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

* *

CA strain for 2609210641052849957

--- 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
ASN 1 ILE 2 0.0002

ILE 2 THR 3 -0.0043

THR 3 THR 4 -0.0002

THR 4 GLU 5 0.0005

GLU 5 ARG 6 0.0002

ARG 6 ALA 7 0.0031

ALA 7 VAL 8 0.0001

VAL 8 LEU 9 0.0058

LEU 9 THR 10 -0.0000

THR 10 LEU 11 0.0099

LEU 11 ASN 12 -0.0001

ASN 12 GLY 13 0.0023

GLY 13 LEU 14 0.0000

LEU 14 GLN 15 -0.0000

GLN 15 ILE 16 -0.0002

ILE 16 LYS 17 0.0020

LYS 17 LEU 18 0.0004

LEU 18 HIS 19 0.0026

HIS 19 LYS 20 -0.0002

LYS 20 VAL 21 -0.0001

VAL 21 VAL 22 -0.0002

VAL 22 GLY 23 -0.0005

GLY 23 GLU 24 0.0003

GLU 24 SER 25 -0.0016

SER 25 ARG 26 0.0001

ARG 26 ASP 27 0.0004

ASP 27 ASP 28 0.0001

ASP 28 ILE 29 -0.0006

ILE 29 VAL 30 -0.0001

VAL 30 ALA 31 -0.0005

ALA 31 LYS 32 0.0001

LYS 32 MET 33 0.0059

MET 33 LYS 34 0.0001

LYS 34 ASP 35 -0.0012

ASP 35 LEU 36 0.0002

LEU 36 ALA 37 0.0095

ALA 37 MET 38 0.0004

MET 38 ASP 39 -0.0024

ASP 39 ASP 40 0.0002

ASP 40 HIS 41 0.0000

HIS 41 LYS 42 -0.0003

LYS 42 PHE 43 -0.0016

PHE 43 PRO 44 -0.0006

PRO 44 ARG 45 0.0044

ARG 45 LEU 46 -0.0002

LEU 46 PRO 47 -0.0059

PRO 47 GLY 48 0.0000

GLY 48 PRO 49 0.0213

PRO 49 ASN 50 -0.0002

ASN 50 PRO 51 0.0335

PRO 51 VAL 52 0.0003

VAL 52 SER 53 0.0390

SER 53 ILE 54 -0.0001

ILE 54 GLU 55 -0.0037

GLU 55 ARG 56 -0.0003

ARG 56 LYS 57 -0.0061

LYS 57 ASP 58 -0.0002

ASP 58 PHE 59 0.0201

PHE 59 GLU 60 -0.0002

GLU 60 LYS 61 -0.0026

LYS 61 LEU 62 -0.0002

LEU 62 LYS 63 0.0133

LYS 63 GLN 64 0.0002

GLN 64 ASN 65 -0.0217

ASN 65 LYS 66 0.0003

LYS 66 TYR 67 0.0098

TYR 67 VAL 68 0.0001

VAL 68 VAL 69 0.0050

VAL 69 SER 70 0.0001

SER 70 GLU 71 0.0126

GLU 71 LYS 72 0.0001

LYS 72 THR 73 0.0103

THR 73 ASP 74 -0.0002

ASP 74 GLY 75 0.0373

GLY 75 ILE 76 -0.0002

ILE 76 ARG 77 -0.0132

ARG 77 PHE 78 0.0000

PHE 78 MET 79 -0.0015

MET 79 MET 80 -0.0001

MET 80 PHE 81 0.0052

PHE 81 PHE 82 0.0001

PHE 82 THR 83 -0.0006

THR 83 ARG 84 -0.0000

ARG 84 VAL 85 -0.0082

VAL 85 PHE 86 -0.0001

PHE 86 GLY 87 -0.0002

GLY 87 PHE 88 0.0001

PHE 88 LYS 89 -0.0001

LYS 89 VAL 90 0.0004

VAL 90 CYS 91 0.0064

CYS 91 THR 92 -0.0004

THR 92 ILE 93 0.0076

ILE 93 ILE 94 0.0000

ILE 94 ASP 95 0.0036

ASP 95 ARG 96 -0.0004

ARG 96 ALA 97 0.0092

ALA 97 MET 98 -0.0000

MET 98 THR 99 -0.0025

THR 99 VAL 100 0.0004

VAL 100 TYR 101 -0.0022

TYR 101 LEU 102 0.0001

LEU 102 LEU 103 -0.0037

LEU 103 PRO 104 -0.0001

PRO 104 PHE 105 -0.0045

PHE 105 LYS 106 -0.0001

LYS 106 ASN 107 -0.0026

ASN 107 ILE 108 -0.0001

ILE 108 PRO 109 0.0025

PRO 109 ARG 110 0.0003

ARG 110 VAL 111 -0.0002

VAL 111 LEU 112 0.0004

LEU 112 PHE 113 -0.0043

PHE 113 GLN 114 0.0002

GLN 114 GLY 115 0.0047

GLY 115 SER 116 -0.0001

SER 116 ILE 117 0.0085

ILE 117 PHE 118 -0.0003

PHE 118 ASP 119 0.0090

ASP 119 GLY 120 -0.0003

GLY 120 GLU 121 0.0033

GLU 121 LEU 122 0.0004

LEU 122 CYS 123 -0.0076

CYS 123 VAL 124 0.0003

VAL 124 ASP 125 -0.0054

ASP 125 ILE 126 -0.0001

ILE 126 VAL 127 0.0029

VAL 127 GLU 128 -0.0001

GLU 128 LYS 129 -0.0039

LYS 129 LYS 130 0.0001

LYS 130 PHE 131 -0.0031

PHE 131 ALA 132 0.0000

ALA 132 PHE 133 -0.0069

PHE 133 VAL 134 -0.0002

VAL 134 LEU 135 0.0029

LEU 135 PHE 136 -0.0003

PHE 136 ASP 137 0.0004

ASP 137 ALA 138 0.0002

ALA 138 VAL 139 0.0007

VAL 139 VAL 140 0.0001

VAL 140 VAL 141 0.0067

VAL 141 SER 142 -0.0000

SER 142 GLY 143 0.0029

GLY 143 VAL 144 0.0004

VAL 144 THR 145 -0.0009

THR 145 VAL 146 0.0003

VAL 146 SER 147 0.0069

SER 147 GLN 148 0.0000

GLN 148 MET 149 0.0058

MET 149 ASP 150 -0.0000

ASP 150 LEU 151 0.0082

LEU 151 ALA 152 -0.0000

ALA 152 SER 153 -0.0031

SER 153 ARG 154 -0.0000

ARG 154 PHE 155 0.0049

PHE 155 PHE 156 0.0001

PHE 156 ALA 157 -0.0010

ALA 157 MET 158 -0.0001

MET 158 LYS 159 0.0005

LYS 159 ARG 160 -0.0003

ARG 160 SER 161 -0.0076

SER 161 LEU 162 -0.0001

LEU 162 LYS 163 0.0035

LYS 163 GLU 164 -0.0002

GLU 164 PHE 165 0.0014

PHE 165 LYS 166 -0.0003

LYS 166 ASN 167 0.0015

ASN 167 VAL 168 0.0003

VAL 168 PRO 169 0.0010

PRO 169 GLU 170 0.0002

GLU 170 ASP 171 0.0002

ASP 171 PRO 172 0.0001

PRO 172 ALA 173 -0.0038

ALA 173 ILE 174 -0.0001

ILE 174 LEU 175 -0.0038

LEU 175 ARG 176 -0.0001

ARG 176 TYR 177 -0.0133

TYR 177 LYS 178 -0.0001

LYS 178 GLU 179 -0.0349

GLU 179 TRP 180 -0.0002

TRP 180 ILE 181 -0.0351

ILE 181 PRO 182 -0.0001

PRO 182 LEU 183 -0.0197

LEU 183 GLU 184 -0.0001

GLU 184 HIS 185 0.0061

HIS 185 PRO 186 -0.0001

PRO 186 THR 187 -0.0025

THR 187 ILE 188 -0.0002

ILE 188 ILE 189 0.0034

ILE 189 LYS 190 -0.0002

LYS 190 ASP 191 -0.0122

ASP 191 HIS 192 0.0000

HIS 192 LEU 193 0.0043

LEU 193 LYS 194 -0.0002

LYS 194 LYS 195 -0.0012

LYS 195 ALA 196 0.0004

ALA 196 ASN 197 -0.0042

ASN 197 ALA 198 -0.0003

ALA 198 ILE 199 0.0004

ILE 199 TYR 200 0.0002

TYR 200 HIS 201 0.0065

HIS 201 THR 202 -0.0004

THR 202 ASP 203 0.0440

ASP 203 GLY 204 0.0003

GLY 204 LEU 205 0.0210

LEU 205 ILE 206 0.0003

ILE 206 ILE 207 0.0144

ILE 207 MET 208 0.0000

MET 208 SER 209 -0.0062

SER 209 VAL 210 -0.0004

VAL 210 ASP 211 0.0092

ASP 211 GLU 212 -0.0001

GLU 212 PRO 213 -0.0135

PRO 213 VAL 214 -0.0000

VAL 214 ILE 215 0.0212

ILE 215 TYR 216 0.0003

TYR 216 GLY 217 0.0945

GLY 217 ARG 218 -0.0002

ARG 218 ASN 219 0.0313

ASN 219 PHE 220 -0.0001

PHE 220 ASN 221 0.0193

ASN 221 LEU 222 0.0001

LEU 222 PHE 223 -0.0007

PHE 223 LYS 224 0.0001

LYS 224 LEU 225 -0.0056

LEU 225 LYS 226 0.0003

LYS 226 PRO 227 -0.0107

PRO 227 GLY 228 0.0001

GLY 228 THR 229 -0.0452

THR 229 HIS 230 -0.0002

HIS 230 HIS 231 -0.0502

HIS 231 THR 232 0.0002

THR 232 ILE 233 0.0405

ILE 233 ASP 234 -0.0003

ASP 234 PHE 235 0.0165

PHE 235 ILE 236 0.0002

ILE 236 ILE 237 0.0070

ILE 237 MET 238 0.0000

MET 238 SER 239 0.0080

SER 239 GLU 240 0.0000

GLU 240 ASP 241 -0.0050

ASP 241 GLY 242 0.0000

GLY 242 THR 243 0.0047

THR 243 ILE 244 0.0000

ILE 244 GLY 245 0.0118

GLY 245 ILE 246 -0.0004

ILE 246 PHE 247 -0.0107

PHE 247 ASP 248 -0.0002

ASP 248 PRO 249 -0.0014

PRO 249 ASN 250 0.0006

ASN 250 LEU 251 0.0019

LEU 251 ARG 252 0.0001

ARG 252 LYS 253 -0.0073

LYS 253 ASN 254 -0.0001

ASN 254 VAL 255 -0.0059

VAL 255 PRO 256 -0.0002

PRO 256 VAL 257 -0.0103

VAL 257 GLY 258 0.0001

GLY 258 LYS 259 0.0025

LYS 259 LEU 260 -0.0002

LEU 260 ASP 261 0.0077

ASP 261 GLY 262 -0.0003

GLY 262 TYR 263 -0.0132

TYR 263 TYR 264 0.0002

TYR 264 ASN 265 -0.0061

ASN 265 LYS 266 -0.0002

LYS 266 GLY 267 0.0013

GLY 267 SER 268 -0.0000

SER 268 ILE 269 0.0094

ILE 269 VAL 270 -0.0000

VAL 270 GLU 271 0.0223

GLU 271 CYS 272 -0.0002

CYS 272 GLY 273 -0.0009

GLY 273 PHE 274 0.0000

PHE 274 ALA 275 0.0130

ALA 275 ASP 276 0.0002

ASP 276 GLY 277 0.0041

GLY 277 THR 278 -0.0000

THR 278 TRP 279 0.0229

TRP 279 LYS 280 0.0001

LYS 280 TYR 281 -0.0366

TYR 281 ILE 282 0.0000

ILE 282 GLN 283 -0.0137

GLN 283 GLY 284 0.0002

GLY 284 ARG 285 -0.0114

ARG 285 SER 286 0.0000

SER 286 ASP 287 -0.0005

ASP 287 LYS 288 -0.0001

LYS 288 ASN 289 -0.0026

ASN 289 GLN 290 0.0001

GLN 290 ALA 291 0.0077

ALA 291 ASN 292 -0.0000

ASN 292 ASP 293 -0.0062

ASP 293 ARG 294 -0.0002

ARG 294 LEU 295 0.0487

LEU 295 THR 296 -0.0004

THR 296 TYR 297 0.0195

TYR 297 GLU 298 0.0002

GLU 298 LYS 299 -0.0228

LYS 299 THR 300 -0.0001

THR 300 LEU 301 0.0423

LEU 301 LEU 302 -0.0003

LEU 302 ASN 303 0.0051

ASN 303 ILE 304 0.0001

ILE 304 GLU 305 0.0098

GLU 305 GLU 306 0.0002

GLU 306 ASN 307 0.0263

ASN 307 ILE 308 0.0000

ILE 308 THR 309 -0.0211

THR 309 ILE 310 0.0001

ILE 310 ASP 311 0.0119

ASP 311 GLU 312 0.0001

GLU 312 LEU 313 -0.0071

LEU 313 LEU 314 0.0002

LEU 314 ASP 315 0.0070

ASP 315 LEU 316 0.0001

LEU 316 PHE 317 -0.0199

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.

*** ***

CA strain for 2609210641052849957

--- 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.

* *