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

* *

CA strain for 2404101804023332396

--- normal mode 9 ---

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 0.0000

MET 1 LYS 2 0.0007

LYS 2 ARG 3 -0.0002

ARG 3 LEU 4 -0.0139

LEU 4 THR 5 0.0000

THR 5 TYR 6 -0.0029

TYR 6 ILE 7 -0.0003

ILE 7 SER 8 0.0094

SER 8 LYS 9 0.0000

LYS 9 PHE 10 -0.0008

PHE 10 SER 11 0.0001

SER 11 ARG 12 -0.0005

ARG 12 PRO 13 0.0002

PRO 13 LEU 14 0.0009

LEU 14 SER 15 0.0001

SER 15 GLY 16 -0.0079

GLY 16 ASP 17 -0.0002

ASP 17 GLU 18 -0.0035

GLU 18 ILE 19 0.0000

ILE 19 GLU 20 -0.0019

GLU 20 ALA 21 0.0001

ALA 21 ILE 22 0.0001

ILE 22 GLY 23 0.0001

GLY 23 ARG 24 0.0005

ARG 24 ARG 24 0.0566

ARG 24 ILE 25 0.0000

ILE 25 SER 26 -0.0021

SER 26 SER 27 0.0001

SER 27 GLN 28 0.0007

GLN 28 GLN 28 0.0742

GLN 28 LYS 29 -0.0001

LYS 29 ASN 30 0.0010

ASN 30 GLN 31 -0.0002

GLN 31 GLN 32 0.0002

GLN 32 ALA 33 0.0005

ALA 33 ASN 34 0.0002

ASN 34 VAL 35 -0.0002

VAL 35 THR 36 -0.0014

THR 36 GLY 37 -0.0002

GLY 37 VAL 38 0.0033

VAL 38 LEU 39 -0.0000

LEU 39 LEU 40 -0.0006

LEU 40 CYS 41 -0.0001

CYS 41 LEU 42 -0.0040

LEU 42 ASP 43 0.0001

ASP 43 GLY 44 -0.0056

GLY 44 ILE 45 -0.0001

ILE 45 PHE 46 -0.0020

PHE 46 PHE 47 -0.0003

PHE 47 GLN 48 0.0006

GLN 48 ILE 49 0.0001

ILE 49 LEU 50 0.0008

LEU 50 GLU 51 -0.0000

GLU 51 GLY 52 0.0019

GLY 52 GLU 53 -0.0001

GLU 53 ALA 54 -0.0030

ALA 54 GLU 55 -0.0001

GLU 55 LYS 56 -0.0040

LYS 56 ILE 57 0.0004

ILE 57 ASP 58 0.0005

ASP 58 ARG 59 0.0002

ARG 59 ILE 60 -0.0036

ILE 60 TYR 61 -0.0000

TYR 61 GLU 62 0.0027

GLU 62 ARG 63 -0.0001

ARG 63 ILE 64 -0.0005

ILE 64 LEU 65 0.0001

LEU 65 ALA 66 -0.0033

ALA 66 ASP 67 -0.0003

ASP 67 GLU 68 -0.0052

GLU 68 ARG 69 0.0003

ARG 69 HIS 70 0.0026

HIS 70 THR 71 -0.0002

THR 71 ASP 72 0.0009

ASP 72 ILE 73 0.0001

ILE 73 LEU 74 -0.0077

LEU 74 CYS 75 -0.0001

CYS 75 LEU 76 -0.0123

LEU 76 LYS 77 -0.0000

LYS 77 SER 78 0.0033

SER 78 GLU 79 -0.0001

GLU 79 VAL 80 -0.0134

VAL 80 GLU 81 -0.0001

GLU 81 VAL 82 0.0042

VAL 82 GLN 83 0.0000

GLN 83 GLU 84 0.0051

GLU 84 ARG 85 0.0002

ARG 85 MET 86 -0.0031

MET 86 PHE 87 -0.0001

PHE 87 PRO 88 -0.0027

PRO 88 ASP 89 0.0002

ASP 89 TRP 90 0.0015

TRP 90 SER 91 -0.0002

SER 91 MET 92 -0.0025

MET 92 GLN 93 0.0005

GLN 93 THR 94 0.0050

THR 94 ILE 95 -0.0002

ILE 95 ASN 96 0.0082

ASN 96 LEU 97 -0.0001

LEU 97 ASP 98 0.0059

ASP 98 GLU 99 0.0005

GLU 99 ASN 100 -0.0105

ASN 100 THR 101 -0.0004

THR 101 ASP 102 -0.0071

ASP 102 PHE 103 -0.0001

PHE 103 LEU 104 -0.0015

LEU 104 ILE 105 0.0002

ILE 105 ARG 106 0.0001

ARG 106 PRO 107 0.0003

PRO 107 ILE 108 0.0038

ILE 108 LYS 109 0.0002

LYS 109 VAL 110 0.0015

VAL 110 LEU 111 -0.0001

LEU 111 LEU 112 0.0066

LEU 112 GLN 113 0.0001

GLN 113 THR 114 0.0035

THR 114 LEU 115 -0.0003

LEU 115 THR 116 0.0035

THR 116 GLU 117 -0.0002

GLU 117 SER 118 0.0040

SER 118 HIS 119 0.0001

HIS 119 ARG 120 0.0079

ARG 120 ILE 121 -0.0002

ILE 121 LEU 122 0.0016

LEU 122 GLU 123 0.0002

GLU 123 LYS 124 0.0020

LYS 124 TYR 125 0.0002

TYR 125 THR 126 0.0016

THR 126 GLN 127 0.0005

GLN 127 PRO 128 -0.0103

PRO 128 SER 129 -0.0003

SER 129 ILE 130 0.0403

ILE 130 PHE 131 -0.0001

PHE 131 LYS 132 0.0032

LYS 132 ILE 133 -0.0004

ILE 133 ILE 134 0.0766

ILE 134 SER 135 0.0001

SER 135 GLN 136 -0.0353

GLN 136 GLY 137 -0.0001

GLY 137 THR 138 0.0403

THR 138 ASN 139 -0.0000

ASN 139 PRO 140 0.0171

PRO 140 LEU 141 0.0004

LEU 141 ASN 142 -0.0027

ASN 142 ILE 143 -0.0000

ILE 143 ARG 144 0.0144

ARG 144 PRO 145 -0.0000

PRO 145 LYS 146 -0.0001

LYS 146 ALA 147 0.0001

ALA 147 VAL 148 -0.0053

VAL 148 VAL 148 -0.0226

VAL 148 GLU 149 -0.0000

GLU 149 LYS 150 -0.0139

LYS 150 ILE 151 0.0001

ILE 151 VAL 152 -0.0018

VAL 152 PHE 153 -0.0000

PHE 153 PHE 154 0.0102

PHE 154 SER 155 -0.0003

SER 155 ASP 156 0.0054

ASP 156 ILE 157 0.0001

ILE 157 VAL 158 -0.0103

VAL 158 SER 159 -0.0003

SER 159 PHE 160 -0.0049

PHE 160 SER 161 -0.0000

SER 161 THR 162 -0.0058

THR 162 PHE 163 -0.0003

PHE 163 ALA 164 0.0008

ALA 164 GLU 165 0.0001

GLU 165 LYS 166 -0.0005

LYS 166 LEU 167 0.0004

LEU 167 PRO 168 0.0022

PRO 168 VAL 169 -0.0001

VAL 169 GLU 170 0.0001

GLU 170 GLU 171 -0.0004

GLU 171 VAL 172 0.0013

VAL 172 VAL 173 -0.0000

VAL 173 SER 174 0.0020

SER 174 VAL 175 0.0000

VAL 175 VAL 176 -0.0039

VAL 176 ASN 177 0.0003

ASN 177 SER 178 0.0026

SER 178 TYR 179 0.0000

TYR 179 PHE 180 -0.0097

PHE 180 SER 181 -0.0002

SER 181 VAL 182 0.0066

VAL 182 CYS 183 0.0002

CYS 183 THR 184 -0.0032

THR 184 ALA 185 -0.0001

ALA 185 ILE 186 0.0021

ILE 186 ILE 187 -0.0002

ILE 187 THR 188 0.0039

THR 188 ARG 189 0.0001

ARG 189 GLN 190 -0.0014

GLN 190 GLY 191 0.0001

GLY 191 GLY 192 0.0002

GLY 192 GLU 193 -0.0001

GLU 193 VAL 194 -0.0012

VAL 194 THR 195 -0.0000

THR 195 LYS 196 0.0008

LYS 196 PHE 197 0.0004

PHE 197 ILE 198 -0.0161

ILE 198 GLY 199 -0.0003

GLY 199 ASP 200 -0.0011

ASP 200 CYS 201 0.0003

CYS 201 VAL 202 -0.0027

VAL 202 MET 203 -0.0002

MET 203 ALA 204 0.0139

ALA 204 TYR 205 0.0001

TYR 205 PHE 206 0.0049

PHE 206 ASP 207 0.0004

ASP 207 GLY 208 -0.0024

GLY 208 ASP 209 -0.0004

ASP 209 CYS 210 -0.0038

CYS 210 ALA 211 0.0001

ALA 211 ASP 212 0.0001

ASP 212 GLN 213 0.0001

GLN 213 ALA 214 0.0005

ALA 214 ILE 215 0.0003

ILE 215 GLN 216 0.0005

GLN 216 ALA 217 -0.0000

ALA 217 SER 218 0.0017

SER 218 LEU 219 0.0000

LEU 219 ASP 220 0.0016

ASP 220 ILE 221 -0.0001

ILE 221 LEU 222 -0.0027

LEU 222 MET 223 -0.0001

MET 223 MET 223 -0.1531

MET 223 GLU 224 0.0025

GLU 224 LEU 225 0.0002

LEU 225 GLU 226 -0.0020

GLU 226 ILE 227 -0.0004

ILE 227 LEU 228 0.0028

LEU 228 ARG 229 -0.0002

ARG 229 ASN 230 0.0003

ASN 230 SER 231 0.0000

SER 231 ALA 232 0.0002

ALA 232 PRO 233 -0.0004

PRO 233 GLU 234 -0.0016

GLU 234 GLY 235 0.0000

GLY 235 SER 236 -0.0010

SER 236 PRO 237 -0.0000

PRO 237 LEU 238 -0.0012

LEU 238 ARG 239 0.0000

ARG 239 VAL 240 0.0012

VAL 240 LEU 241 0.0001

LEU 241 TYR 242 0.0047

TYR 242 SER 243 -0.0001

SER 243 GLY 244 0.0116

GLY 244 ILE 245 -0.0001

ILE 245 GLY 246 0.0159

GLY 246 LEU 247 0.0001

LEU 247 ALA 248 0.0214

ALA 248 LYS 249 0.0002

LYS 249 GLY 250 0.0197

GLY 250 LYS 251 -0.0000

LYS 251 VAL 252 0.0038

VAL 252 ILE 253 0.0004

ILE 253 GLU 254 0.0227

GLU 254 GLY 255 0.0002

GLY 255 ASN 256 0.0122

ASN 256 ILE 257 0.0000

ILE 257 GLY 258 -0.0173

GLY 258 SER 259 0.0002

SER 259 GLU 260 -0.0002

GLU 260 LEU 261 -0.0000

LEU 261 LYS 262 0.0025

LYS 262 ARG 263 0.0000

ARG 263 ASP 264 0.0192

ASP 264 TYR 265 -0.0003

TYR 265 THR 266 0.0134

THR 266 ILE 267 0.0000

ILE 267 LEU 268 -0.0114

LEU 268 GLY 269 -0.0001

GLY 269 ASP 270 0.0174

ASP 270 ALA 271 0.0000

ALA 271 VAL 272 0.0020

VAL 272 ASN 273 -0.0002

ASN 273 VAL 274 0.0001

VAL 274 ALA 275 -0.0004

ALA 275 ALA 276 -0.0070

ALA 276 ARG 277 0.0001

ARG 277 LEU 278 0.0026

LEU 278 GLU 279 -0.0002

GLU 279 ALA 280 -0.0088

ALA 280 LEU 281 0.0002

LEU 281 THR 282 0.0028

THR 282 ARG 283 -0.0002

ARG 283 GLN 284 -0.0008

GLN 284 LEU 285 -0.0002

LEU 285 SER 286 0.0074

SER 286 GLN 287 -0.0000

GLN 287 ALA 288 -0.0042

ALA 288 LEU 289 0.0001

LEU 289 VAL 290 0.0050

VAL 290 PHE 291 -0.0002

PHE 291 SER 292 0.0047

SER 292 SER 293 -0.0003

SER 293 GLU 294 0.0181

GLU 294 VAL 295 -0.0001

VAL 295 LYS 296 0.0026

LYS 296 ASN 297 0.0002

ASN 297 SER 298 0.0081

SER 298 ALA 299 0.0000

ALA 299 THR 300 0.0003

THR 300 LYS 301 0.0000

LYS 301 SER 302 0.0006

SER 302 TRP 303 0.0002

TRP 303 ASN 304 -0.0004

ASN 304 PHE 305 0.0004

PHE 305 ILE 306 -0.0017

ILE 306 TRP 307 -0.0001

TRP 307 LEU 308 -0.0003

LEU 308 THR 309 0.0003

THR 309 ASP 310 -0.0019

ASP 310 SER 311 -0.0001

SER 311 GLU 312 -0.0019

GLU 312 LEU 313 -0.0003

LEU 313 LYS 314 0.0033

LYS 314 GLY 315 -0.0001

GLY 315 LYS 316 -0.0053

LYS 316 SER 317 -0.0002

SER 317 GLU 318 -0.0004

GLU 318 SER 319 -0.0005

SER 319 ILE 320 0.0019

ILE 320 ASP 321 -0.0001

ASP 321 ILE 322 -0.0007

ILE 322 TYR 323 -0.0001

TYR 323 SER 324 0.0012

SER 324 ILE 325 0.0005

ILE 325 ASP 326 0.0007

ASP 326 ASN 327 -0.0004

ASN 327 GLU 328 -0.0000

GLU 328 MET 329 0.0000

MET 329 THR 330 0.0024

THR 330 ARG 331 -0.0000

ARG 331 LYS 332 0.0052

LYS 332 SER 333 -0.0000

SER 333 SER 334 0.0005

SER 334 GLY 336 -0.0026

GLY 336 LEU 337 0.0001

LEU 337 GLU 338 0.0027

GLU 338 ILE 339 -0.0000

ILE 339 ALA 340 0.0006

ALA 340 ARG 341 -0.0000

ARG 341 ASN 342 -0.0039

ASN 342 ILE 343 0.0004

ILE 343 GLY 344 0.0001

GLY 344 HIS 345 0.0003

HIS 345 TYR 346 0.0004

TYR 346 LEU 347 0.0003

LEU 347 GLU 348 -0.0018

GLU 348 ARG 349 0.0001

ARG 349 VAL 350 -0.0002

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 9 ---

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

* *