Should you encounter any unexpected behaviour,
please let us know.

* *

CA strain for 250216174952674896

--- 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 PRO 2 -0.0002

PRO 2 PRO 3 -0.0003

PRO 3 PRO 4 -0.0001

PRO 4 ARG 5 -0.0000

ARG 5 LEU 6 0.0004

LEU 6 LEU 7 -0.0006

LEU 7 PHE 8 -0.0002

PHE 8 PHE 9 0.0013

PHE 9 LEU 10 0.0000

LEU 10 LEU 11 -0.0006

LEU 11 PHE 12 0.0001

PHE 12 LEU 13 -0.0005

LEU 13 THR 14 -0.0002

THR 14 PRO 15 0.0144

PRO 15 MET 16 -0.0001

MET 16 GLU 17 0.0219

GLU 17 VAL 18 0.0001

VAL 18 ARG 19 0.0032

ARG 19 PRO 20 0.0000

PRO 20 GLU 21 0.0030

GLU 21 GLU 22 -0.0000

GLU 22 PRO 23 0.0018

PRO 23 LEU 24 0.0003

LEU 24 VAL 25 0.0021

VAL 25 VAL 26 0.0000

VAL 26 LYS 27 0.0066

LYS 27 VAL 28 0.0001

VAL 28 GLU 29 0.0186

GLU 29 GLU 30 0.0002

GLU 30 GLY 31 0.0022

GLY 31 ASP 32 0.0001

ASP 32 ASN 33 0.0076

ASN 33 ALA 34 0.0002

ALA 34 VAL 35 0.0031

VAL 35 LEU 36 0.0002

LEU 36 GLN 37 0.0017

GLN 37 CYS 38 -0.0001

CYS 38 LEU 39 0.0005

LEU 39 LYS 40 0.0000

LYS 40 GLY 41 -0.0004

GLY 41 THR 42 -0.0002

THR 42 SER 43 -0.0002

SER 43 ASP 44 0.0002

ASP 44 GLY 45 0.0004

GLY 45 PRO 46 0.0001

PRO 46 THR 47 -0.0003

THR 47 GLN 48 0.0002

GLN 48 GLN 49 -0.0004

GLN 49 LEU 50 0.0003

LEU 50 THR 51 -0.0018

THR 51 TRP 52 0.0004

TRP 52 SER 53 -0.0013

SER 53 ARG 54 -0.0002

ARG 54 GLU 55 0.0004

GLU 55 SER 56 0.0001

SER 56 PRO 57 -0.0002

PRO 57 LEU 58 0.0002

LEU 58 LYS 59 0.0013

LYS 59 PRO 60 -0.0002

PRO 60 PHE 61 0.0001

PHE 61 LEU 62 0.0000

LEU 62 LYS 63 -0.0004

LYS 63 LEU 64 -0.0003

LEU 64 SER 65 -0.0008

SER 65 LEU 66 0.0001

LEU 66 GLY 67 0.0000

GLY 67 LEU 68 -0.0002

LEU 68 PRO 69 0.0006

PRO 69 GLY 70 -0.0002

GLY 70 LEU 71 -0.0003

LEU 71 GLY 72 0.0001

GLY 72 ILE 73 -0.0003

ILE 73 HIS 74 0.0002

HIS 74 MET 75 0.0003

MET 75 ARG 76 -0.0001

ARG 76 PRO 77 0.0004

PRO 77 LEU 78 -0.0004

LEU 78 ALA 79 0.0004

ALA 79 ILE 80 -0.0003

ILE 80 TRP 81 0.0005

TRP 81 LEU 82 -0.0002

LEU 82 PHE 83 0.0003

PHE 83 ILE 84 -0.0000

ILE 84 PHE 85 -0.0001

PHE 85 ASN 86 0.0003

ASN 86 VAL 87 0.0001

VAL 87 SER 88 0.0001

SER 88 GLN 89 0.0005

GLN 89 GLN 90 -0.0001

GLN 90 MET 91 0.0003

MET 91 GLY 92 -0.0001

GLY 92 GLY 93 0.0003

GLY 93 PHE 94 0.0000

PHE 94 TYR 95 -0.0001

TYR 95 LEU 96 0.0002

LEU 96 CYS 97 -0.0007

CYS 97 GLN 98 0.0002

GLN 98 PRO 99 -0.0004

PRO 99 GLY 100 -0.0001

GLY 100 PRO 101 -0.0000

PRO 101 PRO 102 -0.0002

PRO 102 SER 103 0.0004

SER 103 GLU 104 -0.0001

GLU 104 LYS 105 -0.0002

LYS 105 ALA 106 -0.0003

ALA 106 TRP 107 0.0002

TRP 107 GLN 108 0.0001

GLN 108 PRO 109 0.0004

PRO 109 GLY 110 0.0000

GLY 110 TRP 111 0.0000

TRP 111 THR 112 -0.0002

THR 112 VAL 113 -0.0005

VAL 113 ASN 114 0.0003

ASN 114 VAL 115 -0.0003

VAL 115 GLU 116 0.0001

GLU 116 GLY 117 -0.0002

GLY 117 SER 118 0.0001

SER 118 GLY 119 0.0009

GLY 119 GLU 120 -0.0001

GLU 120 LEU 121 -0.0001

LEU 121 PHE 122 -0.0000

PHE 122 ARG 123 0.0004

ARG 123 TRP 124 -0.0004

TRP 124 ASN 125 0.0001

ASN 125 VAL 126 0.0002

VAL 126 SER 127 0.0001

SER 127 ASP 128 0.0002

ASP 128 LEU 129 0.0006

LEU 129 GLY 130 -0.0003

GLY 130 GLY 131 0.0012

GLY 131 LEU 132 -0.0004

LEU 132 GLY 133 -0.0004

GLY 133 CYS 134 0.0001

CYS 134 GLY 135 0.0003

GLY 135 LEU 136 0.0000

LEU 136 LYS 137 0.0011

LYS 137 ASN 138 -0.0000

ASN 138 ARG 139 -0.0004

ARG 139 SER 140 -0.0002

SER 140 SER 141 0.0003

SER 141 GLU 142 -0.0002

GLU 142 GLY 143 0.0000

GLY 143 PRO 144 0.0002

PRO 144 SER 145 -0.0008

SER 145 SER 146 0.0001

SER 146 PRO 147 0.0006

PRO 147 SER 148 0.0000

SER 148 GLY 149 0.0009

GLY 149 LYS 150 0.0004

LYS 150 LEU 151 0.0010

LEU 151 MET 152 -0.0000

MET 152 SER 153 0.0002

SER 153 PRO 154 -0.0003

PRO 154 LYS 155 -0.0002

LYS 155 LEU 156 0.0002

LEU 156 TYR 157 -0.0008

TYR 157 VAL 158 0.0003

VAL 158 TRP 159 -0.0003

TRP 159 ALA 160 0.0002

ALA 160 LYS 161 -0.0002

LYS 161 ASP 162 0.0003

ASP 162 ARG 163 -0.0002

ARG 163 PRO 164 0.0001

PRO 164 GLU 165 -0.0000

GLU 165 ILE 166 -0.0002

ILE 166 TRP 167 0.0004

TRP 167 GLU 168 -0.0000

GLU 168 GLY 169 -0.0001

GLY 169 GLU 170 0.0001

GLU 170 PRO 171 -0.0001

PRO 171 PRO 172 0.0004

PRO 172 CYS 173 0.0005

CYS 173 LEU 174 -0.0003

LEU 174 PRO 175 0.0006

PRO 175 PRO 176 -0.0000

PRO 176 ARG 177 0.0000

ARG 177 ASP 178 0.0002

ASP 178 SER 179 0.0002

SER 179 LEU 180 -0.0004

LEU 180 ASN 181 -0.0000

ASN 181 GLN 182 -0.0001

GLN 182 SER 183 0.0005

SER 183 LEU 184 0.0003

LEU 184 SER 185 0.0002

SER 185 GLN 186 -0.0002

GLN 186 ASP 187 0.0002

ASP 187 LEU 188 0.0001

LEU 188 THR 189 0.0003

THR 189 MET 190 0.0003

MET 190 ALA 191 -0.0004

ALA 191 PRO 192 -0.0003

PRO 192 GLY 193 0.0001

GLY 193 SER 194 -0.0002

SER 194 THR 195 0.0009

THR 195 LEU 196 -0.0003

LEU 196 TRP 197 0.0007

TRP 197 LEU 198 0.0001

LEU 198 SER 199 -0.0005

SER 199 CYS 200 0.0004

CYS 200 GLY 201 0.0007

GLY 201 VAL 202 -0.0000

VAL 202 PRO 203 0.0000

PRO 203 PRO 204 -0.0002

PRO 204 ASP 205 -0.0001

ASP 205 SER 206 0.0003

SER 206 VAL 207 0.0008

VAL 207 SER 208 0.0001

SER 208 ARG 209 0.0006

ARG 209 GLY 210 0.0002

GLY 210 PRO 211 -0.0023

PRO 211 LEU 212 -0.0001

LEU 212 SER 213 -0.0011

SER 213 TRP 214 -0.0000

TRP 214 THR 215 -0.0011

THR 215 HIS 216 0.0003

HIS 216 VAL 217 -0.0003

VAL 217 HIS 218 0.0003

HIS 218 PRO 219 -0.0001

PRO 219 LYS 220 0.0001

LYS 220 GLY 221 -0.0008

GLY 221 PRO 222 -0.0000

PRO 222 LYS 223 0.0004

LYS 223 SER 224 0.0001

SER 224 LEU 225 -0.0001

LEU 225 LEU 226 -0.0002

LEU 226 SER 227 -0.0009

SER 227 LEU 228 0.0001

LEU 228 GLU 229 -0.0016

GLU 229 LEU 230 0.0001

LEU 230 LYS 231 -0.0006

LYS 231 ASP 232 0.0003

ASP 232 ASP 233 -0.0008

ASP 233 ARG 234 -0.0000

ARG 234 PRO 235 -0.0021

PRO 235 ALA 236 -0.0003

ALA 236 ARG 237 -0.0006

ARG 237 ASP 238 -0.0002

ASP 238 MET 239 -0.0002

MET 239 TRP 240 -0.0002

TRP 240 VAL 241 -0.0009

VAL 241 MET 242 -0.0003

MET 242 GLU 243 -0.0005

GLU 243 THR 244 0.0004

THR 244 GLY 245 0.0014

GLY 245 LEU 246 -0.0001

LEU 246 LEU 247 0.0011

LEU 247 LEU 248 0.0003

LEU 248 PRO 249 -0.0014

PRO 249 ARG 250 -0.0004

ARG 250 ALA 251 0.0019

ALA 251 THR 252 0.0002

THR 252 ALA 253 0.0051

ALA 253 GLN 254 0.0003

GLN 254 ASP 255 0.0011

ASP 255 ALA 256 -0.0001

ALA 256 GLY 257 -0.0017

GLY 257 LYS 258 -0.0002

LYS 258 TYR 259 0.0000

TYR 259 TYR 260 -0.0001

TYR 260 CYS 261 -0.0012

CYS 261 HIS 262 0.0003

HIS 262 ARG 263 -0.0005

ARG 263 GLY 264 -0.0002

GLY 264 ASN 265 0.0009

ASN 265 LEU 266 0.0001

LEU 266 THR 267 -0.0015

THR 267 MET 268 0.0003

MET 268 SER 269 -0.0003

SER 269 PHE 270 0.0001

PHE 270 HIS 271 0.0002

HIS 271 LEU 272 -0.0003

LEU 272 GLU 273 -0.0012

GLU 273 ILE 274 -0.0001

ILE 274 THR 275 -0.0033

THR 275 ALA 276 0.0003

ALA 276 ARG 277 -0.0065

ARG 277 PRO 278 0.0005

PRO 278 VAL 279 0.0040

VAL 279 LEU 280 -0.0001

LEU 280 TRP 281 0.0095

TRP 281 HIS 282 -0.0001

HIS 282 TRP 283 -0.0171

TRP 283 LEU 284 -0.0003

LEU 284 LEU 285 0.0103

LEU 285 ARG 286 0.0003

ARG 286 THR 287 -0.0141

THR 287 GLY 288 -0.0003

GLY 288 GLY 289 -0.0026

GLY 289 TRP 290 0.0001

TRP 290 LYS 291 0.0046

LYS 291 VAL 292 -0.0001

VAL 292 SER 293 0.0195

SER 293 ALA 294 -0.0002

ALA 294 VAL 295 -0.0065

VAL 295 THR 296 -0.0001

THR 296 LEU 297 -0.0008

LEU 297 ALA 298 0.0000

ALA 298 TYR 299 -0.0030

TYR 299 LEU 300 0.0001

LEU 300 ILE 301 -0.0028

ILE 301 PHE 302 -0.0001

PHE 302 CYS 303 0.0019

CYS 303 LEU 304 -0.0001

LEU 304 CYS 305 -0.0179

CYS 305 SER 306 0.0001

SER 306 LEU 307 0.0096

LEU 307 VAL 308 -0.0000

VAL 308 GLY 309 -0.0036

GLY 309 ILE 310 -0.0000

ILE 310 LEU 311 0.0111

LEU 311 HIS 312 -0.0003

HIS 312 LEU 313 -0.0041

LEU 313 GLN 314 0.0002

GLN 314 ARG 315 0.0030

ARG 315 ALA 316 -0.0001

ALA 316 LEU 317 -0.0006

LEU 317 VAL 318 0.0001

VAL 318 LEU 319 -0.0019

LEU 319 ARG 320 -0.0000

ARG 320 ARG 321 0.0031

ARG 321 LYS 322 -0.0001

LYS 322 ARG 323 -0.0020

ARG 323 LYS 324 0.0002

LYS 324 ARG 325 0.0030

ARG 325 MET 326 0.0000

MET 326 THR 327 -0.0006

THR 327 ASP 328 -0.0003

ASP 328 PRO 329 0.0007

PRO 329 THR 330 -0.0002

THR 330 ARG 331 -0.0010

ARG 331 ARG 332 0.0002

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).
Last modification: April 8th, 2025.

Should you encounter any unexpected behaviour, please let us know.

*** ***

CA strain for 250216174952674896

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.

* *