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

* *

CA strain for 230101190352136506

--- normal mode 12 ---

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 0.0002

ASP 2 MET 3 0.0670

MET 3 ILE 4 -0.0002

ILE 4 ARG 5 -0.0155

ARG 5 LEU 6 -0.0000

LEU 6 ALA 7 -0.0056

ALA 7 THR 8 -0.0004

THR 8 ASN 9 -0.0175

ASN 9 LYS 10 -0.0000

LYS 10 PHE 11 0.0273

PHE 11 SER 12 0.0001

SER 12 GLU 13 -0.0007

GLU 13 ASP 14 -0.0000

ASP 14 ASN 15 -0.0031

ASN 15 LYS 16 -0.0000

LYS 16 ILE 17 0.0022

ILE 17 GLY 18 -0.0003

GLY 18 GLU 19 -0.1428

GLU 19 GLY 20 -0.0002

GLY 20 GLY 21 0.0248

GLY 21 PHE 22 -0.0003

PHE 22 GLY 23 0.1664

GLY 23 ASP 24 0.0001

ASP 24 VAL 25 -0.0508

VAL 25 TYR 26 -0.0002

TYR 26 LYS 27 -0.0373

LYS 27 GLY 28 0.0001

GLY 28 MET 29 0.0016

MET 29 PHE 30 0.0004

PHE 30 PRO 31 -0.0173

PRO 31 ASN 32 0.0004

ASN 32 GLY 33 0.0670

GLY 33 TYR 34 -0.0003

TYR 34 GLU 35 0.0510

GLU 35 ILE 36 -0.0000

ILE 36 ALA 37 -0.0327

ALA 37 VAL 38 -0.0002

VAL 38 LYS 39 -0.0035

LYS 39 ARG 40 -0.0005

ARG 40 LEU 41 0.0091

LEU 41 ILE 42 -0.0001

ILE 42 ARG 43 -0.0117

ARG 43 ASN 44 -0.0001

ASN 44 SER 45 0.0073

SER 45 SER 46 0.0001

SER 46 GLN 47 -0.0076

GLN 47 GLY 48 -0.0002

GLY 48 ALA 49 -0.0179

ALA 49 VAL 50 -0.0000

VAL 50 GLU 51 -0.0068

GLU 51 PHE 52 0.0000

PHE 52 LYS 53 -0.0299

LYS 53 ASN 54 0.0001

ASN 54 GLU 55 0.0233

GLU 55 VAL 56 0.0001

VAL 56 LEU 57 -0.0805

LEU 57 LEU 58 0.0000

LEU 58 ILE 59 -0.0036

ILE 59 ALA 60 0.0001

ALA 60 LYS 61 -0.1029

LYS 61 LEU 62 0.0000

LEU 62 GLN 63 0.0202

GLN 63 HIS 64 -0.0002

HIS 64 ARG 65 0.0575

ARG 65 ASN 66 0.0000

ASN 66 LEU 67 -0.0312

LEU 67 VAL 68 -0.0001

VAL 68 ARG 69 -0.0009

ARG 69 LEU 70 -0.0001

LEU 70 LEU 71 -0.0559

LEU 71 GLY 72 -0.0003

GLY 72 PHE 73 0.0096

PHE 73 CYS 74 0.0003

CYS 74 ILE 75 0.0044

ILE 75 GLN 76 0.0002

GLN 76 ARG 77 -0.0221

ARG 77 ASN 78 0.0001

ASN 78 GLU 79 -0.0152

GLU 79 LYS 80 0.0001

LYS 80 ILE 81 -0.0058

ILE 81 LEU 82 0.0003

LEU 82 ILE 83 -0.0176

ILE 83 TYR 84 -0.0002

TYR 84 GLU 85 -0.0009

GLU 85 TYR 86 -0.0000

TYR 86 MET 87 0.0791

MET 87 HIS 88 -0.0000

HIS 88 ASN 89 0.0830

ASN 89 LYS 90 0.0002

LYS 90 SER 91 0.0744

SER 91 LEU 92 -0.0002

LEU 92 ASP 93 0.0408

ASP 93 TYR 94 -0.0001

TYR 94 TYR 95 -0.0046

TYR 95 LEU 96 -0.0001

LEU 96 PHE 97 0.0109

PHE 97 SER 98 0.0000

SER 98 PRO 99 0.0068

PRO 99 GLU 100 -0.0004

GLU 100 ASN 101 0.0059

ASN 101 HIS 102 0.0001

HIS 102 ARG 103 -0.0123

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 0.0012

LEU 105 THR 106 0.0001

THR 106 TRP 107 0.0047

TRP 107 HIS 108 0.0004

HIS 108 ALA 109 -0.0152

ALA 109 ARG 110 -0.0003

ARG 110 TYR 111 0.0112

TYR 111 LYS 112 0.0002

LYS 112 ILE 113 0.0133

ILE 113 ILE 114 -0.0002

ILE 114 ARG 115 0.0011

ARG 115 GLY 116 -0.0001

GLY 116 ILE 117 -0.0171

ILE 117 ALA 118 -0.0004

ALA 118 ARG 119 -0.0402

ARG 119 GLY 120 0.0003

GLY 120 ILE 121 -0.0076

ILE 121 LEU 122 0.0001

LEU 122 TYR 123 -0.0726

TYR 123 LEU 124 0.0000

LEU 124 HIS 125 -0.0258

HIS 125 GLU 126 0.0002

GLU 126 ASP 127 -0.0261

ASP 127 SER 128 -0.0003

SER 128 HIS 129 0.0000

HIS 129 LEU 130 0.0002

LEU 130 LYS 131 -0.0236

LYS 131 ILE 132 0.0005

ILE 132 ILE 133 -0.0313

ILE 133 HIS 134 0.0003

HIS 134 CYS 135 -0.0088

CYS 135 ASP 136 -0.0000

ASP 136 LEU 137 -0.0163

LEU 137 LYS 138 -0.0001

LYS 138 PRO 139 -0.0411

PRO 139 SER 140 -0.0001

SER 140 ASN 141 -0.0085

ASN 141 ILE 142 -0.0004

ILE 142 LEU 143 0.0353

LEU 143 LEU 144 0.0001

LEU 144 ASP 145 0.0183

ASP 145 ASP 146 0.0000

ASP 146 LYS 147 -0.0582

LYS 147 MET 148 0.0002

MET 148 ASN 149 0.0410

ASN 149 ALA 150 0.0001

ALA 150 LYS 151 -0.0359

LYS 151 ILE 152 -0.0002

ILE 152 SER 153 -0.0200

SER 153 ASP 154 0.0002

ASP 154 PHE 155 -0.0469

PHE 155 GLY 156 0.0003

GLY 156 LEU 157 0.0331

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 0.0360

ARG 159 ILE 160 -0.0005

ILE 160 VAL 161 0.0056

VAL 161 ALA 162 -0.0000

ALA 162 ILE 163 0.0246

ILE 163 ASP 164 0.0001

ASP 164 GLN 165 -0.0222

GLN 165 MET 166 -0.0001

MET 166 GLN 167 -0.0660

GLN 167 GLY 168 0.0000

GLY 168 ASN 169 -0.1020

ASN 169 THR 170 0.0001

THR 170 SER 171 -0.2339

SER 171 ILE 172 0.0001

ILE 172 ILE 173 0.0217

ILE 173 ALA 174 0.0002

ALA 174 GLY 175 -0.0503

GLY 175 THR 176 -0.0002

THR 176 TYR 177 0.0416

TYR 177 GLY 178 -0.0001

GLY 178 TYR 179 -0.0090

TYR 179 MET 180 -0.0005

MET 180 SER 181 0.0434

SER 181 PRO 182 0.0002

PRO 182 GLU 183 -0.0120

GLU 183 TYR 184 0.0000

TYR 184 ALA 185 -0.0482

ALA 185 MET 186 0.0001

MET 186 LEU 187 -0.0119

LEU 187 GLY 188 -0.0003

GLY 188 GLN 189 -0.0434

GLN 189 PHE 190 0.0002

PHE 190 SER 191 -0.0396

SER 191 VAL 192 -0.0001

VAL 192 LYS 193 -0.0293

LYS 193 SER 194 -0.0004

SER 194 ASP 195 -0.0121

ASP 195 VAL 196 -0.0002

VAL 196 PHE 197 -0.0120

PHE 197 SER 198 -0.0002

SER 198 PHE 199 0.0006

PHE 199 GLY 200 -0.0001

GLY 200 VAL 201 -0.0035

VAL 201 ILE 202 -0.0003

ILE 202 MET 203 0.0047

MET 203 LEU 204 0.0005

LEU 204 GLU 205 0.0248

GLU 205 ILE 206 0.0003

ILE 206 VAL 207 0.0103

VAL 207 SER 208 -0.0001

SER 208 GLY 209 0.0292

GLY 209 LYS 210 0.0005

LYS 210 ARG 211 -0.0382

ARG 211 ASN 212 0.0003

ASN 212 VAL 213 -0.0026

VAL 213 ASP 214 0.0002

ASP 214 TYR 215 0.0714

TYR 215 ASN 216 -0.0002

ASN 216 GLY 217 0.0502

GLY 217 VAL 218 -0.0001

VAL 218 ASN 219 -0.0045

ASN 219 SER 220 0.0005

SER 220 ILE 221 0.0641

ILE 221 ASP 222 -0.0000

ASP 222 ASP 223 -0.0052

ASP 223 LEU 224 0.0001

LEU 224 VAL 225 -0.0056

VAL 225 SER 226 0.0000

SER 226 HIS 227 0.0063

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 -0.0008

TRP 229 LYS 230 0.0003

LYS 230 LYS 231 0.0019

LYS 231 TRP 232 -0.0000

TRP 232 THR 233 -0.0058

THR 233 GLU 234 -0.0000

GLU 234 ASN 235 0.0033

ASN 235 LYS 236 -0.0001

LYS 236 GLN 237 -0.0042

GLN 237 MET 238 0.0001

MET 238 GLU 239 -0.0157

GLU 239 LEU 240 0.0005

LEU 240 LEU 241 0.0053

LEU 241 ASP 242 -0.0000

ASP 242 PRO 243 -0.0031

PRO 243 ALA 244 0.0000

ALA 244 LEU 245 0.0143

LEU 245 THR 246 0.0005

THR 246 TYR 247 -0.0064

TYR 247 SER 248 0.0001

SER 248 PHE 249 0.0091

PHE 249 SER 250 -0.0002

SER 250 GLU 251 -0.0052

GLU 251 THR 252 -0.0002

THR 252 GLU 253 -0.0143

GLU 253 VAL 254 0.0002

VAL 254 SER 255 -0.0003

SER 255 ARG 256 0.0004

ARG 256 CYS 257 0.0022

CYS 257 ILE 258 0.0000

ILE 258 GLN 259 0.0044

GLN 259 LEU 260 0.0005

LEU 260 GLY 261 0.0086

GLY 261 LEU 262 0.0004

LEU 262 LEU 263 -0.0125

LEU 263 CYS 264 -0.0001

CYS 264 VAL 265 -0.0050

VAL 265 GLN 266 -0.0001

GLN 266 GLU 267 0.0172

GLU 267 ASN 268 0.0004

ASN 268 PRO 269 -0.0169

PRO 269 ASP 270 -0.0002

ASP 270 GLN 271 0.0047

GLN 271 ARG 272 -0.0001

ARG 272 PRO 273 -0.0218

PRO 273 THR 274 -0.0003

THR 274 MET 275 -0.0283

MET 275 ALA 276 0.0000

ALA 276 THR 277 -0.0184

THR 277 ILE 278 0.0004

ILE 278 ALA 279 -0.0046

ALA 279 LEU 280 0.0001

LEU 280 TYR 281 -0.0054

TYR 281 PHE 282 0.0004

PHE 282 ASN 283 -0.0069

ASN 283 ILE 284 0.0001

ILE 284 ASP 285 0.0089

ASP 285 SER 286 0.0000

SER 286 ILE 287 0.0054

ILE 287 ASP 288 0.0002

ASP 288 LEU 289 0.0156

LEU 289 PRO 290 -0.0003

PRO 290 LEU 291 -0.0099

LEU 291 PRO 292 0.0003

PRO 292 GLN 293 0.0170

GLN 293 GLN 294 -0.0003

GLN 294 PRO 295 0.0086

PRO 295 PRO 296 0.0000

PRO 296 PHE 297 -0.0097

PHE 297 TYR 298 0.0003

TYR 298 MET 299 0.0532

MET 299 ARG 300 -0.0002

ARG 300 GLY 301 -0.0132

GLY 301 LYS 302 -0.0002

LYS 302 ILE 303 -0.0579

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 -0.0434

SER 305 LYS 306 0.0003

LYS 306 VAL 307 0.0053

VAL 307 ALA 308 0.0003

ALA 308 SER 309 -0.2579

SER 309 LYS 310 0.0001

LYS 310 LYS 311 0.0540

LYS 311 THR 312 0.0001

THR 312 MET 313 0.1154

MET 313 SER 314 -0.0001

SER 314 GLY 315 -0.0197

GLY 315 ARG 316 -0.0000

ARG 316 PRO 317 0.1379

PRO 317 ARG 318 -0.0000

ARG 318 SER 319 -0.1715

SER 319 TYR 320 0.0001

TYR 320 SER 321 -0.0465

SER 321 VAL 322 0.0002

VAL 322 THR 323 0.0397

THR 323 ARG 324 0.0002

ARG 324 PHE 325 0.1013

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 12 ---

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

* *