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

* DMD *

CA strain for 2609111750043690248

--- normal mode 10 ---

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 ARG 2 -0.0002

ARG 2 GLU 3 -0.0065

GLU 3 GLN 4 -0.0002

GLN 4 LEU 5 0.0015

LEU 5 LYS 6 0.0003

LYS 6 GLY 7 0.0037

GLY 7 HIS 8 -0.0001

HIS 8 GLU 9 -0.0011

GLU 9 THR 10 -0.0001

THR 10 GLN 11 -0.0023

GLN 11 THR 12 0.0004

THR 12 THR 13 -0.0078

THR 13 CYS 14 -0.0001

CYS 14 TRP 15 -0.0015

TRP 15 ASP 16 0.0003

ASP 16 HIS 17 -0.0022

HIS 17 PRO 18 -0.0002

PRO 18 LYS 19 0.0025

LYS 19 MET 20 0.0001

MET 20 THR 21 -0.0014

THR 21 GLU 22 -0.0004

GLU 22 LEU 23 0.0024

LEU 23 TYR 24 -0.0000

TYR 24 GLN 25 -0.0007

GLN 25 SER 26 -0.0003

SER 26 LEU 27 -0.0024

LEU 27 ALA 28 0.0000

ALA 28 ASP 29 0.0019

ASP 29 LEU 30 -0.0002

LEU 30 ASN 31 -0.0056

ASN 31 ASN 32 -0.0001

ASN 32 VAL 33 -0.0096

VAL 33 ARG 34 0.0002

ARG 34 PHE 35 0.0000

PHE 35 SER 36 -0.0001

SER 36 ALA 37 -0.0014

ALA 37 TYR 38 -0.0001

TYR 38 ARG 39 -0.0001

ARG 39 THR 40 -0.0002

THR 40 ALA 41 -0.0022

ALA 41 MET 42 -0.0002

MET 42 LYS 43 0.0072

LYS 43 LEU 44 0.0001

LEU 44 ARG 45 0.0011

ARG 45 ARG 46 -0.0005

ARG 46 LEU 47 0.0035

LEU 47 GLN 48 -0.0002

GLN 48 LYS 49 -0.0006

LYS 49 ALA 50 0.0002

ALA 50 LEU 51 0.0028

LEU 51 CYS 52 0.0002

CYS 52 LEU 53 0.0001

LEU 53 ASP 54 0.0002

ASP 54 LEU 55 -0.0015

LEU 55 LEU 56 -0.0001

LEU 56 SER 57 0.0024

SER 57 LEU 58 -0.0004

LEU 58 SER 59 0.0006

SER 59 ALA 60 -0.0001

ALA 60 ALA 61 0.0016

ALA 61 CYS 62 0.0003

CYS 62 ASP 63 0.0022

ASP 63 ALA 64 0.0000

ALA 64 LEU 65 0.0009

LEU 65 ASP 66 0.0000

ASP 66 GLN 67 0.0003

GLN 67 HIS 68 0.0000

HIS 68 ASN 69 0.0010

ASN 69 LEU 70 -0.0001

LEU 70 LYS 71 0.0001

LYS 71 GLN 72 0.0003

GLN 72 ASN 73 0.0008

ASN 73 ASP 74 -0.0001

ASP 74 GLN 75 -0.0009

GLN 75 PRO 76 0.0001

PRO 76 MET 77 -0.0001

MET 77 ASP 78 -0.0002

ASP 78 ILE 79 -0.0002

ILE 79 LEU 80 0.0001

LEU 80 GLN 81 -0.0003

GLN 81 ILE 82 -0.0001

ILE 82 ILE 83 -0.0000

ILE 83 ASN 84 0.0001

ASN 84 CYS 85 0.0002

CYS 85 LEU 86 0.0002

LEU 86 THR 87 0.0002

THR 87 THR 88 0.0002

THR 88 ILE 89 -0.0004

ILE 89 TYR 90 -0.0004

TYR 90 ASP 91 0.0001

ASP 91 ARG 92 0.0002

ARG 92 LEU 93 -0.0015

LEU 93 GLU 94 -0.0001

GLU 94 GLN 95 -0.0001

GLN 95 GLU 96 0.0001

GLU 96 HIS 97 0.0004

HIS 97 ASN 98 0.0000

ASN 98 ASN 99 0.0004

ASN 99 LEU 100 -0.0003

LEU 100 VAL 101 0.0000

VAL 101 ASN 102 0.0001

ASN 102 VAL 103 0.0000

VAL 103 PRO 104 0.0002

PRO 104 LEU 105 0.0006

LEU 105 CYS 106 0.0001

CYS 106 VAL 107 0.0003

VAL 107 ASP 108 -0.0001

ASP 108 MET 109 0.0006

MET 109 CYS 110 -0.0000

CYS 110 LEU 111 0.0006

LEU 111 ASN 112 0.0001

ASN 112 TRP 113 -0.0013

TRP 113 LEU 114 -0.0002

LEU 114 LEU 115 -0.0004

LEU 115 ASN 116 0.0000

ASN 116 VAL 117 -0.0041

VAL 117 TYR 118 0.0001

TYR 118 ASP 119 -0.0051

ASP 119 THR 120 0.0000

THR 120 GLY 121 -0.0013

GLY 121 ARG 122 -0.0002

ARG 122 THR 123 -0.0004

THR 123 GLY 124 -0.0002

GLY 124 ARG 125 -0.0029

ARG 125 ILE 126 -0.0000

ILE 126 ARG 127 -0.0022

ARG 127 VAL 128 0.0001

VAL 128 LEU 129 -0.0001

LEU 129 SER 130 0.0004

SER 130 PHE 131 0.0001

PHE 131 LYS 132 -0.0001

LYS 132 THR 133 0.0022

THR 133 GLY 134 -0.0001

GLY 134 ILE 135 0.0009

ILE 135 ILE 136 -0.0000

ILE 136 SER 137 -0.0007

SER 137 LEU 138 -0.0001

LEU 138 CYS 139 0.0018

CYS 139 LYS 140 -0.0000

LYS 140 ALA 141 0.0046

ALA 141 HIS 142 -0.0004

HIS 142 LEU 143 0.0037

LEU 143 GLU 144 0.0001

GLU 144 ASP 145 -0.0000

ASP 145 LYS 146 -0.0000

LYS 146 TYR 147 0.0027

TYR 147 ARG 148 0.0002

ARG 148 TYR 149 0.0023

TYR 149 LEU 150 0.0003

LEU 150 PHE 151 0.0005

PHE 151 LYS 152 -0.0001

LYS 152 GLN 153 0.0001

GLN 153 VAL 154 -0.0001

VAL 154 ALA 155 0.0013

ALA 155 SER 156 -0.0000

SER 156 SER 157 0.0012

SER 157 THR 158 0.0001

THR 158 GLY 159 -0.0015

GLY 159 PHE 160 -0.0003

PHE 160 CYS 161 0.0017

CYS 161 ASP 162 0.0001

ASP 162 GLN 163 0.0018

GLN 163 ARG 164 0.0005

ARG 164 ARG 165 -0.0003

ARG 165 LEU 166 -0.0005

LEU 166 GLY 167 0.0013

GLY 167 LEU 168 0.0004

LEU 168 LEU 169 -0.0011

LEU 169 LEU 170 -0.0001

LEU 170 HIS 171 -0.0018

HIS 171 ASP 172 -0.0003

ASP 172 SER 173 -0.0013

SER 173 ILE 174 0.0002

ILE 174 GLN 175 -0.0036

GLN 175 ILE 176 0.0001

ILE 176 PRO 177 0.0009

PRO 177 ARG 178 0.0000

ARG 178 GLN 179 -0.0082

GLN 179 LEU 180 0.0003

LEU 180 GLY 181 -0.0124

GLY 181 GLU 182 -0.0002

GLU 182 VAL 183 0.0105

VAL 183 ALA 184 -0.0003

ALA 184 SER 185 0.0120

SER 185 PHE 186 -0.0003

PHE 186 GLY 187 0.0127

GLY 187 GLY 188 -0.0002

GLY 188 SER 189 -0.0023

SER 189 ASN 190 0.0001

ASN 190 ILE 191 -0.0012

ILE 191 GLU 192 0.0003

GLU 192 PRO 193 -0.0000

PRO 193 SER 194 0.0002

SER 194 VAL 195 0.0046

VAL 195 ARG 196 0.0001

ARG 196 SER 197 -0.0014

SER 197 CYS 198 0.0002

CYS 198 PHE 199 0.0001

PHE 199 GLN 200 -0.0003

GLN 200 PHE 201 -0.0007

PHE 201 ALA 202 0.0002

ALA 202 ASN 203 -0.0012

ASN 203 ASN 204 -0.0001

ASN 204 LYS 205 0.0001

LYS 205 PRO 206 0.0002

PRO 206 GLU 207 -0.0003

GLU 207 ILE 208 -0.0003

ILE 208 GLU 209 -0.0001

GLU 209 ALA 210 0.0000

ALA 210 ALA 211 -0.0007

ALA 211 LEU 212 0.0001

LEU 212 PHE 213 0.0003

PHE 213 LEU 214 -0.0000

LEU 214 ASP 215 0.0004

ASP 215 TRP 216 -0.0000

TRP 216 MET 217 -0.0032

MET 217 ARG 218 0.0000

ARG 218 LEU 219 -0.0011

LEU 219 GLU 220 0.0005

GLU 220 PRO 221 0.0070

PRO 221 GLN 222 -0.0002

GLN 222 SER 223 0.0051

SER 223 MET 224 -0.0000

MET 224 VAL 225 -0.0121

VAL 225 TRP 226 -0.0002

TRP 226 LEU 227 0.0045

LEU 227 PRO 228 -0.0001

PRO 228 VAL 229 -0.0101

VAL 229 LEU 230 0.0001

LEU 230 HIS 231 -0.0024

HIS 231 ARG 232 -0.0001

ARG 232 VAL 233 -0.0004

VAL 233 ALA 234 0.0000

ALA 234 ALA 235 -0.0075

ALA 235 ALA 236 0.0003

ALA 236 GLU 237 0.0002

GLU 237 THR 238 -0.0000

THR 238 ALA 239 0.0044

ALA 239 LYS 240 0.0003

LYS 240 HIS 241 0.0034

HIS 241 GLN 242 0.0003

GLN 242 ALA 243 0.0016

ALA 243 LYS 244 0.0003

LYS 244 CYS 245 0.0001

CYS 245 ASN 246 0.0002

ASN 246 ILE 247 0.0004

ILE 247 CYS 248 0.0002

CYS 248 LYS 249 -0.0005

LYS 249 GLU 250 -0.0001

GLU 250 CYS 251 -0.0011

CYS 251 PRO 252 0.0005

PRO 252 ILE 253 -0.0001

ILE 253 ILE 254 -0.0002

ILE 254 GLY 255 0.0001

GLY 255 PHE 256 -0.0000

PHE 256 ARG 257 0.0015

ARG 257 TYR 258 -0.0002

TYR 258 ARG 259 0.0025

ARG 259 SER 260 0.0001

SER 260 LEU 261 0.0024

LEU 261 LYS 262 -0.0002

LYS 262 HIS 263 0.0028

HIS 263 PHE 264 -0.0001

PHE 264 ASN 265 0.0026

ASN 265 TYR 266 -0.0003

TYR 266 ASP 267 0.0027

ASP 267 ILE 268 0.0000

ILE 268 CYS 269 0.0059

CYS 269 GLN 270 -0.0002

GLN 270 SER 271 0.0014

SER 271 CYS 272 -0.0002

CYS 272 PHE 273 -0.0074

PHE 273 PHE 274 -0.0004

PHE 274 SER 275 0.0003

SER 275 GLY 276 0.0002

GLY 276 ARG 277 -0.0032

ARG 277 VAL 278 0.0000

VAL 278 ALA 279 0.0028

ALA 279 LYS 280 -0.0003

LYS 280 GLY 281 -0.0013

GLY 281 HIS 282 -0.0001

HIS 282 LYS 283 -0.0026

LYS 283 MET 284 0.0005

MET 284 HIS 285 0.0081

HIS 285 TYR 286 -0.0002

TYR 286 PRO 287 0.0016

PRO 287 MET 288 -0.0003

MET 288 VAL 289 -0.0030

VAL 289 GLU 290 0.0004

GLU 290 TYR 291 0.0025

TYR 291 CYS 292 -0.0004

CYS 292 THR 293 -0.0013

THR 293 PRO 294 0.0001

PRO 294 THR 295 0.0017

THR 295 THR 296 -0.0002

THR 296 SER 297 -0.0000

SER 297 GLY 298 -0.0002

GLY 298 GLU 299 -0.0002

GLU 299 ASP 300 0.0003

ASP 300 VAL 301 0.0002

VAL 301 ARG 302 -0.0001

ARG 302 ASP 303 0.0007

ASP 303 PHE 304 0.0001

PHE 304 ALA 305 -0.0003

ALA 305 LYS 306 0.0003

LYS 306 VAL 307 0.0010

VAL 307 LEU 308 0.0000

LEU 308 LYS 309 0.0019

LYS 309 ASN 310 0.0000

ASN 310 LYS 311 -0.0008

LYS 311 PHE 312 0.0001

PHE 312 ARG 313 -0.0014

ARG 313 THR 314 0.0003

THR 314 LYS 315 0.0003

LYS 315 ARG 316 -0.0002

ARG 316 TYR 317 -0.0006

TYR 317 PHE 318 -0.0001

PHE 318 ALA 319 0.0038

ALA 319 LYS 320 0.0001

LYS 320 HIS 321 -0.0019

HIS 321 PRO 322 0.0000

PRO 322 ARG 323 -0.0086

ARG 323 MET 324 0.0003

MET 324 GLY 325 -0.0371

GLY 325 TYR 326 -0.0001

TYR 326 LEU 327 -0.0317

LEU 327 PRO 328 -0.0005

PRO 328 VAL 329 0.0156

VAL 329 GLN 330 0.0002

GLN 330 THR 331 0.0713

THR 331 VAL 332 0.0001

VAL 332 LEU 333 -0.0142

LEU 333 GLU 334 0.0004

GLU 334 GLY 335 -0.3277

GLY 335 ASP 336 0.0001

ASP 336 ASN 337 -0.0022

ASN 337 MET 338 0.0000

MET 338 GLU 339 -0.0029

GLU 339 THR 340 -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).
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.

*** DMD ***

CA strain for 2609111750043690248

--- normal mode 10 ---

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

* DMD *