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

* ADENOSINE_KINASE *

CA strain for 220501082405107263

--- 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
PRO 12 MET 13 0.0001

MET 13 ARG 14 0.0163

ARG 14 VAL 15 -0.0003

VAL 15 PHE 16 0.0287

PHE 16 ALA 17 -0.0002

ALA 17 ILE 18 0.0101

ILE 18 GLY 19 0.0000

GLY 19 ASN 20 0.0143

ASN 20 PRO 21 -0.0004

PRO 21 ILE 22 0.0534

ILE 22 LEU 23 -0.0001

LEU 23 ASP 24 0.0200

ASP 24 LEU 25 -0.0004

LEU 25 VAL 26 0.0135

VAL 26 ALA 27 0.0000

ALA 27 GLU 28 -0.0433

GLU 28 VAL 29 0.0001

VAL 29 PRO 30 0.0001

PRO 30 SER 31 0.0001

SER 31 SER 32 -0.0628

SER 32 PHE 33 0.0002

PHE 33 LEU 34 0.0133

LEU 34 ASP 35 0.0001

ASP 35 GLU 36 -0.0327

GLU 36 PHE 37 0.0007

PHE 37 PHE 38 -0.0005

PHE 38 LEU 39 -0.0000

LEU 39 LYS 40 -0.0357

LYS 40 ARG 41 0.0004

ARG 41 GLY 42 0.0327

GLY 42 ASP 43 0.0002

ASP 43 ALA 44 0.0295

ALA 44 THR 45 0.0002

THR 45 LEU 46 0.0262

LEU 46 ALA 47 0.0001

ALA 47 THR 48 -0.0456

THR 48 PRO 49 -0.0001

PRO 49 GLU 50 -0.0199

GLU 50 GLN 51 0.0001

GLN 51 MET 52 0.0347

MET 52 ARG 53 0.0000

ARG 53 ILE 54 -0.0421

ILE 54 TYR 55 -0.0005

TYR 55 SER 56 -0.0532

SER 56 THR 57 0.0003

THR 57 LEU 58 -0.0348

LEU 58 ASP 59 0.0001

ASP 59 GLN 60 -0.0160

GLN 60 PHE 61 -0.0002

PHE 61 ASN 62 0.0011

ASN 62 PRO 63 -0.0000

PRO 63 THR 64 -0.0181

THR 64 SER 65 0.0001

SER 65 LEU 66 -0.0461

LEU 66 PRO 67 -0.0000

PRO 67 GLY 68 -0.0629

GLY 68 GLY 69 0.0001

GLY 69 SER 70 -0.0642

SER 70 ALA 71 0.0002

ALA 71 LEU 72 -0.0549

LEU 72 ASN 73 -0.0001

ASN 73 SER 74 0.0072

SER 74 VAL 75 0.0003

VAL 75 ARG 76 0.0414

ARG 76 VAL 77 0.0001

VAL 77 VAL 78 0.0342

VAL 78 GLN 79 0.0000

GLN 79 LYS 80 0.0755

LYS 80 LEU 81 -0.0004

LEU 81 LEU 82 0.0780

LEU 82 ARG 83 -0.0002

ARG 83 LYS 84 0.0283

LYS 84 PRO 85 0.0002

PRO 85 GLY 86 0.0062

GLY 86 SER 87 0.0004

SER 87 ALA 88 0.0001

ALA 88 GLY 89 0.0002

GLY 89 TYR 90 0.0144

TYR 90 MET 91 -0.0002

MET 91 GLY 92 0.0376

GLY 92 ALA 93 0.0002

ALA 93 ILE 94 -0.0191

ILE 94 GLY 95 -0.0002

GLY 95 ASP 96 -0.0246

ASP 96 ASP 97 -0.0000

ASP 97 PRO 98 -0.0140

PRO 98 ARG 99 -0.0000

ARG 99 GLY 100 0.0555

GLY 100 GLN 101 -0.0000

GLN 101 VAL 102 0.0001

VAL 102 LEU 103 -0.0001

LEU 103 LYS 104 -0.0148

LYS 104 GLU 105 -0.0000

GLU 105 LEU 106 0.0329

LEU 106 CYS 107 0.0003

CYS 107 ASP 108 -0.0623

ASP 108 LYS 109 -0.0001

LYS 109 GLU 110 0.0657

GLU 110 GLY 111 0.0000

GLY 111 LEU 112 -0.0433

LEU 112 ALA 113 0.0003

ALA 113 THR 114 0.0097

THR 114 ARG 115 0.0002

ARG 115 PHE 116 0.0866

PHE 116 MET 117 0.0003

MET 117 VAL 118 0.1094

VAL 118 ALA 119 0.0002

ALA 119 PRO 120 -0.0061

PRO 120 GLY 121 0.0002

GLY 121 GLN 122 -0.0182

GLN 122 SER 123 0.0000

SER 123 THR 124 0.0137

THR 124 GLY 125 -0.0000

GLY 125 THR 126 0.0796

THR 126 CYS 127 0.0001

CYS 127 ALA 128 0.0150

ALA 128 VAL 129 -0.0002

VAL 129 LEU 130 0.0033

LEU 130 ILE 131 -0.0002

ILE 131 ASN 132 0.0760

ASN 132 GLU 133 -0.0001

GLU 133 LYS 134 -0.1083

LYS 134 GLU 135 0.0001

GLU 135 ARG 136 -0.1972

ARG 136 THR 137 -0.0001

THR 137 LEU 138 -0.0237

LEU 138 CYS 139 -0.0002

CYS 139 THR 140 0.0710

THR 140 HIS 141 -0.0002

HIS 141 LEU 142 0.0143

LEU 142 GLY 143 -0.0002

GLY 143 ALA 144 -0.0200

ALA 144 CYS 145 -0.0000

CYS 145 GLY 146 -0.0642

GLY 146 SER 147 -0.0000

SER 147 PHE 148 0.0448

PHE 148 ARG 149 0.0002

ARG 149 ILE 150 0.0073

ILE 150 PRO 151 0.0002

PRO 151 GLU 152 0.0461

GLU 152 ASP 153 -0.0001

ASP 153 TRP 154 -0.0096

TRP 154 THR 155 0.0000

THR 155 THR 156 0.0032

THR 156 PHE 157 0.0001

PHE 157 ALA 158 -0.0132

ALA 158 SER 159 0.0002

SER 159 GLY 160 0.0066

GLY 160 ALA 161 -0.0001

ALA 161 LEU 162 -0.0096

LEU 162 ILE 163 -0.0001

ILE 163 PHE 164 0.0217

PHE 164 TYR 165 0.0002

TYR 165 ALA 166 -0.0261

ALA 166 THR 167 0.0001

THR 167 ALA 168 -0.0238

ALA 168 TYR 169 0.0001

TYR 169 THR 170 -0.0115

THR 170 LEU 171 -0.0006

LEU 171 THR 172 -0.0233

THR 172 ALA 173 0.0000

ALA 173 THR 174 -0.0216

THR 174 PRO 175 0.0005

PRO 175 LYS 176 0.0500

LYS 176 ASN 177 -0.0004

ASN 177 ALA 178 -0.0203

ALA 178 LEU 179 -0.0001

LEU 179 GLU 180 0.0839

GLU 180 VAL 181 -0.0002

VAL 181 ALA 182 -0.0048

ALA 182 GLY 183 0.0003

GLY 183 TYR 184 0.0573

TYR 184 ALA 185 0.0000

ALA 185 HIS 186 0.0076

HIS 186 GLY 187 -0.0000

GLY 187 ILE 188 -0.0209

ILE 188 PRO 189 0.0001

PRO 189 ASN 190 -0.0641

ASN 190 ALA 191 -0.0001

ALA 191 ILE 192 0.0104

ILE 192 PHE 193 -0.0001

PHE 193 THR 194 -0.0258

THR 194 LEU 195 -0.0002

LEU 195 ASN 196 -0.0840

ASN 196 LEU 197 -0.0000

LEU 197 SER 198 0.0255

SER 198 ALA 199 -0.0001

ALA 199 PRO 200 -0.1066

PRO 200 PHE 201 0.0001

PHE 201 CYS 202 0.0225

CYS 202 VAL 203 -0.0001

VAL 203 GLU 204 0.0058

GLU 204 LEU 205 0.0001

LEU 205 TYR 206 0.0725

TYR 206 LYS 207 -0.0002

LYS 207 ASP 208 -0.0042

ASP 208 ALA 209 0.0001

ALA 209 MET 210 -0.0076

MET 210 GLN 211 -0.0001

GLN 211 SER 212 0.1574

SER 212 LEU 213 -0.0003

LEU 213 LEU 214 -0.0273

LEU 214 LEU 215 -0.0004

LEU 215 HIS 216 0.0585

HIS 216 THR 217 0.0000

THR 217 ASN 218 0.0226

ASN 218 ILE 219 0.0001

ILE 219 LEU 220 0.0573

LEU 220 PHE 221 0.0002

PHE 221 GLY 222 -0.0621

GLY 222 ASN 223 -0.0002

ASN 223 GLU 224 0.0758

GLU 224 GLU 225 -0.0000

GLU 225 GLU 226 -0.0605

GLU 226 PHE 227 0.0002

PHE 227 ALA 228 0.0886

ALA 228 HIS 229 -0.0003

HIS 229 LEU 230 0.0865

LEU 230 ALA 231 0.0001

ALA 231 LYS 232 0.1452

LYS 232 VAL 233 0.0004

VAL 233 HIS 234 -0.0009

HIS 234 ASN 235 -0.0002

ASN 235 LEU 236 0.1714

LEU 236 VAL 237 0.0001

VAL 237 ALA 238 -0.0478

ALA 238 LYS 241 -0.3446

LYS 241 THR 242 -0.0000

THR 242 ALA 243 -0.0275

ALA 243 LEU 244 -0.0001

LEU 244 SER 245 0.0178

SER 245 THR 246 0.0000

THR 246 ALA 247 0.3291

ALA 247 ASN 248 -0.0001

ASN 248 LYS 249 0.4248

LYS 249 GLU 250 0.0002

GLU 250 HIS 251 -0.1083

HIS 251 ALA 252 -0.0002

ALA 252 VAL 253 -0.0636

VAL 253 GLU 254 0.0002

GLU 254 GLY 270 0.1008

GLY 270 ALA 271 -0.0002

ALA 271 THR 272 0.0389

THR 272 LYS 273 0.0002

LYS 273 LEU 274 -0.0243

LEU 274 VAL 275 0.0005

VAL 275 VAL 276 -0.0619

VAL 276 MET 277 0.0001

MET 277 THR 278 -0.0562

THR 278 ARG 279 0.0001

ARG 279 GLY 280 -0.2348

GLY 280 HIS 281 -0.0003

HIS 281 ASN 282 -0.0553

ASN 282 PRO 283 0.0001

PRO 283 VAL 284 0.0901

VAL 284 ILE 285 -0.0000

ILE 285 ALA 286 -0.0970

ALA 286 ALA 287 -0.0000

ALA 287 GLU 288 -0.0061

GLU 288 GLN 289 -0.0003

GLN 289 THR 290 -0.0081

THR 290 ALA 291 -0.0002

ALA 291 ASP 292 -0.1035

ASP 292 GLY 293 -0.0000

GLY 293 THR 294 -0.0198

THR 294 VAL 295 -0.0001

VAL 295 VAL 296 0.0131

VAL 296 VAL 297 0.0001

VAL 297 HIS 298 0.0442

HIS 298 GLU 299 -0.0002

GLU 299 VAL 300 -0.0237

VAL 300 GLY 301 -0.0000

GLY 301 VAL 302 -0.1194

VAL 302 PRO 303 -0.0002

PRO 303 VAL 304 0.0656

VAL 304 VAL 305 0.0002

VAL 305 ALA 306 -0.2266

ALA 306 ALA 307 -0.0003

ALA 307 GLU 308 -0.0824

GLU 308 LYS 309 -0.0003

LYS 309 ILE 310 -0.1081

ILE 310 VAL 311 -0.0001

VAL 311 ASP 312 -0.1332

ASP 312 THR 313 0.0000

THR 313 ASN 314 -0.1703

ASN 314 GLY 315 0.0001

GLY 315 ALA 316 0.0223

ALA 316 GLY 317 -0.0003

GLY 317 ASP 318 -0.0135

ASP 318 ALA 319 -0.0003

ALA 319 PHE 320 -0.0509

PHE 320 VAL 321 -0.0001

VAL 321 GLY 322 0.0149

GLY 322 GLY 323 0.0004

GLY 323 PHE 324 0.0486

PHE 324 LEU 325 0.0001

LEU 325 TYR 326 0.0128

TYR 326 GLY 327 0.0002

GLY 327 LEU 328 0.0520

LEU 328 SER 329 -0.0003

SER 329 GLN 330 0.0133

GLN 330 GLY 331 0.0001

GLY 331 LYS 332 0.0051

LYS 332 THR 333 -0.0002

THR 333 VAL 334 -0.0115

VAL 334 LYS 335 -0.0000

LYS 335 GLN 336 0.0187

GLN 336 CYS 337 0.0001

CYS 337 ILE 338 0.0425

ILE 338 MET 339 0.0001

MET 339 CYS 340 0.0442

CYS 340 GLY 341 -0.0003

GLY 341 ASN 342 0.1681

ASN 342 ALA 343 -0.0002

ALA 343 CYS 344 0.0663

CYS 344 ALA 345 -0.0001

ALA 345 GLN 346 0.0475

GLN 346 ASP 347 -0.0000

ASP 347 VAL 348 0.0358

VAL 348 ILE 349 0.0002

ILE 349 GLN 350 -0.0044

GLN 350 HIS 351 -0.0000

HIS 351 VAL 352 -0.2586

VAL 352 GLY 353 0.0003

GLY 353 PHE 354 -0.0936

PHE 354 SER 355 -0.0000

SER 355 LEU 356 -0.0762

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.

*** ADENOSINE_KINASE ***

CA strain for 220501082405107263

--- normal mode 11 ---

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

* ADENOSINE_KINASE *