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

* *

CA strain for 2401161745071321422

--- 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 -0.0002

GLU 2 LEU 3 -0.0063

LEU 3 ARG 4 0.0000

ARG 4 HIS 5 0.0105

HIS 5 THR 6 -0.0001

THR 6 PRO 7 0.0119

PRO 7 ALA 8 0.0001

ALA 8 ARG 9 0.0068

ARG 9 ASP 10 -0.0001

ASP 10 LEU 11 -0.0085

LEU 11 ASP 12 0.0001

ASP 12 LYS 13 0.0196

LYS 13 PHE 14 -0.0001

PHE 14 ILE 15 -0.0140

ILE 15 GLU 16 0.0003

GLU 16 ASP 17 -0.0009

ASP 17 HIS 18 -0.0003

HIS 18 LEU 19 0.0064

LEU 19 LEU 20 0.0003

LEU 20 PRO 21 -0.0518

PRO 21 ASN 22 0.0002

ASN 22 THR 23 -0.0359

THR 23 CYS 24 -0.0002

CYS 24 PHE 25 0.0150

PHE 25 ARG 26 0.0001

ARG 26 THR 27 -0.0158

THR 27 GLN 28 -0.0001

GLN 28 VAL 29 0.0114

VAL 29 LYS 30 0.0000

LYS 30 GLU 31 -0.0320

GLU 31 ALA 32 -0.0001

ALA 32 ILE 33 -0.0051

ILE 33 ASP 34 -0.0001

ASP 34 ILE 35 -0.0234

ILE 35 VAL 36 0.0003

VAL 36 CYS 37 0.0184

CYS 37 ARG 38 0.0002

ARG 38 PHE 39 -0.0139

PHE 39 LEU 40 -0.0001

LEU 40 LYS 41 0.0135

LYS 41 GLU 42 -0.0002

GLU 42 ARG 43 -0.0112

ARG 43 CYS 44 0.0000

CYS 44 PHE 45 0.0171

PHE 45 GLN 46 0.0002

GLN 46 GLY 47 -0.0184

GLY 47 THR 48 -0.0000

THR 48 ALA 49 0.0316

ALA 49 ASP 50 0.0001

ASP 50 PRO 51 -0.0287

PRO 51 VAL 52 -0.0003

VAL 52 ARG 53 -0.0150

ARG 53 VAL 54 -0.0004

VAL 54 SER 55 -0.0772

SER 55 LYS 56 0.0002

LYS 56 VAL 57 0.0195

VAL 57 VAL 58 0.0004

VAL 58 LYS 59 0.0285

LYS 59 GLY 60 -0.0001

GLY 60 GLY 61 0.0595

GLY 61 SER 62 0.0004

SER 62 SER 63 0.0261

SER 63 GLY 64 0.0002

GLY 64 LYS 65 -0.0516

LYS 65 GLY 66 -0.0005

GLY 66 THR 67 0.0105

THR 67 THR 68 0.0001

THR 68 LEU 69 0.0281

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 0.0505

GLY 71 ARG 72 0.0002

ARG 72 SER 73 0.0764

SER 73 ASP 74 0.0001

ASP 74 ALA 75 0.0903

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 0.0472

LEU 77 VAL 78 -0.0002

VAL 78 VAL 79 0.0221

VAL 79 PHE 80 -0.0000

PHE 80 LEU 81 -0.0288

LEU 81 THR 82 0.0001

THR 82 LYS 83 -0.0053

LYS 83 LEU 84 -0.0003

LEU 84 THR 85 -0.0112

THR 85 SER 86 0.0002

SER 86 PHE 87 0.0283

PHE 87 GLU 88 -0.0002

GLU 88 ASP 89 0.0337

ASP 89 GLN 90 -0.0002

GLN 90 LEU 91 -0.0039

LEU 91 ARG 92 0.0001

ARG 92 ARG 93 0.0354

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 0.0026

GLY 95 GLU 96 0.0000

GLU 96 PHE 97 -0.0104

PHE 97 ILE 98 0.0000

ILE 98 GLN 99 0.0151

GLN 99 GLU 100 -0.0002

GLU 100 ILE 101 0.0089

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 0.0252

ARG 103 GLN 104 0.0003

GLN 104 LEU 105 0.0242

LEU 105 GLU 106 0.0000

GLU 106 ALA 107 0.0063

ALA 107 CYS 108 -0.0000

CYS 108 GLN 109 0.0150

GLN 109 ARG 110 -0.0002

ARG 110 GLU 111 -0.0051

GLU 111 GLN 112 0.0001

GLN 112 LYS 113 0.0242

LYS 113 PHE 114 -0.0000

PHE 114 LYS 115 0.0270

LYS 115 VAL 116 0.0001

VAL 116 THR 117 -0.0306

THR 117 PHE 118 -0.0002

PHE 118 GLY 119 -0.0285

GLY 119 GLY 120 -0.0004

GLY 120 GLY 121 -0.0105

GLY 121 PHE 122 -0.0002

PHE 122 VAL 123 -0.0111

VAL 123 LEU 124 0.0001

LEU 124 SER 125 -0.0186

SER 125 SER 126 0.0003

SER 126 PRO 127 -0.0030

PRO 127 GLN 128 -0.0002

GLN 128 LEU 129 -0.0070

LEU 129 GLN 130 0.0001

GLN 130 GLN 131 -0.0185

GLN 131 GLU 132 0.0003

GLU 132 VAL 133 -0.0614

VAL 133 GLU 134 -0.0001

GLU 134 PHE 135 -0.0176

PHE 135 ASP 136 -0.0001

ASP 136 VAL 137 0.0449

VAL 137 LEU 138 0.0006

LEU 138 PRO 139 -0.0087

PRO 139 ALA 140 -0.0004

ALA 140 PHE 141 -0.0369

PHE 141 ASP 142 0.0003

ASP 142 ALA 143 -0.0221

ALA 143 LEU 144 -0.0002

LEU 144 GLY 145 0.0072

GLY 145 GLN 146 -0.0003

GLN 146 TRP 147 -0.0414

TRP 147 THR 148 0.0002

THR 148 PRO 149 -0.0509

PRO 149 GLY 150 0.0002

GLY 150 TYR 151 0.0329

TYR 151 LYS 152 0.0001

LYS 152 PRO 153 -0.0191

PRO 153 ASN 154 -0.0003

ASN 154 PRO 155 0.0033

PRO 155 GLU 156 -0.0002

GLU 156 ILE 157 -0.0125

ILE 157 TYR 158 -0.0000

TYR 158 VAL 159 0.0005

VAL 159 GLN 160 0.0001

GLN 160 LEU 161 0.0348

LEU 161 ILE 162 0.0003

ILE 162 LYS 163 0.0003

LYS 163 GLU 164 -0.0001

GLU 164 CYS 165 0.0452

CYS 165 LYS 166 -0.0002

LYS 166 SER 167 0.0361

SER 167 ARG 168 0.0004

ARG 168 GLY 169 0.0340

GLY 169 LYS 170 0.0001

LYS 170 GLU 171 0.1231

GLU 171 GLY 172 0.0003

GLY 172 GLU 173 0.1525

GLU 173 PHE 174 0.0001

PHE 174 SER 175 0.0195

SER 175 THR 176 -0.0000

THR 176 CYS 177 -0.0068

CYS 177 PHE 178 0.0000

PHE 178 THR 179 -0.0135

THR 179 GLU 180 0.0000

GLU 180 LEU 181 -0.0427

LEU 181 GLN 182 -0.0004

GLN 182 ARG 183 0.0035

ARG 183 ASP 184 -0.0004

ASP 184 PHE 185 -0.1064

PHE 185 LEU 186 -0.0003

LEU 186 ARG 187 0.0535

ARG 187 ASN 188 0.0002

ASN 188 ARG 189 -0.1724

ARG 189 PRO 190 0.0002

PRO 190 THR 191 0.0264

THR 191 LYS 192 -0.0001

LYS 192 LEU 193 0.0158

LEU 193 LYS 194 0.0000

LYS 194 SER 195 -0.0229

SER 195 LEU 196 0.0005

LEU 196 ILE 197 0.0097

ILE 197 ARG 198 -0.0001

ARG 198 LEU 199 0.0015

LEU 199 VAL 200 -0.0000

VAL 200 LYS 201 0.0287

LYS 201 HIS 202 0.0002

HIS 202 TRP 203 0.0254

TRP 203 TYR 204 0.0000

TYR 204 GLN 205 0.0048

GLN 205 THR 206 -0.0001

THR 206 CYS 207 -0.0067

CYS 207 LYS 208 0.0003

LYS 208 LYS 209 -0.0036

LYS 209 THR 210 -0.0002

THR 210 HIS 211 0.0136

HIS 211 GLY 212 -0.0001

GLY 212 ASN 213 -0.0183

ASN 213 LYS 214 0.0000

LYS 214 LEU 215 0.0238

LEU 215 PRO 216 0.0001

PRO 216 PRO 217 0.0434

PRO 217 GLN 218 -0.0002

GLN 218 TYR 219 0.0623

TYR 219 ALA 220 -0.0000

ALA 220 LEU 221 0.0188

LEU 221 GLU 222 0.0003

GLU 222 LEU 223 -0.0107

LEU 223 LEU 224 -0.0001

LEU 224 THR 225 0.0046

THR 225 VAL 226 -0.0002

VAL 226 TYR 227 -0.0013

TYR 227 ALA 228 0.0001

ALA 228 TRP 229 0.0054

TRP 229 GLU 230 0.0001

GLU 230 GLN 231 -0.0214

GLN 231 GLY 232 0.0000

GLY 232 SER 233 0.0084

SER 233 ARG 234 -0.0000

ARG 234 LYS 235 0.0287

LYS 235 THR 236 -0.0002

THR 236 ASP 237 -0.0220

ASP 237 PHE 238 -0.0000

PHE 238 SER 239 -0.0311

SER 239 THR 240 -0.0002

THR 240 ALA 241 -0.0236

ALA 241 GLN 242 0.0000

GLN 242 GLY 243 -0.0120

GLY 243 PHE 244 0.0001

PHE 244 GLN 245 0.0039

GLN 245 THR 246 -0.0002

THR 246 VAL 247 0.0121

VAL 247 LEU 248 0.0000

LEU 248 GLU 249 0.0035

GLU 249 LEU 250 -0.0002

LEU 250 VAL 251 -0.0111

VAL 251 LEU 252 -0.0000

LEU 252 LYS 253 0.0058

LYS 253 HIS 254 -0.0001

HIS 254 GLN 255 0.0117

GLN 255 LYS 256 -0.0002

LYS 256 LEU 257 -0.0458

LEU 257 CYS 258 0.0003

CYS 258 ILE 259 -0.0442

ILE 259 PHE 260 0.0001

PHE 260 TRP 261 -0.0560

TRP 261 GLU 262 0.0000

GLU 262 ALA 263 -0.0063

ALA 263 TYR 264 -0.0002

TYR 264 TYR 265 0.0276

TYR 265 ASP 266 -0.0006

ASP 266 PHE 267 0.0190

PHE 267 THR 268 0.0002

THR 268 ASN 269 -0.0295

ASN 269 PRO 270 0.0000

PRO 270 VAL 271 -0.0023

VAL 271 VAL 272 0.0003

VAL 272 GLY 273 -0.0150

GLY 273 ARG 274 -0.0000

ARG 274 CYS 275 0.0020

CYS 275 MET 276 0.0001

MET 276 LEU 277 0.0101

LEU 277 GLN 278 -0.0002

GLN 278 GLN 279 -0.0084

GLN 279 LEU 280 0.0001

LEU 280 LYS 281 -0.0009

LYS 281 LYS 282 -0.0000

LYS 282 PRO 283 0.0316

PRO 283 ARG 284 -0.0001

ARG 284 PRO 285 -0.0230

PRO 285 VAL 286 0.0001

VAL 286 ILE 287 -0.0143

ILE 287 LEU 288 -0.0001

LEU 288 ASP 289 0.0064

ASP 289 PRO 290 0.0002

PRO 290 ALA 291 -0.0265

ALA 291 ASP 292 0.0002

ASP 292 PRO 293 -0.0145

PRO 293 THR 294 -0.0002

THR 294 GLY 295 0.0799

GLY 295 ASN 296 0.0003

ASN 296 VAL 297 -0.0382

VAL 297 GLY 298 -0.0002

GLY 298 GLY 299 -0.0009

GLY 299 GLY 300 -0.0002

GLY 300 ASP 301 0.0078

ASP 301 THR 302 0.0002

THR 302 HIS 303 -0.0170

HIS 303 SER 304 0.0001

SER 304 TRP 305 -0.0063

TRP 305 GLN 306 0.0000

GLN 306 ARG 307 -0.0055

ARG 307 LEU 308 -0.0000

LEU 308 ALA 309 0.0008

ALA 309 GLN 310 0.0001

GLN 310 GLU 311 0.0063

GLU 311 ALA 312 0.0003

ALA 312 ARG 313 0.0076

ARG 313 VAL 314 -0.0002

VAL 314 TRP 315 -0.0022

TRP 315 LEU 316 -0.0001

LEU 316 GLY 317 -0.0046

GLY 317 TYR 318 0.0001

TYR 318 PRO 319 0.0037

PRO 319 CYS 320 -0.0001

CYS 320 CYS 321 0.0016

CYS 321 LYS 322 0.0001

LYS 322 ASN 323 0.0197

ASN 323 LEU 324 0.0001

LEU 324 ASP 325 -0.0070

ASP 325 GLY 326 -0.0000

GLY 326 SER 327 -0.0046

SER 327 LEU 328 0.0002

LEU 328 VAL 329 -0.0253

VAL 329 GLY 330 0.0001

GLY 330 ALA 331 -0.0178

ALA 331 TRP 332 -0.0003

TRP 332 THR 333 -0.0028

THR 333 MET 334 0.0001

MET 334 LEU 335 -0.0086

LEU 335 GLN 336 0.0001

GLN 336 LYS 337 -0.0244

LYS 337 ILE 338 -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 25th, 2023.

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

*** ***

CA strain for 2401161745071321422

--- normal mode 7 ---

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

* *