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

* *

CA strain for 22092323273356655

--- 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 HIS 2 -0.0002

HIS 2 GLU 3 -0.0012

GLU 3 LEU 4 -0.0001

LEU 4 LEU 5 -0.0032

LEU 5 THR 6 0.0004

THR 6 VAL 7 -0.0029

VAL 7 GLN 8 -0.0000

GLN 8 GLN 9 0.0003

GLN 9 VAL 10 -0.0001

VAL 10 ASP 11 0.0066

ASP 11 PRO 12 0.0001

PRO 12 TRP 13 0.0089

TRP 13 LEU 14 0.0000

LEU 14 GLN 15 0.0155

GLN 15 PHE 16 -0.0007

PHE 16 ASN 17 0.0289

ASN 17 PRO 18 -0.0002

PRO 18 HIS 19 0.0168

HIS 19 ILE 20 -0.0001

ILE 20 VAL 21 -0.0077

VAL 21 SER 22 -0.0000

SER 22 GLY 23 0.0017

GLY 23 TYR 24 0.0001

TYR 24 ARG 25 0.0068

ARG 25 PRO 26 0.0002

PRO 26 ARG 27 -0.0013

ARG 27 MET 28 -0.0004

MET 28 SER 29 0.0030

SER 29 VAL 30 0.0003

VAL 30 ARG 31 -0.0013

ARG 31 ALA 32 0.0000

ALA 32 ALA 33 0.0004

ALA 33 LEU 34 0.0003

LEU 34 ARG 35 -0.0023

ARG 35 SER 36 -0.0000

SER 36 PHE 37 0.0006

PHE 37 PHE 38 -0.0002

PHE 38 GLU 39 -0.0046

GLU 39 TRP 40 0.0002

TRP 40 HIS 41 0.0042

HIS 41 ASN 42 -0.0004

ASN 42 GLU 43 -0.0001

GLU 43 SER 44 -0.0001

SER 44 PHE 45 0.0022

PHE 45 ASN 46 -0.0002

ASN 46 VAL 47 -0.0018

VAL 47 TRP 48 0.0002

TRP 48 SER 49 0.0147

SER 49 HIS 50 -0.0001

HIS 50 ALA 51 0.0032

ALA 51 LEU 52 -0.0002

LEU 52 ALA 53 0.0071

ALA 53 ALA 54 -0.0000

ALA 54 CYS 55 0.0051

CYS 55 PHE 56 -0.0003

PHE 56 VAL 57 0.0002

VAL 57 LEU 58 0.0002

LEU 58 TYR 59 0.0066

TYR 59 LEU 60 0.0001

LEU 60 ALA 61 0.0030

ALA 61 LEU 62 -0.0001

LEU 62 PHE 63 0.0035

PHE 63 PRO 64 -0.0001

PRO 64 PRO 65 -0.0089

PRO 65 THR 66 0.0004

THR 66 MET 67 0.0041

MET 67 GLU 68 -0.0001

GLU 68 ILE 69 0.0004

ILE 69 SER 70 0.0001

SER 70 THR 71 -0.0696

THR 71 THR 72 -0.0002

THR 72 SER 73 -0.0654

SER 73 THR 74 -0.0002

THR 74 VAL 75 0.0022

VAL 75 ASN 76 -0.0001

ASN 76 GLY 77 0.0011

GLY 77 ARG 78 0.0001

ARG 78 GLY 79 0.0171

GLY 79 VAL 80 -0.0000

VAL 80 GLY 81 -0.0225

GLY 81 THR 82 -0.0003

THR 82 SER 83 -0.0092

SER 83 GLY 84 -0.0001

GLY 84 MET 85 0.0143

MET 85 ALA 86 0.0003

ALA 86 PRO 87 -0.0289

PRO 87 THR 88 0.0002

THR 88 ASP 89 -0.0125

ASP 89 VAL 90 0.0001

VAL 90 SER 91 -0.0908

SER 91 LEU 92 -0.0001

LEU 92 THR 93 -0.0071

THR 93 PRO 94 -0.0003

PRO 94 HIS 95 -0.0075

HIS 95 ASP 96 0.0002

ASP 96 ARG 97 -0.0083

ARG 97 ARG 98 -0.0002

ARG 98 TRP 99 -0.0185

TRP 99 LEU 100 0.0001

LEU 100 GLY 101 0.0781

GLY 101 SER 102 0.0000

SER 102 SER 103 0.0274

SER 103 SER 104 -0.0001

SER 104 GLU 105 0.0306

GLU 105 HIS 106 0.0004

HIS 106 LEU 107 0.0410

LEU 107 LEU 108 -0.0001

LEU 108 GLY 109 -0.0015

GLY 109 ALA 110 -0.0002

ALA 110 SER 111 0.0341

SER 111 SER 112 -0.0003

SER 112 THR 113 -0.0180

THR 113 THR 114 -0.0000

THR 114 THR 115 0.0009

THR 115 PHE 116 0.0002

PHE 116 ARG 117 0.0004

ARG 117 CYS 118 -0.0000

CYS 118 THR 119 -0.0000

THR 119 CYS 120 -0.0003

CYS 120 LEU 121 -0.0004

LEU 121 VAL 122 0.0001

VAL 122 PHE 123 -0.0022

PHE 123 PHE 124 -0.0001

PHE 124 PHE 125 0.0022

PHE 125 ILE 126 -0.0000

ILE 126 PHE 127 -0.0106

PHE 127 ILE 128 0.0001

ILE 128 CYS 129 0.0024

CYS 129 SER 130 0.0002

SER 130 VAL 131 -0.0029

VAL 131 VAL 132 -0.0000

VAL 132 TYR 133 0.0073

TYR 133 HIS 134 -0.0003

HIS 134 LEU 135 0.0005

LEU 135 PHE 136 -0.0002

PHE 136 MET 137 0.0052

MET 137 PRO 138 0.0004

PRO 138 CYS 139 -0.0020

CYS 139 THR 140 -0.0002

THR 140 THR 141 0.0021

THR 141 SER 142 -0.0004

SER 142 GLU 143 0.0007

GLU 143 SER 144 0.0000

SER 144 LEU 145 -0.0040

LEU 145 TYR 146 0.0003

TYR 146 ARG 147 0.0021

ARG 147 ARG 148 -0.0002

ARG 148 LEU 149 -0.0056

LEU 149 LEU 150 -0.0002

LEU 150 SER 151 0.0065

SER 151 CYS 152 -0.0000

CYS 152 ASP 153 -0.0006

ASP 153 VAL 154 0.0001

VAL 154 PHE 155 0.0044

PHE 155 GLY 156 0.0005

GLY 156 VAL 157 -0.0016

VAL 157 VAL 158 -0.0001

VAL 158 ILE 159 0.0004

ILE 159 CYS 160 -0.0003

CYS 160 ILE 161 -0.0009

ILE 161 THR 162 -0.0001

THR 162 GLY 163 0.0021

GLY 163 THR 164 -0.0000

THR 164 SER 165 -0.0074

SER 165 TRP 166 -0.0002

TRP 166 SER 167 0.0016

SER 167 LEU 168 0.0000

LEU 168 VAL 169 -0.0059

VAL 169 TYR 170 0.0000

TYR 170 ARG 171 0.0151

ARG 171 GLY 172 -0.0004

GLY 172 ASN 173 -0.0036

ASN 173 ALA 174 0.0002

ALA 174 CYS 175 -0.0012

CYS 175 SER 176 -0.0003

SER 176 GLN 177 -0.0058

GLN 177 ASN 178 0.0001

ASN 178 TRP 179 0.0050

TRP 179 SER 180 0.0001

SER 180 CYS 181 -0.0026

CYS 181 HIS 182 -0.0001

HIS 182 VAL 183 0.0105

VAL 183 GLY 184 0.0002

GLY 184 MET 185 -0.0032

MET 185 GLY 186 0.0003

GLY 186 ALA 187 0.0099

ALA 187 LEU 188 -0.0001

LEU 188 LEU 189 -0.0053

LEU 189 LEU 190 -0.0003

LEU 190 SER 191 0.0046

SER 191 ALA 192 -0.0003

ALA 192 LEU 193 -0.0058

LEU 193 PHE 194 -0.0001

PHE 194 VAL 195 0.0046

VAL 195 LEU 196 -0.0002

LEU 196 TYR 197 -0.0044

TYR 197 GLY 198 -0.0001

GLY 198 ALA 199 -0.0007

ALA 199 VAL 200 0.0000

VAL 200 PHE 201 -0.0041

PHE 201 ASN 202 0.0001

ASN 202 ALA 203 0.0199

ALA 203 SER 204 0.0001

SER 204 CYS 205 -0.0023

CYS 205 GLY 206 -0.0001

GLY 206 SER 207 0.0114

SER 207 PHE 208 -0.0002

PHE 208 GLY 209 0.0140

GLY 209 ARG 210 -0.0002

ARG 210 PHE 211 0.0010

PHE 211 LYS 212 -0.0001

LYS 212 ALA 213 0.0241

ALA 213 ILE 214 0.0004

ILE 214 GLY 215 -0.0028

GLY 215 PHE 216 0.0001

PHE 216 HIS 217 0.0034

HIS 217 SER 218 -0.0003

SER 218 VAL 219 0.0059

VAL 219 LEU 220 -0.0003

LEU 220 ARG 221 -0.0037

ARG 221 PHE 222 -0.0000

PHE 222 LEU 223 0.0074

LEU 223 ILE 224 0.0002

ILE 224 LEU 225 -0.0025

LEU 225 LEU 226 -0.0002

LEU 226 TRP 227 0.0063

TRP 227 VAL 228 -0.0002

VAL 228 GLU 229 -0.0008

GLU 229 LEU 230 0.0002

LEU 230 PRO 231 -0.0017

PRO 231 LYS 232 -0.0001

LYS 232 VAL 233 0.0007

VAL 233 GLN 234 -0.0002

GLN 234 SER 235 0.0011

SER 235 GLN 236 0.0002

GLN 236 GLY 237 -0.0001

GLY 237 TYR 238 -0.0003

TYR 238 HIS 239 -0.0075

HIS 239 GLN 240 0.0000

GLN 240 ALA 241 0.0041

ALA 241 VAL 242 0.0001

VAL 242 HIS 243 -0.0019

HIS 243 CYS 244 -0.0004

CYS 244 HIS 245 -0.0054

HIS 245 ALA 246 -0.0001

ALA 246 MET 247 0.0092

MET 247 SER 248 0.0003

SER 248 PHE 249 -0.0045

PHE 249 VAL 250 0.0000

VAL 250 PHE 251 0.0133

PHE 251 LEU 252 -0.0001

LEU 252 ALA 253 -0.0010

ALA 253 LEU 254 -0.0003

LEU 254 GLY 255 0.0059

GLY 255 ALA 256 0.0003

ALA 256 VAL 257 0.0103

VAL 257 ILE 258 0.0002

ILE 258 ASN 259 -0.0110

ASN 259 ALA 260 -0.0002

ALA 260 LEU 261 0.0392

LEU 261 ARG 262 0.0003

ARG 262 PHE 263 0.0030

PHE 263 PRO 264 0.0001

PRO 264 GLU 265 -0.0011

GLU 265 LYS 266 -0.0002

LYS 266 HIS 267 0.0190

HIS 267 LEU 268 -0.0001

LEU 268 ARG 269 0.0036

ARG 269 ARG 270 -0.0001

ARG 270 ALA 271 0.0221

ALA 271 THR 272 0.0004

THR 272 ARG 273 -0.0030

ARG 273 LEU 274 0.0000

LEU 274 LEU 275 -0.0008

LEU 275 PRO 276 -0.0002

PRO 276 ALA 277 0.0097

ALA 277 SER 278 -0.0002

SER 278 SER 279 0.0006

SER 279 SER 280 -0.0001

SER 280 SER 281 0.0045

SER 281 PRO 282 -0.0000

PRO 282 GLU 283 -0.0010

GLU 283 ALA 284 -0.0001

ALA 284 THR 285 0.0017

THR 285 VAL 286 -0.0003

VAL 286 ALA 287 0.0022

ALA 287 SER 288 -0.0003

SER 288 ARG 289 0.0059

ARG 289 CYS 290 -0.0001

CYS 290 TRP 291 -0.0044

TRP 291 ARG 292 -0.0002

ARG 292 TRP 293 0.0071

TRP 293 LEU 294 -0.0000

LEU 294 GLY 295 0.0045

GLY 295 ARG 296 0.0002

ARG 296 PHE 297 0.0027

PHE 297 VAL 298 -0.0001

VAL 298 VAL 299 0.0007

VAL 299 SER 300 -0.0001

SER 300 GLY 301 0.0140

GLY 301 GLU 302 -0.0002

GLU 302 GLU 303 -0.0013

GLU 303 ILE 304 -0.0001

ILE 304 ASP 305 -0.0032

ASP 305 TYR 306 -0.0001

TYR 306 THR 307 0.0036

THR 307 TRP 308 -0.0003

TRP 308 ASN 309 0.0078

ASN 309 SER 310 -0.0003

SER 310 HIS 311 -0.0025

HIS 311 GLY 312 -0.0001

GLY 312 PHE 313 0.0004

PHE 313 TRP 314 0.0000

TRP 314 HIS 315 -0.0127

HIS 315 TYR 316 0.0001

TYR 316 CYS 317 0.0112

CYS 317 ILE 318 -0.0002

ILE 318 ILE 319 0.0056

ILE 319 LEU 320 0.0000

LEU 320 SER 321 0.0046

SER 321 THR 322 0.0002

THR 322 THR 323 0.0058

THR 323 MET 324 -0.0000

MET 324 MET 325 -0.0042

MET 325 LEU 326 0.0001

LEU 326 LEU 327 0.0123

LEU 327 GLY 328 0.0001

GLY 328 CYS 329 0.0046

CYS 329 TYR 330 -0.0001

TYR 330 TYR 331 0.0137

TYR 331 ASP 332 0.0001

ASP 332 LEU 333 0.0004

LEU 333 GLU 334 -0.0002

GLU 334 GLU 335 0.0053

GLU 335 PHE 336 -0.0003

PHE 336 GLU 337 0.0273

GLU 337 LEU 338 0.0002

LEU 338 ALA 339 0.0294

ALA 339 LYS 340 -0.0001

LYS 340 CYS 341 0.0054

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: October 18th, 2018.

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

*** ***

CA strain for 22092323273356655

--- normal mode 10 ---

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

* *