Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* Zm A1b DHK *

CA strain for 2610090027463442181

--- normal mode 11 ---

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
GLY 1 PRO 2 0.0003

PRO 2 VAL 3 -0.0101

VAL 3 VAL 4 0.0002

VAL 4 VAL 5 0.0137

VAL 5 THR 6 0.0003

THR 6 GLY 7 -0.0407

GLY 7 ALA 8 0.0002

ALA 8 SER 9 0.0094

SER 9 GLY 10 0.0001

GLY 10 PHE 11 0.3365

PHE 11 VAL 12 0.0004

VAL 12 GLY 13 0.0249

GLY 13 SER 14 0.0002

SER 14 TRP 15 0.0618

TRP 15 LEU 16 0.0001

LEU 16 VAL 17 0.0362

VAL 17 MET 18 -0.0003

MET 18 LYS 19 0.0561

LYS 19 LEU 20 0.0004

LEU 20 LEU 21 0.0010

LEU 21 GLN 22 0.0003

GLN 22 ALA 23 0.0157

ALA 23 GLY 24 0.0001

GLY 24 TYR 25 0.0289

TYR 25 THR 26 -0.0002

THR 26 VAL 27 -0.0073

VAL 27 ARG 28 0.0002

ARG 28 ALA 29 -0.0179

ALA 29 THR 30 0.0001

THR 30 VAL 31 -0.0094

VAL 31 ARG 32 -0.0001

ARG 32 ASP 33 0.0018

ASP 33 PRO 34 0.0001

PRO 34 GLU 35 0.0259

GLU 35 ASN 36 -0.0002

ASN 36 VAL 37 -0.0093

VAL 37 GLY 38 -0.0003

GLY 38 LYS 39 0.1566

LYS 39 THR 40 0.0001

THR 40 LYS 41 0.0175

LYS 41 PRO 42 -0.0002

PRO 42 LEU 43 0.0440

LEU 43 LEU 44 0.0000

LEU 44 ASP 45 0.0072

ASP 45 LEU 46 -0.0002

LEU 46 PRO 47 -0.0161

PRO 47 GLY 48 0.0000

GLY 48 ALA 49 -0.0010

ALA 49 THR 50 -0.0001

THR 50 GLU 51 -0.0219

GLU 51 ARG 52 -0.0003

ARG 52 LEU 53 -0.0011

LEU 53 SER 54 -0.0001

SER 54 ILE 55 -0.0290

ILE 55 TRP 56 0.0001

TRP 56 LYS 57 -0.0152

LYS 57 ALA 58 0.0003

ALA 58 ASP 59 0.1086

ASP 59 MET 60 0.0001

MET 60 ALA 61 0.0014

ALA 61 ASP 62 0.0000

ASP 62 GLU 63 0.0512

GLU 63 ASP 64 0.0000

ASP 64 SER 65 -0.0675

SER 65 PHE 66 -0.0002

PHE 66 ASP 67 0.0078

ASP 67 GLU 68 0.0002

GLU 68 ALA 69 -0.0303

ALA 69 ILE 70 0.0000

ILE 70 ARG 71 0.0057

ARG 71 GLY 72 0.0005

GLY 72 CYS 73 -0.0384

CYS 73 THR 74 -0.0001

THR 74 GLY 75 0.0179

GLY 75 VAL 76 0.0004

VAL 76 PHE 77 0.0200

PHE 77 HIS 78 0.0000

HIS 78 VAL 79 -0.0796

VAL 79 ALA 80 0.0002

ALA 80 THR 81 0.0534

THR 81 PRO 82 -0.0003

PRO 82 THR 83 0.5299

THR 83 ASP 84 -0.0001

ASP 84 PHE 85 0.0990

PHE 85 GLU 86 0.0000

GLU 86 SER 87 -0.1740

SER 87 LYS 88 -0.0003

LYS 88 ASP 89 -0.0191

ASP 89 PRO 90 0.0002

PRO 90 GLU 91 0.0233

GLU 91 ASN 92 0.0000

ASN 92 GLU 93 -0.1029

GLU 93 VAL 94 0.0001

VAL 94 ILE 95 0.1641

ILE 95 LYS 96 0.0001

LYS 96 PRO 97 -0.1393

PRO 97 THR 98 -0.0001

THR 98 VAL 99 0.0801

VAL 99 GLU 100 -0.0000

GLU 100 GLY 101 -0.1264

GLY 101 MET 102 -0.0003

MET 102 ILE 103 0.0728

ILE 103 ARG 104 -0.0002

ARG 104 ILE 105 0.0327

ILE 105 LEU 106 0.0002

LEU 106 ARG 107 -0.0914

ARG 107 ALA 108 0.0002

ALA 108 CYS 109 -0.0072

CYS 109 LYS 110 0.0001

LYS 110 GLU 111 -0.0979

GLU 111 ALA 112 0.0003

ALA 112 GLY 113 -0.0346

GLY 113 THR 114 0.0000

THR 114 VAL 115 -0.0416

VAL 115 ARG 116 -0.0004

ARG 116 ARG 117 -0.0252

ARG 117 ILE 118 -0.0001

ILE 118 VAL 119 -0.0586

VAL 119 PHE 120 -0.0004

PHE 120 THR 121 -0.0612

THR 121 SER 122 0.0003

SER 122 SER 123 0.0599

SER 123 ALA 124 -0.0001

ALA 124 GLY 125 -0.0514

GLY 125 THR 126 -0.0002

THR 126 VAL 127 -0.0288

VAL 127 CYS 128 0.0001

CYS 128 VAL 129 -0.1192

VAL 129 GLU 130 0.0002

GLU 130 GLU 131 0.0604

GLU 131 ARG 132 -0.0002

ARG 132 ARG 133 0.1163

ARG 133 ARG 134 0.0001

ARG 134 PRO 135 -0.0116

PRO 135 VAL 136 -0.0003

VAL 136 TYR 137 0.0040

TYR 137 ASP 138 -0.0002

ASP 138 HIS 139 0.0394

HIS 139 ASP 140 0.0001

ASP 140 ASN 141 -0.0463

ASN 141 TRP 142 -0.0003

TRP 142 SER 143 -0.0797

SER 143 ASP 144 0.0001

ASP 144 VAL 145 0.0437

VAL 145 ASP 146 -0.0002

ASP 146 PHE 147 0.0420

PHE 147 CYS 148 -0.0001

CYS 148 ARG 149 -0.0305

ARG 149 ARG 150 0.0004

ARG 150 VAL 151 0.0715

VAL 151 LYS 152 -0.0002

LYS 152 MET 153 0.0290

MET 153 THR 154 0.0000

THR 154 GLY 155 0.0406

GLY 155 TRP 156 -0.0001

TRP 156 MET 157 -0.0877

MET 157 TYR 158 -0.0000

TYR 158 PHE 159 -0.1279

PHE 159 VAL 160 0.0004

VAL 160 SER 161 0.0397

SER 161 LYS 162 0.0001

LYS 162 SER 163 0.0791

SER 163 LEU 164 -0.0001

LEU 164 ALA 165 -0.0590

ALA 165 GLU 166 -0.0002

GLU 166 LYS 167 0.0116

LYS 167 ALA 168 0.0002

ALA 168 ALA 169 0.0208

ALA 169 MET 170 0.0001

MET 170 ALA 171 -0.0325

ALA 171 TYR 172 -0.0000

TYR 172 ALA 173 0.0296

ALA 173 ALA 174 -0.0004

ALA 174 GLU 175 -0.0017

GLU 175 HIS 176 -0.0000

HIS 176 GLY 177 -0.0168

GLY 177 LEU 178 -0.0002

LEU 178 ASP 179 -0.0782

ASP 179 LEU 180 0.0002

LEU 180 VAL 181 -0.0606

VAL 181 SER 182 -0.0005

SER 182 VAL 183 -0.0577

VAL 183 ILE 184 0.0000

ILE 184 PRO 185 0.0313

PRO 185 THR 186 0.0003

THR 186 LEU 187 0.1123

LEU 187 VAL 188 -0.0002

VAL 188 VAL 189 -0.0189

VAL 189 GLY 190 -0.0002

GLY 190 PRO 191 0.0505

PRO 191 PHE 192 -0.0001

PHE 192 LEU 193 0.1532

LEU 193 SER 194 -0.0001

SER 194 ALA 195 -0.0423

ALA 195 ALA 196 0.0000

ALA 196 MET 197 0.0652

MET 197 PRO 198 0.0000

PRO 198 PRO 199 -0.0258

PRO 199 SER 200 -0.0004

SER 200 LEU 201 0.0184

LEU 201 VAL 202 0.0001

VAL 202 THR 203 0.0174

THR 203 ALA 204 -0.0001

ALA 204 LEU 205 0.0041

LEU 205 ALA 206 -0.0003

ALA 206 LEU 207 0.0145

LEU 207 VAL 208 -0.0002

VAL 208 THR 209 0.0805

THR 209 GLY 210 0.0003

GLY 210 ASN 211 0.0895

ASN 211 GLU 212 -0.0004

GLU 212 ALA 213 0.1369

ALA 213 HIS 214 0.0001

HIS 214 TYR 215 -0.0074

TYR 215 SER 216 0.0002

SER 216 ILE 217 0.2661

ILE 217 LEU 218 -0.0003

LEU 218 LYS 219 0.0427

LYS 219 GLN 220 -0.0001

GLN 220 VAL 221 0.0788

VAL 221 GLN 222 -0.0002

GLN 222 PHE 223 0.0802

PHE 223 VAL 224 -0.0000

VAL 224 HIS 225 0.0142

HIS 225 LEU 226 -0.0001

LEU 226 ASP 227 -0.0334

ASP 227 ASP 228 -0.0001

ASP 228 LEU 229 -0.0585

LEU 229 CYS 230 -0.0002

CYS 230 ASP 231 0.0551

ASP 231 ALA 232 -0.0001

ALA 232 GLU 233 -0.0455

GLU 233 ILE 234 0.0002

ILE 234 PHE 235 0.0490

PHE 235 LEU 236 0.0002

LEU 236 PHE 237 -0.0487

PHE 237 GLU 238 -0.0001

GLU 238 HIS 239 -0.0338

HIS 239 PRO 240 -0.0001

PRO 240 ALA 241 0.0050

ALA 241 ALA 242 0.0000

ALA 242 ALA 243 0.0263

ALA 243 GLY 244 -0.0001

GLY 244 ARG 245 -0.0257

ARG 245 TYR 246 -0.0002

TYR 246 VAL 247 -0.0155

VAL 247 CYS 248 0.0001

CYS 248 SER 249 -0.0779

SER 249 SER 250 0.0001

SER 250 HIS 251 -0.0524

HIS 251 ASP 252 0.0002

ASP 252 ALA 253 -0.0443

ALA 253 THR 254 0.0003

THR 254 ILE 255 -0.0236

ILE 255 HIS 256 0.0003

HIS 256 GLY 257 -0.0306

GLY 257 LEU 258 0.0001

LEU 258 ALA 259 -0.0266

ALA 259 ALA 260 -0.0002

ALA 260 MET 261 -0.0300

MET 261 LEU 262 0.0001

LEU 262 ARG 263 -0.0300

ARG 263 ASP 264 0.0001

ASP 264 ARG 265 -0.0136

ARG 265 TYR 266 -0.0002

TYR 266 PRO 267 -0.1111

PRO 267 GLU 268 -0.0000

GLU 268 TYR 269 0.0492

TYR 269 ASP 270 -0.0002

ASP 270 ILE 271 0.0553

ILE 271 PRO 272 -0.0004

PRO 272 GLN 273 -0.0024

GLN 273 LYS 274 0.0002

LYS 274 LEU 275 0.0348

LEU 275 ARG 276 0.0002

ARG 276 GLY 277 0.0267

GLY 277 ILE 278 0.0003

ILE 278 GLU 279 -0.0182

GLU 279 ASP 280 -0.0001

ASP 280 ASP 281 -0.0187

ASP 281 LEU 282 -0.0003

LEU 282 GLN 283 0.0509

GLN 283 PRO 284 0.0000

PRO 284 VAL 285 0.0599

VAL 285 HIS 286 -0.0003

HIS 286 PHE 287 0.0383

PHE 287 SER 288 -0.0002

SER 288 SER 289 0.0285

SER 289 LYS 290 -0.0001

LYS 290 LYS 291 0.0123

LYS 291 LEU 292 -0.0001

LEU 292 LEU 293 -0.0021

LEU 293 ASP 294 0.0001

ASP 294 HIS 295 0.0003

HIS 295 GLY 296 -0.0001

GLY 296 PHE 297 -0.0412

PHE 297 THR 298 0.0001

THR 298 PHE 299 -0.1311

PHE 299 ARG 300 -0.0003

ARG 300 TYR 301 -0.2438

TYR 301 THR 302 -0.0001

THR 302 VAL 303 -0.1465

VAL 303 GLU 304 -0.0002

GLU 304 ASP 305 0.0685

ASP 305 MET 306 0.0003

MET 306 PHE 307 -0.1297

PHE 307 ASP 308 0.0002

ASP 308 ALA 309 0.0684

ALA 309 GLY 310 -0.0001

GLY 310 ILE 311 -0.0438

ILE 311 ARG 312 0.0001

ARG 312 THR 313 0.0372

THR 313 CYS 314 -0.0001

CYS 314 ARG 315 0.0304

ARG 315 GLU 316 0.0003

GLU 316 LYS 317 0.0486

LYS 317 GLY 318 -0.0002

GLY 318 LEU 319 0.0562

LEU 319 ILE 320 0.0002

ILE 320 PRO 321 -0.0205

PRO 321 LEU 322 0.0004

LEU 322 ALA 323 -0.0020

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** Zm A1b DHK ***

CA strain for 2610090027463442181

--- normal mode 11 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* Zm A1b DHK *