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

* EXP_1IKQ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA strain for 24021912353031383

--- 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
LYS 1 ARG 2 -0.0002

ARG 2 TRP 3 -0.0001

TRP 3 SER 4 0.1308

SER 4 GLU 5 0.0001

GLU 5 TRP 6 0.0006

TRP 6 ALA 7 -0.0535

ALA 7 SER 8 0.0002

SER 8 GLY 9 -0.0005

GLY 9 LYS 10 -0.0379

LYS 10 VAL 11 -0.0000

VAL 11 LEU 12 -0.0002

LEU 12 CYS 13 0.0106

CYS 13 LEU 14 0.0001

LEU 14 LEU 15 0.0002

LEU 15 ASP 16 -0.0721

ASP 16 PRO 17 0.0001

PRO 17 LEU 18 -0.0002

LEU 18 ASP 19 0.0379

ASP 19 GLY 20 -0.0001

GLY 20 VAL 21 -0.0001

VAL 21 TYR 22 0.1221

TYR 22 ASN 23 0.0001

ASN 23 TYR 24 0.0002

TYR 24 LEU 25 -0.0978

LEU 25 ALA 26 -0.0002

ALA 26 GLN 27 0.0000

GLN 27 GLN 28 -0.1070

GLN 28 ARG 29 0.0004

ARG 29 CYS 30 -0.0002

CYS 30 ASN 31 -0.1041

ASN 31 LEU 32 0.0001

LEU 32 ASP 33 -0.0001

ASP 33 ASP 34 0.1374

ASP 34 THR 35 -0.0002

THR 35 TRP 36 -0.0002

TRP 36 GLU 37 0.0327

GLU 37 GLY 38 -0.0002

GLY 38 LYS 39 -0.0000

LYS 39 ILE 40 -0.0310

ILE 40 TYR 41 0.0000

TYR 41 ARG 42 0.0000

ARG 42 VAL 43 0.0087

VAL 43 LEU 44 -0.0001

LEU 44 ALA 45 0.0001

ALA 45 GLY 46 -0.0644

GLY 46 ASN 47 -0.0006

ASN 47 PRO 48 0.0002

PRO 48 ALA 49 -0.0866

ALA 49 LYS 50 0.0002

LYS 50 HIS 51 -0.0002

HIS 51 ASP 52 -0.0730

ASP 52 LEU 53 -0.0000

LEU 53 ASP 54 -0.0002

ASP 54 ILE 55 -0.1298

ILE 55 LYS 56 -0.0001

LYS 56 PRO 57 0.0002

PRO 57 THR 58 -0.0193

THR 58 VAL 59 -0.0001

VAL 59 ILE 60 0.0000

ILE 60 SER 61 -0.0683

SER 61 HIS 62 -0.0001

HIS 62 ARG 63 -0.0001

ARG 63 LEU 64 -0.0998

LEU 64 HIS 65 0.0001

HIS 65 PHE 66 0.0002

PHE 66 PRO 67 -0.0238

PRO 67 GLU 68 0.0003

GLU 68 GLY 69 -0.0001

GLY 69 GLY 70 -0.0195

GLY 70 SER 71 0.0000

SER 71 LEU 72 0.0003

LEU 72 ALA 73 0.0100

ALA 73 ALA 74 -0.0000

ALA 74 LEU 75 -0.0001

LEU 75 THR 76 0.0147

THR 76 ALA 77 -0.0002

ALA 77 HIS 78 0.0004

HIS 78 GLN 79 -0.0175

GLN 79 ALA 80 -0.0003

ALA 80 CYS 81 -0.0002

CYS 81 HIS 82 -0.0556

HIS 82 LEU 83 -0.0001

LEU 83 PRO 84 0.0003

PRO 84 LEU 85 0.1121

LEU 85 GLU 86 -0.0004

GLU 86 THR 87 0.0003

THR 87 PHE 88 0.0300

PHE 88 THR 89 -0.0000

THR 89 ARG 90 0.0000

ARG 90 HIS 91 -0.0515

HIS 91 ARG 92 -0.0003

ARG 92 GLN 93 0.0004

GLN 93 PRO 94 0.0136

PRO 94 ARG 95 -0.0001

ARG 95 GLY 96 0.0005

GLY 96 TRP 97 -0.1403

TRP 97 GLU 98 0.0002

GLU 98 GLN 99 -0.0002

GLN 99 LEU 100 0.0322

LEU 100 GLU 101 -0.0003

GLU 101 GLN 102 -0.0001

GLN 102 CYS 103 0.0028

CYS 103 GLY 104 -0.0000

GLY 104 TYR 105 0.0001

TYR 105 PRO 106 0.0158

PRO 106 VAL 107 -0.0003

VAL 107 GLN 108 -0.0002

GLN 108 ARG 109 -0.0391

ARG 109 LEU 110 0.0004

LEU 110 VAL 111 -0.0001

VAL 111 ALA 112 0.0182

ALA 112 LEU 113 0.0002

LEU 113 TYR 114 0.0000

TYR 114 LEU 115 0.0100

LEU 115 ALA 116 0.0003

ALA 116 ALA 117 -0.0000

ALA 117 ARG 118 0.0138

ARG 118 LEU 119 0.0002

LEU 119 SER 120 -0.0002

SER 120 TRP 121 0.0024

TRP 121 ASN 122 0.0001

ASN 122 GLN 123 0.0001

GLN 123 VAL 124 0.0006

VAL 124 ASP 125 -0.0002

ASP 125 GLN 126 0.0001

GLN 126 VAL 127 0.0269

VAL 127 ILE 128 0.0003

ILE 128 ARG 129 -0.0004

ARG 129 ASN 130 0.0200

ASN 130 ALA 131 0.0001

ALA 131 LEU 132 0.0000

LEU 132 ALA 133 -0.0445

ALA 133 SER 134 -0.0001

SER 134 PRO 135 -0.0001

PRO 135 GLY 136 0.0214

GLY 136 SER 137 0.0003

SER 137 GLY 138 -0.0004

GLY 138 GLY 139 -0.0292

GLY 139 ASP 140 -0.0002

ASP 140 LEU 141 0.0001

LEU 141 GLY 142 -0.0032

GLY 142 GLU 143 0.0000

GLU 143 ALA 144 -0.0000

ALA 144 ILE 145 0.0054

ILE 145 ARG 146 0.0003

ARG 146 GLU 147 -0.0000

GLU 147 GLN 148 0.0005

GLN 148 PRO 149 -0.0002

PRO 149 GLU 150 0.0002

GLU 150 GLN 151 0.0606

GLN 151 ALA 152 0.0004

ALA 152 ARG 153 0.0000

ARG 153 LEU 154 0.0004

LEU 154 ALA 155 0.0001

ALA 155 LEU 156 -0.0001

LEU 156 THR 157 -0.0005

THR 157 LEU 158 -0.0003

LEU 158 ALA 159 -0.0003

ALA 159 ALA 160 -0.0091

ALA 160 ALA 161 0.0005

ALA 161 GLU 162 -0.0001

GLU 162 SER 163 -0.0510

SER 163 GLU 164 0.0002

GLU 164 ARG 165 0.0002

ARG 165 PHE 166 -0.0683

PHE 166 VAL 167 0.0000

VAL 167 ARG 168 -0.0002

ARG 168 GLN 169 -0.0119

GLN 169 GLY 170 -0.0000

GLY 170 THR 171 -0.0002

THR 171 GLY 172 0.0307

GLY 172 ASN 173 -0.0002

ASN 173 ASP 174 -0.0000

ASP 174 GLU 175 0.0093

GLU 175 ALA 176 0.0001

ALA 176 GLY 177 -0.0001

GLY 177 ALA 178 -0.0116

ALA 178 ALA 179 -0.0001

ALA 179 ASN 180 0.0001

ASN 180 ALA 181 0.0026

ALA 181 ASP 182 0.0001

ASP 182 VAL 183 -0.0001

VAL 183 VAL 184 -0.0315

VAL 184 SER 185 0.0001

SER 185 LEU 186 0.0003

LEU 186 THR 187 0.0599

THR 187 CYS 188 0.0000

CYS 188 PRO 189 -0.0000

PRO 189 VAL 190 -0.0199

VAL 190 ALA 191 -0.0000

ALA 191 ALA 192 0.0002

ALA 192 GLY 193 -0.0842

GLY 193 GLU 194 -0.0004

GLU 194 CYS 195 -0.0000

CYS 195 ALA 196 -0.1084

ALA 196 GLY 197 0.0002

GLY 197 PRO 198 -0.0002

PRO 198 ALA 199 0.0674

ALA 199 ASP 200 0.0001

ASP 200 SER 201 -0.0001

SER 201 GLY 202 0.0113

GLY 202 ASP 203 -0.0000

ASP 203 ALA 204 0.0000

ALA 204 LEU 205 -0.0081

LEU 205 LEU 206 -0.0004

LEU 206 GLU 207 -0.0001

GLU 207 ARG 208 -0.0607

ARG 208 ASN 209 -0.0004

ASN 209 TYR 210 -0.0001

TYR 210 PRO 211 0.1097

PRO 211 THR 212 -0.0001

THR 212 GLY 213 -0.0001

GLY 213 ALA 214 -0.0084

ALA 214 GLU 215 -0.0001

GLU 215 PHE 216 -0.0001

PHE 216 LEU 217 0.0167

LEU 217 GLY 218 0.0002

GLY 218 ASP 219 -0.0004

ASP 219 GLY 220 -0.0057

GLY 220 GLY 221 -0.0001

GLY 221 ASP 222 0.0002

ASP 222 VAL 223 -0.0309

VAL 223 SER 224 0.0003

SER 224 PHE 225 -0.0002

PHE 225 SER 226 0.0604

SER 226 THR 227 -0.0004

THR 227 ARG 228 -0.0002

ARG 228 GLY 229 -0.0493

GLY 229 THR 230 -0.0003

THR 230 GLN 231 0.0002

GLN 231 ASN 232 -0.0675

ASN 232 TRP 233 -0.0002

TRP 233 THR 234 -0.0001

THR 234 VAL 235 -0.0020

VAL 235 GLU 236 0.0001

GLU 236 ARG 237 -0.0003

ARG 237 LEU 238 -0.0096

LEU 238 LEU 239 0.0001

LEU 239 GLN 240 -0.0003

GLN 240 ALA 241 0.0113

ALA 241 HIS 242 -0.0001

HIS 242 ARG 243 0.0001

ARG 243 GLN 244 0.0238

GLN 244 LEU 245 0.0002

LEU 245 GLU 246 -0.0002

GLU 246 GLU 247 0.0082

GLU 247 ARG 248 0.0002

ARG 248 GLY 249 -0.0001

GLY 249 TYR 250 -0.0222

TYR 250 VAL 251 -0.0000

VAL 251 PHE 252 0.0000

PHE 252 VAL 253 0.0025

VAL 253 GLY 254 0.0001

GLY 254 TYR 255 0.0001

TYR 255 HIS 256 0.0301

HIS 256 GLY 257 -0.0002

GLY 257 THR 258 -0.0001

THR 258 PHE 259 0.1062

PHE 259 LEU 260 0.0000

LEU 260 GLU 261 -0.0002

GLU 261 ALA 262 -0.0079

ALA 262 ALA 263 -0.0001

ALA 263 GLN 264 -0.0003

GLN 264 SER 265 -0.0168

SER 265 ILE 266 0.0001

ILE 266 VAL 267 0.0001

VAL 267 PHE 268 0.0431

PHE 268 GLY 269 -0.0000

GLY 269 GLY 270 -0.0004

GLY 270 VAL 271 -0.0041

VAL 271 ARG 272 0.0001

ARG 272 ALA 273 0.0001

ALA 273 ARG 274 0.0752

ARG 274 SER 275 -0.0002

SER 275 GLN 276 -0.0001

GLN 276 ASP 277 -0.0105

ASP 277 LEU 278 -0.0001

LEU 278 ASP 279 -0.0002

ASP 279 ALA 280 0.1119

ALA 280 ILE 281 0.0001

ILE 281 TRP 282 -0.0003

TRP 282 ARG 283 -0.0638

ARG 283 GLY 284 0.0001

GLY 284 PHE 285 -0.0000

PHE 285 TYR 286 -0.0501

TYR 286 ILE 287 -0.0001

ILE 287 ALA 288 -0.0001

ALA 288 GLY 289 -0.1096

GLY 289 ASP 290 -0.0000

ASP 290 PRO 291 0.0003

PRO 291 ALA 292 0.0342

ALA 292 LEU 293 -0.0002

LEU 293 ALA 294 0.0001

ALA 294 TYR 295 0.0429

TYR 295 GLY 296 -0.0000

GLY 296 TYR 297 -0.0001

TYR 297 ALA 298 0.0721

ALA 298 GLN 299 0.0000

GLN 299 ASP 300 -0.0002

ASP 300 GLN 301 -0.1710

GLN 301 GLU 302 0.0000

GLU 302 PRO 303 0.0002

PRO 303 ASP 304 -0.0310

ASP 304 ALA 305 0.0000

ALA 305 ARG 306 0.0003

ARG 306 GLY 307 0.0780

GLY 307 ARG 308 0.0001

ARG 308 ILE 309 -0.0003

ILE 309 ARG 310 -0.1230

ARG 310 ASN 311 0.0000

ASN 311 GLY 312 0.0002

GLY 312 ALA 313 -0.0711

ALA 313 LEU 314 -0.0003

LEU 314 LEU 315 0.0003

LEU 315 ARG 316 -0.0067

ARG 316 VAL 317 0.0003

VAL 317 TYR 318 -0.0000

TYR 318 VAL 319 -0.0161

VAL 319 PRO 320 0.0001

PRO 320 ARG 321 0.0003

ARG 321 SER 322 0.0103

SER 322 SER 323 -0.0001

SER 323 LEU 324 -0.0003

LEU 324 PRO 325 -0.0221

PRO 325 GLY 326 -0.0000

GLY 326 PHE 327 0.0001

PHE 327 TYR 328 -0.0783

TYR 328 ARG 329 -0.0002

ARG 329 THR 330 -0.0001

THR 330 SER 331 -0.0576

SER 331 LEU 332 -0.0001

LEU 332 THR 333 -0.0001

THR 333 LEU 334 -0.0310

LEU 334 ALA 335 0.0002

ALA 335 ALA 336 -0.0003

ALA 336 PRO 337 0.0184

PRO 337 GLU 338 -0.0000

GLU 338 ALA 339 0.0001

ALA 339 ALA 340 -0.0265

ALA 340 GLY 341 0.0001

GLY 341 GLU 342 0.0000

GLU 342 VAL 343 -0.0351

VAL 343 GLU 344 -0.0002

GLU 344 ARG 345 -0.0000

ARG 345 LEU 346 -0.0022

LEU 346 ILE 347 0.0001

ILE 347 GLY 348 -0.0001

GLY 348 HIS 349 0.0250

HIS 349 PRO 350 0.0001

PRO 350 LEU 351 0.0001

LEU 351 PRO 352 0.0055

PRO 352 LEU 353 -0.0002

LEU 353 ARG 354 -0.0002

ARG 354 LEU 355 0.0829

LEU 355 ASP 356 -0.0003

ASP 356 ALA 357 -0.0001

ALA 357 ILE 358 -0.0702

ILE 358 THR 359 0.0003

THR 359 GLY 360 0.0002

GLY 360 PRO 361 -0.0976

PRO 361 GLU 362 -0.0002

GLU 362 GLU 363 -0.0002

GLU 363 GLU 364 0.0407

GLU 364 GLY 365 -0.0000

GLY 365 GLY 366 -0.0002

GLY 366 ARG 367 0.0807

ARG 367 LEU 368 -0.0002

LEU 368 GLU 369 0.0003

GLU 369 THR 370 -0.0980

THR 370 ILE 371 0.0003

ILE 371 LEU 372 -0.0001

LEU 372 GLY 373 -0.0688

GLY 373 TRP 374 -0.0000

TRP 374 PRO 375 0.0001

PRO 375 LEU 376 0.0896

LEU 376 ALA 377 -0.0001

ALA 377 GLU 378 0.0001

GLU 378 ARG 379 0.0912

ARG 379 THR 380 0.0003

THR 380 VAL 381 0.0002

VAL 381 VAL 382 -0.0107

VAL 382 ILE 383 -0.0004

ILE 383 PRO 384 0.0002

PRO 384 SER 385 0.0495

SER 385 ALA 386 0.0004

ALA 386 ILE 387 -0.0002

ILE 387 PRO 388 -0.0575

PRO 388 THR 389 0.0000

THR 389 ASP 390 0.0000

ASP 390 PRO 391 -0.0445

PRO 391 ARG 392 -0.0002

ARG 392 ASN 393 -0.0005

ASN 393 VAL 394 -0.0171

VAL 394 GLY 395 0.0001

GLY 395 GLY 396 -0.0004

GLY 396 ASP 397 0.0239

ASP 397 LEU 398 0.0004

LEU 398 ASP 399 0.0000

ASP 399 PRO 400 0.0100

PRO 400 SER 401 0.0003

SER 401 SER 402 -0.0000

SER 402 ILE 403 -0.0156

ILE 403 PRO 404 -0.0002

PRO 404 ASP 405 0.0002

ASP 405 LYS 406 0.0170

LYS 406 GLU 407 -0.0000

GLU 407 GLN 408 -0.0001

GLN 408 ALA 409 0.0062

ALA 409 ILE 410 0.0002

ILE 410 SER 411 -0.0002

SER 411 ALA 412 0.0418

ALA 412 LEU 413 -0.0000

LEU 413 PRO 414 0.0003

PRO 414 ASP 415 0.0383

ASP 415 TYR 416 -0.0001

TYR 416 ALA 417 -0.0001

ALA 417 SER 418 -0.0877

SER 418 GLN 419 0.0002

GLN 419 PRO 420 0.0002

PRO 420 GLY 421 -0.0434

GLY 421 LYS 422 -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.

*** EXP_1IKQ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA strain for 24021912353031383

--- normal mode 11 ---

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

* EXP_1IKQ_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *