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

* *

CA strain for 2404101804023332396

--- 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
HIS 0 MET 1 0.0001

MET 1 LYS 2 -0.0078

LYS 2 ARG 3 -0.0000

ARG 3 LEU 4 -0.0016

LEU 4 THR 5 -0.0002

THR 5 TYR 6 0.0060

TYR 6 ILE 7 -0.0001

ILE 7 SER 8 0.0051

SER 8 LYS 9 -0.0000

LYS 9 PHE 10 -0.0108

PHE 10 SER 11 0.0001

SER 11 ARG 12 -0.0042

ARG 12 PRO 13 -0.0004

PRO 13 LEU 14 -0.0009

LEU 14 SER 15 -0.0001

SER 15 GLY 16 0.0070

GLY 16 ASP 17 -0.0002

ASP 17 GLU 18 0.0021

GLU 18 ILE 19 -0.0000

ILE 19 GLU 20 -0.0017

GLU 20 ALA 21 0.0000

ALA 21 ILE 22 -0.0014

ILE 22 GLY 23 0.0003

GLY 23 ARG 24 -0.0012

ARG 24 ARG 24 0.0612

ARG 24 ILE 25 0.0001

ILE 25 SER 26 0.0024

SER 26 SER 27 0.0001

SER 27 GLN 28 -0.0007

GLN 28 GLN 28 0.1436

GLN 28 LYS 29 0.0002

LYS 29 ASN 30 -0.0009

ASN 30 GLN 31 0.0000

GLN 31 GLN 32 -0.0007

GLN 32 ALA 33 0.0003

ALA 33 ASN 34 -0.0011

ASN 34 VAL 35 0.0000

VAL 35 THR 36 -0.0002

THR 36 GLY 37 -0.0000

GLY 37 VAL 38 0.0002

VAL 38 LEU 39 -0.0000

LEU 39 LEU 40 0.0023

LEU 40 CYS 41 0.0002

CYS 41 LEU 42 0.0053

LEU 42 ASP 43 0.0002

ASP 43 GLY 44 0.0042

GLY 44 ILE 45 -0.0002

ILE 45 PHE 46 0.0019

PHE 46 PHE 47 -0.0003

PHE 47 GLN 48 0.0011

GLN 48 ILE 49 -0.0003

ILE 49 LEU 50 -0.0020

LEU 50 GLU 51 0.0002

GLU 51 GLY 52 -0.0060

GLY 52 GLU 53 0.0002

GLU 53 ALA 54 0.0051

ALA 54 GLU 55 0.0001

GLU 55 LYS 56 0.0050

LYS 56 ILE 57 -0.0001

ILE 57 ASP 58 -0.0020

ASP 58 ARG 59 0.0002

ARG 59 ILE 60 0.0030

ILE 60 TYR 61 0.0002

TYR 61 GLU 62 -0.0019

GLU 62 ARG 63 0.0001

ARG 63 ILE 64 -0.0001

ILE 64 LEU 65 0.0002

LEU 65 ALA 66 0.0027

ALA 66 ASP 67 -0.0003

ASP 67 GLU 68 0.0086

GLU 68 ARG 69 -0.0002

ARG 69 HIS 70 -0.0093

HIS 70 THR 71 -0.0001

THR 71 ASP 72 -0.0184

ASP 72 ILE 73 0.0000

ILE 73 LEU 74 -0.0030

LEU 74 CYS 75 -0.0004

CYS 75 LEU 76 0.0167

LEU 76 LYS 77 -0.0001

LYS 77 SER 78 -0.0149

SER 78 GLU 79 -0.0000

GLU 79 VAL 80 -0.0033

VAL 80 GLU 81 -0.0000

GLU 81 VAL 82 0.0014

VAL 82 GLN 83 0.0002

GLN 83 GLU 84 -0.0021

GLU 84 ARG 85 -0.0003

ARG 85 MET 86 0.0021

MET 86 PHE 87 0.0001

PHE 87 PRO 88 0.0015

PRO 88 ASP 89 0.0001

ASP 89 TRP 90 -0.0018

TRP 90 SER 91 0.0001

SER 91 MET 92 0.0016

MET 92 GLN 93 -0.0000

GLN 93 THR 94 -0.0007

THR 94 ILE 95 0.0001

ILE 95 ASN 96 -0.0030

ASN 96 LEU 97 -0.0003

LEU 97 ASP 98 -0.0020

ASP 98 GLU 99 -0.0004

GLU 99 ASN 100 0.0066

ASN 100 THR 101 0.0000

THR 101 ASP 102 0.0041

ASP 102 PHE 103 -0.0003

PHE 103 LEU 104 0.0007

LEU 104 ILE 105 -0.0001

ILE 105 ARG 106 0.0001

ARG 106 PRO 107 0.0001

PRO 107 ILE 108 -0.0034

ILE 108 LYS 109 -0.0001

LYS 109 VAL 110 0.0014

VAL 110 LEU 111 -0.0000

LEU 111 LEU 112 -0.0056

LEU 112 GLN 113 -0.0003

GLN 113 THR 114 0.0032

THR 114 LEU 115 0.0003

LEU 115 THR 116 -0.0047

THR 116 GLU 117 -0.0002

GLU 117 SER 118 -0.0001

SER 118 HIS 119 0.0000

HIS 119 ARG 120 0.0019

ARG 120 ILE 121 0.0000

ILE 121 LEU 122 -0.0105

LEU 122 GLU 123 -0.0002

GLU 123 LYS 124 0.0185

LYS 124 TYR 125 -0.0000

TYR 125 THR 126 -0.0389

THR 126 GLN 127 0.0001

GLN 127 PRO 128 -0.0547

PRO 128 SER 129 -0.0000

SER 129 ILE 130 -0.0229

ILE 130 PHE 131 0.0001

PHE 131 LYS 132 0.0392

LYS 132 ILE 133 0.0000

ILE 133 ILE 134 0.0001

ILE 134 SER 135 -0.0000

SER 135 GLN 136 0.0286

GLN 136 GLY 137 -0.0002

GLY 137 THR 138 0.0955

THR 138 ASN 139 -0.0005

ASN 139 PRO 140 0.0141

PRO 140 LEU 141 0.0000

LEU 141 ASN 142 -0.0048

ASN 142 ILE 143 0.0005

ILE 143 ARG 144 0.0353

ARG 144 PRO 145 0.0003

PRO 145 LYS 146 -0.0181

LYS 146 ALA 147 -0.0002

ALA 147 VAL 148 -0.0128

VAL 148 VAL 148 0.0374

VAL 148 GLU 149 0.0002

GLU 149 LYS 150 0.0033

LYS 150 ILE 151 0.0001

ILE 151 VAL 152 0.0011

VAL 152 PHE 153 0.0002

PHE 153 PHE 154 0.0004

PHE 154 SER 155 0.0002

SER 155 ASP 156 0.0025

ASP 156 ILE 157 -0.0003

ILE 157 VAL 158 -0.0023

VAL 158 SER 159 0.0002

SER 159 PHE 160 -0.0018

PHE 160 SER 161 -0.0002

SER 161 THR 162 0.0003

THR 162 PHE 163 -0.0002

PHE 163 ALA 164 -0.0013

ALA 164 GLU 165 0.0003

GLU 165 LYS 166 -0.0001

LYS 166 LEU 167 0.0002

LEU 167 PRO 168 0.0006

PRO 168 VAL 169 -0.0004

VAL 169 GLU 170 0.0001

GLU 170 GLU 171 0.0002

GLU 171 VAL 172 0.0016

VAL 172 VAL 173 -0.0000

VAL 173 SER 174 -0.0001

SER 174 VAL 175 -0.0002

VAL 175 VAL 176 0.0020

VAL 176 ASN 177 0.0001

ASN 177 SER 178 0.0028

SER 178 TYR 179 -0.0000

TYR 179 PHE 180 -0.0018

PHE 180 SER 181 0.0004

SER 181 VAL 182 0.0077

VAL 182 CYS 183 -0.0004

CYS 183 THR 184 -0.0029

THR 184 ALA 185 0.0000

ALA 185 ILE 186 0.0037

ILE 186 ILE 187 0.0002

ILE 187 THR 188 0.0033

THR 188 ARG 189 -0.0001

ARG 189 GLN 190 0.0020

GLN 190 GLY 191 0.0003

GLY 191 GLY 192 0.0109

GLY 192 GLU 193 -0.0003

GLU 193 VAL 194 -0.0019

VAL 194 THR 195 0.0001

THR 195 LYS 196 -0.0121

LYS 196 PHE 197 -0.0001

PHE 197 ILE 198 -0.0183

ILE 198 GLY 199 -0.0001

GLY 199 ASP 200 0.0036

ASP 200 CYS 201 0.0002

CYS 201 VAL 202 -0.0020

VAL 202 MET 203 -0.0002

MET 203 ALA 204 0.0005

ALA 204 TYR 205 -0.0000

TYR 205 PHE 206 0.0064

PHE 206 ASP 207 0.0005

ASP 207 GLY 208 0.0066

GLY 208 ASP 209 0.0001

ASP 209 CYS 210 -0.0023

CYS 210 ALA 211 -0.0001

ALA 211 ASP 212 -0.0037

ASP 212 GLN 213 0.0001

GLN 213 ALA 214 0.0021

ALA 214 ILE 215 -0.0003

ILE 215 GLN 216 0.0004

GLN 216 ALA 217 0.0004

ALA 217 SER 218 0.0003

SER 218 LEU 219 0.0000

LEU 219 ASP 220 0.0028

ASP 220 ILE 221 -0.0002

ILE 221 LEU 222 -0.0023

LEU 222 MET 223 -0.0003

MET 223 MET 223 -0.0871

MET 223 GLU 224 0.0027

GLU 224 LEU 225 -0.0001

LEU 225 GLU 226 0.0018

GLU 226 ILE 227 0.0002

ILE 227 LEU 228 0.0017

LEU 228 ARG 229 0.0001

ARG 229 ASN 230 0.0025

ASN 230 SER 231 -0.0001

SER 231 ALA 232 0.0002

ALA 232 PRO 233 0.0002

PRO 233 GLU 234 -0.0021

GLU 234 GLY 235 -0.0001

GLY 235 SER 236 0.0012

SER 236 PRO 237 -0.0000

PRO 237 LEU 238 -0.0019

LEU 238 ARG 239 0.0002

ARG 239 VAL 240 0.0020

VAL 240 LEU 241 0.0001

LEU 241 TYR 242 0.0010

TYR 242 SER 243 0.0002

SER 243 GLY 244 0.0047

GLY 244 ILE 245 -0.0001

ILE 245 GLY 246 0.0034

GLY 246 LEU 247 0.0000

LEU 247 ALA 248 0.0044

ALA 248 LYS 249 -0.0003

LYS 249 GLY 250 0.0221

GLY 250 LYS 251 0.0001

LYS 251 VAL 252 0.0014

VAL 252 ILE 253 -0.0003

ILE 253 GLU 254 0.0218

GLU 254 GLY 255 -0.0001

GLY 255 ASN 256 -0.0494

ASN 256 ILE 257 0.0000

ILE 257 GLY 258 -0.0192

GLY 258 SER 259 0.0000

SER 259 GLU 260 0.0015

GLU 260 LEU 261 0.0004

LEU 261 LYS 262 0.0017

LYS 262 ARG 263 -0.0004

ARG 263 ASP 264 0.0214

ASP 264 TYR 265 0.0001

TYR 265 THR 266 -0.0021

THR 266 ILE 267 0.0002

ILE 267 LEU 268 0.0358

LEU 268 GLY 269 0.0001

GLY 269 ASP 270 0.0340

ASP 270 ALA 271 -0.0002

ALA 271 VAL 272 0.0051

VAL 272 ASN 273 -0.0003

ASN 273 VAL 274 -0.0066

VAL 274 ALA 275 0.0001

ALA 275 ALA 276 -0.0093

ALA 276 ARG 277 0.0004

ARG 277 LEU 278 0.0013

LEU 278 GLU 279 -0.0004

GLU 279 ALA 280 -0.0088

ALA 280 LEU 281 -0.0002

LEU 281 THR 282 0.0007

THR 282 ARG 283 0.0001

ARG 283 GLN 284 -0.0037

GLN 284 LEU 285 -0.0002

LEU 285 SER 286 0.0019

SER 286 GLN 287 0.0001

GLN 287 ALA 288 -0.0016

ALA 288 LEU 289 -0.0004

LEU 289 VAL 290 0.0017

VAL 290 PHE 291 0.0006

PHE 291 SER 292 0.0004

SER 292 SER 293 0.0002

SER 293 GLU 294 -0.0021

GLU 294 VAL 295 0.0000

VAL 295 LYS 296 -0.0021

LYS 296 ASN 297 -0.0000

ASN 297 SER 298 -0.0008

SER 298 ALA 299 0.0002

ALA 299 THR 300 -0.0005

THR 300 LYS 301 0.0000

LYS 301 SER 302 -0.0009

SER 302 TRP 303 0.0004

TRP 303 ASN 304 -0.0005

ASN 304 PHE 305 -0.0003

PHE 305 ILE 306 0.0010

ILE 306 TRP 307 0.0002

TRP 307 LEU 308 0.0001

LEU 308 THR 309 0.0000

THR 309 ASP 310 0.0013

ASP 310 SER 311 0.0000

SER 311 GLU 312 0.0040

GLU 312 LEU 313 -0.0003

LEU 313 LYS 314 0.0044

LYS 314 GLY 315 0.0001

GLY 315 LYS 316 -0.0024

LYS 316 SER 317 0.0001

SER 317 GLU 318 -0.0000

GLU 318 SER 319 0.0003

SER 319 ILE 320 -0.0000

ILE 320 ASP 321 -0.0003

ASP 321 ILE 322 0.0001

ILE 322 TYR 323 0.0001

TYR 323 SER 324 0.0002

SER 324 ILE 325 -0.0002

ILE 325 ASP 326 -0.0014

ASP 326 ASN 327 0.0002

ASN 327 GLU 328 -0.0013

GLU 328 MET 329 0.0000

MET 329 THR 330 0.0017

THR 330 ARG 331 -0.0003

ARG 331 LYS 332 -0.0053

LYS 332 SER 333 -0.0002

SER 333 SER 334 0.0008

SER 334 GLY 336 -0.0002

GLY 336 LEU 337 0.0000

LEU 337 GLU 338 0.0021

GLU 338 ILE 339 -0.0001

ILE 339 ALA 340 -0.0011

ALA 340 ARG 341 0.0001

ARG 341 ASN 342 -0.0010

ASN 342 ILE 343 0.0000

ILE 343 GLY 344 -0.0000

GLY 344 HIS 345 0.0001

HIS 345 TYR 346 -0.0012

TYR 346 LEU 347 0.0000

LEU 347 GLU 348 -0.0014

GLU 348 ARG 349 -0.0001

ARG 349 VAL 350 -0.0001

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 2404101804023332396

--- normal mode 8 ---

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

* *