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

* *

CA strain for 2405271642113669817

--- normal mode 8 ---

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
HIS 4 PRO 5 0.0001

PRO 5 PRO 6 -0.0114

PRO 6 VAL 7 -0.0003

VAL 7 VAL 8 -0.0608

VAL 8 LEU 9 -0.0003

LEU 9 VAL 10 0.0119

VAL 10 PRO 11 0.0000

PRO 11 GLY 12 0.1106

GLY 12 ASP 13 -0.0002

ASP 13 LEU 14 -0.0892

LEU 14 GLY 15 -0.0000

GLY 15 ASN 16 -0.0933

ASN 16 GLN 17 0.0002

GLN 17 LEU 18 -0.1092

LEU 18 GLU 19 0.0001

GLU 19 ALA 20 -0.2327

ALA 20 LYS 21 0.0001

LYS 21 LEU 22 -0.2283

LEU 22 ASP 23 0.0000

ASP 23 LYS 24 -0.0282

LYS 24 PRO 25 -0.0001

PRO 25 THR 26 0.0099

THR 26 VAL 27 0.0001

VAL 27 VAL 28 -0.0258

VAL 28 HIS 29 -0.0001

HIS 29 TYR 30 0.0798

TYR 30 LEU 31 0.0000

LEU 31 CYS 32 -0.0711

CYS 32 SER 33 0.0001

SER 33 LYS 34 0.0409

LYS 34 LYS 35 -0.0004

LYS 35 THR 36 -0.1090

THR 36 GLU 37 -0.0001

GLU 37 SER 38 -0.1566

SER 38 TYR 39 0.0001

TYR 39 PHE 40 0.0298

PHE 40 THR 41 -0.0001

THR 41 ILE 42 0.0308

ILE 42 TRP 43 0.0003

TRP 43 LEU 44 0.0285

LEU 44 ASN 45 0.0002

ASN 45 LEU 46 -0.0044

LEU 46 GLU 47 0.0002

GLU 47 LEU 48 0.0973

LEU 48 LEU 49 -0.0000

LEU 49 LEU 50 0.0425

LEU 50 PRO 51 0.0002

PRO 51 VAL 52 -0.0158

VAL 52 ILE 53 0.0001

ILE 53 ILE 54 -0.0146

ILE 54 ASP 55 0.0000

ASP 55 CYS 56 0.0435

CYS 56 TRP 57 0.0001

TRP 57 ILE 58 0.1488

ILE 58 ASP 59 -0.0003

ASP 59 ASN 60 -0.0157

ASN 60 ILE 61 0.0000

ILE 61 ARG 62 0.0453

ARG 62 LEU 63 0.0000

LEU 63 VAL 64 0.0209

VAL 64 TYR 65 0.0000

TYR 65 ASN 66 -0.0184

ASN 66 LYS 67 -0.0001

LYS 67 THR 68 0.0072

THR 68 SER 69 -0.0000

SER 69 ARG 70 0.0006

ARG 70 ALA 71 -0.0003

ALA 71 THR 72 0.0576

THR 72 GLN 73 -0.0002

GLN 73 PHE 74 0.1349

PHE 74 PRO 75 -0.0000

PRO 75 ASP 76 0.0968

ASP 76 GLY 77 -0.0001

GLY 77 VAL 78 -0.1244

VAL 78 ASP 79 0.0002

ASP 79 VAL 80 -0.1891

VAL 80 ARG 81 0.0003

ARG 81 VAL 82 -0.4321

VAL 82 PRO 83 -0.0002

PRO 83 GLY 84 -0.3327

GLY 84 PHE 85 -0.0000

PHE 85 GLY 86 -0.2114

GLY 86 LYS 87 0.0001

LYS 87 THR 88 0.0492

THR 88 PHE 89 -0.0001

PHE 89 SER 90 0.0056

SER 90 LEU 91 0.0000

LEU 91 GLU 92 -0.0220

GLU 92 PHE 93 -0.0002

PHE 93 LEU 94 0.0856

LEU 94 ASP 95 -0.0003

ASP 95 PRO 96 0.0184

PRO 96 SER 97 -0.0001

SER 97 LYS 98 -0.0471

LYS 98 SER 99 -0.0002

SER 99 SER 100 -0.0074

SER 100 VAL 101 -0.0002

VAL 101 GLY 102 -0.0199

GLY 102 SER 103 0.0000

SER 103 TYR 104 -0.1057

TYR 104 PHE 105 0.0005

PHE 105 HIS 106 0.0594

HIS 106 THR 107 -0.0006

THR 107 MET 108 -0.0126

MET 108 VAL 109 -0.0000

VAL 109 GLU 110 -0.0216

GLU 110 SER 111 0.0000

SER 111 LEU 112 0.0155

LEU 112 VAL 113 -0.0002

VAL 113 GLY 114 -0.0222

GLY 114 TRP 115 -0.0001

TRP 115 GLY 116 0.0053

GLY 116 TYR 117 0.0005

TYR 117 THR 118 -0.0078

THR 118 ARG 119 0.0000

ARG 119 GLY 120 -0.0141

GLY 120 GLU 121 -0.0002

GLU 121 GLU 121 -0.0134

GLU 121 ASP 122 -0.0104

ASP 122 VAL 123 0.0001

VAL 123 ARG 124 -0.0692

ARG 124 GLY 125 -0.0003

GLY 125 ALA 126 -0.0396

ALA 126 PRO 127 -0.0004

PRO 127 TYR 128 -0.0864

TYR 128 ASP 129 0.0001

ASP 129 TRP 130 0.0598

TRP 130 ARG 131 -0.0003

ARG 131 ARG 132 0.0047

ARG 132 ALA 133 0.0004

ALA 133 PRO 134 -0.0271

PRO 134 ASN 135 0.0001

ASN 135 GLU 136 -0.0006

GLU 136 ASN 137 0.0002

ASN 137 GLY 138 -0.0927

GLY 138 PRO 139 -0.0003

PRO 139 TYR 140 0.0589

TYR 140 PHE 141 -0.0001

PHE 141 LEU 142 -0.0345

LEU 142 ALA 143 0.0000

ALA 143 LEU 144 0.0403

LEU 144 ARG 145 -0.0002

ARG 145 GLU 146 0.0221

GLU 146 GLU 146 0.1752

GLU 146 MET 147 0.0002

MET 147 ILE 148 -0.0075

ILE 148 GLU 149 0.0000

GLU 149 GLU 149 -0.0059

GLU 149 GLU 150 0.0348

GLU 150 GLU 150 0.0094

GLU 150 MET 151 0.0003

MET 151 TYR 152 0.0061

TYR 152 GLN 153 -0.0001

GLN 153 LEU 154 0.0406

LEU 154 TYR 155 0.0002

TYR 155 GLY 156 0.0107

GLY 156 GLY 157 0.0001

GLY 157 PRO 158 0.0101

PRO 158 VAL 159 0.0004

VAL 159 VAL 160 0.0474

VAL 160 LEU 161 -0.0001

LEU 161 VAL 162 0.0364

VAL 162 ALA 163 -0.0000

ALA 163 HIS 164 0.0406

HIS 164 SER 165 0.0000

SER 165 MET 166 0.0370

MET 166 GLY 167 -0.0003

GLY 167 ASN 168 -0.0281

ASN 168 MET 169 -0.0003

MET 169 TYR 170 -0.0336

TYR 170 THR 171 -0.0003

THR 171 LEU 172 -0.0194

LEU 172 TYR 173 -0.0001

TYR 173 PHE 174 -0.0902

PHE 174 LEU 175 0.0002

LEU 175 GLN 176 -0.0003

GLN 176 ARG 177 -0.0004

ARG 177 GLN 178 -0.1418

GLN 178 PRO 179 0.0001

PRO 179 GLN 180 0.0216

GLN 180 ALA 181 0.0000

ALA 181 TRP 182 0.0306

TRP 182 LYS 183 0.0001

LYS 183 ASP 184 -0.0280

ASP 184 LYS 185 -0.0004

LYS 185 TYR 186 0.0069

TYR 186 ILE 187 0.0002

ILE 187 ARG 188 -0.0313

ARG 188 ALA 189 0.0002

ALA 189 PHE 190 0.0332

PHE 190 VAL 191 -0.0001

VAL 191 SER 192 0.0513

SER 192 LEU 193 0.0003

LEU 193 GLY 194 0.0877

GLY 194 ALA 195 0.0000

ALA 195 PRO 196 0.0184

PRO 196 TRP 197 -0.0003

TRP 197 TRP 197 0.0015

TRP 197 GLY 198 -0.0187

GLY 198 GLY 198 0.0025

GLY 198 GLY 199 0.0001

GLY 199 VAL 200 0.0063

VAL 200 ALA 201 0.0003

ALA 201 LYS 202 0.0273

LYS 202 THR 203 -0.0001

THR 203 LEU 204 0.0228

LEU 204 ARG 205 0.0001

ARG 205 VAL 206 -0.0316

VAL 206 LEU 207 0.0000

LEU 207 ALA 208 -0.0617

ALA 208 SER 209 -0.0003

SER 209 GLY 210 -0.0015

GLY 210 ASP 211 -0.0000

ASP 211 ASN 212 -0.0576

ASN 212 ASN 213 -0.0002

ASN 213 ARG 214 -0.0363

ARG 214 ILE 215 -0.0000

ILE 215 PRO 216 0.0567

PRO 216 VAL 217 -0.0003

VAL 217 ILE 218 -0.0511

ILE 218 GLY 219 -0.0002

GLY 219 PRO 220 -0.0208

PRO 220 LEU 221 0.0001

LEU 221 LYS 222 0.2465

LYS 222 ILE 223 -0.0001

ILE 223 ARG 224 0.0124

ARG 224 GLU 225 0.0000

GLU 225 GLN 226 0.0326

GLN 226 GLN 227 -0.0000

GLN 227 ARG 228 0.0159

ARG 228 SER 229 -0.0002

SER 229 ALA 230 0.0368

ALA 230 VAL 231 -0.0001

VAL 231 SER 232 0.0549

SER 232 THR 233 0.0005

THR 233 SER 234 -0.0023

SER 234 TRP 235 0.0001

TRP 235 LEU 236 0.0198

LEU 236 LEU 237 0.0002

LEU 237 PRO 238 0.0074

PRO 238 TYR 239 -0.0001

TYR 239 ASN 240 0.0654

ASN 240 TYR 241 -0.0002

TYR 241 THR 242 0.0103

THR 242 TRP 243 0.0001

TRP 243 TRP 243 -0.0102

TRP 243 SER 244 -0.0179

SER 244 PRO 245 0.0001

PRO 245 GLU 246 -0.0258

GLU 246 LYS 247 -0.0002

LYS 247 VAL 248 -0.0315

VAL 248 PHE 249 -0.0001

PHE 249 VAL 250 0.0029

VAL 250 GLN 251 -0.0002

GLN 251 THR 252 0.0122

THR 252 PRO 253 0.0003

PRO 253 THR 254 0.0147

THR 254 ILE 255 -0.0002

ILE 255 ASN 256 -0.0230

ASN 256 ASN 256 -0.0011

ASN 256 TYR 257 0.0000

TYR 257 THR 258 -0.0734

THR 258 LEU 259 0.0003

LEU 259 ARG 260 -0.0034

ARG 260 ASP 261 -0.0003

ASP 261 TYR 262 0.0331

TYR 262 ARG 263 0.0004

ARG 263 LYS 264 -0.0221

LYS 264 PHE 265 -0.0003

PHE 265 PHE 266 0.0330

PHE 266 GLN 267 -0.0002

GLN 267 ASP 268 -0.0299

ASP 268 ILE 269 0.0003

ILE 269 GLY 270 -0.0262

GLY 270 PHE 271 0.0000

PHE 271 GLU 272 -0.0461

GLU 272 ASP 273 0.0002

ASP 273 GLY 274 0.0004

GLY 274 TRP 275 -0.0005

TRP 275 LEU 276 0.0393

LEU 276 MET 277 0.0002

MET 277 ARG 278 0.0721

ARG 278 GLN 279 0.0001

GLN 279 ASP 280 -0.0648

ASP 280 THR 281 -0.0001

THR 281 GLU 282 0.0599

GLU 282 GLY 283 -0.0004

GLY 283 LEU 284 -0.0907

LEU 284 VAL 285 0.0000

VAL 285 GLU 286 0.0212

GLU 286 ALA 287 0.0001

ALA 287 THR 288 -0.0171

THR 288 MET 289 -0.0000

MET 289 PRO 290 -0.0274

PRO 290 PRO 291 0.0005

PRO 291 GLY 292 -0.0124

GLY 292 VAL 293 -0.0000

VAL 293 GLN 294 0.0126

GLN 294 LEU 295 -0.0002

LEU 295 HIS 296 0.0162

HIS 296 CYS 297 -0.0002

CYS 297 CYS 297 -0.0105

CYS 297 LEU 298 0.0098

LEU 298 TYR 299 0.0002

TYR 299 GLY 300 0.0732

GLY 300 THR 301 0.0004

THR 301 GLY 302 0.0330

GLY 302 VAL 303 0.0002

VAL 303 PRO 304 0.2031

PRO 304 THR 305 -0.0003

THR 305 PRO 306 0.1568

PRO 306 ASP 307 0.0001

ASP 307 SER 308 0.0939

SER 308 PHE 309 0.0001

PHE 309 TYR 310 0.0549

TYR 310 TYR 311 -0.0002

TYR 311 GLU 312 -0.0032

GLU 312 SER 313 0.0002

SER 313 PHE 314 -0.0302

PHE 314 PRO 315 0.0001

PRO 315 ASP 316 -0.0313

ASP 316 ARG 317 -0.0001

ARG 317 ASP 318 0.0600

ASP 318 PRO 319 -0.0000

PRO 319 LYS 320 0.0548

LYS 320 ILE 321 -0.0001

ILE 321 CYS 322 -0.0064

CYS 322 CYS 322 0.0289

CYS 322 PHE 323 -0.0001

PHE 323 GLY 324 0.1467

GLY 324 ASP 325 0.0001

ASP 325 GLY 326 -0.0267

GLY 326 ASP 327 0.0001

ASP 327 GLY 328 0.0980

GLY 328 THR 329 -0.0001

THR 329 VAL 330 0.0698

VAL 330 ASN 331 -0.0002

ASN 331 LEU 332 0.1014

LEU 332 LYS 333 0.0001

LYS 333 SER 334 -0.0107

SER 334 SER 334 0.0010

SER 334 ALA 335 0.0001

ALA 335 ALA 335 0.0004

ALA 335 LEU 336 -0.0014

LEU 336 LEU 336 0.0005

LEU 336 GLN 337 0.0000

GLN 337 GLN 337 0.0006

GLN 337 CYS 338 -0.0024

CYS 338 CYS 338 0.0011

CYS 338 GLN 339 0.0002

GLN 339 ALA 340 -0.0081

ALA 340 TRP 341 0.0001

TRP 341 GLN 342 -0.0269

GLN 342 SER 343 0.0000

SER 343 ARG 344 -0.0187

ARG 344 GLN 345 0.0003

GLN 345 GLU 346 -0.0624

GLU 346 HIS 347 -0.0001

HIS 347 HIS 347 0.0399

HIS 347 GLN 348 0.0598

GLN 348 VAL 349 -0.0002

VAL 349 LEU 350 0.0028

LEU 350 LEU 350 0.0012

LEU 350 LEU 351 0.0001

LEU 351 GLN 352 -0.0120

GLN 352 GLU 353 0.0004

GLU 353 LEU 354 -0.0434

LEU 354 PRO 355 -0.0001

PRO 355 GLY 356 -0.0153

GLY 356 SER 357 0.0000

SER 357 GLU 358 0.0264

GLU 358 HIS 359 -0.0002

HIS 359 ILE 360 -0.0988

ILE 360 GLU 361 0.0004

GLU 361 MET 362 0.0136

MET 362 LEU 363 -0.0001

LEU 363 ALA 364 -0.0102

ALA 364 ASN 365 0.0000

ASN 365 ALA 366 0.0622

ALA 366 THR 367 -0.0001

THR 367 THR 367 0.0508

THR 367 THR 368 -0.0279

THR 368 LEU 369 -0.0000

LEU 369 ALA 370 -0.0155

ALA 370 TYR 371 -0.0002

TYR 371 LEU 372 0.0235

LEU 372 LYS 373 0.0000

LYS 373 ARG 374 -0.0362

ARG 374 ARG 374 0.0039

ARG 374 VAL 375 0.0002

VAL 375 LEU 376 0.0417

LEU 376 LEU 377 0.0002

LEU 377 GLY 378 -0.0550

GLY 378 PRO 379 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 2405271642113669817

--- normal mode 8 ---

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

* *