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

* PTEN_REPRES_TEST *

CA strain for 2402082043421969462

--- normal mode 8 ---

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 -0.0005

ALA 3 ILE 4 -0.0000

ILE 4 ILE 5 0.0145

ILE 5 LYS 6 0.0001

LYS 6 GLU 7 0.0004

GLU 7 ILE 8 0.0002

ILE 8 VAL 9 0.0013

VAL 9 SER 10 0.0002

SER 10 ARG 11 -0.0097

ARG 11 ASN 12 -0.0002

ASN 12 LYS 13 -0.0040

LYS 13 ARG 14 0.0001

ARG 14 ARG 15 0.0035

ARG 15 TYR 16 -0.0002

TYR 16 GLN 17 -0.0029

GLN 17 GLU 18 -0.0000

GLU 18 ASP 19 0.0020

ASP 19 GLY 20 0.0001

GLY 20 PHE 21 0.0009

PHE 21 ASP 22 -0.0000

ASP 22 LEU 23 0.0005

LEU 23 ASP 24 -0.0002

ASP 24 LEU 25 -0.0128

LEU 25 THR 26 -0.0002

THR 26 TYR 27 -0.0109

TYR 27 ILE 28 0.0003

ILE 28 TYR 29 -0.0035

TYR 29 PRO 30 -0.0004

PRO 30 ASN 31 0.0016

ASN 31 ILE 32 -0.0002

ILE 32 ILE 33 -0.0098

ILE 33 ALA 34 -0.0001

ALA 34 MET 35 -0.0130

MET 35 GLY 36 -0.0000

GLY 36 PHE 37 -0.0102

PHE 37 PRO 38 -0.0001

PRO 38 ALA 39 -0.0018

ALA 39 GLU 40 -0.0004

GLU 40 ARG 41 0.0064

ARG 41 LEU 42 0.0003

LEU 42 GLU 43 -0.0030

GLU 43 GLY 44 0.0003

GLY 44 VAL 45 0.0075

VAL 45 TYR 46 0.0001

TYR 46 ARG 47 0.0182

ARG 47 ASN 48 -0.0002

ASN 48 ASN 49 -0.0049

ASN 49 ILE 50 0.0001

ILE 50 ASP 51 0.0013

ASP 51 ASP 52 0.0002

ASP 52 VAL 53 0.0007

VAL 53 VAL 54 0.0000

VAL 54 ARG 55 0.0033

ARG 55 PHE 56 0.0001

PHE 56 LEU 57 -0.0006

LEU 57 ASP 58 0.0003

ASP 58 SER 59 0.0023

SER 59 LYS 60 0.0002

LYS 60 HIS 61 -0.0107

HIS 61 LYS 62 -0.0002

LYS 62 ASN 63 -0.0015

ASN 63 HIS 64 0.0000

HIS 64 TYR 65 -0.0032

TYR 65 LYS 66 -0.0003

LYS 66 ILE 67 -0.0006

ILE 67 TYR 68 0.0003

TYR 68 ASN 69 -0.0006

ASN 69 LEU 70 -0.0001

LEU 70 CYS 71 0.0064

CYS 71 ALA 72 -0.0004

ALA 72 GLU 73 0.0336

GLU 73 ARG 74 -0.0001

ARG 74 HIS 75 -0.0044

HIS 75 TYR 76 -0.0003

TYR 76 ASP 77 -0.0072

ASP 77 THR 78 -0.0000

THR 78 ALA 79 -0.0001

ALA 79 LYS 80 -0.0001

LYS 80 PHE 81 0.0040

PHE 81 ASN 82 -0.0003

ASN 82 CYS 83 0.0032

CYS 83 ARG 84 0.0003

ARG 84 VAL 85 -0.0072

VAL 85 ALA 86 0.0001

ALA 86 GLN 87 -0.0139

GLN 87 TYR 88 0.0001

TYR 88 PRO 89 -0.0109

PRO 89 PHE 90 0.0001

PHE 90 GLU 91 -0.0105

GLU 91 ASP 92 0.0000

ASP 92 HIS 93 -0.0139

HIS 93 ASN 94 0.0002

ASN 94 PRO 95 0.0077

PRO 95 PRO 96 -0.0001

PRO 96 GLN 97 0.0117

GLN 97 LEU 98 -0.0004

LEU 98 GLU 99 0.0070

GLU 99 LEU 100 0.0001

LEU 100 ILE 101 -0.0067

ILE 101 LYS 102 0.0000

LYS 102 PRO 103 0.0215

PRO 103 PHE 104 -0.0002

PHE 104 CYS 105 0.0003

CYS 105 GLU 106 -0.0001

GLU 106 ASP 107 0.0171

ASP 107 LEU 108 0.0000

LEU 108 ASP 109 0.0058

ASP 109 GLN 110 0.0002

GLN 110 TRP 111 -0.0016

TRP 111 LEU 112 -0.0000

LEU 112 SER 113 -0.0011

SER 113 GLU 114 -0.0002

GLU 114 ASP 115 0.0003

ASP 115 ASP 116 -0.0002

ASP 116 ASN 117 -0.0023

ASN 117 HIS 118 0.0001

HIS 118 VAL 119 0.0021

VAL 119 ALA 120 -0.0001

ALA 120 ALA 121 0.0003

ALA 121 ILE 122 0.0000

ILE 122 HIS 123 0.0022

HIS 123 CYS 124 -0.0002

CYS 124 LYS 125 0.0060

LYS 125 ALA 126 -0.0000

ALA 126 GLY 127 -0.0098

GLY 127 LYS 128 -0.0001

LYS 128 GLY 129 0.0348

GLY 129 ARG 130 -0.0000

ARG 130 THR 131 0.0096

THR 131 GLY 132 0.0001

GLY 132 VAL 133 0.0041

VAL 133 MET 134 -0.0000

MET 134 ILE 135 0.0054

ILE 135 CYS 136 -0.0001

CYS 136 ALA 137 -0.0153

ALA 137 TYR 138 0.0003

TYR 138 LEU 139 0.0093

LEU 139 LEU 140 -0.0003

LEU 140 HIS 141 0.0157

HIS 141 ARG 142 -0.0000

ARG 142 GLY 143 0.0249

GLY 143 LYS 144 -0.0000

LYS 144 PHE 145 0.0108

PHE 145 LEU 146 0.0001

LEU 146 LYS 147 0.0291

LYS 147 ALA 148 -0.0003

ALA 148 GLN 149 0.0101

GLN 149 GLU 150 0.0000

GLU 150 ALA 151 -0.0120

ALA 151 LEU 152 0.0003

LEU 152 ASP 153 -0.0041

ASP 153 PHE 154 0.0001

PHE 154 TYR 155 -0.0169

TYR 155 GLY 156 -0.0001

GLY 156 GLU 157 0.0138

GLU 157 VAL 158 0.0003

VAL 158 ARG 159 -0.0129

ARG 159 THR 160 -0.0001

THR 160 ARG 161 0.0053

ARG 161 ASP 162 -0.0005

ASP 162 LYS 163 -0.0115

LYS 163 LYS 164 0.0004

LYS 164 GLY 165 -0.0136

GLY 165 VAL 166 0.0001

VAL 166 THR 167 0.0302

THR 167 ILE 168 0.0001

ILE 168 PRO 169 0.0033

PRO 169 SER 170 0.0001

SER 170 GLN 171 0.0124

GLN 171 ARG 172 -0.0000

ARG 172 ARG 173 0.0018

ARG 173 TYR 174 -0.0001

TYR 174 VAL 175 -0.0065

VAL 175 TYR 176 0.0003

TYR 176 TYR 177 -0.0016

TYR 177 TYR 178 0.0002

TYR 178 SER 179 0.0081

SER 179 TYR 180 0.0003

TYR 180 LEU 181 0.0139

LEU 181 LEU 182 0.0002

LEU 182 LYS 183 0.0301

LYS 183 ASN 184 -0.0001

ASN 184 HIS 185 0.0057

HIS 185 LEU 186 0.0002

LEU 186 ASP 187 0.0184

ASP 187 TYR 188 0.0000

TYR 188 ARG 189 -0.0130

ARG 189 PRO 190 0.0002

PRO 190 VAL 191 0.0128

VAL 191 ALA 192 -0.0002

ALA 192 LEU 193 -0.0121

LEU 193 LEU 194 -0.0003

LEU 194 PHE 195 -0.0021

PHE 195 HIS 196 -0.0000

HIS 196 LYS 197 -0.0064

LYS 197 MET 198 0.0001

MET 198 MET 199 -0.0070

MET 199 PHE 200 -0.0001

PHE 200 GLU 201 -0.0054

GLU 201 THR 202 0.0003

THR 202 ILE 203 0.0015

ILE 203 PRO 204 -0.0003

PRO 204 MET 205 0.0001

MET 205 PHE 206 -0.0003

PHE 206 SER 207 0.0007

SER 207 GLY 208 -0.0001

GLY 208 GLY 209 0.0028

GLY 209 THR 210 -0.0001

THR 210 CYS 211 -0.0036

CYS 211 ASN 212 -0.0005

ASN 212 PRO 213 -0.0057

PRO 213 GLN 214 -0.0001

GLN 214 PHE 215 -0.0111

PHE 215 VAL 216 0.0001

VAL 216 VAL 217 -0.0130

VAL 217 CYS 218 -0.0001

CYS 218 GLN 219 -0.0204

GLN 219 LEU 220 0.0003

LEU 220 LYS 221 -0.0039

LYS 221 VAL 222 0.0001

VAL 222 LYS 223 -0.0113

LYS 223 ILE 224 0.0005

ILE 224 TYR 225 -0.0133

TYR 225 SER 226 -0.0002

SER 226 SER 227 -0.0122

SER 227 ASN 228 0.0005

ASN 228 SER 229 -0.0059

SER 229 GLY 230 0.0001

GLY 230 PRO 231 0.0015

PRO 231 THR 232 0.0001

THR 232 ARG 233 -0.0048

ARG 233 ARG 234 -0.0005

ARG 234 GLU 235 -0.0032

GLU 235 ASP 236 0.0002

ASP 236 LYS 237 0.0006

LYS 237 PHE 238 0.0000

PHE 238 MET 239 -0.0042

MET 239 TYR 240 0.0000

TYR 240 PHE 241 -0.0073

PHE 241 GLU 242 0.0001

GLU 242 PHE 243 -0.0075

PHE 243 PRO 244 -0.0002

PRO 244 GLN 245 -0.0059

GLN 245 PRO 246 -0.0001

PRO 246 LEU 247 -0.0018

LEU 247 PRO 248 -0.0003

PRO 248 VAL 249 -0.0052

VAL 249 CYS 250 -0.0002

CYS 250 GLY 251 -0.0013

GLY 251 ASP 252 -0.0001

ASP 252 ILE 253 -0.0327

ILE 253 LYS 254 0.0002

LYS 254 VAL 255 -0.0150

VAL 255 GLU 256 -0.0001

GLU 256 PHE 257 -0.0102

PHE 257 PHE 258 0.0001

PHE 258 HIS 259 -0.0060

HIS 259 LYS 260 0.0001

LYS 260 GLN 261 -0.0049

GLN 261 ASN 262 0.0001

ASN 262 LYS 263 0.0032

LYS 263 MET 264 0.0004

MET 264 LEU 265 -0.0026

LEU 265 LYS 266 -0.0000

LYS 266 LYS 267 0.0061

LYS 267 ASP 268 -0.0002

ASP 268 LYS 269 0.0064

LYS 269 MET 270 -0.0001

MET 270 PHE 271 -0.0036

PHE 271 HIS 272 -0.0001

HIS 272 PHE 273 -0.0077

PHE 273 TRP 274 -0.0002

TRP 274 VAL 275 0.0080

VAL 275 ASN 276 0.0004

ASN 276 THR 277 0.0147

THR 277 PHE 278 -0.0002

PHE 278 PHE 279 0.0077

PHE 279 ILE 280 0.0001

ILE 280 PRO 281 0.0588

PRO 281 GLY 282 -0.0001

GLY 282 PRO 283 0.1115

PRO 283 GLU 284 -0.0002

GLU 284 GLU 285 -0.1120

GLU 285 THR 286 -0.0002

THR 286 SER 287 -0.1113

SER 287 GLU 288 0.0000

GLU 288 LYS 289 0.0132

LYS 289 VAL 290 0.0002

VAL 290 GLU 291 0.0448

GLU 291 ASN 292 -0.0002

ASN 292 GLY 293 0.0770

GLY 293 SER 294 -0.0002

SER 294 LEU 295 0.0221

LEU 295 CYS 296 -0.0004

CYS 296 ASP 297 -0.0596

ASP 297 GLN 298 0.0001

GLN 298 GLU 299 0.0018

GLU 299 ILE 300 -0.0005

ILE 300 ASP 301 0.0389

ASP 301 SER 302 -0.0001

SER 302 ILE 303 0.0046

ILE 303 CYS 304 0.0002

CYS 304 SER 305 -0.0063

SER 305 ILE 306 -0.0001

ILE 306 GLU 307 0.0008

GLU 307 ARG 308 -0.0001

ARG 308 ALA 309 0.0011

ALA 309 ASP 310 0.0002

ASP 310 ASN 311 -0.0007

ASN 311 ASP 312 0.0002

ASP 312 LYS 313 0.0028

LYS 313 GLU 314 0.0000

GLU 314 TYR 315 -0.0030

TYR 315 LEU 316 0.0001

LEU 316 VAL 317 0.0064

VAL 317 LEU 318 -0.0001

LEU 318 THR 319 -0.0035

THR 319 LEU 320 0.0001

LEU 320 THR 321 -0.0009

THR 321 LYS 322 -0.0002

LYS 322 ASN 323 0.0046

ASN 323 ASP 324 0.0002

ASP 324 LEU 325 0.0025

LEU 325 ASP 326 0.0001

ASP 326 LYS 327 -0.0008

LYS 327 ALA 328 0.0000

ALA 328 ASN 329 0.0025

ASN 329 LYS 330 0.0001

LYS 330 ASP 331 0.0078

ASP 331 LYS 332 -0.0002

LYS 332 ALA 333 0.0024

ALA 333 ASN 334 0.0002

ASN 334 ARG 335 0.0006

ARG 335 TYR 336 -0.0001

TYR 336 PHE 337 -0.0001

PHE 337 SER 338 -0.0003

SER 338 PRO 339 -0.0009

PRO 339 ASN 340 0.0002

ASN 340 PHE 341 0.0017

PHE 341 LYS 342 -0.0003

LYS 342 VAL 343 -0.0032

VAL 343 LYS 344 0.0002

LYS 344 LEU 345 -0.0040

LEU 345 TYR 346 -0.0001

TYR 346 PHE 347 -0.0044

PHE 347 THR 348 0.0003

THR 348 LYS 349 -0.0010

LYS 349 THR 350 -0.0001

THR 350 VAL 351 -0.0006

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 8 ---

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

* PTEN_REPRES_TEST *