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 8 ---

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 -0.0001

ILE 2 THR 3 -0.0031

THR 3 THR 4 -0.0005

THR 4 GLU 5 -0.0075

GLU 5 ARG 6 0.0001

ARG 6 ALA 7 -0.0142

ALA 7 VAL 8 -0.0003

VAL 8 LEU 9 -0.0070

LEU 9 THR 10 -0.0004

THR 10 LEU 11 -0.0132

LEU 11 ASN 12 0.0002

ASN 12 GLY 13 0.0016

GLY 13 LEU 14 -0.0002

LEU 14 GLN 15 -0.0064

GLN 15 ILE 16 -0.0005

ILE 16 LYS 17 -0.0100

LYS 17 LEU 18 0.0002

LEU 18 HIS 19 -0.0077

HIS 19 LYS 20 0.0002

LYS 20 VAL 21 -0.0050

VAL 21 VAL 22 0.0000

VAL 22 GLY 23 -0.0047

GLY 23 GLU 24 0.0001

GLU 24 SER 25 -0.0000

SER 25 ARG 26 0.0000

ARG 26 ASP 27 -0.0016

ASP 27 ASP 28 -0.0000

ASP 28 ILE 29 -0.0008

ILE 29 VAL 30 0.0004

VAL 30 ALA 31 -0.0041

ALA 31 LYS 32 -0.0001

LYS 32 MET 33 0.0012

MET 33 LYS 34 0.0000

LYS 34 ASP 35 -0.0011

ASP 35 LEU 36 -0.0001

LEU 36 ALA 37 -0.0023

ALA 37 MET 38 0.0002

MET 38 ASP 39 0.0015

ASP 39 ASP 40 -0.0003

ASP 40 HIS 41 0.0006

HIS 41 LYS 42 0.0001

LYS 42 PHE 43 -0.0041

PHE 43 PRO 44 0.0001

PRO 44 ARG 45 -0.0018

ARG 45 LEU 46 -0.0002

LEU 46 PRO 47 0.0044

PRO 47 GLY 48 0.0000

GLY 48 PRO 49 -0.0038

PRO 49 ASN 50 -0.0002

ASN 50 PRO 51 -0.0046

PRO 51 VAL 52 -0.0002

VAL 52 SER 53 -0.0506

SER 53 ILE 54 -0.0001

ILE 54 GLU 55 0.0205

GLU 55 ARG 56 -0.0000

ARG 56 LYS 57 0.0390

LYS 57 ASP 58 -0.0003

ASP 58 PHE 59 -0.0279

PHE 59 GLU 60 0.0002

GLU 60 LYS 61 0.0315

LYS 61 LEU 62 0.0005

LEU 62 LYS 63 0.0021

LYS 63 GLN 64 0.0003

GLN 64 ASN 65 0.0068

ASN 65 LYS 66 0.0004

LYS 66 TYR 67 -0.0154

TYR 67 VAL 68 0.0001

VAL 68 VAL 69 0.0053

VAL 69 SER 70 0.0002

SER 70 GLU 71 -0.0112

GLU 71 LYS 72 -0.0001

LYS 72 THR 73 0.0132

THR 73 ASP 74 0.0000

ASP 74 GLY 75 -0.0312

GLY 75 ILE 76 0.0002

ILE 76 ARG 77 0.0150

ARG 77 PHE 78 0.0004

PHE 78 MET 79 -0.0076

MET 79 MET 80 -0.0000

MET 80 PHE 81 -0.0052

PHE 81 PHE 82 0.0001

PHE 82 THR 83 0.0002

THR 83 ARG 84 -0.0003

ARG 84 VAL 85 0.0011

VAL 85 PHE 86 -0.0000

PHE 86 GLY 87 -0.0000

GLY 87 PHE 88 -0.0002

PHE 88 LYS 89 -0.0004

LYS 89 VAL 90 -0.0002

VAL 90 CYS 91 0.0006

CYS 91 THR 92 -0.0001

THR 92 ILE 93 -0.0018

ILE 93 ILE 94 0.0000

ILE 94 ASP 95 0.0079

ASP 95 ARG 96 -0.0000

ARG 96 ALA 97 -0.0007

ALA 97 MET 98 0.0001

MET 98 THR 99 0.0122

THR 99 VAL 100 0.0001

VAL 100 TYR 101 0.0011

TYR 101 LEU 102 -0.0002

LEU 102 LEU 103 -0.0020

LEU 103 PRO 104 0.0000

PRO 104 PHE 105 0.0012

PHE 105 LYS 106 -0.0002

LYS 106 ASN 107 -0.0033

ASN 107 ILE 108 -0.0002

ILE 108 PRO 109 -0.0005

PRO 109 ARG 110 -0.0001

ARG 110 VAL 111 -0.0005

VAL 111 LEU 112 -0.0001

LEU 112 PHE 113 -0.0006

PHE 113 GLN 114 0.0001

GLN 114 GLY 115 -0.0006

GLY 115 SER 116 0.0001

SER 116 ILE 117 -0.0012

ILE 117 PHE 118 0.0005

PHE 118 ASP 119 0.0020

ASP 119 GLY 120 -0.0003

GLY 120 GLU 121 0.0010

GLU 121 LEU 122 0.0001

LEU 122 CYS 123 -0.0072

CYS 123 VAL 124 -0.0000

VAL 124 ASP 125 -0.0082

ASP 125 ILE 126 0.0002

ILE 126 VAL 127 0.0097

VAL 127 GLU 128 -0.0001

GLU 128 LYS 129 -0.0059

LYS 129 LYS 130 -0.0002

LYS 130 PHE 131 0.0014

PHE 131 ALA 132 -0.0001

ALA 132 PHE 133 0.0013

PHE 133 VAL 134 -0.0001

VAL 134 LEU 135 0.0048

LEU 135 PHE 136 0.0004

PHE 136 ASP 137 -0.0005

ASP 137 ALA 138 0.0000

ALA 138 VAL 139 0.0005

VAL 139 VAL 140 0.0002

VAL 140 VAL 141 -0.0011

VAL 141 SER 142 0.0001

SER 142 GLY 143 0.0025

GLY 143 VAL 144 0.0000

VAL 144 THR 145 -0.0001

THR 145 VAL 146 0.0000

VAL 146 SER 147 -0.0059

SER 147 GLN 148 -0.0002

GLN 148 MET 149 0.0030

MET 149 ASP 150 -0.0004

ASP 150 LEU 151 0.0063

LEU 151 ALA 152 0.0001

ALA 152 SER 153 0.0048

SER 153 ARG 154 -0.0002

ARG 154 PHE 155 0.0009

PHE 155 PHE 156 0.0003

PHE 156 ALA 157 0.0066

ALA 157 MET 158 -0.0000

MET 158 LYS 159 0.0008

LYS 159 ARG 160 -0.0002

ARG 160 SER 161 -0.0000

SER 161 LEU 162 -0.0002

LEU 162 LYS 163 0.0056

LYS 163 GLU 164 0.0003

GLU 164 PHE 165 0.0008

PHE 165 LYS 166 -0.0001

LYS 166 ASN 167 0.0006

ASN 167 VAL 168 0.0002

VAL 168 PRO 169 -0.0022

PRO 169 GLU 170 -0.0002

GLU 170 ASP 171 0.0010

ASP 171 PRO 172 -0.0003

PRO 172 ALA 173 -0.0022

ALA 173 ILE 174 0.0000

ILE 174 LEU 175 -0.0051

LEU 175 ARG 176 0.0002

ARG 176 TYR 177 -0.0129

TYR 177 LYS 178 0.0000

LYS 178 GLU 179 -0.0213

GLU 179 TRP 180 0.0003

TRP 180 ILE 181 0.0013

ILE 181 PRO 182 -0.0003

PRO 182 LEU 183 -0.0090

LEU 183 GLU 184 -0.0001

GLU 184 HIS 185 -0.0043

HIS 185 PRO 186 -0.0000

PRO 186 THR 187 -0.0101

THR 187 ILE 188 -0.0002

ILE 188 ILE 189 0.0023

ILE 189 LYS 190 0.0000

LYS 190 ASP 191 -0.0074

ASP 191 HIS 192 -0.0001

HIS 192 LEU 193 0.0132

LEU 193 LYS 194 0.0001

LYS 194 LYS 195 -0.0010

LYS 195 ALA 196 0.0002

ALA 196 ASN 197 0.0029

ASN 197 ALA 198 -0.0000

ALA 198 ILE 199 0.0092

ILE 199 TYR 200 -0.0003

TYR 200 HIS 201 0.0150

HIS 201 THR 202 -0.0003

THR 202 ASP 203 0.0667

ASP 203 GLY 204 0.0001

GLY 204 LEU 205 0.0011

LEU 205 ILE 206 0.0002

ILE 206 ILE 207 0.0011

ILE 207 MET 208 -0.0000

MET 208 SER 209 -0.0014

SER 209 VAL 210 0.0002

VAL 210 ASP 211 0.0038

ASP 211 GLU 212 0.0004

GLU 212 PRO 213 0.0196

PRO 213 VAL 214 0.0004

VAL 214 ILE 215 -0.0174

ILE 215 TYR 216 -0.0000

TYR 216 GLY 217 -0.0270

GLY 217 ARG 218 0.0002

ARG 218 ASN 219 0.0102

ASN 219 PHE 220 -0.0002

PHE 220 ASN 221 -0.0112

ASN 221 LEU 222 -0.0003

LEU 222 PHE 223 -0.0185

PHE 223 LYS 224 -0.0002

LYS 224 LEU 225 -0.0594

LEU 225 LYS 226 -0.0002

LYS 226 PRO 227 0.0046

PRO 227 GLY 228 0.0006

GLY 228 THR 229 0.0168

THR 229 HIS 230 0.0002

HIS 230 HIS 231 0.1853

HIS 231 THR 232 -0.0004

THR 232 ILE 233 0.1560

ILE 233 ASP 234 0.0001

ASP 234 PHE 235 0.0307

PHE 235 ILE 236 -0.0002

ILE 236 ILE 237 -0.0085

ILE 237 MET 238 -0.0002

MET 238 SER 239 -0.0068

SER 239 GLU 240 0.0003

GLU 240 ASP 241 -0.0002

ASP 241 GLY 242 0.0002

GLY 242 THR 243 -0.0010

THR 243 ILE 244 -0.0000

ILE 244 GLY 245 -0.0096

GLY 245 ILE 246 -0.0002

ILE 246 PHE 247 0.0063

PHE 247 ASP 248 -0.0002

ASP 248 PRO 249 0.0030

PRO 249 ASN 250 -0.0002

ASN 250 LEU 251 0.0012

LEU 251 ARG 252 -0.0000

ARG 252 LYS 253 -0.0059

LYS 253 ASN 254 -0.0001

ASN 254 VAL 255 -0.0019

VAL 255 PRO 256 0.0000

PRO 256 VAL 257 -0.0094

VAL 257 GLY 258 0.0001

GLY 258 LYS 259 0.0071

LYS 259 LEU 260 0.0002

LEU 260 ASP 261 0.0007

ASP 261 GLY 262 -0.0004

GLY 262 TYR 263 0.0008

TYR 263 TYR 264 0.0001

TYR 264 ASN 265 0.0028

ASN 265 LYS 266 0.0000

LYS 266 GLY 267 -0.0063

GLY 267 SER 268 -0.0002

SER 268 ILE 269 0.0067

ILE 269 VAL 270 0.0002

VAL 270 GLU 271 0.0346

GLU 271 CYS 272 0.0001

CYS 272 GLY 273 0.0273

GLY 273 PHE 274 0.0002

PHE 274 ALA 275 -0.0096

ALA 275 ASP 276 0.0002

ASP 276 GLY 277 -0.0020

GLY 277 THR 278 -0.0000

THR 278 TRP 279 0.0089

TRP 279 LYS 280 0.0003

LYS 280 TYR 281 0.0147

TYR 281 ILE 282 0.0002

ILE 282 GLN 283 0.0125

GLN 283 GLY 284 0.0002

GLY 284 ARG 285 0.0004

ARG 285 SER 286 -0.0001

SER 286 ASP 287 0.0014

ASP 287 LYS 288 -0.0001

LYS 288 ASN 289 0.0067

ASN 289 GLN 290 0.0000

GLN 290 ALA 291 -0.0131

ALA 291 ASN 292 0.0002

ASN 292 ASP 293 0.0004

ASP 293 ARG 294 0.0001

ARG 294 LEU 295 0.0071

LEU 295 THR 296 -0.0001

THR 296 TYR 297 -0.0037

TYR 297 GLU 298 -0.0003

GLU 298 LYS 299 0.0157

LYS 299 THR 300 0.0001

THR 300 LEU 301 0.0202

LEU 301 LEU 302 -0.0004

LEU 302 ASN 303 -0.0011

ASN 303 ILE 304 0.0002

ILE 304 GLU 305 0.0490

GLU 305 GLU 306 -0.0002

GLU 306 ASN 307 -0.0244

ASN 307 ILE 308 0.0002

ILE 308 THR 309 -0.0048

THR 309 ILE 310 0.0004

ILE 310 ASP 311 0.0065

ASP 311 GLU 312 0.0000

GLU 312 LEU 313 -0.0111

LEU 313 LEU 314 -0.0003

LEU 314 ASP 315 -0.0111

ASP 315 LEU 316 -0.0002

LEU 316 PHE 317 -0.0232

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 8 ---

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

* *