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

* *

CA strain for 2405271642113669817

--- normal mode 11 ---

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 -0.0002

PRO 5 PRO 6 -0.0324

PRO 6 VAL 7 -0.0003

VAL 7 VAL 8 -0.1485

VAL 8 LEU 9 0.0001

LEU 9 VAL 10 -0.1096

VAL 10 PRO 11 -0.0000

PRO 11 GLY 12 -0.0603

GLY 12 ASP 13 -0.0002

ASP 13 LEU 14 0.1404

LEU 14 GLY 15 -0.0002

GLY 15 ASN 16 0.0578

ASN 16 GLN 17 -0.0001

GLN 17 LEU 18 -0.0101

LEU 18 GLU 19 -0.0004

GLU 19 ALA 20 -0.0095

ALA 20 LYS 21 -0.0002

LYS 21 LEU 22 0.0854

LEU 22 ASP 23 -0.0003

ASP 23 LYS 24 0.0382

LYS 24 PRO 25 0.0000

PRO 25 THR 26 0.0419

THR 26 VAL 27 0.0000

VAL 27 VAL 28 0.1339

VAL 28 HIS 29 0.0003

HIS 29 TYR 30 -0.0977

TYR 30 LEU 31 0.0000

LEU 31 CYS 32 0.0444

CYS 32 SER 33 0.0001

SER 33 LYS 34 -0.0383

LYS 34 LYS 35 0.0003

LYS 35 THR 36 0.0914

THR 36 GLU 37 -0.0002

GLU 37 SER 38 0.1084

SER 38 TYR 39 0.0000

TYR 39 PHE 40 -0.0278

PHE 40 THR 41 -0.0002

THR 41 ILE 42 -0.0674

ILE 42 TRP 43 -0.0000

TRP 43 LEU 44 0.0316

LEU 44 ASN 45 0.0002

ASN 45 LEU 46 -0.0385

LEU 46 GLU 47 -0.0000

GLU 47 LEU 48 -0.0005

LEU 48 LEU 49 -0.0005

LEU 49 LEU 50 -0.0906

LEU 50 PRO 51 0.0001

PRO 51 VAL 52 0.1416

VAL 52 ILE 53 0.0001

ILE 53 ILE 54 0.0230

ILE 54 ASP 55 0.0002

ASP 55 CYS 56 -0.0159

CYS 56 TRP 57 0.0000

TRP 57 ILE 58 -0.1503

ILE 58 ASP 59 -0.0005

ASP 59 ASN 60 -0.0804

ASN 60 ILE 61 0.0004

ILE 61 ARG 62 0.0182

ARG 62 LEU 63 -0.0001

LEU 63 VAL 64 0.0726

VAL 64 TYR 65 -0.0001

TYR 65 ASN 66 0.1331

ASN 66 LYS 67 0.0001

LYS 67 THR 68 0.1639

THR 68 SER 69 -0.0003

SER 69 ARG 70 -0.0205

ARG 70 ALA 71 0.0004

ALA 71 THR 72 0.0481

THR 72 GLN 73 -0.0001

GLN 73 PHE 74 -0.1303

PHE 74 PRO 75 -0.0004

PRO 75 ASP 76 -0.0598

ASP 76 GLY 77 -0.0001

GLY 77 VAL 78 0.0112

VAL 78 ASP 79 0.0002

ASP 79 VAL 80 -0.0067

VAL 80 ARG 81 0.0001

ARG 81 VAL 82 -0.1438

VAL 82 PRO 83 -0.0001

PRO 83 GLY 84 -0.3387

GLY 84 PHE 85 0.0001

PHE 85 GLY 86 -0.3227

GLY 86 LYS 87 -0.0001

LYS 87 THR 88 0.1258

THR 88 PHE 89 -0.0000

PHE 89 SER 90 -0.1134

SER 90 LEU 91 -0.0001

LEU 91 GLU 92 -0.0487

GLU 92 PHE 93 0.0000

PHE 93 LEU 94 -0.1549

LEU 94 ASP 95 -0.0004

ASP 95 PRO 96 0.0335

PRO 96 SER 97 -0.0003

SER 97 LYS 98 0.0041

LYS 98 SER 99 -0.0000

SER 99 SER 100 0.0070

SER 100 VAL 101 0.0001

VAL 101 GLY 102 -0.0079

GLY 102 SER 103 -0.0002

SER 103 TYR 104 0.0964

TYR 104 PHE 105 -0.0001

PHE 105 HIS 106 -0.0143

HIS 106 THR 107 -0.0001

THR 107 MET 108 -0.0541

MET 108 VAL 109 -0.0003

VAL 109 GLU 110 0.0184

GLU 110 SER 111 -0.0002

SER 111 LEU 112 0.0555

LEU 112 VAL 113 -0.0003

VAL 113 GLY 114 -0.0228

GLY 114 TRP 115 0.0000

TRP 115 GLY 116 0.0608

GLY 116 TYR 117 0.0004

TYR 117 THR 118 -0.0271

THR 118 ARG 119 0.0001

ARG 119 GLY 120 0.0318

GLY 120 GLU 121 0.0000

GLU 121 GLU 121 -0.0162

GLU 121 ASP 122 0.0023

ASP 122 VAL 123 -0.0002

VAL 123 ARG 124 -0.1240

ARG 124 GLY 125 0.0001

GLY 125 ALA 126 -0.1858

ALA 126 PRO 127 -0.0004

PRO 127 TYR 128 -0.3840

TYR 128 ASP 129 -0.0002

ASP 129 TRP 130 -0.0258

TRP 130 ARG 131 0.0002

ARG 131 ARG 132 0.0800

ARG 132 ALA 133 0.0001

ALA 133 PRO 134 -0.0105

PRO 134 ASN 135 -0.0001

ASN 135 GLU 136 0.0319

GLU 136 ASN 137 -0.0004

ASN 137 GLY 138 -0.0540

GLY 138 PRO 139 0.0000

PRO 139 TYR 140 0.1463

TYR 140 PHE 141 0.0002

PHE 141 LEU 142 -0.0913

LEU 142 ALA 143 0.0001

ALA 143 LEU 144 0.0997

LEU 144 ARG 145 0.0001

ARG 145 GLU 146 0.0154

GLU 146 GLU 146 -0.0911

GLU 146 MET 147 -0.0002

MET 147 ILE 148 -0.0210

ILE 148 GLU 149 -0.0001

GLU 149 GLU 149 0.0086

GLU 149 GLU 150 0.0515

GLU 150 GLU 150 -0.0143

GLU 150 MET 151 0.0002

MET 151 TYR 152 -0.0193

TYR 152 GLN 153 -0.0003

GLN 153 LEU 154 0.0422

LEU 154 TYR 155 0.0000

TYR 155 GLY 156 -0.0389

GLY 156 GLY 157 -0.0003

GLY 157 PRO 158 0.0273

PRO 158 VAL 159 0.0001

VAL 159 VAL 160 0.0942

VAL 160 LEU 161 0.0001

LEU 161 VAL 162 0.0586

VAL 162 ALA 163 0.0000

ALA 163 HIS 164 0.0356

HIS 164 SER 165 0.0005

SER 165 MET 166 -0.0088

MET 166 GLY 167 -0.0003

GLY 167 ASN 168 0.0000

ASN 168 MET 169 -0.0002

MET 169 TYR 170 0.0029

TYR 170 THR 171 0.0001

THR 171 LEU 172 0.0298

LEU 172 TYR 173 -0.0001

TYR 173 PHE 174 -0.1640

PHE 174 LEU 175 0.0001

LEU 175 GLN 176 0.0161

GLN 176 ARG 177 -0.0002

ARG 177 GLN 178 -0.1630

GLN 178 PRO 179 -0.0003

PRO 179 GLN 180 0.0200

GLN 180 ALA 181 -0.0000

ALA 181 TRP 182 0.0188

TRP 182 LYS 183 -0.0004

LYS 183 ASP 184 -0.0158

ASP 184 LYS 185 0.0004

LYS 185 TYR 186 0.0005

TYR 186 ILE 187 0.0001

ILE 187 ARG 188 -0.0776

ARG 188 ALA 189 -0.0000

ALA 189 PHE 190 0.0513

PHE 190 VAL 191 -0.0001

VAL 191 SER 192 0.0773

SER 192 LEU 193 0.0004

LEU 193 GLY 194 0.0967

GLY 194 ALA 195 -0.0002

ALA 195 PRO 196 0.0104

PRO 196 TRP 197 -0.0000

TRP 197 TRP 197 -0.0033

TRP 197 GLY 198 0.0499

GLY 198 GLY 198 -0.0003

GLY 198 GLY 199 0.0002

GLY 199 VAL 200 -0.0207

VAL 200 ALA 201 -0.0004

ALA 201 LYS 202 0.0013

LYS 202 THR 203 -0.0000

THR 203 LEU 204 -0.0740

LEU 204 ARG 205 -0.0003

ARG 205 VAL 206 0.0017

VAL 206 LEU 207 0.0000

LEU 207 ALA 208 -0.1014

ALA 208 SER 209 0.0003

SER 209 GLY 210 -0.0078

GLY 210 ASP 211 -0.0000

ASP 211 ASN 212 0.0771

ASN 212 ASN 213 -0.0000

ASN 213 ARG 214 0.0429

ARG 214 ILE 215 0.0002

ILE 215 PRO 216 -0.1332

PRO 216 VAL 217 -0.0001

VAL 217 ILE 218 0.0392

ILE 218 GLY 219 -0.0003

GLY 219 PRO 220 0.0011

PRO 220 LEU 221 -0.0002

LEU 221 LYS 222 -0.3349

LYS 222 ILE 223 0.0001

ILE 223 ARG 224 -0.0000

ARG 224 GLU 225 0.0002

GLU 225 GLN 226 -0.2181

GLN 226 GLN 227 -0.0002

GLN 227 ARG 228 0.0166

ARG 228 SER 229 -0.0000

SER 229 ALA 230 -0.1637

ALA 230 VAL 231 0.0004

VAL 231 SER 232 -0.0022

SER 232 THR 233 -0.0000

THR 233 SER 234 -0.0007

SER 234 TRP 235 0.0002

TRP 235 LEU 236 0.0218

LEU 236 LEU 237 -0.0004

LEU 237 PRO 238 0.0629

PRO 238 TYR 239 0.0003

TYR 239 ASN 240 -0.0043

ASN 240 TYR 241 0.0002

TYR 241 THR 242 -0.0539

THR 242 TRP 243 0.0003

TRP 243 TRP 243 0.0044

TRP 243 SER 244 0.1126

SER 244 PRO 245 0.0002

PRO 245 GLU 246 -0.0152

GLU 246 LYS 247 0.0001

LYS 247 VAL 248 0.0863

VAL 248 PHE 249 0.0003

PHE 249 VAL 250 0.0988

VAL 250 GLN 251 0.0003

GLN 251 THR 252 0.0471

THR 252 PRO 253 0.0000

PRO 253 THR 254 -0.0458

THR 254 ILE 255 -0.0001

ILE 255 ASN 256 0.1012

ASN 256 ASN 256 0.0027

ASN 256 TYR 257 0.0000

TYR 257 THR 258 0.1179

THR 258 LEU 259 -0.0000

LEU 259 ARG 260 0.0230

ARG 260 ASP 261 0.0000

ASP 261 TYR 262 -0.1329

TYR 262 ARG 263 -0.0000

ARG 263 LYS 264 -0.1365

LYS 264 PHE 265 -0.0003

PHE 265 PHE 266 -0.0888

PHE 266 GLN 267 -0.0001

GLN 267 ASP 268 -0.0284

ASP 268 ILE 269 -0.0000

ILE 269 GLY 270 0.0898

GLY 270 PHE 271 -0.0001

PHE 271 GLU 272 0.1043

GLU 272 ASP 273 0.0002

ASP 273 GLY 274 0.0597

GLY 274 TRP 275 0.0004

TRP 275 LEU 276 -0.0937

LEU 276 MET 277 0.0000

MET 277 ARG 278 0.0355

ARG 278 GLN 279 -0.0000

GLN 279 ASP 280 -0.1537

ASP 280 THR 281 -0.0001

THR 281 GLU 282 -0.0033

GLU 282 GLY 283 0.0003

GLY 283 LEU 284 -0.0257

LEU 284 VAL 285 -0.0001

VAL 285 GLU 286 0.0957

GLU 286 ALA 287 -0.0002

ALA 287 THR 288 0.0744

THR 288 MET 289 0.0001

MET 289 PRO 290 0.0274

PRO 290 PRO 291 -0.0001

PRO 291 GLY 292 0.0121

GLY 292 VAL 293 -0.0001

VAL 293 GLN 294 -0.0342

GLN 294 LEU 295 -0.0001

LEU 295 HIS 296 -0.0429

HIS 296 CYS 297 -0.0004

CYS 297 CYS 297 -0.0052

CYS 297 LEU 298 -0.0214

LEU 298 TYR 299 0.0001

TYR 299 GLY 300 -0.0122

GLY 300 THR 301 -0.0001

THR 301 GLY 302 -0.0807

GLY 302 VAL 303 -0.0001

VAL 303 PRO 304 0.2589

PRO 304 THR 305 -0.0001

THR 305 PRO 306 0.0845

PRO 306 ASP 307 -0.0000

ASP 307 SER 308 0.1511

SER 308 PHE 309 -0.0002

PHE 309 TYR 310 0.0757

TYR 310 TYR 311 -0.0002

TYR 311 GLU 312 0.0206

GLU 312 SER 313 0.0003

SER 313 PHE 314 -0.0369

PHE 314 PRO 315 -0.0003

PRO 315 ASP 316 0.0388

ASP 316 ARG 317 -0.0001

ARG 317 ASP 318 -0.0121

ASP 318 PRO 319 -0.0000

PRO 319 LYS 320 0.0039

LYS 320 ILE 321 -0.0002

ILE 321 CYS 322 0.0566

CYS 322 CYS 322 0.0396

CYS 322 PHE 323 -0.0000

PHE 323 GLY 324 0.2533

GLY 324 ASP 325 0.0002

ASP 325 GLY 326 0.1033

GLY 326 ASP 327 0.0002

ASP 327 GLY 328 -0.0189

GLY 328 THR 329 -0.0001

THR 329 VAL 330 -0.0491

VAL 330 ASN 331 -0.0005

ASN 331 LEU 332 0.0602

LEU 332 LYS 333 -0.0003

LYS 333 SER 334 -0.0141

SER 334 SER 334 -0.0002

SER 334 ALA 335 0.0000

ALA 335 ALA 335 0.0003

ALA 335 LEU 336 -0.0075

LEU 336 LEU 336 -0.0002

LEU 336 GLN 337 -0.0004

GLN 337 GLN 337 -0.0011

GLN 337 CYS 338 0.0897

CYS 338 CYS 338 -0.0062

CYS 338 GLN 339 0.0002

GLN 339 ALA 340 -0.0426

ALA 340 TRP 341 0.0000

TRP 341 GLN 342 0.0220

GLN 342 SER 343 0.0001

SER 343 ARG 344 -0.0021

ARG 344 GLN 345 0.0004

GLN 345 GLU 346 0.0466

GLU 346 HIS 347 -0.0004

HIS 347 HIS 347 0.0122

HIS 347 GLN 348 -0.0181

GLN 348 VAL 349 -0.0002

VAL 349 LEU 350 -0.0632

LEU 350 LEU 350 -0.0229

LEU 350 LEU 351 0.0000

LEU 351 GLN 352 -0.0674

GLN 352 GLU 353 0.0002

GLU 353 LEU 354 -0.0428

LEU 354 PRO 355 -0.0001

PRO 355 GLY 356 -0.0761

GLY 356 SER 357 -0.0002

SER 357 GLU 358 -0.0949

GLU 358 HIS 359 0.0002

HIS 359 ILE 360 0.1185

ILE 360 GLU 361 -0.0001

GLU 361 MET 362 -0.1039

MET 362 LEU 363 0.0002

LEU 363 ALA 364 -0.0310

ALA 364 ASN 365 0.0000

ASN 365 ALA 366 0.0506

ALA 366 THR 367 -0.0001

THR 367 THR 367 -0.0042

THR 367 THR 368 -0.0585

THR 368 LEU 369 -0.0000

LEU 369 ALA 370 -0.0569

ALA 370 TYR 371 0.0000

TYR 371 LEU 372 0.0769

LEU 372 LYS 373 -0.0002

LYS 373 ARG 374 -0.0609

ARG 374 ARG 374 -0.0462

ARG 374 VAL 375 0.0001

VAL 375 LEU 376 0.1090

LEU 376 LEU 377 -0.0000

LEU 377 GLY 378 -0.1464

GLY 378 PRO 379 -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 2405271642113669817

--- normal mode 11 ---

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

* *