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

* PTEN_REPRES_TEST *

CA strain for 2402082043421969462

--- normal mode 7 ---

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 0.0008

ALA 3 ILE 4 0.0002

ILE 4 ILE 5 -0.0023

ILE 5 LYS 6 0.0005

LYS 6 GLU 7 -0.0000

GLU 7 ILE 8 -0.0003

ILE 8 VAL 9 -0.0003

VAL 9 SER 10 0.0000

SER 10 ARG 11 0.0003

ARG 11 ASN 12 -0.0004

ASN 12 LYS 13 -0.0004

LYS 13 ARG 14 0.0002

ARG 14 ARG 15 0.0006

ARG 15 TYR 16 -0.0002

TYR 16 GLN 17 -0.0001

GLN 17 GLU 18 0.0003

GLU 18 ASP 19 -0.0002

ASP 19 GLY 20 -0.0001

GLY 20 PHE 21 0.0002

PHE 21 ASP 22 -0.0001

ASP 22 LEU 23 -0.0009

LEU 23 ASP 24 -0.0003

ASP 24 LEU 25 0.0007

LEU 25 THR 26 0.0000

THR 26 TYR 27 0.0005

TYR 27 ILE 28 0.0000

ILE 28 TYR 29 0.0009

TYR 29 PRO 30 0.0001

PRO 30 ASN 31 0.0006

ASN 31 ILE 32 -0.0005

ILE 32 ILE 33 -0.0015

ILE 33 ALA 34 -0.0003

ALA 34 MET 35 0.0004

MET 35 GLY 36 -0.0000

GLY 36 PHE 37 0.0012

PHE 37 PRO 38 -0.0000

PRO 38 ALA 39 -0.0009

ALA 39 GLU 40 0.0001

GLU 40 ARG 41 -0.0013

ARG 41 LEU 42 -0.0002

LEU 42 GLU 43 -0.0003

GLU 43 GLY 44 0.0001

GLY 44 VAL 45 0.0001

VAL 45 TYR 46 -0.0002

TYR 46 ARG 47 -0.0011

ARG 47 ASN 48 0.0004

ASN 48 ASN 49 0.0001

ASN 49 ILE 50 0.0001

ILE 50 ASP 51 0.0004

ASP 51 ASP 52 -0.0003

ASP 52 VAL 53 -0.0010

VAL 53 VAL 54 0.0003

VAL 54 ARG 55 0.0002

ARG 55 PHE 56 -0.0002

PHE 56 LEU 57 -0.0004

LEU 57 ASP 58 -0.0002

ASP 58 SER 59 -0.0005

SER 59 LYS 60 0.0002

LYS 60 HIS 61 0.0002

HIS 61 LYS 62 0.0001

LYS 62 ASN 63 -0.0000

ASN 63 HIS 64 -0.0003

HIS 64 TYR 65 0.0012

TYR 65 LYS 66 0.0001

LYS 66 ILE 67 0.0009

ILE 67 TYR 68 0.0002

TYR 68 ASN 69 0.0004

ASN 69 LEU 70 -0.0002

LEU 70 CYS 71 -0.0012

CYS 71 ALA 72 -0.0003

ALA 72 GLU 73 -0.0048

GLU 73 ARG 74 0.0000

ARG 74 HIS 75 0.0011

HIS 75 TYR 76 -0.0000

TYR 76 ASP 77 0.0017

ASP 77 THR 78 -0.0001

THR 78 ALA 79 0.0003

ALA 79 LYS 80 -0.0005

LYS 80 PHE 81 -0.0012

PHE 81 ASN 82 -0.0000

ASN 82 CYS 83 -0.0019

CYS 83 ARG 84 0.0005

ARG 84 VAL 85 0.0015

VAL 85 ALA 86 -0.0001

ALA 86 GLN 87 0.0027

GLN 87 TYR 88 -0.0002

TYR 88 PRO 89 0.0005

PRO 89 PHE 90 0.0000

PHE 90 GLU 91 -0.0003

GLU 91 ASP 92 0.0000

ASP 92 HIS 93 0.0029

HIS 93 ASN 94 -0.0000

ASN 94 PRO 95 -0.0034

PRO 95 PRO 96 -0.0001

PRO 96 GLN 97 -0.0005

GLN 97 LEU 98 0.0000

LEU 98 GLU 99 -0.0009

GLU 99 LEU 100 0.0002

LEU 100 ILE 101 0.0007

ILE 101 LYS 102 -0.0001

LYS 102 PRO 103 -0.0052

PRO 103 PHE 104 0.0001

PHE 104 CYS 105 -0.0003

CYS 105 GLU 106 0.0003

GLU 106 ASP 107 -0.0055

ASP 107 LEU 108 -0.0001

LEU 108 ASP 109 -0.0003

ASP 109 GLN 110 0.0000

GLN 110 TRP 111 -0.0014

TRP 111 LEU 112 -0.0007

LEU 112 SER 113 -0.0001

SER 113 GLU 114 0.0005

GLU 114 ASP 115 -0.0009

ASP 115 ASP 116 -0.0003

ASP 116 ASN 117 0.0004

ASN 117 HIS 118 -0.0001

HIS 118 VAL 119 0.0004

VAL 119 ALA 120 -0.0001

ALA 120 ALA 121 0.0001

ALA 121 ILE 122 -0.0001

ILE 122 HIS 123 -0.0010

HIS 123 CYS 124 -0.0003

CYS 124 LYS 125 -0.0009

LYS 125 ALA 126 0.0002

ALA 126 GLY 127 0.0004

GLY 127 LYS 128 0.0001

LYS 128 GLY 129 -0.0022

GLY 129 ARG 130 -0.0005

ARG 130 THR 131 -0.0004

THR 131 GLY 132 0.0000

GLY 132 VAL 133 0.0002

VAL 133 MET 134 0.0003

MET 134 ILE 135 -0.0002

ILE 135 CYS 136 -0.0001

CYS 136 ALA 137 0.0013

ALA 137 TYR 138 0.0001

TYR 138 LEU 139 -0.0018

LEU 139 LEU 140 -0.0000

LEU 140 HIS 141 -0.0043

HIS 141 ARG 142 -0.0002

ARG 142 GLY 143 -0.0086

GLY 143 LYS 144 -0.0001

LYS 144 PHE 145 -0.0091

PHE 145 LEU 146 -0.0002

LEU 146 LYS 147 -0.0052

LYS 147 ALA 148 0.0003

ALA 148 GLN 149 -0.0017

GLN 149 GLU 150 0.0001

GLU 150 ALA 151 0.0038

ALA 151 LEU 152 0.0002

LEU 152 ASP 153 -0.0022

ASP 153 PHE 154 -0.0001

PHE 154 TYR 155 0.0029

TYR 155 GLY 156 -0.0003

GLY 156 GLU 157 -0.0028

GLU 157 VAL 158 0.0002

VAL 158 ARG 159 0.0010

ARG 159 THR 160 0.0003

THR 160 ARG 161 -0.0013

ARG 161 ASP 162 0.0002

ASP 162 LYS 163 0.0032

LYS 163 LYS 164 -0.0001

LYS 164 GLY 165 0.0009

GLY 165 VAL 166 0.0002

VAL 166 THR 167 -0.0036

THR 167 ILE 168 0.0001

ILE 168 PRO 169 -0.0028

PRO 169 SER 170 -0.0002

SER 170 GLN 171 -0.0014

GLN 171 ARG 172 -0.0004

ARG 172 ARG 173 -0.0053

ARG 173 TYR 174 -0.0002

TYR 174 VAL 175 0.0002

VAL 175 TYR 176 -0.0005

TYR 176 TYR 177 -0.0017

TYR 177 TYR 178 0.0003

TYR 178 SER 179 -0.0083

SER 179 TYR 180 0.0001

TYR 180 LEU 181 -0.0000

LEU 181 LEU 182 0.0003

LEU 182 LYS 183 -0.0229

LYS 183 ASN 184 0.0001

ASN 184 HIS 185 -0.0125

HIS 185 LEU 186 0.0004

LEU 186 ASP 187 -0.0127

ASP 187 TYR 188 -0.0001

TYR 188 ARG 189 0.0013

ARG 189 PRO 190 -0.0000

PRO 190 VAL 191 0.0041

VAL 191 ALA 192 0.0002

ALA 192 LEU 193 0.0015

LEU 193 LEU 194 0.0002

LEU 194 PHE 195 0.0001

PHE 195 HIS 196 0.0002

HIS 196 LYS 197 -0.0006

LYS 197 MET 198 0.0003

MET 198 MET 199 -0.0014

MET 199 PHE 200 0.0000

PHE 200 GLU 201 -0.0010

GLU 201 THR 202 -0.0001

THR 202 ILE 203 0.0017

ILE 203 PRO 204 0.0002

PRO 204 MET 205 0.0008

MET 205 PHE 206 0.0001

PHE 206 SER 207 0.0006

SER 207 GLY 208 0.0002

GLY 208 GLY 209 0.0015

GLY 209 THR 210 0.0001

THR 210 CYS 211 -0.0010

CYS 211 ASN 212 0.0000

ASN 212 PRO 213 -0.0009

PRO 213 GLN 214 0.0006

GLN 214 PHE 215 -0.0017

PHE 215 VAL 216 0.0001

VAL 216 VAL 217 -0.0027

VAL 217 CYS 218 0.0001

CYS 218 GLN 219 -0.0018

GLN 219 LEU 220 0.0001

LEU 220 LYS 221 -0.0005

LYS 221 VAL 222 0.0003

VAL 222 LYS 223 -0.0001

LYS 223 ILE 224 -0.0002

ILE 224 TYR 225 -0.0006

TYR 225 SER 226 0.0004

SER 226 SER 227 -0.0005

SER 227 ASN 228 0.0002

ASN 228 SER 229 -0.0014

SER 229 GLY 230 0.0002

GLY 230 PRO 231 0.0014

PRO 231 THR 232 -0.0004

THR 232 ARG 233 -0.0004

ARG 233 ARG 234 0.0003

ARG 234 GLU 235 -0.0010

GLU 235 ASP 236 0.0002

ASP 236 LYS 237 -0.0002

LYS 237 PHE 238 0.0002

PHE 238 MET 239 -0.0008

MET 239 TYR 240 0.0000

TYR 240 PHE 241 -0.0010

PHE 241 GLU 242 0.0001

GLU 242 PHE 243 -0.0011

PHE 243 PRO 244 0.0003

PRO 244 GLN 245 -0.0006

GLN 245 PRO 246 -0.0003

PRO 246 LEU 247 0.0009

LEU 247 PRO 248 -0.0001

PRO 248 VAL 249 0.0015

VAL 249 CYS 250 0.0001

CYS 250 GLY 251 0.0034

GLY 251 ASP 252 -0.0002

ASP 252 ILE 253 0.0005

ILE 253 LYS 254 0.0004

LYS 254 VAL 255 -0.0010

VAL 255 GLU 256 0.0000

GLU 256 PHE 257 -0.0012

PHE 257 PHE 258 0.0000

PHE 258 HIS 259 -0.0008

HIS 259 LYS 260 -0.0003

LYS 260 GLN 261 -0.0000

GLN 261 ASN 262 0.0004

ASN 262 LYS 263 0.0011

LYS 263 MET 264 0.0002

MET 264 LEU 265 -0.0007

LEU 265 LYS 266 -0.0002

LYS 266 LYS 267 0.0013

LYS 267 ASP 268 0.0001

ASP 268 LYS 269 0.0000

LYS 269 MET 270 -0.0002

MET 270 PHE 271 0.0008

PHE 271 HIS 272 -0.0002

HIS 272 PHE 273 0.0002

PHE 273 TRP 274 0.0001

TRP 274 VAL 275 -0.0019

VAL 275 ASN 276 -0.0004

ASN 276 THR 277 0.0011

THR 277 PHE 278 0.0001

PHE 278 PHE 279 0.0022

PHE 279 ILE 280 0.0002

ILE 280 PRO 281 -0.0122

PRO 281 GLY 282 0.0002

GLY 282 PRO 283 -0.0810

PRO 283 GLU 284 0.0004

GLU 284 GLU 285 -0.0040

GLU 285 THR 286 -0.0001

THR 286 SER 287 -0.0507

SER 287 GLU 288 0.0001

GLU 288 LYS 289 -0.0285

LYS 289 VAL 290 -0.0001

VAL 290 GLU 291 0.0370

GLU 291 ASN 292 -0.0000

ASN 292 GLY 293 -0.0046

GLY 293 SER 294 0.0001

SER 294 LEU 295 0.0039

LEU 295 CYS 296 -0.0000

CYS 296 ASP 297 0.1063

ASP 297 GLN 298 -0.0000

GLN 298 GLU 299 0.0142

GLU 299 ILE 300 -0.0001

ILE 300 ASP 301 -0.0124

ASP 301 SER 302 -0.0001

SER 302 ILE 303 0.0095

ILE 303 CYS 304 0.0003

CYS 304 SER 305 -0.0022

SER 305 ILE 306 -0.0001

ILE 306 GLU 307 0.0025

GLU 307 ARG 308 0.0000

ARG 308 ALA 309 0.0090

ALA 309 ASP 310 0.0001

ASP 310 ASN 311 0.0083

ASN 311 ASP 312 -0.0002

ASP 312 LYS 313 0.0034

LYS 313 GLU 314 -0.0000

GLU 314 TYR 315 -0.0013

TYR 315 LEU 316 0.0003

LEU 316 VAL 317 0.0014

VAL 317 LEU 318 0.0000

LEU 318 THR 319 0.0023

THR 319 LEU 320 -0.0001

LEU 320 THR 321 0.0031

THR 321 LYS 322 -0.0001

LYS 322 ASN 323 -0.0009

ASN 323 ASP 324 0.0003

ASP 324 LEU 325 0.0054

LEU 325 ASP 326 0.0002

ASP 326 LYS 327 0.0009

LYS 327 ALA 328 0.0003

ALA 328 ASN 329 -0.0009

ASN 329 LYS 330 0.0001

LYS 330 ASP 331 -0.0013

ASP 331 LYS 332 -0.0001

LYS 332 ALA 333 0.0002

ALA 333 ASN 334 -0.0003

ASN 334 ARG 335 0.0000

ARG 335 TYR 336 -0.0001

TYR 336 PHE 337 0.0024

PHE 337 SER 338 -0.0001

SER 338 PRO 339 -0.0006

PRO 339 ASN 340 -0.0001

ASN 340 PHE 341 -0.0000

PHE 341 LYS 342 0.0001

LYS 342 VAL 343 -0.0015

VAL 343 LYS 344 0.0002

LYS 344 LEU 345 -0.0017

LEU 345 TYR 346 0.0004

TYR 346 PHE 347 0.0003

PHE 347 THR 348 0.0004

THR 348 LYS 349 0.0001

LYS 349 THR 350 -0.0002

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 7 ---

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

* PTEN_REPRES_TEST *