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

* Vv N133C DHK *

CA strain for 2610082102113386154

--- normal mode 10 ---

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
GLU 6 THR 7 -0.0003

THR 7 VAL 8 -0.0386

VAL 8 CYS 9 0.0003

CYS 9 VAL 10 -0.1551

VAL 10 THR 11 -0.0001

THR 11 GLY 12 -0.1220

GLY 12 ALA 13 -0.0001

ALA 13 SER 14 -0.0772

SER 14 GLY 15 0.0002

GLY 15 PHE 16 -0.1636

PHE 16 ILE 17 0.0002

ILE 17 GLY 18 -0.0522

GLY 18 SER 19 -0.0002

SER 19 TRP 20 0.0599

TRP 20 LEU 21 0.0003

LEU 21 VAL 22 0.0001

VAL 22 MET 23 0.0005

MET 23 ARG 24 0.0344

ARG 24 LEU 25 -0.0001

LEU 25 LEU 26 0.0755

LEU 26 GLU 27 0.0002

GLU 27 ARG 28 0.0745

ARG 28 GLY 29 -0.0004

GLY 29 TYR 30 0.0285

TYR 30 THR 31 0.0001

THR 31 VAL 32 0.0058

VAL 32 ARG 33 0.0003

ARG 33 ALA 34 -0.0325

ALA 34 THR 35 -0.0003

THR 35 VAL 36 0.0292

VAL 36 ARG 37 -0.0004

ARG 37 ASP 38 -0.1128

ASP 38 PRO 39 -0.0001

PRO 39 THR 40 0.0895

THR 40 ASN 41 -0.0000

ASN 41 VAL 42 0.0098

VAL 42 LYS 43 0.0000

LYS 43 LYS 44 -0.0512

LYS 44 VAL 45 -0.0001

VAL 45 LYS 46 0.0222

LYS 46 HIS 47 -0.0002

HIS 47 LEU 48 -0.1655

LEU 48 LEU 49 0.0001

LEU 49 ASP 50 0.0899

ASP 50 LEU 51 -0.0001

LEU 51 PRO 52 0.0118

PRO 52 LYS 53 0.0000

LYS 53 ALA 54 0.0190

ALA 54 GLU 55 -0.0003

GLU 55 THR 56 -0.0144

THR 56 HIS 57 -0.0000

HIS 57 LEU 58 0.0022

LEU 58 THR 59 -0.0004

THR 59 LEU 60 0.0934

LEU 60 TRP 61 -0.0005

TRP 61 LYS 62 0.0347

LYS 62 ALA 63 -0.0004

ALA 63 ASP 64 0.0223

ASP 64 LEU 65 0.0002

LEU 65 ALA 66 0.0327

ALA 66 ASP 67 0.0003

ASP 67 GLU 68 -0.0183

GLU 68 GLY 69 -0.0003

GLY 69 SER 70 0.0062

SER 70 PHE 71 0.0001

PHE 71 ASP 72 -0.0485

ASP 72 GLU 73 -0.0004

GLU 73 ALA 74 -0.0357

ALA 74 ILE 75 0.0002

ILE 75 LYS 76 0.0015

LYS 76 GLY 77 -0.0002

GLY 77 CYS 78 0.0148

CYS 78 THR 79 0.0001

THR 79 GLY 80 -0.0367

GLY 80 VAL 81 -0.0002

VAL 81 PHE 82 -0.0708

PHE 82 HIS 83 -0.0000

HIS 83 VAL 84 -0.1185

VAL 84 ALA 85 0.0004

ALA 85 THR 86 -0.2494

THR 86 PRO 87 0.0001

PRO 87 MET 88 -0.0365

MET 88 ASP 89 0.0000

ASP 89 PHE 90 -0.0532

PHE 90 GLU 91 0.0002

GLU 91 SER 92 0.0160

SER 92 LYS 93 -0.0001

LYS 93 ASP 94 0.0252

ASP 94 PRO 95 -0.0000

PRO 95 GLU 96 0.0003

GLU 96 ASN 97 -0.0003

ASN 97 GLU 98 0.0172

GLU 98 VAL 99 -0.0000

VAL 99 ILE 100 0.0228

ILE 100 LYS 101 -0.0001

LYS 101 PRO 102 -0.0269

PRO 102 THR 103 0.0001

THR 103 ILE 104 -0.0207

ILE 104 GLU 105 -0.0000

GLU 105 GLY 106 0.0058

GLY 106 MET 107 -0.0002

MET 107 LEU 108 -0.0710

LEU 108 GLY 109 -0.0000

GLY 109 ILE 110 -0.0025

ILE 110 MET 111 0.0001

MET 111 LYS 112 0.0031

LYS 112 SER 113 0.0002

SER 113 CYS 114 -0.0020

CYS 114 ALA 115 -0.0001

ALA 115 ALA 116 0.0054

ALA 116 ALA 117 0.0000

ALA 117 LYS 118 -0.0461

LYS 118 THR 119 -0.0001

THR 119 VAL 120 0.0371

VAL 120 ARG 121 -0.0004

ARG 121 ARG 122 0.0571

ARG 122 LEU 123 -0.0004

LEU 123 VAL 124 -0.0045

VAL 124 PHE 125 0.0003

PHE 125 THR 126 -0.0438

THR 126 SER 127 0.0001

SER 127 SER 128 -0.0249

SER 128 ALA 129 -0.0002

ALA 129 GLY 130 -0.0259

GLY 130 THR 131 0.0003

THR 131 VAL 132 0.0145

VAL 132 CYS 133 -0.0004

CYS 133 ILE 134 -0.0169

ILE 134 GLN 135 0.0001

GLN 135 GLU 136 0.0129

GLU 136 HIS 137 0.0003

HIS 137 GLN 138 0.0222

GLN 138 LEU 139 -0.0003

LEU 139 PRO 140 -0.0213

PRO 140 VAL 141 0.0001

VAL 141 TYR 142 0.0706

TYR 142 ASP 143 0.0002

ASP 143 GLU 144 0.1985

GLU 144 SER 145 0.0002

SER 145 CYS 146 -0.0234

CYS 146 TRP 147 -0.0002

TRP 147 SER 148 -0.0176

SER 148 ASP 149 -0.0000

ASP 149 MET 150 0.0412

MET 150 GLU 151 -0.0000

GLU 151 PHE 152 0.0778

PHE 152 CYS 153 -0.0000

CYS 153 ARG 154 -0.0254

ARG 154 ALA 155 0.0000

ALA 155 LYS 156 0.0443

LYS 156 LYS 157 0.0000

LYS 157 MET 158 -0.0119

MET 158 THR 159 -0.0000

THR 159 ALA 160 0.0363

ALA 160 TRP 161 -0.0004

TRP 161 MET 162 0.0029

MET 162 TYR 163 0.0000

TYR 163 PHE 164 -0.0387

PHE 164 VAL 165 -0.0002

VAL 165 SER 166 0.0172

SER 166 LYS 167 -0.0004

LYS 167 THR 168 -0.0148

THR 168 LEU 169 0.0001

LEU 169 ALA 170 0.0482

ALA 170 GLU 171 0.0001

GLU 171 GLN 172 -0.0695

GLN 172 ALA 173 -0.0001

ALA 173 ALA 174 0.0129

ALA 174 TRP 175 0.0000

TRP 175 LYS 176 -0.0288

LYS 176 TYR 177 0.0003

TYR 177 ALA 178 -0.0231

ALA 178 LYS 179 0.0003

LYS 179 GLU 180 -0.0006

GLU 180 ASN 181 -0.0000

ASN 181 ASN 182 -0.0357

ASN 182 ILE 183 0.0001

ILE 183 ASP 184 0.0035

ASP 184 PHE 185 0.0002

PHE 185 ILE 186 0.0377

ILE 186 THR 187 -0.0001

THR 187 ILE 188 0.0637

ILE 188 ILE 189 -0.0000

ILE 189 PRO 190 0.0935

PRO 190 THR 191 0.0003

THR 191 LEU 192 -0.0085

LEU 192 VAL 193 -0.0001

VAL 193 VAL 194 -0.0095

VAL 194 GLY 195 -0.0002

GLY 195 PRO 196 -0.1000

PRO 196 PHE 197 0.0003

PHE 197 ILE 198 -0.3442

ILE 198 MET 199 -0.0001

MET 199 SER 200 0.0488

SER 200 SER 201 0.0001

SER 201 MET 202 -0.2417

MET 202 PRO 203 0.0001

PRO 203 PRO 204 -0.1545

PRO 204 SER 205 -0.0003

SER 205 LEU 206 0.0007

LEU 206 ILE 207 0.0001

ILE 207 THR 208 -0.1292

THR 208 ALA 209 0.0000

ALA 209 LEU 210 0.0575

LEU 210 SER 211 0.0003

SER 211 PRO 212 -0.0141

PRO 212 ILE 213 -0.0004

ILE 213 THR 214 0.0042

THR 214 GLY 215 0.0002

GLY 215 ASN 216 0.0346

ASN 216 GLU 217 -0.0003

GLU 217 ALA 218 0.0819

ALA 218 HIS 219 0.0000

HIS 219 TYR 220 -0.0157

TYR 220 SER 221 0.0002

SER 221 ILE 222 0.0357

ILE 222 ILE 223 0.0001

ILE 223 ARG 224 -0.0549

ARG 224 GLN 225 0.0001

GLN 225 GLY 226 -0.0648

GLY 226 GLN 227 0.0003

GLN 227 PHE 228 -0.1083

PHE 228 VAL 229 0.0002

VAL 229 HIS 230 -0.0944

HIS 230 LEU 231 -0.0002

LEU 231 ASP 232 0.0062

ASP 232 ASP 233 -0.0002

ASP 233 LEU 234 -0.0297

LEU 234 CYS 235 -0.0001

CYS 235 ASN 236 0.0307

ASN 236 ALA 237 -0.0001

ALA 237 HIS 238 0.0066

HIS 238 ILE 239 -0.0002

ILE 239 TYR 240 0.0721

TYR 240 LEU 241 0.0001

LEU 241 PHE 242 0.1215

PHE 242 GLU 243 -0.0005

GLU 243 ASN 244 0.1394

ASN 244 PRO 245 -0.0003

PRO 245 LYS 246 0.0227

LYS 246 ALA 247 -0.0001

ALA 247 GLU 248 -0.0161

GLU 248 GLY 249 0.0001

GLY 249 ARG 250 0.1159

ARG 250 TYR 251 -0.0001

TYR 251 ILE 252 0.1965

ILE 252 CYS 253 -0.0003

CYS 253 SER 254 0.1958

SER 254 SER 255 0.0000

SER 255 HIS 256 0.0965

HIS 256 ASP 257 0.0001

ASP 257 CYS 258 0.1970

CYS 258 ILE 259 0.0001

ILE 259 ILE 260 0.0210

ILE 260 LEU 261 0.0003

LEU 261 ASP 262 -0.0427

ASP 262 LEU 263 -0.0000

LEU 263 ALA 264 0.0576

ALA 264 LYS 265 0.0001

LYS 265 MET 266 -0.0848

MET 266 LEU 267 0.0003

LEU 267 ARG 268 -0.0262

ARG 268 GLU 269 0.0002

GLU 269 LYS 270 -0.0842

LYS 270 TYR 271 0.0001

TYR 271 PRO 272 -0.0496

PRO 272 GLU 273 0.0000

GLU 273 TYR 274 0.0250

TYR 274 ASN 275 0.0001

ASN 275 ILE 276 0.0746

ILE 276 PRO 277 0.0003

PRO 277 THR 278 -0.0202

THR 278 GLU 279 0.0001

GLU 279 PHE 280 0.0560

PHE 280 LYS 281 0.0003

LYS 281 GLY 282 0.1893

GLY 282 VAL 283 0.0002

VAL 283 ASP 284 -0.0150

ASP 284 GLU 285 0.0001

GLU 285 ASN 286 0.1688

ASN 286 LEU 287 0.0000

LEU 287 LYS 288 -0.0555

LYS 288 SER 289 0.0000

SER 289 VAL 290 0.0222

VAL 290 CYS 291 -0.0003

CYS 291 PHE 292 0.1102

PHE 292 SER 293 -0.0001

SER 293 SER 294 0.0232

SER 294 LYS 295 -0.0000

LYS 295 LYS 296 0.0098

LYS 296 LEU 297 -0.0003

LEU 297 THR 298 -0.0182

THR 298 ASP 299 0.0001

ASP 299 LEU 300 0.0391

LEU 300 GLY 301 0.0003

GLY 301 PHE 302 0.0326

PHE 302 GLU 303 0.0004

GLU 303 PHE 304 0.0602

PHE 304 LYS 305 -0.0001

LYS 305 TYR 306 0.1057

TYR 306 SER 307 0.0001

SER 307 LEU 308 -0.1164

LEU 308 GLU 309 0.0000

GLU 309 ASP 310 -0.0952

ASP 310 MET 311 0.0001

MET 311 PHE 312 -0.0222

PHE 312 THR 313 0.0000

THR 313 GLY 314 -0.1502

GLY 314 ALA 315 0.0003

ALA 315 VAL 316 -0.1156

VAL 316 ASP 317 0.0001

ASP 317 THR 318 -0.1850

THR 318 CYS 319 -0.0001

CYS 319 ARG 320 -0.0728

ARG 320 ALA 321 0.0000

ALA 321 LYS 322 -0.1569

LYS 322 GLY 323 0.0001

GLY 323 LEU 324 0.0927

LEU 324 LEU 325 0.0001

LEU 325 PRO 326 0.0030

PRO 326 PRO 327 0.0003

PRO 327 SER 328 0.0140

SER 328 HIS 329 0.0001

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.

*** Vv N133C DHK ***

CA strain for 2610082102113386154

--- normal mode 10 ---

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

* Vv N133C DHK *