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

* *

CA strain for 2406061503071366589

--- normal mode 13 ---

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 0.0011

ALA 3 SER 4 0.0002

SER 4 PRO 5 0.0246

PRO 5 ARG 6 0.0003

ARG 6 ALA 7 -0.0294

ALA 7 PRO 8 -0.0001

PRO 8 HIS 9 0.0010

HIS 9 GLN 10 -0.0004

GLN 10 GLU 11 -0.0017

GLU 11 HIS 12 0.0004

HIS 12 VAL 13 0.0043

VAL 13 LEU 14 -0.0002

LEU 14 GLY 15 -0.0005

GLY 15 GLU 16 0.0001

GLU 16 PRO 17 -0.0003

PRO 17 THR 18 0.0001

THR 18 LEU 19 0.0005

LEU 19 GLU 20 0.0003

GLU 20 GLY 21 0.0004

GLY 21 LEU 22 0.0001

LEU 22 ALA 23 0.0007

ALA 23 HIS 24 0.0002

HIS 24 TYR 25 -0.0000

TYR 25 ILE 26 0.0005

ILE 26 ARG 27 -0.0001

ARG 27 GLU 28 -0.0003

GLU 28 LYS 29 0.0002

LYS 29 ASN 30 -0.0001

ASN 30 VAL 31 -0.0000

VAL 31 ARG 32 0.0003

ARG 32 ARG 33 0.0007

ARG 33 ILE 34 -0.0001

ILE 34 LEU 35 -0.0006

LEU 35 VAL 36 0.0001

VAL 36 LEU 37 -0.0010

LEU 37 VAL 38 -0.0002

VAL 38 GLY 39 -0.0001

GLY 39 ALA 40 -0.0002

ALA 40 GLY 41 0.0005

GLY 41 ALA 42 -0.0003

ALA 42 SER 43 0.0000

SER 43 VAL 44 0.0000

VAL 44 ALA 45 0.0004

ALA 45 ALA 46 -0.0000

ALA 46 GLY 47 0.0003

GLY 47 ILE 48 -0.0002

ILE 48 PRO 49 0.0000

PRO 49 ASP 50 -0.0001

ASP 50 PHE 51 -0.0006

PHE 51 ARG 52 0.0004

ARG 52 SER 53 -0.0010

SER 53 PRO 54 0.0000

PRO 54 ASP 55 0.0004

ASP 55 THR 56 0.0003

THR 56 GLY 57 -0.0004

GLY 57 ILE 58 0.0001

ILE 58 TYR 59 -0.0001

TYR 59 ALA 60 -0.0002

ALA 60 LEU 61 0.0000

LEU 61 GLY 62 -0.0002

GLY 62 LYS 63 0.0004

LYS 63 TYR 64 -0.0001

TYR 64 ASN 65 -0.0001

ASN 65 LEU 66 0.0000

LEU 66 GLU 67 -0.0008

GLU 67 ASP 68 -0.0002

ASP 68 PRO 69 0.0010

PRO 69 THR 70 -0.0001

THR 70 ASP 71 -0.0010

ASP 71 ALA 72 0.0000

ALA 72 PHE 73 0.0005

PHE 73 SER 74 -0.0003

SER 74 LEU 75 0.0008

LEU 75 THR 76 -0.0002

THR 76 LEU 77 -0.0000

LEU 77 LEU 78 -0.0004

LEU 78 ARG 79 0.0005

ARG 79 GLU 80 0.0000

GLU 80 LYS 81 -0.0001

LYS 81 PRO 82 -0.0001

PRO 82 GLU 83 0.0001

GLU 83 ILE 84 0.0002

ILE 84 PHE 85 0.0005

PHE 85 TYR 86 0.0002

TYR 86 SER 87 0.0002

SER 87 ILE 88 0.0001

ILE 88 ALA 89 0.0000

ALA 89 ARG 90 0.0001

ARG 90 GLU 91 -0.0008

GLU 91 LEU 92 0.0003

LEU 92 ASN 93 -0.0003

ASN 93 LEU 94 0.0002

LEU 94 TRP 95 -0.0004

TRP 95 PRO 96 0.0001

PRO 96 GLY 97 0.0008

GLY 97 HIS 98 0.0001

HIS 98 PHE 99 -0.0001

PHE 99 GLN 100 -0.0001

GLN 100 PRO 101 0.0008

PRO 101 THR 102 0.0000

THR 102 ALA 103 0.0000

ALA 103 VAL 104 0.0001

VAL 104 HIS 105 0.0003

HIS 105 HIS 106 0.0004

HIS 106 PHE 107 0.0001

PHE 107 ILE 108 -0.0002

ILE 108 ARG 109 -0.0005

ARG 109 LEU 110 -0.0000

LEU 110 LEU 111 0.0006

LEU 111 GLN 112 -0.0000

GLN 112 ASP 113 0.0001

ASP 113 GLU 114 -0.0003

GLU 114 GLY 115 0.0001

GLY 115 ARG 116 0.0003

ARG 116 LEU 117 0.0001

LEU 117 LEU 118 -0.0001

LEU 118 ARG 119 -0.0006

ARG 119 CYS 120 -0.0000

CYS 120 CYS 121 -0.0012

CYS 121 THR 122 0.0004

THR 122 GLN 123 -0.0008

GLN 123 ASN 124 0.0004

ASN 124 ILE 125 -0.0004

ILE 125 ASP 126 0.0002

ASP 126 GLY 127 0.0005

GLY 127 LEU 128 0.0004

LEU 128 GLU 129 0.0015

GLU 129 LYS 130 -0.0002

LYS 130 ALA 131 0.0001

ALA 131 ALA 132 0.0003

ALA 132 GLY 133 0.0005

GLY 133 VAL 134 0.0001

VAL 134 SER 135 -0.0006

SER 135 PRO 136 0.0002

PRO 136 GLU 137 0.0004

GLU 137 LEU 138 -0.0001

LEU 138 LEU 139 -0.0001

LEU 139 VAL 140 -0.0000

VAL 140 GLU 141 0.0010

GLU 141 ALA 142 0.0002

ALA 142 HIS 143 0.0014

HIS 143 GLY 144 0.0001

GLY 144 SER 145 0.0016

SER 145 PHE 146 0.0001

PHE 146 ALA 147 -0.0003

ALA 147 ALA 148 -0.0001

ALA 148 ALA 149 -0.0004

ALA 149 ALA 150 0.0001

ALA 150 CYS 151 0.0001

CYS 151 ILE 152 -0.0004

ILE 152 GLU 153 0.0001

GLU 153 CYS 154 0.0001

CYS 154 HIS 155 -0.0002

HIS 155 THR 156 -0.0001

THR 156 PRO 157 0.0000

PRO 157 PHE 158 0.0000

PHE 158 SER 159 0.0005

SER 159 ILE 160 0.0003

ILE 160 GLU 161 0.0020

GLU 161 GLN 162 -0.0001

GLN 162 ASN 163 -0.0008

ASN 163 TYR 164 -0.0003

TYR 164 LEU 165 0.0008

LEU 165 GLU 166 -0.0002

GLU 166 ALA 167 -0.0006

ALA 167 MET 168 -0.0001

MET 168 SER 169 0.0001

SER 169 GLY 170 0.0002

GLY 170 THR 171 0.0001

THR 171 VAL 172 0.0001

VAL 172 SER 173 0.0001

SER 173 ARG 174 -0.0001

ARG 174 CYS 175 -0.0001

CYS 175 SER 176 -0.0000

SER 176 THR 177 0.0003

THR 177 CYS 178 0.0003

CYS 178 GLY 179 -0.0001

GLY 179 GLY 180 0.0001

GLY 180 ILE 181 0.0002

ILE 181 VAL 182 -0.0001

VAL 182 LYS 183 0.0003

LYS 183 PRO 184 0.0001

PRO 184 ASN 185 0.0012

ASN 185 VAL 186 0.0002

VAL 186 VAL 187 -0.0008

VAL 187 PHE 188 -0.0003

PHE 188 PHE 189 -0.0028

PHE 189 GLY 190 -0.0002

GLY 190 GLU 191 0.0000

GLU 191 ASN 192 -0.0002

ASN 192 LEU 193 -0.0003

LEU 193 PRO 194 0.0001

PRO 194 ASP 195 0.0020

ASP 195 ALA 196 -0.0004

ALA 196 PHE 197 -0.0017

PHE 197 PHE 198 0.0001

PHE 198 ASP 199 -0.0059

ASP 199 ALA 200 0.0005

ALA 200 LEU 201 -0.0004

LEU 201 HIS 202 0.0004

HIS 202 HIS 203 0.0076

HIS 203 ASP 204 0.0001

ASP 204 ALA 205 -0.0020

ALA 205 PRO 206 0.0000

PRO 206 ILE 207 0.0025

ILE 207 ALA 208 0.0001

ALA 208 GLU 209 0.0006

GLU 209 LEU 210 0.0001

LEU 210 VAL 211 -0.0001

VAL 211 ILE 212 -0.0000

ILE 212 ILE 213 -0.0004

ILE 213 ILE 214 -0.0002

ILE 214 GLY 215 -0.0002

GLY 215 THR 216 0.0004

THR 216 SER 217 -0.0012

SER 217 MET 218 -0.0003

MET 218 GLN 219 -0.0002

GLN 219 VAL 220 -0.0001

VAL 220 HIS 221 0.0006

HIS 221 PRO 222 -0.0000

PRO 222 PHE 223 -0.0016

PHE 223 ALA 224 0.0002

ALA 224 LEU 225 -0.0025

LEU 225 LEU 226 -0.0001

LEU 226 PRO 227 -0.0007

PRO 227 CYS 228 0.0000

CYS 228 VAL 229 -0.0036

VAL 229 VAL 230 0.0002

VAL 230 PRO 231 -0.0015

PRO 231 LYS 232 0.0001

LYS 232 SER 233 0.0023

SER 233 VAL 234 -0.0005

VAL 234 PRO 235 -0.0003

PRO 235 ARG 236 -0.0003

ARG 236 VAL 237 -0.0009

VAL 237 VAL 238 -0.0001

VAL 238 MET 239 -0.0002

MET 239 ASN 240 0.0001

ASN 240 ARG 241 0.0001

ARG 241 GLU 242 0.0004

GLU 242 ARG 243 0.0008

ARG 243 VAL 244 0.0003

VAL 244 GLY 245 -0.0012

GLY 245 GLY 246 -0.0001

GLY 246 LEU 247 -0.0064

LEU 247 LEU 248 0.0003

LEU 248 PHE 249 0.0001

PHE 249 ARG 250 -0.0001

ARG 250 PHE 251 0.0015

PHE 251 PRO 252 0.0000

PRO 252 ASP 253 -0.0009

ASP 253 ASP 254 -0.0001

ASP 254 PRO 255 0.0039

PRO 255 LEU 256 -0.0001

LEU 256 ASN 257 0.0062

ASN 257 THR 258 -0.0002

THR 258 VAL 259 0.0019

VAL 259 HIS 260 -0.0002

HIS 260 GLU 261 0.0023

GLU 261 ASP 262 -0.0001

ASP 262 ALA 263 0.0106

ALA 263 VAL 264 -0.0000

VAL 264 ALA 265 0.0083

ALA 265 LYS 266 0.0000

LYS 266 GLU 267 -0.0123

GLU 267 GLY 268 -0.0002

GLY 268 ARG 269 0.0189

ARG 269 SER 270 0.0002

SER 270 SER 271 -0.0260

SER 271 SER 272 -0.0001

SER 272 SER 273 0.0526

SER 273 GLN 274 0.0000

GLN 274 SER 275 0.0437

SER 275 ARG 276 0.0002

ARG 276 SER 277 0.0113

SER 277 PRO 278 -0.0000

PRO 278 SER 279 0.0091

SER 279 ALA 280 -0.0002

ALA 280 SER 281 0.0426

SER 281 PRO 282 -0.0002

PRO 282 ARG 283 0.1844

ARG 283 ARG 284 0.0000

ARG 284 GLU 285 0.0137

GLU 285 GLU 286 -0.0000

GLU 286 GLY 287 0.0532

GLY 287 GLY 288 -0.0002

GLY 288 THR 289 0.1978

THR 289 GLU 290 -0.0001

GLU 290 ASP 291 0.0031

ASP 291 SER 292 0.0001

SER 292 PRO 293 0.0070

PRO 293 SER 294 -0.0004

SER 294 SER 295 0.0088

SER 295 PRO 296 -0.0000

PRO 296 ASN 297 0.0009

ASN 297 GLU 298 -0.0001

GLU 298 GLU 299 -0.0088

GLU 299 VAL 300 0.0003

VAL 300 GLU 301 -0.0115

GLU 301 GLU 302 0.0003

GLU 302 ALA 303 0.0445

ALA 303 SER 304 0.0000

SER 304 THR 305 0.0196

THR 305 SER 306 0.0003

SER 306 SER 307 -0.0062

SER 307 SER 308 0.0000

SER 308 SER 309 0.0004

SER 309 ASP 310 -0.0001

ASP 310 GLY 311 0.0018

GLY 311 TYR 312 0.0000

TYR 312 GLY 313 -0.0084

GLY 313 GLN 314 -0.0001

GLN 314 TYR 315 0.0083

TYR 315 GLY 316 -0.0000

GLY 316 ASP 317 0.0080

ASP 317 TYR 318 -0.0001

TYR 318 HIS 319 0.0092

HIS 319 ALA 320 -0.0000

ALA 320 HIS 321 -0.0009

HIS 321 PRO 322 -0.0000

PRO 322 ASP 323 -0.0034

ASP 323 VAL 324 0.0003

VAL 324 CYS 325 0.0009

CYS 325 ARG 326 -0.0003

ARG 326 ASP 327 -0.0007

ASP 327 VAL 328 -0.0003

VAL 328 LEU 329 -0.0011

LEU 329 PHE 330 -0.0001

PHE 330 ARG 331 -0.0007

ARG 331 GLY 332 0.0001

GLY 332 ASP 333 0.0017

ASP 333 CYS 334 -0.0001

CYS 334 GLN 335 0.0000

GLN 335 GLU 336 0.0003

GLU 336 ASN 337 0.0001

ASN 337 VAL 338 0.0000

VAL 338 VAL 339 -0.0003

VAL 339 THR 340 0.0001

THR 340 LEU 341 -0.0001

LEU 341 ALA 342 0.0001

ALA 342 GLU 343 0.0003

GLU 343 TYR 344 -0.0001

TYR 344 LEU 345 0.0004

LEU 345 GLY 346 0.0001

GLY 346 LEU 347 0.0003

LEU 347 SER 348 -0.0004

SER 348 GLU 349 0.0005

GLU 349 ALA 350 -0.0000

ALA 350 LEU 351 -0.0003

LEU 351 ALA 352 -0.0002

ALA 352 LYS 353 0.0004

LYS 353 ARG 354 0.0001

ARG 354 MET 355 -0.0001

MET 355 ARG 356 0.0001

ARG 356 LEU 357 -0.0004

LEU 357 SER 358 -0.0001

SER 358 ASP 359 0.0004

ASP 359 ALA 360 -0.0001

ALA 360 ALA 361 0.0000

ALA 361 PRO 362 0.0002

PRO 362 ALA 363 -0.0002

ALA 363 THR 364 0.0002

THR 364 ALA 365 -0.0008

ALA 365 GLN 366 -0.0000

GLN 366 ARG 367 0.0028

ARG 367 ALA 368 0.0002

ALA 368 PRO 369 0.0015

PRO 369 ASN 370 -0.0003

ASN 370 GLU 371 0.0010

GLU 371 THR 372 0.0000

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.

*** ***

CA strain for 2406061503071366589

--- normal mode 13 ---

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

* *