Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 01-AUG-25 *

CA strain for 2609181322541682843

--- 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
MET 1 ASP 2 0.0000

ASP 2 LEU 3 0.0024

LEU 3 ASP 4 0.0001

ASP 4 VAL 5 0.0018

VAL 5 VAL 6 0.0000

VAL 6 ASN 7 0.0038

ASN 7 MET 8 -0.0000

MET 8 PHE 9 -0.0005

PHE 9 VAL 10 -0.0000

VAL 10 ILE 11 0.0086

ILE 11 ALA 12 0.0001

ALA 12 GLY 13 0.1066

GLY 13 GLY 14 0.0000

GLY 14 THR 15 0.0233

THR 15 LEU 16 0.0000

LEU 16 ALA 17 0.0674

ALA 17 ILE 18 0.0001

ILE 18 PRO 19 0.0929

PRO 19 ILE 20 0.0002

ILE 20 LEU 21 0.0111

LEU 21 ALA 22 -0.0001

ALA 22 PHE 23 0.1617

PHE 23 VAL 24 0.0004

VAL 24 ALA 25 0.0743

ALA 25 SER 26 -0.0000

SER 26 PHE 27 0.0011

PHE 27 LEU 28 0.0001

LEU 28 LEU 29 0.0349

LEU 29 TRP 30 -0.0004

TRP 30 PRO 31 -0.0199

PRO 31 SER 32 0.0001

SER 32 ALA 33 -0.0086

ALA 33 LEU 34 0.0004

LEU 34 ILE 35 0.0639

ILE 35 ARG 36 -0.0002

ARG 36 ILE 37 -0.0141

ILE 37 TYR 38 0.0000

TYR 38 TYR 39 0.0020

TYR 39 TRP 40 0.0000

TRP 40 TYR 41 -0.0022

TYR 41 TRP 42 -0.0003

TRP 42 ARG 43 -0.0083

ARG 43 ARG 44 -0.0001

ARG 44 THR 45 -0.0003

THR 45 LEU 46 0.0001

LEU 46 GLY 47 -0.0009

GLY 47 MET 48 -0.0002

MET 48 GLN 49 -0.0020

GLN 49 VAL 50 -0.0001

VAL 50 ARG 51 -0.0047

ARG 51 TYR 52 0.0001

TYR 52 VAL 53 -0.0028

VAL 53 HIS 54 -0.0001

HIS 54 HIS 55 -0.0016

HIS 55 GLU 56 -0.0001

GLU 56 ASP 57 0.0005

ASP 57 TYR 58 0.0000

TYR 58 GLN 59 -0.0011

GLN 59 PHE 60 0.0001

PHE 60 CYS 61 -0.0021

CYS 61 TYR 62 -0.0000

TYR 62 SER 63 -0.0011

SER 63 PHE 64 -0.0001

PHE 64 ARG 65 -0.0015

ARG 65 GLY 66 -0.0000

GLY 66 ARG 67 0.0014

ARG 67 PRO 68 -0.0000

PRO 68 GLY 69 0.0023

GLY 69 HIS 70 -0.0001

HIS 70 LYS 71 -0.0001

LYS 71 PRO 72 0.0001

PRO 72 SER 73 0.0009

SER 73 ILE 74 0.0002

ILE 74 LEU 75 -0.0005

LEU 75 MET 76 -0.0000

MET 76 LEU 77 -0.0012

LEU 77 HIS 78 -0.0003

HIS 78 GLY 79 -0.0022

GLY 79 PHE 80 -0.0001

PHE 80 SER 81 -0.0021

SER 81 ALA 82 -0.0005

ALA 82 HIS 83 -0.0005

HIS 83 LYS 84 0.0000

LYS 84 ASP 85 0.0016

ASP 85 MET 86 0.0002

MET 86 TRP 87 0.0006

TRP 87 LEU 88 -0.0001

LEU 88 SER 89 0.0028

SER 89 VAL 90 0.0002

VAL 90 VAL 91 -0.0022

VAL 91 LYS 92 0.0003

LYS 92 PHE 93 0.0093

PHE 93 LEU 94 0.0004

LEU 94 PRO 95 -0.0030

PRO 95 LYS 96 -0.0003

LYS 96 ASN 97 0.0021

ASN 97 LEU 98 -0.0004

LEU 98 HIS 99 -0.0008

HIS 99 LEU 100 -0.0003

LEU 100 VAL 101 -0.0001

VAL 101 CYS 102 0.0000

CYS 102 VAL 103 0.0003

VAL 103 ASP 104 -0.0002

ASP 104 MET 105 -0.0010

MET 105 PRO 106 0.0001

PRO 106 GLY 107 -0.0000

GLY 107 HIS 108 -0.0001

HIS 108 GLU 109 -0.0009

GLU 109 GLY 110 -0.0005

GLY 110 THR 111 -0.0012

THR 111 THR 112 -0.0002

THR 112 ARG 113 0.0023

ARG 113 SER 114 0.0000

SER 114 SER 115 -0.0004

SER 115 LEU 116 -0.0002

LEU 116 ASP 117 -0.0001

ASP 117 ASP 118 -0.0002

ASP 118 LEU 119 0.0004

LEU 119 SER 120 -0.0001

SER 120 ILE 121 -0.0005

ILE 121 ASP 122 0.0001

ASP 122 GLY 123 -0.0007

GLY 123 GLN 124 0.0002

GLN 124 VAL 125 -0.0002

VAL 125 LYS 126 -0.0002

LYS 126 ARG 127 -0.0011

ARG 127 ILE 128 -0.0000

ILE 128 HIS 129 0.0007

HIS 129 GLN 130 0.0001

GLN 130 PHE 131 -0.0002

PHE 131 VAL 132 -0.0003

VAL 132 GLU 133 0.0001

GLU 133 CYS 134 -0.0002

CYS 134 LEU 135 0.0003

LEU 135 LYS 136 0.0001

LYS 136 LEU 137 -0.0008

LEU 137 ASN 138 -0.0001

ASN 138 LYS 139 0.0010

LYS 139 LYS 140 0.0001

LYS 140 PRO 141 -0.0008

PRO 141 PHE 142 0.0002

PHE 142 HIS 143 -0.0015

HIS 143 LEU 144 0.0000

LEU 144 VAL 145 0.0004

VAL 145 GLY 146 -0.0000

GLY 146 THR 147 -0.0024

THR 147 SER 148 -0.0004

SER 148 MET 149 0.0012

MET 149 GLY 150 0.0001

GLY 150 GLY 151 -0.0005

GLY 151 GLN 152 0.0004

GLN 152 VAL 153 0.0003

VAL 153 ALA 154 0.0000

ALA 154 GLY 155 0.0007

GLY 155 VAL 156 0.0004

VAL 156 TYR 157 0.0005

TYR 157 ALA 158 -0.0004

ALA 158 ALA 159 -0.0000

ALA 159 TYR 160 0.0005

TYR 160 TYR 161 0.0000

TYR 161 PRO 162 0.0001

PRO 162 SER 163 -0.0001

SER 163 ASP 164 0.0001

ASP 164 VAL 165 -0.0008

VAL 165 SER 166 0.0002

SER 166 SER 167 -0.0012

SER 167 LEU 168 -0.0000

LEU 168 CYS 169 -0.0008

CYS 169 LEU 170 0.0001

LEU 170 VAL 171 -0.0011

VAL 171 CYS 172 -0.0001

CYS 172 PRO 173 0.0002

PRO 173 ALA 174 0.0002

ALA 174 GLY 175 -0.0000

GLY 175 LEU 176 -0.0003

LEU 176 GLN 177 0.0003

GLN 177 TYR 178 -0.0003

TYR 178 SER 179 0.0001

SER 179 THR 180 -0.0005

THR 180 ASP 181 0.0002

ASP 181 ASN 182 -0.0000

ASN 182 GLN 183 -0.0003

GLN 183 PHE 184 0.0001

PHE 184 VAL 185 0.0000

VAL 185 GLN 186 0.0002

GLN 186 ARG 187 0.0006

ARG 187 LEU 188 0.0000

LEU 188 LYS 189 0.0003

LYS 189 GLU 190 -0.0004

GLU 190 LEU 191 -0.0015

LEU 191 GLN 192 -0.0000

GLN 192 GLY 193 0.0003

GLY 193 SER 194 -0.0002

SER 194 ALA 195 -0.0006

ALA 195 ALA 196 0.0001

ALA 196 VAL 197 0.0006

VAL 197 GLU 198 -0.0001

GLU 198 LYS 199 0.0004

LYS 199 ILE 200 0.0001

ILE 200 PRO 201 0.0029

PRO 201 LEU 202 0.0001

LEU 202 ILE 203 -0.0023

ILE 203 PRO 204 0.0001

PRO 204 SER 205 -0.0025

SER 205 THR 206 -0.0002

THR 206 PRO 207 0.0122

PRO 207 GLU 208 -0.0001

GLU 208 GLU 209 0.0060

GLU 209 MET 210 0.0005

MET 210 SER 211 0.0007

SER 211 GLU 212 0.0001

GLU 212 MET 213 -0.0006

MET 213 LEU 214 0.0000

LEU 214 GLN 215 0.0049

GLN 215 LEU 216 0.0000

LEU 216 CYS 217 -0.0028

CYS 217 SER 218 0.0003

SER 218 TYR 219 -0.0014

TYR 219 VAL 220 0.0000

VAL 220 ARG 221 -0.0050

ARG 221 PHE 222 0.0001

PHE 222 LYS 223 -0.0046

LYS 223 VAL 224 -0.0003

VAL 224 PRO 225 0.0027

PRO 225 GLN 226 0.0002

GLN 226 GLN 227 -0.0279

GLN 227 ILE 228 0.0003

ILE 228 LEU 229 0.0310

LEU 229 GLN 230 -0.0001

GLN 230 GLY 231 0.0015

GLY 231 LEU 232 -0.0003

LEU 232 VAL 233 -0.0028

VAL 233 ASP 234 0.0003

ASP 234 VAL 235 0.0042

VAL 235 ARG 236 -0.0001

ARG 236 ILE 237 -0.0000

ILE 237 PRO 238 -0.0001

PRO 238 HIS 239 0.0010

HIS 239 ASN 240 -0.0001

ASN 240 ASN 241 0.0016

ASN 241 PHE 242 0.0002

PHE 242 TYR 243 0.0010

TYR 243 ARG 244 -0.0002

ARG 244 LYS 245 0.0037

LYS 245 LEU 246 0.0004

LEU 246 PHE 247 0.0019

PHE 247 LEU 248 0.0000

LEU 248 GLU 249 0.0034

GLU 249 ILE 250 0.0003

ILE 250 VAL 251 0.0018

VAL 251 SER 252 0.0002

SER 252 GLU 253 -0.0007

GLU 253 LYS 254 0.0000

LYS 254 SER 255 0.0002

SER 255 ARG 256 0.0001

ARG 256 TYR 257 -0.0009

TYR 257 SER 258 -0.0001

SER 258 LEU 259 -0.0005

LEU 259 HIS 260 -0.0001

HIS 260 GLN 261 0.0005

GLN 261 ASN 262 0.0003

ASN 262 MET 263 -0.0002

MET 263 ASP 264 -0.0001

ASP 264 LYS 265 -0.0004

LYS 265 ILE 266 0.0001

ILE 266 LYS 267 -0.0005

LYS 267 VAL 268 -0.0002

VAL 268 PRO 269 -0.0009

PRO 269 THR 270 -0.0001

THR 270 GLN 271 -0.0008

GLN 271 ILE 272 0.0002

ILE 272 ILE 273 -0.0011

ILE 273 TRP 274 -0.0000

TRP 274 GLY 275 -0.0018

GLY 275 LYS 276 0.0000

LYS 276 GLN 277 -0.0008

GLN 277 ASP 278 0.0001

ASP 278 GLN 279 -0.0002

GLN 279 VAL 280 -0.0002

VAL 280 LEU 281 -0.0003

LEU 281 ASP 282 -0.0000

ASP 282 VAL 283 -0.0004

VAL 283 SER 284 -0.0002

SER 284 GLY 285 0.0007

GLY 285 ALA 286 0.0003

ALA 286 ASP 287 0.0008

ASP 287 MET 288 -0.0002

MET 288 LEU 289 0.0000

LEU 289 ALA 290 -0.0001

ALA 290 LYS 291 0.0011

LYS 291 SER 292 0.0000

SER 292 ILE 293 -0.0003

ILE 293 ALA 294 0.0001

ALA 294 ASN 295 -0.0004

ASN 295 CYS 296 -0.0000

CYS 296 GLN 297 -0.0001

GLN 297 VAL 298 -0.0000

VAL 298 GLU 299 -0.0005

GLU 299 LEU 300 0.0004

LEU 300 LEU 301 -0.0003

LEU 301 GLU 302 0.0002

GLU 302 ASN 303 -0.0020

ASN 303 CYS 304 0.0004

CYS 304 GLY 305 -0.0004

GLY 305 HIS 306 0.0001

HIS 306 SER 307 0.0005

SER 307 VAL 308 -0.0000

VAL 308 VAL 309 0.0032

VAL 309 MET 310 0.0002

MET 310 GLU 311 0.0047

GLU 311 ARG 312 -0.0003

ARG 312 PRO 313 -0.0001

PRO 313 ARG 314 -0.0000

ARG 314 LYS 315 0.0047

LYS 315 THR 316 -0.0004

THR 316 ALA 317 -0.0016

ALA 317 LYS 318 -0.0004

LYS 318 LEU 319 0.0043

LEU 319 ILE 320 0.0002

ILE 320 ILE 321 -0.0011

ILE 321 ASP 322 -0.0002

ASP 322 PHE 323 0.0010

PHE 323 LEU 324 -0.0003

LEU 324 ALA 325 -0.0002

ALA 325 SER 326 -0.0000

SER 326 VAL 327 0.0013

VAL 327 HIS 328 0.0001

HIS 328 ASN 329 0.0015

ASN 329 THR 330 0.0000

THR 330 ASP 331 0.0002

ASP 331 ASN 332 -0.0002

ASN 332 ASN 333 0.0012

ASN 333 LYS 334 -0.0001

LYS 334 LYS 335 -0.0029

LYS 335 LEU 336 0.0004

LEU 336 ASP 337 0.0015

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** 01-AUG-25 ***

CA strain for 2609181322541682843

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 01-AUG-25 *