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

* *

CA strain for 230101190352136506

--- normal mode 13 ---

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
PHE 1 ASP 2 0.0001

ASP 2 MET 3 -0.0650

MET 3 ILE 4 0.0001

ILE 4 ARG 5 0.0133

ARG 5 LEU 6 -0.0001

LEU 6 ALA 7 -0.0085

ALA 7 THR 8 -0.0001

THR 8 ASN 9 0.0107

ASN 9 LYS 10 0.0002

LYS 10 PHE 11 -0.0100

PHE 11 SER 12 -0.0003

SER 12 GLU 13 0.0127

GLU 13 ASP 14 0.0000

ASP 14 ASN 15 0.0055

ASN 15 LYS 16 0.0000

LYS 16 ILE 17 0.0016

ILE 17 GLY 18 0.0002

GLY 18 GLU 19 -0.0625

GLU 19 GLY 20 0.0001

GLY 20 GLY 21 -0.1295

GLY 21 PHE 22 -0.0002

PHE 22 GLY 23 -0.0781

GLY 23 ASP 24 -0.0002

ASP 24 VAL 25 0.0217

VAL 25 TYR 26 -0.0000

TYR 26 LYS 27 -0.0001

LYS 27 GLY 28 -0.0000

GLY 28 MET 29 -0.0106

MET 29 PHE 30 0.0002

PHE 30 PRO 31 0.0127

PRO 31 ASN 32 0.0001

ASN 32 GLY 33 -0.0636

GLY 33 TYR 34 0.0001

TYR 34 GLU 35 -0.0530

GLU 35 ILE 36 0.0001

ILE 36 ALA 37 0.0004

ALA 37 VAL 38 0.0000

VAL 38 LYS 39 0.0022

LYS 39 ARG 40 -0.0001

ARG 40 LEU 41 -0.0349

LEU 41 ILE 42 -0.0003

ILE 42 ARG 43 0.0994

ARG 43 ASN 44 0.0002

ASN 44 SER 45 0.0425

SER 45 SER 46 0.0001

SER 46 GLN 47 -0.0023

GLN 47 GLY 48 0.0001

GLY 48 ALA 49 -0.0247

ALA 49 VAL 50 0.0001

VAL 50 GLU 51 0.0125

GLU 51 PHE 52 -0.0000

PHE 52 LYS 53 0.0041

LYS 53 ASN 54 0.0002

ASN 54 GLU 55 -0.0114

GLU 55 VAL 56 -0.0001

VAL 56 LEU 57 0.0433

LEU 57 LEU 58 -0.0001

LEU 58 ILE 59 0.0254

ILE 59 ALA 60 -0.0006

ALA 60 LYS 61 0.0483

LYS 61 LEU 62 0.0003

LEU 62 GLN 63 -0.0058

GLN 63 HIS 64 0.0000

HIS 64 ARG 65 -0.0538

ARG 65 ASN 66 -0.0002

ASN 66 LEU 67 -0.0099

LEU 67 VAL 68 -0.0000

VAL 68 ARG 69 -0.0065

ARG 69 LEU 70 0.0002

LEU 70 LEU 71 0.0676

LEU 71 GLY 72 0.0000

GLY 72 PHE 73 -0.0448

PHE 73 CYS 74 -0.0003

CYS 74 ILE 75 -0.0306

ILE 75 GLN 76 0.0003

GLN 76 ARG 77 0.0119

ARG 77 ASN 78 0.0000

ASN 78 GLU 79 0.0114

GLU 79 LYS 80 0.0004

LYS 80 ILE 81 0.0030

ILE 81 LEU 82 0.0000

LEU 82 ILE 83 0.0054

ILE 83 TYR 84 0.0004

TYR 84 GLU 85 -0.0348

GLU 85 TYR 86 -0.0001

TYR 86 MET 87 -0.0733

MET 87 HIS 88 0.0001

HIS 88 ASN 89 -0.0834

ASN 89 LYS 90 0.0000

LYS 90 SER 91 -0.0442

SER 91 LEU 92 -0.0001

LEU 92 ASP 93 -0.0158

ASP 93 TYR 94 -0.0001

TYR 94 TYR 95 0.0127

TYR 95 LEU 96 0.0000

LEU 96 PHE 97 -0.0099

PHE 97 SER 98 0.0003

SER 98 PRO 99 0.0037

PRO 99 GLU 100 -0.0004

GLU 100 ASN 101 -0.0052

ASN 101 HIS 102 -0.0001

HIS 102 ARG 103 0.0126

ARG 103 LYS 104 0.0000

LYS 104 LEU 105 0.0070

LEU 105 THR 106 0.0000

THR 106 TRP 107 0.0037

TRP 107 HIS 108 -0.0005

HIS 108 ALA 109 -0.0151

ALA 109 ARG 110 -0.0004

ARG 110 TYR 111 0.0063

TYR 111 LYS 112 -0.0001

LYS 112 ILE 113 0.0078

ILE 113 ILE 114 -0.0001

ILE 114 ARG 115 -0.0009

ARG 115 GLY 116 -0.0002

GLY 116 ILE 117 0.0013

ILE 117 ALA 118 0.0001

ALA 118 ARG 119 0.0045

ARG 119 GLY 120 -0.0000

GLY 120 ILE 121 0.0037

ILE 121 LEU 122 -0.0001

LEU 122 TYR 123 0.0013

TYR 123 LEU 124 -0.0003

LEU 124 HIS 125 0.0145

HIS 125 GLU 126 -0.0002

GLU 126 ASP 127 0.0049

ASP 127 SER 128 -0.0003

SER 128 HIS 129 0.0094

HIS 129 LEU 130 0.0003

LEU 130 LYS 131 0.0065

LYS 131 ILE 132 -0.0001

ILE 132 ILE 133 0.0251

ILE 133 HIS 134 -0.0001

HIS 134 CYS 135 0.0042

CYS 135 ASP 136 -0.0003

ASP 136 LEU 137 0.0232

LEU 137 LYS 138 0.0000

LYS 138 PRO 139 0.0294

PRO 139 SER 140 0.0001

SER 140 ASN 141 0.0226

ASN 141 ILE 142 0.0000

ILE 142 LEU 143 -0.0143

LEU 143 LEU 144 0.0001

LEU 144 ASP 145 -0.0004

ASP 145 ASP 146 -0.0003

ASP 146 LYS 147 -0.0087

LYS 147 MET 148 -0.0004

MET 148 ASN 149 -0.0182

ASN 149 ALA 150 0.0002

ALA 150 LYS 151 -0.0041

LYS 151 ILE 152 0.0005

ILE 152 SER 153 0.0115

SER 153 ASP 154 -0.0001

ASP 154 PHE 155 0.0337

PHE 155 GLY 156 -0.0002

GLY 156 LEU 157 0.0396

LEU 157 ALA 158 -0.0001

ALA 158 ARG 159 -0.0245

ARG 159 ILE 160 -0.0002

ILE 160 VAL 161 -0.0046

VAL 161 ALA 162 -0.0002

ALA 162 ILE 163 -0.0098

ILE 163 ASP 164 0.0002

ASP 164 GLN 165 -0.0021

GLN 165 MET 166 0.0003

MET 166 GLN 167 -0.0207

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 -0.0099

ASN 169 THR 170 -0.0001

THR 170 SER 171 -0.0051

SER 171 ILE 172 0.0001

ILE 172 ILE 173 -0.0057

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 0.0057

GLY 175 THR 176 -0.0000

THR 176 TYR 177 0.1236

TYR 177 GLY 178 0.0000

GLY 178 TYR 179 0.0408

TYR 179 MET 180 0.0001

MET 180 SER 181 -0.0172

SER 181 PRO 182 0.0000

PRO 182 GLU 183 0.0278

GLU 183 TYR 184 -0.0003

TYR 184 ALA 185 0.0051

ALA 185 MET 186 0.0003

MET 186 LEU 187 -0.0147

LEU 187 GLY 188 0.0001

GLY 188 GLN 189 -0.0132

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 -0.0320

SER 191 VAL 192 -0.0003

VAL 192 LYS 193 0.0344

LYS 193 SER 194 -0.0002

SER 194 ASP 195 -0.0139

ASP 195 VAL 196 0.0001

VAL 196 PHE 197 -0.0022

PHE 197 SER 198 0.0002

SER 198 PHE 199 -0.0021

PHE 199 GLY 200 0.0000

GLY 200 VAL 201 0.0004

VAL 201 ILE 202 0.0002

ILE 202 MET 203 0.0197

MET 203 LEU 204 -0.0001

LEU 204 GLU 205 -0.0112

GLU 205 ILE 206 0.0001

ILE 206 VAL 207 -0.0017

VAL 207 SER 208 -0.0001

SER 208 GLY 209 -0.0126

GLY 209 LYS 210 -0.0001

LYS 210 ARG 211 0.0391

ARG 211 ASN 212 -0.0001

ASN 212 VAL 213 0.0193

VAL 213 ASP 214 0.0001

ASP 214 TYR 215 -0.0057

TYR 215 ASN 216 -0.0002

ASN 216 GLY 217 0.0375

GLY 217 VAL 218 0.0001

VAL 218 ASN 219 0.0057

ASN 219 SER 220 -0.0001

SER 220 ILE 221 0.0400

ILE 221 ASP 222 -0.0002

ASP 222 ASP 223 -0.0023

ASP 223 LEU 224 -0.0003

LEU 224 VAL 225 -0.0066

VAL 225 SER 226 -0.0003

SER 226 HIS 227 0.0049

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 -0.0071

TRP 229 LYS 230 -0.0001

LYS 230 LYS 231 -0.0014

LYS 231 TRP 232 -0.0003

TRP 232 THR 233 -0.0014

THR 233 GLU 234 0.0001

GLU 234 ASN 235 -0.0024

ASN 235 LYS 236 0.0002

LYS 236 GLN 237 -0.0040

GLN 237 MET 238 -0.0004

MET 238 GLU 239 0.0081

GLU 239 LEU 240 0.0002

LEU 240 LEU 241 -0.0081

LEU 241 ASP 242 0.0001

ASP 242 PRO 243 0.0047

PRO 243 ALA 244 -0.0000

ALA 244 LEU 245 -0.0044

LEU 245 THR 246 -0.0001

THR 246 TYR 247 0.0126

TYR 247 SER 248 -0.0002

SER 248 PHE 249 -0.0052

PHE 249 SER 250 -0.0001

SER 250 GLU 251 -0.0039

GLU 251 THR 252 -0.0000

THR 252 GLU 253 -0.0002

GLU 253 VAL 254 0.0002

VAL 254 SER 255 -0.0085

SER 255 ARG 256 0.0003

ARG 256 CYS 257 0.0062

CYS 257 ILE 258 0.0003

ILE 258 GLN 259 -0.0028

GLN 259 LEU 260 0.0000

LEU 260 GLY 261 0.0026

GLY 261 LEU 262 -0.0002

LEU 262 LEU 263 0.0026

LEU 263 CYS 264 -0.0005

CYS 264 VAL 265 -0.0059

VAL 265 GLN 266 -0.0002

GLN 266 GLU 267 -0.0160

GLU 267 ASN 268 -0.0002

ASN 268 PRO 269 0.0219

PRO 269 ASP 270 -0.0002

ASP 270 GLN 271 -0.0025

GLN 271 ARG 272 0.0002

ARG 272 PRO 273 -0.0274

PRO 273 THR 274 0.0001

THR 274 MET 275 0.0068

MET 275 ALA 276 -0.0003

ALA 276 THR 277 0.0016

THR 277 ILE 278 0.0001

ILE 278 ALA 279 -0.0025

ALA 279 LEU 280 -0.0000

LEU 280 TYR 281 0.0004

TYR 281 PHE 282 -0.0002

PHE 282 ASN 283 0.0045

ASN 283 ILE 284 -0.0000

ILE 284 ASP 285 -0.0033

ASP 285 SER 286 -0.0000

SER 286 ILE 287 -0.0057

ILE 287 ASP 288 -0.0002

ASP 288 LEU 289 -0.0104

LEU 289 PRO 290 0.0001

PRO 290 LEU 291 -0.0032

LEU 291 PRO 292 -0.0001

PRO 292 GLN 293 -0.0241

GLN 293 GLN 294 -0.0001

GLN 294 PRO 295 -0.0071

PRO 295 PRO 296 0.0002

PRO 296 PHE 297 -0.0130

PHE 297 TYR 298 0.0002

TYR 298 MET 299 -0.0190

MET 299 ARG 300 -0.0001

ARG 300 GLY 301 0.0969

GLY 301 LYS 302 0.0001

LYS 302 ILE 303 0.0127

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 -0.0456

SER 305 LYS 306 0.0000

LYS 306 VAL 307 0.0224

VAL 307 ALA 308 -0.0000

ALA 308 SER 309 -0.1232

SER 309 LYS 310 0.0000

LYS 310 LYS 311 -0.0798

LYS 311 THR 312 0.0001

THR 312 MET 313 0.0699

MET 313 SER 314 0.0003

SER 314 GLY 315 0.0379

GLY 315 ARG 316 0.0001

ARG 316 PRO 317 -0.2590

PRO 317 ARG 318 -0.0001

ARG 318 SER 319 0.2304

SER 319 TYR 320 0.0001

TYR 320 SER 321 -0.0560

SER 321 VAL 322 -0.0002

VAL 322 THR 323 0.0512

THR 323 ARG 324 0.0000

ARG 324 PHE 325 -0.3836

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 230101190352136506

--- normal mode 13 ---

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

* *