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

* *

CA strain for 2407051440252305910

--- 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 -0.0015

LEU 3 ARG 4 -0.0000

ARG 4 ALA 5 -0.0306

ALA 5 ASN 6 0.0001

ASN 6 ASP 7 -0.0337

ASP 7 ALA 8 0.0004

ALA 8 PRO 9 -0.0212

PRO 9 ILE 10 -0.0000

ILE 10 VAL 11 -0.0153

VAL 11 LEU 12 -0.0005

LEU 12 LEU 13 -0.0425

LEU 13 HIS 14 -0.0000

HIS 14 GLY 15 0.0133

GLY 15 PHE 16 0.0004

PHE 16 THR 17 0.0118

THR 17 GLY 18 -0.0000

GLY 18 TRP 19 -0.0276

TRP 19 GLY 20 0.0001

GLY 20 ARG 21 -0.0267

ARG 21 GLU 22 0.0003

GLU 22 GLU 23 -0.1082

GLU 23 MET 24 0.0001

MET 24 PHE 25 0.0609

PHE 25 GLY 26 -0.0001

GLY 26 PHE 27 0.0185

PHE 27 LYS 28 0.0003

LYS 28 TYR 29 -0.0072

TYR 29 TRP 30 -0.0002

TRP 30 GLY 31 0.0196

GLY 31 GLY 32 -0.0003

GLY 32 VAL 33 0.0142

VAL 33 ARG 34 -0.0001

ARG 34 GLY 35 0.0964

GLY 35 ASP 36 -0.0002

ASP 36 ILE 37 -0.0253

ILE 37 GLU 38 -0.0003

GLU 38 GLN 39 0.0467

GLN 39 TRP 40 -0.0003

TRP 40 LEU 41 -0.0021

LEU 41 ASN 42 0.0001

ASN 42 ASP 43 0.0496

ASP 43 ASN 44 -0.0002

ASN 44 GLY 45 0.0385

GLY 45 TYR 46 -0.0000

TYR 46 ARG 47 0.0666

ARG 47 THR 48 0.0001

THR 48 TYR 49 0.0073

TYR 49 THR 50 0.0003

THR 50 LEU 51 0.0328

LEU 51 ALA 52 -0.0004

ALA 52 VAL 53 -0.0428

VAL 53 GLY 54 -0.0001

GLY 54 PRO 55 0.0186

PRO 55 LEU 56 -0.0000

LEU 56 SER 57 0.0012

SER 57 SER 58 0.0000

SER 58 ASN 59 0.0872

ASN 59 TRP 60 0.0003

TRP 60 ASP 61 0.0575

ASP 61 ARG 62 0.0002

ARG 62 ALA 63 0.0170

ALA 63 CYS 64 -0.0003

CYS 64 GLU 65 0.0294

GLU 65 ALA 66 -0.0000

ALA 66 TYR 67 0.0666

TYR 67 ALA 68 -0.0001

ALA 68 GLN 69 0.0943

GLN 69 LEU 70 0.0002

LEU 70 VAL 71 -0.0216

VAL 71 GLY 72 0.0004

GLY 72 GLY 73 0.0797

GLY 73 THR 74 0.0000

THR 74 VAL 75 -0.0216

VAL 75 ASP 76 0.0001

ASP 76 TYR 77 0.0133

TYR 77 GLY 78 0.0000

GLY 78 ALA 79 0.0195

ALA 79 ALA 80 -0.0001

ALA 80 HIS 81 -0.0779

HIS 81 ALA 82 0.0002

ALA 82 ALA 83 0.0047

ALA 83 LYS 84 0.0003

LYS 84 HIS 85 -0.0236

HIS 85 GLY 86 0.0004

GLY 86 HIS 87 0.0152

HIS 87 ALA 88 -0.0001

ALA 88 ARG 89 0.0153

ARG 89 PHE 90 0.0001

PHE 90 GLY 91 0.1894

GLY 91 ARG 92 -0.0001

ARG 92 THR 93 -0.0510

THR 93 TYR 94 0.0003

TYR 94 PRO 95 -0.0087

PRO 95 GLY 96 0.0001

GLY 96 LEU 97 0.0767

LEU 97 LEU 98 -0.0001

LEU 98 PRO 99 0.0368

PRO 99 GLU 100 0.0003

GLU 100 LEU 101 -0.0091

LEU 101 LYS 102 0.0002

LYS 102 ARG 103 -0.0253

ARG 103 GLY 104 0.0003

GLY 104 GLY 105 0.0115

GLY 105 ARG 106 -0.0004

ARG 106 ILE 107 -0.0068

ILE 107 HIS 108 0.0001

HIS 108 ILE 109 -0.0072

ILE 109 ILE 110 -0.0004

ILE 110 ALA 111 -0.0034

ALA 111 HIS 112 -0.0004

HIS 112 SER 113 -0.0015

SER 113 GLN 114 -0.0001

GLN 114 GLY 115 0.0025

GLY 115 GLY 116 0.0002

GLY 116 GLN 117 0.0002

GLN 117 THR 118 -0.0003

THR 118 ALA 119 0.0162

ALA 119 ARG 120 -0.0002

ARG 120 MET 121 -0.0672

MET 121 LEU 122 -0.0001

LEU 122 VAL 123 0.0222

VAL 123 SER 124 0.0002

SER 124 LEU 125 -0.0546

LEU 125 LEU 126 0.0005

LEU 126 GLU 127 -0.0115

GLU 127 ASN 128 0.0001

ASN 128 GLY 129 0.0027

GLY 129 SER 130 -0.0000

SER 130 GLN 131 0.0164

GLN 131 GLU 132 -0.0004

GLU 132 GLU 133 0.0147

GLU 133 ARG 134 -0.0003

ARG 134 GLU 135 0.0995

GLU 135 TYR 136 -0.0001

TYR 136 ALA 137 0.0052

ALA 137 LYS 138 0.0001

LYS 138 ALA 139 0.0235

ALA 139 HIS 140 -0.0002

HIS 140 ASN 141 -0.0250

ASN 141 VAL 142 -0.0003

VAL 142 SER 143 0.0518

SER 143 LEU 144 0.0002

LEU 144 SER 145 0.2023

SER 145 PRO 146 -0.0002

PRO 146 LEU 147 -0.0216

LEU 147 PHE 148 0.0004

PHE 148 GLU 149 0.0092

GLU 149 GLY 150 0.0002

GLY 150 GLY 151 -0.0460

GLY 151 HIS 152 0.0001

HIS 152 HIS 153 0.0694

HIS 153 PHE 154 0.0001

PHE 154 VAL 155 0.0005

VAL 155 LEU 156 0.0002

LEU 156 SER 157 0.0066

SER 157 VAL 158 -0.0000

VAL 158 THR 159 -0.0058

THR 159 THR 160 0.0000

THR 160 ILE 161 -0.0207

ILE 161 ALA 162 0.0001

ALA 162 THR 163 -0.0191

THR 163 PRO 164 0.0001

PRO 164 HIS 165 0.0236

HIS 165 ASP 166 -0.0002

ASP 166 GLY 167 0.0626

GLY 167 THR 168 0.0001

THR 168 THR 169 -0.0193

THR 169 LEU 170 -0.0003

LEU 170 SER 171 -0.0806

SER 171 ASN 172 0.0001

ASN 172 MET 173 0.0488

MET 173 VAL 174 0.0003

VAL 174 ASP 175 -0.0169

ASP 175 PHE 176 -0.0003

PHE 176 THR 177 0.0183

THR 177 ASP 178 -0.0001

ASP 178 ARG 179 -0.0166

ARG 179 PHE 180 -0.0002

PHE 180 PHE 181 0.0534

PHE 181 ASP 182 -0.0002

ASP 182 LEU 183 -0.0043

LEU 183 GLN 184 -0.0003

GLN 184 LYS 185 0.0115

LYS 185 ALA 186 0.0001

ALA 186 VAL 187 -0.0106

VAL 187 LEU 188 -0.0002

LEU 188 GLU 189 0.0106

GLU 189 ALA 190 0.0004

ALA 190 ALA 191 0.0259

ALA 191 ALA 192 0.0002

ALA 192 VAL 193 0.0133

VAL 193 ALA 194 -0.0002

ALA 194 SER 195 -0.0198

SER 195 ASN 196 -0.0001

ASN 196 VAL 197 0.0149

VAL 197 PRO 198 -0.0002

PRO 198 TYR 199 0.0185

TYR 199 THR 200 0.0001

THR 200 SER 201 0.0210

SER 201 GLN 202 0.0002

GLN 202 VAL 203 -0.0895

VAL 203 TYR 204 0.0002

TYR 204 ASP 205 0.1015

ASP 205 PHE 206 -0.0002

PHE 206 LYS 207 0.0495

LYS 207 LEU 208 -0.0000

LEU 208 ASP 209 0.0271

ASP 209 GLN 210 -0.0002

GLN 210 TRP 211 -0.0413

TRP 211 GLY 212 0.0001

GLY 212 LEU 213 0.0501

LEU 213 ARG 214 0.0004

ARG 214 ARG 215 0.1043

ARG 215 GLN 216 -0.0002

GLN 216 PRO 217 0.0155

PRO 217 GLY 218 -0.0000

GLY 218 GLU 219 0.0413

GLU 219 SER 220 0.0002

SER 220 PHE 221 0.0030

PHE 221 ASP 222 -0.0000

ASP 222 HIS 223 -0.0277

HIS 223 TYR 224 0.0001

TYR 224 PHE 225 0.0354

PHE 225 GLU 226 -0.0001

GLU 226 ARG 227 0.0006

ARG 227 LEU 228 -0.0002

LEU 228 LYS 229 0.0241

LYS 229 ARG 230 -0.0003

ARG 230 SER 231 -0.0320

SER 231 PRO 232 -0.0001

PRO 232 VAL 233 0.0061

VAL 233 TRP 234 -0.0002

TRP 234 THR 235 -0.0246

THR 235 SER 236 -0.0001

SER 236 THR 237 0.0864

THR 237 ASP 238 0.0000

ASP 238 THR 239 -0.0702

THR 239 ALA 240 0.0001

ALA 240 ARG 241 -0.0903

ARG 241 TYR 242 -0.0001

TYR 242 ASP 243 0.1109

ASP 243 LEU 244 -0.0003

LEU 244 SER 245 -0.0330

SER 245 VAL 246 0.0002

VAL 246 SER 247 -0.0314

SER 247 GLY 248 0.0000

GLY 248 ALA 249 -0.0222

ALA 249 GLU 250 0.0003

GLU 250 LYS 251 -0.0785

LYS 251 LEU 252 0.0000

LEU 252 ASN 253 0.0588

ASN 253 GLN 254 0.0002

GLN 254 TRP 255 -0.1268

TRP 255 VAL 256 -0.0001

VAL 256 GLN 257 -0.0064

GLN 257 ALA 258 -0.0001

ALA 258 SER 259 -0.0115

SER 259 PRO 260 -0.0003

PRO 260 ASN 261 -0.0134

ASN 261 THR 262 0.0001

THR 262 TYR 263 -0.0095

TYR 263 TYR 264 0.0003

TYR 264 LEU 265 -0.0392

LEU 265 SER 266 0.0001

SER 266 PHE 267 -0.0389

PHE 267 SER 268 -0.0001

SER 268 THR 269 -0.0154

THR 269 GLU 270 -0.0004

GLU 270 ARG 271 -0.0248

ARG 271 THR 272 -0.0000

THR 272 TYR 273 0.0939

TYR 273 ARG 274 -0.0002

ARG 274 GLY 275 0.0690

GLY 275 ALA 276 0.0001

ALA 276 LEU 277 0.1017

LEU 277 THR 278 0.0002

THR 278 GLY 279 -0.0778

GLY 279 ASN 280 -0.0001

ASN 280 HIS 281 0.0321

HIS 281 TYR 282 0.0001

TYR 282 PRO 283 0.0892

PRO 283 GLU 284 0.0001

GLU 284 LEU 285 -0.0127

LEU 285 GLY 286 -0.0001

GLY 286 MET 287 0.0037

MET 287 ASN 288 -0.0002

ASN 288 ALA 289 -0.0240

ALA 289 PHE 290 -0.0000

PHE 290 SER 291 0.0245

SER 291 ALA 292 -0.0002

ALA 292 VAL 293 -0.0278

VAL 293 VAL 294 0.0001

VAL 294 CYS 295 0.0032

CYS 295 ALA 296 -0.0000

ALA 296 PRO 297 0.0087

PRO 297 PHE 298 0.0001

PHE 298 LEU 299 0.0196

LEU 299 GLY 300 -0.0003

GLY 300 SER 301 0.0095

SER 301 TYR 302 -0.0001

TYR 302 ARG 303 0.0297

ARG 303 ASN 304 -0.0002

ASN 304 PRO 305 0.0102

PRO 305 THR 306 0.0003

THR 306 LEU 307 -0.0555

LEU 307 GLY 308 0.0001

GLY 308 ILE 309 0.0255

ILE 309 ASP 310 0.0003

ASP 310 ASP 311 -0.0045

ASP 311 ARG 312 0.0001

ARG 312 TRP 313 -0.0083

TRP 313 LEU 314 0.0002

LEU 314 GLU 315 0.0540

GLU 315 ASN 316 0.0001

ASN 316 ASP 317 0.0342

ASP 317 GLY 318 -0.0002

GLY 318 ILE 319 -0.0221

ILE 319 VAL 320 -0.0003

VAL 320 ASN 321 0.0053

ASN 321 THR 322 0.0003

THR 322 VAL 323 -0.0174

VAL 323 SER 324 0.0003

SER 324 MET 325 0.0181

MET 325 ASN 326 0.0003

ASN 326 GLY 327 -0.0688

GLY 327 PRO 328 -0.0001

PRO 328 LYS 329 0.0018

LYS 329 ARG 330 0.0002

ARG 330 GLY 331 -0.0858

GLY 331 SER 332 -0.0001

SER 332 SER 333 -0.0193

SER 333 ASP 334 0.0002

ASP 334 ARG 335 -0.0243

ARG 335 ILE 336 -0.0002

ILE 336 VAL 337 0.0493

VAL 337 PRO 338 -0.0003

PRO 338 TYR 339 -0.0010

TYR 339 ASP 340 -0.0002

ASP 340 GLY 341 0.0149

GLY 341 THR 342 0.0003

THR 342 LEU 343 0.0012

LEU 343 LYS 344 -0.0003

LYS 344 LYS 345 -0.0215

LYS 345 GLY 346 -0.0002

GLY 346 VAL 347 -0.0088

VAL 347 TRP 348 -0.0003

TRP 348 ASN 349 -0.0216

ASN 349 ASP 350 0.0002

ASP 350 MET 351 -0.0425

MET 351 GLY 352 -0.0003

GLY 352 THR 353 -0.0078

THR 353 TYR 354 0.0001

TYR 354 ASN 355 -0.0166

ASN 355 VAL 356 0.0000

VAL 356 ASP 357 -0.0188

ASP 357 HIS 358 0.0000

HIS 358 LEU 359 -0.0032

LEU 359 GLU 360 0.0001

GLU 360 ILE 361 0.0030

ILE 361 ILE 362 -0.0001

ILE 362 GLY 363 -0.0273

GLY 363 VAL 364 -0.0001

VAL 364 ASP 365 0.0470

ASP 365 PRO 366 -0.0002

PRO 366 ASN 367 0.0096

ASN 367 PRO 368 0.0000

PRO 368 SER 369 -0.0269

SER 369 PHE 370 0.0001

PHE 370 ASP 371 0.0798

ASP 371 ILE 372 0.0003

ILE 372 ARG 373 0.0464

ARG 373 ALA 374 0.0002

ALA 374 PHE 375 0.0020

PHE 375 TYR 376 0.0002

TYR 376 LEU 377 0.0170

LEU 377 ARG 378 -0.0001

ARG 378 LEU 379 -0.0030

LEU 379 ALA 380 0.0003

ALA 380 GLU 381 -0.0002

GLU 381 GLN 382 -0.0005

GLN 382 LEU 383 0.0201

LEU 383 ALA 384 -0.0001

ALA 384 SER 385 -0.0123

SER 385 LEU 386 0.0002

LEU 386 ARG 387 0.0195

ARG 387 PRO 388 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.

*** ***

CA strain for 2407051440252305910

--- normal mode 7 ---

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

* *