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

* PTEN_REPRES_TEST *

CA strain for 2402082043421969462

--- 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 THR 2 0.0000

THR 2 ALA 3 0.0181

ALA 3 ILE 4 0.0001

ILE 4 ILE 5 -0.0074

ILE 5 LYS 6 -0.0002

LYS 6 GLU 7 0.0013

GLU 7 ILE 8 0.0002

ILE 8 VAL 9 -0.0100

VAL 9 SER 10 -0.0000

SER 10 ARG 11 -0.0209

ARG 11 ASN 12 -0.0003

ASN 12 LYS 13 -0.0287

LYS 13 ARG 14 -0.0000

ARG 14 ARG 15 0.0694

ARG 15 TYR 16 -0.0001

TYR 16 GLN 17 0.0066

GLN 17 GLU 18 -0.0001

GLU 18 ASP 19 0.0105

ASP 19 GLY 20 -0.0001

GLY 20 PHE 21 -0.0097

PHE 21 ASP 22 0.0001

ASP 22 LEU 23 -0.0083

LEU 23 ASP 24 0.0003

ASP 24 LEU 25 -0.0188

LEU 25 THR 26 -0.0001

THR 26 TYR 27 -0.0127

TYR 27 ILE 28 0.0001

ILE 28 TYR 29 -0.0217

TYR 29 PRO 30 0.0002

PRO 30 ASN 31 0.0071

ASN 31 ILE 32 -0.0002

ILE 32 ILE 33 -0.0078

ILE 33 ALA 34 -0.0002

ALA 34 MET 35 0.0096

MET 35 GLY 36 -0.0000

GLY 36 PHE 37 -0.0020

PHE 37 PRO 38 0.0000

PRO 38 ALA 39 0.0091

ALA 39 GLU 40 -0.0001

GLU 40 ARG 41 0.0064

ARG 41 LEU 42 0.0001

LEU 42 GLU 43 -0.0067

GLU 43 GLY 44 0.0002

GLY 44 VAL 45 0.0176

VAL 45 TYR 46 -0.0000

TYR 46 ARG 47 0.0099

ARG 47 ASN 48 -0.0003

ASN 48 ASN 49 0.0001

ASN 49 ILE 50 0.0003

ILE 50 ASP 51 -0.0091

ASP 51 ASP 52 0.0004

ASP 52 VAL 53 -0.0067

VAL 53 VAL 54 0.0001

VAL 54 ARG 55 -0.0068

ARG 55 PHE 56 0.0000

PHE 56 LEU 57 -0.0213

LEU 57 ASP 58 0.0001

ASP 58 SER 59 -0.0056

SER 59 LYS 60 0.0002

LYS 60 HIS 61 -0.0391

HIS 61 LYS 62 0.0000

LYS 62 ASN 63 -0.0109

ASN 63 HIS 64 -0.0001

HIS 64 TYR 65 -0.0136

TYR 65 LYS 66 -0.0002

LYS 66 ILE 67 -0.0007

ILE 67 TYR 68 0.0000

TYR 68 ASN 69 0.0183

ASN 69 LEU 70 0.0001

LEU 70 CYS 71 0.0210

CYS 71 ALA 72 0.0001

ALA 72 GLU 73 0.0373

GLU 73 ARG 74 -0.0003

ARG 74 HIS 75 -0.0025

HIS 75 TYR 76 0.0003

TYR 76 ASP 77 -0.0172

ASP 77 THR 78 -0.0002

THR 78 ALA 79 0.0019

ALA 79 LYS 80 0.0003

LYS 80 PHE 81 0.0043

PHE 81 ASN 82 -0.0002

ASN 82 CYS 83 0.0002

CYS 83 ARG 84 -0.0002

ARG 84 VAL 85 -0.0215

VAL 85 ALA 86 -0.0003

ALA 86 GLN 87 -0.0499

GLN 87 TYR 88 -0.0002

TYR 88 PRO 89 0.0271

PRO 89 PHE 90 0.0001

PHE 90 GLU 91 0.0369

GLU 91 ASP 92 0.0000

ASP 92 HIS 93 -0.0077

HIS 93 ASN 94 0.0001

ASN 94 PRO 95 0.0486

PRO 95 PRO 96 -0.0003

PRO 96 GLN 97 0.0076

GLN 97 LEU 98 0.0001

LEU 98 GLU 99 0.0319

GLU 99 LEU 100 -0.0000

LEU 100 ILE 101 0.0287

ILE 101 LYS 102 0.0002

LYS 102 PRO 103 0.0051

PRO 103 PHE 104 -0.0003

PHE 104 CYS 105 0.0067

CYS 105 GLU 106 0.0004

GLU 106 ASP 107 -0.0096

ASP 107 LEU 108 -0.0001

LEU 108 ASP 109 0.0190

ASP 109 GLN 110 0.0003

GLN 110 TRP 111 -0.0286

TRP 111 LEU 112 0.0003

LEU 112 SER 113 -0.0032

SER 113 GLU 114 -0.0003

GLU 114 ASP 115 0.0067

ASP 115 ASP 116 -0.0002

ASP 116 ASN 117 -0.0032

ASN 117 HIS 118 -0.0001

HIS 118 VAL 119 -0.0064

VAL 119 ALA 120 -0.0002

ALA 120 ALA 121 -0.0025

ALA 121 ILE 122 0.0002

ILE 122 HIS 123 0.0124

HIS 123 CYS 124 0.0005

CYS 124 LYS 125 0.0209

LYS 125 ALA 126 -0.0001

ALA 126 GLY 127 -0.0075

GLY 127 LYS 128 -0.0001

LYS 128 GLY 129 0.0434

GLY 129 ARG 130 -0.0000

ARG 130 THR 131 -0.0166

THR 131 GLY 132 0.0001

GLY 132 VAL 133 0.0078

VAL 133 MET 134 0.0003

MET 134 ILE 135 -0.0434

ILE 135 CYS 136 -0.0000

CYS 136 ALA 137 -0.0097

ALA 137 TYR 138 0.0000

TYR 138 LEU 139 -0.0039

LEU 139 LEU 140 0.0000

LEU 140 HIS 141 0.0127

HIS 141 ARG 142 0.0004

ARG 142 GLY 143 0.0368

GLY 143 LYS 144 0.0002

LYS 144 PHE 145 0.0482

PHE 145 LEU 146 -0.0002

LEU 146 LYS 147 0.0218

LYS 147 ALA 148 -0.0000

ALA 148 GLN 149 -0.0173

GLN 149 GLU 150 0.0002

GLU 150 ALA 151 0.0234

ALA 151 LEU 152 0.0002

LEU 152 ASP 153 -0.0048

ASP 153 PHE 154 0.0000

PHE 154 TYR 155 -0.0082

TYR 155 GLY 156 0.0002

GLY 156 GLU 157 -0.0142

GLU 157 VAL 158 -0.0000

VAL 158 ARG 159 -0.0131

ARG 159 THR 160 0.0002

THR 160 ARG 161 -0.0253

ARG 161 ASP 162 0.0002

ASP 162 LYS 163 0.0402

LYS 163 LYS 164 -0.0002

LYS 164 GLY 165 -0.0091

GLY 165 VAL 166 0.0004

VAL 166 THR 167 0.0331

THR 167 ILE 168 -0.0002

ILE 168 PRO 169 0.1067

PRO 169 SER 170 0.0001

SER 170 GLN 171 -0.0042

GLN 171 ARG 172 -0.0002

ARG 172 ARG 173 0.0921

ARG 173 TYR 174 0.0003

TYR 174 VAL 175 -0.0405

VAL 175 TYR 176 0.0001

TYR 176 TYR 177 0.0310

TYR 177 TYR 178 0.0002

TYR 178 SER 179 0.0106

SER 179 TYR 180 0.0002

TYR 180 LEU 181 -0.0167

LEU 181 LEU 182 -0.0003

LEU 182 LYS 183 0.0025

LYS 183 ASN 184 -0.0000

ASN 184 HIS 185 -0.0088

HIS 185 LEU 186 -0.0000

LEU 186 ASP 187 -0.0287

ASP 187 TYR 188 0.0000

TYR 188 ARG 189 -0.0279

ARG 189 PRO 190 -0.0000

PRO 190 VAL 191 -0.0936

VAL 191 ALA 192 -0.0000

ALA 192 LEU 193 -0.0360

LEU 193 LEU 194 -0.0001

LEU 194 PHE 195 -0.0081

PHE 195 HIS 196 -0.0001

HIS 196 LYS 197 -0.0195

LYS 197 MET 198 0.0003

MET 198 MET 199 -0.0269

MET 199 PHE 200 0.0002

PHE 200 GLU 201 -0.0122

GLU 201 THR 202 0.0001

THR 202 ILE 203 0.0061

ILE 203 PRO 204 -0.0000

PRO 204 MET 205 -0.0079

MET 205 PHE 206 -0.0004

PHE 206 SER 207 0.0026

SER 207 GLY 208 -0.0001

GLY 208 GLY 209 -0.0005

GLY 209 THR 210 -0.0000

THR 210 CYS 211 -0.0081

CYS 211 ASN 212 0.0001

ASN 212 PRO 213 -0.0120

PRO 213 GLN 214 0.0002

GLN 214 PHE 215 -0.0189

PHE 215 VAL 216 0.0000

VAL 216 VAL 217 -0.0072

VAL 217 CYS 218 0.0000

CYS 218 GLN 219 -0.0243

GLN 219 LEU 220 -0.0000

LEU 220 LYS 221 -0.0134

LYS 221 VAL 222 -0.0002

VAL 222 LYS 223 -0.0262

LYS 223 ILE 224 0.0002

ILE 224 TYR 225 -0.0315

TYR 225 SER 226 0.0001

SER 226 SER 227 -0.0337

SER 227 ASN 228 0.0004

ASN 228 SER 229 0.0021

SER 229 GLY 230 0.0001

GLY 230 PRO 231 0.0350

PRO 231 THR 232 0.0002

THR 232 ARG 233 -0.0097

ARG 233 ARG 234 0.0003

ARG 234 GLU 235 -0.0098

GLU 235 ASP 236 0.0000

ASP 236 LYS 237 0.0106

LYS 237 PHE 238 0.0002

PHE 238 MET 239 -0.0068

MET 239 TYR 240 -0.0001

TYR 240 PHE 241 -0.0257

PHE 241 GLU 242 -0.0000

GLU 242 PHE 243 -0.0215

PHE 243 PRO 244 0.0002

PRO 244 GLN 245 -0.0119

GLN 245 PRO 246 0.0001

PRO 246 LEU 247 -0.0161

LEU 247 PRO 248 -0.0001

PRO 248 VAL 249 -0.0352

VAL 249 CYS 250 0.0000

CYS 250 GLY 251 -0.0761

GLY 251 ASP 252 -0.0003

ASP 252 ILE 253 -0.0799

ILE 253 LYS 254 0.0005

LYS 254 VAL 255 -0.0324

VAL 255 GLU 256 0.0000

GLU 256 PHE 257 -0.0227

PHE 257 PHE 258 -0.0001

PHE 258 HIS 259 -0.0194

HIS 259 LYS 260 0.0001

LYS 260 GLN 261 0.0020

GLN 261 ASN 262 0.0002

ASN 262 LYS 263 0.0310

LYS 263 MET 264 -0.0001

MET 264 LEU 265 -0.0097

LEU 265 LYS 266 0.0001

LYS 266 LYS 267 -0.0324

LYS 267 ASP 268 0.0001

ASP 268 LYS 269 -0.0749

LYS 269 MET 270 -0.0001

MET 270 PHE 271 -0.0506

PHE 271 HIS 272 0.0001

HIS 272 PHE 273 -0.0295

PHE 273 TRP 274 0.0000

TRP 274 VAL 275 -0.0090

VAL 275 ASN 276 0.0000

ASN 276 THR 277 -0.0294

THR 277 PHE 278 0.0000

PHE 278 PHE 279 -0.0030

PHE 279 ILE 280 -0.0001

ILE 280 PRO 281 -0.0228

PRO 281 GLY 282 -0.0001

GLY 282 PRO 283 -0.0111

PRO 283 GLU 284 -0.0000

GLU 284 GLU 285 0.0204

GLU 285 THR 286 0.0002

THR 286 SER 287 0.0186

SER 287 GLU 288 -0.0004

GLU 288 LYS 289 -0.0018

LYS 289 VAL 290 0.0001

VAL 290 GLU 291 -0.0052

GLU 291 ASN 292 -0.0001

ASN 292 GLY 293 -0.0298

GLY 293 SER 294 -0.0001

SER 294 LEU 295 -0.0072

LEU 295 CYS 296 -0.0002

CYS 296 ASP 297 0.0133

ASP 297 GLN 298 0.0002

GLN 298 GLU 299 -0.0374

GLU 299 ILE 300 0.0000

ILE 300 ASP 301 0.0156

ASP 301 SER 302 0.0000

SER 302 ILE 303 0.0278

ILE 303 CYS 304 0.0002

CYS 304 SER 305 -0.0177

SER 305 ILE 306 0.0001

ILE 306 GLU 307 0.0463

GLU 307 ARG 308 0.0003

ARG 308 ALA 309 0.0089

ALA 309 ASP 310 0.0002

ASP 310 ASN 311 0.0248

ASN 311 ASP 312 -0.0004

ASP 312 LYS 313 0.0140

LYS 313 GLU 314 -0.0002

GLU 314 TYR 315 -0.0085

TYR 315 LEU 316 0.0002

LEU 316 VAL 317 -0.0132

VAL 317 LEU 318 0.0002

LEU 318 THR 319 -0.0261

THR 319 LEU 320 -0.0001

LEU 320 THR 321 -0.0306

THR 321 LYS 322 0.0001

LYS 322 ASN 323 0.0226

ASN 323 ASP 324 0.0001

ASP 324 LEU 325 -0.0115

LEU 325 ASP 326 0.0001

ASP 326 LYS 327 -0.0074

LYS 327 ALA 328 -0.0001

ALA 328 ASN 329 0.0248

ASN 329 LYS 330 -0.0001

LYS 330 ASP 331 0.0431

ASP 331 LYS 332 -0.0000

LYS 332 ALA 333 0.0178

ALA 333 ASN 334 0.0002

ASN 334 ARG 335 0.0029

ARG 335 TYR 336 0.0000

TYR 336 PHE 337 -0.0114

PHE 337 SER 338 -0.0000

SER 338 PRO 339 0.0013

PRO 339 ASN 340 -0.0002

ASN 340 PHE 341 -0.0145

PHE 341 LYS 342 0.0001

LYS 342 VAL 343 -0.0155

VAL 343 LYS 344 0.0001

LYS 344 LEU 345 -0.0161

LEU 345 TYR 346 -0.0001

TYR 346 PHE 347 -0.0281

PHE 347 THR 348 -0.0002

THR 348 LYS 349 -0.0114

LYS 349 THR 350 0.0001

THR 350 VAL 351 -0.0004

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.

*** PTEN_REPRES_TEST ***

CA strain for 2402082043421969462

--- normal mode 11 ---

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

* PTEN_REPRES_TEST *