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

* *

CA strain for 22122720241827122

--- normal mode 7 ---

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 GLU 2 0.0001

GLU 2 LEU 3 0.0082

LEU 3 ARG 4 -0.0002

ARG 4 HIS 5 -0.0082

HIS 5 THR 6 0.0002

THR 6 PRO 7 -0.0107

PRO 7 ALA 8 0.0003

ALA 8 ARG 9 -0.0015

ARG 9 ASP 10 0.0000

ASP 10 LEU 11 -0.0008

LEU 11 ASP 12 0.0002

ASP 12 LYS 13 -0.0169

LYS 13 PHE 14 -0.0001

PHE 14 ILE 15 0.0163

ILE 15 GLU 16 0.0001

GLU 16 ASP 17 0.0071

ASP 17 HIS 18 0.0001

HIS 18 LEU 19 -0.0001

LEU 19 LEU 20 0.0000

LEU 20 PRO 21 0.0682

PRO 21 ASN 22 0.0001

ASN 22 THR 23 0.0584

THR 23 CYS 24 -0.0001

CYS 24 PHE 25 -0.0192

PHE 25 ARG 26 -0.0001

ARG 26 THR 27 0.0105

THR 27 GLN 28 0.0001

GLN 28 VAL 29 0.0044

VAL 29 LYS 30 -0.0000

LYS 30 GLU 31 0.0247

GLU 31 ALA 32 0.0003

ALA 32 ILE 33 0.0088

ILE 33 ASP 34 0.0002

ASP 34 ILE 35 0.0243

ILE 35 VAL 36 -0.0001

VAL 36 CYS 37 -0.0025

CYS 37 ARG 38 0.0001

ARG 38 PHE 39 0.0228

PHE 39 LEU 40 0.0002

LEU 40 LYS 41 -0.0100

LYS 41 GLU 42 0.0001

GLU 42 ARG 43 0.0264

ARG 43 CYS 44 -0.0002

CYS 44 PHE 45 -0.0140

PHE 45 GLN 46 -0.0001

GLN 46 GLY 47 0.0156

GLY 47 THR 48 -0.0002

THR 48 ALA 49 -0.0135

ALA 49 ASP 50 0.0004

ASP 50 PRO 51 0.0343

PRO 51 VAL 52 -0.0001

VAL 52 ARG 53 0.0224

ARG 53 VAL 54 0.0002

VAL 54 SER 55 0.1253

SER 55 LYS 56 0.0000

LYS 56 VAL 57 -0.0153

VAL 57 VAL 58 0.0000

VAL 58 LYS 59 -0.0236

LYS 59 GLY 60 -0.0003

GLY 60 GLY 61 -0.0304

GLY 61 SER 62 0.0002

SER 62 SER 63 -0.0217

SER 63 GLY 64 -0.0003

GLY 64 LYS 65 0.0332

LYS 65 GLY 66 0.0002

GLY 66 THR 67 -0.0321

THR 67 THR 68 -0.0003

THR 68 LEU 69 0.0109

LEU 69 ARG 70 0.0000

ARG 70 GLY 71 -0.0273

GLY 71 ARG 72 0.0002

ARG 72 SER 73 -0.0360

SER 73 ASP 74 0.0003

ASP 74 ALA 75 -0.0746

ALA 75 ASP 76 -0.0005

ASP 76 LEU 77 -0.0409

LEU 77 VAL 78 0.0002

VAL 78 VAL 79 -0.0275

VAL 79 PHE 80 -0.0005

PHE 80 LEU 81 0.0277

LEU 81 THR 82 -0.0003

THR 82 LYS 83 0.0027

LYS 83 LEU 84 0.0004

LEU 84 THR 85 0.0131

THR 85 SER 86 0.0003

SER 86 PHE 87 -0.0162

PHE 87 GLU 88 -0.0002

GLU 88 ASP 89 -0.0400

ASP 89 GLN 90 -0.0002

GLN 90 LEU 91 0.0157

LEU 91 ARG 92 -0.0002

ARG 92 ARG 93 -0.0486

ARG 93 ARG 94 0.0000

ARG 94 GLY 95 0.0139

GLY 95 GLU 96 -0.0001

GLU 96 PHE 97 0.0171

PHE 97 ILE 98 -0.0004

ILE 98 GLN 99 -0.0253

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 -0.0054

ILE 101 ARG 102 0.0001

ARG 102 ARG 103 0.0186

ARG 103 GLN 104 -0.0000

GLN 104 LEU 105 -0.0236

LEU 105 GLU 106 -0.0001

GLU 106 ALA 107 -0.0022

ALA 107 CYS 108 0.0001

CYS 108 GLN 109 -0.0057

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 -0.0090

GLU 111 GLN 112 0.0004

GLN 112 LYS 113 0.0085

LYS 113 PHE 114 0.0001

PHE 114 LYS 115 -0.0029

LYS 115 VAL 116 0.0003

VAL 116 THR 117 0.0000

THR 117 PHE 118 0.0001

PHE 118 GLY 119 -0.0957

GLY 119 VAL 120 -0.0002

VAL 120 GLN 121 0.0522

GLN 121 SER 122 0.0001

SER 122 PRO 123 -0.0819

PRO 123 ARG 124 0.0003

ARG 124 ARG 125 -0.0426

ARG 125 GLU 126 -0.0001

GLU 126 GLY 127 0.1358

GLY 127 PRO 128 0.0001

PRO 128 ARG 129 -0.0682

ARG 129 ALA 130 -0.0001

ALA 130 LEU 131 0.0121

LEU 131 SER 132 0.0002

SER 132 PHE 133 0.0612

PHE 133 VAL 134 0.0001

VAL 134 LEU 135 -0.0014

LEU 135 SER 136 -0.0001

SER 136 SER 137 0.0078

SER 137 PRO 138 0.0001

PRO 138 GLN 139 0.0075

GLN 139 LEU 140 -0.0000

LEU 140 GLN 141 -0.0134

GLN 141 GLN 142 -0.0001

GLN 142 GLU 143 0.0433

GLU 143 VAL 144 -0.0000

VAL 144 GLU 145 0.0796

GLU 145 PHE 146 0.0000

PHE 146 ASP 147 0.0372

ASP 147 VAL 148 0.0001

VAL 148 LEU 149 0.0038

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 0.0191

ALA 151 PHE 152 -0.0001

PHE 152 ASP 153 0.0315

ASP 153 ALA 154 -0.0000

ALA 154 LEU 155 0.0359

LEU 155 GLY 156 0.0001

GLY 156 GLN 157 0.0143

GLN 157 TRP 158 -0.0004

TRP 158 THR 159 0.0220

THR 159 PRO 160 0.0002

PRO 160 GLY 161 -0.0120

GLY 161 TYR 162 -0.0000

TYR 162 LYS 163 0.0011

LYS 163 PRO 164 0.0004

PRO 164 ASN 165 -0.0246

ASN 165 PRO 166 0.0001

PRO 166 GLU 167 0.0107

GLU 167 ILE 168 0.0001

ILE 168 TYR 169 0.0041

TYR 169 VAL 170 0.0000

VAL 170 GLN 171 0.0600

GLN 171 LEU 172 -0.0001

LEU 172 ILE 173 0.0136

ILE 173 LYS 174 0.0001

LYS 174 GLU 175 0.0022

GLU 175 CYS 176 -0.0000

CYS 176 LYS 177 0.0081

LYS 177 SER 178 0.0001

SER 178 ARG 179 -0.0003

ARG 179 GLY 180 -0.0001

GLY 180 ALA 181 0.0785

ALA 181 GLU 182 -0.0001

GLU 182 GLY 183 0.0332

GLY 183 GLU 184 -0.0001

GLU 184 PHE 185 0.0146

PHE 185 SER 186 -0.0002

SER 186 THR 187 -0.0448

THR 187 CYS 188 -0.0001

CYS 188 PHE 189 0.0111

PHE 189 THR 190 0.0005

THR 190 GLU 191 -0.0410

GLU 191 LEU 192 -0.0000

LEU 192 GLN 193 -0.0233

GLN 193 ARG 194 -0.0001

ARG 194 ARG 194 0.0000

ARG 194 ASP 195 -0.0181

ASP 195 PHE 196 0.0003

PHE 196 LEU 197 -0.0096

LEU 197 ARG 198 -0.0001

ARG 198 ASN 199 0.0323

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 0.0439

PRO 201 THR 202 -0.0001

THR 202 LYS 203 0.0410

LYS 203 LEU 204 -0.0001

LEU 204 LYS 205 0.0023

LYS 205 SER 206 0.0003

SER 206 LEU 207 0.0079

LEU 207 ILE 208 -0.0003

ILE 208 ARG 209 0.0020

ARG 209 LEU 210 -0.0000

LEU 210 VAL 211 0.0223

VAL 211 LYS 212 0.0000

LYS 212 HIS 213 0.0010

HIS 213 TRP 214 -0.0004

TRP 214 TYR 215 0.0217

TYR 215 GLN 216 -0.0001

GLN 216 THR 217 -0.0198

THR 217 CYS 218 -0.0003

CYS 218 GLU 219 0.0081

GLU 219 LYS 220 -0.0002

LYS 220 THR 221 -0.0075

THR 221 HIS 222 -0.0005

HIS 222 GLY 223 0.0001

GLY 223 GLY 224 0.0003

GLY 224 LYS 225 0.0198

LYS 225 LEU 226 0.0004

LEU 226 PRO 227 -0.0304

PRO 227 PRO 228 -0.0004

PRO 228 GLN 229 0.0511

GLN 229 TYR 230 -0.0000

TYR 230 ALA 231 -0.0100

ALA 231 LEU 232 0.0001

LEU 232 GLU 233 -0.0165

GLU 233 LEU 234 0.0002

LEU 234 LEU 235 -0.0120

LEU 235 THR 236 0.0001

THR 236 VAL 237 0.0290

VAL 237 TYR 238 -0.0003

TYR 238 ALA 239 0.0207

ALA 239 TRP 240 0.0003

TRP 240 GLU 241 -0.0044

GLU 241 GLN 242 0.0001

GLN 242 GLY 243 0.0079

GLY 243 SER 244 0.0001

SER 244 ARG 245 0.0213

ARG 245 LYS 246 -0.0000

LYS 246 THR 247 -0.0087

THR 247 ASP 248 -0.0000

ASP 248 PHE 249 0.0319

PHE 249 SER 250 0.0001

SER 250 THR 251 -0.0217

THR 251 ALA 252 0.0000

ALA 252 GLN 253 -0.0128

GLN 253 GLY 254 -0.0004

GLY 254 PHE 255 0.0098

PHE 255 GLN 256 0.0001

GLN 256 THR 257 0.0073

THR 257 VAL 258 0.0002

VAL 258 LEU 259 0.0200

LEU 259 GLU 260 -0.0000

GLU 260 LEU 261 -0.0032

LEU 261 VAL 262 -0.0001

VAL 262 LEU 263 0.0026

LEU 263 LYS 264 -0.0002

LYS 264 HIS 265 -0.0182

HIS 265 GLN 266 0.0001

GLN 266 LYS 267 0.0399

LYS 267 LEU 268 0.0001

LEU 268 CYS 269 0.0648

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0971

PHE 271 TRP 272 0.0000

TRP 272 GLU 273 0.0609

GLU 273 ALA 274 -0.0002

ALA 274 TYR 275 0.0366

TYR 275 TYR 276 0.0001

TYR 276 ASP 277 -0.0111

ASP 277 PHE 278 0.0001

PHE 278 THR 279 0.0334

THR 279 ASN 280 0.0002

ASN 280 PRO 281 -0.0054

PRO 281 VAL 282 -0.0001

VAL 282 VAL 283 -0.0057

VAL 283 GLY 284 0.0001

GLY 284 ARG 285 -0.0130

ARG 285 CYS 286 0.0001

CYS 286 MET 287 -0.0101

MET 287 LEU 288 0.0003

LEU 288 GLN 289 -0.0104

GLN 289 GLN 290 -0.0004

GLN 290 LEU 291 -0.0585

LEU 291 LYS 292 -0.0001

LYS 292 LYS 293 0.0525

LYS 293 PRO 294 -0.0001

PRO 294 ARG 295 -0.0248

ARG 295 PRO 296 -0.0002

PRO 296 VAL 297 -0.0002

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0090

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 -0.0049

PRO 301 ALA 302 -0.0002

ALA 302 ASP 303 0.0171

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 -0.0106

THR 305 GLY 306 0.0001

GLY 306 ASN 307 -0.1545

ASN 307 VAL 308 0.0003

VAL 308 GLY 309 -0.0676

GLY 309 GLY 310 0.0002

GLY 310 GLY 311 0.0541

GLY 311 ASP 312 -0.0003

ASP 312 THR 313 -0.0168

THR 313 HIS 314 0.0001

HIS 314 SER 315 -0.0070

SER 315 TRP 316 -0.0003

TRP 316 GLN 317 -0.0067

GLN 317 ARG 318 0.0001

ARG 318 LEU 319 -0.0001

LEU 319 ALA 320 -0.0000

ALA 320 GLN 321 0.0063

GLN 321 GLU 322 -0.0002

GLU 322 ALA 323 0.0129

ALA 323 ARG 324 -0.0002

ARG 324 VAL 325 -0.0031

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 -0.0042

LEU 327 GLY 328 0.0002

GLY 328 TYR 329 0.0000

TYR 329 PRO 330 -0.0002

PRO 330 CYS 331 0.0013

CYS 331 CYS 332 0.0000

CYS 332 LYS 333 0.0011

LYS 333 ASN 334 0.0001

ASN 334 LEU 335 0.0089

LEU 335 ASP 336 0.0000

ASP 336 GLY 337 -0.0221

GLY 337 SER 338 -0.0002

SER 338 LEU 339 -0.0021

LEU 339 VAL 340 0.0002

VAL 340 GLY 341 0.0014

GLY 341 ALA 342 -0.0001

ALA 342 TRP 343 0.0255

TRP 343 THR 344 0.0002

THR 344 MET 345 -0.0044

MET 345 LEU 346 -0.0001

LEU 346 GLN 347 0.0018

GLN 347 LYS 348 -0.0002

LYS 348 ILE 349 0.0001

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 22122720241827122

--- normal mode 7 ---

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

* *