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

* *

CA strain for 2407051440252305910

--- normal mode 10 ---

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 -0.0000

SER 2 LEU 3 -0.0024

LEU 3 ARG 4 -0.0001

ARG 4 ALA 5 -0.0102

ALA 5 ASN 6 0.0002

ASN 6 ASP 7 0.0086

ASP 7 ALA 8 -0.0001

ALA 8 PRO 9 0.0422

PRO 9 ILE 10 -0.0001

ILE 10 VAL 11 0.0385

VAL 11 LEU 12 0.0004

LEU 12 LEU 13 0.0570

LEU 13 HIS 14 -0.0000

HIS 14 GLY 15 -0.0515

GLY 15 PHE 16 -0.0002

PHE 16 THR 17 -0.0003

THR 17 GLY 18 0.0003

GLY 18 TRP 19 -0.0154

TRP 19 GLY 20 0.0000

GLY 20 ARG 21 0.1129

ARG 21 GLU 22 -0.0003

GLU 22 GLU 23 0.1383

GLU 23 MET 24 0.0004

MET 24 PHE 25 -0.1719

PHE 25 GLY 26 -0.0002

GLY 26 PHE 27 0.1691

PHE 27 LYS 28 0.0000

LYS 28 TYR 29 0.0214

TYR 29 TRP 30 0.0000

TRP 30 GLY 31 -0.0186

GLY 31 GLY 32 0.0001

GLY 32 VAL 33 0.0021

VAL 33 ARG 34 0.0003

ARG 34 GLY 35 0.0344

GLY 35 ASP 36 -0.0000

ASP 36 ILE 37 -0.0076

ILE 37 GLU 38 0.0001

GLU 38 GLN 39 0.0069

GLN 39 TRP 40 -0.0001

TRP 40 LEU 41 -0.0064

LEU 41 ASN 42 0.0003

ASN 42 ASP 43 0.0121

ASP 43 ASN 44 0.0000

ASN 44 GLY 45 0.0073

GLY 45 TYR 46 -0.0001

TYR 46 ARG 47 0.1219

ARG 47 THR 48 0.0004

THR 48 TYR 49 0.0525

TYR 49 THR 50 -0.0000

THR 50 LEU 51 0.0380

LEU 51 ALA 52 0.0003

ALA 52 VAL 53 0.0758

VAL 53 GLY 54 0.0001

GLY 54 PRO 55 -0.0509

PRO 55 LEU 56 -0.0002

LEU 56 SER 57 -0.0141

SER 57 SER 58 -0.0002

SER 58 ASN 59 0.0119

ASN 59 TRP 60 -0.0002

TRP 60 ASP 61 -0.0414

ASP 61 ARG 62 0.0001

ARG 62 ALA 63 0.0135

ALA 63 CYS 64 -0.0003

CYS 64 GLU 65 -0.0612

GLU 65 ALA 66 0.0003

ALA 66 TYR 67 -0.0423

TYR 67 ALA 68 -0.0002

ALA 68 GLN 69 -0.0300

GLN 69 LEU 70 -0.0002

LEU 70 VAL 71 -0.0312

VAL 71 GLY 72 0.0001

GLY 72 GLY 73 0.1365

GLY 73 THR 74 0.0002

THR 74 VAL 75 -0.0085

VAL 75 ASP 76 0.0001

ASP 76 TYR 77 0.0055

TYR 77 GLY 78 0.0003

GLY 78 ALA 79 -0.0601

ALA 79 ALA 80 0.0000

ALA 80 HIS 81 -0.0315

HIS 81 ALA 82 -0.0001

ALA 82 ALA 83 0.0321

ALA 83 LYS 84 0.0001

LYS 84 HIS 85 -0.0149

HIS 85 GLY 86 0.0002

GLY 86 HIS 87 0.0288

HIS 87 ALA 88 0.0004

ALA 88 ARG 89 -0.1015

ARG 89 PHE 90 0.0001

PHE 90 GLY 91 -0.1573

GLY 91 ARG 92 -0.0002

ARG 92 THR 93 0.1041

THR 93 TYR 94 0.0001

TYR 94 PRO 95 0.0567

PRO 95 GLY 96 -0.0001

GLY 96 LEU 97 0.0714

LEU 97 LEU 98 0.0005

LEU 98 PRO 99 -0.0595

PRO 99 GLU 100 0.0001

GLU 100 LEU 101 0.0126

LEU 101 LYS 102 -0.0001

LYS 102 ARG 103 0.0183

ARG 103 GLY 104 0.0004

GLY 104 GLY 105 0.0495

GLY 105 ARG 106 -0.0001

ARG 106 ILE 107 -0.0196

ILE 107 HIS 108 0.0001

HIS 108 ILE 109 0.0070

ILE 109 ILE 110 -0.0001

ILE 110 ALA 111 -0.0033

ALA 111 HIS 112 0.0001

HIS 112 SER 113 -0.0333

SER 113 GLN 114 0.0000

GLN 114 GLY 115 0.0144

GLY 115 GLY 116 0.0004

GLY 116 GLN 117 0.0053

GLN 117 THR 118 -0.0002

THR 118 ALA 119 0.0238

ALA 119 ARG 120 -0.0000

ARG 120 MET 121 -0.0049

MET 121 LEU 122 0.0003

LEU 122 VAL 123 0.0058

VAL 123 SER 124 -0.0000

SER 124 LEU 125 0.0256

LEU 125 LEU 126 -0.0002

LEU 126 GLU 127 -0.0061

GLU 127 ASN 128 0.0000

ASN 128 GLY 129 0.0558

GLY 129 SER 130 -0.0003

SER 130 GLN 131 -0.0112

GLN 131 GLU 132 -0.0004

GLU 132 GLU 133 -0.0023

GLU 133 ARG 134 0.0000

ARG 134 GLU 135 -0.0158

GLU 135 TYR 136 0.0001

TYR 136 ALA 137 -0.0153

ALA 137 LYS 138 -0.0003

LYS 138 ALA 139 0.0195

ALA 139 HIS 140 -0.0002

HIS 140 ASN 141 -0.0142

ASN 141 VAL 142 -0.0001

VAL 142 SER 143 0.0912

SER 143 LEU 144 0.0001

LEU 144 SER 145 -0.0017

SER 145 PRO 146 -0.0003

PRO 146 LEU 147 0.0153

LEU 147 PHE 148 -0.0003

PHE 148 GLU 149 -0.0350

GLU 149 GLY 150 0.0001

GLY 150 GLY 151 0.0142

GLY 151 HIS 152 0.0002

HIS 152 HIS 153 0.0618

HIS 153 PHE 154 -0.0002

PHE 154 VAL 155 0.0167

VAL 155 LEU 156 0.0001

LEU 156 SER 157 0.0073

SER 157 VAL 158 -0.0002

VAL 158 THR 159 0.0219

THR 159 THR 160 0.0000

THR 160 ILE 161 0.0320

ILE 161 ALA 162 -0.0001

ALA 162 THR 163 0.0055

THR 163 PRO 164 -0.0003

PRO 164 HIS 165 0.0463

HIS 165 ASP 166 -0.0001

ASP 166 GLY 167 0.0452

GLY 167 THR 168 -0.0002

THR 168 THR 169 -0.0216

THR 169 LEU 170 0.0000

LEU 170 SER 171 -0.0996

SER 171 ASN 172 -0.0002

ASN 172 MET 173 0.1277

MET 173 VAL 174 -0.0001

VAL 174 ASP 175 -0.1274

ASP 175 PHE 176 -0.0001

PHE 176 THR 177 -0.0980

THR 177 ASP 178 0.0001

ASP 178 ARG 179 -0.1402

ARG 179 PHE 180 0.0001

PHE 180 PHE 181 0.0041

PHE 181 ASP 182 -0.0002

ASP 182 LEU 183 -0.0942

LEU 183 GLN 184 -0.0002

GLN 184 LYS 185 0.0488

LYS 185 ALA 186 -0.0000

ALA 186 VAL 187 -0.1039

VAL 187 LEU 188 -0.0002

LEU 188 GLU 189 -0.0267

GLU 189 ALA 190 -0.0002

ALA 190 ALA 191 -0.0031

ALA 191 ALA 192 -0.0002

ALA 192 VAL 193 -0.1357

VAL 193 ALA 194 -0.0004

ALA 194 SER 195 0.1180

SER 195 ASN 196 -0.0003

ASN 196 VAL 197 0.0205

VAL 197 PRO 198 0.0003

PRO 198 TYR 199 0.1089

TYR 199 THR 200 -0.0001

THR 200 SER 201 -0.0695

SER 201 GLN 202 -0.0001

GLN 202 VAL 203 0.1372

VAL 203 TYR 204 0.0001

TYR 204 ASP 205 -0.1560

ASP 205 PHE 206 0.0000

PHE 206 LYS 207 -0.1119

LYS 207 LEU 208 -0.0001

LEU 208 ASP 209 -0.0593

ASP 209 GLN 210 0.0002

GLN 210 TRP 211 0.0874

TRP 211 GLY 212 -0.0001

GLY 212 LEU 213 -0.0413

LEU 213 ARG 214 -0.0001

ARG 214 ARG 215 -0.1713

ARG 215 GLN 216 -0.0002

GLN 216 PRO 217 -0.0337

PRO 217 GLY 218 -0.0002

GLY 218 GLU 219 -0.0721

GLU 219 SER 220 -0.0001

SER 220 PHE 221 -0.0085

PHE 221 ASP 222 0.0003

ASP 222 HIS 223 -0.0106

HIS 223 TYR 224 -0.0000

TYR 224 PHE 225 -0.1094

PHE 225 GLU 226 0.0003

GLU 226 ARG 227 -0.0278

ARG 227 LEU 228 0.0001

LEU 228 LYS 229 -0.0742

LYS 229 ARG 230 0.0001

ARG 230 SER 231 0.1278

SER 231 PRO 232 -0.0004

PRO 232 VAL 233 -0.0079

VAL 233 TRP 234 0.0000

TRP 234 THR 235 0.0692

THR 235 SER 236 -0.0001

SER 236 THR 237 -0.0713

THR 237 ASP 238 -0.0001

ASP 238 THR 239 0.0390

THR 239 ALA 240 0.0002

ALA 240 ARG 241 -0.0753

ARG 241 TYR 242 -0.0002

TYR 242 ASP 243 -0.0108

ASP 243 LEU 244 0.0003

LEU 244 SER 245 -0.0380

SER 245 VAL 246 0.0001

VAL 246 SER 247 0.0261

SER 247 GLY 248 -0.0001

GLY 248 ALA 249 -0.0569

ALA 249 GLU 250 0.0004

GLU 250 LYS 251 -0.0419

LYS 251 LEU 252 0.0004

LEU 252 ASN 253 -0.0020

ASN 253 GLN 254 0.0001

GLN 254 TRP 255 0.0058

TRP 255 VAL 256 -0.0000

VAL 256 GLN 257 -0.0149

GLN 257 ALA 258 0.0000

ALA 258 SER 259 0.0025

SER 259 PRO 260 0.0001

PRO 260 ASN 261 -0.0206

ASN 261 THR 262 -0.0004

THR 262 TYR 263 0.0389

TYR 263 TYR 264 0.0003

TYR 264 LEU 265 0.0380

LEU 265 SER 266 0.0000

SER 266 PHE 267 0.0313

PHE 267 SER 268 -0.0001

SER 268 THR 269 0.0121

THR 269 GLU 270 -0.0002

GLU 270 ARG 271 -0.0050

ARG 271 THR 272 -0.0001

THR 272 TYR 273 0.1308

TYR 273 ARG 274 -0.0001

ARG 274 GLY 275 0.1169

GLY 275 ALA 276 -0.0000

ALA 276 LEU 277 0.1867

LEU 277 THR 278 -0.0001

THR 278 GLY 279 -0.2843

GLY 279 ASN 280 -0.0003

ASN 280 HIS 281 0.0115

HIS 281 TYR 282 -0.0003

TYR 282 PRO 283 0.2307

PRO 283 GLU 284 -0.0001

GLU 284 LEU 285 0.0044

LEU 285 GLY 286 0.0002

GLY 286 MET 287 -0.0326

MET 287 ASN 288 -0.0001

ASN 288 ALA 289 -0.0916

ALA 289 PHE 290 -0.0005

PHE 290 SER 291 0.1779

SER 291 ALA 292 0.0000

ALA 292 VAL 293 -0.1266

VAL 293 VAL 294 -0.0004

VAL 294 CYS 295 0.0090

CYS 295 ALA 296 -0.0000

ALA 296 PRO 297 0.0179

PRO 297 PHE 298 -0.0002

PHE 298 LEU 299 0.0068

LEU 299 GLY 300 0.0001

GLY 300 SER 301 0.0128

SER 301 TYR 302 0.0004

TYR 302 ARG 303 0.0252

ARG 303 ASN 304 0.0000

ASN 304 PRO 305 -0.0060

PRO 305 THR 306 0.0002

THR 306 LEU 307 -0.0871

LEU 307 GLY 308 -0.0001

GLY 308 ILE 309 0.0468

ILE 309 ASP 310 0.0003

ASP 310 ASP 311 0.0034

ASP 311 ARG 312 0.0000

ARG 312 TRP 313 -0.0308

TRP 313 LEU 314 0.0000

LEU 314 GLU 315 0.0618

GLU 315 ASN 316 -0.0002

ASN 316 ASP 317 0.0658

ASP 317 GLY 318 -0.0000

GLY 318 ILE 319 -0.0187

ILE 319 VAL 320 -0.0001

VAL 320 ASN 321 0.0067

ASN 321 THR 322 -0.0000

THR 322 VAL 323 0.0415

VAL 323 SER 324 0.0000

SER 324 MET 325 -0.0381

MET 325 ASN 326 0.0002

ASN 326 GLY 327 0.0213

GLY 327 PRO 328 0.0001

PRO 328 LYS 329 0.0002

LYS 329 ARG 330 0.0001

ARG 330 GLY 331 -0.0053

GLY 331 SER 332 -0.0000

SER 332 SER 333 0.0106

SER 333 ASP 334 0.0001

ASP 334 ARG 335 -0.0031

ARG 335 ILE 336 0.0002

ILE 336 VAL 337 -0.0302

VAL 337 PRO 338 -0.0001

PRO 338 TYR 339 -0.0106

TYR 339 ASP 340 0.0001

ASP 340 GLY 341 -0.0154

GLY 341 THR 342 0.0003

THR 342 LEU 343 0.0105

LEU 343 LYS 344 -0.0002

LYS 344 LYS 345 0.0663

LYS 345 GLY 346 0.0000

GLY 346 VAL 347 0.0072

VAL 347 TRP 348 0.0004

TRP 348 ASN 349 -0.0002

ASN 349 ASP 350 -0.0000

ASP 350 MET 351 0.0214

MET 351 GLY 352 0.0002

GLY 352 THR 353 0.0076

THR 353 TYR 354 0.0002

TYR 354 ASN 355 -0.0019

ASN 355 VAL 356 -0.0002

VAL 356 ASP 357 -0.0564

ASP 357 HIS 358 0.0003

HIS 358 LEU 359 0.0992

LEU 359 GLU 360 0.0001

GLU 360 ILE 361 0.0124

ILE 361 ILE 362 -0.0001

ILE 362 GLY 363 -0.0063

GLY 363 VAL 364 0.0003

VAL 364 ASP 365 0.0855

ASP 365 PRO 366 -0.0005

PRO 366 ASN 367 0.0437

ASN 367 PRO 368 -0.0001

PRO 368 SER 369 -0.0077

SER 369 PHE 370 -0.0004

PHE 370 ASP 371 0.0042

ASP 371 ILE 372 -0.0002

ILE 372 ARG 373 0.0053

ARG 373 ALA 374 -0.0000

ALA 374 PHE 375 -0.0046

PHE 375 TYR 376 -0.0002

TYR 376 LEU 377 -0.0190

LEU 377 ARG 378 0.0001

ARG 378 LEU 379 0.0068

LEU 379 ALA 380 -0.0004

ALA 380 GLU 381 0.0040

GLU 381 GLN 382 -0.0000

GLN 382 LEU 383 0.0298

LEU 383 ALA 384 -0.0003

ALA 384 SER 385 0.0107

SER 385 LEU 386 -0.0003

LEU 386 ARG 387 -0.0050

ARG 387 PRO 388 0.0002

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 2407051440252305910

--- normal mode 10 ---

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

* *