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

* *

CA strain for 22122720241827122

--- normal mode 10 ---

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 0.0189

LEU 3 ARG 4 -0.0002

ARG 4 HIS 5 -0.0261

HIS 5 THR 6 -0.0001

THR 6 PRO 7 -0.0288

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 0.0395

ARG 9 ASP 10 -0.0001

ASP 10 LEU 11 -0.0075

LEU 11 ASP 12 0.0004

ASP 12 LYS 13 0.0815

LYS 13 PHE 14 -0.0002

PHE 14 ILE 15 0.0127

ILE 15 GLU 16 -0.0001

GLU 16 ASP 17 0.0844

ASP 17 HIS 18 -0.0001

HIS 18 LEU 19 0.0167

LEU 19 LEU 20 0.0002

LEU 20 PRO 21 -0.2894

PRO 21 ASN 22 0.0001

ASN 22 THR 23 -0.0497

THR 23 CYS 24 -0.0001

CYS 24 PHE 25 0.1075

PHE 25 ARG 26 -0.0001

ARG 26 THR 27 -0.0118

THR 27 GLN 28 0.0001

GLN 28 VAL 29 0.0722

VAL 29 LYS 30 -0.0003

LYS 30 GLU 31 0.0794

GLU 31 ALA 32 -0.0003

ALA 32 ILE 33 0.0832

ILE 33 ASP 34 -0.0001

ASP 34 ILE 35 0.0755

ILE 35 VAL 36 0.0000

VAL 36 CYS 37 0.0716

CYS 37 ARG 38 -0.0000

ARG 38 PHE 39 0.0142

PHE 39 LEU 40 0.0000

LEU 40 LYS 41 -0.0062

LYS 41 GLU 42 -0.0001

GLU 42 ARG 43 0.1108

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 0.0312

PHE 45 GLN 46 -0.0002

GLN 46 GLY 47 -0.0426

GLY 47 THR 48 0.0002

THR 48 ALA 49 0.0501

ALA 49 ASP 50 0.0001

ASP 50 PRO 51 -0.0602

PRO 51 VAL 52 0.0002

VAL 52 ARG 53 -0.0610

ARG 53 VAL 54 -0.0004

VAL 54 SER 55 0.1742

SER 55 LYS 56 0.0001

LYS 56 VAL 57 0.0302

VAL 57 VAL 58 0.0000

VAL 58 LYS 59 -0.0818

LYS 59 GLY 60 -0.0001

GLY 60 GLY 61 0.0121

GLY 61 SER 62 -0.0000

SER 62 SER 63 0.0468

SER 63 GLY 64 0.0001

GLY 64 LYS 65 -0.0181

LYS 65 GLY 66 0.0001

GLY 66 THR 67 0.0940

THR 67 THR 68 0.0005

THR 68 LEU 69 0.0846

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 -0.1658

GLY 71 ARG 72 0.0001

ARG 72 SER 73 -0.0659

SER 73 ASP 74 0.0002

ASP 74 ALA 75 -0.0978

ALA 75 ASP 76 0.0003

ASP 76 LEU 77 -0.0735

LEU 77 VAL 78 -0.0003

VAL 78 VAL 79 -0.0612

VAL 79 PHE 80 -0.0001

PHE 80 LEU 81 -0.0380

LEU 81 THR 82 0.0006

THR 82 LYS 83 -0.0450

LYS 83 LEU 84 0.0004

LEU 84 THR 85 0.0206

THR 85 SER 86 0.0005

SER 86 PHE 87 0.0944

PHE 87 GLU 88 -0.0003

GLU 88 ASP 89 0.0895

ASP 89 GLN 90 -0.0004

GLN 90 LEU 91 -0.0131

LEU 91 ARG 92 0.0002

ARG 92 ARG 93 0.0201

ARG 93 ARG 94 0.0004

ARG 94 GLY 95 -0.0356

GLY 95 GLU 96 -0.0002

GLU 96 PHE 97 -0.0250

PHE 97 ILE 98 0.0003

ILE 98 GLN 99 -0.0298

GLN 99 GLU 100 0.0004

GLU 100 ILE 101 -0.0266

ILE 101 ARG 102 -0.0001

ARG 102 ARG 103 0.0795

ARG 103 GLN 104 0.0002

GLN 104 LEU 105 -0.0255

LEU 105 GLU 106 -0.0001

GLU 106 ALA 107 0.0116

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0418

GLN 109 ARG 110 -0.0000

ARG 110 GLU 111 -0.0188

GLU 111 GLN 112 0.0000

GLN 112 LYS 113 0.0198

LYS 113 PHE 114 -0.0002

PHE 114 LYS 115 0.0359

LYS 115 VAL 116 0.0004

VAL 116 THR 117 0.0835

THR 117 PHE 118 0.0004

PHE 118 GLY 119 -0.0433

GLY 119 VAL 120 0.0001

VAL 120 GLN 121 0.0272

GLN 121 SER 122 -0.0002

SER 122 PRO 123 0.0473

PRO 123 ARG 124 -0.0001

ARG 124 ARG 125 -0.0192

ARG 125 GLU 126 -0.0000

GLU 126 GLY 127 -0.0328

GLY 127 PRO 128 0.0002

PRO 128 ARG 129 -0.0171

ARG 129 ALA 130 0.0003

ALA 130 LEU 131 -0.1924

LEU 131 SER 132 0.0001

SER 132 PHE 133 0.0146

PHE 133 VAL 134 -0.0001

VAL 134 LEU 135 -0.0113

LEU 135 SER 136 -0.0000

SER 136 SER 137 0.0283

SER 137 PRO 138 0.0000

PRO 138 GLN 139 0.0110

GLN 139 LEU 140 -0.0001

LEU 140 GLN 141 0.0037

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 0.0619

GLU 143 VAL 144 0.0002

VAL 144 GLU 145 0.1017

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 0.0319

ASP 147 VAL 148 -0.0003

VAL 148 LEU 149 -0.0240

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 -0.0393

ALA 151 PHE 152 -0.0004

PHE 152 ASP 153 -0.0587

ASP 153 ALA 154 0.0002

ALA 154 LEU 155 -0.0687

LEU 155 GLY 156 0.0001

GLY 156 GLN 157 -0.0456

GLN 157 TRP 158 0.0002

TRP 158 THR 159 -0.0164

THR 159 PRO 160 0.0003

PRO 160 GLY 161 -0.0055

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 -0.0447

LYS 163 PRO 164 0.0004

PRO 164 ASN 165 0.0350

ASN 165 PRO 166 0.0000

PRO 166 GLU 167 -0.0050

GLU 167 ILE 168 0.0000

ILE 168 TYR 169 0.0503

TYR 169 VAL 170 0.0002

VAL 170 GLN 171 0.0268

GLN 171 LEU 172 -0.0002

LEU 172 ILE 173 0.0368

ILE 173 LYS 174 -0.0000

LYS 174 GLU 175 0.0172

GLU 175 CYS 176 0.0002

CYS 176 LYS 177 -0.0263

LYS 177 SER 178 0.0001

SER 178 ARG 179 0.0030

ARG 179 GLY 180 -0.0001

GLY 180 ALA 181 -0.1352

ALA 181 GLU 182 0.0000

GLU 182 GLY 183 -0.0086

GLY 183 GLU 184 -0.0002

GLU 184 PHE 185 0.0094

PHE 185 SER 186 -0.0004

SER 186 THR 187 0.0388

THR 187 CYS 188 0.0002

CYS 188 PHE 189 0.0102

PHE 189 THR 190 0.0003

THR 190 GLU 191 -0.0011

GLU 191 LEU 192 0.0003

LEU 192 GLN 193 0.0069

GLN 193 ARG 194 -0.0001

ARG 194 ARG 194 -0.0381

ARG 194 ASP 195 0.0188

ASP 195 PHE 196 0.0001

PHE 196 LEU 197 0.0736

LEU 197 ARG 198 0.0001

ARG 198 ASN 199 -0.0789

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 0.0404

PRO 201 THR 202 -0.0001

THR 202 LYS 203 -0.0064

LYS 203 LEU 204 0.0003

LEU 204 LYS 205 -0.1545

LYS 205 SER 206 0.0002

SER 206 LEU 207 -0.0488

LEU 207 ILE 208 0.0001

ILE 208 ARG 209 -0.0369

ARG 209 LEU 210 0.0001

LEU 210 VAL 211 0.0302

VAL 211 LYS 212 -0.0002

LYS 212 HIS 213 -0.0217

HIS 213 TRP 214 0.0000

TRP 214 TYR 215 -0.0200

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 -0.0619

THR 217 CYS 218 0.0002

CYS 218 GLU 219 -0.0303

GLU 219 LYS 220 -0.0002

LYS 220 THR 221 0.0204

THR 221 HIS 222 -0.0001

HIS 222 GLY 223 -0.0010

GLY 223 GLY 224 0.0002

GLY 224 LYS 225 -0.0252

LYS 225 LEU 226 0.0002

LEU 226 PRO 227 -0.0595

PRO 227 PRO 228 -0.0001

PRO 228 GLN 229 0.0198

GLN 229 TYR 230 0.0000

TYR 230 ALA 231 0.0401

ALA 231 LEU 232 0.0001

LEU 232 GLU 233 0.0363

GLU 233 LEU 234 0.0005

LEU 234 LEU 235 0.0419

LEU 235 THR 236 0.0001

THR 236 VAL 237 0.0257

VAL 237 TYR 238 -0.0001

TYR 238 ALA 239 0.1126

ALA 239 TRP 240 -0.0000

TRP 240 GLU 241 0.0428

GLU 241 GLN 242 0.0003

GLN 242 GLY 243 0.0695

GLY 243 SER 244 -0.0004

SER 244 ARG 245 -0.0249

ARG 245 LYS 246 0.0001

LYS 246 THR 247 -0.0218

THR 247 ASP 248 -0.0000

ASP 248 PHE 249 0.0059

PHE 249 SER 250 0.0000

SER 250 THR 251 -0.0323

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 0.0271

GLN 253 GLY 254 -0.0003

GLY 254 PHE 255 0.0098

PHE 255 GLN 256 0.0001

GLN 256 THR 257 0.0583

THR 257 VAL 258 0.0000

VAL 258 LEU 259 -0.0213

LEU 259 GLU 260 -0.0000

GLU 260 LEU 261 0.0750

LEU 261 VAL 262 -0.0002

VAL 262 LEU 263 -0.0193

LEU 263 LYS 264 0.0001

LYS 264 HIS 265 0.0374

HIS 265 GLN 266 0.0000

GLN 266 LYS 267 -0.0511

LYS 267 LEU 268 0.0001

LEU 268 CYS 269 0.0405

CYS 269 ILE 270 -0.0003

ILE 270 PHE 271 -0.0746

PHE 271 TRP 272 0.0000

TRP 272 GLU 273 0.0228

GLU 273 ALA 274 -0.0000

ALA 274 TYR 275 0.0006

TYR 275 TYR 276 0.0001

TYR 276 ASP 277 0.0012

ASP 277 PHE 278 -0.0000

PHE 278 THR 279 -0.0279

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 0.0045

PRO 281 VAL 282 0.0000

VAL 282 VAL 283 0.0215

VAL 283 GLY 284 -0.0001

GLY 284 ARG 285 0.0149

ARG 285 CYS 286 -0.0002

CYS 286 MET 287 0.0903

MET 287 LEU 288 0.0001

LEU 288 GLN 289 -0.0082

GLN 289 GLN 290 -0.0001

GLN 290 LEU 291 0.1349

LEU 291 LYS 292 -0.0000

LYS 292 LYS 293 -0.1252

LYS 293 PRO 294 -0.0005

PRO 294 ARG 295 0.0236

ARG 295 PRO 296 -0.0004

PRO 296 VAL 297 -0.0108

VAL 297 ILE 298 -0.0000

ILE 298 LEU 299 0.0368

LEU 299 ASP 300 0.0000

ASP 300 PRO 301 -0.0215

PRO 301 ALA 302 -0.0001

ALA 302 ASP 303 0.0140

ASP 303 PRO 304 -0.0000

PRO 304 THR 305 -0.0073

THR 305 GLY 306 -0.0002

GLY 306 ASN 307 0.1596

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 0.0762

GLY 309 GLY 310 0.0000

GLY 310 GLY 311 -0.0386

GLY 311 ASP 312 0.0003

ASP 312 THR 313 0.0302

THR 313 HIS 314 0.0004

HIS 314 SER 315 0.0430

SER 315 TRP 316 0.0002

TRP 316 GLN 317 0.0189

GLN 317 ARG 318 0.0002

ARG 318 LEU 319 -0.0045

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 0.0227

GLN 321 GLU 322 -0.0001

GLU 322 ALA 323 -0.0093

ALA 323 ARG 324 -0.0004

ARG 324 VAL 325 0.0376

VAL 325 TRP 326 -0.0002

TRP 326 LEU 327 -0.0201

LEU 327 GLY 328 0.0004

GLY 328 TYR 329 0.0068

TYR 329 PRO 330 -0.0001

PRO 330 CYS 331 0.0258

CYS 331 CYS 332 -0.0001

CYS 332 LYS 333 0.0232

LYS 333 ASN 334 -0.0001

ASN 334 LEU 335 0.1263

LEU 335 ASP 336 0.0003

ASP 336 GLY 337 -0.0551

GLY 337 SER 338 0.0000

SER 338 LEU 339 0.0408

LEU 339 VAL 340 0.0001

VAL 340 GLY 341 0.1400

GLY 341 ALA 342 -0.0003

ALA 342 TRP 343 0.0596

TRP 343 THR 344 -0.0002

THR 344 MET 345 0.0962

MET 345 LEU 346 -0.0004

LEU 346 GLN 347 0.0105

GLN 347 LYS 348 0.0002

LYS 348 ILE 349 0.0165

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 22122720241827122

--- normal mode 10 ---

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

* *