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

* PTEN_REPRES_TEST *

CA strain for 2402082043421969462

--- normal mode 9 ---

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 0.0001

THR 2 ALA 3 -0.0164

ALA 3 ILE 4 -0.0000

ILE 4 ILE 5 0.0197

ILE 5 LYS 6 0.0002

LYS 6 GLU 7 0.0002

GLU 7 ILE 8 -0.0001

ILE 8 VAL 9 0.0104

VAL 9 SER 10 0.0002

SER 10 ARG 11 0.0195

ARG 11 ASN 12 -0.0001

ASN 12 LYS 13 0.0200

LYS 13 ARG 14 0.0003

ARG 14 ARG 15 -0.0206

ARG 15 TYR 16 0.0001

TYR 16 GLN 17 -0.0012

GLN 17 GLU 18 -0.0000

GLU 18 ASP 19 -0.0027

ASP 19 GLY 20 0.0002

GLY 20 PHE 21 -0.0009

PHE 21 ASP 22 -0.0002

ASP 22 LEU 23 0.0031

LEU 23 ASP 24 -0.0003

ASP 24 LEU 25 0.0179

LEU 25 THR 26 0.0001

THR 26 TYR 27 0.0045

TYR 27 ILE 28 -0.0004

ILE 28 TYR 29 -0.0049

TYR 29 PRO 30 0.0002

PRO 30 ASN 31 -0.0066

ASN 31 ILE 32 -0.0000

ILE 32 ILE 33 0.0254

ILE 33 ALA 34 0.0001

ALA 34 MET 35 0.0101

MET 35 GLY 36 -0.0003

GLY 36 PHE 37 0.0134

PHE 37 PRO 38 -0.0001

PRO 38 ALA 39 0.0167

ALA 39 GLU 40 -0.0002

GLU 40 ARG 41 0.0195

ARG 41 LEU 42 -0.0001

LEU 42 GLU 43 0.0135

GLU 43 GLY 44 -0.0000

GLY 44 VAL 45 -0.0178

VAL 45 TYR 46 0.0003

TYR 46 ARG 47 -0.0163

ARG 47 ASN 48 -0.0001

ASN 48 ASN 49 0.0052

ASN 49 ILE 50 -0.0002

ILE 50 ASP 51 -0.0086

ASP 51 ASP 52 0.0001

ASP 52 VAL 53 0.0035

VAL 53 VAL 54 0.0002

VAL 54 ARG 55 -0.0075

ARG 55 PHE 56 0.0001

PHE 56 LEU 57 0.0149

LEU 57 ASP 58 0.0002

ASP 58 SER 59 -0.0024

SER 59 LYS 60 -0.0002

LYS 60 HIS 61 0.0215

HIS 61 LYS 62 0.0004

LYS 62 ASN 63 0.0038

ASN 63 HIS 64 -0.0001

HIS 64 TYR 65 -0.0134

TYR 65 LYS 66 -0.0001

LYS 66 ILE 67 -0.0205

ILE 67 TYR 68 0.0002

TYR 68 ASN 69 -0.0320

ASN 69 LEU 70 0.0001

LEU 70 CYS 71 0.0115

CYS 71 ALA 72 0.0001

ALA 72 GLU 73 0.0253

GLU 73 ARG 74 0.0001

ARG 74 HIS 75 -0.0255

HIS 75 TYR 76 -0.0001

TYR 76 ASP 77 -0.0209

ASP 77 THR 78 -0.0001

THR 78 ALA 79 0.0011

ALA 79 LYS 80 -0.0001

LYS 80 PHE 81 0.0128

PHE 81 ASN 82 -0.0004

ASN 82 CYS 83 0.0147

CYS 83 ARG 84 0.0001

ARG 84 VAL 85 -0.0157

VAL 85 ALA 86 0.0003

ALA 86 GLN 87 -0.0219

GLN 87 TYR 88 -0.0000

TYR 88 PRO 89 -0.0468

PRO 89 PHE 90 0.0004

PHE 90 GLU 91 -0.0295

GLU 91 ASP 92 0.0002

ASP 92 HIS 93 -0.1684

HIS 93 ASN 94 0.0001

ASN 94 PRO 95 0.0072

PRO 95 PRO 96 -0.0002

PRO 96 GLN 97 0.0111

GLN 97 LEU 98 -0.0002

LEU 98 GLU 99 0.0137

GLU 99 LEU 100 -0.0001

LEU 100 ILE 101 -0.0158

ILE 101 LYS 102 0.0002

LYS 102 PRO 103 0.0294

PRO 103 PHE 104 -0.0001

PHE 104 CYS 105 -0.0132

CYS 105 GLU 106 -0.0004

GLU 106 ASP 107 0.0510

ASP 107 LEU 108 -0.0002

LEU 108 ASP 109 -0.0104

ASP 109 GLN 110 -0.0001

GLN 110 TRP 111 0.0326

TRP 111 LEU 112 0.0000

LEU 112 SER 113 0.0027

SER 113 GLU 114 -0.0001

GLU 114 ASP 115 0.0100

ASP 115 ASP 116 0.0001

ASP 116 ASN 117 -0.0029

ASN 117 HIS 118 0.0004

HIS 118 VAL 119 -0.0090

VAL 119 ALA 120 -0.0001

ALA 120 ALA 121 -0.0002

ALA 121 ILE 122 -0.0001

ILE 122 HIS 123 -0.0023

HIS 123 CYS 124 -0.0002

CYS 124 LYS 125 -0.0017

LYS 125 ALA 126 -0.0001

ALA 126 GLY 127 0.0088

GLY 127 LYS 128 0.0002

LYS 128 GLY 129 -0.0729

GLY 129 ARG 130 -0.0002

ARG 130 THR 131 -0.0482

THR 131 GLY 132 0.0002

GLY 132 VAL 133 -0.0186

VAL 133 MET 134 0.0004

MET 134 ILE 135 -0.0161

ILE 135 CYS 136 -0.0002

CYS 136 ALA 137 0.0142

ALA 137 TYR 138 -0.0002

TYR 138 LEU 139 -0.0079

LEU 139 LEU 140 0.0001

LEU 140 HIS 141 0.0083

HIS 141 ARG 142 -0.0001

ARG 142 GLY 143 0.0091

GLY 143 LYS 144 -0.0002

LYS 144 PHE 145 0.0328

PHE 145 LEU 146 -0.0000

LEU 146 LYS 147 0.0245

LYS 147 ALA 148 0.0001

ALA 148 GLN 149 0.0006

GLN 149 GLU 150 -0.0001

GLU 150 ALA 151 -0.0045

ALA 151 LEU 152 -0.0001

LEU 152 ASP 153 -0.0018

ASP 153 PHE 154 0.0001

PHE 154 TYR 155 -0.0072

TYR 155 GLY 156 -0.0002

GLY 156 GLU 157 0.0145

GLU 157 VAL 158 -0.0003

VAL 158 ARG 159 0.0061

ARG 159 THR 160 0.0004

THR 160 ARG 161 0.0196

ARG 161 ASP 162 0.0003

ASP 162 LYS 163 -0.0433

LYS 163 LYS 164 -0.0001

LYS 164 GLY 165 0.0089

GLY 165 VAL 166 0.0003

VAL 166 THR 167 -0.0088

THR 167 ILE 168 0.0003

ILE 168 PRO 169 -0.0712

PRO 169 SER 170 0.0000

SER 170 GLN 171 -0.0453

GLN 171 ARG 172 0.0002

ARG 172 ARG 173 -0.0574

ARG 173 TYR 174 0.0000

TYR 174 VAL 175 -0.0083

VAL 175 TYR 176 0.0002

TYR 176 TYR 177 -0.0116

TYR 177 TYR 178 -0.0004

TYR 178 SER 179 0.0020

SER 179 TYR 180 0.0001

TYR 180 LEU 181 0.0161

LEU 181 LEU 182 0.0003

LEU 182 LYS 183 0.0519

LYS 183 ASN 184 0.0000

ASN 184 HIS 185 0.0105

HIS 185 LEU 186 -0.0003

LEU 186 ASP 187 -0.0008

ASP 187 TYR 188 -0.0002

TYR 188 ARG 189 0.0109

ARG 189 PRO 190 0.0000

PRO 190 VAL 191 0.0443

VAL 191 ALA 192 0.0002

ALA 192 LEU 193 0.0064

LEU 193 LEU 194 -0.0003

LEU 194 PHE 195 0.0038

PHE 195 HIS 196 -0.0004

HIS 196 LYS 197 0.0020

LYS 197 MET 198 -0.0003

MET 198 MET 199 -0.0102

MET 199 PHE 200 -0.0000

PHE 200 GLU 201 -0.0085

GLU 201 THR 202 -0.0001

THR 202 ILE 203 0.0221

ILE 203 PRO 204 0.0001

PRO 204 MET 205 0.0031

MET 205 PHE 206 0.0002

PHE 206 SER 207 -0.0002

SER 207 GLY 208 -0.0002

GLY 208 GLY 209 0.0125

GLY 209 THR 210 0.0003

THR 210 CYS 211 -0.0098

CYS 211 ASN 212 -0.0002

ASN 212 PRO 213 -0.0116

PRO 213 GLN 214 -0.0002

GLN 214 PHE 215 -0.0189

PHE 215 VAL 216 0.0004

VAL 216 VAL 217 -0.0213

VAL 217 CYS 218 -0.0002

CYS 218 GLN 219 -0.0325

GLN 219 LEU 220 -0.0006

LEU 220 LYS 221 -0.0118

LYS 221 VAL 222 0.0000

VAL 222 LYS 223 -0.0209

LYS 223 ILE 224 0.0002

ILE 224 TYR 225 -0.0184

TYR 225 SER 226 0.0001

SER 226 SER 227 -0.0241

SER 227 ASN 228 0.0002

ASN 228 SER 229 -0.0004

SER 229 GLY 230 -0.0004

GLY 230 PRO 231 0.0358

PRO 231 THR 232 -0.0002

THR 232 ARG 233 -0.0083

ARG 233 ARG 234 0.0001

ARG 234 GLU 235 -0.0045

GLU 235 ASP 236 0.0001

ASP 236 LYS 237 -0.0044

LYS 237 PHE 238 0.0002

PHE 238 MET 239 -0.0004

MET 239 TYR 240 0.0002

TYR 240 PHE 241 -0.0182

PHE 241 GLU 242 0.0002

GLU 242 PHE 243 -0.0191

PHE 243 PRO 244 -0.0002

PRO 244 GLN 245 -0.0071

GLN 245 PRO 246 -0.0000

PRO 246 LEU 247 -0.0056

LEU 247 PRO 248 -0.0002

PRO 248 VAL 249 -0.0050

VAL 249 CYS 250 -0.0003

CYS 250 GLY 251 0.0056

GLY 251 ASP 252 0.0001

ASP 252 ILE 253 -0.0370

ILE 253 LYS 254 0.0001

LYS 254 VAL 255 -0.0259

VAL 255 GLU 256 0.0001

GLU 256 PHE 257 -0.0262

PHE 257 PHE 258 0.0001

PHE 258 HIS 259 -0.0294

HIS 259 LYS 260 -0.0002

LYS 260 GLN 261 -0.0001

GLN 261 ASN 262 -0.0004

ASN 262 LYS 263 0.0283

LYS 263 MET 264 0.0002

MET 264 LEU 265 -0.0091

LEU 265 LYS 266 -0.0000

LYS 266 LYS 267 -0.0106

LYS 267 ASP 268 0.0002

ASP 268 LYS 269 -0.0660

LYS 269 MET 270 -0.0003

MET 270 PHE 271 -0.0578

PHE 271 HIS 272 0.0002

HIS 272 PHE 273 -0.0244

PHE 273 TRP 274 -0.0002

TRP 274 VAL 275 -0.0220

VAL 275 ASN 276 0.0000

ASN 276 THR 277 0.0042

THR 277 PHE 278 0.0004

PHE 278 PHE 279 0.0137

PHE 279 ILE 280 -0.0000

ILE 280 PRO 281 -0.0293

PRO 281 GLY 282 0.0000

GLY 282 PRO 283 -0.0149

PRO 283 GLU 284 0.0000

GLU 284 GLU 285 -0.0068

GLU 285 THR 286 -0.0002

THR 286 SER 287 0.0147

SER 287 GLU 288 -0.0001

GLU 288 LYS 289 -0.0009

LYS 289 VAL 290 -0.0001

VAL 290 GLU 291 -0.0124

GLU 291 ASN 292 -0.0003

ASN 292 GLY 293 -0.0219

GLY 293 SER 294 -0.0003

SER 294 LEU 295 0.0146

LEU 295 CYS 296 0.0002

CYS 296 ASP 297 0.0219

ASP 297 GLN 298 -0.0002

GLN 298 GLU 299 -0.0018

GLU 299 ILE 300 -0.0001

ILE 300 ASP 301 0.0052

ASP 301 SER 302 0.0000

SER 302 ILE 303 0.0064

ILE 303 CYS 304 0.0002

CYS 304 SER 305 -0.0410

SER 305 ILE 306 0.0002

ILE 306 GLU 307 0.0351

GLU 307 ARG 308 -0.0003

ARG 308 ALA 309 0.0169

ALA 309 ASP 310 0.0001

ASP 310 ASN 311 0.0290

ASN 311 ASP 312 0.0001

ASP 312 LYS 313 0.0058

LYS 313 GLU 314 -0.0001

GLU 314 TYR 315 0.0089

TYR 315 LEU 316 -0.0002

LEU 316 VAL 317 -0.0087

VAL 317 LEU 318 -0.0003

LEU 318 THR 319 -0.0102

THR 319 LEU 320 -0.0002

LEU 320 THR 321 0.0251

THR 321 LYS 322 0.0000

LYS 322 ASN 323 -0.0100

ASN 323 ASP 324 -0.0000

ASP 324 LEU 325 0.0273

LEU 325 ASP 326 -0.0005

ASP 326 LYS 327 -0.0074

LYS 327 ALA 328 -0.0002

ALA 328 ASN 329 -0.0094

ASN 329 LYS 330 -0.0000

LYS 330 ASP 331 -0.0594

ASP 331 LYS 332 -0.0000

LYS 332 ALA 333 0.0013

ALA 333 ASN 334 -0.0001

ASN 334 ARG 335 0.0037

ARG 335 TYR 336 -0.0002

TYR 336 PHE 337 0.0160

PHE 337 SER 338 0.0000

SER 338 PRO 339 0.0025

PRO 339 ASN 340 -0.0001

ASN 340 PHE 341 0.0050

PHE 341 LYS 342 0.0000

LYS 342 VAL 343 -0.0033

VAL 343 LYS 344 -0.0003

LYS 344 LEU 345 -0.0070

LEU 345 TYR 346 -0.0002

TYR 346 PHE 347 0.0114

PHE 347 THR 348 0.0002

THR 348 LYS 349 0.0015

LYS 349 THR 350 -0.0003

THR 350 VAL 351 0.0023

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 9 ---

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

* PTEN_REPRES_TEST *