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

* ADENOSINE_KINASE *

CA strain for 220501084101121917

--- 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
PRO 12 MET 13 0.0000

MET 13 ARG 14 0.0226

ARG 14 VAL 15 0.0002

VAL 15 PHE 16 0.0374

PHE 16 ALA 17 0.0002

ALA 17 ILE 18 0.0147

ILE 18 GLY 19 -0.0003

GLY 19 ASN 20 0.1391

ASN 20 PRO 21 0.0004

PRO 21 ILE 22 0.1148

ILE 22 LEU 23 -0.0002

LEU 23 ASP 24 0.1099

ASP 24 LEU 25 -0.0003

LEU 25 VAL 26 -0.0063

VAL 26 ALA 27 -0.0000

ALA 27 GLU 28 0.0069

GLU 28 VAL 29 -0.0001

VAL 29 PRO 30 0.0425

PRO 30 SER 31 0.0000

SER 31 SER 32 -0.0561

SER 32 PHE 33 -0.0001

PHE 33 LEU 34 0.0214

LEU 34 ASP 35 0.0001

ASP 35 GLU 36 0.0107

GLU 36 PHE 37 -0.0002

PHE 37 PHE 38 0.0101

PHE 38 LEU 39 -0.0002

LEU 39 LYS 40 -0.0016

LYS 40 ARG 41 -0.0000

ARG 41 GLY 42 0.0165

GLY 42 ASP 43 -0.0000

ASP 43 ALA 44 -0.0449

ALA 44 THR 45 -0.0000

THR 45 LEU 46 -0.0413

LEU 46 ALA 47 -0.0002

ALA 47 THR 48 0.0435

THR 48 PRO 49 -0.0002

PRO 49 GLU 50 -0.0089

GLU 50 GLN 51 0.0001

GLN 51 MET 52 0.0042

MET 52 ARG 53 0.0001

ARG 53 ILE 54 -0.0433

ILE 54 TYR 55 -0.0001

TYR 55 SER 56 0.0512

SER 56 THR 57 -0.0001

THR 57 LEU 58 -0.1046

LEU 58 ASP 59 0.0000

ASP 59 GLN 60 0.1054

GLN 60 PHE 61 -0.0002

PHE 61 ASN 62 0.0071

ASN 62 PRO 63 0.0001

PRO 63 THR 64 -0.0803

THR 64 SER 65 -0.0003

SER 65 LEU 66 -0.1834

LEU 66 PRO 67 0.0001

PRO 67 GLY 68 0.0097

GLY 68 GLY 69 0.0000

GLY 69 SER 70 -0.0592

SER 70 ALA 71 0.0001

ALA 71 LEU 72 -0.0169

LEU 72 ASN 73 0.0003

ASN 73 SER 74 -0.0721

SER 74 VAL 75 -0.0002

VAL 75 ARG 76 -0.0090

ARG 76 VAL 77 -0.0004

VAL 77 VAL 78 -0.0440

VAL 78 GLN 79 0.0003

GLN 79 LYS 80 0.0098

LYS 80 LEU 81 -0.0000

LEU 81 LEU 82 -0.0085

LEU 82 ARG 83 0.0001

ARG 83 LYS 84 0.0003

LYS 84 PRO 85 -0.0003

PRO 85 GLY 86 -0.0079

GLY 86 SER 87 -0.0001

SER 87 ALA 88 0.0090

ALA 88 GLY 89 0.0004

GLY 89 TYR 90 0.0101

TYR 90 MET 91 0.0002

MET 91 GLY 92 0.1018

GLY 92 ALA 93 -0.0002

ALA 93 ILE 94 0.0898

ILE 94 GLY 95 0.0001

GLY 95 ASP 96 -0.0116

ASP 96 ASP 97 0.0001

ASP 97 PRO 98 -0.0480

PRO 98 ARG 99 0.0001

ARG 99 GLY 100 0.0732

GLY 100 GLN 101 0.0001

GLN 101 VAL 102 0.0584

VAL 102 LEU 103 -0.0003

LEU 103 LYS 104 0.0161

LYS 104 GLU 105 -0.0002

GLU 105 LEU 106 0.0308

LEU 106 CYS 107 0.0002

CYS 107 ASP 108 0.0096

ASP 108 LYS 109 -0.0001

LYS 109 GLU 110 -0.0192

GLU 110 GLY 111 -0.0002

GLY 111 LEU 112 -0.0138

LEU 112 ALA 113 0.0002

ALA 113 THR 114 0.0060

THR 114 ARG 115 0.0001

ARG 115 PHE 116 0.0555

PHE 116 MET 117 0.0004

MET 117 VAL 118 0.1127

VAL 118 ALA 119 0.0001

ALA 119 PRO 120 0.0017

PRO 120 GLY 121 0.0004

GLY 121 GLN 122 -0.0181

GLN 122 SER 123 -0.0002

SER 123 THR 124 0.0520

THR 124 GLY 125 0.0003

GLY 125 THR 126 0.0915

THR 126 CYS 127 0.0001

CYS 127 ALA 128 0.0524

ALA 128 VAL 129 0.0001

VAL 129 LEU 130 0.0446

LEU 130 ILE 131 -0.0003

ILE 131 ASN 132 0.1035

ASN 132 GLU 133 -0.0000

GLU 133 LYS 134 -0.2222

LYS 134 GLU 135 -0.0002

GLU 135 ARG 136 0.1845

ARG 136 THR 137 -0.0001

THR 137 LEU 138 0.0158

LEU 138 CYS 139 0.0001

CYS 139 THR 140 -0.0169

THR 140 HIS 141 -0.0001

HIS 141 LEU 142 0.3578

LEU 142 GLY 143 0.0003

GLY 143 ALA 144 -0.1504

ALA 144 CYS 145 0.0004

CYS 145 GLY 146 0.0974

GLY 146 SER 147 0.0001

SER 147 PHE 148 0.1483

PHE 148 ARG 149 0.0001

ARG 149 ILE 150 0.0895

ILE 150 PRO 151 -0.0003

PRO 151 GLU 152 0.0845

GLU 152 ASP 153 -0.0001

ASP 153 TRP 154 -0.0065

TRP 154 THR 155 -0.0001

THR 155 THR 156 -0.0157

THR 156 PHE 157 -0.0001

PHE 157 ALA 158 0.0279

ALA 158 SER 159 -0.0000

SER 159 GLY 160 0.0223

GLY 160 ALA 161 -0.0004

ALA 161 LEU 162 0.0317

LEU 162 ILE 163 0.0002

ILE 163 PHE 164 -0.0043

PHE 164 TYR 165 -0.0001

TYR 165 ALA 166 0.0135

ALA 166 THR 167 0.0002

THR 167 ALA 168 -0.0067

ALA 168 TYR 169 0.0003

TYR 169 THR 170 -0.0630

THR 170 LEU 171 -0.0004

LEU 171 THR 172 0.0582

THR 172 ALA 173 -0.0004

ALA 173 THR 174 0.0625

THR 174 PRO 175 0.0001

PRO 175 LYS 176 -0.0435

LYS 176 ASN 177 0.0001

ASN 177 ALA 178 0.0399

ALA 178 LEU 179 -0.0000

LEU 179 GLU 180 -0.0537

GLU 180 VAL 181 -0.0003

VAL 181 ALA 182 0.0648

ALA 182 GLY 183 -0.0001

GLY 183 TYR 184 -0.0186

TYR 184 ALA 185 -0.0001

ALA 185 HIS 186 0.0082

HIS 186 GLY 187 0.0003

GLY 187 ILE 188 0.0211

ILE 188 PRO 189 0.0002

PRO 189 ASN 190 0.0497

ASN 190 ALA 191 0.0000

ALA 191 ILE 192 -0.0104

ILE 192 PHE 193 0.0001

PHE 193 THR 194 -0.0034

THR 194 LEU 195 0.0003

LEU 195 ASN 196 0.0209

ASN 196 LEU 197 0.0002

LEU 197 SER 198 0.0082

SER 198 ALA 199 -0.0002

ALA 199 PRO 200 0.0017

PRO 200 PHE 201 -0.0002

PHE 201 CYS 202 -0.0062

CYS 202 VAL 203 -0.0000

VAL 203 GLU 204 0.0048

GLU 204 LEU 205 0.0001

LEU 205 TYR 206 -0.0441

TYR 206 LYS 207 0.0001

LYS 207 ASP 208 0.0089

ASP 208 ALA 209 -0.0001

ALA 209 MET 210 0.0003

MET 210 GLN 211 -0.0001

GLN 211 SER 212 -0.0168

SER 212 LEU 213 -0.0000

LEU 213 LEU 214 0.0368

LEU 214 LEU 215 -0.0001

LEU 215 HIS 216 0.0181

HIS 216 THR 217 -0.0005

THR 217 ASN 218 -0.0181

ASN 218 ILE 219 -0.0003

ILE 219 LEU 220 0.0229

LEU 220 PHE 221 0.0005

PHE 221 GLY 222 0.0409

GLY 222 ASN 223 0.0000

ASN 223 GLU 224 -0.0429

GLU 224 GLU 225 -0.0003

GLU 225 GLU 226 -0.0001

GLU 226 PHE 227 0.0002

PHE 227 ALA 228 -0.0226

ALA 228 HIS 229 -0.0003

HIS 229 LEU 230 0.0043

LEU 230 ALA 231 -0.0001

ALA 231 LYS 232 -0.0056

LYS 232 VAL 233 -0.0001

VAL 233 HIS 234 -0.0011

HIS 234 ASN 235 -0.0001

ASN 235 LEU 236 -0.0017

LEU 236 VAL 237 0.0004

VAL 237 ALA 238 0.0213

ALA 238 LYS 241 0.0290

LYS 241 ALA 243 -0.0154

ALA 243 LEU 244 -0.0000

LEU 244 SER 245 -0.0125

SER 245 ASN 248 -0.0248

ASN 248 LYS 249 0.0001

LYS 249 GLU 250 -0.0575

GLU 250 HIS 251 -0.0000

HIS 251 ALA 252 -0.0122

ALA 252 VAL 253 -0.0000

VAL 253 GLU 254 0.0217

GLU 254 GLY 270 -0.0662

GLY 270 ALA 271 0.0001

ALA 271 THR 272 -0.0311

THR 272 LYS 273 -0.0001

LYS 273 LEU 274 -0.0333

LEU 274 VAL 275 0.0001

VAL 275 VAL 276 -0.0062

VAL 276 MET 277 -0.0002

MET 277 THR 278 -0.0239

THR 278 ARG 279 0.0000

ARG 279 GLY 280 -0.0181

GLY 280 HIS 281 0.0000

HIS 281 ASN 282 -0.0590

ASN 282 PRO 283 0.0002

PRO 283 VAL 284 -0.0042

VAL 284 ILE 285 0.0003

ILE 285 ALA 286 -0.0229

ALA 286 ALA 287 -0.0002

ALA 287 GLU 288 -0.0024

GLU 288 GLN 289 0.0000

GLN 289 THR 290 -0.0278

THR 290 ALA 291 0.0001

ALA 291 ASP 292 -0.0229

ASP 292 GLY 293 -0.0001

GLY 293 THR 294 -0.0931

THR 294 VAL 295 -0.0000

VAL 295 VAL 296 -0.1336

VAL 296 VAL 297 -0.0001

VAL 297 HIS 298 -0.0834

HIS 298 GLU 299 0.0000

GLU 299 VAL 300 -0.1742

VAL 300 GLY 301 0.0002

GLY 301 VAL 302 -0.2594

VAL 302 PRO 303 -0.0002

PRO 303 VAL 304 -0.2880

VAL 304 VAL 305 -0.0002

VAL 305 ALA 306 -0.0841

ALA 306 ALA 307 0.0004

ALA 307 GLU 308 -0.1820

GLU 308 LYS 309 0.0002

LYS 309 ILE 310 -0.1054

ILE 310 VAL 311 0.0001

VAL 311 ASP 312 0.0750

ASP 312 THR 313 0.0001

THR 313 ASN 314 -0.0036

ASN 314 GLY 315 0.0002

GLY 315 ALA 316 -0.0426

ALA 316 GLY 317 -0.0002

GLY 317 ASP 318 -0.0529

ASP 318 ALA 319 -0.0001

ALA 319 PHE 320 -0.1089

PHE 320 VAL 321 0.0003

VAL 321 GLY 322 0.0071

GLY 322 GLY 323 -0.0003

GLY 323 PHE 324 -0.0414

PHE 324 LEU 325 0.0003

LEU 325 TYR 326 0.0272

TYR 326 GLY 327 -0.0003

GLY 327 LEU 328 -0.0010

LEU 328 SER 329 -0.0001

SER 329 GLN 330 0.0217

GLN 330 GLY 331 0.0003

GLY 331 LYS 332 0.0286

LYS 332 THR 333 0.0002

THR 333 VAL 334 0.0845

VAL 334 LYS 335 -0.0002

LYS 335 GLN 336 0.0384

GLN 336 CYS 337 -0.0002

CYS 337 ILE 338 0.0584

ILE 338 MET 339 -0.0002

MET 339 CYS 340 0.0597

CYS 340 GLY 341 -0.0003

GLY 341 ASN 342 0.0349

ASN 342 ALA 343 0.0003

ALA 343 CYS 344 0.0216

CYS 344 ALA 345 0.0003

ALA 345 GLN 346 0.1185

GLN 346 ASP 347 0.0001

ASP 347 VAL 348 0.0133

VAL 348 ILE 349 -0.0000

ILE 349 GLN 350 0.1048

GLN 350 HIS 351 -0.0003

HIS 351 VAL 352 -0.2191

VAL 352 GLY 353 0.0004

GLY 353 PHE 354 -0.1520

PHE 354 SER 355 -0.0001

SER 355 LEU 356 -0.0715

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 220501084101121917

--- normal mode 9 ---

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

* ADENOSINE_KINASE *