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

* *

CA strain for 2407051425092282339

--- normal mode 7 ---

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 -0.1239

LEU 3 ARG 4 0.0000

ARG 4 ALA 5 -0.0968

ALA 5 ASN 6 0.0002

ASN 6 ASP 7 0.0126

ASP 7 ALA 8 0.0001

ALA 8 PRO 9 -0.1148

PRO 9 ILE 10 0.0001

ILE 10 VAL 11 -0.0535

VAL 11 LEU 12 -0.0001

LEU 12 LEU 13 -0.0441

LEU 13 HIS 14 0.0002

HIS 14 GLY 15 -0.0057

GLY 15 PHE 16 0.0000

PHE 16 THR 17 0.0036

THR 17 GLY 18 0.0000

GLY 18 TRP 19 -0.0061

TRP 19 GLY 20 -0.0001

GLY 20 ARG 21 0.0324

ARG 21 GLU 22 0.0004

GLU 22 GLU 23 -0.0250

GLU 23 MET 24 0.0001

MET 24 PHE 25 0.0165

PHE 25 GLY 26 -0.0001

GLY 26 PHE 27 0.0094

PHE 27 LYS 28 -0.0002

LYS 28 TYR 29 0.0073

TYR 29 TRP 30 -0.0001

TRP 30 GLY 31 0.0106

GLY 31 GLY 32 -0.0002

GLY 32 VAL 33 0.0093

VAL 33 ARG 34 -0.0004

ARG 34 GLY 35 0.0277

GLY 35 ASP 36 -0.0002

ASP 36 ILE 37 -0.0173

ILE 37 GLU 38 0.0001

GLU 38 GLN 39 0.0379

GLN 39 TRP 40 0.0002

TRP 40 LEU 41 -0.0093

LEU 41 ASN 42 0.0001

ASN 42 ASP 43 0.0293

ASP 43 ASN 44 -0.0001

ASN 44 GLY 45 0.0307

GLY 45 TYR 46 0.0000

TYR 46 ARG 47 -0.0315

ARG 47 THR 48 0.0004

THR 48 TYR 49 -0.0505

TYR 49 THR 50 0.0001

THR 50 LEU 51 -0.0267

LEU 51 ALA 52 0.0002

ALA 52 VAL 53 -0.0282

VAL 53 GLY 54 0.0002

GLY 54 PRO 55 -0.0032

PRO 55 LEU 56 0.0002

LEU 56 SER 57 0.0054

SER 57 SER 58 -0.0001

SER 58 ASN 59 0.0257

ASN 59 TRP 60 0.0002

TRP 60 ASP 61 0.0206

ASP 61 ARG 62 -0.0002

ARG 62 ALA 63 0.0014

ALA 63 CYS 64 -0.0000

CYS 64 GLU 65 0.0159

GLU 65 ALA 66 -0.0001

ALA 66 TYR 67 0.0121

TYR 67 ALA 68 -0.0001

ALA 68 GLN 69 0.0180

GLN 69 LEU 70 0.0003

LEU 70 VAL 71 0.0114

VAL 71 GLY 72 0.0001

GLY 72 GLY 73 -0.0356

GLY 73 THR 74 0.0003

THR 74 VAL 75 -0.0008

VAL 75 ASP 76 0.0002

ASP 76 TYR 77 -0.0054

TYR 77 GLY 78 -0.0001

GLY 78 ALA 79 0.0073

ALA 79 ALA 80 -0.0001

ALA 80 HIS 81 -0.0211

HIS 81 ALA 82 -0.0002

ALA 82 ALA 83 0.0109

ALA 83 LYS 84 0.0004

LYS 84 HIS 85 -0.0276

HIS 85 GLY 86 0.0001

GLY 86 HIS 87 0.0039

HIS 87 ALA 88 -0.0001

ALA 88 ARG 89 -0.0125

ARG 89 PHE 90 -0.0001

PHE 90 GLY 91 0.0983

GLY 91 ARG 92 0.0001

ARG 92 THR 93 -0.0628

THR 93 TYR 94 0.0002

TYR 94 PRO 95 -0.0331

PRO 95 GLY 96 -0.0001

GLY 96 LEU 97 -0.0179

LEU 97 LEU 98 0.0003

LEU 98 PRO 99 0.0274

PRO 99 GLU 100 -0.0002

GLU 100 LEU 101 0.0019

LEU 101 LYS 102 0.0004

LYS 102 ARG 103 -0.0172

ARG 103 GLY 104 -0.0004

GLY 104 GLY 105 -0.0381

GLY 105 ARG 106 0.0003

ARG 106 ILE 107 0.0114

ILE 107 HIS 108 -0.0002

HIS 108 ILE 109 -0.0180

ILE 109 ILE 110 0.0001

ILE 110 ALA 111 0.0026

ALA 111 HIS 112 -0.0001

HIS 112 SER 113 -0.0022

SER 113 GLN 114 0.0004

GLN 114 GLY 115 -0.0038

GLY 115 GLY 116 -0.0004

GLY 116 GLN 117 0.0043

GLN 117 THR 118 0.0001

THR 118 ALA 119 0.0037

ALA 119 ARG 120 -0.0003

ARG 120 MET 121 0.0090

MET 121 LEU 122 -0.0003

LEU 122 VAL 123 0.0114

VAL 123 SER 124 -0.0000

SER 124 LEU 125 -0.0004

LEU 125 LEU 126 -0.0000

LEU 126 GLU 127 0.0024

GLU 127 ASN 128 0.0000

ASN 128 GLY 129 0.0116

GLY 129 SER 130 -0.0002

SER 130 GLN 131 0.0171

GLN 131 GLU 132 -0.0003

GLU 132 GLU 133 -0.0030

GLU 133 ARG 134 -0.0002

ARG 134 GLU 135 0.0332

GLU 135 TYR 136 0.0001

TYR 136 ALA 137 0.0068

ALA 137 LYS 138 0.0004

LYS 138 ALA 139 0.0056

ALA 139 HIS 140 0.0000

HIS 140 ASN 141 -0.0025

ASN 141 VAL 142 0.0000

VAL 142 SER 143 -0.0004

SER 143 LEU 144 -0.0000

LEU 144 SER 145 0.0507

SER 145 PRO 146 -0.0002

PRO 146 LEU 147 0.0024

LEU 147 PHE 148 -0.0002

PHE 148 GLU 149 0.0019

GLU 149 GLY 150 0.0002

GLY 150 GLY 151 0.0026

GLY 151 HIS 152 -0.0000

HIS 152 HIS 153 -0.0052

HIS 153 PHE 154 -0.0001

PHE 154 VAL 155 0.0076

VAL 155 LEU 156 -0.0002

LEU 156 SER 157 0.0071

SER 157 VAL 158 -0.0002

VAL 158 THR 159 0.0021

THR 159 THR 160 -0.0005

THR 160 ILE 161 0.0025

ILE 161 ALA 162 0.0001

ALA 162 THR 163 -0.0101

THR 163 PRO 164 0.0003

PRO 164 HIS 165 -0.0016

HIS 165 ASP 166 0.0005

ASP 166 GLY 167 0.0237

GLY 167 THR 168 -0.0005

THR 168 THR 169 0.0002

THR 169 LEU 170 -0.0003

LEU 170 VAL 171 -0.0173

VAL 171 ASN 172 -0.0002

ASN 172 MET 173 0.0115

MET 173 VAL 174 -0.0001

VAL 174 ASP 175 0.0019

ASP 175 PHE 176 -0.0002

PHE 176 THR 177 -0.0037

THR 177 ASP 178 -0.0001

ASP 178 ARG 179 0.0008

ARG 179 PHE 180 -0.0001

PHE 180 PHE 181 0.0174

PHE 181 ASP 182 0.0003

ASP 182 LEU 183 0.0091

LEU 183 GLN 184 -0.0002

GLN 184 LYS 185 0.0017

LYS 185 ALA 186 0.0002

ALA 186 VAL 187 0.0002

VAL 187 LEU 188 -0.0004

LEU 188 GLU 189 0.0063

GLU 189 ALA 190 0.0002

ALA 190 ALA 191 -0.0054

ALA 191 ALA 192 0.0004

ALA 192 VAL 193 0.0081

VAL 193 ALA 194 -0.0001

ALA 194 SER 195 0.0008

SER 195 ASN 196 0.0002

ASN 196 VAL 197 0.0061

VAL 197 PRO 198 -0.0001

PRO 198 TYR 199 0.0080

TYR 199 THR 200 -0.0002

THR 200 SER 201 0.0118

SER 201 GLN 202 0.0002

GLN 202 VAL 203 -0.0587

VAL 203 TYR 204 -0.0002

TYR 204 ASP 205 0.0602

ASP 205 PHE 206 -0.0004

PHE 206 LYS 207 0.0063

LYS 207 LEU 208 0.0001

LEU 208 ASP 209 -0.0068

ASP 209 GLN 210 -0.0001

GLN 210 TRP 211 -0.0364

TRP 211 GLY 212 -0.0001

GLY 212 LEU 213 0.0087

LEU 213 ARG 214 0.0001

ARG 214 ARG 215 -0.0033

ARG 215 GLN 216 -0.0004

GLN 216 PRO 217 0.0141

PRO 217 GLY 218 0.0002

GLY 218 GLU 219 0.0256

GLU 219 SER 220 0.0005

SER 220 PHE 221 -0.0170

PHE 221 ASP 222 -0.0001

ASP 222 HIS 223 -0.0235

HIS 223 TYR 224 -0.0004

TYR 224 PHE 225 0.0239

PHE 225 GLU 226 0.0003

GLU 226 ARG 227 -0.0097

ARG 227 LEU 228 -0.0003

LEU 228 LYS 229 0.0111

LYS 229 ARG 230 -0.0003

ARG 230 SER 231 -0.0184

SER 231 PRO 232 0.0001

PRO 232 VAL 233 0.0028

VAL 233 TRP 234 0.0004

TRP 234 THR 235 -0.0056

THR 235 SER 236 0.0001

SER 236 THR 237 0.0350

THR 237 ASP 238 0.0001

ASP 238 THR 239 -0.0132

THR 239 ALA 240 0.0001

ALA 240 ARG 241 -0.0190

ARG 241 TYR 242 -0.0002

TYR 242 ASP 243 0.0120

ASP 243 LEU 244 0.0003

LEU 244 SER 245 -0.0230

SER 245 VAL 246 -0.0000

VAL 246 SER 247 -0.0113

SER 247 GLY 248 -0.0001

GLY 248 ALA 249 0.0293

ALA 249 GLU 250 0.0002

GLU 250 LYS 251 -0.0205

LYS 251 LEU 252 -0.0005

LEU 252 ASN 253 0.0213

ASN 253 GLN 254 -0.0002

GLN 254 TRP 255 -0.0401

TRP 255 VAL 256 -0.0002

VAL 256 GLN 257 0.0229

GLN 257 ALA 258 0.0002

ALA 258 SER 259 -0.0034

SER 259 PRO 260 -0.0003

PRO 260 ASN 261 -0.0008

ASN 261 THR 262 0.0005

THR 262 TYR 263 0.0044

TYR 263 TYR 264 -0.0004

TYR 264 LEU 265 -0.0157

LEU 265 SER 266 0.0001

SER 266 PHE 267 -0.0154

PHE 267 SER 268 -0.0001

SER 268 THR 269 0.0170

THR 269 GLU 270 -0.0002

GLU 270 ARG 271 0.0082

ARG 271 THR 272 -0.0000

THR 272 TYR 273 0.0444

TYR 273 ARG 274 0.0003

ARG 274 GLY 275 0.0427

GLY 275 ALA 276 0.0001

ALA 276 LEU 277 0.0372

LEU 277 THR 278 -0.0003

THR 278 GLY 279 0.0035

GLY 279 ASN 280 -0.0002

ASN 280 HIS 281 0.0210

HIS 281 TYR 282 0.0000

TYR 282 PRO 283 0.0010

PRO 283 GLU 284 0.0001

GLU 284 LEU 285 -0.0025

LEU 285 GLY 286 0.0000

GLY 286 MET 287 0.0087

MET 287 ASN 288 -0.0001

ASN 288 ALA 289 0.0017

ALA 289 PHE 290 0.0000

PHE 290 SER 291 0.0005

SER 291 ALA 292 0.0000

ALA 292 VAL 293 0.0016

VAL 293 VAL 294 -0.0001

VAL 294 CYS 295 0.0102

CYS 295 ALA 296 -0.0004

ALA 296 PRO 297 0.0045

PRO 297 PHE 298 0.0002

PHE 298 LEU 299 0.0114

LEU 299 GLY 300 0.0001

GLY 300 SER 301 0.0077

SER 301 TYR 302 -0.0001

TYR 302 ARG 303 0.0017

ARG 303 ASN 304 -0.0002

ASN 304 PRO 305 -0.0068

PRO 305 THR 306 0.0004

THR 306 LEU 307 -0.0113

LEU 307 GLY 308 0.0004

GLY 308 ILE 309 0.0009

ILE 309 ASP 310 -0.0001

ASP 310 ASP 311 -0.0156

ASP 311 ARG 312 -0.0003

ARG 312 TRP 313 -0.0147

TRP 313 LEU 314 0.0002

LEU 314 GLU 315 0.0209

GLU 315 ASN 316 -0.0001

ASN 316 ASP 317 0.0095

ASP 317 GLY 318 0.0002

GLY 318 ILE 319 -0.0096

ILE 319 VAL 320 0.0003

VAL 320 ASN 321 0.0049

ASN 321 THR 322 0.0003

THR 322 VAL 323 -0.0228

VAL 323 SER 324 -0.0005

SER 324 MET 325 0.0340

MET 325 ASN 326 0.0001

ASN 326 GLY 327 -0.0364

GLY 327 PRO 328 -0.0001

PRO 328 LYS 329 -0.0142

LYS 329 ARG 330 0.0000

ARG 330 GLY 331 -0.0110

GLY 331 SER 332 -0.0004

SER 332 SER 333 -0.0048

SER 333 ASP 334 -0.0001

ASP 334 ARG 335 -0.0034

ARG 335 ILE 336 0.0003

ILE 336 VAL 337 0.0596

VAL 337 PRO 338 -0.0001

PRO 338 TYR 339 0.0161

TYR 339 ASP 340 0.0000

ASP 340 GLY 341 0.0070

GLY 341 THR 342 -0.0000

THR 342 LEU 343 -0.0117

LEU 343 LYS 344 0.0003

LYS 344 LYS 345 -0.0286

LYS 345 GLY 346 0.0000

GLY 346 VAL 347 0.0048

VAL 347 TRP 348 -0.0001

TRP 348 ASN 349 0.0044

ASN 349 ASP 350 -0.0004

ASP 350 MET 351 -0.0216

MET 351 GLY 352 0.0000

GLY 352 THR 353 0.0354

THR 353 TYR 354 -0.0001

TYR 354 ASN 355 0.0299

ASN 355 VAL 356 0.0001

VAL 356 ASP 357 -0.0148

ASP 357 HIS 358 -0.0000

HIS 358 LEU 359 -0.0065

LEU 359 GLU 360 0.0001

GLU 360 ILE 361 -0.0072

ILE 361 ILE 362 0.0002

ILE 362 GLY 363 -0.0123

GLY 363 VAL 364 -0.0002

VAL 364 ASP 365 0.0128

ASP 365 PRO 366 -0.0004

PRO 366 ASN 367 0.0075

ASN 367 PRO 368 -0.0005

PRO 368 SER 369 0.0001

SER 369 PHE 370 -0.0002

PHE 370 ASP 371 0.0164

ASP 371 ILE 372 0.0000

ILE 372 ARG 373 0.0368

ARG 373 ALA 374 0.0001

ALA 374 PHE 375 -0.0277

PHE 375 TYR 376 -0.0001

TYR 376 LEU 377 0.0208

LEU 377 ARG 378 0.0001

ARG 378 LEU 379 -0.0275

LEU 379 ALA 380 -0.0002

ALA 380 GLU 381 0.0346

GLU 381 GLN 382 0.0003

GLN 382 LEU 383 0.0026

LEU 383 ALA 384 -0.0003

ALA 384 SER 385 -0.0100

SER 385 LEU 386 -0.0003

LEU 386 ARG 387 -0.0462

ARG 387 PRO 388 0.0003

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 7 ---

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

* *