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

* *

CA strain for 22122720105119216

--- 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
MET 1 GLU 2 -0.0001

GLU 2 LEU 3 -0.0076

LEU 3 ARG 4 -0.0002

ARG 4 HIS 5 -0.0189

HIS 5 THR 6 0.0002

THR 6 PRO 7 0.0031

PRO 7 ALA 8 0.0001

ALA 8 ARG 9 -0.0032

ARG 9 ASP 10 -0.0000

ASP 10 LEU 11 0.0056

LEU 11 ASP 12 -0.0002

ASP 12 LYS 13 0.0098

LYS 13 PHE 14 0.0000

PHE 14 ILE 15 0.0329

ILE 15 GLU 16 0.0000

GLU 16 ASP 17 0.0391

ASP 17 HIS 18 -0.0002

HIS 18 LEU 19 -0.0046

LEU 19 LEU 20 -0.0003

LEU 20 PRO 21 -0.0688

PRO 21 ASN 22 0.0001

ASN 22 THR 23 0.0118

THR 23 CYS 24 -0.0002

CYS 24 PHE 25 0.0581

PHE 25 ARG 26 -0.0004

ARG 26 THR 27 0.0384

THR 27 GLN 28 -0.0001

GLN 28 VAL 29 -0.0165

VAL 29 LYS 30 -0.0002

LYS 30 GLU 31 -0.0433

GLU 31 ALA 32 0.0002

ALA 32 ILE 33 -0.0469

ILE 33 ASP 34 0.0001

ASP 34 ILE 35 -0.0322

ILE 35 VAL 36 0.0000

VAL 36 CYS 37 -0.0460

CYS 37 ARG 38 -0.0001

ARG 38 PHE 39 0.0305

PHE 39 LEU 40 0.0000

LEU 40 LYS 41 -0.0024

LYS 41 GLU 42 -0.0002

GLU 42 ARG 43 -0.0536

ARG 43 CYS 44 0.0002

CYS 44 PHE 45 -0.0197

PHE 45 GLN 46 -0.0002

GLN 46 GLY 47 0.0214

GLY 47 THR 48 0.0001

THR 48 ALA 49 -0.0463

ALA 49 ASP 50 0.0001

ASP 50 PRO 51 0.0237

PRO 51 VAL 52 0.0005

VAL 52 ARG 53 0.0340

ARG 53 VAL 54 0.0001

VAL 54 SER 55 -0.0939

SER 55 LYS 56 -0.0002

LYS 56 VAL 57 -0.0309

VAL 57 VAL 58 0.0001

VAL 58 LYS 59 0.0639

LYS 59 GLY 60 -0.0001

GLY 60 GLY 61 -0.0540

GLY 61 SER 62 0.0003

SER 62 SER 63 0.0411

SER 63 GLY 64 -0.0004

GLY 64 LYS 65 -0.0037

LYS 65 GLY 66 0.0001

GLY 66 THR 67 0.0442

THR 67 THR 68 -0.0004

THR 68 LEU 69 0.0156

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 -0.1507

GLY 71 ARG 72 0.0002

ARG 72 SER 73 -0.1180

SER 73 ASP 74 0.0000

ASP 74 ALA 75 -0.0427

ALA 75 ASP 76 0.0001

ASP 76 LEU 77 -0.0497

LEU 77 VAL 78 0.0001

VAL 78 VAL 79 0.0145

VAL 79 PHE 80 -0.0005

PHE 80 LEU 81 0.0303

LEU 81 THR 82 -0.0002

THR 82 LYS 83 0.0277

LYS 83 LEU 84 0.0003

LEU 84 THR 85 -0.0204

THR 85 SER 86 -0.0001

SER 86 PHE 87 -0.0433

PHE 87 GLU 88 0.0000

GLU 88 ASP 89 -0.0190

ASP 89 GLN 90 0.0001

GLN 90 LEU 91 -0.0038

LEU 91 ARG 92 -0.0000

ARG 92 ARG 93 0.0224

ARG 93 ARG 94 -0.0002

ARG 94 GLY 95 0.0325

GLY 95 GLU 96 -0.0002

GLU 96 PHE 97 0.0017

PHE 97 ILE 98 -0.0000

ILE 98 GLN 99 0.0063

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 -0.0173

ILE 101 ARG 102 -0.0001

ARG 102 ARG 103 -0.0534

ARG 103 GLN 104 0.0002

GLN 104 LEU 105 -0.0222

LEU 105 GLU 106 -0.0002

GLU 106 ALA 107 -0.0141

ALA 107 CYS 108 0.0003

CYS 108 GLN 109 -0.0275

GLN 109 ARG 110 -0.0002

ARG 110 GLU 111 0.0078

GLU 111 GLN 112 -0.0003

GLN 112 LYS 113 -0.0207

LYS 113 PHE 114 0.0003

PHE 114 LYS 115 0.0222

LYS 115 VAL 116 -0.0002

VAL 116 THR 117 0.0160

THR 117 PHE 118 0.0003

PHE 118 GLU 119 -0.0090

GLU 119 VAL 120 -0.0001

VAL 120 GLN 121 0.0358

GLN 121 SER 122 -0.0001

SER 122 PRO 123 -0.0459

PRO 123 ARG 124 -0.0000

ARG 124 ARG 125 -0.0113

ARG 125 GLU 126 0.0003

GLU 126 ASN 127 0.0318

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 -0.0040

ARG 129 ALA 130 0.0001

ALA 130 LEU 131 0.2421

LEU 131 SER 132 0.0001

SER 132 PHE 133 0.0692

PHE 133 VAL 134 -0.0001

VAL 134 LEU 135 0.0147

LEU 135 SER 136 -0.0003

SER 136 SER 137 0.0345

SER 137 PRO 138 -0.0003

PRO 138 GLN 139 -0.0086

GLN 139 LEU 140 0.0001

LEU 140 GLN 141 -0.0067

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 -0.0257

GLU 143 VAL 144 0.0005

VAL 144 GLU 145 0.0242

GLU 145 PHE 146 0.0003

PHE 146 ASP 147 0.0156

ASP 147 VAL 148 0.0001

VAL 148 LEU 149 0.0051

LEU 149 PRO 150 -0.0004

PRO 150 ALA 151 0.0236

ALA 151 PHE 152 -0.0003

PHE 152 ASP 153 0.0325

ASP 153 ALA 154 0.0005

ALA 154 LEU 155 0.0850

LEU 155 GLY 156 -0.0001

GLY 156 GLN 157 0.0191

GLN 157 TRP 158 0.0000

TRP 158 THR 159 0.0053

THR 159 PRO 160 -0.0001

PRO 160 GLY 161 -0.0056

GLY 161 TYR 162 -0.0000

TYR 162 LYS 163 -0.0247

LYS 163 PRO 164 -0.0000

PRO 164 ASN 165 -0.0054

ASN 165 PRO 166 -0.0001

PRO 166 GLU 167 0.0370

GLU 167 ILE 168 -0.0002

ILE 168 TYR 169 -0.0296

TYR 169 VAL 170 -0.0002

VAL 170 GLN 171 0.0067

GLN 171 LEU 172 -0.0001

LEU 172 ILE 173 0.0075

ILE 173 LYS 174 -0.0002

LYS 174 GLU 175 0.0403

GLU 175 CYS 176 -0.0000

CYS 176 LYS 177 -0.0176

LYS 177 SER 178 0.0002

SER 178 ARG 179 0.0348

ARG 179 GLY 180 0.0003

GLY 180 LYS 181 0.0139

LYS 181 GLU 182 0.0001

GLU 182 GLY 183 -0.0033

GLY 183 GLU 184 -0.0001

GLU 184 PHE 185 -0.0277

PHE 185 SER 186 -0.0001

SER 186 THR 187 0.0917

THR 187 CYS 188 0.0000

CYS 188 PHE 189 0.0185

PHE 189 THR 190 0.0001

THR 190 GLU 191 -0.0084

GLU 191 LEU 192 -0.0004

LEU 192 GLN 193 0.0009

GLN 193 ARG 194 -0.0000

ARG 194 ARG 194 0.0749

ARG 194 ASP 195 -0.0100

ASP 195 PHE 196 0.0000

PHE 196 LEU 197 0.0635

LEU 197 ARG 198 0.0003

ARG 198 ASN 199 -0.0361

ASN 199 ARG 200 -0.0002

ARG 200 PRO 201 0.0824

PRO 201 THR 202 0.0001

THR 202 LYS 203 0.0506

LYS 203 LEU 204 0.0003

LEU 204 LYS 205 -0.0639

LYS 205 SER 206 0.0002

SER 206 LEU 207 -0.0195

LEU 207 ILE 208 -0.0002

ILE 208 ARG 209 -0.0116

ARG 209 LEU 210 -0.0001

LEU 210 VAL 211 -0.0063

VAL 211 LYS 212 0.0002

LYS 212 HIS 213 -0.0506

HIS 213 TRP 214 -0.0003

TRP 214 TYR 215 -0.0339

TYR 215 GLN 216 0.0001

GLN 216 THR 217 -0.0355

THR 217 CYS 218 0.0003

CYS 218 LYS 219 -0.0302

LYS 219 LYS 220 -0.0003

LYS 220 THR 221 0.0113

THR 221 HIS 222 0.0000

HIS 222 GLY 223 -0.0293

GLY 223 ASN 224 0.0000

ASN 224 LYS 225 0.0193

LYS 225 LEU 226 0.0003

LEU 226 PRO 227 -0.0814

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 0.0667

GLN 229 TYR 230 0.0000

TYR 230 ALA 231 0.0239

ALA 231 LEU 232 -0.0003

LEU 232 GLU 233 0.0225

GLU 233 LEU 234 -0.0001

LEU 234 LEU 235 -0.0045

LEU 235 THR 236 -0.0002

THR 236 VAL 237 0.0356

VAL 237 TYR 238 -0.0002

TYR 238 ALA 239 0.0470

ALA 239 TRP 240 0.0005

TRP 240 GLU 241 0.0179

GLU 241 GLN 242 0.0001

GLN 242 GLY 243 0.0331

GLY 243 SER 244 0.0003

SER 244 ARG 245 0.0076

ARG 245 LYS 246 0.0004

LYS 246 THR 247 -0.0206

THR 247 ASP 248 0.0001

ASP 248 PHE 249 0.0275

PHE 249 SER 250 -0.0002

SER 250 THR 251 -0.0275

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 -0.0039

GLN 253 GLY 254 0.0000

GLY 254 PHE 255 0.0137

PHE 255 GLN 256 0.0001

GLN 256 THR 257 0.0238

THR 257 VAL 258 0.0001

VAL 258 LEU 259 0.0124

LEU 259 GLU 260 0.0000

GLU 260 LEU 261 -0.0054

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 0.0113

LEU 263 LYS 264 -0.0001

LYS 264 HIS 265 -0.0209

HIS 265 GLN 266 0.0001

GLN 266 LYS 267 0.0426

LYS 267 LEU 268 0.0003

LEU 268 CYS 269 0.0565

CYS 269 ILE 270 0.0004

ILE 270 PHE 271 0.0485

PHE 271 TRP 272 0.0004

TRP 272 GLU 273 0.0815

GLU 273 ALA 274 -0.0005

ALA 274 TYR 275 0.0312

TYR 275 TYR 276 0.0002

TYR 276 ASP 277 -0.0390

ASP 277 PHE 278 -0.0006

PHE 278 THR 279 0.0257

THR 279 ASN 280 0.0000

ASN 280 PRO 281 -0.0377

PRO 281 VAL 282 0.0001

VAL 282 VAL 283 0.0098

VAL 283 GLY 284 0.0000

GLY 284 ARG 285 -0.0015

ARG 285 CYS 286 -0.0004

CYS 286 MET 287 0.0253

MET 287 LEU 288 0.0000

LEU 288 GLN 289 0.0098

GLN 289 GLN 290 -0.0000

GLN 290 LEU 291 0.0344

LEU 291 LYS 292 -0.0003

LYS 292 LYS 293 -0.0099

LYS 293 PRO 294 0.0002

PRO 294 ARG 295 -0.0312

ARG 295 PRO 296 -0.0000

PRO 296 VAL 297 -0.0427

VAL 297 ILE 298 -0.0005

ILE 298 LEU 299 -0.0259

LEU 299 ASP 300 -0.0001

ASP 300 PRO 301 -0.0358

PRO 301 ALA 302 0.0002

ALA 302 ASP 303 0.0190

ASP 303 PRO 304 0.0001

PRO 304 THR 305 0.0309

THR 305 GLY 306 -0.0001

GLY 306 ASN 307 -0.1514

ASN 307 VAL 308 0.0003

VAL 308 GLY 309 -0.0640

GLY 309 GLY 310 0.0002

GLY 310 GLY 311 0.0599

GLY 311 ASP 312 0.0000

ASP 312 THR 313 -0.0069

THR 313 HIS 314 -0.0001

HIS 314 SER 315 0.0189

SER 315 TRP 316 -0.0000

TRP 316 GLN 317 -0.0129

GLN 317 ARG 318 0.0000

ARG 318 LEU 319 0.0183

LEU 319 ALA 320 0.0002

ALA 320 GLN 321 0.0140

GLN 321 GLU 322 -0.0002

GLU 322 ALA 323 0.0076

ALA 323 ARG 324 0.0001

ARG 324 VAL 325 0.0073

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 -0.0023

LEU 327 GLY 328 0.0001

GLY 328 TYR 329 -0.0009

TYR 329 PRO 330 0.0002

PRO 330 CYS 331 0.0159

CYS 331 CYS 332 0.0000

CYS 332 LYS 333 0.0085

LYS 333 ASN 334 0.0005

ASN 334 LEU 335 0.0345

LEU 335 ASP 336 0.0002

ASP 336 GLY 337 -0.0464

GLY 337 SER 338 0.0000

SER 338 LEU 339 -0.0062

LEU 339 VAL 340 -0.0000

VAL 340 GLY 341 0.0248

GLY 341 ALA 342 -0.0004

ALA 342 TRP 343 0.0394

TRP 343 THR 344 -0.0002

THR 344 MET 345 0.0255

MET 345 LEU 346 0.0002

LEU 346 GLN 347 -0.0002

GLN 347 LYS 348 0.0000

LYS 348 ILE 349 -0.0011

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: October 18th, 2018.

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

*** ***

CA strain for 22122720105119216

--- normal mode 8 ---

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

* *