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 DHQ *

CA strain for 2610090028133442294

--- 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
GLY 1 PRO 2 -0.0000

PRO 2 VAL 3 -0.0182

VAL 3 VAL 4 -0.0002

VAL 4 VAL 5 0.0161

VAL 5 THR 6 -0.0002

THR 6 GLY 7 0.1081

GLY 7 ALA 8 0.0005

ALA 8 SER 9 0.0100

SER 9 GLY 10 -0.0000

GLY 10 PHE 11 0.0816

PHE 11 VAL 12 -0.0002

VAL 12 GLY 13 0.0288

GLY 13 SER 14 0.0001

SER 14 TRP 15 0.2044

TRP 15 LEU 16 0.0001

LEU 16 VAL 17 0.0289

VAL 17 MET 18 0.0000

MET 18 LYS 19 0.1324

LYS 19 LEU 20 -0.0003

LEU 20 LEU 21 0.0704

LEU 21 GLN 22 0.0001

GLN 22 ALA 23 0.0564

ALA 23 GLY 24 0.0002

GLY 24 TYR 25 0.0023

TYR 25 THR 26 0.0002

THR 26 VAL 27 -0.0020

VAL 27 ARG 28 -0.0000

ARG 28 ALA 29 0.0424

ALA 29 THR 30 0.0002

THR 30 VAL 31 -0.0029

VAL 31 ARG 32 -0.0001

ARG 32 ASP 33 -0.1263

ASP 33 PRO 34 0.0000

PRO 34 GLU 35 0.0376

GLU 35 ASN 36 0.0001

ASN 36 VAL 37 -0.0260

VAL 37 GLY 38 -0.0005

GLY 38 LYS 39 0.0358

LYS 39 THR 40 -0.0002

THR 40 LYS 41 -0.0600

LYS 41 PRO 42 -0.0001

PRO 42 LEU 43 -0.0203

LEU 43 LEU 44 0.0000

LEU 44 ASP 45 -0.0011

ASP 45 LEU 46 0.0001

LEU 46 PRO 47 -0.0348

PRO 47 GLY 48 0.0002

GLY 48 ALA 49 -0.0078

ALA 49 THR 50 -0.0001

THR 50 GLU 51 0.0056

GLU 51 ARG 52 -0.0001

ARG 52 LEU 53 -0.0346

LEU 53 SER 54 0.0000

SER 54 ILE 55 -0.0389

ILE 55 TRP 56 -0.0001

TRP 56 LYS 57 -0.0983

LYS 57 ALA 58 -0.0004

ALA 58 ASP 59 -0.1269

ASP 59 MET 60 0.0003

MET 60 ALA 61 0.0670

ALA 61 ASP 62 -0.0002

ASP 62 GLU 63 -0.0120

GLU 63 ASP 64 -0.0004

ASP 64 SER 65 0.0499

SER 65 PHE 66 0.0004

PHE 66 ASP 67 0.0055

ASP 67 GLU 68 0.0004

GLU 68 ALA 69 0.0400

ALA 69 ILE 70 -0.0001

ILE 70 ARG 71 0.0120

ARG 71 GLY 72 0.0003

GLY 72 CYS 73 -0.0225

CYS 73 THR 74 0.0004

THR 74 GLY 75 -0.0190

GLY 75 VAL 76 -0.0001

VAL 76 PHE 77 -0.0259

PHE 77 HIS 78 0.0003

HIS 78 VAL 79 0.0785

VAL 79 ALA 80 0.0001

ALA 80 THR 81 -0.1835

THR 81 PRO 82 -0.0001

PRO 82 THR 83 0.0176

THR 83 ASP 84 -0.0002

ASP 84 PHE 85 0.0171

PHE 85 GLU 86 0.0001

GLU 86 SER 87 0.1006

SER 87 LYS 88 -0.0001

LYS 88 ASP 89 0.0325

ASP 89 PRO 90 0.0004

PRO 90 GLU 91 0.0365

GLU 91 ASN 92 -0.0004

ASN 92 GLU 93 -0.0100

GLU 93 VAL 94 0.0003

VAL 94 ILE 95 0.0112

ILE 95 LYS 96 -0.0000

LYS 96 PRO 97 -0.0383

PRO 97 THR 98 -0.0001

THR 98 VAL 99 -0.0241

VAL 99 GLU 100 -0.0004

GLU 100 GLY 101 -0.0287

GLY 101 MET 102 0.0001

MET 102 ILE 103 0.0078

ILE 103 ARG 104 -0.0004

ARG 104 ILE 105 0.0319

ILE 105 LEU 106 -0.0001

LEU 106 ARG 107 -0.0287

ARG 107 ALA 108 -0.0001

ALA 108 CYS 109 -0.0170

CYS 109 LYS 110 0.0001

LYS 110 GLU 111 0.0145

GLU 111 ALA 112 -0.0001

ALA 112 GLY 113 -0.0180

GLY 113 THR 114 0.0001

THR 114 VAL 115 0.0005

VAL 115 ARG 116 0.0005

ARG 116 ARG 117 0.0148

ARG 117 ILE 118 -0.0001

ILE 118 VAL 119 -0.0097

VAL 119 PHE 120 0.0002

PHE 120 THR 121 0.0206

THR 121 SER 122 -0.0003

SER 122 SER 123 -0.0276

SER 123 ALA 124 0.0003

ALA 124 GLY 125 -0.0080

GLY 125 THR 126 0.0000

THR 126 VAL 127 -0.0333

VAL 127 CYS 128 -0.0000

CYS 128 VAL 129 0.0096

VAL 129 GLU 130 0.0000

GLU 130 GLU 131 0.0431

GLU 131 ARG 132 0.0000

ARG 132 ARG 133 -0.0414

ARG 133 ARG 134 -0.0001

ARG 134 PRO 135 -0.0137

PRO 135 VAL 136 -0.0001

VAL 136 TYR 137 0.0295

TYR 137 ASP 138 -0.0002

ASP 138 HIS 139 0.0327

HIS 139 ASP 140 -0.0001

ASP 140 ASN 141 0.0630

ASN 141 TRP 142 0.0003

TRP 142 SER 143 0.0945

SER 143 ASP 144 -0.0001

ASP 144 VAL 145 -0.0626

VAL 145 ASP 146 -0.0001

ASP 146 PHE 147 -0.0493

PHE 147 CYS 148 -0.0000

CYS 148 ARG 149 -0.0284

ARG 149 ARG 150 0.0002

ARG 150 VAL 151 0.0085

VAL 151 LYS 152 -0.0000

LYS 152 MET 153 0.0581

MET 153 THR 154 -0.0001

THR 154 GLY 155 0.0645

GLY 155 TRP 156 0.0002

TRP 156 MET 157 -0.0136

MET 157 TYR 158 0.0000

TYR 158 PHE 159 0.0166

PHE 159 VAL 160 -0.0000

VAL 160 SER 161 -0.0781

SER 161 LYS 162 0.0001

LYS 162 SER 163 -0.0510

SER 163 LEU 164 0.0004

LEU 164 ALA 165 -0.0118

ALA 165 GLU 166 0.0003

GLU 166 LYS 167 -0.0012

LYS 167 ALA 168 -0.0004

ALA 168 ALA 169 0.0182

ALA 169 MET 170 -0.0001

MET 170 ALA 171 -0.0692

ALA 171 TYR 172 -0.0005

TYR 172 ALA 173 -0.0084

ALA 173 ALA 174 -0.0002

ALA 174 GLU 175 -0.0049

GLU 175 HIS 176 -0.0002

HIS 176 GLY 177 -0.0644

GLY 177 LEU 178 0.0003

LEU 178 ASP 179 -0.1308

ASP 179 LEU 180 0.0001

LEU 180 VAL 181 -0.0685

VAL 181 SER 182 -0.0001

SER 182 VAL 183 -0.0119

VAL 183 ILE 184 0.0003

ILE 184 PRO 185 0.0194

PRO 185 THR 186 -0.0001

THR 186 LEU 187 0.1076

LEU 187 VAL 188 -0.0003

VAL 188 VAL 189 0.0668

VAL 189 GLY 190 -0.0001

GLY 190 PRO 191 0.0229

PRO 191 PHE 192 -0.0000

PHE 192 LEU 193 0.0724

LEU 193 SER 194 -0.0001

SER 194 ALA 195 0.0351

ALA 195 ALA 196 -0.0003

ALA 196 MET 197 -0.0104

MET 197 PRO 198 0.0002

PRO 198 PRO 199 -0.0139

PRO 199 SER 200 0.0001

SER 200 LEU 201 0.0767

LEU 201 VAL 202 0.0002

VAL 202 THR 203 -0.0318

THR 203 ALA 204 0.0000

ALA 204 LEU 205 -0.0099

LEU 205 ALA 206 0.0002

ALA 206 LEU 207 0.0945

LEU 207 VAL 208 -0.0000

VAL 208 THR 209 0.0842

THR 209 GLY 210 -0.0000

GLY 210 ASN 211 0.1057

ASN 211 GLU 212 -0.0001

GLU 212 ALA 213 0.1019

ALA 213 HIS 214 0.0001

HIS 214 TYR 215 0.0715

TYR 215 SER 216 -0.0001

SER 216 ILE 217 0.0123

ILE 217 LEU 218 0.0000

LEU 218 LYS 219 -0.0714

LYS 219 GLN 220 0.0002

GLN 220 VAL 221 -0.0374

VAL 221 GLN 222 -0.0001

GLN 222 PHE 223 0.0172

PHE 223 VAL 224 0.0001

VAL 224 HIS 225 0.0222

HIS 225 LEU 226 -0.0002

LEU 226 ASP 227 -0.0129

ASP 227 ASP 228 -0.0001

ASP 228 LEU 229 0.0161

LEU 229 CYS 230 0.0001

CYS 230 ASP 231 0.0266

ASP 231 ALA 232 0.0002

ALA 232 GLU 233 0.0084

GLU 233 ILE 234 0.0002

ILE 234 PHE 235 0.1416

PHE 235 LEU 236 0.0001

LEU 236 PHE 237 0.0278

PHE 237 GLU 238 0.0002

GLU 238 HIS 239 0.1006

HIS 239 PRO 240 -0.0001

PRO 240 ALA 241 0.0697

ALA 241 ALA 242 -0.0001

ALA 242 ALA 243 0.0562

ALA 243 GLY 244 0.0004

GLY 244 ARG 245 0.0390

ARG 245 TYR 246 -0.0002

TYR 246 VAL 247 -0.0123

VAL 247 CYS 248 -0.0001

CYS 248 SER 249 -0.0675

SER 249 SER 250 -0.0001

SER 250 HIS 251 0.0089

HIS 251 ASP 252 0.0001

ASP 252 ALA 253 -0.0124

ALA 253 THR 254 0.0002

THR 254 ILE 255 -0.0005

ILE 255 HIS 256 -0.0002

HIS 256 GLY 257 0.0417

GLY 257 LEU 258 -0.0001

LEU 258 ALA 259 -0.0559

ALA 259 ALA 260 -0.0001

ALA 260 MET 261 0.0379

MET 261 LEU 262 0.0000

LEU 262 ARG 263 -0.0155

ARG 263 ASP 264 -0.0002

ASP 264 ARG 265 0.0555

ARG 265 TYR 266 -0.0000

TYR 266 PRO 267 0.0034

PRO 267 GLU 268 0.0002

GLU 268 TYR 269 0.0415

TYR 269 ASP 270 -0.0002

ASP 270 ILE 271 -0.0407

ILE 271 PRO 272 0.0001

PRO 272 GLN 273 0.0249

GLN 273 LYS 274 0.0000

LYS 274 LEU 275 0.0317

LEU 275 ARG 276 0.0002

ARG 276 GLY 277 -0.0350

GLY 277 ILE 278 0.0002

ILE 278 GLU 279 0.0647

GLU 279 ASP 280 0.0001

ASP 280 ASP 281 -0.0250

ASP 281 LEU 282 0.0001

LEU 282 GLN 283 0.0673

GLN 283 PRO 284 -0.0002

PRO 284 VAL 285 0.0611

VAL 285 HIS 286 0.0001

HIS 286 PHE 287 0.0845

PHE 287 SER 288 -0.0001

SER 288 SER 289 0.0964

SER 289 LYS 290 -0.0002

LYS 290 LYS 291 -0.0205

LYS 291 LEU 292 0.0001

LEU 292 LEU 293 -0.0259

LEU 293 ASP 294 -0.0000

ASP 294 HIS 295 0.0061

HIS 295 GLY 296 -0.0001

GLY 296 PHE 297 -0.0707

PHE 297 THR 298 -0.0003

THR 298 PHE 299 -0.1779

PHE 299 ARG 300 -0.0000

ARG 300 TYR 301 -0.1867

TYR 301 THR 302 -0.0002

THR 302 VAL 303 0.0591

VAL 303 GLU 304 -0.0000

GLU 304 ASP 305 0.0581

ASP 305 MET 306 -0.0002

MET 306 PHE 307 -0.0586

PHE 307 ASP 308 -0.0000

ASP 308 ALA 309 0.0968

ALA 309 GLY 310 0.0002

GLY 310 ILE 311 -0.0069

ILE 311 ARG 312 -0.0002

ARG 312 THR 313 0.0850

THR 313 CYS 314 -0.0003

CYS 314 ARG 315 0.0538

ARG 315 GLU 316 -0.0002

GLU 316 LYS 317 0.0579

LYS 317 GLY 318 0.0001

GLY 318 LEU 319 0.0492

LEU 319 ILE 320 0.0001

ILE 320 PRO 321 0.0522

PRO 321 LEU 322 -0.0001

LEU 322 ALA 323 0.0438

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 DHQ ***

CA strain for 2610090028133442294

--- normal mode 7 ---

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 DHQ *