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

* *

CA strain for 2407051425092282339

--- normal mode 9 ---

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
ALA 1 SER 2 -0.0001

SER 2 LEU 3 0.0178

LEU 3 ARG 4 0.0001

ARG 4 ALA 5 -0.0766

ALA 5 ASN 6 0.0001

ASN 6 ASP 7 -0.0268

ASP 7 ALA 8 0.0001

ALA 8 PRO 9 0.0007

PRO 9 ILE 10 0.0004

ILE 10 VAL 11 0.0088

VAL 11 LEU 12 -0.0002

LEU 12 LEU 13 0.0088

LEU 13 HIS 14 0.0001

HIS 14 GLY 15 -0.0254

GLY 15 PHE 16 0.0003

PHE 16 THR 17 0.0206

THR 17 GLY 18 -0.0000

GLY 18 TRP 19 -0.0146

TRP 19 GLY 20 -0.0000

GLY 20 ARG 21 -0.0029

ARG 21 GLU 22 -0.0000

GLU 22 GLU 23 0.0095

GLU 23 MET 24 -0.0004

MET 24 PHE 25 -0.0349

PHE 25 GLY 26 -0.0000

GLY 26 PHE 27 0.0441

PHE 27 LYS 28 0.0002

LYS 28 TYR 29 -0.0034

TYR 29 TRP 30 0.0003

TRP 30 GLY 31 -0.0072

GLY 31 GLY 32 -0.0003

GLY 32 VAL 33 0.0067

VAL 33 ARG 34 -0.0000

ARG 34 GLY 35 -0.0196

GLY 35 ASP 36 -0.0002

ASP 36 ILE 37 -0.0027

ILE 37 GLU 38 0.0002

GLU 38 GLN 39 0.0093

GLN 39 TRP 40 0.0000

TRP 40 LEU 41 -0.0170

LEU 41 ASN 42 -0.0004

ASN 42 ASP 43 0.0097

ASP 43 ASN 44 -0.0000

ASN 44 GLY 45 0.0089

GLY 45 TYR 46 0.0001

TYR 46 ARG 47 0.0553

ARG 47 THR 48 0.0002

THR 48 TYR 49 0.0416

TYR 49 THR 50 0.0001

THR 50 LEU 51 0.0478

LEU 51 ALA 52 -0.0001

ALA 52 VAL 53 -0.0050

VAL 53 GLY 54 -0.0001

GLY 54 PRO 55 -0.0653

PRO 55 LEU 56 -0.0004

LEU 56 SER 57 -0.0195

SER 57 SER 58 0.0002

SER 58 ASN 59 -0.0035

ASN 59 TRP 60 -0.0001

TRP 60 ASP 61 0.0122

ASP 61 ARG 62 0.0002

ARG 62 ALA 63 -0.0324

ALA 63 CYS 64 0.0002

CYS 64 GLU 65 0.0040

GLU 65 ALA 66 -0.0002

ALA 66 TYR 67 -0.0206

TYR 67 ALA 68 -0.0000

ALA 68 GLN 69 0.0153

GLN 69 LEU 70 0.0000

LEU 70 VAL 71 -0.0217

VAL 71 GLY 72 0.0000

GLY 72 GLY 73 0.0240

GLY 73 THR 74 0.0003

THR 74 VAL 75 -0.0013

VAL 75 ASP 76 0.0002

ASP 76 TYR 77 -0.0061

TYR 77 GLY 78 0.0000

GLY 78 ALA 79 0.0053

ALA 79 ALA 80 -0.0003

ALA 80 HIS 81 -0.0056

HIS 81 ALA 82 0.0001

ALA 82 ALA 83 0.0157

ALA 83 LYS 84 -0.0001

LYS 84 HIS 85 -0.0170

HIS 85 GLY 86 -0.0001

GLY 86 HIS 87 0.0165

HIS 87 ALA 88 0.0000

ALA 88 ARG 89 -0.0206

ARG 89 PHE 90 0.0001

PHE 90 GLY 91 -0.0118

GLY 91 ARG 92 0.0003

ARG 92 THR 93 -0.0240

THR 93 TYR 94 -0.0001

TYR 94 PRO 95 -0.0291

PRO 95 GLY 96 0.0001

GLY 96 LEU 97 0.0404

LEU 97 LEU 98 -0.0001

LEU 98 PRO 99 -0.0222

PRO 99 GLU 100 0.0004

GLU 100 LEU 101 0.0126

LEU 101 LYS 102 0.0001

LYS 102 ARG 103 -0.0031

ARG 103 GLY 104 0.0000

GLY 104 GLY 105 0.0955

GLY 105 ARG 106 0.0001

ARG 106 ILE 107 -0.0152

ILE 107 HIS 108 0.0001

HIS 108 ILE 109 0.0049

ILE 109 ILE 110 -0.0001

ILE 110 ALA 111 0.0069

ALA 111 HIS 112 -0.0000

HIS 112 SER 113 -0.0065

SER 113 GLN 114 -0.0002

GLN 114 GLY 115 -0.0097

GLY 115 GLY 116 0.0004

GLY 116 GLN 117 -0.0181

GLN 117 THR 118 0.0003

THR 118 ALA 119 -0.0180

ALA 119 ARG 120 0.0003

ARG 120 MET 121 0.0158

MET 121 LEU 122 0.0001

LEU 122 VAL 123 -0.0190

VAL 123 SER 124 0.0000

SER 124 LEU 125 0.0139

LEU 125 LEU 126 -0.0001

LEU 126 GLU 127 0.0010

GLU 127 ASN 128 -0.0001

ASN 128 GLY 129 -0.0351

GLY 129 SER 130 -0.0000

SER 130 GLN 131 -0.0139

GLN 131 GLU 132 0.0001

GLU 132 GLU 133 0.0066

GLU 133 ARG 134 0.0003

ARG 134 GLU 135 -0.0203

GLU 135 TYR 136 -0.0001

TYR 136 ALA 137 -0.0061

ALA 137 LYS 138 -0.0001

LYS 138 ALA 139 0.0073

ALA 139 HIS 140 -0.0002

HIS 140 ASN 141 -0.0025

ASN 141 VAL 142 -0.0002

VAL 142 SER 143 0.0122

SER 143 LEU 144 -0.0000

LEU 144 SER 145 0.0147

SER 145 PRO 146 0.0001

PRO 146 LEU 147 0.0077

LEU 147 PHE 148 -0.0002

PHE 148 GLU 149 -0.0088

GLU 149 GLY 150 0.0002

GLY 150 GLY 151 -0.0349

GLY 151 HIS 152 -0.0002

HIS 152 HIS 153 -0.0639

HIS 153 PHE 154 0.0002

PHE 154 VAL 155 0.0422

VAL 155 LEU 156 0.0000

LEU 156 SER 157 0.0543

SER 157 VAL 158 -0.0002

VAL 158 THR 159 0.0337

THR 159 THR 160 0.0000

THR 160 ILE 161 0.0376

ILE 161 ALA 162 0.0001

ALA 162 THR 163 -0.0237

THR 163 PRO 164 -0.0001

PRO 164 HIS 165 -0.0201

HIS 165 ASP 166 0.0001

ASP 166 GLY 167 0.0023

GLY 167 THR 168 0.0000

THR 168 THR 169 0.0008

THR 169 LEU 170 0.0003

LEU 170 VAL 171 -0.0530

VAL 171 ASN 172 0.0000

ASN 172 MET 173 0.0553

MET 173 VAL 174 -0.0004

VAL 174 ASP 175 -0.0854

ASP 175 PHE 176 -0.0003

PHE 176 THR 177 -0.2376

THR 177 ASP 178 0.0003

ASP 178 ARG 179 -0.1018

ARG 179 PHE 180 -0.0000

PHE 180 PHE 181 -0.1253

PHE 181 ASP 182 -0.0000

ASP 182 LEU 183 0.0086

LEU 183 GLN 184 0.0001

GLN 184 LYS 185 0.0243

LYS 185 ALA 186 0.0000

ALA 186 VAL 187 -0.0385

VAL 187 LEU 188 -0.0001

LEU 188 GLU 189 -0.0068

GLU 189 ALA 190 0.0001

ALA 190 ALA 191 -0.0419

ALA 191 ALA 192 -0.0001

ALA 192 VAL 193 0.0022

VAL 193 ALA 194 -0.0001

ALA 194 SER 195 0.0337

SER 195 ASN 196 0.0003

ASN 196 VAL 197 0.0266

VAL 197 PRO 198 -0.0001

PRO 198 TYR 199 0.0249

TYR 199 THR 200 -0.0002

THR 200 SER 201 0.0299

SER 201 GLN 202 0.0001

GLN 202 VAL 203 0.1365

VAL 203 TYR 204 0.0003

TYR 204 ASP 205 -0.0296

ASP 205 PHE 206 -0.0002

PHE 206 LYS 207 -0.0459

LYS 207 LEU 208 -0.0001

LEU 208 ASP 209 -0.0143

ASP 209 GLN 210 -0.0002

GLN 210 TRP 211 -0.0074

TRP 211 GLY 212 0.0000

GLY 212 LEU 213 0.0036

LEU 213 ARG 214 -0.0002

ARG 214 ARG 215 0.0374

ARG 215 GLN 216 -0.0001

GLN 216 PRO 217 -0.0282

PRO 217 GLY 218 0.0001

GLY 218 GLU 219 -0.0845

GLU 219 SER 220 -0.0001

SER 220 PHE 221 0.0190

PHE 221 ASP 222 0.0003

ASP 222 HIS 223 0.0602

HIS 223 TYR 224 -0.0000

TYR 224 PHE 225 -0.1147

PHE 225 GLU 226 0.0001

GLU 226 ARG 227 0.0208

ARG 227 LEU 228 -0.0001

LEU 228 LYS 229 -0.0992

LYS 229 ARG 230 -0.0003

ARG 230 SER 231 0.0457

SER 231 PRO 232 -0.0001

PRO 232 VAL 233 0.0086

VAL 233 TRP 234 0.0001

TRP 234 THR 235 0.0341

THR 235 SER 236 0.0002

SER 236 THR 237 -0.0045

THR 237 ASP 238 0.0002

ASP 238 THR 239 0.0096

THR 239 ALA 240 0.0000

ALA 240 ARG 241 -0.0328

ARG 241 TYR 242 0.0003

TYR 242 ASP 243 -0.0055

ASP 243 LEU 244 -0.0002

LEU 244 SER 245 -0.0286

SER 245 VAL 246 -0.0001

VAL 246 SER 247 -0.0050

SER 247 GLY 248 0.0001

GLY 248 ALA 249 -0.0072

ALA 249 GLU 250 0.0000

GLU 250 LYS 251 0.0137

LYS 251 LEU 252 0.0001

LEU 252 ASN 253 0.0065

ASN 253 GLN 254 -0.0003

GLN 254 TRP 255 0.0353

TRP 255 VAL 256 0.0003

VAL 256 GLN 257 -0.0521

GLN 257 ALA 258 -0.0000

ALA 258 SER 259 0.0488

SER 259 PRO 260 0.0001

PRO 260 ASN 261 -0.0000

ASN 261 THR 262 -0.0001

THR 262 TYR 263 0.0110

TYR 263 TYR 264 -0.0003

TYR 264 LEU 265 0.0641

LEU 265 SER 266 -0.0002

SER 266 PHE 267 0.0508

PHE 267 SER 268 0.0003

SER 268 THR 269 0.1441

THR 269 GLU 270 0.0002

GLU 270 ARG 271 0.0525

ARG 271 THR 272 0.0004

THR 272 TYR 273 0.2100

TYR 273 ARG 274 -0.0002

ARG 274 GLY 275 0.1870

GLY 275 ALA 276 0.0002

ALA 276 LEU 277 0.2116

LEU 277 THR 278 -0.0000

THR 278 GLY 279 0.1799

GLY 279 ASN 280 -0.0001

ASN 280 HIS 281 0.1272

HIS 281 TYR 282 -0.0001

TYR 282 PRO 283 -0.1637

PRO 283 GLU 284 0.0003

GLU 284 LEU 285 0.0323

LEU 285 GLY 286 0.0000

GLY 286 MET 287 -0.0083

MET 287 ASN 288 -0.0004

ASN 288 ALA 289 0.0242

ALA 289 PHE 290 0.0006

PHE 290 SER 291 -0.0255

SER 291 ALA 292 0.0005

ALA 292 VAL 293 0.0036

VAL 293 VAL 294 0.0002

VAL 294 CYS 295 0.0470

CYS 295 ALA 296 -0.0002

ALA 296 PRO 297 0.0074

PRO 297 PHE 298 0.0003

PHE 298 LEU 299 0.0130

LEU 299 GLY 300 -0.0003

GLY 300 SER 301 0.0317

SER 301 TYR 302 0.0002

TYR 302 ARG 303 -0.0230

ARG 303 ASN 304 0.0003

ASN 304 PRO 305 -0.0381

PRO 305 THR 306 0.0003

THR 306 LEU 307 -0.0080

LEU 307 GLY 308 -0.0001

GLY 308 ILE 309 0.0114

ILE 309 ASP 310 0.0002

ASP 310 ASP 311 -0.0306

ASP 311 ARG 312 -0.0002

ARG 312 TRP 313 -0.0606

TRP 313 LEU 314 -0.0001

LEU 314 GLU 315 0.0284

GLU 315 ASN 316 -0.0002

ASN 316 ASP 317 0.0100

ASP 317 GLY 318 0.0002

GLY 318 ILE 319 -0.0264

ILE 319 VAL 320 0.0003

VAL 320 ASN 321 0.0047

ASN 321 THR 322 -0.0001

THR 322 VAL 323 -0.0917

VAL 323 SER 324 0.0002

SER 324 MET 325 0.0591

MET 325 ASN 326 0.0002

ASN 326 GLY 327 0.0011

GLY 327 PRO 328 -0.0001

PRO 328 LYS 329 0.0089

LYS 329 ARG 330 0.0000

ARG 330 GLY 331 0.0113

GLY 331 SER 332 0.0003

SER 332 SER 333 0.0288

SER 333 ASP 334 -0.0003

ASP 334 ARG 335 -0.0431

ARG 335 ILE 336 0.0002

ILE 336 VAL 337 -0.0123

VAL 337 PRO 338 -0.0001

PRO 338 TYR 339 -0.0356

TYR 339 ASP 340 -0.0002

ASP 340 GLY 341 0.0169

GLY 341 THR 342 0.0003

THR 342 LEU 343 -0.0248

LEU 343 LYS 344 -0.0003

LYS 344 LYS 345 -0.0138

LYS 345 GLY 346 -0.0001

GLY 346 VAL 347 0.0640

VAL 347 TRP 348 0.0001

TRP 348 ASN 349 -0.0187

ASN 349 ASP 350 -0.0002

ASP 350 MET 351 -0.0677

MET 351 GLY 352 -0.0000

GLY 352 THR 353 0.2459

THR 353 TYR 354 0.0004

TYR 354 ASN 355 0.1471

ASN 355 VAL 356 0.0003

VAL 356 ASP 357 -0.0386

ASP 357 HIS 358 -0.0002

HIS 358 LEU 359 0.0053

LEU 359 GLU 360 0.0004

GLU 360 ILE 361 -0.0160

ILE 361 ILE 362 -0.0001

ILE 362 GLY 363 -0.0066

GLY 363 VAL 364 -0.0002

VAL 364 ASP 365 0.0050

ASP 365 PRO 366 0.0001

PRO 366 ASN 367 0.0436

ASN 367 PRO 368 -0.0001

PRO 368 SER 369 0.0068

SER 369 PHE 370 -0.0004

PHE 370 ASP 371 -0.0021

ASP 371 ILE 372 -0.0001

ILE 372 ARG 373 0.0287

ARG 373 ALA 374 -0.0001

ALA 374 PHE 375 -0.0300

PHE 375 TYR 376 0.0005

TYR 376 LEU 377 0.0410

LEU 377 ARG 378 0.0001

ARG 378 LEU 379 -0.0398

LEU 379 ALA 380 -0.0003

ALA 380 GLU 381 0.0458

GLU 381 GLN 382 -0.0002

GLN 382 LEU 383 0.0017

LEU 383 ALA 384 -0.0001

ALA 384 SER 385 -0.0124

SER 385 LEU 386 0.0000

LEU 386 ARG 387 0.0508

ARG 387 PRO 388 0.0000

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.

*** ***

CA strain for 2407051425092282339

--- normal mode 9 ---

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

* *