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

* *

CA strain for 22122720241827122

--- 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 0.0002

GLU 2 LEU 3 0.0393

LEU 3 ARG 4 -0.0002

ARG 4 HIS 5 -0.0211

HIS 5 THR 6 -0.0000

THR 6 PRO 7 -0.0464

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 0.0197

ARG 9 ASP 10 0.0001

ASP 10 LEU 11 -0.0123

LEU 11 ASP 12 -0.0002

ASP 12 LYS 13 0.0117

LYS 13 PHE 14 0.0003

PHE 14 ILE 15 -0.0226

ILE 15 GLU 16 0.0001

GLU 16 ASP 17 0.0235

ASP 17 HIS 18 -0.0003

HIS 18 LEU 19 0.0093

LEU 19 LEU 20 -0.0001

LEU 20 PRO 21 -0.0842

PRO 21 ASN 22 0.0000

ASN 22 THR 23 -0.0377

THR 23 CYS 24 -0.0003

CYS 24 PHE 25 -0.0184

PHE 25 ARG 26 0.0000

ARG 26 THR 27 -0.1168

THR 27 GLN 28 0.0001

GLN 28 VAL 29 0.0946

VAL 29 LYS 30 0.0002

LYS 30 GLU 31 0.0536

GLU 31 ALA 32 -0.0003

ALA 32 ILE 33 0.1287

ILE 33 ASP 34 -0.0000

ASP 34 ILE 35 0.0256

ILE 35 VAL 36 0.0004

VAL 36 CYS 37 0.0974

CYS 37 ARG 38 -0.0003

ARG 38 PHE 39 -0.0589

PHE 39 LEU 40 0.0000

LEU 40 LYS 41 0.0245

LYS 41 GLU 42 -0.0003

GLU 42 ARG 43 0.0274

ARG 43 CYS 44 -0.0001

CYS 44 PHE 45 0.0183

PHE 45 GLN 46 -0.0002

GLN 46 GLY 47 -0.0564

GLY 47 THR 48 -0.0001

THR 48 ALA 49 0.1072

ALA 49 ASP 50 -0.0001

ASP 50 PRO 51 -0.1175

PRO 51 VAL 52 0.0001

VAL 52 ARG 53 -0.0648

ARG 53 VAL 54 0.0004

VAL 54 SER 55 -0.0625

SER 55 LYS 56 -0.0004

LYS 56 VAL 57 0.0363

VAL 57 VAL 58 0.0002

VAL 58 LYS 59 -0.1923

LYS 59 GLY 60 0.0003

GLY 60 GLY 61 -0.1074

GLY 61 SER 62 -0.0002

SER 62 SER 63 -0.0458

SER 63 GLY 64 0.0001

GLY 64 LYS 65 0.0293

LYS 65 GLY 66 0.0000

GLY 66 THR 67 -0.0597

THR 67 THR 68 0.0004

THR 68 LEU 69 -0.0058

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 0.0425

GLY 71 ARG 72 -0.0000

ARG 72 SER 73 -0.0607

SER 73 ASP 74 -0.0003

ASP 74 ALA 75 -0.1576

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 -0.1265

LEU 77 VAL 78 0.0001

VAL 78 VAL 79 -0.0526

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 -0.0982

LEU 81 THR 82 -0.0001

THR 82 LYS 83 -0.0024

LYS 83 LEU 84 -0.0000

LEU 84 THR 85 -0.0188

THR 85 SER 86 0.0001

SER 86 PHE 87 0.0298

PHE 87 GLU 88 -0.0001

GLU 88 ASP 89 0.0393

ASP 89 GLN 90 0.0003

GLN 90 LEU 91 0.0009

LEU 91 ARG 92 -0.0001

ARG 92 ARG 93 -0.0244

ARG 93 ARG 94 -0.0000

ARG 94 GLY 95 0.0522

GLY 95 GLU 96 -0.0001

GLU 96 PHE 97 0.0140

PHE 97 ILE 98 0.0002

ILE 98 GLN 99 0.0595

GLN 99 GLU 100 0.0002

GLU 100 ILE 101 -0.0011

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 -0.0314

ARG 103 GLN 104 0.0001

GLN 104 LEU 105 0.0169

LEU 105 GLU 106 -0.0000

GLU 106 ALA 107 -0.0088

ALA 107 CYS 108 -0.0002

CYS 108 GLN 109 0.0418

GLN 109 ARG 110 -0.0001

ARG 110 GLU 111 -0.0116

GLU 111 GLN 112 0.0002

GLN 112 LYS 113 0.0167

LYS 113 PHE 114 -0.0000

PHE 114 LYS 115 -0.0415

LYS 115 VAL 116 0.0000

VAL 116 THR 117 -0.1481

THR 117 PHE 118 -0.0003

PHE 118 GLY 119 0.0062

GLY 119 VAL 120 -0.0001

VAL 120 GLN 121 -0.0855

GLN 121 SER 122 0.0000

SER 122 PRO 123 -0.0477

PRO 123 ARG 124 0.0000

ARG 124 ARG 125 -0.0119

ARG 125 GLU 126 0.0000

GLU 126 GLY 127 0.0736

GLY 127 PRO 128 0.0001

PRO 128 ARG 129 0.1147

ARG 129 ALA 130 0.0001

ALA 130 LEU 131 -0.1392

LEU 131 SER 132 -0.0002

SER 132 PHE 133 -0.1843

PHE 133 VAL 134 0.0001

VAL 134 LEU 135 0.0026

LEU 135 SER 136 0.0001

SER 136 SER 137 -0.0605

SER 137 PRO 138 -0.0000

PRO 138 GLN 139 0.0091

GLN 139 LEU 140 0.0002

LEU 140 GLN 141 0.0486

GLN 141 GLN 142 -0.0002

GLN 142 GLU 143 -0.0216

GLU 143 VAL 144 0.0003

VAL 144 GLU 145 -0.0790

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 -0.1101

ASP 147 VAL 148 0.0002

VAL 148 LEU 149 -0.0494

LEU 149 PRO 150 -0.0001

PRO 150 ALA 151 0.0083

ALA 151 PHE 152 0.0001

PHE 152 ASP 153 -0.0319

ASP 153 ALA 154 0.0002

ALA 154 LEU 155 -0.0596

LEU 155 GLY 156 -0.0001

GLY 156 GLN 157 -0.0438

GLN 157 TRP 158 0.0002

TRP 158 THR 159 -0.0225

THR 159 PRO 160 -0.0005

PRO 160 GLY 161 0.0077

GLY 161 TYR 162 0.0002

TYR 162 LYS 163 -0.0181

LYS 163 PRO 164 0.0001

PRO 164 ASN 165 0.0439

ASN 165 PRO 166 0.0001

PRO 166 GLU 167 0.0057

GLU 167 ILE 168 -0.0001

ILE 168 TYR 169 0.0109

TYR 169 VAL 170 -0.0002

VAL 170 GLN 171 0.0077

GLN 171 LEU 172 -0.0004

LEU 172 ILE 173 0.0317

ILE 173 LYS 174 -0.0001

LYS 174 GLU 175 0.0011

GLU 175 CYS 176 0.0001

CYS 176 LYS 177 -0.0219

LYS 177 SER 178 -0.0002

SER 178 ARG 179 -0.0045

ARG 179 GLY 180 0.0002

GLY 180 ALA 181 -0.0676

ALA 181 GLU 182 0.0001

GLU 182 GLY 183 -0.0135

GLY 183 GLU 184 0.0001

GLU 184 PHE 185 -0.0641

PHE 185 SER 186 0.0002

SER 186 THR 187 0.0628

THR 187 CYS 188 0.0001

CYS 188 PHE 189 -0.0173

PHE 189 THR 190 0.0000

THR 190 GLU 191 0.0292

GLU 191 LEU 192 0.0003

LEU 192 GLN 193 -0.0487

GLN 193 ARG 194 -0.0003

ARG 194 ARG 194 -0.1147

ARG 194 ASP 195 0.0354

ASP 195 PHE 196 0.0004

PHE 196 LEU 197 0.0548

LEU 197 ARG 198 -0.0001

ARG 198 ASN 199 0.0064

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 0.0261

PRO 201 THR 202 -0.0001

THR 202 LYS 203 0.0086

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 0.0089

LYS 205 SER 206 0.0000

SER 206 LEU 207 0.0022

LEU 207 ILE 208 -0.0000

ILE 208 ARG 209 0.0245

ARG 209 LEU 210 0.0002

LEU 210 VAL 211 0.0264

VAL 211 LYS 212 -0.0003

LYS 212 HIS 213 -0.0107

HIS 213 TRP 214 0.0001

TRP 214 TYR 215 0.0110

TYR 215 GLN 216 0.0001

GLN 216 THR 217 -0.0610

THR 217 CYS 218 0.0000

CYS 218 GLU 219 0.0189

GLU 219 LYS 220 0.0002

LYS 220 THR 221 -0.0108

THR 221 HIS 222 0.0005

HIS 222 GLY 223 0.0211

GLY 223 GLY 224 -0.0000

GLY 224 LYS 225 0.0109

LYS 225 LEU 226 -0.0000

LEU 226 PRO 227 -0.0870

PRO 227 PRO 228 -0.0004

PRO 228 GLN 229 0.0311

GLN 229 TYR 230 0.0002

TYR 230 ALA 231 0.0032

ALA 231 LEU 232 0.0001

LEU 232 GLU 233 -0.0310

GLU 233 LEU 234 0.0003

LEU 234 LEU 235 -0.0044

LEU 235 THR 236 0.0002

THR 236 VAL 237 0.0275

VAL 237 TYR 238 0.0002

TYR 238 ALA 239 0.0640

ALA 239 TRP 240 -0.0004

TRP 240 GLU 241 0.0298

GLU 241 GLN 242 -0.0002

GLN 242 GLY 243 0.0456

GLY 243 SER 244 -0.0001

SER 244 ARG 245 0.0101

ARG 245 LYS 246 0.0002

LYS 246 THR 247 -0.0047

THR 247 ASP 248 -0.0002

ASP 248 PHE 249 0.0280

PHE 249 SER 250 0.0004

SER 250 THR 251 -0.0255

THR 251 ALA 252 0.0004

ALA 252 GLN 253 0.0016

GLN 253 GLY 254 0.0001

GLY 254 PHE 255 0.0205

PHE 255 GLN 256 -0.0001

GLN 256 THR 257 0.0360

THR 257 VAL 258 -0.0002

VAL 258 LEU 259 0.0087

LEU 259 GLU 260 -0.0004

GLU 260 LEU 261 0.0332

LEU 261 VAL 262 0.0004

VAL 262 LEU 263 -0.0193

LEU 263 LYS 264 -0.0000

LYS 264 HIS 265 0.0036

HIS 265 GLN 266 -0.0002

GLN 266 LYS 267 0.0107

LYS 267 LEU 268 0.0000

LEU 268 CYS 269 0.0803

CYS 269 ILE 270 -0.0003

ILE 270 PHE 271 0.0350

PHE 271 TRP 272 0.0001

TRP 272 GLU 273 0.0397

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 0.0155

TYR 275 TYR 276 -0.0003

TYR 276 ASP 277 0.0139

ASP 277 PHE 278 -0.0004

PHE 278 THR 279 0.0010

THR 279 ASN 280 0.0001

ASN 280 PRO 281 0.0008

PRO 281 VAL 282 -0.0003

VAL 282 VAL 283 0.0207

VAL 283 GLY 284 0.0004

GLY 284 ARG 285 0.0079

ARG 285 CYS 286 0.0003

CYS 286 MET 287 0.0483

MET 287 LEU 288 0.0001

LEU 288 GLN 289 -0.0022

GLN 289 GLN 290 -0.0002

GLN 290 LEU 291 0.0628

LEU 291 LYS 292 -0.0002

LYS 292 LYS 293 -0.0347

LYS 293 PRO 294 0.0001

PRO 294 ARG 295 -0.0104

ARG 295 PRO 296 -0.0004

PRO 296 VAL 297 -0.0232

VAL 297 ILE 298 0.0000

ILE 298 LEU 299 -0.0061

LEU 299 ASP 300 0.0002

ASP 300 PRO 301 -0.0287

PRO 301 ALA 302 0.0002

ALA 302 ASP 303 0.0231

ASP 303 PRO 304 -0.0003

PRO 304 THR 305 0.0118

THR 305 GLY 306 -0.0001

GLY 306 ASN 307 -0.0575

ASN 307 VAL 308 0.0001

VAL 308 GLY 309 -0.0374

GLY 309 GLY 310 -0.0001

GLY 310 GLY 311 0.0295

GLY 311 ASP 312 -0.0001

ASP 312 THR 313 0.0084

THR 313 HIS 314 -0.0002

HIS 314 SER 315 0.0065

SER 315 TRP 316 -0.0002

TRP 316 GLN 317 -0.0059

GLN 317 ARG 318 0.0001

ARG 318 LEU 319 -0.0012

LEU 319 ALA 320 -0.0000

ALA 320 GLN 321 0.0151

GLN 321 GLU 322 -0.0002

GLU 322 ALA 323 0.0262

ALA 323 ARG 324 0.0003

ARG 324 VAL 325 0.0058

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 -0.0165

LEU 327 GLY 328 -0.0002

GLY 328 TYR 329 -0.0036

TYR 329 PRO 330 0.0003

PRO 330 CYS 331 0.0033

CYS 331 CYS 332 0.0002

CYS 332 LYS 333 0.0076

LYS 333 ASN 334 -0.0002

ASN 334 LEU 335 0.0796

LEU 335 ASP 336 -0.0003

ASP 336 GLY 337 -0.0666

GLY 337 SER 338 -0.0001

SER 338 LEU 339 0.0256

LEU 339 VAL 340 -0.0001

VAL 340 GLY 341 0.0807

GLY 341 ALA 342 0.0002

ALA 342 TRP 343 0.0616

TRP 343 THR 344 0.0005

THR 344 MET 345 0.0469

MET 345 LEU 346 0.0004

LEU 346 GLN 347 0.0081

GLN 347 LYS 348 0.0002

LYS 348 ILE 349 0.0292

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 11 ---

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

* *