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

* PTEN_REPRES_TEST *

CA strain for 2402082043421969462

--- 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 THR 2 0.0003

THR 2 ALA 3 -0.0064

ALA 3 ILE 4 0.0000

ILE 4 ILE 5 -0.0186

ILE 5 LYS 6 0.0000

LYS 6 GLU 7 -0.0013

GLU 7 ILE 8 0.0003

ILE 8 VAL 9 0.0020

VAL 9 SER 10 -0.0002

SER 10 ARG 11 0.0247

ARG 11 ASN 12 0.0000

ASN 12 LYS 13 0.0147

LYS 13 ARG 14 0.0001

ARG 14 ARG 15 -0.0153

ARG 15 TYR 16 0.0000

TYR 16 GLN 17 0.0018

GLN 17 GLU 18 -0.0004

GLU 18 ASP 19 -0.0044

ASP 19 GLY 20 0.0001

GLY 20 PHE 21 -0.0017

PHE 21 ASP 22 0.0002

ASP 22 LEU 23 -0.0018

LEU 23 ASP 24 0.0002

ASP 24 LEU 25 0.0247

LEU 25 THR 26 -0.0001

THR 26 TYR 27 0.0180

TYR 27 ILE 28 -0.0001

ILE 28 TYR 29 0.0059

TYR 29 PRO 30 0.0002

PRO 30 ASN 31 -0.0044

ASN 31 ILE 32 -0.0000

ILE 32 ILE 33 0.0213

ILE 33 ALA 34 0.0000

ALA 34 MET 35 0.0196

MET 35 GLY 36 0.0002

GLY 36 PHE 37 0.0199

PHE 37 PRO 38 -0.0001

PRO 38 ALA 39 0.0050

ALA 39 GLU 40 -0.0001

GLU 40 ARG 41 -0.0062

ARG 41 LEU 42 -0.0002

LEU 42 GLU 43 0.0096

GLU 43 GLY 44 -0.0000

GLY 44 VAL 45 -0.0200

VAL 45 TYR 46 -0.0003

TYR 46 ARG 47 -0.0357

ARG 47 ASN 48 -0.0000

ASN 48 ASN 49 0.0097

ASN 49 ILE 50 0.0000

ILE 50 ASP 51 -0.0036

ASP 51 ASP 52 -0.0000

ASP 52 VAL 53 -0.0014

VAL 53 VAL 54 -0.0002

VAL 54 ARG 55 -0.0060

ARG 55 PHE 56 0.0004

PHE 56 LEU 57 0.0051

LEU 57 ASP 58 0.0001

ASP 58 SER 59 -0.0029

SER 59 LYS 60 -0.0003

LYS 60 HIS 61 0.0238

HIS 61 LYS 62 -0.0002

LYS 62 ASN 63 0.0049

ASN 63 HIS 64 -0.0002

HIS 64 TYR 65 0.0025

TYR 65 LYS 66 -0.0000

LYS 66 ILE 67 -0.0018

ILE 67 TYR 68 0.0001

TYR 68 ASN 69 -0.0010

ASN 69 LEU 70 0.0002

LEU 70 CYS 71 -0.0079

CYS 71 ALA 72 -0.0002

ALA 72 GLU 73 -0.0525

GLU 73 ARG 74 -0.0004

ARG 74 HIS 75 0.0035

HIS 75 TYR 76 0.0000

TYR 76 ASP 77 0.0078

ASP 77 THR 78 -0.0003

THR 78 ALA 79 0.0004

ALA 79 LYS 80 0.0005

LYS 80 PHE 81 -0.0037

PHE 81 ASN 82 -0.0001

ASN 82 CYS 83 -0.0035

CYS 83 ARG 84 0.0003

ARG 84 VAL 85 0.0086

VAL 85 ALA 86 -0.0002

ALA 86 GLN 87 0.0164

GLN 87 TYR 88 -0.0001

TYR 88 PRO 89 0.0187

PRO 89 PHE 90 -0.0000

PHE 90 GLU 91 0.0277

GLU 91 ASP 92 0.0001

ASP 92 HIS 93 0.0085

HIS 93 ASN 94 -0.0000

ASN 94 PRO 95 0.0032

PRO 95 PRO 96 0.0000

PRO 96 GLN 97 -0.0219

GLN 97 LEU 98 0.0000

LEU 98 GLU 99 -0.0008

GLU 99 LEU 100 0.0001

LEU 100 ILE 101 0.0103

ILE 101 LYS 102 0.0002

LYS 102 PRO 103 -0.0231

PRO 103 PHE 104 0.0000

PHE 104 CYS 105 -0.0020

CYS 105 GLU 106 -0.0003

GLU 106 ASP 107 -0.0135

ASP 107 LEU 108 0.0001

LEU 108 ASP 109 -0.0085

ASP 109 GLN 110 0.0006

GLN 110 TRP 111 0.0106

TRP 111 LEU 112 -0.0001

LEU 112 SER 113 0.0017

SER 113 GLU 114 -0.0004

GLU 114 ASP 115 0.0010

ASP 115 ASP 116 0.0001

ASP 116 ASN 117 0.0020

ASN 117 HIS 118 -0.0003

HIS 118 VAL 119 -0.0026

VAL 119 ALA 120 -0.0003

ALA 120 ALA 121 0.0022

ALA 121 ILE 122 0.0001

ILE 122 HIS 123 -0.0021

HIS 123 CYS 124 0.0003

CYS 124 LYS 125 -0.0109

LYS 125 ALA 126 0.0000

ALA 126 GLY 127 0.0147

GLY 127 LYS 128 -0.0000

LYS 128 GLY 129 -0.0771

GLY 129 ARG 130 0.0001

ARG 130 THR 131 -0.0252

THR 131 GLY 132 0.0002

GLY 132 VAL 133 -0.0154

VAL 133 MET 134 0.0001

MET 134 ILE 135 -0.0184

ILE 135 CYS 136 0.0001

CYS 136 ALA 137 0.0212

ALA 137 TYR 138 -0.0002

TYR 138 LEU 139 -0.0162

LEU 139 LEU 140 0.0002

LEU 140 HIS 141 -0.0187

HIS 141 ARG 142 0.0004

ARG 142 GLY 143 -0.0262

GLY 143 LYS 144 0.0002

LYS 144 PHE 145 -0.0048

PHE 145 LEU 146 0.0001

LEU 146 LYS 147 -0.0228

LYS 147 ALA 148 -0.0001

ALA 148 GLN 149 0.0137

GLN 149 GLU 150 -0.0003

GLU 150 ALA 151 -0.0018

ALA 151 LEU 152 0.0001

LEU 152 ASP 153 0.0156

ASP 153 PHE 154 0.0001

PHE 154 TYR 155 0.0125

TYR 155 GLY 156 -0.0003

GLY 156 GLU 157 -0.0119

GLU 157 VAL 158 -0.0000

VAL 158 ARG 159 0.0195

ARG 159 THR 160 0.0001

THR 160 ARG 161 -0.0002

ARG 161 ASP 162 -0.0004

ASP 162 LYS 163 -0.0002

LYS 163 LYS 164 -0.0004

LYS 164 GLY 165 0.0247

GLY 165 VAL 166 0.0001

VAL 166 THR 167 -0.0544

THR 167 ILE 168 -0.0003

ILE 168 PRO 169 0.0180

PRO 169 SER 170 -0.0001

SER 170 GLN 171 -0.0340

GLN 171 ARG 172 0.0002

ARG 172 ARG 173 0.0141

ARG 173 TYR 174 -0.0005

TYR 174 VAL 175 -0.0113

VAL 175 TYR 176 0.0000

TYR 176 TYR 177 0.0064

TYR 177 TYR 178 0.0003

TYR 178 SER 179 -0.0006

SER 179 TYR 180 0.0001

TYR 180 LEU 181 -0.0168

LEU 181 LEU 182 -0.0001

LEU 182 LYS 183 -0.0099

LYS 183 ASN 184 -0.0001

ASN 184 HIS 185 0.0018

HIS 185 LEU 186 0.0000

LEU 186 ASP 187 -0.0075

ASP 187 TYR 188 0.0002

TYR 188 ARG 189 0.0164

ARG 189 PRO 190 -0.0000

PRO 190 VAL 191 -0.0474

VAL 191 ALA 192 -0.0003

ALA 192 LEU 193 -0.0024

LEU 193 LEU 194 0.0002

LEU 194 PHE 195 -0.0013

PHE 195 HIS 196 0.0001

HIS 196 LYS 197 0.0070

LYS 197 MET 198 0.0002

MET 198 MET 199 0.0027

MET 199 PHE 200 -0.0003

PHE 200 GLU 201 0.0087

GLU 201 THR 202 0.0002

THR 202 ILE 203 -0.0033

ILE 203 PRO 204 0.0001

PRO 204 MET 205 -0.0034

MET 205 PHE 206 0.0003

PHE 206 SER 207 -0.0046

SER 207 GLY 208 -0.0001

GLY 208 GLY 209 -0.0123

GLY 209 THR 210 -0.0002

THR 210 CYS 211 0.0100

CYS 211 ASN 212 -0.0000

ASN 212 PRO 213 0.0161

PRO 213 GLN 214 0.0000

GLN 214 PHE 215 0.0268

PHE 215 VAL 216 0.0000

VAL 216 VAL 217 0.0458

VAL 217 CYS 218 0.0002

CYS 218 GLN 219 0.0404

GLN 219 LEU 220 -0.0000

LEU 220 LYS 221 0.0047

LYS 221 VAL 222 0.0001

VAL 222 LYS 223 0.0072

LYS 223 ILE 224 -0.0000

ILE 224 TYR 225 0.0163

TYR 225 SER 226 -0.0001

SER 226 SER 227 0.0095

SER 227 ASN 228 -0.0000

ASN 228 SER 229 0.0285

SER 229 GLY 230 0.0002

GLY 230 PRO 231 0.0197

PRO 231 THR 232 0.0001

THR 232 ARG 233 0.0049

ARG 233 ARG 234 0.0000

ARG 234 GLU 235 0.0031

GLU 235 ASP 236 -0.0002

ASP 236 LYS 237 0.0039

LYS 237 PHE 238 0.0003

PHE 238 MET 239 0.0063

MET 239 TYR 240 -0.0002

TYR 240 PHE 241 0.0004

PHE 241 GLU 242 -0.0000

GLU 242 PHE 243 0.0018

PHE 243 PRO 244 -0.0001

PRO 244 GLN 245 0.0125

GLN 245 PRO 246 -0.0003

PRO 246 LEU 247 -0.0123

LEU 247 PRO 248 0.0003

PRO 248 VAL 249 -0.0198

VAL 249 CYS 250 0.0001

CYS 250 GLY 251 -0.0424

GLY 251 ASP 252 -0.0001

ASP 252 ILE 253 0.0388

ILE 253 LYS 254 -0.0000

LYS 254 VAL 255 0.0253

VAL 255 GLU 256 0.0002

GLU 256 PHE 257 0.0158

PHE 257 PHE 258 -0.0000

PHE 258 HIS 259 0.0088

HIS 259 LYS 260 0.0001

LYS 260 GLN 261 0.0316

GLN 261 ASN 262 -0.0001

ASN 262 LYS 263 0.0056

LYS 263 MET 264 -0.0001

MET 264 LEU 265 0.0074

LEU 265 LYS 266 -0.0001

LYS 266 LYS 267 -0.0354

LYS 267 ASP 268 -0.0001

ASP 268 LYS 269 -0.0708

LYS 269 MET 270 0.0003

MET 270 PHE 271 -0.0287

PHE 271 HIS 272 0.0001

HIS 272 PHE 273 0.0042

PHE 273 TRP 274 0.0001

TRP 274 VAL 275 -0.0040

VAL 275 ASN 276 -0.0000

ASN 276 THR 277 -0.0332

THR 277 PHE 278 0.0002

PHE 278 PHE 279 -0.0211

PHE 279 ILE 280 -0.0003

ILE 280 PRO 281 0.0285

PRO 281 GLY 282 0.0001

GLY 282 PRO 283 0.0798

PRO 283 GLU 284 -0.0000

GLU 284 GLU 285 -0.0846

GLU 285 THR 286 -0.0001

THR 286 SER 287 -0.0846

SER 287 GLU 288 -0.0002

GLU 288 LYS 289 0.0123

LYS 289 VAL 290 -0.0001

VAL 290 GLU 291 0.0319

GLU 291 ASN 292 -0.0001

ASN 292 GLY 293 0.0621

GLY 293 SER 294 0.0000

SER 294 LEU 295 0.0109

LEU 295 CYS 296 0.0003

CYS 296 ASP 297 -0.0403

ASP 297 GLN 298 0.0001

GLN 298 GLU 299 -0.0151

GLU 299 ILE 300 -0.0001

ILE 300 ASP 301 0.0259

ASP 301 SER 302 -0.0001

SER 302 ILE 303 0.0071

ILE 303 CYS 304 -0.0002

CYS 304 SER 305 0.0054

SER 305 ILE 306 0.0003

ILE 306 GLU 307 0.0053

GLU 307 ARG 308 0.0004

ARG 308 ALA 309 0.0028

ALA 309 ASP 310 0.0000

ASP 310 ASN 311 -0.0008

ASN 311 ASP 312 0.0003

ASP 312 LYS 313 0.0082

LYS 313 GLU 314 -0.0002

GLU 314 TYR 315 -0.0061

TYR 315 LEU 316 -0.0004

LEU 316 VAL 317 -0.0073

VAL 317 LEU 318 -0.0001

LEU 318 THR 319 -0.0147

THR 319 LEU 320 -0.0000

LEU 320 THR 321 -0.0196

THR 321 LYS 322 -0.0002

LYS 322 ASN 323 -0.0053

ASN 323 ASP 324 0.0001

ASP 324 LEU 325 -0.0182

LEU 325 ASP 326 -0.0001

ASP 326 LYS 327 -0.0100

LYS 327 ALA 328 -0.0000

ALA 328 ASN 329 0.0011

ASN 329 LYS 330 0.0002

LYS 330 ASP 331 -0.0210

ASP 331 LYS 332 0.0000

LYS 332 ALA 333 -0.0023

ALA 333 ASN 334 -0.0002

ASN 334 ARG 335 -0.0013

ARG 335 TYR 336 -0.0002

TYR 336 PHE 337 -0.0077

PHE 337 SER 338 -0.0001

SER 338 PRO 339 0.0038

PRO 339 ASN 340 0.0002

ASN 340 PHE 341 -0.0105

PHE 341 LYS 342 -0.0005

LYS 342 VAL 343 0.0050

VAL 343 LYS 344 -0.0001

LYS 344 LEU 345 -0.0004

LEU 345 TYR 346 -0.0001

TYR 346 PHE 347 -0.0090

PHE 347 THR 348 -0.0001

THR 348 LYS 349 -0.0063

LYS 349 THR 350 -0.0000

THR 350 VAL 351 -0.0082

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 10 ---

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

* PTEN_REPRES_TEST *