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

* 2CMZ *

CA strain for 240228060628930665

--- 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
LYS 1 PHE 2 -0.0001

PHE 2 THR 3 0.0001

THR 3 ILE 4 -0.0017

ILE 4 VAL 5 0.0002

VAL 5 PHE 6 -0.0002

PHE 6 PRO 7 0.0004

PRO 7 HIS 8 0.0003

HIS 8 ASN 9 0.0000

ASN 9 GLN 10 0.0010

GLN 10 LYS 11 -0.0001

LYS 11 GLY 12 -0.0002

GLY 12 ASN 13 0.0009

ASN 13 TRP 14 -0.0000

TRP 14 LYS 15 0.0000

LYS 15 ASN 16 0.0004

ASN 16 VAL 17 0.0000

VAL 17 PRO 18 0.0004

PRO 18 SER 19 0.0019

SER 19 ASN 20 0.0002

ASN 20 TYR 21 -0.0001

TYR 21 HIS 22 0.0011

HIS 22 TYR 23 -0.0000

TYR 23 CYS 24 -0.0000

CYS 24 PRO 25 -0.0113

PRO 25 SER 26 -0.0004

SER 26 SER 27 0.0002

SER 27 SER 28 -0.0405

SER 28 ASP 29 0.0003

ASP 29 LEU 30 0.0000

LEU 30 ASN 31 0.0081

ASN 31 TRP 32 -0.0004

TRP 32 HIS 33 -0.0003

HIS 33 ASN 34 -0.0456

ASN 34 ASP 35 -0.0000

ASP 35 LEU 36 0.0002

LEU 36 ILE 37 0.0068

ILE 37 GLY 38 0.0002

GLY 38 THR 39 0.0000

THR 39 ALA 40 0.0135

ALA 40 ILE 41 -0.0001

ILE 41 GLN 42 -0.0002

GLN 42 VAL 43 0.0025

VAL 43 LYS 44 0.0002

LYS 44 MET 45 0.0000

MET 45 PRO 46 0.0128

PRO 46 LYS 47 -0.0001

LYS 47 SER 48 -0.0002

SER 48 HIS 49 0.0612

HIS 49 LYS 50 0.0002

LYS 50 ALA 51 0.0001

ALA 51 ILE 52 0.0032

ILE 52 GLN 53 -0.0000

GLN 53 ALA 54 0.0001

ALA 54 ASP 55 0.0785

ASP 55 GLY 56 -0.0000

GLY 56 TRP 57 0.0001

TRP 57 MET 58 0.0105

MET 58 CYS 59 -0.0002

CYS 59 HIS 60 0.0004

HIS 60 ALA 61 -0.0076

ALA 61 SER 62 0.0002

SER 62 LYS 63 -0.0002

LYS 63 TRP 64 -0.0158

TRP 64 VAL 65 0.0000

VAL 65 THR 66 0.0003

THR 66 THR 67 0.0055

THR 67 CYS 68 0.0002

CYS 68 ASP 69 -0.0000

ASP 69 PHE 70 -0.0044

PHE 70 ARG 71 -0.0000

ARG 71 TRP 72 0.0000

TRP 72 TYR 73 -0.0005

TYR 73 GLY 74 0.0002

GLY 74 PRO 75 0.0001

PRO 75 LYS 76 0.0075

LYS 76 TYR 77 -0.0000

TYR 77 ILE 78 -0.0001

ILE 78 THR 79 -0.0033

THR 79 GLN 80 0.0000

GLN 80 SER 81 0.0002

SER 81 ILE 82 -0.0208

ILE 82 ARG 83 -0.0000

ARG 83 SER 84 0.0002

SER 84 PHE 85 0.0017

PHE 85 THR 86 0.0001

THR 86 PRO 87 0.0003

PRO 87 SER 88 -0.0076

SER 88 VAL 89 -0.0002

VAL 89 GLU 90 0.0002

GLU 90 GLN 91 -0.0038

GLN 91 CYS 92 -0.0000

CYS 92 LYS 93 -0.0003

LYS 93 GLU 94 -0.0057

GLU 94 SER 95 0.0003

SER 95 ILE 96 0.0003

ILE 96 GLU 97 -0.0027

GLU 97 GLN 98 -0.0003

GLN 98 THR 99 0.0001

THR 99 LYS 100 0.0104

LYS 100 GLN 101 -0.0002

GLN 101 GLY 102 -0.0001

GLY 102 THR 103 0.0162

THR 103 TRP 104 -0.0002

TRP 104 LEU 105 0.0004

LEU 105 ASN 106 0.0256

ASN 106 PRO 107 -0.0004

PRO 107 GLY 108 -0.0001

GLY 108 PHE 109 0.0415

PHE 109 PRO 110 0.0002

PRO 110 PRO 111 -0.0001

PRO 111 GLN 112 0.0349

GLN 112 SER 113 0.0001

SER 113 CYS 114 -0.0002

CYS 114 GLY 115 0.0134

GLY 115 TYR 116 -0.0002

TYR 116 ALA 117 0.0001

ALA 117 THR 118 -0.0100

THR 118 VAL 119 -0.0005

VAL 119 THR 120 -0.0001

THR 120 ASP 121 -0.0251

ASP 121 ALA 122 0.0000

ALA 122 GLU 123 -0.0001

GLU 123 ALA 124 -0.0009

ALA 124 VAL 125 -0.0000

VAL 125 ILE 126 0.0001

ILE 126 VAL 127 0.0115

VAL 127 GLN 128 0.0001

GLN 128 VAL 129 -0.0002

VAL 129 THR 130 0.0260

THR 130 PRO 131 -0.0001

PRO 131 HIS 132 0.0002

HIS 132 HIS 133 0.0497

HIS 133 VAL 134 -0.0003

VAL 134 LEU 135 -0.0001

LEU 135 VAL 136 0.0065

VAL 136 ASP 137 -0.0002

ASP 137 GLU 138 0.0001

GLU 138 TYR 139 0.0125

TYR 139 THR 140 0.0003

THR 140 GLY 141 -0.0000

GLY 141 GLU 142 -0.0352

GLU 142 TRP 143 0.0001

TRP 143 VAL 144 -0.0002

VAL 144 ASP 145 -0.0058

ASP 145 SER 146 -0.0001

SER 146 GLN 147 0.0002

GLN 147 PHE 148 0.0021

PHE 148 ILE 149 0.0001

ILE 149 ASN 150 0.0002

ASN 150 GLY 151 -0.0028

GLY 151 LYS 152 -0.0001

LYS 152 CYS 153 -0.0001

CYS 153 SER 154 0.0040

SER 154 ASN 155 -0.0003

ASN 155 TYR 156 -0.0001

TYR 156 ILE 157 -0.0163

ILE 157 CYS 158 0.0001

CYS 158 PRO 159 -0.0002

PRO 159 THR 160 0.0229

THR 160 VAL 161 -0.0001

VAL 161 HIS 162 0.0004

HIS 162 ASN 163 0.0058

ASN 163 SER 164 0.0002

SER 164 THR 165 -0.0001

THR 165 THR 166 -0.0104

THR 166 TRP 167 -0.0000

TRP 167 HIS 168 0.0000

HIS 168 SER 169 -0.0011

SER 169 ASP 170 0.0000

ASP 170 TYR 171 -0.0000

TYR 171 LYS 172 -0.0246

LYS 172 VAL 173 -0.0000

VAL 173 LYS 174 0.0001

LYS 174 GLY 175 0.0003

GLY 175 LEU 176 -0.0004

LEU 176 CYS 177 0.0001

CYS 177 ASP 178 0.0095

ASP 178 SER 179 0.0001

SER 179 ASN 180 0.0003

ASN 180 LEU 181 0.0123

LEU 181 ILE 182 0.0002

ILE 182 SER 183 0.0002

SER 183 MET 184 0.0236

MET 184 ASP 185 -0.0002

ASP 185 ILE 186 0.0004

ILE 186 THR 187 0.0179

THR 187 PHE 188 -0.0003

PHE 188 PHE 189 0.0000

PHE 189 SER 190 0.0073

SER 190 GLU 191 -0.0001

GLU 191 ASP 192 -0.0002

ASP 192 GLY 193 0.0011

GLY 193 GLU 194 -0.0000

GLU 194 LEU 195 0.0004

LEU 195 SER 196 0.0053

SER 196 SER 197 -0.0002

SER 197 LEU 198 -0.0000

LEU 198 GLY 199 -0.0002

GLY 199 LYS 200 0.0002

LYS 200 GLU 201 -0.0003

GLU 201 GLY 202 -0.0138

GLY 202 THR 203 0.0002

THR 203 GLY 204 -0.0000

GLY 204 PHE 205 -0.0021

PHE 205 ARG 206 -0.0002

ARG 206 SER 207 -0.0001

SER 207 ASN 208 -0.0002

ASN 208 TYR 209 0.0002

TYR 209 PHE 210 -0.0002

PHE 210 ALA 211 0.0130

ALA 211 TYR 212 -0.0001

TYR 212 GLU 213 0.0003

GLU 213 THR 214 -0.0085

THR 214 GLY 215 -0.0001

GLY 215 GLY 216 -0.0002

GLY 216 LYS 217 -0.0122

LYS 217 ALA 218 -0.0000

ALA 218 CYS 219 0.0002

CYS 219 LYS 220 -0.0335

LYS 220 MET 221 -0.0003

MET 221 GLN 222 0.0000

GLN 222 TYR 223 0.0066

TYR 223 CYS 224 -0.0001

CYS 224 LYS 225 0.0001

LYS 225 HIS 226 -0.0432

HIS 226 TRP 227 -0.0001

TRP 227 GLY 228 0.0003

GLY 228 VAL 229 -0.0200

VAL 229 ARG 230 0.0001

ARG 230 LEU 231 0.0001

LEU 231 PRO 232 0.0042

PRO 232 SER 233 0.0004

SER 233 GLY 234 0.0002

GLY 234 VAL 235 -0.0055

VAL 235 TRP 236 -0.0003

TRP 236 PHE 237 0.0005

PHE 237 GLU 238 -0.0023

GLU 238 MET 239 0.0001

MET 239 ALA 240 -0.0004

ALA 240 ASP 241 -0.0007

ASP 241 LYS 242 -0.0003

LYS 242 ASP 243 0.0001

ASP 243 LEU 244 -0.0060

LEU 244 PHE 245 0.0000

PHE 245 ALA 246 0.0004

ALA 246 ALA 247 -0.0087

ALA 247 ALA 248 -0.0002

ALA 248 ARG 249 0.0001

ARG 249 PHE 250 0.0107

PHE 250 PRO 251 0.0002

PRO 251 GLU 252 0.0004

GLU 252 CYS 253 0.0048

CYS 253 PRO 254 0.0001

PRO 254 GLU 255 0.0000

GLU 255 GLY 256 -0.0018

GLY 256 SER 257 0.0001

SER 257 SER 258 0.0000

SER 258 ILE 259 0.0110

ILE 259 SER 260 0.0004

SER 260 ALA 261 -0.0001

ALA 261 PRO 262 0.0113

PRO 262 SER 263 -0.0002

SER 263 GLN 264 0.0004

GLN 264 THR 265 0.0096

THR 265 SER 266 -0.0003

SER 266 VAL 267 0.0001

VAL 267 ASP 268 0.0052

ASP 268 VAL 269 -0.0004

VAL 269 SER 270 0.0003

SER 270 LEU 271 -0.0087

LEU 271 ILE 272 0.0001

ILE 272 GLN 273 -0.0000

GLN 273 ASP 274 -0.0128

ASP 274 VAL 275 -0.0004

VAL 275 GLU 276 -0.0001

GLU 276 ARG 277 0.0098

ARG 277 ILE 278 -0.0002

ILE 278 LEU 279 0.0000

LEU 279 ASP 280 0.0020

ASP 280 TYR 281 0.0001

TYR 281 SER 282 -0.0000

SER 282 LEU 283 -0.0063

LEU 283 CYS 284 0.0002

CYS 284 GLN 285 0.0002

GLN 285 GLU 286 -0.0087

GLU 286 THR 287 0.0001

THR 287 TRP 288 0.0002

TRP 288 SER 289 -0.0063

SER 289 LYS 290 0.0001

LYS 290 ILE 291 0.0001

ILE 291 ARG 292 -0.0002

ARG 292 ALA 293 -0.0001

ALA 293 GLY 294 -0.0002

GLY 294 LEU 295 -0.0005

LEU 295 PRO 296 0.0002

PRO 296 ILE 297 0.0001

ILE 297 SER 298 -0.0030

SER 298 PRO 299 0.0003

PRO 299 VAL 300 -0.0004

VAL 300 ASP 301 -0.0031

ASP 301 LEU 302 -0.0002

LEU 302 SER 303 -0.0001

SER 303 TYR 304 -0.0002

TYR 304 LEU 305 0.0000

LEU 305 ALA 306 -0.0001

ALA 306 PRO 307 -0.0010

PRO 307 LYS 308 -0.0000

LYS 308 ASN 309 0.0000

ASN 309 PRO 310 -0.0025

PRO 310 GLY 311 0.0001

GLY 311 THR 312 -0.0004

THR 312 GLY 313 0.0018

GLY 313 PRO 314 -0.0001

PRO 314 ALA 315 -0.0003

ALA 315 PHE 316 -0.0001

PHE 316 THR 317 0.0005

THR 317 ILE 318 -0.0004

ILE 318 ILE 319 0.0008

ILE 319 ASN 320 0.0002

ASN 320 GLY 321 -0.0000

GLY 321 THR 322 -0.0011

THR 322 LEU 323 0.0001

LEU 323 LYS 324 -0.0002

LYS 324 TYR 325 -0.0019

TYR 325 PHE 326 0.0000

PHE 326 GLU 327 -0.0000

GLU 327 THR 328 -0.0004

THR 328 ARG 329 -0.0003

ARG 329 TYR 330 -0.0000

TYR 330 ILE 331 -0.0017

ILE 331 ARG 332 -0.0002

ARG 332 VAL 333 0.0004

VAL 333 ASP 334 0.0039

ASP 334 ILE 335 0.0001

ILE 335 ALA 336 -0.0004

ALA 336 ALA 337 0.0007

ALA 337 PRO 338 0.0001

PRO 338 ILE 339 0.0000

ILE 339 LEU 340 0.0004

LEU 340 SER 341 0.0002

SER 341 ARG 342 -0.0003

ARG 342 MET 343 0.0006

MET 343 VAL 344 0.0001

VAL 344 GLY 345 -0.0004

GLY 345 MET 346 0.0003

MET 346 ILE 347 -0.0003

ILE 347 SER 348 -0.0002

SER 348 GLY 349 0.0008

GLY 349 THR 350 -0.0002

THR 350 THR 351 0.0002

THR 351 THR 352 0.0022

THR 352 GLU 353 -0.0002

GLU 353 ARG 354 0.0000

ARG 354 GLU 355 0.0015

GLU 355 LEU 356 -0.0000

LEU 356 TRP 357 -0.0000

TRP 357 ASP 358 -0.0009

ASP 358 ASP 359 -0.0001

ASP 359 TRP 360 -0.0001

TRP 360 ALA 361 -0.0006

ALA 361 PRO 362 0.0002

PRO 362 TYR 363 0.0003

TYR 363 GLU 364 -0.0018

GLU 364 ASP 365 0.0002

ASP 365 VAL 366 0.0002

VAL 366 GLU 367 -0.0010

GLU 367 ILE 368 0.0002

ILE 368 GLY 369 0.0000

GLY 369 PRO 370 -0.0018

PRO 370 ASN 371 0.0001

ASN 371 GLY 372 -0.0001

GLY 372 VAL 373 -0.0011

VAL 373 LEU 374 -0.0001

LEU 374 ARG 375 0.0002

ARG 375 THR 376 -0.0003

THR 376 SER 377 -0.0001

SER 377 SER 378 0.0000

SER 378 GLY 379 -0.0004

GLY 379 TYR 380 0.0002

TYR 380 LYS 381 -0.0001

LYS 381 PHE 382 0.0025

PHE 382 PRO 383 -0.0002

PRO 383 LEU 384 0.0003

LEU 384 TYR 385 0.0064

TYR 385 MET 386 0.0002

MET 386 ILE 387 -0.0004

ILE 387 GLY 388 0.0111

GLY 388 HIS 389 0.0001

HIS 389 GLY 390 0.0002

GLY 390 MET 391 -0.0004

MET 391 LEU 392 0.0000

LEU 392 ASP 393 -0.0001

ASP 393 SER 394 0.0088

SER 394 ASP 395 -0.0000

ASP 395 LEU 396 -0.0000

LEU 396 HIS 397 0.0254

HIS 397 LEU 398 -0.0001

LEU 398 SER 399 0.0001

SER 399 SER 400 0.0153

SER 400 LYS 401 0.0002

LYS 401 ALA 402 -0.0001

ALA 402 GLN 403 -0.0093

GLN 403 VAL 404 -0.0002

VAL 404 PHE 405 0.0004

PHE 405 GLU 406 -0.0220

GLU 406 HIS 407 0.0000

HIS 407 PRO 408 -0.0002

PRO 408 HIS 409 0.0038

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.

*** 2CMZ ***

CA strain for 240228060628930665

--- normal mode 8 ---

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

* 2CMZ *