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 7 ---

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 -0.0001

ARG 2 GLU 3 -0.0000

GLU 3 GLN 4 0.0001

GLN 4 LEU 5 -0.0005

LEU 5 LYS 6 0.0000

LYS 6 GLY 7 -0.0002

GLY 7 HIS 8 -0.0001

HIS 8 GLU 9 0.0002

GLU 9 THR 10 -0.0001

THR 10 GLN 11 -0.0000

GLN 11 THR 12 -0.0001

THR 12 THR 13 0.0005

THR 13 CYS 14 0.0003

CYS 14 TRP 15 -0.0003

TRP 15 ASP 16 -0.0001

ASP 16 HIS 17 0.0001

HIS 17 PRO 18 -0.0001

PRO 18 LYS 19 -0.0002

LYS 19 MET 20 0.0003

MET 20 THR 21 -0.0002

THR 21 GLU 22 0.0002

GLU 22 LEU 23 -0.0004

LEU 23 TYR 24 -0.0004

TYR 24 GLN 25 0.0005

GLN 25 SER 26 0.0004

SER 26 LEU 27 -0.0000

LEU 27 ALA 28 0.0003

ALA 28 ASP 29 -0.0001

ASP 29 LEU 30 -0.0001

LEU 30 ASN 31 0.0001

ASN 31 ASN 32 0.0001

ASN 32 VAL 33 0.0006

VAL 33 ARG 34 -0.0004

ARG 34 PHE 35 0.0002

PHE 35 SER 36 0.0001

SER 36 ALA 37 0.0003

ALA 37 TYR 38 -0.0004

TYR 38 ARG 39 -0.0005

ARG 39 THR 40 -0.0001

THR 40 ALA 41 -0.0002

ALA 41 MET 42 0.0002

MET 42 LYS 43 -0.0001

LYS 43 LEU 44 0.0001

LEU 44 ARG 45 -0.0004

ARG 45 ARG 46 0.0003

ARG 46 LEU 47 0.0004

LEU 47 GLN 48 0.0000

GLN 48 LYS 49 -0.0003

LYS 49 ALA 50 0.0003

ALA 50 LEU 51 0.0002

LEU 51 CYS 52 -0.0002

CYS 52 LEU 53 -0.0004

LEU 53 ASP 54 -0.0002

ASP 54 LEU 55 0.0002

LEU 55 LEU 56 -0.0001

LEU 56 SER 57 -0.0002

SER 57 LEU 58 -0.0002

LEU 58 SER 59 -0.0005

SER 59 ALA 60 0.0000

ALA 60 ALA 61 -0.0002

ALA 61 CYS 62 -0.0002

CYS 62 ASP 63 -0.0003

ASP 63 ALA 64 -0.0001

ALA 64 LEU 65 0.0001

LEU 65 ASP 66 -0.0000

ASP 66 GLN 67 -0.0001

GLN 67 HIS 68 -0.0000

HIS 68 ASN 69 -0.0002

ASN 69 LEU 70 -0.0000

LEU 70 LYS 71 -0.0003

LYS 71 GLN 72 -0.0001

GLN 72 ASN 73 -0.0002

ASN 73 ASP 74 0.0002

ASP 74 GLN 75 0.0001

GLN 75 PRO 76 0.0003

PRO 76 MET 77 -0.0002

MET 77 ASP 78 0.0000

ASP 78 ILE 79 0.0001

ILE 79 LEU 80 0.0002

LEU 80 GLN 81 -0.0004

GLN 81 ILE 82 0.0001

ILE 82 ILE 83 -0.0002

ILE 83 ASN 84 0.0001

ASN 84 CYS 85 0.0001

CYS 85 LEU 86 -0.0004

LEU 86 THR 87 -0.0001

THR 87 THR 88 -0.0002

THR 88 ILE 89 -0.0002

ILE 89 TYR 90 -0.0001

TYR 90 ASP 91 0.0000

ASP 91 ARG 92 0.0001

ARG 92 LEU 93 0.0004

LEU 93 GLU 94 0.0001

GLU 94 GLN 95 -0.0001

GLN 95 GLU 96 0.0001

GLU 96 HIS 97 -0.0002

HIS 97 ASN 98 0.0002

ASN 98 ASN 99 -0.0004

ASN 99 LEU 100 -0.0001

LEU 100 VAL 101 0.0002

VAL 101 ASN 102 0.0003

ASN 102 VAL 103 0.0004

VAL 103 PRO 104 -0.0003

PRO 104 LEU 105 0.0003

LEU 105 CYS 106 0.0001

CYS 106 VAL 107 0.0004

VAL 107 ASP 108 -0.0003

ASP 108 MET 109 -0.0002

MET 109 CYS 110 0.0001

CYS 110 LEU 111 0.0001

LEU 111 ASN 112 -0.0002

ASN 112 TRP 113 -0.0000

TRP 113 LEU 114 0.0003

LEU 114 LEU 115 0.0003

LEU 115 ASN 116 0.0001

ASN 116 VAL 117 -0.0003

VAL 117 TYR 118 0.0002

TYR 118 ASP 119 0.0001

ASP 119 THR 120 -0.0001

THR 120 GLY 121 0.0002

GLY 121 ARG 122 -0.0001

ARG 122 THR 123 0.0001

THR 123 GLY 124 0.0003

GLY 124 ARG 125 -0.0001

ARG 125 ILE 126 -0.0000

ILE 126 ARG 127 0.0003

ARG 127 VAL 128 0.0001

VAL 128 LEU 129 -0.0003

LEU 129 SER 130 -0.0001

SER 130 PHE 131 -0.0003

PHE 131 LYS 132 -0.0001

LYS 132 THR 133 -0.0005

THR 133 GLY 134 0.0001

GLY 134 ILE 135 -0.0002

ILE 135 ILE 136 -0.0003

ILE 136 SER 137 -0.0004

SER 137 LEU 138 -0.0001

LEU 138 CYS 139 -0.0003

CYS 139 LYS 140 0.0002

LYS 140 ALA 141 -0.0002

ALA 141 HIS 142 -0.0003

HIS 142 LEU 143 -0.0001

LEU 143 GLU 144 0.0001

GLU 144 ASP 145 0.0001

ASP 145 LYS 146 0.0002

LYS 146 TYR 147 -0.0001

TYR 147 ARG 148 -0.0000

ARG 148 TYR 149 -0.0004

TYR 149 LEU 150 -0.0000

LEU 150 PHE 151 0.0003

PHE 151 LYS 152 -0.0001

LYS 152 GLN 153 0.0001

GLN 153 VAL 154 -0.0003

VAL 154 ALA 155 -0.0000

ALA 155 SER 156 0.0002

SER 156 SER 157 0.0003

SER 157 THR 158 0.0001

THR 158 GLY 159 -0.0002

GLY 159 PHE 160 0.0001

PHE 160 CYS 161 -0.0003

CYS 161 ASP 162 -0.0002

ASP 162 GLN 163 0.0000

GLN 163 ARG 164 0.0003

ARG 164 ARG 165 0.0000

ARG 165 LEU 166 0.0001

LEU 166 GLY 167 0.0005

GLY 167 LEU 168 0.0000

LEU 168 LEU 169 0.0003

LEU 169 LEU 170 -0.0002

LEU 170 HIS 171 -0.0003

HIS 171 ASP 172 0.0003

ASP 172 SER 173 -0.0003

SER 173 ILE 174 0.0000

ILE 174 GLN 175 -0.0004

GLN 175 ILE 176 0.0003

ILE 176 PRO 177 -0.0011

PRO 177 ARG 178 -0.0001

ARG 178 GLN 179 -0.0003

GLN 179 LEU 180 -0.0001

LEU 180 GLY 181 0.0001

GLY 181 GLU 182 0.0001

GLU 182 VAL 183 -0.0005

VAL 183 ALA 184 -0.0002

ALA 184 SER 185 -0.0003

SER 185 PHE 186 -0.0000

PHE 186 GLY 187 -0.0019

GLY 187 GLY 188 -0.0000

GLY 188 SER 189 0.0002

SER 189 ASN 190 0.0003

ASN 190 ILE 191 0.0003

ILE 191 GLU 192 -0.0000

GLU 192 PRO 193 0.0001

PRO 193 SER 194 0.0001

SER 194 VAL 195 -0.0005

VAL 195 ARG 196 -0.0003

ARG 196 SER 197 0.0005

SER 197 CYS 198 0.0002

CYS 198 PHE 199 -0.0005

PHE 199 GLN 200 -0.0003

GLN 200 PHE 201 -0.0000

PHE 201 ALA 202 -0.0001

ALA 202 ASN 203 -0.0000

ASN 203 ASN 204 0.0003

ASN 204 LYS 205 -0.0001

LYS 205 PRO 206 -0.0001

PRO 206 GLU 207 0.0005

GLU 207 ILE 208 -0.0001

ILE 208 GLU 209 0.0003

GLU 209 ALA 210 0.0002

ALA 210 ALA 211 -0.0002

ALA 211 LEU 212 -0.0002

LEU 212 PHE 213 0.0002

PHE 213 LEU 214 0.0002

LEU 214 ASP 215 0.0003

ASP 215 TRP 216 -0.0001

TRP 216 MET 217 0.0003

MET 217 ARG 218 0.0000

ARG 218 LEU 219 0.0008

LEU 219 GLU 220 -0.0001

GLU 220 PRO 221 -0.0013

PRO 221 GLN 222 -0.0002

GLN 222 SER 223 -0.0031

SER 223 MET 224 -0.0003

MET 224 VAL 225 0.0018

VAL 225 TRP 226 -0.0002

TRP 226 LEU 227 -0.0006

LEU 227 PRO 228 -0.0001

PRO 228 VAL 229 0.0015

VAL 229 LEU 230 0.0001

LEU 230 HIS 231 0.0001

HIS 231 ARG 232 0.0001

ARG 232 VAL 233 -0.0001

VAL 233 ALA 234 -0.0005

ALA 234 ALA 235 0.0004

ALA 235 ALA 236 -0.0001

ALA 236 GLU 237 0.0006

GLU 237 THR 238 0.0003

THR 238 ALA 239 -0.0006

ALA 239 LYS 240 0.0001

LYS 240 HIS 241 -0.0004

HIS 241 GLN 242 0.0004

GLN 242 ALA 243 -0.0002

ALA 243 LYS 244 0.0001

LYS 244 CYS 245 0.0001

CYS 245 ASN 246 0.0001

ASN 246 ILE 247 0.0000

ILE 247 CYS 248 0.0002

CYS 248 LYS 249 -0.0003

LYS 249 GLU 250 0.0001

GLU 250 CYS 251 0.0001

CYS 251 PRO 252 0.0003

PRO 252 ILE 253 -0.0001

ILE 253 ILE 254 0.0003

ILE 254 GLY 255 -0.0003

GLY 255 PHE 256 0.0007

PHE 256 ARG 257 -0.0004

ARG 257 TYR 258 -0.0001

TYR 258 ARG 259 0.0000

ARG 259 SER 260 0.0001

SER 260 LEU 261 -0.0004

LEU 261 LYS 262 -0.0002

LYS 262 HIS 263 0.0002

HIS 263 PHE 264 0.0001

PHE 264 ASN 265 -0.0001

ASN 265 TYR 266 -0.0001

TYR 266 ASP 267 -0.0001

ASP 267 ILE 268 -0.0000

ILE 268 CYS 269 -0.0003

CYS 269 GLN 270 0.0003

GLN 270 SER 271 -0.0002

SER 271 CYS 272 -0.0000

CYS 272 PHE 273 0.0002

PHE 273 PHE 274 0.0001

PHE 274 SER 275 -0.0004

SER 275 GLY 276 -0.0002

GLY 276 ARG 277 0.0002

ARG 277 VAL 278 0.0002

VAL 278 ALA 279 -0.0001

ALA 279 LYS 280 0.0003

LYS 280 GLY 281 -0.0002

GLY 281 HIS 282 0.0002

HIS 282 LYS 283 -0.0001

LYS 283 MET 284 -0.0001

MET 284 HIS 285 -0.0007

HIS 285 TYR 286 0.0002

TYR 286 PRO 287 0.0002

PRO 287 MET 288 0.0000

MET 288 VAL 289 0.0001

VAL 289 GLU 290 0.0004

GLU 290 TYR 291 0.0005

TYR 291 CYS 292 -0.0004

CYS 292 THR 293 -0.0001

THR 293 PRO 294 0.0001

PRO 294 THR 295 -0.0005

THR 295 THR 296 0.0002

THR 296 SER 297 0.0002

SER 297 GLY 298 0.0003

GLY 298 GLU 299 0.0000

GLU 299 ASP 300 -0.0002

ASP 300 VAL 301 0.0002

VAL 301 ARG 302 -0.0000

ARG 302 ASP 303 0.0003

ASP 303 PHE 304 0.0001

PHE 304 ALA 305 -0.0002

ALA 305 LYS 306 -0.0000

LYS 306 VAL 307 0.0000

VAL 307 LEU 308 0.0003

LEU 308 LYS 309 -0.0001

LYS 309 ASN 310 -0.0002

ASN 310 LYS 311 -0.0003

LYS 311 PHE 312 -0.0001

PHE 312 ARG 313 0.0001

ARG 313 THR 314 0.0001

THR 314 LYS 315 -0.0003

LYS 315 ARG 316 -0.0000

ARG 316 TYR 317 -0.0001

TYR 317 PHE 318 0.0000

PHE 318 ALA 319 -0.0002

ALA 319 LYS 320 0.0004

LYS 320 HIS 321 0.0002

HIS 321 PRO 322 0.0001

PRO 322 ARG 323 0.0007

ARG 323 MET 324 -0.0000

MET 324 GLY 325 0.0028

GLY 325 TYR 326 0.0003

TYR 326 LEU 327 0.0112

LEU 327 PRO 328 0.0004

PRO 328 VAL 329 -0.0053

VAL 329 GLN 330 0.0002

GLN 330 THR 331 -0.0829

THR 331 VAL 332 -0.0002

VAL 332 LEU 333 0.0121

LEU 333 GLU 334 0.0001

GLU 334 GLY 335 -0.0606

GLY 335 ASP 336 -0.0000

ASP 336 ASN 337 0.0076

ASN 337 MET 338 -0.0001

MET 338 GLU 339 0.0033

GLU 339 THR 340 0.0003

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 7 ---

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 *