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 9 ---

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 0.0002

PRO 2 VAL 3 0.0444

VAL 3 VAL 4 -0.0002

VAL 4 VAL 5 0.1220

VAL 5 THR 6 -0.0003

THR 6 GLY 7 0.0923

GLY 7 ALA 8 -0.0003

ALA 8 SER 9 0.0324

SER 9 GLY 10 -0.0002

GLY 10 PHE 11 0.1875

PHE 11 VAL 12 -0.0001

VAL 12 GLY 13 0.0909

GLY 13 SER 14 0.0001

SER 14 TRP 15 0.0075

TRP 15 LEU 16 -0.0001

LEU 16 VAL 17 0.0558

VAL 17 MET 18 -0.0000

MET 18 LYS 19 -0.0666

LYS 19 LEU 20 0.0001

LEU 20 LEU 21 -0.0454

LEU 21 GLN 22 0.0001

GLN 22 ALA 23 -0.0567

ALA 23 GLY 24 -0.0001

GLY 24 TYR 25 -0.0425

TYR 25 THR 26 -0.0002

THR 26 VAL 27 0.0043

VAL 27 ARG 28 0.0001

ARG 28 ALA 29 -0.0077

ALA 29 THR 30 0.0002

THR 30 VAL 31 -0.0589

VAL 31 ARG 32 -0.0001

ARG 32 ASP 33 0.0765

ASP 33 PRO 34 -0.0001

PRO 34 GLU 35 -0.0523

GLU 35 ASN 36 -0.0001

ASN 36 VAL 37 0.0016

VAL 37 GLY 38 0.0000

GLY 38 LYS 39 0.0687

LYS 39 THR 40 0.0001

THR 40 LYS 41 -0.0224

LYS 41 PRO 42 -0.0000

PRO 42 LEU 43 0.0917

LEU 43 LEU 44 0.0002

LEU 44 ASP 45 -0.0662

ASP 45 LEU 46 -0.0001

LEU 46 PRO 47 0.0086

PRO 47 GLY 48 -0.0002

GLY 48 ALA 49 -0.0168

ALA 49 THR 50 -0.0002

THR 50 GLU 51 0.0267

GLU 51 ARG 52 -0.0002

ARG 52 LEU 53 0.0038

LEU 53 SER 54 -0.0005

SER 54 ILE 55 -0.0288

ILE 55 TRP 56 0.0000

TRP 56 LYS 57 -0.0077

LYS 57 ALA 58 -0.0004

ALA 58 ASP 59 -0.0098

ASP 59 MET 60 -0.0001

MET 60 ALA 61 -0.0142

ALA 61 ASP 62 0.0001

ASP 62 GLU 63 0.0124

GLU 63 ASP 64 -0.0000

ASP 64 SER 65 0.0122

SER 65 PHE 66 0.0002

PHE 66 ASP 67 0.0220

ASP 67 GLU 68 0.0001

GLU 68 ALA 69 0.0250

ALA 69 ILE 70 0.0003

ILE 70 ARG 71 -0.0061

ARG 71 GLY 72 0.0001

GLY 72 CYS 73 0.0193

CYS 73 THR 74 0.0002

THR 74 GLY 75 0.0372

GLY 75 VAL 76 -0.0000

VAL 76 PHE 77 0.0867

PHE 77 HIS 78 -0.0000

HIS 78 VAL 79 0.0895

VAL 79 ALA 80 0.0002

ALA 80 THR 81 0.1023

THR 81 PRO 82 0.0001

PRO 82 THR 83 -0.0216

THR 83 ASP 84 -0.0001

ASP 84 PHE 85 -0.0309

PHE 85 GLU 86 -0.0000

GLU 86 SER 87 -0.1204

SER 87 LYS 88 0.0002

LYS 88 ASP 89 -0.0257

ASP 89 PRO 90 -0.0002

PRO 90 GLU 91 -0.0240

GLU 91 ASN 92 -0.0000

ASN 92 GLU 93 -0.0055

GLU 93 VAL 94 0.0001

VAL 94 ILE 95 -0.0151

ILE 95 LYS 96 0.0004

LYS 96 PRO 97 -0.0016

PRO 97 THR 98 -0.0002

THR 98 VAL 99 0.0389

VAL 99 GLU 100 -0.0001

GLU 100 GLY 101 -0.0067

GLY 101 MET 102 -0.0002

MET 102 ILE 103 0.0662

ILE 103 ARG 104 -0.0002

ARG 104 ILE 105 -0.0012

ILE 105 LEU 106 0.0002

LEU 106 ARG 107 0.0222

ARG 107 ALA 108 -0.0000

ALA 108 CYS 109 0.0179

CYS 109 LYS 110 -0.0002

LYS 110 GLU 111 -0.0323

GLU 111 ALA 112 0.0002

ALA 112 GLY 113 0.0206

GLY 113 THR 114 -0.0002

THR 114 VAL 115 -0.0153

VAL 115 ARG 116 0.0002

ARG 116 ARG 117 -0.0715

ARG 117 ILE 118 0.0003

ILE 118 VAL 119 0.0313

VAL 119 PHE 120 0.0000

PHE 120 THR 121 0.0342

THR 121 SER 122 -0.0002

SER 122 SER 123 0.0064

SER 123 ALA 124 0.0001

ALA 124 GLY 125 -0.0021

GLY 125 THR 126 -0.0000

THR 126 VAL 127 0.0195

VAL 127 CYS 128 -0.0002

CYS 128 VAL 129 -0.0198

VAL 129 GLU 130 0.0003

GLU 130 GLU 131 -0.0097

GLU 131 ARG 132 0.0001

ARG 132 ARG 133 -0.0945

ARG 133 ARG 134 0.0000

ARG 134 PRO 135 0.0487

PRO 135 VAL 136 0.0000

VAL 136 TYR 137 -0.0595

TYR 137 ASP 138 -0.0001

ASP 138 HIS 139 -0.1019

HIS 139 ASP 140 0.0000

ASP 140 ASN 141 -0.0025

ASN 141 TRP 142 -0.0001

TRP 142 SER 143 0.0438

SER 143 ASP 144 0.0001

ASP 144 VAL 145 -0.0368

VAL 145 ASP 146 -0.0001

ASP 146 PHE 147 -0.0581

PHE 147 CYS 148 0.0001

CYS 148 ARG 149 0.0087

ARG 149 ARG 150 -0.0003

ARG 150 VAL 151 -0.0052

VAL 151 LYS 152 -0.0002

LYS 152 MET 153 -0.1339

MET 153 THR 154 -0.0002

THR 154 GLY 155 -0.1973

GLY 155 TRP 156 0.0002

TRP 156 MET 157 -0.0154

MET 157 TYR 158 -0.0004

TYR 158 PHE 159 0.0378

PHE 159 VAL 160 0.0003

VAL 160 SER 161 0.0028

SER 161 LYS 162 -0.0002

LYS 162 SER 163 0.0406

SER 163 LEU 164 -0.0002

LEU 164 ALA 165 -0.0632

ALA 165 GLU 166 -0.0001

GLU 166 LYS 167 0.0559

LYS 167 ALA 168 -0.0004

ALA 168 ALA 169 -0.0587

ALA 169 MET 170 0.0000

MET 170 ALA 171 0.0192

ALA 171 TYR 172 -0.0001

TYR 172 ALA 173 0.0557

ALA 173 ALA 174 0.0001

ALA 174 GLU 175 -0.0165

GLU 175 HIS 176 0.0002

HIS 176 GLY 177 0.0624

GLY 177 LEU 178 -0.0000

LEU 178 ASP 179 0.0762

ASP 179 LEU 180 0.0002

LEU 180 VAL 181 0.0149

VAL 181 SER 182 -0.0002

SER 182 VAL 183 -0.0359

VAL 183 ILE 184 0.0005

ILE 184 PRO 185 -0.0558

PRO 185 THR 186 -0.0003

THR 186 LEU 187 0.0490

LEU 187 VAL 188 -0.0002

VAL 188 VAL 189 0.0422

VAL 189 GLY 190 0.0000

GLY 190 PRO 191 -0.0112

PRO 191 PHE 192 -0.0002

PHE 192 LEU 193 0.1978

LEU 193 SER 194 0.0002

SER 194 ALA 195 0.1058

ALA 195 ALA 196 -0.0002

ALA 196 MET 197 0.0210

MET 197 PRO 198 0.0001

PRO 198 PRO 199 0.1543

PRO 199 SER 200 -0.0001

SER 200 LEU 201 -0.0306

LEU 201 VAL 202 -0.0001

VAL 202 THR 203 0.0782

THR 203 ALA 204 0.0003

ALA 204 LEU 205 -0.0446

LEU 205 ALA 206 0.0002

ALA 206 LEU 207 -0.0507

LEU 207 VAL 208 -0.0000

VAL 208 THR 209 -0.0443

THR 209 GLY 210 0.0002

GLY 210 ASN 211 -0.0584

ASN 211 GLU 212 -0.0001

GLU 212 ALA 213 -0.2650

ALA 213 HIS 214 -0.0002

HIS 214 TYR 215 -0.1218

TYR 215 SER 216 -0.0001

SER 216 ILE 217 0.0219

ILE 217 LEU 218 -0.0001

LEU 218 LYS 219 0.0077

LYS 219 GLN 220 -0.0001

GLN 220 VAL 221 0.0541

VAL 221 GLN 222 0.0001

GLN 222 PHE 223 0.1023

PHE 223 VAL 224 -0.0003

VAL 224 HIS 225 0.0740

HIS 225 LEU 226 -0.0000

LEU 226 ASP 227 0.0088

ASP 227 ASP 228 0.0002

ASP 228 LEU 229 -0.0039

LEU 229 CYS 230 -0.0003

CYS 230 ASP 231 -0.0326

ASP 231 ALA 232 0.0001

ALA 232 GLU 233 0.0079

GLU 233 ILE 234 -0.0002

ILE 234 PHE 235 -0.1101

PHE 235 LEU 236 -0.0003

LEU 236 PHE 237 -0.0644

PHE 237 GLU 238 -0.0002

GLU 238 HIS 239 -0.0988

HIS 239 PRO 240 0.0004

PRO 240 ALA 241 -0.0602

ALA 241 ALA 242 -0.0002

ALA 242 ALA 243 -0.0446

ALA 243 GLY 244 -0.0002

GLY 244 ARG 245 -0.0631

ARG 245 TYR 246 0.0002

TYR 246 VAL 247 -0.1025

VAL 247 CYS 248 -0.0002

CYS 248 SER 249 -0.0709

SER 249 SER 250 0.0002

SER 250 HIS 251 0.0709

HIS 251 ASP 252 0.0004

ASP 252 ALA 253 0.0226

ALA 253 THR 254 -0.0000

THR 254 ILE 255 0.0005

ILE 255 HIS 256 -0.0002

HIS 256 GLY 257 0.0337

GLY 257 LEU 258 0.0004

LEU 258 ALA 259 -0.0401

ALA 259 ALA 260 0.0001

ALA 260 MET 261 0.1022

MET 261 LEU 262 -0.0002

LEU 262 ARG 263 0.0265

ARG 263 ASP 264 0.0002

ASP 264 ARG 265 0.0882

ARG 265 TYR 266 0.0002

TYR 266 PRO 267 0.0800

PRO 267 GLU 268 -0.0003

GLU 268 TYR 269 -0.0145

TYR 269 ASP 270 0.0003

ASP 270 ILE 271 -0.0071

ILE 271 PRO 272 -0.0004

PRO 272 GLN 273 0.0304

GLN 273 LYS 274 -0.0000

LYS 274 LEU 275 -0.0888

LEU 275 ARG 276 -0.0001

ARG 276 GLY 277 -0.1702

GLY 277 ILE 278 -0.0002

ILE 278 GLU 279 0.0347

GLU 279 ASP 280 -0.0001

ASP 280 ASP 281 -0.1914

ASP 281 LEU 282 -0.0000

LEU 282 GLN 283 0.0018

GLN 283 PRO 284 -0.0002

PRO 284 VAL 285 0.0392

VAL 285 HIS 286 0.0000

HIS 286 PHE 287 0.0250

PHE 287 SER 288 0.0000

SER 288 SER 289 0.0036

SER 289 LYS 290 -0.0001

LYS 290 LYS 291 -0.0122

LYS 291 LEU 292 -0.0002

LEU 292 LEU 293 0.0038

LEU 293 ASP 294 -0.0000

ASP 294 HIS 295 -0.0132

HIS 295 GLY 296 0.0001

GLY 296 PHE 297 -0.0003

PHE 297 THR 298 0.0001

THR 298 PHE 299 0.0053

PHE 299 ARG 300 -0.0002

ARG 300 TYR 301 0.0104

TYR 301 THR 302 0.0003

THR 302 VAL 303 0.1141

VAL 303 GLU 304 -0.0000

GLU 304 ASP 305 0.1512

ASP 305 MET 306 -0.0000

MET 306 PHE 307 0.0552

PHE 307 ASP 308 0.0001

ASP 308 ALA 309 0.1609

ALA 309 GLY 310 -0.0002

GLY 310 ILE 311 0.1267

ILE 311 ARG 312 -0.0000

ARG 312 THR 313 0.0935

THR 313 CYS 314 -0.0002

CYS 314 ARG 315 0.0793

ARG 315 GLU 316 -0.0002

GLU 316 LYS 317 0.0357

LYS 317 GLY 318 -0.0002

GLY 318 LEU 319 -0.0241

LEU 319 ILE 320 0.0002

ILE 320 PRO 321 -0.0000

PRO 321 LEU 322 0.0002

LEU 322 ALA 323 0.0242

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 9 ---

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 *