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

* *

CA strain for 22092323273356655

--- normal mode 11 ---

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 -0.0023

GLU 3 LEU 4 0.0004

LEU 4 LEU 5 -0.0058

LEU 5 THR 6 -0.0000

THR 6 VAL 7 -0.0078

VAL 7 GLN 8 -0.0001

GLN 8 GLN 9 0.0044

GLN 9 VAL 10 -0.0000

VAL 10 ASP 11 0.0092

ASP 11 PRO 12 -0.0002

PRO 12 TRP 13 0.0137

TRP 13 LEU 14 0.0000

LEU 14 GLN 15 0.0414

GLN 15 PHE 16 -0.0002

PHE 16 ASN 17 0.0689

ASN 17 PRO 18 0.0005

PRO 18 HIS 19 0.0429

HIS 19 ILE 20 -0.0001

ILE 20 VAL 21 -0.0223

VAL 21 SER 22 0.0003

SER 22 GLY 23 0.0144

GLY 23 TYR 24 0.0003

TYR 24 ARG 25 0.0178

ARG 25 PRO 26 0.0001

PRO 26 ARG 27 -0.0074

ARG 27 MET 28 -0.0003

MET 28 SER 29 0.0089

SER 29 VAL 30 -0.0001

VAL 30 ARG 31 -0.0054

ARG 31 ALA 32 0.0000

ALA 32 ALA 33 0.0025

ALA 33 LEU 34 0.0000

LEU 34 ARG 35 -0.0077

ARG 35 SER 36 0.0005

SER 36 PHE 37 0.0120

PHE 37 PHE 38 0.0002

PHE 38 GLU 39 -0.0057

GLU 39 TRP 40 -0.0002

TRP 40 HIS 41 0.0085

HIS 41 ASN 42 -0.0001

ASN 42 GLU 43 0.0078

GLU 43 SER 44 0.0001

SER 44 PHE 45 0.0054

PHE 45 ASN 46 -0.0001

ASN 46 VAL 47 -0.0044

VAL 47 TRP 48 -0.0001

TRP 48 SER 49 0.0472

SER 49 HIS 50 -0.0002

HIS 50 ALA 51 0.0044

ALA 51 LEU 52 -0.0003

LEU 52 ALA 53 0.0218

ALA 53 ALA 54 0.0002

ALA 54 CYS 55 0.0084

CYS 55 PHE 56 0.0002

PHE 56 VAL 57 -0.0059

VAL 57 LEU 58 0.0003

LEU 58 TYR 59 0.0228

TYR 59 LEU 60 0.0003

LEU 60 ALA 61 -0.0037

ALA 61 LEU 62 0.0000

LEU 62 PHE 63 0.0242

PHE 63 PRO 64 -0.0000

PRO 64 PRO 65 0.0409

PRO 65 THR 66 0.0001

THR 66 MET 67 0.0253

MET 67 GLU 68 -0.0002

GLU 68 ILE 69 0.0253

ILE 69 SER 70 -0.0004

SER 70 THR 71 0.0618

THR 71 THR 72 -0.0002

THR 72 SER 73 0.0309

SER 73 THR 74 -0.0003

THR 74 VAL 75 0.0205

VAL 75 ASN 76 -0.0001

ASN 76 GLY 77 0.0042

GLY 77 ARG 78 0.0004

ARG 78 GLY 79 -0.0511

GLY 79 VAL 80 0.0001

VAL 80 GLY 81 0.0662

GLY 81 THR 82 0.0000

THR 82 SER 83 -0.0184

SER 83 GLY 84 -0.0000

GLY 84 MET 85 -0.0106

MET 85 ALA 86 0.0001

ALA 86 PRO 87 -0.0385

PRO 87 THR 88 0.0000

THR 88 ASP 89 0.0269

ASP 89 VAL 90 -0.0002

VAL 90 SER 91 0.0845

SER 91 LEU 92 -0.0001

LEU 92 THR 93 0.0121

THR 93 PRO 94 -0.0003

PRO 94 HIS 95 0.0043

HIS 95 ASP 96 0.0002

ASP 96 ARG 97 -0.0100

ARG 97 ARG 98 -0.0001

ARG 98 TRP 99 -0.0030

TRP 99 LEU 100 -0.0002

LEU 100 GLY 101 0.0078

GLY 101 SER 102 0.0001

SER 102 SER 103 0.0072

SER 103 SER 104 -0.0002

SER 104 GLU 105 0.0116

GLU 105 HIS 106 -0.0002

HIS 106 LEU 107 0.0183

LEU 107 LEU 108 0.0001

LEU 108 GLY 109 0.0048

GLY 109 ALA 110 0.0000

ALA 110 SER 111 0.0249

SER 111 SER 112 -0.0002

SER 112 THR 113 -0.0001

THR 113 THR 114 0.0002

THR 114 THR 115 0.0152

THR 115 PHE 116 -0.0001

PHE 116 ARG 117 -0.0043

ARG 117 CYS 118 -0.0003

CYS 118 THR 119 0.0013

THR 119 CYS 120 0.0001

CYS 120 LEU 121 0.0042

LEU 121 VAL 122 0.0003

VAL 122 PHE 123 -0.0092

PHE 123 PHE 124 0.0002

PHE 124 PHE 125 0.0225

PHE 125 ILE 126 -0.0000

ILE 126 PHE 127 -0.0212

PHE 127 ILE 128 0.0001

ILE 128 CYS 129 0.0197

CYS 129 SER 130 0.0000

SER 130 VAL 131 -0.0094

VAL 131 VAL 132 0.0000

VAL 132 TYR 133 0.0235

TYR 133 HIS 134 -0.0000

HIS 134 LEU 135 -0.0070

LEU 135 PHE 136 -0.0002

PHE 136 MET 137 0.0153

MET 137 PRO 138 0.0001

PRO 138 CYS 139 -0.0062

CYS 139 THR 140 0.0003

THR 140 THR 141 0.0099

THR 141 SER 142 0.0002

SER 142 GLU 143 -0.0091

GLU 143 SER 144 0.0003

SER 144 LEU 145 -0.0103

LEU 145 TYR 146 0.0002

TYR 146 ARG 147 -0.0040

ARG 147 ARG 148 0.0001

ARG 148 LEU 149 -0.0083

LEU 149 LEU 150 -0.0001

LEU 150 SER 151 0.0021

SER 151 CYS 152 0.0002

CYS 152 ASP 153 -0.0021

ASP 153 VAL 154 0.0002

VAL 154 PHE 155 0.0074

PHE 155 GLY 156 -0.0002

GLY 156 VAL 157 -0.0020

VAL 157 VAL 158 0.0001

VAL 158 ILE 159 0.0055

ILE 159 CYS 160 -0.0002

CYS 160 ILE 161 0.0010

ILE 161 THR 162 -0.0002

THR 162 GLY 163 0.0093

GLY 163 THR 164 0.0001

THR 164 SER 165 -0.0042

SER 165 TRP 166 0.0002

TRP 166 SER 167 0.0002

SER 167 LEU 168 0.0001

LEU 168 VAL 169 -0.0039

VAL 169 TYR 170 0.0001

TYR 170 ARG 171 0.0079

ARG 171 GLY 172 -0.0003

GLY 172 ASN 173 0.0023

ASN 173 ALA 174 0.0000

ALA 174 CYS 175 -0.0001

CYS 175 SER 176 -0.0003

SER 176 GLN 177 0.0036

GLN 177 ASN 178 -0.0000

ASN 178 TRP 179 0.0000

TRP 179 SER 180 -0.0002

SER 180 CYS 181 -0.0007

CYS 181 HIS 182 0.0000

HIS 182 VAL 183 0.0079

VAL 183 GLY 184 -0.0001

GLY 184 MET 185 -0.0003

MET 185 GLY 186 -0.0001

GLY 186 ALA 187 0.0141

ALA 187 LEU 188 -0.0002

LEU 188 LEU 189 -0.0055

LEU 189 LEU 190 -0.0000

LEU 190 SER 191 0.0098

SER 191 ALA 192 -0.0001

ALA 192 LEU 193 -0.0053

LEU 193 PHE 194 -0.0000

PHE 194 VAL 195 0.0084

VAL 195 LEU 196 -0.0003

LEU 196 TYR 197 -0.0028

TYR 197 GLY 198 0.0003

GLY 198 ALA 199 0.0018

ALA 199 VAL 200 -0.0001

VAL 200 PHE 201 -0.0058

PHE 201 ASN 202 -0.0001

ASN 202 ALA 203 0.0198

ALA 203 SER 204 -0.0001

SER 204 CYS 205 -0.0024

CYS 205 GLY 206 0.0002

GLY 206 SER 207 0.0254

SER 207 PHE 208 0.0003

PHE 208 GLY 209 0.0312

GLY 209 ARG 210 0.0000

ARG 210 PHE 211 0.0042

PHE 211 LYS 212 -0.0005

LYS 212 ALA 213 0.0483

ALA 213 ILE 214 0.0001

ILE 214 GLY 215 -0.0090

GLY 215 PHE 216 -0.0003

PHE 216 HIS 217 0.0058

HIS 217 SER 218 -0.0000

SER 218 VAL 219 0.0101

VAL 219 LEU 220 -0.0002

LEU 220 ARG 221 -0.0037

ARG 221 PHE 222 0.0004

PHE 222 LEU 223 0.0172

LEU 223 ILE 224 0.0002

ILE 224 LEU 225 -0.0054

LEU 225 LEU 226 -0.0001

LEU 226 TRP 227 0.0171

TRP 227 VAL 228 -0.0000

VAL 228 GLU 229 0.0015

GLU 229 LEU 230 -0.0000

LEU 230 PRO 231 -0.0014

PRO 231 LYS 232 0.0001

LYS 232 VAL 233 0.0047

VAL 233 GLN 234 0.0001

GLN 234 SER 235 0.0011

SER 235 GLN 236 0.0001

GLN 236 GLY 237 0.0051

GLY 237 TYR 238 0.0000

TYR 238 HIS 239 -0.0090

HIS 239 GLN 240 0.0001

GLN 240 ALA 241 0.0065

ALA 241 VAL 242 -0.0002

VAL 242 HIS 243 -0.0014

HIS 243 CYS 244 -0.0003

CYS 244 HIS 245 -0.0067

HIS 245 ALA 246 -0.0001

ALA 246 MET 247 0.0200

MET 247 SER 248 -0.0001

SER 248 PHE 249 -0.0061

PHE 249 VAL 250 0.0002

VAL 250 PHE 251 0.0257

PHE 251 LEU 252 0.0001

LEU 252 ALA 253 -0.0009

ALA 253 LEU 254 0.0001

LEU 254 GLY 255 0.0149

GLY 255 ALA 256 0.0003

ALA 256 VAL 257 0.0208

VAL 257 ILE 258 -0.0001

ILE 258 ASN 259 -0.0246

ASN 259 ALA 260 -0.0000

ALA 260 LEU 261 0.0766

LEU 261 ARG 262 -0.0000

ARG 262 PHE 263 0.0117

PHE 263 PRO 264 -0.0000

PRO 264 GLU 265 -0.0038

GLU 265 LYS 266 -0.0001

LYS 266 HIS 267 0.0536

HIS 267 LEU 268 0.0001

LEU 268 ARG 269 0.0004

ARG 269 ARG 270 -0.0002

ARG 270 ALA 271 0.0551

ALA 271 THR 272 0.0002

THR 272 ARG 273 0.0041

ARG 273 LEU 274 0.0001

LEU 274 LEU 275 0.0050

LEU 275 PRO 276 0.0000

PRO 276 ALA 277 0.0251

ALA 277 SER 278 0.0003

SER 278 SER 279 -0.0055

SER 279 SER 280 -0.0003

SER 280 SER 281 0.0062

SER 281 PRO 282 0.0004

PRO 282 GLU 283 -0.0038

GLU 283 ALA 284 0.0003

ALA 284 THR 285 0.0058

THR 285 VAL 286 -0.0001

VAL 286 ALA 287 0.0073

ALA 287 SER 288 -0.0001

SER 288 ARG 289 0.0096

ARG 289 CYS 290 0.0001

CYS 290 TRP 291 -0.0092

TRP 291 ARG 292 0.0002

ARG 292 TRP 293 0.0174

TRP 293 LEU 294 0.0004

LEU 294 GLY 295 0.0108

GLY 295 ARG 296 -0.0000

ARG 296 PHE 297 0.0102

PHE 297 VAL 298 -0.0000

VAL 298 VAL 299 -0.0064

VAL 299 SER 300 -0.0001

SER 300 GLY 301 0.0266

GLY 301 GLU 302 -0.0000

GLU 302 GLU 303 -0.0017

GLU 303 ILE 304 -0.0002

ILE 304 ASP 305 -0.0138

ASP 305 TYR 306 -0.0001

TYR 306 THR 307 0.0076

THR 307 TRP 308 0.0001

TRP 308 ASN 309 0.0150

ASN 309 SER 310 -0.0000

SER 310 HIS 311 -0.0068

HIS 311 GLY 312 0.0002

GLY 312 PHE 313 -0.0003

PHE 313 TRP 314 -0.0003

TRP 314 HIS 315 -0.0295

HIS 315 TYR 316 0.0000

TYR 316 CYS 317 0.0319

CYS 317 ILE 318 0.0001

ILE 318 ILE 319 0.0079

ILE 319 LEU 320 -0.0000

LEU 320 SER 321 0.0105

SER 321 THR 322 0.0001

THR 322 THR 323 0.0094

THR 323 MET 324 -0.0001

MET 324 MET 325 -0.0077

MET 325 LEU 326 0.0002

LEU 326 LEU 327 0.0245

LEU 327 GLY 328 0.0003

GLY 328 CYS 329 0.0007

CYS 329 TYR 330 0.0000

TYR 330 TYR 331 0.0144

TYR 331 ASP 332 0.0003

ASP 332 LEU 333 -0.0071

LEU 333 GLU 334 0.0002

GLU 334 GLU 335 -0.0037

GLU 335 PHE 336 0.0000

PHE 336 GLU 337 -0.0078

GLU 337 LEU 338 0.0001

LEU 338 ALA 339 -0.0135

ALA 339 LYS 340 -0.0003

LYS 340 CYS 341 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).
Last modification: October 18th, 2018.

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

*** ***

CA strain for 22092323273356655

--- normal mode 11 ---

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

* *