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

* *

CA strain for 22122720180123252

--- 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
MET 1 GLU 2 0.0000

GLU 2 LEU 3 0.0025

LEU 3 ARG 4 0.0001

ARG 4 HIS 5 0.0057

HIS 5 THR 6 -0.0002

THR 6 PRO 7 0.0178

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 -0.0273

ARG 9 ASP 10 0.0001

ASP 10 LEU 11 0.0184

LEU 11 ASP 12 0.0003

ASP 12 LYS 13 -0.0479

LYS 13 PHE 14 0.0001

PHE 14 ILE 15 0.0270

ILE 15 GLU 16 0.0003

GLU 16 ASP 17 -0.0340

ASP 17 HIS 18 0.0004

HIS 18 LEU 19 0.0192

LEU 19 LEU 20 -0.0003

LEU 20 PRO 21 0.0581

PRO 21 ASN 22 0.0000

ASN 22 THR 23 0.0153

THR 23 CYS 24 -0.0002

CYS 24 PHE 25 -0.0469

PHE 25 ARG 26 -0.0000

ARG 26 THR 27 -0.0407

THR 27 GLN 28 -0.0002

GLN 28 VAL 29 0.0040

VAL 29 LYS 30 0.0002

LYS 30 GLU 31 0.0041

GLU 31 ALA 32 -0.0002

ALA 32 ILE 33 0.0070

ILE 33 ASP 34 -0.0001

ASP 34 ILE 35 -0.0012

ILE 35 VAL 36 -0.0002

VAL 36 CYS 37 0.0109

CYS 37 ARG 38 -0.0000

ARG 38 PHE 39 -0.0066

PHE 39 LEU 40 -0.0003

LEU 40 LYS 41 -0.0006

LYS 41 GLU 42 -0.0004

GLU 42 ARG 43 0.0105

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 0.0105

PHE 45 GLN 46 0.0004

GLN 46 GLY 47 -0.0117

GLY 47 THR 48 0.0001

THR 48 ALA 49 0.0544

ALA 49 ASP 50 0.0001

ASP 50 PRO 51 -0.0418

PRO 51 VAL 52 0.0000

VAL 52 ARG 53 -0.0315

ARG 53 VAL 54 -0.0001

VAL 54 SER 55 -0.0522

SER 55 LYS 56 -0.0000

LYS 56 VAL 57 0.0288

VAL 57 VAL 58 0.0006

VAL 58 LYS 59 0.0251

LYS 59 GLY 60 0.0004

GLY 60 GLY 61 0.0233

GLY 61 SER 62 0.0002

SER 62 SER 63 -0.0532

SER 63 GLY 64 -0.0003

GLY 64 LYS 65 -0.0126

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 0.0027

THR 67 THR 68 0.0001

THR 68 LEU 69 0.0416

LEU 69 ARG 70 0.0002

ARG 70 GLY 71 0.0646

GLY 71 ARG 72 0.0001

ARG 72 SER 73 0.0662

SER 73 ASP 74 -0.0000

ASP 74 ALA 75 0.0383

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 0.0317

LEU 77 VAL 78 -0.0004

VAL 78 VAL 79 -0.0027

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 -0.0317

LEU 81 THR 82 -0.0001

THR 82 LYS 83 -0.0007

LYS 83 LEU 84 -0.0002

LEU 84 THR 85 -0.0031

THR 85 SER 86 0.0003

SER 86 PHE 87 0.0037

PHE 87 GLU 88 0.0002

GLU 88 ASP 89 0.0128

ASP 89 GLN 90 0.0004

GLN 90 LEU 91 0.0112

LEU 91 ARG 92 -0.0000

ARG 92 ARG 93 0.0077

ARG 93 ARG 94 0.0002

ARG 94 GLY 95 -0.0188

GLY 95 GLU 96 0.0002

GLU 96 PHE 97 0.0014

PHE 97 ILE 98 0.0000

ILE 98 GLN 99 -0.0046

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 0.0031

ILE 101 ARG 102 0.0002

ARG 102 ARG 103 0.0426

ARG 103 GLN 104 -0.0001

GLN 104 LEU 105 0.0065

LEU 105 GLU 106 0.0004

GLU 106 ALA 107 0.0204

ALA 107 CYS 108 0.0001

CYS 108 GLN 109 0.0096

GLN 109 ARG 110 -0.0002

ARG 110 GLU 111 0.0021

GLU 111 GLN 112 -0.0000

GLN 112 LYS 113 0.0019

LYS 113 PHE 114 -0.0001

PHE 114 LYS 115 0.0061

LYS 115 VAL 116 0.0004

VAL 116 THR 117 0.0153

THR 117 PHE 118 -0.0002

PHE 118 GLY 119 -0.0312

GLY 119 VAL 120 -0.0003

VAL 120 GLN 121 0.0020

GLN 121 SER 122 -0.0001

SER 122 PRO 123 0.0212

PRO 123 ARG 124 0.0001

ARG 124 ARG 125 -0.0176

ARG 125 GLU 126 0.0000

GLU 126 GLY 127 0.0158

GLY 127 PRO 128 -0.0002

PRO 128 ARG 129 0.0109

ARG 129 ALA 130 -0.0001

ALA 130 LEU 131 -0.1156

LEU 131 SER 132 -0.0001

SER 132 PHE 133 -0.0378

PHE 133 VAL 134 -0.0002

VAL 134 LEU 135 -0.0196

LEU 135 SER 136 0.0001

SER 136 SER 137 -0.0160

SER 137 PRO 138 0.0005

PRO 138 GLN 139 -0.0007

GLN 139 LEU 140 0.0001

LEU 140 GLN 141 0.0126

GLN 141 GLN 142 0.0003

GLN 142 GLU 143 -0.0142

GLU 143 VAL 144 0.0000

VAL 144 GLU 145 -0.0212

GLU 145 PHE 146 -0.0004

PHE 146 ASP 147 0.0036

ASP 147 VAL 148 0.0002

VAL 148 LEU 149 0.0056

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 -0.0282

ALA 151 PHE 152 -0.0001

PHE 152 ASP 153 -0.0219

ASP 153 ALA 154 0.0001

ALA 154 LEU 155 -0.0172

LEU 155 GLY 156 -0.0000

GLY 156 GLN 157 -0.0251

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 -0.0118

THR 159 PRO 160 0.0000

PRO 160 GLY 161 0.0087

GLY 161 TYR 162 0.0000

TYR 162 LYS 163 -0.0100

LYS 163 PRO 164 -0.0001

PRO 164 ASN 165 0.0453

ASN 165 PRO 166 0.0002

PRO 166 GLU 167 -0.0045

GLU 167 ILE 168 0.0002

ILE 168 TYR 169 -0.0116

TYR 169 VAL 170 -0.0002

VAL 170 GLN 171 -0.0129

GLN 171 LEU 172 -0.0001

LEU 172 ILE 173 0.0079

ILE 173 LYS 174 0.0001

LYS 174 GLU 175 -0.0069

GLU 175 CYS 176 0.0000

CYS 176 LYS 177 -0.0019

LYS 177 SER 178 -0.0000

SER 178 ARG 179 -0.0072

ARG 179 GLY 180 -0.0001

GLY 180 LYS 181 -0.0060

LYS 181 GLU 182 0.0000

GLU 182 GLY 183 -0.0095

GLY 183 GLU 184 0.0001

GLU 184 PHE 185 -0.0048

PHE 185 SER 186 0.0003

SER 186 THR 187 -0.0459

THR 187 CYS 188 -0.0003

CYS 188 PHE 189 -0.0242

PHE 189 THR 190 -0.0004

THR 190 GLU 191 0.0287

GLU 191 LEU 192 0.0000

LEU 192 GLN 193 -0.0022

GLN 193 ARG 194 -0.0003

ARG 194 ARG 194 0.1533

ARG 194 ASP 195 0.0231

ASP 195 PHE 196 0.0007

PHE 196 LEU 197 0.0709

LEU 197 ARG 198 -0.0002

ARG 198 ASN 199 -0.0155

ASN 199 ARG 200 0.0003

ARG 200 PRO 201 0.0729

PRO 201 THR 202 0.0002

THR 202 LYS 203 0.0685

LYS 203 LEU 204 0.0002

LEU 204 LYS 205 -0.0404

LYS 205 SER 206 0.0001

SER 206 LEU 207 0.0376

LEU 207 ILE 208 0.0005

ILE 208 ARG 209 0.0188

ARG 209 LEU 210 -0.0003

LEU 210 VAL 211 -0.0078

VAL 211 LYS 212 0.0005

LYS 212 HIS 213 0.0544

HIS 213 TRP 214 0.0001

TRP 214 TYR 215 0.0017

TYR 215 GLN 216 -0.0001

GLN 216 THR 217 0.0343

THR 217 CYS 218 0.0000

CYS 218 LYS 219 0.0228

LYS 219 LYS 220 0.0005

LYS 220 THR 221 -0.0090

THR 221 HIS 222 -0.0002

HIS 222 GLY 223 0.0180

GLY 223 ASN 224 -0.0001

ASN 224 LYS 225 0.0221

LYS 225 LEU 226 -0.0001

LEU 226 PRO 227 0.0078

PRO 227 PRO 228 0.0001

PRO 228 GLN 229 -0.0158

GLN 229 TYR 230 0.0002

TYR 230 ALA 231 -0.0215

ALA 231 LEU 232 -0.0001

LEU 232 GLU 233 -0.0244

GLU 233 LEU 234 -0.0000

LEU 234 LEU 235 -0.0560

LEU 235 THR 236 -0.0005

THR 236 VAL 237 -0.0922

VAL 237 TYR 238 -0.0002

TYR 238 ALA 239 -0.0153

ALA 239 TRP 240 0.0001

TRP 240 GLU 241 -0.1048

GLU 241 GLN 242 -0.0003

GLN 242 GLY 243 -0.0056

GLY 243 SER 244 0.0000

SER 244 ARG 245 0.0621

ARG 245 LYS 246 -0.0003

LYS 246 THR 247 -0.0420

THR 247 ASP 248 0.0003

ASP 248 PHE 249 0.0396

PHE 249 SER 250 0.0000

SER 250 THR 251 -0.0132

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 -0.0027

GLN 253 GLY 254 -0.0002

GLY 254 PHE 255 -0.0005

PHE 255 GLN 256 0.0000

GLN 256 THR 257 0.0326

THR 257 VAL 258 -0.0002

VAL 258 LEU 259 0.0584

LEU 259 GLU 260 0.0002

GLU 260 LEU 261 -0.0379

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 0.0362

LEU 263 LYS 264 0.0003

LYS 264 HIS 265 -0.0323

HIS 265 GLN 266 -0.0001

GLN 266 LYS 267 0.0708

LYS 267 LEU 268 -0.0002

LEU 268 CYS 269 -0.0729

CYS 269 ILE 270 0.0000

ILE 270 PHE 271 -0.0849

PHE 271 TRP 272 0.0004

TRP 272 GLU 273 0.0433

GLU 273 ALA 274 0.0002

ALA 274 TYR 275 -0.0443

TYR 275 TYR 276 0.0004

TYR 276 ASP 277 0.0321

ASP 277 PHE 278 0.0001

PHE 278 THR 279 -0.0137

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 0.0060

PRO 281 VAL 282 -0.0003

VAL 282 VAL 283 0.0191

VAL 283 GLY 284 0.0001

GLY 284 ARG 285 0.0084

ARG 285 CYS 286 0.0004

CYS 286 MET 287 0.0338

MET 287 LEU 288 0.0003

LEU 288 GLN 289 0.0371

GLN 289 GLN 290 0.0001

GLN 290 LEU 291 0.0235

LEU 291 LYS 292 0.0001

LYS 292 LYS 293 0.0262

LYS 293 PRO 294 -0.0002

PRO 294 ARG 295 -0.0417

ARG 295 PRO 296 -0.0002

PRO 296 VAL 297 -0.0485

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0614

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 -0.0285

PRO 301 ALA 302 0.0002

ALA 302 ASP 303 0.0137

ASP 303 PRO 304 -0.0001

PRO 304 THR 305 0.0139

THR 305 GLY 306 0.0004

GLY 306 ASN 307 -0.0847

ASN 307 VAL 308 0.0002

VAL 308 GLY 309 -0.0613

GLY 309 GLY 310 0.0000

GLY 310 GLY 311 0.0263

GLY 311 ASP 312 0.0002

ASP 312 THR 313 -0.0054

THR 313 HIS 314 -0.0003

HIS 314 SER 315 -0.0169

SER 315 TRP 316 -0.0003

TRP 316 GLN 317 -0.0121

GLN 317 ARG 318 -0.0003

ARG 318 LEU 319 0.0168

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 0.0157

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 0.0442

ALA 323 ARG 324 -0.0001

ARG 324 VAL 325 -0.0248

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 0.0176

LEU 327 GLY 328 -0.0001

GLY 328 TYR 329 -0.0082

TYR 329 PRO 330 0.0000

PRO 330 CYS 331 0.0015

CYS 331 CYS 332 -0.0002

CYS 332 LYS 333 -0.0144

LYS 333 ASN 334 -0.0001

ASN 334 LEU 335 -0.0501

LEU 335 ASP 336 0.0001

ASP 336 GLY 337 -0.0103

GLY 337 SER 338 0.0001

SER 338 LEU 339 -0.0337

LEU 339 VAL 340 -0.0001

VAL 340 GLY 341 -0.0348

GLY 341 ALA 342 -0.0003

ALA 342 TRP 343 0.0133

TRP 343 THR 344 0.0002

THR 344 MET 345 -0.0001

MET 345 LEU 346 0.0002

LEU 346 GLN 347 0.0039

GLN 347 LYS 348 -0.0002

LYS 348 ILE 349 -0.0289

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 22122720180123252

--- normal mode 11 ---

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

* *