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

* *

CA strain for 230101190352136506

--- normal mode 28 ---

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 -0.0000

MET 3 ILE 4 -0.0001

ILE 4 ARG 5 -0.0065

ARG 5 LEU 6 -0.0003

LEU 6 ALA 7 0.0665

ALA 7 THR 8 0.0002

THR 8 ASN 9 0.0801

ASN 9 LYS 10 -0.0004

LYS 10 PHE 11 -0.0303

PHE 11 SER 12 0.0000

SER 12 GLU 13 -0.0138

GLU 13 ASP 14 0.0000

ASP 14 ASN 15 0.0297

ASN 15 LYS 16 0.0001

LYS 16 ILE 17 0.0017

ILE 17 GLY 18 -0.0001

GLY 18 GLU 19 -0.0529

GLU 19 GLY 20 0.0001

GLY 20 GLY 21 0.2129

GLY 21 PHE 22 0.0001

PHE 22 GLY 23 -0.0007

GLY 23 ASP 24 0.0003

ASP 24 VAL 25 -0.0010

VAL 25 TYR 26 -0.0001

TYR 26 LYS 27 -0.1136

LYS 27 GLY 28 -0.0000

GLY 28 MET 29 -0.1798

MET 29 PHE 30 -0.0002

PHE 30 PRO 31 0.0305

PRO 31 ASN 32 0.0001

ASN 32 GLY 33 -0.1752

GLY 33 TYR 34 -0.0003

TYR 34 GLU 35 -0.0865

GLU 35 ILE 36 -0.0002

ILE 36 ALA 37 -0.0583

ALA 37 VAL 38 0.0001

VAL 38 LYS 39 0.0487

LYS 39 ARG 40 0.0000

ARG 40 LEU 41 0.0112

LEU 41 ILE 42 0.0001

ILE 42 ARG 43 0.0157

ARG 43 ASN 44 -0.0003

ASN 44 SER 45 0.0135

SER 45 SER 46 -0.0001

SER 46 GLN 47 -0.0246

GLN 47 GLY 48 -0.0000

GLY 48 ALA 49 -0.0236

ALA 49 VAL 50 -0.0001

VAL 50 GLU 51 0.0029

GLU 51 PHE 52 -0.0000

PHE 52 LYS 53 -0.0185

LYS 53 ASN 54 0.0000

ASN 54 GLU 55 0.1418

GLU 55 VAL 56 0.0001

VAL 56 LEU 57 0.0717

LEU 57 LEU 58 -0.0001

LEU 58 ILE 59 0.2544

ILE 59 ALA 60 0.0001

ALA 60 LYS 61 0.0666

LYS 61 LEU 62 0.0002

LEU 62 GLN 63 0.0516

GLN 63 HIS 64 0.0000

HIS 64 ARG 65 -0.0536

ARG 65 ASN 66 -0.0001

ASN 66 LEU 67 -0.1438

LEU 67 VAL 68 0.0001

VAL 68 ARG 69 -0.0512

ARG 69 LEU 70 -0.0003

LEU 70 LEU 71 0.2058

LEU 71 GLY 72 -0.0003

GLY 72 PHE 73 -0.0833

PHE 73 CYS 74 -0.0000

CYS 74 ILE 75 -0.0366

ILE 75 GLN 76 0.0003

GLN 76 ARG 77 -0.0480

ARG 77 ASN 78 -0.0001

ASN 78 GLU 79 -0.0293

GLU 79 LYS 80 -0.0002

LYS 80 ILE 81 -0.0609

ILE 81 LEU 82 -0.0002

LEU 82 ILE 83 -0.0019

ILE 83 TYR 84 -0.0003

TYR 84 GLU 85 -0.0712

GLU 85 TYR 86 0.0003

TYR 86 MET 87 -0.0103

MET 87 HIS 88 0.0004

HIS 88 ASN 89 -0.0214

ASN 89 LYS 90 0.0001

LYS 90 SER 91 0.0969

SER 91 LEU 92 0.0000

LEU 92 ASP 93 -0.0204

ASP 93 TYR 94 -0.0001

TYR 94 TYR 95 0.0193

TYR 95 LEU 96 0.0001

LEU 96 PHE 97 -0.0368

PHE 97 SER 98 -0.0002

SER 98 PRO 99 0.0713

PRO 99 GLU 100 -0.0002

GLU 100 ASN 101 -0.1094

ASN 101 HIS 102 0.0002

HIS 102 ARG 103 0.1652

ARG 103 LYS 104 0.0001

LYS 104 LEU 105 -0.2134

LEU 105 THR 106 0.0005

THR 106 TRP 107 -0.2163

TRP 107 HIS 108 0.0000

HIS 108 ALA 109 0.0303

ALA 109 ARG 110 0.0004

ARG 110 TYR 111 -0.1181

TYR 111 LYS 112 -0.0002

LYS 112 ILE 113 -0.0004

ILE 113 ILE 114 0.0002

ILE 114 ARG 115 0.0525

ARG 115 GLY 116 -0.0004

GLY 116 ILE 117 -0.0573

ILE 117 ALA 118 0.0001

ALA 118 ARG 119 -0.0181

ARG 119 GLY 120 -0.0001

GLY 120 ILE 121 0.0623

ILE 121 LEU 122 0.0007

LEU 122 TYR 123 -0.1318

TYR 123 LEU 124 0.0003

LEU 124 HIS 125 0.0038

HIS 125 GLU 126 -0.0001

GLU 126 ASP 127 -0.0388

ASP 127 SER 128 -0.0002

SER 128 HIS 129 0.1178

HIS 129 LEU 130 0.0002

LEU 130 LYS 131 -0.0009

LYS 131 ILE 132 -0.0004

ILE 132 ILE 133 0.0410

ILE 133 HIS 134 -0.0003

HIS 134 CYS 135 0.0876

CYS 135 ASP 136 0.0000

ASP 136 LEU 137 0.0000

LEU 137 LYS 138 0.0002

LYS 138 PRO 139 0.1585

PRO 139 SER 140 -0.0003

SER 140 ASN 141 0.0421

ASN 141 ILE 142 0.0001

ILE 142 LEU 143 0.1157

LEU 143 LEU 144 0.0001

LEU 144 ASP 145 0.0670

ASP 145 ASP 146 -0.0001

ASP 146 LYS 147 -0.0224

LYS 147 MET 148 0.0000

MET 148 ASN 149 -0.0689

ASN 149 ALA 150 0.0003

ALA 150 LYS 151 -0.0833

LYS 151 ILE 152 -0.0000

ILE 152 SER 153 -0.2386

SER 153 ASP 154 0.0001

ASP 154 PHE 155 -0.0328

PHE 155 GLY 156 -0.0001

GLY 156 LEU 157 0.1002

LEU 157 ALA 158 -0.0001

ALA 158 ARG 159 0.1451

ARG 159 ILE 160 0.0001

ILE 160 VAL 161 0.2897

VAL 161 ALA 162 0.0001

ALA 162 ILE 163 -0.0014

ILE 163 ASP 164 -0.0000

ASP 164 GLN 165 -0.0766

GLN 165 MET 166 -0.0001

MET 166 GLN 167 -0.0163

GLN 167 GLY 168 0.0000

GLY 168 ASN 169 -0.0192

ASN 169 THR 170 0.0004

THR 170 SER 171 0.0404

SER 171 ILE 172 0.0003

ILE 172 ILE 173 0.1200

ILE 173 ALA 174 0.0003

ALA 174 GLY 175 0.2343

GLY 175 THR 176 0.0004

THR 176 TYR 177 0.1776

TYR 177 GLY 178 -0.0000

GLY 178 TYR 179 0.0862

TYR 179 MET 180 0.0002

MET 180 SER 181 0.1212

SER 181 PRO 182 0.0001

PRO 182 GLU 183 -0.1164

GLU 183 TYR 184 -0.0003

TYR 184 ALA 185 -0.0158

ALA 185 MET 186 0.0002

MET 186 LEU 187 -0.0526

LEU 187 GLY 188 0.0001

GLY 188 GLN 189 -0.0384

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 -0.0798

SER 191 VAL 192 -0.0002

VAL 192 LYS 193 -0.0850

LYS 193 SER 194 0.0000

SER 194 ASP 195 0.0626

ASP 195 VAL 196 -0.0001

VAL 196 PHE 197 -0.0456

PHE 197 SER 198 -0.0002

SER 198 PHE 199 0.0282

PHE 199 GLY 200 0.0004

GLY 200 VAL 201 0.0437

VAL 201 ILE 202 0.0000

ILE 202 MET 203 -0.0292

MET 203 LEU 204 -0.0002

LEU 204 GLU 205 0.0497

GLU 205 ILE 206 -0.0002

ILE 206 VAL 207 -0.0694

VAL 207 SER 208 -0.0002

SER 208 GLY 209 -0.0892

GLY 209 LYS 210 -0.0000

LYS 210 ARG 211 -0.1541

ARG 211 ASN 212 -0.0001

ASN 212 VAL 213 0.0624

VAL 213 ASP 214 -0.0002

ASP 214 TYR 215 0.2633

TYR 215 ASN 216 -0.0002

ASN 216 GLY 217 0.3013

GLY 217 VAL 218 0.0000

VAL 218 ASN 219 0.0077

ASN 219 SER 220 -0.0000

SER 220 ILE 221 -0.5717

ILE 221 ASP 222 -0.0003

ASP 222 ASP 223 0.0626

ASP 223 LEU 224 0.0001

LEU 224 VAL 225 0.0168

VAL 225 SER 226 -0.0001

SER 226 HIS 227 -0.0235

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 0.0116

TRP 229 LYS 230 -0.0001

LYS 230 LYS 231 0.0063

LYS 231 TRP 232 0.0001

TRP 232 THR 233 0.0241

THR 233 GLU 234 0.0001

GLU 234 ASN 235 -0.0232

ASN 235 LYS 236 0.0003

LYS 236 GLN 237 0.0120

GLN 237 MET 238 0.0004

MET 238 GLU 239 0.1657

GLU 239 LEU 240 -0.0000

LEU 240 LEU 241 -0.0302

LEU 241 ASP 242 0.0003

ASP 242 PRO 243 -0.0310

PRO 243 ALA 244 -0.0001

ALA 244 LEU 245 -0.1106

LEU 245 THR 246 -0.0002

THR 246 TYR 247 -0.0888

TYR 247 SER 248 -0.0000

SER 248 PHE 249 -0.2073

PHE 249 SER 250 0.0000

SER 250 GLU 251 0.0385

GLU 251 THR 252 -0.0001

THR 252 GLU 253 -0.0130

GLU 253 VAL 254 0.0001

VAL 254 SER 255 -0.0236

SER 255 ARG 256 0.0004

ARG 256 CYS 257 0.0380

CYS 257 ILE 258 0.0004

ILE 258 GLN 259 0.0082

GLN 259 LEU 260 -0.0001

LEU 260 GLY 261 0.0682

GLY 261 LEU 262 0.0000

LEU 262 LEU 263 -0.0078

LEU 263 CYS 264 0.0001

CYS 264 VAL 265 -0.0344

VAL 265 GLN 266 0.0002

GLN 266 GLU 267 0.0358

GLU 267 ASN 268 0.0004

ASN 268 PRO 269 -0.0642

PRO 269 ASP 270 0.0001

ASP 270 GLN 271 -0.0457

GLN 271 ARG 272 -0.0000

ARG 272 PRO 273 -0.0720

PRO 273 THR 274 0.0000

THR 274 MET 275 0.0412

MET 275 ALA 276 -0.0001

ALA 276 THR 277 -0.1044

THR 277 ILE 278 0.0000

ILE 278 ALA 279 0.0101

ALA 279 LEU 280 0.0003

LEU 280 TYR 281 0.0150

TYR 281 PHE 282 0.0002

PHE 282 ASN 283 0.0279

ASN 283 ILE 284 0.0004

ILE 284 ASP 285 0.0013

ASP 285 SER 286 -0.0001

SER 286 ILE 287 -0.0612

ILE 287 ASP 288 -0.0003

ASP 288 LEU 289 0.0320

LEU 289 PRO 290 -0.0001

PRO 290 LEU 291 0.0558

LEU 291 PRO 292 0.0002

PRO 292 GLN 293 -0.0447

GLN 293 GLN 294 -0.0002

GLN 294 PRO 295 0.0453

PRO 295 PRO 296 0.0000

PRO 296 PHE 297 -0.1663

PHE 297 TYR 298 -0.0001

TYR 298 MET 299 -0.1284

MET 299 ARG 300 0.0000

ARG 300 GLY 301 0.0390

GLY 301 LYS 302 0.0002

LYS 302 ILE 303 0.0419

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 0.0520

SER 305 LYS 306 0.0001

LYS 306 VAL 307 0.0231

VAL 307 ALA 308 -0.0002

ALA 308 SER 309 0.1577

SER 309 LYS 310 0.0003

LYS 310 LYS 311 0.0921

LYS 311 THR 312 0.0000

THR 312 MET 313 0.0958

MET 313 SER 314 0.0002

SER 314 GLY 315 0.1134

GLY 315 ARG 316 -0.0004

ARG 316 PRO 317 -0.0508

PRO 317 ARG 318 0.0002

ARG 318 SER 319 0.1296

SER 319 TYR 320 0.0001

TYR 320 SER 321 0.0497

SER 321 VAL 322 0.0001

VAL 322 THR 323 0.0657

THR 323 ARG 324 -0.0001

ARG 324 PHE 325 -0.2276

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 28 ---

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

* *