0.0003

VAL 207 TYR 208 -0.0109

TYR 208 SER 209 -0.0004

SER 209 ARG 210 0.0004

ARG 210 VAL 211 -0.0235

VAL 211 LYS 212 0.0000

LYS 212 ASP 213 -0.0001

ASP 213 TYR 214 -0.0151

TYR 214 TRP 215 0.0003

TRP 215 ALA 216 -0.0001

ALA 216 ALA 217 0.0140

ALA 217 ASN 218 0.0001

ASN 218 ASN 218 0.0412

ASN 218 LEU 219 0.0001

LEU 219 PRO 220 0.0144

PRO 220 VAL 221 -0.0000

VAL 221 ASN 222 -0.0002

ASN 222 ARG 223 -0.0130

ARG 223 GLY 224 0.0002

GLY 224 ARG 225 0.0002

ARG 225 TRP 226 -0.0016

TRP 226 ASN 227 -0.0000

ASN 227 PHE 228 0.0000

PHE 228 ASP 229 -0.0050

ASP 229 THR 230 0.0002

THR 230 ILE 231 0.0000

ILE 231 ARG 232 0.0010

ARG 232 TYR 233 0.0003

TYR 233 ASP 234 0.0003

ASP 234 TYR 235 -0.0311

TYR 235 TYR 236 -0.0000

TYR 236 LEU 237 -0.0000

LEU 237 ASP 238 -0.0059

ASP 238 ASP 239 -0.0000

ASP 239 ASN 240 -0.0002

ASN 240 VAL 241 -0.0189

VAL 241 ALA 242 0.0002

ALA 242 PHE 243 0.0001

PHE 243 GLU 244 -0.0130

GLU 244 ALA 245 -0.0001

ALA 245 PHE 246 0.0002

PHE 246 LYS 247 -0.0175

LYS 247 ALA 248 -0.0001

ALA 248 GLY 249 0.0000

GLY 249 ALA 250 -0.0963

ALA 250 PHE 251 0.0000

PHE 251 ASP 252 -0.0000

ASP 252 LEU 253 -0.0593

LEU 253 ARG 254 -0.0000

ARG 254 MET 255 0.0005

MET 255 GLU 256 -0.0152

GLU 256 ASN 257 -0.0004

ASN 257 ASP 258 -0.0000

ASP 258 ALA 259 0.0130

ALA 259 LYS 260 -0.0001

LYS 260 ASN 261 0.0000

ASN 261 TRP 262 0.0315

TRP 262 ALA 263 -0.0000

ALA 263 THR 264 0.0001

THR 264 ARG 265 -0.0136

ARG 265 TYR 266 0.0001

TYR 266 THR 267 -0.0001

THR 267 GLY 268 0.0678

GLY 268 LYS 269 -0.0002

LYS 269 ASN 270 0.0005

ASN 270 PHE 271 -0.0217

PHE 271 ASP 272 0.0000

ASP 272 LYS 273 0.0002

LYS 273 LYS 274 -0.0344

LYS 274 TYR 275 -0.0001

TYR 275 ILE 276 0.0000

ILE 276 ILE 277 0.0282

ILE 277 LYS 278 0.0003

LYS 278 ASP 279 0.0001

ASP 279 GLU 280 0.0227

GLU 280 GLN 281 0.0003

GLN 281 LYS 282 -0.0001

LYS 282 ASN 283 -0.0107

ASN 283 GLU 284 0.0001

GLU 284 SER 285 0.0001

SER 285 ALA 286 0.0137

ALA 286 GLN 287 0.0003

GLN 287 ASP 288 -0.0003

ASP 288 THR 289 0.0198

THR 289 ARG 290 0.0003

ARG 290 TRP 291 -0.0002

TRP 291 LEU 292 0.0141

LEU 292 ALA 293 -0.0002

ALA 293 PHE 294 -0.0002

PHE 294 ASN 295 -0.0039

ASN 295 ILE 296 0.0000

ILE 296 GLN 297 -0.0002

GLN 297 ARG 298 0.0094

ARG 298 PRO 299 -0.0000

PRO 299 VAL 300 0.0000

VAL 300 PHE 301 0.0030

PHE 301 SER 302 0.0002

SER 302 ASP 303 0.0002

ASP 303 ARG 304 -0.0019

ARG 304 ARG 305 -0.0001

ARG 305 VAL 306 0.0002

VAL 306 ARG 307 -0.0019

ARG 307 GLU 308 -0.0005

GLU 308 ALA 309 -0.0001

ALA 309 ILE 310 -0.0009

ILE 310 THR 311 0.0000

THR 311 LEU 312 -0.0000

LEU 312 ALA 313 0.0001

ALA 313 PHE 314 -0.0001

PHE 314 ASP 315 0.0002

ASP 315 PHE 316 -0.0192

PHE 316 GLU 317 0.0000

GLU 317 TRP 318 -0.0003

TRP 318 MET 319 -0.0286

MET 319 ASN 320 0.0000

ASN 320 LYS 321 0.0003

LYS 321 ALA 322 -0.0015

ALA 322 LEU 323 0.0001

LEU 323 PHE 324 -0.0003

PHE 324 TYR 325 0.0445

TYR 325 ASN 326 -0.0003

ASN 326 ASN 326 -0.0010

ASN 326 ALA 327 0.0004

ALA 327 TRP 328 -0.0312

TRP 328 SER 329 0.0003

SER 329 ARG 330 0.0005

ARG 330 THR 331 0.0246

THR 331 ASN 332 0.0000

ASN 332 SER 333 -0.0004

SER 333 TYR 334 0.0170

TYR 334 PHE 335 0.0001

PHE 335 GLN 336 -0.0003

GLN 336 ASN 337 -0.0206

ASN 337 THR 338 -0.0003

THR 338 GLU 339 0.0001

GLU 339 TYR 340 -0.0164

TYR 340 ALA 341 -0.0002

ALA 341 ALA 342 0.0005

ALA 342 ARG 343 0.0220

ARG 343 ASN 344 -0.0002

ASN 344 TYR 345 -0.0001

TYR 345 PRO 346 -0.0034

PRO 346 ASP 347 0.0001

ASP 347 ALA 348 -0.0000

ALA 348 ALA 349 -0.0052

ALA 349 GLU 350 -0.0003

GLU 350 LEU 351 -0.0001

LEU 351 VAL 352 -0.0012

VAL 352 LEU 353 0.0001

LEU 353 LEU 354 0.0002

LEU 354 ALA 355 -0.0183

ALA 355 PRO 356 0.0002

PRO 356 MET 357 0.0003

MET 357 LYS 358 0.0038

LYS 358 LYS 359 0.0001

LYS 359 ASP 360 0.0001

ASP 360 LEU 361 -0.0192

LEU 361 PRO 362 -0.0001

PRO 362 SER 363 -0.0002

SER 363 GLU 364 -0.0089

GLU 364 VAL 365 -0.0001

VAL 365 PHE 366 -0.0001

PHE 366 THR 367 -0.0009

THR 367 GLN 368 0.0003

GLN 368 ILE 369 -0.0002

ILE 369 TYR 370 -0.0083

TYR 370 GLN 371 0.0003

GLN 371 PRO 372 0.0001

PRO 372 PRO 373 0.0682

PRO 373 VAL 374 -0.0002

VAL 374 SER 375 0.0002

SER 375 LYS 376 0.0384

LYS 376 GLY 377 0.0002

GLY 377 ASP 378 0.0002

ASP 378 GLY 379 -0.0072

GLY 379 TYR 380 -0.0001

TYR 380 ASP 381 -0.0000

ASP 381 ARG 382 -0.0338

ARG 382 ASP 383 -0.0002

ASP 383 ASN 384 -0.0002

ASN 384 LEU 385 -0.0168

LEU 385 LEU 386 0.0000

LEU 386 LYS 387 0.0000

LYS 387 ALA 388 -0.0015

ALA 388 ASP 389 -0.0000

ASP 389 LYS 390 -0.0002

LYS 390 LEU 391 0.0121

LEU 391 LEU 392 -0.0002

LEU 392 ASN 393 -0.0001

ASN 393 GLU 394 0.0104

GLU 394 ALA 395 0.0002

ALA 395 GLY 396 -0.0001

GLY 396 TRP 397 0.0089

TRP 397 VAL 398 0.0003

VAL 398 LEU 399 -0.0000

LEU 399 LYS 400 -0.0043

LYS 400 GLY 401 -0.0000

GLY 401 GLN 402 0.0002

GLN 402 GLN 403 0.0014

GLN 403 GLN 403 0.0023

GLN 403 ARG 404 0.0000

ARG 404 VAL 405 0.0001

VAL 405 ASN 406 0.0017

ASN 406 ALA 407 -0.0004

ALA 407 THR 408 -0.0000

THR 408 THR 409 0.0040

THR 409 GLY 410 0.0002

GLY 410 GLN 411 0.0001

GLN 411 PRO 412 0.0198

PRO 412 LEU 413 0.0001

LEU 413 SER 414 0.0001

SER 414 PHE 415 0.0660

PHE 415 GLU 416 0.0002

GLU 416 LEU 417 0.0001

LEU 417 LEU 418 0.0099

LEU 418 LEU 419 -0.0002

LEU 419 PRO 420 -0.0000

PRO 420 ALA 421 -0.0090

ALA 421 SER 422 -0.0002

SER 422 SER 423 0.0002

SER 423 ASN 424 -0.0036

ASN 424 SER 425 -0.0004

SER 425 GLN 426 -0.0002

GLN 426 TRP 427 -0.0061

TRP 427 VAL 428 -0.0001

VAL 428 LEU 429 0.0002

LEU 429 PRO 430 -0.0079

PRO 430 PHE 431 -0.0003

PHE 431 GLN 432 0.0003

GLN 432 HIS 433 -0.0104

HIS 433 SER 434 0.0001

SER 434 SER 434 0.0000

SER 434 LEU 435 -0.0001

LEU 435 GLN 436 -0.0019

GLN 436 ARG 437 0.0002

ARG 437 LEU 438 0.0003

LEU 438 GLY 439 -0.0070

GLY 439 ILE 440 0.0002

ILE 440 ASN 441 0.0002

ASN 441 MET 442 0.0228

MET 442 ASP 443 0.0004

ASP 443 ILE 444 -0.0001

ILE 444 ARG 445 -0.0016

ARG 445 LYS 446 0.0002

LYS 446 VAL 447 -0.0003

VAL 447 ASP 448 0.0058

ASP 448 ASN 449 -0.0001

ASN 449 SER 450 0.0002

SER 450 GLN 451 0.0192

GLN 451 ILE 452 -0.0002

ILE 452 THR 453 0.0002

THR 453 ASN 454 0.0056

ASN 454 ARG 455 0.0000

ARG 455 MET 456 0.0001

MET 456 MET 456 0.0000

MET 456 ARG 457 -0.0040

ARG 457 SER 458 -0.0004

SER 458 ARG 459 0.0001

ARG 459 ASP 460 0.0095

ASP 460 TYR 461 0.0000

TYR 461 ASP 462 -0.0000

ASP 462 MET 463 -0.0011

MET 463 MET 464 -0.0001

MET 464 PRO 465 -0.0001

PRO 465 ARG 466 0.0124

ARG 466 VAL 467 -0.0001

VAL 467 TRP 468 -0.0003

TRP 468 ARG 469 0.0160

ARG 469 ALA 470 -0.0002

ALA 470 MET 471 0.0002

MET 471 PRO 472 -0.0040

PRO 472 TRP 473 -0.0003

TRP 473 PRO 474 0.0000

PRO 474 SER 475 -0.0079

SER 475 SER 476 -0.0002

SER 476 ASP 477 0.0003

ASP 477 LEU 478 0.0157

LEU 478 GLN 479 0.0000

GLN 479 ILE 480 0.0003

ILE 480 SER 481 0.0475

SER 481 TRP 482 -0.0002

TRP 482 SER 483 0.0004

SER 483 SER 484 -0.0273

SER 484 SER 484 -0.0023

SER 484 GLU 485 0.0001

GLU 485 TYR 486 0.0001

TYR 486 ILE 487 0.0160

ILE 487 ASN 488 0.0003

ASN 488 SER 489 0.0003

SER 489 THR 490 0.0141

THR 490 TYR 491 0.0000

TYR 491 ASN 492 0.0002

ASN 492 ALA 493 0.0305

ALA 493 PRO 494 0.0000

PRO 494 GLY 495 -0.0001

GLY 495 VAL 496 -0.0138

VAL 496 GLN 497 -0.0002

GLN 497 SER 498 0.0000

SER 498 PRO 499 -0.0158

PRO 499 VAL 500 0.0001

VAL 500 ILE 501 -0.0002

ILE 501 ASP 502 0.0113

ASP 502 SER 503 0.0001

SER 503 LEU 504 0.0002

LEU 504 ILE 505 0.0181

ILE 505 ASN 506 0.0001

ASN 506 GLN 507 0.0001

GLN 507 ILE 508 -0.0119

ILE 508 ILE 509 0.0002

ILE 509 ALA 510 -0.0003

ALA 510 ALA 511 -0.0146

ALA 511 GLN 512 0.0002

GLN 512 GLY 513 -0.0000

GLY 513 ASN 514 -0.0046

ASN 514 LYS 515 0.0000

LYS 515 GLU 516 -0.0002

GLU 516 LYS 517 -0.0021

LYS 517 LEU 518 -0.0002

LEU 518 LEU 519 0.0001

LEU 519 PRO 520 -0.0198

PRO 520 LEU 521 0.0001

LEU 521 GLY 522 0.0001

GLY 522 ARG 523 0.0123

ARG 523 ALA 524 0.0001

ALA 524 LEU 525 0.0001

LEU 525 ASP 526 0.0101

ASP 526 ARG 527 0.0002

ARG 527 VAL 528 0.0001

VAL 528 LEU 529 -0.0095

LEU 529 THR 530 0.0002

THR 530 TRP 531 -0.0001

TRP 531 ASN 532 0.0084

ASN 532 TYR 533 0.0001

TYR 533 TYR 534 -0.0003

TYR 534 MET 535 -0.0105

MET 535 LEU 536 0.0001

LEU 536 PRO 537 0.0001

PRO 537 MET 538 -0.0217

MET 538 TRP 539 0.0000

TRP 539 TYR 540 -0.0000

TYR 540 MET 541 0.0189

MET 541 ALA 542 0.0001

ALA 542 GLU 543 0.0003

GLU 543 ASP 544 -0.0867

ASP 544 ARG 545 -0.0002

ARG 545 LEU 546 -0.0003

LEU 546 ALA 547 -0.1003

ALA 547 TRP 548 0.0002

TRP 548 TRP 549 -0.0001

TRP 549 ASP 550 0.0392

ASP 550 LYS 551 0.0000

LYS 551 PHE 552 -0.0001

PHE 552 SER 553 -0.0172

SER 553 GLN 554 -0.0001

GLN 554 PRO 555 0.0003

PRO 555 ALA 556 0.0113

ALA 556 VAL 557 0.0002

VAL 557 ARG 558 0.0001

ARG 558 PRO 559 -0.0117

PRO 559 ILE 560 -0.0003

ILE 560 TYR 561 0.0003

TYR 561 SER 562 -0.0968

SER 562 LEU 563 -0.0003

LEU 563 GLY 564 -0.0003

GLY 564 ILE 565 -0.0458

ILE 565 ASP 566 -0.0001

ASP 566 THR 567 -0.0001

THR 567 TRP 568 -0.0441

TRP 568 TRP 569 -0.0004

TRP 569 TYR 570 0.0000

TYR 570 ASP 571 -0.0044

ASP 571 VAL 572 -0.0000

VAL 572 ASN 573 -0.0003

ASN 573 LYS 574 0.0089

LYS 574 ALA 575 0.0003

ALA 575 ALA 576 0.0003

ALA 576 LYS 577 -0.2022

LYS 577 LEU 578 -0.0003

LEU 578 PRO 579 -0.0001

PRO 579 SER 580 0.0555

SER 580 LEU 1 -0.8088

LEU 1 GLY 2 -0.0000

GLY 2 GLU 3 -0.0002

GLU 3 PRO 4 -0.0109

PRO 4 ARG 5 0.0000

ARG 5 TYR 6 -0.0003

TYR 6 ALA 7 0.0260

ALA 7 PHE 8 0.0001

PHE 8 ASN 9 0.0002

ASN 9 PHE 10 -0.0218

PHE 10 ASN 11 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.

*** YejA NMA ***

CA strain for 240125141212352800

--- normal mode 11 ---

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

* YejA NMA *